data_5CQG
# 
_entry.id   5CQG 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.379 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   5CQG         pdb_00005cqg 10.2210/pdb5cqg/pdb 
WWPDB D_1000212034 ?            ?                   
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        5CQG 
_pdbx_database_status.recvd_initial_deposition_date   2015-07-21 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Bryan, C.'        1 
'Rice, C.'         2 
'Hoffman, H.'      3 
'Harkisheimer, M.' 4 
'Sweeney, M.'      5 
'Skordalakes, E.'  6 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Structure 
_citation.journal_id_ASTM           STRUE6 
_citation.journal_id_CSD            2005 
_citation.journal_id_ISSN           1878-4186 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            23 
_citation.language                  ? 
_citation.page_first                1934 
_citation.page_last                 1942 
_citation.title                     'Structural Basis of Telomerase Inhibition by the Highly Specific BIBR1532.' 
_citation.year                      2015 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.str.2015.08.006 
_citation.pdbx_database_id_PubMed   26365799 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Bryan, C.'        1 ? 
primary 'Rice, C.'         2 ? 
primary 'Hoffman, H.'      3 ? 
primary 'Harkisheimer, M.' 4 ? 
primary 'Sweeney, M.'      5 ? 
primary 'Skordalakes, E.'  6 ? 
# 
_cell.entry_id           5CQG 
_cell.length_a           117.719 
_cell.length_b           84.902 
_cell.length_c           123.333 
_cell.angle_alpha        90.00 
_cell.angle_beta         116.20 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         5CQG 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Telomerase reverse transcriptase'                           70588.719 2   ? ? ? ? 
2 non-polymer syn '2-{[(2E)-3-(naphthalen-2-yl)but-2-enoyl]amino}benzoic acid' 331.365   2   ? ? ? ? 
3 water       nat water                                                        18.015    409 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MVHYYRLSLKSRQKAPKIVNSKYNSILNIALKNFRLCKKHKTKKPVQILALLQEIIPKSYFGTTTNLKRFYKVVEKILTQ
SSFECIHLSVLHKCYDYDAIPWLQNVEPNLRPKLLLKHNLFLLDNIVKPIIAFYYKPIKTLNGHEIKFIRKEEYISFESK
VFHKLKKMKYLVEVQDEVKPRGVLNIIPKQDNFRAIVSIFPDSARKPFFKLLTSKIYKVLEEKYKTSGSLYTCWSEFTQK
TQGQIYGIKVDIRDAYGNVKIPVLCKLIQSIPTHLLDSEKKNFIVDHISNQFVAFRRKIYKWNHGLLQGDPLSGCLCELY
MAFMDRLYFSNLDKDAFIHRTVDDYFFCSPHPHKVYDFELLIKGVYQVNPTKTRTNLPTHRHPQDEIPYCGKIFNLTTRQ
VRTLYKLPPNYEIRHKFKLWNFNNQISDDNPARFLQKAMDFPFICNSFTKFEFNTVFNDQRTVFANFYDAMICVAYKFDA
AMMALRTSFLVNDFGFIWLVLSSTVRAYASRAFKKIVTYKGGKYRKVTFQCLKSIAWRAFLAVLKRRTEIYKGLIDRIKS
REKLTMKFHDGEVDASYFCKLPEKFRFVKINRKASI
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MVHYYRLSLKSRQKAPKIVNSKYNSILNIALKNFRLCKKHKTKKPVQILALLQEIIPKSYFGTTTNLKRFYKVVEKILTQ
SSFECIHLSVLHKCYDYDAIPWLQNVEPNLRPKLLLKHNLFLLDNIVKPIIAFYYKPIKTLNGHEIKFIRKEEYISFESK
VFHKLKKMKYLVEVQDEVKPRGVLNIIPKQDNFRAIVSIFPDSARKPFFKLLTSKIYKVLEEKYKTSGSLYTCWSEFTQK
TQGQIYGIKVDIRDAYGNVKIPVLCKLIQSIPTHLLDSEKKNFIVDHISNQFVAFRRKIYKWNHGLLQGDPLSGCLCELY
MAFMDRLYFSNLDKDAFIHRTVDDYFFCSPHPHKVYDFELLIKGVYQVNPTKTRTNLPTHRHPQDEIPYCGKIFNLTTRQ
VRTLYKLPPNYEIRHKFKLWNFNNQISDDNPARFLQKAMDFPFICNSFTKFEFNTVFNDQRTVFANFYDAMICVAYKFDA
AMMALRTSFLVNDFGFIWLVLSSTVRAYASRAFKKIVTYKGGKYRKVTFQCLKSIAWRAFLAVLKRRTEIYKGLIDRIKS
REKLTMKFHDGEVDASYFCKLPEKFRFVKINRKASI
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   VAL n 
1 3   HIS n 
1 4   TYR n 
1 5   TYR n 
1 6   ARG n 
1 7   LEU n 
1 8   SER n 
1 9   LEU n 
1 10  LYS n 
1 11  SER n 
1 12  ARG n 
1 13  GLN n 
1 14  LYS n 
1 15  ALA n 
1 16  PRO n 
1 17  LYS n 
1 18  ILE n 
1 19  VAL n 
1 20  ASN n 
1 21  SER n 
1 22  LYS n 
1 23  TYR n 
1 24  ASN n 
1 25  SER n 
1 26  ILE n 
1 27  LEU n 
1 28  ASN n 
1 29  ILE n 
1 30  ALA n 
1 31  LEU n 
1 32  LYS n 
1 33  ASN n 
1 34  PHE n 
1 35  ARG n 
1 36  LEU n 
1 37  CYS n 
1 38  LYS n 
1 39  LYS n 
1 40  HIS n 
1 41  LYS n 
1 42  THR n 
1 43  LYS n 
1 44  LYS n 
1 45  PRO n 
1 46  VAL n 
1 47  GLN n 
1 48  ILE n 
1 49  LEU n 
1 50  ALA n 
1 51  LEU n 
1 52  LEU n 
1 53  GLN n 
1 54  GLU n 
1 55  ILE n 
1 56  ILE n 
1 57  PRO n 
1 58  LYS n 
1 59  SER n 
1 60  TYR n 
1 61  PHE n 
1 62  GLY n 
1 63  THR n 
1 64  THR n 
1 65  THR n 
1 66  ASN n 
1 67  LEU n 
1 68  LYS n 
1 69  ARG n 
1 70  PHE n 
1 71  TYR n 
1 72  LYS n 
1 73  VAL n 
1 74  VAL n 
1 75  GLU n 
1 76  LYS n 
1 77  ILE n 
1 78  LEU n 
1 79  THR n 
1 80  GLN n 
1 81  SER n 
1 82  SER n 
1 83  PHE n 
1 84  GLU n 
1 85  CYS n 
1 86  ILE n 
1 87  HIS n 
1 88  LEU n 
1 89  SER n 
1 90  VAL n 
1 91  LEU n 
1 92  HIS n 
1 93  LYS n 
1 94  CYS n 
1 95  TYR n 
1 96  ASP n 
1 97  TYR n 
1 98  ASP n 
1 99  ALA n 
1 100 ILE n 
1 101 PRO n 
1 102 TRP n 
1 103 LEU n 
1 104 GLN n 
1 105 ASN n 
1 106 VAL n 
1 107 GLU n 
1 108 PRO n 
1 109 ASN n 
1 110 LEU n 
1 111 ARG n 
1 112 PRO n 
1 113 LYS n 
1 114 LEU n 
1 115 LEU n 
1 116 LEU n 
1 117 LYS n 
1 118 HIS n 
1 119 ASN n 
1 120 LEU n 
1 121 PHE n 
1 122 LEU n 
1 123 LEU n 
1 124 ASP n 
1 125 ASN n 
1 126 ILE n 
1 127 VAL n 
1 128 LYS n 
1 129 PRO n 
1 130 ILE n 
1 131 ILE n 
1 132 ALA n 
1 133 PHE n 
1 134 TYR n 
1 135 TYR n 
1 136 LYS n 
1 137 PRO n 
1 138 ILE n 
1 139 LYS n 
1 140 THR n 
1 141 LEU n 
1 142 ASN n 
1 143 GLY n 
1 144 HIS n 
1 145 GLU n 
1 146 ILE n 
1 147 LYS n 
1 148 PHE n 
1 149 ILE n 
1 150 ARG n 
1 151 LYS n 
1 152 GLU n 
1 153 GLU n 
1 154 TYR n 
1 155 ILE n 
1 156 SER n 
1 157 PHE n 
1 158 GLU n 
1 159 SER n 
1 160 LYS n 
1 161 VAL n 
1 162 PHE n 
1 163 HIS n 
1 164 LYS n 
1 165 LEU n 
1 166 LYS n 
1 167 LYS n 
1 168 MET n 
1 169 LYS n 
1 170 TYR n 
1 171 LEU n 
1 172 VAL n 
1 173 GLU n 
1 174 VAL n 
1 175 GLN n 
1 176 ASP n 
1 177 GLU n 
1 178 VAL n 
1 179 LYS n 
1 180 PRO n 
1 181 ARG n 
1 182 GLY n 
1 183 VAL n 
1 184 LEU n 
1 185 ASN n 
1 186 ILE n 
1 187 ILE n 
1 188 PRO n 
1 189 LYS n 
1 190 GLN n 
1 191 ASP n 
1 192 ASN n 
1 193 PHE n 
1 194 ARG n 
1 195 ALA n 
1 196 ILE n 
1 197 VAL n 
1 198 SER n 
1 199 ILE n 
1 200 PHE n 
1 201 PRO n 
1 202 ASP n 
1 203 SER n 
1 204 ALA n 
1 205 ARG n 
1 206 LYS n 
1 207 PRO n 
1 208 PHE n 
1 209 PHE n 
1 210 LYS n 
1 211 LEU n 
1 212 LEU n 
1 213 THR n 
1 214 SER n 
1 215 LYS n 
1 216 ILE n 
1 217 TYR n 
1 218 LYS n 
1 219 VAL n 
1 220 LEU n 
1 221 GLU n 
1 222 GLU n 
1 223 LYS n 
1 224 TYR n 
1 225 LYS n 
1 226 THR n 
1 227 SER n 
1 228 GLY n 
1 229 SER n 
1 230 LEU n 
1 231 TYR n 
1 232 THR n 
1 233 CYS n 
1 234 TRP n 
1 235 SER n 
1 236 GLU n 
1 237 PHE n 
1 238 THR n 
1 239 GLN n 
1 240 LYS n 
1 241 THR n 
1 242 GLN n 
1 243 GLY n 
1 244 GLN n 
1 245 ILE n 
1 246 TYR n 
1 247 GLY n 
1 248 ILE n 
1 249 LYS n 
1 250 VAL n 
1 251 ASP n 
1 252 ILE n 
1 253 ARG n 
1 254 ASP n 
1 255 ALA n 
1 256 TYR n 
1 257 GLY n 
1 258 ASN n 
1 259 VAL n 
1 260 LYS n 
1 261 ILE n 
1 262 PRO n 
1 263 VAL n 
1 264 LEU n 
1 265 CYS n 
1 266 LYS n 
1 267 LEU n 
1 268 ILE n 
1 269 GLN n 
1 270 SER n 
1 271 ILE n 
1 272 PRO n 
1 273 THR n 
1 274 HIS n 
1 275 LEU n 
1 276 LEU n 
1 277 ASP n 
1 278 SER n 
1 279 GLU n 
1 280 LYS n 
1 281 LYS n 
1 282 ASN n 
1 283 PHE n 
1 284 ILE n 
1 285 VAL n 
1 286 ASP n 
1 287 HIS n 
1 288 ILE n 
1 289 SER n 
1 290 ASN n 
1 291 GLN n 
1 292 PHE n 
1 293 VAL n 
1 294 ALA n 
1 295 PHE n 
1 296 ARG n 
1 297 ARG n 
1 298 LYS n 
1 299 ILE n 
1 300 TYR n 
1 301 LYS n 
1 302 TRP n 
1 303 ASN n 
1 304 HIS n 
1 305 GLY n 
1 306 LEU n 
1 307 LEU n 
1 308 GLN n 
1 309 GLY n 
1 310 ASP n 
1 311 PRO n 
1 312 LEU n 
1 313 SER n 
1 314 GLY n 
1 315 CYS n 
1 316 LEU n 
1 317 CYS n 
1 318 GLU n 
1 319 LEU n 
1 320 TYR n 
1 321 MET n 
1 322 ALA n 
1 323 PHE n 
1 324 MET n 
1 325 ASP n 
1 326 ARG n 
1 327 LEU n 
1 328 TYR n 
1 329 PHE n 
1 330 SER n 
1 331 ASN n 
1 332 LEU n 
1 333 ASP n 
1 334 LYS n 
1 335 ASP n 
1 336 ALA n 
1 337 PHE n 
1 338 ILE n 
1 339 HIS n 
1 340 ARG n 
1 341 THR n 
1 342 VAL n 
1 343 ASP n 
1 344 ASP n 
1 345 TYR n 
1 346 PHE n 
1 347 PHE n 
1 348 CYS n 
1 349 SER n 
1 350 PRO n 
1 351 HIS n 
1 352 PRO n 
1 353 HIS n 
1 354 LYS n 
1 355 VAL n 
1 356 TYR n 
1 357 ASP n 
1 358 PHE n 
1 359 GLU n 
1 360 LEU n 
1 361 LEU n 
1 362 ILE n 
1 363 LYS n 
1 364 GLY n 
1 365 VAL n 
1 366 TYR n 
1 367 GLN n 
1 368 VAL n 
1 369 ASN n 
1 370 PRO n 
1 371 THR n 
1 372 LYS n 
1 373 THR n 
1 374 ARG n 
1 375 THR n 
1 376 ASN n 
1 377 LEU n 
1 378 PRO n 
1 379 THR n 
1 380 HIS n 
1 381 ARG n 
1 382 HIS n 
1 383 PRO n 
1 384 GLN n 
1 385 ASP n 
1 386 GLU n 
1 387 ILE n 
1 388 PRO n 
1 389 TYR n 
1 390 CYS n 
1 391 GLY n 
1 392 LYS n 
1 393 ILE n 
1 394 PHE n 
1 395 ASN n 
1 396 LEU n 
1 397 THR n 
1 398 THR n 
1 399 ARG n 
1 400 GLN n 
1 401 VAL n 
1 402 ARG n 
1 403 THR n 
1 404 LEU n 
1 405 TYR n 
1 406 LYS n 
1 407 LEU n 
1 408 PRO n 
1 409 PRO n 
1 410 ASN n 
1 411 TYR n 
1 412 GLU n 
1 413 ILE n 
1 414 ARG n 
1 415 HIS n 
1 416 LYS n 
1 417 PHE n 
1 418 LYS n 
1 419 LEU n 
1 420 TRP n 
1 421 ASN n 
1 422 PHE n 
1 423 ASN n 
1 424 ASN n 
1 425 GLN n 
1 426 ILE n 
1 427 SER n 
1 428 ASP n 
1 429 ASP n 
1 430 ASN n 
1 431 PRO n 
1 432 ALA n 
1 433 ARG n 
1 434 PHE n 
1 435 LEU n 
1 436 GLN n 
1 437 LYS n 
1 438 ALA n 
1 439 MET n 
1 440 ASP n 
1 441 PHE n 
1 442 PRO n 
1 443 PHE n 
1 444 ILE n 
1 445 CYS n 
1 446 ASN n 
1 447 SER n 
1 448 PHE n 
1 449 THR n 
1 450 LYS n 
1 451 PHE n 
1 452 GLU n 
1 453 PHE n 
1 454 ASN n 
1 455 THR n 
1 456 VAL n 
1 457 PHE n 
1 458 ASN n 
1 459 ASP n 
1 460 GLN n 
1 461 ARG n 
1 462 THR n 
1 463 VAL n 
1 464 PHE n 
1 465 ALA n 
1 466 ASN n 
1 467 PHE n 
1 468 TYR n 
1 469 ASP n 
1 470 ALA n 
1 471 MET n 
1 472 ILE n 
1 473 CYS n 
1 474 VAL n 
1 475 ALA n 
1 476 TYR n 
1 477 LYS n 
1 478 PHE n 
1 479 ASP n 
1 480 ALA n 
1 481 ALA n 
1 482 MET n 
1 483 MET n 
1 484 ALA n 
1 485 LEU n 
1 486 ARG n 
1 487 THR n 
1 488 SER n 
1 489 PHE n 
1 490 LEU n 
1 491 VAL n 
1 492 ASN n 
1 493 ASP n 
1 494 PHE n 
1 495 GLY n 
1 496 PHE n 
1 497 ILE n 
1 498 TRP n 
1 499 LEU n 
1 500 VAL n 
1 501 LEU n 
1 502 SER n 
1 503 SER n 
1 504 THR n 
1 505 VAL n 
1 506 ARG n 
1 507 ALA n 
1 508 TYR n 
1 509 ALA n 
1 510 SER n 
1 511 ARG n 
1 512 ALA n 
1 513 PHE n 
1 514 LYS n 
1 515 LYS n 
1 516 ILE n 
1 517 VAL n 
1 518 THR n 
1 519 TYR n 
1 520 LYS n 
1 521 GLY n 
1 522 GLY n 
1 523 LYS n 
1 524 TYR n 
1 525 ARG n 
1 526 LYS n 
1 527 VAL n 
1 528 THR n 
1 529 PHE n 
1 530 GLN n 
1 531 CYS n 
1 532 LEU n 
1 533 LYS n 
1 534 SER n 
1 535 ILE n 
1 536 ALA n 
1 537 TRP n 
1 538 ARG n 
1 539 ALA n 
1 540 PHE n 
1 541 LEU n 
1 542 ALA n 
1 543 VAL n 
1 544 LEU n 
1 545 LYS n 
1 546 ARG n 
1 547 ARG n 
1 548 THR n 
1 549 GLU n 
1 550 ILE n 
1 551 TYR n 
1 552 LYS n 
1 553 GLY n 
1 554 LEU n 
1 555 ILE n 
1 556 ASP n 
1 557 ARG n 
1 558 ILE n 
1 559 LYS n 
1 560 SER n 
1 561 ARG n 
1 562 GLU n 
1 563 LYS n 
1 564 LEU n 
1 565 THR n 
1 566 MET n 
1 567 LYS n 
1 568 PHE n 
1 569 HIS n 
1 570 ASP n 
1 571 GLY n 
1 572 GLU n 
1 573 VAL n 
1 574 ASP n 
1 575 ALA n 
1 576 SER n 
1 577 TYR n 
1 578 PHE n 
1 579 CYS n 
1 580 LYS n 
1 581 LEU n 
1 582 PRO n 
1 583 GLU n 
1 584 LYS n 
1 585 PHE n 
1 586 ARG n 
1 587 PHE n 
1 588 VAL n 
1 589 LYS n 
1 590 ILE n 
1 591 ASN n 
1 592 ARG n 
1 593 LYS n 
1 594 ALA n 
1 595 SER n 
1 596 ILE n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   596 
_entity_src_gen.gene_src_common_name               'Red flour beetle' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'TERT, TcasGA2_TC010963' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Tribolium castaneum' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     7070 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q0QHL8_TRICA 
_struct_ref.pdbx_db_accession          Q0QHL8 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MVHYYRLSLKSRQKAPKIVNSKYNSILNIALKNFRLCKKHKTKKPVQILALLQEIIPKSYFGTTTNLKRFYKVVEKILTQ
SSFECIHLSVLHKCYDYDAIPWLQNVEPNLRPKLLLKHNLFLLDNIVKPIIAFYYKPIKTLNGHEIKFIRKEEYISFESK
VFHKLKKMKYLVEVQDEVKPRGVLNIIPKQDNFRAIVSIFPDSARKPFFKLLTSKIYKVLEEKYKTSGSLYTCWSEFTQK
TQGQIYGIKVDIRDAYGNVKIPVLCKLIQSIPTHLLDSEKKNFIVDHISNQFVAFRRKIYKWNHGLLQGDPLSGCLCELY
MAFMDRLYFSNLDKDAFIHRTVDDYFFCSPHPHKVYDFELLIKGVYQVNPTKTRTNLPTHRHPQDEIPYCGKIFNLTTRQ
VRTLYKLPPNYEIRHKFKLWNFNNQISDDNPARFLQKAMDFPFICNSFTKFEFNTVFNDQRTVFANFYDAMICVAYKFDA
AMMALRTSFLVNDFGFIWLVLSSTVRAYASRAFKKIVTYKGGKYRKVTFQCLKSIAWRAFLAVLKRRTEIYKGLIDRIKS
REKLTMKFHDGEVDASYFCKLPEKFRFVKINRKASI
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 5CQG A 1 ? 596 ? Q0QHL8 1 ? 596 ? 1 596 
2 1 5CQG B 1 ? 596 ? Q0QHL8 1 ? 596 ? 1 596 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
55C non-polymer         . '2-{[(2E)-3-(naphthalen-2-yl)but-2-enoyl]amino}benzoic acid' 'BIBR 1532' 'C21 H17 N O3'   331.365 
ALA 'L-peptide linking' y ALANINE                                                      ?           'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                                                     ?           'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                   ?           'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                              ?           'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE                                                     ?           'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE                                                    ?           'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                              ?           'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                                                      ?           'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                                                    ?           'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                                                        ?           'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                   ?           'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                                                      ?           'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                                                       ?           'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                                                   ?           'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                                ?           'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                                                      ?           'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                                                       ?           'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE                                                    ?           'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                   ?           'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                                                     ?           'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                                                       ?           'C5 H11 N O2'    117.146 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   5CQG 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                      ? 
_exptl_crystal.density_diffrn              ? 
_exptl_crystal.density_Matthews            3.92 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         68.60 
_exptl_crystal.description                 ? 
_exptl_crystal.F_000                       ? 
_exptl_crystal.id                          1 
_exptl_crystal.preparation                 ? 
_exptl_crystal.size_max                    ? 
_exptl_crystal.size_mid                    ? 
_exptl_crystal.size_min                    ? 
_exptl_crystal.size_rad                    ? 
_exptl_crystal.colour_lustre               ? 
_exptl_crystal.colour_modifier             ? 
_exptl_crystal.colour_primary              ? 
_exptl_crystal.density_meas                ? 
_exptl_crystal.density_meas_esd            ? 
_exptl_crystal.density_meas_gt             ? 
_exptl_crystal.density_meas_lt             ? 
_exptl_crystal.density_meas_temp           ? 
_exptl_crystal.density_meas_temp_esd       ? 
_exptl_crystal.density_meas_temp_gt        ? 
_exptl_crystal.density_meas_temp_lt        ? 
_exptl_crystal.pdbx_crystal_image_url      ? 
_exptl_crystal.pdbx_crystal_image_format   ? 
_exptl_crystal.pdbx_mosaicity              ? 
_exptl_crystal.pdbx_mosaicity_esd          ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;1.3M NaNO3
100mM Tris 8.5
;
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment    ? 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.ambient_temp_esd       ? 
_diffrn.crystal_id             1 
_diffrn.crystal_support        ? 
_diffrn.crystal_treatment      ? 
_diffrn.details                ? 
_diffrn.id                     1 
_diffrn.ambient_pressure       ? 
_diffrn.ambient_pressure_esd   ? 
_diffrn.ambient_pressure_gt    ? 
_diffrn.ambient_pressure_lt    ? 
_diffrn.ambient_temp_gt        ? 
_diffrn.ambient_temp_lt        ? 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2011-11-04 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.1 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'NSLS BEAMLINE X25' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.1 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X25 
_diffrn_source.pdbx_synchrotron_site       NSLS 
# 
_reflns.B_iso_Wilson_estimate            ? 
_reflns.entry_id                         5CQG 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                2.3 
_reflns.d_resolution_low                 20 
_reflns.details                          ? 
_reflns.limit_h_max                      ? 
_reflns.limit_h_min                      ? 
_reflns.limit_k_max                      ? 
_reflns.limit_k_min                      ? 
_reflns.limit_l_max                      ? 
_reflns.limit_l_min                      ? 
_reflns.number_all                       ? 
_reflns.number_obs                       97056 
_reflns.observed_criterion               ? 
_reflns.observed_criterion_F_max         ? 
_reflns.observed_criterion_F_min         ? 
_reflns.observed_criterion_I_max         ? 
_reflns.observed_criterion_I_min         ? 
_reflns.observed_criterion_sigma_F       ? 
_reflns.observed_criterion_sigma_I       ? 
_reflns.percent_possible_obs             99.6 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  3.0 
_reflns.pdbx_Rmerge_I_obs                0.123 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  ? 
_reflns.pdbx_netI_over_av_sigmaI         ? 
_reflns.pdbx_netI_over_sigmaI            4.3 
_reflns.pdbx_res_netI_over_av_sigmaI_2   ? 
_reflns.pdbx_res_netI_over_sigmaI_2      ? 
_reflns.pdbx_chi_squared                 ? 
_reflns.pdbx_scaling_rejects             ? 
_reflns.pdbx_d_res_high_opt              ? 
_reflns.pdbx_d_res_low_opt               ? 
_reflns.pdbx_d_res_opt_method            ? 
_reflns.phase_calculation_details        ? 
_reflns.pdbx_Rrim_I_all                  ? 
_reflns.pdbx_Rpim_I_all                  ? 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         ? 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     ? 
_reflns.pdbx_R_split                     ? 
# 
_reflns_shell.Rmerge_F_all                ? 
_reflns_shell.Rmerge_F_gt                 ? 
_reflns_shell.Rmerge_F_obs                ? 
_reflns_shell.Rmerge_I_all                ? 
_reflns_shell.Rmerge_I_gt                 ? 
_reflns_shell.Rmerge_I_obs                0.471 
_reflns_shell.d_res_high                  2.3 
_reflns_shell.d_res_low                   2.42 
_reflns_shell.meanI_over_sigI_all         ? 
_reflns_shell.meanI_over_sigI_gt          ? 
_reflns_shell.meanI_over_sigI_obs         ? 
_reflns_shell.meanI_over_uI_all           ? 
_reflns_shell.meanI_over_uI_gt            ? 
_reflns_shell.number_measured_all         ? 
_reflns_shell.number_measured_gt          ? 
_reflns_shell.number_measured_obs         ? 
_reflns_shell.number_possible             ? 
_reflns_shell.number_unique_all           ? 
_reflns_shell.number_unique_gt            ? 
_reflns_shell.number_unique_obs           ? 
_reflns_shell.pdbx_CC_half                ? 
_reflns_shell.pdbx_R_split                ? 
_reflns_shell.pdbx_Rpim_I_all             ? 
_reflns_shell.pdbx_Rrim_I_all             ? 
_reflns_shell.pdbx_Rsym_value             ? 
_reflns_shell.pdbx_chi_squared            ? 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_netI_over_sigmaI_all   ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs   ? 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.pdbx_redundancy             2.9 
_reflns_shell.pdbx_rejects                ? 
_reflns_shell.percent_possible_all        98.9 
_reflns_shell.percent_possible_gt         ? 
_reflns_shell.percent_possible_obs        ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 5CQG 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     91683 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             20.00 
_refine.ls_d_res_high                            2.30 
_refine.ls_percent_reflns_obs                    99.39 
_refine.ls_R_factor_obs                          0.23696 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.23504 
_refine.ls_R_factor_R_free                       0.27326 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_number_reflns_R_free                  4857 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.929 
_refine.correlation_coeff_Fo_to_Fc_free          0.905 
_refine.B_iso_mean                               61.957 
_refine.aniso_B[1][1]                            0.08 
_refine.aniso_B[2][2]                            2.70 
_refine.aniso_B[3][3]                            -2.78 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.01 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT' 
_refine.pdbx_starting_model                      3DU6 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.252 
_refine.pdbx_overall_ESU_R_Free                  0.216 
_refine.overall_SU_ML                            0.173 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             13.859 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        9964 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         50 
_refine_hist.number_atoms_solvent             409 
_refine_hist.number_atoms_total               10423 
_refine_hist.d_res_high                       2.30 
_refine_hist.d_res_low                        20.00 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.009  0.020  ? 10282 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.043  1.961  ? 13860 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       6.511  5.000  ? 1190  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       34.082 22.979 ? 470   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       18.885 15.000 ? 1922  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       15.695 15.000 ? 64    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.077  0.200  ? 1494  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.006  0.021  ? 7650  'X-RAY DIFFRACTION' ? 
r_gen_planes_other           ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_mcbond_it                  ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_mcangle_it                 ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_scbond_it                  ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_scbond_other               ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_scangle_other              ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_long_range_B_other         ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       2.300 
_refine_ls_shell.d_res_low                        2.359 
_refine_ls_shell.number_reflns_R_work             6464 
_refine_ls_shell.R_factor_R_work                  0.358 
_refine_ls_shell.percent_reflns_obs               98.38 
_refine_ls_shell.R_factor_R_free                  0.370 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             333 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.number_reflns_obs                ? 
# 
_struct.entry_id                     5CQG 
_struct.title                        'Structure of Tribolium telomerase in complex with the highly specific inhibitor BIBR1532' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               ? 
# 
_struct_keywords.entry_id        5CQG 
_struct_keywords.text            
'Telomerase Reverse transcriptase fold TERT BIBR15312, Telomerase Inhibitor, Transferase-Transferase inhibitor complex' 
_struct_keywords.pdbx_keywords   'Transferase/Transferase inhibitor' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 8   ? ARG A 12  ? SER A 8   ARG A 12  5 ? 5  
HELX_P HELX_P2  AA2 SER A 25  ? HIS A 40  ? SER A 25  HIS A 40  1 ? 16 
HELX_P HELX_P3  AA3 GLN A 47  ? ILE A 56  ? GLN A 47  ILE A 56  1 ? 10 
HELX_P HELX_P4  AA4 PRO A 57  ? PHE A 61  ? PRO A 57  PHE A 61  5 ? 5  
HELX_P HELX_P5  AA5 THR A 63  ? LEU A 78  ? THR A 63  LEU A 78  1 ? 16 
HELX_P HELX_P6  AA6 SER A 89  ? HIS A 92  ? SER A 89  HIS A 92  5 ? 4  
HELX_P HELX_P7  AA7 ASP A 96  ? GLN A 104 ? ASP A 96  GLN A 104 5 ? 9  
HELX_P HELX_P8  AA8 GLU A 107 ? ASN A 109 ? GLU A 107 ASN A 109 5 ? 3  
HELX_P HELX_P9  AA9 LEU A 110 ? ILE A 126 ? LEU A 110 ILE A 126 1 ? 17 
HELX_P HELX_P10 AB1 ILE A 126 ? TYR A 134 ? ILE A 126 TYR A 134 1 ? 9  
HELX_P HELX_P11 AB2 LYS A 151 ? LYS A 167 ? LYS A 151 LYS A 167 1 ? 17 
HELX_P HELX_P12 AB3 ARG A 205 ? GLU A 221 ? ARG A 205 GLU A 221 1 ? 17 
HELX_P HELX_P13 AB4 SER A 229 ? THR A 241 ? SER A 229 THR A 241 1 ? 13 
HELX_P HELX_P14 AB5 LYS A 260 ? SER A 270 ? LYS A 260 SER A 270 1 ? 11 
HELX_P HELX_P15 AB6 ASP A 277 ? SER A 289 ? ASP A 277 SER A 289 1 ? 13 
HELX_P HELX_P16 AB7 LEU A 312 ? PHE A 329 ? LEU A 312 PHE A 329 1 ? 18 
HELX_P HELX_P17 AB8 HIS A 351 ? TYR A 366 ? HIS A 351 TYR A 366 1 ? 16 
HELX_P HELX_P18 AB9 GLU A 412 ? PHE A 417 ? GLU A 412 PHE A 417 5 ? 6  
HELX_P HELX_P19 AC1 ASN A 430 ? ASP A 440 ? ASN A 430 ASP A 440 1 ? 11 
HELX_P HELX_P20 AC2 PHE A 441 ? PHE A 448 ? PHE A 441 PHE A 448 5 ? 8  
HELX_P HELX_P21 AC3 THR A 449 ? ASN A 454 ? THR A 449 ASN A 454 1 ? 6  
HELX_P HELX_P22 AC4 ASP A 459 ? SER A 488 ? ASP A 459 SER A 488 1 ? 30 
HELX_P HELX_P23 AC5 PHE A 496 ? TYR A 519 ? PHE A 496 TYR A 519 1 ? 24 
HELX_P HELX_P24 AC6 THR A 528 ? LYS A 545 ? THR A 528 LYS A 545 1 ? 18 
HELX_P HELX_P25 AC7 ARG A 547 ? GLU A 562 ? ARG A 547 GLU A 562 1 ? 16 
HELX_P HELX_P26 AC8 ASP A 574 ? LYS A 580 ? ASP A 574 LYS A 580 5 ? 7  
HELX_P HELX_P27 AC9 PRO A 582 ? PHE A 587 ? PRO A 582 PHE A 587 1 ? 6  
HELX_P HELX_P28 AD1 SER B 8   ? ARG B 12  ? SER B 8   ARG B 12  5 ? 5  
HELX_P HELX_P29 AD2 SER B 25  ? HIS B 40  ? SER B 25  HIS B 40  1 ? 16 
HELX_P HELX_P30 AD3 GLN B 47  ? ILE B 56  ? GLN B 47  ILE B 56  1 ? 10 
HELX_P HELX_P31 AD4 PRO B 57  ? PHE B 61  ? PRO B 57  PHE B 61  5 ? 5  
HELX_P HELX_P32 AD5 THR B 63  ? THR B 79  ? THR B 63  THR B 79  1 ? 17 
HELX_P HELX_P33 AD6 SER B 89  ? HIS B 92  ? SER B 89  HIS B 92  5 ? 4  
HELX_P HELX_P34 AD7 ILE B 100 ? GLN B 104 ? ILE B 100 GLN B 104 5 ? 5  
HELX_P HELX_P35 AD8 GLU B 107 ? ASN B 109 ? GLU B 107 ASN B 109 5 ? 3  
HELX_P HELX_P36 AD9 LEU B 110 ? ILE B 126 ? LEU B 110 ILE B 126 1 ? 17 
HELX_P HELX_P37 AE1 ILE B 126 ? TYR B 134 ? ILE B 126 TYR B 134 1 ? 9  
HELX_P HELX_P38 AE2 LYS B 151 ? LYS B 167 ? LYS B 151 LYS B 167 1 ? 17 
HELX_P HELX_P39 AE3 LYS B 206 ? LEU B 220 ? LYS B 206 LEU B 220 1 ? 15 
HELX_P HELX_P40 AE4 SER B 229 ? THR B 241 ? SER B 229 THR B 241 1 ? 13 
HELX_P HELX_P41 AE5 LYS B 260 ? GLN B 269 ? LYS B 260 GLN B 269 1 ? 10 
HELX_P HELX_P42 AE6 GLU B 279 ? ASN B 290 ? GLU B 279 ASN B 290 1 ? 12 
HELX_P HELX_P43 AE7 LEU B 312 ? PHE B 329 ? LEU B 312 PHE B 329 1 ? 18 
HELX_P HELX_P44 AE8 HIS B 351 ? TYR B 366 ? HIS B 351 TYR B 366 1 ? 16 
HELX_P HELX_P45 AE9 ASN B 369 ? THR B 373 ? ASN B 369 THR B 373 5 ? 5  
HELX_P HELX_P46 AF1 GLU B 412 ? PHE B 417 ? GLU B 412 PHE B 417 5 ? 6  
HELX_P HELX_P47 AF2 ASN B 430 ? ASP B 440 ? ASN B 430 ASP B 440 1 ? 11 
HELX_P HELX_P48 AF3 PHE B 441 ? PHE B 448 ? PHE B 441 PHE B 448 5 ? 8  
HELX_P HELX_P49 AF4 THR B 449 ? ASN B 454 ? THR B 449 ASN B 454 1 ? 6  
HELX_P HELX_P50 AF5 ASP B 459 ? SER B 488 ? ASP B 459 SER B 488 1 ? 30 
HELX_P HELX_P51 AF6 PHE B 496 ? TYR B 519 ? PHE B 496 TYR B 519 1 ? 24 
HELX_P HELX_P52 AF7 THR B 528 ? LYS B 545 ? THR B 528 LYS B 545 1 ? 18 
HELX_P HELX_P53 AF8 ARG B 547 ? GLU B 562 ? ARG B 547 GLU B 562 1 ? 16 
HELX_P HELX_P54 AF9 ASP B 574 ? CYS B 579 ? ASP B 574 CYS B 579 5 ? 6  
HELX_P HELX_P55 AG1 PRO B 582 ? PHE B 587 ? PRO B 582 PHE B 587 1 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 PHE 200 A . ? PHE 200 A PRO 201 A ? PRO 201 A 1 -3.36  
2 SER 270 A . ? SER 270 A ILE 271 A ? ILE 271 A 1 -10.53 
3 SER 289 A . ? SER 289 A ASN 290 A ? ASN 290 A 1 20.56  
4 TYR 405 A . ? TYR 405 A LYS 406 A ? LYS 406 A 1 11.85  
5 ASP 176 B . ? ASP 176 B GLU 177 B ? GLU 177 B 1 -9.59  
6 PHE 200 B . ? PHE 200 B PRO 201 B ? PRO 201 B 1 -0.23  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 2 ? 
AA3 ? 3 ? 
AA4 ? 2 ? 
AA5 ? 4 ? 
AA6 ? 3 ? 
AA7 ? 2 ? 
AA8 ? 2 ? 
AA9 ? 3 ? 
AB1 ? 2 ? 
AB2 ? 4 ? 
AB3 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB2 2 3 ? anti-parallel 
AB2 3 4 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 TYR A 4   ? ARG A 6   ? TYR A 4   ARG A 6   
AA1 2 CYS A 85  ? HIS A 87  ? CYS A 85  HIS A 87  
AA2 1 TYR A 135 ? LYS A 139 ? TYR A 135 LYS A 139 
AA2 2 ILE A 146 ? ARG A 150 ? ILE A 146 ARG A 150 
AA3 1 LEU A 171 ? GLU A 173 ? LEU A 171 GLU A 173 
AA3 2 ILE A 299 ? TRP A 302 ? ILE A 299 TRP A 302 
AA3 3 GLN A 291 ? ALA A 294 ? GLN A 291 ALA A 294 
AA4 1 VAL A 183 ? LYS A 189 ? VAL A 183 LYS A 189 
AA4 2 ASN A 192 ? SER A 198 ? ASN A 192 SER A 198 
AA5 1 PHE A 337 ? ARG A 340 ? PHE A 337 ARG A 340 
AA5 2 ASP A 344 ? SER A 349 ? ASP A 344 SER A 349 
AA5 3 TYR A 246 ? ASP A 251 ? TYR A 246 ASP A 251 
AA5 4 ARG A 374 ? THR A 375 ? ARG A 374 THR A 375 
AA6 1 GLU A 386 ? TYR A 389 ? GLU A 386 TYR A 389 
AA6 2 LYS A 392 ? ASN A 395 ? LYS A 392 ASN A 395 
AA6 3 VAL A 401 ? THR A 403 ? VAL A 401 THR A 403 
AA7 1 TYR B 4   ? ARG B 6   ? TYR B 4   ARG B 6   
AA7 2 CYS B 85  ? HIS B 87  ? CYS B 85  HIS B 87  
AA8 1 TYR B 135 ? LYS B 139 ? TYR B 135 LYS B 139 
AA8 2 ILE B 146 ? ARG B 150 ? ILE B 146 ARG B 150 
AA9 1 LEU B 171 ? GLU B 173 ? LEU B 171 GLU B 173 
AA9 2 ILE B 299 ? TRP B 302 ? ILE B 299 TRP B 302 
AA9 3 GLN B 291 ? ALA B 294 ? GLN B 291 ALA B 294 
AB1 1 VAL B 183 ? PRO B 188 ? VAL B 183 PRO B 188 
AB1 2 PHE B 193 ? SER B 198 ? PHE B 193 SER B 198 
AB2 1 PHE B 337 ? ARG B 340 ? PHE B 337 ARG B 340 
AB2 2 ASP B 344 ? SER B 349 ? ASP B 344 SER B 349 
AB2 3 TYR B 246 ? ASP B 251 ? TYR B 246 ASP B 251 
AB2 4 ARG B 374 ? THR B 375 ? ARG B 374 THR B 375 
AB3 1 GLU B 386 ? TYR B 389 ? GLU B 386 TYR B 389 
AB3 2 LYS B 392 ? ASN B 395 ? LYS B 392 ASN B 395 
AB3 3 VAL B 401 ? THR B 403 ? VAL B 401 THR B 403 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N TYR A 5   ? N TYR A 5   O ILE A 86  ? O ILE A 86  
AA2 1 2 N ILE A 138 ? N ILE A 138 O LYS A 147 ? O LYS A 147 
AA3 1 2 N VAL A 172 ? N VAL A 172 O LYS A 301 ? O LYS A 301 
AA3 2 3 O TRP A 302 ? O TRP A 302 N GLN A 291 ? N GLN A 291 
AA4 1 2 N ASN A 185 ? N ASN A 185 O ILE A 196 ? O ILE A 196 
AA5 1 2 N PHE A 337 ? N PHE A 337 O CYS A 348 ? O CYS A 348 
AA5 2 3 O SER A 349 ? O SER A 349 N TYR A 246 ? N TYR A 246 
AA5 3 4 N LYS A 249 ? N LYS A 249 O ARG A 374 ? O ARG A 374 
AA6 1 2 N ILE A 387 ? N ILE A 387 O PHE A 394 ? O PHE A 394 
AA6 2 3 N ILE A 393 ? N ILE A 393 O ARG A 402 ? O ARG A 402 
AA7 1 2 N TYR B 5   ? N TYR B 5   O ILE B 86  ? O ILE B 86  
AA8 1 2 N LYS B 136 ? N LYS B 136 O ILE B 149 ? O ILE B 149 
AA9 1 2 N VAL B 172 ? N VAL B 172 O LYS B 301 ? O LYS B 301 
AA9 2 3 O TRP B 302 ? O TRP B 302 N GLN B 291 ? N GLN B 291 
AB1 1 2 N ASN B 185 ? N ASN B 185 O ILE B 196 ? O ILE B 196 
AB2 1 2 N PHE B 337 ? N PHE B 337 O CYS B 348 ? O CYS B 348 
AB2 2 3 O TYR B 345 ? O TYR B 345 N VAL B 250 ? N VAL B 250 
AB2 3 4 N LYS B 249 ? N LYS B 249 O ARG B 374 ? O ARG B 374 
AB3 1 2 N TYR B 389 ? N TYR B 389 O LYS B 392 ? O LYS B 392 
AB3 2 3 N ILE B 393 ? N ILE B 393 O ARG B 402 ? O ARG B 402 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A 55C 601 ? 8  'binding site for residue 55C A 601' 
AC2 Software B 55C 601 ? 10 'binding site for residue 55C B 601' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 8  MET A 483 ? MET A 483 . ? 1_555 ? 
2  AC1 8  ARG A 486 ? ARG A 486 . ? 1_555 ? 
3  AC1 8  PHE A 494 ? PHE A 494 . ? 1_555 ? 
4  AC1 8  ILE A 550 ? ILE A 550 . ? 1_555 ? 
5  AC1 8  TYR A 551 ? TYR A 551 . ? 1_555 ? 
6  AC1 8  LEU A 554 ? LEU A 554 . ? 1_555 ? 
7  AC1 8  ARG A 557 ? ARG A 557 . ? 1_555 ? 
8  AC1 8  HOH E .   ? HOH A 784 . ? 1_555 ? 
9  AC2 10 MET B 483 ? MET B 483 . ? 1_555 ? 
10 AC2 10 ARG B 486 ? ARG B 486 . ? 1_555 ? 
11 AC2 10 PHE B 494 ? PHE B 494 . ? 1_555 ? 
12 AC2 10 ILE B 550 ? ILE B 550 . ? 1_555 ? 
13 AC2 10 TYR B 551 ? TYR B 551 . ? 1_555 ? 
14 AC2 10 GLY B 553 ? GLY B 553 . ? 1_555 ? 
15 AC2 10 LEU B 554 ? LEU B 554 . ? 1_555 ? 
16 AC2 10 ARG B 557 ? ARG B 557 . ? 1_555 ? 
17 AC2 10 HOH F .   ? HOH B 735 . ? 1_555 ? 
18 AC2 10 HOH F .   ? HOH B 841 . ? 1_555 ? 
# 
_atom_sites.entry_id                    5CQG 
_atom_sites.fract_transf_matrix[1][1]   0.008495 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.004180 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011778 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.009036 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N N   . MET A 1 1   ? 21.546  28.956  -51.201 1.00 70.61  ? 1   MET A N   1 
ATOM   2     C CA  . MET A 1 1   ? 20.194  28.325  -51.232 1.00 67.59  ? 1   MET A CA  1 
ATOM   3     C C   . MET A 1 1   ? 20.265  26.786  -51.302 1.00 61.73  ? 1   MET A C   1 
ATOM   4     O O   . MET A 1 1   ? 19.755  26.102  -50.407 1.00 62.98  ? 1   MET A O   1 
ATOM   5     C CB  . MET A 1 1   ? 19.352  28.895  -52.394 1.00 71.70  ? 1   MET A CB  1 
ATOM   6     C CG  . MET A 1 1   ? 17.917  28.361  -52.458 1.00 76.51  ? 1   MET A CG  1 
ATOM   7     S SD  . MET A 1 1   ? 16.845  29.111  -53.717 1.00 81.54  ? 1   MET A SD  1 
ATOM   8     C CE  . MET A 1 1   ? 17.455  28.369  -55.232 1.00 72.65  ? 1   MET A CE  1 
ATOM   9     N N   . VAL A 1 2   ? 20.912  26.250  -52.342 1.00 56.42  ? 2   VAL A N   1 
ATOM   10    C CA  . VAL A 1 2   ? 20.817  24.800  -52.661 1.00 50.54  ? 2   VAL A CA  1 
ATOM   11    C C   . VAL A 1 2   ? 21.791  23.909  -51.897 1.00 45.98  ? 2   VAL A C   1 
ATOM   12    O O   . VAL A 1 2   ? 23.007  24.066  -52.020 1.00 48.84  ? 2   VAL A O   1 
ATOM   13    C CB  . VAL A 1 2   ? 20.948  24.530  -54.172 1.00 49.90  ? 2   VAL A CB  1 
ATOM   14    C CG1 . VAL A 1 2   ? 20.835  23.038  -54.459 1.00 48.57  ? 2   VAL A CG1 1 
ATOM   15    C CG2 . VAL A 1 2   ? 19.871  25.295  -54.935 1.00 52.76  ? 2   VAL A CG2 1 
ATOM   16    N N   . HIS A 1 3   ? 21.245  22.947  -51.145 1.00 41.25  ? 3   HIS A N   1 
ATOM   17    C CA  . HIS A 1 3   ? 22.043  22.044  -50.310 1.00 37.63  ? 3   HIS A CA  1 
ATOM   18    C C   . HIS A 1 3   ? 21.996  20.608  -50.768 1.00 34.11  ? 3   HIS A C   1 
ATOM   19    O O   . HIS A 1 3   ? 22.870  19.823  -50.420 1.00 30.51  ? 3   HIS A O   1 
ATOM   20    C CB  . HIS A 1 3   ? 21.581  22.108  -48.854 1.00 39.77  ? 3   HIS A CB  1 
ATOM   21    C CG  . HIS A 1 3   ? 21.731  23.472  -48.223 1.00 42.36  ? 3   HIS A CG  1 
ATOM   22    N ND1 . HIS A 1 3   ? 20.670  24.242  -47.900 1.00 43.03  ? 3   HIS A ND1 1 
ATOM   23    C CD2 . HIS A 1 3   ? 22.864  24.200  -47.874 1.00 42.08  ? 3   HIS A CD2 1 
ATOM   24    C CE1 . HIS A 1 3   ? 21.101  25.397  -47.367 1.00 43.39  ? 3   HIS A CE1 1 
ATOM   25    N NE2 . HIS A 1 3   ? 22.444  25.373  -47.354 1.00 43.55  ? 3   HIS A NE2 1 
ATOM   26    N N   . TYR A 1 4   ? 20.979  20.270  -51.560 1.00 32.27  ? 4   TYR A N   1 
ATOM   27    C CA  . TYR A 1 4   ? 20.626  18.887  -51.867 1.00 31.67  ? 4   TYR A CA  1 
ATOM   28    C C   . TYR A 1 4   ? 20.924  18.490  -53.320 1.00 33.12  ? 4   TYR A C   1 
ATOM   29    O O   . TYR A 1 4   ? 20.712  19.265  -54.254 1.00 32.78  ? 4   TYR A O   1 
ATOM   30    C CB  . TYR A 1 4   ? 19.117  18.658  -51.653 1.00 30.41  ? 4   TYR A CB  1 
ATOM   31    C CG  . TYR A 1 4   ? 18.585  18.713  -50.242 1.00 28.58  ? 4   TYR A CG  1 
ATOM   32    C CD1 . TYR A 1 4   ? 19.439  18.799  -49.129 1.00 29.02  ? 4   TYR A CD1 1 
ATOM   33    C CD2 . TYR A 1 4   ? 17.218  18.611  -50.015 1.00 27.90  ? 4   TYR A CD2 1 
ATOM   34    C CE1 . TYR A 1 4   ? 18.928  18.833  -47.831 1.00 28.23  ? 4   TYR A CE1 1 
ATOM   35    C CE2 . TYR A 1 4   ? 16.698  18.648  -48.734 1.00 28.18  ? 4   TYR A CE2 1 
ATOM   36    C CZ  . TYR A 1 4   ? 17.553  18.761  -47.643 1.00 28.67  ? 4   TYR A CZ  1 
ATOM   37    O OH  . TYR A 1 4   ? 17.021  18.798  -46.378 1.00 27.77  ? 4   TYR A OH  1 
ATOM   38    N N   . TYR A 1 5   ? 21.354  17.252  -53.497 1.00 33.53  ? 5   TYR A N   1 
ATOM   39    C CA  . TYR A 1 5   ? 21.326  16.601  -54.799 1.00 33.44  ? 5   TYR A CA  1 
ATOM   40    C C   . TYR A 1 5   ? 20.202  15.560  -54.760 1.00 33.09  ? 5   TYR A C   1 
ATOM   41    O O   . TYR A 1 5   ? 20.089  14.792  -53.812 1.00 34.18  ? 5   TYR A O   1 
ATOM   42    C CB  . TYR A 1 5   ? 22.683  15.945  -55.080 1.00 34.15  ? 5   TYR A CB  1 
ATOM   43    C CG  . TYR A 1 5   ? 22.758  15.140  -56.366 1.00 35.03  ? 5   TYR A CG  1 
ATOM   44    C CD1 . TYR A 1 5   ? 22.721  15.769  -57.624 1.00 34.73  ? 5   TYR A CD1 1 
ATOM   45    C CD2 . TYR A 1 5   ? 22.883  13.744  -56.329 1.00 34.81  ? 5   TYR A CD2 1 
ATOM   46    C CE1 . TYR A 1 5   ? 22.794  15.032  -58.799 1.00 34.05  ? 5   TYR A CE1 1 
ATOM   47    C CE2 . TYR A 1 5   ? 22.969  12.994  -57.505 1.00 35.44  ? 5   TYR A CE2 1 
ATOM   48    C CZ  . TYR A 1 5   ? 22.919  13.636  -58.730 1.00 36.19  ? 5   TYR A CZ  1 
ATOM   49    O OH  . TYR A 1 5   ? 22.993  12.880  -59.883 1.00 39.11  ? 5   TYR A OH  1 
ATOM   50    N N   . ARG A 1 6   ? 19.327  15.592  -55.735 1.00 31.39  ? 6   ARG A N   1 
ATOM   51    C CA  . ARG A 1 6   ? 18.213  14.692  -55.737 1.00 32.27  ? 6   ARG A CA  1 
ATOM   52    C C   . ARG A 1 6   ? 18.669  13.364  -56.285 1.00 32.65  ? 6   ARG A C   1 
ATOM   53    O O   . ARG A 1 6   ? 19.452  13.337  -57.236 1.00 32.92  ? 6   ARG A O   1 
ATOM   54    C CB  . ARG A 1 6   ? 17.111  15.249  -56.626 1.00 34.90  ? 6   ARG A CB  1 
ATOM   55    C CG  . ARG A 1 6   ? 16.294  16.329  -55.974 1.00 35.77  ? 6   ARG A CG  1 
ATOM   56    C CD  . ARG A 1 6   ? 15.366  16.976  -56.974 1.00 39.65  ? 6   ARG A CD  1 
ATOM   57    N NE  . ARG A 1 6   ? 16.091  17.470  -58.140 1.00 45.49  ? 6   ARG A NE  1 
ATOM   58    C CZ  . ARG A 1 6   ? 15.604  18.353  -59.008 1.00 46.67  ? 6   ARG A CZ  1 
ATOM   59    N NH1 . ARG A 1 6   ? 14.382  18.850  -58.838 1.00 49.35  ? 6   ARG A NH1 1 
ATOM   60    N NH2 . ARG A 1 6   ? 16.337  18.733  -60.045 1.00 45.56  ? 6   ARG A NH2 1 
ATOM   61    N N   . LEU A 1 7   ? 18.202  12.264  -55.691 1.00 31.10  ? 7   LEU A N   1 
ATOM   62    C CA  . LEU A 1 7   ? 18.614  10.908  -56.148 1.00 30.92  ? 7   LEU A CA  1 
ATOM   63    C C   . LEU A 1 7   ? 17.840  10.391  -57.376 1.00 32.22  ? 7   LEU A C   1 
ATOM   64    O O   . LEU A 1 7   ? 18.259  9.411   -58.026 1.00 32.82  ? 7   LEU A O   1 
ATOM   65    C CB  . LEU A 1 7   ? 18.532  9.884   -55.013 1.00 28.52  ? 7   LEU A CB  1 
ATOM   66    C CG  . LEU A 1 7   ? 19.307  10.112  -53.696 1.00 28.42  ? 7   LEU A CG  1 
ATOM   67    C CD1 . LEU A 1 7   ? 19.167  8.882   -52.801 1.00 27.72  ? 7   LEU A CD1 1 
ATOM   68    C CD2 . LEU A 1 7   ? 20.785  10.452  -53.904 1.00 27.51  ? 7   LEU A CD2 1 
ATOM   69    N N   . SER A 1 8   ? 16.734  11.054  -57.702 1.00 33.12  ? 8   SER A N   1 
ATOM   70    C CA  . SER A 1 8   ? 15.867  10.626  -58.804 1.00 35.35  ? 8   SER A CA  1 
ATOM   71    C C   . SER A 1 8   ? 16.582  10.555  -60.160 1.00 36.58  ? 8   SER A C   1 
ATOM   72    O O   . SER A 1 8   ? 17.354  11.445  -60.532 1.00 34.04  ? 8   SER A O   1 
ATOM   73    C CB  . SER A 1 8   ? 14.650  11.547  -58.925 1.00 37.75  ? 8   SER A CB  1 
ATOM   74    O OG  . SER A 1 8   ? 13.783  11.111  -59.961 1.00 40.65  ? 8   SER A OG  1 
ATOM   75    N N   . LEU A 1 9   ? 16.294  9.488   -60.890 1.00 37.96  ? 9   LEU A N   1 
ATOM   76    C CA  . LEU A 1 9   ? 16.810  9.285   -62.228 1.00 40.42  ? 9   LEU A CA  1 
ATOM   77    C C   . LEU A 1 9   ? 16.289  10.367  -63.180 1.00 44.40  ? 9   LEU A C   1 
ATOM   78    O O   . LEU A 1 9   ? 16.988  10.778  -64.104 1.00 46.13  ? 9   LEU A O   1 
ATOM   79    C CB  . LEU A 1 9   ? 16.400  7.897   -62.720 1.00 37.86  ? 9   LEU A CB  1 
ATOM   80    C CG  . LEU A 1 9   ? 17.456  6.793   -62.688 1.00 36.95  ? 9   LEU A CG  1 
ATOM   81    C CD1 . LEU A 1 9   ? 18.282  6.802   -61.404 1.00 33.58  ? 9   LEU A CD1 1 
ATOM   82    C CD2 . LEU A 1 9   ? 16.812  5.428   -62.946 1.00 35.22  ? 9   LEU A CD2 1 
ATOM   83    N N   . LYS A 1 10  ? 15.076  10.851  -62.909 1.00 47.39  ? 10  LYS A N   1 
ATOM   84    C CA  . LYS A 1 10  ? 14.403  11.863  -63.733 1.00 49.73  ? 10  LYS A CA  1 
ATOM   85    C C   . LYS A 1 10  ? 15.274  13.056  -64.100 1.00 48.83  ? 10  LYS A C   1 
ATOM   86    O O   . LYS A 1 10  ? 15.064  13.691  -65.136 1.00 51.11  ? 10  LYS A O   1 
ATOM   87    C CB  . LYS A 1 10  ? 13.119  12.347  -63.045 1.00 53.98  ? 10  LYS A CB  1 
ATOM   88    C CG  . LYS A 1 10  ? 11.986  11.331  -63.079 1.00 59.34  ? 10  LYS A CG  1 
ATOM   89    C CD  . LYS A 1 10  ? 10.774  11.797  -62.286 1.00 61.89  ? 10  LYS A CD  1 
ATOM   90    C CE  . LYS A 1 10  ? 9.747   10.676  -62.168 1.00 66.37  ? 10  LYS A CE  1 
ATOM   91    N NZ  . LYS A 1 10  ? 8.424   11.158  -61.670 1.00 69.56  ? 10  LYS A NZ  1 
ATOM   92    N N   . SER A 1 11  ? 16.253  13.360  -63.260 1.00 47.23  ? 11  SER A N   1 
ATOM   93    C CA  . SER A 1 11  ? 17.115  14.516  -63.501 1.00 48.49  ? 11  SER A CA  1 
ATOM   94    C C   . SER A 1 11  ? 18.412  14.188  -64.253 1.00 47.04  ? 11  SER A C   1 
ATOM   95    O O   . SER A 1 11  ? 19.265  15.063  -64.413 1.00 46.31  ? 11  SER A O   1 
ATOM   96    C CB  . SER A 1 11  ? 17.431  15.230  -62.192 1.00 45.58  ? 11  SER A CB  1 
ATOM   97    O OG  . SER A 1 11  ? 17.692  14.285  -61.173 1.00 45.96  ? 11  SER A OG  1 
ATOM   98    N N   . ARG A 1 12  ? 18.556  12.946  -64.721 1.00 45.57  ? 12  ARG A N   1 
ATOM   99    C CA  . ARG A 1 12  ? 19.778  12.544  -65.453 1.00 46.49  ? 12  ARG A CA  1 
ATOM   100   C C   . ARG A 1 12  ? 19.947  13.361  -66.716 1.00 49.14  ? 12  ARG A C   1 
ATOM   101   O O   . ARG A 1 12  ? 18.968  13.877  -67.270 1.00 51.59  ? 12  ARG A O   1 
ATOM   102   C CB  . ARG A 1 12  ? 19.769  11.047  -65.809 1.00 42.91  ? 12  ARG A CB  1 
ATOM   103   C CG  . ARG A 1 12  ? 18.732  10.633  -66.843 1.00 41.15  ? 12  ARG A CG  1 
ATOM   104   C CD  . ARG A 1 12  ? 18.392  9.172   -66.676 1.00 41.95  ? 12  ARG A CD  1 
ATOM   105   N NE  . ARG A 1 12  ? 17.571  8.632   -67.763 1.00 42.68  ? 12  ARG A NE  1 
ATOM   106   C CZ  . ARG A 1 12  ? 16.246  8.520   -67.724 1.00 41.39  ? 12  ARG A CZ  1 
ATOM   107   N NH1 . ARG A 1 12  ? 15.560  8.928   -66.661 1.00 40.16  ? 12  ARG A NH1 1 
ATOM   108   N NH2 . ARG A 1 12  ? 15.606  8.001   -68.754 1.00 41.71  ? 12  ARG A NH2 1 
ATOM   109   N N   . GLN A 1 13  ? 21.185  13.462  -67.186 1.00 48.91  ? 13  GLN A N   1 
ATOM   110   C CA  . GLN A 1 13  ? 21.450  14.130  -68.445 1.00 50.28  ? 13  GLN A CA  1 
ATOM   111   C C   . GLN A 1 13  ? 21.881  13.158  -69.535 1.00 50.23  ? 13  GLN A C   1 
ATOM   112   O O   . GLN A 1 13  ? 22.371  12.068  -69.247 1.00 46.85  ? 13  GLN A O   1 
ATOM   113   C CB  . GLN A 1 13  ? 22.467  15.258  -68.254 1.00 52.66  ? 13  GLN A CB  1 
ATOM   114   C CG  . GLN A 1 13  ? 21.846  16.553  -67.722 1.00 57.31  ? 13  GLN A CG  1 
ATOM   115   C CD  . GLN A 1 13  ? 22.826  17.404  -66.927 1.00 58.30  ? 13  GLN A CD  1 
ATOM   116   O OE1 . GLN A 1 13  ? 22.511  17.859  -65.824 1.00 58.04  ? 13  GLN A OE1 1 
ATOM   117   N NE2 . GLN A 1 13  ? 24.031  17.619  -67.482 1.00 55.71  ? 13  GLN A NE2 1 
ATOM   118   N N   . LYS A 1 14  ? 21.628  13.550  -70.786 1.00 54.12  ? 14  LYS A N   1 
ATOM   119   C CA  . LYS A 1 14  ? 22.171  12.882  -71.962 1.00 55.79  ? 14  LYS A CA  1 
ATOM   120   C C   . LYS A 1 14  ? 23.646  13.270  -72.109 1.00 55.34  ? 14  LYS A C   1 
ATOM   121   O O   . LYS A 1 14  ? 23.971  14.448  -72.263 1.00 58.59  ? 14  LYS A O   1 
ATOM   122   C CB  . LYS A 1 14  ? 21.374  13.292  -73.210 1.00 58.91  ? 14  LYS A CB  1 
ATOM   123   C CG  . LYS A 1 14  ? 21.901  12.707  -74.511 1.00 62.25  ? 14  LYS A CG  1 
ATOM   124   C CD  . LYS A 1 14  ? 20.993  13.038  -75.680 1.00 66.22  ? 14  LYS A CD  1 
ATOM   125   C CE  . LYS A 1 14  ? 21.509  12.422  -76.976 1.00 69.66  ? 14  LYS A CE  1 
ATOM   126   N NZ  . LYS A 1 14  ? 20.550  12.642  -78.100 1.00 72.22  ? 14  LYS A NZ  1 
ATOM   127   N N   . ALA A 1 15  ? 24.534  12.281  -72.028 1.00 53.07  ? 15  ALA A N   1 
ATOM   128   C CA  . ALA A 1 15  ? 25.988  12.538  -72.032 1.00 50.22  ? 15  ALA A CA  1 
ATOM   129   C C   . ALA A 1 15  ? 26.471  13.025  -73.379 1.00 49.39  ? 15  ALA A C   1 
ATOM   130   O O   . ALA A 1 15  ? 26.079  12.476  -74.404 1.00 49.58  ? 15  ALA A O   1 
ATOM   131   C CB  . ALA A 1 15  ? 26.755  11.281  -71.644 1.00 46.97  ? 15  ALA A CB  1 
ATOM   132   N N   . PRO A 1 16  ? 27.343  14.047  -73.383 1.00 48.73  ? 16  PRO A N   1 
ATOM   133   C CA  . PRO A 1 16  ? 28.066  14.414  -74.604 1.00 49.86  ? 16  PRO A CA  1 
ATOM   134   C C   . PRO A 1 16  ? 29.022  13.295  -74.987 1.00 51.43  ? 16  PRO A C   1 
ATOM   135   O O   . PRO A 1 16  ? 29.180  12.336  -74.212 1.00 47.72  ? 16  PRO A O   1 
ATOM   136   C CB  . PRO A 1 16  ? 28.869  15.647  -74.176 1.00 49.77  ? 16  PRO A CB  1 
ATOM   137   C CG  . PRO A 1 16  ? 29.030  15.496  -72.690 1.00 48.64  ? 16  PRO A CG  1 
ATOM   138   C CD  . PRO A 1 16  ? 27.755  14.861  -72.224 1.00 47.17  ? 16  PRO A CD  1 
ATOM   139   N N   . LYS A 1 17  ? 29.653  13.410  -76.164 1.00 52.28  ? 17  LYS A N   1 
ATOM   140   C CA  . LYS A 1 17  ? 30.721  12.488  -76.558 1.00 51.67  ? 17  LYS A CA  1 
ATOM   141   C C   . LYS A 1 17  ? 32.004  12.759  -75.790 1.00 49.83  ? 17  LYS A C   1 
ATOM   142   O O   . LYS A 1 17  ? 32.617  11.836  -75.265 1.00 49.81  ? 17  LYS A O   1 
ATOM   143   C CB  . LYS A 1 17  ? 30.977  12.522  -78.074 1.00 55.49  ? 17  LYS A CB  1 
ATOM   144   C CG  . LYS A 1 17  ? 29.879  11.881  -78.925 1.00 58.24  ? 17  LYS A CG  1 
ATOM   145   C CD  . LYS A 1 17  ? 29.266  10.652  -78.253 1.00 57.60  ? 17  LYS A CD  1 
ATOM   146   C CE  . LYS A 1 17  ? 28.571  9.755   -79.266 1.00 58.99  ? 17  LYS A CE  1 
ATOM   147   N NZ  . LYS A 1 17  ? 29.565  8.987   -80.075 1.00 58.60  ? 17  LYS A NZ  1 
ATOM   148   N N   . ILE A 1 18  ? 32.414  14.021  -75.736 1.00 50.80  ? 18  ILE A N   1 
ATOM   149   C CA  . ILE A 1 18  ? 33.549  14.436  -74.897 1.00 51.56  ? 18  ILE A CA  1 
ATOM   150   C C   . ILE A 1 18  ? 33.156  15.660  -74.055 1.00 53.54  ? 18  ILE A C   1 
ATOM   151   O O   . ILE A 1 18  ? 32.062  16.198  -74.220 1.00 52.25  ? 18  ILE A O   1 
ATOM   152   C CB  . ILE A 1 18  ? 34.854  14.694  -75.725 1.00 53.58  ? 18  ILE A CB  1 
ATOM   153   C CG1 . ILE A 1 18  ? 34.718  15.931  -76.638 1.00 53.54  ? 18  ILE A CG1 1 
ATOM   154   C CG2 . ILE A 1 18  ? 35.265  13.443  -76.513 1.00 50.79  ? 18  ILE A CG2 1 
ATOM   155   C CD1 . ILE A 1 18  ? 36.016  16.360  -77.316 1.00 52.67  ? 18  ILE A CD1 1 
ATOM   156   N N   . VAL A 1 19  ? 34.026  16.075  -73.135 1.00 55.96  ? 19  VAL A N   1 
ATOM   157   C CA  . VAL A 1 19  ? 33.716  17.212  -72.259 1.00 59.76  ? 19  VAL A CA  1 
ATOM   158   C C   . VAL A 1 19  ? 34.286  18.530  -72.789 1.00 65.37  ? 19  VAL A C   1 
ATOM   159   O O   . VAL A 1 19  ? 35.095  18.531  -73.725 1.00 70.83  ? 19  VAL A O   1 
ATOM   160   C CB  . VAL A 1 19  ? 34.154  16.966  -70.792 1.00 57.94  ? 19  VAL A CB  1 
ATOM   161   C CG1 . VAL A 1 19  ? 33.376  15.801  -70.197 1.00 57.32  ? 19  VAL A CG1 1 
ATOM   162   C CG2 . VAL A 1 19  ? 35.652  16.722  -70.688 1.00 55.99  ? 19  VAL A CG2 1 
ATOM   163   N N   . ASN A 1 20  ? 33.856  19.644  -72.194 1.00 69.80  ? 20  ASN A N   1 
ATOM   164   C CA  . ASN A 1 20  ? 34.269  20.982  -72.645 1.00 78.91  ? 20  ASN A CA  1 
ATOM   165   C C   . ASN A 1 20  ? 35.495  21.544  -71.905 1.00 81.45  ? 20  ASN A C   1 
ATOM   166   O O   . ASN A 1 20  ? 36.254  20.796  -71.283 1.00 80.78  ? 20  ASN A O   1 
ATOM   167   C CB  . ASN A 1 20  ? 33.088  21.963  -72.584 1.00 81.92  ? 20  ASN A CB  1 
ATOM   168   C CG  . ASN A 1 20  ? 32.413  21.981  -71.228 1.00 82.92  ? 20  ASN A CG  1 
ATOM   169   O OD1 . ASN A 1 20  ? 32.796  22.740  -70.342 1.00 84.46  ? 20  ASN A OD1 1 
ATOM   170   N ND2 . ASN A 1 20  ? 31.395  21.143  -71.062 1.00 85.58  ? 20  ASN A ND2 1 
ATOM   171   N N   . SER A 1 21  ? 35.685  22.860  -71.987 1.00 85.70  ? 21  SER A N   1 
ATOM   172   C CA  . SER A 1 21  ? 36.839  23.518  -71.365 1.00 87.07  ? 21  SER A CA  1 
ATOM   173   C C   . SER A 1 21  ? 36.878  23.351  -69.850 1.00 82.72  ? 21  SER A C   1 
ATOM   174   O O   . SER A 1 21  ? 37.955  23.322  -69.253 1.00 83.26  ? 21  SER A O   1 
ATOM   175   C CB  . SER A 1 21  ? 36.867  25.008  -71.718 1.00 89.61  ? 21  SER A CB  1 
ATOM   176   O OG  . SER A 1 21  ? 37.512  25.221  -72.959 1.00 94.37  ? 21  SER A OG  1 
ATOM   177   N N   . LYS A 1 22  ? 35.700  23.234  -69.243 1.00 80.11  ? 22  LYS A N   1 
ATOM   178   C CA  . LYS A 1 22  ? 35.561  23.217  -67.787 1.00 76.30  ? 22  LYS A CA  1 
ATOM   179   C C   . LYS A 1 22  ? 36.137  21.956  -67.140 1.00 72.13  ? 22  LYS A C   1 
ATOM   180   O O   . LYS A 1 22  ? 36.823  22.030  -66.113 1.00 72.09  ? 22  LYS A O   1 
ATOM   181   C CB  . LYS A 1 22  ? 34.089  23.375  -67.399 1.00 78.57  ? 22  LYS A CB  1 
ATOM   182   C CG  . LYS A 1 22  ? 33.531  24.784  -67.570 1.00 82.32  ? 22  LYS A CG  1 
ATOM   183   C CD  . LYS A 1 22  ? 32.034  24.762  -67.859 1.00 81.07  ? 22  LYS A CD  1 
ATOM   184   C CE  . LYS A 1 22  ? 31.259  24.023  -66.779 1.00 78.05  ? 22  LYS A CE  1 
ATOM   185   N NZ  . LYS A 1 22  ? 29.999  23.438  -67.316 1.00 79.30  ? 22  LYS A NZ  1 
ATOM   186   N N   . TYR A 1 23  ? 35.864  20.807  -67.752 1.00 66.83  ? 23  TYR A N   1 
ATOM   187   C CA  . TYR A 1 23  ? 36.139  19.513  -67.128 1.00 60.24  ? 23  TYR A CA  1 
ATOM   188   C C   . TYR A 1 23  ? 37.478  18.919  -67.526 1.00 58.31  ? 23  TYR A C   1 
ATOM   189   O O   . TYR A 1 23  ? 37.940  19.100  -68.656 1.00 58.65  ? 23  TYR A O   1 
ATOM   190   C CB  . TYR A 1 23  ? 35.041  18.521  -67.469 1.00 56.69  ? 23  TYR A CB  1 
ATOM   191   C CG  . TYR A 1 23  ? 33.672  18.898  -66.970 1.00 56.55  ? 23  TYR A CG  1 
ATOM   192   C CD1 . TYR A 1 23  ? 33.345  18.781  -65.621 1.00 54.84  ? 23  TYR A CD1 1 
ATOM   193   C CD2 . TYR A 1 23  ? 32.685  19.332  -67.856 1.00 57.35  ? 23  TYR A CD2 1 
ATOM   194   C CE1 . TYR A 1 23  ? 32.080  19.097  -65.163 1.00 54.77  ? 23  TYR A CE1 1 
ATOM   195   C CE2 . TYR A 1 23  ? 31.417  19.657  -67.409 1.00 55.51  ? 23  TYR A CE2 1 
ATOM   196   C CZ  . TYR A 1 23  ? 31.119  19.534  -66.063 1.00 56.75  ? 23  TYR A CZ  1 
ATOM   197   O OH  . TYR A 1 23  ? 29.859  19.848  -65.611 1.00 59.89  ? 23  TYR A OH  1 
ATOM   198   N N   . ASN A 1 24  ? 38.081  18.181  -66.596 1.00 52.89  ? 24  ASN A N   1 
ATOM   199   C CA  . ASN A 1 24  ? 39.291  17.439  -66.873 1.00 48.25  ? 24  ASN A CA  1 
ATOM   200   C C   . ASN A 1 24  ? 39.019  16.308  -67.854 1.00 50.31  ? 24  ASN A C   1 
ATOM   201   O O   . ASN A 1 24  ? 37.966  15.662  -67.797 1.00 48.27  ? 24  ASN A O   1 
ATOM   202   C CB  . ASN A 1 24  ? 39.889  16.895  -65.579 1.00 47.44  ? 24  ASN A CB  1 
ATOM   203   C CG  . ASN A 1 24  ? 41.246  16.262  -65.783 1.00 47.62  ? 24  ASN A CG  1 
ATOM   204   O OD1 . ASN A 1 24  ? 41.371  15.239  -66.454 1.00 49.00  ? 24  ASN A OD1 1 
ATOM   205   N ND2 . ASN A 1 24  ? 42.273  16.860  -65.195 1.00 46.11  ? 24  ASN A ND2 1 
ATOM   206   N N   . SER A 1 25  ? 39.987  16.076  -68.746 1.00 48.99  ? 25  SER A N   1 
ATOM   207   C CA  . SER A 1 25  ? 39.883  15.080  -69.806 1.00 46.96  ? 25  SER A CA  1 
ATOM   208   C C   . SER A 1 25  ? 39.624  13.662  -69.333 1.00 42.99  ? 25  SER A C   1 
ATOM   209   O O   . SER A 1 25  ? 39.164  12.826  -70.106 1.00 42.28  ? 25  SER A O   1 
ATOM   210   C CB  . SER A 1 25  ? 41.155  15.085  -70.653 1.00 47.82  ? 25  SER A CB  1 
ATOM   211   O OG  . SER A 1 25  ? 41.059  16.063  -71.657 1.00 52.28  ? 25  SER A OG  1 
ATOM   212   N N   . ILE A 1 26  ? 39.958  13.374  -68.084 1.00 41.48  ? 26  ILE A N   1 
ATOM   213   C CA  . ILE A 1 26  ? 39.720  12.040  -67.531 1.00 40.59  ? 26  ILE A CA  1 
ATOM   214   C C   . ILE A 1 26  ? 38.247  11.591  -67.708 1.00 39.53  ? 26  ILE A C   1 
ATOM   215   O O   . ILE A 1 26  ? 37.967  10.410  -67.914 1.00 40.52  ? 26  ILE A O   1 
ATOM   216   C CB  . ILE A 1 26  ? 40.189  11.937  -66.065 1.00 38.88  ? 26  ILE A CB  1 
ATOM   217   C CG1 . ILE A 1 26  ? 40.333  10.466  -65.645 1.00 39.52  ? 26  ILE A CG1 1 
ATOM   218   C CG2 . ILE A 1 26  ? 39.258  12.722  -65.145 1.00 38.07  ? 26  ILE A CG2 1 
ATOM   219   C CD1 . ILE A 1 26  ? 41.131  10.266  -64.367 1.00 41.02  ? 26  ILE A CD1 1 
ATOM   220   N N   . LEU A 1 27  ? 37.327  12.550  -67.705 1.00 39.39  ? 27  LEU A N   1 
ATOM   221   C CA  . LEU A 1 27  ? 35.912  12.257  -67.912 1.00 39.19  ? 27  LEU A CA  1 
ATOM   222   C C   . LEU A 1 27  ? 35.590  11.677  -69.293 1.00 39.52  ? 27  LEU A C   1 
ATOM   223   O O   . LEU A 1 27  ? 34.622  10.928  -69.442 1.00 40.60  ? 27  LEU A O   1 
ATOM   224   C CB  . LEU A 1 27  ? 35.060  13.487  -67.653 1.00 38.75  ? 27  LEU A CB  1 
ATOM   225   C CG  . LEU A 1 27  ? 35.068  14.054  -66.237 1.00 38.94  ? 27  LEU A CG  1 
ATOM   226   C CD1 . LEU A 1 27  ? 34.170  15.280  -66.188 1.00 38.54  ? 27  LEU A CD1 1 
ATOM   227   C CD2 . LEU A 1 27  ? 34.634  13.017  -65.212 1.00 37.53  ? 27  LEU A CD2 1 
ATOM   228   N N   . ASN A 1 28  ? 36.389  12.027  -70.296 1.00 39.03  ? 28  ASN A N   1 
ATOM   229   C CA  . ASN A 1 28  ? 36.253  11.421  -71.625 1.00 39.39  ? 28  ASN A CA  1 
ATOM   230   C C   . ASN A 1 28  ? 36.443  9.884   -71.657 1.00 38.91  ? 28  ASN A C   1 
ATOM   231   O O   . ASN A 1 28  ? 35.790  9.200   -72.441 1.00 37.66  ? 28  ASN A O   1 
ATOM   232   C CB  . ASN A 1 28  ? 37.208  12.079  -72.615 1.00 41.41  ? 28  ASN A CB  1 
ATOM   233   C CG  . ASN A 1 28  ? 36.870  13.535  -72.875 1.00 43.84  ? 28  ASN A CG  1 
ATOM   234   O OD1 . ASN A 1 28  ? 35.774  14.002  -72.563 1.00 43.79  ? 28  ASN A OD1 1 
ATOM   235   N ND2 . ASN A 1 28  ? 37.810  14.257  -73.469 1.00 45.24  ? 28  ASN A ND2 1 
ATOM   236   N N   . ILE A 1 29  ? 37.358  9.363   -70.827 1.00 37.39  ? 29  ILE A N   1 
ATOM   237   C CA  . ILE A 1 29  ? 37.607  7.916   -70.744 1.00 35.60  ? 29  ILE A CA  1 
ATOM   238   C C   . ILE A 1 29  ? 36.345  7.198   -70.282 1.00 34.20  ? 29  ILE A C   1 
ATOM   239   O O   . ILE A 1 29  ? 35.859  6.273   -70.957 1.00 33.10  ? 29  ILE A O   1 
ATOM   240   C CB  . ILE A 1 29  ? 38.797  7.588   -69.806 1.00 36.08  ? 29  ILE A CB  1 
ATOM   241   C CG1 . ILE A 1 29  ? 40.079  8.253   -70.329 1.00 36.22  ? 29  ILE A CG1 1 
ATOM   242   C CG2 . ILE A 1 29  ? 39.017  6.084   -69.719 1.00 35.67  ? 29  ILE A CG2 1 
ATOM   243   C CD1 . ILE A 1 29  ? 41.194  8.308   -69.312 1.00 36.88  ? 29  ILE A CD1 1 
ATOM   244   N N   . ALA A 1 30  ? 35.792  7.678   -69.167 1.00 33.23  ? 30  ALA A N   1 
ATOM   245   C CA  . ALA A 1 30  ? 34.552  7.165   -68.602 1.00 33.21  ? 30  ALA A CA  1 
ATOM   246   C C   . ALA A 1 30  ? 33.369  7.248   -69.578 1.00 33.97  ? 30  ALA A C   1 
ATOM   247   O O   . ALA A 1 30  ? 32.609  6.295   -69.711 1.00 36.89  ? 30  ALA A O   1 
ATOM   248   C CB  . ALA A 1 30  ? 34.231  7.886   -67.292 1.00 31.57  ? 30  ALA A CB  1 
ATOM   249   N N   . LEU A 1 31  ? 33.224  8.378   -70.261 1.00 33.82  ? 31  LEU A N   1 
ATOM   250   C CA  . LEU A 1 31  ? 32.196  8.525   -71.299 1.00 34.44  ? 31  LEU A CA  1 
ATOM   251   C C   . LEU A 1 31  ? 32.344  7.428   -72.348 1.00 34.48  ? 31  LEU A C   1 
ATOM   252   O O   . LEU A 1 31  ? 31.347  6.857   -72.815 1.00 34.00  ? 31  LEU A O   1 
ATOM   253   C CB  . LEU A 1 31  ? 32.295  9.913   -71.988 1.00 34.23  ? 31  LEU A CB  1 
ATOM   254   C CG  . LEU A 1 31  ? 31.695  11.134  -71.258 1.00 35.94  ? 31  LEU A CG  1 
ATOM   255   C CD1 . LEU A 1 31  ? 32.030  12.445  -71.980 1.00 35.35  ? 31  LEU A CD1 1 
ATOM   256   C CD2 . LEU A 1 31  ? 30.180  10.980  -71.065 1.00 34.30  ? 31  LEU A CD2 1 
ATOM   257   N N   . LYS A 1 32  ? 33.599  7.171   -72.723 1.00 35.18  ? 32  LYS A N   1 
ATOM   258   C CA  . LYS A 1 32  ? 33.976  6.175   -73.717 1.00 36.96  ? 32  LYS A CA  1 
ATOM   259   C C   . LYS A 1 32  ? 33.548  4.779   -73.259 1.00 36.28  ? 32  LYS A C   1 
ATOM   260   O O   . LYS A 1 32  ? 32.723  4.124   -73.908 1.00 35.78  ? 32  LYS A O   1 
ATOM   261   C CB  . LYS A 1 32  ? 35.501  6.256   -73.935 1.00 40.47  ? 32  LYS A CB  1 
ATOM   262   C CG  . LYS A 1 32  ? 36.145  5.105   -74.687 1.00 42.43  ? 32  LYS A CG  1 
ATOM   263   C CD  . LYS A 1 32  ? 35.934  5.247   -76.174 1.00 45.24  ? 32  LYS A CD  1 
ATOM   264   C CE  . LYS A 1 32  ? 36.628  4.126   -76.932 1.00 47.65  ? 32  LYS A CE  1 
ATOM   265   N NZ  . LYS A 1 32  ? 36.283  4.192   -78.382 1.00 51.97  ? 32  LYS A NZ  1 
ATOM   266   N N   . ASN A 1 33  ? 34.067  4.372   -72.102 1.00 36.19  ? 33  ASN A N   1 
ATOM   267   C CA  . ASN A 1 33  ? 33.701  3.112   -71.456 1.00 35.57  ? 33  ASN A CA  1 
ATOM   268   C C   . ASN A 1 33  ? 32.200  2.977   -71.231 1.00 36.03  ? 33  ASN A C   1 
ATOM   269   O O   . ASN A 1 33  ? 31.665  1.870   -71.293 1.00 36.62  ? 33  ASN A O   1 
ATOM   270   C CB  . ASN A 1 33  ? 34.455  2.936   -70.128 1.00 34.84  ? 33  ASN A CB  1 
ATOM   271   C CG  . ASN A 1 33  ? 35.970  3.090   -70.280 1.00 36.10  ? 33  ASN A CG  1 
ATOM   272   O OD1 . ASN A 1 33  ? 36.541  2.805   -71.336 1.00 37.03  ? 33  ASN A OD1 1 
ATOM   273   N ND2 . ASN A 1 33  ? 36.621  3.546   -69.224 1.00 35.69  ? 33  ASN A ND2 1 
ATOM   274   N N   . PHE A 1 34  ? 31.518  4.097   -70.990 1.00 34.48  ? 34  PHE A N   1 
ATOM   275   C CA  . PHE A 1 34  ? 30.048  4.087   -70.911 1.00 35.05  ? 34  PHE A CA  1 
ATOM   276   C C   . PHE A 1 34  ? 29.406  3.657   -72.235 1.00 34.38  ? 34  PHE A C   1 
ATOM   277   O O   . PHE A 1 34  ? 28.575  2.747   -72.270 1.00 34.70  ? 34  PHE A O   1 
ATOM   278   C CB  . PHE A 1 34  ? 29.498  5.450   -70.440 1.00 35.52  ? 34  PHE A CB  1 
ATOM   279   C CG  . PHE A 1 34  ? 27.990  5.499   -70.327 1.00 36.91  ? 34  PHE A CG  1 
ATOM   280   C CD1 . PHE A 1 34  ? 27.267  4.396   -69.885 1.00 38.11  ? 34  PHE A CD1 1 
ATOM   281   C CD2 . PHE A 1 34  ? 27.298  6.663   -70.626 1.00 37.85  ? 34  PHE A CD2 1 
ATOM   282   C CE1 . PHE A 1 34  ? 25.877  4.450   -69.780 1.00 37.90  ? 34  PHE A CE1 1 
ATOM   283   C CE2 . PHE A 1 34  ? 25.917  6.723   -70.524 1.00 35.84  ? 34  PHE A CE2 1 
ATOM   284   C CZ  . PHE A 1 34  ? 25.208  5.624   -70.104 1.00 36.76  ? 34  PHE A CZ  1 
ATOM   285   N N   . ARG A 1 35  ? 29.807  4.302   -73.320 1.00 34.22  ? 35  ARG A N   1 
ATOM   286   C CA  . ARG A 1 35  ? 29.348  3.910   -74.652 1.00 36.33  ? 35  ARG A CA  1 
ATOM   287   C C   . ARG A 1 35  ? 29.723  2.451   -75.017 1.00 35.60  ? 35  ARG A C   1 
ATOM   288   O O   . ARG A 1 35  ? 28.927  1.751   -75.647 1.00 35.96  ? 35  ARG A O   1 
ATOM   289   C CB  . ARG A 1 35  ? 29.874  4.878   -75.729 1.00 36.39  ? 35  ARG A CB  1 
ATOM   290   C CG  . ARG A 1 35  ? 29.425  6.334   -75.566 1.00 35.80  ? 35  ARG A CG  1 
ATOM   291   C CD  . ARG A 1 35  ? 29.766  7.161   -76.806 1.00 37.26  ? 35  ARG A CD  1 
ATOM   292   N NE  . ARG A 1 35  ? 31.213  7.217   -77.087 1.00 37.02  ? 35  ARG A NE  1 
ATOM   293   C CZ  . ARG A 1 35  ? 32.051  8.128   -76.575 1.00 37.74  ? 35  ARG A CZ  1 
ATOM   294   N NH1 . ARG A 1 35  ? 31.606  9.075   -75.742 1.00 37.61  ? 35  ARG A NH1 1 
ATOM   295   N NH2 . ARG A 1 35  ? 33.338  8.094   -76.887 1.00 36.81  ? 35  ARG A NH2 1 
ATOM   296   N N   . LEU A 1 36  ? 30.926  2.014   -74.623 1.00 35.60  ? 36  LEU A N   1 
ATOM   297   C CA  . LEU A 1 36  ? 31.404  0.645   -74.900 1.00 33.89  ? 36  LEU A CA  1 
ATOM   298   C C   . LEU A 1 36  ? 30.530  -0.370  -74.184 1.00 32.74  ? 36  LEU A C   1 
ATOM   299   O O   . LEU A 1 36  ? 30.103  -1.348  -74.770 1.00 32.80  ? 36  LEU A O   1 
ATOM   300   C CB  . LEU A 1 36  ? 32.867  0.485   -74.470 1.00 32.80  ? 36  LEU A CB  1 
ATOM   301   C CG  . LEU A 1 36  ? 34.031  0.451   -75.474 1.00 35.22  ? 36  LEU A CG  1 
ATOM   302   C CD1 . LEU A 1 36  ? 33.675  0.840   -76.919 1.00 34.76  ? 36  LEU A CD1 1 
ATOM   303   C CD2 . LEU A 1 36  ? 35.241  1.239   -74.964 1.00 34.73  ? 36  LEU A CD2 1 
ATOM   304   N N   . CYS A 1 37  ? 30.255  -0.110  -72.911 1.00 33.18  ? 37  CYS A N   1 
ATOM   305   C CA  . CYS A 1 37  ? 29.398  -0.969  -72.081 1.00 34.28  ? 37  CYS A CA  1 
ATOM   306   C C   . CYS A 1 37  ? 27.990  -1.133  -72.692 1.00 35.09  ? 37  CYS A C   1 
ATOM   307   O O   . CYS A 1 37  ? 27.424  -2.240  -72.699 1.00 33.01  ? 37  CYS A O   1 
ATOM   308   C CB  . CYS A 1 37  ? 29.284  -0.383  -70.660 1.00 34.19  ? 37  CYS A CB  1 
ATOM   309   S SG  . CYS A 1 37  ? 28.313  -1.360  -69.487 1.00 39.03  ? 37  CYS A SG  1 
ATOM   310   N N   . LYS A 1 38  ? 27.431  -0.025  -73.190 1.00 35.49  ? 38  LYS A N   1 
ATOM   311   C CA  . LYS A 1 38  ? 26.103  -0.052  -73.787 1.00 37.54  ? 38  LYS A CA  1 
ATOM   312   C C   . LYS A 1 38  ? 26.039  -0.912  -75.040 1.00 39.14  ? 38  LYS A C   1 
ATOM   313   O O   . LYS A 1 38  ? 25.003  -1.516  -75.319 1.00 41.77  ? 38  LYS A O   1 
ATOM   314   C CB  . LYS A 1 38  ? 25.588  1.367   -74.059 1.00 39.30  ? 38  LYS A CB  1 
ATOM   315   C CG  . LYS A 1 38  ? 25.095  2.076   -72.794 1.00 39.27  ? 38  LYS A CG  1 
ATOM   316   C CD  . LYS A 1 38  ? 24.441  3.401   -73.115 1.00 39.48  ? 38  LYS A CD  1 
ATOM   317   C CE  . LYS A 1 38  ? 25.464  4.485   -73.403 1.00 39.61  ? 38  LYS A CE  1 
ATOM   318   N NZ  . LYS A 1 38  ? 24.768  5.773   -73.676 1.00 40.96  ? 38  LYS A NZ  1 
ATOM   319   N N   . LYS A 1 39  ? 27.153  -0.980  -75.778 1.00 39.19  ? 39  LYS A N   1 
ATOM   320   C CA  . LYS A 1 39  ? 27.222  -1.744  -77.033 1.00 40.03  ? 39  LYS A CA  1 
ATOM   321   C C   . LYS A 1 39  ? 27.459  -3.233  -76.818 1.00 39.69  ? 39  LYS A C   1 
ATOM   322   O O   . LYS A 1 39  ? 27.075  -4.041  -77.642 1.00 42.19  ? 39  LYS A O   1 
ATOM   323   C CB  . LYS A 1 39  ? 28.313  -1.195  -77.939 1.00 41.15  ? 39  LYS A CB  1 
ATOM   324   C CG  . LYS A 1 39  ? 28.023  0.173   -78.512 1.00 42.73  ? 39  LYS A CG  1 
ATOM   325   C CD  . LYS A 1 39  ? 29.209  0.685   -79.321 1.00 45.23  ? 39  LYS A CD  1 
ATOM   326   C CE  . LYS A 1 39  ? 28.932  2.067   -79.904 1.00 46.59  ? 39  LYS A CE  1 
ATOM   327   N NZ  . LYS A 1 39  ? 30.204  2.771   -80.225 1.00 49.97  ? 39  LYS A NZ  1 
ATOM   328   N N   . HIS A 1 40  ? 28.121  -3.581  -75.723 1.00 39.49  ? 40  HIS A N   1 
ATOM   329   C CA  . HIS A 1 40  ? 28.382  -4.966  -75.382 1.00 40.33  ? 40  HIS A CA  1 
ATOM   330   C C   . HIS A 1 40  ? 27.136  -5.705  -74.988 1.00 44.54  ? 40  HIS A C   1 
ATOM   331   O O   . HIS A 1 40  ? 26.566  -5.460  -73.924 1.00 45.92  ? 40  HIS A O   1 
ATOM   332   C CB  . HIS A 1 40  ? 29.402  -5.048  -74.253 1.00 37.01  ? 40  HIS A CB  1 
ATOM   333   C CG  . HIS A 1 40  ? 29.784  -6.463  -73.885 1.00 36.65  ? 40  HIS A CG  1 
ATOM   334   N ND1 . HIS A 1 40  ? 30.043  -6.841  -72.614 1.00 35.18  ? 40  HIS A ND1 1 
ATOM   335   C CD2 . HIS A 1 40  ? 29.913  -7.619  -74.673 1.00 35.49  ? 40  HIS A CD2 1 
ATOM   336   C CE1 . HIS A 1 40  ? 30.343  -8.155  -72.594 1.00 34.81  ? 40  HIS A CE1 1 
ATOM   337   N NE2 . HIS A 1 40  ? 30.255  -8.627  -73.852 1.00 34.59  ? 40  HIS A NE2 1 
ATOM   338   N N   . LYS A 1 41  ? 26.721  -6.647  -75.826 1.00 51.43  ? 41  LYS A N   1 
ATOM   339   C CA  . LYS A 1 41  ? 25.594  -7.513  -75.504 1.00 56.06  ? 41  LYS A CA  1 
ATOM   340   C C   . LYS A 1 41  ? 26.092  -8.762  -74.778 1.00 58.99  ? 41  LYS A C   1 
ATOM   341   O O   . LYS A 1 41  ? 26.724  -9.635  -75.373 1.00 63.99  ? 41  LYS A O   1 
ATOM   342   C CB  . LYS A 1 41  ? 24.802  -7.877  -76.770 1.00 59.38  ? 41  LYS A CB  1 
ATOM   343   C CG  . LYS A 1 41  ? 24.438  -6.684  -77.663 1.00 60.59  ? 41  LYS A CG  1 
ATOM   344   C CD  . LYS A 1 41  ? 23.451  -5.735  -76.981 1.00 62.20  ? 41  LYS A CD  1 
ATOM   345   C CE  . LYS A 1 41  ? 23.209  -4.477  -77.808 1.00 62.36  ? 41  LYS A CE  1 
ATOM   346   N NZ  . LYS A 1 41  ? 22.659  -3.358  -76.988 1.00 64.76  ? 41  LYS A NZ  1 
ATOM   347   N N   . THR A 1 42  ? 25.826  -8.811  -73.480 1.00 61.31  ? 42  THR A N   1 
ATOM   348   C CA  . THR A 1 42  ? 26.253  -9.907  -72.620 1.00 64.87  ? 42  THR A CA  1 
ATOM   349   C C   . THR A 1 42  ? 25.047  -10.732 -72.172 1.00 70.88  ? 42  THR A C   1 
ATOM   350   O O   . THR A 1 42  ? 23.968  -10.183 -71.909 1.00 65.76  ? 42  THR A O   1 
ATOM   351   C CB  . THR A 1 42  ? 27.005  -9.383  -71.367 1.00 66.02  ? 42  THR A CB  1 
ATOM   352   O OG1 . THR A 1 42  ? 26.592  -10.118 -70.208 1.00 63.27  ? 42  THR A OG1 1 
ATOM   353   C CG2 . THR A 1 42  ? 26.716  -7.901  -71.130 1.00 61.21  ? 42  THR A CG2 1 
ATOM   354   N N   . LYS A 1 43  ? 25.243  -12.047 -72.070 1.00 76.08  ? 43  LYS A N   1 
ATOM   355   C CA  . LYS A 1 43  ? 24.178  -12.968 -71.652 1.00 83.21  ? 43  LYS A CA  1 
ATOM   356   C C   . LYS A 1 43  ? 23.843  -12.868 -70.152 1.00 84.16  ? 43  LYS A C   1 
ATOM   357   O O   . LYS A 1 43  ? 22.669  -12.951 -69.767 1.00 83.05  ? 43  LYS A O   1 
ATOM   358   C CB  . LYS A 1 43  ? 24.544  -14.415 -72.015 1.00 85.29  ? 43  LYS A CB  1 
ATOM   359   C CG  . LYS A 1 43  ? 23.362  -15.262 -72.461 1.00 86.83  ? 43  LYS A CG  1 
ATOM   360   C CD  . LYS A 1 43  ? 23.781  -16.697 -72.747 1.00 88.56  ? 43  LYS A CD  1 
ATOM   361   C CE  . LYS A 1 43  ? 23.240  -17.185 -74.084 1.00 87.73  ? 43  LYS A CE  1 
ATOM   362   N NZ  . LYS A 1 43  ? 21.761  -17.056 -74.188 1.00 88.59  ? 43  LYS A NZ  1 
ATOM   363   N N   . LYS A 1 44  ? 24.876  -12.673 -69.323 1.00 85.41  ? 44  LYS A N   1 
ATOM   364   C CA  . LYS A 1 44  ? 24.740  -12.749 -67.856 1.00 86.26  ? 44  LYS A CA  1 
ATOM   365   C C   . LYS A 1 44  ? 24.447  -11.407 -67.159 1.00 82.26  ? 44  LYS A C   1 
ATOM   366   O O   . LYS A 1 44  ? 25.109  -10.396 -67.435 1.00 73.76  ? 44  LYS A O   1 
ATOM   367   C CB  . LYS A 1 44  ? 25.958  -13.448 -67.225 1.00 88.60  ? 44  LYS A CB  1 
ATOM   368   C CG  . LYS A 1 44  ? 26.033  -14.948 -67.511 1.00 92.95  ? 44  LYS A CG  1 
ATOM   369   C CD  . LYS A 1 44  ? 25.064  -15.747 -66.646 1.00 94.74  ? 44  LYS A CD  1 
ATOM   370   C CE  . LYS A 1 44  ? 24.731  -17.103 -67.262 1.00 99.69  ? 44  LYS A CE  1 
ATOM   371   N NZ  . LYS A 1 44  ? 25.886  -18.047 -67.272 1.00 101.31 ? 44  LYS A NZ  1 
ATOM   372   N N   . PRO A 1 45  ? 23.451  -11.411 -66.244 1.00 80.22  ? 45  PRO A N   1 
ATOM   373   C CA  . PRO A 1 45  ? 22.875  -10.261 -65.542 1.00 75.36  ? 45  PRO A CA  1 
ATOM   374   C C   . PRO A 1 45  ? 23.848  -9.168  -65.099 1.00 69.27  ? 45  PRO A C   1 
ATOM   375   O O   . PRO A 1 45  ? 24.994  -9.440  -64.733 1.00 67.06  ? 45  PRO A O   1 
ATOM   376   C CB  . PRO A 1 45  ? 22.202  -10.906 -64.333 1.00 79.73  ? 45  PRO A CB  1 
ATOM   377   C CG  . PRO A 1 45  ? 21.722  -12.219 -64.860 1.00 81.04  ? 45  PRO A CG  1 
ATOM   378   C CD  . PRO A 1 45  ? 22.725  -12.654 -65.905 1.00 82.30  ? 45  PRO A CD  1 
ATOM   379   N N   . VAL A 1 46  ? 23.340  -7.942  -65.092 1.00 64.56  ? 46  VAL A N   1 
ATOM   380   C CA  . VAL A 1 46  ? 24.148  -6.752  -64.926 1.00 61.21  ? 46  VAL A CA  1 
ATOM   381   C C   . VAL A 1 46  ? 24.186  -6.297  -63.459 1.00 59.62  ? 46  VAL A C   1 
ATOM   382   O O   . VAL A 1 46  ? 23.142  -6.013  -62.852 1.00 65.06  ? 46  VAL A O   1 
ATOM   383   C CB  . VAL A 1 46  ? 23.652  -5.606  -65.864 1.00 59.16  ? 46  VAL A CB  1 
ATOM   384   C CG1 . VAL A 1 46  ? 23.386  -6.138  -67.268 1.00 53.79  ? 46  VAL A CG1 1 
ATOM   385   C CG2 . VAL A 1 46  ? 22.400  -4.945  -65.320 1.00 55.06  ? 46  VAL A CG2 1 
ATOM   386   N N   . GLN A 1 47  ? 25.383  -6.278  -62.882 1.00 53.22  ? 47  GLN A N   1 
ATOM   387   C CA  . GLN A 1 47  ? 25.594  -5.645  -61.580 1.00 52.42  ? 47  GLN A CA  1 
ATOM   388   C C   . GLN A 1 47  ? 26.147  -4.211  -61.753 1.00 45.76  ? 47  GLN A C   1 
ATOM   389   O O   . GLN A 1 47  ? 27.285  -4.024  -62.190 1.00 43.13  ? 47  GLN A O   1 
ATOM   390   C CB  . GLN A 1 47  ? 26.520  -6.503  -60.712 1.00 56.69  ? 47  GLN A CB  1 
ATOM   391   C CG  . GLN A 1 47  ? 25.810  -7.581  -59.887 1.00 62.48  ? 47  GLN A CG  1 
ATOM   392   C CD  . GLN A 1 47  ? 25.283  -7.066  -58.552 1.00 61.20  ? 47  GLN A CD  1 
ATOM   393   O OE1 . GLN A 1 47  ? 25.076  -5.864  -58.371 1.00 64.01  ? 47  GLN A OE1 1 
ATOM   394   N NE2 . GLN A 1 47  ? 25.069  -7.976  -57.610 1.00 60.60  ? 47  GLN A NE2 1 
ATOM   395   N N   . ILE A 1 48  ? 25.327  -3.207  -61.449 1.00 41.64  ? 48  ILE A N   1 
ATOM   396   C CA  . ILE A 1 48  ? 25.684  -1.820  -61.780 1.00 39.37  ? 48  ILE A CA  1 
ATOM   397   C C   . ILE A 1 48  ? 27.004  -1.365  -61.114 1.00 37.86  ? 48  ILE A C   1 
ATOM   398   O O   . ILE A 1 48  ? 27.876  -0.792  -61.782 1.00 35.99  ? 48  ILE A O   1 
ATOM   399   C CB  . ILE A 1 48  ? 24.502  -0.824  -61.582 1.00 38.08  ? 48  ILE A CB  1 
ATOM   400   C CG1 . ILE A 1 48  ? 23.710  -0.664  -62.878 1.00 40.86  ? 48  ILE A CG1 1 
ATOM   401   C CG2 . ILE A 1 48  ? 25.002  0.580   -61.285 1.00 35.08  ? 48  ILE A CG2 1 
ATOM   402   C CD1 . ILE A 1 48  ? 23.066  -1.911  -63.399 1.00 43.49  ? 48  ILE A CD1 1 
ATOM   403   N N   . LEU A 1 49  ? 27.163  -1.664  -59.826 1.00 37.35  ? 49  LEU A N   1 
ATOM   404   C CA  . LEU A 1 49  ? 28.395  -1.297  -59.090 1.00 37.45  ? 49  LEU A CA  1 
ATOM   405   C C   . LEU A 1 49  ? 29.610  -1.837  -59.816 1.00 36.62  ? 49  LEU A C   1 
ATOM   406   O O   . LEU A 1 49  ? 30.560  -1.106  -60.071 1.00 35.44  ? 49  LEU A O   1 
ATOM   407   C CB  . LEU A 1 49  ? 28.366  -1.822  -57.651 1.00 36.11  ? 49  LEU A CB  1 
ATOM   408   C CG  . LEU A 1 49  ? 28.007  -0.943  -56.435 1.00 36.74  ? 49  LEU A CG  1 
ATOM   409   C CD1 . LEU A 1 49  ? 27.436  0.421   -56.790 1.00 34.92  ? 49  LEU A CD1 1 
ATOM   410   C CD2 . LEU A 1 49  ? 27.076  -1.687  -55.469 1.00 36.62  ? 49  LEU A CD2 1 
ATOM   411   N N   . ALA A 1 50  ? 29.542  -3.113  -60.194 1.00 37.33  ? 50  ALA A N   1 
ATOM   412   C CA  . ALA A 1 50  ? 30.612  -3.774  -60.950 1.00 36.22  ? 50  ALA A CA  1 
ATOM   413   C C   . ALA A 1 50  ? 30.868  -3.179  -62.344 1.00 36.31  ? 50  ALA A C   1 
ATOM   414   O O   . ALA A 1 50  ? 32.018  -3.088  -62.771 1.00 38.95  ? 50  ALA A O   1 
ATOM   415   C CB  . ALA A 1 50  ? 30.341  -5.273  -61.051 1.00 37.16  ? 50  ALA A CB  1 
ATOM   416   N N   . LEU A 1 51  ? 29.814  -2.801  -63.066 1.00 34.69  ? 51  LEU A N   1 
ATOM   417   C CA  . LEU A 1 51  ? 30.010  -2.181  -64.386 1.00 34.36  ? 51  LEU A CA  1 
ATOM   418   C C   . LEU A 1 51  ? 30.668  -0.837  -64.221 1.00 32.26  ? 51  LEU A C   1 
ATOM   419   O O   . LEU A 1 51  ? 31.586  -0.479  -64.958 1.00 34.96  ? 51  LEU A O   1 
ATOM   420   C CB  . LEU A 1 51  ? 28.692  -2.006  -65.157 1.00 32.70  ? 51  LEU A CB  1 
ATOM   421   C CG  . LEU A 1 51  ? 28.050  -3.221  -65.804 1.00 34.52  ? 51  LEU A CG  1 
ATOM   422   C CD1 . LEU A 1 51  ? 26.739  -2.814  -66.488 1.00 33.92  ? 51  LEU A CD1 1 
ATOM   423   C CD2 . LEU A 1 51  ? 29.023  -3.869  -66.790 1.00 35.41  ? 51  LEU A CD2 1 
ATOM   424   N N   . LEU A 1 52  ? 30.184  -0.089  -63.249 1.00 32.45  ? 52  LEU A N   1 
ATOM   425   C CA  . LEU A 1 52  ? 30.591  1.297   -63.067 1.00 31.71  ? 52  LEU A CA  1 
ATOM   426   C C   . LEU A 1 52  ? 32.081  1.367   -62.709 1.00 31.04  ? 52  LEU A C   1 
ATOM   427   O O   . LEU A 1 52  ? 32.788  2.287   -63.124 1.00 28.42  ? 52  LEU A O   1 
ATOM   428   C CB  . LEU A 1 52  ? 29.739  1.925   -61.991 1.00 30.07  ? 52  LEU A CB  1 
ATOM   429   C CG  . LEU A 1 52  ? 28.957  3.215   -62.272 1.00 32.74  ? 52  LEU A CG  1 
ATOM   430   C CD1 . LEU A 1 52  ? 28.635  3.441   -63.737 1.00 30.76  ? 52  LEU A CD1 1 
ATOM   431   C CD2 . LEU A 1 52  ? 27.690  3.270   -61.400 1.00 30.15  ? 52  LEU A CD2 1 
ATOM   432   N N   . GLN A 1 53  ? 32.544  0.352   -61.984 1.00 30.93  ? 53  GLN A N   1 
ATOM   433   C CA  . GLN A 1 53  ? 33.934  0.259   -61.580 1.00 32.77  ? 53  GLN A CA  1 
ATOM   434   C C   . GLN A 1 53  ? 34.884  -0.061  -62.752 1.00 33.60  ? 53  GLN A C   1 
ATOM   435   O O   . GLN A 1 53  ? 36.089  0.191   -62.667 1.00 31.78  ? 53  GLN A O   1 
ATOM   436   C CB  . GLN A 1 53  ? 34.083  -0.714  -60.408 1.00 33.72  ? 53  GLN A CB  1 
ATOM   437   C CG  . GLN A 1 53  ? 33.940  0.004   -59.064 1.00 37.14  ? 53  GLN A CG  1 
ATOM   438   C CD  . GLN A 1 53  ? 33.388  -0.860  -57.953 1.00 38.67  ? 53  GLN A CD  1 
ATOM   439   O OE1 . GLN A 1 53  ? 33.747  -2.021  -57.810 1.00 41.88  ? 53  GLN A OE1 1 
ATOM   440   N NE2 . GLN A 1 53  ? 32.511  -0.282  -57.149 1.00 40.52  ? 53  GLN A NE2 1 
ATOM   441   N N   . GLU A 1 54  ? 34.321  -0.543  -63.861 1.00 32.67  ? 54  GLU A N   1 
ATOM   442   C CA  . GLU A 1 54  ? 35.062  -0.649  -65.111 1.00 34.45  ? 54  GLU A CA  1 
ATOM   443   C C   . GLU A 1 54  ? 34.951  0.615   -65.972 1.00 34.93  ? 54  GLU A C   1 
ATOM   444   O O   . GLU A 1 54  ? 35.843  0.931   -66.769 1.00 33.33  ? 54  GLU A O   1 
ATOM   445   C CB  . GLU A 1 54  ? 34.570  -1.843  -65.892 1.00 36.67  ? 54  GLU A CB  1 
ATOM   446   C CG  . GLU A 1 54  ? 34.658  -3.129  -65.097 1.00 39.03  ? 54  GLU A CG  1 
ATOM   447   C CD  . GLU A 1 54  ? 33.944  -4.245  -65.763 1.00 39.50  ? 54  GLU A CD  1 
ATOM   448   O OE1 . GLU A 1 54  ? 33.229  -3.966  -66.735 1.00 42.01  ? 54  GLU A OE1 1 
ATOM   449   O OE2 . GLU A 1 54  ? 34.089  -5.397  -65.310 1.00 43.08  ? 54  GLU A OE2 1 
ATOM   450   N N   . ILE A 1 55  ? 33.842  1.326   -65.815 1.00 33.39  ? 55  ILE A N   1 
ATOM   451   C CA  . ILE A 1 55  ? 33.555  2.474   -66.642 1.00 32.56  ? 55  ILE A CA  1 
ATOM   452   C C   . ILE A 1 55  ? 34.335  3.693   -66.172 1.00 32.63  ? 55  ILE A C   1 
ATOM   453   O O   . ILE A 1 55  ? 34.985  4.355   -66.972 1.00 34.76  ? 55  ILE A O   1 
ATOM   454   C CB  . ILE A 1 55  ? 32.041  2.745   -66.686 1.00 32.73  ? 55  ILE A CB  1 
ATOM   455   C CG1 . ILE A 1 55  ? 31.361  1.717   -67.587 1.00 31.42  ? 55  ILE A CG1 1 
ATOM   456   C CG2 . ILE A 1 55  ? 31.746  4.179   -67.125 1.00 32.33  ? 55  ILE A CG2 1 
ATOM   457   C CD1 . ILE A 1 55  ? 29.941  1.431   -67.189 1.00 30.59  ? 55  ILE A CD1 1 
ATOM   458   N N   . ILE A 1 56  ? 34.272  3.978   -64.868 1.00 33.27  ? 56  ILE A N   1 
ATOM   459   C CA  . ILE A 1 56  ? 35.046  5.062   -64.260 1.00 31.73  ? 56  ILE A CA  1 
ATOM   460   C C   . ILE A 1 56  ? 36.406  4.534   -63.802 1.00 31.82  ? 56  ILE A C   1 
ATOM   461   O O   . ILE A 1 56  ? 36.496  3.733   -62.883 1.00 31.63  ? 56  ILE A O   1 
ATOM   462   C CB  . ILE A 1 56  ? 34.282  5.731   -63.084 1.00 31.15  ? 56  ILE A CB  1 
ATOM   463   C CG1 . ILE A 1 56  ? 32.824  5.994   -63.478 1.00 30.62  ? 56  ILE A CG1 1 
ATOM   464   C CG2 . ILE A 1 56  ? 34.969  7.035   -62.665 1.00 30.78  ? 56  ILE A CG2 1 
ATOM   465   C CD1 . ILE A 1 56  ? 31.963  6.636   -62.397 1.00 30.16  ? 56  ILE A CD1 1 
ATOM   466   N N   . PRO A 1 57  ? 37.476  4.986   -64.446 1.00 32.73  ? 57  PRO A N   1 
ATOM   467   C CA  . PRO A 1 57  ? 38.792  4.414   -64.154 1.00 33.02  ? 57  PRO A CA  1 
ATOM   468   C C   . PRO A 1 57  ? 39.221  4.777   -62.763 1.00 32.88  ? 57  PRO A C   1 
ATOM   469   O O   . PRO A 1 57  ? 38.884  5.875   -62.283 1.00 33.17  ? 57  PRO A O   1 
ATOM   470   C CB  . PRO A 1 57  ? 39.704  5.112   -65.173 1.00 33.73  ? 57  PRO A CB  1 
ATOM   471   C CG  . PRO A 1 57  ? 39.064  6.457   -65.374 1.00 33.01  ? 57  PRO A CG  1 
ATOM   472   C CD  . PRO A 1 57  ? 37.568  6.232   -65.236 1.00 33.61  ? 57  PRO A CD  1 
ATOM   473   N N   . LYS A 1 58  ? 39.988  3.905   -62.120 1.00 33.58  ? 58  LYS A N   1 
ATOM   474   C CA  . LYS A 1 58  ? 40.345  4.133   -60.721 1.00 36.36  ? 58  LYS A CA  1 
ATOM   475   C C   . LYS A 1 58  ? 41.146  5.393   -60.508 1.00 37.71  ? 58  LYS A C   1 
ATOM   476   O O   . LYS A 1 58  ? 41.118  5.979   -59.417 1.00 40.35  ? 58  LYS A O   1 
ATOM   477   C CB  . LYS A 1 58  ? 41.095  2.959   -60.110 1.00 37.89  ? 58  LYS A CB  1 
ATOM   478   C CG  . LYS A 1 58  ? 40.915  2.935   -58.599 1.00 39.21  ? 58  LYS A CG  1 
ATOM   479   C CD  . LYS A 1 58  ? 41.922  2.052   -57.885 1.00 40.82  ? 58  LYS A CD  1 
ATOM   480   C CE  . LYS A 1 58  ? 41.821  2.267   -56.385 1.00 41.15  ? 58  LYS A CE  1 
ATOM   481   N NZ  . LYS A 1 58  ? 42.472  1.154   -55.655 1.00 42.89  ? 58  LYS A NZ  1 
ATOM   482   N N   . SER A 1 59  ? 41.864  5.805   -61.540 1.00 36.44  ? 59  SER A N   1 
ATOM   483   C CA  . SER A 1 59  ? 42.647  7.025   -61.485 1.00 37.70  ? 59  SER A CA  1 
ATOM   484   C C   . SER A 1 59  ? 41.790  8.275   -61.250 1.00 37.60  ? 59  SER A C   1 
ATOM   485   O O   . SER A 1 59  ? 42.319  9.324   -60.865 1.00 37.81  ? 59  SER A O   1 
ATOM   486   C CB  . SER A 1 59  ? 43.462  7.184   -62.763 1.00 36.92  ? 59  SER A CB  1 
ATOM   487   O OG  . SER A 1 59  ? 42.614  7.085   -63.882 1.00 37.30  ? 59  SER A OG  1 
ATOM   488   N N   . TYR A 1 60  ? 40.479  8.177   -61.491 1.00 36.29  ? 60  TYR A N   1 
ATOM   489   C CA  . TYR A 1 60  ? 39.597  9.286   -61.157 1.00 35.73  ? 60  TYR A CA  1 
ATOM   490   C C   . TYR A 1 60  ? 39.508  9.526   -59.647 1.00 35.12  ? 60  TYR A C   1 
ATOM   491   O O   . TYR A 1 60  ? 39.415  10.672  -59.212 1.00 33.77  ? 60  TYR A O   1 
ATOM   492   C CB  . TYR A 1 60  ? 38.196  9.153   -61.770 1.00 34.99  ? 60  TYR A CB  1 
ATOM   493   C CG  . TYR A 1 60  ? 37.273  10.251  -61.290 1.00 34.33  ? 60  TYR A CG  1 
ATOM   494   C CD1 . TYR A 1 60  ? 37.328  11.521  -61.852 1.00 34.94  ? 60  TYR A CD1 1 
ATOM   495   C CD2 . TYR A 1 60  ? 36.400  10.042  -60.221 1.00 35.08  ? 60  TYR A CD2 1 
ATOM   496   C CE1 . TYR A 1 60  ? 36.514  12.537  -61.399 1.00 35.13  ? 60  TYR A CE1 1 
ATOM   497   C CE2 . TYR A 1 60  ? 35.590  11.066  -59.737 1.00 33.43  ? 60  TYR A CE2 1 
ATOM   498   C CZ  . TYR A 1 60  ? 35.654  12.307  -60.334 1.00 33.97  ? 60  TYR A CZ  1 
ATOM   499   O OH  . TYR A 1 60  ? 34.847  13.320  -59.904 1.00 35.38  ? 60  TYR A OH  1 
ATOM   500   N N   . PHE A 1 61  ? 39.552  8.452   -58.859 1.00 34.90  ? 61  PHE A N   1 
ATOM   501   C CA  . PHE A 1 61  ? 39.436  8.567   -57.392 1.00 35.97  ? 61  PHE A CA  1 
ATOM   502   C C   . PHE A 1 61  ? 40.774  8.501   -56.665 1.00 38.21  ? 61  PHE A C   1 
ATOM   503   O O   . PHE A 1 61  ? 40.850  8.849   -55.504 1.00 41.96  ? 61  PHE A O   1 
ATOM   504   C CB  . PHE A 1 61  ? 38.549  7.464   -56.823 1.00 34.43  ? 61  PHE A CB  1 
ATOM   505   C CG  . PHE A 1 61  ? 37.212  7.347   -57.484 1.00 33.02  ? 61  PHE A CG  1 
ATOM   506   C CD1 . PHE A 1 61  ? 36.180  8.202   -57.144 1.00 31.39  ? 61  PHE A CD1 1 
ATOM   507   C CD2 . PHE A 1 61  ? 36.972  6.346   -58.412 1.00 31.70  ? 61  PHE A CD2 1 
ATOM   508   C CE1 . PHE A 1 61  ? 34.936  8.083   -57.734 1.00 30.80  ? 61  PHE A CE1 1 
ATOM   509   C CE2 . PHE A 1 61  ? 35.722  6.218   -59.001 1.00 31.96  ? 61  PHE A CE2 1 
ATOM   510   C CZ  . PHE A 1 61  ? 34.700  7.090   -58.659 1.00 30.82  ? 61  PHE A CZ  1 
ATOM   511   N N   . GLY A 1 62  ? 41.808  7.982   -57.319 1.00 39.79  ? 62  GLY A N   1 
ATOM   512   C CA  . GLY A 1 62  ? 43.132  7.874   -56.698 1.00 40.22  ? 62  GLY A CA  1 
ATOM   513   C C   . GLY A 1 62  ? 43.298  6.714   -55.724 1.00 42.10  ? 62  GLY A C   1 
ATOM   514   O O   . GLY A 1 62  ? 44.262  5.963   -55.816 1.00 44.43  ? 62  GLY A O   1 
ATOM   515   N N   . THR A 1 63  ? 42.378  6.577   -54.769 1.00 42.38  ? 63  THR A N   1 
ATOM   516   C CA  . THR A 1 63  ? 42.491  5.530   -53.730 1.00 41.37  ? 63  THR A CA  1 
ATOM   517   C C   . THR A 1 63  ? 41.196  4.762   -53.570 1.00 40.68  ? 63  THR A C   1 
ATOM   518   O O   . THR A 1 63  ? 40.117  5.242   -53.932 1.00 38.97  ? 63  THR A O   1 
ATOM   519   C CB  . THR A 1 63  ? 42.814  6.120   -52.340 1.00 42.42  ? 63  THR A CB  1 
ATOM   520   O OG1 . THR A 1 63  ? 41.814  7.081   -51.997 1.00 44.11  ? 63  THR A OG1 1 
ATOM   521   C CG2 . THR A 1 63  ? 44.190  6.786   -52.311 1.00 41.21  ? 63  THR A CG2 1 
ATOM   522   N N   . THR A 1 64  ? 41.304  3.576   -52.990 1.00 40.73  ? 64  THR A N   1 
ATOM   523   C CA  . THR A 1 64  ? 40.141  2.767   -52.675 1.00 40.92  ? 64  THR A CA  1 
ATOM   524   C C   . THR A 1 64  ? 39.177  3.519   -51.751 1.00 40.66  ? 64  THR A C   1 
ATOM   525   O O   . THR A 1 64  ? 37.960  3.452   -51.938 1.00 40.64  ? 64  THR A O   1 
ATOM   526   C CB  . THR A 1 64  ? 40.564  1.421   -52.054 1.00 42.26  ? 64  THR A CB  1 
ATOM   527   O OG1 . THR A 1 64  ? 41.589  0.833   -52.865 1.00 43.17  ? 64  THR A OG1 1 
ATOM   528   C CG2 . THR A 1 64  ? 39.391  0.456   -51.973 1.00 42.24  ? 64  THR A CG2 1 
ATOM   529   N N   . THR A 1 65  ? 39.722  4.269   -50.790 1.00 40.89  ? 65  THR A N   1 
ATOM   530   C CA  . THR A 1 65  ? 38.886  4.989   -49.819 1.00 39.46  ? 65  THR A CA  1 
ATOM   531   C C   . THR A 1 65  ? 38.062  6.084   -50.483 1.00 38.58  ? 65  THR A C   1 
ATOM   532   O O   . THR A 1 65  ? 36.863  6.183   -50.219 1.00 36.49  ? 65  THR A O   1 
ATOM   533   C CB  . THR A 1 65  ? 39.692  5.553   -48.629 1.00 41.53  ? 65  THR A CB  1 
ATOM   534   O OG1 . THR A 1 65  ? 40.573  4.539   -48.125 1.00 42.98  ? 65  THR A OG1 1 
ATOM   535   C CG2 . THR A 1 65  ? 38.749  5.983   -47.499 1.00 40.28  ? 65  THR A CG2 1 
ATOM   536   N N   . ASN A 1 66  ? 38.694  6.891   -51.347 1.00 36.29  ? 66  ASN A N   1 
ATOM   537   C CA  . ASN A 1 66  ? 37.944  7.829   -52.196 1.00 36.79  ? 66  ASN A CA  1 
ATOM   538   C C   . ASN A 1 66  ? 36.876  7.112   -53.059 1.00 37.86  ? 66  ASN A C   1 
ATOM   539   O O   . ASN A 1 66  ? 35.700  7.506   -53.092 1.00 36.45  ? 66  ASN A O   1 
ATOM   540   C CB  . ASN A 1 66  ? 38.887  8.625   -53.103 1.00 37.62  ? 66  ASN A CB  1 
ATOM   541   C CG  . ASN A 1 66  ? 39.776  9.592   -52.333 1.00 40.58  ? 66  ASN A CG  1 
ATOM   542   O OD1 . ASN A 1 66  ? 39.537  9.881   -51.150 1.00 41.97  ? 66  ASN A OD1 1 
ATOM   543   N ND2 . ASN A 1 66  ? 40.802  10.117  -53.010 1.00 38.47  ? 66  ASN A ND2 1 
ATOM   544   N N   . LEU A 1 67  ? 37.276  6.043   -53.737 1.00 36.98  ? 67  LEU A N   1 
ATOM   545   C CA  . LEU A 1 67  ? 36.336  5.330   -54.589 1.00 37.03  ? 67  LEU A CA  1 
ATOM   546   C C   . LEU A 1 67  ? 35.113  4.854   -53.767 1.00 37.18  ? 67  LEU A C   1 
ATOM   547   O O   . LEU A 1 67  ? 33.963  5.000   -54.197 1.00 36.47  ? 67  LEU A O   1 
ATOM   548   C CB  . LEU A 1 67  ? 37.042  4.170   -55.294 1.00 34.91  ? 67  LEU A CB  1 
ATOM   549   C CG  . LEU A 1 67  ? 36.237  3.195   -56.140 1.00 33.54  ? 67  LEU A CG  1 
ATOM   550   C CD1 . LEU A 1 67  ? 37.170  2.566   -57.151 1.00 33.71  ? 67  LEU A CD1 1 
ATOM   551   C CD2 . LEU A 1 67  ? 35.593  2.117   -55.276 1.00 33.91  ? 67  LEU A CD2 1 
ATOM   552   N N   . LYS A 1 68  ? 35.374  4.307   -52.584 1.00 38.69  ? 68  LYS A N   1 
ATOM   553   C CA  . LYS A 1 68  ? 34.313  3.742   -51.749 1.00 42.34  ? 68  LYS A CA  1 
ATOM   554   C C   . LYS A 1 68  ? 33.352  4.812   -51.236 1.00 40.17  ? 68  LYS A C   1 
ATOM   555   O O   . LYS A 1 68  ? 32.164  4.555   -51.021 1.00 40.81  ? 68  LYS A O   1 
ATOM   556   C CB  . LYS A 1 68  ? 34.902  2.932   -50.593 1.00 47.01  ? 68  LYS A CB  1 
ATOM   557   C CG  . LYS A 1 68  ? 34.868  1.431   -50.828 1.00 51.17  ? 68  LYS A CG  1 
ATOM   558   C CD  . LYS A 1 68  ? 35.987  0.712   -50.090 1.00 57.71  ? 68  LYS A CD  1 
ATOM   559   C CE  . LYS A 1 68  ? 35.694  -0.779  -49.981 1.00 57.84  ? 68  LYS A CE  1 
ATOM   560   N NZ  . LYS A 1 68  ? 34.760  -1.047  -48.846 1.00 61.47  ? 68  LYS A NZ  1 
ATOM   561   N N   . ARG A 1 69  ? 33.862  6.022   -51.113 1.00 39.01  ? 69  ARG A N   1 
ATOM   562   C CA  . ARG A 1 69  ? 33.070  7.143   -50.672 1.00 37.81  ? 69  ARG A CA  1 
ATOM   563   C C   . ARG A 1 69  ? 32.057  7.560   -51.750 1.00 36.81  ? 69  ARG A C   1 
ATOM   564   O O   . ARG A 1 69  ? 30.862  7.679   -51.457 1.00 37.83  ? 69  ARG A O   1 
ATOM   565   C CB  . ARG A 1 69  ? 33.988  8.304   -50.237 1.00 40.26  ? 69  ARG A CB  1 
ATOM   566   C CG  . ARG A 1 69  ? 33.271  9.434   -49.516 1.00 46.04  ? 69  ARG A CG  1 
ATOM   567   C CD  . ARG A 1 69  ? 34.235  10.467  -48.947 1.00 48.61  ? 69  ARG A CD  1 
ATOM   568   N NE  . ARG A 1 69  ? 34.655  10.130  -47.587 1.00 55.63  ? 69  ARG A NE  1 
ATOM   569   C CZ  . ARG A 1 69  ? 35.884  9.734   -47.256 1.00 58.11  ? 69  ARG A CZ  1 
ATOM   570   N NH1 . ARG A 1 69  ? 36.836  9.633   -48.188 1.00 57.90  ? 69  ARG A NH1 1 
ATOM   571   N NH2 . ARG A 1 69  ? 36.169  9.450   -45.989 1.00 56.70  ? 69  ARG A NH2 1 
ATOM   572   N N   . PHE A 1 70  ? 32.524  7.745   -52.992 1.00 34.29  ? 70  PHE A N   1 
ATOM   573   C CA  . PHE A 1 70  ? 31.643  8.050   -54.131 1.00 33.11  ? 70  PHE A CA  1 
ATOM   574   C C   . PHE A 1 70  ? 30.545  6.987   -54.288 1.00 32.56  ? 70  PHE A C   1 
ATOM   575   O O   . PHE A 1 70  ? 29.388  7.333   -54.444 1.00 34.87  ? 70  PHE A O   1 
ATOM   576   C CB  . PHE A 1 70  ? 32.471  8.210   -55.440 1.00 32.10  ? 70  PHE A CB  1 
ATOM   577   C CG  . PHE A 1 70  ? 31.643  8.485   -56.693 1.00 30.32  ? 70  PHE A CG  1 
ATOM   578   C CD1 . PHE A 1 70  ? 31.304  9.790   -57.059 1.00 31.56  ? 70  PHE A CD1 1 
ATOM   579   C CD2 . PHE A 1 70  ? 31.263  7.444   -57.544 1.00 30.45  ? 70  PHE A CD2 1 
ATOM   580   C CE1 . PHE A 1 70  ? 30.573  10.040  -58.226 1.00 29.74  ? 70  PHE A CE1 1 
ATOM   581   C CE2 . PHE A 1 70  ? 30.540  7.690   -58.710 1.00 27.24  ? 70  PHE A CE2 1 
ATOM   582   C CZ  . PHE A 1 70  ? 30.207  8.979   -59.048 1.00 28.80  ? 70  PHE A CZ  1 
ATOM   583   N N   . TYR A 1 71  ? 30.917  5.705   -54.199 1.00 31.20  ? 71  TYR A N   1 
ATOM   584   C CA  . TYR A 1 71  ? 30.000  4.594   -54.518 1.00 30.88  ? 71  TYR A CA  1 
ATOM   585   C C   . TYR A 1 71  ? 28.923  4.351   -53.457 1.00 31.22  ? 71  TYR A C   1 
ATOM   586   O O   . TYR A 1 71  ? 27.895  3.742   -53.743 1.00 30.12  ? 71  TYR A O   1 
ATOM   587   C CB  . TYR A 1 71  ? 30.774  3.298   -54.839 1.00 30.08  ? 71  TYR A CB  1 
ATOM   588   C CG  . TYR A 1 71  ? 31.322  3.279   -56.262 1.00 32.33  ? 71  TYR A CG  1 
ATOM   589   C CD1 . TYR A 1 71  ? 30.509  2.921   -57.337 1.00 32.05  ? 71  TYR A CD1 1 
ATOM   590   C CD2 . TYR A 1 71  ? 32.646  3.676   -56.541 1.00 31.87  ? 71  TYR A CD2 1 
ATOM   591   C CE1 . TYR A 1 71  ? 30.999  2.947   -58.646 1.00 33.06  ? 71  TYR A CE1 1 
ATOM   592   C CE2 . TYR A 1 71  ? 33.140  3.697   -57.847 1.00 31.98  ? 71  TYR A CE2 1 
ATOM   593   C CZ  . TYR A 1 71  ? 32.304  3.330   -58.893 1.00 32.43  ? 71  TYR A CZ  1 
ATOM   594   O OH  . TYR A 1 71  ? 32.771  3.318   -60.190 1.00 34.74  ? 71  TYR A OH  1 
ATOM   595   N N   . LYS A 1 72  ? 29.142  4.850   -52.244 1.00 32.01  ? 72  LYS A N   1 
ATOM   596   C CA  . LYS A 1 72  ? 28.051  4.888   -51.250 1.00 33.78  ? 72  LYS A CA  1 
ATOM   597   C C   . LYS A 1 72  ? 26.900  5.750   -51.769 1.00 31.47  ? 72  LYS A C   1 
ATOM   598   O O   . LYS A 1 72  ? 25.740  5.434   -51.535 1.00 30.59  ? 72  LYS A O   1 
ATOM   599   C CB  . LYS A 1 72  ? 28.530  5.418   -49.895 1.00 35.74  ? 72  LYS A CB  1 
ATOM   600   C CG  . LYS A 1 72  ? 29.406  4.459   -49.098 1.00 39.47  ? 72  LYS A CG  1 
ATOM   601   C CD  . LYS A 1 72  ? 28.602  3.564   -48.169 1.00 43.39  ? 72  LYS A CD  1 
ATOM   602   C CE  . LYS A 1 72  ? 28.528  2.124   -48.672 1.00 49.65  ? 72  LYS A CE  1 
ATOM   603   N NZ  . LYS A 1 72  ? 27.398  1.886   -49.629 1.00 53.02  ? 72  LYS A NZ  1 
ATOM   604   N N   . VAL A 1 73  ? 27.228  6.834   -52.477 1.00 29.09  ? 73  VAL A N   1 
ATOM   605   C CA  . VAL A 1 73  ? 26.209  7.632   -53.126 1.00 29.51  ? 73  VAL A CA  1 
ATOM   606   C C   . VAL A 1 73  ? 25.465  6.807   -54.200 1.00 29.24  ? 73  VAL A C   1 
ATOM   607   O O   . VAL A 1 73  ? 24.234  6.681   -54.165 1.00 29.42  ? 73  VAL A O   1 
ATOM   608   C CB  . VAL A 1 73  ? 26.824  8.878   -53.755 1.00 29.79  ? 73  VAL A CB  1 
ATOM   609   C CG1 . VAL A 1 73  ? 25.777  9.614   -54.574 1.00 28.14  ? 73  VAL A CG1 1 
ATOM   610   C CG2 . VAL A 1 73  ? 27.449  9.756   -52.663 1.00 28.66  ? 73  VAL A CG2 1 
ATOM   611   N N   . VAL A 1 74  ? 26.235  6.219   -55.109 1.00 26.90  ? 74  VAL A N   1 
ATOM   612   C CA  . VAL A 1 74  ? 25.719  5.344   -56.157 1.00 28.24  ? 74  VAL A CA  1 
ATOM   613   C C   . VAL A 1 74  ? 24.806  4.282   -55.574 1.00 29.06  ? 74  VAL A C   1 
ATOM   614   O O   . VAL A 1 74  ? 23.773  3.932   -56.157 1.00 30.75  ? 74  VAL A O   1 
ATOM   615   C CB  . VAL A 1 74  ? 26.886  4.655   -56.929 1.00 27.70  ? 74  VAL A CB  1 
ATOM   616   C CG1 . VAL A 1 74  ? 26.374  3.575   -57.871 1.00 27.96  ? 74  VAL A CG1 1 
ATOM   617   C CG2 . VAL A 1 74  ? 27.695  5.681   -57.700 1.00 27.19  ? 74  VAL A CG2 1 
ATOM   618   N N   . GLU A 1 75  ? 25.198  3.773   -54.421 1.00 28.90  ? 75  GLU A N   1 
ATOM   619   C CA  . GLU A 1 75  ? 24.459  2.765   -53.746 1.00 31.02  ? 75  GLU A CA  1 
ATOM   620   C C   . GLU A 1 75  ? 23.117  3.296   -53.196 1.00 30.26  ? 75  GLU A C   1 
ATOM   621   O O   . GLU A 1 75  ? 22.125  2.569   -53.168 1.00 29.76  ? 75  GLU A O   1 
ATOM   622   C CB  . GLU A 1 75  ? 25.334  2.163   -52.645 1.00 35.11  ? 75  GLU A CB  1 
ATOM   623   C CG  . GLU A 1 75  ? 24.647  1.121   -51.779 1.00 44.32  ? 75  GLU A CG  1 
ATOM   624   C CD  . GLU A 1 75  ? 25.523  -0.102  -51.520 1.00 54.06  ? 75  GLU A CD  1 
ATOM   625   O OE1 . GLU A 1 75  ? 26.767  0.074   -51.370 1.00 58.51  ? 75  GLU A OE1 1 
ATOM   626   O OE2 . GLU A 1 75  ? 24.964  -1.240  -51.470 1.00 54.63  ? 75  GLU A OE2 1 
ATOM   627   N N   . LYS A 1 76  ? 23.074  4.557   -52.768 1.00 28.57  ? 76  LYS A N   1 
ATOM   628   C CA  . LYS A 1 76  ? 21.791  5.152   -52.349 1.00 28.92  ? 76  LYS A CA  1 
ATOM   629   C C   . LYS A 1 76  ? 20.879  5.277   -53.539 1.00 29.47  ? 76  LYS A C   1 
ATOM   630   O O   . LYS A 1 76  ? 19.686  4.969   -53.465 1.00 27.86  ? 76  LYS A O   1 
ATOM   631   C CB  . LYS A 1 76  ? 21.991  6.526   -51.737 1.00 29.80  ? 76  LYS A CB  1 
ATOM   632   C CG  . LYS A 1 76  ? 22.530  6.469   -50.323 1.00 32.05  ? 76  LYS A CG  1 
ATOM   633   C CD  . LYS A 1 76  ? 22.423  7.817   -49.632 1.00 35.04  ? 76  LYS A CD  1 
ATOM   634   C CE  . LYS A 1 76  ? 22.528  7.639   -48.109 1.00 35.25  ? 76  LYS A CE  1 
ATOM   635   N NZ  . LYS A 1 76  ? 22.341  8.914   -47.359 1.00 34.47  ? 76  LYS A NZ  1 
ATOM   636   N N   . ILE A 1 77  ? 21.466  5.708   -54.658 1.00 29.60  ? 77  ILE A N   1 
ATOM   637   C CA  . ILE A 1 77  ? 20.718  5.929   -55.854 1.00 28.29  ? 77  ILE A CA  1 
ATOM   638   C C   . ILE A 1 77  ? 20.148  4.598   -56.268 1.00 29.46  ? 77  ILE A C   1 
ATOM   639   O O   . ILE A 1 77  ? 18.990  4.517   -56.732 1.00 32.27  ? 77  ILE A O   1 
ATOM   640   C CB  . ILE A 1 77  ? 21.625  6.541   -56.962 1.00 27.90  ? 77  ILE A CB  1 
ATOM   641   C CG1 . ILE A 1 77  ? 21.971  7.999   -56.599 1.00 26.90  ? 77  ILE A CG1 1 
ATOM   642   C CG2 . ILE A 1 77  ? 20.969  6.426   -58.332 1.00 25.24  ? 77  ILE A CG2 1 
ATOM   643   C CD1 . ILE A 1 77  ? 22.855  8.709   -57.606 1.00 27.12  ? 77  ILE A CD1 1 
ATOM   644   N N   . LEU A 1 78  ? 20.931  3.538   -56.071 1.00 27.42  ? 78  LEU A N   1 
ATOM   645   C CA  . LEU A 1 78  ? 20.466  2.194   -56.448 1.00 28.79  ? 78  LEU A CA  1 
ATOM   646   C C   . LEU A 1 78  ? 19.334  1.686   -55.550 1.00 29.57  ? 78  LEU A C   1 
ATOM   647   O O   . LEU A 1 78  ? 18.688  0.683   -55.877 1.00 30.01  ? 78  LEU A O   1 
ATOM   648   C CB  . LEU A 1 78  ? 21.619  1.190   -56.473 1.00 26.75  ? 78  LEU A CB  1 
ATOM   649   C CG  . LEU A 1 78  ? 22.578  1.306   -57.653 1.00 26.58  ? 78  LEU A CG  1 
ATOM   650   C CD1 . LEU A 1 78  ? 23.789  0.395   -57.429 1.00 25.80  ? 78  LEU A CD1 1 
ATOM   651   C CD2 . LEU A 1 78  ? 21.837  0.917   -58.923 1.00 26.63  ? 78  LEU A CD2 1 
ATOM   652   N N   . THR A 1 79  ? 19.088  2.388   -54.441 1.00 28.69  ? 79  THR A N   1 
ATOM   653   C CA  . THR A 1 79  ? 18.131  1.934   -53.422 1.00 30.15  ? 79  THR A CA  1 
ATOM   654   C C   . THR A 1 79  ? 17.166  3.064   -52.992 1.00 30.49  ? 79  THR A C   1 
ATOM   655   O O   . THR A 1 79  ? 16.472  2.953   -51.969 1.00 28.15  ? 79  THR A O   1 
ATOM   656   C CB  . THR A 1 79  ? 18.874  1.432   -52.169 1.00 31.69  ? 79  THR A CB  1 
ATOM   657   O OG1 . THR A 1 79  ? 19.711  2.486   -51.663 1.00 33.04  ? 79  THR A OG1 1 
ATOM   658   C CG2 . THR A 1 79  ? 19.738  0.188   -52.491 1.00 29.60  ? 79  THR A CG2 1 
ATOM   659   N N   . GLN A 1 80  ? 17.099  4.121   -53.807 1.00 30.84  ? 80  GLN A N   1 
ATOM   660   C CA  . GLN A 1 80  ? 16.417  5.360   -53.438 1.00 31.10  ? 80  GLN A CA  1 
ATOM   661   C C   . GLN A 1 80  ? 14.944  5.174   -53.126 1.00 31.80  ? 80  GLN A C   1 
ATOM   662   O O   . GLN A 1 80  ? 14.326  4.199   -53.575 1.00 32.43  ? 80  GLN A O   1 
ATOM   663   C CB  . GLN A 1 80  ? 16.560  6.380   -54.544 1.00 30.58  ? 80  GLN A CB  1 
ATOM   664   C CG  . GLN A 1 80  ? 16.103  5.863   -55.902 1.00 33.44  ? 80  GLN A CG  1 
ATOM   665   C CD  . GLN A 1 80  ? 16.383  6.849   -57.013 1.00 34.38  ? 80  GLN A CD  1 
ATOM   666   O OE1 . GLN A 1 80  ? 15.701  7.864   -57.133 1.00 33.45  ? 80  GLN A OE1 1 
ATOM   667   N NE2 . GLN A 1 80  ? 17.413  6.562   -57.827 1.00 35.10  ? 80  GLN A NE2 1 
ATOM   668   N N   . SER A 1 81  ? 14.394  6.109   -52.349 1.00 29.73  ? 81  SER A N   1 
ATOM   669   C CA  . SER A 1 81  ? 12.941  6.286   -52.248 1.00 31.74  ? 81  SER A CA  1 
ATOM   670   C C   . SER A 1 81  ? 12.545  7.462   -53.146 1.00 33.53  ? 81  SER A C   1 
ATOM   671   O O   . SER A 1 81  ? 13.412  8.237   -53.550 1.00 36.86  ? 81  SER A O   1 
ATOM   672   C CB  . SER A 1 81  ? 12.553  6.605   -50.803 1.00 30.25  ? 81  SER A CB  1 
ATOM   673   O OG  . SER A 1 81  ? 12.558  5.460   -49.991 1.00 28.83  ? 81  SER A OG  1 
ATOM   674   N N   . SER A 1 82  ? 11.258  7.629   -53.444 1.00 32.69  ? 82  SER A N   1 
ATOM   675   C CA  . SER A 1 82  ? 10.819  8.845   -54.131 1.00 33.22  ? 82  SER A CA  1 
ATOM   676   C C   . SER A 1 82  ? 11.169  10.024  -53.266 1.00 32.89  ? 82  SER A C   1 
ATOM   677   O O   . SER A 1 82  ? 10.998  9.965   -52.058 1.00 34.66  ? 82  SER A O   1 
ATOM   678   C CB  . SER A 1 82  ? 9.315   8.835   -54.356 1.00 34.56  ? 82  SER A CB  1 
ATOM   679   O OG  . SER A 1 82  ? 8.958   7.894   -55.343 1.00 37.51  ? 82  SER A OG  1 
ATOM   680   N N   . PHE A 1 83  ? 11.677  11.088  -53.877 1.00 33.21  ? 83  PHE A N   1 
ATOM   681   C CA  . PHE A 1 83  ? 11.910  12.369  -53.187 1.00 33.26  ? 83  PHE A CA  1 
ATOM   682   C C   . PHE A 1 83  ? 13.192  12.421  -52.354 1.00 31.86  ? 83  PHE A C   1 
ATOM   683   O O   . PHE A 1 83  ? 13.512  13.450  -51.786 1.00 31.40  ? 83  PHE A O   1 
ATOM   684   C CB  . PHE A 1 83  ? 10.710  12.745  -52.288 1.00 37.45  ? 83  PHE A CB  1 
ATOM   685   C CG  . PHE A 1 83  ? 9.455   13.113  -53.043 1.00 40.11  ? 83  PHE A CG  1 
ATOM   686   C CD1 . PHE A 1 83  ? 9.394   14.278  -53.807 1.00 42.40  ? 83  PHE A CD1 1 
ATOM   687   C CD2 . PHE A 1 83  ? 8.310   12.320  -52.945 1.00 41.95  ? 83  PHE A CD2 1 
ATOM   688   C CE1 . PHE A 1 83  ? 8.225   14.628  -54.487 1.00 43.16  ? 83  PHE A CE1 1 
ATOM   689   C CE2 . PHE A 1 83  ? 7.139   12.663  -53.624 1.00 42.91  ? 83  PHE A CE2 1 
ATOM   690   C CZ  . PHE A 1 83  ? 7.099   13.816  -54.399 1.00 43.01  ? 83  PHE A CZ  1 
ATOM   691   N N   . GLU A 1 84  ? 13.891  11.301  -52.233 1.00 30.06  ? 84  GLU A N   1 
ATOM   692   C CA  . GLU A 1 84  ? 15.081  11.257  -51.411 1.00 30.79  ? 84  GLU A CA  1 
ATOM   693   C C   . GLU A 1 84  ? 16.197  12.083  -52.034 1.00 32.00  ? 84  GLU A C   1 
ATOM   694   O O   . GLU A 1 84  ? 16.376  12.092  -53.268 1.00 32.69  ? 84  GLU A O   1 
ATOM   695   C CB  . GLU A 1 84  ? 15.559  9.804   -51.208 1.00 31.61  ? 84  GLU A CB  1 
ATOM   696   C CG  . GLU A 1 84  ? 16.778  9.657   -50.312 1.00 29.07  ? 84  GLU A CG  1 
ATOM   697   C CD  . GLU A 1 84  ? 17.101  8.209   -50.011 1.00 30.43  ? 84  GLU A CD  1 
ATOM   698   O OE1 . GLU A 1 84  ? 16.616  7.316   -50.745 1.00 32.21  ? 84  GLU A OE1 1 
ATOM   699   O OE2 . GLU A 1 84  ? 17.847  7.958   -49.043 1.00 30.76  ? 84  GLU A OE2 1 
ATOM   700   N N   . CYS A 1 85  ? 16.939  12.769  -51.167 1.00 31.01  ? 85  CYS A N   1 
ATOM   701   C CA  . CYS A 1 85  ? 18.125  13.502  -51.543 1.00 29.95  ? 85  CYS A CA  1 
ATOM   702   C C   . CYS A 1 85  ? 19.253  13.068  -50.646 1.00 30.18  ? 85  CYS A C   1 
ATOM   703   O O   . CYS A 1 85  ? 19.028  12.383  -49.660 1.00 31.34  ? 85  CYS A O   1 
ATOM   704   C CB  . CYS A 1 85  ? 17.891  14.985  -51.340 1.00 29.57  ? 85  CYS A CB  1 
ATOM   705   S SG  . CYS A 1 85  ? 16.499  15.623  -52.297 1.00 30.08  ? 85  CYS A SG  1 
ATOM   706   N N   . ILE A 1 86  ? 20.474  13.454  -51.008 1.00 31.33  ? 86  ILE A N   1 
ATOM   707   C CA  . ILE A 1 86  ? 21.580  13.587  -50.061 1.00 30.30  ? 86  ILE A CA  1 
ATOM   708   C C   . ILE A 1 86  ? 22.019  15.046  -50.121 1.00 31.64  ? 86  ILE A C   1 
ATOM   709   O O   . ILE A 1 86  ? 21.540  15.787  -50.978 1.00 32.64  ? 86  ILE A O   1 
ATOM   710   C CB  . ILE A 1 86  ? 22.767  12.709  -50.449 1.00 29.41  ? 86  ILE A CB  1 
ATOM   711   C CG1 . ILE A 1 86  ? 23.055  12.839  -51.940 1.00 29.85  ? 86  ILE A CG1 1 
ATOM   712   C CG2 . ILE A 1 86  ? 22.477  11.258  -50.139 1.00 31.41  ? 86  ILE A CG2 1 
ATOM   713   C CD1 . ILE A 1 86  ? 24.517  13.066  -52.262 1.00 28.47  ? 86  ILE A CD1 1 
ATOM   714   N N   . HIS A 1 87  ? 22.934  15.447  -49.231 1.00 32.49  ? 87  HIS A N   1 
ATOM   715   C CA  . HIS A 1 87  ? 23.628  16.747  -49.335 1.00 33.36  ? 87  HIS A CA  1 
ATOM   716   C C   . HIS A 1 87  ? 24.676  16.813  -50.427 1.00 34.69  ? 87  HIS A C   1 
ATOM   717   O O   . HIS A 1 87  ? 25.515  15.913  -50.552 1.00 33.76  ? 87  HIS A O   1 
ATOM   718   C CB  . HIS A 1 87  ? 24.285  17.117  -48.001 1.00 34.49  ? 87  HIS A CB  1 
ATOM   719   C CG  . HIS A 1 87  ? 23.296  17.475  -46.917 1.00 34.95  ? 87  HIS A CG  1 
ATOM   720   N ND1 . HIS A 1 87  ? 22.708  16.540  -46.128 1.00 34.87  ? 87  HIS A ND1 1 
ATOM   721   C CD2 . HIS A 1 87  ? 22.771  18.706  -46.530 1.00 33.42  ? 87  HIS A CD2 1 
ATOM   722   C CE1 . HIS A 1 87  ? 21.853  17.150  -45.286 1.00 34.93  ? 87  HIS A CE1 1 
ATOM   723   N NE2 . HIS A 1 87  ? 21.900  18.476  -45.524 1.00 34.24  ? 87  HIS A NE2 1 
ATOM   724   N N   . LEU A 1 88  ? 24.678  17.926  -51.168 1.00 34.37  ? 88  LEU A N   1 
ATOM   725   C CA  . LEU A 1 88  ? 25.682  18.210  -52.168 1.00 33.60  ? 88  LEU A CA  1 
ATOM   726   C C   . LEU A 1 88  ? 27.111  18.133  -51.592 1.00 35.67  ? 88  LEU A C   1 
ATOM   727   O O   . LEU A 1 88  ? 28.058  17.757  -52.302 1.00 35.80  ? 88  LEU A O   1 
ATOM   728   C CB  . LEU A 1 88  ? 25.427  19.585  -52.812 1.00 32.00  ? 88  LEU A CB  1 
ATOM   729   C CG  . LEU A 1 88  ? 24.422  19.684  -53.984 1.00 33.52  ? 88  LEU A CG  1 
ATOM   730   C CD1 . LEU A 1 88  ? 24.080  21.141  -54.277 1.00 33.26  ? 88  LEU A CD1 1 
ATOM   731   C CD2 . LEU A 1 88  ? 24.942  19.012  -55.271 1.00 32.54  ? 88  LEU A CD2 1 
ATOM   732   N N   . SER A 1 89  ? 27.268  18.482  -50.316 1.00 34.75  ? 89  SER A N   1 
ATOM   733   C CA  . SER A 1 89  ? 28.586  18.441  -49.665 1.00 34.91  ? 89  SER A CA  1 
ATOM   734   C C   . SER A 1 89  ? 29.139  17.024  -49.444 1.00 34.39  ? 89  SER A C   1 
ATOM   735   O O   . SER A 1 89  ? 30.340  16.858  -49.229 1.00 35.03  ? 89  SER A O   1 
ATOM   736   C CB  . SER A 1 89  ? 28.555  19.192  -48.338 1.00 35.20  ? 89  SER A CB  1 
ATOM   737   O OG  . SER A 1 89  ? 27.792  18.479  -47.372 1.00 35.76  ? 89  SER A OG  1 
ATOM   738   N N   . VAL A 1 90  ? 28.275  16.008  -49.489 1.00 35.21  ? 90  VAL A N   1 
ATOM   739   C CA  . VAL A 1 90  ? 28.738  14.597  -49.412 1.00 36.30  ? 90  VAL A CA  1 
ATOM   740   C C   . VAL A 1 90  ? 29.693  14.290  -50.553 1.00 37.05  ? 90  VAL A C   1 
ATOM   741   O O   . VAL A 1 90  ? 30.465  13.301  -50.514 1.00 40.20  ? 90  VAL A O   1 
ATOM   742   C CB  . VAL A 1 90  ? 27.564  13.578  -49.480 1.00 38.02  ? 90  VAL A CB  1 
ATOM   743   C CG1 . VAL A 1 90  ? 28.094  12.160  -49.401 1.00 36.97  ? 90  VAL A CG1 1 
ATOM   744   C CG2 . VAL A 1 90  ? 26.554  13.815  -48.354 1.00 37.89  ? 90  VAL A CG2 1 
ATOM   745   N N   . LEU A 1 91  ? 29.633  15.119  -51.587 1.00 34.78  ? 91  LEU A N   1 
ATOM   746   C CA  . LEU A 1 91  ? 30.339  14.821  -52.815 1.00 34.62  ? 91  LEU A CA  1 
ATOM   747   C C   . LEU A 1 91  ? 31.731  15.442  -52.812 1.00 37.82  ? 91  LEU A C   1 
ATOM   748   O O   . LEU A 1 91  ? 32.504  15.259  -53.757 1.00 39.54  ? 91  LEU A O   1 
ATOM   749   C CB  . LEU A 1 91  ? 29.507  15.261  -54.029 1.00 33.72  ? 91  LEU A CB  1 
ATOM   750   C CG  . LEU A 1 91  ? 28.140  14.557  -54.277 1.00 32.80  ? 91  LEU A CG  1 
ATOM   751   C CD1 . LEU A 1 91  ? 27.418  15.112  -55.492 1.00 29.70  ? 91  LEU A CD1 1 
ATOM   752   C CD2 . LEU A 1 91  ? 28.294  13.038  -54.423 1.00 31.83  ? 91  LEU A CD2 1 
ATOM   753   N N   . HIS A 1 92  ? 32.063  16.155  -51.735 1.00 39.46  ? 92  HIS A N   1 
ATOM   754   C CA  . HIS A 1 92  ? 33.412  16.693  -51.581 1.00 41.01  ? 92  HIS A CA  1 
ATOM   755   C C   . HIS A 1 92  ? 34.011  16.583  -50.205 1.00 42.80  ? 92  HIS A C   1 
ATOM   756   O O   . HIS A 1 92  ? 35.236  16.531  -50.069 1.00 44.57  ? 92  HIS A O   1 
ATOM   757   C CB  . HIS A 1 92  ? 33.512  18.119  -52.124 1.00 40.45  ? 92  HIS A CB  1 
ATOM   758   C CG  . HIS A 1 92  ? 32.710  19.130  -51.357 1.00 39.45  ? 92  HIS A CG  1 
ATOM   759   N ND1 . HIS A 1 92  ? 33.172  19.722  -50.238 1.00 40.69  ? 92  HIS A ND1 1 
ATOM   760   C CD2 . HIS A 1 92  ? 31.456  19.687  -51.605 1.00 39.36  ? 92  HIS A CD2 1 
ATOM   761   C CE1 . HIS A 1 92  ? 32.258  20.602  -49.785 1.00 38.07  ? 92  HIS A CE1 1 
ATOM   762   N NE2 . HIS A 1 92  ? 31.210  20.582  -50.620 1.00 38.05  ? 92  HIS A NE2 1 
ATOM   763   N N   . LYS A 1 93  ? 33.173  16.518  -49.174 1.00 44.09  ? 93  LYS A N   1 
ATOM   764   C CA  . LYS A 1 93  ? 33.676  16.434  -47.794 1.00 47.52  ? 93  LYS A CA  1 
ATOM   765   C C   . LYS A 1 93  ? 34.448  15.139  -47.542 1.00 47.99  ? 93  LYS A C   1 
ATOM   766   O O   . LYS A 1 93  ? 33.990  14.055  -47.907 1.00 46.51  ? 93  LYS A O   1 
ATOM   767   C CB  . LYS A 1 93  ? 32.528  16.536  -46.780 1.00 49.67  ? 93  LYS A CB  1 
ATOM   768   C CG  . LYS A 1 93  ? 32.173  17.942  -46.319 1.00 53.77  ? 93  LYS A CG  1 
ATOM   769   C CD  . LYS A 1 93  ? 30.967  17.897  -45.383 1.00 54.51  ? 93  LYS A CD  1 
ATOM   770   C CE  . LYS A 1 93  ? 31.008  18.991  -44.324 1.00 56.97  ? 93  LYS A CE  1 
ATOM   771   N NZ  . LYS A 1 93  ? 30.707  20.340  -44.877 1.00 57.66  ? 93  LYS A NZ  1 
ATOM   772   N N   . CYS A 1 94  ? 35.618  15.268  -46.912 1.00 50.36  ? 94  CYS A N   1 
ATOM   773   C CA  . CYS A 1 94  ? 36.391  14.123  -46.382 1.00 50.26  ? 94  CYS A CA  1 
ATOM   774   C C   . CYS A 1 94  ? 37.082  13.239  -47.435 1.00 52.01  ? 94  CYS A C   1 
ATOM   775   O O   . CYS A 1 94  ? 37.557  12.145  -47.109 1.00 55.07  ? 94  CYS A O   1 
ATOM   776   C CB  . CYS A 1 94  ? 35.525  13.247  -45.462 1.00 53.71  ? 94  CYS A CB  1 
ATOM   777   S SG  . CYS A 1 94  ? 34.815  14.095  -44.040 1.00 55.92  ? 94  CYS A SG  1 
ATOM   778   N N   . TYR A 1 95  ? 37.132  13.693  -48.686 1.00 49.51  ? 95  TYR A N   1 
ATOM   779   C CA  . TYR A 1 95  ? 37.925  13.004  -49.703 1.00 50.41  ? 95  TYR A CA  1 
ATOM   780   C C   . TYR A 1 95  ? 39.416  13.229  -49.457 1.00 51.62  ? 95  TYR A C   1 
ATOM   781   O O   . TYR A 1 95  ? 39.824  14.310  -49.038 1.00 51.78  ? 95  TYR A O   1 
ATOM   782   C CB  . TYR A 1 95  ? 37.560  13.492  -51.104 1.00 47.67  ? 95  TYR A CB  1 
ATOM   783   C CG  . TYR A 1 95  ? 36.367  12.807  -51.697 1.00 46.58  ? 95  TYR A CG  1 
ATOM   784   C CD1 . TYR A 1 95  ? 35.070  13.179  -51.326 1.00 46.33  ? 95  TYR A CD1 1 
ATOM   785   C CD2 . TYR A 1 95  ? 36.519  11.800  -52.652 1.00 47.00  ? 95  TYR A CD2 1 
ATOM   786   C CE1 . TYR A 1 95  ? 33.958  12.555  -51.878 1.00 43.89  ? 95  TYR A CE1 1 
ATOM   787   C CE2 . TYR A 1 95  ? 35.409  11.163  -53.207 1.00 45.81  ? 95  TYR A CE2 1 
ATOM   788   C CZ  . TYR A 1 95  ? 34.133  11.547  -52.818 1.00 45.53  ? 95  TYR A CZ  1 
ATOM   789   O OH  . TYR A 1 95  ? 33.028  10.930  -53.361 1.00 44.69  ? 95  TYR A OH  1 
ATOM   790   N N   . ASP A 1 96  ? 40.219  12.203  -49.722 1.00 51.54  ? 96  ASP A N   1 
ATOM   791   C CA  . ASP A 1 96  ? 41.669  12.331  -49.684 1.00 52.39  ? 96  ASP A CA  1 
ATOM   792   C C   . ASP A 1 96  ? 42.108  13.098  -50.923 1.00 51.63  ? 96  ASP A C   1 
ATOM   793   O O   . ASP A 1 96  ? 42.242  12.525  -52.005 1.00 52.67  ? 96  ASP A O   1 
ATOM   794   C CB  . ASP A 1 96  ? 42.320  10.941  -49.637 1.00 55.08  ? 96  ASP A CB  1 
ATOM   795   C CG  . ASP A 1 96  ? 43.813  10.987  -49.315 1.00 57.61  ? 96  ASP A CG  1 
ATOM   796   O OD1 . ASP A 1 96  ? 44.383  12.095  -49.185 1.00 57.24  ? 96  ASP A OD1 1 
ATOM   797   O OD2 . ASP A 1 96  ? 44.419  9.896   -49.196 1.00 58.97  ? 96  ASP A OD2 1 
ATOM   798   N N   . TYR A 1 97  ? 42.306  14.401  -50.774 1.00 50.13  ? 97  TYR A N   1 
ATOM   799   C CA  . TYR A 1 97  ? 42.597  15.247  -51.928 1.00 52.52  ? 97  TYR A CA  1 
ATOM   800   C C   . TYR A 1 97  ? 44.022  15.099  -52.452 1.00 54.57  ? 97  TYR A C   1 
ATOM   801   O O   . TYR A 1 97  ? 44.258  15.254  -53.650 1.00 58.13  ? 97  TYR A O   1 
ATOM   802   C CB  . TYR A 1 97  ? 42.265  16.706  -51.641 1.00 50.77  ? 97  TYR A CB  1 
ATOM   803   C CG  . TYR A 1 97  ? 40.789  16.974  -51.669 1.00 51.32  ? 97  TYR A CG  1 
ATOM   804   C CD1 . TYR A 1 97  ? 40.129  17.179  -52.876 1.00 51.19  ? 97  TYR A CD1 1 
ATOM   805   C CD2 . TYR A 1 97  ? 40.040  16.999  -50.491 1.00 50.57  ? 97  TYR A CD2 1 
ATOM   806   C CE1 . TYR A 1 97  ? 38.771  17.420  -52.916 1.00 51.36  ? 97  TYR A CE1 1 
ATOM   807   C CE2 . TYR A 1 97  ? 38.680  17.231  -50.517 1.00 50.50  ? 97  TYR A CE2 1 
ATOM   808   C CZ  . TYR A 1 97  ? 38.050  17.442  -51.736 1.00 53.36  ? 97  TYR A CZ  1 
ATOM   809   O OH  . TYR A 1 97  ? 36.696  17.678  -51.786 1.00 54.13  ? 97  TYR A OH  1 
ATOM   810   N N   . ASP A 1 98  ? 44.960  14.785  -51.561 1.00 54.20  ? 98  ASP A N   1 
ATOM   811   C CA  . ASP A 1 98  ? 46.362  14.600  -51.950 1.00 57.73  ? 98  ASP A CA  1 
ATOM   812   C C   . ASP A 1 98  ? 46.577  13.369  -52.841 1.00 57.24  ? 98  ASP A C   1 
ATOM   813   O O   . ASP A 1 98  ? 47.633  13.216  -53.456 1.00 58.58  ? 98  ASP A O   1 
ATOM   814   C CB  . ASP A 1 98  ? 47.256  14.507  -50.708 1.00 60.18  ? 98  ASP A CB  1 
ATOM   815   C CG  . ASP A 1 98  ? 47.557  15.868  -50.101 1.00 63.91  ? 98  ASP A CG  1 
ATOM   816   O OD1 . ASP A 1 98  ? 47.866  16.803  -50.870 1.00 63.99  ? 98  ASP A OD1 1 
ATOM   817   O OD2 . ASP A 1 98  ? 47.486  16.000  -48.855 1.00 64.83  ? 98  ASP A OD2 1 
ATOM   818   N N   . ALA A 1 99  ? 45.571  12.502  -52.905 1.00 54.10  ? 99  ALA A N   1 
ATOM   819   C CA  . ALA A 1 99  ? 45.706  11.219  -53.576 1.00 51.42  ? 99  ALA A CA  1 
ATOM   820   C C   . ALA A 1 99  ? 45.003  11.188  -54.930 1.00 49.79  ? 99  ALA A C   1 
ATOM   821   O O   . ALA A 1 99  ? 45.055  10.178  -55.628 1.00 51.49  ? 99  ALA A O   1 
ATOM   822   C CB  . ALA A 1 99  ? 45.198  10.099  -52.680 1.00 49.42  ? 99  ALA A CB  1 
ATOM   823   N N   . ILE A 1 100 ? 44.356  12.291  -55.297 1.00 46.62  ? 100 ILE A N   1 
ATOM   824   C CA  . ILE A 1 100 ? 43.652  12.374  -56.567 1.00 46.04  ? 100 ILE A CA  1 
ATOM   825   C C   . ILE A 1 100 ? 44.572  13.005  -57.610 1.00 48.02  ? 100 ILE A C   1 
ATOM   826   O O   . ILE A 1 100 ? 44.794  14.217  -57.588 1.00 49.18  ? 100 ILE A O   1 
ATOM   827   C CB  . ILE A 1 100 ? 42.309  13.152  -56.450 1.00 45.09  ? 100 ILE A CB  1 
ATOM   828   C CG1 . ILE A 1 100 ? 41.369  12.455  -55.452 1.00 44.25  ? 100 ILE A CG1 1 
ATOM   829   C CG2 . ILE A 1 100 ? 41.625  13.269  -57.809 1.00 42.98  ? 100 ILE A CG2 1 
ATOM   830   C CD1 . ILE A 1 100 ? 40.272  13.343  -54.903 1.00 43.06  ? 100 ILE A CD1 1 
ATOM   831   N N   . PRO A 1 101 ? 45.119  12.172  -58.525 1.00 48.03  ? 101 PRO A N   1 
ATOM   832   C CA  . PRO A 1 101 ? 46.140  12.584  -59.491 1.00 48.69  ? 101 PRO A CA  1 
ATOM   833   C C   . PRO A 1 101 ? 45.726  13.779  -60.335 1.00 48.97  ? 101 PRO A C   1 
ATOM   834   O O   . PRO A 1 101 ? 46.499  14.737  -60.459 1.00 53.53  ? 101 PRO A O   1 
ATOM   835   C CB  . PRO A 1 101 ? 46.312  11.338  -60.375 1.00 48.52  ? 101 PRO A CB  1 
ATOM   836   C CG  . PRO A 1 101 ? 45.929  10.206  -59.487 1.00 47.62  ? 101 PRO A CG  1 
ATOM   837   C CD  . PRO A 1 101 ? 44.797  10.739  -58.658 1.00 47.62  ? 101 PRO A CD  1 
ATOM   838   N N   . TRP A 1 102 ? 44.522  13.743  -60.903 1.00 47.91  ? 102 TRP A N   1 
ATOM   839   C CA  . TRP A 1 102 ? 44.106  14.799  -61.824 1.00 47.58  ? 102 TRP A CA  1 
ATOM   840   C C   . TRP A 1 102 ? 43.919  16.136  -61.146 1.00 50.11  ? 102 TRP A C   1 
ATOM   841   O O   . TRP A 1 102 ? 43.596  17.127  -61.800 1.00 49.32  ? 102 TRP A O   1 
ATOM   842   C CB  . TRP A 1 102 ? 42.868  14.391  -62.621 1.00 47.37  ? 102 TRP A CB  1 
ATOM   843   C CG  . TRP A 1 102 ? 41.606  14.192  -61.808 1.00 45.95  ? 102 TRP A CG  1 
ATOM   844   C CD1 . TRP A 1 102 ? 41.163  13.018  -61.203 1.00 46.43  ? 102 TRP A CD1 1 
ATOM   845   C CD2 . TRP A 1 102 ? 40.557  15.188  -61.522 1.00 46.92  ? 102 TRP A CD2 1 
ATOM   846   N NE1 . TRP A 1 102 ? 39.953  13.218  -60.570 1.00 45.95  ? 102 TRP A NE1 1 
ATOM   847   C CE2 . TRP A 1 102 ? 39.543  14.500  -60.716 1.00 46.20  ? 102 TRP A CE2 1 
ATOM   848   C CE3 . TRP A 1 102 ? 40.378  16.539  -61.822 1.00 46.43  ? 102 TRP A CE3 1 
ATOM   849   C CZ2 . TRP A 1 102 ? 38.405  15.147  -60.255 1.00 45.69  ? 102 TRP A CZ2 1 
ATOM   850   C CZ3 . TRP A 1 102 ? 39.225  17.180  -61.356 1.00 46.14  ? 102 TRP A CZ3 1 
ATOM   851   C CH2 . TRP A 1 102 ? 38.262  16.500  -60.588 1.00 46.35  ? 102 TRP A CH2 1 
ATOM   852   N N   . LEU A 1 103 ? 44.168  16.183  -59.834 1.00 53.01  ? 103 LEU A N   1 
ATOM   853   C CA  . LEU A 1 103 ? 43.937  17.393  -59.042 1.00 56.50  ? 103 LEU A CA  1 
ATOM   854   C C   . LEU A 1 103 ? 45.209  18.042  -58.485 1.00 61.60  ? 103 LEU A C   1 
ATOM   855   O O   . LEU A 1 103 ? 45.140  19.102  -57.857 1.00 59.72  ? 103 LEU A O   1 
ATOM   856   C CB  . LEU A 1 103 ? 42.936  17.120  -57.904 1.00 54.37  ? 103 LEU A CB  1 
ATOM   857   C CG  . LEU A 1 103 ? 41.435  17.204  -58.238 1.00 53.60  ? 103 LEU A CG  1 
ATOM   858   C CD1 . LEU A 1 103 ? 40.572  16.847  -57.031 1.00 51.21  ? 103 LEU A CD1 1 
ATOM   859   C CD2 . LEU A 1 103 ? 41.052  18.574  -58.784 1.00 52.35  ? 103 LEU A CD2 1 
ATOM   860   N N   . GLN A 1 104 ? 46.365  17.426  -58.739 1.00 68.00  ? 104 GLN A N   1 
ATOM   861   C CA  . GLN A 1 104 ? 47.642  17.897  -58.166 1.00 72.28  ? 104 GLN A CA  1 
ATOM   862   C C   . GLN A 1 104 ? 48.090  19.265  -58.679 1.00 72.89  ? 104 GLN A C   1 
ATOM   863   O O   . GLN A 1 104 ? 48.681  20.043  -57.932 1.00 71.73  ? 104 GLN A O   1 
ATOM   864   C CB  . GLN A 1 104 ? 48.759  16.865  -58.366 1.00 74.75  ? 104 GLN A CB  1 
ATOM   865   C CG  . GLN A 1 104 ? 48.578  15.565  -57.584 1.00 80.55  ? 104 GLN A CG  1 
ATOM   866   C CD  . GLN A 1 104 ? 48.467  15.773  -56.077 1.00 85.30  ? 104 GLN A CD  1 
ATOM   867   O OE1 . GLN A 1 104 ? 47.388  16.081  -55.550 1.00 86.75  ? 104 GLN A OE1 1 
ATOM   868   N NE2 . GLN A 1 104 ? 49.578  15.574  -55.370 1.00 86.53  ? 104 GLN A NE2 1 
ATOM   869   N N   . ASN A 1 105 ? 47.798  19.555  -59.946 1.00 75.44  ? 105 ASN A N   1 
ATOM   870   C CA  . ASN A 1 105 ? 48.164  20.846  -60.559 1.00 80.35  ? 105 ASN A CA  1 
ATOM   871   C C   . ASN A 1 105 ? 47.253  22.022  -60.164 1.00 79.32  ? 105 ASN A C   1 
ATOM   872   O O   . ASN A 1 105 ? 47.395  23.132  -60.686 1.00 79.59  ? 105 ASN A O   1 
ATOM   873   C CB  . ASN A 1 105 ? 48.255  20.722  -62.093 1.00 85.94  ? 105 ASN A CB  1 
ATOM   874   C CG  . ASN A 1 105 ? 47.043  20.023  -62.711 1.00 90.90  ? 105 ASN A CG  1 
ATOM   875   O OD1 . ASN A 1 105 ? 45.998  19.851  -62.069 1.00 86.10  ? 105 ASN A OD1 1 
ATOM   876   N ND2 . ASN A 1 105 ? 47.184  19.614  -63.971 1.00 91.07  ? 105 ASN A ND2 1 
ATOM   877   N N   . VAL A 1 106 ? 46.322  21.761  -59.248 1.00 77.04  ? 106 VAL A N   1 
ATOM   878   C CA  . VAL A 1 106 ? 45.390  22.773  -58.743 1.00 75.20  ? 106 VAL A CA  1 
ATOM   879   C C   . VAL A 1 106 ? 45.694  23.011  -57.264 1.00 75.69  ? 106 VAL A C   1 
ATOM   880   O O   . VAL A 1 106 ? 45.790  22.054  -56.486 1.00 73.62  ? 106 VAL A O   1 
ATOM   881   C CB  . VAL A 1 106 ? 43.916  22.306  -58.895 1.00 73.14  ? 106 VAL A CB  1 
ATOM   882   C CG1 . VAL A 1 106 ? 42.948  23.410  -58.497 1.00 72.02  ? 106 VAL A CG1 1 
ATOM   883   C CG2 . VAL A 1 106 ? 43.634  21.834  -60.316 1.00 69.66  ? 106 VAL A CG2 1 
ATOM   884   N N   . GLU A 1 107 ? 45.849  24.275  -56.870 1.00 78.09  ? 107 GLU A N   1 
ATOM   885   C CA  . GLU A 1 107 ? 46.126  24.581  -55.462 1.00 82.32  ? 107 GLU A CA  1 
ATOM   886   C C   . GLU A 1 107 ? 44.943  24.226  -54.536 1.00 78.49  ? 107 GLU A C   1 
ATOM   887   O O   . GLU A 1 107 ? 43.777  24.481  -54.870 1.00 73.09  ? 107 GLU A O   1 
ATOM   888   C CB  . GLU A 1 107 ? 46.629  26.028  -55.259 1.00 92.07  ? 107 GLU A CB  1 
ATOM   889   C CG  . GLU A 1 107 ? 45.554  27.102  -55.189 1.00 98.95  ? 107 GLU A CG  1 
ATOM   890   C CD  . GLU A 1 107 ? 45.218  27.687  -56.547 1.00 105.51 ? 107 GLU A CD  1 
ATOM   891   O OE1 . GLU A 1 107 ? 44.829  26.913  -57.456 1.00 108.24 ? 107 GLU A OE1 1 
ATOM   892   O OE2 . GLU A 1 107 ? 45.334  28.923  -56.703 1.00 105.71 ? 107 GLU A OE2 1 
ATOM   893   N N   . PRO A 1 108 ? 45.256  23.604  -53.382 1.00 77.46  ? 108 PRO A N   1 
ATOM   894   C CA  . PRO A 1 108 ? 44.328  22.910  -52.485 1.00 76.16  ? 108 PRO A CA  1 
ATOM   895   C C   . PRO A 1 108 ? 42.931  23.523  -52.343 1.00 76.44  ? 108 PRO A C   1 
ATOM   896   O O   . PRO A 1 108 ? 41.946  22.783  -52.300 1.00 73.06  ? 108 PRO A O   1 
ATOM   897   C CB  . PRO A 1 108 ? 45.065  22.943  -51.146 1.00 76.52  ? 108 PRO A CB  1 
ATOM   898   C CG  . PRO A 1 108 ? 46.509  22.877  -51.529 1.00 76.62  ? 108 PRO A CG  1 
ATOM   899   C CD  . PRO A 1 108 ? 46.648  23.514  -52.890 1.00 76.58  ? 108 PRO A CD  1 
ATOM   900   N N   . ASN A 1 109 ? 42.850  24.853  -52.279 1.00 78.93  ? 109 ASN A N   1 
ATOM   901   C CA  . ASN A 1 109 ? 41.590  25.540  -51.949 1.00 79.67  ? 109 ASN A CA  1 
ATOM   902   C C   . ASN A 1 109 ? 40.496  25.503  -53.035 1.00 75.35  ? 109 ASN A C   1 
ATOM   903   O O   . ASN A 1 109 ? 39.315  25.694  -52.730 1.00 77.15  ? 109 ASN A O   1 
ATOM   904   C CB  . ASN A 1 109 ? 41.848  26.982  -51.460 1.00 82.86  ? 109 ASN A CB  1 
ATOM   905   C CG  . ASN A 1 109 ? 42.639  27.814  -52.462 1.00 90.01  ? 109 ASN A CG  1 
ATOM   906   O OD1 . ASN A 1 109 ? 42.078  28.370  -53.411 1.00 90.83  ? 109 ASN A OD1 1 
ATOM   907   N ND2 . ASN A 1 109 ? 43.950  27.917  -52.245 1.00 91.43  ? 109 ASN A ND2 1 
ATOM   908   N N   . LEU A 1 110 ? 40.885  25.248  -54.286 1.00 69.31  ? 110 LEU A N   1 
ATOM   909   C CA  . LEU A 1 110 ? 39.916  25.120  -55.384 1.00 63.75  ? 110 LEU A CA  1 
ATOM   910   C C   . LEU A 1 110 ? 39.492  23.670  -55.642 1.00 61.50  ? 110 LEU A C   1 
ATOM   911   O O   . LEU A 1 110 ? 38.560  23.418  -56.411 1.00 62.24  ? 110 LEU A O   1 
ATOM   912   C CB  . LEU A 1 110 ? 40.465  25.726  -56.684 1.00 64.88  ? 110 LEU A CB  1 
ATOM   913   C CG  . LEU A 1 110 ? 40.634  27.244  -56.834 1.00 65.19  ? 110 LEU A CG  1 
ATOM   914   C CD1 . LEU A 1 110 ? 40.482  27.632  -58.298 1.00 64.16  ? 110 LEU A CD1 1 
ATOM   915   C CD2 . LEU A 1 110 ? 39.644  28.018  -55.982 1.00 64.75  ? 110 LEU A CD2 1 
ATOM   916   N N   . ARG A 1 111 ? 40.175  22.723  -55.000 1.00 56.82  ? 111 ARG A N   1 
ATOM   917   C CA  . ARG A 1 111 ? 39.963  21.304  -55.264 1.00 54.72  ? 111 ARG A CA  1 
ATOM   918   C C   . ARG A 1 111 ? 38.534  20.828  -54.972 1.00 54.61  ? 111 ARG A C   1 
ATOM   919   O O   . ARG A 1 111 ? 37.890  20.243  -55.856 1.00 54.25  ? 111 ARG A O   1 
ATOM   920   C CB  . ARG A 1 111 ? 40.984  20.446  -54.514 1.00 53.56  ? 111 ARG A CB  1 
ATOM   921   C CG  . ARG A 1 111 ? 42.340  20.416  -55.180 1.00 54.99  ? 111 ARG A CG  1 
ATOM   922   C CD  . ARG A 1 111 ? 43.384  19.758  -54.304 1.00 55.93  ? 111 ARG A CD  1 
ATOM   923   N NE  . ARG A 1 111 ? 44.727  19.964  -54.846 1.00 57.65  ? 111 ARG A NE  1 
ATOM   924   C CZ  . ARG A 1 111 ? 45.834  19.437  -54.330 1.00 57.24  ? 111 ARG A CZ  1 
ATOM   925   N NH1 . ARG A 1 111 ? 45.768  18.662  -53.252 1.00 59.34  ? 111 ARG A NH1 1 
ATOM   926   N NH2 . ARG A 1 111 ? 47.005  19.689  -54.888 1.00 53.47  ? 111 ARG A NH2 1 
ATOM   927   N N   . PRO A 1 112 ? 38.032  21.070  -53.736 1.00 50.68  ? 112 PRO A N   1 
ATOM   928   C CA  . PRO A 1 112 ? 36.700  20.579  -53.420 1.00 49.05  ? 112 PRO A CA  1 
ATOM   929   C C   . PRO A 1 112 ? 35.658  20.972  -54.451 1.00 48.21  ? 112 PRO A C   1 
ATOM   930   O O   . PRO A 1 112 ? 34.819  20.150  -54.796 1.00 49.74  ? 112 PRO A O   1 
ATOM   931   C CB  . PRO A 1 112 ? 36.405  21.219  -52.058 1.00 51.43  ? 112 PRO A CB  1 
ATOM   932   C CG  . PRO A 1 112 ? 37.748  21.295  -51.408 1.00 51.41  ? 112 PRO A CG  1 
ATOM   933   C CD  . PRO A 1 112 ? 38.720  21.589  -52.536 1.00 51.50  ? 112 PRO A CD  1 
ATOM   934   N N   . LYS A 1 113 ? 35.729  22.197  -54.963 1.00 50.54  ? 113 LYS A N   1 
ATOM   935   C CA  . LYS A 1 113 ? 34.749  22.687  -55.941 1.00 51.81  ? 113 LYS A CA  1 
ATOM   936   C C   . LYS A 1 113 ? 34.807  21.900  -57.241 1.00 49.09  ? 113 LYS A C   1 
ATOM   937   O O   . LYS A 1 113 ? 33.772  21.614  -57.857 1.00 47.59  ? 113 LYS A O   1 
ATOM   938   C CB  . LYS A 1 113 ? 34.982  24.164  -56.244 1.00 57.49  ? 113 LYS A CB  1 
ATOM   939   C CG  . LYS A 1 113 ? 33.739  24.904  -56.712 1.00 63.47  ? 113 LYS A CG  1 
ATOM   940   C CD  . LYS A 1 113 ? 33.259  25.903  -55.657 1.00 68.99  ? 113 LYS A CD  1 
ATOM   941   C CE  . LYS A 1 113 ? 32.663  25.204  -54.438 1.00 70.87  ? 113 LYS A CE  1 
ATOM   942   N NZ  . LYS A 1 113 ? 32.772  26.041  -53.209 1.00 75.66  ? 113 LYS A NZ  1 
ATOM   943   N N   . LEU A 1 114 ? 36.020  21.570  -57.668 1.00 47.17  ? 114 LEU A N   1 
ATOM   944   C CA  . LEU A 1 114 ? 36.205  20.798  -58.884 1.00 45.82  ? 114 LEU A CA  1 
ATOM   945   C C   . LEU A 1 114 ? 35.721  19.359  -58.695 1.00 43.53  ? 114 LEU A C   1 
ATOM   946   O O   . LEU A 1 114 ? 34.944  18.851  -59.508 1.00 42.84  ? 114 LEU A O   1 
ATOM   947   C CB  . LEU A 1 114 ? 37.662  20.839  -59.331 1.00 47.05  ? 114 LEU A CB  1 
ATOM   948   C CG  . LEU A 1 114 ? 38.035  22.038  -60.204 1.00 50.08  ? 114 LEU A CG  1 
ATOM   949   C CD1 . LEU A 1 114 ? 39.541  22.132  -60.377 1.00 50.48  ? 114 LEU A CD1 1 
ATOM   950   C CD2 . LEU A 1 114 ? 37.342  21.968  -61.561 1.00 51.00  ? 114 LEU A CD2 1 
ATOM   951   N N   . LEU A 1 115 ? 36.154  18.716  -57.612 1.00 41.62  ? 115 LEU A N   1 
ATOM   952   C CA  . LEU A 1 115 ? 35.721  17.351  -57.326 1.00 41.04  ? 115 LEU A CA  1 
ATOM   953   C C   . LEU A 1 115 ? 34.195  17.253  -57.313 1.00 40.26  ? 115 LEU A C   1 
ATOM   954   O O   . LEU A 1 115 ? 33.615  16.330  -57.909 1.00 44.23  ? 115 LEU A O   1 
ATOM   955   C CB  . LEU A 1 115 ? 36.305  16.841  -56.010 1.00 40.73  ? 115 LEU A CB  1 
ATOM   956   C CG  . LEU A 1 115 ? 35.980  15.374  -55.700 1.00 41.99  ? 115 LEU A CG  1 
ATOM   957   C CD1 . LEU A 1 115 ? 36.532  14.402  -56.752 1.00 40.23  ? 115 LEU A CD1 1 
ATOM   958   C CD2 . LEU A 1 115 ? 36.478  15.003  -54.313 1.00 42.37  ? 115 LEU A CD2 1 
ATOM   959   N N   . LEU A 1 116 ? 33.550  18.226  -56.681 1.00 36.95  ? 116 LEU A N   1 
ATOM   960   C CA  . LEU A 1 116 ? 32.089  18.287  -56.633 1.00 37.07  ? 116 LEU A CA  1 
ATOM   961   C C   . LEU A 1 116 ? 31.531  18.385  -58.034 1.00 36.84  ? 116 LEU A C   1 
ATOM   962   O O   . LEU A 1 116 ? 30.596  17.676  -58.395 1.00 35.66  ? 116 LEU A O   1 
ATOM   963   C CB  . LEU A 1 116 ? 31.601  19.484  -55.788 1.00 36.00  ? 116 LEU A CB  1 
ATOM   964   C CG  . LEU A 1 116 ? 30.088  19.793  -55.834 1.00 36.58  ? 116 LEU A CG  1 
ATOM   965   C CD1 . LEU A 1 116 ? 29.321  18.725  -55.069 1.00 35.33  ? 116 LEU A CD1 1 
ATOM   966   C CD2 . LEU A 1 116 ? 29.736  21.195  -55.308 1.00 35.40  ? 116 LEU A CD2 1 
ATOM   967   N N   . LYS A 1 117 ? 32.121  19.269  -58.823 1.00 39.14  ? 117 LYS A N   1 
ATOM   968   C CA  . LYS A 1 117 ? 31.655  19.520  -60.175 1.00 41.43  ? 117 LYS A CA  1 
ATOM   969   C C   . LYS A 1 117 ? 31.792  18.263  -61.062 1.00 39.84  ? 117 LYS A C   1 
ATOM   970   O O   . LYS A 1 117 ? 30.884  17.936  -61.833 1.00 38.84  ? 117 LYS A O   1 
ATOM   971   C CB  . LYS A 1 117 ? 32.430  20.688  -60.759 1.00 43.63  ? 117 LYS A CB  1 
ATOM   972   C CG  . LYS A 1 117 ? 31.893  21.214  -62.065 1.00 47.65  ? 117 LYS A CG  1 
ATOM   973   C CD  . LYS A 1 117 ? 33.043  21.745  -62.912 1.00 49.56  ? 117 LYS A CD  1 
ATOM   974   C CE  . LYS A 1 117 ? 32.602  22.929  -63.738 1.00 54.06  ? 117 LYS A CE  1 
ATOM   975   N NZ  . LYS A 1 117 ? 33.764  23.793  -64.083 1.00 60.85  ? 117 LYS A NZ  1 
ATOM   976   N N   . HIS A 1 118 ? 32.909  17.550  -60.921 1.00 39.04  ? 118 HIS A N   1 
ATOM   977   C CA  . HIS A 1 118 ? 33.149  16.319  -61.704 1.00 40.03  ? 118 HIS A CA  1 
ATOM   978   C C   . HIS A 1 118 ? 32.356  15.144  -61.208 1.00 39.09  ? 118 HIS A C   1 
ATOM   979   O O   . HIS A 1 118 ? 31.798  14.381  -62.019 1.00 41.26  ? 118 HIS A O   1 
ATOM   980   C CB  . HIS A 1 118 ? 34.644  15.996  -61.785 1.00 40.57  ? 118 HIS A CB  1 
ATOM   981   C CG  . HIS A 1 118 ? 35.433  17.013  -62.573 1.00 43.36  ? 118 HIS A CG  1 
ATOM   982   N ND1 . HIS A 1 118 ? 36.200  16.681  -63.633 1.00 44.92  ? 118 HIS A ND1 1 
ATOM   983   C CD2 . HIS A 1 118 ? 35.515  18.404  -62.449 1.00 43.69  ? 118 HIS A CD2 1 
ATOM   984   C CE1 . HIS A 1 118 ? 36.757  17.799  -64.144 1.00 45.30  ? 118 HIS A CE1 1 
ATOM   985   N NE2 . HIS A 1 118 ? 36.329  18.850  -63.424 1.00 43.32  ? 118 HIS A NE2 1 
ATOM   986   N N   . ASN A 1 119 ? 32.269  14.993  -59.883 1.00 36.80  ? 119 ASN A N   1 
ATOM   987   C CA  . ASN A 1 119 ? 31.378  14.007  -59.307 1.00 34.99  ? 119 ASN A CA  1 
ATOM   988   C C   . ASN A 1 119 ? 29.964  14.208  -59.835 1.00 34.40  ? 119 ASN A C   1 
ATOM   989   O O   . ASN A 1 119 ? 29.317  13.250  -60.305 1.00 34.47  ? 119 ASN A O   1 
ATOM   990   C CB  . ASN A 1 119 ? 31.381  14.066  -57.768 1.00 35.40  ? 119 ASN A CB  1 
ATOM   991   C CG  . ASN A 1 119 ? 32.502  13.254  -57.141 1.00 34.30  ? 119 ASN A CG  1 
ATOM   992   O OD1 . ASN A 1 119 ? 32.659  13.243  -55.914 1.00 38.66  ? 119 ASN A OD1 1 
ATOM   993   N ND2 . ASN A 1 119 ? 33.288  12.597  -57.958 1.00 32.24  ? 119 ASN A ND2 1 
ATOM   994   N N   . LEU A 1 120 ? 29.478  15.444  -59.780 1.00 31.65  ? 120 LEU A N   1 
ATOM   995   C CA  . LEU A 1 120 ? 28.160  15.734  -60.326 1.00 32.59  ? 120 LEU A CA  1 
ATOM   996   C C   . LEU A 1 120 ? 28.061  15.312  -61.806 1.00 34.35  ? 120 LEU A C   1 
ATOM   997   O O   . LEU A 1 120 ? 27.072  14.693  -62.224 1.00 37.00  ? 120 LEU A O   1 
ATOM   998   C CB  . LEU A 1 120 ? 27.785  17.212  -60.138 1.00 32.70  ? 120 LEU A CB  1 
ATOM   999   C CG  . LEU A 1 120 ? 27.321  17.678  -58.739 1.00 32.86  ? 120 LEU A CG  1 
ATOM   1000  C CD1 . LEU A 1 120 ? 27.166  19.201  -58.704 1.00 32.93  ? 120 LEU A CD1 1 
ATOM   1001  C CD2 . LEU A 1 120 ? 26.024  16.986  -58.310 1.00 30.55  ? 120 LEU A CD2 1 
ATOM   1002  N N   . PHE A 1 121 ? 29.091  15.611  -62.594 1.00 34.02  ? 121 PHE A N   1 
ATOM   1003  C CA  . PHE A 1 121 ? 29.055  15.221  -63.994 1.00 34.72  ? 121 PHE A CA  1 
ATOM   1004  C C   . PHE A 1 121 ? 28.870  13.717  -64.107 1.00 33.78  ? 121 PHE A C   1 
ATOM   1005  O O   . PHE A 1 121 ? 27.944  13.256  -64.781 1.00 34.48  ? 121 PHE A O   1 
ATOM   1006  C CB  . PHE A 1 121 ? 30.304  15.685  -64.768 1.00 34.83  ? 121 PHE A CB  1 
ATOM   1007  C CG  . PHE A 1 121 ? 30.309  15.251  -66.210 1.00 34.36  ? 121 PHE A CG  1 
ATOM   1008  C CD1 . PHE A 1 121 ? 30.712  13.970  -66.564 1.00 33.08  ? 121 PHE A CD1 1 
ATOM   1009  C CD2 . PHE A 1 121 ? 29.876  16.118  -67.216 1.00 34.86  ? 121 PHE A CD2 1 
ATOM   1010  C CE1 . PHE A 1 121 ? 30.702  13.572  -67.887 1.00 34.05  ? 121 PHE A CE1 1 
ATOM   1011  C CE2 . PHE A 1 121 ? 29.842  15.714  -68.532 1.00 33.65  ? 121 PHE A CE2 1 
ATOM   1012  C CZ  . PHE A 1 121 ? 30.262  14.443  -68.869 1.00 33.61  ? 121 PHE A CZ  1 
ATOM   1013  N N   . LEU A 1 122 ? 29.737  12.953  -63.439 1.00 33.99  ? 122 LEU A N   1 
ATOM   1014  C CA  . LEU A 1 122 ? 29.625  11.478  -63.452 1.00 32.97  ? 122 LEU A CA  1 
ATOM   1015  C C   . LEU A 1 122 ? 28.229  10.983  -63.090 1.00 33.67  ? 122 LEU A C   1 
ATOM   1016  O O   . LEU A 1 122 ? 27.633  10.198  -63.825 1.00 35.56  ? 122 LEU A O   1 
ATOM   1017  C CB  . LEU A 1 122 ? 30.665  10.831  -62.546 1.00 31.74  ? 122 LEU A CB  1 
ATOM   1018  C CG  . LEU A 1 122 ? 32.119  10.974  -63.003 1.00 32.46  ? 122 LEU A CG  1 
ATOM   1019  C CD1 . LEU A 1 122 ? 33.091  10.523  -61.914 1.00 30.67  ? 122 LEU A CD1 1 
ATOM   1020  C CD2 . LEU A 1 122 ? 32.345  10.216  -64.311 1.00 32.00  ? 122 LEU A CD2 1 
ATOM   1021  N N   . LEU A 1 123 ? 27.692  11.460  -61.973 1.00 34.78  ? 123 LEU A N   1 
ATOM   1022  C CA  . LEU A 1 123 ? 26.383  10.999  -61.529 1.00 33.65  ? 123 LEU A CA  1 
ATOM   1023  C C   . LEU A 1 123 ? 25.306  11.387  -62.522 1.00 34.21  ? 123 LEU A C   1 
ATOM   1024  O O   . LEU A 1 123 ? 24.349  10.640  -62.704 1.00 35.20  ? 123 LEU A O   1 
ATOM   1025  C CB  . LEU A 1 123 ? 26.020  11.560  -60.151 1.00 33.07  ? 123 LEU A CB  1 
ATOM   1026  C CG  . LEU A 1 123 ? 26.873  11.234  -58.934 1.00 33.77  ? 123 LEU A CG  1 
ATOM   1027  C CD1 . LEU A 1 123 ? 26.534  12.225  -57.827 1.00 33.14  ? 123 LEU A CD1 1 
ATOM   1028  C CD2 . LEU A 1 123 ? 26.704  9.789   -58.460 1.00 31.85  ? 123 LEU A CD2 1 
ATOM   1029  N N   . ASP A 1 124 ? 25.436  12.565  -63.137 1.00 34.08  ? 124 ASP A N   1 
ATOM   1030  C CA  . ASP A 1 124 ? 24.363  13.075  -63.983 1.00 34.39  ? 124 ASP A CA  1 
ATOM   1031  C C   . ASP A 1 124 ? 24.411  12.394  -65.332 1.00 34.04  ? 124 ASP A C   1 
ATOM   1032  O O   . ASP A 1 124 ? 23.375  12.095  -65.905 1.00 34.82  ? 124 ASP A O   1 
ATOM   1033  C CB  . ASP A 1 124 ? 24.443  14.607  -64.169 1.00 35.75  ? 124 ASP A CB  1 
ATOM   1034  C CG  . ASP A 1 124 ? 23.944  15.404  -62.939 1.00 38.17  ? 124 ASP A CG  1 
ATOM   1035  O OD1 . ASP A 1 124 ? 23.040  14.942  -62.185 1.00 37.15  ? 124 ASP A OD1 1 
ATOM   1036  O OD2 . ASP A 1 124 ? 24.449  16.533  -62.755 1.00 38.72  ? 124 ASP A OD2 1 
ATOM   1037  N N   . ASN A 1 125 ? 25.620  12.149  -65.836 1.00 33.27  ? 125 ASN A N   1 
ATOM   1038  C CA  . ASN A 1 125 ? 25.805  11.667  -67.216 1.00 33.53  ? 125 ASN A CA  1 
ATOM   1039  C C   . ASN A 1 125 ? 26.056  10.146  -67.386 1.00 33.22  ? 125 ASN A C   1 
ATOM   1040  O O   . ASN A 1 125 ? 25.856  9.589   -68.460 1.00 34.51  ? 125 ASN A O   1 
ATOM   1041  C CB  . ASN A 1 125 ? 26.899  12.483  -67.901 1.00 32.60  ? 125 ASN A CB  1 
ATOM   1042  C CG  . ASN A 1 125 ? 26.531  13.952  -68.008 1.00 33.43  ? 125 ASN A CG  1 
ATOM   1043  O OD1 . ASN A 1 125 ? 26.970  14.772  -67.206 1.00 34.99  ? 125 ASN A OD1 1 
ATOM   1044  N ND2 . ASN A 1 125 ? 25.653  14.269  -68.933 1.00 32.15  ? 125 ASN A ND2 1 
ATOM   1045  N N   . ILE A 1 126 ? 26.475  9.486   -66.322 1.00 32.41  ? 126 ILE A N   1 
ATOM   1046  C CA  . ILE A 1 126 ? 26.950  8.110   -66.428 1.00 31.47  ? 126 ILE A CA  1 
ATOM   1047  C C   . ILE A 1 126 ? 26.230  7.207   -65.437 1.00 30.56  ? 126 ILE A C   1 
ATOM   1048  O O   . ILE A 1 126 ? 25.653  6.198   -65.825 1.00 32.04  ? 126 ILE A O   1 
ATOM   1049  C CB  . ILE A 1 126 ? 28.486  8.057   -66.240 1.00 30.72  ? 126 ILE A CB  1 
ATOM   1050  C CG1 . ILE A 1 126 ? 29.152  9.007   -67.251 1.00 29.62  ? 126 ILE A CG1 1 
ATOM   1051  C CG2 . ILE A 1 126 ? 29.006  6.618   -66.315 1.00 29.44  ? 126 ILE A CG2 1 
ATOM   1052  C CD1 . ILE A 1 126 ? 30.581  8.678   -67.609 1.00 30.05  ? 126 ILE A CD1 1 
ATOM   1053  N N   . VAL A 1 127 ? 26.188  7.613   -64.173 1.00 29.16  ? 127 VAL A N   1 
ATOM   1054  C CA  . VAL A 1 127 ? 25.585  6.749   -63.137 1.00 28.81  ? 127 VAL A CA  1 
ATOM   1055  C C   . VAL A 1 127 ? 24.086  6.632   -63.288 1.00 27.45  ? 127 VAL A C   1 
ATOM   1056  O O   . VAL A 1 127 ? 23.564  5.542   -63.436 1.00 27.91  ? 127 VAL A O   1 
ATOM   1057  C CB  . VAL A 1 127 ? 25.977  7.164   -61.708 1.00 28.02  ? 127 VAL A CB  1 
ATOM   1058  C CG1 . VAL A 1 127 ? 25.297  6.264   -60.694 1.00 26.72  ? 127 VAL A CG1 1 
ATOM   1059  C CG2 . VAL A 1 127 ? 27.503  7.104   -61.550 1.00 27.84  ? 127 VAL A CG2 1 
ATOM   1060  N N   . LYS A 1 128 ? 23.392  7.752   -63.300 1.00 27.71  ? 128 LYS A N   1 
ATOM   1061  C CA  . LYS A 1 128 ? 21.954  7.708   -63.539 1.00 28.55  ? 128 LYS A CA  1 
ATOM   1062  C C   . LYS A 1 128 ? 21.570  7.117   -64.913 1.00 30.05  ? 128 LYS A C   1 
ATOM   1063  O O   . LYS A 1 128 ? 20.730  6.224   -64.970 1.00 30.50  ? 128 LYS A O   1 
ATOM   1064  C CB  . LYS A 1 128 ? 21.314  9.057   -63.268 1.00 28.38  ? 128 LYS A CB  1 
ATOM   1065  C CG  . LYS A 1 128 ? 21.191  9.322   -61.780 1.00 28.51  ? 128 LYS A CG  1 
ATOM   1066  C CD  . LYS A 1 128 ? 20.947  10.780  -61.492 1.00 28.98  ? 128 LYS A CD  1 
ATOM   1067  C CE  . LYS A 1 128 ? 20.685  10.965  -60.005 1.00 28.52  ? 128 LYS A CE  1 
ATOM   1068  N NZ  . LYS A 1 128 ? 20.003  12.258  -59.735 1.00 28.78  ? 128 LYS A NZ  1 
ATOM   1069  N N   . PRO A 1 129 ? 22.224  7.569   -66.015 1.00 30.79  ? 129 PRO A N   1 
ATOM   1070  C CA  . PRO A 1 129 ? 21.885  6.939   -67.305 1.00 31.81  ? 129 PRO A CA  1 
ATOM   1071  C C   . PRO A 1 129 ? 22.179  5.431   -67.417 1.00 32.49  ? 129 PRO A C   1 
ATOM   1072  O O   . PRO A 1 129 ? 21.382  4.711   -68.047 1.00 32.55  ? 129 PRO A O   1 
ATOM   1073  C CB  . PRO A 1 129 ? 22.707  7.746   -68.311 1.00 32.19  ? 129 PRO A CB  1 
ATOM   1074  C CG  . PRO A 1 129 ? 22.733  9.118   -67.703 1.00 31.88  ? 129 PRO A CG  1 
ATOM   1075  C CD  . PRO A 1 129 ? 22.907  8.863   -66.219 1.00 31.02  ? 129 PRO A CD  1 
ATOM   1076  N N   . ILE A 1 130 ? 23.286  4.941   -66.830 1.00 31.82  ? 130 ILE A N   1 
ATOM   1077  C CA  . ILE A 1 130 ? 23.513  3.483   -66.830 1.00 30.73  ? 130 ILE A CA  1 
ATOM   1078  C C   . ILE A 1 130 ? 22.367  2.698   -66.192 1.00 30.73  ? 130 ILE A C   1 
ATOM   1079  O O   . ILE A 1 130 ? 21.884  1.715   -66.760 1.00 31.47  ? 130 ILE A O   1 
ATOM   1080  C CB  . ILE A 1 130 ? 24.865  3.043   -66.247 1.00 30.01  ? 130 ILE A CB  1 
ATOM   1081  C CG1 . ILE A 1 130 ? 25.171  1.634   -66.737 1.00 29.93  ? 130 ILE A CG1 1 
ATOM   1082  C CG2 . ILE A 1 130 ? 24.866  3.045   -64.721 1.00 28.63  ? 130 ILE A CG2 1 
ATOM   1083  C CD1 . ILE A 1 130 ? 26.470  1.550   -67.485 1.00 31.64  ? 130 ILE A CD1 1 
ATOM   1084  N N   . ILE A 1 131 ? 21.918  3.161   -65.033 1.00 30.57  ? 131 ILE A N   1 
ATOM   1085  C CA  . ILE A 1 131 ? 20.777  2.566   -64.355 1.00 32.12  ? 131 ILE A CA  1 
ATOM   1086  C C   . ILE A 1 131 ? 19.541  2.604   -65.263 1.00 33.74  ? 131 ILE A C   1 
ATOM   1087  O O   . ILE A 1 131 ? 18.878  1.575   -65.450 1.00 35.36  ? 131 ILE A O   1 
ATOM   1088  C CB  . ILE A 1 131 ? 20.542  3.230   -62.967 1.00 32.78  ? 131 ILE A CB  1 
ATOM   1089  C CG1 . ILE A 1 131 ? 21.781  3.020   -62.090 1.00 31.12  ? 131 ILE A CG1 1 
ATOM   1090  C CG2 . ILE A 1 131 ? 19.330  2.640   -62.242 1.00 33.56  ? 131 ILE A CG2 1 
ATOM   1091  C CD1 . ILE A 1 131 ? 21.767  3.848   -60.826 1.00 31.02  ? 131 ILE A CD1 1 
ATOM   1092  N N   . ALA A 1 132 ? 19.290  3.753   -65.897 1.00 33.31  ? 132 ALA A N   1 
ATOM   1093  C CA  . ALA A 1 132 ? 18.119  3.923   -66.762 1.00 34.42  ? 132 ALA A CA  1 
ATOM   1094  C C   . ALA A 1 132 ? 18.196  3.037   -67.992 1.00 36.00  ? 132 ALA A C   1 
ATOM   1095  O O   . ALA A 1 132 ? 17.169  2.632   -68.540 1.00 35.35  ? 132 ALA A O   1 
ATOM   1096  C CB  . ALA A 1 132 ? 17.968  5.378   -67.179 1.00 34.72  ? 132 ALA A CB  1 
ATOM   1097  N N   . PHE A 1 133 ? 19.424  2.753   -68.429 1.00 36.02  ? 133 PHE A N   1 
ATOM   1098  C CA  . PHE A 1 133 ? 19.648  1.971   -69.626 1.00 36.47  ? 133 PHE A CA  1 
ATOM   1099  C C   . PHE A 1 133 ? 19.247  0.532   -69.390 1.00 36.50  ? 133 PHE A C   1 
ATOM   1100  O O   . PHE A 1 133 ? 18.686  -0.108  -70.272 1.00 39.62  ? 133 PHE A O   1 
ATOM   1101  C CB  . PHE A 1 133 ? 21.121  2.046   -70.070 1.00 37.49  ? 133 PHE A CB  1 
ATOM   1102  C CG  . PHE A 1 133 ? 21.393  1.339   -71.378 1.00 39.48  ? 133 PHE A CG  1 
ATOM   1103  C CD1 . PHE A 1 133 ? 20.962  1.890   -72.590 1.00 40.15  ? 133 PHE A CD1 1 
ATOM   1104  C CD2 . PHE A 1 133 ? 22.065  0.119   -71.401 1.00 39.56  ? 133 PHE A CD2 1 
ATOM   1105  C CE1 . PHE A 1 133 ? 21.209  1.241   -73.792 1.00 41.26  ? 133 PHE A CE1 1 
ATOM   1106  C CE2 . PHE A 1 133 ? 22.310  -0.537  -72.602 1.00 42.03  ? 133 PHE A CE2 1 
ATOM   1107  C CZ  . PHE A 1 133 ? 21.882  0.023   -73.799 1.00 41.35  ? 133 PHE A CZ  1 
ATOM   1108  N N   . TYR A 1 134 ? 19.533  0.030   -68.191 1.00 36.32  ? 134 TYR A N   1 
ATOM   1109  C CA  . TYR A 1 134 ? 19.248  -1.367  -67.843 1.00 35.53  ? 134 TYR A CA  1 
ATOM   1110  C C   . TYR A 1 134 ? 17.970  -1.582  -67.021 1.00 36.77  ? 134 TYR A C   1 
ATOM   1111  O O   . TYR A 1 134 ? 17.431  -2.693  -67.001 1.00 36.91  ? 134 TYR A O   1 
ATOM   1112  C CB  . TYR A 1 134 ? 20.458  -1.994  -67.132 1.00 33.82  ? 134 TYR A CB  1 
ATOM   1113  C CG  . TYR A 1 134 ? 21.705  -2.079  -68.014 1.00 33.77  ? 134 TYR A CG  1 
ATOM   1114  C CD1 . TYR A 1 134 ? 21.735  -2.916  -69.123 1.00 33.55  ? 134 TYR A CD1 1 
ATOM   1115  C CD2 . TYR A 1 134 ? 22.842  -1.318  -67.729 1.00 31.72  ? 134 TYR A CD2 1 
ATOM   1116  C CE1 . TYR A 1 134 ? 22.862  -3.013  -69.921 1.00 35.09  ? 134 TYR A CE1 1 
ATOM   1117  C CE2 . TYR A 1 134 ? 23.971  -1.391  -68.523 1.00 32.04  ? 134 TYR A CE2 1 
ATOM   1118  C CZ  . TYR A 1 134 ? 23.984  -2.252  -69.618 1.00 34.43  ? 134 TYR A CZ  1 
ATOM   1119  O OH  . TYR A 1 134 ? 25.089  -2.332  -70.439 1.00 33.29  ? 134 TYR A OH  1 
ATOM   1120  N N   . TYR A 1 135 ? 17.487  -0.537  -66.338 1.00 37.35  ? 135 TYR A N   1 
ATOM   1121  C CA  . TYR A 1 135 ? 16.310  -0.689  -65.449 1.00 38.00  ? 135 TYR A CA  1 
ATOM   1122  C C   . TYR A 1 135 ? 15.210  0.315   -65.660 1.00 39.20  ? 135 TYR A C   1 
ATOM   1123  O O   . TYR A 1 135 ? 15.460  1.465   -65.993 1.00 39.24  ? 135 TYR A O   1 
ATOM   1124  C CB  . TYR A 1 135 ? 16.720  -0.656  -63.982 1.00 35.43  ? 135 TYR A CB  1 
ATOM   1125  C CG  . TYR A 1 135 ? 17.623  -1.781  -63.612 1.00 36.99  ? 135 TYR A CG  1 
ATOM   1126  C CD1 . TYR A 1 135 ? 17.110  -2.972  -63.132 1.00 37.30  ? 135 TYR A CD1 1 
ATOM   1127  C CD2 . TYR A 1 135 ? 19.010  -1.661  -63.750 1.00 37.09  ? 135 TYR A CD2 1 
ATOM   1128  C CE1 . TYR A 1 135 ? 17.944  -4.015  -62.799 1.00 39.13  ? 135 TYR A CE1 1 
ATOM   1129  C CE2 . TYR A 1 135 ? 19.845  -2.699  -63.417 1.00 37.23  ? 135 TYR A CE2 1 
ATOM   1130  C CZ  . TYR A 1 135 ? 19.304  -3.871  -62.944 1.00 38.77  ? 135 TYR A CZ  1 
ATOM   1131  O OH  . TYR A 1 135 ? 20.131  -4.907  -62.605 1.00 42.53  ? 135 TYR A OH  1 
ATOM   1132  N N   . LYS A 1 136 ? 13.982  -0.139  -65.427 1.00 42.27  ? 136 LYS A N   1 
ATOM   1133  C CA  . LYS A 1 136 ? 12.832  0.738   -65.326 1.00 42.77  ? 136 LYS A CA  1 
ATOM   1134  C C   . LYS A 1 136 ? 12.523  0.955   -63.847 1.00 40.67  ? 136 LYS A C   1 
ATOM   1135  O O   . LYS A 1 136 ? 12.262  -0.004  -63.115 1.00 42.01  ? 136 LYS A O   1 
ATOM   1136  C CB  . LYS A 1 136 ? 11.635  0.121   -66.062 1.00 47.73  ? 136 LYS A CB  1 
ATOM   1137  C CG  . LYS A 1 136 ? 10.459  1.063   -66.321 1.00 53.26  ? 136 LYS A CG  1 
ATOM   1138  C CD  . LYS A 1 136 ? 10.850  2.263   -67.176 1.00 59.59  ? 136 LYS A CD  1 
ATOM   1139  C CE  . LYS A 1 136 ? 9.716   2.697   -68.101 1.00 62.81  ? 136 LYS A CE  1 
ATOM   1140  N NZ  . LYS A 1 136 ? 8.414   2.752   -67.382 1.00 65.90  ? 136 LYS A NZ  1 
ATOM   1141  N N   . PRO A 1 137 ? 12.589  2.212   -63.388 1.00 39.33  ? 137 PRO A N   1 
ATOM   1142  C CA  . PRO A 1 137 ? 12.163  2.509   -62.026 1.00 39.85  ? 137 PRO A CA  1 
ATOM   1143  C C   . PRO A 1 137 ? 10.640  2.533   -61.913 1.00 43.26  ? 137 PRO A C   1 
ATOM   1144  O O   . PRO A 1 137 ? 9.959   3.234   -62.664 1.00 46.28  ? 137 PRO A O   1 
ATOM   1145  C CB  . PRO A 1 137 ? 12.749  3.895   -61.758 1.00 38.45  ? 137 PRO A CB  1 
ATOM   1146  C CG  . PRO A 1 137 ? 12.933  4.508   -63.099 1.00 38.83  ? 137 PRO A CG  1 
ATOM   1147  C CD  . PRO A 1 137 ? 13.125  3.394   -64.087 1.00 38.51  ? 137 PRO A CD  1 
ATOM   1148  N N   . ILE A 1 138 ? 10.117  1.757   -60.982 1.00 45.38  ? 138 ILE A N   1 
ATOM   1149  C CA  . ILE A 1 138 ? 8.686   1.620   -60.811 1.00 46.98  ? 138 ILE A CA  1 
ATOM   1150  C C   . ILE A 1 138 ? 8.308   2.055   -59.391 1.00 46.77  ? 138 ILE A C   1 
ATOM   1151  O O   . ILE A 1 138 ? 8.831   1.511   -58.411 1.00 46.07  ? 138 ILE A O   1 
ATOM   1152  C CB  . ILE A 1 138 ? 8.239   0.159   -61.117 1.00 48.45  ? 138 ILE A CB  1 
ATOM   1153  C CG1 . ILE A 1 138 ? 7.541   0.081   -62.472 1.00 51.73  ? 138 ILE A CG1 1 
ATOM   1154  C CG2 . ILE A 1 138 ? 7.278   -0.368  -60.065 1.00 51.25  ? 138 ILE A CG2 1 
ATOM   1155  C CD1 . ILE A 1 138 ? 8.464   0.091   -63.658 1.00 50.56  ? 138 ILE A CD1 1 
ATOM   1156  N N   . LYS A 1 139 ? 7.444   3.065   -59.285 1.00 45.57  ? 139 LYS A N   1 
ATOM   1157  C CA  . LYS A 1 139 ? 6.875   3.460   -57.990 1.00 46.33  ? 139 LYS A CA  1 
ATOM   1158  C C   . LYS A 1 139 ? 5.764   2.496   -57.619 1.00 45.35  ? 139 LYS A C   1 
ATOM   1159  O O   . LYS A 1 139 ? 4.735   2.466   -58.280 1.00 45.50  ? 139 LYS A O   1 
ATOM   1160  C CB  . LYS A 1 139 ? 6.343   4.893   -58.030 1.00 47.82  ? 139 LYS A CB  1 
ATOM   1161  C CG  . LYS A 1 139 ? 7.401   5.947   -58.324 1.00 49.80  ? 139 LYS A CG  1 
ATOM   1162  C CD  . LYS A 1 139 ? 6.832   7.350   -58.166 1.00 55.61  ? 139 LYS A CD  1 
ATOM   1163  C CE  . LYS A 1 139 ? 7.699   8.397   -58.861 1.00 59.45  ? 139 LYS A CE  1 
ATOM   1164  N NZ  . LYS A 1 139 ? 9.022   8.582   -58.197 1.00 59.42  ? 139 LYS A NZ  1 
ATOM   1165  N N   . THR A 1 140 ? 5.993   1.685   -56.585 1.00 44.72  ? 140 THR A N   1 
ATOM   1166  C CA  . THR A 1 140 ? 5.014   0.688   -56.147 1.00 47.72  ? 140 THR A CA  1 
ATOM   1167  C C   . THR A 1 140 ? 3.787   1.374   -55.558 1.00 51.42  ? 140 THR A C   1 
ATOM   1168  O O   . THR A 1 140 ? 2.704   0.798   -55.531 1.00 52.97  ? 140 THR A O   1 
ATOM   1169  C CB  . THR A 1 140 ? 5.600   -0.304  -55.108 1.00 47.78  ? 140 THR A CB  1 
ATOM   1170  O OG1 . THR A 1 140 ? 5.982   0.401   -53.911 1.00 46.67  ? 140 THR A OG1 1 
ATOM   1171  C CG2 . THR A 1 140 ? 6.825   -1.038  -55.680 1.00 44.78  ? 140 THR A CG2 1 
ATOM   1172  N N   . LEU A 1 141 ? 3.978   2.619   -55.114 1.00 53.59  ? 141 LEU A N   1 
ATOM   1173  C CA  . LEU A 1 141 ? 2.930   3.445   -54.496 1.00 56.23  ? 141 LEU A CA  1 
ATOM   1174  C C   . LEU A 1 141 ? 2.691   3.046   -53.041 1.00 57.38  ? 141 LEU A C   1 
ATOM   1175  O O   . LEU A 1 141 ? 1.990   3.741   -52.296 1.00 59.82  ? 141 LEU A O   1 
ATOM   1176  C CB  . LEU A 1 141 ? 1.617   3.456   -55.317 1.00 58.26  ? 141 LEU A CB  1 
ATOM   1177  C CG  . LEU A 1 141 ? 1.635   4.023   -56.756 1.00 58.76  ? 141 LEU A CG  1 
ATOM   1178  C CD1 . LEU A 1 141 ? 0.243   3.974   -57.367 1.00 62.57  ? 141 LEU A CD1 1 
ATOM   1179  C CD2 . LEU A 1 141 ? 2.185   5.443   -56.822 1.00 57.24  ? 141 LEU A CD2 1 
ATOM   1180  N N   . ASN A 1 142 ? 3.295   1.937   -52.636 1.00 52.04  ? 142 ASN A N   1 
ATOM   1181  C CA  . ASN A 1 142 ? 3.468   1.664   -51.229 1.00 52.53  ? 142 ASN A CA  1 
ATOM   1182  C C   . ASN A 1 142 ? 4.497   2.617   -50.610 1.00 50.50  ? 142 ASN A C   1 
ATOM   1183  O O   . ASN A 1 142 ? 5.714   2.356   -50.613 1.00 48.72  ? 142 ASN A O   1 
ATOM   1184  C CB  . ASN A 1 142 ? 3.854   0.210   -50.995 1.00 54.87  ? 142 ASN A CB  1 
ATOM   1185  C CG  . ASN A 1 142 ? 3.424   -0.280  -49.632 1.00 59.68  ? 142 ASN A CG  1 
ATOM   1186  O OD1 . ASN A 1 142 ? 3.464   0.471   -48.649 1.00 59.38  ? 142 ASN A OD1 1 
ATOM   1187  N ND2 . ASN A 1 142 ? 2.999   -1.540  -49.561 1.00 61.20  ? 142 ASN A ND2 1 
ATOM   1188  N N   . GLY A 1 143 ? 3.995   3.724   -50.074 1.00 47.47  ? 143 GLY A N   1 
ATOM   1189  C CA  . GLY A 1 143 ? 4.843   4.827   -49.670 1.00 45.66  ? 143 GLY A CA  1 
ATOM   1190  C C   . GLY A 1 143 ? 5.684   5.327   -50.837 1.00 43.66  ? 143 GLY A C   1 
ATOM   1191  O O   . GLY A 1 143 ? 5.210   5.437   -51.949 1.00 45.56  ? 143 GLY A O   1 
ATOM   1192  N N   . HIS A 1 144 ? 6.943   5.614   -50.571 1.00 43.09  ? 144 HIS A N   1 
ATOM   1193  C CA  . HIS A 1 144 ? 7.831   6.183   -51.569 1.00 43.21  ? 144 HIS A CA  1 
ATOM   1194  C C   . HIS A 1 144 ? 8.739   5.132   -52.165 1.00 43.77  ? 144 HIS A C   1 
ATOM   1195  O O   . HIS A 1 144 ? 9.703   5.449   -52.861 1.00 47.10  ? 144 HIS A O   1 
ATOM   1196  C CB  . HIS A 1 144 ? 8.600   7.350   -50.965 1.00 40.19  ? 144 HIS A CB  1 
ATOM   1197  C CG  . HIS A 1 144 ? 7.706   8.402   -50.350 1.00 39.29  ? 144 HIS A CG  1 
ATOM   1198  N ND1 . HIS A 1 144 ? 7.426   8.440   -49.027 1.00 40.69  ? 144 HIS A ND1 1 
ATOM   1199  C CD2 . HIS A 1 144 ? 6.976   9.439   -50.932 1.00 40.34  ? 144 HIS A CD2 1 
ATOM   1200  C CE1 . HIS A 1 144 ? 6.586   9.466   -48.775 1.00 39.80  ? 144 HIS A CE1 1 
ATOM   1201  N NE2 . HIS A 1 144 ? 6.311   10.076  -49.939 1.00 38.48  ? 144 HIS A NE2 1 
ATOM   1202  N N   . GLU A 1 145 ? 8.393   3.865   -51.940 1.00 43.36  ? 145 GLU A N   1 
ATOM   1203  C CA  . GLU A 1 145 ? 9.170   2.748   -52.450 1.00 43.22  ? 145 GLU A CA  1 
ATOM   1204  C C   . GLU A 1 145 ? 9.348   2.814   -53.962 1.00 43.47  ? 145 GLU A C   1 
ATOM   1205  O O   . GLU A 1 145 ? 8.384   3.015   -54.696 1.00 43.20  ? 145 GLU A O   1 
ATOM   1206  C CB  . GLU A 1 145 ? 8.533   1.412   -52.059 1.00 43.93  ? 145 GLU A CB  1 
ATOM   1207  C CG  . GLU A 1 145 ? 9.228   0.200   -52.679 1.00 45.90  ? 145 GLU A CG  1 
ATOM   1208  C CD  . GLU A 1 145 ? 8.542   -1.124  -52.362 1.00 48.53  ? 145 GLU A CD  1 
ATOM   1209  O OE1 . GLU A 1 145 ? 9.247   -2.073  -51.976 1.00 52.04  ? 145 GLU A OE1 1 
ATOM   1210  O OE2 . GLU A 1 145 ? 7.303   -1.230  -52.509 1.00 49.05  ? 145 GLU A OE2 1 
ATOM   1211  N N   . ILE A 1 146 ? 10.594  2.654   -54.415 1.00 41.80  ? 146 ILE A N   1 
ATOM   1212  C CA  . ILE A 1 146 ? 10.873  2.435   -55.822 1.00 39.98  ? 146 ILE A CA  1 
ATOM   1213  C C   . ILE A 1 146 ? 11.463  1.041   -56.020 1.00 40.90  ? 146 ILE A C   1 
ATOM   1214  O O   . ILE A 1 146 ? 12.311  0.599   -55.246 1.00 39.60  ? 146 ILE A O   1 
ATOM   1215  C CB  . ILE A 1 146 ? 11.806  3.518   -56.407 1.00 39.52  ? 146 ILE A CB  1 
ATOM   1216  C CG1 . ILE A 1 146 ? 11.071  4.863   -56.469 1.00 35.97  ? 146 ILE A CG1 1 
ATOM   1217  C CG2 . ILE A 1 146 ? 12.293  3.122   -57.810 1.00 39.24  ? 146 ILE A CG2 1 
ATOM   1218  C CD1 . ILE A 1 146 ? 11.976  6.055   -56.612 1.00 33.28  ? 146 ILE A CD1 1 
ATOM   1219  N N   . LYS A 1 147 ? 10.960  0.339   -57.030 1.00 40.93  ? 147 LYS A N   1 
ATOM   1220  C CA  . LYS A 1 147 ? 11.513  -0.940  -57.435 1.00 42.01  ? 147 LYS A CA  1 
ATOM   1221  C C   . LYS A 1 147 ? 12.156  -0.798  -58.820 1.00 40.80  ? 147 LYS A C   1 
ATOM   1222  O O   . LYS A 1 147 ? 11.644  -0.073  -59.695 1.00 37.63  ? 147 LYS A O   1 
ATOM   1223  C CB  . LYS A 1 147 ? 10.425  -2.009  -57.442 1.00 47.35  ? 147 LYS A CB  1 
ATOM   1224  C CG  . LYS A 1 147 ? 10.827  -3.313  -56.767 1.00 52.23  ? 147 LYS A CG  1 
ATOM   1225  C CD  . LYS A 1 147 ? 9.616   -4.000  -56.136 1.00 58.71  ? 147 LYS A CD  1 
ATOM   1226  C CE  . LYS A 1 147 ? 10.033  -4.976  -55.029 1.00 60.95  ? 147 LYS A CE  1 
ATOM   1227  N NZ  . LYS A 1 147 ? 9.153   -4.865  -53.826 1.00 58.67  ? 147 LYS A NZ  1 
ATOM   1228  N N   . PHE A 1 148 ? 13.312  -1.430  -58.992 1.00 38.06  ? 148 PHE A N   1 
ATOM   1229  C CA  . PHE A 1 148 ? 14.020  -1.364  -60.260 1.00 36.44  ? 148 PHE A CA  1 
ATOM   1230  C C   . PHE A 1 148 ? 13.875  -2.677  -60.976 1.00 37.51  ? 148 PHE A C   1 
ATOM   1231  O O   . PHE A 1 148 ? 14.400  -3.698  -60.522 1.00 36.70  ? 148 PHE A O   1 
ATOM   1232  C CB  . PHE A 1 148 ? 15.498  -1.022  -60.056 1.00 35.51  ? 148 PHE A CB  1 
ATOM   1233  C CG  . PHE A 1 148 ? 15.748  0.424   -59.688 1.00 33.90  ? 148 PHE A CG  1 
ATOM   1234  C CD1 . PHE A 1 148 ? 15.568  1.442   -60.628 1.00 32.87  ? 148 PHE A CD1 1 
ATOM   1235  C CD2 . PHE A 1 148 ? 16.178  0.763   -58.408 1.00 32.20  ? 148 PHE A CD2 1 
ATOM   1236  C CE1 . PHE A 1 148 ? 15.795  2.765   -60.289 1.00 32.82  ? 148 PHE A CE1 1 
ATOM   1237  C CE2 . PHE A 1 148 ? 16.410  2.087   -58.063 1.00 31.30  ? 148 PHE A CE2 1 
ATOM   1238  C CZ  . PHE A 1 148 ? 16.230  3.091   -59.009 1.00 31.87  ? 148 PHE A CZ  1 
ATOM   1239  N N   . ILE A 1 149 ? 13.133  -2.644  -62.086 1.00 38.12  ? 149 ILE A N   1 
ATOM   1240  C CA  . ILE A 1 149 ? 12.845  -3.831  -62.881 1.00 41.45  ? 149 ILE A CA  1 
ATOM   1241  C C   . ILE A 1 149 ? 13.766  -3.835  -64.097 1.00 42.69  ? 149 ILE A C   1 
ATOM   1242  O O   . ILE A 1 149 ? 13.975  -2.792  -64.718 1.00 41.43  ? 149 ILE A O   1 
ATOM   1243  C CB  . ILE A 1 149 ? 11.364  -3.843  -63.350 1.00 42.07  ? 149 ILE A CB  1 
ATOM   1244  C CG1 . ILE A 1 149 ? 10.422  -3.588  -62.168 1.00 42.58  ? 149 ILE A CG1 1 
ATOM   1245  C CG2 . ILE A 1 149 ? 11.013  -5.155  -64.041 1.00 42.64  ? 149 ILE A CG2 1 
ATOM   1246  C CD1 . ILE A 1 149 ? 10.585  -4.563  -61.019 1.00 42.24  ? 149 ILE A CD1 1 
ATOM   1247  N N   . ARG A 1 150 ? 14.340  -4.996  -64.415 1.00 46.33  ? 150 ARG A N   1 
ATOM   1248  C CA  . ARG A 1 150 ? 15.169  -5.128  -65.617 1.00 50.92  ? 150 ARG A CA  1 
ATOM   1249  C C   . ARG A 1 150 ? 14.358  -4.699  -66.827 1.00 52.98  ? 150 ARG A C   1 
ATOM   1250  O O   . ARG A 1 150 ? 13.195  -5.086  -66.975 1.00 55.16  ? 150 ARG A O   1 
ATOM   1251  C CB  . ARG A 1 150 ? 15.685  -6.554  -65.783 1.00 54.88  ? 150 ARG A CB  1 
ATOM   1252  C CG  . ARG A 1 150 ? 16.696  -6.962  -64.724 1.00 61.27  ? 150 ARG A CG  1 
ATOM   1253  C CD  . ARG A 1 150 ? 17.620  -8.070  -65.206 1.00 70.15  ? 150 ARG A CD  1 
ATOM   1254  N NE  . ARG A 1 150 ? 18.411  -7.659  -66.373 1.00 78.59  ? 150 ARG A NE  1 
ATOM   1255  C CZ  . ARG A 1 150 ? 19.366  -8.397  -66.940 1.00 82.12  ? 150 ARG A CZ  1 
ATOM   1256  N NH1 . ARG A 1 150 ? 19.675  -9.592  -66.451 1.00 84.48  ? 150 ARG A NH1 1 
ATOM   1257  N NH2 . ARG A 1 150 ? 20.019  -7.935  -67.999 1.00 86.38  ? 150 ARG A NH2 1 
ATOM   1258  N N   . LYS A 1 151 ? 14.957  -3.858  -67.662 1.00 53.15  ? 151 LYS A N   1 
ATOM   1259  C CA  . LYS A 1 151 ? 14.240  -3.196  -68.744 1.00 56.31  ? 151 LYS A CA  1 
ATOM   1260  C C   . LYS A 1 151 ? 13.606  -4.182  -69.734 1.00 58.85  ? 151 LYS A C   1 
ATOM   1261  O O   . LYS A 1 151 ? 12.485  -3.968  -70.180 1.00 61.04  ? 151 LYS A O   1 
ATOM   1262  C CB  . LYS A 1 151 ? 15.167  -2.219  -69.467 1.00 57.84  ? 151 LYS A CB  1 
ATOM   1263  C CG  . LYS A 1 151 ? 14.462  -1.090  -70.195 1.00 59.60  ? 151 LYS A CG  1 
ATOM   1264  C CD  . LYS A 1 151 ? 15.301  0.177   -70.124 1.00 60.81  ? 151 LYS A CD  1 
ATOM   1265  C CE  . LYS A 1 151 ? 14.960  1.152   -71.240 1.00 62.85  ? 151 LYS A CE  1 
ATOM   1266  N NZ  . LYS A 1 151 ? 15.468  2.513   -70.913 1.00 61.87  ? 151 LYS A NZ  1 
ATOM   1267  N N   . GLU A 1 152 ? 14.312  -5.265  -70.055 1.00 60.44  ? 152 GLU A N   1 
ATOM   1268  C CA  . GLU A 1 152 ? 13.782  -6.271  -70.993 1.00 64.85  ? 152 GLU A CA  1 
ATOM   1269  C C   . GLU A 1 152 ? 12.565  -7.000  -70.422 1.00 63.60  ? 152 GLU A C   1 
ATOM   1270  O O   . GLU A 1 152 ? 11.631  -7.326  -71.156 1.00 62.82  ? 152 GLU A O   1 
ATOM   1271  C CB  . GLU A 1 152 ? 14.866  -7.265  -71.479 1.00 66.77  ? 152 GLU A CB  1 
ATOM   1272  C CG  . GLU A 1 152 ? 15.841  -7.764  -70.410 1.00 75.06  ? 152 GLU A CG  1 
ATOM   1273  C CD  . GLU A 1 152 ? 16.965  -6.773  -70.109 1.00 79.46  ? 152 GLU A CD  1 
ATOM   1274  O OE1 . GLU A 1 152 ? 17.473  -6.127  -71.054 1.00 85.81  ? 152 GLU A OE1 1 
ATOM   1275  O OE2 . GLU A 1 152 ? 17.345  -6.638  -68.924 1.00 80.18  ? 152 GLU A OE2 1 
ATOM   1276  N N   . GLU A 1 153 ? 12.572  -7.232  -69.110 1.00 62.16  ? 153 GLU A N   1 
ATOM   1277  C CA  . GLU A 1 153 ? 11.440  -7.866  -68.433 1.00 63.76  ? 153 GLU A CA  1 
ATOM   1278  C C   . GLU A 1 153 ? 10.226  -6.956  -68.445 1.00 61.16  ? 153 GLU A C   1 
ATOM   1279  O O   . GLU A 1 153 ? 9.098   -7.407  -68.673 1.00 61.32  ? 153 GLU A O   1 
ATOM   1280  C CB  . GLU A 1 153 ? 11.799  -8.233  -66.996 1.00 66.80  ? 153 GLU A CB  1 
ATOM   1281  C CG  . GLU A 1 153 ? 12.672  -9.468  -66.876 1.00 74.20  ? 153 GLU A CG  1 
ATOM   1282  C CD  . GLU A 1 153 ? 13.143  -9.718  -65.456 1.00 79.71  ? 153 GLU A CD  1 
ATOM   1283  O OE1 . GLU A 1 153 ? 12.365  -9.446  -64.509 1.00 84.26  ? 153 GLU A OE1 1 
ATOM   1284  O OE2 . GLU A 1 153 ? 14.291  -10.194 -65.288 1.00 80.14  ? 153 GLU A OE2 1 
ATOM   1285  N N   . TYR A 1 154 ? 10.464  -5.670  -68.211 1.00 57.23  ? 154 TYR A N   1 
ATOM   1286  C CA  . TYR A 1 154 ? 9.392   -4.706  -68.183 1.00 55.30  ? 154 TYR A CA  1 
ATOM   1287  C C   . TYR A 1 154 ? 8.778   -4.536  -69.562 1.00 56.30  ? 154 TYR A C   1 
ATOM   1288  O O   . TYR A 1 154 ? 7.554   -4.515  -69.698 1.00 57.42  ? 154 TYR A O   1 
ATOM   1289  C CB  . TYR A 1 154 ? 9.859   -3.354  -67.644 1.00 53.29  ? 154 TYR A CB  1 
ATOM   1290  C CG  . TYR A 1 154 ? 8.831   -2.273  -67.855 1.00 54.76  ? 154 TYR A CG  1 
ATOM   1291  C CD1 . TYR A 1 154 ? 7.700   -2.196  -67.041 1.00 56.02  ? 154 TYR A CD1 1 
ATOM   1292  C CD2 . TYR A 1 154 ? 8.956   -1.360  -68.899 1.00 55.51  ? 154 TYR A CD2 1 
ATOM   1293  C CE1 . TYR A 1 154 ? 6.730   -1.230  -67.249 1.00 58.39  ? 154 TYR A CE1 1 
ATOM   1294  C CE2 . TYR A 1 154 ? 7.996   -0.384  -69.113 1.00 59.35  ? 154 TYR A CE2 1 
ATOM   1295  C CZ  . TYR A 1 154 ? 6.881   -0.324  -68.284 1.00 61.58  ? 154 TYR A CZ  1 
ATOM   1296  O OH  . TYR A 1 154 ? 5.917   0.645   -68.487 1.00 63.54  ? 154 TYR A OH  1 
ATOM   1297  N N   . ILE A 1 155 ? 9.624   -4.397  -70.579 1.00 56.31  ? 155 ILE A N   1 
ATOM   1298  C CA  . ILE A 1 155 ? 9.142   -4.225  -71.945 1.00 58.16  ? 155 ILE A CA  1 
ATOM   1299  C C   . ILE A 1 155 ? 8.320   -5.429  -72.409 1.00 60.63  ? 155 ILE A C   1 
ATOM   1300  O O   . ILE A 1 155 ? 7.269   -5.270  -73.035 1.00 62.61  ? 155 ILE A O   1 
ATOM   1301  C CB  . ILE A 1 155 ? 10.290  -3.917  -72.924 1.00 57.38  ? 155 ILE A CB  1 
ATOM   1302  C CG1 . ILE A 1 155 ? 10.806  -2.496  -72.669 1.00 54.90  ? 155 ILE A CG1 1 
ATOM   1303  C CG2 . ILE A 1 155 ? 9.829   -4.091  -74.375 1.00 55.81  ? 155 ILE A CG2 1 
ATOM   1304  C CD1 . ILE A 1 155 ? 12.045  -2.137  -73.454 1.00 55.16  ? 155 ILE A CD1 1 
ATOM   1305  N N   . SER A 1 156 ? 8.793   -6.626  -72.070 1.00 61.15  ? 156 SER A N   1 
ATOM   1306  C CA  . SER A 1 156 ? 8.063   -7.856  -72.340 1.00 63.22  ? 156 SER A CA  1 
ATOM   1307  C C   . SER A 1 156 ? 6.680   -7.810  -71.681 1.00 66.46  ? 156 SER A C   1 
ATOM   1308  O O   . SER A 1 156 ? 5.655   -8.014  -72.344 1.00 70.99  ? 156 SER A O   1 
ATOM   1309  C CB  . SER A 1 156 ? 8.880   -9.063  -71.861 1.00 62.80  ? 156 SER A CB  1 
ATOM   1310  O OG  . SER A 1 156 ? 8.054   -10.117 -71.407 1.00 65.92  ? 156 SER A OG  1 
ATOM   1311  N N   . PHE A 1 157 ? 6.661   -7.510  -70.382 1.00 67.42  ? 157 PHE A N   1 
ATOM   1312  C CA  . PHE A 1 157 ? 5.422   -7.302  -69.637 1.00 64.89  ? 157 PHE A CA  1 
ATOM   1313  C C   . PHE A 1 157 ? 4.553   -6.225  -70.302 1.00 65.53  ? 157 PHE A C   1 
ATOM   1314  O O   . PHE A 1 157 ? 3.353   -6.420  -70.502 1.00 64.92  ? 157 PHE A O   1 
ATOM   1315  C CB  . PHE A 1 157 ? 5.739   -6.933  -68.175 1.00 63.74  ? 157 PHE A CB  1 
ATOM   1316  C CG  . PHE A 1 157 ? 4.579   -6.326  -67.431 1.00 63.26  ? 157 PHE A CG  1 
ATOM   1317  C CD1 . PHE A 1 157 ? 4.342   -4.949  -67.478 1.00 62.77  ? 157 PHE A CD1 1 
ATOM   1318  C CD2 . PHE A 1 157 ? 3.724   -7.122  -66.682 1.00 64.53  ? 157 PHE A CD2 1 
ATOM   1319  C CE1 . PHE A 1 157 ? 3.269   -4.387  -66.809 1.00 61.55  ? 157 PHE A CE1 1 
ATOM   1320  C CE2 . PHE A 1 157 ? 2.652   -6.564  -66.004 1.00 65.21  ? 157 PHE A CE2 1 
ATOM   1321  C CZ  . PHE A 1 157 ? 2.425   -5.196  -66.070 1.00 64.33  ? 157 PHE A CZ  1 
ATOM   1322  N N   . GLU A 1 158 ? 5.174   -5.099  -70.653 1.00 65.39  ? 158 GLU A N   1 
ATOM   1323  C CA  . GLU A 1 158 ? 4.462   -3.955  -71.226 1.00 66.50  ? 158 GLU A CA  1 
ATOM   1324  C C   . GLU A 1 158 ? 3.810   -4.330  -72.558 1.00 69.13  ? 158 GLU A C   1 
ATOM   1325  O O   . GLU A 1 158 ? 2.700   -3.893  -72.855 1.00 69.54  ? 158 GLU A O   1 
ATOM   1326  C CB  . GLU A 1 158 ? 5.422   -2.774  -71.413 1.00 66.24  ? 158 GLU A CB  1 
ATOM   1327  C CG  . GLU A 1 158 ? 4.766   -1.451  -71.786 1.00 67.86  ? 158 GLU A CG  1 
ATOM   1328  C CD  . GLU A 1 158 ? 5.747   -0.465  -72.406 1.00 70.14  ? 158 GLU A CD  1 
ATOM   1329  O OE1 . GLU A 1 158 ? 5.350   0.682   -72.693 1.00 72.45  ? 158 GLU A OE1 1 
ATOM   1330  O OE2 . GLU A 1 158 ? 6.918   -0.836  -72.616 1.00 71.94  ? 158 GLU A OE2 1 
ATOM   1331  N N   . SER A 1 159 ? 4.506   -5.145  -73.348 1.00 68.86  ? 159 SER A N   1 
ATOM   1332  C CA  . SER A 1 159 ? 3.992   -5.588  -74.637 1.00 71.73  ? 159 SER A CA  1 
ATOM   1333  C C   . SER A 1 159 ? 2.862   -6.597  -74.471 1.00 72.48  ? 159 SER A C   1 
ATOM   1334  O O   . SER A 1 159 ? 1.845   -6.515  -75.160 1.00 71.31  ? 159 SER A O   1 
ATOM   1335  C CB  . SER A 1 159 ? 5.114   -6.172  -75.499 1.00 70.53  ? 159 SER A CB  1 
ATOM   1336  O OG  . SER A 1 159 ? 5.908   -5.139  -76.058 1.00 71.33  ? 159 SER A OG  1 
ATOM   1337  N N   . LYS A 1 160 ? 3.049   -7.534  -73.543 1.00 72.69  ? 160 LYS A N   1 
ATOM   1338  C CA  . LYS A 1 160 ? 2.074   -8.589  -73.269 1.00 75.23  ? 160 LYS A CA  1 
ATOM   1339  C C   . LYS A 1 160 ? 0.721   -8.022  -72.804 1.00 76.35  ? 160 LYS A C   1 
ATOM   1340  O O   . LYS A 1 160 ? -0.328  -8.608  -73.067 1.00 80.27  ? 160 LYS A O   1 
ATOM   1341  C CB  . LYS A 1 160 ? 2.649   -9.572  -72.238 1.00 75.20  ? 160 LYS A CB  1 
ATOM   1342  C CG  . LYS A 1 160 ? 1.690   -10.643 -71.741 1.00 78.45  ? 160 LYS A CG  1 
ATOM   1343  C CD  . LYS A 1 160 ? 2.183   -11.233 -70.428 1.00 81.20  ? 160 LYS A CD  1 
ATOM   1344  C CE  . LYS A 1 160 ? 1.030   -11.521 -69.479 1.00 83.61  ? 160 LYS A CE  1 
ATOM   1345  N NZ  . LYS A 1 160 ? 1.438   -11.354 -68.055 1.00 80.54  ? 160 LYS A NZ  1 
ATOM   1346  N N   . VAL A 1 161 ? 0.756   -6.876  -72.129 1.00 76.19  ? 161 VAL A N   1 
ATOM   1347  C CA  . VAL A 1 161 ? -0.462  -6.193  -71.680 1.00 75.41  ? 161 VAL A CA  1 
ATOM   1348  C C   . VAL A 1 161 ? -1.042  -5.357  -72.825 1.00 77.09  ? 161 VAL A C   1 
ATOM   1349  O O   . VAL A 1 161 ? -2.265  -5.262  -72.985 1.00 78.37  ? 161 VAL A O   1 
ATOM   1350  C CB  . VAL A 1 161 ? -0.192  -5.309  -70.429 1.00 72.70  ? 161 VAL A CB  1 
ATOM   1351  C CG1 . VAL A 1 161 ? -1.358  -4.367  -70.145 1.00 69.99  ? 161 VAL A CG1 1 
ATOM   1352  C CG2 . VAL A 1 161 ? 0.105   -6.177  -69.211 1.00 70.13  ? 161 VAL A CG2 1 
ATOM   1353  N N   . PHE A 1 162 ? -0.150  -4.770  -73.620 1.00 77.06  ? 162 PHE A N   1 
ATOM   1354  C CA  . PHE A 1 162 ? -0.521  -3.975  -74.792 1.00 81.07  ? 162 PHE A CA  1 
ATOM   1355  C C   . PHE A 1 162 ? -1.367  -4.771  -75.794 1.00 84.36  ? 162 PHE A C   1 
ATOM   1356  O O   . PHE A 1 162 ? -2.317  -4.237  -76.376 1.00 83.61  ? 162 PHE A O   1 
ATOM   1357  C CB  . PHE A 1 162 ? 0.742   -3.425  -75.466 1.00 80.25  ? 162 PHE A CB  1 
ATOM   1358  C CG  . PHE A 1 162 ? 0.498   -2.757  -76.792 1.00 82.65  ? 162 PHE A CG  1 
ATOM   1359  C CD1 . PHE A 1 162 ? -0.316  -1.633  -76.888 1.00 82.74  ? 162 PHE A CD1 1 
ATOM   1360  C CD2 . PHE A 1 162 ? 1.119   -3.233  -77.947 1.00 84.81  ? 162 PHE A CD2 1 
ATOM   1361  C CE1 . PHE A 1 162 ? -0.520  -1.011  -78.109 1.00 84.64  ? 162 PHE A CE1 1 
ATOM   1362  C CE2 . PHE A 1 162 ? 0.916   -2.616  -79.173 1.00 84.53  ? 162 PHE A CE2 1 
ATOM   1363  C CZ  . PHE A 1 162 ? 0.099   -1.503  -79.254 1.00 85.79  ? 162 PHE A CZ  1 
ATOM   1364  N N   . HIS A 1 163 ? -1.021  -6.044  -75.982 1.00 87.05  ? 163 HIS A N   1 
ATOM   1365  C CA  . HIS A 1 163 ? -1.742  -6.914  -76.914 1.00 91.37  ? 163 HIS A CA  1 
ATOM   1366  C C   . HIS A 1 163 ? -3.061  -7.380  -76.365 1.00 90.65  ? 163 HIS A C   1 
ATOM   1367  O O   . HIS A 1 163 ? -4.010  -7.593  -77.121 1.00 92.20  ? 163 HIS A O   1 
ATOM   1368  C CB  . HIS A 1 163 ? -0.876  -8.096  -77.341 1.00 93.87  ? 163 HIS A CB  1 
ATOM   1369  C CG  . HIS A 1 163 ? 0.270   -7.711  -78.249 1.00 97.56  ? 163 HIS A CG  1 
ATOM   1370  N ND1 . HIS A 1 163 ? 0.078   -7.205  -79.485 1.00 100.14 ? 163 HIS A ND1 1 
ATOM   1371  C CD2 . HIS A 1 163 ? 1.652   -7.764  -78.057 1.00 97.31  ? 163 HIS A CD2 1 
ATOM   1372  C CE1 . HIS A 1 163 ? 1.272   -6.948  -80.054 1.00 101.89 ? 163 HIS A CE1 1 
ATOM   1373  N NE2 . HIS A 1 163 ? 2.234   -7.290  -79.179 1.00 100.98 ? 163 HIS A NE2 1 
ATOM   1374  N N   . LYS A 1 164 ? -3.131  -7.535  -75.044 1.00 87.54  ? 164 LYS A N   1 
ATOM   1375  C CA  . LYS A 1 164 ? -4.374  -7.886  -74.365 1.00 86.35  ? 164 LYS A CA  1 
ATOM   1376  C C   . LYS A 1 164 ? -5.384  -6.743  -74.468 1.00 86.98  ? 164 LYS A C   1 
ATOM   1377  O O   . LYS A 1 164 ? -6.565  -6.976  -74.713 1.00 91.33  ? 164 LYS A O   1 
ATOM   1378  C CB  . LYS A 1 164 ? -4.102  -8.234  -72.901 1.00 85.22  ? 164 LYS A CB  1 
ATOM   1379  C CG  . LYS A 1 164 ? -5.152  -9.131  -72.262 1.00 86.49  ? 164 LYS A CG  1 
ATOM   1380  C CD  . LYS A 1 164 ? -4.719  -9.597  -70.879 1.00 85.84  ? 164 LYS A CD  1 
ATOM   1381  C CE  . LYS A 1 164 ? -3.712  -10.736 -70.966 1.00 86.87  ? 164 LYS A CE  1 
ATOM   1382  N NZ  . LYS A 1 164 ? -2.900  -10.856 -69.723 1.00 87.55  ? 164 LYS A NZ  1 
ATOM   1383  N N   . LEU A 1 165 ? -4.904  -5.511  -74.301 1.00 86.64  ? 165 LEU A N   1 
ATOM   1384  C CA  . LEU A 1 165 ? -5.735  -4.313  -74.479 1.00 86.62  ? 165 LEU A CA  1 
ATOM   1385  C C   . LEU A 1 165 ? -6.169  -4.153  -75.932 1.00 89.44  ? 165 LEU A C   1 
ATOM   1386  O O   . LEU A 1 165 ? -7.299  -3.750  -76.207 1.00 91.29  ? 165 LEU A O   1 
ATOM   1387  C CB  . LEU A 1 165 ? -4.988  -3.054  -74.021 1.00 84.58  ? 165 LEU A CB  1 
ATOM   1388  C CG  . LEU A 1 165 ? -4.584  -2.921  -72.547 1.00 81.24  ? 165 LEU A CG  1 
ATOM   1389  C CD1 . LEU A 1 165 ? -3.714  -1.687  -72.351 1.00 75.98  ? 165 LEU A CD1 1 
ATOM   1390  C CD2 . LEU A 1 165 ? -5.803  -2.875  -71.637 1.00 78.26  ? 165 LEU A CD2 1 
ATOM   1391  N N   . LYS A 1 166 ? -5.255  -4.460  -76.852 1.00 90.11  ? 166 LYS A N   1 
ATOM   1392  C CA  . LYS A 1 166 ? -5.557  -4.509  -78.281 1.00 92.74  ? 166 LYS A CA  1 
ATOM   1393  C C   . LYS A 1 166 ? -6.630  -5.555  -78.581 1.00 94.38  ? 166 LYS A C   1 
ATOM   1394  O O   . LYS A 1 166 ? -7.699  -5.229  -79.099 1.00 90.57  ? 166 LYS A O   1 
ATOM   1395  C CB  . LYS A 1 166 ? -4.292  -4.832  -79.084 1.00 93.76  ? 166 LYS A CB  1 
ATOM   1396  C CG  . LYS A 1 166 ? -3.630  -3.638  -79.752 1.00 95.67  ? 166 LYS A CG  1 
ATOM   1397  C CD  . LYS A 1 166 ? -2.509  -4.096  -80.677 1.00 98.55  ? 166 LYS A CD  1 
ATOM   1398  C CE  . LYS A 1 166 ? -2.246  -3.085  -81.783 1.00 100.03 ? 166 LYS A CE  1 
ATOM   1399  N NZ  . LYS A 1 166 ? -1.463  -3.681  -82.899 1.00 98.76  ? 166 LYS A NZ  1 
ATOM   1400  N N   . LYS A 1 167 ? -6.337  -6.811  -78.246 1.00 97.05  ? 167 LYS A N   1 
ATOM   1401  C CA  . LYS A 1 167 ? -7.247  -7.920  -78.525 1.00 100.68 ? 167 LYS A CA  1 
ATOM   1402  C C   . LYS A 1 167 ? -8.401  -7.988  -77.530 1.00 101.81 ? 167 LYS A C   1 
ATOM   1403  O O   . LYS A 1 167 ? -8.973  -9.051  -77.289 1.00 105.30 ? 167 LYS A O   1 
ATOM   1404  C CB  . LYS A 1 167 ? -6.485  -9.253  -78.607 1.00 103.29 ? 167 LYS A CB  1 
ATOM   1405  C CG  . LYS A 1 167 ? -6.368  -9.830  -80.020 1.00 105.90 ? 167 LYS A CG  1 
ATOM   1406  C CD  . LYS A 1 167 ? -6.180  -8.754  -81.090 1.00 106.65 ? 167 LYS A CD  1 
ATOM   1407  C CE  . LYS A 1 167 ? -4.714  -8.488  -81.390 1.00 105.15 ? 167 LYS A CE  1 
ATOM   1408  N NZ  . LYS A 1 167 ? -4.171  -9.473  -82.363 1.00 104.94 ? 167 LYS A NZ  1 
ATOM   1409  N N   . MET A 1 168 ? -8.720  -6.838  -76.945 1.00 100.77 ? 168 MET A N   1 
ATOM   1410  C CA  . MET A 1 168 ? -10.006 -6.613  -76.306 1.00 99.85  ? 168 MET A CA  1 
ATOM   1411  C C   . MET A 1 168 ? -10.602 -5.338  -76.889 1.00 98.47  ? 168 MET A C   1 
ATOM   1412  O O   . MET A 1 168 ? -10.209 -4.899  -77.965 1.00 94.95  ? 168 MET A O   1 
ATOM   1413  C CB  . MET A 1 168 ? -9.848  -6.498  -74.789 1.00 98.98  ? 168 MET A CB  1 
ATOM   1414  C CG  . MET A 1 168 ? -9.624  -7.825  -74.083 1.00 98.48  ? 168 MET A CG  1 
ATOM   1415  S SD  . MET A 1 168 ? -9.182  -7.610  -72.350 1.00 99.92  ? 168 MET A SD  1 
ATOM   1416  C CE  . MET A 1 168 ? -8.877  -9.305  -71.853 1.00 99.90  ? 168 MET A CE  1 
ATOM   1417  N N   . LYS A 1 169 ? -11.551 -4.744  -76.182 1.00 101.19 ? 169 LYS A N   1 
ATOM   1418  C CA  . LYS A 1 169 ? -12.163 -3.506  -76.644 1.00 105.55 ? 169 LYS A CA  1 
ATOM   1419  C C   . LYS A 1 169 ? -11.336 -2.308  -76.192 1.00 102.13 ? 169 LYS A C   1 
ATOM   1420  O O   . LYS A 1 169 ? -11.423 -1.228  -76.777 1.00 102.26 ? 169 LYS A O   1 
ATOM   1421  C CB  . LYS A 1 169 ? -13.606 -3.375  -76.120 1.00 110.30 ? 169 LYS A CB  1 
ATOM   1422  C CG  . LYS A 1 169 ? -14.268 -4.688  -75.720 1.00 111.35 ? 169 LYS A CG  1 
ATOM   1423  C CD  . LYS A 1 169 ? -15.721 -4.746  -76.164 1.00 110.64 ? 169 LYS A CD  1 
ATOM   1424  C CE  . LYS A 1 169 ? -16.261 -6.158  -76.031 1.00 109.26 ? 169 LYS A CE  1 
ATOM   1425  N NZ  . LYS A 1 169 ? -17.189 -6.497  -77.140 1.00 112.83 ? 169 LYS A NZ  1 
ATOM   1426  N N   . TYR A 1 170 ? -10.509 -2.526  -75.169 1.00 100.66 ? 170 TYR A N   1 
ATOM   1427  C CA  . TYR A 1 170 ? -9.951  -1.444  -74.347 1.00 96.58  ? 170 TYR A CA  1 
ATOM   1428  C C   . TYR A 1 170 ? -9.109  -0.436  -75.126 1.00 93.60  ? 170 TYR A C   1 
ATOM   1429  O O   . TYR A 1 170 ? -9.222  0.772   -74.909 1.00 90.67  ? 170 TYR A O   1 
ATOM   1430  C CB  . TYR A 1 170 ? -9.156  -2.016  -73.158 1.00 96.53  ? 170 TYR A CB  1 
ATOM   1431  C CG  . TYR A 1 170 ? -9.946  -2.964  -72.256 1.00 100.34 ? 170 TYR A CG  1 
ATOM   1432  C CD1 . TYR A 1 170 ? -11.308 -3.207  -72.475 1.00 102.04 ? 170 TYR A CD1 1 
ATOM   1433  C CD2 . TYR A 1 170 ? -9.338  -3.587  -71.164 1.00 100.05 ? 170 TYR A CD2 1 
ATOM   1434  C CE1 . TYR A 1 170 ? -12.028 -4.064  -71.657 1.00 102.20 ? 170 TYR A CE1 1 
ATOM   1435  C CE2 . TYR A 1 170 ? -10.055 -4.440  -70.333 1.00 102.04 ? 170 TYR A CE2 1 
ATOM   1436  C CZ  . TYR A 1 170 ? -11.399 -4.674  -70.587 1.00 104.21 ? 170 TYR A CZ  1 
ATOM   1437  O OH  . TYR A 1 170 ? -12.121 -5.516  -69.776 1.00 104.43 ? 170 TYR A OH  1 
ATOM   1438  N N   . LEU A 1 171 ? -8.281  -0.936  -76.038 1.00 94.47  ? 171 LEU A N   1 
ATOM   1439  C CA  . LEU A 1 171 ? -7.423  -0.084  -76.851 1.00 96.38  ? 171 LEU A CA  1 
ATOM   1440  C C   . LEU A 1 171 ? -7.657  -0.353  -78.338 1.00 98.39  ? 171 LEU A C   1 
ATOM   1441  O O   . LEU A 1 171 ? -7.350  -1.439  -78.833 1.00 99.11  ? 171 LEU A O   1 
ATOM   1442  C CB  . LEU A 1 171 ? -5.955  -0.328  -76.487 1.00 98.60  ? 171 LEU A CB  1 
ATOM   1443  C CG  . LEU A 1 171 ? -4.937  0.800   -76.680 1.00 100.16 ? 171 LEU A CG  1 
ATOM   1444  C CD1 . LEU A 1 171 ? -5.293  2.021   -75.843 1.00 99.28  ? 171 LEU A CD1 1 
ATOM   1445  C CD2 . LEU A 1 171 ? -3.537  0.311   -76.332 1.00 100.07 ? 171 LEU A CD2 1 
ATOM   1446  N N   . VAL A 1 172 ? -8.222  0.633   -79.037 1.00 99.61  ? 172 VAL A N   1 
ATOM   1447  C CA  . VAL A 1 172 ? -8.455  0.533   -80.485 1.00 102.25 ? 172 VAL A CA  1 
ATOM   1448  C C   . VAL A 1 172 ? -7.502  1.457   -81.238 1.00 104.21 ? 172 VAL A C   1 
ATOM   1449  O O   . VAL A 1 172 ? -7.369  2.635   -80.901 1.00 104.17 ? 172 VAL A O   1 
ATOM   1450  C CB  . VAL A 1 172 ? -9.917  0.879   -80.869 1.00 102.39 ? 172 VAL A CB  1 
ATOM   1451  C CG1 . VAL A 1 172 ? -10.068 1.017   -82.380 1.00 102.87 ? 172 VAL A CG1 1 
ATOM   1452  C CG2 . VAL A 1 172 ? -10.879 -0.173  -80.334 1.00 102.44 ? 172 VAL A CG2 1 
ATOM   1453  N N   . GLU A 1 173 ? -6.847  0.912   -82.260 1.00 107.08 ? 173 GLU A N   1 
ATOM   1454  C CA  . GLU A 1 173 ? -5.904  1.673   -83.070 1.00 109.50 ? 173 GLU A CA  1 
ATOM   1455  C C   . GLU A 1 173 ? -6.610  2.792   -83.840 1.00 113.70 ? 173 GLU A C   1 
ATOM   1456  O O   . GLU A 1 173 ? -7.684  2.587   -84.413 1.00 113.87 ? 173 GLU A O   1 
ATOM   1457  C CB  . GLU A 1 173 ? -5.168  0.742   -84.030 1.00 110.21 ? 173 GLU A CB  1 
ATOM   1458  C CG  . GLU A 1 173 ? -3.792  1.232   -84.446 1.00 109.28 ? 173 GLU A CG  1 
ATOM   1459  C CD  . GLU A 1 173 ? -3.218  0.428   -85.594 1.00 109.67 ? 173 GLU A CD  1 
ATOM   1460  O OE1 . GLU A 1 173 ? -3.062  -0.804  -85.447 1.00 109.10 ? 173 GLU A OE1 1 
ATOM   1461  O OE2 . GLU A 1 173 ? -2.924  1.029   -86.647 1.00 111.78 ? 173 GLU A OE2 1 
ATOM   1462  N N   . VAL A 1 174 ? -6.002  3.976   -83.832 1.00 116.75 ? 174 VAL A N   1 
ATOM   1463  C CA  . VAL A 1 174 ? -6.556  5.148   -84.512 1.00 119.85 ? 174 VAL A CA  1 
ATOM   1464  C C   . VAL A 1 174 ? -5.713  5.528   -85.741 1.00 124.24 ? 174 VAL A C   1 
ATOM   1465  O O   . VAL A 1 174 ? -4.550  5.135   -85.852 1.00 121.42 ? 174 VAL A O   1 
ATOM   1466  C CB  . VAL A 1 174 ? -6.730  6.333   -83.526 1.00 117.12 ? 174 VAL A CB  1 
ATOM   1467  C CG1 . VAL A 1 174 ? -6.534  7.674   -84.214 1.00 119.45 ? 174 VAL A CG1 1 
ATOM   1468  C CG2 . VAL A 1 174 ? -8.103  6.272   -82.873 1.00 117.09 ? 174 VAL A CG2 1 
ATOM   1469  N N   . GLN A 1 175 ? -6.317  6.282   -86.659 1.00 133.14 ? 175 GLN A N   1 
ATOM   1470  C CA  . GLN A 1 175 ? -5.722  6.576   -87.971 1.00 138.92 ? 175 GLN A CA  1 
ATOM   1471  C C   . GLN A 1 175 ? -4.684  7.713   -87.949 1.00 145.25 ? 175 GLN A C   1 
ATOM   1472  O O   . GLN A 1 175 ? -4.214  8.152   -89.006 1.00 146.59 ? 175 GLN A O   1 
ATOM   1473  C CB  . GLN A 1 175 ? -6.825  6.890   -88.995 1.00 137.15 ? 175 GLN A CB  1 
ATOM   1474  C CG  . GLN A 1 175 ? -7.847  5.772   -89.197 1.00 135.86 ? 175 GLN A CG  1 
ATOM   1475  C CD  . GLN A 1 175 ? -8.972  5.780   -88.166 1.00 131.92 ? 175 GLN A CD  1 
ATOM   1476  O OE1 . GLN A 1 175 ? -9.054  6.670   -87.315 1.00 127.71 ? 175 GLN A OE1 1 
ATOM   1477  N NE2 . GLN A 1 175 ? -9.847  4.784   -88.243 1.00 130.78 ? 175 GLN A NE2 1 
ATOM   1478  N N   . ASP A 1 176 ? -4.329  8.171   -86.744 1.00 149.55 ? 176 ASP A N   1 
ATOM   1479  C CA  . ASP A 1 176 ? -3.389  9.295   -86.536 1.00 150.26 ? 176 ASP A CA  1 
ATOM   1480  C C   . ASP A 1 176 ? -4.017  10.674  -86.787 1.00 155.45 ? 176 ASP A C   1 
ATOM   1481  O O   . ASP A 1 176 ? -3.436  11.703  -86.425 1.00 153.87 ? 176 ASP A O   1 
ATOM   1482  C CB  . ASP A 1 176 ? -2.105  9.122   -87.363 1.00 146.35 ? 176 ASP A CB  1 
ATOM   1483  C CG  . ASP A 1 176 ? -1.390  7.814   -87.068 1.00 144.45 ? 176 ASP A CG  1 
ATOM   1484  O OD1 . ASP A 1 176 ? -0.896  7.643   -85.932 1.00 141.09 ? 176 ASP A OD1 1 
ATOM   1485  O OD2 . ASP A 1 176 ? -1.321  6.958   -87.976 1.00 143.66 ? 176 ASP A OD2 1 
ATOM   1486  N N   . GLU A 1 177 ? -5.204  10.680  -87.398 1.00 160.07 ? 177 GLU A N   1 
ATOM   1487  C CA  . GLU A 1 177 ? -5.948  11.912  -87.675 1.00 159.30 ? 177 GLU A CA  1 
ATOM   1488  C C   . GLU A 1 177 ? -6.943  12.219  -86.543 1.00 161.93 ? 177 GLU A C   1 
ATOM   1489  O O   . GLU A 1 177 ? -8.127  12.480  -86.792 1.00 163.57 ? 177 GLU A O   1 
ATOM   1490  C CB  . GLU A 1 177 ? -6.668  11.802  -89.032 1.00 157.05 ? 177 GLU A CB  1 
ATOM   1491  C CG  . GLU A 1 177 ? -7.263  13.104  -89.561 1.00 155.32 ? 177 GLU A CG  1 
ATOM   1492  C CD  . GLU A 1 177 ? -6.258  13.962  -90.307 1.00 152.49 ? 177 GLU A CD  1 
ATOM   1493  O OE1 . GLU A 1 177 ? -5.269  14.415  -89.686 1.00 152.25 ? 177 GLU A OE1 1 
ATOM   1494  O OE2 . GLU A 1 177 ? -6.469  14.198  -91.517 1.00 149.90 ? 177 GLU A OE2 1 
ATOM   1495  N N   . VAL A 1 178 ? -6.452  12.176  -85.302 1.00 159.89 ? 178 VAL A N   1 
ATOM   1496  C CA  . VAL A 1 178 ? -7.271  12.472  -84.114 1.00 154.91 ? 178 VAL A CA  1 
ATOM   1497  C C   . VAL A 1 178 ? -6.529  13.386  -83.118 1.00 148.10 ? 178 VAL A C   1 
ATOM   1498  O O   . VAL A 1 178 ? -7.145  14.254  -82.488 1.00 145.74 ? 178 VAL A O   1 
ATOM   1499  C CB  . VAL A 1 178 ? -7.776  11.176  -83.420 1.00 154.83 ? 178 VAL A CB  1 
ATOM   1500  C CG1 . VAL A 1 178 ? -8.363  11.482  -82.054 1.00 151.94 ? 178 VAL A CG1 1 
ATOM   1501  C CG2 . VAL A 1 178 ? -8.819  10.471  -84.279 1.00 156.43 ? 178 VAL A CG2 1 
ATOM   1502  N N   . LYS A 1 179 ? -5.213  13.187  -82.996 1.00 139.25 ? 179 LYS A N   1 
ATOM   1503  C CA  . LYS A 1 179 ? -4.335  14.040  -82.169 1.00 132.98 ? 179 LYS A CA  1 
ATOM   1504  C C   . LYS A 1 179 ? -4.547  13.846  -80.657 1.00 131.99 ? 179 LYS A C   1 
ATOM   1505  O O   . LYS A 1 179 ? -5.532  14.336  -80.093 1.00 132.61 ? 179 LYS A O   1 
ATOM   1506  C CB  . LYS A 1 179 ? -4.468  15.522  -82.563 1.00 132.37 ? 179 LYS A CB  1 
ATOM   1507  C CG  . LYS A 1 179 ? -3.319  16.406  -82.101 1.00 128.62 ? 179 LYS A CG  1 
ATOM   1508  C CD  . LYS A 1 179 ? -3.346  17.756  -82.803 1.00 125.68 ? 179 LYS A CD  1 
ATOM   1509  C CE  . LYS A 1 179 ? -2.178  18.628  -82.372 1.00 121.33 ? 179 LYS A CE  1 
ATOM   1510  N NZ  . LYS A 1 179 ? -2.114  19.900  -83.142 1.00 118.05 ? 179 LYS A NZ  1 
ATOM   1511  N N   . PRO A 1 180 ? -3.601  13.145  -79.996 1.00 127.66 ? 180 PRO A N   1 
ATOM   1512  C CA  . PRO A 1 180 ? -3.747  12.700  -78.606 1.00 121.75 ? 180 PRO A CA  1 
ATOM   1513  C C   . PRO A 1 180 ? -3.584  13.832  -77.600 1.00 117.65 ? 180 PRO A C   1 
ATOM   1514  O O   . PRO A 1 180 ? -3.056  14.889  -77.941 1.00 119.60 ? 180 PRO A O   1 
ATOM   1515  C CB  . PRO A 1 180 ? -2.610  11.693  -78.447 1.00 119.92 ? 180 PRO A CB  1 
ATOM   1516  C CG  . PRO A 1 180 ? -1.556  12.175  -79.382 1.00 121.80 ? 180 PRO A CG  1 
ATOM   1517  C CD  . PRO A 1 180 ? -2.266  12.824  -80.539 1.00 124.70 ? 180 PRO A CD  1 
ATOM   1518  N N   . ARG A 1 181 ? -4.039  13.605  -76.370 1.00 114.45 ? 181 ARG A N   1 
ATOM   1519  C CA  . ARG A 1 181 ? -3.886  14.590  -75.298 1.00 112.98 ? 181 ARG A CA  1 
ATOM   1520  C C   . ARG A 1 181 ? -3.348  13.962  -74.003 1.00 107.64 ? 181 ARG A C   1 
ATOM   1521  O O   . ARG A 1 181 ? -3.822  14.264  -72.905 1.00 108.11 ? 181 ARG A O   1 
ATOM   1522  C CB  . ARG A 1 181 ? -5.201  15.347  -75.057 1.00 116.17 ? 181 ARG A CB  1 
ATOM   1523  C CG  . ARG A 1 181 ? -5.538  16.352  -76.154 1.00 119.55 ? 181 ARG A CG  1 
ATOM   1524  C CD  . ARG A 1 181 ? -6.868  17.053  -75.912 1.00 122.09 ? 181 ARG A CD  1 
ATOM   1525  N NE  . ARG A 1 181 ? -7.153  18.036  -76.961 1.00 124.52 ? 181 ARG A NE  1 
ATOM   1526  C CZ  . ARG A 1 181 ? -8.237  18.809  -77.010 1.00 124.70 ? 181 ARG A CZ  1 
ATOM   1527  N NH1 . ARG A 1 181 ? -9.169  18.731  -76.066 1.00 122.78 ? 181 ARG A NH1 1 
ATOM   1528  N NH2 . ARG A 1 181 ? -8.388  19.667  -78.010 1.00 126.05 ? 181 ARG A NH2 1 
ATOM   1529  N N   . GLY A 1 182 ? -2.339  13.103  -74.156 1.00 101.76 ? 182 GLY A N   1 
ATOM   1530  C CA  . GLY A 1 182 ? -1.691  12.411  -73.038 1.00 95.19  ? 182 GLY A CA  1 
ATOM   1531  C C   . GLY A 1 182 ? -1.110  11.081  -73.493 1.00 92.32  ? 182 GLY A C   1 
ATOM   1532  O O   . GLY A 1 182 ? -1.573  10.508  -74.479 1.00 93.75  ? 182 GLY A O   1 
ATOM   1533  N N   . VAL A 1 183 ? -0.101  10.584  -72.779 1.00 89.32  ? 183 VAL A N   1 
ATOM   1534  C CA  . VAL A 1 183 ? 0.562   9.323   -73.159 1.00 89.91  ? 183 VAL A CA  1 
ATOM   1535  C C   . VAL A 1 183 ? 0.171   8.144   -72.248 1.00 89.51  ? 183 VAL A C   1 
ATOM   1536  O O   . VAL A 1 183 ? 0.197   8.260   -71.016 1.00 88.98  ? 183 VAL A O   1 
ATOM   1537  C CB  . VAL A 1 183 ? 2.111   9.484   -73.258 1.00 89.21  ? 183 VAL A CB  1 
ATOM   1538  C CG1 . VAL A 1 183 ? 2.723   9.850   -71.910 1.00 88.38  ? 183 VAL A CG1 1 
ATOM   1539  C CG2 . VAL A 1 183 ? 2.761   8.230   -73.831 1.00 88.16  ? 183 VAL A CG2 1 
ATOM   1540  N N   . LEU A 1 184 ? -0.203  7.020   -72.865 1.00 87.74  ? 184 LEU A N   1 
ATOM   1541  C CA  . LEU A 1 184 ? -0.611  5.824   -72.121 1.00 85.34  ? 184 LEU A CA  1 
ATOM   1542  C C   . LEU A 1 184 ? 0.564   5.167   -71.407 1.00 82.31  ? 184 LEU A C   1 
ATOM   1543  O O   . LEU A 1 184 ? 1.549   4.779   -72.037 1.00 86.08  ? 184 LEU A O   1 
ATOM   1544  C CB  . LEU A 1 184 ? -1.303  4.804   -73.037 1.00 86.14  ? 184 LEU A CB  1 
ATOM   1545  C CG  . LEU A 1 184 ? -1.609  3.423   -72.426 1.00 85.68  ? 184 LEU A CG  1 
ATOM   1546  C CD1 . LEU A 1 184 ? -2.786  3.475   -71.461 1.00 84.58  ? 184 LEU A CD1 1 
ATOM   1547  C CD2 . LEU A 1 184 ? -1.860  2.391   -73.512 1.00 88.39  ? 184 LEU A CD2 1 
ATOM   1548  N N   . ASN A 1 185 ? 0.446   5.031   -70.092 1.00 78.66  ? 185 ASN A N   1 
ATOM   1549  C CA  . ASN A 1 185 ? 1.481   4.399   -69.297 1.00 73.53  ? 185 ASN A CA  1 
ATOM   1550  C C   . ASN A 1 185 ? 0.975   3.109   -68.674 1.00 70.64  ? 185 ASN A C   1 
ATOM   1551  O O   . ASN A 1 185 ? -0.070  3.094   -68.016 1.00 73.00  ? 185 ASN A O   1 
ATOM   1552  C CB  . ASN A 1 185 ? 1.971   5.357   -68.212 1.00 74.54  ? 185 ASN A CB  1 
ATOM   1553  C CG  . ASN A 1 185 ? 3.478   5.379   -68.097 1.00 76.68  ? 185 ASN A CG  1 
ATOM   1554  O OD1 . ASN A 1 185 ? 4.185   5.623   -69.078 1.00 74.90  ? 185 ASN A OD1 1 
ATOM   1555  N ND2 . ASN A 1 185 ? 3.982   5.125   -66.895 1.00 77.60  ? 185 ASN A ND2 1 
ATOM   1556  N N   . ILE A 1 186 ? 1.706   2.024   -68.895 1.00 65.60  ? 186 ILE A N   1 
ATOM   1557  C CA  . ILE A 1 186 ? 1.357   0.739   -68.302 1.00 64.56  ? 186 ILE A CA  1 
ATOM   1558  C C   . ILE A 1 186 ? 2.225   0.484   -67.069 1.00 64.84  ? 186 ILE A C   1 
ATOM   1559  O O   . ILE A 1 186 ? 3.451   0.462   -67.159 1.00 65.39  ? 186 ILE A O   1 
ATOM   1560  C CB  . ILE A 1 186 ? 1.473   -0.416  -69.327 1.00 61.77  ? 186 ILE A CB  1 
ATOM   1561  C CG1 . ILE A 1 186 ? 0.476   -0.204  -70.467 1.00 62.16  ? 186 ILE A CG1 1 
ATOM   1562  C CG2 . ILE A 1 186 ? 1.229   -1.766  -68.663 1.00 60.62  ? 186 ILE A CG2 1 
ATOM   1563  C CD1 . ILE A 1 186 ? 0.762   -1.028  -71.704 1.00 61.98  ? 186 ILE A CD1 1 
ATOM   1564  N N   . ILE A 1 187 ? 1.573   0.332   -65.916 1.00 67.90  ? 187 ILE A N   1 
ATOM   1565  C CA  . ILE A 1 187 ? 2.257   0.119   -64.633 1.00 67.35  ? 187 ILE A CA  1 
ATOM   1566  C C   . ILE A 1 187 ? 1.981   -1.298  -64.149 1.00 66.69  ? 187 ILE A C   1 
ATOM   1567  O O   . ILE A 1 187 ? 0.830   -1.705  -64.097 1.00 68.40  ? 187 ILE A O   1 
ATOM   1568  C CB  . ILE A 1 187 ? 1.751   1.099   -63.533 1.00 69.58  ? 187 ILE A CB  1 
ATOM   1569  C CG1 . ILE A 1 187 ? 1.703   2.550   -64.039 1.00 69.28  ? 187 ILE A CG1 1 
ATOM   1570  C CG2 . ILE A 1 187 ? 2.582   0.971   -62.251 1.00 67.99  ? 187 ILE A CG2 1 
ATOM   1571  C CD1 . ILE A 1 187 ? 3.045   3.128   -64.430 1.00 71.22  ? 187 ILE A CD1 1 
ATOM   1572  N N   . PRO A 1 188 ? 3.031   -2.045  -63.765 1.00 68.54  ? 188 PRO A N   1 
ATOM   1573  C CA  . PRO A 1 188 ? 2.791   -3.348  -63.140 1.00 71.69  ? 188 PRO A CA  1 
ATOM   1574  C C   . PRO A 1 188 ? 2.171   -3.181  -61.751 1.00 75.95  ? 188 PRO A C   1 
ATOM   1575  O O   . PRO A 1 188 ? 2.699   -2.431  -60.927 1.00 76.43  ? 188 PRO A O   1 
ATOM   1576  C CB  . PRO A 1 188 ? 4.199   -3.963  -63.030 1.00 69.30  ? 188 PRO A CB  1 
ATOM   1577  C CG  . PRO A 1 188 ? 5.088   -3.098  -63.865 1.00 67.89  ? 188 PRO A CG  1 
ATOM   1578  C CD  . PRO A 1 188 ? 4.466   -1.737  -63.858 1.00 67.41  ? 188 PRO A CD  1 
ATOM   1579  N N   . LYS A 1 189 ? 1.036   -3.841  -61.520 1.00 83.31  ? 189 LYS A N   1 
ATOM   1580  C CA  . LYS A 1 189 ? 0.359   -3.809  -60.221 1.00 86.82  ? 189 LYS A CA  1 
ATOM   1581  C C   . LYS A 1 189 ? 0.283   -5.201  -59.610 1.00 92.51  ? 189 LYS A C   1 
ATOM   1582  O O   . LYS A 1 189 ? -0.656  -5.955  -59.882 1.00 93.12  ? 189 LYS A O   1 
ATOM   1583  C CB  . LYS A 1 189 ? -1.052  -3.208  -60.338 1.00 86.41  ? 189 LYS A CB  1 
ATOM   1584  C CG  . LYS A 1 189 ? -1.110  -1.686  -60.271 1.00 86.47  ? 189 LYS A CG  1 
ATOM   1585  C CD  . LYS A 1 189 ? -0.580  -1.140  -58.951 1.00 80.87  ? 189 LYS A CD  1 
ATOM   1586  C CE  . LYS A 1 189 ? -0.271  0.346   -59.059 1.00 79.93  ? 189 LYS A CE  1 
ATOM   1587  N NZ  . LYS A 1 189 ? 0.519   0.823   -57.894 1.00 76.71  ? 189 LYS A NZ  1 
ATOM   1588  N N   . GLN A 1 190 ? 1.290   -5.532  -58.798 1.00 96.50  ? 190 GLN A N   1 
ATOM   1589  C CA  . GLN A 1 190 ? 1.328   -6.777  -58.016 1.00 100.54 ? 190 GLN A CA  1 
ATOM   1590  C C   . GLN A 1 190 ? 1.120   -8.038  -58.866 1.00 102.64 ? 190 GLN A C   1 
ATOM   1591  O O   . GLN A 1 190 ? 2.088   -8.674  -59.287 1.00 106.44 ? 190 GLN A O   1 
ATOM   1592  C CB  . GLN A 1 190 ? 0.333   -6.714  -56.847 1.00 105.57 ? 190 GLN A CB  1 
ATOM   1593  C CG  . GLN A 1 190 ? 0.587   -5.553  -55.888 1.00 110.84 ? 190 GLN A CG  1 
ATOM   1594  C CD  . GLN A 1 190 ? -0.692  -4.942  -55.330 1.00 112.60 ? 190 GLN A CD  1 
ATOM   1595  O OE1 . GLN A 1 190 ? -1.799  -5.328  -55.706 1.00 117.19 ? 190 GLN A OE1 1 
ATOM   1596  N NE2 . GLN A 1 190 ? -0.539  -3.970  -54.438 1.00 112.37 ? 190 GLN A NE2 1 
ATOM   1597  N N   . ASP A 1 191 ? -0.139  -8.389  -59.116 1.00 103.06 ? 191 ASP A N   1 
ATOM   1598  C CA  . ASP A 1 191 ? -0.470  -9.540  -59.953 1.00 103.94 ? 191 ASP A CA  1 
ATOM   1599  C C   . ASP A 1 191 ? -0.937  -9.107  -61.345 1.00 103.64 ? 191 ASP A C   1 
ATOM   1600  O O   . ASP A 1 191 ? -0.757  -9.837  -62.324 1.00 107.43 ? 191 ASP A O   1 
ATOM   1601  C CB  . ASP A 1 191 ? -1.540  -10.406 -59.277 1.00 105.33 ? 191 ASP A CB  1 
ATOM   1602  C CG  . ASP A 1 191 ? -1.666  -11.785 -59.909 1.00 107.24 ? 191 ASP A CG  1 
ATOM   1603  O OD1 . ASP A 1 191 ? -0.703  -12.580 -59.821 1.00 108.03 ? 191 ASP A OD1 1 
ATOM   1604  O OD2 . ASP A 1 191 ? -2.733  -12.078 -60.485 1.00 106.12 ? 191 ASP A OD2 1 
ATOM   1605  N N   . ASN A 1 192 ? -1.540  -7.922  -61.425 1.00 99.11  ? 192 ASN A N   1 
ATOM   1606  C CA  . ASN A 1 192 ? -2.047  -7.395  -62.692 1.00 95.82  ? 192 ASN A CA  1 
ATOM   1607  C C   . ASN A 1 192 ? -1.274  -6.173  -63.191 1.00 87.62  ? 192 ASN A C   1 
ATOM   1608  O O   . ASN A 1 192 ? -0.042  -6.166  -63.184 1.00 83.98  ? 192 ASN A O   1 
ATOM   1609  C CB  . ASN A 1 192 ? -3.548  -7.090  -62.590 1.00 100.44 ? 192 ASN A CB  1 
ATOM   1610  C CG  . ASN A 1 192 ? -4.411  -8.214  -63.133 1.00 104.56 ? 192 ASN A CG  1 
ATOM   1611  O OD1 . ASN A 1 192 ? -3.905  -9.190  -63.689 1.00 106.73 ? 192 ASN A OD1 1 
ATOM   1612  N ND2 . ASN A 1 192 ? -5.726  -8.080  -62.980 1.00 108.16 ? 192 ASN A ND2 1 
ATOM   1613  N N   . PHE A 1 193 ? -2.007  -5.153  -63.634 1.00 80.24  ? 193 PHE A N   1 
ATOM   1614  C CA  . PHE A 1 193 ? -1.416  -3.926  -64.156 1.00 76.49  ? 193 PHE A CA  1 
ATOM   1615  C C   . PHE A 1 193 ? -2.362  -2.741  -63.978 1.00 76.01  ? 193 PHE A C   1 
ATOM   1616  O O   . PHE A 1 193 ? -3.512  -2.910  -63.590 1.00 77.51  ? 193 PHE A O   1 
ATOM   1617  C CB  . PHE A 1 193 ? -1.078  -4.085  -65.640 1.00 72.32  ? 193 PHE A CB  1 
ATOM   1618  C CG  . PHE A 1 193 ? -2.283  -4.115  -66.530 1.00 69.06  ? 193 PHE A CG  1 
ATOM   1619  C CD1 . PHE A 1 193 ? -2.834  -2.934  -67.020 1.00 68.37  ? 193 PHE A CD1 1 
ATOM   1620  C CD2 . PHE A 1 193 ? -2.875  -5.323  -66.873 1.00 69.05  ? 193 PHE A CD2 1 
ATOM   1621  C CE1 . PHE A 1 193 ? -3.950  -2.957  -67.838 1.00 69.24  ? 193 PHE A CE1 1 
ATOM   1622  C CE2 . PHE A 1 193 ? -3.990  -5.355  -67.695 1.00 70.25  ? 193 PHE A CE2 1 
ATOM   1623  C CZ  . PHE A 1 193 ? -4.528  -4.170  -68.178 1.00 70.72  ? 193 PHE A CZ  1 
ATOM   1624  N N   . ARG A 1 194 ? -1.873  -1.548  -64.297 1.00 77.82  ? 194 ARG A N   1 
ATOM   1625  C CA  . ARG A 1 194 ? -2.687  -0.344  -64.259 1.00 79.81  ? 194 ARG A CA  1 
ATOM   1626  C C   . ARG A 1 194 ? -2.363  0.520   -65.470 1.00 79.00  ? 194 ARG A C   1 
ATOM   1627  O O   . ARG A 1 194 ? -1.207  0.891   -65.689 1.00 78.29  ? 194 ARG A O   1 
ATOM   1628  C CB  . ARG A 1 194 ? -2.427  0.428   -62.966 1.00 85.04  ? 194 ARG A CB  1 
ATOM   1629  C CG  . ARG A 1 194 ? -3.553  1.353   -62.560 1.00 93.65  ? 194 ARG A CG  1 
ATOM   1630  C CD  . ARG A 1 194 ? -3.155  2.207   -61.371 1.00 100.44 ? 194 ARG A CD  1 
ATOM   1631  N NE  . ARG A 1 194 ? -4.070  3.331   -61.200 1.00 109.57 ? 194 ARG A NE  1 
ATOM   1632  C CZ  . ARG A 1 194 ? -3.787  4.442   -60.524 1.00 114.76 ? 194 ARG A CZ  1 
ATOM   1633  N NH1 . ARG A 1 194 ? -2.600  4.597   -59.944 1.00 119.22 ? 194 ARG A NH1 1 
ATOM   1634  N NH2 . ARG A 1 194 ? -4.694  5.408   -60.437 1.00 117.81 ? 194 ARG A NH2 1 
ATOM   1635  N N   . ALA A 1 195 ? -3.383  0.818   -66.268 1.00 76.87  ? 195 ALA A N   1 
ATOM   1636  C CA  . ALA A 1 195 ? -3.203  1.607   -67.476 1.00 77.40  ? 195 ALA A CA  1 
ATOM   1637  C C   . ALA A 1 195 ? -3.668  3.042   -67.270 1.00 79.01  ? 195 ALA A C   1 
ATOM   1638  O O   . ALA A 1 195 ? -4.840  3.364   -67.466 1.00 79.78  ? 195 ALA A O   1 
ATOM   1639  C CB  . ALA A 1 195 ? -3.933  0.966   -68.643 1.00 78.89  ? 195 ALA A CB  1 
ATOM   1640  N N   . ILE A 1 196 ? -2.733  3.900   -66.873 1.00 81.96  ? 196 ILE A N   1 
ATOM   1641  C CA  . ILE A 1 196 ? -3.030  5.304   -66.584 1.00 82.66  ? 196 ILE A CA  1 
ATOM   1642  C C   . ILE A 1 196 ? -2.437  6.226   -67.651 1.00 84.96  ? 196 ILE A C   1 
ATOM   1643  O O   . ILE A 1 196 ? -1.581  5.807   -68.436 1.00 83.97  ? 196 ILE A O   1 
ATOM   1644  C CB  . ILE A 1 196 ? -2.520  5.720   -65.180 1.00 81.57  ? 196 ILE A CB  1 
ATOM   1645  C CG1 . ILE A 1 196 ? -0.997  5.546   -65.072 1.00 82.34  ? 196 ILE A CG1 1 
ATOM   1646  C CG2 . ILE A 1 196 ? -3.231  4.919   -64.098 1.00 82.50  ? 196 ILE A CG2 1 
ATOM   1647  C CD1 . ILE A 1 196 ? -0.386  6.150   -63.821 1.00 80.72  ? 196 ILE A CD1 1 
ATOM   1648  N N   . VAL A 1 197 ? -2.896  7.477   -67.676 1.00 85.71  ? 197 VAL A N   1 
ATOM   1649  C CA  . VAL A 1 197 ? -2.382  8.466   -68.623 1.00 85.10  ? 197 VAL A CA  1 
ATOM   1650  C C   . VAL A 1 197 ? -1.664  9.624   -67.950 1.00 88.55  ? 197 VAL A C   1 
ATOM   1651  O O   . VAL A 1 197 ? -2.140  10.182  -66.958 1.00 88.00  ? 197 VAL A O   1 
ATOM   1652  C CB  . VAL A 1 197 ? -3.484  9.027   -69.545 1.00 82.57  ? 197 VAL A CB  1 
ATOM   1653  C CG1 . VAL A 1 197 ? -3.981  7.945   -70.479 1.00 83.39  ? 197 VAL A CG1 1 
ATOM   1654  C CG2 . VAL A 1 197 ? -4.627  9.623   -68.737 1.00 80.51  ? 197 VAL A CG2 1 
ATOM   1655  N N   . SER A 1 198 ? -0.513  9.980   -68.503 1.00 94.87  ? 198 SER A N   1 
ATOM   1656  C CA  . SER A 1 198 ? 0.196   11.173  -68.085 1.00 101.68 ? 198 SER A CA  1 
ATOM   1657  C C   . SER A 1 198 ? -0.094  12.295  -69.075 1.00 108.17 ? 198 SER A C   1 
ATOM   1658  O O   . SER A 1 198 ? 0.169   12.161  -70.274 1.00 107.77 ? 198 SER A O   1 
ATOM   1659  C CB  . SER A 1 198 ? 1.699   10.899  -67.998 1.00 101.75 ? 198 SER A CB  1 
ATOM   1660  O OG  . SER A 1 198 ? 1.974   9.852   -67.078 1.00 96.38  ? 198 SER A OG  1 
ATOM   1661  N N   . ILE A 1 199 ? -0.664  13.387  -68.572 1.00 113.87 ? 199 ILE A N   1 
ATOM   1662  C CA  . ILE A 1 199 ? -1.004  14.539  -69.407 1.00 122.15 ? 199 ILE A CA  1 
ATOM   1663  C C   . ILE A 1 199 ? 0.236   15.420  -69.617 1.00 128.36 ? 199 ILE A C   1 
ATOM   1664  O O   . ILE A 1 199 ? 1.269   15.203  -68.978 1.00 127.37 ? 199 ILE A O   1 
ATOM   1665  C CB  . ILE A 1 199 ? -2.163  15.375  -68.799 1.00 121.69 ? 199 ILE A CB  1 
ATOM   1666  C CG1 . ILE A 1 199 ? -3.006  14.541  -67.813 1.00 118.69 ? 199 ILE A CG1 1 
ATOM   1667  C CG2 . ILE A 1 199 ? -3.020  15.992  -69.901 1.00 122.82 ? 199 ILE A CG2 1 
ATOM   1668  C CD1 . ILE A 1 199 ? -3.981  13.573  -68.459 1.00 118.67 ? 199 ILE A CD1 1 
ATOM   1669  N N   . PHE A 1 200 ? 0.128   16.408  -70.508 1.00 137.33 ? 200 PHE A N   1 
ATOM   1670  C CA  . PHE A 1 200 ? 1.273   17.252  -70.899 1.00 145.67 ? 200 PHE A CA  1 
ATOM   1671  C C   . PHE A 1 200 ? 1.865   18.182  -69.814 1.00 151.10 ? 200 PHE A C   1 
ATOM   1672  O O   . PHE A 1 200 ? 3.087   18.327  -69.744 1.00 144.46 ? 200 PHE A O   1 
ATOM   1673  C CB  . PHE A 1 200 ? 0.966   18.038  -72.182 1.00 149.86 ? 200 PHE A CB  1 
ATOM   1674  C CG  . PHE A 1 200 ? 0.863   17.177  -73.412 1.00 153.42 ? 200 PHE A CG  1 
ATOM   1675  C CD1 . PHE A 1 200 ? 2.007   16.761  -74.087 1.00 154.97 ? 200 PHE A CD1 1 
ATOM   1676  C CD2 . PHE A 1 200 ? -0.378  16.787  -73.902 1.00 155.88 ? 200 PHE A CD2 1 
ATOM   1677  C CE1 . PHE A 1 200 ? 1.914   15.969  -75.224 1.00 155.10 ? 200 PHE A CE1 1 
ATOM   1678  C CE2 . PHE A 1 200 ? -0.476  15.997  -75.039 1.00 155.61 ? 200 PHE A CE2 1 
ATOM   1679  C CZ  . PHE A 1 200 ? 0.670   15.587  -75.700 1.00 154.69 ? 200 PHE A CZ  1 
ATOM   1680  N N   . PRO A 1 201 ? 1.014   18.832  -68.981 1.00 161.97 ? 201 PRO A N   1 
ATOM   1681  C CA  . PRO A 1 201 ? -0.448  18.856  -68.969 1.00 169.02 ? 201 PRO A CA  1 
ATOM   1682  C C   . PRO A 1 201 ? -1.032  20.039  -69.753 1.00 174.85 ? 201 PRO A C   1 
ATOM   1683  O O   . PRO A 1 201 ? -1.452  19.866  -70.900 1.00 180.13 ? 201 PRO A O   1 
ATOM   1684  C CB  . PRO A 1 201 ? -0.784  18.977  -67.470 1.00 167.75 ? 201 PRO A CB  1 
ATOM   1685  C CG  . PRO A 1 201 ? 0.472   19.469  -66.802 1.00 163.66 ? 201 PRO A CG  1 
ATOM   1686  C CD  . PRO A 1 201 ? 1.560   19.581  -67.836 1.00 161.78 ? 201 PRO A CD  1 
ATOM   1687  N N   . ASP A 1 202 ? -1.046  21.222  -69.133 1.00 174.41 ? 202 ASP A N   1 
ATOM   1688  C CA  . ASP A 1 202 ? -1.629  22.436  -69.721 1.00 175.55 ? 202 ASP A CA  1 
ATOM   1689  C C   . ASP A 1 202 ? -3.102  22.252  -70.120 1.00 184.28 ? 202 ASP A C   1 
ATOM   1690  O O   . ASP A 1 202 ? -3.995  22.428  -69.287 1.00 186.84 ? 202 ASP A O   1 
ATOM   1691  C CB  . ASP A 1 202 ? -0.785  22.942  -70.904 1.00 167.47 ? 202 ASP A CB  1 
ATOM   1692  C CG  . ASP A 1 202 ? -1.149  24.358  -71.322 1.00 162.74 ? 202 ASP A CG  1 
ATOM   1693  O OD1 . ASP A 1 202 ? -1.445  25.190  -70.437 1.00 158.58 ? 202 ASP A OD1 1 
ATOM   1694  O OD2 . ASP A 1 202 ? -1.129  24.642  -72.538 1.00 159.89 ? 202 ASP A OD2 1 
ATOM   1695  N N   . SER A 1 203 ? -3.333  21.877  -71.384 1.00 189.34 ? 203 SER A N   1 
ATOM   1696  C CA  . SER A 1 203 ? -4.685  21.691  -71.956 1.00 190.30 ? 203 SER A CA  1 
ATOM   1697  C C   . SER A 1 203 ? -5.653  22.834  -71.625 1.00 190.76 ? 203 SER A C   1 
ATOM   1698  O O   . SER A 1 203 ? -6.345  22.803  -70.601 1.00 188.89 ? 203 SER A O   1 
ATOM   1699  C CB  . SER A 1 203 ? -5.276  20.326  -71.569 1.00 189.36 ? 203 SER A CB  1 
ATOM   1700  O OG  . SER A 1 203 ? -5.265  20.133  -70.166 1.00 187.78 ? 203 SER A OG  1 
ATOM   1701  N N   . ALA A 1 204 ? -5.709  23.822  -72.521 1.00 191.46 ? 204 ALA A N   1 
ATOM   1702  C CA  . ALA A 1 204 ? -6.359  25.110  -72.253 1.00 191.37 ? 204 ALA A CA  1 
ATOM   1703  C C   . ALA A 1 204 ? -5.746  25.765  -71.012 1.00 191.21 ? 204 ALA A C   1 
ATOM   1704  O O   . ALA A 1 204 ? -4.779  26.522  -71.120 1.00 194.19 ? 204 ALA A O   1 
ATOM   1705  C CB  . ALA A 1 204 ? -7.871  24.949  -72.110 1.00 189.30 ? 204 ALA A CB  1 
ATOM   1706  N N   . ARG A 1 205 ? -6.303  25.454  -69.842 1.00 186.54 ? 205 ARG A N   1 
ATOM   1707  C CA  . ARG A 1 205 ? -5.727  25.861  -68.560 1.00 178.80 ? 205 ARG A CA  1 
ATOM   1708  C C   . ARG A 1 205 ? -6.007  24.809  -67.492 1.00 172.82 ? 205 ARG A C   1 
ATOM   1709  O O   . ARG A 1 205 ? -7.039  24.137  -67.530 1.00 170.90 ? 205 ARG A O   1 
ATOM   1710  C CB  . ARG A 1 205 ? -6.276  27.224  -68.125 1.00 179.77 ? 205 ARG A CB  1 
ATOM   1711  C CG  . ARG A 1 205 ? -5.446  28.407  -68.598 1.00 181.20 ? 205 ARG A CG  1 
ATOM   1712  C CD  . ARG A 1 205 ? -6.299  29.651  -68.776 1.00 183.44 ? 205 ARG A CD  1 
ATOM   1713  N NE  . ARG A 1 205 ? -5.584  30.702  -69.502 1.00 184.70 ? 205 ARG A NE  1 
ATOM   1714  C CZ  . ARG A 1 205 ? -6.163  31.773  -70.043 1.00 185.30 ? 205 ARG A CZ  1 
ATOM   1715  N NH1 . ARG A 1 205 ? -7.478  31.946  -69.953 1.00 185.79 ? 205 ARG A NH1 1 
ATOM   1716  N NH2 . ARG A 1 205 ? -5.425  32.671  -70.682 1.00 183.39 ? 205 ARG A NH2 1 
ATOM   1717  N N   . LYS A 1 206 ? -5.081  24.666  -66.548 1.00 168.57 ? 206 LYS A N   1 
ATOM   1718  C CA  . LYS A 1 206 ? -5.247  23.720  -65.446 1.00 165.68 ? 206 LYS A CA  1 
ATOM   1719  C C   . LYS A 1 206 ? -6.267  24.184  -64.388 1.00 168.05 ? 206 LYS A C   1 
ATOM   1720  O O   . LYS A 1 206 ? -6.943  23.348  -63.785 1.00 169.71 ? 206 LYS A O   1 
ATOM   1721  C CB  . LYS A 1 206 ? -3.900  23.384  -64.797 1.00 161.61 ? 206 LYS A CB  1 
ATOM   1722  C CG  . LYS A 1 206 ? -3.914  22.089  -64.001 1.00 159.79 ? 206 LYS A CG  1 
ATOM   1723  C CD  . LYS A 1 206 ? -2.588  21.838  -63.308 1.00 158.27 ? 206 LYS A CD  1 
ATOM   1724  C CE  . LYS A 1 206 ? -2.654  20.585  -62.451 1.00 156.27 ? 206 LYS A CE  1 
ATOM   1725  N NZ  . LYS A 1 206 ? -1.349  20.290  -61.799 1.00 154.89 ? 206 LYS A NZ  1 
ATOM   1726  N N   . PRO A 1 207 ? -6.377  25.516  -64.155 1.00 170.59 ? 207 PRO A N   1 
ATOM   1727  C CA  . PRO A 1 207 ? -7.421  26.038  -63.254 1.00 166.67 ? 207 PRO A CA  1 
ATOM   1728  C C   . PRO A 1 207 ? -8.840  25.864  -63.801 1.00 161.45 ? 207 PRO A C   1 
ATOM   1729  O O   . PRO A 1 207 ? -9.799  25.842  -63.026 1.00 156.43 ? 207 PRO A O   1 
ATOM   1730  C CB  . PRO A 1 207 ? -7.080  27.532  -63.143 1.00 170.30 ? 207 PRO A CB  1 
ATOM   1731  C CG  . PRO A 1 207 ? -6.241  27.829  -64.341 1.00 173.25 ? 207 PRO A CG  1 
ATOM   1732  C CD  . PRO A 1 207 ? -5.443  26.582  -64.565 1.00 172.65 ? 207 PRO A CD  1 
ATOM   1733  N N   . PHE A 1 208 ? -8.962  25.757  -65.125 1.00 159.01 ? 208 PHE A N   1 
ATOM   1734  C CA  . PHE A 1 208 ? -10.243 25.471  -65.774 1.00 153.92 ? 208 PHE A CA  1 
ATOM   1735  C C   . PHE A 1 208 ? -10.780 24.116  -65.330 1.00 148.42 ? 208 PHE A C   1 
ATOM   1736  O O   . PHE A 1 208 ? -11.973 23.975  -65.063 1.00 146.92 ? 208 PHE A O   1 
ATOM   1737  C CB  . PHE A 1 208 ? -10.098 25.516  -67.302 1.00 156.42 ? 208 PHE A CB  1 
ATOM   1738  C CG  . PHE A 1 208 ? -11.327 25.062  -68.047 1.00 155.87 ? 208 PHE A CG  1 
ATOM   1739  C CD1 . PHE A 1 208 ? -12.454 25.876  -68.122 1.00 158.52 ? 208 PHE A CD1 1 
ATOM   1740  C CD2 . PHE A 1 208 ? -11.354 23.825  -68.683 1.00 153.90 ? 208 PHE A CD2 1 
ATOM   1741  C CE1 . PHE A 1 208 ? -13.586 25.462  -68.810 1.00 159.26 ? 208 PHE A CE1 1 
ATOM   1742  C CE2 . PHE A 1 208 ? -12.482 23.406  -69.372 1.00 156.05 ? 208 PHE A CE2 1 
ATOM   1743  C CZ  . PHE A 1 208 ? -13.600 24.225  -69.436 1.00 158.32 ? 208 PHE A CZ  1 
ATOM   1744  N N   . PHE A 1 209 ? -9.889  23.128  -65.252 1.00 141.35 ? 209 PHE A N   1 
ATOM   1745  C CA  . PHE A 1 209 ? -10.242 21.794  -64.770 1.00 136.33 ? 209 PHE A CA  1 
ATOM   1746  C C   . PHE A 1 209 ? -10.579 21.788  -63.278 1.00 133.97 ? 209 PHE A C   1 
ATOM   1747  O O   . PHE A 1 209 ? -11.552 21.157  -62.865 1.00 133.93 ? 209 PHE A O   1 
ATOM   1748  C CB  . PHE A 1 209 ? -9.115  20.792  -65.054 1.00 131.99 ? 209 PHE A CB  1 
ATOM   1749  C CG  . PHE A 1 209 ? -9.067  20.309  -66.480 1.00 131.09 ? 209 PHE A CG  1 
ATOM   1750  C CD1 . PHE A 1 209 ? -10.211 19.828  -67.111 1.00 131.21 ? 209 PHE A CD1 1 
ATOM   1751  C CD2 . PHE A 1 209 ? -7.867  20.302  -67.183 1.00 130.66 ? 209 PHE A CD2 1 
ATOM   1752  C CE1 . PHE A 1 209 ? -10.163 19.374  -68.421 1.00 128.99 ? 209 PHE A CE1 1 
ATOM   1753  C CE2 . PHE A 1 209 ? -7.815  19.847  -68.492 1.00 129.06 ? 209 PHE A CE2 1 
ATOM   1754  C CZ  . PHE A 1 209 ? -8.963  19.382  -69.111 1.00 127.10 ? 209 PHE A CZ  1 
ATOM   1755  N N   . LYS A 1 210 ? -9.777  22.494  -62.480 1.00 131.46 ? 210 LYS A N   1 
ATOM   1756  C CA  . LYS A 1 210 ? -9.936  22.493  -61.020 1.00 128.81 ? 210 LYS A CA  1 
ATOM   1757  C C   . LYS A 1 210 ? -11.250 23.134  -60.569 1.00 130.62 ? 210 LYS A C   1 
ATOM   1758  O O   . LYS A 1 210 ? -11.859 22.690  -59.593 1.00 127.33 ? 210 LYS A O   1 
ATOM   1759  C CB  . LYS A 1 210 ? -8.738  23.156  -60.327 1.00 125.03 ? 210 LYS A CB  1 
ATOM   1760  C CG  . LYS A 1 210 ? -8.641  22.851  -58.837 1.00 121.13 ? 210 LYS A CG  1 
ATOM   1761  C CD  . LYS A 1 210 ? -7.199  22.824  -58.358 1.00 117.62 ? 210 LYS A CD  1 
ATOM   1762  C CE  . LYS A 1 210 ? -7.114  22.374  -56.909 1.00 114.51 ? 210 LYS A CE  1 
ATOM   1763  N NZ  . LYS A 1 210 ? -5.743  21.916  -56.554 1.00 110.40 ? 210 LYS A NZ  1 
ATOM   1764  N N   . LEU A 1 211 ? -11.681 24.174  -61.280 1.00 135.04 ? 211 LEU A N   1 
ATOM   1765  C CA  . LEU A 1 211 ? -12.985 24.788  -61.019 1.00 138.09 ? 211 LEU A CA  1 
ATOM   1766  C C   . LEU A 1 211 ? -14.094 24.209  -61.911 1.00 137.31 ? 211 LEU A C   1 
ATOM   1767  O O   . LEU A 1 211 ? -15.240 24.666  -61.870 1.00 140.70 ? 211 LEU A O   1 
ATOM   1768  C CB  . LEU A 1 211 ? -12.914 26.322  -61.129 1.00 141.36 ? 211 LEU A CB  1 
ATOM   1769  C CG  . LEU A 1 211 ? -12.551 27.094  -59.847 1.00 138.39 ? 211 LEU A CG  1 
ATOM   1770  C CD1 . LEU A 1 211 ? -11.045 27.278  -59.716 1.00 134.41 ? 211 LEU A CD1 1 
ATOM   1771  C CD2 . LEU A 1 211 ? -13.260 28.442  -59.803 1.00 137.17 ? 211 LEU A CD2 1 
ATOM   1772  N N   . LEU A 1 212 ? -13.744 23.199  -62.707 1.00 131.42 ? 212 LEU A N   1 
ATOM   1773  C CA  . LEU A 1 212 ? -14.732 22.404  -63.434 1.00 125.72 ? 212 LEU A CA  1 
ATOM   1774  C C   . LEU A 1 212 ? -15.160 21.223  -62.569 1.00 121.97 ? 212 LEU A C   1 
ATOM   1775  O O   . LEU A 1 212 ? -16.350 20.936  -62.438 1.00 119.58 ? 212 LEU A O   1 
ATOM   1776  C CB  . LEU A 1 212 ? -14.156 21.914  -64.770 1.00 122.86 ? 212 LEU A CB  1 
ATOM   1777  C CG  . LEU A 1 212 ? -15.087 21.510  -65.924 1.00 121.96 ? 212 LEU A CG  1 
ATOM   1778  C CD1 . LEU A 1 212 ? -15.521 20.056  -65.820 1.00 119.80 ? 212 LEU A CD1 1 
ATOM   1779  C CD2 . LEU A 1 212 ? -16.291 22.439  -66.044 1.00 124.52 ? 212 LEU A CD2 1 
ATOM   1780  N N   . THR A 1 213 ? -14.179 20.548  -61.972 1.00 121.92 ? 213 THR A N   1 
ATOM   1781  C CA  . THR A 1 213 ? -14.449 19.468  -61.022 1.00 122.24 ? 213 THR A CA  1 
ATOM   1782  C C   . THR A 1 213 ? -15.081 19.997  -59.736 1.00 120.39 ? 213 THR A C   1 
ATOM   1783  O O   . THR A 1 213 ? -15.860 19.298  -59.086 1.00 121.41 ? 213 THR A O   1 
ATOM   1784  C CB  . THR A 1 213 ? -13.181 18.636  -60.694 1.00 121.15 ? 213 THR A CB  1 
ATOM   1785  O OG1 . THR A 1 213 ? -13.482 17.687  -59.663 1.00 121.01 ? 213 THR A OG1 1 
ATOM   1786  C CG2 . THR A 1 213 ? -12.036 19.524  -60.225 1.00 120.92 ? 213 THR A CG2 1 
ATOM   1787  N N   . SER A 1 214 ? -14.747 21.237  -59.383 1.00 119.97 ? 214 SER A N   1 
ATOM   1788  C CA  . SER A 1 214 ? -15.336 21.900  -58.224 1.00 120.29 ? 214 SER A CA  1 
ATOM   1789  C C   . SER A 1 214 ? -16.830 22.126  -58.434 1.00 120.54 ? 214 SER A C   1 
ATOM   1790  O O   . SER A 1 214 ? -17.614 22.084  -57.484 1.00 119.17 ? 214 SER A O   1 
ATOM   1791  C CB  . SER A 1 214 ? -14.633 23.229  -57.950 1.00 120.99 ? 214 SER A CB  1 
ATOM   1792  O OG  . SER A 1 214 ? -14.864 23.663  -56.622 1.00 121.22 ? 214 SER A OG  1 
ATOM   1793  N N   . LYS A 1 215 ? -17.217 22.357  -59.687 1.00 119.94 ? 215 LYS A N   1 
ATOM   1794  C CA  . LYS A 1 215 ? -18.625 22.461  -60.052 1.00 122.74 ? 215 LYS A CA  1 
ATOM   1795  C C   . LYS A 1 215 ? -19.341 21.113  -59.950 1.00 121.03 ? 215 LYS A C   1 
ATOM   1796  O O   . LYS A 1 215 ? -20.551 21.065  -59.713 1.00 122.42 ? 215 LYS A O   1 
ATOM   1797  C CB  . LYS A 1 215 ? -18.781 23.045  -61.459 1.00 125.43 ? 215 LYS A CB  1 
ATOM   1798  C CG  . LYS A 1 215 ? -18.816 24.565  -61.499 1.00 127.65 ? 215 LYS A CG  1 
ATOM   1799  C CD  . LYS A 1 215 ? -19.341 25.075  -62.833 1.00 130.48 ? 215 LYS A CD  1 
ATOM   1800  C CE  . LYS A 1 215 ? -19.822 26.515  -62.723 1.00 129.45 ? 215 LYS A CE  1 
ATOM   1801  N NZ  . LYS A 1 215 ? -20.384 27.019  -64.006 1.00 131.59 ? 215 LYS A NZ  1 
ATOM   1802  N N   . ILE A 1 216 ? -18.587 20.025  -60.115 1.00 114.34 ? 216 ILE A N   1 
ATOM   1803  C CA  . ILE A 1 216 ? -19.145 18.672  -60.033 1.00 109.99 ? 216 ILE A CA  1 
ATOM   1804  C C   . ILE A 1 216 ? -19.348 18.199  -58.587 1.00 109.53 ? 216 ILE A C   1 
ATOM   1805  O O   . ILE A 1 216 ? -20.399 17.646  -58.258 1.00 111.26 ? 216 ILE A O   1 
ATOM   1806  C CB  . ILE A 1 216 ? -18.303 17.653  -60.831 1.00 105.86 ? 216 ILE A CB  1 
ATOM   1807  C CG1 . ILE A 1 216 ? -18.382 17.968  -62.327 1.00 107.35 ? 216 ILE A CG1 1 
ATOM   1808  C CG2 . ILE A 1 216 ? -18.781 16.230  -60.570 1.00 103.92 ? 216 ILE A CG2 1 
ATOM   1809  C CD1 . ILE A 1 216 ? -17.246 17.391  -63.144 1.00 107.63 ? 216 ILE A CD1 1 
ATOM   1810  N N   . TYR A 1 217 ? -18.355 18.429  -57.726 1.00 106.94 ? 217 TYR A N   1 
ATOM   1811  C CA  . TYR A 1 217 ? -18.462 18.037  -56.315 1.00 105.66 ? 217 TYR A CA  1 
ATOM   1812  C C   . TYR A 1 217 ? -19.655 18.685  -55.618 1.00 108.83 ? 217 TYR A C   1 
ATOM   1813  O O   . TYR A 1 217 ? -20.187 18.142  -54.647 1.00 108.80 ? 217 TYR A O   1 
ATOM   1814  C CB  . TYR A 1 217 ? -17.167 18.324  -55.557 1.00 104.06 ? 217 TYR A CB  1 
ATOM   1815  C CG  . TYR A 1 217 ? -16.132 17.234  -55.708 1.00 102.64 ? 217 TYR A CG  1 
ATOM   1816  C CD1 . TYR A 1 217 ? -16.273 16.014  -55.046 1.00 103.21 ? 217 TYR A CD1 1 
ATOM   1817  C CD2 . TYR A 1 217 ? -15.013 17.416  -56.518 1.00 103.98 ? 217 TYR A CD2 1 
ATOM   1818  C CE1 . TYR A 1 217 ? -15.329 15.007  -55.187 1.00 101.73 ? 217 TYR A CE1 1 
ATOM   1819  C CE2 . TYR A 1 217 ? -14.061 16.415  -56.664 1.00 101.64 ? 217 TYR A CE2 1 
ATOM   1820  C CZ  . TYR A 1 217 ? -14.225 15.214  -55.999 1.00 99.33  ? 217 TYR A CZ  1 
ATOM   1821  O OH  . TYR A 1 217 ? -13.286 14.220  -56.143 1.00 97.38  ? 217 TYR A OH  1 
ATOM   1822  N N   . LYS A 1 218 ? -20.069 19.846  -56.123 1.00 113.22 ? 218 LYS A N   1 
ATOM   1823  C CA  . LYS A 1 218 ? -21.345 20.440  -55.748 1.00 114.84 ? 218 LYS A CA  1 
ATOM   1824  C C   . LYS A 1 218 ? -22.466 19.465  -56.080 1.00 115.33 ? 218 LYS A C   1 
ATOM   1825  O O   . LYS A 1 218 ? -23.136 18.958  -55.182 1.00 116.79 ? 218 LYS A O   1 
ATOM   1826  C CB  . LYS A 1 218 ? -21.574 21.759  -56.491 1.00 118.73 ? 218 LYS A CB  1 
ATOM   1827  C CG  . LYS A 1 218 ? -20.639 22.890  -56.098 1.00 122.15 ? 218 LYS A CG  1 
ATOM   1828  C CD  . LYS A 1 218 ? -20.980 24.161  -56.862 1.00 124.47 ? 218 LYS A CD  1 
ATOM   1829  C CE  . LYS A 1 218 ? -19.912 25.226  -56.678 1.00 123.65 ? 218 LYS A CE  1 
ATOM   1830  N NZ  . LYS A 1 218 ? -20.249 26.469  -57.422 1.00 125.50 ? 218 LYS A NZ  1 
ATOM   1831  N N   . VAL A 1 219 ? -22.633 19.182  -57.375 1.00 115.18 ? 219 VAL A N   1 
ATOM   1832  C CA  . VAL A 1 219 ? -23.711 18.312  -57.877 1.00 115.61 ? 219 VAL A CA  1 
ATOM   1833  C C   . VAL A 1 219 ? -23.798 17.000  -57.098 1.00 115.32 ? 219 VAL A C   1 
ATOM   1834  O O   . VAL A 1 219 ? -24.893 16.488  -56.849 1.00 115.50 ? 219 VAL A O   1 
ATOM   1835  C CB  . VAL A 1 219 ? -23.544 17.994  -59.386 1.00 113.61 ? 219 VAL A CB  1 
ATOM   1836  C CG1 . VAL A 1 219 ? -24.751 17.231  -59.915 1.00 112.43 ? 219 VAL A CG1 1 
ATOM   1837  C CG2 . VAL A 1 219 ? -23.331 19.269  -60.189 1.00 115.28 ? 219 VAL A CG2 1 
ATOM   1838  N N   . LEU A 1 220 ? -22.639 16.472  -56.711 1.00 114.52 ? 220 LEU A N   1 
ATOM   1839  C CA  . LEU A 1 220 ? -22.564 15.227  -55.957 1.00 113.71 ? 220 LEU A CA  1 
ATOM   1840  C C   . LEU A 1 220 ? -23.327 15.333  -54.639 1.00 114.51 ? 220 LEU A C   1 
ATOM   1841  O O   . LEU A 1 220 ? -24.081 14.430  -54.280 1.00 113.76 ? 220 LEU A O   1 
ATOM   1842  C CB  . LEU A 1 220 ? -21.105 14.850  -55.692 1.00 111.89 ? 220 LEU A CB  1 
ATOM   1843  C CG  . LEU A 1 220 ? -20.678 13.398  -55.934 1.00 111.79 ? 220 LEU A CG  1 
ATOM   1844  C CD1 . LEU A 1 220 ? -19.243 13.199  -55.468 1.00 110.07 ? 220 LEU A CD1 1 
ATOM   1845  C CD2 . LEU A 1 220 ? -21.602 12.400  -55.249 1.00 111.85 ? 220 LEU A CD2 1 
ATOM   1846  N N   . GLU A 1 221 ? -23.138 16.445  -53.931 1.00 117.38 ? 221 GLU A N   1 
ATOM   1847  C CA  . GLU A 1 221 ? -23.841 16.682  -52.666 1.00 120.33 ? 221 GLU A CA  1 
ATOM   1848  C C   . GLU A 1 221 ? -25.102 17.545  -52.828 1.00 123.87 ? 221 GLU A C   1 
ATOM   1849  O O   . GLU A 1 221 ? -25.570 18.159  -51.869 1.00 127.66 ? 221 GLU A O   1 
ATOM   1850  C CB  . GLU A 1 221 ? -22.891 17.261  -51.598 1.00 121.36 ? 221 GLU A CB  1 
ATOM   1851  C CG  . GLU A 1 221 ? -22.002 18.411  -52.064 1.00 120.98 ? 221 GLU A CG  1 
ATOM   1852  C CD  . GLU A 1 221 ? -22.590 19.779  -51.766 1.00 121.00 ? 221 GLU A CD  1 
ATOM   1853  O OE1 . GLU A 1 221 ? -22.927 20.045  -50.593 1.00 117.57 ? 221 GLU A OE1 1 
ATOM   1854  O OE2 . GLU A 1 221 ? -22.695 20.600  -52.702 1.00 122.10 ? 221 GLU A OE2 1 
ATOM   1855  N N   . GLU A 1 222 ? -25.653 17.567  -54.042 1.00 126.45 ? 222 GLU A N   1 
ATOM   1856  C CA  . GLU A 1 222 ? -26.894 18.292  -54.324 1.00 126.22 ? 222 GLU A CA  1 
ATOM   1857  C C   . GLU A 1 222 ? -28.053 17.327  -54.550 1.00 125.69 ? 222 GLU A C   1 
ATOM   1858  O O   . GLU A 1 222 ? -28.949 17.212  -53.711 1.00 125.36 ? 222 GLU A O   1 
ATOM   1859  C CB  . GLU A 1 222 ? -26.733 19.201  -55.551 1.00 131.12 ? 222 GLU A CB  1 
ATOM   1860  C CG  . GLU A 1 222 ? -25.787 20.380  -55.363 1.00 131.84 ? 222 GLU A CG  1 
ATOM   1861  C CD  . GLU A 1 222 ? -26.331 21.445  -54.428 1.00 134.23 ? 222 GLU A CD  1 
ATOM   1862  O OE1 . GLU A 1 222 ? -27.564 21.658  -54.407 1.00 136.74 ? 222 GLU A OE1 1 
ATOM   1863  O OE2 . GLU A 1 222 ? -25.517 22.078  -53.721 1.00 131.37 ? 222 GLU A OE2 1 
ATOM   1864  N N   . LYS A 1 223 ? -28.029 16.637  -55.689 1.00 125.04 ? 223 LYS A N   1 
ATOM   1865  C CA  . LYS A 1 223 ? -29.103 15.718  -56.063 1.00 126.07 ? 223 LYS A CA  1 
ATOM   1866  C C   . LYS A 1 223 ? -28.898 14.322  -55.465 1.00 124.33 ? 223 LYS A C   1 
ATOM   1867  O O   . LYS A 1 223 ? -29.700 13.413  -55.698 1.00 126.82 ? 223 LYS A O   1 
ATOM   1868  C CB  . LYS A 1 223 ? -29.260 15.648  -57.592 1.00 126.59 ? 223 LYS A CB  1 
ATOM   1869  C CG  . LYS A 1 223 ? -29.545 16.987  -58.272 1.00 125.80 ? 223 LYS A CG  1 
ATOM   1870  C CD  . LYS A 1 223 ? -30.754 17.698  -57.671 1.00 126.61 ? 223 LYS A CD  1 
ATOM   1871  C CE  . LYS A 1 223 ? -30.882 19.121  -58.197 1.00 125.99 ? 223 LYS A CE  1 
ATOM   1872  N NZ  . LYS A 1 223 ? -31.790 19.957  -57.362 1.00 122.66 ? 223 LYS A NZ  1 
ATOM   1873  N N   . TYR A 1 224 ? -27.821 14.166  -54.696 1.00 121.81 ? 224 TYR A N   1 
ATOM   1874  C CA  . TYR A 1 224 ? -27.567 12.947  -53.921 1.00 118.33 ? 224 TYR A CA  1 
ATOM   1875  C C   . TYR A 1 224 ? -27.464 13.310  -52.441 1.00 116.10 ? 224 TYR A C   1 
ATOM   1876  O O   . TYR A 1 224 ? -26.477 13.909  -52.008 1.00 113.00 ? 224 TYR A O   1 
ATOM   1877  C CB  . TYR A 1 224 ? -26.285 12.243  -54.402 1.00 115.01 ? 224 TYR A CB  1 
ATOM   1878  C CG  . TYR A 1 224 ? -26.263 11.966  -55.894 1.00 115.21 ? 224 TYR A CG  1 
ATOM   1879  C CD1 . TYR A 1 224 ? -25.747 12.903  -56.792 1.00 113.42 ? 224 TYR A CD1 1 
ATOM   1880  C CD2 . TYR A 1 224 ? -26.777 10.776  -56.409 1.00 115.70 ? 224 TYR A CD2 1 
ATOM   1881  C CE1 . TYR A 1 224 ? -25.746 12.661  -58.158 1.00 113.10 ? 224 TYR A CE1 1 
ATOM   1882  C CE2 . TYR A 1 224 ? -26.776 10.524  -57.773 1.00 113.29 ? 224 TYR A CE2 1 
ATOM   1883  C CZ  . TYR A 1 224 ? -26.261 11.467  -58.642 1.00 113.21 ? 224 TYR A CZ  1 
ATOM   1884  O OH  . TYR A 1 224 ? -26.259 11.215  -59.994 1.00 110.08 ? 224 TYR A OH  1 
ATOM   1885  N N   . LYS A 1 225 ? -28.498 12.959  -51.677 1.00 119.49 ? 225 LYS A N   1 
ATOM   1886  C CA  . LYS A 1 225 ? -28.604 13.342  -50.261 1.00 121.12 ? 225 LYS A CA  1 
ATOM   1887  C C   . LYS A 1 225 ? -27.617 12.599  -49.353 1.00 120.69 ? 225 LYS A C   1 
ATOM   1888  O O   . LYS A 1 225 ? -27.851 12.457  -48.147 1.00 118.30 ? 225 LYS A O   1 
ATOM   1889  C CB  . LYS A 1 225 ? -30.040 13.154  -49.752 1.00 120.17 ? 225 LYS A CB  1 
ATOM   1890  C CG  . LYS A 1 225 ? -30.977 14.307  -50.072 1.00 121.02 ? 225 LYS A CG  1 
ATOM   1891  C CD  . LYS A 1 225 ? -32.288 14.176  -49.312 1.00 121.06 ? 225 LYS A CD  1 
ATOM   1892  C CE  . LYS A 1 225 ? -33.233 15.321  -49.637 1.00 119.73 ? 225 LYS A CE  1 
ATOM   1893  N NZ  . LYS A 1 225 ? -34.552 15.148  -48.972 1.00 116.71 ? 225 LYS A NZ  1 
ATOM   1894  N N   . THR A 1 226 ? -26.510 12.142  -49.939 1.00 119.74 ? 226 THR A N   1 
ATOM   1895  C CA  . THR A 1 226 ? -25.466 11.447  -49.198 1.00 117.28 ? 226 THR A CA  1 
ATOM   1896  C C   . THR A 1 226 ? -24.703 12.420  -48.301 1.00 116.80 ? 226 THR A C   1 
ATOM   1897  O O   . THR A 1 226 ? -24.379 13.540  -48.714 1.00 113.42 ? 226 THR A O   1 
ATOM   1898  C CB  . THR A 1 226 ? -24.469 10.749  -50.148 1.00 117.47 ? 226 THR A CB  1 
ATOM   1899  O OG1 . THR A 1 226 ? -25.157 10.270  -51.311 1.00 117.13 ? 226 THR A OG1 1 
ATOM   1900  C CG2 . THR A 1 226 ? -23.768 9.579   -49.443 1.00 116.14 ? 226 THR A CG2 1 
ATOM   1901  N N   . SER A 1 227 ? -24.439 11.989  -47.070 1.00 116.79 ? 227 SER A N   1 
ATOM   1902  C CA  . SER A 1 227 ? -23.566 12.720  -46.155 1.00 115.88 ? 227 SER A CA  1 
ATOM   1903  C C   . SER A 1 227 ? -22.311 11.888  -45.856 1.00 113.40 ? 227 SER A C   1 
ATOM   1904  O O   . SER A 1 227 ? -21.269 12.072  -46.494 1.00 113.31 ? 227 SER A O   1 
ATOM   1905  C CB  . SER A 1 227 ? -24.313 13.085  -44.865 1.00 116.79 ? 227 SER A CB  1 
ATOM   1906  O OG  . SER A 1 227 ? -24.877 11.936  -44.254 1.00 117.73 ? 227 SER A OG  1 
ATOM   1907  N N   . GLY A 1 228 ? -22.422 10.970  -44.897 1.00 107.41 ? 228 GLY A N   1 
ATOM   1908  C CA  . GLY A 1 228 ? -21.375 9.989   -44.634 1.00 99.17  ? 228 GLY A CA  1 
ATOM   1909  C C   . GLY A 1 228 ? -20.156 10.509  -43.886 1.00 92.88  ? 228 GLY A C   1 
ATOM   1910  O O   . GLY A 1 228 ? -19.421 11.373  -44.380 1.00 95.89  ? 228 GLY A O   1 
ATOM   1911  N N   . SER A 1 229 ? -19.960 9.987   -42.680 1.00 81.18  ? 229 SER A N   1 
ATOM   1912  C CA  . SER A 1 229 ? -18.665 10.048  -42.001 1.00 74.28  ? 229 SER A CA  1 
ATOM   1913  C C   . SER A 1 229 ? -18.412 8.714   -41.311 1.00 65.60  ? 229 SER A C   1 
ATOM   1914  O O   . SER A 1 229 ? -19.179 8.310   -40.436 1.00 64.66  ? 229 SER A O   1 
ATOM   1915  C CB  . SER A 1 229 ? -18.624 11.185  -40.982 1.00 73.97  ? 229 SER A CB  1 
ATOM   1916  O OG  . SER A 1 229 ? -17.479 11.065  -40.158 1.00 71.33  ? 229 SER A OG  1 
ATOM   1917  N N   . LEU A 1 230 ? -17.350 8.028   -41.723 1.00 59.50  ? 230 LEU A N   1 
ATOM   1918  C CA  . LEU A 1 230 ? -17.064 6.671   -41.252 1.00 57.35  ? 230 LEU A CA  1 
ATOM   1919  C C   . LEU A 1 230 ? -17.164 6.564   -39.734 1.00 54.84  ? 230 LEU A C   1 
ATOM   1920  O O   . LEU A 1 230 ? -17.770 5.631   -39.208 1.00 54.78  ? 230 LEU A O   1 
ATOM   1921  C CB  . LEU A 1 230 ? -15.670 6.233   -41.702 1.00 55.90  ? 230 LEU A CB  1 
ATOM   1922  C CG  . LEU A 1 230 ? -15.481 4.804   -42.220 1.00 56.25  ? 230 LEU A CG  1 
ATOM   1923  C CD1 . LEU A 1 230 ? -14.016 4.412   -42.087 1.00 53.21  ? 230 LEU A CD1 1 
ATOM   1924  C CD2 . LEU A 1 230 ? -16.386 3.787   -41.529 1.00 55.08  ? 230 LEU A CD2 1 
ATOM   1925  N N   . TYR A 1 231 ? -16.575 7.536   -39.043 1.00 53.09  ? 231 TYR A N   1 
ATOM   1926  C CA  . TYR A 1 231 ? -16.556 7.554   -37.594 1.00 51.60  ? 231 TYR A CA  1 
ATOM   1927  C C   . TYR A 1 231 ? -17.955 7.685   -37.001 1.00 53.38  ? 231 TYR A C   1 
ATOM   1928  O O   . TYR A 1 231 ? -18.317 6.950   -36.079 1.00 54.59  ? 231 TYR A O   1 
ATOM   1929  C CB  . TYR A 1 231 ? -15.645 8.677   -37.080 1.00 49.35  ? 231 TYR A CB  1 
ATOM   1930  C CG  . TYR A 1 231 ? -15.575 8.734   -35.578 1.00 47.14  ? 231 TYR A CG  1 
ATOM   1931  C CD1 . TYR A 1 231 ? -14.644 7.961   -34.876 1.00 45.39  ? 231 TYR A CD1 1 
ATOM   1932  C CD2 . TYR A 1 231 ? -16.452 9.536   -34.851 1.00 46.92  ? 231 TYR A CD2 1 
ATOM   1933  C CE1 . TYR A 1 231 ? -14.578 7.999   -33.497 1.00 43.84  ? 231 TYR A CE1 1 
ATOM   1934  C CE2 . TYR A 1 231 ? -16.399 9.577   -33.466 1.00 47.13  ? 231 TYR A CE2 1 
ATOM   1935  C CZ  . TYR A 1 231 ? -15.455 8.804   -32.795 1.00 46.27  ? 231 TYR A CZ  1 
ATOM   1936  O OH  . TYR A 1 231 ? -15.393 8.831   -31.420 1.00 47.46  ? 231 TYR A OH  1 
ATOM   1937  N N   . THR A 1 232 ? -18.731 8.631   -37.524 1.00 55.38  ? 232 THR A N   1 
ATOM   1938  C CA  . THR A 1 232 ? -20.097 8.857   -37.053 1.00 57.08  ? 232 THR A CA  1 
ATOM   1939  C C   . THR A 1 232 ? -20.969 7.631   -37.304 1.00 56.13  ? 232 THR A C   1 
ATOM   1940  O O   . THR A 1 232 ? -21.698 7.196   -36.418 1.00 57.09  ? 232 THR A O   1 
ATOM   1941  C CB  . THR A 1 232 ? -20.735 10.086  -37.726 1.00 58.90  ? 232 THR A CB  1 
ATOM   1942  O OG1 . THR A 1 232 ? -19.843 11.202  -37.628 1.00 61.70  ? 232 THR A OG1 1 
ATOM   1943  C CG2 . THR A 1 232 ? -22.045 10.442  -37.057 1.00 59.53  ? 232 THR A CG2 1 
ATOM   1944  N N   . CYS A 1 233 ? -20.874 7.068   -38.506 1.00 55.66  ? 233 CYS A N   1 
ATOM   1945  C CA  . CYS A 1 233 ? -21.658 5.885   -38.864 1.00 57.53  ? 233 CYS A CA  1 
ATOM   1946  C C   . CYS A 1 233 ? -21.387 4.729   -37.902 1.00 55.81  ? 233 CYS A C   1 
ATOM   1947  O O   . CYS A 1 233 ? -22.305 4.231   -37.254 1.00 55.96  ? 233 CYS A O   1 
ATOM   1948  C CB  . CYS A 1 233 ? -21.372 5.448   -40.307 1.00 60.86  ? 233 CYS A CB  1 
ATOM   1949  S SG  . CYS A 1 233 ? -21.956 6.571   -41.603 1.00 63.40  ? 233 CYS A SG  1 
ATOM   1950  N N   . TRP A 1 234 ? -20.118 4.333   -37.789 1.00 53.96  ? 234 TRP A N   1 
ATOM   1951  C CA  . TRP A 1 234 ? -19.728 3.211   -36.935 1.00 51.77  ? 234 TRP A CA  1 
ATOM   1952  C C   . TRP A 1 234 ? -20.113 3.433   -35.505 1.00 51.62  ? 234 TRP A C   1 
ATOM   1953  O O   . TRP A 1 234 ? -20.533 2.505   -34.809 1.00 52.54  ? 234 TRP A O   1 
ATOM   1954  C CB  . TRP A 1 234 ? -18.229 2.955   -37.033 1.00 49.36  ? 234 TRP A CB  1 
ATOM   1955  C CG  . TRP A 1 234 ? -17.781 1.740   -36.247 1.00 46.84  ? 234 TRP A CG  1 
ATOM   1956  C CD1 . TRP A 1 234 ? -17.087 1.716   -35.035 1.00 44.16  ? 234 TRP A CD1 1 
ATOM   1957  C CD2 . TRP A 1 234 ? -17.994 0.331   -36.600 1.00 46.63  ? 234 TRP A CD2 1 
ATOM   1958  N NE1 . TRP A 1 234 ? -16.856 0.420   -34.632 1.00 43.86  ? 234 TRP A NE1 1 
ATOM   1959  C CE2 . TRP A 1 234 ? -17.377 -0.459  -35.536 1.00 46.10  ? 234 TRP A CE2 1 
ATOM   1960  C CE3 . TRP A 1 234 ? -18.615 -0.331  -37.663 1.00 47.29  ? 234 TRP A CE3 1 
ATOM   1961  C CZ2 . TRP A 1 234 ? -17.396 -1.850  -35.547 1.00 46.21  ? 234 TRP A CZ2 1 
ATOM   1962  C CZ3 . TRP A 1 234 ? -18.623 -1.732  -37.665 1.00 47.25  ? 234 TRP A CZ3 1 
ATOM   1963  C CH2 . TRP A 1 234 ? -18.022 -2.473  -36.632 1.00 46.16  ? 234 TRP A CH2 1 
ATOM   1964  N N   . SER A 1 235 ? -19.979 4.672   -35.053 1.00 51.37  ? 235 SER A N   1 
ATOM   1965  C CA  . SER A 1 235 ? -20.261 5.005   -33.672 1.00 52.68  ? 235 SER A CA  1 
ATOM   1966  C C   . SER A 1 235 ? -21.753 4.889   -33.381 1.00 55.39  ? 235 SER A C   1 
ATOM   1967  O O   . SER A 1 235 ? -22.162 4.196   -32.436 1.00 54.36  ? 235 SER A O   1 
ATOM   1968  C CB  . SER A 1 235 ? -19.747 6.407   -33.347 1.00 51.66  ? 235 SER A CB  1 
ATOM   1969  O OG  . SER A 1 235 ? -19.949 6.705   -31.988 1.00 51.94  ? 235 SER A OG  1 
ATOM   1970  N N   . GLU A 1 236 ? -22.565 5.557   -34.198 1.00 57.24  ? 236 GLU A N   1 
ATOM   1971  C CA  . GLU A 1 236 ? -24.016 5.502   -34.036 1.00 59.40  ? 236 GLU A CA  1 
ATOM   1972  C C   . GLU A 1 236 ? -24.540 4.076   -34.204 1.00 57.60  ? 236 GLU A C   1 
ATOM   1973  O O   . GLU A 1 236 ? -25.395 3.643   -33.436 1.00 58.08  ? 236 GLU A O   1 
ATOM   1974  C CB  . GLU A 1 236 ? -24.717 6.479   -34.989 1.00 63.97  ? 236 GLU A CB  1 
ATOM   1975  C CG  . GLU A 1 236 ? -24.829 7.899   -34.431 1.00 68.50  ? 236 GLU A CG  1 
ATOM   1976  C CD  . GLU A 1 236 ? -25.075 8.961   -35.500 1.00 72.12  ? 236 GLU A CD  1 
ATOM   1977  O OE1 . GLU A 1 236 ? -24.735 10.139  -35.249 1.00 73.51  ? 236 GLU A OE1 1 
ATOM   1978  O OE2 . GLU A 1 236 ? -25.614 8.630   -36.582 1.00 73.61  ? 236 GLU A OE2 1 
ATOM   1979  N N   . PHE A 1 237 ? -23.983 3.342   -35.172 1.00 56.52  ? 237 PHE A N   1 
ATOM   1980  C CA  . PHE A 1 237 ? -24.360 1.945   -35.414 1.00 56.18  ? 237 PHE A CA  1 
ATOM   1981  C C   . PHE A 1 237 ? -24.071 1.007   -34.239 1.00 56.78  ? 237 PHE A C   1 
ATOM   1982  O O   . PHE A 1 237 ? -24.968 0.302   -33.784 1.00 60.91  ? 237 PHE A O   1 
ATOM   1983  C CB  . PHE A 1 237 ? -23.704 1.398   -36.688 1.00 55.30  ? 237 PHE A CB  1 
ATOM   1984  C CG  . PHE A 1 237 ? -23.981 -0.067  -36.933 1.00 56.15  ? 237 PHE A CG  1 
ATOM   1985  C CD1 . PHE A 1 237 ? -25.221 -0.488  -37.422 1.00 58.40  ? 237 PHE A CD1 1 
ATOM   1986  C CD2 . PHE A 1 237 ? -23.014 -1.027  -36.664 1.00 54.96  ? 237 PHE A CD2 1 
ATOM   1987  C CE1 . PHE A 1 237 ? -25.478 -1.834  -37.641 1.00 58.32  ? 237 PHE A CE1 1 
ATOM   1988  C CE2 . PHE A 1 237 ? -23.267 -2.375  -36.882 1.00 56.03  ? 237 PHE A CE2 1 
ATOM   1989  C CZ  . PHE A 1 237 ? -24.500 -2.779  -37.370 1.00 57.90  ? 237 PHE A CZ  1 
ATOM   1990  N N   . THR A 1 238 ? -22.824 0.984   -33.761 1.00 54.16  ? 238 THR A N   1 
ATOM   1991  C CA  . THR A 1 238 ? -22.441 0.060   -32.689 1.00 52.60  ? 238 THR A CA  1 
ATOM   1992  C C   . THR A 1 238 ? -23.222 0.312   -31.398 1.00 54.26  ? 238 THR A C   1 
ATOM   1993  O O   . THR A 1 238 ? -23.592 -0.632  -30.701 1.00 53.06  ? 238 THR A O   1 
ATOM   1994  C CB  . THR A 1 238 ? -20.919 0.085   -32.376 1.00 50.80  ? 238 THR A CB  1 
ATOM   1995  O OG1 . THR A 1 238 ? -20.515 1.401   -31.986 1.00 49.89  ? 238 THR A OG1 1 
ATOM   1996  C CG2 . THR A 1 238 ? -20.115 -0.354  -33.561 1.00 48.59  ? 238 THR A CG2 1 
ATOM   1997  N N   . GLN A 1 239 ? -23.477 1.583   -31.088 1.00 56.11  ? 239 GLN A N   1 
ATOM   1998  C CA  . GLN A 1 239 ? -24.133 1.943   -29.828 1.00 58.99  ? 239 GLN A CA  1 
ATOM   1999  C C   . GLN A 1 239 ? -25.605 1.525   -29.767 1.00 62.86  ? 239 GLN A C   1 
ATOM   2000  O O   . GLN A 1 239 ? -26.107 1.179   -28.694 1.00 64.24  ? 239 GLN A O   1 
ATOM   2001  C CB  . GLN A 1 239 ? -23.968 3.436   -29.511 1.00 59.83  ? 239 GLN A CB  1 
ATOM   2002  C CG  . GLN A 1 239 ? -22.511 3.905   -29.372 1.00 63.00  ? 239 GLN A CG  1 
ATOM   2003  C CD  . GLN A 1 239 ? -21.651 3.007   -28.480 1.00 63.12  ? 239 GLN A CD  1 
ATOM   2004  O OE1 . GLN A 1 239 ? -21.851 2.948   -27.263 1.00 65.20  ? 239 GLN A OE1 1 
ATOM   2005  N NE2 . GLN A 1 239 ? -20.677 2.316   -29.083 1.00 59.73  ? 239 GLN A NE2 1 
ATOM   2006  N N   . LYS A 1 240 ? -26.289 1.525   -30.910 1.00 65.36  ? 240 LYS A N   1 
ATOM   2007  C CA  . LYS A 1 240 ? -27.672 1.040   -30.946 1.00 68.66  ? 240 LYS A CA  1 
ATOM   2008  C C   . LYS A 1 240 ? -27.795 -0.478  -31.118 1.00 69.72  ? 240 LYS A C   1 
ATOM   2009  O O   . LYS A 1 240 ? -28.796 -1.064  -30.722 1.00 77.51  ? 240 LYS A O   1 
ATOM   2010  C CB  . LYS A 1 240 ? -28.521 1.790   -31.985 1.00 69.34  ? 240 LYS A CB  1 
ATOM   2011  C CG  . LYS A 1 240 ? -28.070 1.672   -33.430 1.00 68.66  ? 240 LYS A CG  1 
ATOM   2012  C CD  . LYS A 1 240 ? -28.786 2.713   -34.277 1.00 71.69  ? 240 LYS A CD  1 
ATOM   2013  C CE  . LYS A 1 240 ? -28.348 2.665   -35.732 1.00 73.89  ? 240 LYS A CE  1 
ATOM   2014  N NZ  . LYS A 1 240 ? -29.035 3.704   -36.553 1.00 73.36  ? 240 LYS A NZ  1 
ATOM   2015  N N   . THR A 1 241 ? -26.771 -1.110  -31.681 1.00 68.72  ? 241 THR A N   1 
ATOM   2016  C CA  . THR A 1 241 ? -26.811 -2.549  -31.939 1.00 68.72  ? 241 THR A CA  1 
ATOM   2017  C C   . THR A 1 241 ? -26.267 -3.352  -30.760 1.00 70.38  ? 241 THR A C   1 
ATOM   2018  O O   . THR A 1 241 ? -25.062 -3.355  -30.500 1.00 71.05  ? 241 THR A O   1 
ATOM   2019  C CB  . THR A 1 241 ? -26.027 -2.916  -33.210 1.00 68.98  ? 241 THR A CB  1 
ATOM   2020  O OG1 . THR A 1 241 ? -26.296 -1.954  -34.240 1.00 69.57  ? 241 THR A OG1 1 
ATOM   2021  C CG2 . THR A 1 241 ? -26.418 -4.303  -33.693 1.00 70.08  ? 241 THR A CG2 1 
ATOM   2022  N N   . GLN A 1 242 ? -27.160 -4.048  -30.064 1.00 72.75  ? 242 GLN A N   1 
ATOM   2023  C CA  . GLN A 1 242 ? -26.795 -4.787  -28.856 1.00 71.95  ? 242 GLN A CA  1 
ATOM   2024  C C   . GLN A 1 242 ? -26.323 -6.212  -29.154 1.00 68.27  ? 242 GLN A C   1 
ATOM   2025  O O   . GLN A 1 242 ? -25.425 -6.725  -28.487 1.00 65.72  ? 242 GLN A O   1 
ATOM   2026  C CB  . GLN A 1 242 ? -27.964 -4.798  -27.871 1.00 77.90  ? 242 GLN A CB  1 
ATOM   2027  C CG  . GLN A 1 242 ? -28.357 -3.409  -27.390 1.00 83.22  ? 242 GLN A CG  1 
ATOM   2028  C CD  . GLN A 1 242 ? -29.489 -3.436  -26.385 1.00 91.75  ? 242 GLN A CD  1 
ATOM   2029  O OE1 . GLN A 1 242 ? -30.612 -3.834  -26.708 1.00 96.12  ? 242 GLN A OE1 1 
ATOM   2030  N NE2 . GLN A 1 242 ? -29.204 -3.001  -25.156 1.00 92.77  ? 242 GLN A NE2 1 
ATOM   2031  N N   . GLY A 1 243 ? -26.926 -6.838  -30.162 1.00 65.60  ? 243 GLY A N   1 
ATOM   2032  C CA  . GLY A 1 243 ? -26.573 -8.202  -30.548 1.00 64.01  ? 243 GLY A CA  1 
ATOM   2033  C C   . GLY A 1 243 ? -25.346 -8.304  -31.446 1.00 63.79  ? 243 GLY A C   1 
ATOM   2034  O O   . GLY A 1 243 ? -24.733 -7.290  -31.811 1.00 62.30  ? 243 GLY A O   1 
ATOM   2035  N N   . GLN A 1 244 ? -25.004 -9.540  -31.807 1.00 61.96  ? 244 GLN A N   1 
ATOM   2036  C CA  . GLN A 1 244 ? -23.849 -9.841  -32.641 1.00 60.24  ? 244 GLN A CA  1 
ATOM   2037  C C   . GLN A 1 244 ? -23.942 -9.129  -33.985 1.00 60.75  ? 244 GLN A C   1 
ATOM   2038  O O   . GLN A 1 244 ? -24.936 -9.271  -34.703 1.00 66.14  ? 244 GLN A O   1 
ATOM   2039  C CB  . GLN A 1 244 ? -23.734 -11.364 -32.842 1.00 59.32  ? 244 GLN A CB  1 
ATOM   2040  C CG  . GLN A 1 244 ? -22.638 -11.814 -33.808 1.00 58.49  ? 244 GLN A CG  1 
ATOM   2041  C CD  . GLN A 1 244 ? -21.230 -11.549 -33.291 1.00 55.81  ? 244 GLN A CD  1 
ATOM   2042  O OE1 . GLN A 1 244 ? -20.916 -11.820 -32.132 1.00 54.09  ? 244 GLN A OE1 1 
ATOM   2043  N NE2 . GLN A 1 244 ? -20.369 -11.037 -34.163 1.00 55.32  ? 244 GLN A NE2 1 
ATOM   2044  N N   . ILE A 1 245 ? -22.909 -8.360  -34.321 1.00 57.29  ? 245 ILE A N   1 
ATOM   2045  C CA  . ILE A 1 245 ? -22.856 -7.669  -35.606 1.00 55.21  ? 245 ILE A CA  1 
ATOM   2046  C C   . ILE A 1 245 ? -22.354 -8.623  -36.689 1.00 56.37  ? 245 ILE A C   1 
ATOM   2047  O O   . ILE A 1 245 ? -21.361 -9.320  -36.494 1.00 58.73  ? 245 ILE A O   1 
ATOM   2048  C CB  . ILE A 1 245 ? -21.949 -6.417  -35.537 1.00 53.29  ? 245 ILE A CB  1 
ATOM   2049  C CG1 . ILE A 1 245 ? -22.609 -5.313  -34.710 1.00 52.91  ? 245 ILE A CG1 1 
ATOM   2050  C CG2 . ILE A 1 245 ? -21.607 -5.903  -36.932 1.00 53.23  ? 245 ILE A CG2 1 
ATOM   2051  C CD1 . ILE A 1 245 ? -21.646 -4.240  -34.230 1.00 51.00  ? 245 ILE A CD1 1 
ATOM   2052  N N   . TYR A 1 246 ? -23.059 -8.668  -37.817 1.00 55.93  ? 246 TYR A N   1 
ATOM   2053  C CA  . TYR A 1 246 ? -22.568 -9.347  -39.016 1.00 55.70  ? 246 TYR A CA  1 
ATOM   2054  C C   . TYR A 1 246 ? -22.248 -8.296  -40.050 1.00 55.15  ? 246 TYR A C   1 
ATOM   2055  O O   . TYR A 1 246 ? -22.885 -7.245  -40.084 1.00 56.04  ? 246 TYR A O   1 
ATOM   2056  C CB  . TYR A 1 246 ? -23.615 -10.334 -39.555 1.00 59.36  ? 246 TYR A CB  1 
ATOM   2057  C CG  . TYR A 1 246 ? -23.811 -11.517 -38.642 1.00 59.90  ? 246 TYR A CG  1 
ATOM   2058  C CD1 . TYR A 1 246 ? -22.946 -12.609 -38.696 1.00 60.90  ? 246 TYR A CD1 1 
ATOM   2059  C CD2 . TYR A 1 246 ? -24.818 -11.521 -37.682 1.00 60.89  ? 246 TYR A CD2 1 
ATOM   2060  C CE1 . TYR A 1 246 ? -23.093 -13.682 -37.836 1.00 62.52  ? 246 TYR A CE1 1 
ATOM   2061  C CE2 . TYR A 1 246 ? -24.971 -12.588 -36.812 1.00 63.16  ? 246 TYR A CE2 1 
ATOM   2062  C CZ  . TYR A 1 246 ? -24.107 -13.669 -36.899 1.00 63.71  ? 246 TYR A CZ  1 
ATOM   2063  O OH  . TYR A 1 246 ? -24.252 -14.737 -36.044 1.00 67.57  ? 246 TYR A OH  1 
ATOM   2064  N N   . GLY A 1 247 ? -21.250 -8.554  -40.884 1.00 54.38  ? 247 GLY A N   1 
ATOM   2065  C CA  . GLY A 1 247 ? -20.825 -7.546  -41.841 1.00 53.79  ? 247 GLY A CA  1 
ATOM   2066  C C   . GLY A 1 247 ? -19.931 -8.072  -42.926 1.00 54.79  ? 247 GLY A C   1 
ATOM   2067  O O   . GLY A 1 247 ? -19.343 -9.146  -42.798 1.00 56.40  ? 247 GLY A O   1 
ATOM   2068  N N   . ILE A 1 248 ? -19.823 -7.303  -43.999 1.00 54.02  ? 248 ILE A N   1 
ATOM   2069  C CA  . ILE A 1 248 ? -19.025 -7.699  -45.135 1.00 55.65  ? 248 ILE A CA  1 
ATOM   2070  C C   . ILE A 1 248 ? -18.298 -6.496  -45.722 1.00 53.90  ? 248 ILE A C   1 
ATOM   2071  O O   . ILE A 1 248 ? -18.786 -5.374  -45.654 1.00 54.84  ? 248 ILE A O   1 
ATOM   2072  C CB  . ILE A 1 248 ? -19.889 -8.422  -46.211 1.00 57.96  ? 248 ILE A CB  1 
ATOM   2073  C CG1 . ILE A 1 248 ? -19.009 -9.032  -47.303 1.00 58.95  ? 248 ILE A CG1 1 
ATOM   2074  C CG2 . ILE A 1 248 ? -20.951 -7.496  -46.801 1.00 57.47  ? 248 ILE A CG2 1 
ATOM   2075  C CD1 . ILE A 1 248 ? -19.726 -10.071 -48.143 1.00 62.78  ? 248 ILE A CD1 1 
ATOM   2076  N N   . LYS A 1 249 ? -17.109 -6.737  -46.250 1.00 53.59  ? 249 LYS A N   1 
ATOM   2077  C CA  . LYS A 1 249 ? -16.420 -5.747  -47.055 1.00 55.58  ? 249 LYS A CA  1 
ATOM   2078  C C   . LYS A 1 249 ? -16.230 -6.318  -48.448 1.00 55.94  ? 249 LYS A C   1 
ATOM   2079  O O   . LYS A 1 249 ? -15.715 -7.420  -48.607 1.00 54.04  ? 249 LYS A O   1 
ATOM   2080  C CB  . LYS A 1 249 ? -15.068 -5.375  -46.438 1.00 53.65  ? 249 LYS A CB  1 
ATOM   2081  C CG  . LYS A 1 249 ? -14.395 -4.147  -47.062 1.00 53.37  ? 249 LYS A CG  1 
ATOM   2082  C CD  . LYS A 1 249 ? -13.333 -4.510  -48.082 1.00 50.80  ? 249 LYS A CD  1 
ATOM   2083  C CE  . LYS A 1 249 ? -12.171 -5.238  -47.426 1.00 52.91  ? 249 LYS A CE  1 
ATOM   2084  N NZ  . LYS A 1 249 ? -11.053 -5.515  -48.373 1.00 53.05  ? 249 LYS A NZ  1 
ATOM   2085  N N   . VAL A 1 250 ? -16.673 -5.569  -49.451 1.00 59.20  ? 250 VAL A N   1 
ATOM   2086  C CA  . VAL A 1 250 ? -16.584 -6.016  -50.835 1.00 64.66  ? 250 VAL A CA  1 
ATOM   2087  C C   . VAL A 1 250 ? -15.682 -5.082  -51.637 1.00 67.44  ? 250 VAL A C   1 
ATOM   2088  O O   . VAL A 1 250 ? -15.874 -3.861  -51.637 1.00 69.94  ? 250 VAL A O   1 
ATOM   2089  C CB  . VAL A 1 250 ? -17.979 -6.134  -51.500 1.00 66.29  ? 250 VAL A CB  1 
ATOM   2090  C CG1 . VAL A 1 250 ? -17.848 -6.585  -52.942 1.00 68.85  ? 250 VAL A CG1 1 
ATOM   2091  C CG2 . VAL A 1 250 ? -18.865 -7.107  -50.733 1.00 67.20  ? 250 VAL A CG2 1 
ATOM   2092  N N   . ASP A 1 251 ? -14.690 -5.673  -52.302 1.00 68.81  ? 251 ASP A N   1 
ATOM   2093  C CA  . ASP A 1 251 ? -13.734 -4.944  -53.114 1.00 71.19  ? 251 ASP A CA  1 
ATOM   2094  C C   . ASP A 1 251 ? -14.281 -4.801  -54.536 1.00 72.11  ? 251 ASP A C   1 
ATOM   2095  O O   . ASP A 1 251 ? -14.525 -5.802  -55.211 1.00 75.24  ? 251 ASP A O   1 
ATOM   2096  C CB  . ASP A 1 251 ? -12.425 -5.729  -53.158 1.00 75.46  ? 251 ASP A CB  1 
ATOM   2097  C CG  . ASP A 1 251 ? -11.239 -4.913  -52.718 1.00 80.95  ? 251 ASP A CG  1 
ATOM   2098  O OD1 . ASP A 1 251 ? -11.270 -4.382  -51.581 1.00 83.73  ? 251 ASP A OD1 1 
ATOM   2099  O OD2 . ASP A 1 251 ? -10.259 -4.828  -53.497 1.00 84.02  ? 251 ASP A OD2 1 
ATOM   2100  N N   . ILE A 1 252 ? -14.466 -3.566  -54.994 1.00 69.13  ? 252 ILE A N   1 
ATOM   2101  C CA  . ILE A 1 252 ? -14.927 -3.332  -56.362 1.00 69.68  ? 252 ILE A CA  1 
ATOM   2102  C C   . ILE A 1 252 ? -13.780 -3.399  -57.367 1.00 69.38  ? 252 ILE A C   1 
ATOM   2103  O O   . ILE A 1 252 ? -12.832 -2.611  -57.290 1.00 67.11  ? 252 ILE A O   1 
ATOM   2104  C CB  . ILE A 1 252 ? -15.674 -1.989  -56.507 1.00 69.71  ? 252 ILE A CB  1 
ATOM   2105  C CG1 . ILE A 1 252 ? -16.763 -1.872  -55.439 1.00 67.42  ? 252 ILE A CG1 1 
ATOM   2106  C CG2 . ILE A 1 252 ? -16.282 -1.862  -57.904 1.00 68.67  ? 252 ILE A CG2 1 
ATOM   2107  C CD1 . ILE A 1 252 ? -17.334 -0.482  -55.304 1.00 67.23  ? 252 ILE A CD1 1 
ATOM   2108  N N   . ARG A 1 253 ? -13.879 -4.336  -58.311 1.00 72.55  ? 253 ARG A N   1 
ATOM   2109  C CA  . ARG A 1 253 ? -12.887 -4.464  -59.389 1.00 73.12  ? 253 ARG A CA  1 
ATOM   2110  C C   . ARG A 1 253 ? -13.034 -3.330  -60.407 1.00 71.62  ? 253 ARG A C   1 
ATOM   2111  O O   . ARG A 1 253 ? -14.144 -3.008  -60.836 1.00 71.17  ? 253 ARG A O   1 
ATOM   2112  C CB  . ARG A 1 253 ? -12.985 -5.836  -60.077 1.00 74.39  ? 253 ARG A CB  1 
ATOM   2113  C CG  . ARG A 1 253 ? -11.871 -6.123  -61.076 1.00 77.12  ? 253 ARG A CG  1 
ATOM   2114  C CD  . ARG A 1 253 ? -11.872 -7.581  -61.512 1.00 82.84  ? 253 ARG A CD  1 
ATOM   2115  N NE  . ARG A 1 253 ? -11.198 -8.438  -60.540 1.00 86.34  ? 253 ARG A NE  1 
ATOM   2116  C CZ  . ARG A 1 253 ? -11.037 -9.756  -60.665 1.00 90.73  ? 253 ARG A CZ  1 
ATOM   2117  N NH1 . ARG A 1 253 ? -11.508 -10.397 -61.729 1.00 90.54  ? 253 ARG A NH1 1 
ATOM   2118  N NH2 . ARG A 1 253 ? -10.400 -10.436 -59.715 1.00 92.52  ? 253 ARG A NH2 1 
ATOM   2119  N N   . ASP A 1 254 ? -11.897 -2.721  -60.746 1.00 69.75  ? 254 ASP A N   1 
ATOM   2120  C CA  . ASP A 1 254 ? -11.793 -1.611  -61.701 1.00 66.35  ? 254 ASP A CA  1 
ATOM   2121  C C   . ASP A 1 254 ? -13.058 -0.768  -61.863 1.00 68.05  ? 254 ASP A C   1 
ATOM   2122  O O   . ASP A 1 254 ? -13.754 -0.877  -62.867 1.00 71.87  ? 254 ASP A O   1 
ATOM   2123  C CB  . ASP A 1 254 ? -11.304 -2.126  -63.054 1.00 66.49  ? 254 ASP A CB  1 
ATOM   2124  C CG  . ASP A 1 254 ? -10.687 -1.025  -63.917 1.00 68.80  ? 254 ASP A CG  1 
ATOM   2125  O OD1 . ASP A 1 254 ? -10.629 0.144   -63.463 1.00 67.48  ? 254 ASP A OD1 1 
ATOM   2126  O OD2 . ASP A 1 254 ? -10.261 -1.333  -65.057 1.00 69.76  ? 254 ASP A OD2 1 
ATOM   2127  N N   . ALA A 1 255 ? -13.349 0.073   -60.870 1.00 67.66  ? 255 ALA A N   1 
ATOM   2128  C CA  . ALA A 1 255 ? -14.510 0.959   -60.929 1.00 66.74  ? 255 ALA A CA  1 
ATOM   2129  C C   . ALA A 1 255 ? -14.392 1.966   -62.074 1.00 68.64  ? 255 ALA A C   1 
ATOM   2130  O O   . ALA A 1 255 ? -15.378 2.238   -62.774 1.00 70.52  ? 255 ALA A O   1 
ATOM   2131  C CB  . ALA A 1 255 ? -14.709 1.674   -59.610 1.00 64.42  ? 255 ALA A CB  1 
ATOM   2132  N N   . TYR A 1 256 ? -13.188 2.499   -62.272 1.00 67.36  ? 256 TYR A N   1 
ATOM   2133  C CA  . TYR A 1 256 ? -12.925 3.424   -63.375 1.00 71.39  ? 256 TYR A CA  1 
ATOM   2134  C C   . TYR A 1 256 ? -13.242 2.794   -64.728 1.00 71.90  ? 256 TYR A C   1 
ATOM   2135  O O   . TYR A 1 256 ? -13.933 3.392   -65.550 1.00 70.52  ? 256 TYR A O   1 
ATOM   2136  C CB  . TYR A 1 256 ? -11.474 3.905   -63.358 1.00 72.70  ? 256 TYR A CB  1 
ATOM   2137  C CG  . TYR A 1 256 ? -11.197 4.977   -62.329 1.00 79.83  ? 256 TYR A CG  1 
ATOM   2138  C CD1 . TYR A 1 256 ? -11.224 4.685   -60.965 1.00 79.07  ? 256 TYR A CD1 1 
ATOM   2139  C CD2 . TYR A 1 256 ? -10.892 6.282   -62.714 1.00 83.82  ? 256 TYR A CD2 1 
ATOM   2140  C CE1 . TYR A 1 256 ? -10.973 5.663   -60.016 1.00 81.88  ? 256 TYR A CE1 1 
ATOM   2141  C CE2 . TYR A 1 256 ? -10.625 7.266   -61.768 1.00 83.29  ? 256 TYR A CE2 1 
ATOM   2142  C CZ  . TYR A 1 256 ? -10.672 6.952   -60.422 1.00 83.36  ? 256 TYR A CZ  1 
ATOM   2143  O OH  . TYR A 1 256 ? -10.416 7.919   -59.470 1.00 85.42  ? 256 TYR A OH  1 
ATOM   2144  N N   . GLY A 1 257 ? -12.743 1.579   -64.939 1.00 72.88  ? 257 GLY A N   1 
ATOM   2145  C CA  . GLY A 1 257 ? -12.845 0.906   -66.230 1.00 74.11  ? 257 GLY A CA  1 
ATOM   2146  C C   . GLY A 1 257 ? -14.180 0.228   -66.471 1.00 77.41  ? 257 GLY A C   1 
ATOM   2147  O O   . GLY A 1 257 ? -14.489 -0.157  -67.601 1.00 77.87  ? 257 GLY A O   1 
ATOM   2148  N N   . ASN A 1 258 ? -14.966 0.068   -65.407 1.00 76.72  ? 258 ASN A N   1 
ATOM   2149  C CA  . ASN A 1 258 ? -16.300 -0.514  -65.520 1.00 76.42  ? 258 ASN A CA  1 
ATOM   2150  C C   . ASN A 1 258 ? -17.415 0.523   -65.604 1.00 76.89  ? 258 ASN A C   1 
ATOM   2151  O O   . ASN A 1 258 ? -18.599 0.174   -65.649 1.00 79.59  ? 258 ASN A O   1 
ATOM   2152  C CB  . ASN A 1 258 ? -16.559 -1.528  -64.401 1.00 74.72  ? 258 ASN A CB  1 
ATOM   2153  C CG  . ASN A 1 258 ? -15.834 -2.845  -64.635 1.00 75.49  ? 258 ASN A CG  1 
ATOM   2154  O OD1 . ASN A 1 258 ? -15.277 -3.430  -63.705 1.00 72.87  ? 258 ASN A OD1 1 
ATOM   2155  N ND2 . ASN A 1 258 ? -15.817 -3.305  -65.891 1.00 73.53  ? 258 ASN A ND2 1 
ATOM   2156  N N   . VAL A 1 259 ? -17.034 1.797   -65.653 1.00 73.43  ? 259 VAL A N   1 
ATOM   2157  C CA  . VAL A 1 259 ? -17.980 2.844   -65.996 1.00 73.96  ? 259 VAL A CA  1 
ATOM   2158  C C   . VAL A 1 259 ? -18.501 2.623   -67.421 1.00 75.16  ? 259 VAL A C   1 
ATOM   2159  O O   . VAL A 1 259 ? -17.727 2.570   -68.387 1.00 74.54  ? 259 VAL A O   1 
ATOM   2160  C CB  . VAL A 1 259 ? -17.366 4.248   -65.851 1.00 72.30  ? 259 VAL A CB  1 
ATOM   2161  C CG1 . VAL A 1 259 ? -18.289 5.303   -66.433 1.00 74.14  ? 259 VAL A CG1 1 
ATOM   2162  C CG2 . VAL A 1 259 ? -17.102 4.549   -64.393 1.00 74.28  ? 259 VAL A CG2 1 
ATOM   2163  N N   . LYS A 1 260 ? -19.810 2.435   -67.531 1.00 76.45  ? 260 LYS A N   1 
ATOM   2164  C CA  . LYS A 1 260 ? -20.473 2.403   -68.823 1.00 78.28  ? 260 LYS A CA  1 
ATOM   2165  C C   . LYS A 1 260 ? -20.628 3.851   -69.273 1.00 77.10  ? 260 LYS A C   1 
ATOM   2166  O O   . LYS A 1 260 ? -21.395 4.625   -68.686 1.00 75.07  ? 260 LYS A O   1 
ATOM   2167  C CB  . LYS A 1 260 ? -21.827 1.696   -68.715 1.00 82.96  ? 260 LYS A CB  1 
ATOM   2168  C CG  . LYS A 1 260 ? -21.774 0.380   -67.940 1.00 86.72  ? 260 LYS A CG  1 
ATOM   2169  C CD  . LYS A 1 260 ? -22.848 0.329   -66.851 1.00 89.61  ? 260 LYS A CD  1 
ATOM   2170  C CE  . LYS A 1 260 ? -22.425 -0.516  -65.651 1.00 87.59  ? 260 LYS A CE  1 
ATOM   2171  N NZ  . LYS A 1 260 ? -22.906 -1.925  -65.726 1.00 88.39  ? 260 LYS A NZ  1 
ATOM   2172  N N   . ILE A 1 261 ? -19.850 4.216   -70.290 1.00 78.48  ? 261 ILE A N   1 
ATOM   2173  C CA  . ILE A 1 261 ? -19.725 5.607   -70.746 1.00 79.70  ? 261 ILE A CA  1 
ATOM   2174  C C   . ILE A 1 261 ? -21.063 6.239   -71.180 1.00 80.26  ? 261 ILE A C   1 
ATOM   2175  O O   . ILE A 1 261 ? -21.396 7.346   -70.738 1.00 80.71  ? 261 ILE A O   1 
ATOM   2176  C CB  . ILE A 1 261 ? -18.655 5.739   -71.865 1.00 80.15  ? 261 ILE A CB  1 
ATOM   2177  C CG1 . ILE A 1 261 ? -17.275 5.315   -71.348 1.00 79.55  ? 261 ILE A CG1 1 
ATOM   2178  C CG2 . ILE A 1 261 ? -18.613 7.153   -72.423 1.00 81.74  ? 261 ILE A CG2 1 
ATOM   2179  C CD1 . ILE A 1 261 ? -16.934 5.858   -69.971 1.00 78.65  ? 261 ILE A CD1 1 
ATOM   2180  N N   . PRO A 1 262 ? -21.835 5.535   -72.032 1.00 79.96  ? 262 PRO A N   1 
ATOM   2181  C CA  . PRO A 1 262 ? -23.147 6.056   -72.426 1.00 82.67  ? 262 PRO A CA  1 
ATOM   2182  C C   . PRO A 1 262 ? -24.039 6.472   -71.235 1.00 82.62  ? 262 PRO A C   1 
ATOM   2183  O O   . PRO A 1 262 ? -24.644 7.550   -71.264 1.00 83.71  ? 262 PRO A O   1 
ATOM   2184  C CB  . PRO A 1 262 ? -23.771 4.886   -73.186 1.00 84.03  ? 262 PRO A CB  1 
ATOM   2185  C CG  . PRO A 1 262 ? -22.611 4.128   -73.750 1.00 82.50  ? 262 PRO A CG  1 
ATOM   2186  C CD  . PRO A 1 262 ? -21.417 4.386   -72.863 1.00 80.15  ? 262 PRO A CD  1 
ATOM   2187  N N   . VAL A 1 263 ? -24.106 5.630   -70.204 1.00 80.28  ? 263 VAL A N   1 
ATOM   2188  C CA  . VAL A 1 263 ? -24.916 5.913   -69.015 1.00 79.34  ? 263 VAL A CA  1 
ATOM   2189  C C   . VAL A 1 263 ? -24.438 7.175   -68.278 1.00 80.45  ? 263 VAL A C   1 
ATOM   2190  O O   . VAL A 1 263 ? -25.255 8.004   -67.858 1.00 79.42  ? 263 VAL A O   1 
ATOM   2191  C CB  . VAL A 1 263 ? -24.952 4.695   -68.055 1.00 78.08  ? 263 VAL A CB  1 
ATOM   2192  C CG1 . VAL A 1 263 ? -25.542 5.069   -66.701 1.00 75.96  ? 263 VAL A CG1 1 
ATOM   2193  C CG2 . VAL A 1 263 ? -25.731 3.547   -68.683 1.00 77.60  ? 263 VAL A CG2 1 
ATOM   2194  N N   . LEU A 1 264 ? -23.117 7.322   -68.139 1.00 81.05  ? 264 LEU A N   1 
ATOM   2195  C CA  . LEU A 1 264 ? -22.528 8.501   -67.488 1.00 81.15  ? 264 LEU A CA  1 
ATOM   2196  C C   . LEU A 1 264 ? -22.847 9.806   -68.234 1.00 83.67  ? 264 LEU A C   1 
ATOM   2197  O O   . LEU A 1 264 ? -23.129 10.829  -67.609 1.00 85.60  ? 264 LEU A O   1 
ATOM   2198  C CB  . LEU A 1 264 ? -21.005 8.333   -67.305 1.00 79.33  ? 264 LEU A CB  1 
ATOM   2199  C CG  . LEU A 1 264 ? -20.219 9.425   -66.557 1.00 76.45  ? 264 LEU A CG  1 
ATOM   2200  C CD1 . LEU A 1 264 ? -20.871 9.809   -65.236 1.00 75.24  ? 264 LEU A CD1 1 
ATOM   2201  C CD2 . LEU A 1 264 ? -18.776 8.996   -66.328 1.00 76.19  ? 264 LEU A CD2 1 
ATOM   2202  N N   . CYS A 1 265 ? -22.815 9.762   -69.564 1.00 84.34  ? 265 CYS A N   1 
ATOM   2203  C CA  . CYS A 1 265 ? -23.173 10.927  -70.378 1.00 87.97  ? 265 CYS A CA  1 
ATOM   2204  C C   . CYS A 1 265 ? -24.588 11.423  -70.098 1.00 89.91  ? 265 CYS A C   1 
ATOM   2205  O O   . CYS A 1 265 ? -24.783 12.597  -69.779 1.00 91.14  ? 265 CYS A O   1 
ATOM   2206  C CB  . CYS A 1 265 ? -23.006 10.624  -71.867 1.00 89.75  ? 265 CYS A CB  1 
ATOM   2207  S SG  . CYS A 1 265 ? -21.306 10.259  -72.339 1.00 87.13  ? 265 CYS A SG  1 
ATOM   2208  N N   . LYS A 1 266 ? -25.566 10.524  -70.204 1.00 91.32  ? 266 LYS A N   1 
ATOM   2209  C CA  . LYS A 1 266 ? -26.969 10.865  -69.939 1.00 93.66  ? 266 LYS A CA  1 
ATOM   2210  C C   . LYS A 1 266 ? -27.135 11.434  -68.534 1.00 94.62  ? 266 LYS A C   1 
ATOM   2211  O O   . LYS A 1 266 ? -27.971 12.311  -68.298 1.00 97.38  ? 266 LYS A O   1 
ATOM   2212  C CB  . LYS A 1 266 ? -27.880 9.643   -70.127 1.00 93.86  ? 266 LYS A CB  1 
ATOM   2213  C CG  . LYS A 1 266 ? -27.744 8.943   -71.475 1.00 94.69  ? 266 LYS A CG  1 
ATOM   2214  C CD  . LYS A 1 266 ? -28.284 9.787   -72.616 1.00 97.10  ? 266 LYS A CD  1 
ATOM   2215  C CE  . LYS A 1 266 ? -27.990 9.131   -73.951 1.00 99.76  ? 266 LYS A CE  1 
ATOM   2216  N NZ  . LYS A 1 266 ? -28.796 9.725   -75.051 1.00 103.12 ? 266 LYS A NZ  1 
ATOM   2217  N N   . LEU A 1 267 ? -26.323 10.929  -67.608 1.00 93.87  ? 267 LEU A N   1 
ATOM   2218  C CA  . LEU A 1 267 ? -26.293 11.430  -66.245 1.00 93.53  ? 267 LEU A CA  1 
ATOM   2219  C C   . LEU A 1 267 ? -25.807 12.878  -66.223 1.00 93.73  ? 267 LEU A C   1 
ATOM   2220  O O   . LEU A 1 267 ? -26.357 13.720  -65.512 1.00 94.18  ? 267 LEU A O   1 
ATOM   2221  C CB  . LEU A 1 267 ? -25.368 10.558  -65.393 1.00 91.35  ? 267 LEU A CB  1 
ATOM   2222  C CG  . LEU A 1 267 ? -25.725 10.271  -63.936 1.00 89.57  ? 267 LEU A CG  1 
ATOM   2223  C CD1 . LEU A 1 267 ? -24.600 9.474   -63.295 1.00 89.35  ? 267 LEU A CD1 1 
ATOM   2224  C CD2 . LEU A 1 267 ? -25.984 11.548  -63.154 1.00 91.01  ? 267 LEU A CD2 1 
ATOM   2225  N N   . ILE A 1 268 ? -24.772 13.159  -67.007 1.00 94.35  ? 268 ILE A N   1 
ATOM   2226  C CA  . ILE A 1 268 ? -24.210 14.500  -67.073 1.00 96.08  ? 268 ILE A CA  1 
ATOM   2227  C C   . ILE A 1 268 ? -25.195 15.465  -67.731 1.00 99.90  ? 268 ILE A C   1 
ATOM   2228  O O   . ILE A 1 268 ? -25.472 16.537  -67.189 1.00 100.25 ? 268 ILE A O   1 
ATOM   2229  C CB  . ILE A 1 268 ? -22.846 14.510  -67.799 1.00 94.65  ? 268 ILE A CB  1 
ATOM   2230  C CG1 . ILE A 1 268 ? -21.778 13.844  -66.922 1.00 90.66  ? 268 ILE A CG1 1 
ATOM   2231  C CG2 . ILE A 1 268 ? -22.428 15.934  -68.148 1.00 95.44  ? 268 ILE A CG2 1 
ATOM   2232  C CD1 . ILE A 1 268 ? -20.712 13.105  -67.704 1.00 90.37  ? 268 ILE A CD1 1 
ATOM   2233  N N   . GLN A 1 269 ? -25.746 15.058  -68.875 1.00 102.61 ? 269 GLN A N   1 
ATOM   2234  C CA  . GLN A 1 269 ? -26.674 15.895  -69.639 1.00 109.96 ? 269 GLN A CA  1 
ATOM   2235  C C   . GLN A 1 269 ? -27.741 16.519  -68.739 1.00 113.61 ? 269 GLN A C   1 
ATOM   2236  O O   . GLN A 1 269 ? -27.898 17.741  -68.704 1.00 115.61 ? 269 GLN A O   1 
ATOM   2237  C CB  . GLN A 1 269 ? -27.355 15.090  -70.760 1.00 110.45 ? 269 GLN A CB  1 
ATOM   2238  C CG  . GLN A 1 269 ? -26.415 14.303  -71.667 1.00 109.18 ? 269 GLN A CG  1 
ATOM   2239  C CD  . GLN A 1 269 ? -25.930 15.092  -72.870 1.00 109.43 ? 269 GLN A CD  1 
ATOM   2240  O OE1 . GLN A 1 269 ? -26.086 16.311  -72.936 1.00 109.95 ? 269 GLN A OE1 1 
ATOM   2241  N NE2 . GLN A 1 269 ? -25.331 14.393  -73.832 1.00 108.59 ? 269 GLN A NE2 1 
ATOM   2242  N N   . SER A 1 270 ? -28.448 15.672  -67.995 1.00 116.86 ? 270 SER A N   1 
ATOM   2243  C CA  . SER A 1 270 ? -29.628 16.094  -67.247 1.00 122.44 ? 270 SER A CA  1 
ATOM   2244  C C   . SER A 1 270 ? -29.607 15.590  -65.801 1.00 121.79 ? 270 SER A C   1 
ATOM   2245  O O   . SER A 1 270 ? -29.180 14.465  -65.548 1.00 119.57 ? 270 SER A O   1 
ATOM   2246  C CB  . SER A 1 270 ? -30.899 15.598  -67.953 1.00 125.96 ? 270 SER A CB  1 
ATOM   2247  O OG  . SER A 1 270 ? -31.351 16.529  -68.925 1.00 126.61 ? 270 SER A OG  1 
ATOM   2248  N N   . ILE A 1 271 ? -30.045 16.420  -64.848 1.00 125.23 ? 271 ILE A N   1 
ATOM   2249  C CA  . ILE A 1 271 ? -30.330 17.847  -65.077 1.00 130.76 ? 271 ILE A CA  1 
ATOM   2250  C C   . ILE A 1 271 ? -29.515 18.697  -64.088 1.00 127.75 ? 271 ILE A C   1 
ATOM   2251  O O   . ILE A 1 271 ? -29.912 18.871  -62.931 1.00 123.25 ? 271 ILE A O   1 
ATOM   2252  C CB  . ILE A 1 271 ? -31.851 18.199  -64.955 1.00 134.12 ? 271 ILE A CB  1 
ATOM   2253  C CG1 . ILE A 1 271 ? -32.703 17.378  -65.937 1.00 135.39 ? 271 ILE A CG1 1 
ATOM   2254  C CG2 . ILE A 1 271 ? -32.083 19.690  -65.198 1.00 135.16 ? 271 ILE A CG2 1 
ATOM   2255  C CD1 . ILE A 1 271 ? -34.199 17.618  -65.835 1.00 136.11 ? 271 ILE A CD1 1 
ATOM   2256  N N   . PRO A 1 272 ? -28.338 19.170  -64.522 1.00 128.86 ? 272 PRO A N   1 
ATOM   2257  C CA  . PRO A 1 272 ? -27.670 20.227  -63.788 1.00 132.71 ? 272 PRO A CA  1 
ATOM   2258  C C   . PRO A 1 272 ? -27.511 21.509  -64.628 1.00 137.23 ? 272 PRO A C   1 
ATOM   2259  O O   . PRO A 1 272 ? -26.428 21.775  -65.157 1.00 139.24 ? 272 PRO A O   1 
ATOM   2260  C CB  . PRO A 1 272 ? -26.296 19.604  -63.464 1.00 129.72 ? 272 PRO A CB  1 
ATOM   2261  C CG  . PRO A 1 272 ? -26.171 18.384  -64.351 1.00 128.49 ? 272 PRO A CG  1 
ATOM   2262  C CD  . PRO A 1 272 ? -27.365 18.362  -65.265 1.00 128.69 ? 272 PRO A CD  1 
ATOM   2263  N N   . THR A 1 273 ? -28.588 22.287  -64.749 1.00 140.50 ? 273 THR A N   1 
ATOM   2264  C CA  . THR A 1 273 ? -28.559 23.547  -65.510 1.00 142.29 ? 273 THR A CA  1 
ATOM   2265  C C   . THR A 1 273 ? -28.115 24.723  -64.633 1.00 142.57 ? 273 THR A C   1 
ATOM   2266  O O   . THR A 1 273 ? -27.292 25.542  -65.047 1.00 140.80 ? 273 THR A O   1 
ATOM   2267  C CB  . THR A 1 273 ? -29.926 23.870  -66.164 1.00 143.36 ? 273 THR A CB  1 
ATOM   2268  O OG1 . THR A 1 273 ? -30.931 24.009  -65.152 1.00 143.39 ? 273 THR A OG1 1 
ATOM   2269  C CG2 . THR A 1 273 ? -30.340 22.770  -67.140 1.00 142.94 ? 273 THR A CG2 1 
ATOM   2270  N N   . HIS A 1 274 ? -28.665 24.786  -63.421 1.00 145.90 ? 274 HIS A N   1 
ATOM   2271  C CA  . HIS A 1 274 ? -28.296 25.791  -62.417 1.00 148.64 ? 274 HIS A CA  1 
ATOM   2272  C C   . HIS A 1 274 ? -26.853 25.648  -62.005 1.00 144.87 ? 274 HIS A C   1 
ATOM   2273  O O   . HIS A 1 274 ? -26.260 26.568  -61.438 1.00 144.02 ? 274 HIS A O   1 
ATOM   2274  C CB  . HIS A 1 274 ? -29.221 25.659  -61.200 1.00 154.26 ? 274 HIS A CB  1 
ATOM   2275  C CG  . HIS A 1 274 ? -28.949 26.662  -60.094 1.00 158.92 ? 274 HIS A CG  1 
ATOM   2276  N ND1 . HIS A 1 274 ? -29.382 27.937  -60.145 1.00 162.07 ? 274 HIS A ND1 1 
ATOM   2277  C CD2 . HIS A 1 274 ? -28.288 26.521  -58.870 1.00 157.75 ? 274 HIS A CD2 1 
ATOM   2278  C CE1 . HIS A 1 274 ? -29.005 28.584  -59.023 1.00 161.22 ? 274 HIS A CE1 1 
ATOM   2279  N NE2 . HIS A 1 274 ? -28.337 27.717  -58.245 1.00 157.58 ? 274 HIS A NE2 1 
ATOM   2280  N N   . LEU A 1 275 ? -26.267 24.496  -62.319 1.00 141.36 ? 275 LEU A N   1 
ATOM   2281  C CA  . LEU A 1 275 ? -24.947 24.140  -61.819 1.00 139.43 ? 275 LEU A CA  1 
ATOM   2282  C C   . LEU A 1 275 ? -23.887 24.140  -62.920 1.00 142.67 ? 275 LEU A C   1 
ATOM   2283  O O   . LEU A 1 275 ? -22.804 24.701  -62.743 1.00 144.37 ? 275 LEU A O   1 
ATOM   2284  C CB  . LEU A 1 275 ? -25.003 22.779  -61.124 1.00 135.47 ? 275 LEU A CB  1 
ATOM   2285  C CG  . LEU A 1 275 ? -26.175 22.597  -60.152 1.00 134.65 ? 275 LEU A CG  1 
ATOM   2286  C CD1 . LEU A 1 275 ? -26.610 21.142  -60.080 1.00 134.62 ? 275 LEU A CD1 1 
ATOM   2287  C CD2 . LEU A 1 275 ? -25.842 23.138  -58.768 1.00 132.97 ? 275 LEU A CD2 1 
ATOM   2288  N N   . LEU A 1 276 ? -24.204 23.514  -64.052 1.00 144.61 ? 276 LEU A N   1 
ATOM   2289  C CA  . LEU A 1 276 ? -23.279 23.445  -65.187 1.00 146.87 ? 276 LEU A CA  1 
ATOM   2290  C C   . LEU A 1 276 ? -23.919 23.972  -66.463 1.00 150.28 ? 276 LEU A C   1 
ATOM   2291  O O   . LEU A 1 276 ? -23.374 24.857  -67.128 1.00 148.99 ? 276 LEU A O   1 
ATOM   2292  C CB  . LEU A 1 276 ? -22.813 22.003  -65.419 1.00 144.61 ? 276 LEU A CB  1 
ATOM   2293  C CG  . LEU A 1 276 ? -21.816 21.364  -64.454 1.00 141.41 ? 276 LEU A CG  1 
ATOM   2294  C CD1 . LEU A 1 276 ? -21.827 19.855  -64.634 1.00 141.48 ? 276 LEU A CD1 1 
ATOM   2295  C CD2 . LEU A 1 276 ? -20.414 21.919  -64.660 1.00 139.21 ? 276 LEU A CD2 1 
ATOM   2296  N N   . ASP A 1 277 ? -25.085 23.419  -66.789 1.00 153.98 ? 277 ASP A N   1 
ATOM   2297  C CA  . ASP A 1 277 ? -25.746 23.638  -68.073 1.00 159.07 ? 277 ASP A CA  1 
ATOM   2298  C C   . ASP A 1 277 ? -24.928 23.061  -69.239 1.00 158.69 ? 277 ASP A C   1 
ATOM   2299  O O   . ASP A 1 277 ? -24.339 21.986  -69.113 1.00 154.28 ? 277 ASP A O   1 
ATOM   2300  C CB  . ASP A 1 277 ? -26.090 25.122  -68.289 1.00 163.95 ? 277 ASP A CB  1 
ATOM   2301  C CG  . ASP A 1 277 ? -27.360 25.318  -69.111 1.00 168.18 ? 277 ASP A CG  1 
ATOM   2302  O OD1 . ASP A 1 277 ? -28.286 24.485  -68.999 1.00 168.28 ? 277 ASP A OD1 1 
ATOM   2303  O OD2 . ASP A 1 277 ? -27.434 26.311  -69.865 1.00 169.36 ? 277 ASP A OD2 1 
ATOM   2304  N N   . SER A 1 278 ? -24.867 23.801  -70.347 1.00 160.68 ? 278 SER A N   1 
ATOM   2305  C CA  . SER A 1 278 ? -24.546 23.225  -71.656 1.00 160.11 ? 278 SER A CA  1 
ATOM   2306  C C   . SER A 1 278 ? -23.061 23.240  -72.038 1.00 157.75 ? 278 SER A C   1 
ATOM   2307  O O   . SER A 1 278 ? -22.482 22.190  -72.322 1.00 154.14 ? 278 SER A O   1 
ATOM   2308  C CB  . SER A 1 278 ? -25.389 23.891  -72.749 1.00 162.92 ? 278 SER A CB  1 
ATOM   2309  O OG  . SER A 1 278 ? -25.484 23.067  -73.896 1.00 165.44 ? 278 SER A OG  1 
ATOM   2310  N N   . GLU A 1 279 ? -22.460 24.430  -72.054 1.00 160.13 ? 279 GLU A N   1 
ATOM   2311  C CA  . GLU A 1 279 ? -21.075 24.604  -72.519 1.00 158.96 ? 279 GLU A CA  1 
ATOM   2312  C C   . GLU A 1 279 ? -20.136 23.647  -71.799 1.00 152.98 ? 279 GLU A C   1 
ATOM   2313  O O   . GLU A 1 279 ? -19.200 23.111  -72.396 1.00 151.02 ? 279 GLU A O   1 
ATOM   2314  C CB  . GLU A 1 279 ? -20.595 26.050  -72.321 1.00 162.89 ? 279 GLU A CB  1 
ATOM   2315  C CG  . GLU A 1 279 ? -21.703 27.073  -72.124 1.00 169.46 ? 279 GLU A CG  1 
ATOM   2316  C CD  . GLU A 1 279 ? -22.151 27.167  -70.675 1.00 171.67 ? 279 GLU A CD  1 
ATOM   2317  O OE1 . GLU A 1 279 ? -21.436 27.801  -69.873 1.00 171.15 ? 279 GLU A OE1 1 
ATOM   2318  O OE2 . GLU A 1 279 ? -23.215 26.604  -70.338 1.00 173.88 ? 279 GLU A OE2 1 
ATOM   2319  N N   . LYS A 1 280 ? -20.406 23.430  -70.515 1.00 147.94 ? 280 LYS A N   1 
ATOM   2320  C CA  . LYS A 1 280 ? -19.632 22.501  -69.709 1.00 141.86 ? 280 LYS A CA  1 
ATOM   2321  C C   . LYS A 1 280 ? -19.986 21.064  -70.080 1.00 139.79 ? 280 LYS A C   1 
ATOM   2322  O O   . LYS A 1 280 ? -19.099 20.266  -70.393 1.00 138.89 ? 280 LYS A O   1 
ATOM   2323  C CB  . LYS A 1 280 ? -19.882 22.735  -68.214 1.00 140.16 ? 280 LYS A CB  1 
ATOM   2324  C CG  . LYS A 1 280 ? -20.599 24.034  -67.875 1.00 140.47 ? 280 LYS A CG  1 
ATOM   2325  C CD  . LYS A 1 280 ? -19.660 25.228  -67.815 1.00 137.92 ? 280 LYS A CD  1 
ATOM   2326  C CE  . LYS A 1 280 ? -20.401 26.461  -67.327 1.00 137.24 ? 280 LYS A CE  1 
ATOM   2327  N NZ  . LYS A 1 280 ? -19.580 27.696  -67.438 1.00 134.97 ? 280 LYS A NZ  1 
ATOM   2328  N N   . LYS A 1 281 ? -21.285 20.748  -70.066 1.00 137.65 ? 281 LYS A N   1 
ATOM   2329  C CA  . LYS A 1 281 ? -21.754 19.380  -70.312 1.00 134.65 ? 281 LYS A CA  1 
ATOM   2330  C C   . LYS A 1 281 ? -21.255 18.835  -71.650 1.00 131.88 ? 281 LYS A C   1 
ATOM   2331  O O   . LYS A 1 281 ? -20.830 17.685  -71.733 1.00 127.81 ? 281 LYS A O   1 
ATOM   2332  C CB  . LYS A 1 281 ? -23.289 19.278  -70.208 1.00 136.50 ? 281 LYS A CB  1 
ATOM   2333  C CG  . LYS A 1 281 ? -24.044 19.459  -71.522 1.00 142.49 ? 281 LYS A CG  1 
ATOM   2334  C CD  . LYS A 1 281 ? -25.492 18.994  -71.424 1.00 143.59 ? 281 LYS A CD  1 
ATOM   2335  C CE  . LYS A 1 281 ? -26.455 20.160  -71.220 1.00 146.59 ? 281 LYS A CE  1 
ATOM   2336  N NZ  . LYS A 1 281 ? -27.871 19.770  -71.482 1.00 145.03 ? 281 LYS A NZ  1 
ATOM   2337  N N   . ASN A 1 282 ? -21.285 19.679  -72.680 1.00 131.58 ? 282 ASN A N   1 
ATOM   2338  C CA  . ASN A 1 282 ? -20.815 19.302  -74.007 1.00 128.95 ? 282 ASN A CA  1 
ATOM   2339  C C   . ASN A 1 282 ? -19.349 18.902  -73.996 1.00 125.82 ? 282 ASN A C   1 
ATOM   2340  O O   . ASN A 1 282 ? -18.962 17.929  -74.646 1.00 125.01 ? 282 ASN A O   1 
ATOM   2341  C CB  . ASN A 1 282 ? -21.039 20.443  -75.002 1.00 132.31 ? 282 ASN A CB  1 
ATOM   2342  C CG  . ASN A 1 282 ? -22.501 20.824  -75.137 1.00 134.23 ? 282 ASN A CG  1 
ATOM   2343  O OD1 . ASN A 1 282 ? -23.378 19.963  -75.203 1.00 133.52 ? 282 ASN A OD1 1 
ATOM   2344  N ND2 . ASN A 1 282 ? -22.769 22.123  -75.181 1.00 135.04 ? 282 ASN A ND2 1 
ATOM   2345  N N   . PHE A 1 283 ? -18.540 19.650  -73.244 1.00 123.30 ? 283 PHE A N   1 
ATOM   2346  C CA  . PHE A 1 283 ? -17.111 19.365  -73.128 1.00 119.63 ? 283 PHE A CA  1 
ATOM   2347  C C   . PHE A 1 283 ? -16.842 18.074  -72.366 1.00 116.77 ? 283 PHE A C   1 
ATOM   2348  O O   . PHE A 1 283 ? -15.913 17.336  -72.698 1.00 116.50 ? 283 PHE A O   1 
ATOM   2349  C CB  . PHE A 1 283 ? -16.359 20.526  -72.468 1.00 118.58 ? 283 PHE A CB  1 
ATOM   2350  C CG  . PHE A 1 283 ? -14.889 20.258  -72.279 1.00 117.56 ? 283 PHE A CG  1 
ATOM   2351  C CD1 . PHE A 1 283 ? -14.005 20.356  -73.352 1.00 116.93 ? 283 PHE A CD1 1 
ATOM   2352  C CD2 . PHE A 1 283 ? -14.391 19.879  -71.035 1.00 115.60 ? 283 PHE A CD2 1 
ATOM   2353  C CE1 . PHE A 1 283 ? -12.653 20.095  -73.184 1.00 116.12 ? 283 PHE A CE1 1 
ATOM   2354  C CE2 . PHE A 1 283 ? -13.040 19.616  -70.862 1.00 113.30 ? 283 PHE A CE2 1 
ATOM   2355  C CZ  . PHE A 1 283 ? -12.170 19.726  -71.937 1.00 113.75 ? 283 PHE A CZ  1 
ATOM   2356  N N   . ILE A 1 284 ? -17.642 17.815  -71.336 1.00 112.18 ? 284 ILE A N   1 
ATOM   2357  C CA  . ILE A 1 284 ? -17.514 16.581  -70.572 1.00 108.60 ? 284 ILE A CA  1 
ATOM   2358  C C   . ILE A 1 284 ? -18.029 15.387  -71.382 1.00 109.85 ? 284 ILE A C   1 
ATOM   2359  O O   . ILE A 1 284 ? -17.379 14.342  -71.426 1.00 108.46 ? 284 ILE A O   1 
ATOM   2360  C CB  . ILE A 1 284 ? -18.221 16.669  -69.201 1.00 108.27 ? 284 ILE A CB  1 
ATOM   2361  C CG1 . ILE A 1 284 ? -17.801 17.947  -68.463 1.00 107.04 ? 284 ILE A CG1 1 
ATOM   2362  C CG2 . ILE A 1 284 ? -17.892 15.448  -68.350 1.00 106.08 ? 284 ILE A CG2 1 
ATOM   2363  C CD1 . ILE A 1 284 ? -18.634 18.263  -67.237 1.00 105.91 ? 284 ILE A CD1 1 
ATOM   2364  N N   . VAL A 1 285 ? -19.173 15.562  -72.049 1.00 110.69 ? 285 VAL A N   1 
ATOM   2365  C CA  . VAL A 1 285 ? -19.784 14.495  -72.856 1.00 110.70 ? 285 VAL A CA  1 
ATOM   2366  C C   . VAL A 1 285 ? -18.787 13.871  -73.835 1.00 109.73 ? 285 VAL A C   1 
ATOM   2367  O O   . VAL A 1 285 ? -18.557 12.660  -73.814 1.00 108.96 ? 285 VAL A O   1 
ATOM   2368  C CB  . VAL A 1 285 ? -21.048 14.985  -73.608 1.00 113.81 ? 285 VAL A CB  1 
ATOM   2369  C CG1 . VAL A 1 285 ? -21.463 13.996  -74.689 1.00 114.90 ? 285 VAL A CG1 1 
ATOM   2370  C CG2 . VAL A 1 285 ? -22.193 15.200  -72.633 1.00 114.42 ? 285 VAL A CG2 1 
ATOM   2371  N N   . ASP A 1 286 ? -18.177 14.701  -74.673 1.00 110.88 ? 286 ASP A N   1 
ATOM   2372  C CA  . ASP A 1 286 ? -17.229 14.197  -75.657 1.00 111.09 ? 286 ASP A CA  1 
ATOM   2373  C C   . ASP A 1 286 ? -15.881 13.846  -75.027 1.00 107.23 ? 286 ASP A C   1 
ATOM   2374  O O   . ASP A 1 286 ? -15.056 13.174  -75.643 1.00 107.07 ? 286 ASP A O   1 
ATOM   2375  C CB  . ASP A 1 286 ? -17.066 15.177  -76.834 1.00 115.35 ? 286 ASP A CB  1 
ATOM   2376  C CG  . ASP A 1 286 ? -16.382 16.479  -76.435 1.00 116.23 ? 286 ASP A CG  1 
ATOM   2377  O OD1 . ASP A 1 286 ? -16.238 16.743  -75.220 1.00 115.87 ? 286 ASP A OD1 1 
ATOM   2378  O OD2 . ASP A 1 286 ? -15.991 17.241  -77.348 1.00 113.42 ? 286 ASP A OD2 1 
ATOM   2379  N N   . HIS A 1 287 ? -15.666 14.290  -73.793 1.00 108.38 ? 287 HIS A N   1 
ATOM   2380  C CA  . HIS A 1 287 ? -14.422 13.983  -73.095 1.00 106.55 ? 287 HIS A CA  1 
ATOM   2381  C C   . HIS A 1 287 ? -14.363 12.549  -72.641 1.00 103.73 ? 287 HIS A C   1 
ATOM   2382  O O   . HIS A 1 287 ? -13.309 11.919  -72.725 1.00 101.91 ? 287 HIS A O   1 
ATOM   2383  C CB  . HIS A 1 287 ? -14.196 14.931  -71.927 1.00 106.65 ? 287 HIS A CB  1 
ATOM   2384  C CG  . HIS A 1 287 ? -12.744 15.260  -71.690 1.00 107.59 ? 287 HIS A CG  1 
ATOM   2385  N ND1 . HIS A 1 287 ? -12.090 14.892  -70.573 1.00 106.70 ? 287 HIS A ND1 1 
ATOM   2386  C CD2 . HIS A 1 287 ? -11.816 15.931  -72.487 1.00 108.30 ? 287 HIS A CD2 1 
ATOM   2387  C CE1 . HIS A 1 287 ? -10.815 15.315  -70.642 1.00 106.45 ? 287 HIS A CE1 1 
ATOM   2388  N NE2 . HIS A 1 287 ? -10.649 15.948  -71.814 1.00 109.03 ? 287 HIS A NE2 1 
ATOM   2389  N N   . ILE A 1 288 ? -15.500 12.022  -72.178 1.00 102.22 ? 288 ILE A N   1 
ATOM   2390  C CA  . ILE A 1 288 ? -15.599 10.628  -71.703 1.00 101.18 ? 288 ILE A CA  1 
ATOM   2391  C C   . ILE A 1 288 ? -15.431 9.638   -72.863 1.00 99.68  ? 288 ILE A C   1 
ATOM   2392  O O   . ILE A 1 288 ? -14.797 8.592   -72.730 1.00 98.98  ? 288 ILE A O   1 
ATOM   2393  C CB  . ILE A 1 288 ? -16.955 10.352  -70.993 1.00 103.20 ? 288 ILE A CB  1 
ATOM   2394  C CG1 . ILE A 1 288 ? -17.441 11.572  -70.198 1.00 103.88 ? 288 ILE A CG1 1 
ATOM   2395  C CG2 . ILE A 1 288 ? -16.853 9.134   -70.088 1.00 101.68 ? 288 ILE A CG2 1 
ATOM   2396  C CD1 . ILE A 1 288 ? -16.526 11.990  -69.063 1.00 103.82 ? 288 ILE A CD1 1 
ATOM   2397  N N   . SER A 1 289 ? -16.035 9.970   -73.990 1.00 99.15  ? 289 SER A N   1 
ATOM   2398  C CA  . SER A 1 289 ? -15.773 9.288   -75.236 1.00 101.06 ? 289 SER A CA  1 
ATOM   2399  C C   . SER A 1 289 ? -15.816 10.380  -76.281 1.00 104.38 ? 289 SER A C   1 
ATOM   2400  O O   . SER A 1 289 ? -16.861 11.005  -76.476 1.00 110.00 ? 289 SER A O   1 
ATOM   2401  C CB  . SER A 1 289 ? -16.850 8.243   -75.508 1.00 100.46 ? 289 SER A CB  1 
ATOM   2402  O OG  . SER A 1 289 ? -18.142 8.808   -75.370 1.00 98.06  ? 289 SER A OG  1 
ATOM   2403  N N   . ASN A 1 290 ? -14.699 10.617  -76.966 1.00 101.62 ? 290 ASN A N   1 
ATOM   2404  C CA  . ASN A 1 290 ? -13.612 9.655   -77.092 1.00 99.90  ? 290 ASN A CA  1 
ATOM   2405  C C   . ASN A 1 290 ? -12.330 10.094  -76.392 1.00 98.25  ? 290 ASN A C   1 
ATOM   2406  O O   . ASN A 1 290 ? -11.926 11.257  -76.472 1.00 98.62  ? 290 ASN A O   1 
ATOM   2407  C CB  . ASN A 1 290 ? -13.323 9.431   -78.574 1.00 101.76 ? 290 ASN A CB  1 
ATOM   2408  C CG  . ASN A 1 290 ? -14.296 10.180  -79.475 1.00 103.39 ? 290 ASN A CG  1 
ATOM   2409  O OD1 . ASN A 1 290 ? -14.475 11.393  -79.344 1.00 103.09 ? 290 ASN A OD1 1 
ATOM   2410  N ND2 . ASN A 1 290 ? -14.933 9.459   -80.388 1.00 102.99 ? 290 ASN A ND2 1 
ATOM   2411  N N   . GLN A 1 291 ? -11.682 9.146   -75.728 1.00 94.81  ? 291 GLN A N   1 
ATOM   2412  C CA  . GLN A 1 291 ? -10.432 9.407   -75.029 1.00 92.20  ? 291 GLN A CA  1 
ATOM   2413  C C   . GLN A 1 291 ? -9.265  8.859   -75.841 1.00 92.56  ? 291 GLN A C   1 
ATOM   2414  O O   . GLN A 1 291 ? -9.122  7.647   -75.993 1.00 92.68  ? 291 GLN A O   1 
ATOM   2415  C CB  . GLN A 1 291 ? -10.458 8.760   -73.645 1.00 88.85  ? 291 GLN A CB  1 
ATOM   2416  C CG  . GLN A 1 291 ? -11.589 9.245   -72.755 1.00 87.84  ? 291 GLN A CG  1 
ATOM   2417  C CD  . GLN A 1 291 ? -11.772 8.395   -71.508 1.00 85.56  ? 291 GLN A CD  1 
ATOM   2418  O OE1 . GLN A 1 291 ? -11.714 7.166   -71.563 1.00 84.47  ? 291 GLN A OE1 1 
ATOM   2419  N NE2 . GLN A 1 291 ? -12.013 9.051   -70.377 1.00 82.99  ? 291 GLN A NE2 1 
ATOM   2420  N N   . PHE A 1 292 ? -8.436  9.755   -76.365 1.00 93.30  ? 292 PHE A N   1 
ATOM   2421  C CA  . PHE A 1 292 ? -7.354  9.358   -77.263 1.00 94.67  ? 292 PHE A CA  1 
ATOM   2422  C C   . PHE A 1 292 ? -5.981  9.555   -76.633 1.00 93.79  ? 292 PHE A C   1 
ATOM   2423  O O   . PHE A 1 292 ? -5.707  10.594  -76.024 1.00 93.81  ? 292 PHE A O   1 
ATOM   2424  C CB  . PHE A 1 292 ? -7.453  10.102  -78.599 1.00 100.03 ? 292 PHE A CB  1 
ATOM   2425  C CG  . PHE A 1 292 ? -8.071  11.471  -78.493 1.00 104.23 ? 292 PHE A CG  1 
ATOM   2426  C CD1 . PHE A 1 292 ? -7.382  12.521  -77.884 1.00 105.76 ? 292 PHE A CD1 1 
ATOM   2427  C CD2 . PHE A 1 292 ? -9.340  11.713  -79.006 1.00 106.24 ? 292 PHE A CD2 1 
ATOM   2428  C CE1 . PHE A 1 292 ? -7.950  13.781  -77.787 1.00 107.63 ? 292 PHE A CE1 1 
ATOM   2429  C CE2 . PHE A 1 292 ? -9.912  12.974  -78.917 1.00 108.83 ? 292 PHE A CE2 1 
ATOM   2430  C CZ  . PHE A 1 292 ? -9.216  14.009  -78.307 1.00 109.52 ? 292 PHE A CZ  1 
ATOM   2431  N N   . VAL A 1 293 ? -5.121  8.550   -76.780 1.00 91.07  ? 293 VAL A N   1 
ATOM   2432  C CA  . VAL A 1 293 ? -3.828  8.542   -76.098 1.00 88.53  ? 293 VAL A CA  1 
ATOM   2433  C C   . VAL A 1 293 ? -2.644  8.210   -77.008 1.00 89.76  ? 293 VAL A C   1 
ATOM   2434  O O   . VAL A 1 293 ? -2.736  7.361   -77.901 1.00 89.55  ? 293 VAL A O   1 
ATOM   2435  C CB  . VAL A 1 293 ? -3.823  7.584   -74.886 1.00 86.50  ? 293 VAL A CB  1 
ATOM   2436  C CG1 . VAL A 1 293 ? -4.751  8.098   -73.801 1.00 85.16  ? 293 VAL A CG1 1 
ATOM   2437  C CG2 . VAL A 1 293 ? -4.209  6.172   -75.304 1.00 88.80  ? 293 VAL A CG2 1 
ATOM   2438  N N   . ALA A 1 294 ? -1.529  8.892   -76.764 1.00 90.14  ? 294 ALA A N   1 
ATOM   2439  C CA  . ALA A 1 294 ? -0.277  8.599   -77.441 1.00 91.23  ? 294 ALA A CA  1 
ATOM   2440  C C   . ALA A 1 294 ? 0.335   7.317   -76.892 1.00 91.04  ? 294 ALA A C   1 
ATOM   2441  O O   . ALA A 1 294 ? 0.204   7.008   -75.706 1.00 91.92  ? 294 ALA A O   1 
ATOM   2442  C CB  . ALA A 1 294 ? 0.693   9.760   -77.280 1.00 90.19  ? 294 ALA A CB  1 
ATOM   2443  N N   . PHE A 1 295 ? 0.988   6.564   -77.767 1.00 93.36  ? 295 PHE A N   1 
ATOM   2444  C CA  . PHE A 1 295 ? 1.741   5.393   -77.352 1.00 93.89  ? 295 PHE A CA  1 
ATOM   2445  C C   . PHE A 1 295 ? 3.041   5.280   -78.168 1.00 99.50  ? 295 PHE A C   1 
ATOM   2446  O O   . PHE A 1 295 ? 3.745   6.280   -78.367 1.00 103.05 ? 295 PHE A O   1 
ATOM   2447  C CB  . PHE A 1 295 ? 0.874   4.126   -77.448 1.00 89.65  ? 295 PHE A CB  1 
ATOM   2448  C CG  . PHE A 1 295 ? 1.341   3.003   -76.561 1.00 85.64  ? 295 PHE A CG  1 
ATOM   2449  C CD1 . PHE A 1 295 ? 1.571   3.216   -75.208 1.00 83.27  ? 295 PHE A CD1 1 
ATOM   2450  C CD2 . PHE A 1 295 ? 1.553   1.731   -77.079 1.00 83.81  ? 295 PHE A CD2 1 
ATOM   2451  C CE1 . PHE A 1 295 ? 2.015   2.184   -74.393 1.00 82.13  ? 295 PHE A CE1 1 
ATOM   2452  C CE2 . PHE A 1 295 ? 1.992   0.697   -76.269 1.00 79.53  ? 295 PHE A CE2 1 
ATOM   2453  C CZ  . PHE A 1 295 ? 2.223   0.922   -74.926 1.00 80.68  ? 295 PHE A CZ  1 
ATOM   2454  N N   . ARG A 1 296 ? 3.359   4.074   -78.633 1.00 98.56  ? 296 ARG A N   1 
ATOM   2455  C CA  . ARG A 1 296 ? 4.584   3.835   -79.394 1.00 93.97  ? 296 ARG A CA  1 
ATOM   2456  C C   . ARG A 1 296 ? 4.477   4.415   -80.804 1.00 97.26  ? 296 ARG A C   1 
ATOM   2457  O O   . ARG A 1 296 ? 4.143   3.707   -81.758 1.00 96.89  ? 296 ARG A O   1 
ATOM   2458  C CB  . ARG A 1 296 ? 4.896   2.338   -79.436 1.00 87.13  ? 296 ARG A CB  1 
ATOM   2459  C CG  . ARG A 1 296 ? 5.104   1.735   -78.058 1.00 79.42  ? 296 ARG A CG  1 
ATOM   2460  C CD  . ARG A 1 296 ? 5.106   0.221   -78.105 1.00 75.02  ? 296 ARG A CD  1 
ATOM   2461  N NE  . ARG A 1 296 ? 5.512   -0.355  -76.826 1.00 69.86  ? 296 ARG A NE  1 
ATOM   2462  C CZ  . ARG A 1 296 ? 5.590   -1.661  -76.587 1.00 68.50  ? 296 ARG A CZ  1 
ATOM   2463  N NH1 . ARG A 1 296 ? 5.279   -2.532  -77.541 1.00 69.07  ? 296 ARG A NH1 1 
ATOM   2464  N NH2 . ARG A 1 296 ? 5.969   -2.098  -75.395 1.00 64.74  ? 296 ARG A NH2 1 
ATOM   2465  N N   . ARG A 1 297 ? 4.751   5.718   -80.910 1.00 101.57 ? 297 ARG A N   1 
ATOM   2466  C CA  . ARG A 1 297 ? 4.623   6.480   -82.164 1.00 106.20 ? 297 ARG A CA  1 
ATOM   2467  C C   . ARG A 1 297 ? 3.171   6.597   -82.646 1.00 107.36 ? 297 ARG A C   1 
ATOM   2468  O O   . ARG A 1 297 ? 2.846   7.474   -83.450 1.00 108.17 ? 297 ARG A O   1 
ATOM   2469  C CB  . ARG A 1 297 ? 5.534   5.911   -83.273 1.00 107.16 ? 297 ARG A CB  1 
ATOM   2470  C CG  . ARG A 1 297 ? 7.027   6.142   -83.051 1.00 105.47 ? 297 ARG A CG  1 
ATOM   2471  C CD  . ARG A 1 297 ? 7.838   5.860   -84.315 1.00 107.55 ? 297 ARG A CD  1 
ATOM   2472  N NE  . ARG A 1 297 ? 8.302   4.470   -84.395 1.00 106.40 ? 297 ARG A NE  1 
ATOM   2473  C CZ  . ARG A 1 297 ? 8.855   3.913   -85.476 1.00 104.54 ? 297 ARG A CZ  1 
ATOM   2474  N NH1 . ARG A 1 297 ? 9.014   4.614   -86.592 1.00 105.07 ? 297 ARG A NH1 1 
ATOM   2475  N NH2 . ARG A 1 297 ? 9.245   2.644   -85.445 1.00 100.81 ? 297 ARG A NH2 1 
ATOM   2476  N N   . LYS A 1 298 ? 2.304   5.727   -82.127 1.00 110.33 ? 298 LYS A N   1 
ATOM   2477  C CA  . LYS A 1 298 ? 0.914   5.626   -82.585 1.00 112.39 ? 298 LYS A CA  1 
ATOM   2478  C C   . LYS A 1 298 ? -0.080  6.258   -81.602 1.00 111.70 ? 298 LYS A C   1 
ATOM   2479  O O   . LYS A 1 298 ? 0.226   6.437   -80.418 1.00 108.49 ? 298 LYS A O   1 
ATOM   2480  C CB  . LYS A 1 298 ? 0.539   4.158   -82.838 1.00 114.36 ? 298 LYS A CB  1 
ATOM   2481  C CG  . LYS A 1 298 ? 1.332   3.477   -83.949 1.00 117.01 ? 298 LYS A CG  1 
ATOM   2482  C CD  . LYS A 1 298 ? 1.061   1.976   -84.002 1.00 119.12 ? 298 LYS A CD  1 
ATOM   2483  C CE  . LYS A 1 298 ? 1.751   1.232   -82.862 1.00 120.04 ? 298 LYS A CE  1 
ATOM   2484  N NZ  . LYS A 1 298 ? 1.483   -0.235  -82.891 1.00 118.77 ? 298 LYS A NZ  1 
ATOM   2485  N N   . ILE A 1 299 ? -1.270  6.582   -82.109 1.00 110.86 ? 299 ILE A N   1 
ATOM   2486  C CA  . ILE A 1 299 ? -2.344  7.185   -81.310 1.00 109.42 ? 299 ILE A CA  1 
ATOM   2487  C C   . ILE A 1 299 ? -3.522  6.205   -81.172 1.00 107.48 ? 299 ILE A C   1 
ATOM   2488  O O   . ILE A 1 299 ? -3.960  5.607   -82.161 1.00 109.46 ? 299 ILE A O   1 
ATOM   2489  C CB  . ILE A 1 299 ? -2.823  8.521   -81.934 1.00 110.53 ? 299 ILE A CB  1 
ATOM   2490  C CG1 . ILE A 1 299 ? -1.642  9.484   -82.106 1.00 110.93 ? 299 ILE A CG1 1 
ATOM   2491  C CG2 . ILE A 1 299 ? -3.907  9.167   -81.081 1.00 108.88 ? 299 ILE A CG2 1 
ATOM   2492  C CD1 . ILE A 1 299 ? -1.765  10.409  -83.299 1.00 114.94 ? 299 ILE A CD1 1 
ATOM   2493  N N   . TYR A 1 300 ? -4.017  6.041   -79.942 1.00 100.25 ? 300 TYR A N   1 
ATOM   2494  C CA  . TYR A 1 300 ? -5.082  5.073   -79.643 1.00 96.71  ? 300 TYR A CA  1 
ATOM   2495  C C   . TYR A 1 300 ? -6.287  5.708   -78.943 1.00 93.28  ? 300 TYR A C   1 
ATOM   2496  O O   . TYR A 1 300 ? -6.145  6.674   -78.193 1.00 88.69  ? 300 TYR A O   1 
ATOM   2497  C CB  . TYR A 1 300 ? -4.541  3.935   -78.775 1.00 96.43  ? 300 TYR A CB  1 
ATOM   2498  C CG  . TYR A 1 300 ? -3.653  2.948   -79.497 1.00 96.54  ? 300 TYR A CG  1 
ATOM   2499  C CD1 . TYR A 1 300 ? -2.312  3.241   -79.753 1.00 96.57  ? 300 TYR A CD1 1 
ATOM   2500  C CD2 . TYR A 1 300 ? -4.141  1.708   -79.895 1.00 98.00  ? 300 TYR A CD2 1 
ATOM   2501  C CE1 . TYR A 1 300 ? -1.491  2.333   -80.404 1.00 96.50  ? 300 TYR A CE1 1 
ATOM   2502  C CE2 . TYR A 1 300 ? -3.328  0.792   -80.546 1.00 99.09  ? 300 TYR A CE2 1 
ATOM   2503  C CZ  . TYR A 1 300 ? -2.005  1.110   -80.800 1.00 97.28  ? 300 TYR A CZ  1 
ATOM   2504  O OH  . TYR A 1 300 ? -1.198  0.206   -81.449 1.00 98.87  ? 300 TYR A OH  1 
ATOM   2505  N N   . LYS A 1 301 ? -7.473  5.154   -79.199 1.00 94.00  ? 301 LYS A N   1 
ATOM   2506  C CA  . LYS A 1 301 ? -8.674  5.506   -78.440 1.00 93.62  ? 301 LYS A CA  1 
ATOM   2507  C C   . LYS A 1 301 ? -8.898  4.526   -77.300 1.00 88.03  ? 301 LYS A C   1 
ATOM   2508  O O   . LYS A 1 301 ? -8.867  3.306   -77.494 1.00 85.02  ? 301 LYS A O   1 
ATOM   2509  C CB  . LYS A 1 301 ? -9.911  5.553   -79.338 1.00 101.07 ? 301 LYS A CB  1 
ATOM   2510  C CG  . LYS A 1 301 ? -10.273 6.943   -79.830 1.00 105.70 ? 301 LYS A CG  1 
ATOM   2511  C CD  . LYS A 1 301 ? -11.573 6.913   -80.612 1.00 112.17 ? 301 LYS A CD  1 
ATOM   2512  C CE  . LYS A 1 301 ? -11.608 8.020   -81.656 1.00 117.02 ? 301 LYS A CE  1 
ATOM   2513  N NZ  . LYS A 1 301 ? -12.752 7.873   -82.602 1.00 116.33 ? 301 LYS A NZ  1 
ATOM   2514  N N   . TRP A 1 302 ? -9.108  5.074   -76.107 1.00 83.37  ? 302 TRP A N   1 
ATOM   2515  C CA  . TRP A 1 302 ? -9.354  4.276   -74.923 1.00 80.19  ? 302 TRP A CA  1 
ATOM   2516  C C   . TRP A 1 302 ? -10.822 4.052   -74.766 1.00 80.80  ? 302 TRP A C   1 
ATOM   2517  O O   . TRP A 1 302 ? -11.581 4.988   -74.487 1.00 79.55  ? 302 TRP A O   1 
ATOM   2518  C CB  . TRP A 1 302 ? -8.780  4.957   -73.685 1.00 78.11  ? 302 TRP A CB  1 
ATOM   2519  C CG  . TRP A 1 302 ? -8.892  4.118   -72.435 1.00 76.28  ? 302 TRP A CG  1 
ATOM   2520  C CD1 . TRP A 1 302 ? -9.860  4.204   -71.442 1.00 75.08  ? 302 TRP A CD1 1 
ATOM   2521  C CD2 . TRP A 1 302 ? -8.008  3.025   -72.014 1.00 74.74  ? 302 TRP A CD2 1 
ATOM   2522  N NE1 . TRP A 1 302 ? -9.636  3.267   -70.461 1.00 74.20  ? 302 TRP A NE1 1 
ATOM   2523  C CE2 . TRP A 1 302 ? -8.543  2.527   -70.749 1.00 73.18  ? 302 TRP A CE2 1 
ATOM   2524  C CE3 . TRP A 1 302 ? -6.867  2.433   -72.543 1.00 73.48  ? 302 TRP A CE3 1 
ATOM   2525  C CZ2 . TRP A 1 302 ? -7.948  1.485   -70.057 1.00 73.28  ? 302 TRP A CZ2 1 
ATOM   2526  C CZ3 . TRP A 1 302 ? -6.274  1.378   -71.837 1.00 72.39  ? 302 TRP A CZ3 1 
ATOM   2527  C CH2 . TRP A 1 302 ? -6.806  0.914   -70.626 1.00 71.22  ? 302 TRP A CH2 1 
ATOM   2528  N N   . ASN A 1 303 ? -11.237 2.805   -74.965 1.00 82.24  ? 303 ASN A N   1 
ATOM   2529  C CA  . ASN A 1 303 ? -12.642 2.430   -74.852 1.00 84.51  ? 303 ASN A CA  1 
ATOM   2530  C C   . ASN A 1 303 ? -12.894 1.431   -73.732 1.00 82.99  ? 303 ASN A C   1 
ATOM   2531  O O   . ASN A 1 303 ? -13.349 0.310   -73.969 1.00 84.76  ? 303 ASN A O   1 
ATOM   2532  C CB  . ASN A 1 303 ? -13.169 1.901   -76.188 1.00 86.18  ? 303 ASN A CB  1 
ATOM   2533  C CG  . ASN A 1 303 ? -13.607 3.016   -77.118 1.00 90.17  ? 303 ASN A CG  1 
ATOM   2534  O OD1 . ASN A 1 303 ? -14.364 3.908   -76.722 1.00 92.04  ? 303 ASN A OD1 1 
ATOM   2535  N ND2 . ASN A 1 303 ? -13.132 2.976   -78.361 1.00 90.18  ? 303 ASN A ND2 1 
ATOM   2536  N N   . HIS A 1 304 ? -12.568 1.842   -72.511 1.00 79.89  ? 304 HIS A N   1 
ATOM   2537  C CA  . HIS A 1 304 ? -12.888 1.063   -71.324 1.00 78.89  ? 304 HIS A CA  1 
ATOM   2538  C C   . HIS A 1 304 ? -13.143 1.957   -70.155 1.00 74.61  ? 304 HIS A C   1 
ATOM   2539  O O   . HIS A 1 304 ? -12.313 2.084   -69.258 1.00 71.89  ? 304 HIS A O   1 
ATOM   2540  C CB  . HIS A 1 304 ? -11.790 0.059   -71.006 1.00 79.94  ? 304 HIS A CB  1 
ATOM   2541  C CG  . HIS A 1 304 ? -12.148 -0.896  -69.895 1.00 82.90  ? 304 HIS A CG  1 
ATOM   2542  N ND1 . HIS A 1 304 ? -11.404 -1.023  -68.778 1.00 82.47  ? 304 HIS A ND1 1 
ATOM   2543  C CD2 . HIS A 1 304 ? -13.231 -1.765  -69.747 1.00 83.94  ? 304 HIS A CD2 1 
ATOM   2544  C CE1 . HIS A 1 304 ? -11.967 -1.939  -67.969 1.00 81.81  ? 304 HIS A CE1 1 
ATOM   2545  N NE2 . HIS A 1 304 ? -13.089 -2.385  -68.559 1.00 83.06  ? 304 HIS A NE2 1 
ATOM   2546  N N   . GLY A 1 305 ? -14.303 2.598   -70.168 1.00 73.92  ? 305 GLY A N   1 
ATOM   2547  C CA  . GLY A 1 305 ? -14.698 3.488   -69.095 1.00 73.15  ? 305 GLY A CA  1 
ATOM   2548  C C   . GLY A 1 305 ? -13.893 4.763   -69.091 1.00 71.92  ? 305 GLY A C   1 
ATOM   2549  O O   . GLY A 1 305 ? -13.431 5.222   -70.133 1.00 72.05  ? 305 GLY A O   1 
ATOM   2550  N N   . LEU A 1 306 ? -13.743 5.341   -67.907 1.00 73.19  ? 306 LEU A N   1 
ATOM   2551  C CA  . LEU A 1 306 ? -12.898 6.504   -67.713 1.00 73.41  ? 306 LEU A CA  1 
ATOM   2552  C C   . LEU A 1 306 ? -11.428 6.105   -67.684 1.00 72.23  ? 306 LEU A C   1 
ATOM   2553  O O   . LEU A 1 306 ? -11.072 5.034   -67.176 1.00 70.11  ? 306 LEU A O   1 
ATOM   2554  C CB  . LEU A 1 306 ? -13.264 7.202   -66.404 1.00 71.86  ? 306 LEU A CB  1 
ATOM   2555  C CG  . LEU A 1 306 ? -14.641 7.847   -66.325 1.00 72.13  ? 306 LEU A CG  1 
ATOM   2556  C CD1 . LEU A 1 306 ? -14.983 8.156   -64.878 1.00 71.54  ? 306 LEU A CD1 1 
ATOM   2557  C CD2 . LEU A 1 306 ? -14.686 9.110   -67.169 1.00 74.43  ? 306 LEU A CD2 1 
ATOM   2558  N N   . LEU A 1 307 ? -10.582 6.970   -68.237 1.00 73.64  ? 307 LEU A N   1 
ATOM   2559  C CA  . LEU A 1 307 ? -9.132  6.811   -68.131 1.00 75.23  ? 307 LEU A CA  1 
ATOM   2560  C C   . LEU A 1 307 ? -8.628  7.251   -66.772 1.00 71.91  ? 307 LEU A C   1 
ATOM   2561  O O   . LEU A 1 307 ? -8.762  8.416   -66.407 1.00 71.56  ? 307 LEU A O   1 
ATOM   2562  C CB  . LEU A 1 307 ? -8.417  7.627   -69.205 1.00 76.87  ? 307 LEU A CB  1 
ATOM   2563  C CG  . LEU A 1 307 ? -7.938  6.914   -70.464 1.00 77.92  ? 307 LEU A CG  1 
ATOM   2564  C CD1 . LEU A 1 307 ? -7.428  7.943   -71.456 1.00 78.72  ? 307 LEU A CD1 1 
ATOM   2565  C CD2 . LEU A 1 307 ? -6.861  5.887   -70.144 1.00 77.00  ? 307 LEU A CD2 1 
ATOM   2566  N N   . GLN A 1 308 ? -8.049  6.320   -66.025 1.00 71.74  ? 308 GLN A N   1 
ATOM   2567  C CA  . GLN A 1 308 ? -7.277  6.676   -64.840 1.00 74.91  ? 308 GLN A CA  1 
ATOM   2568  C C   . GLN A 1 308 ? -6.140  7.612   -65.243 1.00 76.04  ? 308 GLN A C   1 
ATOM   2569  O O   . GLN A 1 308 ? -5.403  7.329   -66.192 1.00 73.37  ? 308 GLN A O   1 
ATOM   2570  C CB  . GLN A 1 308 ? -6.719  5.426   -64.164 1.00 74.22  ? 308 GLN A CB  1 
ATOM   2571  C CG  . GLN A 1 308 ? -7.586  4.875   -63.045 1.00 74.93  ? 308 GLN A CG  1 
ATOM   2572  C CD  . GLN A 1 308 ? -7.314  3.408   -62.769 1.00 74.89  ? 308 GLN A CD  1 
ATOM   2573  O OE1 . GLN A 1 308 ? -7.407  2.570   -63.668 1.00 75.12  ? 308 GLN A OE1 1 
ATOM   2574  N NE2 . GLN A 1 308 ? -6.979  3.089   -61.522 1.00 73.39  ? 308 GLN A NE2 1 
ATOM   2575  N N   . GLY A 1 309 ? -6.023  8.737   -64.543 1.00 79.41  ? 309 GLY A N   1 
ATOM   2576  C CA  . GLY A 1 309 ? -5.004  9.738   -64.864 1.00 84.73  ? 309 GLY A CA  1 
ATOM   2577  C C   . GLY A 1 309 ? -5.566  11.046  -65.398 1.00 87.30  ? 309 GLY A C   1 
ATOM   2578  O O   . GLY A 1 309 ? -4.963  12.107  -65.217 1.00 90.13  ? 309 GLY A O   1 
ATOM   2579  N N   . ASP A 1 310 ? -6.712  10.972  -66.070 1.00 86.61  ? 310 ASP A N   1 
ATOM   2580  C CA  . ASP A 1 310 ? -7.428  12.172  -66.496 1.00 89.71  ? 310 ASP A CA  1 
ATOM   2581  C C   . ASP A 1 310 ? -7.981  12.897  -65.262 1.00 90.63  ? 310 ASP A C   1 
ATOM   2582  O O   . ASP A 1 310 ? -8.651  12.284  -64.429 1.00 90.16  ? 310 ASP A O   1 
ATOM   2583  C CB  . ASP A 1 310 ? -8.558  11.813  -67.473 1.00 89.17  ? 310 ASP A CB  1 
ATOM   2584  C CG  . ASP A 1 310 ? -9.112  13.026  -68.213 1.00 89.87  ? 310 ASP A CG  1 
ATOM   2585  O OD1 . ASP A 1 310 ? -9.424  14.044  -67.565 1.00 92.21  ? 310 ASP A OD1 1 
ATOM   2586  O OD2 . ASP A 1 310 ? -9.264  12.949  -69.448 1.00 92.02  ? 310 ASP A OD2 1 
ATOM   2587  N N   . PRO A 1 311 ? -7.677  14.201  -65.134 1.00 93.30  ? 311 PRO A N   1 
ATOM   2588  C CA  . PRO A 1 311 ? -8.093  15.043  -64.002 1.00 94.14  ? 311 PRO A CA  1 
ATOM   2589  C C   . PRO A 1 311 ? -9.574  14.925  -63.601 1.00 94.92  ? 311 PRO A C   1 
ATOM   2590  O O   . PRO A 1 311 ? -9.907  15.109  -62.428 1.00 95.30  ? 311 PRO A O   1 
ATOM   2591  C CB  . PRO A 1 311 ? -7.788  16.476  -64.493 1.00 95.60  ? 311 PRO A CB  1 
ATOM   2592  C CG  . PRO A 1 311 ? -7.276  16.343  -65.902 1.00 95.49  ? 311 PRO A CG  1 
ATOM   2593  C CD  . PRO A 1 311 ? -6.789  14.937  -66.047 1.00 94.12  ? 311 PRO A CD  1 
ATOM   2594  N N   . LEU A 1 312 ? -10.446 14.622  -64.560 1.00 95.26  ? 312 LEU A N   1 
ATOM   2595  C CA  . LEU A 1 312 ? -11.885 14.580  -64.297 1.00 92.67  ? 312 LEU A CA  1 
ATOM   2596  C C   . LEU A 1 312 ? -12.397 13.211  -63.853 1.00 88.92  ? 312 LEU A C   1 
ATOM   2597  O O   . LEU A 1 312 ? -13.483 13.106  -63.282 1.00 88.14  ? 312 LEU A O   1 
ATOM   2598  C CB  . LEU A 1 312 ? -12.671 15.065  -65.515 1.00 96.63  ? 312 LEU A CB  1 
ATOM   2599  C CG  . LEU A 1 312 ? -12.766 16.580  -65.718 1.00 100.18 ? 312 LEU A CG  1 
ATOM   2600  C CD1 . LEU A 1 312 ? -13.584 16.893  -66.961 1.00 102.80 ? 312 LEU A CD1 1 
ATOM   2601  C CD2 . LEU A 1 312 ? -13.362 17.270  -64.497 1.00 101.46 ? 312 LEU A CD2 1 
ATOM   2602  N N   . SER A 1 313 ? -11.614 12.170  -64.110 1.00 84.85  ? 313 SER A N   1 
ATOM   2603  C CA  . SER A 1 313 ? -12.042 10.804  -63.833 1.00 82.90  ? 313 SER A CA  1 
ATOM   2604  C C   . SER A 1 313 ? -12.534 10.604  -62.399 1.00 81.17  ? 313 SER A C   1 
ATOM   2605  O O   . SER A 1 313 ? -13.636 10.103  -62.187 1.00 81.89  ? 313 SER A O   1 
ATOM   2606  C CB  . SER A 1 313 ? -10.934 9.807   -64.175 1.00 80.52  ? 313 SER A CB  1 
ATOM   2607  O OG  . SER A 1 313 ? -10.804 9.671   -65.580 1.00 82.76  ? 313 SER A OG  1 
ATOM   2608  N N   . GLY A 1 314 ? -11.728 11.027  -61.426 1.00 79.47  ? 314 GLY A N   1 
ATOM   2609  C CA  . GLY A 1 314 ? -12.044 10.839  -60.008 1.00 76.62  ? 314 GLY A CA  1 
ATOM   2610  C C   . GLY A 1 314 ? -13.432 11.313  -59.618 1.00 77.31  ? 314 GLY A C   1 
ATOM   2611  O O   . GLY A 1 314 ? -14.226 10.548  -59.070 1.00 78.26  ? 314 GLY A O   1 
ATOM   2612  N N   . CYS A 1 315 ? -13.724 12.578  -59.914 1.00 77.69  ? 315 CYS A N   1 
ATOM   2613  C CA  . CYS A 1 315 ? -14.993 13.203  -59.533 1.00 78.66  ? 315 CYS A CA  1 
ATOM   2614  C C   . CYS A 1 315 ? -16.174 12.687  -60.358 1.00 80.07  ? 315 CYS A C   1 
ATOM   2615  O O   . CYS A 1 315 ? -17.314 12.686  -59.889 1.00 80.79  ? 315 CYS A O   1 
ATOM   2616  C CB  . CYS A 1 315 ? -14.900 14.720  -59.679 1.00 80.37  ? 315 CYS A CB  1 
ATOM   2617  S SG  . CYS A 1 315 ? -14.852 15.291  -61.397 1.00 82.99  ? 315 CYS A SG  1 
ATOM   2618  N N   . LEU A 1 316 ? -15.901 12.282  -61.595 1.00 77.65  ? 316 LEU A N   1 
ATOM   2619  C CA  . LEU A 1 316 ? -16.934 11.725  -62.449 1.00 78.76  ? 316 LEU A CA  1 
ATOM   2620  C C   . LEU A 1 316 ? -17.248 10.290  -62.056 1.00 79.00  ? 316 LEU A C   1 
ATOM   2621  O O   . LEU A 1 316 ? -18.398 9.855   -62.143 1.00 81.89  ? 316 LEU A O   1 
ATOM   2622  C CB  . LEU A 1 316 ? -16.538 11.816  -63.923 1.00 78.89  ? 316 LEU A CB  1 
ATOM   2623  C CG  . LEU A 1 316 ? -16.550 13.219  -64.538 1.00 79.42  ? 316 LEU A CG  1 
ATOM   2624  C CD1 . LEU A 1 316 ? -16.062 13.172  -65.974 1.00 79.39  ? 316 LEU A CD1 1 
ATOM   2625  C CD2 . LEU A 1 316 ? -17.927 13.857  -64.464 1.00 80.83  ? 316 LEU A CD2 1 
ATOM   2626  N N   . CYS A 1 317 ? -16.229 9.564   -61.604 1.00 76.87  ? 317 CYS A N   1 
ATOM   2627  C CA  . CYS A 1 317 ? -16.421 8.211   -61.096 1.00 75.84  ? 317 CYS A CA  1 
ATOM   2628  C C   . CYS A 1 317 ? -17.244 8.214   -59.809 1.00 76.18  ? 317 CYS A C   1 
ATOM   2629  O O   . CYS A 1 317 ? -18.090 7.346   -59.611 1.00 77.04  ? 317 CYS A O   1 
ATOM   2630  C CB  . CYS A 1 317 ? -15.082 7.514   -60.870 1.00 73.08  ? 317 CYS A CB  1 
ATOM   2631  S SG  . CYS A 1 317 ? -15.223 5.773   -60.402 1.00 70.80  ? 317 CYS A SG  1 
ATOM   2632  N N   . GLU A 1 318 ? -17.002 9.198   -58.945 1.00 75.93  ? 318 GLU A N   1 
ATOM   2633  C CA  . GLU A 1 318 ? -17.803 9.375   -57.731 1.00 76.59  ? 318 GLU A CA  1 
ATOM   2634  C C   . GLU A 1 318 ? -19.249 9.725   -58.079 1.00 76.59  ? 318 GLU A C   1 
ATOM   2635  O O   . GLU A 1 318 ? -20.189 9.199   -57.484 1.00 77.59  ? 318 GLU A O   1 
ATOM   2636  C CB  . GLU A 1 318 ? -17.203 10.467  -56.843 1.00 79.54  ? 318 GLU A CB  1 
ATOM   2637  C CG  . GLU A 1 318 ? -15.936 10.058  -56.106 1.00 84.39  ? 318 GLU A CG  1 
ATOM   2638  C CD  . GLU A 1 318 ? -15.564 11.032  -54.998 1.00 86.75  ? 318 GLU A CD  1 
ATOM   2639  O OE1 . GLU A 1 318 ? -14.420 11.541  -55.016 1.00 87.59  ? 318 GLU A OE1 1 
ATOM   2640  O OE2 . GLU A 1 318 ? -16.416 11.293  -54.116 1.00 86.62  ? 318 GLU A OE2 1 
ATOM   2641  N N   . LEU A 1 319 ? -19.405 10.626  -59.045 1.00 75.42  ? 319 LEU A N   1 
ATOM   2642  C CA  . LEU A 1 319 ? -20.710 11.037  -59.549 1.00 75.05  ? 319 LEU A CA  1 
ATOM   2643  C C   . LEU A 1 319 ? -21.482 9.833   -60.083 1.00 73.58  ? 319 LEU A C   1 
ATOM   2644  O O   . LEU A 1 319 ? -22.619 9.589   -59.681 1.00 75.34  ? 319 LEU A O   1 
ATOM   2645  C CB  . LEU A 1 319 ? -20.522 12.091  -60.648 1.00 76.92  ? 319 LEU A CB  1 
ATOM   2646  C CG  . LEU A 1 319 ? -21.681 12.977  -61.114 1.00 78.01  ? 319 LEU A CG  1 
ATOM   2647  C CD1 . LEU A 1 319 ? -22.332 12.402  -62.360 1.00 79.05  ? 319 LEU A CD1 1 
ATOM   2648  C CD2 . LEU A 1 319 ? -22.699 13.218  -60.008 1.00 79.03  ? 319 LEU A CD2 1 
ATOM   2649  N N   . TYR A 1 320 ? -20.844 9.082   -60.977 1.00 70.35  ? 320 TYR A N   1 
ATOM   2650  C CA  . TYR A 1 320 ? -21.393 7.840   -61.508 1.00 70.62  ? 320 TYR A CA  1 
ATOM   2651  C C   . TYR A 1 320 ? -21.742 6.823   -60.408 1.00 72.47  ? 320 TYR A C   1 
ATOM   2652  O O   . TYR A 1 320 ? -22.855 6.278   -60.391 1.00 72.20  ? 320 TYR A O   1 
ATOM   2653  C CB  . TYR A 1 320 ? -20.413 7.241   -62.509 1.00 68.76  ? 320 TYR A CB  1 
ATOM   2654  C CG  . TYR A 1 320 ? -20.833 5.929   -63.133 1.00 70.35  ? 320 TYR A CG  1 
ATOM   2655  C CD1 . TYR A 1 320 ? -21.668 5.896   -64.255 1.00 70.98  ? 320 TYR A CD1 1 
ATOM   2656  C CD2 . TYR A 1 320 ? -20.353 4.718   -62.634 1.00 69.79  ? 320 TYR A CD2 1 
ATOM   2657  C CE1 . TYR A 1 320 ? -22.031 4.692   -64.842 1.00 71.82  ? 320 TYR A CE1 1 
ATOM   2658  C CE2 . TYR A 1 320 ? -20.709 3.511   -63.211 1.00 70.39  ? 320 TYR A CE2 1 
ATOM   2659  C CZ  . TYR A 1 320 ? -21.546 3.501   -64.313 1.00 72.10  ? 320 TYR A CZ  1 
ATOM   2660  O OH  . TYR A 1 320 ? -21.887 2.297   -64.878 1.00 72.39  ? 320 TYR A OH  1 
ATOM   2661  N N   . MET A 1 321 ? -20.801 6.587   -59.489 1.00 71.07  ? 321 MET A N   1 
ATOM   2662  C CA  . MET A 1 321 ? -20.956 5.556   -58.452 1.00 70.66  ? 321 MET A CA  1 
ATOM   2663  C C   . MET A 1 321 ? -22.067 5.882   -57.452 1.00 70.56  ? 321 MET A C   1 
ATOM   2664  O O   . MET A 1 321 ? -22.689 4.977   -56.890 1.00 70.60  ? 321 MET A O   1 
ATOM   2665  C CB  . MET A 1 321 ? -19.632 5.320   -57.706 1.00 73.28  ? 321 MET A CB  1 
ATOM   2666  C CG  . MET A 1 321 ? -18.531 4.668   -58.536 1.00 75.01  ? 321 MET A CG  1 
ATOM   2667  S SD  . MET A 1 321 ? -18.838 2.924   -58.878 1.00 78.94  ? 321 MET A SD  1 
ATOM   2668  C CE  . MET A 1 321 ? -18.264 2.191   -57.347 1.00 75.73  ? 321 MET A CE  1 
ATOM   2669  N N   . ALA A 1 322 ? -22.299 7.171   -57.215 1.00 69.14  ? 322 ALA A N   1 
ATOM   2670  C CA  . ALA A 1 322 ? -23.400 7.604   -56.359 1.00 70.17  ? 322 ALA A CA  1 
ATOM   2671  C C   . ALA A 1 322 ? -24.738 7.287   -57.028 1.00 73.30  ? 322 ALA A C   1 
ATOM   2672  O O   . ALA A 1 322 ? -25.708 6.927   -56.359 1.00 73.25  ? 322 ALA A O   1 
ATOM   2673  C CB  . ALA A 1 322 ? -23.291 9.090   -56.065 1.00 70.95  ? 322 ALA A CB  1 
ATOM   2674  N N   . PHE A 1 323 ? -24.769 7.419   -58.354 1.00 73.18  ? 323 PHE A N   1 
ATOM   2675  C CA  . PHE A 1 323 ? -25.950 7.122   -59.138 1.00 78.40  ? 323 PHE A CA  1 
ATOM   2676  C C   . PHE A 1 323 ? -26.271 5.630   -59.116 1.00 79.60  ? 323 PHE A C   1 
ATOM   2677  O O   . PHE A 1 323 ? -27.442 5.249   -58.991 1.00 81.13  ? 323 PHE A O   1 
ATOM   2678  C CB  . PHE A 1 323 ? -25.771 7.621   -60.579 1.00 81.13  ? 323 PHE A CB  1 
ATOM   2679  C CG  . PHE A 1 323 ? -26.944 7.343   -61.478 1.00 81.87  ? 323 PHE A CG  1 
ATOM   2680  C CD1 . PHE A 1 323 ? -28.204 7.859   -61.187 1.00 83.85  ? 323 PHE A CD1 1 
ATOM   2681  C CD2 . PHE A 1 323 ? -26.782 6.590   -62.633 1.00 83.50  ? 323 PHE A CD2 1 
ATOM   2682  C CE1 . PHE A 1 323 ? -29.282 7.611   -62.021 1.00 86.05  ? 323 PHE A CE1 1 
ATOM   2683  C CE2 . PHE A 1 323 ? -27.854 6.344   -63.477 1.00 86.04  ? 323 PHE A CE2 1 
ATOM   2684  C CZ  . PHE A 1 323 ? -29.107 6.854   -63.170 1.00 87.42  ? 323 PHE A CZ  1 
ATOM   2685  N N   . MET A 1 324 ? -25.238 4.793   -59.232 1.00 77.79  ? 324 MET A N   1 
ATOM   2686  C CA  . MET A 1 324 ? -25.414 3.341   -59.150 1.00 78.84  ? 324 MET A CA  1 
ATOM   2687  C C   . MET A 1 324 ? -25.967 2.964   -57.777 1.00 79.56  ? 324 MET A C   1 
ATOM   2688  O O   . MET A 1 324 ? -26.743 2.011   -57.646 1.00 81.86  ? 324 MET A O   1 
ATOM   2689  C CB  . MET A 1 324 ? -24.095 2.604   -59.393 1.00 76.16  ? 324 MET A CB  1 
ATOM   2690  C CG  . MET A 1 324 ? -23.455 2.843   -60.747 1.00 77.23  ? 324 MET A CG  1 
ATOM   2691  S SD  . MET A 1 324 ? -24.139 1.836   -62.076 1.00 78.53  ? 324 MET A SD  1 
ATOM   2692  C CE  . MET A 1 324 ? -25.170 3.042   -62.906 1.00 81.75  ? 324 MET A CE  1 
ATOM   2693  N N   . ASP A 1 325 ? -25.577 3.735   -56.765 1.00 77.18  ? 325 ASP A N   1 
ATOM   2694  C CA  . ASP A 1 325 ? -26.012 3.503   -55.396 1.00 80.18  ? 325 ASP A CA  1 
ATOM   2695  C C   . ASP A 1 325 ? -27.515 3.778   -55.197 1.00 80.74  ? 325 ASP A C   1 
ATOM   2696  O O   . ASP A 1 325 ? -28.224 2.989   -54.564 1.00 79.43  ? 325 ASP A O   1 
ATOM   2697  C CB  . ASP A 1 325 ? -25.174 4.351   -54.437 1.00 81.33  ? 325 ASP A CB  1 
ATOM   2698  C CG  . ASP A 1 325 ? -25.399 3.986   -52.994 1.00 85.45  ? 325 ASP A CG  1 
ATOM   2699  O OD1 . ASP A 1 325 ? -26.449 4.372   -52.438 1.00 88.42  ? 325 ASP A OD1 1 
ATOM   2700  O OD2 . ASP A 1 325 ? -24.518 3.326   -52.407 1.00 91.06  ? 325 ASP A OD2 1 
ATOM   2701  N N   . ARG A 1 326 ? -27.989 4.899   -55.729 1.00 80.81  ? 326 ARG A N   1 
ATOM   2702  C CA  . ARG A 1 326 ? -29.408 5.246   -55.659 1.00 82.67  ? 326 ARG A CA  1 
ATOM   2703  C C   . ARG A 1 326 ? -30.228 4.252   -56.487 1.00 81.90  ? 326 ARG A C   1 
ATOM   2704  O O   . ARG A 1 326 ? -31.339 3.889   -56.117 1.00 81.20  ? 326 ARG A O   1 
ATOM   2705  C CB  . ARG A 1 326 ? -29.617 6.671   -56.169 1.00 84.81  ? 326 ARG A CB  1 
ATOM   2706  C CG  . ARG A 1 326 ? -30.923 7.322   -55.744 1.00 88.56  ? 326 ARG A CG  1 
ATOM   2707  C CD  . ARG A 1 326 ? -30.803 8.843   -55.738 1.00 90.86  ? 326 ARG A CD  1 
ATOM   2708  N NE  . ARG A 1 326 ? -30.084 9.352   -56.908 1.00 90.51  ? 326 ARG A NE  1 
ATOM   2709  C CZ  . ARG A 1 326 ? -30.654 9.960   -57.946 1.00 93.61  ? 326 ARG A CZ  1 
ATOM   2710  N NH1 . ARG A 1 326 ? -31.971 10.156  -57.974 1.00 94.43  ? 326 ARG A NH1 1 
ATOM   2711  N NH2 . ARG A 1 326 ? -29.901 10.377  -58.960 1.00 91.87  ? 326 ARG A NH2 1 
ATOM   2712  N N   . LEU A 1 327 ? -29.630 3.796   -57.586 1.00 82.69  ? 327 LEU A N   1 
ATOM   2713  C CA  . LEU A 1 327 ? -30.241 2.854   -58.524 1.00 82.73  ? 327 LEU A CA  1 
ATOM   2714  C C   . LEU A 1 327 ? -30.458 1.458   -57.927 1.00 83.06  ? 327 LEU A C   1 
ATOM   2715  O O   . LEU A 1 327 ? -31.570 0.933   -57.957 1.00 84.14  ? 327 LEU A O   1 
ATOM   2716  C CB  . LEU A 1 327 ? -29.355 2.746   -59.767 1.00 81.79  ? 327 LEU A CB  1 
ATOM   2717  C CG  . LEU A 1 327 ? -29.963 2.545   -61.152 1.00 82.30  ? 327 LEU A CG  1 
ATOM   2718  C CD1 . LEU A 1 327 ? -31.095 3.530   -61.423 1.00 83.28  ? 327 LEU A CD1 1 
ATOM   2719  C CD2 . LEU A 1 327 ? -28.866 2.681   -62.193 1.00 79.52  ? 327 LEU A CD2 1 
ATOM   2720  N N   . TYR A 1 328 ? -29.392 0.871   -57.376 1.00 82.91  ? 328 TYR A N   1 
ATOM   2721  C CA  . TYR A 1 328 ? -29.407 -0.538  -56.966 1.00 80.30  ? 328 TYR A CA  1 
ATOM   2722  C C   . TYR A 1 328 ? -29.315 -0.783  -55.454 1.00 80.21  ? 328 TYR A C   1 
ATOM   2723  O O   . TYR A 1 328 ? -29.543 -1.905  -54.989 1.00 78.85  ? 328 TYR A O   1 
ATOM   2724  C CB  . TYR A 1 328 ? -28.299 -1.311  -57.675 1.00 78.03  ? 328 TYR A CB  1 
ATOM   2725  C CG  . TYR A 1 328 ? -28.295 -1.179  -59.180 1.00 76.72  ? 328 TYR A CG  1 
ATOM   2726  C CD1 . TYR A 1 328 ? -29.345 -1.688  -59.956 1.00 76.39  ? 328 TYR A CD1 1 
ATOM   2727  C CD2 . TYR A 1 328 ? -27.228 -0.573  -59.831 1.00 74.04  ? 328 TYR A CD2 1 
ATOM   2728  C CE1 . TYR A 1 328 ? -29.333 -1.578  -61.337 1.00 75.71  ? 328 TYR A CE1 1 
ATOM   2729  C CE2 . TYR A 1 328 ? -27.203 -0.460  -61.210 1.00 75.17  ? 328 TYR A CE2 1 
ATOM   2730  C CZ  . TYR A 1 328 ? -28.257 -0.962  -61.960 1.00 77.05  ? 328 TYR A CZ  1 
ATOM   2731  O OH  . TYR A 1 328 ? -28.217 -0.844  -63.332 1.00 77.42  ? 328 TYR A OH  1 
ATOM   2732  N N   . PHE A 1 329 ? -28.977 0.256   -54.695 1.00 81.37  ? 329 PHE A N   1 
ATOM   2733  C CA  . PHE A 1 329 ? -28.869 0.133   -53.245 1.00 83.24  ? 329 PHE A CA  1 
ATOM   2734  C C   . PHE A 1 329 ? -29.897 1.027   -52.570 1.00 90.08  ? 329 PHE A C   1 
ATOM   2735  O O   . PHE A 1 329 ? -29.553 1.992   -51.872 1.00 94.02  ? 329 PHE A O   1 
ATOM   2736  C CB  . PHE A 1 329 ? -27.446 0.454   -52.774 1.00 80.64  ? 329 PHE A CB  1 
ATOM   2737  C CG  . PHE A 1 329 ? -26.403 -0.460  -53.348 1.00 77.87  ? 329 PHE A CG  1 
ATOM   2738  C CD1 . PHE A 1 329 ? -26.155 -1.700  -52.774 1.00 77.05  ? 329 PHE A CD1 1 
ATOM   2739  C CD2 . PHE A 1 329 ? -25.685 -0.092  -54.476 1.00 77.09  ? 329 PHE A CD2 1 
ATOM   2740  C CE1 . PHE A 1 329 ? -25.209 -2.553  -53.313 1.00 74.95  ? 329 PHE A CE1 1 
ATOM   2741  C CE2 . PHE A 1 329 ? -24.738 -0.939  -55.019 1.00 76.17  ? 329 PHE A CE2 1 
ATOM   2742  C CZ  . PHE A 1 329 ? -24.500 -2.170  -54.437 1.00 75.27  ? 329 PHE A CZ  1 
ATOM   2743  N N   . SER A 1 330 ? -31.166 0.680   -52.781 1.00 93.27  ? 330 SER A N   1 
ATOM   2744  C CA  . SER A 1 330 ? -32.293 1.489   -52.334 1.00 95.09  ? 330 SER A CA  1 
ATOM   2745  C C   . SER A 1 330 ? -33.093 0.813   -51.224 1.00 95.65  ? 330 SER A C   1 
ATOM   2746  O O   . SER A 1 330 ? -33.720 1.491   -50.406 1.00 97.45  ? 330 SER A O   1 
ATOM   2747  C CB  . SER A 1 330 ? -33.211 1.824   -53.519 1.00 98.14  ? 330 SER A CB  1 
ATOM   2748  O OG  . SER A 1 330 ? -33.383 0.704   -54.375 1.00 98.02  ? 330 SER A OG  1 
ATOM   2749  N N   . ASN A 1 331 ? -33.068 -0.519  -51.197 1.00 96.85  ? 331 ASN A N   1 
ATOM   2750  C CA  . ASN A 1 331 ? -33.833 -1.288  -50.208 1.00 100.25 ? 331 ASN A CA  1 
ATOM   2751  C C   . ASN A 1 331 ? -32.971 -1.947  -49.138 1.00 100.12 ? 331 ASN A C   1 
ATOM   2752  O O   . ASN A 1 331 ? -33.309 -3.022  -48.629 1.00 100.56 ? 331 ASN A O   1 
ATOM   2753  C CB  . ASN A 1 331 ? -34.702 -2.332  -50.904 1.00 102.31 ? 331 ASN A CB  1 
ATOM   2754  C CG  . ASN A 1 331 ? -35.651 -1.715  -51.902 1.00 103.08 ? 331 ASN A CG  1 
ATOM   2755  O OD1 . ASN A 1 331 ? -35.527 -1.936  -53.104 1.00 104.32 ? 331 ASN A OD1 1 
ATOM   2756  N ND2 . ASN A 1 331 ? -36.583 -0.907  -51.411 1.00 102.06 ? 331 ASN A ND2 1 
ATOM   2757  N N   . LEU A 1 332 ? -31.872 -1.281  -48.786 1.00 99.56  ? 332 LEU A N   1 
ATOM   2758  C CA  . LEU A 1 332 ? -30.910 -1.810  -47.824 1.00 97.38  ? 332 LEU A CA  1 
ATOM   2759  C C   . LEU A 1 332 ? -31.468 -1.880  -46.396 1.00 94.62  ? 332 LEU A C   1 
ATOM   2760  O O   . LEU A 1 332 ? -31.572 -2.969  -45.828 1.00 95.47  ? 332 LEU A O   1 
ATOM   2761  C CB  . LEU A 1 332 ? -29.607 -0.997  -47.858 1.00 97.27  ? 332 LEU A CB  1 
ATOM   2762  C CG  . LEU A 1 332 ? -28.782 -1.030  -49.150 1.00 98.13  ? 332 LEU A CG  1 
ATOM   2763  C CD1 . LEU A 1 332 ? -27.649 -0.017  -49.092 1.00 96.99  ? 332 LEU A CD1 1 
ATOM   2764  C CD2 . LEU A 1 332 ? -28.242 -2.426  -49.419 1.00 97.23  ? 332 LEU A CD2 1 
ATOM   2765  N N   . ASP A 1 333 ? -31.830 -0.720  -45.838 1.00 91.07  ? 333 ASP A N   1 
ATOM   2766  C CA  . ASP A 1 333 ? -32.296 -0.592  -44.444 1.00 89.53  ? 333 ASP A CA  1 
ATOM   2767  C C   . ASP A 1 333 ? -31.790 0.722   -43.861 1.00 90.81  ? 333 ASP A C   1 
ATOM   2768  O O   . ASP A 1 333 ? -30.613 1.059   -44.000 1.00 92.65  ? 333 ASP A O   1 
ATOM   2769  C CB  . ASP A 1 333 ? -31.808 -1.766  -43.574 1.00 86.06  ? 333 ASP A CB  1 
ATOM   2770  C CG  . ASP A 1 333 ? -32.448 -1.791  -42.182 1.00 86.57  ? 333 ASP A CG  1 
ATOM   2771  O OD1 . ASP A 1 333 ? -32.953 -0.749  -41.710 1.00 86.33  ? 333 ASP A OD1 1 
ATOM   2772  O OD2 . ASP A 1 333 ? -32.433 -2.868  -41.549 1.00 85.72  ? 333 ASP A OD2 1 
ATOM   2773  N N   . LYS A 1 334 ? -32.676 1.452   -43.195 1.00 93.16  ? 334 LYS A N   1 
ATOM   2774  C CA  . LYS A 1 334 ? -32.292 2.690   -42.521 1.00 95.92  ? 334 LYS A CA  1 
ATOM   2775  C C   . LYS A 1 334 ? -31.427 2.422   -41.270 1.00 94.45  ? 334 LYS A C   1 
ATOM   2776  O O   . LYS A 1 334 ? -30.678 3.298   -40.821 1.00 93.31  ? 334 LYS A O   1 
ATOM   2777  C CB  . LYS A 1 334 ? -33.536 3.508   -42.156 1.00 98.63  ? 334 LYS A CB  1 
ATOM   2778  C CG  . LYS A 1 334 ? -33.264 4.988   -41.945 1.00 99.76  ? 334 LYS A CG  1 
ATOM   2779  C CD  . LYS A 1 334 ? -34.103 5.536   -40.807 1.00 101.92 ? 334 LYS A CD  1 
ATOM   2780  C CE  . LYS A 1 334 ? -33.296 6.512   -39.964 1.00 101.32 ? 334 LYS A CE  1 
ATOM   2781  N NZ  . LYS A 1 334 ? -34.059 6.969   -38.769 1.00 100.26 ? 334 LYS A NZ  1 
ATOM   2782  N N   . ASP A 1 335 ? -31.524 1.204   -40.734 1.00 90.62  ? 335 ASP A N   1 
ATOM   2783  C CA  . ASP A 1 335 ? -30.859 0.839   -39.482 1.00 85.86  ? 335 ASP A CA  1 
ATOM   2784  C C   . ASP A 1 335 ? -29.557 0.049   -39.672 1.00 80.70  ? 335 ASP A C   1 
ATOM   2785  O O   . ASP A 1 335 ? -28.838 -0.223  -38.704 1.00 80.68  ? 335 ASP A O   1 
ATOM   2786  C CB  . ASP A 1 335 ? -31.823 0.068   -38.579 1.00 88.87  ? 335 ASP A CB  1 
ATOM   2787  C CG  . ASP A 1 335 ? -32.997 0.913   -38.126 1.00 91.27  ? 335 ASP A CG  1 
ATOM   2788  O OD1 . ASP A 1 335 ? -32.776 2.079   -37.726 1.00 92.40  ? 335 ASP A OD1 1 
ATOM   2789  O OD2 . ASP A 1 335 ? -34.140 0.410   -38.166 1.00 92.59  ? 335 ASP A OD2 1 
ATOM   2790  N N   . ALA A 1 336 ? -29.257 -0.316  -40.912 1.00 75.06  ? 336 ALA A N   1 
ATOM   2791  C CA  . ALA A 1 336 ? -28.005 -0.987  -41.224 1.00 69.55  ? 336 ALA A CA  1 
ATOM   2792  C C   . ALA A 1 336 ? -26.845 0.004   -41.261 1.00 66.31  ? 336 ALA A C   1 
ATOM   2793  O O   . ALA A 1 336 ? -27.050 1.216   -41.369 1.00 64.85  ? 336 ALA A O   1 
ATOM   2794  C CB  . ALA A 1 336 ? -28.117 -1.723  -42.547 1.00 67.69  ? 336 ALA A CB  1 
ATOM   2795  N N   . PHE A 1 337 ? -25.629 -0.522  -41.146 1.00 63.35  ? 337 PHE A N   1 
ATOM   2796  C CA  . PHE A 1 337 ? -24.420 0.260   -41.381 1.00 61.01  ? 337 PHE A CA  1 
ATOM   2797  C C   . PHE A 1 337 ? -23.998 0.125   -42.836 1.00 59.18  ? 337 PHE A C   1 
ATOM   2798  O O   . PHE A 1 337 ? -23.804 -0.987  -43.331 1.00 59.07  ? 337 PHE A O   1 
ATOM   2799  C CB  . PHE A 1 337 ? -23.279 -0.213  -40.470 1.00 59.36  ? 337 PHE A CB  1 
ATOM   2800  C CG  . PHE A 1 337 ? -21.954 0.430   -40.780 1.00 57.96  ? 337 PHE A CG  1 
ATOM   2801  C CD1 . PHE A 1 337 ? -21.129 -0.087  -41.767 1.00 56.35  ? 337 PHE A CD1 1 
ATOM   2802  C CD2 . PHE A 1 337 ? -21.537 1.561   -40.087 1.00 57.01  ? 337 PHE A CD2 1 
ATOM   2803  C CE1 . PHE A 1 337 ? -19.925 0.516   -42.066 1.00 56.03  ? 337 PHE A CE1 1 
ATOM   2804  C CE2 . PHE A 1 337 ? -20.328 2.164   -40.379 1.00 55.04  ? 337 PHE A CE2 1 
ATOM   2805  C CZ  . PHE A 1 337 ? -19.520 1.642   -41.366 1.00 54.61  ? 337 PHE A CZ  1 
ATOM   2806  N N   . ILE A 1 338 ? -23.857 1.256   -43.521 1.00 58.09  ? 338 ILE A N   1 
ATOM   2807  C CA  . ILE A 1 338 ? -23.323 1.269   -44.885 1.00 57.82  ? 338 ILE A CA  1 
ATOM   2808  C C   . ILE A 1 338 ? -22.291 2.383   -45.031 1.00 56.19  ? 338 ILE A C   1 
ATOM   2809  O O   . ILE A 1 338 ? -22.496 3.498   -44.553 1.00 57.14  ? 338 ILE A O   1 
ATOM   2810  C CB  . ILE A 1 338 ? -24.422 1.461   -45.966 1.00 58.93  ? 338 ILE A CB  1 
ATOM   2811  C CG1 . ILE A 1 338 ? -25.628 0.548   -45.718 1.00 62.12  ? 338 ILE A CG1 1 
ATOM   2812  C CG2 . ILE A 1 338 ? -23.861 1.172   -47.351 1.00 59.96  ? 338 ILE A CG2 1 
ATOM   2813  C CD1 . ILE A 1 338 ? -26.830 1.237   -45.091 1.00 63.23  ? 338 ILE A CD1 1 
ATOM   2814  N N   . HIS A 1 339 ? -21.182 2.074   -45.688 1.00 54.04  ? 339 HIS A N   1 
ATOM   2815  C CA  . HIS A 1 339 ? -20.213 3.089   -46.063 1.00 55.06  ? 339 HIS A CA  1 
ATOM   2816  C C   . HIS A 1 339 ? -19.471 2.638   -47.274 1.00 55.38  ? 339 HIS A C   1 
ATOM   2817  O O   . HIS A 1 339 ? -19.237 1.439   -47.461 1.00 56.20  ? 339 HIS A O   1 
ATOM   2818  C CB  . HIS A 1 339 ? -19.240 3.387   -44.907 1.00 54.62  ? 339 HIS A CB  1 
ATOM   2819  C CG  . HIS A 1 339 ? -18.501 4.704   -45.056 1.00 53.00  ? 339 HIS A CG  1 
ATOM   2820  N ND1 . HIS A 1 339 ? -17.386 4.835   -45.822 1.00 52.10  ? 339 HIS A ND1 1 
ATOM   2821  C CD2 . HIS A 1 339 ? -18.764 5.971   -44.519 1.00 51.37  ? 339 HIS A CD2 1 
ATOM   2822  C CE1 . HIS A 1 339 ? -16.958 6.115   -45.771 1.00 52.13  ? 339 HIS A CE1 1 
ATOM   2823  N NE2 . HIS A 1 339 ? -17.804 6.809   -44.973 1.00 52.56  ? 339 HIS A NE2 1 
ATOM   2824  N N   . ARG A 1 340 ? -19.090 3.592   -48.118 1.00 57.26  ? 340 ARG A N   1 
ATOM   2825  C CA  . ARG A 1 340 ? -18.474 3.267   -49.399 1.00 58.35  ? 340 ARG A CA  1 
ATOM   2826  C C   . ARG A 1 340 ? -17.374 4.252   -49.790 1.00 56.98  ? 340 ARG A C   1 
ATOM   2827  O O   . ARG A 1 340 ? -17.368 5.402   -49.351 1.00 54.88  ? 340 ARG A O   1 
ATOM   2828  C CB  . ARG A 1 340 ? -19.549 3.182   -50.507 1.00 61.57  ? 340 ARG A CB  1 
ATOM   2829  C CG  . ARG A 1 340 ? -20.383 4.448   -50.672 1.00 64.54  ? 340 ARG A CG  1 
ATOM   2830  C CD  . ARG A 1 340 ? -21.433 4.304   -51.769 1.00 72.04  ? 340 ARG A CD  1 
ATOM   2831  N NE  . ARG A 1 340 ? -21.427 5.458   -52.671 1.00 72.55  ? 340 ARG A NE  1 
ATOM   2832  C CZ  . ARG A 1 340 ? -20.525 5.644   -53.630 1.00 73.16  ? 340 ARG A CZ  1 
ATOM   2833  N NH1 . ARG A 1 340 ? -19.569 4.741   -53.831 1.00 74.50  ? 340 ARG A NH1 1 
ATOM   2834  N NH2 . ARG A 1 340 ? -20.574 6.731   -54.390 1.00 74.26  ? 340 ARG A NH2 1 
ATOM   2835  N N   . THR A 1 341 ? -16.427 3.776   -50.593 1.00 58.27  ? 341 THR A N   1 
ATOM   2836  C CA  . THR A 1 341 ? -15.545 4.646   -51.354 1.00 61.58  ? 341 THR A CA  1 
ATOM   2837  C C   . THR A 1 341 ? -15.690 4.215   -52.801 1.00 68.09  ? 341 THR A C   1 
ATOM   2838  O O   . THR A 1 341 ? -16.546 3.389   -53.118 1.00 71.98  ? 341 THR A O   1 
ATOM   2839  C CB  . THR A 1 341 ? -14.063 4.508   -50.933 1.00 59.37  ? 341 THR A CB  1 
ATOM   2840  O OG1 . THR A 1 341 ? -13.602 3.185   -51.221 1.00 60.55  ? 341 THR A OG1 1 
ATOM   2841  C CG2 . THR A 1 341 ? -13.873 4.801   -49.450 1.00 56.92  ? 341 THR A CG2 1 
ATOM   2842  N N   . VAL A 1 342 ? -14.853 4.757   -53.681 1.00 72.64  ? 342 VAL A N   1 
ATOM   2843  C CA  . VAL A 1 342 ? -14.878 4.348   -55.087 1.00 77.25  ? 342 VAL A CA  1 
ATOM   2844  C C   . VAL A 1 342 ? -14.508 2.871   -55.255 1.00 79.59  ? 342 VAL A C   1 
ATOM   2845  O O   . VAL A 1 342 ? -15.011 2.196   -56.158 1.00 80.27  ? 342 VAL A O   1 
ATOM   2846  C CB  . VAL A 1 342 ? -13.977 5.237   -55.982 1.00 78.07  ? 342 VAL A CB  1 
ATOM   2847  C CG1 . VAL A 1 342 ? -14.768 6.434   -56.490 1.00 77.98  ? 342 VAL A CG1 1 
ATOM   2848  C CG2 . VAL A 1 342 ? -12.718 5.680   -55.238 1.00 74.07  ? 342 VAL A CG2 1 
ATOM   2849  N N   . ASP A 1 343 ? -13.645 2.375   -54.369 1.00 78.36  ? 343 ASP A N   1 
ATOM   2850  C CA  . ASP A 1 343 ? -13.173 0.990   -54.440 1.00 76.96  ? 343 ASP A CA  1 
ATOM   2851  C C   . ASP A 1 343 ? -13.949 0.045   -53.502 1.00 75.95  ? 343 ASP A C   1 
ATOM   2852  O O   . ASP A 1 343 ? -13.923 -1.175  -53.684 1.00 75.93  ? 343 ASP A O   1 
ATOM   2853  C CB  . ASP A 1 343 ? -11.664 0.902   -54.132 1.00 76.15  ? 343 ASP A CB  1 
ATOM   2854  C CG  . ASP A 1 343 ? -10.870 2.112   -54.643 1.00 77.27  ? 343 ASP A CG  1 
ATOM   2855  O OD1 . ASP A 1 343 ? -11.270 2.721   -55.658 1.00 79.63  ? 343 ASP A OD1 1 
ATOM   2856  O OD2 . ASP A 1 343 ? -9.830  2.443   -54.026 1.00 72.91  ? 343 ASP A OD2 1 
ATOM   2857  N N   . ASP A 1 344 ? -14.646 0.609   -52.515 1.00 72.98  ? 344 ASP A N   1 
ATOM   2858  C CA  . ASP A 1 344 ? -15.037 -0.156  -51.328 1.00 66.56  ? 344 ASP A CA  1 
ATOM   2859  C C   . ASP A 1 344 ? -16.489 -0.020  -50.967 1.00 64.80  ? 344 ASP A C   1 
ATOM   2860  O O   . ASP A 1 344 ? -17.037 1.075   -50.996 1.00 67.02  ? 344 ASP A O   1 
ATOM   2861  C CB  . ASP A 1 344 ? -14.226 0.301   -50.127 1.00 63.96  ? 344 ASP A CB  1 
ATOM   2862  C CG  . ASP A 1 344 ? -12.830 -0.228  -50.135 1.00 64.90  ? 344 ASP A CG  1 
ATOM   2863  O OD1 . ASP A 1 344 ? -12.649 -1.437  -50.397 1.00 64.51  ? 344 ASP A OD1 1 
ATOM   2864  O OD2 . ASP A 1 344 ? -11.908 0.568   -49.853 1.00 67.63  ? 344 ASP A OD2 1 
ATOM   2865  N N   . TYR A 1 345 ? -17.095 -1.138  -50.582 1.00 62.96  ? 345 TYR A N   1 
ATOM   2866  C CA  . TYR A 1 345 ? -18.369 -1.127  -49.881 1.00 62.43  ? 345 TYR A CA  1 
ATOM   2867  C C   . TYR A 1 345 ? -18.237 -1.883  -48.564 1.00 57.09  ? 345 TYR A C   1 
ATOM   2868  O O   . TYR A 1 345 ? -17.620 -2.946  -48.505 1.00 56.05  ? 345 TYR A O   1 
ATOM   2869  C CB  . TYR A 1 345 ? -19.461 -1.761  -50.743 1.00 69.75  ? 345 TYR A CB  1 
ATOM   2870  C CG  . TYR A 1 345 ? -20.318 -0.776  -51.515 1.00 74.40  ? 345 TYR A CG  1 
ATOM   2871  C CD1 . TYR A 1 345 ? -21.583 -0.409  -51.051 1.00 76.90  ? 345 TYR A CD1 1 
ATOM   2872  C CD2 . TYR A 1 345 ? -19.880 -0.233  -52.723 1.00 77.08  ? 345 TYR A CD2 1 
ATOM   2873  C CE1 . TYR A 1 345 ? -22.376 0.484   -51.758 1.00 79.70  ? 345 TYR A CE1 1 
ATOM   2874  C CE2 . TYR A 1 345 ? -20.667 0.662   -53.439 1.00 78.99  ? 345 TYR A CE2 1 
ATOM   2875  C CZ  . TYR A 1 345 ? -21.912 1.016   -52.953 1.00 80.70  ? 345 TYR A CZ  1 
ATOM   2876  O OH  . TYR A 1 345 ? -22.697 1.903   -53.662 1.00 84.97  ? 345 TYR A OH  1 
ATOM   2877  N N   . PHE A 1 346 ? -18.820 -1.331  -47.510 1.00 53.95  ? 346 PHE A N   1 
ATOM   2878  C CA  . PHE A 1 346 ? -18.754 -1.940  -46.187 1.00 51.45  ? 346 PHE A CA  1 
ATOM   2879  C C   . PHE A 1 346 ? -20.120 -1.883  -45.546 1.00 51.55  ? 346 PHE A C   1 
ATOM   2880  O O   . PHE A 1 346 ? -20.666 -0.803  -45.330 1.00 53.17  ? 346 PHE A O   1 
ATOM   2881  C CB  . PHE A 1 346 ? -17.711 -1.219  -45.316 1.00 49.83  ? 346 PHE A CB  1 
ATOM   2882  C CG  . PHE A 1 346 ? -17.496 -1.845  -43.955 1.00 47.95  ? 346 PHE A CG  1 
ATOM   2883  C CD1 . PHE A 1 346 ? -17.575 -3.225  -43.776 1.00 47.62  ? 346 PHE A CD1 1 
ATOM   2884  C CD2 . PHE A 1 346 ? -17.166 -1.048  -42.860 1.00 46.05  ? 346 PHE A CD2 1 
ATOM   2885  C CE1 . PHE A 1 346 ? -17.362 -3.792  -42.524 1.00 48.26  ? 346 PHE A CE1 1 
ATOM   2886  C CE2 . PHE A 1 346 ? -16.939 -1.609  -41.608 1.00 46.68  ? 346 PHE A CE2 1 
ATOM   2887  C CZ  . PHE A 1 346 ? -17.041 -2.981  -41.436 1.00 47.21  ? 346 PHE A CZ  1 
ATOM   2888  N N   . PHE A 1 347 ? -20.668 -3.053  -45.237 1.00 51.58  ? 347 PHE A N   1 
ATOM   2889  C CA  . PHE A 1 347 ? -22.060 -3.164  -44.822 1.00 52.23  ? 347 PHE A CA  1 
ATOM   2890  C C   . PHE A 1 347 ? -22.174 -4.060  -43.597 1.00 51.77  ? 347 PHE A C   1 
ATOM   2891  O O   . PHE A 1 347 ? -21.614 -5.155  -43.572 1.00 52.85  ? 347 PHE A O   1 
ATOM   2892  C CB  . PHE A 1 347 ? -22.912 -3.719  -45.992 1.00 54.21  ? 347 PHE A CB  1 
ATOM   2893  C CG  . PHE A 1 347 ? -24.364 -3.928  -45.650 1.00 55.50  ? 347 PHE A CG  1 
ATOM   2894  C CD1 . PHE A 1 347 ? -24.796 -5.120  -45.062 1.00 56.69  ? 347 PHE A CD1 1 
ATOM   2895  C CD2 . PHE A 1 347 ? -25.299 -2.940  -45.911 1.00 56.29  ? 347 PHE A CD2 1 
ATOM   2896  C CE1 . PHE A 1 347 ? -26.130 -5.316  -44.742 1.00 57.86  ? 347 PHE A CE1 1 
ATOM   2897  C CE2 . PHE A 1 347 ? -26.639 -3.136  -45.605 1.00 59.40  ? 347 PHE A CE2 1 
ATOM   2898  C CZ  . PHE A 1 347 ? -27.054 -4.325  -45.018 1.00 59.37  ? 347 PHE A CZ  1 
ATOM   2899  N N   . CYS A 1 348 ? -22.899 -3.592  -42.585 1.00 51.77  ? 348 CYS A N   1 
ATOM   2900  C CA  . CYS A 1 348 ? -23.124 -4.369  -41.371 1.00 52.71  ? 348 CYS A CA  1 
ATOM   2901  C C   . CYS A 1 348 ? -24.577 -4.297  -40.931 1.00 54.75  ? 348 CYS A C   1 
ATOM   2902  O O   . CYS A 1 348 ? -25.257 -3.293  -41.169 1.00 54.91  ? 348 CYS A O   1 
ATOM   2903  C CB  . CYS A 1 348 ? -22.230 -3.881  -40.227 1.00 51.27  ? 348 CYS A CB  1 
ATOM   2904  S SG  . CYS A 1 348 ? -20.474 -3.863  -40.629 1.00 51.04  ? 348 CYS A SG  1 
ATOM   2905  N N   . SER A 1 349 ? -25.033 -5.370  -40.282 1.00 54.66  ? 349 SER A N   1 
ATOM   2906  C CA  . SER A 1 349 ? -26.354 -5.449  -39.680 1.00 56.60  ? 349 SER A CA  1 
ATOM   2907  C C   . SER A 1 349 ? -26.348 -6.585  -38.669 1.00 57.63  ? 349 SER A C   1 
ATOM   2908  O O   . SER A 1 349 ? -25.610 -7.562  -38.838 1.00 57.06  ? 349 SER A O   1 
ATOM   2909  C CB  . SER A 1 349 ? -27.427 -5.715  -40.752 1.00 58.52  ? 349 SER A CB  1 
ATOM   2910  O OG  . SER A 1 349 ? -28.660 -6.119  -40.166 1.00 58.64  ? 349 SER A OG  1 
ATOM   2911  N N   . PRO A 1 350 ? -27.171 -6.468  -37.612 1.00 59.28  ? 350 PRO A N   1 
ATOM   2912  C CA  . PRO A 1 350 ? -27.366 -7.599  -36.696 1.00 61.33  ? 350 PRO A CA  1 
ATOM   2913  C C   . PRO A 1 350 ? -28.123 -8.753  -37.367 1.00 64.49  ? 350 PRO A C   1 
ATOM   2914  O O   . PRO A 1 350 ? -28.184 -9.853  -36.817 1.00 65.32  ? 350 PRO A O   1 
ATOM   2915  C CB  . PRO A 1 350 ? -28.208 -6.997  -35.566 1.00 60.64  ? 350 PRO A CB  1 
ATOM   2916  C CG  . PRO A 1 350 ? -28.891 -5.816  -36.178 1.00 59.77  ? 350 PRO A CG  1 
ATOM   2917  C CD  . PRO A 1 350 ? -27.935 -5.274  -37.197 1.00 59.26  ? 350 PRO A CD  1 
ATOM   2918  N N   . HIS A 1 351 ? -28.684 -8.490  -38.550 1.00 67.13  ? 351 HIS A N   1 
ATOM   2919  C CA  . HIS A 1 351 ? -29.461 -9.489  -39.296 1.00 68.96  ? 351 HIS A CA  1 
ATOM   2920  C C   . HIS A 1 351 ? -28.623 -10.126 -40.372 1.00 69.99  ? 351 HIS A C   1 
ATOM   2921  O O   . HIS A 1 351 ? -28.377 -9.520  -41.423 1.00 70.86  ? 351 HIS A O   1 
ATOM   2922  C CB  . HIS A 1 351 ? -30.741 -8.871  -39.870 1.00 69.45  ? 351 HIS A CB  1 
ATOM   2923  C CG  . HIS A 1 351 ? -31.584 -8.152  -38.836 1.00 70.01  ? 351 HIS A CG  1 
ATOM   2924  N ND1 . HIS A 1 351 ? -32.101 -8.779  -37.754 1.00 70.88  ? 351 HIS A ND1 1 
ATOM   2925  C CD2 . HIS A 1 351 ? -31.969 -6.814  -38.736 1.00 70.01  ? 351 HIS A CD2 1 
ATOM   2926  C CE1 . HIS A 1 351 ? -32.780 -7.889  -37.002 1.00 70.50  ? 351 HIS A CE1 1 
ATOM   2927  N NE2 . HIS A 1 351 ? -32.701 -6.688  -37.604 1.00 71.21  ? 351 HIS A NE2 1 
ATOM   2928  N N   . PRO A 1 352 ? -28.157 -11.364 -40.119 1.00 70.46  ? 352 PRO A N   1 
ATOM   2929  C CA  . PRO A 1 352 ? -27.190 -12.026 -40.997 1.00 69.55  ? 352 PRO A CA  1 
ATOM   2930  C C   . PRO A 1 352 ? -27.702 -12.148 -42.423 1.00 72.07  ? 352 PRO A C   1 
ATOM   2931  O O   . PRO A 1 352 ? -26.923 -11.999 -43.365 1.00 70.46  ? 352 PRO A O   1 
ATOM   2932  C CB  . PRO A 1 352 ? -27.029 -13.420 -40.372 1.00 70.49  ? 352 PRO A CB  1 
ATOM   2933  C CG  . PRO A 1 352 ? -27.554 -13.299 -38.981 1.00 70.43  ? 352 PRO A CG  1 
ATOM   2934  C CD  . PRO A 1 352 ? -28.617 -12.248 -39.033 1.00 70.79  ? 352 PRO A CD  1 
ATOM   2935  N N   . HIS A 1 353 ? -29.006 -12.397 -42.580 1.00 74.08  ? 353 HIS A N   1 
ATOM   2936  C CA  . HIS A 1 353 ? -29.591 -12.572 -43.910 1.00 77.01  ? 353 HIS A CA  1 
ATOM   2937  C C   . HIS A 1 353 ? -29.458 -11.334 -44.760 1.00 76.88  ? 353 HIS A C   1 
ATOM   2938  O O   . HIS A 1 353 ? -29.262 -11.433 -45.972 1.00 78.44  ? 353 HIS A O   1 
ATOM   2939  C CB  . HIS A 1 353 ? -31.043 -13.071 -43.837 1.00 78.66  ? 353 HIS A CB  1 
ATOM   2940  C CG  . HIS A 1 353 ? -32.061 -11.987 -43.545 1.00 80.30  ? 353 HIS A CG  1 
ATOM   2941  N ND1 . HIS A 1 353 ? -32.511 -11.727 -42.296 1.00 81.88  ? 353 HIS A ND1 1 
ATOM   2942  C CD2 . HIS A 1 353 ? -32.723 -11.097 -44.395 1.00 79.11  ? 353 HIS A CD2 1 
ATOM   2943  C CE1 . HIS A 1 353 ? -33.406 -10.721 -42.344 1.00 82.02  ? 353 HIS A CE1 1 
ATOM   2944  N NE2 . HIS A 1 353 ? -33.532 -10.335 -43.629 1.00 80.74  ? 353 HIS A NE2 1 
ATOM   2945  N N   . LYS A 1 354 ? -29.528 -10.158 -44.133 1.00 75.19  ? 354 LYS A N   1 
ATOM   2946  C CA  . LYS A 1 354 ? -29.320 -8.896  -44.855 1.00 75.89  ? 354 LYS A CA  1 
ATOM   2947  C C   . LYS A 1 354 ? -27.888 -8.764  -45.402 1.00 74.85  ? 354 LYS A C   1 
ATOM   2948  O O   . LYS A 1 354 ? -27.661 -8.094  -46.415 1.00 73.63  ? 354 LYS A O   1 
ATOM   2949  C CB  . LYS A 1 354 ? -29.653 -7.692  -43.973 1.00 75.76  ? 354 LYS A CB  1 
ATOM   2950  C CG  . LYS A 1 354 ? -31.126 -7.515  -43.665 1.00 76.25  ? 354 LYS A CG  1 
ATOM   2951  C CD  . LYS A 1 354 ? -31.384 -6.150  -43.050 1.00 76.98  ? 354 LYS A CD  1 
ATOM   2952  C CE  . LYS A 1 354 ? -32.443 -6.216  -41.960 1.00 80.30  ? 354 LYS A CE  1 
ATOM   2953  N NZ  . LYS A 1 354 ? -33.802 -6.523  -42.490 1.00 84.43  ? 354 LYS A NZ  1 
ATOM   2954  N N   . VAL A 1 355 ? -26.931 -9.405  -44.734 1.00 73.68  ? 355 VAL A N   1 
ATOM   2955  C CA  . VAL A 1 355 ? -25.539 -9.382  -45.192 1.00 73.48  ? 355 VAL A CA  1 
ATOM   2956  C C   . VAL A 1 355 ? -25.334 -10.284 -46.423 1.00 74.17  ? 355 VAL A C   1 
ATOM   2957  O O   . VAL A 1 355 ? -24.434 -10.044 -47.223 1.00 74.12  ? 355 VAL A O   1 
ATOM   2958  C CB  . VAL A 1 355 ? -24.539 -9.711  -44.055 1.00 70.02  ? 355 VAL A CB  1 
ATOM   2959  C CG1 . VAL A 1 355 ? -23.108 -9.538  -44.529 1.00 67.58  ? 355 VAL A CG1 1 
ATOM   2960  C CG2 . VAL A 1 355 ? -24.790 -8.811  -42.851 1.00 68.36  ? 355 VAL A CG2 1 
ATOM   2961  N N   . TYR A 1 356 ? -26.187 -11.299 -46.579 1.00 78.30  ? 356 TYR A N   1 
ATOM   2962  C CA  . TYR A 1 356 ? -26.252 -12.069 -47.833 1.00 80.31  ? 356 TYR A CA  1 
ATOM   2963  C C   . TYR A 1 356 ? -26.955 -11.269 -48.914 1.00 79.31  ? 356 TYR A C   1 
ATOM   2964  O O   . TYR A 1 356 ? -26.422 -11.096 -50.010 1.00 78.56  ? 356 TYR A O   1 
ATOM   2965  C CB  . TYR A 1 356 ? -26.971 -13.411 -47.644 1.00 85.83  ? 356 TYR A CB  1 
ATOM   2966  C CG  . TYR A 1 356 ? -26.287 -14.345 -46.680 1.00 90.01  ? 356 TYR A CG  1 
ATOM   2967  C CD1 . TYR A 1 356 ? -25.198 -15.121 -47.078 1.00 92.64  ? 356 TYR A CD1 1 
ATOM   2968  C CD2 . TYR A 1 356 ? -26.728 -14.452 -45.364 1.00 92.74  ? 356 TYR A CD2 1 
ATOM   2969  C CE1 . TYR A 1 356 ? -24.562 -15.974 -46.183 1.00 94.83  ? 356 TYR A CE1 1 
ATOM   2970  C CE2 . TYR A 1 356 ? -26.105 -15.301 -44.460 1.00 95.52  ? 356 TYR A CE2 1 
ATOM   2971  C CZ  . TYR A 1 356 ? -25.024 -16.061 -44.868 1.00 96.04  ? 356 TYR A CZ  1 
ATOM   2972  O OH  . TYR A 1 356 ? -24.413 -16.898 -43.955 1.00 95.52  ? 356 TYR A OH  1 
ATOM   2973  N N   . ASP A 1 357 ? -28.156 -10.781 -48.602 1.00 79.57  ? 357 ASP A N   1 
ATOM   2974  C CA  . ASP A 1 357 ? -28.914 -9.952  -49.542 1.00 79.95  ? 357 ASP A CA  1 
ATOM   2975  C C   . ASP A 1 357 ? -28.033 -8.829  -50.082 1.00 76.94  ? 357 ASP A C   1 
ATOM   2976  O O   . ASP A 1 357 ? -28.209 -8.389  -51.217 1.00 77.78  ? 357 ASP A O   1 
ATOM   2977  C CB  . ASP A 1 357 ? -30.185 -9.382  -48.893 1.00 81.20  ? 357 ASP A CB  1 
ATOM   2978  C CG  . ASP A 1 357 ? -31.147 -10.472 -48.412 1.00 82.97  ? 357 ASP A CG  1 
ATOM   2979  O OD1 . ASP A 1 357 ? -30.941 -11.655 -48.761 1.00 83.14  ? 357 ASP A OD1 1 
ATOM   2980  O OD2 . ASP A 1 357 ? -32.106 -10.142 -47.673 1.00 82.12  ? 357 ASP A OD2 1 
ATOM   2981  N N   . PHE A 1 358 ? -27.065 -8.391  -49.277 1.00 72.42  ? 358 PHE A N   1 
ATOM   2982  C CA  . PHE A 1 358 ? -26.109 -7.392  -49.735 1.00 68.83  ? 358 PHE A CA  1 
ATOM   2983  C C   . PHE A 1 358 ? -24.997 -7.976  -50.593 1.00 68.08  ? 358 PHE A C   1 
ATOM   2984  O O   . PHE A 1 358 ? -24.679 -7.423  -51.643 1.00 68.61  ? 358 PHE A O   1 
ATOM   2985  C CB  . PHE A 1 358 ? -25.506 -6.589  -48.584 1.00 66.03  ? 358 PHE A CB  1 
ATOM   2986  C CG  . PHE A 1 358 ? -24.671 -5.433  -49.051 1.00 62.64  ? 358 PHE A CG  1 
ATOM   2987  C CD1 . PHE A 1 358 ? -23.334 -5.610  -49.366 1.00 59.77  ? 358 PHE A CD1 1 
ATOM   2988  C CD2 . PHE A 1 358 ? -25.244 -4.186  -49.244 1.00 61.65  ? 358 PHE A CD2 1 
ATOM   2989  C CE1 . PHE A 1 358 ? -22.579 -4.556  -49.835 1.00 59.64  ? 358 PHE A CE1 1 
ATOM   2990  C CE2 . PHE A 1 358 ? -24.493 -3.126  -49.701 1.00 59.93  ? 358 PHE A CE2 1 
ATOM   2991  C CZ  . PHE A 1 358 ? -23.159 -3.311  -50.001 1.00 59.79  ? 358 PHE A CZ  1 
ATOM   2992  N N   . GLU A 1 359 ? -24.389 -9.073  -50.142 1.00 69.20  ? 359 GLU A N   1 
ATOM   2993  C CA  . GLU A 1 359 ? -23.347 -9.724  -50.936 1.00 73.06  ? 359 GLU A CA  1 
ATOM   2994  C C   . GLU A 1 359 ? -23.839 -10.082 -52.345 1.00 75.58  ? 359 GLU A C   1 
ATOM   2995  O O   . GLU A 1 359 ? -23.201 -9.720  -53.339 1.00 77.02  ? 359 GLU A O   1 
ATOM   2996  C CB  . GLU A 1 359 ? -22.780 -10.963 -50.237 1.00 74.08  ? 359 GLU A CB  1 
ATOM   2997  C CG  . GLU A 1 359 ? -21.585 -11.562 -50.980 1.00 75.70  ? 359 GLU A CG  1 
ATOM   2998  C CD  . GLU A 1 359 ? -20.953 -12.747 -50.270 1.00 78.10  ? 359 GLU A CD  1 
ATOM   2999  O OE1 . GLU A 1 359 ? -21.631 -13.382 -49.429 1.00 80.04  ? 359 GLU A OE1 1 
ATOM   3000  O OE2 . GLU A 1 359 ? -19.770 -13.046 -50.563 1.00 79.27  ? 359 GLU A OE2 1 
ATOM   3001  N N   . LEU A 1 360 ? -24.970 -10.782 -52.424 1.00 78.06  ? 360 LEU A N   1 
ATOM   3002  C CA  . LEU A 1 360 ? -25.534 -11.182 -53.716 1.00 81.43  ? 360 LEU A CA  1 
ATOM   3003  C C   . LEU A 1 360 ? -25.855 -9.967  -54.590 1.00 79.48  ? 360 LEU A C   1 
ATOM   3004  O O   . LEU A 1 360 ? -25.466 -9.923  -55.749 1.00 79.76  ? 360 LEU A O   1 
ATOM   3005  C CB  . LEU A 1 360 ? -26.773 -12.067 -53.530 1.00 86.42  ? 360 LEU A CB  1 
ATOM   3006  C CG  . LEU A 1 360 ? -26.569 -13.563 -53.239 1.00 88.49  ? 360 LEU A CG  1 
ATOM   3007  C CD1 . LEU A 1 360 ? -26.008 -13.811 -51.844 1.00 87.96  ? 360 LEU A CD1 1 
ATOM   3008  C CD2 . LEU A 1 360 ? -27.882 -14.305 -53.405 1.00 91.20  ? 360 LEU A CD2 1 
ATOM   3009  N N   . LEU A 1 361 ? -26.529 -8.973  -54.012 1.00 78.66  ? 361 LEU A N   1 
ATOM   3010  C CA  . LEU A 1 361 ? -26.869 -7.737  -54.727 1.00 77.48  ? 361 LEU A CA  1 
ATOM   3011  C C   . LEU A 1 361 ? -25.649 -7.026  -55.320 1.00 77.72  ? 361 LEU A C   1 
ATOM   3012  O O   . LEU A 1 361 ? -25.670 -6.630  -56.489 1.00 78.68  ? 361 LEU A O   1 
ATOM   3013  C CB  . LEU A 1 361 ? -27.646 -6.780  -53.811 1.00 77.40  ? 361 LEU A CB  1 
ATOM   3014  C CG  . LEU A 1 361 ? -27.748 -5.291  -54.179 1.00 77.73  ? 361 LEU A CG  1 
ATOM   3015  C CD1 . LEU A 1 361 ? -28.486 -5.079  -55.493 1.00 79.87  ? 361 LEU A CD1 1 
ATOM   3016  C CD2 . LEU A 1 361 ? -28.424 -4.509  -53.063 1.00 77.02  ? 361 LEU A CD2 1 
ATOM   3017  N N   . ILE A 1 362 ? -24.597 -6.860  -54.513 1.00 74.89  ? 362 ILE A N   1 
ATOM   3018  C CA  . ILE A 1 362 ? -23.428 -6.088  -54.920 1.00 72.89  ? 362 ILE A CA  1 
ATOM   3019  C C   . ILE A 1 362 ? -22.663 -6.800  -56.031 1.00 73.05  ? 362 ILE A C   1 
ATOM   3020  O O   . ILE A 1 362 ? -22.027 -6.158  -56.863 1.00 73.37  ? 362 ILE A O   1 
ATOM   3021  C CB  . ILE A 1 362 ? -22.502 -5.757  -53.705 1.00 73.25  ? 362 ILE A CB  1 
ATOM   3022  C CG1 . ILE A 1 362 ? -21.899 -4.346  -53.823 1.00 71.61  ? 362 ILE A CG1 1 
ATOM   3023  C CG2 . ILE A 1 362 ? -21.433 -6.828  -53.494 1.00 71.42  ? 362 ILE A CG2 1 
ATOM   3024  C CD1 . ILE A 1 362 ? -20.504 -4.294  -54.406 1.00 71.05  ? 362 ILE A CD1 1 
ATOM   3025  N N   . LYS A 1 363 ? -22.736 -8.129  -56.044 1.00 75.01  ? 363 LYS A N   1 
ATOM   3026  C CA  . LYS A 1 363 ? -22.134 -8.920  -57.117 1.00 79.59  ? 363 LYS A CA  1 
ATOM   3027  C C   . LYS A 1 363 ? -22.890 -8.751  -58.429 1.00 81.85  ? 363 LYS A C   1 
ATOM   3028  O O   . LYS A 1 363 ? -22.303 -8.852  -59.510 1.00 85.78  ? 363 LYS A O   1 
ATOM   3029  C CB  . LYS A 1 363 ? -22.070 -10.398 -56.734 1.00 81.85  ? 363 LYS A CB  1 
ATOM   3030  C CG  . LYS A 1 363 ? -20.743 -10.821 -56.130 1.00 83.88  ? 363 LYS A CG  1 
ATOM   3031  C CD  . LYS A 1 363 ? -20.870 -12.151 -55.408 1.00 85.87  ? 363 LYS A CD  1 
ATOM   3032  C CE  . LYS A 1 363 ? -19.531 -12.602 -54.853 1.00 85.48  ? 363 LYS A CE  1 
ATOM   3033  N NZ  . LYS A 1 363 ? -19.713 -13.519 -53.693 1.00 86.56  ? 363 LYS A NZ  1 
ATOM   3034  N N   . GLY A 1 364 ? -24.196 -8.504  -58.326 1.00 83.52  ? 364 GLY A N   1 
ATOM   3035  C CA  . GLY A 1 364 ? -25.039 -8.250  -59.494 1.00 83.63  ? 364 GLY A CA  1 
ATOM   3036  C C   . GLY A 1 364 ? -24.762 -6.897  -60.125 1.00 83.78  ? 364 GLY A C   1 
ATOM   3037  O O   . GLY A 1 364 ? -24.817 -6.752  -61.346 1.00 86.67  ? 364 GLY A O   1 
ATOM   3038  N N   . VAL A 1 365 ? -24.453 -5.906  -59.291 1.00 80.12  ? 365 VAL A N   1 
ATOM   3039  C CA  . VAL A 1 365 ? -24.166 -4.554  -59.768 1.00 79.46  ? 365 VAL A CA  1 
ATOM   3040  C C   . VAL A 1 365 ? -22.759 -4.443  -60.360 1.00 80.77  ? 365 VAL A C   1 
ATOM   3041  O O   . VAL A 1 365 ? -22.583 -3.939  -61.468 1.00 85.09  ? 365 VAL A O   1 
ATOM   3042  C CB  . VAL A 1 365 ? -24.342 -3.507  -58.645 1.00 76.11  ? 365 VAL A CB  1 
ATOM   3043  C CG1 . VAL A 1 365 ? -24.014 -2.106  -59.149 1.00 74.10  ? 365 VAL A CG1 1 
ATOM   3044  C CG2 . VAL A 1 365 ? -25.757 -3.562  -58.093 1.00 75.52  ? 365 VAL A CG2 1 
ATOM   3045  N N   . TYR A 1 366 ? -21.765 -4.926  -59.618 1.00 81.01  ? 366 TYR A N   1 
ATOM   3046  C CA  . TYR A 1 366 ? -20.359 -4.691  -59.952 1.00 79.09  ? 366 TYR A CA  1 
ATOM   3047  C C   . TYR A 1 366 ? -19.595 -5.988  -60.224 1.00 78.91  ? 366 TYR A C   1 
ATOM   3048  O O   . TYR A 1 366 ? -20.035 -7.077  -59.845 1.00 77.34  ? 366 TYR A O   1 
ATOM   3049  C CB  . TYR A 1 366 ? -19.659 -3.939  -58.809 1.00 76.25  ? 366 TYR A CB  1 
ATOM   3050  C CG  . TYR A 1 366 ? -20.199 -2.553  -58.488 1.00 75.99  ? 366 TYR A CG  1 
ATOM   3051  C CD1 . TYR A 1 366 ? -20.020 -1.488  -59.369 1.00 74.59  ? 366 TYR A CD1 1 
ATOM   3052  C CD2 . TYR A 1 366 ? -20.838 -2.296  -57.270 1.00 74.27  ? 366 TYR A CD2 1 
ATOM   3053  C CE1 . TYR A 1 366 ? -20.495 -0.219  -59.063 1.00 74.27  ? 366 TYR A CE1 1 
ATOM   3054  C CE2 . TYR A 1 366 ? -21.307 -1.027  -56.957 1.00 72.86  ? 366 TYR A CE2 1 
ATOM   3055  C CZ  . TYR A 1 366 ? -21.132 0.005   -57.858 1.00 72.91  ? 366 TYR A CZ  1 
ATOM   3056  O OH  . TYR A 1 366 ? -21.591 1.265   -57.558 1.00 74.17  ? 366 TYR A OH  1 
ATOM   3057  N N   . GLN A 1 367 ? -18.445 -5.860  -60.881 1.00 80.66  ? 367 GLN A N   1 
ATOM   3058  C CA  . GLN A 1 367 ? -17.435 -6.909  -60.852 1.00 83.77  ? 367 GLN A CA  1 
ATOM   3059  C C   . GLN A 1 367 ? -16.591 -6.695  -59.603 1.00 84.80  ? 367 GLN A C   1 
ATOM   3060  O O   . GLN A 1 367 ? -16.082 -5.591  -59.368 1.00 85.35  ? 367 GLN A O   1 
ATOM   3061  C CB  . GLN A 1 367 ? -16.555 -6.861  -62.101 1.00 84.46  ? 367 GLN A CB  1 
ATOM   3062  C CG  . GLN A 1 367 ? -16.174 -8.232  -62.650 1.00 87.20  ? 367 GLN A CG  1 
ATOM   3063  C CD  . GLN A 1 367 ? -17.267 -8.847  -63.522 1.00 89.68  ? 367 GLN A CD  1 
ATOM   3064  O OE1 . GLN A 1 367 ? -18.350 -9.187  -63.039 1.00 89.73  ? 367 GLN A OE1 1 
ATOM   3065  N NE2 . GLN A 1 367 ? -16.981 -8.998  -64.812 1.00 87.57  ? 367 GLN A NE2 1 
ATOM   3066  N N   . VAL A 1 368 ? -16.469 -7.739  -58.786 1.00 85.05  ? 368 VAL A N   1 
ATOM   3067  C CA  . VAL A 1 368 ? -15.814 -7.623  -57.481 1.00 82.52  ? 368 VAL A CA  1 
ATOM   3068  C C   . VAL A 1 368 ? -14.745 -8.696  -57.263 1.00 83.77  ? 368 VAL A C   1 
ATOM   3069  O O   . VAL A 1 368 ? -14.916 -9.839  -57.680 1.00 86.97  ? 368 VAL A O   1 
ATOM   3070  C CB  . VAL A 1 368 ? -16.841 -7.654  -56.323 1.00 78.60  ? 368 VAL A CB  1 
ATOM   3071  C CG1 . VAL A 1 368 ? -17.880 -6.557  -56.499 1.00 77.66  ? 368 VAL A CG1 1 
ATOM   3072  C CG2 . VAL A 1 368 ? -17.508 -9.016  -56.214 1.00 78.37  ? 368 VAL A CG2 1 
ATOM   3073  N N   . ASN A 1 369 ? -13.647 -8.321  -56.611 1.00 82.49  ? 369 ASN A N   1 
ATOM   3074  C CA  . ASN A 1 369 ? -12.590 -9.278  -56.266 1.00 84.73  ? 369 ASN A CA  1 
ATOM   3075  C C   . ASN A 1 369 ? -13.025 -10.208 -55.132 1.00 85.09  ? 369 ASN A C   1 
ATOM   3076  O O   . ASN A 1 369 ? -12.890 -9.855  -53.962 1.00 81.18  ? 369 ASN A O   1 
ATOM   3077  C CB  . ASN A 1 369 ? -11.304 -8.548  -55.863 1.00 83.36  ? 369 ASN A CB  1 
ATOM   3078  C CG  . ASN A 1 369 ? -10.804 -7.601  -56.935 1.00 85.70  ? 369 ASN A CG  1 
ATOM   3079  O OD1 . ASN A 1 369 ? -11.026 -7.820  -58.125 1.00 88.57  ? 369 ASN A OD1 1 
ATOM   3080  N ND2 . ASN A 1 369 ? -10.115 -6.541  -56.515 1.00 83.76  ? 369 ASN A ND2 1 
ATOM   3081  N N   . PRO A 1 370 ? -13.528 -11.414 -55.476 1.00 88.06  ? 370 PRO A N   1 
ATOM   3082  C CA  . PRO A 1 370 ? -14.182 -12.277 -54.484 1.00 88.43  ? 370 PRO A CA  1 
ATOM   3083  C C   . PRO A 1 370 ? -13.221 -12.913 -53.465 1.00 87.32  ? 370 PRO A C   1 
ATOM   3084  O O   . PRO A 1 370 ? -13.667 -13.373 -52.408 1.00 90.22  ? 370 PRO A O   1 
ATOM   3085  C CB  . PRO A 1 370 ? -14.851 -13.350 -55.344 1.00 87.90  ? 370 PRO A CB  1 
ATOM   3086  C CG  . PRO A 1 370 ? -13.982 -13.447 -56.551 1.00 87.72  ? 370 PRO A CG  1 
ATOM   3087  C CD  . PRO A 1 370 ? -13.400 -12.081 -56.788 1.00 86.60  ? 370 PRO A CD  1 
ATOM   3088  N N   . THR A 1 371 ? -11.925 -12.936 -53.777 1.00 84.13  ? 371 THR A N   1 
ATOM   3089  C CA  . THR A 1 371 ? -10.915 -13.412 -52.828 1.00 81.37  ? 371 THR A CA  1 
ATOM   3090  C C   . THR A 1 371 ? -10.583 -12.317 -51.816 1.00 80.79  ? 371 THR A C   1 
ATOM   3091  O O   . THR A 1 371 ? -10.090 -12.600 -50.720 1.00 80.80  ? 371 THR A O   1 
ATOM   3092  C CB  . THR A 1 371 ? -9.608  -13.861 -53.527 1.00 82.33  ? 371 THR A CB  1 
ATOM   3093  O OG1 . THR A 1 371 ? -8.791  -12.716 -53.823 1.00 80.06  ? 371 THR A OG1 1 
ATOM   3094  C CG2 . THR A 1 371 ? -9.904  -14.644 -54.813 1.00 81.34  ? 371 THR A CG2 1 
ATOM   3095  N N   . LYS A 1 372 ? -10.852 -11.068 -52.195 1.00 78.64  ? 372 LYS A N   1 
ATOM   3096  C CA  . LYS A 1 372 ? -10.584 -9.919  -51.335 1.00 75.42  ? 372 LYS A CA  1 
ATOM   3097  C C   . LYS A 1 372 ? -11.790 -9.549  -50.468 1.00 70.96  ? 372 LYS A C   1 
ATOM   3098  O O   . LYS A 1 372 ? -11.771 -8.543  -49.747 1.00 69.43  ? 372 LYS A O   1 
ATOM   3099  C CB  . LYS A 1 372 ? -10.104 -8.715  -52.158 1.00 80.38  ? 372 LYS A CB  1 
ATOM   3100  C CG  . LYS A 1 372 ? -8.617  -8.749  -52.497 1.00 83.04  ? 372 LYS A CG  1 
ATOM   3101  C CD  . LYS A 1 372 ? -7.979  -7.378  -52.337 1.00 83.33  ? 372 LYS A CD  1 
ATOM   3102  C CE  . LYS A 1 372 ? -6.504  -7.500  -51.989 1.00 85.35  ? 372 LYS A CE  1 
ATOM   3103  N NZ  . LYS A 1 372 ? -5.962  -6.251  -51.382 1.00 82.87  ? 372 LYS A NZ  1 
ATOM   3104  N N   . THR A 1 373 ? -12.828 -10.374 -50.526 1.00 65.81  ? 373 THR A N   1 
ATOM   3105  C CA  . THR A 1 373 ? -13.980 -10.188 -49.663 1.00 65.08  ? 373 THR A CA  1 
ATOM   3106  C C   . THR A 1 373 ? -13.669 -10.631 -48.235 1.00 63.49  ? 373 THR A C   1 
ATOM   3107  O O   . THR A 1 373 ? -13.040 -11.669 -48.024 1.00 65.59  ? 373 THR A O   1 
ATOM   3108  C CB  . THR A 1 373 ? -15.199 -10.949 -50.191 1.00 63.65  ? 373 THR A CB  1 
ATOM   3109  O OG1 . THR A 1 373 ? -15.501 -10.486 -51.509 1.00 63.48  ? 373 THR A OG1 1 
ATOM   3110  C CG2 . THR A 1 373 ? -16.390 -10.710 -49.298 1.00 61.71  ? 373 THR A CG2 1 
ATOM   3111  N N   . ARG A 1 374 ? -14.095 -9.824  -47.264 1.00 59.42  ? 374 ARG A N   1 
ATOM   3112  C CA  . ARG A 1 374 ? -13.934 -10.155 -45.852 1.00 58.20  ? 374 ARG A CA  1 
ATOM   3113  C C   . ARG A 1 374 ? -15.271 -10.087 -45.129 1.00 56.86  ? 374 ARG A C   1 
ATOM   3114  O O   . ARG A 1 374 ? -15.968 -9.072  -45.189 1.00 56.57  ? 374 ARG A O   1 
ATOM   3115  C CB  . ARG A 1 374 ? -12.921 -9.217  -45.177 1.00 58.46  ? 374 ARG A CB  1 
ATOM   3116  C CG  . ARG A 1 374 ? -11.521 -9.254  -45.780 1.00 59.37  ? 374 ARG A CG  1 
ATOM   3117  C CD  . ARG A 1 374 ? -10.868 -10.620 -45.612 1.00 61.16  ? 374 ARG A CD  1 
ATOM   3118  N NE  . ARG A 1 374 ? -9.474  -10.624 -46.058 1.00 62.07  ? 374 ARG A NE  1 
ATOM   3119  C CZ  . ARG A 1 374 ? -9.069  -10.972 -47.280 1.00 62.26  ? 374 ARG A CZ  1 
ATOM   3120  N NH1 . ARG A 1 374 ? -9.946  -11.353 -48.198 1.00 61.99  ? 374 ARG A NH1 1 
ATOM   3121  N NH2 . ARG A 1 374 ? -7.779  -10.937 -47.583 1.00 61.91  ? 374 ARG A NH2 1 
ATOM   3122  N N   . THR A 1 375 ? -15.616 -11.172 -44.440 1.00 56.04  ? 375 THR A N   1 
ATOM   3123  C CA  . THR A 1 375 ? -16.907 -11.295 -43.762 1.00 56.59  ? 375 THR A CA  1 
ATOM   3124  C C   . THR A 1 375 ? -16.787 -12.232 -42.567 1.00 56.82  ? 375 THR A C   1 
ATOM   3125  O O   . THR A 1 375 ? -15.860 -13.036 -42.503 1.00 55.92  ? 375 THR A O   1 
ATOM   3126  C CB  . THR A 1 375 ? -18.002 -11.829 -44.720 1.00 58.13  ? 375 THR A CB  1 
ATOM   3127  O OG1 . THR A 1 375 ? -19.222 -12.016 -43.997 1.00 58.85  ? 375 THR A OG1 1 
ATOM   3128  C CG2 . THR A 1 375 ? -17.585 -13.156 -45.335 1.00 58.81  ? 375 THR A CG2 1 
ATOM   3129  N N   . ASN A 1 376 ? -17.722 -12.117 -41.621 1.00 57.99  ? 376 ASN A N   1 
ATOM   3130  C CA  . ASN A 1 376 ? -17.808 -13.056 -40.495 1.00 59.53  ? 376 ASN A CA  1 
ATOM   3131  C C   . ASN A 1 376 ? -18.972 -14.049 -40.628 1.00 62.72  ? 376 ASN A C   1 
ATOM   3132  O O   . ASN A 1 376 ? -19.292 -14.771 -39.675 1.00 64.87  ? 376 ASN A O   1 
ATOM   3133  C CB  . ASN A 1 376 ? -17.900 -12.310 -39.158 1.00 57.55  ? 376 ASN A CB  1 
ATOM   3134  C CG  . ASN A 1 376 ? -19.146 -11.444 -39.051 1.00 56.97  ? 376 ASN A CG  1 
ATOM   3135  O OD1 . ASN A 1 376 ? -19.678 -10.969 -40.059 1.00 57.76  ? 376 ASN A OD1 1 
ATOM   3136  N ND2 . ASN A 1 376 ? -19.600 -11.209 -37.823 1.00 55.20  ? 376 ASN A ND2 1 
ATOM   3137  N N   . LEU A 1 377 ? -19.607 -14.067 -41.801 1.00 65.32  ? 377 LEU A N   1 
ATOM   3138  C CA  . LEU A 1 377 ? -20.704 -15.006 -42.083 1.00 68.02  ? 377 LEU A CA  1 
ATOM   3139  C C   . LEU A 1 377 ? -20.223 -16.458 -42.018 1.00 69.86  ? 377 LEU A C   1 
ATOM   3140  O O   . LEU A 1 377 ? -19.263 -16.826 -42.700 1.00 69.00  ? 377 LEU A O   1 
ATOM   3141  C CB  . LEU A 1 377 ? -21.333 -14.712 -43.449 1.00 66.48  ? 377 LEU A CB  1 
ATOM   3142  C CG  . LEU A 1 377 ? -22.166 -13.434 -43.565 1.00 65.53  ? 377 LEU A CG  1 
ATOM   3143  C CD1 . LEU A 1 377 ? -22.390 -13.076 -45.022 1.00 64.41  ? 377 LEU A CD1 1 
ATOM   3144  C CD2 . LEU A 1 377 ? -23.488 -13.556 -42.820 1.00 66.18  ? 377 LEU A CD2 1 
ATOM   3145  N N   . PRO A 1 378 ? -20.891 -17.287 -41.191 1.00 73.30  ? 378 PRO A N   1 
ATOM   3146  C CA  . PRO A 1 378 ? -20.436 -18.658 -40.932 1.00 76.41  ? 378 PRO A CA  1 
ATOM   3147  C C   . PRO A 1 378 ? -20.505 -19.591 -42.148 1.00 80.05  ? 378 PRO A C   1 
ATOM   3148  O O   . PRO A 1 378 ? -19.868 -20.647 -42.140 1.00 82.02  ? 378 PRO A O   1 
ATOM   3149  C CB  . PRO A 1 378 ? -21.385 -19.141 -39.824 1.00 77.05  ? 378 PRO A CB  1 
ATOM   3150  C CG  . PRO A 1 378 ? -21.920 -17.891 -39.203 1.00 75.90  ? 378 PRO A CG  1 
ATOM   3151  C CD  . PRO A 1 378 ? -22.045 -16.931 -40.349 1.00 75.22  ? 378 PRO A CD  1 
ATOM   3152  N N   . THR A 1 379 ? -21.249 -19.197 -43.183 1.00 81.92  ? 379 THR A N   1 
ATOM   3153  C CA  . THR A 1 379 ? -21.386 -20.021 -44.390 1.00 85.84  ? 379 THR A CA  1 
ATOM   3154  C C   . THR A 1 379 ? -20.180 -19.934 -45.323 1.00 83.99  ? 379 THR A C   1 
ATOM   3155  O O   . THR A 1 379 ? -20.008 -20.788 -46.196 1.00 84.42  ? 379 THR A O   1 
ATOM   3156  C CB  . THR A 1 379 ? -22.657 -19.675 -45.192 1.00 88.73  ? 379 THR A CB  1 
ATOM   3157  O OG1 . THR A 1 379 ? -22.655 -18.277 -45.516 1.00 88.77  ? 379 THR A OG1 1 
ATOM   3158  C CG2 . THR A 1 379 ? -23.918 -20.035 -44.394 1.00 88.94  ? 379 THR A CG2 1 
ATOM   3159  N N   . HIS A 1 380 ? -19.360 -18.900 -45.145 1.00 82.59  ? 380 HIS A N   1 
ATOM   3160  C CA  . HIS A 1 380 ? -18.153 -18.716 -45.961 1.00 83.75  ? 380 HIS A CA  1 
ATOM   3161  C C   . HIS A 1 380 ? -17.076 -19.694 -45.597 1.00 83.78  ? 380 HIS A C   1 
ATOM   3162  O O   . HIS A 1 380 ? -17.094 -20.278 -44.508 1.00 83.75  ? 380 HIS A O   1 
ATOM   3163  C CB  . HIS A 1 380 ? -17.626 -17.291 -45.832 1.00 83.62  ? 380 HIS A CB  1 
ATOM   3164  C CG  . HIS A 1 380 ? -18.274 -16.312 -46.782 1.00 85.92  ? 380 HIS A CG  1 
ATOM   3165  N ND1 . HIS A 1 380 ? -17.587 -15.692 -47.764 1.00 85.58  ? 380 HIS A ND1 1 
ATOM   3166  C CD2 . HIS A 1 380 ? -19.592 -15.852 -46.871 1.00 86.02  ? 380 HIS A CD2 1 
ATOM   3167  C CE1 . HIS A 1 380 ? -18.420 -14.882 -48.449 1.00 86.38  ? 380 HIS A CE1 1 
ATOM   3168  N NE2 . HIS A 1 380 ? -19.645 -14.980 -47.901 1.00 86.44  ? 380 HIS A NE2 1 
ATOM   3169  N N   . ARG A 1 381 ? -16.131 -19.885 -46.517 1.00 86.39  ? 381 ARG A N   1 
ATOM   3170  C CA  . ARG A 1 381 ? -14.976 -20.755 -46.293 1.00 88.94  ? 381 ARG A CA  1 
ATOM   3171  C C   . ARG A 1 381 ? -14.282 -20.381 -44.992 1.00 89.19  ? 381 ARG A C   1 
ATOM   3172  O O   . ARG A 1 381 ? -14.241 -21.175 -44.046 1.00 87.87  ? 381 ARG A O   1 
ATOM   3173  C CB  . ARG A 1 381 ? -13.982 -20.637 -47.454 1.00 91.21  ? 381 ARG A CB  1 
ATOM   3174  C CG  . ARG A 1 381 ? -14.438 -21.269 -48.760 1.00 96.64  ? 381 ARG A CG  1 
ATOM   3175  C CD  . ARG A 1 381 ? -13.829 -20.540 -49.950 1.00 97.37  ? 381 ARG A CD  1 
ATOM   3176  N NE  . ARG A 1 381 ? -13.874 -21.328 -51.181 1.00 101.97 ? 381 ARG A NE  1 
ATOM   3177  C CZ  . ARG A 1 381 ? -14.936 -21.431 -51.980 1.00 104.59 ? 381 ARG A CZ  1 
ATOM   3178  N NH1 . ARG A 1 381 ? -16.071 -20.809 -51.678 1.00 104.90 ? 381 ARG A NH1 1 
ATOM   3179  N NH2 . ARG A 1 381 ? -14.865 -22.169 -53.083 1.00 104.36 ? 381 ARG A NH2 1 
ATOM   3180  N N   . HIS A 1 382 ? -13.761 -19.154 -44.948 1.00 88.36  ? 382 HIS A N   1 
ATOM   3181  C CA  . HIS A 1 382 ? -13.005 -18.665 -43.801 1.00 85.62  ? 382 HIS A CA  1 
ATOM   3182  C C   . HIS A 1 382 ? -13.575 -17.372 -43.270 1.00 80.97  ? 382 HIS A C   1 
ATOM   3183  O O   . HIS A 1 382 ? -13.085 -16.284 -43.607 1.00 76.52  ? 382 HIS A O   1 
ATOM   3184  C CB  . HIS A 1 382 ? -11.529 -18.505 -44.165 1.00 89.31  ? 382 HIS A CB  1 
ATOM   3185  C CG  . HIS A 1 382 ? -10.904 -19.756 -44.744 1.00 95.97  ? 382 HIS A CG  1 
ATOM   3186  N ND1 . HIS A 1 382 ? -10.627 -19.890 -46.059 1.00 98.55  ? 382 HIS A ND1 1 
ATOM   3187  C CD2 . HIS A 1 382 ? -10.517 -20.953 -44.139 1.00 97.69  ? 382 HIS A CD2 1 
ATOM   3188  C CE1 . HIS A 1 382 ? -10.086 -21.102 -46.283 1.00 98.51  ? 382 HIS A CE1 1 
ATOM   3189  N NE2 . HIS A 1 382 ? -10.019 -21.752 -45.109 1.00 100.85 ? 382 HIS A NE2 1 
ATOM   3190  N N   . PRO A 1 383 ? -14.633 -17.471 -42.436 1.00 78.21  ? 383 PRO A N   1 
ATOM   3191  C CA  . PRO A 1 383 ? -15.223 -16.305 -41.771 1.00 77.03  ? 383 PRO A CA  1 
ATOM   3192  C C   . PRO A 1 383 ? -14.228 -15.594 -40.849 1.00 74.68  ? 383 PRO A C   1 
ATOM   3193  O O   . PRO A 1 383 ? -13.337 -16.233 -40.281 1.00 74.03  ? 383 PRO A O   1 
ATOM   3194  C CB  . PRO A 1 383 ? -16.376 -16.905 -40.954 1.00 78.20  ? 383 PRO A CB  1 
ATOM   3195  C CG  . PRO A 1 383 ? -16.053 -18.355 -40.823 1.00 78.77  ? 383 PRO A CG  1 
ATOM   3196  C CD  . PRO A 1 383 ? -15.347 -18.713 -42.093 1.00 78.77  ? 383 PRO A CD  1 
ATOM   3197  N N   . GLN A 1 384 ? -14.408 -14.283 -40.693 1.00 72.84  ? 384 GLN A N   1 
ATOM   3198  C CA  . GLN A 1 384 ? -13.414 -13.422 -40.063 1.00 69.04  ? 384 GLN A CA  1 
ATOM   3199  C C   . GLN A 1 384 ? -14.083 -12.300 -39.280 1.00 66.07  ? 384 GLN A C   1 
ATOM   3200  O O   . GLN A 1 384 ? -14.933 -11.593 -39.813 1.00 65.97  ? 384 GLN A O   1 
ATOM   3201  C CB  . GLN A 1 384 ? -12.520 -12.817 -41.137 1.00 68.35  ? 384 GLN A CB  1 
ATOM   3202  C CG  . GLN A 1 384 ? -11.054 -12.812 -40.779 1.00 72.18  ? 384 GLN A CG  1 
ATOM   3203  C CD  . GLN A 1 384 ? -10.186 -12.315 -41.916 1.00 72.73  ? 384 GLN A CD  1 
ATOM   3204  O OE1 . GLN A 1 384 ? -9.453  -13.087 -42.530 1.00 74.43  ? 384 GLN A OE1 1 
ATOM   3205  N NE2 . GLN A 1 384 ? -10.267 -11.017 -42.204 1.00 71.41  ? 384 GLN A NE2 1 
ATOM   3206  N N   . ASP A 1 385 ? -13.677 -12.122 -38.025 1.00 64.19  ? 385 ASP A N   1 
ATOM   3207  C CA  . ASP A 1 385 ? -14.214 -11.047 -37.181 1.00 62.22  ? 385 ASP A CA  1 
ATOM   3208  C C   . ASP A 1 385 ? -13.675 -9.655  -37.533 1.00 58.84  ? 385 ASP A C   1 
ATOM   3209  O O   . ASP A 1 385 ? -14.374 -8.648  -37.381 1.00 57.29  ? 385 ASP A O   1 
ATOM   3210  C CB  . ASP A 1 385 ? -13.959 -11.348 -35.706 1.00 62.96  ? 385 ASP A CB  1 
ATOM   3211  C CG  . ASP A 1 385 ? -15.041 -12.209 -35.094 1.00 65.33  ? 385 ASP A CG  1 
ATOM   3212  O OD1 . ASP A 1 385 ? -16.028 -12.527 -35.798 1.00 67.55  ? 385 ASP A OD1 1 
ATOM   3213  O OD2 . ASP A 1 385 ? -14.911 -12.557 -33.904 1.00 65.78  ? 385 ASP A OD2 1 
ATOM   3214  N N   . GLU A 1 386 ? -12.438 -9.605  -38.006 1.00 55.52  ? 386 GLU A N   1 
ATOM   3215  C CA  . GLU A 1 386 ? -11.765 -8.336  -38.212 1.00 53.91  ? 386 GLU A CA  1 
ATOM   3216  C C   . GLU A 1 386 ? -11.809 -7.950  -39.674 1.00 53.21  ? 386 GLU A C   1 
ATOM   3217  O O   . GLU A 1 386 ? -11.397 -8.719  -40.551 1.00 55.12  ? 386 GLU A O   1 
ATOM   3218  C CB  . GLU A 1 386 ? -10.329 -8.390  -37.685 1.00 53.11  ? 386 GLU A CB  1 
ATOM   3219  C CG  . GLU A 1 386 ? -10.251 -8.930  -36.268 1.00 55.08  ? 386 GLU A CG  1 
ATOM   3220  C CD  . GLU A 1 386 ? -9.098  -8.370  -35.465 1.00 58.31  ? 386 GLU A CD  1 
ATOM   3221  O OE1 . GLU A 1 386 ? -7.945  -8.412  -35.964 1.00 59.88  ? 386 GLU A OE1 1 
ATOM   3222  O OE2 . GLU A 1 386 ? -9.349  -7.910  -34.320 1.00 55.86  ? 386 GLU A OE2 1 
ATOM   3223  N N   . ILE A 1 387 ? -12.333 -6.760  -39.935 1.00 49.28  ? 387 ILE A N   1 
ATOM   3224  C CA  . ILE A 1 387 ? -12.589 -6.325  -41.294 1.00 48.73  ? 387 ILE A CA  1 
ATOM   3225  C C   . ILE A 1 387 ? -11.755 -5.092  -41.601 1.00 47.18  ? 387 ILE A C   1 
ATOM   3226  O O   . ILE A 1 387 ? -11.930 -4.053  -40.969 1.00 48.80  ? 387 ILE A O   1 
ATOM   3227  C CB  . ILE A 1 387 ? -14.089 -6.000  -41.502 1.00 49.08  ? 387 ILE A CB  1 
ATOM   3228  C CG1 . ILE A 1 387 ? -14.994 -7.168  -41.044 1.00 49.16  ? 387 ILE A CG1 1 
ATOM   3229  C CG2 . ILE A 1 387 ? -14.359 -5.580  -42.936 1.00 47.60  ? 387 ILE A CG2 1 
ATOM   3230  C CD1 . ILE A 1 387 ? -14.746 -8.499  -41.735 1.00 48.69  ? 387 ILE A CD1 1 
ATOM   3231  N N   . PRO A 1 388 ? -10.835 -5.201  -42.567 1.00 46.55  ? 388 PRO A N   1 
ATOM   3232  C CA  . PRO A 1 388 ? -10.087 -4.017  -42.947 1.00 47.13  ? 388 PRO A CA  1 
ATOM   3233  C C   . PRO A 1 388 ? -10.906 -3.135  -43.885 1.00 48.96  ? 388 PRO A C   1 
ATOM   3234  O O   . PRO A 1 388 ? -11.483 -3.633  -44.858 1.00 52.48  ? 388 PRO A O   1 
ATOM   3235  C CB  . PRO A 1 388 ? -8.853  -4.593  -43.665 1.00 46.94  ? 388 PRO A CB  1 
ATOM   3236  C CG  . PRO A 1 388 ? -9.314  -5.895  -44.224 1.00 48.76  ? 388 PRO A CG  1 
ATOM   3237  C CD  . PRO A 1 388 ? -10.451 -6.387  -43.356 1.00 48.92  ? 388 PRO A CD  1 
ATOM   3238  N N   . TYR A 1 389 ? -10.969 -1.840  -43.582 1.00 48.16  ? 389 TYR A N   1 
ATOM   3239  C CA  . TYR A 1 389 ? -11.669 -0.875  -44.427 1.00 47.28  ? 389 TYR A CA  1 
ATOM   3240  C C   . TYR A 1 389 ? -11.168 0.543   -44.143 1.00 46.65  ? 389 TYR A C   1 
ATOM   3241  O O   . TYR A 1 389 ? -11.148 0.985   -42.993 1.00 45.99  ? 389 TYR A O   1 
ATOM   3242  C CB  . TYR A 1 389 ? -13.179 -0.970  -44.193 1.00 48.09  ? 389 TYR A CB  1 
ATOM   3243  C CG  . TYR A 1 389 ? -13.983 0.048   -44.948 1.00 49.39  ? 389 TYR A CG  1 
ATOM   3244  C CD1 . TYR A 1 389 ? -14.271 -0.126  -46.310 1.00 50.74  ? 389 TYR A CD1 1 
ATOM   3245  C CD2 . TYR A 1 389 ? -14.470 1.184   -44.311 1.00 48.75  ? 389 TYR A CD2 1 
ATOM   3246  C CE1 . TYR A 1 389 ? -15.021 0.809   -47.012 1.00 50.29  ? 389 TYR A CE1 1 
ATOM   3247  C CE2 . TYR A 1 389 ? -15.218 2.125   -45.005 1.00 51.08  ? 389 TYR A CE2 1 
ATOM   3248  C CZ  . TYR A 1 389 ? -15.492 1.933   -46.353 1.00 51.82  ? 389 TYR A CZ  1 
ATOM   3249  O OH  . TYR A 1 389 ? -16.231 2.871   -47.033 1.00 52.84  ? 389 TYR A OH  1 
ATOM   3250  N N   . CYS A 1 390 ? -10.744 1.234   -45.195 1.00 47.56  ? 390 CYS A N   1 
ATOM   3251  C CA  . CYS A 1 390 ? -10.247 2.614   -45.103 1.00 49.24  ? 390 CYS A CA  1 
ATOM   3252  C C   . CYS A 1 390 ? -9.084  2.847   -44.121 1.00 46.46  ? 390 CYS A C   1 
ATOM   3253  O O   . CYS A 1 390 ? -9.103  3.798   -43.347 1.00 40.87  ? 390 CYS A O   1 
ATOM   3254  C CB  . CYS A 1 390 ? -11.396 3.571   -44.802 1.00 52.69  ? 390 CYS A CB  1 
ATOM   3255  S SG  . CYS A 1 390 ? -12.504 3.741   -46.203 1.00 61.59  ? 390 CYS A SG  1 
ATOM   3256  N N   . GLY A 1 391 ? -8.070  1.984   -44.185 1.00 47.35  ? 391 GLY A N   1 
ATOM   3257  C CA  . GLY A 1 391 ? -6.913  2.076   -43.289 1.00 44.94  ? 391 GLY A CA  1 
ATOM   3258  C C   . GLY A 1 391 ? -7.233  1.742   -41.840 1.00 46.06  ? 391 GLY A C   1 
ATOM   3259  O O   . GLY A 1 391 ? -6.494  2.118   -40.923 1.00 48.40  ? 391 GLY A O   1 
ATOM   3260  N N   . LYS A 1 392 ? -8.336  1.042   -41.624 1.00 43.90  ? 392 LYS A N   1 
ATOM   3261  C CA  . LYS A 1 392 ? -8.734  0.674   -40.283 1.00 43.80  ? 392 LYS A CA  1 
ATOM   3262  C C   . LYS A 1 392 ? -9.135  -0.799  -40.223 1.00 44.48  ? 392 LYS A C   1 
ATOM   3263  O O   . LYS A 1 392 ? -9.544  -1.384  -41.231 1.00 47.27  ? 392 LYS A O   1 
ATOM   3264  C CB  . LYS A 1 392 ? -9.881  1.568   -39.811 1.00 44.72  ? 392 LYS A CB  1 
ATOM   3265  C CG  . LYS A 1 392 ? -9.460  2.724   -38.916 1.00 48.13  ? 392 LYS A CG  1 
ATOM   3266  C CD  . LYS A 1 392 ? -8.796  3.883   -39.647 1.00 49.03  ? 392 LYS A CD  1 
ATOM   3267  C CE  . LYS A 1 392 ? -8.252  4.883   -38.635 1.00 49.73  ? 392 LYS A CE  1 
ATOM   3268  N NZ  . LYS A 1 392 ? -7.663  6.110   -39.241 1.00 49.23  ? 392 LYS A NZ  1 
ATOM   3269  N N   . ILE A 1 393 ? -8.993  -1.398  -39.048 1.00 42.85  ? 393 ILE A N   1 
ATOM   3270  C CA  . ILE A 1 393 ? -9.503  -2.739  -38.805 1.00 42.81  ? 393 ILE A CA  1 
ATOM   3271  C C   . ILE A 1 393 ? -10.664 -2.669  -37.822 1.00 42.66  ? 393 ILE A C   1 
ATOM   3272  O O   . ILE A 1 393 ? -10.500 -2.232  -36.683 1.00 41.65  ? 393 ILE A O   1 
ATOM   3273  C CB  . ILE A 1 393 ? -8.415  -3.681  -38.258 1.00 43.15  ? 393 ILE A CB  1 
ATOM   3274  C CG1 . ILE A 1 393 ? -7.268  -3.813  -39.265 1.00 44.31  ? 393 ILE A CG1 1 
ATOM   3275  C CG2 . ILE A 1 393 ? -9.004  -5.052  -37.935 1.00 44.14  ? 393 ILE A CG2 1 
ATOM   3276  C CD1 . ILE A 1 393 ? -5.941  -4.199  -38.643 1.00 43.89  ? 393 ILE A CD1 1 
ATOM   3277  N N   . PHE A 1 394 ? -11.839 -3.081  -38.292 1.00 42.77  ? 394 PHE A N   1 
ATOM   3278  C CA  . PHE A 1 394 ? -13.042 -3.141  -37.480 1.00 43.90  ? 394 PHE A CA  1 
ATOM   3279  C C   . PHE A 1 394 ? -13.256 -4.581  -37.008 1.00 44.85  ? 394 PHE A C   1 
ATOM   3280  O O   . PHE A 1 394 ? -13.306 -5.506  -37.809 1.00 48.61  ? 394 PHE A O   1 
ATOM   3281  C CB  . PHE A 1 394 ? -14.266 -2.667  -38.291 1.00 42.68  ? 394 PHE A CB  1 
ATOM   3282  C CG  . PHE A 1 394 ? -14.166 -1.244  -38.783 1.00 41.37  ? 394 PHE A CG  1 
ATOM   3283  C CD1 . PHE A 1 394 ? -13.381 -0.925  -39.882 1.00 40.68  ? 394 PHE A CD1 1 
ATOM   3284  C CD2 . PHE A 1 394 ? -14.871 -0.224  -38.149 1.00 41.30  ? 394 PHE A CD2 1 
ATOM   3285  C CE1 . PHE A 1 394 ? -13.291 0.387   -40.330 1.00 41.00  ? 394 PHE A CE1 1 
ATOM   3286  C CE2 . PHE A 1 394 ? -14.783 1.089   -38.592 1.00 40.46  ? 394 PHE A CE2 1 
ATOM   3287  C CZ  . PHE A 1 394 ? -13.990 1.396   -39.680 1.00 39.96  ? 394 PHE A CZ  1 
ATOM   3288  N N   . ASN A 1 395 ? -13.360 -4.774  -35.707 1.00 45.30  ? 395 ASN A N   1 
ATOM   3289  C CA  . ASN A 1 395 ? -13.745 -6.071  -35.190 1.00 46.12  ? 395 ASN A CA  1 
ATOM   3290  C C   . ASN A 1 395 ? -15.257 -6.085  -34.955 1.00 45.70  ? 395 ASN A C   1 
ATOM   3291  O O   . ASN A 1 395 ? -15.769 -5.344  -34.126 1.00 44.29  ? 395 ASN A O   1 
ATOM   3292  C CB  . ASN A 1 395 ? -12.967 -6.389  -33.913 1.00 44.93  ? 395 ASN A CB  1 
ATOM   3293  C CG  . ASN A 1 395 ? -13.274 -7.767  -33.374 1.00 45.14  ? 395 ASN A CG  1 
ATOM   3294  O OD1 . ASN A 1 395 ? -14.439 -8.137  -33.217 1.00 47.48  ? 395 ASN A OD1 1 
ATOM   3295  N ND2 . ASN A 1 395 ? -12.231 -8.523  -33.057 1.00 42.55  ? 395 ASN A ND2 1 
ATOM   3296  N N   . LEU A 1 396 ? -15.965 -6.907  -35.717 1.00 46.65  ? 396 LEU A N   1 
ATOM   3297  C CA  . LEU A 1 396 ? -17.424 -6.893  -35.705 1.00 48.53  ? 396 LEU A CA  1 
ATOM   3298  C C   . LEU A 1 396 ? -17.999 -7.378  -34.383 1.00 49.96  ? 396 LEU A C   1 
ATOM   3299  O O   . LEU A 1 396 ? -19.130 -7.036  -34.031 1.00 50.60  ? 396 LEU A O   1 
ATOM   3300  C CB  . LEU A 1 396 ? -17.976 -7.721  -36.863 1.00 49.37  ? 396 LEU A CB  1 
ATOM   3301  C CG  . LEU A 1 396 ? -17.591 -7.231  -38.265 1.00 49.83  ? 396 LEU A CG  1 
ATOM   3302  C CD1 . LEU A 1 396 ? -18.208 -8.125  -39.322 1.00 49.98  ? 396 LEU A CD1 1 
ATOM   3303  C CD2 . LEU A 1 396 ? -17.988 -5.774  -38.492 1.00 48.78  ? 396 LEU A CD2 1 
ATOM   3304  N N   . THR A 1 397 ? -17.200 -8.144  -33.638 1.00 50.09  ? 397 THR A N   1 
ATOM   3305  C CA  . THR A 1 397 ? -17.648 -8.713  -32.368 1.00 50.18  ? 397 THR A CA  1 
ATOM   3306  C C   . THR A 1 397 ? -17.366 -7.751  -31.221 1.00 48.85  ? 397 THR A C   1 
ATOM   3307  O O   . THR A 1 397 ? -18.273 -7.406  -30.470 1.00 50.48  ? 397 THR A O   1 
ATOM   3308  C CB  . THR A 1 397 ? -17.012 -10.105 -32.102 1.00 51.32  ? 397 THR A CB  1 
ATOM   3309  O OG1 . THR A 1 397 ? -17.420 -11.029 -33.129 1.00 52.49  ? 397 THR A OG1 1 
ATOM   3310  C CG2 . THR A 1 397 ? -17.437 -10.651 -30.738 1.00 49.08  ? 397 THR A CG2 1 
ATOM   3311  N N   . THR A 1 398 ? -16.118 -7.293  -31.112 1.00 47.28  ? 398 THR A N   1 
ATOM   3312  C CA  . THR A 1 398 ? -15.707 -6.423  -30.005 1.00 45.98  ? 398 THR A CA  1 
ATOM   3313  C C   . THR A 1 398 ? -15.986 -4.941  -30.270 1.00 45.16  ? 398 THR A C   1 
ATOM   3314  O O   . THR A 1 398 ? -16.005 -4.128  -29.336 1.00 44.52  ? 398 THR A O   1 
ATOM   3315  C CB  . THR A 1 398 ? -14.212 -6.606  -29.655 1.00 46.63  ? 398 THR A CB  1 
ATOM   3316  O OG1 . THR A 1 398 ? -13.402 -6.278  -30.795 1.00 45.13  ? 398 THR A OG1 1 
ATOM   3317  C CG2 . THR A 1 398 ? -13.924 -8.045  -29.217 1.00 45.81  ? 398 THR A CG2 1 
ATOM   3318  N N   . ARG A 1 399 ? -16.183 -4.599  -31.545 1.00 44.75  ? 399 ARG A N   1 
ATOM   3319  C CA  . ARG A 1 399 ? -16.468 -3.222  -31.991 1.00 44.64  ? 399 ARG A CA  1 
ATOM   3320  C C   . ARG A 1 399 ? -15.255 -2.304  -31.935 1.00 45.14  ? 399 ARG A C   1 
ATOM   3321  O O   . ARG A 1 399 ? -15.330 -1.140  -32.338 1.00 47.42  ? 399 ARG A O   1 
ATOM   3322  C CB  . ARG A 1 399 ? -17.640 -2.604  -31.224 1.00 44.80  ? 399 ARG A CB  1 
ATOM   3323  C CG  . ARG A 1 399 ? -18.977 -3.261  -31.491 1.00 46.37  ? 399 ARG A CG  1 
ATOM   3324  C CD  . ARG A 1 399 ? -19.348 -4.223  -30.373 1.00 47.43  ? 399 ARG A CD  1 
ATOM   3325  N NE  . ARG A 1 399 ? -20.548 -4.996  -30.688 1.00 49.82  ? 399 ARG A NE  1 
ATOM   3326  C CZ  . ARG A 1 399 ? -21.793 -4.539  -30.572 1.00 48.86  ? 399 ARG A CZ  1 
ATOM   3327  N NH1 . ARG A 1 399 ? -22.020 -3.299  -30.165 1.00 48.18  ? 399 ARG A NH1 1 
ATOM   3328  N NH2 . ARG A 1 399 ? -22.808 -5.324  -30.873 1.00 50.95  ? 399 ARG A NH2 1 
ATOM   3329  N N   . GLN A 1 400 ? -14.142 -2.834  -31.433 1.00 44.04  ? 400 GLN A N   1 
ATOM   3330  C CA  . GLN A 1 400 ? -12.869 -2.126  -31.394 1.00 41.79  ? 400 GLN A CA  1 
ATOM   3331  C C   . GLN A 1 400 ? -12.405 -1.765  -32.787 1.00 41.00  ? 400 GLN A C   1 
ATOM   3332  O O   . GLN A 1 400 ? -12.629 -2.517  -33.735 1.00 42.00  ? 400 GLN A O   1 
ATOM   3333  C CB  . GLN A 1 400 ? -11.802 -2.995  -30.727 1.00 41.76  ? 400 GLN A CB  1 
ATOM   3334  C CG  . GLN A 1 400 ? -12.157 -3.458  -29.325 1.00 41.29  ? 400 GLN A CG  1 
ATOM   3335  C CD  . GLN A 1 400 ? -12.612 -2.314  -28.445 1.00 43.44  ? 400 GLN A CD  1 
ATOM   3336  O OE1 . GLN A 1 400 ? -13.816 -2.068  -28.287 1.00 47.11  ? 400 GLN A OE1 1 
ATOM   3337  N NE2 . GLN A 1 400 ? -11.663 -1.600  -27.875 1.00 40.50  ? 400 GLN A NE2 1 
ATOM   3338  N N   . VAL A 1 401 ? -11.753 -0.613  -32.912 1.00 39.84  ? 401 VAL A N   1 
ATOM   3339  C CA  . VAL A 1 401 ? -11.133 -0.233  -34.176 1.00 38.39  ? 401 VAL A CA  1 
ATOM   3340  C C   . VAL A 1 401 ? -9.643  0.056   -33.988 1.00 38.14  ? 401 VAL A C   1 
ATOM   3341  O O   . VAL A 1 401 ? -9.256  0.840   -33.120 1.00 37.31  ? 401 VAL A O   1 
ATOM   3342  C CB  . VAL A 1 401 ? -11.848 0.958   -34.845 1.00 37.75  ? 401 VAL A CB  1 
ATOM   3343  C CG1 . VAL A 1 401 ? -11.182 1.306   -36.170 1.00 36.46  ? 401 VAL A CG1 1 
ATOM   3344  C CG2 . VAL A 1 401 ? -13.324 0.645   -35.060 1.00 38.61  ? 401 VAL A CG2 1 
ATOM   3345  N N   . ARG A 1 402 ? -8.825  -0.591  -34.814 1.00 38.54  ? 402 ARG A N   1 
ATOM   3346  C CA  . ARG A 1 402 ? -7.371  -0.426  -34.795 1.00 39.64  ? 402 ARG A CA  1 
ATOM   3347  C C   . ARG A 1 402 ? -6.908  0.156   -36.137 1.00 39.89  ? 402 ARG A C   1 
ATOM   3348  O O   . ARG A 1 402 ? -7.592  0.013   -37.158 1.00 39.45  ? 402 ARG A O   1 
ATOM   3349  C CB  . ARG A 1 402 ? -6.679  -1.787  -34.554 1.00 39.00  ? 402 ARG A CB  1 
ATOM   3350  C CG  . ARG A 1 402 ? -7.055  -2.501  -33.254 1.00 40.49  ? 402 ARG A CG  1 
ATOM   3351  C CD  . ARG A 1 402 ? -6.321  -1.922  -32.029 1.00 42.52  ? 402 ARG A CD  1 
ATOM   3352  N NE  . ARG A 1 402 ? -4.862  -1.976  -32.167 1.00 42.24  ? 402 ARG A NE  1 
ATOM   3353  C CZ  . ARG A 1 402 ? -4.113  -3.021  -31.813 1.00 42.25  ? 402 ARG A CZ  1 
ATOM   3354  N NH1 . ARG A 1 402 ? -4.677  -4.086  -31.261 1.00 44.71  ? 402 ARG A NH1 1 
ATOM   3355  N NH2 . ARG A 1 402 ? -2.797  -2.989  -31.981 1.00 38.98  ? 402 ARG A NH2 1 
ATOM   3356  N N   . THR A 1 403 ? -5.752  0.813   -36.141 1.00 40.51  ? 403 THR A N   1 
ATOM   3357  C CA  . THR A 1 403 ? -5.139  1.250   -37.403 1.00 41.72  ? 403 THR A CA  1 
ATOM   3358  C C   . THR A 1 403 ? -4.583  0.046   -38.155 1.00 41.30  ? 403 THR A C   1 
ATOM   3359  O O   . THR A 1 403 ? -4.054  -0.869  -37.545 1.00 41.11  ? 403 THR A O   1 
ATOM   3360  C CB  . THR A 1 403 ? -4.002  2.237   -37.147 1.00 41.58  ? 403 THR A CB  1 
ATOM   3361  O OG1 . THR A 1 403 ? -4.486  3.320   -36.352 1.00 44.88  ? 403 THR A OG1 1 
ATOM   3362  C CG2 . THR A 1 403 ? -3.417  2.767   -38.457 1.00 40.95  ? 403 THR A CG2 1 
ATOM   3363  N N   . LEU A 1 404 ? -4.727  0.045   -39.475 1.00 43.58  ? 404 LEU A N   1 
ATOM   3364  C CA  . LEU A 1 404 ? -4.187  -1.029  -40.301 1.00 44.45  ? 404 LEU A CA  1 
ATOM   3365  C C   . LEU A 1 404 ? -2.770  -0.715  -40.778 1.00 44.62  ? 404 LEU A C   1 
ATOM   3366  O O   . LEU A 1 404 ? -2.484  0.388   -41.236 1.00 43.22  ? 404 LEU A O   1 
ATOM   3367  C CB  . LEU A 1 404 ? -5.105  -1.291  -41.492 1.00 45.81  ? 404 LEU A CB  1 
ATOM   3368  C CG  . LEU A 1 404 ? -4.638  -2.154  -42.677 1.00 46.25  ? 404 LEU A CG  1 
ATOM   3369  C CD1 . LEU A 1 404 ? -4.581  -3.627  -42.311 1.00 45.50  ? 404 LEU A CD1 1 
ATOM   3370  C CD2 . LEU A 1 404 ? -5.547  -1.944  -43.886 1.00 45.26  ? 404 LEU A CD2 1 
ATOM   3371  N N   . TYR A 1 405 ? -1.888  -1.698  -40.630 1.00 48.26  ? 405 TYR A N   1 
ATOM   3372  C CA  . TYR A 1 405 ? -0.553  -1.692  -41.230 1.00 49.36  ? 405 TYR A CA  1 
ATOM   3373  C C   . TYR A 1 405 ? -0.303  -3.129  -41.771 1.00 54.48  ? 405 TYR A C   1 
ATOM   3374  O O   . TYR A 1 405 ? -0.335  -4.079  -40.977 1.00 62.13  ? 405 TYR A O   1 
ATOM   3375  C CB  . TYR A 1 405 ? 0.520   -1.367  -40.164 1.00 43.76  ? 405 TYR A CB  1 
ATOM   3376  C CG  . TYR A 1 405 ? 0.244   -0.215  -39.194 1.00 40.29  ? 405 TYR A CG  1 
ATOM   3377  C CD1 . TYR A 1 405 ? 0.756   1.063   -39.434 1.00 39.42  ? 405 TYR A CD1 1 
ATOM   3378  C CD2 . TYR A 1 405 ? -0.437  -0.430  -37.982 1.00 38.72  ? 405 TYR A CD2 1 
ATOM   3379  C CE1 . TYR A 1 405 ? 0.561   2.107   -38.530 1.00 37.00  ? 405 TYR A CE1 1 
ATOM   3380  C CE2 . TYR A 1 405 ? -0.643  0.613   -37.077 1.00 37.48  ? 405 TYR A CE2 1 
ATOM   3381  C CZ  . TYR A 1 405 ? -0.143  1.884   -37.362 1.00 37.90  ? 405 TYR A CZ  1 
ATOM   3382  O OH  . TYR A 1 405 ? -0.332  2.935   -36.477 1.00 37.91  ? 405 TYR A OH  1 
ATOM   3383  N N   . LYS A 1 406 ? -0.044  -3.339  -43.072 1.00 60.28  ? 406 LYS A N   1 
ATOM   3384  C CA  . LYS A 1 406 ? 0.284   -2.331  -44.108 1.00 65.17  ? 406 LYS A CA  1 
ATOM   3385  C C   . LYS A 1 406 ? 1.688   -2.603  -44.711 1.00 62.75  ? 406 LYS A C   1 
ATOM   3386  O O   . LYS A 1 406 ? 2.251   -1.761  -45.440 1.00 61.15  ? 406 LYS A O   1 
ATOM   3387  C CB  . LYS A 1 406 ? 0.199   -0.900  -43.561 1.00 63.83  ? 406 LYS A CB  1 
ATOM   3388  C CG  . LYS A 1 406 ? -0.277  0.130   -44.565 1.00 65.05  ? 406 LYS A CG  1 
ATOM   3389  C CD  . LYS A 1 406 ? -0.042  1.536   -44.040 1.00 66.91  ? 406 LYS A CD  1 
ATOM   3390  C CE  . LYS A 1 406 ? 1.408   1.743   -43.651 1.00 62.59  ? 406 LYS A CE  1 
ATOM   3391  N NZ  . LYS A 1 406 ? 1.685   3.171   -43.338 1.00 66.98  ? 406 LYS A NZ  1 
ATOM   3392  N N   . LEU A 1 407 ? 2.259   -3.764  -44.388 1.00 57.81  ? 407 LEU A N   1 
ATOM   3393  C CA  . LEU A 1 407 ? 3.657   -4.023  -44.724 1.00 60.22  ? 407 LEU A CA  1 
ATOM   3394  C C   . LEU A 1 407 ? 3.855   -5.374  -45.394 1.00 62.51  ? 407 LEU A C   1 
ATOM   3395  O O   . LEU A 1 407 ? 3.744   -6.417  -44.745 1.00 61.98  ? 407 LEU A O   1 
ATOM   3396  C CB  . LEU A 1 407 ? 4.577   -3.912  -43.483 1.00 61.57  ? 407 LEU A CB  1 
ATOM   3397  C CG  . LEU A 1 407 ? 4.860   -2.591  -42.728 1.00 58.23  ? 407 LEU A CG  1 
ATOM   3398  C CD1 . LEU A 1 407 ? 5.113   -1.412  -43.656 1.00 60.23  ? 407 LEU A CD1 1 
ATOM   3399  C CD2 . LEU A 1 407 ? 3.774   -2.263  -41.715 1.00 57.46  ? 407 LEU A CD2 1 
ATOM   3400  N N   . PRO A 1 408 ? 4.167   -5.358  -46.703 1.00 62.91  ? 408 PRO A N   1 
ATOM   3401  C CA  . PRO A 1 408 ? 4.640   -6.551  -47.394 1.00 62.66  ? 408 PRO A CA  1 
ATOM   3402  C C   . PRO A 1 408 ? 5.869   -7.128  -46.686 1.00 65.57  ? 408 PRO A C   1 
ATOM   3403  O O   . PRO A 1 408 ? 6.593   -6.382  -46.012 1.00 62.48  ? 408 PRO A O   1 
ATOM   3404  C CB  . PRO A 1 408 ? 5.050   -6.015  -48.767 1.00 62.12  ? 408 PRO A CB  1 
ATOM   3405  C CG  . PRO A 1 408 ? 4.234   -4.793  -48.960 1.00 62.48  ? 408 PRO A CG  1 
ATOM   3406  C CD  . PRO A 1 408 ? 4.103   -4.187  -47.595 1.00 62.29  ? 408 PRO A CD  1 
ATOM   3407  N N   . PRO A 1 409 ? 6.107   -8.452  -46.830 1.00 69.51  ? 409 PRO A N   1 
ATOM   3408  C CA  . PRO A 1 409 ? 7.370   -9.028  -46.350 1.00 67.74  ? 409 PRO A CA  1 
ATOM   3409  C C   . PRO A 1 409 ? 8.550   -8.410  -47.103 1.00 66.16  ? 409 PRO A C   1 
ATOM   3410  O O   . PRO A 1 409 ? 8.420   -8.084  -48.284 1.00 66.31  ? 409 PRO A O   1 
ATOM   3411  C CB  . PRO A 1 409 ? 7.232   -10.520 -46.694 1.00 70.37  ? 409 PRO A CB  1 
ATOM   3412  C CG  . PRO A 1 409 ? 6.200   -10.584 -47.778 1.00 69.40  ? 409 PRO A CG  1 
ATOM   3413  C CD  . PRO A 1 409 ? 5.254   -9.456  -47.502 1.00 69.37  ? 409 PRO A CD  1 
ATOM   3414  N N   . ASN A 1 410 ? 9.673   -8.213  -46.416 1.00 65.31  ? 410 ASN A N   1 
ATOM   3415  C CA  . ASN A 1 410 ? 10.867  -7.628  -47.039 1.00 64.12  ? 410 ASN A CA  1 
ATOM   3416  C C   . ASN A 1 410 ? 10.739  -6.135  -47.354 1.00 62.35  ? 410 ASN A C   1 
ATOM   3417  O O   . ASN A 1 410 ? 11.597  -5.571  -48.062 1.00 62.87  ? 410 ASN A O   1 
ATOM   3418  C CB  . ASN A 1 410 ? 11.239  -8.367  -48.342 1.00 68.49  ? 410 ASN A CB  1 
ATOM   3419  C CG  . ASN A 1 410 ? 11.448  -9.849  -48.144 1.00 72.48  ? 410 ASN A CG  1 
ATOM   3420  O OD1 . ASN A 1 410 ? 11.880  -10.299 -47.079 1.00 76.60  ? 410 ASN A OD1 1 
ATOM   3421  N ND2 . ASN A 1 410 ? 11.148  -10.623 -49.179 1.00 77.13  ? 410 ASN A ND2 1 
ATOM   3422  N N   . TYR A 1 411 ? 9.670   -5.497  -46.874 1.00 54.46  ? 411 TYR A N   1 
ATOM   3423  C CA  . TYR A 1 411 ? 9.495   -4.071  -47.126 1.00 47.80  ? 411 TYR A CA  1 
ATOM   3424  C C   . TYR A 1 411 ? 10.467  -3.275  -46.267 1.00 45.79  ? 411 TYR A C   1 
ATOM   3425  O O   . TYR A 1 411 ? 10.606  -3.539  -45.075 1.00 46.52  ? 411 TYR A O   1 
ATOM   3426  C CB  . TYR A 1 411 ? 8.063   -3.632  -46.865 1.00 44.19  ? 411 TYR A CB  1 
ATOM   3427  C CG  . TYR A 1 411 ? 7.776   -2.185  -47.222 1.00 41.25  ? 411 TYR A CG  1 
ATOM   3428  C CD1 . TYR A 1 411 ? 7.425   -1.817  -48.523 1.00 40.18  ? 411 TYR A CD1 1 
ATOM   3429  C CD2 . TYR A 1 411 ? 7.818   -1.186  -46.250 1.00 37.16  ? 411 TYR A CD2 1 
ATOM   3430  C CE1 . TYR A 1 411 ? 7.142   -0.493  -48.842 1.00 37.34  ? 411 TYR A CE1 1 
ATOM   3431  C CE2 . TYR A 1 411 ? 7.533   0.135   -46.563 1.00 35.06  ? 411 TYR A CE2 1 
ATOM   3432  C CZ  . TYR A 1 411 ? 7.206   0.478   -47.848 1.00 35.36  ? 411 TYR A CZ  1 
ATOM   3433  O OH  . TYR A 1 411 ? 6.937   1.794   -48.148 1.00 36.15  ? 411 TYR A OH  1 
ATOM   3434  N N   . GLU A 1 412 ? 11.153  -2.322  -46.893 1.00 40.16  ? 412 GLU A N   1 
ATOM   3435  C CA  . GLU A 1 412 ? 12.059  -1.439  -46.193 1.00 37.69  ? 412 GLU A CA  1 
ATOM   3436  C C   . GLU A 1 412 ? 11.308  -0.219  -45.702 1.00 36.18  ? 412 GLU A C   1 
ATOM   3437  O O   . GLU A 1 412 ? 10.885  0.642   -46.482 1.00 40.41  ? 412 GLU A O   1 
ATOM   3438  C CB  . GLU A 1 412 ? 13.221  -1.023  -47.095 1.00 38.29  ? 412 GLU A CB  1 
ATOM   3439  C CG  . GLU A 1 412 ? 14.340  -2.035  -47.143 1.00 39.38  ? 412 GLU A CG  1 
ATOM   3440  C CD  . GLU A 1 412 ? 15.446  -1.630  -48.098 1.00 40.38  ? 412 GLU A CD  1 
ATOM   3441  O OE1 . GLU A 1 412 ? 16.393  -0.913  -47.683 1.00 38.89  ? 412 GLU A OE1 1 
ATOM   3442  O OE2 . GLU A 1 412 ? 15.368  -2.043  -49.263 1.00 40.63  ? 412 GLU A OE2 1 
ATOM   3443  N N   . ILE A 1 413 ? 11.190  -0.133  -44.396 1.00 34.58  ? 413 ILE A N   1 
ATOM   3444  C CA  . ILE A 1 413 ? 10.264  0.780   -43.745 1.00 33.44  ? 413 ILE A CA  1 
ATOM   3445  C C   . ILE A 1 413 ? 10.655  2.245   -44.003 1.00 32.41  ? 413 ILE A C   1 
ATOM   3446  O O   . ILE A 1 413 ? 9.811   3.123   -43.990 1.00 32.30  ? 413 ILE A O   1 
ATOM   3447  C CB  . ILE A 1 413 ? 10.144  0.436   -42.228 1.00 32.17  ? 413 ILE A CB  1 
ATOM   3448  C CG1 . ILE A 1 413 ? 8.997   1.202   -41.545 1.00 33.19  ? 413 ILE A CG1 1 
ATOM   3449  C CG2 . ILE A 1 413 ? 11.489  0.593   -41.511 1.00 30.71  ? 413 ILE A CG2 1 
ATOM   3450  C CD1 . ILE A 1 413 ? 7.647   0.544   -41.651 1.00 32.31  ? 413 ILE A CD1 1 
ATOM   3451  N N   . ARG A 1 414 ? 11.929  2.478   -44.309 1.00 31.75  ? 414 ARG A N   1 
ATOM   3452  C CA  . ARG A 1 414 ? 12.414  3.819   -44.629 1.00 29.93  ? 414 ARG A CA  1 
ATOM   3453  C C   . ARG A 1 414 ? 11.676  4.416   -45.810 1.00 31.03  ? 414 ARG A C   1 
ATOM   3454  O O   . ARG A 1 414 ? 11.721  5.629   -46.002 1.00 30.83  ? 414 ARG A O   1 
ATOM   3455  C CB  . ARG A 1 414 ? 13.912  3.805   -44.909 1.00 29.40  ? 414 ARG A CB  1 
ATOM   3456  C CG  . ARG A 1 414 ? 14.286  3.175   -46.241 1.00 27.71  ? 414 ARG A CG  1 
ATOM   3457  C CD  . ARG A 1 414 ? 15.774  3.194   -46.469 1.00 26.93  ? 414 ARG A CD  1 
ATOM   3458  N NE  . ARG A 1 414 ? 16.141  2.172   -47.431 1.00 25.64  ? 414 ARG A NE  1 
ATOM   3459  C CZ  . ARG A 1 414 ? 16.070  2.320   -48.751 1.00 26.02  ? 414 ARG A CZ  1 
ATOM   3460  N NH1 . ARG A 1 414 ? 15.643  3.466   -49.303 1.00 25.18  ? 414 ARG A NH1 1 
ATOM   3461  N NH2 . ARG A 1 414 ? 16.383  1.305   -49.520 1.00 25.76  ? 414 ARG A NH2 1 
ATOM   3462  N N   . HIS A 1 415 ? 11.007  3.554   -46.596 1.00 33.08  ? 415 HIS A N   1 
ATOM   3463  C CA  . HIS A 1 415 ? 10.216  3.964   -47.765 1.00 34.46  ? 415 HIS A CA  1 
ATOM   3464  C C   . HIS A 1 415 ? 8.917   4.609   -47.383 1.00 36.17  ? 415 HIS A C   1 
ATOM   3465  O O   . HIS A 1 415 ? 8.291   5.266   -48.222 1.00 39.15  ? 415 HIS A O   1 
ATOM   3466  C CB  . HIS A 1 415 ? 9.904   2.765   -48.685 1.00 37.27  ? 415 HIS A CB  1 
ATOM   3467  C CG  . HIS A 1 415 ? 11.065  2.316   -49.528 1.00 38.91  ? 415 HIS A CG  1 
ATOM   3468  N ND1 . HIS A 1 415 ? 11.720  3.143   -50.362 1.00 37.95  ? 415 HIS A ND1 1 
ATOM   3469  C CD2 . HIS A 1 415 ? 11.678  1.076   -49.648 1.00 38.92  ? 415 HIS A CD2 1 
ATOM   3470  C CE1 . HIS A 1 415 ? 12.714  2.477   -50.952 1.00 38.83  ? 415 HIS A CE1 1 
ATOM   3471  N NE2 . HIS A 1 415 ? 12.686  1.211   -50.516 1.00 37.79  ? 415 HIS A NE2 1 
ATOM   3472  N N   . LYS A 1 416 ? 8.453   4.375   -46.151 1.00 35.45  ? 416 LYS A N   1 
ATOM   3473  C CA  . LYS A 1 416 ? 7.228   5.011   -45.647 1.00 35.64  ? 416 LYS A CA  1 
ATOM   3474  C C   . LYS A 1 416 ? 7.406   6.520   -45.418 1.00 34.75  ? 416 LYS A C   1 
ATOM   3475  O O   . LYS A 1 416 ? 6.429   7.279   -45.427 1.00 35.80  ? 416 LYS A O   1 
ATOM   3476  C CB  . LYS A 1 416 ? 6.745   4.332   -44.343 1.00 39.04  ? 416 LYS A CB  1 
ATOM   3477  C CG  . LYS A 1 416 ? 5.342   3.688   -44.408 1.00 42.74  ? 416 LYS A CG  1 
ATOM   3478  C CD  . LYS A 1 416 ? 4.963   3.244   -45.822 1.00 43.48  ? 416 LYS A CD  1 
ATOM   3479  C CE  . LYS A 1 416 ? 3.588   2.616   -45.888 1.00 47.11  ? 416 LYS A CE  1 
ATOM   3480  N NZ  . LYS A 1 416 ? 3.630   1.124   -45.948 1.00 47.43  ? 416 LYS A NZ  1 
ATOM   3481  N N   . PHE A 1 417 ? 8.653   6.948   -45.274 1.00 30.52  ? 417 PHE A N   1 
ATOM   3482  C CA  . PHE A 1 417 ? 8.956   8.265   -44.769 1.00 30.94  ? 417 PHE A CA  1 
ATOM   3483  C C   . PHE A 1 417 ? 9.523   9.219   -45.817 1.00 32.68  ? 417 PHE A C   1 
ATOM   3484  O O   . PHE A 1 417 ? 10.136  8.800   -46.789 1.00 36.28  ? 417 PHE A O   1 
ATOM   3485  C CB  . PHE A 1 417 ? 9.881   8.128   -43.553 1.00 29.88  ? 417 PHE A CB  1 
ATOM   3486  C CG  . PHE A 1 417 ? 9.362   7.155   -42.522 1.00 29.06  ? 417 PHE A CG  1 
ATOM   3487  C CD1 . PHE A 1 417 ? 8.124   7.360   -41.924 1.00 29.29  ? 417 PHE A CD1 1 
ATOM   3488  C CD2 . PHE A 1 417 ? 10.070  6.022   -42.196 1.00 29.46  ? 417 PHE A CD2 1 
ATOM   3489  C CE1 . PHE A 1 417 ? 7.621   6.474   -40.992 1.00 29.14  ? 417 PHE A CE1 1 
ATOM   3490  C CE2 . PHE A 1 417 ? 9.572   5.114   -41.267 1.00 29.83  ? 417 PHE A CE2 1 
ATOM   3491  C CZ  . PHE A 1 417 ? 8.340   5.338   -40.674 1.00 29.28  ? 417 PHE A CZ  1 
ATOM   3492  N N   . LYS A 1 418 ? 9.275   10.508  -45.627 1.00 34.28  ? 418 LYS A N   1 
ATOM   3493  C CA  . LYS A 1 418 ? 9.823   11.548  -46.481 1.00 34.71  ? 418 LYS A CA  1 
ATOM   3494  C C   . LYS A 1 418 ? 10.662  12.507  -45.629 1.00 34.92  ? 418 LYS A C   1 
ATOM   3495  O O   . LYS A 1 418 ? 10.126  13.398  -44.970 1.00 35.66  ? 418 LYS A O   1 
ATOM   3496  C CB  . LYS A 1 418 ? 8.693   12.297  -47.204 1.00 35.68  ? 418 LYS A CB  1 
ATOM   3497  C CG  . LYS A 1 418 ? 9.170   13.492  -48.021 1.00 37.79  ? 418 LYS A CG  1 
ATOM   3498  C CD  . LYS A 1 418 ? 8.022   14.217  -48.731 1.00 38.67  ? 418 LYS A CD  1 
ATOM   3499  C CE  . LYS A 1 418 ? 8.582   15.130  -49.815 1.00 41.04  ? 418 LYS A CE  1 
ATOM   3500  N NZ  . LYS A 1 418 ? 7.672   16.235  -50.227 1.00 44.31  ? 418 LYS A NZ  1 
ATOM   3501  N N   . LEU A 1 419 ? 11.981  12.315  -45.647 1.00 34.42  ? 419 LEU A N   1 
ATOM   3502  C CA  . LEU A 1 419 ? 12.877  13.095  -44.811 1.00 33.03  ? 419 LEU A CA  1 
ATOM   3503  C C   . LEU A 1 419 ? 13.424  14.317  -45.528 1.00 34.42  ? 419 LEU A C   1 
ATOM   3504  O O   . LEU A 1 419 ? 13.953  15.236  -44.892 1.00 34.19  ? 419 LEU A O   1 
ATOM   3505  C CB  . LEU A 1 419 ? 14.043  12.226  -44.353 1.00 35.51  ? 419 LEU A CB  1 
ATOM   3506  C CG  . LEU A 1 419 ? 13.696  10.888  -43.696 1.00 38.46  ? 419 LEU A CG  1 
ATOM   3507  C CD1 . LEU A 1 419 ? 14.967  10.149  -43.302 1.00 36.38  ? 419 LEU A CD1 1 
ATOM   3508  C CD2 . LEU A 1 419 ? 12.782  11.106  -42.483 1.00 39.51  ? 419 LEU A CD2 1 
ATOM   3509  N N   . TRP A 1 420 ? 13.324  14.308  -46.856 1.00 34.72  ? 420 TRP A N   1 
ATOM   3510  C CA  . TRP A 1 420 ? 13.952  15.320  -47.692 1.00 35.99  ? 420 TRP A CA  1 
ATOM   3511  C C   . TRP A 1 420 ? 12.928  16.092  -48.448 1.00 35.52  ? 420 TRP A C   1 
ATOM   3512  O O   . TRP A 1 420 ? 12.106  15.512  -49.159 1.00 36.06  ? 420 TRP A O   1 
ATOM   3513  C CB  . TRP A 1 420 ? 14.917  14.657  -48.679 1.00 35.69  ? 420 TRP A CB  1 
ATOM   3514  C CG  . TRP A 1 420 ? 15.901  13.760  -47.997 1.00 34.66  ? 420 TRP A CG  1 
ATOM   3515  C CD1 . TRP A 1 420 ? 15.773  12.402  -47.739 1.00 33.54  ? 420 TRP A CD1 1 
ATOM   3516  C CD2 . TRP A 1 420 ? 17.194  14.136  -47.445 1.00 34.20  ? 420 TRP A CD2 1 
ATOM   3517  N NE1 . TRP A 1 420 ? 16.879  11.929  -47.082 1.00 32.18  ? 420 TRP A NE1 1 
ATOM   3518  C CE2 . TRP A 1 420 ? 17.773  12.923  -46.891 1.00 33.78  ? 420 TRP A CE2 1 
ATOM   3519  C CE3 . TRP A 1 420 ? 17.915  15.312  -47.383 1.00 36.47  ? 420 TRP A CE3 1 
ATOM   3520  C CZ2 . TRP A 1 420 ? 19.007  12.917  -46.274 1.00 35.57  ? 420 TRP A CZ2 1 
ATOM   3521  C CZ3 . TRP A 1 420 ? 19.176  15.291  -46.764 1.00 37.39  ? 420 TRP A CZ3 1 
ATOM   3522  C CH2 . TRP A 1 420 ? 19.697  14.124  -46.219 1.00 36.58  ? 420 TRP A CH2 1 
ATOM   3523  N N   . ASN A 1 421 ? 12.965  17.410  -48.315 1.00 35.42  ? 421 ASN A N   1 
ATOM   3524  C CA  . ASN A 1 421 ? 12.058  18.247  -49.074 1.00 38.01  ? 421 ASN A CA  1 
ATOM   3525  C C   . ASN A 1 421 ? 12.835  19.249  -49.892 1.00 37.81  ? 421 ASN A C   1 
ATOM   3526  O O   . ASN A 1 421 ? 13.332  20.250  -49.360 1.00 37.91  ? 421 ASN A O   1 
ATOM   3527  C CB  . ASN A 1 421 ? 11.023  18.948  -48.167 1.00 40.03  ? 421 ASN A CB  1 
ATOM   3528  C CG  . ASN A 1 421 ? 10.051  19.831  -48.956 1.00 43.43  ? 421 ASN A CG  1 
ATOM   3529  O OD1 . ASN A 1 421 ? 10.152  19.956  -50.185 1.00 44.13  ? 421 ASN A OD1 1 
ATOM   3530  N ND2 . ASN A 1 421 ? 9.104   20.450  -48.250 1.00 44.61  ? 421 ASN A ND2 1 
ATOM   3531  N N   . PHE A 1 422 ? 12.922  18.982  -51.196 1.00 36.59  ? 422 PHE A N   1 
ATOM   3532  C CA  . PHE A 1 422 ? 13.722  19.801  -52.093 1.00 36.37  ? 422 PHE A CA  1 
ATOM   3533  C C   . PHE A 1 422 ? 13.338  21.282  -52.074 1.00 36.90  ? 422 PHE A C   1 
ATOM   3534  O O   . PHE A 1 422 ? 14.156  22.125  -52.411 1.00 36.34  ? 422 PHE A O   1 
ATOM   3535  C CB  . PHE A 1 422 ? 13.689  19.257  -53.524 1.00 36.16  ? 422 PHE A CB  1 
ATOM   3536  C CG  . PHE A 1 422 ? 14.843  19.729  -54.373 1.00 35.48  ? 422 PHE A CG  1 
ATOM   3537  C CD1 . PHE A 1 422 ? 16.121  19.202  -54.184 1.00 32.44  ? 422 PHE A CD1 1 
ATOM   3538  C CD2 . PHE A 1 422 ? 14.657  20.726  -55.346 1.00 36.32  ? 422 PHE A CD2 1 
ATOM   3539  C CE1 . PHE A 1 422 ? 17.194  19.631  -54.960 1.00 33.27  ? 422 PHE A CE1 1 
ATOM   3540  C CE2 . PHE A 1 422 ? 15.736  21.171  -56.123 1.00 36.63  ? 422 PHE A CE2 1 
ATOM   3541  C CZ  . PHE A 1 422 ? 17.012  20.616  -55.927 1.00 34.20  ? 422 PHE A CZ  1 
ATOM   3542  N N   . ASN A 1 423 ? 12.105  21.579  -51.667 1.00 38.67  ? 423 ASN A N   1 
ATOM   3543  C CA  . ASN A 1 423 ? 11.612  22.969  -51.529 1.00 42.26  ? 423 ASN A CA  1 
ATOM   3544  C C   . ASN A 1 423 ? 11.950  23.643  -50.187 1.00 40.96  ? 423 ASN A C   1 
ATOM   3545  O O   . ASN A 1 423 ? 11.764  24.858  -50.037 1.00 39.83  ? 423 ASN A O   1 
ATOM   3546  C CB  . ASN A 1 423 ? 10.093  23.021  -51.723 1.00 46.69  ? 423 ASN A CB  1 
ATOM   3547  C CG  . ASN A 1 423 ? 9.643   22.351  -53.004 1.00 55.74  ? 423 ASN A CG  1 
ATOM   3548  O OD1 . ASN A 1 423 ? 10.034  22.754  -54.111 1.00 60.88  ? 423 ASN A OD1 1 
ATOM   3549  N ND2 . ASN A 1 423 ? 8.812   21.315  -52.865 1.00 58.60  ? 423 ASN A ND2 1 
ATOM   3550  N N   . ASN A 1 424 ? 12.395  22.851  -49.204 1.00 37.39  ? 424 ASN A N   1 
ATOM   3551  C CA  . ASN A 1 424 ? 12.709  23.371  -47.875 1.00 34.26  ? 424 ASN A CA  1 
ATOM   3552  C C   . ASN A 1 424 ? 13.947  22.667  -47.357 1.00 32.80  ? 424 ASN A C   1 
ATOM   3553  O O   . ASN A 1 424 ? 13.854  21.721  -46.577 1.00 31.96  ? 424 ASN A O   1 
ATOM   3554  C CB  . ASN A 1 424 ? 11.505  23.192  -46.925 1.00 34.18  ? 424 ASN A CB  1 
ATOM   3555  C CG  . ASN A 1 424 ? 11.565  24.113  -45.698 1.00 34.16  ? 424 ASN A CG  1 
ATOM   3556  O OD1 . ASN A 1 424 ? 12.461  24.949  -45.571 1.00 34.74  ? 424 ASN A OD1 1 
ATOM   3557  N ND2 . ASN A 1 424 ? 10.603  23.964  -44.801 1.00 33.21  ? 424 ASN A ND2 1 
ATOM   3558  N N   . GLN A 1 425 ? 15.108  23.121  -47.827 1.00 33.41  ? 425 GLN A N   1 
ATOM   3559  C CA  . GLN A 1 425 ? 16.381  22.402  -47.661 1.00 33.95  ? 425 GLN A CA  1 
ATOM   3560  C C   . GLN A 1 425 ? 17.122  22.829  -46.394 1.00 33.73  ? 425 GLN A C   1 
ATOM   3561  O O   . GLN A 1 425 ? 17.104  24.004  -46.021 1.00 33.05  ? 425 GLN A O   1 
ATOM   3562  C CB  . GLN A 1 425 ? 17.296  22.570  -48.903 1.00 33.16  ? 425 GLN A CB  1 
ATOM   3563  C CG  . GLN A 1 425 ? 16.577  22.474  -50.246 1.00 33.32  ? 425 GLN A CG  1 
ATOM   3564  C CD  . GLN A 1 425 ? 17.475  22.096  -51.436 1.00 33.73  ? 425 GLN A CD  1 
ATOM   3565  O OE1 . GLN A 1 425 ? 18.707  22.073  -51.347 1.00 32.72  ? 425 GLN A OE1 1 
ATOM   3566  N NE2 . GLN A 1 425 ? 16.840  21.811  -52.567 1.00 33.12  ? 425 GLN A NE2 1 
ATOM   3567  N N   . ILE A 1 426 ? 17.785  21.867  -45.753 1.00 32.19  ? 426 ILE A N   1 
ATOM   3568  C CA  . ILE A 1 426 ? 18.417  22.072  -44.456 1.00 31.09  ? 426 ILE A CA  1 
ATOM   3569  C C   . ILE A 1 426 ? 19.909  21.859  -44.631 1.00 32.14  ? 426 ILE A C   1 
ATOM   3570  O O   . ILE A 1 426 ? 20.324  20.842  -45.188 1.00 31.81  ? 426 ILE A O   1 
ATOM   3571  C CB  . ILE A 1 426 ? 17.850  21.067  -43.426 1.00 30.81  ? 426 ILE A CB  1 
ATOM   3572  C CG1 . ILE A 1 426 ? 16.332  21.240  -43.309 1.00 30.29  ? 426 ILE A CG1 1 
ATOM   3573  C CG2 . ILE A 1 426 ? 18.584  21.161  -42.076 1.00 31.04  ? 426 ILE A CG2 1 
ATOM   3574  C CD1 . ILE A 1 426 ? 15.630  20.258  -42.388 1.00 32.11  ? 426 ILE A CD1 1 
ATOM   3575  N N   . SER A 1 427 ? 20.734  22.818  -44.209 1.00 33.79  ? 427 SER A N   1 
ATOM   3576  C CA  . SER A 1 427 ? 22.170  22.687  -44.498 1.00 35.85  ? 427 SER A CA  1 
ATOM   3577  C C   . SER A 1 427 ? 22.755  21.506  -43.730 1.00 34.83  ? 427 SER A C   1 
ATOM   3578  O O   . SER A 1 427 ? 22.164  21.036  -42.756 1.00 33.38  ? 427 SER A O   1 
ATOM   3579  C CB  . SER A 1 427 ? 22.957  23.980  -44.228 1.00 37.15  ? 427 SER A CB  1 
ATOM   3580  O OG  . SER A 1 427 ? 23.392  24.070  -42.885 1.00 39.84  ? 427 SER A OG  1 
ATOM   3581  N N   . ASP A 1 428 ? 23.918  21.050  -44.157 1.00 34.91  ? 428 ASP A N   1 
ATOM   3582  C CA  . ASP A 1 428 ? 24.502  19.851  -43.599 1.00 38.54  ? 428 ASP A CA  1 
ATOM   3583  C C   . ASP A 1 428 ? 24.980  19.991  -42.154 1.00 40.10  ? 428 ASP A C   1 
ATOM   3584  O O   . ASP A 1 428 ? 25.387  18.996  -41.536 1.00 43.61  ? 428 ASP A O   1 
ATOM   3585  C CB  . ASP A 1 428 ? 25.619  19.308  -44.508 1.00 38.94  ? 428 ASP A CB  1 
ATOM   3586  C CG  . ASP A 1 428 ? 26.768  20.285  -44.692 1.00 39.82  ? 428 ASP A CG  1 
ATOM   3587  O OD1 . ASP A 1 428 ? 26.766  21.373  -44.077 1.00 42.29  ? 428 ASP A OD1 1 
ATOM   3588  O OD2 . ASP A 1 428 ? 27.704  19.948  -45.440 1.00 39.15  ? 428 ASP A OD2 1 
ATOM   3589  N N   . ASP A 1 429 ? 24.933  21.209  -41.613 1.00 40.13  ? 429 ASP A N   1 
ATOM   3590  C CA  . ASP A 1 429 ? 25.365  21.423  -40.226 1.00 42.11  ? 429 ASP A CA  1 
ATOM   3591  C C   . ASP A 1 429 ? 24.221  21.745  -39.260 1.00 41.15  ? 429 ASP A C   1 
ATOM   3592  O O   . ASP A 1 429 ? 24.450  22.237  -38.152 1.00 43.95  ? 429 ASP A O   1 
ATOM   3593  C CB  . ASP A 1 429 ? 26.511  22.449  -40.129 1.00 46.21  ? 429 ASP A CB  1 
ATOM   3594  C CG  . ASP A 1 429 ? 26.069  23.882  -40.436 1.00 51.81  ? 429 ASP A CG  1 
ATOM   3595  O OD1 . ASP A 1 429 ? 24.879  24.125  -40.738 1.00 50.36  ? 429 ASP A OD1 1 
ATOM   3596  O OD2 . ASP A 1 429 ? 26.941  24.780  -40.374 1.00 57.08  ? 429 ASP A OD2 1 
ATOM   3597  N N   . ASN A 1 430 ? 22.994  21.472  -39.694 1.00 38.07  ? 430 ASN A N   1 
ATOM   3598  C CA  . ASN A 1 430 ? 21.836  21.571  -38.832 1.00 36.90  ? 430 ASN A CA  1 
ATOM   3599  C C   . ASN A 1 430 ? 21.086  20.251  -38.749 1.00 34.27  ? 430 ASN A C   1 
ATOM   3600  O O   . ASN A 1 430 ? 19.907  20.181  -39.095 1.00 35.09  ? 430 ASN A O   1 
ATOM   3601  C CB  . ASN A 1 430 ? 20.898  22.699  -39.288 1.00 39.62  ? 430 ASN A CB  1 
ATOM   3602  C CG  . ASN A 1 430 ? 20.058  23.268  -38.133 1.00 43.69  ? 430 ASN A CG  1 
ATOM   3603  O OD1 . ASN A 1 430 ? 19.821  22.589  -37.114 1.00 42.50  ? 430 ASN A OD1 1 
ATOM   3604  N ND2 . ASN A 1 430 ? 19.605  24.513  -38.287 1.00 43.08  ? 430 ASN A ND2 1 
ATOM   3605  N N   . PRO A 1 431 ? 21.763  19.188  -38.278 1.00 32.07  ? 431 PRO A N   1 
ATOM   3606  C CA  . PRO A 1 431 ? 21.078  17.916  -38.127 1.00 31.11  ? 431 PRO A CA  1 
ATOM   3607  C C   . PRO A 1 431 ? 19.915  17.961  -37.137 1.00 31.21  ? 431 PRO A C   1 
ATOM   3608  O O   . PRO A 1 431 ? 18.901  17.288  -37.350 1.00 33.17  ? 431 PRO A O   1 
ATOM   3609  C CB  . PRO A 1 431 ? 22.191  16.968  -37.644 1.00 31.77  ? 431 PRO A CB  1 
ATOM   3610  C CG  . PRO A 1 431 ? 23.241  17.847  -37.091 1.00 31.96  ? 431 PRO A CG  1 
ATOM   3611  C CD  . PRO A 1 431 ? 23.187  19.094  -37.916 1.00 31.65  ? 431 PRO A CD  1 
ATOM   3612  N N   . ALA A 1 432 ? 20.028  18.783  -36.094 1.00 30.46  ? 432 ALA A N   1 
ATOM   3613  C CA  . ALA A 1 432 ? 18.987  18.855  -35.073 1.00 29.38  ? 432 ALA A CA  1 
ATOM   3614  C C   . ALA A 1 432 ? 17.643  19.304  -35.684 1.00 28.93  ? 432 ALA A C   1 
ATOM   3615  O O   . ALA A 1 432 ? 16.597  18.698  -35.428 1.00 27.15  ? 432 ALA A O   1 
ATOM   3616  C CB  . ALA A 1 432 ? 19.422  19.768  -33.926 1.00 29.64  ? 432 ALA A CB  1 
ATOM   3617  N N   . ARG A 1 433 ? 17.689  20.335  -36.521 1.00 28.90  ? 433 ARG A N   1 
ATOM   3618  C CA  . ARG A 1 433 ? 16.518  20.759  -37.271 1.00 30.33  ? 433 ARG A CA  1 
ATOM   3619  C C   . ARG A 1 433 ? 15.942  19.616  -38.132 1.00 30.32  ? 433 ARG A C   1 
ATOM   3620  O O   . ARG A 1 433 ? 14.750  19.372  -38.115 1.00 32.24  ? 433 ARG A O   1 
ATOM   3621  C CB  . ARG A 1 433 ? 16.861  21.974  -38.149 1.00 31.80  ? 433 ARG A CB  1 
ATOM   3622  C CG  . ARG A 1 433 ? 15.691  22.434  -38.990 1.00 33.13  ? 433 ARG A CG  1 
ATOM   3623  C CD  . ARG A 1 433 ? 16.013  23.579  -39.933 1.00 35.74  ? 433 ARG A CD  1 
ATOM   3624  N NE  . ARG A 1 433 ? 14.958  23.689  -40.948 1.00 37.32  ? 433 ARG A NE  1 
ATOM   3625  C CZ  . ARG A 1 433 ? 15.093  24.303  -42.124 1.00 37.80  ? 433 ARG A CZ  1 
ATOM   3626  N NH1 . ARG A 1 433 ? 16.232  24.898  -42.456 1.00 37.49  ? 433 ARG A NH1 1 
ATOM   3627  N NH2 . ARG A 1 433 ? 14.077  24.323  -42.968 1.00 39.66  ? 433 ARG A NH2 1 
ATOM   3628  N N   . PHE A 1 434 ? 16.796  18.934  -38.886 1.00 29.68  ? 434 PHE A N   1 
ATOM   3629  C CA  . PHE A 1 434 ? 16.380  17.766  -39.667 1.00 30.08  ? 434 PHE A CA  1 
ATOM   3630  C C   . PHE A 1 434 ? 15.694  16.758  -38.761 1.00 29.19  ? 434 PHE A C   1 
ATOM   3631  O O   . PHE A 1 434 ? 14.575  16.305  -39.053 1.00 27.53  ? 434 PHE A O   1 
ATOM   3632  C CB  . PHE A 1 434 ? 17.604  17.132  -40.370 1.00 29.61  ? 434 PHE A CB  1 
ATOM   3633  C CG  . PHE A 1 434 ? 17.291  15.912  -41.215 1.00 29.08  ? 434 PHE A CG  1 
ATOM   3634  C CD1 . PHE A 1 434 ? 16.884  16.045  -42.530 1.00 29.67  ? 434 PHE A CD1 1 
ATOM   3635  C CD2 . PHE A 1 434 ? 17.532  14.624  -40.730 1.00 30.50  ? 434 PHE A CD2 1 
ATOM   3636  C CE1 . PHE A 1 434 ? 16.664  14.927  -43.330 1.00 30.08  ? 434 PHE A CE1 1 
ATOM   3637  C CE2 . PHE A 1 434 ? 17.325  13.499  -41.533 1.00 28.96  ? 434 PHE A CE2 1 
ATOM   3638  C CZ  . PHE A 1 434 ? 16.875  13.650  -42.826 1.00 27.69  ? 434 PHE A CZ  1 
ATOM   3639  N N   . LEU A 1 435 ? 16.343  16.430  -37.642 1.00 30.11  ? 435 LEU A N   1 
ATOM   3640  C CA  . LEU A 1 435 ? 15.724  15.531  -36.674 1.00 30.90  ? 435 LEU A CA  1 
ATOM   3641  C C   . LEU A 1 435 ? 14.350  16.027  -36.227 1.00 31.00  ? 435 LEU A C   1 
ATOM   3642  O O   . LEU A 1 435 ? 13.364  15.294  -36.330 1.00 32.31  ? 435 LEU A O   1 
ATOM   3643  C CB  . LEU A 1 435 ? 16.613  15.315  -35.467 1.00 32.59  ? 435 LEU A CB  1 
ATOM   3644  C CG  . LEU A 1 435 ? 16.647  13.877  -34.940 1.00 34.29  ? 435 LEU A CG  1 
ATOM   3645  C CD1 . LEU A 1 435 ? 17.003  13.898  -33.468 1.00 32.65  ? 435 LEU A CD1 1 
ATOM   3646  C CD2 . LEU A 1 435 ? 15.346  13.134  -35.165 1.00 32.56  ? 435 LEU A CD2 1 
ATOM   3647  N N   . GLN A 1 436 ? 14.284  17.274  -35.759 1.00 30.41  ? 436 GLN A N   1 
ATOM   3648  C CA  . GLN A 1 436 ? 13.037  17.831  -35.266 1.00 31.54  ? 436 GLN A CA  1 
ATOM   3649  C C   . GLN A 1 436 ? 11.978  17.894  -36.339 1.00 32.32  ? 436 GLN A C   1 
ATOM   3650  O O   . GLN A 1 436 ? 10.811  17.580  -36.080 1.00 34.85  ? 436 GLN A O   1 
ATOM   3651  C CB  . GLN A 1 436 ? 13.237  19.224  -34.678 1.00 32.87  ? 436 GLN A CB  1 
ATOM   3652  C CG  . GLN A 1 436 ? 14.079  19.254  -33.428 1.00 34.66  ? 436 GLN A CG  1 
ATOM   3653  C CD  . GLN A 1 436 ? 14.729  20.601  -33.214 1.00 39.08  ? 436 GLN A CD  1 
ATOM   3654  O OE1 . GLN A 1 436 ? 14.590  21.508  -34.038 1.00 43.15  ? 436 GLN A OE1 1 
ATOM   3655  N NE2 . GLN A 1 436 ? 15.459  20.737  -32.114 1.00 38.61  ? 436 GLN A NE2 1 
ATOM   3656  N N   . LYS A 1 437 ? 12.357  18.304  -37.543 1.00 31.05  ? 437 LYS A N   1 
ATOM   3657  C CA  . LYS A 1 437 ? 11.386  18.350  -38.631 1.00 33.09  ? 437 LYS A CA  1 
ATOM   3658  C C   . LYS A 1 437 ? 10.819  16.937  -38.880 1.00 30.84  ? 437 LYS A C   1 
ATOM   3659  O O   . LYS A 1 437 ? 9.630   16.767  -39.091 1.00 33.33  ? 437 LYS A O   1 
ATOM   3660  C CB  . LYS A 1 437 ? 12.004  18.961  -39.907 1.00 34.89  ? 437 LYS A CB  1 
ATOM   3661  C CG  . LYS A 1 437 ? 11.000  19.276  -40.998 1.00 37.45  ? 437 LYS A CG  1 
ATOM   3662  C CD  . LYS A 1 437 ? 11.717  19.767  -42.240 1.00 43.09  ? 437 LYS A CD  1 
ATOM   3663  C CE  . LYS A 1 437 ? 10.971  19.380  -43.511 1.00 48.45  ? 437 LYS A CE  1 
ATOM   3664  N NZ  . LYS A 1 437 ? 9.918   20.369  -43.885 1.00 54.71  ? 437 LYS A NZ  1 
ATOM   3665  N N   . ALA A 1 438 ? 11.661  15.924  -38.782 1.00 29.05  ? 438 ALA A N   1 
ATOM   3666  C CA  . ALA A 1 438 ? 11.204  14.550  -38.982 1.00 28.30  ? 438 ALA A CA  1 
ATOM   3667  C C   . ALA A 1 438 ? 10.226  14.095  -37.887 1.00 29.86  ? 438 ALA A C   1 
ATOM   3668  O O   . ALA A 1 438 ? 9.338   13.296  -38.145 1.00 29.89  ? 438 ALA A O   1 
ATOM   3669  C CB  . ALA A 1 438 ? 12.392  13.611  -39.071 1.00 26.74  ? 438 ALA A CB  1 
ATOM   3670  N N   . MET A 1 439 ? 10.380  14.610  -36.671 1.00 30.81  ? 439 MET A N   1 
ATOM   3671  C CA  . MET A 1 439 ? 9.479   14.214  -35.570 1.00 33.32  ? 439 MET A CA  1 
ATOM   3672  C C   . MET A 1 439 ? 8.175   15.044  -35.460 1.00 35.06  ? 439 MET A C   1 
ATOM   3673  O O   . MET A 1 439 ? 7.327   14.751  -34.626 1.00 35.64  ? 439 MET A O   1 
ATOM   3674  C CB  . MET A 1 439 ? 10.232  14.167  -34.243 1.00 30.31  ? 439 MET A CB  1 
ATOM   3675  C CG  . MET A 1 439 ? 11.272  13.060  -34.191 1.00 31.04  ? 439 MET A CG  1 
ATOM   3676  S SD  . MET A 1 439 ? 10.517  11.410  -34.249 1.00 32.77  ? 439 MET A SD  1 
ATOM   3677  C CE  . MET A 1 439 ? 10.712  10.895  -35.967 1.00 29.80  ? 439 MET A CE  1 
ATOM   3678  N N   . ASP A 1 440 ? 8.035   16.056  -36.314 1.00 36.17  ? 440 ASP A N   1 
ATOM   3679  C CA  . ASP A 1 440 ? 6.788   16.816  -36.479 1.00 41.00  ? 440 ASP A CA  1 
ATOM   3680  C C   . ASP A 1 440 ? 5.585   15.908  -36.793 1.00 43.75  ? 440 ASP A C   1 
ATOM   3681  O O   . ASP A 1 440 ? 5.695   14.943  -37.552 1.00 39.61  ? 440 ASP A O   1 
ATOM   3682  C CB  . ASP A 1 440 ? 6.932   17.861  -37.611 1.00 41.39  ? 440 ASP A CB  1 
ATOM   3683  C CG  . ASP A 1 440 ? 7.615   19.163  -37.158 1.00 43.12  ? 440 ASP A CG  1 
ATOM   3684  O OD1 . ASP A 1 440 ? 7.722   19.412  -35.945 1.00 44.92  ? 440 ASP A OD1 1 
ATOM   3685  O OD2 . ASP A 1 440 ? 8.003   19.973  -38.035 1.00 46.45  ? 440 ASP A OD2 1 
ATOM   3686  N N   . PHE A 1 441 ? 4.432   16.293  -36.255 1.00 48.33  ? 441 PHE A N   1 
ATOM   3687  C CA  . PHE A 1 441 ? 3.201   15.499  -36.249 1.00 56.35  ? 441 PHE A CA  1 
ATOM   3688  C C   . PHE A 1 441 ? 2.559   15.132  -37.615 1.00 60.40  ? 441 PHE A C   1 
ATOM   3689  O O   . PHE A 1 441 ? 2.123   13.990  -37.794 1.00 62.11  ? 441 PHE A O   1 
ATOM   3690  C CB  . PHE A 1 441 ? 2.179   16.199  -35.327 1.00 62.78  ? 441 PHE A CB  1 
ATOM   3691  C CG  . PHE A 1 441 ? 0.811   15.563  -35.301 1.00 68.58  ? 441 PHE A CG  1 
ATOM   3692  C CD1 . PHE A 1 441 ? 0.564   14.429  -34.525 1.00 68.60  ? 441 PHE A CD1 1 
ATOM   3693  C CD2 . PHE A 1 441 ? -0.255  16.142  -35.998 1.00 71.74  ? 441 PHE A CD2 1 
ATOM   3694  C CE1 . PHE A 1 441 ? -0.706  13.869  -34.472 1.00 69.77  ? 441 PHE A CE1 1 
ATOM   3695  C CE2 . PHE A 1 441 ? -1.526  15.582  -35.949 1.00 72.53  ? 441 PHE A CE2 1 
ATOM   3696  C CZ  . PHE A 1 441 ? -1.751  14.445  -35.184 1.00 71.53  ? 441 PHE A CZ  1 
ATOM   3697  N N   . PRO A 1 442 ? 2.480   16.088  -38.571 1.00 61.53  ? 442 PRO A N   1 
ATOM   3698  C CA  . PRO A 1 442 ? 1.600   15.877  -39.742 1.00 64.39  ? 442 PRO A CA  1 
ATOM   3699  C C   . PRO A 1 442 ? 1.694   14.501  -40.429 1.00 63.67  ? 442 PRO A C   1 
ATOM   3700  O O   . PRO A 1 442 ? 0.669   13.957  -40.843 1.00 67.56  ? 442 PRO A O   1 
ATOM   3701  C CB  . PRO A 1 442 ? 2.023   16.996  -40.699 1.00 62.09  ? 442 PRO A CB  1 
ATOM   3702  C CG  . PRO A 1 442 ? 2.433   18.095  -39.783 1.00 62.67  ? 442 PRO A CG  1 
ATOM   3703  C CD  . PRO A 1 442 ? 3.136   17.409  -38.632 1.00 63.73  ? 442 PRO A CD  1 
ATOM   3704  N N   . PHE A 1 443 ? 2.899   13.947  -40.534 1.00 61.41  ? 443 PHE A N   1 
ATOM   3705  C CA  . PHE A 1 443 ? 3.105   12.670  -41.230 1.00 64.53  ? 443 PHE A CA  1 
ATOM   3706  C C   . PHE A 1 443 ? 2.355   11.497  -40.566 1.00 63.49  ? 443 PHE A C   1 
ATOM   3707  O O   . PHE A 1 443 ? 1.916   10.563  -41.251 1.00 65.71  ? 443 PHE A O   1 
ATOM   3708  C CB  . PHE A 1 443 ? 4.614   12.348  -41.348 1.00 62.25  ? 443 PHE A CB  1 
ATOM   3709  C CG  . PHE A 1 443 ? 5.164   11.616  -40.158 1.00 58.55  ? 443 PHE A CG  1 
ATOM   3710  C CD1 . PHE A 1 443 ? 5.501   12.310  -38.992 1.00 55.82  ? 443 PHE A CD1 1 
ATOM   3711  C CD2 . PHE A 1 443 ? 5.278   10.221  -40.171 1.00 57.11  ? 443 PHE A CD2 1 
ATOM   3712  C CE1 . PHE A 1 443 ? 5.980   11.637  -37.877 1.00 53.77  ? 443 PHE A CE1 1 
ATOM   3713  C CE2 . PHE A 1 443 ? 5.752   9.539   -39.055 1.00 55.03  ? 443 PHE A CE2 1 
ATOM   3714  C CZ  . PHE A 1 443 ? 6.105   10.248  -37.910 1.00 56.08  ? 443 PHE A CZ  1 
ATOM   3715  N N   . ILE A 1 444 ? 2.225   11.549  -39.238 1.00 62.11  ? 444 ILE A N   1 
ATOM   3716  C CA  . ILE A 1 444 ? 1.636   10.439  -38.452 1.00 65.40  ? 444 ILE A CA  1 
ATOM   3717  C C   . ILE A 1 444 ? 0.167   10.739  -38.071 1.00 67.78  ? 444 ILE A C   1 
ATOM   3718  O O   . ILE A 1 444 ? -0.445  9.995   -37.290 1.00 68.42  ? 444 ILE A O   1 
ATOM   3719  C CB  . ILE A 1 444 ? 2.518   10.094  -37.192 1.00 59.14  ? 444 ILE A CB  1 
ATOM   3720  C CG1 . ILE A 1 444 ? 2.033   8.832   -36.445 1.00 59.38  ? 444 ILE A CG1 1 
ATOM   3721  C CG2 . ILE A 1 444 ? 2.585   11.268  -36.232 1.00 58.64  ? 444 ILE A CG2 1 
ATOM   3722  C CD1 . ILE A 1 444 ? 2.596   7.517   -36.955 1.00 52.08  ? 444 ILE A CD1 1 
ATOM   3723  N N   . CYS A 1 445 ? -0.398  11.800  -38.663 1.00 69.28  ? 445 CYS A N   1 
ATOM   3724  C CA  . CYS A 1 445 ? -1.722  12.324  -38.267 1.00 73.05  ? 445 CYS A CA  1 
ATOM   3725  C C   . CYS A 1 445 ? -2.880  11.316  -38.398 1.00 73.25  ? 445 CYS A C   1 
ATOM   3726  O O   . CYS A 1 445 ? -3.795  11.307  -37.560 1.00 71.58  ? 445 CYS A O   1 
ATOM   3727  C CB  . CYS A 1 445 ? -2.052  13.668  -38.977 1.00 78.33  ? 445 CYS A CB  1 
ATOM   3728  S SG  . CYS A 1 445 ? -2.486  13.611  -40.750 1.00 81.55  ? 445 CYS A SG  1 
ATOM   3729  N N   . ASN A 1 446 ? -2.819  10.457  -39.424 1.00 70.77  ? 446 ASN A N   1 
ATOM   3730  C CA  . ASN A 1 446 ? -3.862  9.436   -39.662 1.00 69.49  ? 446 ASN A CA  1 
ATOM   3731  C C   . ASN A 1 446 ? -3.713  8.162   -38.807 1.00 67.64  ? 446 ASN A C   1 
ATOM   3732  O O   . ASN A 1 446 ? -4.381  7.148   -39.046 1.00 68.24  ? 446 ASN A O   1 
ATOM   3733  C CB  . ASN A 1 446 ? -3.982  9.103   -41.161 1.00 69.78  ? 446 ASN A CB  1 
ATOM   3734  C CG  . ASN A 1 446 ? -5.030  9.961   -41.871 1.00 71.60  ? 446 ASN A CG  1 
ATOM   3735  O OD1 . ASN A 1 446 ? -6.176  10.076  -41.413 1.00 69.53  ? 446 ASN A OD1 1 
ATOM   3736  N ND2 . ASN A 1 446 ? -4.645  10.555  -43.004 1.00 67.91  ? 446 ASN A ND2 1 
ATOM   3737  N N   . SER A 1 447 ? -2.830  8.234   -37.815 1.00 64.82  ? 447 SER A N   1 
ATOM   3738  C CA  . SER A 1 447 ? -2.703  7.212   -36.790 1.00 61.21  ? 447 SER A CA  1 
ATOM   3739  C C   . SER A 1 447 ? -3.175  7.839   -35.478 1.00 61.78  ? 447 SER A C   1 
ATOM   3740  O O   . SER A 1 447 ? -3.269  7.166   -34.451 1.00 63.35  ? 447 SER A O   1 
ATOM   3741  C CB  . SER A 1 447 ? -1.236  6.795   -36.669 1.00 62.30  ? 447 SER A CB  1 
ATOM   3742  O OG  . SER A 1 447 ? -1.086  5.391   -36.635 1.00 63.63  ? 447 SER A OG  1 
ATOM   3743  N N   . PHE A 1 448 ? -3.477  9.136   -35.536 1.00 58.57  ? 448 PHE A N   1 
ATOM   3744  C CA  . PHE A 1 448 ? -3.822  9.928   -34.355 1.00 57.17  ? 448 PHE A CA  1 
ATOM   3745  C C   . PHE A 1 448 ? -5.205  10.567  -34.467 1.00 52.49  ? 448 PHE A C   1 
ATOM   3746  O O   . PHE A 1 448 ? -5.362  11.774  -34.264 1.00 53.24  ? 448 PHE A O   1 
ATOM   3747  C CB  . PHE A 1 448 ? -2.773  11.023  -34.138 1.00 61.23  ? 448 PHE A CB  1 
ATOM   3748  C CG  . PHE A 1 448 ? -1.770  10.703  -33.075 1.00 58.51  ? 448 PHE A CG  1 
ATOM   3749  C CD1 . PHE A 1 448 ? -0.929  9.601   -33.197 1.00 60.10  ? 448 PHE A CD1 1 
ATOM   3750  C CD2 . PHE A 1 448 ? -1.650  11.519  -31.955 1.00 58.69  ? 448 PHE A CD2 1 
ATOM   3751  C CE1 . PHE A 1 448 ? -0.006  9.302   -32.201 1.00 57.17  ? 448 PHE A CE1 1 
ATOM   3752  C CE2 . PHE A 1 448 ? -0.719  11.237  -30.967 1.00 57.43  ? 448 PHE A CE2 1 
ATOM   3753  C CZ  . PHE A 1 448 ? 0.102   10.126  -31.091 1.00 57.83  ? 448 PHE A CZ  1 
ATOM   3754  N N   . THR A 1 449 ? -6.205  9.753   -34.783 1.00 48.45  ? 449 THR A N   1 
ATOM   3755  C CA  . THR A 1 449 ? -7.550  10.249  -35.021 1.00 47.78  ? 449 THR A CA  1 
ATOM   3756  C C   . THR A 1 449 ? -8.504  9.809   -33.909 1.00 47.64  ? 449 THR A C   1 
ATOM   3757  O O   . THR A 1 449 ? -8.097  9.137   -32.946 1.00 46.38  ? 449 THR A O   1 
ATOM   3758  C CB  . THR A 1 449 ? -8.092  9.732   -36.361 1.00 47.64  ? 449 THR A CB  1 
ATOM   3759  O OG1 . THR A 1 449 ? -8.357  8.329   -36.252 1.00 47.07  ? 449 THR A OG1 1 
ATOM   3760  C CG2 . THR A 1 449 ? -7.081  9.958   -37.468 1.00 46.76  ? 449 THR A CG2 1 
ATOM   3761  N N   . LYS A 1 450 ? -9.777  10.177  -34.063 1.00 47.82  ? 450 LYS A N   1 
ATOM   3762  C CA  . LYS A 1 450 ? -10.832 9.773   -33.136 1.00 46.59  ? 450 LYS A CA  1 
ATOM   3763  C C   . LYS A 1 450 ? -11.009 8.261   -33.165 1.00 43.52  ? 450 LYS A C   1 
ATOM   3764  O O   . LYS A 1 450 ? -11.461 7.667   -32.195 1.00 42.60  ? 450 LYS A O   1 
ATOM   3765  C CB  . LYS A 1 450 ? -12.175 10.436  -33.488 1.00 51.60  ? 450 LYS A CB  1 
ATOM   3766  C CG  . LYS A 1 450 ? -12.095 11.712  -34.314 1.00 56.48  ? 450 LYS A CG  1 
ATOM   3767  C CD  . LYS A 1 450 ? -13.478 12.289  -34.604 1.00 58.73  ? 450 LYS A CD  1 
ATOM   3768  C CE  . LYS A 1 450 ? -13.965 11.934  -36.001 1.00 60.66  ? 450 LYS A CE  1 
ATOM   3769  N NZ  . LYS A 1 450 ? -13.194 12.626  -37.078 1.00 65.30  ? 450 LYS A NZ  1 
ATOM   3770  N N   . PHE A 1 451 ? -10.678 7.646   -34.292 1.00 42.31  ? 451 PHE A N   1 
ATOM   3771  C CA  . PHE A 1 451 ? -10.789 6.199   -34.416 1.00 42.79  ? 451 PHE A CA  1 
ATOM   3772  C C   . PHE A 1 451 ? -9.832  5.495   -33.469 1.00 41.85  ? 451 PHE A C   1 
ATOM   3773  O O   . PHE A 1 451 ? -10.178 4.488   -32.873 1.00 41.30  ? 451 PHE A O   1 
ATOM   3774  C CB  . PHE A 1 451 ? -10.511 5.757   -35.843 1.00 44.29  ? 451 PHE A CB  1 
ATOM   3775  C CG  . PHE A 1 451 ? -11.745 5.592   -36.681 1.00 48.24  ? 451 PHE A CG  1 
ATOM   3776  C CD1 . PHE A 1 451 ? -12.721 4.660   -36.334 1.00 49.16  ? 451 PHE A CD1 1 
ATOM   3777  C CD2 . PHE A 1 451 ? -11.915 6.337   -37.845 1.00 49.89  ? 451 PHE A CD2 1 
ATOM   3778  C CE1 . PHE A 1 451 ? -13.853 4.492   -37.116 1.00 51.55  ? 451 PHE A CE1 1 
ATOM   3779  C CE2 . PHE A 1 451 ? -13.043 6.166   -38.637 1.00 49.86  ? 451 PHE A CE2 1 
ATOM   3780  C CZ  . PHE A 1 451 ? -14.007 5.242   -38.276 1.00 50.68  ? 451 PHE A CZ  1 
ATOM   3781  N N   . GLU A 1 452 ? -8.625  6.033   -33.335 1.00 40.72  ? 452 GLU A N   1 
ATOM   3782  C CA  . GLU A 1 452 ? -7.642  5.429   -32.469 1.00 40.49  ? 452 GLU A CA  1 
ATOM   3783  C C   . GLU A 1 452 ? -7.869  5.773   -31.001 1.00 38.75  ? 452 GLU A C   1 
ATOM   3784  O O   . GLU A 1 452 ? -7.702  4.917   -30.142 1.00 36.18  ? 452 GLU A O   1 
ATOM   3785  C CB  . GLU A 1 452 ? -6.225  5.801   -32.901 1.00 42.01  ? 452 GLU A CB  1 
ATOM   3786  C CG  . GLU A 1 452 ? -5.744  5.047   -34.142 1.00 46.69  ? 452 GLU A CG  1 
ATOM   3787  C CD  . GLU A 1 452 ? -6.204  5.681   -35.456 1.00 47.72  ? 452 GLU A CD  1 
ATOM   3788  O OE1 . GLU A 1 452 ? -6.063  5.023   -36.509 1.00 50.99  ? 452 GLU A OE1 1 
ATOM   3789  O OE2 . GLU A 1 452 ? -6.689  6.838   -35.448 1.00 46.75  ? 452 GLU A OE2 1 
ATOM   3790  N N   . PHE A 1 453 ? -8.280  7.012   -30.722 1.00 38.01  ? 453 PHE A N   1 
ATOM   3791  C CA  . PHE A 1 453 ? -8.226  7.542   -29.351 1.00 37.04  ? 453 PHE A CA  1 
ATOM   3792  C C   . PHE A 1 453 ? -9.561  7.646   -28.604 1.00 37.11  ? 453 PHE A C   1 
ATOM   3793  O O   . PHE A 1 453 ? -9.574  7.932   -27.406 1.00 38.24  ? 453 PHE A O   1 
ATOM   3794  C CB  . PHE A 1 453 ? -7.497  8.891   -29.321 1.00 37.38  ? 453 PHE A CB  1 
ATOM   3795  C CG  . PHE A 1 453 ? -6.028  8.777   -29.558 1.00 39.03  ? 453 PHE A CG  1 
ATOM   3796  C CD1 . PHE A 1 453 ? -5.192  8.279   -28.572 1.00 39.54  ? 453 PHE A CD1 1 
ATOM   3797  C CD2 . PHE A 1 453 ? -5.477  9.141   -30.772 1.00 40.44  ? 453 PHE A CD2 1 
ATOM   3798  C CE1 . PHE A 1 453 ? -3.838  8.145   -28.793 1.00 39.99  ? 453 PHE A CE1 1 
ATOM   3799  C CE2 . PHE A 1 453 ? -4.123  9.015   -30.991 1.00 40.44  ? 453 PHE A CE2 1 
ATOM   3800  C CZ  . PHE A 1 453 ? -3.304  8.512   -30.004 1.00 40.59  ? 453 PHE A CZ  1 
ATOM   3801  N N   . ASN A 1 454 ? -10.675 7.413   -29.292 1.00 35.95  ? 454 ASN A N   1 
ATOM   3802  C CA  . ASN A 1 454 ? -11.970 7.493   -28.641 1.00 36.16  ? 454 ASN A CA  1 
ATOM   3803  C C   . ASN A 1 454 ? -12.132 6.410   -27.576 1.00 36.27  ? 454 ASN A C   1 
ATOM   3804  O O   . ASN A 1 454 ? -11.570 5.318   -27.698 1.00 34.86  ? 454 ASN A O   1 
ATOM   3805  C CB  . ASN A 1 454 ? -13.110 7.401   -29.671 1.00 37.58  ? 454 ASN A CB  1 
ATOM   3806  C CG  . ASN A 1 454 ? -13.436 5.967   -30.059 1.00 36.59  ? 454 ASN A CG  1 
ATOM   3807  O OD1 . ASN A 1 454 ? -14.254 5.321   -29.414 1.00 37.53  ? 454 ASN A OD1 1 
ATOM   3808  N ND2 . ASN A 1 454 ? -12.756 5.450   -31.080 1.00 35.49  ? 454 ASN A ND2 1 
ATOM   3809  N N   . THR A 1 455 ? -12.894 6.716   -26.528 1.00 37.05  ? 455 THR A N   1 
ATOM   3810  C CA  . THR A 1 455 ? -13.373 5.678   -25.617 1.00 39.01  ? 455 THR A CA  1 
ATOM   3811  C C   . THR A 1 455 ? -14.907 5.628   -25.580 1.00 41.02  ? 455 THR A C   1 
ATOM   3812  O O   . THR A 1 455 ? -15.513 5.444   -24.522 1.00 43.02  ? 455 THR A O   1 
ATOM   3813  C CB  . THR A 1 455 ? -12.781 5.800   -24.201 1.00 37.55  ? 455 THR A CB  1 
ATOM   3814  O OG1 . THR A 1 455 ? -12.808 7.165   -23.793 1.00 39.19  ? 455 THR A OG1 1 
ATOM   3815  C CG2 . THR A 1 455 ? -11.339 5.298   -24.176 1.00 37.47  ? 455 THR A CG2 1 
ATOM   3816  N N   . VAL A 1 456 ? -15.514 5.788   -26.755 1.00 41.79  ? 456 VAL A N   1 
ATOM   3817  C CA  . VAL A 1 456 ? -16.954 5.613   -26.933 1.00 41.85  ? 456 VAL A CA  1 
ATOM   3818  C C   . VAL A 1 456 ? -17.214 4.140   -27.273 1.00 40.98  ? 456 VAL A C   1 
ATOM   3819  O O   . VAL A 1 456 ? -17.759 3.396   -26.457 1.00 38.00  ? 456 VAL A O   1 
ATOM   3820  C CB  . VAL A 1 456 ? -17.494 6.540   -28.055 1.00 44.60  ? 456 VAL A CB  1 
ATOM   3821  C CG1 . VAL A 1 456 ? -19.000 6.379   -28.216 1.00 44.44  ? 456 VAL A CG1 1 
ATOM   3822  C CG2 . VAL A 1 456 ? -17.135 7.996   -27.763 1.00 44.65  ? 456 VAL A CG2 1 
ATOM   3823  N N   . PHE A 1 457 ? -16.779 3.713   -28.461 1.00 39.79  ? 457 PHE A N   1 
ATOM   3824  C CA  . PHE A 1 457 ? -16.787 2.291   -28.794 1.00 40.75  ? 457 PHE A CA  1 
ATOM   3825  C C   . PHE A 1 457 ? -15.498 1.535   -28.411 1.00 41.28  ? 457 PHE A C   1 
ATOM   3826  O O   . PHE A 1 457 ? -15.556 0.360   -28.061 1.00 43.04  ? 457 PHE A O   1 
ATOM   3827  C CB  . PHE A 1 457 ? -17.171 2.047   -30.266 1.00 40.09  ? 457 PHE A CB  1 
ATOM   3828  C CG  . PHE A 1 457 ? -16.371 2.845   -31.258 1.00 40.26  ? 457 PHE A CG  1 
ATOM   3829  C CD1 . PHE A 1 457 ? -15.190 2.335   -31.793 1.00 39.26  ? 457 PHE A CD1 1 
ATOM   3830  C CD2 . PHE A 1 457 ? -16.822 4.089   -31.698 1.00 40.77  ? 457 PHE A CD2 1 
ATOM   3831  C CE1 . PHE A 1 457 ? -14.463 3.060   -32.725 1.00 38.96  ? 457 PHE A CE1 1 
ATOM   3832  C CE2 . PHE A 1 457 ? -16.101 4.816   -32.634 1.00 40.42  ? 457 PHE A CE2 1 
ATOM   3833  C CZ  . PHE A 1 457 ? -14.918 4.302   -33.148 1.00 39.13  ? 457 PHE A CZ  1 
ATOM   3834  N N   . ASN A 1 458 ? -14.348 2.204   -28.483 1.00 40.15  ? 458 ASN A N   1 
ATOM   3835  C CA  . ASN A 1 458 ? -13.064 1.591   -28.103 1.00 39.47  ? 458 ASN A CA  1 
ATOM   3836  C C   . ASN A 1 458 ? -12.854 1.528   -26.599 1.00 38.70  ? 458 ASN A C   1 
ATOM   3837  O O   . ASN A 1 458 ? -13.085 2.511   -25.892 1.00 41.01  ? 458 ASN A O   1 
ATOM   3838  C CB  . ASN A 1 458 ? -11.898 2.378   -28.707 1.00 36.93  ? 458 ASN A CB  1 
ATOM   3839  C CG  . ASN A 1 458 ? -11.517 1.902   -30.093 1.00 37.59  ? 458 ASN A CG  1 
ATOM   3840  O OD1 . ASN A 1 458 ? -12.043 0.904   -30.594 1.00 38.85  ? 458 ASN A OD1 1 
ATOM   3841  N ND2 . ASN A 1 458 ? -10.596 2.613   -30.724 1.00 34.60  ? 458 ASN A ND2 1 
ATOM   3842  N N   . ASP A 1 459 ? -12.363 0.401   -26.107 1.00 38.78  ? 459 ASP A N   1 
ATOM   3843  C CA  . ASP A 1 459 ? -11.842 0.351   -24.727 1.00 39.20  ? 459 ASP A CA  1 
ATOM   3844  C C   . ASP A 1 459 ? -10.545 1.143   -24.581 1.00 37.80  ? 459 ASP A C   1 
ATOM   3845  O O   . ASP A 1 459 ? -9.874  1.484   -25.566 1.00 36.87  ? 459 ASP A O   1 
ATOM   3846  C CB  . ASP A 1 459 ? -11.591 -1.088  -24.277 1.00 40.75  ? 459 ASP A CB  1 
ATOM   3847  C CG  . ASP A 1 459 ? -12.868 -1.879  -24.128 1.00 44.95  ? 459 ASP A CG  1 
ATOM   3848  O OD1 . ASP A 1 459 ? -13.686 -1.537  -23.235 1.00 46.33  ? 459 ASP A OD1 1 
ATOM   3849  O OD2 . ASP A 1 459 ? -13.045 -2.849  -24.896 1.00 46.14  ? 459 ASP A OD2 1 
ATOM   3850  N N   . GLN A 1 460 ? -10.181 1.404   -23.341 1.00 36.90  ? 460 GLN A N   1 
ATOM   3851  C CA  . GLN A 1 460 ? -8.943  2.090   -23.037 1.00 36.29  ? 460 GLN A CA  1 
ATOM   3852  C C   . GLN A 1 460 ? -7.729  1.242   -23.427 1.00 34.51  ? 460 GLN A C   1 
ATOM   3853  O O   . GLN A 1 460 ? -6.744  1.764   -23.955 1.00 33.51  ? 460 GLN A O   1 
ATOM   3854  C CB  . GLN A 1 460 ? -8.924  2.444   -21.553 1.00 37.43  ? 460 GLN A CB  1 
ATOM   3855  C CG  . GLN A 1 460 ? -7.702  3.174   -21.076 1.00 36.31  ? 460 GLN A CG  1 
ATOM   3856  C CD  . GLN A 1 460 ? -7.867  3.634   -19.647 1.00 36.64  ? 460 GLN A CD  1 
ATOM   3857  O OE1 . GLN A 1 460 ? -8.892  4.212   -19.292 1.00 37.20  ? 460 GLN A OE1 1 
ATOM   3858  N NE2 . GLN A 1 460 ? -6.858  3.394   -18.825 1.00 34.79  ? 460 GLN A NE2 1 
ATOM   3859  N N   . ARG A 1 461 ? -7.812  -0.068  -23.221 1.00 34.72  ? 461 ARG A N   1 
ATOM   3860  C CA  . ARG A 1 461 ? -6.711  -0.951  -23.630 1.00 35.47  ? 461 ARG A CA  1 
ATOM   3861  C C   . ARG A 1 461 ? -6.466  -0.887  -25.142 1.00 34.64  ? 461 ARG A C   1 
ATOM   3862  O O   . ARG A 1 461 ? -5.337  -0.983  -25.609 1.00 35.92  ? 461 ARG A O   1 
ATOM   3863  C CB  . ARG A 1 461 ? -6.943  -2.386  -23.149 1.00 37.59  ? 461 ARG A CB  1 
ATOM   3864  C CG  . ARG A 1 461 ? -8.173  -3.077  -23.722 1.00 40.75  ? 461 ARG A CG  1 
ATOM   3865  C CD  . ARG A 1 461 ? -8.531  -4.287  -22.876 1.00 42.52  ? 461 ARG A CD  1 
ATOM   3866  N NE  . ARG A 1 461 ? -9.073  -5.384  -23.674 1.00 47.18  ? 461 ARG A NE  1 
ATOM   3867  C CZ  . ARG A 1 461 ? -10.332 -5.801  -23.615 1.00 49.47  ? 461 ARG A CZ  1 
ATOM   3868  N NH1 . ARG A 1 461 ? -11.197 -5.214  -22.788 1.00 53.35  ? 461 ARG A NH1 1 
ATOM   3869  N NH2 . ARG A 1 461 ? -10.721 -6.815  -24.365 1.00 49.59  ? 461 ARG A NH2 1 
ATOM   3870  N N   . THR A 1 462 ? -7.537  -0.668  -25.890 1.00 33.86  ? 462 THR A N   1 
ATOM   3871  C CA  . THR A 1 462 ? -7.455  -0.462  -27.321 1.00 33.11  ? 462 THR A CA  1 
ATOM   3872  C C   . THR A 1 462 ? -6.769  0.863   -27.687 1.00 31.23  ? 462 THR A C   1 
ATOM   3873  O O   . THR A 1 462 ? -5.900  0.904   -28.559 1.00 29.99  ? 462 THR A O   1 
ATOM   3874  C CB  . THR A 1 462 ? -8.855  -0.573  -27.941 1.00 33.68  ? 462 THR A CB  1 
ATOM   3875  O OG1 . THR A 1 462 ? -9.325  -1.915  -27.745 1.00 34.93  ? 462 THR A OG1 1 
ATOM   3876  C CG2 . THR A 1 462 ? -8.838  -0.253  -29.441 1.00 33.04  ? 462 THR A CG2 1 
ATOM   3877  N N   . VAL A 1 463 ? -7.137  1.929   -26.996 1.00 29.87  ? 463 VAL A N   1 
ATOM   3878  C CA  . VAL A 1 463 ? -6.501  3.224   -27.212 1.00 29.84  ? 463 VAL A CA  1 
ATOM   3879  C C   . VAL A 1 463 ? -4.976  3.110   -27.009 1.00 29.52  ? 463 VAL A C   1 
ATOM   3880  O O   . VAL A 1 463 ? -4.187  3.530   -27.863 1.00 28.59  ? 463 VAL A O   1 
ATOM   3881  C CB  . VAL A 1 463 ? -7.102  4.289   -26.272 1.00 30.00  ? 463 VAL A CB  1 
ATOM   3882  C CG1 . VAL A 1 463 ? -6.266  5.555   -26.300 1.00 31.20  ? 463 VAL A CG1 1 
ATOM   3883  C CG2 . VAL A 1 463 ? -8.544  4.592   -26.676 1.00 30.83  ? 463 VAL A CG2 1 
ATOM   3884  N N   . PHE A 1 464 ? -4.578  2.490   -25.897 1.00 29.52  ? 464 PHE A N   1 
ATOM   3885  C CA  . PHE A 1 464 ? -3.176  2.232   -25.608 1.00 29.47  ? 464 PHE A CA  1 
ATOM   3886  C C   . PHE A 1 464 ? -2.459  1.434   -26.726 1.00 30.11  ? 464 PHE A C   1 
ATOM   3887  O O   . PHE A 1 464 ? -1.356  1.787   -27.128 1.00 28.91  ? 464 PHE A O   1 
ATOM   3888  C CB  . PHE A 1 464 ? -3.038  1.529   -24.252 1.00 29.35  ? 464 PHE A CB  1 
ATOM   3889  C CG  . PHE A 1 464 ? -3.313  2.418   -23.072 1.00 30.67  ? 464 PHE A CG  1 
ATOM   3890  C CD1 . PHE A 1 464 ? -3.228  3.817   -23.183 1.00 30.71  ? 464 PHE A CD1 1 
ATOM   3891  C CD2 . PHE A 1 464 ? -3.647  1.864   -21.828 1.00 31.38  ? 464 PHE A CD2 1 
ATOM   3892  C CE1 . PHE A 1 464 ? -3.462  4.633   -22.079 1.00 30.76  ? 464 PHE A CE1 1 
ATOM   3893  C CE2 . PHE A 1 464 ? -3.899  2.680   -20.732 1.00 31.46  ? 464 PHE A CE2 1 
ATOM   3894  C CZ  . PHE A 1 464 ? -3.794  4.060   -20.851 1.00 31.65  ? 464 PHE A CZ  1 
ATOM   3895  N N   . ALA A 1 465 ? -3.093  0.373   -27.231 1.00 30.02  ? 465 ALA A N   1 
ATOM   3896  C CA  . ALA A 1 465 ? -2.509  -0.399  -28.351 1.00 30.28  ? 465 ALA A CA  1 
ATOM   3897  C C   . ALA A 1 465 ? -2.366  0.455   -29.615 1.00 30.12  ? 465 ALA A C   1 
ATOM   3898  O O   . ALA A 1 465 ? -1.318  0.477   -30.263 1.00 28.76  ? 465 ALA A O   1 
ATOM   3899  C CB  . ALA A 1 465 ? -3.353  -1.634  -28.643 1.00 29.68  ? 465 ALA A CB  1 
ATOM   3900  N N   . ASN A 1 466 ? -3.446  1.129   -29.986 1.00 31.30  ? 466 ASN A N   1 
ATOM   3901  C CA  . ASN A 1 466 ? -3.369  2.088   -31.066 1.00 31.14  ? 466 ASN A CA  1 
ATOM   3902  C C   . ASN A 1 466 ? -2.195  3.043   -30.852 1.00 29.66  ? 466 ASN A C   1 
ATOM   3903  O O   . ASN A 1 466 ? -1.395  3.242   -31.750 1.00 30.56  ? 466 ASN A O   1 
ATOM   3904  C CB  . ASN A 1 466 ? -4.696  2.844   -31.234 1.00 31.59  ? 466 ASN A CB  1 
ATOM   3905  C CG  . ASN A 1 466 ? -5.780  1.988   -31.869 1.00 32.93  ? 466 ASN A CG  1 
ATOM   3906  O OD1 . ASN A 1 466 ? -5.492  1.116   -32.686 1.00 35.44  ? 466 ASN A OD1 1 
ATOM   3907  N ND2 . ASN A 1 466 ? -7.041  2.234   -31.495 1.00 32.28  ? 466 ASN A ND2 1 
ATOM   3908  N N   . PHE A 1 467 ? -2.066  3.596   -29.647 1.00 28.07  ? 467 PHE A N   1 
ATOM   3909  C CA  . PHE A 1 467 ? -1.018  4.579   -29.392 1.00 26.58  ? 467 PHE A CA  1 
ATOM   3910  C C   . PHE A 1 467 ? 0.380   3.975   -29.509 1.00 26.76  ? 467 PHE A C   1 
ATOM   3911  O O   . PHE A 1 467 ? 1.296   4.574   -30.100 1.00 26.63  ? 467 PHE A O   1 
ATOM   3912  C CB  . PHE A 1 467 ? -1.199  5.205   -28.016 1.00 26.38  ? 467 PHE A CB  1 
ATOM   3913  C CG  . PHE A 1 467 ? -0.192  6.271   -27.703 1.00 26.82  ? 467 PHE A CG  1 
ATOM   3914  C CD1 . PHE A 1 467 ? -0.091  7.406   -28.500 1.00 26.34  ? 467 PHE A CD1 1 
ATOM   3915  C CD2 . PHE A 1 467 ? 0.643   6.154   -26.591 1.00 26.94  ? 467 PHE A CD2 1 
ATOM   3916  C CE1 . PHE A 1 467 ? 0.842   8.392   -28.213 1.00 27.01  ? 467 PHE A CE1 1 
ATOM   3917  C CE2 . PHE A 1 467 ? 1.554   7.143   -26.286 1.00 25.92  ? 467 PHE A CE2 1 
ATOM   3918  C CZ  . PHE A 1 467 ? 1.653   8.261   -27.097 1.00 26.77  ? 467 PHE A CZ  1 
ATOM   3919  N N   . TYR A 1 468 ? 0.542   2.785   -28.944 1.00 25.58  ? 468 TYR A N   1 
ATOM   3920  C CA  . TYR A 1 468 ? 1.822   2.117   -28.939 1.00 25.53  ? 468 TYR A CA  1 
ATOM   3921  C C   . TYR A 1 468 ? 2.254   1.853   -30.386 1.00 26.07  ? 468 TYR A C   1 
ATOM   3922  O O   . TYR A 1 468 ? 3.404   2.109   -30.761 1.00 26.59  ? 468 TYR A O   1 
ATOM   3923  C CB  . TYR A 1 468 ? 1.706   0.820   -28.128 1.00 24.91  ? 468 TYR A CB  1 
ATOM   3924  C CG  . TYR A 1 468 ? 2.954   -0.030  -28.065 1.00 24.25  ? 468 TYR A CG  1 
ATOM   3925  C CD1 . TYR A 1 468 ? 4.075   0.373   -27.310 1.00 23.16  ? 468 TYR A CD1 1 
ATOM   3926  C CD2 . TYR A 1 468 ? 2.997   -1.270  -28.719 1.00 23.99  ? 468 TYR A CD2 1 
ATOM   3927  C CE1 . TYR A 1 468 ? 5.190   -0.437  -27.212 1.00 23.43  ? 468 TYR A CE1 1 
ATOM   3928  C CE2 . TYR A 1 468 ? 4.099   -2.096  -28.632 1.00 22.96  ? 468 TYR A CE2 1 
ATOM   3929  C CZ  . TYR A 1 468 ? 5.200   -1.694  -27.906 1.00 24.19  ? 468 TYR A CZ  1 
ATOM   3930  O OH  . TYR A 1 468 ? 6.311   -2.534  -27.866 1.00 23.07  ? 468 TYR A OH  1 
ATOM   3931  N N   . ASP A 1 469 ? 1.308   1.413   -31.209 1.00 26.43  ? 469 ASP A N   1 
ATOM   3932  C CA  . ASP A 1 469 ? 1.566   1.153   -32.612 1.00 26.86  ? 469 ASP A CA  1 
ATOM   3933  C C   . ASP A 1 469 ? 2.010   2.417   -33.361 1.00 27.57  ? 469 ASP A C   1 
ATOM   3934  O O   . ASP A 1 469 ? 2.952   2.378   -34.176 1.00 26.94  ? 469 ASP A O   1 
ATOM   3935  C CB  . ASP A 1 469 ? 0.316   0.574   -33.281 1.00 27.77  ? 469 ASP A CB  1 
ATOM   3936  C CG  . ASP A 1 469 ? 0.089   -0.884  -32.939 1.00 28.33  ? 469 ASP A CG  1 
ATOM   3937  O OD1 . ASP A 1 469 ? 0.989   -1.513  -32.371 1.00 28.17  ? 469 ASP A OD1 1 
ATOM   3938  O OD2 . ASP A 1 469 ? -0.986  -1.409  -33.271 1.00 29.83  ? 469 ASP A OD2 1 
ATOM   3939  N N   . ALA A 1 470 ? 1.329   3.532   -33.111 1.00 28.23  ? 470 ALA A N   1 
ATOM   3940  C CA  . ALA A 1 470 ? 1.683   4.791   -33.799 1.00 27.36  ? 470 ALA A CA  1 
ATOM   3941  C C   . ALA A 1 470 ? 3.088   5.184   -33.394 1.00 27.42  ? 470 ALA A C   1 
ATOM   3942  O O   . ALA A 1 470 ? 3.854   5.689   -34.202 1.00 30.82  ? 470 ALA A O   1 
ATOM   3943  C CB  . ALA A 1 470 ? 0.684   5.897   -33.465 1.00 26.30  ? 470 ALA A CB  1 
ATOM   3944  N N   . MET A 1 471 ? 3.451   4.897   -32.146 1.00 26.31  ? 471 MET A N   1 
ATOM   3945  C CA  . MET A 1 471 ? 4.758   5.311   -31.640 1.00 25.90  ? 471 MET A CA  1 
ATOM   3946  C C   . MET A 1 471 ? 5.900   4.413   -32.164 1.00 25.68  ? 471 MET A C   1 
ATOM   3947  O O   . MET A 1 471 ? 7.015   4.888   -32.362 1.00 24.10  ? 471 MET A O   1 
ATOM   3948  C CB  . MET A 1 471 ? 4.767   5.442   -30.101 1.00 25.52  ? 471 MET A CB  1 
ATOM   3949  C CG  . MET A 1 471 ? 3.893   6.574   -29.537 1.00 25.65  ? 471 MET A CG  1 
ATOM   3950  S SD  . MET A 1 471 ? 4.105   8.197   -30.341 1.00 26.99  ? 471 MET A SD  1 
ATOM   3951  C CE  . MET A 1 471 ? 5.835   8.543   -29.974 1.00 24.90  ? 471 MET A CE  1 
ATOM   3952  N N   . ILE A 1 472 ? 5.597   3.136   -32.430 1.00 25.95  ? 472 ILE A N   1 
ATOM   3953  C CA  . ILE A 1 472 ? 6.505   2.246   -33.143 1.00 26.17  ? 472 ILE A CA  1 
ATOM   3954  C C   . ILE A 1 472 ? 6.794   2.829   -34.551 1.00 27.69  ? 472 ILE A C   1 
ATOM   3955  O O   . ILE A 1 472 ? 7.955   2.930   -34.979 1.00 26.48  ? 472 ILE A O   1 
ATOM   3956  C CB  . ILE A 1 472 ? 5.888   0.823   -33.290 1.00 28.69  ? 472 ILE A CB  1 
ATOM   3957  C CG1 . ILE A 1 472 ? 5.825   0.084   -31.937 1.00 27.11  ? 472 ILE A CG1 1 
ATOM   3958  C CG2 . ILE A 1 472 ? 6.598   0.009   -34.390 1.00 27.65  ? 472 ILE A CG2 1 
ATOM   3959  C CD1 . ILE A 1 472 ? 7.155   -0.472  -31.459 1.00 27.29  ? 472 ILE A CD1 1 
ATOM   3960  N N   . CYS A 1 473 ? 5.752   3.252   -35.264 1.00 28.65  ? 473 CYS A N   1 
ATOM   3961  C CA  . CYS A 1 473 ? 5.995   3.938   -36.542 1.00 30.34  ? 473 CYS A CA  1 
ATOM   3962  C C   . CYS A 1 473 ? 6.911   5.146   -36.398 1.00 29.11  ? 473 CYS A C   1 
ATOM   3963  O O   . CYS A 1 473 ? 7.875   5.272   -37.142 1.00 28.74  ? 473 CYS A O   1 
ATOM   3964  C CB  . CYS A 1 473 ? 4.710   4.340   -37.223 1.00 32.04  ? 473 CYS A CB  1 
ATOM   3965  S SG  . CYS A 1 473 ? 3.743   2.931   -37.727 1.00 40.70  ? 473 CYS A SG  1 
ATOM   3966  N N   . VAL A 1 474 ? 6.578   6.051   -35.472 1.00 28.63  ? 474 VAL A N   1 
ATOM   3967  C CA  . VAL A 1 474 ? 7.434   7.248   -35.172 1.00 26.70  ? 474 VAL A CA  1 
ATOM   3968  C C   . VAL A 1 474 ? 8.884   6.861   -34.842 1.00 26.02  ? 474 VAL A C   1 
ATOM   3969  O O   . VAL A 1 474 ? 9.833   7.557   -35.236 1.00 26.01  ? 474 VAL A O   1 
ATOM   3970  C CB  . VAL A 1 474 ? 6.844   8.062   -33.982 1.00 26.96  ? 474 VAL A CB  1 
ATOM   3971  C CG1 . VAL A 1 474 ? 7.814   9.128   -33.481 1.00 24.72  ? 474 VAL A CG1 1 
ATOM   3972  C CG2 . VAL A 1 474 ? 5.493   8.680   -34.378 1.00 26.45  ? 474 VAL A CG2 1 
ATOM   3973  N N   . ALA A 1 475 ? 9.055   5.758   -34.114 1.00 25.19  ? 475 ALA A N   1 
ATOM   3974  C CA  . ALA A 1 475 ? 10.387  5.313   -33.695 1.00 24.70  ? 475 ALA A CA  1 
ATOM   3975  C C   . ALA A 1 475 ? 11.206  4.828   -34.910 1.00 26.28  ? 475 ALA A C   1 
ATOM   3976  O O   . ALA A 1 475 ? 12.424  5.068   -34.999 1.00 27.95  ? 475 ALA A O   1 
ATOM   3977  C CB  . ALA A 1 475 ? 10.269  4.215   -32.649 1.00 24.84  ? 475 ALA A CB  1 
ATOM   3978  N N   . TYR A 1 476 ? 10.519  4.184   -35.852 1.00 25.46  ? 476 TYR A N   1 
ATOM   3979  C CA  . TYR A 1 476 ? 11.117  3.738   -37.078 1.00 26.16  ? 476 TYR A CA  1 
ATOM   3980  C C   . TYR A 1 476 ? 11.497  4.939   -37.941 1.00 26.32  ? 476 TYR A C   1 
ATOM   3981  O O   . TYR A 1 476 ? 12.584  4.958   -38.529 1.00 26.72  ? 476 TYR A O   1 
ATOM   3982  C CB  . TYR A 1 476 ? 10.170  2.820   -37.841 1.00 26.57  ? 476 TYR A CB  1 
ATOM   3983  C CG  . TYR A 1 476 ? 10.276  1.359   -37.521 1.00 27.15  ? 476 TYR A CG  1 
ATOM   3984  C CD1 . TYR A 1 476 ? 11.491  0.682   -37.639 1.00 28.52  ? 476 TYR A CD1 1 
ATOM   3985  C CD2 . TYR A 1 476 ? 9.136   0.622   -37.174 1.00 28.48  ? 476 TYR A CD2 1 
ATOM   3986  C CE1 . TYR A 1 476 ? 11.580  -0.680  -37.373 1.00 30.01  ? 476 TYR A CE1 1 
ATOM   3987  C CE2 . TYR A 1 476 ? 9.204   -0.743  -36.909 1.00 29.37  ? 476 TYR A CE2 1 
ATOM   3988  C CZ  . TYR A 1 476 ? 10.428  -1.386  -36.997 1.00 30.11  ? 476 TYR A CZ  1 
ATOM   3989  O OH  . TYR A 1 476 ? 10.506  -2.723  -36.737 1.00 30.38  ? 476 TYR A OH  1 
ATOM   3990  N N   . LYS A 1 477 ? 10.629  5.949   -37.998 1.00 25.54  ? 477 LYS A N   1 
ATOM   3991  C CA  . LYS A 1 477 ? 11.015  7.209   -38.647 1.00 26.74  ? 477 LYS A CA  1 
ATOM   3992  C C   . LYS A 1 477 ? 12.257  7.782   -37.967 1.00 27.30  ? 477 LYS A C   1 
ATOM   3993  O O   . LYS A 1 477 ? 13.152  8.265   -38.637 1.00 27.62  ? 477 LYS A O   1 
ATOM   3994  C CB  . LYS A 1 477 ? 9.879   8.231   -38.640 1.00 26.40  ? 477 LYS A CB  1 
ATOM   3995  C CG  . LYS A 1 477 ? 9.929   9.181   -39.835 1.00 28.20  ? 477 LYS A CG  1 
ATOM   3996  C CD  . LYS A 1 477 ? 9.298   10.563  -39.588 1.00 29.85  ? 477 LYS A CD  1 
ATOM   3997  C CE  . LYS A 1 477 ? 8.687   11.073  -40.887 1.00 30.83  ? 477 LYS A CE  1 
ATOM   3998  N NZ  . LYS A 1 477 ? 8.717   12.538  -41.159 1.00 28.88  ? 477 LYS A NZ  1 
ATOM   3999  N N   . PHE A 1 478 ? 12.322  7.689   -36.630 1.00 27.16  ? 478 PHE A N   1 
ATOM   4000  C CA  . PHE A 1 478 ? 13.452  8.249   -35.887 1.00 27.00  ? 478 PHE A CA  1 
ATOM   4001  C C   . PHE A 1 478 ? 14.708  7.526   -36.323 1.00 28.03  ? 478 PHE A C   1 
ATOM   4002  O O   . PHE A 1 478 ? 15.762  8.127   -36.545 1.00 26.23  ? 478 PHE A O   1 
ATOM   4003  C CB  . PHE A 1 478 ? 13.246  8.066   -34.382 1.00 25.82  ? 478 PHE A CB  1 
ATOM   4004  C CG  . PHE A 1 478 ? 14.474  8.364   -33.545 1.00 25.39  ? 478 PHE A CG  1 
ATOM   4005  C CD1 . PHE A 1 478 ? 15.358  7.354   -33.202 1.00 26.30  ? 478 PHE A CD1 1 
ATOM   4006  C CD2 . PHE A 1 478 ? 14.700  9.638   -33.042 1.00 25.88  ? 478 PHE A CD2 1 
ATOM   4007  C CE1 . PHE A 1 478 ? 16.478  7.603   -32.406 1.00 27.36  ? 478 PHE A CE1 1 
ATOM   4008  C CE2 . PHE A 1 478 ? 15.810  9.901   -32.244 1.00 27.15  ? 478 PHE A CE2 1 
ATOM   4009  C CZ  . PHE A 1 478 ? 16.710  8.888   -31.934 1.00 26.65  ? 478 PHE A CZ  1 
ATOM   4010  N N   . ASP A 1 479 ? 14.578  6.208   -36.431 1.00 29.48  ? 479 ASP A N   1 
ATOM   4011  C CA  . ASP A 1 479 ? 15.688  5.368   -36.758 1.00 29.27  ? 479 ASP A CA  1 
ATOM   4012  C C   . ASP A 1 479 ? 16.197  5.710   -38.177 1.00 28.87  ? 479 ASP A C   1 
ATOM   4013  O O   . ASP A 1 479 ? 17.409  5.813   -38.405 1.00 25.81  ? 479 ASP A O   1 
ATOM   4014  C CB  . ASP A 1 479 ? 15.261  3.915   -36.643 1.00 29.31  ? 479 ASP A CB  1 
ATOM   4015  C CG  . ASP A 1 479 ? 16.285  2.986   -37.186 1.00 29.87  ? 479 ASP A CG  1 
ATOM   4016  O OD1 . ASP A 1 479 ? 17.405  2.944   -36.631 1.00 28.48  ? 479 ASP A OD1 1 
ATOM   4017  O OD2 . ASP A 1 479 ? 15.957  2.292   -38.174 1.00 32.09  ? 479 ASP A OD2 1 
ATOM   4018  N N   . ALA A 1 480 ? 15.254  5.958   -39.093 1.00 28.07  ? 480 ALA A N   1 
ATOM   4019  C CA  . ALA A 1 480 ? 15.583  6.296   -40.474 1.00 28.79  ? 480 ALA A CA  1 
ATOM   4020  C C   . ALA A 1 480 ? 16.245  7.682   -40.592 1.00 29.44  ? 480 ALA A C   1 
ATOM   4021  O O   . ALA A 1 480 ? 17.203  7.863   -41.365 1.00 30.33  ? 480 ALA A O   1 
ATOM   4022  C CB  . ALA A 1 480 ? 14.334  6.202   -41.363 1.00 29.78  ? 480 ALA A CB  1 
ATOM   4023  N N   . ALA A 1 481 ? 15.733  8.651   -39.842 1.00 27.45  ? 481 ALA A N   1 
ATOM   4024  C CA  . ALA A 1 481 ? 16.462  9.913   -39.593 1.00 29.54  ? 481 ALA A CA  1 
ATOM   4025  C C   . ALA A 1 481 ? 17.891  9.687   -39.068 1.00 31.53  ? 481 ALA A C   1 
ATOM   4026  O O   . ALA A 1 481 ? 18.851  10.329  -39.545 1.00 32.48  ? 481 ALA A O   1 
ATOM   4027  C CB  . ALA A 1 481 ? 15.682  10.804  -38.631 1.00 27.95  ? 481 ALA A CB  1 
ATOM   4028  N N   . MET A 1 482 ? 18.052  8.782   -38.103 1.00 31.30  ? 482 MET A N   1 
ATOM   4029  C CA  . MET A 1 482 ? 19.397  8.525   -37.578 1.00 32.86  ? 482 MET A CA  1 
ATOM   4030  C C   . MET A 1 482 ? 20.307  8.079   -38.702 1.00 33.36  ? 482 MET A C   1 
ATOM   4031  O O   . MET A 1 482 ? 21.504  8.377   -38.684 1.00 37.32  ? 482 MET A O   1 
ATOM   4032  C CB  . MET A 1 482 ? 19.411  7.454   -36.473 1.00 32.01  ? 482 MET A CB  1 
ATOM   4033  C CG  . MET A 1 482 ? 18.875  7.870   -35.117 1.00 32.08  ? 482 MET A CG  1 
ATOM   4034  S SD  . MET A 1 482 ? 19.348  9.539   -34.620 1.00 34.28  ? 482 MET A SD  1 
ATOM   4035  C CE  . MET A 1 482 ? 17.916  10.408  -35.272 1.00 34.34  ? 482 MET A CE  1 
ATOM   4036  N N   . MET A 1 483 ? 19.765  7.320   -39.653 1.00 33.05  ? 483 MET A N   1 
ATOM   4037  C CA  . MET A 1 483 ? 20.614  6.740   -40.692 1.00 35.04  ? 483 MET A CA  1 
ATOM   4038  C C   . MET A 1 483 ? 21.022  7.853   -41.637 1.00 33.38  ? 483 MET A C   1 
ATOM   4039  O O   . MET A 1 483 ? 22.174  7.972   -42.002 1.00 31.55  ? 483 MET A O   1 
ATOM   4040  C CB  . MET A 1 483 ? 19.913  5.598   -41.444 1.00 36.77  ? 483 MET A CB  1 
ATOM   4041  C CG  . MET A 1 483 ? 19.710  4.324   -40.632 1.00 41.63  ? 483 MET A CG  1 
ATOM   4042  S SD  . MET A 1 483 ? 21.202  3.707   -39.798 1.00 45.21  ? 483 MET A SD  1 
ATOM   4043  C CE  . MET A 1 483 ? 20.955  4.354   -38.143 1.00 44.56  ? 483 MET A CE  1 
ATOM   4044  N N   . ALA A 1 484 ? 20.060  8.694   -41.979 1.00 33.96  ? 484 ALA A N   1 
ATOM   4045  C CA  . ALA A 1 484 ? 20.322  9.856   -42.797 1.00 35.00  ? 484 ALA A CA  1 
ATOM   4046  C C   . ALA A 1 484 ? 21.293  10.785  -42.102 1.00 34.59  ? 484 ALA A C   1 
ATOM   4047  O O   . ALA A 1 484 ? 22.153  11.360  -42.755 1.00 37.83  ? 484 ALA A O   1 
ATOM   4048  C CB  . ALA A 1 484 ? 19.017  10.588  -43.149 1.00 33.30  ? 484 ALA A CB  1 
ATOM   4049  N N   . LEU A 1 485 ? 21.161  10.958  -40.784 1.00 35.64  ? 485 LEU A N   1 
ATOM   4050  C CA  . LEU A 1 485 ? 22.052  11.916  -40.085 1.00 36.26  ? 485 LEU A CA  1 
ATOM   4051  C C   . LEU A 1 485 ? 23.515  11.463  -40.180 1.00 35.61  ? 485 LEU A C   1 
ATOM   4052  O O   . LEU A 1 485 ? 24.415  12.290  -40.291 1.00 34.21  ? 485 LEU A O   1 
ATOM   4053  C CB  . LEU A 1 485 ? 21.646  12.165  -38.623 1.00 33.64  ? 485 LEU A CB  1 
ATOM   4054  C CG  . LEU A 1 485 ? 20.369  12.950  -38.255 1.00 35.29  ? 485 LEU A CG  1 
ATOM   4055  C CD1 . LEU A 1 485 ? 20.228  12.996  -36.746 1.00 34.62  ? 485 LEU A CD1 1 
ATOM   4056  C CD2 . LEU A 1 485 ? 20.329  14.370  -38.819 1.00 36.74  ? 485 LEU A CD2 1 
ATOM   4057  N N   . ARG A 1 486 ? 23.727  10.144  -40.163 1.00 35.58  ? 486 ARG A N   1 
ATOM   4058  C CA  . ARG A 1 486 ? 25.064  9.567   -40.250 1.00 38.42  ? 486 ARG A CA  1 
ATOM   4059  C C   . ARG A 1 486 ? 25.679  9.600   -41.666 1.00 37.86  ? 486 ARG A C   1 
ATOM   4060  O O   . ARG A 1 486 ? 26.870  9.891   -41.820 1.00 37.99  ? 486 ARG A O   1 
ATOM   4061  C CB  . ARG A 1 486 ? 25.049  8.139   -39.694 1.00 43.02  ? 486 ARG A CB  1 
ATOM   4062  C CG  . ARG A 1 486 ? 26.134  7.208   -40.214 1.00 45.54  ? 486 ARG A CG  1 
ATOM   4063  C CD  . ARG A 1 486 ? 27.546  7.690   -39.895 1.00 52.89  ? 486 ARG A CD  1 
ATOM   4064  N NE  . ARG A 1 486 ? 27.937  7.436   -38.516 1.00 56.46  ? 486 ARG A NE  1 
ATOM   4065  C CZ  . ARG A 1 486 ? 29.196  7.405   -38.091 1.00 61.65  ? 486 ARG A CZ  1 
ATOM   4066  N NH1 . ARG A 1 486 ? 30.193  7.606   -38.948 1.00 62.65  ? 486 ARG A NH1 1 
ATOM   4067  N NH2 . ARG A 1 486 ? 29.461  7.178   -36.806 1.00 65.39  ? 486 ARG A NH2 1 
ATOM   4068  N N   . THR A 1 487 ? 24.864  9.317   -42.684 1.00 38.03  ? 487 THR A N   1 
ATOM   4069  C CA  . THR A 1 487 ? 25.352  9.096   -44.058 1.00 36.12  ? 487 THR A CA  1 
ATOM   4070  C C   . THR A 1 487 ? 25.376  10.336  -44.929 1.00 36.50  ? 487 THR A C   1 
ATOM   4071  O O   . THR A 1 487 ? 26.057  10.353  -45.953 1.00 38.00  ? 487 THR A O   1 
ATOM   4072  C CB  . THR A 1 487 ? 24.513  8.059   -44.809 1.00 35.98  ? 487 THR A CB  1 
ATOM   4073  O OG1 . THR A 1 487 ? 23.157  8.504   -44.865 1.00 34.91  ? 487 THR A OG1 1 
ATOM   4074  C CG2 . THR A 1 487 ? 24.591  6.692   -44.132 1.00 36.63  ? 487 THR A CG2 1 
ATOM   4075  N N   . SER A 1 488 ? 24.604  11.351  -44.555 1.00 34.84  ? 488 SER A N   1 
ATOM   4076  C CA  . SER A 1 488 ? 24.520  12.581  -45.337 1.00 34.12  ? 488 SER A CA  1 
ATOM   4077  C C   . SER A 1 488 ? 24.931  13.863  -44.556 1.00 36.07  ? 488 SER A C   1 
ATOM   4078  O O   . SER A 1 488 ? 25.612  14.734  -45.101 1.00 39.31  ? 488 SER A O   1 
ATOM   4079  C CB  . SER A 1 488 ? 23.114  12.726  -45.901 1.00 31.88  ? 488 SER A CB  1 
ATOM   4080  O OG  . SER A 1 488 ? 22.943  13.996  -46.489 1.00 32.49  ? 488 SER A OG  1 
ATOM   4081  N N   . PHE A 1 489 ? 24.490  13.993  -43.308 1.00 33.14  ? 489 PHE A N   1 
ATOM   4082  C CA  . PHE A 1 489 ? 24.859  15.152  -42.499 1.00 35.70  ? 489 PHE A CA  1 
ATOM   4083  C C   . PHE A 1 489 ? 26.223  14.872  -41.926 1.00 37.60  ? 489 PHE A C   1 
ATOM   4084  O O   . PHE A 1 489 ? 26.865  15.743  -41.333 1.00 36.80  ? 489 PHE A O   1 
ATOM   4085  C CB  . PHE A 1 489 ? 23.865  15.364  -41.360 1.00 32.08  ? 489 PHE A CB  1 
ATOM   4086  C CG  . PHE A 1 489 ? 22.546  15.922  -41.802 1.00 30.65  ? 489 PHE A CG  1 
ATOM   4087  C CD1 . PHE A 1 489 ? 21.589  15.098  -42.389 1.00 28.80  ? 489 PHE A CD1 1 
ATOM   4088  C CD2 . PHE A 1 489 ? 22.239  17.262  -41.586 1.00 29.97  ? 489 PHE A CD2 1 
ATOM   4089  C CE1 . PHE A 1 489 ? 20.370  15.597  -42.771 1.00 26.86  ? 489 PHE A CE1 1 
ATOM   4090  C CE2 . PHE A 1 489 ? 21.018  17.769  -41.980 1.00 29.36  ? 489 PHE A CE2 1 
ATOM   4091  C CZ  . PHE A 1 489 ? 20.088  16.937  -42.581 1.00 28.05  ? 489 PHE A CZ  1 
ATOM   4092  N N   . LEU A 1 490 ? 26.645  13.626  -42.105 1.00 40.68  ? 490 LEU A N   1 
ATOM   4093  C CA  . LEU A 1 490 ? 27.895  13.119  -41.557 1.00 43.50  ? 490 LEU A CA  1 
ATOM   4094  C C   . LEU A 1 490 ? 28.068  13.457  -40.077 1.00 43.35  ? 490 LEU A C   1 
ATOM   4095  O O   . LEU A 1 490 ? 29.097  13.997  -39.683 1.00 47.88  ? 490 LEU A O   1 
ATOM   4096  C CB  . LEU A 1 490 ? 29.103  13.608  -42.386 1.00 42.83  ? 490 LEU A CB  1 
ATOM   4097  C CG  . LEU A 1 490 ? 29.104  13.412  -43.917 1.00 45.41  ? 490 LEU A CG  1 
ATOM   4098  C CD1 . LEU A 1 490 ? 30.458  13.834  -44.505 1.00 42.96  ? 490 LEU A CD1 1 
ATOM   4099  C CD2 . LEU A 1 490 ? 28.747  11.976  -44.323 1.00 43.34  ? 490 LEU A CD2 1 
ATOM   4100  N N   . VAL A 1 491 ? 27.080  13.106  -39.256 1.00 44.49  ? 491 VAL A N   1 
ATOM   4101  C CA  . VAL A 1 491 ? 27.189  13.292  -37.783 1.00 47.43  ? 491 VAL A CA  1 
ATOM   4102  C C   . VAL A 1 491 ? 28.028  12.177  -37.132 1.00 48.90  ? 491 VAL A C   1 
ATOM   4103  O O   . VAL A 1 491 ? 27.908  11.005  -37.498 1.00 52.37  ? 491 VAL A O   1 
ATOM   4104  C CB  . VAL A 1 491 ? 25.790  13.345  -37.104 1.00 46.99  ? 491 VAL A CB  1 
ATOM   4105  C CG1 . VAL A 1 491 ? 25.900  13.389  -35.578 1.00 44.77  ? 491 VAL A CG1 1 
ATOM   4106  C CG2 . VAL A 1 491 ? 24.995  14.530  -37.613 1.00 44.26  ? 491 VAL A CG2 1 
ATOM   4107  N N   . ASN A 1 492 ? 28.879  12.543  -36.180 1.00 52.78  ? 492 ASN A N   1 
ATOM   4108  C CA  . ASN A 1 492 ? 29.592  11.546  -35.365 1.00 61.09  ? 492 ASN A CA  1 
ATOM   4109  C C   . ASN A 1 492 ? 29.267  11.601  -33.865 1.00 63.24  ? 492 ASN A C   1 
ATOM   4110  O O   . ASN A 1 492 ? 29.314  10.568  -33.184 1.00 64.47  ? 492 ASN A O   1 
ATOM   4111  C CB  . ASN A 1 492 ? 31.110  11.590  -35.603 1.00 63.96  ? 492 ASN A CB  1 
ATOM   4112  C CG  . ASN A 1 492 ? 31.582  12.935  -36.121 1.00 72.08  ? 492 ASN A CG  1 
ATOM   4113  O OD1 . ASN A 1 492 ? 31.240  13.988  -35.568 1.00 76.76  ? 492 ASN A OD1 1 
ATOM   4114  N ND2 . ASN A 1 492 ? 32.370  12.909  -37.194 1.00 71.42  ? 492 ASN A ND2 1 
ATOM   4115  N N   . ASP A 1 493 ? 28.938  12.796  -33.357 1.00 60.60  ? 493 ASP A N   1 
ATOM   4116  C CA  . ASP A 1 493 ? 28.444  12.937  -31.979 1.00 60.17  ? 493 ASP A CA  1 
ATOM   4117  C C   . ASP A 1 493 ? 26.924  13.102  -31.928 1.00 55.98  ? 493 ASP A C   1 
ATOM   4118  O O   . ASP A 1 493 ? 26.379  14.168  -32.251 1.00 53.40  ? 493 ASP A O   1 
ATOM   4119  C CB  . ASP A 1 493 ? 29.139  14.083  -31.227 1.00 62.10  ? 493 ASP A CB  1 
ATOM   4120  C CG  . ASP A 1 493 ? 28.862  14.051  -29.709 1.00 65.43  ? 493 ASP A CG  1 
ATOM   4121  O OD1 . ASP A 1 493 ? 27.704  13.790  -29.301 1.00 62.89  ? 493 ASP A OD1 1 
ATOM   4122  O OD2 . ASP A 1 493 ? 29.805  14.300  -28.922 1.00 70.35  ? 493 ASP A OD2 1 
ATOM   4123  N N   . PHE A 1 494 ? 26.253  12.047  -31.485 1.00 51.18  ? 494 PHE A N   1 
ATOM   4124  C CA  . PHE A 1 494 ? 24.804  12.014  -31.485 1.00 51.94  ? 494 PHE A CA  1 
ATOM   4125  C C   . PHE A 1 494 ? 24.190  12.505  -30.165 1.00 50.88  ? 494 PHE A C   1 
ATOM   4126  O O   . PHE A 1 494 ? 23.069  12.140  -29.833 1.00 53.11  ? 494 PHE A O   1 
ATOM   4127  C CB  . PHE A 1 494 ? 24.306  10.604  -31.839 1.00 53.06  ? 494 PHE A CB  1 
ATOM   4128  C CG  . PHE A 1 494 ? 24.575  10.201  -33.272 1.00 53.62  ? 494 PHE A CG  1 
ATOM   4129  C CD1 . PHE A 1 494 ? 23.640  10.462  -34.271 1.00 52.47  ? 494 PHE A CD1 1 
ATOM   4130  C CD2 . PHE A 1 494 ? 25.766  9.567   -33.622 1.00 54.28  ? 494 PHE A CD2 1 
ATOM   4131  C CE1 . PHE A 1 494 ? 23.883  10.096  -35.587 1.00 55.46  ? 494 PHE A CE1 1 
ATOM   4132  C CE2 . PHE A 1 494 ? 26.017  9.206   -34.935 1.00 56.46  ? 494 PHE A CE2 1 
ATOM   4133  C CZ  . PHE A 1 494 ? 25.073  9.468   -35.920 1.00 56.76  ? 494 PHE A CZ  1 
ATOM   4134  N N   . GLY A 1 495 ? 24.914  13.361  -29.446 1.00 46.40  ? 495 GLY A N   1 
ATOM   4135  C CA  . GLY A 1 495 ? 24.497  13.817  -28.122 1.00 45.46  ? 495 GLY A CA  1 
ATOM   4136  C C   . GLY A 1 495 ? 23.200  14.616  -28.087 1.00 43.64  ? 495 GLY A C   1 
ATOM   4137  O O   . GLY A 1 495 ? 22.272  14.276  -27.329 1.00 42.38  ? 495 GLY A O   1 
ATOM   4138  N N   . PHE A 1 496 ? 23.154  15.685  -28.891 1.00 41.09  ? 496 PHE A N   1 
ATOM   4139  C CA  . PHE A 1 496 ? 21.960  16.516  -29.091 1.00 37.89  ? 496 PHE A CA  1 
ATOM   4140  C C   . PHE A 1 496 ? 20.679  15.704  -29.304 1.00 35.62  ? 496 PHE A C   1 
ATOM   4141  O O   . PHE A 1 496 ? 19.588  16.208  -29.080 1.00 34.24  ? 496 PHE A O   1 
ATOM   4142  C CB  . PHE A 1 496 ? 22.168  17.494  -30.275 1.00 38.49  ? 496 PHE A CB  1 
ATOM   4143  C CG  . PHE A 1 496 ? 22.053  16.845  -31.643 1.00 38.17  ? 496 PHE A CG  1 
ATOM   4144  C CD1 . PHE A 1 496 ? 20.821  16.746  -32.280 1.00 38.49  ? 496 PHE A CD1 1 
ATOM   4145  C CD2 . PHE A 1 496 ? 23.178  16.325  -32.282 1.00 38.00  ? 496 PHE A CD2 1 
ATOM   4146  C CE1 . PHE A 1 496 ? 20.708  16.124  -33.518 1.00 40.92  ? 496 PHE A CE1 1 
ATOM   4147  C CE2 . PHE A 1 496 ? 23.076  15.726  -33.529 1.00 40.17  ? 496 PHE A CE2 1 
ATOM   4148  C CZ  . PHE A 1 496 ? 21.837  15.620  -34.148 1.00 40.83  ? 496 PHE A CZ  1 
ATOM   4149  N N   . ILE A 1 497 ? 20.820  14.451  -29.736 1.00 35.16  ? 497 ILE A N   1 
ATOM   4150  C CA  . ILE A 1 497 ? 19.673  13.571  -29.966 1.00 35.20  ? 497 ILE A CA  1 
ATOM   4151  C C   . ILE A 1 497 ? 18.813  13.370  -28.710 1.00 34.34  ? 497 ILE A C   1 
ATOM   4152  O O   . ILE A 1 497 ? 17.562  13.398  -28.788 1.00 33.36  ? 497 ILE A O   1 
ATOM   4153  C CB  . ILE A 1 497 ? 20.107  12.213  -30.572 1.00 37.08  ? 497 ILE A CB  1 
ATOM   4154  C CG1 . ILE A 1 497 ? 20.053  12.282  -32.087 1.00 37.32  ? 497 ILE A CG1 1 
ATOM   4155  C CG2 . ILE A 1 497 ? 19.226  11.055  -30.105 1.00 37.07  ? 497 ILE A CG2 1 
ATOM   4156  C CD1 . ILE A 1 497 ? 21.365  12.678  -32.711 1.00 40.25  ? 497 ILE A CD1 1 
ATOM   4157  N N   . TRP A 1 498 ? 19.467  13.204  -27.558 1.00 32.25  ? 498 TRP A N   1 
ATOM   4158  C CA  . TRP A 1 498 ? 18.737  12.892  -26.314 1.00 31.12  ? 498 TRP A CA  1 
ATOM   4159  C C   . TRP A 1 498 ? 17.581  13.815  -26.033 1.00 30.65  ? 498 TRP A C   1 
ATOM   4160  O O   . TRP A 1 498 ? 16.453  13.367  -25.803 1.00 28.48  ? 498 TRP A O   1 
ATOM   4161  C CB  . TRP A 1 498 ? 19.660  12.856  -25.098 1.00 31.09  ? 498 TRP A CB  1 
ATOM   4162  C CG  . TRP A 1 498 ? 18.878  12.508  -23.871 1.00 30.42  ? 498 TRP A CG  1 
ATOM   4163  C CD1 . TRP A 1 498 ? 18.694  13.278  -22.735 1.00 31.28  ? 498 TRP A CD1 1 
ATOM   4164  C CD2 . TRP A 1 498 ? 18.038  11.318  -23.670 1.00 30.65  ? 498 TRP A CD2 1 
ATOM   4165  N NE1 . TRP A 1 498 ? 17.845  12.648  -21.848 1.00 30.23  ? 498 TRP A NE1 1 
ATOM   4166  C CE2 . TRP A 1 498 ? 17.419  11.466  -22.359 1.00 31.24  ? 498 TRP A CE2 1 
ATOM   4167  C CE3 . TRP A 1 498 ? 17.767  10.178  -24.417 1.00 29.16  ? 498 TRP A CE3 1 
ATOM   4168  C CZ2 . TRP A 1 498 ? 16.574  10.493  -21.827 1.00 30.27  ? 498 TRP A CZ2 1 
ATOM   4169  C CZ3 . TRP A 1 498 ? 16.917  9.219   -23.882 1.00 30.04  ? 498 TRP A CZ3 1 
ATOM   4170  C CH2 . TRP A 1 498 ? 16.340  9.370   -22.610 1.00 29.89  ? 498 TRP A CH2 1 
ATOM   4171  N N   . LEU A 1 499 ? 17.851  15.121  -26.045 1.00 31.19  ? 499 LEU A N   1 
ATOM   4172  C CA  . LEU A 1 499 ? 16.810  16.087  -25.721 1.00 31.30  ? 499 LEU A CA  1 
ATOM   4173  C C   . LEU A 1 499 ? 15.763  16.225  -26.817 1.00 29.24  ? 499 LEU A C   1 
ATOM   4174  O O   . LEU A 1 499 ? 14.609  16.507  -26.523 1.00 29.48  ? 499 LEU A O   1 
ATOM   4175  C CB  . LEU A 1 499 ? 17.402  17.455  -25.320 1.00 33.31  ? 499 LEU A CB  1 
ATOM   4176  C CG  . LEU A 1 499 ? 18.163  17.456  -23.978 1.00 35.43  ? 499 LEU A CG  1 
ATOM   4177  C CD1 . LEU A 1 499 ? 19.151  18.611  -23.915 1.00 36.76  ? 499 LEU A CD1 1 
ATOM   4178  C CD2 . LEU A 1 499 ? 17.221  17.458  -22.759 1.00 35.01  ? 499 LEU A CD2 1 
ATOM   4179  N N   . VAL A 1 500 ? 16.144  15.995  -28.072 1.00 27.93  ? 500 VAL A N   1 
ATOM   4180  C CA  . VAL A 1 500 ? 15.156  15.999  -29.154 1.00 28.39  ? 500 VAL A CA  1 
ATOM   4181  C C   . VAL A 1 500 ? 14.224  14.780  -28.985 1.00 28.60  ? 500 VAL A C   1 
ATOM   4182  O O   . VAL A 1 500 ? 12.999  14.919  -29.048 1.00 27.52  ? 500 VAL A O   1 
ATOM   4183  C CB  . VAL A 1 500 ? 15.815  15.966  -30.565 1.00 30.71  ? 500 VAL A CB  1 
ATOM   4184  C CG1 . VAL A 1 500 ? 14.751  15.999  -31.666 1.00 28.14  ? 500 VAL A CG1 1 
ATOM   4185  C CG2 . VAL A 1 500 ? 16.821  17.110  -30.737 1.00 29.47  ? 500 VAL A CG2 1 
ATOM   4186  N N   . LEU A 1 501 ? 14.816  13.598  -28.760 1.00 27.75  ? 501 LEU A N   1 
ATOM   4187  C CA  . LEU A 1 501 ? 14.054  12.386  -28.458 1.00 27.98  ? 501 LEU A CA  1 
ATOM   4188  C C   . LEU A 1 501 ? 13.093  12.612  -27.260 1.00 27.99  ? 501 LEU A C   1 
ATOM   4189  O O   . LEU A 1 501 ? 11.882  12.361  -27.377 1.00 26.96  ? 501 LEU A O   1 
ATOM   4190  C CB  . LEU A 1 501 ? 14.996  11.176  -28.187 1.00 28.31  ? 501 LEU A CB  1 
ATOM   4191  C CG  . LEU A 1 501 ? 14.313  9.816   -27.901 1.00 28.68  ? 501 LEU A CG  1 
ATOM   4192  C CD1 . LEU A 1 501 ? 13.269  9.492   -28.965 1.00 28.24  ? 501 LEU A CD1 1 
ATOM   4193  C CD2 . LEU A 1 501 ? 15.304  8.661   -27.754 1.00 28.16  ? 501 LEU A CD2 1 
ATOM   4194  N N   . SER A 1 502 ? 13.635  13.104  -26.138 1.00 29.07  ? 502 SER A N   1 
ATOM   4195  C CA  . SER A 1 502 ? 12.829  13.470  -24.935 1.00 30.06  ? 502 SER A CA  1 
ATOM   4196  C C   . SER A 1 502 ? 11.660  14.436  -25.195 1.00 30.15  ? 502 SER A C   1 
ATOM   4197  O O   . SER A 1 502 ? 10.541  14.172  -24.750 1.00 31.80  ? 502 SER A O   1 
ATOM   4198  C CB  . SER A 1 502 ? 13.720  14.026  -23.810 1.00 32.04  ? 502 SER A CB  1 
ATOM   4199  O OG  . SER A 1 502 ? 14.716  13.082  -23.437 1.00 36.28  ? 502 SER A OG  1 
ATOM   4200  N N   . SER A 1 503 ? 11.922  15.566  -25.857 1.00 28.45  ? 503 SER A N   1 
ATOM   4201  C CA  . SER A 1 503 ? 10.848  16.468  -26.301 1.00 29.34  ? 503 SER A CA  1 
ATOM   4202  C C   . SER A 1 503 ? 9.770   15.756  -27.117 1.00 28.80  ? 503 SER A C   1 
ATOM   4203  O O   . SER A 1 503 ? 8.561   15.946  -26.876 1.00 29.45  ? 503 SER A O   1 
ATOM   4204  C CB  . SER A 1 503 ? 11.417  17.570  -27.168 1.00 32.58  ? 503 SER A CB  1 
ATOM   4205  O OG  . SER A 1 503 ? 12.327  18.319  -26.418 1.00 45.07  ? 503 SER A OG  1 
ATOM   4206  N N   . THR A 1 504 ? 10.210  14.963  -28.097 1.00 27.73  ? 504 THR A N   1 
ATOM   4207  C CA  . THR A 1 504 ? 9.314   14.172  -28.942 1.00 27.63  ? 504 THR A CA  1 
ATOM   4208  C C   . THR A 1 504 ? 8.397   13.265  -28.144 1.00 27.18  ? 504 THR A C   1 
ATOM   4209  O O   . THR A 1 504 ? 7.193   13.285  -28.350 1.00 29.24  ? 504 THR A O   1 
ATOM   4210  C CB  . THR A 1 504 ? 10.106  13.331  -29.956 1.00 28.41  ? 504 THR A CB  1 
ATOM   4211  O OG1 . THR A 1 504 ? 11.002  14.187  -30.667 1.00 28.78  ? 504 THR A OG1 1 
ATOM   4212  C CG2 . THR A 1 504 ? 9.167   12.646  -30.952 1.00 28.18  ? 504 THR A CG2 1 
ATOM   4213  N N   . VAL A 1 505 ? 8.951   12.468  -27.231 1.00 27.16  ? 505 VAL A N   1 
ATOM   4214  C CA  . VAL A 1 505 ? 8.098   11.596  -26.380 1.00 26.60  ? 505 VAL A CA  1 
ATOM   4215  C C   . VAL A 1 505 ? 7.113   12.444  -25.564 1.00 25.74  ? 505 VAL A C   1 
ATOM   4216  O O   . VAL A 1 505 ? 5.927   12.126  -25.465 1.00 25.07  ? 505 VAL A O   1 
ATOM   4217  C CB  . VAL A 1 505 ? 8.931   10.719  -25.429 1.00 26.74  ? 505 VAL A CB  1 
ATOM   4218  C CG1 . VAL A 1 505 ? 8.038   10.041  -24.373 1.00 26.31  ? 505 VAL A CG1 1 
ATOM   4219  C CG2 . VAL A 1 505 ? 9.746   9.697   -26.210 1.00 25.56  ? 505 VAL A CG2 1 
ATOM   4220  N N   . ARG A 1 506 ? 7.603   13.550  -25.021 1.00 26.20  ? 506 ARG A N   1 
ATOM   4221  C CA  . ARG A 1 506 ? 6.731   14.493  -24.337 1.00 26.72  ? 506 ARG A CA  1 
ATOM   4222  C C   . ARG A 1 506 ? 5.591   14.979  -25.261 1.00 25.53  ? 506 ARG A C   1 
ATOM   4223  O O   . ARG A 1 506 ? 4.439   14.878  -24.910 1.00 24.59  ? 506 ARG A O   1 
ATOM   4224  C CB  . ARG A 1 506 ? 7.559   15.646  -23.736 1.00 28.71  ? 506 ARG A CB  1 
ATOM   4225  C CG  . ARG A 1 506 ? 6.733   16.692  -22.978 1.00 30.61  ? 506 ARG A CG  1 
ATOM   4226  C CD  . ARG A 1 506 ? 6.578   17.907  -23.906 1.00 33.81  ? 506 ARG A CD  1 
ATOM   4227  N NE  . ARG A 1 506 ? 5.212   18.392  -23.914 1.00 34.05  ? 506 ARG A NE  1 
ATOM   4228  C CZ  . ARG A 1 506 ? 4.679   19.148  -24.858 1.00 35.24  ? 506 ARG A CZ  1 
ATOM   4229  N NH1 . ARG A 1 506 ? 5.391   19.517  -25.936 1.00 32.52  ? 506 ARG A NH1 1 
ATOM   4230  N NH2 . ARG A 1 506 ? 3.414   19.526  -24.718 1.00 35.95  ? 506 ARG A NH2 1 
ATOM   4231  N N   . ALA A 1 507 ? 5.932   15.409  -26.473 1.00 25.37  ? 507 ALA A N   1 
ATOM   4232  C CA  . ALA A 1 507 ? 4.963   15.991  -27.409 1.00 25.91  ? 507 ALA A CA  1 
ATOM   4233  C C   . ALA A 1 507 ? 3.917   15.014  -27.893 1.00 26.59  ? 507 ALA A C   1 
ATOM   4234  O O   . ALA A 1 507 ? 2.737   15.382  -28.017 1.00 28.62  ? 507 ALA A O   1 
ATOM   4235  C CB  . ALA A 1 507 ? 5.676   16.624  -28.602 1.00 25.36  ? 507 ALA A CB  1 
ATOM   4236  N N   . TYR A 1 508 ? 4.330   13.782  -28.203 1.00 26.08  ? 508 TYR A N   1 
ATOM   4237  C CA  . TYR A 1 508 ? 3.381   12.785  -28.701 1.00 26.54  ? 508 TYR A CA  1 
ATOM   4238  C C   . TYR A 1 508 ? 2.459   12.289  -27.594 1.00 28.10  ? 508 TYR A C   1 
ATOM   4239  O O   . TYR A 1 508 ? 1.246   12.154  -27.798 1.00 28.05  ? 508 TYR A O   1 
ATOM   4240  C CB  . TYR A 1 508 ? 4.107   11.639  -29.401 1.00 26.91  ? 508 TYR A CB  1 
ATOM   4241  C CG  . TYR A 1 508 ? 4.404   11.962  -30.855 1.00 28.45  ? 508 TYR A CG  1 
ATOM   4242  C CD1 . TYR A 1 508 ? 3.420   11.829  -31.821 1.00 28.76  ? 508 TYR A CD1 1 
ATOM   4243  C CD2 . TYR A 1 508 ? 5.645   12.446  -31.248 1.00 28.95  ? 508 TYR A CD2 1 
ATOM   4244  C CE1 . TYR A 1 508 ? 3.671   12.119  -33.139 1.00 29.77  ? 508 TYR A CE1 1 
ATOM   4245  C CE2 . TYR A 1 508 ? 5.909   12.751  -32.579 1.00 30.44  ? 508 TYR A CE2 1 
ATOM   4246  C CZ  . TYR A 1 508 ? 4.910   12.593  -33.522 1.00 30.42  ? 508 TYR A CZ  1 
ATOM   4247  O OH  . TYR A 1 508 ? 5.125   12.913  -34.859 1.00 29.76  ? 508 TYR A OH  1 
ATOM   4248  N N   . ALA A 1 509 ? 3.029   12.080  -26.404 1.00 28.14  ? 509 ALA A N   1 
ATOM   4249  C CA  . ALA A 1 509 ? 2.240   11.776  -25.209 1.00 29.78  ? 509 ALA A CA  1 
ATOM   4250  C C   . ALA A 1 509 ? 1.192   12.857  -24.912 1.00 29.84  ? 509 ALA A C   1 
ATOM   4251  O O   . ALA A 1 509 ? 0.071   12.554  -24.478 1.00 28.39  ? 509 ALA A O   1 
ATOM   4252  C CB  . ALA A 1 509 ? 3.156   11.574  -24.002 1.00 29.22  ? 509 ALA A CB  1 
ATOM   4253  N N   . SER A 1 510 ? 1.563   14.112  -25.149 1.00 29.96  ? 510 SER A N   1 
ATOM   4254  C CA  . SER A 1 510 ? 0.659   15.215  -24.904 1.00 32.88  ? 510 SER A CA  1 
ATOM   4255  C C   . SER A 1 510 ? -0.466  15.273  -25.940 1.00 34.23  ? 510 SER A C   1 
ATOM   4256  O O   . SER A 1 510 ? -1.621  15.453  -25.588 1.00 36.23  ? 510 SER A O   1 
ATOM   4257  C CB  . SER A 1 510 ? 1.418   16.534  -24.878 1.00 33.14  ? 510 SER A CB  1 
ATOM   4258  O OG  . SER A 1 510 ? 0.508   17.600  -24.979 1.00 34.34  ? 510 SER A OG  1 
ATOM   4259  N N   . ARG A 1 511 ? -0.132  15.102  -27.213 1.00 36.55  ? 511 ARG A N   1 
ATOM   4260  C CA  . ARG A 1 511 ? -1.170  15.046  -28.250 1.00 37.41  ? 511 ARG A CA  1 
ATOM   4261  C C   . ARG A 1 511 ? -2.130  13.894  -28.000 1.00 35.41  ? 511 ARG A C   1 
ATOM   4262  O O   . ARG A 1 511 ? -3.333  14.052  -28.164 1.00 35.16  ? 511 ARG A O   1 
ATOM   4263  C CB  . ARG A 1 511 ? -0.569  14.976  -29.666 1.00 39.99  ? 511 ARG A CB  1 
ATOM   4264  C CG  . ARG A 1 511 ? 0.002   16.311  -30.143 1.00 48.00  ? 511 ARG A CG  1 
ATOM   4265  C CD  . ARG A 1 511 ? 0.485   16.267  -31.594 1.00 51.53  ? 511 ARG A CD  1 
ATOM   4266  N NE  . ARG A 1 511 ? 1.638   17.153  -31.844 1.00 55.52  ? 511 ARG A NE  1 
ATOM   4267  C CZ  . ARG A 1 511 ? 2.896   16.729  -32.028 1.00 53.99  ? 511 ARG A CZ  1 
ATOM   4268  N NH1 . ARG A 1 511 ? 3.183   15.439  -31.983 1.00 49.04  ? 511 ARG A NH1 1 
ATOM   4269  N NH2 . ARG A 1 511 ? 3.874   17.602  -32.258 1.00 53.79  ? 511 ARG A NH2 1 
ATOM   4270  N N   . ALA A 1 512 ? -1.598  12.742  -27.592 1.00 32.77  ? 512 ALA A N   1 
ATOM   4271  C CA  . ALA A 1 512 ? -2.441  11.618  -27.240 1.00 32.64  ? 512 ALA A CA  1 
ATOM   4272  C C   . ALA A 1 512 ? -3.406  11.973  -26.095 1.00 33.32  ? 512 ALA A C   1 
ATOM   4273  O O   . ALA A 1 512 ? -4.619  11.746  -26.214 1.00 33.09  ? 512 ALA A O   1 
ATOM   4274  C CB  . ALA A 1 512 ? -1.602  10.400  -26.885 1.00 30.50  ? 512 ALA A CB  1 
ATOM   4275  N N   . PHE A 1 513 ? -2.869  12.532  -25.000 1.00 32.93  ? 513 PHE A N   1 
ATOM   4276  C CA  . PHE A 1 513 ? -3.680  12.921  -23.832 1.00 33.67  ? 513 PHE A CA  1 
ATOM   4277  C C   . PHE A 1 513 ? -4.883  13.777  -24.244 1.00 34.93  ? 513 PHE A C   1 
ATOM   4278  O O   . PHE A 1 513 ? -6.014  13.506  -23.831 1.00 35.18  ? 513 PHE A O   1 
ATOM   4279  C CB  . PHE A 1 513 ? -2.819  13.658  -22.774 1.00 34.17  ? 513 PHE A CB  1 
ATOM   4280  C CG  . PHE A 1 513 ? -3.533  13.908  -21.458 1.00 33.53  ? 513 PHE A CG  1 
ATOM   4281  C CD1 . PHE A 1 513 ? -4.325  15.046  -21.278 1.00 34.00  ? 513 PHE A CD1 1 
ATOM   4282  C CD2 . PHE A 1 513 ? -3.408  13.006  -20.392 1.00 34.05  ? 513 PHE A CD2 1 
ATOM   4283  C CE1 . PHE A 1 513 ? -4.981  15.279  -20.062 1.00 34.16  ? 513 PHE A CE1 1 
ATOM   4284  C CE2 . PHE A 1 513 ? -4.060  13.233  -19.175 1.00 34.12  ? 513 PHE A CE2 1 
ATOM   4285  C CZ  . PHE A 1 513 ? -4.848  14.369  -19.010 1.00 33.78  ? 513 PHE A CZ  1 
ATOM   4286  N N   . LYS A 1 514 ? -4.630  14.794  -25.069 1.00 36.98  ? 514 LYS A N   1 
ATOM   4287  C CA  . LYS A 1 514 ? -5.670  15.711  -25.540 1.00 38.83  ? 514 LYS A CA  1 
ATOM   4288  C C   . LYS A 1 514 ? -6.712  15.019  -26.392 1.00 37.69  ? 514 LYS A C   1 
ATOM   4289  O O   . LYS A 1 514 ? -7.900  15.230  -26.211 1.00 37.60  ? 514 LYS A O   1 
ATOM   4290  C CB  . LYS A 1 514 ? -5.054  16.868  -26.326 1.00 43.97  ? 514 LYS A CB  1 
ATOM   4291  C CG  . LYS A 1 514 ? -4.521  17.981  -25.443 1.00 51.97  ? 514 LYS A CG  1 
ATOM   4292  C CD  . LYS A 1 514 ? -3.979  19.148  -26.262 1.00 58.77  ? 514 LYS A CD  1 
ATOM   4293  C CE  . LYS A 1 514 ? -3.472  20.266  -25.352 1.00 61.54  ? 514 LYS A CE  1 
ATOM   4294  N NZ  . LYS A 1 514 ? -2.627  19.739  -24.239 1.00 63.64  ? 514 LYS A NZ  1 
ATOM   4295  N N   . LYS A 1 515 ? -6.263  14.193  -27.328 1.00 37.37  ? 515 LYS A N   1 
ATOM   4296  C CA  . LYS A 1 515 ? -7.175  13.453  -28.182 1.00 38.69  ? 515 LYS A CA  1 
ATOM   4297  C C   . LYS A 1 515 ? -8.072  12.532  -27.351 1.00 38.40  ? 515 LYS A C   1 
ATOM   4298  O O   . LYS A 1 515 ? -9.267  12.439  -27.599 1.00 40.21  ? 515 LYS A O   1 
ATOM   4299  C CB  . LYS A 1 515 ? -6.397  12.668  -29.241 1.00 40.87  ? 515 LYS A CB  1 
ATOM   4300  C CG  . LYS A 1 515 ? -6.439  13.275  -30.638 1.00 44.42  ? 515 LYS A CG  1 
ATOM   4301  C CD  . LYS A 1 515 ? -5.526  14.486  -30.780 1.00 48.33  ? 515 LYS A CD  1 
ATOM   4302  C CE  . LYS A 1 515 ? -5.243  14.808  -32.248 1.00 50.97  ? 515 LYS A CE  1 
ATOM   4303  N NZ  . LYS A 1 515 ? -6.404  15.439  -32.949 1.00 53.49  ? 515 LYS A NZ  1 
ATOM   4304  N N   . ILE A 1 516 ? -7.492  11.892  -26.337 1.00 36.88  ? 516 ILE A N   1 
ATOM   4305  C CA  . ILE A 1 516 ? -8.224  11.000  -25.451 1.00 36.27  ? 516 ILE A CA  1 
ATOM   4306  C C   . ILE A 1 516 ? -9.288  11.759  -24.643 1.00 38.48  ? 516 ILE A C   1 
ATOM   4307  O O   . ILE A 1 516 ? -10.409 11.261  -24.459 1.00 37.66  ? 516 ILE A O   1 
ATOM   4308  C CB  . ILE A 1 516 ? -7.265  10.196  -24.525 1.00 34.97  ? 516 ILE A CB  1 
ATOM   4309  C CG1 . ILE A 1 516 ? -6.597  9.060   -25.313 1.00 33.86  ? 516 ILE A CG1 1 
ATOM   4310  C CG2 . ILE A 1 516 ? -8.003  9.634   -23.312 1.00 34.17  ? 516 ILE A CG2 1 
ATOM   4311  C CD1 . ILE A 1 516 ? -5.444  8.382   -24.594 1.00 32.26  ? 516 ILE A CD1 1 
ATOM   4312  N N   . VAL A 1 517 ? -8.943  12.972  -24.198 1.00 38.32  ? 517 VAL A N   1 
ATOM   4313  C CA  . VAL A 1 517 ? -9.875  13.831  -23.473 1.00 39.34  ? 517 VAL A CA  1 
ATOM   4314  C C   . VAL A 1 517 ? -11.025 14.277  -24.381 1.00 42.51  ? 517 VAL A C   1 
ATOM   4315  O O   . VAL A 1 517 ? -12.195 14.134  -24.032 1.00 44.53  ? 517 VAL A O   1 
ATOM   4316  C CB  . VAL A 1 517 ? -9.148  15.055  -22.847 1.00 39.57  ? 517 VAL A CB  1 
ATOM   4317  C CG1 . VAL A 1 517 ? -10.138 16.149  -22.445 1.00 40.00  ? 517 VAL A CG1 1 
ATOM   4318  C CG2 . VAL A 1 517 ? -8.317  14.622  -21.637 1.00 36.98  ? 517 VAL A CG2 1 
ATOM   4319  N N   . THR A 1 518 ? -10.682 14.791  -25.555 1.00 45.01  ? 518 THR A N   1 
ATOM   4320  C CA  . THR A 1 518 ? -11.666 15.281  -26.522 1.00 48.00  ? 518 THR A CA  1 
ATOM   4321  C C   . THR A 1 518 ? -12.696 14.223  -26.936 1.00 48.70  ? 518 THR A C   1 
ATOM   4322  O O   . THR A 1 518 ? -13.878 14.531  -27.090 1.00 50.88  ? 518 THR A O   1 
ATOM   4323  C CB  . THR A 1 518 ? -10.969 15.822  -27.783 1.00 47.29  ? 518 THR A CB  1 
ATOM   4324  O OG1 . THR A 1 518 ? -10.141 16.926  -27.421 1.00 47.92  ? 518 THR A OG1 1 
ATOM   4325  C CG2 . THR A 1 518 ? -11.985 16.291  -28.815 1.00 48.93  ? 518 THR A CG2 1 
ATOM   4326  N N   . TYR A 1 519 ? -12.237 12.990  -27.127 1.00 45.66  ? 519 TYR A N   1 
ATOM   4327  C CA  . TYR A 1 519 ? -13.094 11.928  -27.633 1.00 44.25  ? 519 TYR A CA  1 
ATOM   4328  C C   . TYR A 1 519 ? -13.403 10.895  -26.567 1.00 43.27  ? 519 TYR A C   1 
ATOM   4329  O O   . TYR A 1 519 ? -13.683 9.735   -26.866 1.00 43.09  ? 519 TYR A O   1 
ATOM   4330  C CB  . TYR A 1 519 ? -12.465 11.294  -28.867 1.00 44.67  ? 519 TYR A CB  1 
ATOM   4331  C CG  . TYR A 1 519 ? -12.244 12.306  -29.953 1.00 46.32  ? 519 TYR A CG  1 
ATOM   4332  C CD1 . TYR A 1 519 ? -13.319 13.024  -30.474 1.00 48.71  ? 519 TYR A CD1 1 
ATOM   4333  C CD2 . TYR A 1 519 ? -10.962 12.584  -30.438 1.00 45.42  ? 519 TYR A CD2 1 
ATOM   4334  C CE1 . TYR A 1 519 ? -13.135 13.977  -31.461 1.00 51.27  ? 519 TYR A CE1 1 
ATOM   4335  C CE2 . TYR A 1 519 ? -10.768 13.535  -31.431 1.00 47.55  ? 519 TYR A CE2 1 
ATOM   4336  C CZ  . TYR A 1 519 ? -11.861 14.231  -31.935 1.00 49.66  ? 519 TYR A CZ  1 
ATOM   4337  O OH  . TYR A 1 519 ? -11.708 15.180  -32.917 1.00 53.62  ? 519 TYR A OH  1 
ATOM   4338  N N   . LYS A 1 520 ? -13.358 11.345  -25.317 1.00 42.72  ? 520 LYS A N   1 
ATOM   4339  C CA  . LYS A 1 520 ? -13.698 10.528  -24.165 1.00 43.06  ? 520 LYS A CA  1 
ATOM   4340  C C   . LYS A 1 520 ? -15.147 10.051  -24.234 1.00 43.06  ? 520 LYS A C   1 
ATOM   4341  O O   . LYS A 1 520 ? -16.052 10.823  -24.538 1.00 43.44  ? 520 LYS A O   1 
ATOM   4342  C CB  . LYS A 1 520 ? -13.473 11.338  -22.889 1.00 42.60  ? 520 LYS A CB  1 
ATOM   4343  C CG  . LYS A 1 520 ? -13.718 10.570  -21.599 1.00 43.79  ? 520 LYS A CG  1 
ATOM   4344  C CD  . LYS A 1 520 ? -13.358 11.403  -20.379 1.00 42.74  ? 520 LYS A CD  1 
ATOM   4345  C CE  . LYS A 1 520 ? -11.849 11.555  -20.252 1.00 43.67  ? 520 LYS A CE  1 
ATOM   4346  N NZ  . LYS A 1 520 ? -11.492 12.449  -19.115 1.00 45.50  ? 520 LYS A NZ  1 
ATOM   4347  N N   . GLY A 1 521 ? -15.354 8.771   -23.964 1.00 42.90  ? 521 GLY A N   1 
ATOM   4348  C CA  . GLY A 1 521 ? -16.701 8.229   -23.848 1.00 44.96  ? 521 GLY A CA  1 
ATOM   4349  C C   . GLY A 1 521 ? -16.864 7.327   -22.643 1.00 44.91  ? 521 GLY A C   1 
ATOM   4350  O O   . GLY A 1 521 ? -15.945 7.179   -21.835 1.00 44.97  ? 521 GLY A O   1 
ATOM   4351  N N   . GLY A 1 522 ? -18.021 6.681   -22.552 1.00 45.80  ? 522 GLY A N   1 
ATOM   4352  C CA  . GLY A 1 522 ? -18.380 5.877   -21.389 1.00 43.68  ? 522 GLY A CA  1 
ATOM   4353  C C   . GLY A 1 522 ? -17.402 4.783   -20.999 1.00 43.95  ? 522 GLY A C   1 
ATOM   4354  O O   . GLY A 1 522 ? -17.471 4.278   -19.892 1.00 44.15  ? 522 GLY A O   1 
ATOM   4355  N N   . LYS A 1 523 ? -16.491 4.407   -21.901 1.00 45.38  ? 523 LYS A N   1 
ATOM   4356  C CA  . LYS A 1 523 ? -15.540 3.310   -21.619 1.00 43.15  ? 523 LYS A CA  1 
ATOM   4357  C C   . LYS A 1 523 ? -14.229 3.802   -20.998 1.00 43.91  ? 523 LYS A C   1 
ATOM   4358  O O   . LYS A 1 523 ? -13.343 2.997   -20.656 1.00 44.73  ? 523 LYS A O   1 
ATOM   4359  C CB  . LYS A 1 523 ? -15.279 2.474   -22.878 1.00 42.35  ? 523 LYS A CB  1 
ATOM   4360  C CG  . LYS A 1 523 ? -16.522 1.748   -23.375 1.00 42.32  ? 523 LYS A CG  1 
ATOM   4361  C CD  . LYS A 1 523 ? -16.248 0.834   -24.544 1.00 41.19  ? 523 LYS A CD  1 
ATOM   4362  C CE  . LYS A 1 523 ? -17.534 0.115   -24.921 1.00 43.78  ? 523 LYS A CE  1 
ATOM   4363  N NZ  . LYS A 1 523 ? -17.420 -0.682  -26.164 1.00 42.40  ? 523 LYS A NZ  1 
ATOM   4364  N N   . TYR A 1 524 ? -14.113 5.118   -20.840 1.00 41.22  ? 524 TYR A N   1 
ATOM   4365  C CA  . TYR A 1 524 ? -12.926 5.708   -20.242 1.00 41.66  ? 524 TYR A CA  1 
ATOM   4366  C C   . TYR A 1 524 ? -12.773 5.201   -18.829 1.00 42.42  ? 524 TYR A C   1 
ATOM   4367  O O   . TYR A 1 524 ? -13.763 5.081   -18.105 1.00 43.81  ? 524 TYR A O   1 
ATOM   4368  C CB  . TYR A 1 524 ? -13.042 7.231   -20.221 1.00 41.61  ? 524 TYR A CB  1 
ATOM   4369  C CG  . TYR A 1 524 ? -11.868 7.912   -19.569 1.00 40.66  ? 524 TYR A CG  1 
ATOM   4370  C CD1 . TYR A 1 524 ? -10.646 8.031   -20.242 1.00 39.67  ? 524 TYR A CD1 1 
ATOM   4371  C CD2 . TYR A 1 524 ? -11.968 8.430   -18.286 1.00 40.48  ? 524 TYR A CD2 1 
ATOM   4372  C CE1 . TYR A 1 524 ? -9.560  8.646   -19.649 1.00 39.93  ? 524 TYR A CE1 1 
ATOM   4373  C CE2 . TYR A 1 524 ? -10.884 9.049   -17.677 1.00 40.97  ? 524 TYR A CE2 1 
ATOM   4374  C CZ  . TYR A 1 524 ? -9.683  9.157   -18.366 1.00 40.85  ? 524 TYR A CZ  1 
ATOM   4375  O OH  . TYR A 1 524 ? -8.602  9.761   -17.772 1.00 41.13  ? 524 TYR A OH  1 
ATOM   4376  N N   . ARG A 1 525 ? -11.543 4.898   -18.424 1.00 43.03  ? 525 ARG A N   1 
ATOM   4377  C CA  . ARG A 1 525 ? -11.299 4.521   -17.025 1.00 43.00  ? 525 ARG A CA  1 
ATOM   4378  C C   . ARG A 1 525 ? -10.464 5.596   -16.345 1.00 41.70  ? 525 ARG A C   1 
ATOM   4379  O O   . ARG A 1 525 ? -10.928 6.280   -15.439 1.00 44.04  ? 525 ARG A O   1 
ATOM   4380  C CB  . ARG A 1 525 ? -10.612 3.150   -16.897 1.00 43.80  ? 525 ARG A CB  1 
ATOM   4381  C CG  . ARG A 1 525 ? -11.010 2.097   -17.921 1.00 48.69  ? 525 ARG A CG  1 
ATOM   4382  C CD  . ARG A 1 525 ? -12.224 1.290   -17.511 1.00 52.70  ? 525 ARG A CD  1 
ATOM   4383  N NE  . ARG A 1 525 ? -11.885 0.151   -16.654 1.00 59.67  ? 525 ARG A NE  1 
ATOM   4384  C CZ  . ARG A 1 525 ? -12.029 -1.135  -16.991 1.00 57.50  ? 525 ARG A CZ  1 
ATOM   4385  N NH1 . ARG A 1 525 ? -12.496 -1.478  -18.185 1.00 53.88  ? 525 ARG A NH1 1 
ATOM   4386  N NH2 . ARG A 1 525 ? -11.703 -2.083  -16.119 1.00 56.18  ? 525 ARG A NH2 1 
ATOM   4387  N N   . LYS A 1 526 ? -9.228  5.736   -16.803 1.00 40.95  ? 526 LYS A N   1 
ATOM   4388  C CA  . LYS A 1 526 ? -8.295  6.713   -16.296 1.00 38.63  ? 526 LYS A CA  1 
ATOM   4389  C C   . LYS A 1 526 ? -7.006  6.597   -17.091 1.00 36.88  ? 526 LYS A C   1 
ATOM   4390  O O   . LYS A 1 526 ? -6.343  5.552   -17.063 1.00 34.85  ? 526 LYS A O   1 
ATOM   4391  C CB  . LYS A 1 526 ? -8.001  6.476   -14.806 1.00 41.19  ? 526 LYS A CB  1 
ATOM   4392  C CG  . LYS A 1 526 ? -6.926  7.401   -14.243 1.00 41.65  ? 526 LYS A CG  1 
ATOM   4393  C CD  . LYS A 1 526 ? -6.590  7.078   -12.792 1.00 43.36  ? 526 LYS A CD  1 
ATOM   4394  C CE  . LYS A 1 526 ? -5.457  7.960   -12.284 1.00 43.23  ? 526 LYS A CE  1 
ATOM   4395  N NZ  . LYS A 1 526 ? -4.976  7.501   -10.951 1.00 46.45  ? 526 LYS A NZ  1 
ATOM   4396  N N   . VAL A 1 527 ? -6.651  7.684   -17.776 1.00 35.50  ? 527 VAL A N   1 
ATOM   4397  C CA  . VAL A 1 527 ? -5.416  7.771   -18.535 1.00 32.58  ? 527 VAL A CA  1 
ATOM   4398  C C   . VAL A 1 527 ? -4.564  8.921   -17.989 1.00 31.78  ? 527 VAL A C   1 
ATOM   4399  O O   . VAL A 1 527 ? -4.993  10.067  -18.009 1.00 33.55  ? 527 VAL A O   1 
ATOM   4400  C CB  . VAL A 1 527 ? -5.692  8.027   -20.035 1.00 32.60  ? 527 VAL A CB  1 
ATOM   4401  C CG1 . VAL A 1 527 ? -4.377  8.244   -20.796 1.00 33.17  ? 527 VAL A CG1 1 
ATOM   4402  C CG2 . VAL A 1 527 ? -6.468  6.864   -20.645 1.00 33.35  ? 527 VAL A CG2 1 
ATOM   4403  N N   . THR A 1 528 ? -3.353  8.625   -17.540 1.00 28.35  ? 528 THR A N   1 
ATOM   4404  C CA  . THR A 1 528 ? -2.451  9.669   -17.150 1.00 29.73  ? 528 THR A CA  1 
ATOM   4405  C C   . THR A 1 528 ? -1.455  9.984   -18.250 1.00 29.61  ? 528 THR A C   1 
ATOM   4406  O O   . THR A 1 528 ? -1.183  9.158   -19.102 1.00 29.85  ? 528 THR A O   1 
ATOM   4407  C CB  . THR A 1 528 ? -1.643  9.284   -15.931 1.00 29.55  ? 528 THR A CB  1 
ATOM   4408  O OG1 . THR A 1 528 ? -0.749  8.248   -16.311 1.00 29.11  ? 528 THR A OG1 1 
ATOM   4409  C CG2 . THR A 1 528 ? -2.566  8.829   -14.767 1.00 29.48  ? 528 THR A CG2 1 
ATOM   4410  N N   . PHE A 1 529 ? -0.920  11.199  -18.210 1.00 29.37  ? 529 PHE A N   1 
ATOM   4411  C CA  . PHE A 1 529 ? 0.207   11.592  -19.036 1.00 29.87  ? 529 PHE A CA  1 
ATOM   4412  C C   . PHE A 1 529 ? 1.390   10.638  -18.832 1.00 31.00  ? 529 PHE A C   1 
ATOM   4413  O O   . PHE A 1 529 ? 2.056   10.238  -19.798 1.00 30.48  ? 529 PHE A O   1 
ATOM   4414  C CB  . PHE A 1 529 ? 0.634   13.024  -18.701 1.00 27.42  ? 529 PHE A CB  1 
ATOM   4415  C CG  . PHE A 1 529 ? 1.757   13.539  -19.565 1.00 26.65  ? 529 PHE A CG  1 
ATOM   4416  C CD1 . PHE A 1 529 ? 1.508   13.988  -20.861 1.00 25.43  ? 529 PHE A CD1 1 
ATOM   4417  C CD2 . PHE A 1 529 ? 3.075   13.554  -19.093 1.00 26.25  ? 529 PHE A CD2 1 
ATOM   4418  C CE1 . PHE A 1 529 ? 2.539   14.469  -21.657 1.00 24.74  ? 529 PHE A CE1 1 
ATOM   4419  C CE2 . PHE A 1 529 ? 4.113   14.030  -19.897 1.00 26.19  ? 529 PHE A CE2 1 
ATOM   4420  C CZ  . PHE A 1 529 ? 3.840   14.485  -21.179 1.00 24.86  ? 529 PHE A CZ  1 
ATOM   4421  N N   . GLN A 1 530 ? 1.643   10.294  -17.574 1.00 32.44  ? 530 GLN A N   1 
ATOM   4422  C CA  . GLN A 1 530 ? 2.710   9.363   -17.210 1.00 35.48  ? 530 GLN A CA  1 
ATOM   4423  C C   . GLN A 1 530 ? 2.558   8.014   -17.935 1.00 34.05  ? 530 GLN A C   1 
ATOM   4424  O O   . GLN A 1 530 ? 3.529   7.497   -18.519 1.00 31.60  ? 530 GLN A O   1 
ATOM   4425  C CB  . GLN A 1 530 ? 2.752   9.152   -15.686 1.00 37.60  ? 530 GLN A CB  1 
ATOM   4426  C CG  . GLN A 1 530 ? 3.191   10.376  -14.875 1.00 43.60  ? 530 GLN A CG  1 
ATOM   4427  C CD  . GLN A 1 530 ? 2.212   11.572  -14.937 1.00 45.84  ? 530 GLN A CD  1 
ATOM   4428  O OE1 . GLN A 1 530 ? 0.982   11.412  -14.829 1.00 42.75  ? 530 GLN A OE1 1 
ATOM   4429  N NE2 . GLN A 1 530 ? 2.767   12.779  -15.097 1.00 45.90  ? 530 GLN A NE2 1 
ATOM   4430  N N   . CYS A 1 531 ? 1.346   7.461   -17.919 1.00 32.16  ? 531 CYS A N   1 
ATOM   4431  C CA  . CYS A 1 531 ? 1.106   6.174   -18.567 1.00 32.16  ? 531 CYS A CA  1 
ATOM   4432  C C   . CYS A 1 531 ? 1.431   6.221   -20.084 1.00 30.93  ? 531 CYS A C   1 
ATOM   4433  O O   . CYS A 1 531 ? 2.137   5.343   -20.617 1.00 29.33  ? 531 CYS A O   1 
ATOM   4434  C CB  . CYS A 1 531 ? -0.327  5.699   -18.327 1.00 33.86  ? 531 CYS A CB  1 
ATOM   4435  S SG  . CYS A 1 531 ? -0.683  4.070   -19.063 1.00 40.50  ? 531 CYS A SG  1 
ATOM   4436  N N   . LEU A 1 532 ? 0.936   7.265   -20.755 1.00 29.20  ? 532 LEU A N   1 
ATOM   4437  C CA  . LEU A 1 532 ? 1.193   7.477   -22.153 1.00 27.22  ? 532 LEU A CA  1 
ATOM   4438  C C   . LEU A 1 532 ? 2.675   7.642   -22.442 1.00 27.68  ? 532 LEU A C   1 
ATOM   4439  O O   . LEU A 1 532 ? 3.210   7.082   -23.423 1.00 27.50  ? 532 LEU A O   1 
ATOM   4440  C CB  . LEU A 1 532 ? 0.420   8.692   -22.650 1.00 29.22  ? 532 LEU A CB  1 
ATOM   4441  C CG  . LEU A 1 532 ? -1.102  8.538   -22.780 1.00 28.86  ? 532 LEU A CG  1 
ATOM   4442  C CD1 . LEU A 1 532 ? -1.764  9.894   -22.940 1.00 28.65  ? 532 LEU A CD1 1 
ATOM   4443  C CD2 . LEU A 1 532 ? -1.462  7.610   -23.940 1.00 29.19  ? 532 LEU A CD2 1 
ATOM   4444  N N   . LYS A 1 533 ? 3.363   8.391   -21.591 1.00 27.09  ? 533 LYS A N   1 
ATOM   4445  C CA  . LYS A 1 533 ? 4.771   8.619   -21.805 1.00 26.35  ? 533 LYS A CA  1 
ATOM   4446  C C   . LYS A 1 533 ? 5.536   7.311   -21.779 1.00 25.68  ? 533 LYS A C   1 
ATOM   4447  O O   . LYS A 1 533 ? 6.445   7.106   -22.583 1.00 24.29  ? 533 LYS A O   1 
ATOM   4448  C CB  . LYS A 1 533 ? 5.303   9.553   -20.760 1.00 28.64  ? 533 LYS A CB  1 
ATOM   4449  C CG  . LYS A 1 533 ? 6.564   10.284  -21.159 1.00 31.37  ? 533 LYS A CG  1 
ATOM   4450  C CD  . LYS A 1 533 ? 6.556   11.682  -20.573 1.00 30.89  ? 533 LYS A CD  1 
ATOM   4451  C CE  . LYS A 1 533 ? 6.655   11.639  -19.053 1.00 33.01  ? 533 LYS A CE  1 
ATOM   4452  N NZ  . LYS A 1 533 ? 8.068   11.758  -18.598 1.00 34.41  ? 533 LYS A NZ  1 
ATOM   4453  N N   . SER A 1 534 ? 5.149   6.419   -20.871 1.00 25.92  ? 534 SER A N   1 
ATOM   4454  C CA  . SER A 1 534 ? 5.783   5.089   -20.754 1.00 27.18  ? 534 SER A CA  1 
ATOM   4455  C C   . SER A 1 534 ? 5.550   4.193   -21.959 1.00 27.58  ? 534 SER A C   1 
ATOM   4456  O O   . SER A 1 534 ? 6.446   3.483   -22.379 1.00 29.26  ? 534 SER A O   1 
ATOM   4457  C CB  . SER A 1 534 ? 5.286   4.350   -19.510 1.00 26.81  ? 534 SER A CB  1 
ATOM   4458  O OG  . SER A 1 534 ? 5.731   4.996   -18.361 1.00 28.85  ? 534 SER A OG  1 
ATOM   4459  N N   . ILE A 1 535 ? 4.318   4.167   -22.455 1.00 28.28  ? 535 ILE A N   1 
ATOM   4460  C CA  . ILE A 1 535 ? 3.977   3.416   -23.670 1.00 27.70  ? 535 ILE A CA  1 
ATOM   4461  C C   . ILE A 1 535 ? 4.859   3.886   -24.852 1.00 28.26  ? 535 ILE A C   1 
ATOM   4462  O O   . ILE A 1 535 ? 5.447   3.056   -25.591 1.00 27.65  ? 535 ILE A O   1 
ATOM   4463  C CB  . ILE A 1 535 ? 2.456   3.546   -23.951 1.00 27.42  ? 535 ILE A CB  1 
ATOM   4464  C CG1 . ILE A 1 535 ? 1.676   2.800   -22.852 1.00 27.37  ? 535 ILE A CG1 1 
ATOM   4465  C CG2 . ILE A 1 535 ? 2.084   3.054   -25.343 1.00 27.69  ? 535 ILE A CG2 1 
ATOM   4466  C CD1 . ILE A 1 535 ? 0.169   2.831   -23.006 1.00 27.78  ? 535 ILE A CD1 1 
ATOM   4467  N N   . ALA A 1 536 ? 5.031   5.208   -24.953 1.00 26.10  ? 536 ALA A N   1 
ATOM   4468  C CA  . ALA A 1 536 ? 5.876   5.819   -25.979 1.00 26.11  ? 536 ALA A CA  1 
ATOM   4469  C C   . ALA A 1 536 ? 7.348   5.390   -25.846 1.00 26.13  ? 536 ALA A C   1 
ATOM   4470  O O   . ALA A 1 536 ? 7.963   4.987   -26.827 1.00 24.23  ? 536 ALA A O   1 
ATOM   4471  C CB  . ALA A 1 536 ? 5.758   7.352   -25.934 1.00 24.70  ? 536 ALA A CB  1 
ATOM   4472  N N   . TRP A 1 537 ? 7.907   5.486   -24.635 1.00 25.90  ? 537 TRP A N   1 
ATOM   4473  C CA  . TRP A 1 537 ? 9.289   5.044   -24.411 1.00 26.90  ? 537 TRP A CA  1 
ATOM   4474  C C   . TRP A 1 537 ? 9.445   3.587   -24.782 1.00 28.79  ? 537 TRP A C   1 
ATOM   4475  O O   . TRP A 1 537 ? 10.497  3.163   -25.320 1.00 28.21  ? 537 TRP A O   1 
ATOM   4476  C CB  . TRP A 1 537 ? 9.725   5.276   -22.962 1.00 25.60  ? 537 TRP A CB  1 
ATOM   4477  C CG  . TRP A 1 537 ? 10.125  6.707   -22.687 1.00 24.64  ? 537 TRP A CG  1 
ATOM   4478  C CD1 . TRP A 1 537 ? 9.568   7.587   -21.745 1.00 24.16  ? 537 TRP A CD1 1 
ATOM   4479  C CD2 . TRP A 1 537 ? 11.186  7.461   -23.342 1.00 23.32  ? 537 TRP A CD2 1 
ATOM   4480  N NE1 . TRP A 1 537 ? 10.194  8.823   -21.800 1.00 24.36  ? 537 TRP A NE1 1 
ATOM   4481  C CE2 . TRP A 1 537 ? 11.170  8.814   -22.740 1.00 24.08  ? 537 TRP A CE2 1 
ATOM   4482  C CE3 . TRP A 1 537 ? 12.094  7.183   -24.359 1.00 22.88  ? 537 TRP A CE3 1 
ATOM   4483  C CZ2 . TRP A 1 537 ? 12.053  9.805   -23.139 1.00 23.50  ? 537 TRP A CZ2 1 
ATOM   4484  C CZ3 . TRP A 1 537 ? 12.968  8.191   -24.770 1.00 22.46  ? 537 TRP A CZ3 1 
ATOM   4485  C CH2 . TRP A 1 537 ? 12.952  9.478   -24.166 1.00 23.83  ? 537 TRP A CH2 1 
ATOM   4486  N N   . ARG A 1 538 ? 8.400   2.809   -24.520 1.00 28.59  ? 538 ARG A N   1 
ATOM   4487  C CA  . ARG A 1 538 ? 8.471   1.380   -24.782 1.00 31.71  ? 538 ARG A CA  1 
ATOM   4488  C C   . ARG A 1 538 ? 8.500   1.150   -26.274 1.00 30.17  ? 538 ARG A C   1 
ATOM   4489  O O   . ARG A 1 538 ? 9.108   0.209   -26.740 1.00 30.72  ? 538 ARG A O   1 
ATOM   4490  C CB  . ARG A 1 538 ? 7.311   0.614   -24.115 1.00 31.86  ? 538 ARG A CB  1 
ATOM   4491  C CG  . ARG A 1 538 ? 7.524   0.407   -22.622 1.00 34.97  ? 538 ARG A CG  1 
ATOM   4492  C CD  . ARG A 1 538 ? 6.610   -0.673  -22.114 1.00 38.89  ? 538 ARG A CD  1 
ATOM   4493  N NE  . ARG A 1 538 ? 6.673   -0.904  -20.664 1.00 42.46  ? 538 ARG A NE  1 
ATOM   4494  C CZ  . ARG A 1 538 ? 7.100   -2.039  -20.102 1.00 42.74  ? 538 ARG A CZ  1 
ATOM   4495  N NH1 . ARG A 1 538 ? 7.578   -3.024  -20.860 1.00 43.43  ? 538 ARG A NH1 1 
ATOM   4496  N NH2 . ARG A 1 538 ? 7.065   -2.188  -18.786 1.00 39.27  ? 538 ARG A NH2 1 
ATOM   4497  N N   . ALA A 1 539 ? 7.835   2.030   -27.018 1.00 29.92  ? 539 ALA A N   1 
ATOM   4498  C CA  . ALA A 1 539 ? 7.704   1.856   -28.459 1.00 27.53  ? 539 ALA A CA  1 
ATOM   4499  C C   . ALA A 1 539 ? 9.045   2.154   -29.101 1.00 28.15  ? 539 ALA A C   1 
ATOM   4500  O O   . ALA A 1 539 ? 9.442   1.480   -30.056 1.00 30.53  ? 539 ALA A O   1 
ATOM   4501  C CB  . ALA A 1 539 ? 6.618   2.751   -29.011 1.00 24.71  ? 539 ALA A CB  1 
ATOM   4502  N N   . PHE A 1 540 ? 9.751   3.145   -28.553 1.00 27.22  ? 540 PHE A N   1 
ATOM   4503  C CA  . PHE A 1 540 ? 11.070  3.502   -29.013 1.00 27.94  ? 540 PHE A CA  1 
ATOM   4504  C C   . PHE A 1 540 ? 12.061  2.400   -28.682 1.00 30.29  ? 540 PHE A C   1 
ATOM   4505  O O   . PHE A 1 540 ? 12.855  2.008   -29.530 1.00 32.30  ? 540 PHE A O   1 
ATOM   4506  C CB  . PHE A 1 540 ? 11.512  4.855   -28.431 1.00 26.43  ? 540 PHE A CB  1 
ATOM   4507  C CG  . PHE A 1 540 ? 11.117  6.036   -29.283 1.00 26.53  ? 540 PHE A CG  1 
ATOM   4508  C CD1 . PHE A 1 540 ? 11.909  6.437   -30.353 1.00 26.48  ? 540 PHE A CD1 1 
ATOM   4509  C CD2 . PHE A 1 540 ? 9.930   6.715   -29.054 1.00 27.36  ? 540 PHE A CD2 1 
ATOM   4510  C CE1 . PHE A 1 540 ? 11.530  7.511   -31.169 1.00 27.32  ? 540 PHE A CE1 1 
ATOM   4511  C CE2 . PHE A 1 540 ? 9.542   7.793   -29.865 1.00 27.61  ? 540 PHE A CE2 1 
ATOM   4512  C CZ  . PHE A 1 540 ? 10.344  8.188   -30.923 1.00 27.06  ? 540 PHE A CZ  1 
ATOM   4513  N N   . LEU A 1 541 ? 11.998  1.885   -27.453 1.00 32.01  ? 541 LEU A N   1 
ATOM   4514  C CA  . LEU A 1 541 ? 12.832  0.763   -27.053 1.00 31.26  ? 541 LEU A CA  1 
ATOM   4515  C C   . LEU A 1 541 ? 12.683  -0.459  -27.948 1.00 32.77  ? 541 LEU A C   1 
ATOM   4516  O O   . LEU A 1 541 ? 13.653  -1.153  -28.221 1.00 35.86  ? 541 LEU A O   1 
ATOM   4517  C CB  . LEU A 1 541 ? 12.525  0.361   -25.627 1.00 33.32  ? 541 LEU A CB  1 
ATOM   4518  C CG  . LEU A 1 541 ? 13.077  1.257   -24.532 1.00 32.98  ? 541 LEU A CG  1 
ATOM   4519  C CD1 . LEU A 1 541 ? 12.669  0.648   -23.227 1.00 34.14  ? 541 LEU A CD1 1 
ATOM   4520  C CD2 . LEU A 1 541 ? 14.603  1.393   -24.626 1.00 33.90  ? 541 LEU A CD2 1 
ATOM   4521  N N   . ALA A 1 542 ? 11.471  -0.754  -28.382 1.00 31.36  ? 542 ALA A N   1 
ATOM   4522  C CA  . ALA A 1 542 ? 11.270  -1.971  -29.125 1.00 30.42  ? 542 ALA A CA  1 
ATOM   4523  C C   . ALA A 1 542 ? 11.932  -1.867  -30.523 1.00 29.49  ? 542 ALA A C   1 
ATOM   4524  O O   . ALA A 1 542 ? 12.257  -2.870  -31.142 1.00 27.01  ? 542 ALA A O   1 
ATOM   4525  C CB  . ALA A 1 542 ? 9.784   -2.295  -29.224 1.00 29.04  ? 542 ALA A CB  1 
ATOM   4526  N N   . VAL A 1 543 ? 12.147  -0.641  -30.988 1.00 29.63  ? 543 VAL A N   1 
ATOM   4527  C CA  . VAL A 1 543 ? 12.728  -0.411  -32.307 1.00 29.92  ? 543 VAL A CA  1 
ATOM   4528  C C   . VAL A 1 543 ? 14.226  -0.247  -32.182 1.00 30.52  ? 543 VAL A C   1 
ATOM   4529  O O   . VAL A 1 543 ? 14.979  -0.821  -32.942 1.00 31.58  ? 543 VAL A O   1 
ATOM   4530  C CB  . VAL A 1 543 ? 12.150  0.861   -32.961 1.00 31.22  ? 543 VAL A CB  1 
ATOM   4531  C CG1 . VAL A 1 543 ? 13.021  1.312   -34.118 1.00 31.43  ? 543 VAL A CG1 1 
ATOM   4532  C CG2 . VAL A 1 543 ? 10.726  0.629   -33.424 1.00 30.37  ? 543 VAL A CG2 1 
ATOM   4533  N N   . LEU A 1 544 ? 14.653  0.549   -31.212 1.00 30.52  ? 544 LEU A N   1 
ATOM   4534  C CA  . LEU A 1 544 ? 16.057  0.805   -31.016 1.00 30.22  ? 544 LEU A CA  1 
ATOM   4535  C C   . LEU A 1 544 ? 16.817  -0.491  -30.749 1.00 33.83  ? 544 LEU A C   1 
ATOM   4536  O O   . LEU A 1 544 ? 18.005  -0.614  -31.126 1.00 33.06  ? 544 LEU A O   1 
ATOM   4537  C CB  . LEU A 1 544 ? 16.265  1.791   -29.864 1.00 28.10  ? 544 LEU A CB  1 
ATOM   4538  C CG  . LEU A 1 544 ? 15.767  3.236   -30.058 1.00 27.75  ? 544 LEU A CG  1 
ATOM   4539  C CD1 . LEU A 1 544 ? 15.826  4.006   -28.734 1.00 25.05  ? 544 LEU A CD1 1 
ATOM   4540  C CD2 . LEU A 1 544 ? 16.554  3.950   -31.154 1.00 24.82  ? 544 LEU A CD2 1 
ATOM   4541  N N   . LYS A 1 545 ? 16.144  -1.450  -30.097 1.00 34.65  ? 545 LYS A N   1 
ATOM   4542  C CA  . LYS A 1 545 ? 16.773  -2.737  -29.725 1.00 37.26  ? 545 LYS A CA  1 
ATOM   4543  C C   . LYS A 1 545 ? 17.201  -3.518  -30.955 1.00 37.72  ? 545 LYS A C   1 
ATOM   4544  O O   . LYS A 1 545 ? 18.072  -4.392  -30.875 1.00 37.03  ? 545 LYS A O   1 
ATOM   4545  C CB  . LYS A 1 545 ? 15.815  -3.601  -28.901 1.00 37.60  ? 545 LYS A CB  1 
ATOM   4546  C CG  . LYS A 1 545 ? 15.986  -3.476  -27.400 1.00 40.98  ? 545 LYS A CG  1 
ATOM   4547  C CD  . LYS A 1 545 ? 14.734  -3.989  -26.720 1.00 43.47  ? 545 LYS A CD  1 
ATOM   4548  C CE  . LYS A 1 545 ? 15.075  -4.765  -25.477 1.00 47.91  ? 545 LYS A CE  1 
ATOM   4549  N NZ  . LYS A 1 545 ? 13.934  -5.627  -25.063 1.00 53.43  ? 545 LYS A NZ  1 
ATOM   4550  N N   . ARG A 1 546 ? 16.553  -3.222  -32.084 1.00 35.92  ? 546 ARG A N   1 
ATOM   4551  C CA  . ARG A 1 546 ? 16.886  -3.857  -33.359 1.00 34.88  ? 546 ARG A CA  1 
ATOM   4552  C C   . ARG A 1 546 ? 18.295  -3.520  -33.835 1.00 34.32  ? 546 ARG A C   1 
ATOM   4553  O O   . ARG A 1 546 ? 18.801  -4.169  -34.749 1.00 33.55  ? 546 ARG A O   1 
ATOM   4554  C CB  . ARG A 1 546 ? 15.861  -3.512  -34.429 1.00 31.27  ? 546 ARG A CB  1 
ATOM   4555  C CG  . ARG A 1 546 ? 14.531  -4.181  -34.208 1.00 32.06  ? 546 ARG A CG  1 
ATOM   4556  C CD  . ARG A 1 546 ? 13.671  -4.102  -35.463 1.00 32.42  ? 546 ARG A CD  1 
ATOM   4557  N NE  . ARG A 1 546 ? 14.216  -4.898  -36.556 1.00 28.87  ? 546 ARG A NE  1 
ATOM   4558  C CZ  . ARG A 1 546 ? 13.593  -5.093  -37.713 1.00 29.81  ? 546 ARG A CZ  1 
ATOM   4559  N NH1 . ARG A 1 546 ? 12.385  -4.560  -37.930 1.00 28.35  ? 546 ARG A NH1 1 
ATOM   4560  N NH2 . ARG A 1 546 ? 14.161  -5.850  -38.643 1.00 28.45  ? 546 ARG A NH2 1 
ATOM   4561  N N   . ARG A 1 547 ? 18.908  -2.499  -33.229 1.00 33.19  ? 547 ARG A N   1 
ATOM   4562  C CA  . ARG A 1 547 ? 20.335  -2.185  -33.456 1.00 35.59  ? 547 ARG A CA  1 
ATOM   4563  C C   . ARG A 1 547 ? 21.032  -1.991  -32.125 1.00 36.62  ? 547 ARG A C   1 
ATOM   4564  O O   . ARG A 1 547 ? 21.486  -0.869  -31.807 1.00 34.64  ? 547 ARG A O   1 
ATOM   4565  C CB  . ARG A 1 547 ? 20.512  -0.902  -34.282 1.00 36.16  ? 547 ARG A CB  1 
ATOM   4566  C CG  . ARG A 1 547 ? 19.816  -0.874  -35.638 1.00 37.61  ? 547 ARG A CG  1 
ATOM   4567  C CD  . ARG A 1 547 ? 20.297  0.333   -36.457 1.00 38.52  ? 547 ARG A CD  1 
ATOM   4568  N NE  . ARG A 1 547 ? 19.287  0.817   -37.399 1.00 38.18  ? 547 ARG A NE  1 
ATOM   4569  C CZ  . ARG A 1 547 ? 19.135  0.361   -38.643 1.00 40.34  ? 547 ARG A CZ  1 
ATOM   4570  N NH1 . ARG A 1 547 ? 19.933  -0.598  -39.109 1.00 41.10  ? 547 ARG A NH1 1 
ATOM   4571  N NH2 . ARG A 1 547 ? 18.185  0.865   -39.430 1.00 38.19  ? 547 ARG A NH2 1 
ATOM   4572  N N   . THR A 1 548 ? 21.102  -3.065  -31.335 1.00 38.52  ? 548 THR A N   1 
ATOM   4573  C CA  . THR A 1 548 ? 21.593  -2.982  -29.946 1.00 43.09  ? 548 THR A CA  1 
ATOM   4574  C C   . THR A 1 548 ? 23.015  -2.429  -29.873 1.00 44.82  ? 548 THR A C   1 
ATOM   4575  O O   . THR A 1 548 ? 23.342  -1.703  -28.945 1.00 50.95  ? 548 THR A O   1 
ATOM   4576  C CB  . THR A 1 548 ? 21.528  -4.346  -29.189 1.00 44.04  ? 548 THR A CB  1 
ATOM   4577  O OG1 . THR A 1 548 ? 21.752  -5.422  -30.109 1.00 48.29  ? 548 THR A OG1 1 
ATOM   4578  C CG2 . THR A 1 548 ? 20.173  -4.558  -28.523 1.00 41.51  ? 548 THR A CG2 1 
ATOM   4579  N N   . GLU A 1 549 ? 23.848  -2.762  -30.853 1.00 45.14  ? 549 GLU A N   1 
ATOM   4580  C CA  . GLU A 1 549 ? 25.238  -2.250  -30.909 1.00 48.69  ? 549 GLU A CA  1 
ATOM   4581  C C   . GLU A 1 549 ? 25.307  -0.732  -31.122 1.00 45.19  ? 549 GLU A C   1 
ATOM   4582  O O   . GLU A 1 549 ? 26.048  -0.039  -30.447 1.00 49.65  ? 549 GLU A O   1 
ATOM   4583  C CB  . GLU A 1 549 ? 26.059  -2.986  -31.994 1.00 52.06  ? 549 GLU A CB  1 
ATOM   4584  C CG  . GLU A 1 549 ? 25.640  -2.703  -33.447 1.00 58.62  ? 549 GLU A CG  1 
ATOM   4585  C CD  . GLU A 1 549 ? 24.207  -3.148  -33.786 1.00 58.17  ? 549 GLU A CD  1 
ATOM   4586  O OE1 . GLU A 1 549 ? 23.748  -4.175  -33.242 1.00 62.66  ? 549 GLU A OE1 1 
ATOM   4587  O OE2 . GLU A 1 549 ? 23.546  -2.484  -34.617 1.00 53.80  ? 549 GLU A OE2 1 
ATOM   4588  N N   . ILE A 1 550 ? 24.530  -0.226  -32.061 1.00 41.11  ? 550 ILE A N   1 
ATOM   4589  C CA  . ILE A 1 550 ? 24.469  1.212   -32.303 1.00 39.63  ? 550 ILE A CA  1 
ATOM   4590  C C   . ILE A 1 550 ? 23.773  1.956   -31.147 1.00 39.48  ? 550 ILE A C   1 
ATOM   4591  O O   . ILE A 1 550 ? 24.249  2.976   -30.682 1.00 38.79  ? 550 ILE A O   1 
ATOM   4592  C CB  . ILE A 1 550 ? 23.786  1.507   -33.665 1.00 37.85  ? 550 ILE A CB  1 
ATOM   4593  C CG1 . ILE A 1 550 ? 24.813  1.343   -34.809 1.00 38.76  ? 550 ILE A CG1 1 
ATOM   4594  C CG2 . ILE A 1 550 ? 23.211  2.901   -33.688 1.00 37.18  ? 550 ILE A CG2 1 
ATOM   4595  C CD1 . ILE A 1 550 ? 24.264  0.753   -36.098 1.00 34.85  ? 550 ILE A CD1 1 
ATOM   4596  N N   . TYR A 1 551 ? 22.670  1.404   -30.657 1.00 38.51  ? 551 TYR A N   1 
ATOM   4597  C CA  . TYR A 1 551 ? 21.795  2.137   -29.757 1.00 36.18  ? 551 TYR A CA  1 
ATOM   4598  C C   . TYR A 1 551 ? 21.938  1.748   -28.260 1.00 36.99  ? 551 TYR A C   1 
ATOM   4599  O O   . TYR A 1 551 ? 21.202  2.254   -27.402 1.00 36.07  ? 551 TYR A O   1 
ATOM   4600  C CB  . TYR A 1 551 ? 20.362  1.949   -30.217 1.00 33.41  ? 551 TYR A CB  1 
ATOM   4601  C CG  . TYR A 1 551 ? 19.992  2.664   -31.502 1.00 30.82  ? 551 TYR A CG  1 
ATOM   4602  C CD1 . TYR A 1 551 ? 20.291  4.021   -31.695 1.00 30.86  ? 551 TYR A CD1 1 
ATOM   4603  C CD2 . TYR A 1 551 ? 19.253  2.019   -32.470 1.00 28.79  ? 551 TYR A CD2 1 
ATOM   4604  C CE1 . TYR A 1 551 ? 19.912  4.679   -32.859 1.00 29.21  ? 551 TYR A CE1 1 
ATOM   4605  C CE2 . TYR A 1 551 ? 18.861  2.664   -33.611 1.00 29.21  ? 551 TYR A CE2 1 
ATOM   4606  C CZ  . TYR A 1 551 ? 19.188  3.996   -33.802 1.00 30.16  ? 551 TYR A CZ  1 
ATOM   4607  O OH  . TYR A 1 551 ? 18.759  4.624   -34.951 1.00 31.29  ? 551 TYR A OH  1 
ATOM   4608  N N   . LYS A 1 552 ? 22.885  0.855   -27.981 1.00 37.82  ? 552 LYS A N   1 
ATOM   4609  C CA  . LYS A 1 552 ? 23.264  0.436   -26.633 1.00 41.02  ? 552 LYS A CA  1 
ATOM   4610  C C   . LYS A 1 552 ? 23.154  1.525   -25.568 1.00 37.78  ? 552 LYS A C   1 
ATOM   4611  O O   . LYS A 1 552 ? 22.405  1.383   -24.592 1.00 37.54  ? 552 LYS A O   1 
ATOM   4612  C CB  . LYS A 1 552 ? 24.706  -0.095  -26.658 1.00 46.40  ? 552 LYS A CB  1 
ATOM   4613  C CG  . LYS A 1 552 ? 25.230  -0.591  -25.315 1.00 53.36  ? 552 LYS A CG  1 
ATOM   4614  C CD  . LYS A 1 552 ? 25.221  -2.109  -25.229 1.00 57.65  ? 552 LYS A CD  1 
ATOM   4615  C CE  . LYS A 1 552 ? 25.826  -2.588  -23.913 1.00 63.10  ? 552 LYS A CE  1 
ATOM   4616  N NZ  . LYS A 1 552 ? 24.992  -2.201  -22.734 1.00 62.62  ? 552 LYS A NZ  1 
ATOM   4617  N N   . GLY A 1 553 ? 23.921  2.593   -25.744 1.00 35.52  ? 553 GLY A N   1 
ATOM   4618  C CA  . GLY A 1 553 ? 23.978  3.673   -24.764 1.00 34.65  ? 553 GLY A CA  1 
ATOM   4619  C C   . GLY A 1 553 ? 22.632  4.359   -24.600 1.00 34.16  ? 553 GLY A C   1 
ATOM   4620  O O   . GLY A 1 553 ? 22.271  4.772   -23.502 1.00 35.20  ? 553 GLY A O   1 
ATOM   4621  N N   . LEU A 1 554 ? 21.895  4.480   -25.703 1.00 32.39  ? 554 LEU A N   1 
ATOM   4622  C CA  . LEU A 1 554 ? 20.624  5.187   -25.708 1.00 31.40  ? 554 LEU A CA  1 
ATOM   4623  C C   . LEU A 1 554 ? 19.558  4.380   -24.952 1.00 31.96  ? 554 LEU A C   1 
ATOM   4624  O O   . LEU A 1 554 ? 18.895  4.899   -24.069 1.00 30.96  ? 554 LEU A O   1 
ATOM   4625  C CB  . LEU A 1 554 ? 20.196  5.460   -27.140 1.00 29.77  ? 554 LEU A CB  1 
ATOM   4626  C CG  . LEU A 1 554 ? 18.943  6.291   -27.415 1.00 30.38  ? 554 LEU A CG  1 
ATOM   4627  C CD1 . LEU A 1 554 ? 18.954  7.588   -26.608 1.00 29.92  ? 554 LEU A CD1 1 
ATOM   4628  C CD2 . LEU A 1 554 ? 18.851  6.581   -28.915 1.00 28.46  ? 554 LEU A CD2 1 
ATOM   4629  N N   . ILE A 1 555 ? 19.447  3.095   -25.293 1.00 33.19  ? 555 ILE A N   1 
ATOM   4630  C CA  . ILE A 1 555 ? 18.622  2.139   -24.570 1.00 34.35  ? 555 ILE A CA  1 
ATOM   4631  C C   . ILE A 1 555 ? 18.900  2.146   -23.067 1.00 35.77  ? 555 ILE A C   1 
ATOM   4632  O O   . ILE A 1 555 ? 17.967  2.193   -22.271 1.00 39.71  ? 555 ILE A O   1 
ATOM   4633  C CB  . ILE A 1 555 ? 18.813  0.705   -25.122 1.00 33.96  ? 555 ILE A CB  1 
ATOM   4634  C CG1 . ILE A 1 555 ? 18.422  0.642   -26.602 1.00 32.00  ? 555 ILE A CG1 1 
ATOM   4635  C CG2 . ILE A 1 555 ? 18.016  -0.303  -24.306 1.00 31.56  ? 555 ILE A CG2 1 
ATOM   4636  C CD1 . ILE A 1 555 ? 18.917  -0.612  -27.301 1.00 32.11  ? 555 ILE A CD1 1 
ATOM   4637  N N   . ASP A 1 556 ? 20.175  2.105   -22.680 1.00 37.03  ? 556 ASP A N   1 
ATOM   4638  C CA  . ASP A 1 556 ? 20.548  2.149   -21.266 1.00 36.95  ? 556 ASP A CA  1 
ATOM   4639  C C   . ASP A 1 556 ? 20.129  3.444   -20.613 1.00 36.85  ? 556 ASP A C   1 
ATOM   4640  O O   . ASP A 1 556 ? 19.617  3.434   -19.491 1.00 38.91  ? 556 ASP A O   1 
ATOM   4641  C CB  . ASP A 1 556 ? 22.050  1.929   -21.081 1.00 40.43  ? 556 ASP A CB  1 
ATOM   4642  C CG  . ASP A 1 556 ? 22.470  0.504   -21.407 1.00 46.16  ? 556 ASP A CG  1 
ATOM   4643  O OD1 . ASP A 1 556 ? 21.591  -0.400  -21.396 1.00 48.05  ? 556 ASP A OD1 1 
ATOM   4644  O OD2 . ASP A 1 556 ? 23.670  0.284   -21.697 1.00 49.27  ? 556 ASP A OD2 1 
ATOM   4645  N N   . ARG A 1 557 ? 20.352  4.568   -21.292 1.00 34.11  ? 557 ARG A N   1 
ATOM   4646  C CA  . ARG A 1 557 ? 19.859  5.841   -20.772 1.00 34.99  ? 557 ARG A CA  1 
ATOM   4647  C C   . ARG A 1 557 ? 18.335  5.798   -20.558 1.00 33.51  ? 557 ARG A C   1 
ATOM   4648  O O   . ARG A 1 557 ? 17.841  6.296   -19.564 1.00 34.70  ? 557 ARG A O   1 
ATOM   4649  C CB  . ARG A 1 557 ? 20.257  7.029   -21.680 1.00 34.99  ? 557 ARG A CB  1 
ATOM   4650  C CG  . ARG A 1 557 ? 19.835  8.392   -21.142 1.00 36.64  ? 557 ARG A CG  1 
ATOM   4651  C CD  . ARG A 1 557 ? 20.441  9.563   -21.929 1.00 38.33  ? 557 ARG A CD  1 
ATOM   4652  N NE  . ARG A 1 557 ? 21.886  9.670   -21.735 1.00 41.41  ? 557 ARG A NE  1 
ATOM   4653  C CZ  . ARG A 1 557 ? 22.650  10.694  -22.134 1.00 43.90  ? 557 ARG A CZ  1 
ATOM   4654  N NH1 . ARG A 1 557 ? 22.126  11.750  -22.762 1.00 41.11  ? 557 ARG A NH1 1 
ATOM   4655  N NH2 . ARG A 1 557 ? 23.958  10.655  -21.901 1.00 43.36  ? 557 ARG A NH2 1 
ATOM   4656  N N   . ILE A 1 558 ? 17.597  5.183   -21.472 1.00 31.05  ? 558 ILE A N   1 
ATOM   4657  C CA  . ILE A 1 558 ? 16.157  5.199   -21.340 1.00 30.46  ? 558 ILE A CA  1 
ATOM   4658  C C   . ILE A 1 558 ? 15.743  4.392   -20.112 1.00 31.55  ? 558 ILE A C   1 
ATOM   4659  O O   . ILE A 1 558 ? 14.927  4.833   -19.312 1.00 29.91  ? 558 ILE A O   1 
ATOM   4660  C CB  . ILE A 1 558 ? 15.443  4.714   -22.620 1.00 28.70  ? 558 ILE A CB  1 
ATOM   4661  C CG1 . ILE A 1 558 ? 15.778  5.640   -23.797 1.00 27.00  ? 558 ILE A CG1 1 
ATOM   4662  C CG2 . ILE A 1 558 ? 13.933  4.654   -22.397 1.00 28.21  ? 558 ILE A CG2 1 
ATOM   4663  C CD1 . ILE A 1 558 ? 15.297  5.139   -25.149 1.00 25.41  ? 558 ILE A CD1 1 
ATOM   4664  N N   . LYS A 1 559 ? 16.361  3.230   -19.948 1.00 33.47  ? 559 LYS A N   1 
ATOM   4665  C CA  . LYS A 1 559 ? 16.037  2.346   -18.835 1.00 34.57  ? 559 LYS A CA  1 
ATOM   4666  C C   . LYS A 1 559 ? 16.459  2.923   -17.492 1.00 34.31  ? 559 LYS A C   1 
ATOM   4667  O O   . LYS A 1 559 ? 15.797  2.679   -16.481 1.00 32.55  ? 559 LYS A O   1 
ATOM   4668  C CB  . LYS A 1 559 ? 16.673  0.976   -19.030 1.00 35.88  ? 559 LYS A CB  1 
ATOM   4669  C CG  . LYS A 1 559 ? 16.116  0.223   -20.213 1.00 36.14  ? 559 LYS A CG  1 
ATOM   4670  C CD  . LYS A 1 559 ? 16.581  -1.213  -20.226 1.00 38.54  ? 559 LYS A CD  1 
ATOM   4671  C CE  . LYS A 1 559 ? 15.777  -1.993  -21.260 1.00 41.04  ? 559 LYS A CE  1 
ATOM   4672  N NZ  . LYS A 1 559 ? 16.338  -3.350  -21.466 1.00 45.82  ? 559 LYS A NZ  1 
ATOM   4673  N N   . SER A 1 560 ? 17.541  3.696   -17.467 1.00 33.60  ? 560 SER A N   1 
ATOM   4674  C CA  . SER A 1 560 ? 17.965  4.262   -16.186 1.00 35.65  ? 560 SER A CA  1 
ATOM   4675  C C   . SER A 1 560 ? 17.300  5.573   -15.836 1.00 35.00  ? 560 SER A C   1 
ATOM   4676  O O   . SER A 1 560 ? 17.175  5.898   -14.648 1.00 35.77  ? 560 SER A O   1 
ATOM   4677  C CB  . SER A 1 560 ? 19.494  4.354   -16.040 1.00 36.21  ? 560 SER A CB  1 
ATOM   4678  O OG  . SER A 1 560 ? 20.085  5.003   -17.129 1.00 39.38  ? 560 SER A OG  1 
ATOM   4679  N N   . ARG A 1 561 ? 16.857  6.317   -16.852 1.00 33.50  ? 561 ARG A N   1 
ATOM   4680  C CA  . ARG A 1 561 ? 16.395  7.694   -16.646 1.00 34.11  ? 561 ARG A CA  1 
ATOM   4681  C C   . ARG A 1 561 ? 14.891  7.846   -16.747 1.00 33.58  ? 561 ARG A C   1 
ATOM   4682  O O   . ARG A 1 561 ? 14.329  8.755   -16.144 1.00 32.55  ? 561 ARG A O   1 
ATOM   4683  C CB  . ARG A 1 561 ? 17.070  8.663   -17.623 1.00 35.75  ? 561 ARG A CB  1 
ATOM   4684  C CG  . ARG A 1 561 ? 18.494  9.069   -17.251 1.00 37.80  ? 561 ARG A CG  1 
ATOM   4685  C CD  . ARG A 1 561 ? 18.965  10.262  -18.084 1.00 38.52  ? 561 ARG A CD  1 
ATOM   4686  N NE  . ARG A 1 561 ? 20.427  10.405  -18.066 1.00 41.81  ? 561 ARG A NE  1 
ATOM   4687  C CZ  . ARG A 1 561 ? 21.107  11.413  -18.627 1.00 43.37  ? 561 ARG A CZ  1 
ATOM   4688  N NH1 . ARG A 1 561 ? 20.474  12.408  -19.272 1.00 41.74  ? 561 ARG A NH1 1 
ATOM   4689  N NH2 . ARG A 1 561 ? 22.428  11.429  -18.538 1.00 42.14  ? 561 ARG A NH2 1 
ATOM   4690  N N   . GLU A 1 562 ? 14.242  6.984   -17.528 1.00 32.45  ? 562 GLU A N   1 
ATOM   4691  C CA  . GLU A 1 562 ? 12.796  7.083   -17.722 1.00 32.31  ? 562 GLU A CA  1 
ATOM   4692  C C   . GLU A 1 562 ? 12.045  5.986   -17.012 1.00 32.93  ? 562 GLU A C   1 
ATOM   4693  O O   . GLU A 1 562 ? 12.554  4.898   -16.791 1.00 31.90  ? 562 GLU A O   1 
ATOM   4694  C CB  . GLU A 1 562 ? 12.396  7.051   -19.212 1.00 32.09  ? 562 GLU A CB  1 
ATOM   4695  C CG  . GLU A 1 562 ? 13.084  8.084   -20.102 1.00 33.27  ? 562 GLU A CG  1 
ATOM   4696  C CD  . GLU A 1 562 ? 13.064  9.475   -19.507 1.00 31.53  ? 562 GLU A CD  1 
ATOM   4697  O OE1 . GLU A 1 562 ? 11.983  9.945   -19.079 1.00 31.77  ? 562 GLU A OE1 1 
ATOM   4698  O OE2 . GLU A 1 562 ? 14.132  10.081  -19.462 1.00 31.73  ? 562 GLU A OE2 1 
ATOM   4699  N N   . LYS A 1 563 ? 10.801  6.308   -16.696 1.00 33.62  ? 563 LYS A N   1 
ATOM   4700  C CA  . LYS A 1 563 ? 9.849   5.408   -16.128 1.00 33.96  ? 563 LYS A CA  1 
ATOM   4701  C C   . LYS A 1 563 ? 9.216   4.575   -17.251 1.00 33.70  ? 563 LYS A C   1 
ATOM   4702  O O   . LYS A 1 563 ? 8.557   5.122   -18.133 1.00 34.02  ? 563 LYS A O   1 
ATOM   4703  C CB  . LYS A 1 563 ? 8.794   6.267   -15.402 1.00 34.23  ? 563 LYS A CB  1 
ATOM   4704  C CG  . LYS A 1 563 ? 7.553   5.543   -14.926 1.00 35.57  ? 563 LYS A CG  1 
ATOM   4705  C CD  . LYS A 1 563 ? 7.873   4.569   -13.810 1.00 35.47  ? 563 LYS A CD  1 
ATOM   4706  C CE  . LYS A 1 563 ? 7.477   5.150   -12.463 1.00 37.65  ? 563 LYS A CE  1 
ATOM   4707  N NZ  . LYS A 1 563 ? 7.515   4.121   -11.376 1.00 35.76  ? 563 LYS A NZ  1 
ATOM   4708  N N   . LEU A 1 564 ? 9.402   3.256   -17.202 1.00 35.96  ? 564 LEU A N   1 
ATOM   4709  C CA  . LEU A 1 564 ? 8.885   2.329   -18.247 1.00 36.60  ? 564 LEU A CA  1 
ATOM   4710  C C   . LEU A 1 564 ? 7.716   1.435   -17.780 1.00 36.85  ? 564 LEU A C   1 
ATOM   4711  O O   . LEU A 1 564 ? 7.065   0.757   -18.593 1.00 36.74  ? 564 LEU A O   1 
ATOM   4712  C CB  . LEU A 1 564 ? 10.018  1.445   -18.783 1.00 38.08  ? 564 LEU A CB  1 
ATOM   4713  C CG  . LEU A 1 564 ? 11.235  2.139   -19.416 1.00 39.43  ? 564 LEU A CG  1 
ATOM   4714  C CD1 . LEU A 1 564 ? 12.335  1.121   -19.641 1.00 39.53  ? 564 LEU A CD1 1 
ATOM   4715  C CD2 . LEU A 1 564 ? 10.857  2.813   -20.728 1.00 38.03  ? 564 LEU A CD2 1 
ATOM   4716  N N   . THR A 1 565 ? 7.466   1.422   -16.476 1.00 37.30  ? 565 THR A N   1 
ATOM   4717  C CA  . THR A 1 565 ? 6.371   0.640   -15.901 1.00 37.08  ? 565 THR A CA  1 
ATOM   4718  C C   . THR A 1 565 ? 5.129   1.529   -15.805 1.00 38.08  ? 565 THR A C   1 
ATOM   4719  O O   . THR A 1 565 ? 5.240   2.718   -15.533 1.00 39.47  ? 565 THR A O   1 
ATOM   4720  C CB  . THR A 1 565 ? 6.743   0.102   -14.509 1.00 36.00  ? 565 THR A CB  1 
ATOM   4721  O OG1 . THR A 1 565 ? 7.136   1.190   -13.666 1.00 34.08  ? 565 THR A OG1 1 
ATOM   4722  C CG2 . THR A 1 565 ? 7.900   -0.903  -14.608 1.00 35.83  ? 565 THR A CG2 1 
ATOM   4723  N N   . MET A 1 566 ? 3.959   0.967   -16.077 1.00 38.52  ? 566 MET A N   1 
ATOM   4724  C CA  . MET A 1 566 ? 2.715   1.718   -15.951 1.00 39.54  ? 566 MET A CA  1 
ATOM   4725  C C   . MET A 1 566 ? 1.644   0.895   -15.265 1.00 40.37  ? 566 MET A C   1 
ATOM   4726  O O   . MET A 1 566 ? 1.682   -0.323  -15.287 1.00 41.02  ? 566 MET A O   1 
ATOM   4727  C CB  . MET A 1 566 ? 2.207   2.204   -17.316 1.00 40.55  ? 566 MET A CB  1 
ATOM   4728  C CG  . MET A 1 566 ? 1.981   1.117   -18.350 1.00 43.09  ? 566 MET A CG  1 
ATOM   4729  S SD  . MET A 1 566 ? 3.483   0.737   -19.276 1.00 51.11  ? 566 MET A SD  1 
ATOM   4730  C CE  . MET A 1 566 ? 2.831   -0.010  -20.761 1.00 39.78  ? 566 MET A CE  1 
ATOM   4731  N N   . LYS A 1 567 ? 0.696   1.584   -14.646 1.00 40.35  ? 567 LYS A N   1 
ATOM   4732  C CA  . LYS A 1 567 ? -0.452  0.954   -14.032 1.00 40.47  ? 567 LYS A CA  1 
ATOM   4733  C C   . LYS A 1 567 ? -1.588  0.819   -15.065 1.00 39.00  ? 567 LYS A C   1 
ATOM   4734  O O   . LYS A 1 567 ? -1.919  1.783   -15.763 1.00 36.11  ? 567 LYS A O   1 
ATOM   4735  C CB  . LYS A 1 567 ? -0.907  1.803   -12.841 1.00 40.23  ? 567 LYS A CB  1 
ATOM   4736  C CG  . LYS A 1 567 ? -2.025  1.194   -12.017 1.00 40.45  ? 567 LYS A CG  1 
ATOM   4737  C CD  . LYS A 1 567 ? -2.470  2.167   -10.939 1.00 40.74  ? 567 LYS A CD  1 
ATOM   4738  C CE  . LYS A 1 567 ? -3.454  1.519   -9.961  1.00 43.37  ? 567 LYS A CE  1 
ATOM   4739  N NZ  . LYS A 1 567 ? -3.367  2.182   -8.618  1.00 43.97  ? 567 LYS A NZ  1 
ATOM   4740  N N   . PHE A 1 568 ? -2.171  -0.376  -15.154 1.00 37.56  ? 568 PHE A N   1 
ATOM   4741  C CA  . PHE A 1 568 ? -3.305  -0.628  -16.057 1.00 37.34  ? 568 PHE A CA  1 
ATOM   4742  C C   . PHE A 1 568 ? -4.614  -0.693  -15.281 1.00 37.91  ? 568 PHE A C   1 
ATOM   4743  O O   . PHE A 1 568 ? -4.628  -1.069  -14.113 1.00 41.84  ? 568 PHE A O   1 
ATOM   4744  C CB  . PHE A 1 568 ? -3.116  -1.939  -16.829 1.00 37.11  ? 568 PHE A CB  1 
ATOM   4745  C CG  . PHE A 1 568 ? -2.026  -1.895  -17.863 1.00 38.56  ? 568 PHE A CG  1 
ATOM   4746  C CD1 . PHE A 1 568 ? -2.160  -1.109  -19.016 1.00 37.94  ? 568 PHE A CD1 1 
ATOM   4747  C CD2 . PHE A 1 568 ? -0.875  -2.672  -17.715 1.00 38.78  ? 568 PHE A CD2 1 
ATOM   4748  C CE1 . PHE A 1 568 ? -1.153  -1.085  -19.980 1.00 38.34  ? 568 PHE A CE1 1 
ATOM   4749  C CE2 . PHE A 1 568 ? 0.132   -2.653  -18.686 1.00 39.18  ? 568 PHE A CE2 1 
ATOM   4750  C CZ  . PHE A 1 568 ? -0.005  -1.856  -19.809 1.00 37.40  ? 568 PHE A CZ  1 
ATOM   4751  N N   . HIS A 1 569 ? -5.718  -0.353  -15.930 1.00 37.96  ? 569 HIS A N   1 
ATOM   4752  C CA  . HIS A 1 569 ? -7.009  -0.288  -15.242 1.00 37.38  ? 569 HIS A CA  1 
ATOM   4753  C C   . HIS A 1 569 ? -8.036  -1.223  -15.781 1.00 37.85  ? 569 HIS A C   1 
ATOM   4754  O O   . HIS A 1 569 ? -9.192  -1.209  -15.355 1.00 38.30  ? 569 HIS A O   1 
ATOM   4755  C CB  . HIS A 1 569 ? -7.530  1.131   -15.247 1.00 36.38  ? 569 HIS A CB  1 
ATOM   4756  C CG  . HIS A 1 569 ? -6.716  2.058   -14.416 1.00 37.01  ? 569 HIS A CG  1 
ATOM   4757  N ND1 . HIS A 1 569 ? -5.760  2.839   -14.937 1.00 37.63  ? 569 HIS A ND1 1 
ATOM   4758  C CD2 . HIS A 1 569 ? -6.717  2.296   -13.051 1.00 38.02  ? 569 HIS A CD2 1 
ATOM   4759  C CE1 . HIS A 1 569 ? -5.184  3.559   -13.961 1.00 36.80  ? 569 HIS A CE1 1 
ATOM   4760  N NE2 . HIS A 1 569 ? -5.770  3.228   -12.807 1.00 39.22  ? 569 HIS A NE2 1 
ATOM   4761  N N   . ASP A 1 570 ? -7.627  -2.066  -16.712 1.00 38.56  ? 570 ASP A N   1 
ATOM   4762  C CA  . ASP A 1 570 ? -8.512  -3.090  -17.233 1.00 41.94  ? 570 ASP A CA  1 
ATOM   4763  C C   . ASP A 1 570 ? -7.817  -4.446  -17.113 1.00 41.55  ? 570 ASP A C   1 
ATOM   4764  O O   . ASP A 1 570 ? -6.706  -4.625  -17.595 1.00 42.72  ? 570 ASP A O   1 
ATOM   4765  C CB  . ASP A 1 570 ? -8.885  -2.765  -18.690 1.00 42.21  ? 570 ASP A CB  1 
ATOM   4766  C CG  . ASP A 1 570 ? -9.820  -3.798  -19.309 1.00 45.17  ? 570 ASP A CG  1 
ATOM   4767  O OD1 . ASP A 1 570 ? -9.884  -4.937  -18.807 1.00 44.44  ? 570 ASP A OD1 1 
ATOM   4768  O OD2 . ASP A 1 570 ? -10.483 -3.471  -20.324 1.00 47.86  ? 570 ASP A OD2 1 
ATOM   4769  N N   . GLY A 1 571 ? -8.462  -5.392  -16.446 1.00 42.44  ? 571 GLY A N   1 
ATOM   4770  C CA  . GLY A 1 571 ? -7.871  -6.728  -16.252 1.00 44.18  ? 571 GLY A CA  1 
ATOM   4771  C C   . GLY A 1 571 ? -7.838  -7.570  -17.522 1.00 42.98  ? 571 GLY A C   1 
ATOM   4772  O O   . GLY A 1 571 ? -7.303  -8.676  -17.537 1.00 44.26  ? 571 GLY A O   1 
ATOM   4773  N N   . GLU A 1 572 ? -8.406  -7.030  -18.589 1.00 44.68  ? 572 GLU A N   1 
ATOM   4774  C CA  . GLU A 1 572 ? -8.538  -7.730  -19.859 1.00 44.98  ? 572 GLU A CA  1 
ATOM   4775  C C   . GLU A 1 572 ? -7.392  -7.328  -20.776 1.00 42.56  ? 572 GLU A C   1 
ATOM   4776  O O   . GLU A 1 572 ? -7.211  -7.899  -21.864 1.00 41.08  ? 572 GLU A O   1 
ATOM   4777  C CB  . GLU A 1 572 ? -9.858  -7.332  -20.503 1.00 49.04  ? 572 GLU A CB  1 
ATOM   4778  C CG  . GLU A 1 572 ? -10.543 -8.435  -21.276 1.00 55.51  ? 572 GLU A CG  1 
ATOM   4779  C CD  . GLU A 1 572 ? -11.526 -9.198  -20.433 1.00 57.45  ? 572 GLU A CD  1 
ATOM   4780  O OE1 . GLU A 1 572 ? -11.764 -8.777  -19.290 1.00 58.35  ? 572 GLU A OE1 1 
ATOM   4781  O OE2 . GLU A 1 572 ? -12.059 -10.222 -20.918 1.00 65.96  ? 572 GLU A OE2 1 
ATOM   4782  N N   . VAL A 1 573 ? -6.634  -6.325  -20.342 1.00 40.05  ? 573 VAL A N   1 
ATOM   4783  C CA  . VAL A 1 573 ? -5.489  -5.835  -21.093 1.00 38.95  ? 573 VAL A CA  1 
ATOM   4784  C C   . VAL A 1 573 ? -4.548  -6.982  -21.396 1.00 39.16  ? 573 VAL A C   1 
ATOM   4785  O O   . VAL A 1 573 ? -4.361  -7.893  -20.561 1.00 37.34  ? 573 VAL A O   1 
ATOM   4786  C CB  . VAL A 1 573 ? -4.733  -4.727  -20.308 1.00 38.66  ? 573 VAL A CB  1 
ATOM   4787  C CG1 . VAL A 1 573 ? -3.874  -5.314  -19.191 1.00 36.74  ? 573 VAL A CG1 1 
ATOM   4788  C CG2 . VAL A 1 573 ? -3.909  -3.849  -21.251 1.00 37.65  ? 573 VAL A CG2 1 
ATOM   4789  N N   . ASP A 1 574 ? -3.982  -6.961  -22.599 1.00 39.75  ? 574 ASP A N   1 
ATOM   4790  C CA  . ASP A 1 574 ? -2.831  -7.803  -22.896 1.00 39.75  ? 574 ASP A CA  1 
ATOM   4791  C C   . ASP A 1 574 ? -1.593  -7.005  -22.594 1.00 37.26  ? 574 ASP A C   1 
ATOM   4792  O O   . ASP A 1 574 ? -1.194  -6.140  -23.374 1.00 35.26  ? 574 ASP A O   1 
ATOM   4793  C CB  . ASP A 1 574 ? -2.808  -8.259  -24.347 1.00 40.91  ? 574 ASP A CB  1 
ATOM   4794  C CG  . ASP A 1 574 ? -1.662  -9.220  -24.628 1.00 43.44  ? 574 ASP A CG  1 
ATOM   4795  O OD1 . ASP A 1 574 ? -0.784  -9.367  -23.758 1.00 43.31  ? 574 ASP A OD1 1 
ATOM   4796  O OD2 . ASP A 1 574 ? -1.647  -9.844  -25.706 1.00 48.29  ? 574 ASP A OD2 1 
ATOM   4797  N N   . ALA A 1 575 ? -1.003  -7.276  -21.437 1.00 37.40  ? 575 ALA A N   1 
ATOM   4798  C CA  . ALA A 1 575 ? 0.150   -6.499  -20.966 1.00 36.17  ? 575 ALA A CA  1 
ATOM   4799  C C   . ALA A 1 575 ? 1.383   -6.842  -21.795 1.00 34.03  ? 575 ALA A C   1 
ATOM   4800  O O   . ALA A 1 575 ? 2.306   -6.036  -21.898 1.00 31.51  ? 575 ALA A O   1 
ATOM   4801  C CB  . ALA A 1 575 ? 0.405   -6.767  -19.494 1.00 34.69  ? 575 ALA A CB  1 
ATOM   4802  N N   . SER A 1 576 ? 1.378   -8.036  -22.393 1.00 32.16  ? 576 SER A N   1 
ATOM   4803  C CA  . SER A 1 576 ? 2.509   -8.493  -23.167 1.00 32.96  ? 576 SER A CA  1 
ATOM   4804  C C   . SER A 1 576 ? 2.684   -7.662  -24.425 1.00 33.08  ? 576 SER A C   1 
ATOM   4805  O O   . SER A 1 576 ? 3.805   -7.477  -24.914 1.00 34.59  ? 576 SER A O   1 
ATOM   4806  C CB  . SER A 1 576 ? 2.410   -9.984  -23.500 1.00 33.97  ? 576 SER A CB  1 
ATOM   4807  O OG  . SER A 1 576 ? 1.268   -10.275 -24.305 1.00 35.54  ? 576 SER A OG  1 
ATOM   4808  N N   . TYR A 1 577 ? 1.594   -7.121  -24.937 1.00 32.78  ? 577 TYR A N   1 
ATOM   4809  C CA  . TYR A 1 577 ? 1.685   -6.338  -26.160 1.00 32.63  ? 577 TYR A CA  1 
ATOM   4810  C C   . TYR A 1 577 ? 2.767   -5.262  -26.046 1.00 32.19  ? 577 TYR A C   1 
ATOM   4811  O O   . TYR A 1 577 ? 3.460   -4.974  -27.014 1.00 32.53  ? 577 TYR A O   1 
ATOM   4812  C CB  . TYR A 1 577 ? 0.334   -5.725  -26.523 1.00 31.97  ? 577 TYR A CB  1 
ATOM   4813  C CG  . TYR A 1 577 ? 0.259   -5.251  -27.944 1.00 32.63  ? 577 TYR A CG  1 
ATOM   4814  C CD1 . TYR A 1 577 ? 0.262   -6.164  -29.007 1.00 32.81  ? 577 TYR A CD1 1 
ATOM   4815  C CD2 . TYR A 1 577 ? 0.189   -3.884  -28.244 1.00 32.05  ? 577 TYR A CD2 1 
ATOM   4816  C CE1 . TYR A 1 577 ? 0.184   -5.728  -30.320 1.00 33.06  ? 577 TYR A CE1 1 
ATOM   4817  C CE2 . TYR A 1 577 ? 0.104   -3.446  -29.554 1.00 31.13  ? 577 TYR A CE2 1 
ATOM   4818  C CZ  . TYR A 1 577 ? 0.110   -4.369  -30.586 1.00 32.33  ? 577 TYR A CZ  1 
ATOM   4819  O OH  . TYR A 1 577 ? 0.038   -3.939  -31.898 1.00 33.90  ? 577 TYR A OH  1 
ATOM   4820  N N   . PHE A 1 578 ? 2.957   -4.726  -24.846 1.00 31.23  ? 578 PHE A N   1 
ATOM   4821  C CA  . PHE A 1 578 ? 3.816   -3.556  -24.666 1.00 32.79  ? 578 PHE A CA  1 
ATOM   4822  C C   . PHE A 1 578 ? 5.299   -3.877  -24.420 1.00 34.47  ? 578 PHE A C   1 
ATOM   4823  O O   . PHE A 1 578 ? 6.136   -2.965  -24.266 1.00 34.39  ? 578 PHE A O   1 
ATOM   4824  C CB  . PHE A 1 578 ? 3.215   -2.631  -23.592 1.00 32.65  ? 578 PHE A CB  1 
ATOM   4825  C CG  . PHE A 1 578 ? 1.781   -2.248  -23.878 1.00 32.13  ? 578 PHE A CG  1 
ATOM   4826  C CD1 . PHE A 1 578 ? 1.480   -1.216  -24.788 1.00 32.40  ? 578 PHE A CD1 1 
ATOM   4827  C CD2 . PHE A 1 578 ? 0.734   -2.975  -23.331 1.00 30.72  ? 578 PHE A CD2 1 
ATOM   4828  C CE1 . PHE A 1 578 ? 0.151   -0.895  -25.094 1.00 32.57  ? 578 PHE A CE1 1 
ATOM   4829  C CE2 . PHE A 1 578 ? -0.591  -2.672  -23.652 1.00 31.51  ? 578 PHE A CE2 1 
ATOM   4830  C CZ  . PHE A 1 578 ? -0.883  -1.622  -24.522 1.00 30.85  ? 578 PHE A CZ  1 
ATOM   4831  N N   . CYS A 1 579 ? 5.613   -5.171  -24.460 1.00 37.24  ? 579 CYS A N   1 
ATOM   4832  C CA  . CYS A 1 579 ? 6.933   -5.720  -24.128 1.00 40.88  ? 579 CYS A CA  1 
ATOM   4833  C C   . CYS A 1 579 ? 7.821   -5.796  -25.352 1.00 41.30  ? 579 CYS A C   1 
ATOM   4834  O O   . CYS A 1 579 ? 9.045   -5.832  -25.238 1.00 41.84  ? 579 CYS A O   1 
ATOM   4835  C CB  . CYS A 1 579 ? 6.782   -7.165  -23.637 1.00 44.81  ? 579 CYS A CB  1 
ATOM   4836  S SG  . CYS A 1 579 ? 6.291   -7.388  -21.932 1.00 53.93  ? 579 CYS A SG  1 
ATOM   4837  N N   . LYS A 1 580 ? 7.195   -5.897  -26.517 1.00 38.90  ? 580 LYS A N   1 
ATOM   4838  C CA  . LYS A 1 580 ? 7.882   -6.350  -27.711 1.00 38.86  ? 580 LYS A CA  1 
ATOM   4839  C C   . LYS A 1 580 ? 7.352   -5.655  -28.956 1.00 36.27  ? 580 LYS A C   1 
ATOM   4840  O O   . LYS A 1 580 ? 6.259   -5.093  -28.951 1.00 34.47  ? 580 LYS A O   1 
ATOM   4841  C CB  . LYS A 1 580 ? 7.690   -7.869  -27.861 1.00 40.50  ? 580 LYS A CB  1 
ATOM   4842  C CG  . LYS A 1 580 ? 6.217   -8.293  -27.890 1.00 41.55  ? 580 LYS A CG  1 
ATOM   4843  C CD  . LYS A 1 580 ? 6.019   -9.793  -27.673 1.00 43.51  ? 580 LYS A CD  1 
ATOM   4844  C CE  . LYS A 1 580 ? 4.536   -10.152 -27.484 1.00 44.63  ? 580 LYS A CE  1 
ATOM   4845  N NZ  . LYS A 1 580 ? 3.686   -9.878  -28.686 1.00 44.95  ? 580 LYS A NZ  1 
ATOM   4846  N N   . LEU A 1 581 ? 8.136   -5.700  -30.019 1.00 34.35  ? 581 LEU A N   1 
ATOM   4847  C CA  . LEU A 1 581 ? 7.629   -5.414  -31.336 1.00 36.64  ? 581 LEU A CA  1 
ATOM   4848  C C   . LEU A 1 581 ? 6.433   -6.309  -31.586 1.00 36.80  ? 581 LEU A C   1 
ATOM   4849  O O   . LEU A 1 581 ? 6.545   -7.513  -31.437 1.00 39.71  ? 581 LEU A O   1 
ATOM   4850  C CB  . LEU A 1 581 ? 8.714   -5.713  -32.385 1.00 36.89  ? 581 LEU A CB  1 
ATOM   4851  C CG  . LEU A 1 581 ? 9.362   -4.578  -33.180 1.00 39.02  ? 581 LEU A CG  1 
ATOM   4852  C CD1 . LEU A 1 581 ? 9.100   -3.193  -32.603 1.00 38.34  ? 581 LEU A CD1 1 
ATOM   4853  C CD2 . LEU A 1 581 ? 10.856  -4.810  -33.377 1.00 39.84  ? 581 LEU A CD2 1 
ATOM   4854  N N   . PRO A 1 582 ? 5.284   -5.726  -31.972 1.00 36.42  ? 582 PRO A N   1 
ATOM   4855  C CA  . PRO A 1 582 ? 4.193   -6.531  -32.505 1.00 36.94  ? 582 PRO A CA  1 
ATOM   4856  C C   . PRO A 1 582 ? 4.629   -7.185  -33.804 1.00 39.01  ? 582 PRO A C   1 
ATOM   4857  O O   . PRO A 1 582 ? 5.369   -6.576  -34.592 1.00 38.62  ? 582 PRO A O   1 
ATOM   4858  C CB  . PRO A 1 582 ? 3.102   -5.495  -32.804 1.00 35.95  ? 582 PRO A CB  1 
ATOM   4859  C CG  . PRO A 1 582 ? 3.491   -4.281  -32.037 1.00 35.29  ? 582 PRO A CG  1 
ATOM   4860  C CD  . PRO A 1 582 ? 4.977   -4.294  -32.030 1.00 35.45  ? 582 PRO A CD  1 
ATOM   4861  N N   . GLU A 1 583 ? 4.156   -8.396  -34.051 1.00 42.10  ? 583 GLU A N   1 
ATOM   4862  C CA  . GLU A 1 583 ? 4.614   -9.149  -35.216 1.00 45.68  ? 583 GLU A CA  1 
ATOM   4863  C C   . GLU A 1 583 ? 4.405   -8.426  -36.588 1.00 41.97  ? 583 GLU A C   1 
ATOM   4864  O O   . GLU A 1 583 ? 5.241   -8.535  -37.478 1.00 40.38  ? 583 GLU A O   1 
ATOM   4865  C CB  . GLU A 1 583 ? 4.074   -10.591 -35.198 1.00 50.78  ? 583 GLU A CB  1 
ATOM   4866  C CG  . GLU A 1 583 ? 4.224   -11.328 -33.848 1.00 58.76  ? 583 GLU A CG  1 
ATOM   4867  C CD  . GLU A 1 583 ? 5.553   -11.069 -33.101 1.00 65.67  ? 583 GLU A CD  1 
ATOM   4868  O OE1 . GLU A 1 583 ? 6.484   -11.899 -33.233 1.00 64.63  ? 583 GLU A OE1 1 
ATOM   4869  O OE2 . GLU A 1 583 ? 5.656   -10.066 -32.341 1.00 65.10  ? 583 GLU A OE2 1 
ATOM   4870  N N   . LYS A 1 584 ? 3.350   -7.632  -36.722 1.00 39.59  ? 584 LYS A N   1 
ATOM   4871  C CA  . LYS A 1 584 ? 3.184   -6.833  -37.949 1.00 39.69  ? 584 LYS A CA  1 
ATOM   4872  C C   . LYS A 1 584 ? 4.337   -5.845  -38.196 1.00 39.66  ? 584 LYS A C   1 
ATOM   4873  O O   . LYS A 1 584 ? 4.586   -5.467  -39.331 1.00 44.33  ? 584 LYS A O   1 
ATOM   4874  C CB  . LYS A 1 584 ? 1.836   -6.115  -37.970 1.00 37.38  ? 584 LYS A CB  1 
ATOM   4875  C CG  . LYS A 1 584 ? 1.671   -5.067  -36.889 1.00 38.74  ? 584 LYS A CG  1 
ATOM   4876  C CD  . LYS A 1 584 ? 0.207   -4.727  -36.687 1.00 40.04  ? 584 LYS A CD  1 
ATOM   4877  C CE  . LYS A 1 584 ? 0.059   -3.559  -35.735 1.00 41.01  ? 584 LYS A CE  1 
ATOM   4878  N NZ  . LYS A 1 584 ? -1.161  -3.721  -34.904 1.00 41.33  ? 584 LYS A NZ  1 
ATOM   4879  N N   . PHE A 1 585 ? 5.040   -5.444  -37.133 1.00 38.72  ? 585 PHE A N   1 
ATOM   4880  C CA  . PHE A 1 585 ? 6.189   -4.537  -37.256 1.00 37.14  ? 585 PHE A CA  1 
ATOM   4881  C C   . PHE A 1 585 ? 7.547   -5.245  -37.085 1.00 37.97  ? 585 PHE A C   1 
ATOM   4882  O O   . PHE A 1 585 ? 8.601   -4.624  -37.239 1.00 35.79  ? 585 PHE A O   1 
ATOM   4883  C CB  . PHE A 1 585 ? 6.090   -3.407  -36.210 1.00 35.30  ? 585 PHE A CB  1 
ATOM   4884  C CG  . PHE A 1 585 ? 4.953   -2.425  -36.449 1.00 33.24  ? 585 PHE A CG  1 
ATOM   4885  C CD1 . PHE A 1 585 ? 4.923   -1.633  -37.584 1.00 31.01  ? 585 PHE A CD1 1 
ATOM   4886  C CD2 . PHE A 1 585 ? 3.957   -2.253  -35.494 1.00 30.81  ? 585 PHE A CD2 1 
ATOM   4887  C CE1 . PHE A 1 585 ? 3.904   -0.711  -37.782 1.00 31.55  ? 585 PHE A CE1 1 
ATOM   4888  C CE2 . PHE A 1 585 ? 2.942   -1.336  -35.691 1.00 31.27  ? 585 PHE A CE2 1 
ATOM   4889  C CZ  . PHE A 1 585 ? 2.915   -0.559  -36.834 1.00 29.92  ? 585 PHE A CZ  1 
ATOM   4890  N N   . ARG A 1 586 ? 7.517   -6.529  -36.730 1.00 40.66  ? 586 ARG A N   1 
ATOM   4891  C CA  . ARG A 1 586 ? 8.711   -7.214  -36.236 1.00 42.51  ? 586 ARG A CA  1 
ATOM   4892  C C   . ARG A 1 586 ? 9.725   -7.543  -37.334 1.00 43.87  ? 586 ARG A C   1 
ATOM   4893  O O   . ARG A 1 586 ? 10.920  -7.640  -37.051 1.00 47.80  ? 586 ARG A O   1 
ATOM   4894  C CB  . ARG A 1 586 ? 8.337   -8.480  -35.445 1.00 44.83  ? 586 ARG A CB  1 
ATOM   4895  C CG  . ARG A 1 586 ? 9.493   -9.125  -34.689 1.00 49.22  ? 586 ARG A CG  1 
ATOM   4896  C CD  . ARG A 1 586 ? 9.023   -10.025 -33.546 1.00 55.53  ? 586 ARG A CD  1 
ATOM   4897  N NE  . ARG A 1 586 ? 8.829   -11.425 -33.941 1.00 62.99  ? 586 ARG A NE  1 
ATOM   4898  C CZ  . ARG A 1 586 ? 9.718   -12.410 -33.750 1.00 68.59  ? 586 ARG A CZ  1 
ATOM   4899  N NH1 . ARG A 1 586 ? 10.898  -12.160 -33.183 1.00 69.87  ? 586 ARG A NH1 1 
ATOM   4900  N NH2 . ARG A 1 586 ? 9.430   -13.656 -34.134 1.00 63.06  ? 586 ARG A NH2 1 
ATOM   4901  N N   . PHE A 1 587 ? 9.265   -7.694  -38.573 1.00 41.78  ? 587 PHE A N   1 
ATOM   4902  C CA  . PHE A 1 587 ? 10.152  -8.153  -39.650 1.00 46.54  ? 587 PHE A CA  1 
ATOM   4903  C C   . PHE A 1 587 ? 10.227  -7.200  -40.838 1.00 47.70  ? 587 PHE A C   1 
ATOM   4904  O O   . PHE A 1 587 ? 10.490  -7.635  -41.959 1.00 48.51  ? 587 PHE A O   1 
ATOM   4905  C CB  . PHE A 1 587 ? 9.738   -9.551  -40.161 1.00 49.39  ? 587 PHE A CB  1 
ATOM   4906  C CG  . PHE A 1 587 ? 9.527   -10.575 -39.071 1.00 51.66  ? 587 PHE A CG  1 
ATOM   4907  C CD1 . PHE A 1 587 ? 10.608  -11.080 -38.339 1.00 52.47  ? 587 PHE A CD1 1 
ATOM   4908  C CD2 . PHE A 1 587 ? 8.246   -11.063 -38.799 1.00 52.62  ? 587 PHE A CD2 1 
ATOM   4909  C CE1 . PHE A 1 587 ? 10.411  -12.039 -37.351 1.00 53.51  ? 587 PHE A CE1 1 
ATOM   4910  C CE2 . PHE A 1 587 ? 8.044   -12.024 -37.810 1.00 53.59  ? 587 PHE A CE2 1 
ATOM   4911  C CZ  . PHE A 1 587 ? 9.125   -12.515 -37.092 1.00 54.31  ? 587 PHE A CZ  1 
ATOM   4912  N N   . VAL A 1 588 ? 9.986   -5.907  -40.611 1.00 46.43  ? 588 VAL A N   1 
ATOM   4913  C CA  . VAL A 1 588 ? 10.240  -4.909  -41.656 1.00 40.52  ? 588 VAL A CA  1 
ATOM   4914  C C   . VAL A 1 588 ? 11.739  -4.817  -41.835 1.00 38.08  ? 588 VAL A C   1 
ATOM   4915  O O   . VAL A 1 588 ? 12.485  -4.987  -40.871 1.00 36.71  ? 588 VAL A O   1 
ATOM   4916  C CB  . VAL A 1 588 ? 9.646   -3.506  -41.320 1.00 39.88  ? 588 VAL A CB  1 
ATOM   4917  C CG1 . VAL A 1 588 ? 8.167   -3.603  -41.007 1.00 39.96  ? 588 VAL A CG1 1 
ATOM   4918  C CG2 . VAL A 1 588 ? 10.382  -2.843  -40.179 1.00 35.39  ? 588 VAL A CG2 1 
ATOM   4919  N N   . LYS A 1 589 ? 12.192  -4.601  -43.065 1.00 38.60  ? 589 LYS A N   1 
ATOM   4920  C CA  . LYS A 1 589 ? 13.632  -4.470  -43.317 1.00 38.98  ? 589 LYS A CA  1 
ATOM   4921  C C   . LYS A 1 589 ? 14.124  -3.090  -42.881 1.00 37.99  ? 589 LYS A C   1 
ATOM   4922  O O   . LYS A 1 589 ? 13.510  -2.069  -43.210 1.00 35.55  ? 589 LYS A O   1 
ATOM   4923  C CB  . LYS A 1 589 ? 13.957  -4.701  -44.799 1.00 43.08  ? 589 LYS A CB  1 
ATOM   4924  C CG  . LYS A 1 589 ? 14.453  -6.103  -45.138 1.00 47.34  ? 589 LYS A CG  1 
ATOM   4925  C CD  . LYS A 1 589 ? 15.447  -6.076  -46.302 1.00 49.20  ? 589 LYS A CD  1 
ATOM   4926  C CE  . LYS A 1 589 ? 14.845  -6.671  -47.573 1.00 54.64  ? 589 LYS A CE  1 
ATOM   4927  N NZ  . LYS A 1 589 ? 15.395  -6.075  -48.833 1.00 54.27  ? 589 LYS A NZ  1 
ATOM   4928  N N   . ILE A 1 590 ? 15.229  -3.058  -42.141 1.00 36.19  ? 590 ILE A N   1 
ATOM   4929  C CA  . ILE A 1 590 ? 15.850  -1.787  -41.771 1.00 35.09  ? 590 ILE A CA  1 
ATOM   4930  C C   . ILE A 1 590 ? 17.283  -1.665  -42.302 1.00 35.46  ? 590 ILE A C   1 
ATOM   4931  O O   . ILE A 1 590 ? 17.999  -0.730  -41.975 1.00 35.31  ? 590 ILE A O   1 
ATOM   4932  C CB  . ILE A 1 590 ? 15.811  -1.557  -40.239 1.00 35.09  ? 590 ILE A CB  1 
ATOM   4933  C CG1 . ILE A 1 590 ? 16.754  -2.540  -39.507 1.00 35.34  ? 590 ILE A CG1 1 
ATOM   4934  C CG2 . ILE A 1 590 ? 14.383  -1.694  -39.735 1.00 34.12  ? 590 ILE A CG2 1 
ATOM   4935  C CD1 . ILE A 1 590 ? 16.812  -2.356  -38.005 1.00 35.00  ? 590 ILE A CD1 1 
ATOM   4936  N N   . ASN A 1 591 ? 17.716  -2.634  -43.087 1.00 37.03  ? 591 ASN A N   1 
ATOM   4937  C CA  . ASN A 1 591 ? 19.072  -2.596  -43.597 1.00 39.74  ? 591 ASN A CA  1 
ATOM   4938  C C   . ASN A 1 591 ? 19.069  -2.309  -45.087 1.00 40.12  ? 591 ASN A C   1 
ATOM   4939  O O   . ASN A 1 591 ? 18.419  -3.012  -45.865 1.00 38.76  ? 591 ASN A O   1 
ATOM   4940  C CB  . ASN A 1 591 ? 19.824  -3.896  -43.294 1.00 42.30  ? 591 ASN A CB  1 
ATOM   4941  C CG  . ASN A 1 591 ? 20.168  -4.047  -41.821 1.00 44.05  ? 591 ASN A CG  1 
ATOM   4942  O OD1 . ASN A 1 591 ? 20.471  -3.063  -41.126 1.00 46.98  ? 591 ASN A OD1 1 
ATOM   4943  N ND2 . ASN A 1 591 ? 20.138  -5.284  -41.337 1.00 42.06  ? 591 ASN A ND2 1 
ATOM   4944  N N   . ARG A 1 592 ? 19.784  -1.259  -45.463 1.00 37.02  ? 592 ARG A N   1 
ATOM   4945  C CA  . ARG A 1 592 ? 19.831  -0.807  -46.834 1.00 40.06  ? 592 ARG A CA  1 
ATOM   4946  C C   . ARG A 1 592 ? 20.975  -1.472  -47.591 1.00 40.44  ? 592 ARG A C   1 
ATOM   4947  O O   . ARG A 1 592 ? 22.141  -1.268  -47.253 1.00 45.03  ? 592 ARG A O   1 
ATOM   4948  C CB  . ARG A 1 592 ? 20.041  0.711   -46.830 1.00 37.64  ? 592 ARG A CB  1 
ATOM   4949  C CG  . ARG A 1 592 ? 19.576  1.395   -48.082 1.00 34.00  ? 592 ARG A CG  1 
ATOM   4950  C CD  . ARG A 1 592 ? 19.732  2.902   -47.997 1.00 31.45  ? 592 ARG A CD  1 
ATOM   4951  N NE  . ARG A 1 592 ? 19.363  3.521   -49.272 1.00 29.01  ? 592 ARG A NE  1 
ATOM   4952  C CZ  . ARG A 1 592 ? 19.001  4.791   -49.402 1.00 29.49  ? 592 ARG A CZ  1 
ATOM   4953  N NH1 . ARG A 1 592 ? 18.907  5.561   -48.325 1.00 30.41  ? 592 ARG A NH1 1 
ATOM   4954  N NH2 . ARG A 1 592 ? 18.693  5.283   -50.596 1.00 28.83  ? 592 ARG A NH2 1 
ATOM   4955  N N   . LYS A 1 593 ? 20.665  -2.241  -48.621 1.00 42.07  ? 593 LYS A N   1 
ATOM   4956  C CA  . LYS A 1 593 ? 21.728  -2.707  -49.536 1.00 49.33  ? 593 LYS A CA  1 
ATOM   4957  C C   . LYS A 1 593 ? 21.314  -2.828  -51.012 1.00 48.97  ? 593 LYS A C   1 
ATOM   4958  O O   . LYS A 1 593 ? 20.180  -3.200  -51.316 1.00 46.76  ? 593 LYS A O   1 
ATOM   4959  C CB  . LYS A 1 593 ? 22.356  -4.017  -49.047 1.00 54.48  ? 593 LYS A CB  1 
ATOM   4960  C CG  . LYS A 1 593 ? 23.845  -4.138  -49.389 1.00 60.39  ? 593 LYS A CG  1 
ATOM   4961  C CD  . LYS A 1 593 ? 24.486  -5.365  -48.745 1.00 64.18  ? 593 LYS A CD  1 
ATOM   4962  C CE  . LYS A 1 593 ? 24.093  -6.650  -49.461 1.00 66.97  ? 593 LYS A CE  1 
ATOM   4963  N NZ  . LYS A 1 593 ? 24.750  -6.773  -50.796 1.00 70.58  ? 593 LYS A NZ  1 
ATOM   4964  N N   . ALA A 1 594 ? 22.258  -2.530  -51.913 1.00 51.13  ? 594 ALA A N   1 
ATOM   4965  C CA  . ALA A 1 594 ? 22.032  -2.601  -53.376 1.00 50.97  ? 594 ALA A CA  1 
ATOM   4966  C C   . ALA A 1 594 ? 21.771  -4.014  -53.871 1.00 52.06  ? 594 ALA A C   1 
ATOM   4967  O O   . ALA A 1 594 ? 22.487  -4.951  -53.507 1.00 50.73  ? 594 ALA A O   1 
ATOM   4968  C CB  . ALA A 1 594 ? 23.199  -1.992  -54.130 1.00 50.40  ? 594 ALA A CB  1 
ATOM   4969  N N   . SER A 1 595 ? 20.748  -4.150  -54.717 1.00 53.29  ? 595 SER A N   1 
ATOM   4970  C CA  . SER A 1 595 ? 20.281  -5.458  -55.198 1.00 57.62  ? 595 SER A CA  1 
ATOM   4971  C C   . SER A 1 595 ? 20.184  -5.514  -56.737 1.00 56.20  ? 595 SER A C   1 
ATOM   4972  O O   . SER A 1 595 ? 19.662  -6.481  -57.299 1.00 57.40  ? 595 SER A O   1 
ATOM   4973  C CB  . SER A 1 595 ? 18.919  -5.795  -54.559 1.00 58.61  ? 595 SER A CB  1 
ATOM   4974  O OG  . SER A 1 595 ? 18.438  -7.065  -54.977 1.00 60.21  ? 595 SER A OG  1 
ATOM   4975  N N   . ILE A 1 596 ? 20.672  -4.467  -57.402 1.00 52.59  ? 596 ILE A N   1 
ATOM   4976  C CA  . ILE A 1 596 ? 20.788  -4.451  -58.866 1.00 52.39  ? 596 ILE A CA  1 
ATOM   4977  C C   . ILE A 1 596 ? 22.123  -3.832  -59.355 1.00 52.94  ? 596 ILE A C   1 
ATOM   4978  O O   . ILE A 1 596 ? 22.612  -4.137  -60.458 1.00 51.16  ? 596 ILE A O   1 
ATOM   4979  C CB  . ILE A 1 596 ? 19.555  -3.789  -59.571 1.00 50.28  ? 596 ILE A CB  1 
ATOM   4980  C CG1 . ILE A 1 596 ? 19.526  -2.256  -59.413 1.00 48.36  ? 596 ILE A CG1 1 
ATOM   4981  C CG2 . ILE A 1 596 ? 18.245  -4.429  -59.129 1.00 51.79  ? 596 ILE A CG2 1 
ATOM   4982  C CD1 . ILE A 1 596 ? 19.222  -1.767  -58.020 1.00 47.53  ? 596 ILE A CD1 1 
ATOM   4983  N N   . MET B 1 1   ? -0.084  11.971  -6.793  1.00 73.40  ? 1   MET B N   1 
ATOM   4984  C CA  . MET B 1 1   ? -0.584  12.531  -8.083  1.00 69.90  ? 1   MET B CA  1 
ATOM   4985  C C   . MET B 1 1   ? -0.993  14.015  -7.997  1.00 63.37  ? 1   MET B C   1 
ATOM   4986  O O   . MET B 1 1   ? -1.079  14.686  -9.032  1.00 66.43  ? 1   MET B O   1 
ATOM   4987  C CB  . MET B 1 1   ? -1.739  11.680  -8.648  1.00 75.78  ? 1   MET B CB  1 
ATOM   4988  C CG  . MET B 1 1   ? -3.059  11.782  -7.876  1.00 80.83  ? 1   MET B CG  1 
ATOM   4989  S SD  . MET B 1 1   ? -4.549  11.573  -8.895  1.00 89.46  ? 1   MET B SD  1 
ATOM   4990  C CE  . MET B 1 1   ? -5.855  11.811  -7.684  1.00 85.69  ? 1   MET B CE  1 
ATOM   4991  N N   . VAL B 1 2   ? -1.248  14.523  -6.784  1.00 55.31  ? 2   VAL B N   1 
ATOM   4992  C CA  . VAL B 1 2   ? -1.647  15.936  -6.608  1.00 50.88  ? 2   VAL B CA  1 
ATOM   4993  C C   . VAL B 1 2   ? -0.460  16.862  -6.356  1.00 46.95  ? 2   VAL B C   1 
ATOM   4994  O O   . VAL B 1 2   ? 0.241   16.722  -5.342  1.00 46.21  ? 2   VAL B O   1 
ATOM   4995  C CB  . VAL B 1 2   ? -2.674  16.146  -5.472  1.00 52.06  ? 2   VAL B CB  1 
ATOM   4996  C CG1 . VAL B 1 2   ? -3.421  17.455  -5.687  1.00 50.32  ? 2   VAL B CG1 1 
ATOM   4997  C CG2 . VAL B 1 2   ? -3.642  14.971  -5.382  1.00 55.49  ? 2   VAL B CG2 1 
ATOM   4998  N N   . HIS B 1 3   ? -0.255  17.816  -7.272  1.00 40.53  ? 3   HIS B N   1 
ATOM   4999  C CA  . HIS B 1 3   ? 0.880   18.734  -7.198  1.00 37.11  ? 3   HIS B CA  1 
ATOM   5000  C C   . HIS B 1 3   ? 0.456   20.183  -6.949  1.00 33.84  ? 3   HIS B C   1 
ATOM   5001  O O   . HIS B 1 3   ? 1.236   20.977  -6.406  1.00 29.53  ? 3   HIS B O   1 
ATOM   5002  C CB  . HIS B 1 3   ? 1.726   18.643  -8.477  1.00 39.26  ? 3   HIS B CB  1 
ATOM   5003  C CG  . HIS B 1 3   ? 2.309   17.257  -8.747  1.00 42.43  ? 3   HIS B CG  1 
ATOM   5004  N ND1 . HIS B 1 3   ? 1.952   16.512  -9.818  1.00 44.21  ? 3   HIS B ND1 1 
ATOM   5005  C CD2 . HIS B 1 3   ? 3.257   16.508  -8.052  1.00 41.68  ? 3   HIS B CD2 1 
ATOM   5006  C CE1 . HIS B 1 3   ? 2.624   15.343  -9.796  1.00 43.89  ? 3   HIS B CE1 1 
ATOM   5007  N NE2 . HIS B 1 3   ? 3.417   15.340  -8.717  1.00 43.19  ? 3   HIS B NE2 1 
ATOM   5008  N N   . TYR B 1 4   ? -0.788  20.508  -7.330  1.00 31.04  ? 4   TYR B N   1 
ATOM   5009  C CA  . TYR B 1 4   ? -1.274  21.869  -7.429  1.00 31.10  ? 4   TYR B CA  1 
ATOM   5010  C C   . TYR B 1 4   ? -2.197  22.280  -6.288  1.00 32.92  ? 4   TYR B C   1 
ATOM   5011  O O   . TYR B 1 4   ? -2.985  21.483  -5.774  1.00 32.53  ? 4   TYR B O   1 
ATOM   5012  C CB  . TYR B 1 4   ? -2.054  22.087  -8.741  1.00 30.35  ? 4   TYR B CB  1 
ATOM   5013  C CG  . TYR B 1 4   ? -1.268  21.957  -10.026 1.00 30.27  ? 4   TYR B CG  1 
ATOM   5014  C CD1 . TYR B 1 4   ? 0.126   21.789  -10.022 1.00 29.71  ? 4   TYR B CD1 1 
ATOM   5015  C CD2 . TYR B 1 4   ? -1.920  22.034  -11.263 1.00 30.04  ? 4   TYR B CD2 1 
ATOM   5016  C CE1 . TYR B 1 4   ? 0.839   21.681  -11.211 1.00 29.49  ? 4   TYR B CE1 1 
ATOM   5017  C CE2 . TYR B 1 4   ? -1.214  21.925  -12.447 1.00 29.91  ? 4   TYR B CE2 1 
ATOM   5018  C CZ  . TYR B 1 4   ? 0.165   21.748  -12.413 1.00 29.37  ? 4   TYR B CZ  1 
ATOM   5019  O OH  . TYR B 1 4   ? 0.863   21.642  -13.589 1.00 29.45  ? 4   TYR B OH  1 
ATOM   5020  N N   . TYR B 1 5   ? -2.110  23.554  -5.931  1.00 32.53  ? 5   TYR B N   1 
ATOM   5021  C CA  . TYR B 1 5   ? -3.104  24.182  -5.106  1.00 32.76  ? 5   TYR B CA  1 
ATOM   5022  C C   . TYR B 1 5   ? -3.803  25.207  -5.984  1.00 32.88  ? 5   TYR B C   1 
ATOM   5023  O O   . TYR B 1 5   ? -3.160  26.074  -6.548  1.00 33.87  ? 5   TYR B O   1 
ATOM   5024  C CB  . TYR B 1 5   ? -2.440  24.864  -3.889  1.00 31.70  ? 5   TYR B CB  1 
ATOM   5025  C CG  . TYR B 1 5   ? -3.423  25.604  -3.013  1.00 31.82  ? 5   TYR B CG  1 
ATOM   5026  C CD1 . TYR B 1 5   ? -4.394  24.909  -2.280  1.00 31.70  ? 5   TYR B CD1 1 
ATOM   5027  C CD2 . TYR B 1 5   ? -3.421  27.004  -2.950  1.00 31.14  ? 5   TYR B CD2 1 
ATOM   5028  C CE1 . TYR B 1 5   ? -5.319  25.579  -1.496  1.00 32.19  ? 5   TYR B CE1 1 
ATOM   5029  C CE2 . TYR B 1 5   ? -4.331  27.690  -2.144  1.00 31.49  ? 5   TYR B CE2 1 
ATOM   5030  C CZ  . TYR B 1 5   ? -5.282  26.976  -1.429  1.00 32.15  ? 5   TYR B CZ  1 
ATOM   5031  O OH  . TYR B 1 5   ? -6.196  27.637  -0.652  1.00 33.18  ? 5   TYR B OH  1 
ATOM   5032  N N   . ARG B 1 6   ? -5.111  25.096  -6.119  1.00 32.96  ? 6   ARG B N   1 
ATOM   5033  C CA  . ARG B 1 6   ? -5.854  26.053  -6.921  1.00 33.69  ? 6   ARG B CA  1 
ATOM   5034  C C   . ARG B 1 6   ? -5.943  27.401  -6.214  1.00 32.90  ? 6   ARG B C   1 
ATOM   5035  O O   . ARG B 1 6   ? -6.101  27.451  -4.998  1.00 32.84  ? 6   ARG B O   1 
ATOM   5036  C CB  . ARG B 1 6   ? -7.254  25.521  -7.217  1.00 35.16  ? 6   ARG B CB  1 
ATOM   5037  C CG  . ARG B 1 6   ? -7.280  24.405  -8.241  1.00 36.94  ? 6   ARG B CG  1 
ATOM   5038  C CD  . ARG B 1 6   ? -8.670  23.812  -8.357  1.00 41.58  ? 6   ARG B CD  1 
ATOM   5039  N NE  . ARG B 1 6   ? -9.216  23.453  -7.039  1.00 46.36  ? 6   ARG B NE  1 
ATOM   5040  C CZ  . ARG B 1 6   ? -10.198 22.581  -6.841  1.00 47.28  ? 6   ARG B CZ  1 
ATOM   5041  N NH1 . ARG B 1 6   ? -10.754 21.952  -7.871  1.00 49.59  ? 6   ARG B NH1 1 
ATOM   5042  N NH2 . ARG B 1 6   ? -10.626 22.340  -5.612  1.00 47.84  ? 6   ARG B NH2 1 
ATOM   5043  N N   . LEU B 1 7   ? -5.837  28.490  -6.968  1.00 31.24  ? 7   LEU B N   1 
ATOM   5044  C CA  . LEU B 1 7   ? -5.926  29.834  -6.368  1.00 30.62  ? 7   LEU B CA  1 
ATOM   5045  C C   . LEU B 1 7   ? -7.360  30.344  -6.237  1.00 32.33  ? 7   LEU B C   1 
ATOM   5046  O O   . LEU B 1 7   ? -7.605  31.373  -5.588  1.00 33.68  ? 7   LEU B O   1 
ATOM   5047  C CB  . LEU B 1 7   ? -5.114  30.848  -7.160  1.00 28.41  ? 7   LEU B CB  1 
ATOM   5048  C CG  . LEU B 1 7   ? -3.614  30.639  -7.374  1.00 28.44  ? 7   LEU B CG  1 
ATOM   5049  C CD1 . LEU B 1 7   ? -3.060  31.926  -7.996  1.00 28.61  ? 7   LEU B CD1 1 
ATOM   5050  C CD2 . LEU B 1 7   ? -2.889  30.290  -6.064  1.00 27.23  ? 7   LEU B CD2 1 
ATOM   5051  N N   . SER B 1 8   ? -8.294  29.626  -6.844  1.00 32.54  ? 8   SER B N   1 
ATOM   5052  C CA  . SER B 1 8   ? -9.695  30.043  -6.908  1.00 36.00  ? 8   SER B CA  1 
ATOM   5053  C C   . SER B 1 8   ? -10.353 30.200  -5.521  1.00 37.64  ? 8   SER B C   1 
ATOM   5054  O O   . SER B 1 8   ? -10.245 29.323  -4.651  1.00 35.51  ? 8   SER B O   1 
ATOM   5055  C CB  . SER B 1 8   ? -10.489 29.027  -7.743  1.00 38.29  ? 8   SER B CB  1 
ATOM   5056  O OG  . SER B 1 8   ? -11.826 29.440  -7.939  1.00 40.26  ? 8   SER B OG  1 
ATOM   5057  N N   . LEU B 1 9   ? -11.029 31.323  -5.323  1.00 37.53  ? 9   LEU B N   1 
ATOM   5058  C CA  . LEU B 1 9   ? -11.845 31.520  -4.132  1.00 39.90  ? 9   LEU B CA  1 
ATOM   5059  C C   . LEU B 1 9   ? -12.897 30.415  -3.949  1.00 43.15  ? 9   LEU B C   1 
ATOM   5060  O O   . LEU B 1 9   ? -13.202 30.037  -2.821  1.00 43.33  ? 9   LEU B O   1 
ATOM   5061  C CB  . LEU B 1 9   ? -12.524 32.887  -4.188  1.00 37.89  ? 9   LEU B CB  1 
ATOM   5062  C CG  . LEU B 1 9   ? -11.846 34.018  -3.419  1.00 37.06  ? 9   LEU B CG  1 
ATOM   5063  C CD1 . LEU B 1 9   ? -10.321 33.990  -3.535  1.00 35.26  ? 9   LEU B CD1 1 
ATOM   5064  C CD2 . LEU B 1 9   ? -12.434 35.357  -3.852  1.00 36.52  ? 9   LEU B CD2 1 
ATOM   5065  N N   . LYS B 1 10  ? -13.424 29.896  -5.068  1.00 45.02  ? 10  LYS B N   1 
ATOM   5066  C CA  . LYS B 1 10  ? -14.512 28.887  -5.074  1.00 47.68  ? 10  LYS B CA  1 
ATOM   5067  C C   . LYS B 1 10  ? -14.273 27.681  -4.164  1.00 46.84  ? 10  LYS B C   1 
ATOM   5068  O O   . LYS B 1 10  ? -15.219 27.075  -3.653  1.00 48.56  ? 10  LYS B O   1 
ATOM   5069  C CB  . LYS B 1 10  ? -14.795 28.399  -6.509  1.00 51.84  ? 10  LYS B CB  1 
ATOM   5070  C CG  . LYS B 1 10  ? -15.230 29.494  -7.476  1.00 56.93  ? 10  LYS B CG  1 
ATOM   5071  C CD  . LYS B 1 10  ? -15.574 28.940  -8.854  1.00 60.67  ? 10  LYS B CD  1 
ATOM   5072  C CE  . LYS B 1 10  ? -15.702 30.069  -9.869  1.00 63.45  ? 10  LYS B CE  1 
ATOM   5073  N NZ  . LYS B 1 10  ? -16.639 29.734  -10.978 1.00 67.08  ? 10  LYS B NZ  1 
ATOM   5074  N N   . SER B 1 11  ? -13.011 27.334  -3.969  1.00 47.90  ? 11  SER B N   1 
ATOM   5075  C CA  . SER B 1 11  ? -12.651 26.210  -3.113  1.00 50.18  ? 11  SER B CA  1 
ATOM   5076  C C   . SER B 1 11  ? -12.331 26.618  -1.666  1.00 49.18  ? 11  SER B C   1 
ATOM   5077  O O   . SER B 1 11  ? -11.723 25.845  -0.919  1.00 52.93  ? 11  SER B O   1 
ATOM   5078  C CB  . SER B 1 11  ? -11.484 25.428  -3.725  1.00 48.72  ? 11  SER B CB  1 
ATOM   5079  O OG  . SER B 1 11  ? -10.455 26.306  -4.135  1.00 46.19  ? 11  SER B OG  1 
ATOM   5080  N N   . ARG B 1 12  ? -12.762 27.812  -1.261  1.00 46.63  ? 12  ARG B N   1 
ATOM   5081  C CA  . ARG B 1 12  ? -12.615 28.237  0.142   1.00 46.48  ? 12  ARG B CA  1 
ATOM   5082  C C   . ARG B 1 12  ? -13.507 27.419  1.073   1.00 49.66  ? 12  ARG B C   1 
ATOM   5083  O O   . ARG B 1 12  ? -14.512 26.831  0.641   1.00 49.64  ? 12  ARG B O   1 
ATOM   5084  C CB  . ARG B 1 12  ? -12.924 29.726  0.307   1.00 44.04  ? 12  ARG B CB  1 
ATOM   5085  C CG  . ARG B 1 12  ? -14.382 30.098  0.106   1.00 42.30  ? 12  ARG B CG  1 
ATOM   5086  C CD  . ARG B 1 12  ? -14.529 31.600  0.044   1.00 41.96  ? 12  ARG B CD  1 
ATOM   5087  N NE  . ARG B 1 12  ? -15.918 31.999  -0.148  1.00 42.07  ? 12  ARG B NE  1 
ATOM   5088  C CZ  . ARG B 1 12  ? -16.492 32.193  -1.333  1.00 40.80  ? 12  ARG B CZ  1 
ATOM   5089  N NH1 . ARG B 1 12  ? -15.806 32.024  -2.455  1.00 40.60  ? 12  ARG B NH1 1 
ATOM   5090  N NH2 . ARG B 1 12  ? -17.757 32.559  -1.393  1.00 41.93  ? 12  ARG B NH2 1 
ATOM   5091  N N   . GLN B 1 13  ? -13.156 27.402  2.355   1.00 49.32  ? 13  GLN B N   1 
ATOM   5092  C CA  . GLN B 1 13  ? -13.946 26.669  3.339   1.00 50.01  ? 13  GLN B CA  1 
ATOM   5093  C C   . GLN B 1 13  ? -14.505 27.572  4.419   1.00 49.27  ? 13  GLN B C   1 
ATOM   5094  O O   . GLN B 1 13  ? -14.006 28.673  4.625   1.00 49.42  ? 13  GLN B O   1 
ATOM   5095  C CB  . GLN B 1 13  ? -13.128 25.525  3.939   1.00 50.58  ? 13  GLN B CB  1 
ATOM   5096  C CG  . GLN B 1 13  ? -13.146 24.269  3.073   1.00 54.29  ? 13  GLN B CG  1 
ATOM   5097  C CD  . GLN B 1 13  ? -12.062 23.276  3.437   1.00 55.23  ? 13  GLN B CD  1 
ATOM   5098  O OE1 . GLN B 1 13  ? -11.560 22.557  2.573   1.00 57.29  ? 13  GLN B OE1 1 
ATOM   5099  N NE2 . GLN B 1 13  ? -11.685 23.234  4.719   1.00 52.54  ? 13  GLN B NE2 1 
ATOM   5100  N N   . LYS B 1 14  ? -15.569 27.120  5.079   1.00 52.81  ? 14  LYS B N   1 
ATOM   5101  C CA  . LYS B 1 14  ? -16.090 27.817  6.244   1.00 53.19  ? 14  LYS B CA  1 
ATOM   5102  C C   . LYS B 1 14  ? -15.274 27.435  7.464   1.00 51.97  ? 14  LYS B C   1 
ATOM   5103  O O   . LYS B 1 14  ? -15.273 26.274  7.876   1.00 53.84  ? 14  LYS B O   1 
ATOM   5104  C CB  . LYS B 1 14  ? -17.571 27.510  6.474   1.00 56.13  ? 14  LYS B CB  1 
ATOM   5105  C CG  . LYS B 1 14  ? -18.105 28.185  7.729   1.00 59.43  ? 14  LYS B CG  1 
ATOM   5106  C CD  . LYS B 1 14  ? -19.622 28.183  7.822   1.00 61.81  ? 14  LYS B CD  1 
ATOM   5107  C CE  . LYS B 1 14  ? -20.069 28.906  9.089   1.00 62.69  ? 14  LYS B CE  1 
ATOM   5108  N NZ  . LYS B 1 14  ? -21.505 28.677  9.408   1.00 65.94  ? 14  LYS B NZ  1 
ATOM   5109  N N   . ALA B 1 15  ? -14.555 28.409  8.014   1.00 48.30  ? 15  ALA B N   1 
ATOM   5110  C CA  . ALA B 1 15  ? -13.778 28.217  9.245   1.00 48.80  ? 15  ALA B CA  1 
ATOM   5111  C C   . ALA B 1 15  ? -14.660 27.767  10.398  1.00 50.03  ? 15  ALA B C   1 
ATOM   5112  O O   . ALA B 1 15  ? -15.743 28.325  10.609  1.00 48.95  ? 15  ALA B O   1 
ATOM   5113  C CB  . ALA B 1 15  ? -13.061 29.507  9.631   1.00 45.82  ? 15  ALA B CB  1 
ATOM   5114  N N   . PRO B 1 16  ? -14.195 26.763  11.156  1.00 49.96  ? 16  PRO B N   1 
ATOM   5115  C CA  . PRO B 1 16  ? -14.835 26.430  12.417  1.00 50.84  ? 16  PRO B CA  1 
ATOM   5116  C C   . PRO B 1 16  ? -14.531 27.514  13.458  1.00 54.72  ? 16  PRO B C   1 
ATOM   5117  O O   . PRO B 1 16  ? -13.734 28.421  13.190  1.00 52.00  ? 16  PRO B O   1 
ATOM   5118  C CB  . PRO B 1 16  ? -14.168 25.107  12.814  1.00 51.16  ? 16  PRO B CB  1 
ATOM   5119  C CG  . PRO B 1 16  ? -12.834 25.127  12.128  1.00 51.81  ? 16  PRO B CG  1 
ATOM   5120  C CD  . PRO B 1 16  ? -13.042 25.889  10.851  1.00 50.10  ? 16  PRO B CD  1 
ATOM   5121  N N   . LYS B 1 17  ? -15.154 27.413  14.631  1.00 55.87  ? 17  LYS B N   1 
ATOM   5122  C CA  . LYS B 1 17  ? -14.873 28.325  15.734  1.00 56.40  ? 17  LYS B CA  1 
ATOM   5123  C C   . LYS B 1 17  ? -13.460 28.086  16.278  1.00 54.10  ? 17  LYS B C   1 
ATOM   5124  O O   . LYS B 1 17  ? -12.710 29.030  16.520  1.00 53.16  ? 17  LYS B O   1 
ATOM   5125  C CB  . LYS B 1 17  ? -15.917 28.153  16.847  1.00 60.14  ? 17  LYS B CB  1 
ATOM   5126  C CG  . LYS B 1 17  ? -16.065 29.356  17.765  1.00 65.96  ? 17  LYS B CG  1 
ATOM   5127  C CD  . LYS B 1 17  ? -16.549 28.948  19.150  1.00 67.02  ? 17  LYS B CD  1 
ATOM   5128  C CE  . LYS B 1 17  ? -16.878 30.166  19.999  1.00 69.43  ? 17  LYS B CE  1 
ATOM   5129  N NZ  . LYS B 1 17  ? -15.653 30.854  20.487  1.00 72.84  ? 17  LYS B NZ  1 
ATOM   5130  N N   . ILE B 1 18  ? -13.119 26.820  16.491  1.00 53.51  ? 18  ILE B N   1 
ATOM   5131  C CA  . ILE B 1 18  ? -11.762 26.426  16.891  1.00 54.10  ? 18  ILE B CA  1 
ATOM   5132  C C   . ILE B 1 18  ? -11.332 25.179  16.111  1.00 55.33  ? 18  ILE B C   1 
ATOM   5133  O O   . ILE B 1 18  ? -12.172 24.457  15.549  1.00 54.36  ? 18  ILE B O   1 
ATOM   5134  C CB  . ILE B 1 18  ? -11.634 26.168  18.425  1.00 56.04  ? 18  ILE B CB  1 
ATOM   5135  C CG1 . ILE B 1 18  ? -12.449 24.928  18.854  1.00 56.14  ? 18  ILE B CG1 1 
ATOM   5136  C CG2 . ILE B 1 18  ? -12.023 27.413  19.222  1.00 54.30  ? 18  ILE B CG2 1 
ATOM   5137  C CD1 . ILE B 1 18  ? -12.077 24.356  20.216  1.00 55.67  ? 18  ILE B CD1 1 
ATOM   5138  N N   . VAL B 1 19  ? -10.029 24.928  16.063  1.00 56.77  ? 19  VAL B N   1 
ATOM   5139  C CA  . VAL B 1 19  ? -9.529  23.755  15.357  1.00 58.81  ? 19  VAL B CA  1 
ATOM   5140  C C   . VAL B 1 19  ? -9.634  22.487  16.196  1.00 62.50  ? 19  VAL B C   1 
ATOM   5141  O O   . VAL B 1 19  ? -9.727  22.546  17.429  1.00 62.18  ? 19  VAL B O   1 
ATOM   5142  C CB  . VAL B 1 19  ? -8.094  23.947  14.818  1.00 56.69  ? 19  VAL B CB  1 
ATOM   5143  C CG1 . VAL B 1 19  ? -8.089  25.022  13.750  1.00 56.77  ? 19  VAL B CG1 1 
ATOM   5144  C CG2 . VAL B 1 19  ? -7.112  24.276  15.935  1.00 54.58  ? 19  VAL B CG2 1 
ATOM   5145  N N   . ASN B 1 20  ? -9.648  21.348  15.510  1.00 65.85  ? 20  ASN B N   1 
ATOM   5146  C CA  . ASN B 1 20  ? -9.641  20.046  16.164  1.00 73.61  ? 20  ASN B CA  1 
ATOM   5147  C C   . ASN B 1 20  ? -8.229  19.608  16.555  1.00 76.57  ? 20  ASN B C   1 
ATOM   5148  O O   . ASN B 1 20  ? -7.248  20.283  16.230  1.00 77.63  ? 20  ASN B O   1 
ATOM   5149  C CB  . ASN B 1 20  ? -10.326 18.989  15.283  1.00 74.56  ? 20  ASN B CB  1 
ATOM   5150  C CG  . ASN B 1 20  ? -9.752  18.929  13.878  1.00 76.67  ? 20  ASN B CG  1 
ATOM   5151  O OD1 . ASN B 1 20  ? -9.341  17.868  13.417  1.00 78.22  ? 20  ASN B OD1 1 
ATOM   5152  N ND2 . ASN B 1 20  ? -9.729  20.072  13.185  1.00 76.63  ? 20  ASN B ND2 1 
ATOM   5153  N N   . SER B 1 21  ? -8.138  18.481  17.259  1.00 79.29  ? 21  SER B N   1 
ATOM   5154  C CA  . SER B 1 21  ? -6.863  17.950  17.752  1.00 79.18  ? 21  SER B CA  1 
ATOM   5155  C C   . SER B 1 21  ? -5.794  17.835  16.664  1.00 77.59  ? 21  SER B C   1 
ATOM   5156  O O   . SER B 1 21  ? -4.600  17.814  16.964  1.00 80.94  ? 21  SER B O   1 
ATOM   5157  C CB  . SER B 1 21  ? -7.078  16.582  18.411  1.00 79.37  ? 21  SER B CB  1 
ATOM   5158  O OG  . SER B 1 21  ? -8.025  16.664  19.455  1.00 75.59  ? 21  SER B OG  1 
ATOM   5159  N N   . LYS B 1 22  ? -6.233  17.762  15.407  1.00 76.25  ? 22  LYS B N   1 
ATOM   5160  C CA  . LYS B 1 22  ? -5.330  17.665  14.253  1.00 74.03  ? 22  LYS B CA  1 
ATOM   5161  C C   . LYS B 1 22  ? -4.348  18.839  14.127  1.00 69.90  ? 22  LYS B C   1 
ATOM   5162  O O   . LYS B 1 22  ? -3.224  18.669  13.648  1.00 71.41  ? 22  LYS B O   1 
ATOM   5163  C CB  . LYS B 1 22  ? -6.139  17.536  12.961  1.00 76.09  ? 22  LYS B CB  1 
ATOM   5164  C CG  . LYS B 1 22  ? -6.424  16.106  12.523  1.00 81.23  ? 22  LYS B CG  1 
ATOM   5165  C CD  . LYS B 1 22  ? -7.530  16.051  11.471  1.00 82.34  ? 22  LYS B CD  1 
ATOM   5166  C CE  . LYS B 1 22  ? -7.281  17.011  10.314  1.00 79.61  ? 22  LYS B CE  1 
ATOM   5167  N NZ  . LYS B 1 22  ? -8.528  17.295  9.551   1.00 79.55  ? 22  LYS B NZ  1 
ATOM   5168  N N   . TYR B 1 23  ? -4.781  20.024  14.547  1.00 65.53  ? 23  TYR B N   1 
ATOM   5169  C CA  . TYR B 1 23  ? -4.005  21.249  14.337  1.00 59.27  ? 23  TYR B CA  1 
ATOM   5170  C C   . TYR B 1 23  ? -3.485  21.830  15.635  1.00 55.54  ? 23  TYR B C   1 
ATOM   5171  O O   . TYR B 1 23  ? -4.106  21.678  16.685  1.00 54.30  ? 23  TYR B O   1 
ATOM   5172  C CB  . TYR B 1 23  ? -4.856  22.301  13.638  1.00 57.50  ? 23  TYR B CB  1 
ATOM   5173  C CG  . TYR B 1 23  ? -5.338  21.918  12.254  1.00 59.98  ? 23  TYR B CG  1 
ATOM   5174  C CD1 . TYR B 1 23  ? -4.504  22.048  11.140  1.00 57.59  ? 23  TYR B CD1 1 
ATOM   5175  C CD2 . TYR B 1 23  ? -6.642  21.459  12.052  1.00 60.92  ? 23  TYR B CD2 1 
ATOM   5176  C CE1 . TYR B 1 23  ? -4.952  21.729  9.873   1.00 57.16  ? 23  TYR B CE1 1 
ATOM   5177  C CE2 . TYR B 1 23  ? -7.097  21.132  10.786  1.00 59.26  ? 23  TYR B CE2 1 
ATOM   5178  C CZ  . TYR B 1 23  ? -6.249  21.272  9.702   1.00 59.63  ? 23  TYR B CZ  1 
ATOM   5179  O OH  . TYR B 1 23  ? -6.692  20.947  8.441   1.00 62.16  ? 23  TYR B OH  1 
ATOM   5180  N N   . ASN B 1 24  ? -2.343  22.506  15.555  1.00 51.21  ? 24  ASN B N   1 
ATOM   5181  C CA  . ASN B 1 24  ? -1.853  23.305  16.655  1.00 46.81  ? 24  ASN B CA  1 
ATOM   5182  C C   . ASN B 1 24  ? -2.872  24.401  16.958  1.00 48.32  ? 24  ASN B C   1 
ATOM   5183  O O   . ASN B 1 24  ? -3.420  25.034  16.044  1.00 47.35  ? 24  ASN B O   1 
ATOM   5184  C CB  . ASN B 1 24  ? -0.480  23.888  16.317  1.00 45.92  ? 24  ASN B CB  1 
ATOM   5185  C CG  . ASN B 1 24  ? 0.175   24.578  17.495  1.00 46.87  ? 24  ASN B CG  1 
ATOM   5186  O OD1 . ASN B 1 24  ? -0.302  25.598  17.964  1.00 48.47  ? 24  ASN B OD1 1 
ATOM   5187  N ND2 . ASN B 1 24  ? 1.284   24.028  17.968  1.00 48.13  ? 24  ASN B ND2 1 
ATOM   5188  N N   . SER B 1 25  ? -3.152  24.604  18.243  1.00 46.12  ? 25  SER B N   1 
ATOM   5189  C CA  . SER B 1 25  ? -4.179  25.549  18.649  1.00 45.93  ? 25  SER B CA  1 
ATOM   5190  C C   . SER B 1 25  ? -3.785  27.009  18.384  1.00 42.86  ? 25  SER B C   1 
ATOM   5191  O O   . SER B 1 25  ? -4.559  27.924  18.667  1.00 41.92  ? 25  SER B O   1 
ATOM   5192  C CB  . SER B 1 25  ? -4.546  25.347  20.120  1.00 45.62  ? 25  SER B CB  1 
ATOM   5193  O OG  . SER B 1 25  ? -3.447  25.645  20.946  1.00 46.99  ? 25  SER B OG  1 
ATOM   5194  N N   . ILE B 1 26  ? -2.592  27.220  17.825  1.00 40.59  ? 26  ILE B N   1 
ATOM   5195  C CA  . ILE B 1 26  ? -2.190  28.555  17.366  1.00 38.41  ? 26  ILE B CA  1 
ATOM   5196  C C   . ILE B 1 26  ? -3.169  29.092  16.309  1.00 37.20  ? 26  ILE B C   1 
ATOM   5197  O O   . ILE B 1 26  ? -3.476  30.266  16.300  1.00 37.15  ? 26  ILE B O   1 
ATOM   5198  C CB  . ILE B 1 26  ? -0.729  28.581  16.856  1.00 37.52  ? 26  ILE B CB  1 
ATOM   5199  C CG1 . ILE B 1 26  ? -0.208  30.026  16.760  1.00 36.34  ? 26  ILE B CG1 1 
ATOM   5200  C CG2 . ILE B 1 26  ? -0.578  27.789  15.556  1.00 35.48  ? 26  ILE B CG2 1 
ATOM   5201  C CD1 . ILE B 1 26  ? 1.281   30.136  16.492  1.00 34.13  ? 26  ILE B CD1 1 
ATOM   5202  N N   . LEU B 1 27  ? -3.693  28.198  15.474  1.00 38.47  ? 27  LEU B N   1 
ATOM   5203  C CA  . LEU B 1 27  ? -4.730  28.533  14.488  1.00 38.75  ? 27  LEU B CA  1 
ATOM   5204  C C   . LEU B 1 27  ? -5.979  29.134  15.117  1.00 40.00  ? 27  LEU B C   1 
ATOM   5205  O O   . LEU B 1 27  ? -6.686  29.923  14.482  1.00 40.31  ? 27  LEU B O   1 
ATOM   5206  C CB  . LEU B 1 27  ? -5.121  27.299  13.688  1.00 37.66  ? 27  LEU B CB  1 
ATOM   5207  C CG  . LEU B 1 27  ? -4.038  26.692  12.814  1.00 39.64  ? 27  LEU B CG  1 
ATOM   5208  C CD1 . LEU B 1 27  ? -4.593  25.474  12.070  1.00 39.33  ? 27  LEU B CD1 1 
ATOM   5209  C CD2 . LEU B 1 27  ? -3.489  27.740  11.843  1.00 37.70  ? 27  LEU B CD2 1 
ATOM   5210  N N   . ASN B 1 28  ? -6.255  28.747  16.358  1.00 40.30  ? 28  ASN B N   1 
ATOM   5211  C CA  . ASN B 1 28  ? -7.348  29.340  17.121  1.00 42.71  ? 28  ASN B CA  1 
ATOM   5212  C C   . ASN B 1 28  ? -7.248  30.857  17.275  1.00 41.80  ? 28  ASN B C   1 
ATOM   5213  O O   . ASN B 1 28  ? -8.253  31.549  17.190  1.00 45.05  ? 28  ASN B O   1 
ATOM   5214  C CB  . ASN B 1 28  ? -7.479  28.668  18.493  1.00 43.31  ? 28  ASN B CB  1 
ATOM   5215  C CG  . ASN B 1 28  ? -7.880  27.211  18.386  1.00 45.40  ? 28  ASN B CG  1 
ATOM   5216  O OD1 . ASN B 1 28  ? -8.425  26.778  17.372  1.00 44.50  ? 28  ASN B OD1 1 
ATOM   5217  N ND2 . ASN B 1 28  ? -7.622  26.448  19.440  1.00 47.88  ? 28  ASN B ND2 1 
ATOM   5218  N N   . ILE B 1 29  ? -6.039  31.364  17.512  1.00 40.46  ? 29  ILE B N   1 
ATOM   5219  C CA  . ILE B 1 29  ? -5.804  32.809  17.627  1.00 38.84  ? 29  ILE B CA  1 
ATOM   5220  C C   . ILE B 1 29  ? -6.175  33.521  16.316  1.00 38.61  ? 29  ILE B C   1 
ATOM   5221  O O   . ILE B 1 29  ? -6.862  34.559  16.322  1.00 38.13  ? 29  ILE B O   1 
ATOM   5222  C CB  . ILE B 1 29  ? -4.330  33.103  18.001  1.00 37.61  ? 29  ILE B CB  1 
ATOM   5223  C CG1 . ILE B 1 29  ? -4.013  32.504  19.385  1.00 36.67  ? 29  ILE B CG1 1 
ATOM   5224  C CG2 . ILE B 1 29  ? -4.072  34.600  18.026  1.00 36.61  ? 29  ILE B CG2 1 
ATOM   5225  C CD1 . ILE B 1 29  ? -2.539  32.307  19.637  1.00 36.51  ? 29  ILE B CD1 1 
ATOM   5226  N N   . ALA B 1 30  ? -5.756  32.929  15.198  1.00 36.21  ? 30  ALA B N   1 
ATOM   5227  C CA  . ALA B 1 30  ? -6.016  33.496  13.887  1.00 35.74  ? 30  ALA B CA  1 
ATOM   5228  C C   . ALA B 1 30  ? -7.506  33.456  13.563  1.00 34.73  ? 30  ALA B C   1 
ATOM   5229  O O   . ALA B 1 30  ? -8.049  34.399  13.002  1.00 36.28  ? 30  ALA B O   1 
ATOM   5230  C CB  . ALA B 1 30  ? -5.192  32.770  12.815  1.00 35.13  ? 30  ALA B CB  1 
ATOM   5231  N N   . LEU B 1 31  ? -8.168  32.370  13.939  1.00 34.51  ? 31  LEU B N   1 
ATOM   5232  C CA  . LEU B 1 31  ? -9.625  32.257  13.772  1.00 34.77  ? 31  LEU B CA  1 
ATOM   5233  C C   . LEU B 1 31  ? -10.361 33.361  14.519  1.00 34.70  ? 31  LEU B C   1 
ATOM   5234  O O   . LEU B 1 31  ? -11.344 33.920  14.018  1.00 34.33  ? 31  LEU B O   1 
ATOM   5235  C CB  . LEU B 1 31  ? -10.127 30.882  14.256  1.00 34.33  ? 31  LEU B CB  1 
ATOM   5236  C CG  . LEU B 1 31  ? -9.796  29.670  13.363  1.00 34.63  ? 31  LEU B CG  1 
ATOM   5237  C CD1 . LEU B 1 31  ? -10.168 28.359  14.062  1.00 36.73  ? 31  LEU B CD1 1 
ATOM   5238  C CD2 . LEU B 1 31  ? -10.462 29.764  11.996  1.00 32.35  ? 31  LEU B CD2 1 
ATOM   5239  N N   . LYS B 1 32  ? -9.875  33.663  15.722  1.00 34.48  ? 32  LYS B N   1 
ATOM   5240  C CA  . LYS B 1 32  ? -10.517 34.600  16.614  1.00 35.03  ? 32  LYS B CA  1 
ATOM   5241  C C   . LYS B 1 32  ? -10.406 35.968  15.962  1.00 34.53  ? 32  LYS B C   1 
ATOM   5242  O O   . LYS B 1 32  ? -11.409 36.635  15.719  1.00 34.70  ? 32  LYS B O   1 
ATOM   5243  C CB  . LYS B 1 32  ? -9.826  34.536  17.995  1.00 38.60  ? 32  LYS B CB  1 
ATOM   5244  C CG  . LYS B 1 32  ? -10.203 35.603  19.002  1.00 38.88  ? 32  LYS B CG  1 
ATOM   5245  C CD  . LYS B 1 32  ? -11.544 35.322  19.643  1.00 42.66  ? 32  LYS B CD  1 
ATOM   5246  C CE  . LYS B 1 32  ? -12.035 36.522  20.457  1.00 46.47  ? 32  LYS B CE  1 
ATOM   5247  N NZ  . LYS B 1 32  ? -13.522 36.670  20.399  1.00 47.73  ? 32  LYS B NZ  1 
ATOM   5248  N N   . ASN B 1 33  ? -9.187  36.321  15.573  1.00 33.94  ? 33  ASN B N   1 
ATOM   5249  C CA  . ASN B 1 33  ? -8.916  37.593  14.903  1.00 31.91  ? 33  ASN B CA  1 
ATOM   5250  C C   . ASN B 1 33  ? -9.709  37.786  13.627  1.00 32.22  ? 33  ASN B C   1 
ATOM   5251  O O   . ASN B 1 33  ? -10.158 38.884  13.355  1.00 33.70  ? 33  ASN B O   1 
ATOM   5252  C CB  . ASN B 1 33  ? -7.424  37.755  14.655  1.00 30.50  ? 33  ASN B CB  1 
ATOM   5253  C CG  . ASN B 1 33  ? -6.624  37.782  15.949  1.00 31.30  ? 33  ASN B CG  1 
ATOM   5254  O OD1 . ASN B 1 33  ? -7.161  38.114  17.013  1.00 31.58  ? 33  ASN B OD1 1 
ATOM   5255  N ND2 . ASN B 1 33  ? -5.341  37.423  15.870  1.00 30.01  ? 33  ASN B ND2 1 
ATOM   5256  N N   . PHE B 1 34  ? -9.895  36.715  12.855  1.00 32.38  ? 34  PHE B N   1 
ATOM   5257  C CA  . PHE B 1 34  ? -10.742 36.756  11.664  1.00 32.86  ? 34  PHE B CA  1 
ATOM   5258  C C   . PHE B 1 34  ? -12.176 37.208  11.999  1.00 33.33  ? 34  PHE B C   1 
ATOM   5259  O O   . PHE B 1 34  ? -12.660 38.220  11.479  1.00 33.52  ? 34  PHE B O   1 
ATOM   5260  C CB  . PHE B 1 34  ? -10.741 35.385  10.959  1.00 34.23  ? 34  PHE B CB  1 
ATOM   5261  C CG  . PHE B 1 34  ? -11.547 35.345  9.680   1.00 34.83  ? 34  PHE B CG  1 
ATOM   5262  C CD1 . PHE B 1 34  ? -11.610 36.449  8.832   1.00 35.95  ? 34  PHE B CD1 1 
ATOM   5263  C CD2 . PHE B 1 34  ? -12.197 34.177  9.297   1.00 36.18  ? 34  PHE B CD2 1 
ATOM   5264  C CE1 . PHE B 1 34  ? -12.350 36.402  7.651   1.00 36.55  ? 34  PHE B CE1 1 
ATOM   5265  C CE2 . PHE B 1 34  ? -12.923 34.119  8.118   1.00 35.71  ? 34  PHE B CE2 1 
ATOM   5266  C CZ  . PHE B 1 34  ? -13.008 35.232  7.297   1.00 35.83  ? 34  PHE B CZ  1 
ATOM   5267  N N   . ARG B 1 35  ? -12.842 36.463  12.875  1.00 32.87  ? 35  ARG B N   1 
ATOM   5268  C CA  . ARG B 1 35  ? -14.151 36.868  13.393  1.00 35.42  ? 35  ARG B CA  1 
ATOM   5269  C C   . ARG B 1 35  ? -14.154 38.340  13.859  1.00 34.51  ? 35  ARG B C   1 
ATOM   5270  O O   . ARG B 1 35  ? -15.069 39.089  13.529  1.00 35.94  ? 35  ARG B O   1 
ATOM   5271  C CB  . ARG B 1 35  ? -14.603 35.953  14.557  1.00 35.35  ? 35  ARG B CB  1 
ATOM   5272  C CG  . ARG B 1 35  ? -14.882 34.496  14.169  1.00 37.15  ? 35  ARG B CG  1 
ATOM   5273  C CD  . ARG B 1 35  ? -15.571 33.733  15.307  1.00 39.79  ? 35  ARG B CD  1 
ATOM   5274  N NE  . ARG B 1 35  ? -14.748 33.630  16.524  1.00 41.28  ? 35  ARG B NE  1 
ATOM   5275  C CZ  . ARG B 1 35  ? -13.894 32.633  16.782  1.00 45.31  ? 35  ARG B CZ  1 
ATOM   5276  N NH1 . ARG B 1 35  ? -13.731 31.636  15.914  1.00 48.52  ? 35  ARG B NH1 1 
ATOM   5277  N NH2 . ARG B 1 35  ? -13.197 32.625  17.910  1.00 45.74  ? 35  ARG B NH2 1 
ATOM   5278  N N   . LEU B 1 36  ? -13.136 38.727  14.636  1.00 33.02  ? 36  LEU B N   1 
ATOM   5279  C CA  . LEU B 1 36  ? -13.020 40.087  15.162  1.00 32.52  ? 36  LEU B CA  1 
ATOM   5280  C C   . LEU B 1 36  ? -12.929 41.116  14.051  1.00 32.71  ? 36  LEU B C   1 
ATOM   5281  O O   . LEU B 1 36  ? -13.535 42.179  14.134  1.00 33.04  ? 36  LEU B O   1 
ATOM   5282  C CB  . LEU B 1 36  ? -11.809 40.195  16.082  1.00 32.33  ? 36  LEU B CB  1 
ATOM   5283  C CG  . LEU B 1 36  ? -11.980 40.381  17.605  1.00 34.29  ? 36  LEU B CG  1 
ATOM   5284  C CD1 . LEU B 1 36  ? -13.255 39.804  18.212  1.00 32.97  ? 36  LEU B CD1 1 
ATOM   5285  C CD2 . LEU B 1 36  ? -10.738 39.933  18.368  1.00 32.86  ? 36  LEU B CD2 1 
ATOM   5286  N N   . CYS B 1 37  ? -12.163 40.799  13.006  1.00 32.25  ? 37  CYS B N   1 
ATOM   5287  C CA  . CYS B 1 37  ? -12.009 41.691  11.861  1.00 33.19  ? 37  CYS B CA  1 
ATOM   5288  C C   . CYS B 1 37  ? -13.356 41.907  11.139  1.00 33.99  ? 37  CYS B C   1 
ATOM   5289  O O   . CYS B 1 37  ? -13.733 43.052  10.821  1.00 31.39  ? 37  CYS B O   1 
ATOM   5290  C CB  . CYS B 1 37  ? -10.945 41.144  10.898  1.00 34.03  ? 37  CYS B CB  1 
ATOM   5291  S SG  . CYS B 1 37  ? -10.522 42.227  9.524   1.00 38.21  ? 37  CYS B SG  1 
ATOM   5292  N N   . LYS B 1 38  ? -14.080 40.809  10.908  1.00 34.59  ? 38  LYS B N   1 
ATOM   5293  C CA  . LYS B 1 38  ? -15.376 40.874  10.240  1.00 36.49  ? 38  LYS B CA  1 
ATOM   5294  C C   . LYS B 1 38  ? -16.392 41.699  11.035  1.00 37.76  ? 38  LYS B C   1 
ATOM   5295  O O   . LYS B 1 38  ? -17.207 42.411  10.451  1.00 38.73  ? 38  LYS B O   1 
ATOM   5296  C CB  . LYS B 1 38  ? -15.918 39.466  9.962   1.00 37.26  ? 38  LYS B CB  1 
ATOM   5297  C CG  . LYS B 1 38  ? -15.190 38.741  8.831   1.00 37.02  ? 38  LYS B CG  1 
ATOM   5298  C CD  . LYS B 1 38  ? -15.855 37.417  8.513   1.00 37.65  ? 38  LYS B CD  1 
ATOM   5299  C CE  . LYS B 1 38  ? -15.454 36.344  9.511   1.00 38.22  ? 38  LYS B CE  1 
ATOM   5300  N NZ  . LYS B 1 38  ? -16.032 35.041  9.095   1.00 38.96  ? 38  LYS B NZ  1 
ATOM   5301  N N   . LYS B 1 39  ? -16.313 41.627  12.362  1.00 37.29  ? 39  LYS B N   1 
ATOM   5302  C CA  . LYS B 1 39  ? -17.202 42.394  13.229  1.00 38.47  ? 39  LYS B CA  1 
ATOM   5303  C C   . LYS B 1 39  ? -16.895 43.891  13.245  1.00 37.94  ? 39  LYS B C   1 
ATOM   5304  O O   . LYS B 1 39  ? -17.762 44.700  13.553  1.00 39.18  ? 39  LYS B O   1 
ATOM   5305  C CB  . LYS B 1 39  ? -17.164 41.843  14.647  1.00 40.46  ? 39  LYS B CB  1 
ATOM   5306  C CG  . LYS B 1 39  ? -17.855 40.505  14.812  1.00 43.44  ? 39  LYS B CG  1 
ATOM   5307  C CD  . LYS B 1 39  ? -17.673 39.961  16.223  1.00 47.24  ? 39  LYS B CD  1 
ATOM   5308  C CE  . LYS B 1 39  ? -18.305 38.583  16.378  1.00 50.96  ? 39  LYS B CE  1 
ATOM   5309  N NZ  . LYS B 1 39  ? -17.709 37.823  17.515  1.00 53.86  ? 39  LYS B NZ  1 
ATOM   5310  N N   . HIS B 1 40  ? -15.662 44.253  12.921  1.00 38.13  ? 40  HIS B N   1 
ATOM   5311  C CA  . HIS B 1 40  ? -15.230 45.641  12.962  1.00 39.25  ? 40  HIS B CA  1 
ATOM   5312  C C   . HIS B 1 40  ? -15.612 46.439  11.741  1.00 42.59  ? 40  HIS B C   1 
ATOM   5313  O O   . HIS B 1 40  ? -15.111 46.210  10.655  1.00 42.38  ? 40  HIS B O   1 
ATOM   5314  C CB  . HIS B 1 40  ? -13.731 45.722  13.185  1.00 37.18  ? 40  HIS B CB  1 
ATOM   5315  C CG  . HIS B 1 40  ? -13.216 47.136  13.307  1.00 39.13  ? 40  HIS B CG  1 
ATOM   5316  N ND1 . HIS B 1 40  ? -12.077 47.550  12.711  1.00 38.84  ? 40  HIS B ND1 1 
ATOM   5317  C CD2 . HIS B 1 40  ? -13.760 48.265  13.941  1.00 37.60  ? 40  HIS B CD2 1 
ATOM   5318  C CE1 . HIS B 1 40  ? -11.878 48.854  12.987  1.00 36.61  ? 40  HIS B CE1 1 
ATOM   5319  N NE2 . HIS B 1 40  ? -12.915 49.288  13.729  1.00 37.32  ? 40  HIS B NE2 1 
ATOM   5320  N N   . LYS B 1 41  ? -16.479 47.423  11.932  1.00 50.36  ? 41  LYS B N   1 
ATOM   5321  C CA  . LYS B 1 41  ? -16.895 48.314  10.854  1.00 54.70  ? 41  LYS B CA  1 
ATOM   5322  C C   . LYS B 1 41  ? -16.048 49.584  10.868  1.00 57.88  ? 41  LYS B C   1 
ATOM   5323  O O   . LYS B 1 41  ? -16.296 50.499  11.657  1.00 60.16  ? 41  LYS B O   1 
ATOM   5324  C CB  . LYS B 1 41  ? -18.389 48.676  10.987  1.00 57.78  ? 41  LYS B CB  1 
ATOM   5325  C CG  . LYS B 1 41  ? -19.304 47.543  11.447  1.00 59.16  ? 41  LYS B CG  1 
ATOM   5326  C CD  . LYS B 1 41  ? -19.543 46.526  10.335  1.00 63.49  ? 41  LYS B CD  1 
ATOM   5327  C CE  . LYS B 1 41  ? -20.405 45.365  10.813  1.00 64.60  ? 41  LYS B CE  1 
ATOM   5328  N NZ  . LYS B 1 41  ? -20.478 44.280  9.794   1.00 62.75  ? 41  LYS B NZ  1 
ATOM   5329  N N   . THR B 1 42  ? -15.023 49.606  10.026  1.00 61.62  ? 42  THR B N   1 
ATOM   5330  C CA  . THR B 1 42  ? -14.311 50.831  9.689   1.00 67.75  ? 42  THR B CA  1 
ATOM   5331  C C   . THR B 1 42  ? -14.744 51.342  8.328   1.00 74.33  ? 42  THR B C   1 
ATOM   5332  O O   . THR B 1 42  ? -14.938 50.560  7.389   1.00 69.36  ? 42  THR B O   1 
ATOM   5333  C CB  . THR B 1 42  ? -12.790 50.615  9.599   1.00 68.49  ? 42  THR B CB  1 
ATOM   5334  O OG1 . THR B 1 42  ? -12.504 49.227  9.365   1.00 62.06  ? 42  THR B OG1 1 
ATOM   5335  C CG2 . THR B 1 42  ? -12.109 51.088  10.868  1.00 70.09  ? 42  THR B CG2 1 
ATOM   5336  N N   . LYS B 1 43  ? -14.878 52.662  8.221   1.00 82.21  ? 43  LYS B N   1 
ATOM   5337  C CA  . LYS B 1 43  ? -14.970 53.322  6.919   1.00 88.31  ? 43  LYS B CA  1 
ATOM   5338  C C   . LYS B 1 43  ? -13.560 53.545  6.343   1.00 86.41  ? 43  LYS B C   1 
ATOM   5339  O O   . LYS B 1 43  ? -13.395 54.210  5.321   1.00 85.48  ? 43  LYS B O   1 
ATOM   5340  C CB  . LYS B 1 43  ? -15.756 54.639  7.026   1.00 92.29  ? 43  LYS B CB  1 
ATOM   5341  C CG  . LYS B 1 43  ? -17.251 54.440  7.254   1.00 94.28  ? 43  LYS B CG  1 
ATOM   5342  C CD  . LYS B 1 43  ? -18.026 55.743  7.130   1.00 95.89  ? 43  LYS B CD  1 
ATOM   5343  C CE  . LYS B 1 43  ? -19.522 55.500  7.260   1.00 97.01  ? 43  LYS B CE  1 
ATOM   5344  N NZ  . LYS B 1 43  ? -20.312 56.754  7.112   1.00 96.72  ? 43  LYS B NZ  1 
ATOM   5345  N N   . LYS B 1 44  ? -12.561 52.975  7.024   1.00 83.20  ? 44  LYS B N   1 
ATOM   5346  C CA  . LYS B 1 44  ? -11.184 52.896  6.538   1.00 78.87  ? 44  LYS B CA  1 
ATOM   5347  C C   . LYS B 1 44  ? -11.039 51.762  5.498   1.00 73.99  ? 44  LYS B C   1 
ATOM   5348  O O   . LYS B 1 44  ? -11.172 50.585  5.839   1.00 73.74  ? 44  LYS B O   1 
ATOM   5349  C CB  . LYS B 1 44  ? -10.228 52.676  7.725   1.00 80.58  ? 44  LYS B CB  1 
ATOM   5350  C CG  . LYS B 1 44  ? -8.779  52.397  7.344   1.00 82.56  ? 44  LYS B CG  1 
ATOM   5351  C CD  . LYS B 1 44  ? -7.853  52.395  8.555   1.00 88.32  ? 44  LYS B CD  1 
ATOM   5352  C CE  . LYS B 1 44  ? -7.565  50.984  9.063   1.00 90.11  ? 44  LYS B CE  1 
ATOM   5353  N NZ  . LYS B 1 44  ? -8.672  50.416  9.888   1.00 89.61  ? 44  LYS B NZ  1 
ATOM   5354  N N   . PRO B 1 45  ? -10.767 52.121  4.227   1.00 69.36  ? 45  PRO B N   1 
ATOM   5355  C CA  . PRO B 1 45  ? -10.648 51.162  3.120   1.00 65.44  ? 45  PRO B CA  1 
ATOM   5356  C C   . PRO B 1 45  ? -9.837  49.896  3.438   1.00 59.97  ? 45  PRO B C   1 
ATOM   5357  O O   . PRO B 1 45  ? -8.838  49.936  4.164   1.00 56.00  ? 45  PRO B O   1 
ATOM   5358  C CB  . PRO B 1 45  ? -9.958  51.979  2.029   1.00 64.99  ? 45  PRO B CB  1 
ATOM   5359  C CG  . PRO B 1 45  ? -10.451 53.364  2.258   1.00 70.29  ? 45  PRO B CG  1 
ATOM   5360  C CD  . PRO B 1 45  ? -10.639 53.513  3.750   1.00 71.30  ? 45  PRO B CD  1 
ATOM   5361  N N   . VAL B 1 46  ? -10.269 48.794  2.845   1.00 55.06  ? 46  VAL B N   1 
ATOM   5362  C CA  . VAL B 1 46  ? -9.753  47.470  3.142   1.00 52.15  ? 46  VAL B CA  1 
ATOM   5363  C C   . VAL B 1 46  ? -8.506  47.101  2.292   1.00 51.76  ? 46  VAL B C   1 
ATOM   5364  O O   . VAL B 1 46  ? -8.569  47.096  1.041   1.00 53.48  ? 46  VAL B O   1 
ATOM   5365  C CB  . VAL B 1 46  ? -10.894 46.434  2.984   1.00 47.25  ? 46  VAL B CB  1 
ATOM   5366  C CG1 . VAL B 1 46  ? -10.352 45.034  2.733   1.00 43.37  ? 46  VAL B CG1 1 
ATOM   5367  C CG2 . VAL B 1 46  ? -11.781 46.468  4.214   1.00 44.71  ? 46  VAL B CG2 1 
ATOM   5368  N N   . GLN B 1 47  ? -7.378  46.842  2.972   1.00 46.34  ? 47  GLN B N   1 
ATOM   5369  C CA  . GLN B 1 47  ? -6.186  46.241  2.330   1.00 47.20  ? 47  GLN B CA  1 
ATOM   5370  C C   . GLN B 1 47  ? -5.909  44.818  2.890   1.00 44.01  ? 47  GLN B C   1 
ATOM   5371  O O   . GLN B 1 47  ? -5.443  44.659  4.019   1.00 42.57  ? 47  GLN B O   1 
ATOM   5372  C CB  . GLN B 1 47  ? -4.940  47.130  2.498   1.00 50.99  ? 47  GLN B CB  1 
ATOM   5373  C CG  . GLN B 1 47  ? -4.830  48.341  1.562   1.00 58.37  ? 47  GLN B CG  1 
ATOM   5374  C CD  . GLN B 1 47  ? -4.096  48.052  0.240   1.00 60.09  ? 47  GLN B CD  1 
ATOM   5375  O OE1 . GLN B 1 47  ? -4.639  47.413  -0.661  1.00 66.09  ? 47  GLN B OE1 1 
ATOM   5376  N NE2 . GLN B 1 47  ? -2.880  48.575  0.107   1.00 59.51  ? 47  GLN B NE2 1 
ATOM   5377  N N   . ILE B 1 48  ? -6.187  43.796  2.096   1.00 40.39  ? 48  ILE B N   1 
ATOM   5378  C CA  . ILE B 1 48  ? -6.132  42.422  2.599   1.00 38.43  ? 48  ILE B CA  1 
ATOM   5379  C C   . ILE B 1 48  ? -4.801  42.016  3.240   1.00 36.63  ? 48  ILE B C   1 
ATOM   5380  O O   . ILE B 1 48  ? -4.796  41.407  4.314   1.00 35.93  ? 48  ILE B O   1 
ATOM   5381  C CB  . ILE B 1 48  ? -6.609  41.395  1.545   1.00 36.31  ? 48  ILE B CB  1 
ATOM   5382  C CG1 . ILE B 1 48  ? -8.117  41.265  1.629   1.00 38.70  ? 48  ILE B CG1 1 
ATOM   5383  C CG2 . ILE B 1 48  ? -6.017  40.016  1.803   1.00 33.34  ? 48  ILE B CG2 1 
ATOM   5384  C CD1 . ILE B 1 48  ? -8.859  42.444  1.079   1.00 39.72  ? 48  ILE B CD1 1 
ATOM   5385  N N   . LEU B 1 49  ? -3.683  42.354  2.605   1.00 35.84  ? 49  LEU B N   1 
ATOM   5386  C CA  . LEU B 1 49  ? -2.371  41.959  3.146   1.00 37.94  ? 49  LEU B CA  1 
ATOM   5387  C C   . LEU B 1 49  ? -2.154  42.524  4.538   1.00 39.15  ? 49  LEU B C   1 
ATOM   5388  O O   . LEU B 1 49  ? -1.782  41.791  5.468   1.00 39.08  ? 49  LEU B O   1 
ATOM   5389  C CB  . LEU B 1 49  ? -1.211  42.377  2.224   1.00 37.61  ? 49  LEU B CB  1 
ATOM   5390  C CG  . LEU B 1 49  ? -1.163  41.769  0.817   1.00 37.64  ? 49  LEU B CG  1 
ATOM   5391  C CD1 . LEU B 1 49  ? -0.124  42.490  -0.044  1.00 38.90  ? 49  LEU B CD1 1 
ATOM   5392  C CD2 . LEU B 1 49  ? -0.916  40.264  0.830   1.00 34.41  ? 49  LEU B CD2 1 
ATOM   5393  N N   . ALA B 1 50  ? -2.423  43.823  4.688   1.00 37.57  ? 50  ALA B N   1 
ATOM   5394  C CA  . ALA B 1 50  ? -2.243  44.501  5.970   1.00 36.49  ? 50  ALA B CA  1 
ATOM   5395  C C   . ALA B 1 50  ? -3.162  43.919  7.042   1.00 36.95  ? 50  ALA B C   1 
ATOM   5396  O O   . ALA B 1 50  ? -2.792  43.846  8.218   1.00 38.98  ? 50  ALA B O   1 
ATOM   5397  C CB  . ALA B 1 50  ? -2.475  46.007  5.814   1.00 34.78  ? 50  ALA B CB  1 
ATOM   5398  N N   . LEU B 1 51  ? -4.357  43.508  6.631   1.00 34.51  ? 51  LEU B N   1 
ATOM   5399  C CA  . LEU B 1 51  ? -5.373  43.036  7.559   1.00 35.37  ? 51  LEU B CA  1 
ATOM   5400  C C   . LEU B 1 51  ? -4.987  41.647  8.059   1.00 34.85  ? 51  LEU B C   1 
ATOM   5401  O O   . LEU B 1 51  ? -5.064  41.355  9.260   1.00 36.17  ? 51  LEU B O   1 
ATOM   5402  C CB  . LEU B 1 51  ? -6.716  42.973  6.849   1.00 35.87  ? 51  LEU B CB  1 
ATOM   5403  C CG  . LEU B 1 51  ? -7.976  43.560  7.468   1.00 37.86  ? 51  LEU B CG  1 
ATOM   5404  C CD1 . LEU B 1 51  ? -7.731  44.929  8.112   1.00 37.87  ? 51  LEU B CD1 1 
ATOM   5405  C CD2 . LEU B 1 51  ? -9.077  43.629  6.403   1.00 36.39  ? 51  LEU B CD2 1 
ATOM   5406  N N   . LEU B 1 52  ? -4.544  40.809  7.123   1.00 33.65  ? 52  LEU B N   1 
ATOM   5407  C CA  . LEU B 1 52  ? -4.106  39.453  7.416   1.00 31.82  ? 52  LEU B CA  1 
ATOM   5408  C C   . LEU B 1 52  ? -2.899  39.424  8.364   1.00 30.79  ? 52  LEU B C   1 
ATOM   5409  O O   . LEU B 1 52  ? -2.765  38.512  9.181   1.00 28.25  ? 52  LEU B O   1 
ATOM   5410  C CB  . LEU B 1 52  ? -3.774  38.723  6.119   1.00 30.29  ? 52  LEU B CB  1 
ATOM   5411  C CG  . LEU B 1 52  ? -4.661  37.571  5.634   1.00 31.88  ? 52  LEU B CG  1 
ATOM   5412  C CD1 . LEU B 1 52  ? -6.061  37.615  6.199   1.00 31.12  ? 52  LEU B CD1 1 
ATOM   5413  C CD2 . LEU B 1 52  ? -4.680  37.537  4.101   1.00 30.04  ? 52  LEU B CD2 1 
ATOM   5414  N N   . GLN B 1 53  ? -2.029  40.425  8.250   1.00 31.14  ? 53  GLN B N   1 
ATOM   5415  C CA  . GLN B 1 53  ? -0.851  40.490  9.119   1.00 33.38  ? 53  GLN B CA  1 
ATOM   5416  C C   . GLN B 1 53  ? -1.198  40.875  10.582  1.00 33.66  ? 53  GLN B C   1 
ATOM   5417  O O   . GLN B 1 53  ? -0.354  40.779  11.469  1.00 35.84  ? 53  GLN B O   1 
ATOM   5418  C CB  . GLN B 1 53  ? 0.230   41.385  8.513   1.00 32.86  ? 53  GLN B CB  1 
ATOM   5419  C CG  . GLN B 1 53  ? 0.987   40.704  7.378   1.00 34.86  ? 53  GLN B CG  1 
ATOM   5420  C CD  . GLN B 1 53  ? 1.772   41.676  6.513   1.00 35.33  ? 53  GLN B CD  1 
ATOM   5421  O OE1 . GLN B 1 53  ? 2.525   42.503  7.014   1.00 38.50  ? 53  GLN B OE1 1 
ATOM   5422  N NE2 . GLN B 1 53  ? 1.613   41.562  5.211   1.00 36.40  ? 53  GLN B NE2 1 
ATOM   5423  N N   . GLU B 1 54  ? -2.447  41.259  10.822  1.00 32.10  ? 54  GLU B N   1 
ATOM   5424  C CA  . GLU B 1 54  ? -2.953  41.395  12.186  1.00 34.17  ? 54  GLU B CA  1 
ATOM   5425  C C   . GLU B 1 54  ? -3.673  40.137  12.631  1.00 33.00  ? 54  GLU B C   1 
ATOM   5426  O O   . GLU B 1 54  ? -3.677  39.793  13.824  1.00 31.54  ? 54  GLU B O   1 
ATOM   5427  C CB  . GLU B 1 54  ? -3.879  42.591  12.289  1.00 35.47  ? 54  GLU B CB  1 
ATOM   5428  C CG  . GLU B 1 54  ? -3.191  43.881  11.914  1.00 37.82  ? 54  GLU B CG  1 
ATOM   5429  C CD  . GLU B 1 54  ? -4.151  45.000  11.709  1.00 41.51  ? 54  GLU B CD  1 
ATOM   5430  O OE1 . GLU B 1 54  ? -5.370  44.728  11.666  1.00 45.18  ? 54  GLU B OE1 1 
ATOM   5431  O OE2 . GLU B 1 54  ? -3.689  46.154  11.586  1.00 44.64  ? 54  GLU B OE2 1 
ATOM   5432  N N   . ILE B 1 55  ? -4.263  39.444  11.657  1.00 30.74  ? 55  ILE B N   1 
ATOM   5433  C CA  . ILE B 1 55  ? -5.063  38.263  11.912  1.00 29.91  ? 55  ILE B CA  1 
ATOM   5434  C C   . ILE B 1 55  ? -4.192  37.041  12.206  1.00 30.69  ? 55  ILE B C   1 
ATOM   5435  O O   . ILE B 1 55  ? -4.348  36.415  13.245  1.00 32.43  ? 55  ILE B O   1 
ATOM   5436  C CB  . ILE B 1 55  ? -6.075  38.023  10.761  1.00 29.31  ? 55  ILE B CB  1 
ATOM   5437  C CG1 . ILE B 1 55  ? -7.200  39.064  10.826  1.00 28.27  ? 55  ILE B CG1 1 
ATOM   5438  C CG2 . ILE B 1 55  ? -6.662  36.625  10.802  1.00 28.10  ? 55  ILE B CG2 1 
ATOM   5439  C CD1 . ILE B 1 55  ? -7.868  39.302  9.492   1.00 26.60  ? 55  ILE B CD1 1 
ATOM   5440  N N   . ILE B 1 56  ? -3.267  36.701  11.306  1.00 31.39  ? 56  ILE B N   1 
ATOM   5441  C CA  . ILE B 1 56  ? -2.352  35.591  11.564  1.00 31.37  ? 56  ILE B CA  1 
ATOM   5442  C C   . ILE B 1 56  ? -1.186  36.137  12.374  1.00 31.52  ? 56  ILE B C   1 
ATOM   5443  O O   . ILE B 1 56  ? -0.439  36.951  11.881  1.00 32.65  ? 56  ILE B O   1 
ATOM   5444  C CB  . ILE B 1 56  ? -1.834  34.928  10.261  1.00 31.27  ? 56  ILE B CB  1 
ATOM   5445  C CG1 . ILE B 1 56  ? -2.990  34.616  9.302   1.00 31.93  ? 56  ILE B CG1 1 
ATOM   5446  C CG2 . ILE B 1 56  ? -1.072  33.638  10.573  1.00 30.18  ? 56  ILE B CG2 1 
ATOM   5447  C CD1 . ILE B 1 56  ? -2.544  34.111  7.931   1.00 30.94  ? 56  ILE B CD1 1 
ATOM   5448  N N   . PRO B 1 57  ? -1.026  35.691  13.626  1.00 32.85  ? 57  PRO B N   1 
ATOM   5449  C CA  . PRO B 1 57  ? 0.013   36.312  14.462  1.00 33.63  ? 57  PRO B CA  1 
ATOM   5450  C C   . PRO B 1 57  ? 1.393   35.934  13.978  1.00 33.83  ? 57  PRO B C   1 
ATOM   5451  O O   . PRO B 1 57  ? 1.586   34.822  13.479  1.00 33.82  ? 57  PRO B O   1 
ATOM   5452  C CB  . PRO B 1 57  ? -0.244  35.707  15.842  1.00 34.27  ? 57  PRO B CB  1 
ATOM   5453  C CG  . PRO B 1 57  ? -0.840  34.377  15.559  1.00 33.68  ? 57  PRO B CG  1 
ATOM   5454  C CD  . PRO B 1 57  ? -1.576  34.473  14.242  1.00 33.06  ? 57  PRO B CD  1 
ATOM   5455  N N   . LYS B 1 58  ? 2.354   36.835  14.135  1.00 35.19  ? 58  LYS B N   1 
ATOM   5456  C CA  . LYS B 1 58  ? 3.674   36.609  13.557  1.00 36.65  ? 58  LYS B CA  1 
ATOM   5457  C C   . LYS B 1 58  ? 4.327   35.363  14.117  1.00 37.96  ? 58  LYS B C   1 
ATOM   5458  O O   . LYS B 1 58  ? 5.169   34.738  13.460  1.00 38.74  ? 58  LYS B O   1 
ATOM   5459  C CB  . LYS B 1 58  ? 4.600   37.797  13.763  1.00 37.53  ? 58  LYS B CB  1 
ATOM   5460  C CG  . LYS B 1 58  ? 5.855   37.668  12.927  1.00 36.72  ? 58  LYS B CG  1 
ATOM   5461  C CD  . LYS B 1 58  ? 6.946   38.616  13.357  1.00 37.94  ? 58  LYS B CD  1 
ATOM   5462  C CE  . LYS B 1 58  ? 8.133   38.473  12.416  1.00 39.39  ? 58  LYS B CE  1 
ATOM   5463  N NZ  . LYS B 1 58  ? 8.753   39.794  12.144  1.00 40.57  ? 58  LYS B NZ  1 
ATOM   5464  N N   . SER B 1 59  ? 3.941   35.004  15.334  1.00 37.35  ? 59  SER B N   1 
ATOM   5465  C CA  . SER B 1 59  ? 4.492   33.825  15.979  1.00 39.43  ? 59  SER B CA  1 
ATOM   5466  C C   . SER B 1 59  ? 4.201   32.535  15.186  1.00 38.54  ? 59  SER B C   1 
ATOM   5467  O O   . SER B 1 59  ? 4.891   31.536  15.359  1.00 40.20  ? 59  SER B O   1 
ATOM   5468  C CB  . SER B 1 59  ? 3.971   33.706  17.407  1.00 39.46  ? 59  SER B CB  1 
ATOM   5469  O OG  . SER B 1 59  ? 2.564   33.623  17.413  1.00 40.71  ? 59  SER B OG  1 
ATOM   5470  N N   . TYR B 1 60  ? 3.186   32.565  14.323  1.00 36.34  ? 60  TYR B N   1 
ATOM   5471  C CA  . TYR B 1 60  ? 2.939   31.435  13.428  1.00 35.66  ? 60  TYR B CA  1 
ATOM   5472  C C   . TYR B 1 60  ? 4.090   31.254  12.402  1.00 35.99  ? 60  TYR B C   1 
ATOM   5473  O O   . TYR B 1 60  ? 4.422   30.129  12.015  1.00 34.45  ? 60  TYR B O   1 
ATOM   5474  C CB  . TYR B 1 60  ? 1.556   31.534  12.736  1.00 33.56  ? 60  TYR B CB  1 
ATOM   5475  C CG  . TYR B 1 60  ? 1.383   30.464  11.692  1.00 33.46  ? 60  TYR B CG  1 
ATOM   5476  C CD1 . TYR B 1 60  ? 0.976   29.175  12.046  1.00 32.76  ? 60  TYR B CD1 1 
ATOM   5477  C CD2 . TYR B 1 60  ? 1.734   30.700  10.368  1.00 32.61  ? 60  TYR B CD2 1 
ATOM   5478  C CE1 . TYR B 1 60  ? 0.880   28.178  11.101  1.00 32.33  ? 60  TYR B CE1 1 
ATOM   5479  C CE2 . TYR B 1 60  ? 1.648   29.690  9.408   1.00 32.56  ? 60  TYR B CE2 1 
ATOM   5480  C CZ  . TYR B 1 60  ? 1.228   28.437  9.784   1.00 31.78  ? 60  TYR B CZ  1 
ATOM   5481  O OH  . TYR B 1 60  ? 1.124   27.450  8.841   1.00 32.59  ? 60  TYR B OH  1 
ATOM   5482  N N   . PHE B 1 61  ? 4.713   32.362  11.991  1.00 36.45  ? 61  PHE B N   1 
ATOM   5483  C CA  . PHE B 1 61  ? 5.816   32.300  11.028  1.00 36.59  ? 61  PHE B CA  1 
ATOM   5484  C C   . PHE B 1 61  ? 7.204   32.314  11.674  1.00 40.03  ? 61  PHE B C   1 
ATOM   5485  O O   . PHE B 1 61  ? 8.166   31.865  11.072  1.00 41.58  ? 61  PHE B O   1 
ATOM   5486  C CB  . PHE B 1 61  ? 5.703   33.421  9.997   1.00 34.78  ? 61  PHE B CB  1 
ATOM   5487  C CG  . PHE B 1 61  ? 4.407   33.408  9.230   1.00 34.44  ? 61  PHE B CG  1 
ATOM   5488  C CD1 . PHE B 1 61  ? 4.152   32.425  8.278   1.00 33.27  ? 61  PHE B CD1 1 
ATOM   5489  C CD2 . PHE B 1 61  ? 3.438   34.375  9.461   1.00 33.52  ? 61  PHE B CD2 1 
ATOM   5490  C CE1 . PHE B 1 61  ? 2.959   32.412  7.575   1.00 33.20  ? 61  PHE B CE1 1 
ATOM   5491  C CE2 . PHE B 1 61  ? 2.238   34.365  8.748   1.00 33.65  ? 61  PHE B CE2 1 
ATOM   5492  C CZ  . PHE B 1 61  ? 2.002   33.390  7.803   1.00 32.06  ? 61  PHE B CZ  1 
ATOM   5493  N N   . GLY B 1 62  ? 7.312   32.843  12.888  1.00 40.30  ? 62  GLY B N   1 
ATOM   5494  C CA  . GLY B 1 62  ? 8.610   32.921  13.552  1.00 42.48  ? 62  GLY B CA  1 
ATOM   5495  C C   . GLY B 1 62  ? 9.479   34.068  13.055  1.00 44.07  ? 62  GLY B C   1 
ATOM   5496  O O   . GLY B 1 62  ? 9.917   34.909  13.845  1.00 47.15  ? 62  GLY B O   1 
ATOM   5497  N N   . THR B 1 63  ? 9.729   34.112  11.748  1.00 44.50  ? 63  THR B N   1 
ATOM   5498  C CA  . THR B 1 63  ? 10.561  35.171  11.159  1.00 42.84  ? 63  THR B CA  1 
ATOM   5499  C C   . THR B 1 63  ? 9.881   35.906  10.014  1.00 42.45  ? 63  THR B C   1 
ATOM   5500  O O   . THR B 1 63  ? 8.963   35.387  9.353   1.00 40.82  ? 63  THR B O   1 
ATOM   5501  C CB  . THR B 1 63  ? 11.884  34.622  10.614  1.00 43.60  ? 63  THR B CB  1 
ATOM   5502  O OG1 . THR B 1 63  ? 11.607  33.665  9.589   1.00 45.16  ? 63  THR B OG1 1 
ATOM   5503  C CG2 . THR B 1 63  ? 12.706  33.966  11.720  1.00 43.47  ? 63  THR B CG2 1 
ATOM   5504  N N   . THR B 1 64  ? 10.369  37.112  9.761   1.00 41.90  ? 64  THR B N   1 
ATOM   5505  C CA  . THR B 1 64  ? 9.921   37.907  8.637   1.00 40.81  ? 64  THR B CA  1 
ATOM   5506  C C   . THR B 1 64  ? 10.114  37.173  7.304   1.00 39.51  ? 64  THR B C   1 
ATOM   5507  O O   . THR B 1 64  ? 9.299   37.301  6.401   1.00 39.98  ? 64  THR B O   1 
ATOM   5508  C CB  . THR B 1 64  ? 10.649  39.255  8.610   1.00 42.20  ? 64  THR B CB  1 
ATOM   5509  O OG1 . THR B 1 64  ? 10.678  39.794  9.937   1.00 44.29  ? 64  THR B OG1 1 
ATOM   5510  C CG2 . THR B 1 64  ? 9.940   40.236  7.684   1.00 42.96  ? 64  THR B CG2 1 
ATOM   5511  N N   . THR B 1 65  ? 11.177  36.389  7.192   1.00 40.11  ? 65  THR B N   1 
ATOM   5512  C CA  . THR B 1 65  ? 11.431  35.672  5.942   1.00 41.02  ? 65  THR B CA  1 
ATOM   5513  C C   . THR B 1 65  ? 10.359  34.626  5.672   1.00 38.70  ? 65  THR B C   1 
ATOM   5514  O O   . THR B 1 65  ? 9.819   34.593  4.580   1.00 38.47  ? 65  THR B O   1 
ATOM   5515  C CB  . THR B 1 65  ? 12.858  35.083  5.867   1.00 40.73  ? 65  THR B CB  1 
ATOM   5516  O OG1 . THR B 1 65  ? 13.796  36.152  5.992   1.00 42.39  ? 65  THR B OG1 1 
ATOM   5517  C CG2 . THR B 1 65  ? 13.097  34.413  4.530   1.00 38.99  ? 65  THR B CG2 1 
ATOM   5518  N N   . ASN B 1 66  ? 10.037  33.805  6.675   1.00 36.88  ? 66  ASN B N   1 
ATOM   5519  C CA  . ASN B 1 66  ? 8.918   32.875  6.566   1.00 36.94  ? 66  ASN B CA  1 
ATOM   5520  C C   . ASN B 1 66  ? 7.594   33.594  6.257   1.00 36.79  ? 66  ASN B C   1 
ATOM   5521  O O   . ASN B 1 66  ? 6.809   33.156  5.423   1.00 36.24  ? 66  ASN B O   1 
ATOM   5522  C CB  . ASN B 1 66  ? 8.760   32.058  7.850   1.00 38.11  ? 66  ASN B CB  1 
ATOM   5523  C CG  . ASN B 1 66  ? 9.891   31.065  8.066   1.00 39.48  ? 66  ASN B CG  1 
ATOM   5524  O OD1 . ASN B 1 66  ? 10.742  30.866  7.202   1.00 42.37  ? 66  ASN B OD1 1 
ATOM   5525  N ND2 . ASN B 1 66  ? 9.888   30.421  9.217   1.00 39.09  ? 66  ASN B ND2 1 
ATOM   5526  N N   . LEU B 1 67  ? 7.352   34.701  6.934   1.00 37.18  ? 67  LEU B N   1 
ATOM   5527  C CA  . LEU B 1 67  ? 6.111   35.408  6.749   1.00 37.51  ? 67  LEU B CA  1 
ATOM   5528  C C   . LEU B 1 67  ? 6.012   35.882  5.290   1.00 36.71  ? 67  LEU B C   1 
ATOM   5529  O O   . LEU B 1 67  ? 4.968   35.741  4.658   1.00 36.64  ? 67  LEU B O   1 
ATOM   5530  C CB  . LEU B 1 67  ? 5.997   36.571  7.756   1.00 36.91  ? 67  LEU B CB  1 
ATOM   5531  C CG  . LEU B 1 67  ? 4.824   37.553  7.630   1.00 36.60  ? 67  LEU B CG  1 
ATOM   5532  C CD1 . LEU B 1 67  ? 4.514   38.179  8.982   1.00 37.48  ? 67  LEU B CD1 1 
ATOM   5533  C CD2 . LEU B 1 67  ? 5.096   38.637  6.585   1.00 35.91  ? 67  LEU B CD2 1 
ATOM   5534  N N   . LYS B 1 68  ? 7.100   36.418  4.756   1.00 37.87  ? 68  LYS B N   1 
ATOM   5535  C CA  . LYS B 1 68  ? 7.084   36.929  3.382   1.00 42.35  ? 68  LYS B CA  1 
ATOM   5536  C C   . LYS B 1 68  ? 6.864   35.851  2.307   1.00 39.87  ? 68  LYS B C   1 
ATOM   5537  O O   . LYS B 1 68  ? 6.277   36.131  1.252   1.00 37.73  ? 68  LYS B O   1 
ATOM   5538  C CB  . LYS B 1 68  ? 8.318   37.790  3.076   1.00 46.49  ? 68  LYS B CB  1 
ATOM   5539  C CG  . LYS B 1 68  ? 8.041   39.280  3.224   1.00 50.57  ? 68  LYS B CG  1 
ATOM   5540  C CD  . LYS B 1 68  ? 9.277   40.095  3.562   1.00 53.14  ? 68  LYS B CD  1 
ATOM   5541  C CE  . LYS B 1 68  ? 8.876   41.528  3.895   1.00 56.72  ? 68  LYS B CE  1 
ATOM   5542  N NZ  . LYS B 1 68  ? 10.051  42.421  4.121   1.00 60.84  ? 68  LYS B NZ  1 
ATOM   5543  N N   . ARG B 1 69  ? 7.290   34.624  2.595   1.00 38.02  ? 69  ARG B N   1 
ATOM   5544  C CA  . ARG B 1 69  ? 7.053   33.510  1.684   1.00 37.86  ? 69  ARG B CA  1 
ATOM   5545  C C   . ARG B 1 69  ? 5.571   33.190  1.572   1.00 36.81  ? 69  ARG B C   1 
ATOM   5546  O O   . ARG B 1 69  ? 5.031   33.147  0.463   1.00 35.48  ? 69  ARG B O   1 
ATOM   5547  C CB  . ARG B 1 69  ? 7.844   32.264  2.102   1.00 42.43  ? 69  ARG B CB  1 
ATOM   5548  C CG  . ARG B 1 69  ? 9.344   32.346  1.854   1.00 45.16  ? 69  ARG B CG  1 
ATOM   5549  C CD  . ARG B 1 69  ? 10.035  30.989  2.015   1.00 48.95  ? 69  ARG B CD  1 
ATOM   5550  N NE  . ARG B 1 69  ? 9.492   29.989  1.100   1.00 52.04  ? 69  ARG B NE  1 
ATOM   5551  C CZ  . ARG B 1 69  ? 9.862   29.840  -0.181  1.00 56.32  ? 69  ARG B CZ  1 
ATOM   5552  N NH1 . ARG B 1 69  ? 10.789  30.647  -0.714  1.00 51.23  ? 69  ARG B NH1 1 
ATOM   5553  N NH2 . ARG B 1 69  ? 9.293   28.881  -0.938  1.00 50.85  ? 69  ARG B NH2 1 
ATOM   5554  N N   . PHE B 1 70  ? 4.910   32.987  2.718   1.00 34.67  ? 70  PHE B N   1 
ATOM   5555  C CA  . PHE B 1 70  ? 3.466   32.704  2.743   1.00 33.09  ? 70  PHE B CA  1 
ATOM   5556  C C   . PHE B 1 70  ? 2.682   33.762  1.970   1.00 32.04  ? 70  PHE B C   1 
ATOM   5557  O O   . PHE B 1 70  ? 1.784   33.430  1.182   1.00 34.44  ? 70  PHE B O   1 
ATOM   5558  C CB  . PHE B 1 70  ? 2.957   32.589  4.207   1.00 32.20  ? 70  PHE B CB  1 
ATOM   5559  C CG  . PHE B 1 70  ? 1.478   32.295  4.339   1.00 30.76  ? 70  PHE B CG  1 
ATOM   5560  C CD1 . PHE B 1 70  ? 0.996   30.990  4.247   1.00 31.70  ? 70  PHE B CD1 1 
ATOM   5561  C CD2 . PHE B 1 70  ? 0.564   33.321  4.598   1.00 30.34  ? 70  PHE B CD2 1 
ATOM   5562  C CE1 . PHE B 1 70  ? -0.368  30.722  4.379   1.00 30.67  ? 70  PHE B CE1 1 
ATOM   5563  C CE2 . PHE B 1 70  ? -0.796  33.049  4.745   1.00 27.90  ? 70  PHE B CE2 1 
ATOM   5564  C CZ  . PHE B 1 70  ? -1.257  31.757  4.631   1.00 29.42  ? 70  PHE B CZ  1 
ATOM   5565  N N   . TYR B 1 71  ? 3.024   35.025  2.193   1.00 29.62  ? 71  TYR B N   1 
ATOM   5566  C CA  . TYR B 1 71  ? 2.240   36.137  1.666   1.00 30.42  ? 71  TYR B CA  1 
ATOM   5567  C C   . TYR B 1 71  ? 2.433   36.383  0.165   1.00 30.74  ? 71  TYR B C   1 
ATOM   5568  O O   . TYR B 1 71  ? 1.565   36.943  -0.485  1.00 32.27  ? 71  TYR B O   1 
ATOM   5569  C CB  . TYR B 1 71  ? 2.462   37.430  2.498   1.00 29.50  ? 71  TYR B CB  1 
ATOM   5570  C CG  . TYR B 1 71  ? 1.663   37.456  3.789   1.00 31.32  ? 71  TYR B CG  1 
ATOM   5571  C CD1 . TYR B 1 71  ? 0.316   37.780  3.784   1.00 32.40  ? 71  TYR B CD1 1 
ATOM   5572  C CD2 . TYR B 1 71  ? 2.247   37.100  5.015   1.00 31.82  ? 71  TYR B CD2 1 
ATOM   5573  C CE1 . TYR B 1 71  ? -0.430  37.776  4.965   1.00 33.56  ? 71  TYR B CE1 1 
ATOM   5574  C CE2 . TYR B 1 71  ? 1.507   37.080  6.193   1.00 31.99  ? 71  TYR B CE2 1 
ATOM   5575  C CZ  . TYR B 1 71  ? 0.168   37.425  6.159   1.00 33.48  ? 71  TYR B CZ  1 
ATOM   5576  O OH  . TYR B 1 71  ? -0.580  37.457  7.326   1.00 34.90  ? 71  TYR B OH  1 
ATOM   5577  N N   . LYS B 1 72  ? 3.551   35.949  -0.397  1.00 33.02  ? 72  LYS B N   1 
ATOM   5578  C CA  . LYS B 1 72  ? 3.650   35.909  -1.862  1.00 34.81  ? 72  LYS B CA  1 
ATOM   5579  C C   . LYS B 1 72  ? 2.537   35.027  -2.458  1.00 34.22  ? 72  LYS B C   1 
ATOM   5580  O O   . LYS B 1 72  ? 2.008   35.340  -3.537  1.00 33.04  ? 72  LYS B O   1 
ATOM   5581  C CB  . LYS B 1 72  ? 5.045   35.455  -2.339  1.00 36.81  ? 72  LYS B CB  1 
ATOM   5582  C CG  . LYS B 1 72  ? 6.140   36.518  -2.216  1.00 41.18  ? 72  LYS B CG  1 
ATOM   5583  C CD  . LYS B 1 72  ? 6.030   37.625  -3.279  1.00 46.13  ? 72  LYS B CD  1 
ATOM   5584  C CE  . LYS B 1 72  ? 5.257   38.864  -2.794  1.00 50.68  ? 72  LYS B CE  1 
ATOM   5585  N NZ  . LYS B 1 72  ? 4.708   39.688  -3.926  1.00 50.61  ? 72  LYS B NZ  1 
ATOM   5586  N N   . VAL B 1 73  ? 2.166   33.949  -1.757  1.00 30.09  ? 73  VAL B N   1 
ATOM   5587  C CA  . VAL B 1 73  ? 1.034   33.145  -2.207  1.00 31.61  ? 73  VAL B CA  1 
ATOM   5588  C C   . VAL B 1 73  ? -0.289  33.925  -2.133  1.00 32.04  ? 73  VAL B C   1 
ATOM   5589  O O   . VAL B 1 73  ? -1.103  33.909  -3.092  1.00 31.04  ? 73  VAL B O   1 
ATOM   5590  C CB  . VAL B 1 73  ? 0.872   31.860  -1.381  1.00 31.45  ? 73  VAL B CB  1 
ATOM   5591  C CG1 . VAL B 1 73  ? -0.388  31.148  -1.838  1.00 29.59  ? 73  VAL B CG1 1 
ATOM   5592  C CG2 . VAL B 1 73  ? 2.123   30.973  -1.516  1.00 30.42  ? 73  VAL B CG2 1 
ATOM   5593  N N   . VAL B 1 74  ? -0.489  34.595  -0.993  1.00 29.03  ? 74  VAL B N   1 
ATOM   5594  C CA  . VAL B 1 74  ? -1.645  35.433  -0.769  1.00 29.81  ? 74  VAL B CA  1 
ATOM   5595  C C   . VAL B 1 74  ? -1.698  36.477  -1.860  1.00 31.81  ? 74  VAL B C   1 
ATOM   5596  O O   . VAL B 1 74  ? -2.766  36.737  -2.448  1.00 35.09  ? 74  VAL B O   1 
ATOM   5597  C CB  . VAL B 1 74  ? -1.634  36.128  0.630   1.00 29.87  ? 74  VAL B CB  1 
ATOM   5598  C CG1 . VAL B 1 74  ? -2.849  37.047  0.765   1.00 27.57  ? 74  VAL B CG1 1 
ATOM   5599  C CG2 . VAL B 1 74  ? -1.607  35.089  1.774   1.00 26.98  ? 74  VAL B CG2 1 
ATOM   5600  N N   . GLU B 1 75  ? -0.551  37.055  -2.159  1.00 31.28  ? 75  GLU B N   1 
ATOM   5601  C CA  . GLU B 1 75  ? -0.475  38.025  -3.218  1.00 34.66  ? 75  GLU B CA  1 
ATOM   5602  C C   . GLU B 1 75  ? -0.908  37.425  -4.584  1.00 33.52  ? 75  GLU B C   1 
ATOM   5603  O O   . GLU B 1 75  ? -1.572  38.089  -5.373  1.00 32.85  ? 75  GLU B O   1 
ATOM   5604  C CB  . GLU B 1 75  ? 0.931   38.620  -3.278  1.00 39.80  ? 75  GLU B CB  1 
ATOM   5605  C CG  . GLU B 1 75  ? 1.065   39.790  -4.248  1.00 50.54  ? 75  GLU B CG  1 
ATOM   5606  C CD  . GLU B 1 75  ? 1.692   41.032  -3.606  1.00 60.83  ? 75  GLU B CD  1 
ATOM   5607  O OE1 . GLU B 1 75  ? 2.431   40.881  -2.593  1.00 61.47  ? 75  GLU B OE1 1 
ATOM   5608  O OE2 . GLU B 1 75  ? 1.434   42.162  -4.116  1.00 62.63  ? 75  GLU B OE2 1 
ATOM   5609  N N   . LYS B 1 76  ? -0.551  36.171  -4.849  1.00 30.92  ? 76  LYS B N   1 
ATOM   5610  C CA  . LYS B 1 76  ? -0.953  35.528  -6.104  1.00 30.65  ? 76  LYS B CA  1 
ATOM   5611  C C   . LYS B 1 76  ? -2.448  35.387  -6.150  1.00 29.61  ? 76  LYS B C   1 
ATOM   5612  O O   . LYS B 1 76  ? -3.075  35.674  -7.153  1.00 28.48  ? 76  LYS B O   1 
ATOM   5613  C CB  . LYS B 1 76  ? -0.294  34.158  -6.265  1.00 31.77  ? 76  LYS B CB  1 
ATOM   5614  C CG  . LYS B 1 76  ? 1.134   34.232  -6.744  1.00 32.76  ? 76  LYS B CG  1 
ATOM   5615  C CD  . LYS B 1 76  ? 1.556   32.926  -7.384  1.00 36.19  ? 76  LYS B CD  1 
ATOM   5616  C CE  . LYS B 1 76  ? 2.835   33.092  -8.205  1.00 35.25  ? 76  LYS B CE  1 
ATOM   5617  N NZ  . LYS B 1 76  ? 3.191   31.787  -8.826  1.00 35.91  ? 76  LYS B NZ  1 
ATOM   5618  N N   . ILE B 1 77  ? -3.020  35.001  -5.013  1.00 31.74  ? 77  ILE B N   1 
ATOM   5619  C CA  . ILE B 1 77  ? -4.450  34.824  -4.887  1.00 29.42  ? 77  ILE B CA  1 
ATOM   5620  C C   . ILE B 1 77  ? -5.126  36.151  -5.171  1.00 30.10  ? 77  ILE B C   1 
ATOM   5621  O O   . ILE B 1 77  ? -6.144  36.201  -5.867  1.00 32.45  ? 77  ILE B O   1 
ATOM   5622  C CB  . ILE B 1 77  ? -4.800  34.297  -3.468  1.00 30.36  ? 77  ILE B CB  1 
ATOM   5623  C CG1 . ILE B 1 77  ? -4.271  32.863  -3.290  1.00 30.34  ? 77  ILE B CG1 1 
ATOM   5624  C CG2 . ILE B 1 77  ? -6.297  34.360  -3.193  1.00 28.44  ? 77  ILE B CG2 1 
ATOM   5625  C CD1 . ILE B 1 77  ? -4.270  32.379  -1.846  1.00 32.87  ? 77  ILE B CD1 1 
ATOM   5626  N N   . LEU B 1 78  ? -4.556  37.229  -4.643  1.00 28.69  ? 78  LEU B N   1 
ATOM   5627  C CA  . LEU B 1 78  ? -5.140  38.566  -4.802  1.00 30.98  ? 78  LEU B CA  1 
ATOM   5628  C C   . LEU B 1 78  ? -5.089  39.117  -6.250  1.00 31.31  ? 78  LEU B C   1 
ATOM   5629  O O   . LEU B 1 78  ? -5.709  40.137  -6.553  1.00 32.76  ? 78  LEU B O   1 
ATOM   5630  C CB  . LEU B 1 78  ? -4.478  39.568  -3.835  1.00 29.48  ? 78  LEU B CB  1 
ATOM   5631  C CG  . LEU B 1 78  ? -4.815  39.461  -2.348  1.00 29.05  ? 78  LEU B CG  1 
ATOM   5632  C CD1 . LEU B 1 78  ? -3.868  40.334  -1.548  1.00 29.01  ? 78  LEU B CD1 1 
ATOM   5633  C CD2 . LEU B 1 78  ? -6.256  39.876  -2.112  1.00 28.65  ? 78  LEU B CD2 1 
ATOM   5634  N N   . THR B 1 79  ? -4.339  38.445  -7.119  1.00 31.38  ? 79  THR B N   1 
ATOM   5635  C CA  . THR B 1 79  ? -4.112  38.906  -8.502  1.00 31.72  ? 79  THR B CA  1 
ATOM   5636  C C   . THR B 1 79  ? -4.314  37.735  -9.515  1.00 32.10  ? 79  THR B C   1 
ATOM   5637  O O   . THR B 1 79  ? -3.841  37.791  -10.650 1.00 30.69  ? 79  THR B O   1 
ATOM   5638  C CB  . THR B 1 79  ? -2.667  39.429  -8.661  1.00 31.75  ? 79  THR B CB  1 
ATOM   5639  O OG1 . THR B 1 79  ? -1.741  38.363  -8.361  1.00 31.88  ? 79  THR B OG1 1 
ATOM   5640  C CG2 . THR B 1 79  ? -2.381  40.628  -7.717  1.00 32.18  ? 79  THR B CG2 1 
ATOM   5641  N N   . GLN B 1 80  ? -5.003  36.683  -9.083  1.00 31.68  ? 80  GLN B N   1 
ATOM   5642  C CA  . GLN B 1 80  ? -5.116  35.433  -9.850  1.00 32.62  ? 80  GLN B CA  1 
ATOM   5643  C C   . GLN B 1 80  ? -5.841  35.600  -11.194 1.00 32.95  ? 80  GLN B C   1 
ATOM   5644  O O   . GLN B 1 80  ? -6.608  36.547  -11.383 1.00 34.32  ? 80  GLN B O   1 
ATOM   5645  C CB  . GLN B 1 80  ? -5.867  34.409  -9.024  1.00 31.55  ? 80  GLN B CB  1 
ATOM   5646  C CG  . GLN B 1 80  ? -7.272  34.866  -8.664  1.00 33.12  ? 80  GLN B CG  1 
ATOM   5647  C CD  . GLN B 1 80  ? -7.971  33.912  -7.722  1.00 34.83  ? 80  GLN B CD  1 
ATOM   5648  O OE1 . GLN B 1 80  ? -8.636  32.969  -8.161  1.00 34.28  ? 80  GLN B OE1 1 
ATOM   5649  N NE2 . GLN B 1 80  ? -7.803  34.136  -6.407  1.00 34.39  ? 80  GLN B NE2 1 
ATOM   5650  N N   . SER B 1 81  ? -5.582  34.685  -12.121 1.00 31.54  ? 81  SER B N   1 
ATOM   5651  C CA  . SER B 1 81  ? -6.463  34.518  -13.291 1.00 32.98  ? 81  SER B CA  1 
ATOM   5652  C C   . SER B 1 81  ? -7.273  33.257  -13.047 1.00 33.49  ? 81  SER B C   1 
ATOM   5653  O O   . SER B 1 81  ? -6.929  32.446  -12.174 1.00 33.17  ? 81  SER B O   1 
ATOM   5654  C CB  . SER B 1 81  ? -5.660  34.340  -14.597 1.00 31.31  ? 81  SER B CB  1 
ATOM   5655  O OG  . SER B 1 81  ? -4.545  35.195  -14.684 1.00 30.11  ? 81  SER B OG  1 
ATOM   5656  N N   . SER B 1 82  ? -8.331  33.071  -13.825 1.00 33.43  ? 82  SER B N   1 
ATOM   5657  C CA  . SER B 1 82  ? -9.086  31.830  -13.767 1.00 33.68  ? 82  SER B CA  1 
ATOM   5658  C C   . SER B 1 82  ? -8.159  30.679  -14.044 1.00 32.10  ? 82  SER B C   1 
ATOM   5659  O O   . SER B 1 82  ? -7.304  30.776  -14.911 1.00 35.42  ? 82  SER B O   1 
ATOM   5660  C CB  . SER B 1 82  ? -10.203 31.852  -14.790 1.00 34.12  ? 82  SER B CB  1 
ATOM   5661  O OG  . SER B 1 82  ? -11.064 32.930  -14.526 1.00 34.99  ? 82  SER B OG  1 
ATOM   5662  N N   . PHE B 1 83  ? -8.324  29.601  -13.295 1.00 32.72  ? 83  PHE B N   1 
ATOM   5663  C CA  . PHE B 1 83  ? -7.570  28.349  -13.481 1.00 34.18  ? 83  PHE B CA  1 
ATOM   5664  C C   . PHE B 1 83  ? -6.146  28.363  -12.912 1.00 32.90  ? 83  PHE B C   1 
ATOM   5665  O O   . PHE B 1 83  ? -5.522  27.318  -12.803 1.00 34.60  ? 83  PHE B O   1 
ATOM   5666  C CB  . PHE B 1 83  ? -7.535  27.914  -14.967 1.00 37.24  ? 83  PHE B CB  1 
ATOM   5667  C CG  . PHE B 1 83  ? -8.892  27.678  -15.574 1.00 40.18  ? 83  PHE B CG  1 
ATOM   5668  C CD1 . PHE B 1 83  ? -9.665  26.580  -15.195 1.00 42.24  ? 83  PHE B CD1 1 
ATOM   5669  C CD2 . PHE B 1 83  ? -9.384  28.535  -16.565 1.00 41.33  ? 83  PHE B CD2 1 
ATOM   5670  C CE1 . PHE B 1 83  ? -10.915 26.354  -15.778 1.00 44.66  ? 83  PHE B CE1 1 
ATOM   5671  C CE2 . PHE B 1 83  ? -10.634 28.319  -17.145 1.00 43.34  ? 83  PHE B CE2 1 
ATOM   5672  C CZ  . PHE B 1 83  ? -11.401 27.226  -16.751 1.00 44.37  ? 83  PHE B CZ  1 
ATOM   5673  N N   . GLU B 1 84  ? -5.624  29.533  -12.564 1.00 30.94  ? 84  GLU B N   1 
ATOM   5674  C CA  . GLU B 1 84  ? -4.266  29.610  -12.026 1.00 30.78  ? 84  GLU B CA  1 
ATOM   5675  C C   . GLU B 1 84  ? -4.101  28.736  -10.774 1.00 30.67  ? 84  GLU B C   1 
ATOM   5676  O O   . GLU B 1 84  ? -4.956  28.728  -9.871  1.00 30.82  ? 84  GLU B O   1 
ATOM   5677  C CB  . GLU B 1 84  ? -3.833  31.074  -11.748 1.00 32.65  ? 84  GLU B CB  1 
ATOM   5678  C CG  . GLU B 1 84  ? -2.368  31.243  -11.324 1.00 32.13  ? 84  GLU B CG  1 
ATOM   5679  C CD  . GLU B 1 84  ? -1.892  32.694  -11.311 1.00 34.49  ? 84  GLU B CD  1 
ATOM   5680  O OE1 . GLU B 1 84  ? -2.736  33.625  -11.258 1.00 34.00  ? 84  GLU B OE1 1 
ATOM   5681  O OE2 . GLU B 1 84  ? -0.651  32.909  -11.347 1.00 37.30  ? 84  GLU B OE2 1 
ATOM   5682  N N   . CYS B 1 85  ? -3.010  27.984  -10.745 1.00 30.33  ? 85  CYS B N   1 
ATOM   5683  C CA  . CYS B 1 85  ? -2.604  27.255  -9.552  1.00 30.07  ? 85  CYS B CA  1 
ATOM   5684  C C   . CYS B 1 85  ? -1.195  27.666  -9.219  1.00 29.63  ? 85  CYS B C   1 
ATOM   5685  O O   . CYS B 1 85  ? -0.560  28.372  -9.978  1.00 30.35  ? 85  CYS B O   1 
ATOM   5686  C CB  . CYS B 1 85  ? -2.620  25.755  -9.814  1.00 29.25  ? 85  CYS B CB  1 
ATOM   5687  S SG  . CYS B 1 85  ? -4.195  25.116  -10.412 1.00 30.02  ? 85  CYS B SG  1 
ATOM   5688  N N   . ILE B 1 86  ? -0.708  27.184  -8.087  1.00 30.34  ? 86  ILE B N   1 
ATOM   5689  C CA  . ILE B 1 86  ? 0.717   27.147  -7.775  1.00 30.26  ? 86  ILE B CA  1 
ATOM   5690  C C   . ILE B 1 86  ? 0.991   25.715  -7.368  1.00 29.86  ? 86  ILE B C   1 
ATOM   5691  O O   . ILE B 1 86  ? 0.049   24.959  -7.191  1.00 31.09  ? 86  ILE B O   1 
ATOM   5692  C CB  . ILE B 1 86  ? 1.051   28.068  -6.594  1.00 29.47  ? 86  ILE B CB  1 
ATOM   5693  C CG1 . ILE B 1 86  ? 0.067   27.836  -5.458  1.00 31.23  ? 86  ILE B CG1 1 
ATOM   5694  C CG2 . ILE B 1 86  ? 0.955   29.506  -7.030  1.00 32.12  ? 86  ILE B CG2 1 
ATOM   5695  C CD1 . ILE B 1 86  ? 0.629   28.088  -4.080  1.00 31.85  ? 86  ILE B CD1 1 
ATOM   5696  N N   . HIS B 1 87  ? 2.258   25.338  -7.220  1.00 30.13  ? 87  HIS B N   1 
ATOM   5697  C CA  . HIS B 1 87  ? 2.595   24.048  -6.572  1.00 33.13  ? 87  HIS B CA  1 
ATOM   5698  C C   . HIS B 1 87  ? 2.311   23.981  -5.087  1.00 33.47  ? 87  HIS B C   1 
ATOM   5699  O O   . HIS B 1 87  ? 2.617   24.926  -4.340  1.00 35.03  ? 87  HIS B O   1 
ATOM   5700  C CB  . HIS B 1 87  ? 4.050   23.689  -6.811  1.00 33.65  ? 87  HIS B CB  1 
ATOM   5701  C CG  . HIS B 1 87  ? 4.341   23.278  -8.223  1.00 34.22  ? 87  HIS B CG  1 
ATOM   5702  N ND1 . HIS B 1 87  ? 4.811   24.142  -9.144  1.00 34.62  ? 87  HIS B ND1 1 
ATOM   5703  C CD2 . HIS B 1 87  ? 4.190   22.048  -8.870  1.00 33.40  ? 87  HIS B CD2 1 
ATOM   5704  C CE1 . HIS B 1 87  ? 4.962   23.496  -10.317 1.00 35.42  ? 87  HIS B CE1 1 
ATOM   5705  N NE2 . HIS B 1 87  ? 4.588   22.213  -10.143 1.00 33.62  ? 87  HIS B NE2 1 
ATOM   5706  N N   . LEU B 1 88  ? 1.763   22.846  -4.646  1.00 33.40  ? 88  LEU B N   1 
ATOM   5707  C CA  . LEU B 1 88  ? 1.536   22.571  -3.236  1.00 33.34  ? 88  LEU B CA  1 
ATOM   5708  C C   . LEU B 1 88  ? 2.845   22.653  -2.434  1.00 34.52  ? 88  LEU B C   1 
ATOM   5709  O O   . LEU B 1 88  ? 2.844   23.085  -1.273  1.00 35.86  ? 88  LEU B O   1 
ATOM   5710  C CB  . LEU B 1 88  ? 0.833   21.204  -3.032  1.00 32.28  ? 88  LEU B CB  1 
ATOM   5711  C CG  . LEU B 1 88  ? -0.720  21.135  -3.078  1.00 33.36  ? 88  LEU B CG  1 
ATOM   5712  C CD1 . LEU B 1 88  ? -1.212  19.709  -3.273  1.00 32.93  ? 88  LEU B CD1 1 
ATOM   5713  C CD2 . LEU B 1 88  ? -1.387  21.737  -1.827  1.00 31.88  ? 88  LEU B CD2 1 
ATOM   5714  N N   . SER B 1 89  ? 3.958   22.297  -3.069  1.00 33.40  ? 89  SER B N   1 
ATOM   5715  C CA  . SER B 1 89  ? 5.272   22.292  -2.412  1.00 35.60  ? 89  SER B CA  1 
ATOM   5716  C C   . SER B 1 89  ? 5.834   23.685  -2.041  1.00 36.44  ? 89  SER B C   1 
ATOM   5717  O O   . SER B 1 89  ? 6.783   23.787  -1.244  1.00 35.76  ? 89  SER B O   1 
ATOM   5718  C CB  . SER B 1 89  ? 6.287   21.560  -3.285  1.00 36.02  ? 89  SER B CB  1 
ATOM   5719  O OG  . SER B 1 89  ? 6.590   22.329  -4.426  1.00 36.64  ? 89  SER B OG  1 
ATOM   5720  N N   . VAL B 1 90  ? 5.268   24.746  -2.618  1.00 35.66  ? 90  VAL B N   1 
ATOM   5721  C CA  . VAL B 1 90  ? 5.706   26.102  -2.289  1.00 37.44  ? 90  VAL B CA  1 
ATOM   5722  C C   . VAL B 1 90  ? 5.276   26.468  -0.890  1.00 38.19  ? 90  VAL B C   1 
ATOM   5723  O O   . VAL B 1 90  ? 5.697   27.499  -0.334  1.00 42.50  ? 90  VAL B O   1 
ATOM   5724  C CB  . VAL B 1 90  ? 5.159   27.161  -3.279  1.00 38.78  ? 90  VAL B CB  1 
ATOM   5725  C CG1 . VAL B 1 90  ? 3.808   27.663  -2.826  1.00 36.24  ? 90  VAL B CG1 1 
ATOM   5726  C CG2 . VAL B 1 90  ? 6.130   28.329  -3.392  1.00 38.27  ? 90  VAL B CG2 1 
ATOM   5727  N N   . LEU B 1 91  ? 4.417   25.635  -0.320  1.00 37.92  ? 91  LEU B N   1 
ATOM   5728  C CA  . LEU B 1 91  ? 3.869   25.924  0.991   1.00 36.29  ? 91  LEU B CA  1 
ATOM   5729  C C   . LEU B 1 91  ? 4.709   25.292  2.073   1.00 36.32  ? 91  LEU B C   1 
ATOM   5730  O O   . LEU B 1 91  ? 4.362   25.366  3.248   1.00 37.13  ? 91  LEU B O   1 
ATOM   5731  C CB  . LEU B 1 91  ? 2.409   25.466  1.077   1.00 34.78  ? 91  LEU B CB  1 
ATOM   5732  C CG  . LEU B 1 91  ? 1.387   26.241  0.222   1.00 33.43  ? 91  LEU B CG  1 
ATOM   5733  C CD1 . LEU B 1 91  ? 0.018   25.602  0.354   1.00 32.05  ? 91  LEU B CD1 1 
ATOM   5734  C CD2 . LEU B 1 91  ? 1.329   27.725  0.614   1.00 32.40  ? 91  LEU B CD2 1 
ATOM   5735  N N   . HIS B 1 92  ? 5.824   24.677  1.683   1.00 37.90  ? 92  HIS B N   1 
ATOM   5736  C CA  . HIS B 1 92  ? 6.746   24.095  2.673   1.00 41.38  ? 92  HIS B CA  1 
ATOM   5737  C C   . HIS B 1 92  ? 8.212   24.197  2.353   1.00 42.70  ? 92  HIS B C   1 
ATOM   5738  O O   . HIS B 1 92  ? 9.043   24.110  3.244   1.00 45.93  ? 92  HIS B O   1 
ATOM   5739  C CB  . HIS B 1 92  ? 6.356   22.652  3.043   1.00 40.51  ? 92  HIS B CB  1 
ATOM   5740  C CG  . HIS B 1 92  ? 6.526   21.649  1.921   1.00 40.39  ? 92  HIS B CG  1 
ATOM   5741  N ND1 . HIS B 1 92  ? 7.726   21.146  1.570   1.00 41.30  ? 92  HIS B ND1 1 
ATOM   5742  C CD2 . HIS B 1 92  ? 5.585   21.031  1.091   1.00 40.81  ? 92  HIS B CD2 1 
ATOM   5743  C CE1 . HIS B 1 92  ? 7.566   20.263  0.564   1.00 40.12  ? 92  HIS B CE1 1 
ATOM   5744  N NE2 . HIS B 1 92  ? 6.259   20.197  0.268   1.00 39.51  ? 92  HIS B NE2 1 
ATOM   5745  N N   . LYS B 1 93  ? 8.548   24.404  1.086   1.00 45.01  ? 93  LYS B N   1 
ATOM   5746  C CA  . LYS B 1 93  ? 9.946   24.417  0.685   1.00 45.91  ? 93  LYS B CA  1 
ATOM   5747  C C   . LYS B 1 93  ? 10.633  25.723  1.027   1.00 45.84  ? 93  LYS B C   1 
ATOM   5748  O O   . LYS B 1 93  ? 10.038  26.797  0.931   1.00 43.89  ? 93  LYS B O   1 
ATOM   5749  C CB  . LYS B 1 93  ? 10.087  24.116  -0.808  1.00 48.59  ? 93  LYS B CB  1 
ATOM   5750  C CG  . LYS B 1 93  ? 9.972   22.639  -1.140  1.00 49.47  ? 93  LYS B CG  1 
ATOM   5751  C CD  . LYS B 1 93  ? 10.389  22.359  -2.570  1.00 50.07  ? 93  LYS B CD  1 
ATOM   5752  C CE  . LYS B 1 93  ? 10.379  20.859  -2.844  1.00 48.83  ? 93  LYS B CE  1 
ATOM   5753  N NZ  . LYS B 1 93  ? 10.547  20.603  -4.296  1.00 46.83  ? 93  LYS B NZ  1 
ATOM   5754  N N   . CYS B 1 94  ? 11.890  25.613  1.450   1.00 48.80  ? 94  CYS B N   1 
ATOM   5755  C CA  . CYS B 1 94  ? 12.750  26.774  1.709   1.00 49.89  ? 94  CYS B CA  1 
ATOM   5756  C C   . CYS B 1 94  ? 12.283  27.633  2.895   1.00 50.77  ? 94  CYS B C   1 
ATOM   5757  O O   . CYS B 1 94  ? 12.766  28.753  3.077   1.00 52.64  ? 94  CYS B O   1 
ATOM   5758  C CB  . CYS B 1 94  ? 12.918  27.635  0.438   1.00 52.07  ? 94  CYS B CB  1 
ATOM   5759  S SG  . CYS B 1 94  ? 13.463  26.732  -1.042  1.00 55.34  ? 94  CYS B SG  1 
ATOM   5760  N N   . TYR B 1 95  ? 11.338  27.111  3.684   1.00 48.83  ? 95  TYR B N   1 
ATOM   5761  C CA  . TYR B 1 95  ? 10.966  27.723  4.955   1.00 48.84  ? 95  TYR B CA  1 
ATOM   5762  C C   . TYR B 1 95  ? 12.034  27.435  6.017   1.00 50.66  ? 95  TYR B C   1 
ATOM   5763  O O   . TYR B 1 95  ? 12.590  26.332  6.064   1.00 47.94  ? 95  TYR B O   1 
ATOM   5764  C CB  . TYR B 1 95  ? 9.612   27.189  5.438   1.00 48.02  ? 95  TYR B CB  1 
ATOM   5765  C CG  . TYR B 1 95  ? 8.420   27.947  4.913   1.00 46.38  ? 95  TYR B CG  1 
ATOM   5766  C CD1 . TYR B 1 95  ? 7.933   29.072  5.582   1.00 46.07  ? 95  TYR B CD1 1 
ATOM   5767  C CD2 . TYR B 1 95  ? 7.757   27.532  3.750   1.00 45.03  ? 95  TYR B CD2 1 
ATOM   5768  C CE1 . TYR B 1 95  ? 6.840   29.778  5.091   1.00 43.21  ? 95  TYR B CE1 1 
ATOM   5769  C CE2 . TYR B 1 95  ? 6.659   28.230  3.264   1.00 42.55  ? 95  TYR B CE2 1 
ATOM   5770  C CZ  . TYR B 1 95  ? 6.208   29.353  3.934   1.00 42.67  ? 95  TYR B CZ  1 
ATOM   5771  O OH  . TYR B 1 95  ? 5.112   30.043  3.452   1.00 41.65  ? 95  TYR B OH  1 
ATOM   5772  N N   . ASP B 1 96  ? 12.304  28.422  6.873   1.00 50.91  ? 96  ASP B N   1 
ATOM   5773  C CA  . ASP B 1 96  ? 13.261  28.256  7.967   1.00 51.24  ? 96  ASP B CA  1 
ATOM   5774  C C   . ASP B 1 96  ? 12.552  27.574  9.126   1.00 51.71  ? 96  ASP B C   1 
ATOM   5775  O O   . ASP B 1 96  ? 11.841  28.217  9.907   1.00 51.84  ? 96  ASP B O   1 
ATOM   5776  C CB  . ASP B 1 96  ? 13.849  29.619  8.379   1.00 54.48  ? 96  ASP B CB  1 
ATOM   5777  C CG  . ASP B 1 96  ? 14.815  29.528  9.573   1.00 57.42  ? 96  ASP B CG  1 
ATOM   5778  O OD1 . ASP B 1 96  ? 15.206  28.410  9.988   1.00 58.64  ? 96  ASP B OD1 1 
ATOM   5779  O OD2 . ASP B 1 96  ? 15.189  30.599  10.092  1.00 58.52  ? 96  ASP B OD2 1 
ATOM   5780  N N   . TYR B 1 97  ? 12.742  26.264  9.228   1.00 53.17  ? 97  TYR B N   1 
ATOM   5781  C CA  . TYR B 1 97  ? 12.007  25.446  10.192  1.00 54.84  ? 97  TYR B CA  1 
ATOM   5782  C C   . TYR B 1 97  ? 12.505  25.573  11.626  1.00 57.02  ? 97  TYR B C   1 
ATOM   5783  O O   . TYR B 1 97  ? 11.737  25.370  12.566  1.00 59.32  ? 97  TYR B O   1 
ATOM   5784  C CB  . TYR B 1 97  ? 11.979  23.977  9.755   1.00 54.22  ? 97  TYR B CB  1 
ATOM   5785  C CG  . TYR B 1 97  ? 11.024  23.734  8.614   1.00 54.82  ? 97  TYR B CG  1 
ATOM   5786  C CD1 . TYR B 1 97  ? 9.664   23.545  8.852   1.00 54.12  ? 97  TYR B CD1 1 
ATOM   5787  C CD2 . TYR B 1 97  ? 11.471  23.723  7.294   1.00 54.15  ? 97  TYR B CD2 1 
ATOM   5788  C CE1 . TYR B 1 97  ? 8.778   23.338  7.812   1.00 53.51  ? 97  TYR B CE1 1 
ATOM   5789  C CE2 . TYR B 1 97  ? 10.591  23.524  6.246   1.00 55.23  ? 97  TYR B CE2 1 
ATOM   5790  C CZ  . TYR B 1 97  ? 9.242   23.336  6.515   1.00 55.99  ? 97  TYR B CZ  1 
ATOM   5791  O OH  . TYR B 1 97  ? 8.353   23.140  5.484   1.00 56.14  ? 97  TYR B OH  1 
ATOM   5792  N N   . ASP B 1 98  ? 13.784  25.903  11.795  1.00 58.70  ? 98  ASP B N   1 
ATOM   5793  C CA  . ASP B 1 98  ? 14.340  26.114  13.137  1.00 62.45  ? 98  ASP B CA  1 
ATOM   5794  C C   . ASP B 1 98  ? 13.633  27.272  13.853  1.00 60.72  ? 98  ASP B C   1 
ATOM   5795  O O   . ASP B 1 98  ? 13.467  27.247  15.066  1.00 60.94  ? 98  ASP B O   1 
ATOM   5796  C CB  . ASP B 1 98  ? 15.851  26.390  13.075  1.00 66.87  ? 98  ASP B CB  1 
ATOM   5797  C CG  . ASP B 1 98  ? 16.670  25.142  12.766  1.00 70.70  ? 98  ASP B CG  1 
ATOM   5798  O OD1 . ASP B 1 98  ? 16.425  24.088  13.397  1.00 72.59  ? 98  ASP B OD1 1 
ATOM   5799  O OD2 . ASP B 1 98  ? 17.573  25.224  11.901  1.00 72.31  ? 98  ASP B OD2 1 
ATOM   5800  N N   . ALA B 1 99  ? 13.195  28.263  13.082  1.00 58.59  ? 99  ALA B N   1 
ATOM   5801  C CA  . ALA B 1 99  ? 12.687  29.511  13.643  1.00 56.69  ? 99  ALA B CA  1 
ATOM   5802  C C   . ALA B 1 99  ? 11.168  29.547  13.879  1.00 54.50  ? 99  ALA B C   1 
ATOM   5803  O O   . ALA B 1 99  ? 10.637  30.563  14.347  1.00 55.91  ? 99  ALA B O   1 
ATOM   5804  C CB  . ALA B 1 99  ? 13.122  30.685  12.781  1.00 54.29  ? 99  ALA B CB  1 
ATOM   5805  N N   . ILE B 1 100 ? 10.479  28.449  13.575  1.00 50.11  ? 100 ILE B N   1 
ATOM   5806  C CA  . ILE B 1 100 ? 9.027   28.372  13.780  1.00 49.49  ? 100 ILE B CA  1 
ATOM   5807  C C   . ILE B 1 100 ? 8.718   27.720  15.132  1.00 50.86  ? 100 ILE B C   1 
ATOM   5808  O O   . ILE B 1 100 ? 8.830   26.499  15.271  1.00 51.98  ? 100 ILE B O   1 
ATOM   5809  C CB  . ILE B 1 100 ? 8.321   27.617  12.631  1.00 47.92  ? 100 ILE B CB  1 
ATOM   5810  C CG1 . ILE B 1 100 ? 8.576   28.327  11.295  1.00 47.65  ? 100 ILE B CG1 1 
ATOM   5811  C CG2 . ILE B 1 100 ? 6.826   27.518  12.888  1.00 47.31  ? 100 ILE B CG2 1 
ATOM   5812  C CD1 . ILE B 1 100 ? 8.285   27.488  10.067  1.00 44.78  ? 100 ILE B CD1 1 
ATOM   5813  N N   . PRO B 1 101 ? 8.344   28.544  16.141  1.00 50.16  ? 101 PRO B N   1 
ATOM   5814  C CA  . PRO B 1 101 ? 8.216   28.108  17.537  1.00 50.11  ? 101 PRO B CA  1 
ATOM   5815  C C   . PRO B 1 101 ? 7.306   26.905  17.731  1.00 49.86  ? 101 PRO B C   1 
ATOM   5816  O O   . PRO B 1 101 ? 7.701   25.947  18.393  1.00 53.04  ? 101 PRO B O   1 
ATOM   5817  C CB  . PRO B 1 101 ? 7.629   29.342  18.240  1.00 50.12  ? 101 PRO B CB  1 
ATOM   5818  C CG  . PRO B 1 101 ? 8.101   30.487  17.420  1.00 49.83  ? 101 PRO B CG  1 
ATOM   5819  C CD  . PRO B 1 101 ? 8.075   29.988  15.999  1.00 49.44  ? 101 PRO B CD  1 
ATOM   5820  N N   . TRP B 1 102 ? 6.110   26.936  17.147  1.00 47.32  ? 102 TRP B N   1 
ATOM   5821  C CA  . TRP B 1 102 ? 5.114   25.891  17.405  1.00 47.36  ? 102 TRP B CA  1 
ATOM   5822  C C   . TRP B 1 102 ? 5.464   24.568  16.758  1.00 49.94  ? 102 TRP B C   1 
ATOM   5823  O O   . TRP B 1 102 ? 4.716   23.593  16.869  1.00 47.58  ? 102 TRP B O   1 
ATOM   5824  C CB  . TRP B 1 102 ? 3.731   26.352  16.969  1.00 46.97  ? 102 TRP B CB  1 
ATOM   5825  C CG  . TRP B 1 102 ? 3.619   26.629  15.486  1.00 45.39  ? 102 TRP B CG  1 
ATOM   5826  C CD1 . TRP B 1 102 ? 3.928   27.813  14.815  1.00 44.53  ? 102 TRP B CD1 1 
ATOM   5827  C CD2 . TRP B 1 102 ? 3.155   25.709  14.442  1.00 46.48  ? 102 TRP B CD2 1 
ATOM   5828  N NE1 . TRP B 1 102 ? 3.692   27.692  13.469  1.00 43.10  ? 102 TRP B NE1 1 
ATOM   5829  C CE2 . TRP B 1 102 ? 3.226   26.452  13.178  1.00 45.66  ? 102 TRP B CE2 1 
ATOM   5830  C CE3 . TRP B 1 102 ? 2.701   24.396  14.427  1.00 45.40  ? 102 TRP B CE3 1 
ATOM   5831  C CZ2 . TRP B 1 102 ? 2.859   25.882  11.972  1.00 43.01  ? 102 TRP B CZ2 1 
ATOM   5832  C CZ3 . TRP B 1 102 ? 2.336   23.832  13.201  1.00 46.04  ? 102 TRP B CZ3 1 
ATOM   5833  C CH2 . TRP B 1 102 ? 2.415   24.560  12.004  1.00 44.71  ? 102 TRP B CH2 1 
ATOM   5834  N N   . LEU B 1 103 ? 6.606   24.526  16.077  1.00 50.50  ? 103 LEU B N   1 
ATOM   5835  C CA  . LEU B 1 103 ? 7.054   23.320  15.413  1.00 55.00  ? 103 LEU B CA  1 
ATOM   5836  C C   . LEU B 1 103 ? 8.279   22.725  16.105  1.00 60.06  ? 103 LEU B C   1 
ATOM   5837  O O   . LEU B 1 103 ? 8.751   21.654  15.723  1.00 59.39  ? 103 LEU B O   1 
ATOM   5838  C CB  . LEU B 1 103 ? 7.351   23.596  13.930  1.00 53.99  ? 103 LEU B CB  1 
ATOM   5839  C CG  . LEU B 1 103 ? 6.165   23.484  12.959  1.00 53.59  ? 103 LEU B CG  1 
ATOM   5840  C CD1 . LEU B 1 103 ? 6.568   23.888  11.548  1.00 50.36  ? 103 LEU B CD1 1 
ATOM   5841  C CD2 . LEU B 1 103 ? 5.564   22.079  12.971  1.00 51.94  ? 103 LEU B CD2 1 
ATOM   5842  N N   . GLN B 1 104 ? 8.766   23.407  17.142  1.00 64.39  ? 104 GLN B N   1 
ATOM   5843  C CA  . GLN B 1 104 ? 10.027  23.031  17.797  1.00 70.33  ? 104 GLN B CA  1 
ATOM   5844  C C   . GLN B 1 104 ? 10.010  21.700  18.554  1.00 73.12  ? 104 GLN B C   1 
ATOM   5845  O O   . GLN B 1 104 ? 11.019  20.991  18.580  1.00 72.15  ? 104 GLN B O   1 
ATOM   5846  C CB  . GLN B 1 104 ? 10.554  24.167  18.682  1.00 71.85  ? 104 GLN B CB  1 
ATOM   5847  C CG  . GLN B 1 104 ? 11.059  25.372  17.888  1.00 73.48  ? 104 GLN B CG  1 
ATOM   5848  C CD  . GLN B 1 104 ? 11.821  24.970  16.629  1.00 76.22  ? 104 GLN B CD  1 
ATOM   5849  O OE1 . GLN B 1 104 ? 12.932  24.443  16.705  1.00 79.24  ? 104 GLN B OE1 1 
ATOM   5850  N NE2 . GLN B 1 104 ? 11.222  25.217  15.462  1.00 73.62  ? 104 GLN B NE2 1 
ATOM   5851  N N   . ASN B 1 105 ? 8.870   21.352  19.148  1.00 75.99  ? 105 ASN B N   1 
ATOM   5852  C CA  . ASN B 1 105 ? 8.723   20.046  19.809  1.00 79.34  ? 105 ASN B CA  1 
ATOM   5853  C C   . ASN B 1 105 ? 8.237   18.934  18.862  1.00 79.82  ? 105 ASN B C   1 
ATOM   5854  O O   . ASN B 1 105 ? 7.705   17.909  19.303  1.00 83.11  ? 105 ASN B O   1 
ATOM   5855  C CB  . ASN B 1 105 ? 7.833   20.151  21.060  1.00 82.60  ? 105 ASN B CB  1 
ATOM   5856  C CG  . ASN B 1 105 ? 6.454   20.729  20.764  1.00 87.78  ? 105 ASN B CG  1 
ATOM   5857  O OD1 . ASN B 1 105 ? 6.054   20.887  19.599  1.00 89.10  ? 105 ASN B OD1 1 
ATOM   5858  N ND2 . ASN B 1 105 ? 5.716   21.051  21.825  1.00 83.60  ? 105 ASN B ND2 1 
ATOM   5859  N N   . VAL B 1 106 ? 8.428   19.152  17.562  1.00 74.90  ? 106 VAL B N   1 
ATOM   5860  C CA  . VAL B 1 106 ? 8.092   18.167  16.536  1.00 70.82  ? 106 VAL B CA  1 
ATOM   5861  C C   . VAL B 1 106 ? 9.368   17.758  15.806  1.00 70.66  ? 106 VAL B C   1 
ATOM   5862  O O   . VAL B 1 106 ? 10.193  18.609  15.455  1.00 66.20  ? 106 VAL B O   1 
ATOM   5863  C CB  . VAL B 1 106 ? 7.040   18.724  15.542  1.00 68.20  ? 106 VAL B CB  1 
ATOM   5864  C CG1 . VAL B 1 106 ? 7.044   17.943  14.233  1.00 67.11  ? 106 VAL B CG1 1 
ATOM   5865  C CG2 . VAL B 1 106 ? 5.654   18.712  16.171  1.00 65.46  ? 106 VAL B CG2 1 
ATOM   5866  N N   . GLU B 1 107 ? 9.533   16.452  15.599  1.00 76.14  ? 107 GLU B N   1 
ATOM   5867  C CA  . GLU B 1 107 ? 10.764  15.912  15.014  1.00 80.39  ? 107 GLU B CA  1 
ATOM   5868  C C   . GLU B 1 107 ? 10.968  16.381  13.568  1.00 78.39  ? 107 GLU B C   1 
ATOM   5869  O O   . GLU B 1 107 ? 10.079  16.216  12.723  1.00 75.06  ? 107 GLU B O   1 
ATOM   5870  C CB  . GLU B 1 107 ? 10.816  14.378  15.136  1.00 86.79  ? 107 GLU B CB  1 
ATOM   5871  C CG  . GLU B 1 107 ? 11.033  13.889  16.571  1.00 92.95  ? 107 GLU B CG  1 
ATOM   5872  C CD  . GLU B 1 107 ? 11.274  12.387  16.679  1.00 97.08  ? 107 GLU B CD  1 
ATOM   5873  O OE1 . GLU B 1 107 ? 11.568  11.742  15.648  1.00 102.38 ? 107 GLU B OE1 1 
ATOM   5874  O OE2 . GLU B 1 107 ? 11.177  11.849  17.804  1.00 96.06  ? 107 GLU B OE2 1 
ATOM   5875  N N   . PRO B 1 108 ? 12.141  16.987  13.293  1.00 78.54  ? 108 PRO B N   1 
ATOM   5876  C CA  . PRO B 1 108 ? 12.489  17.682  12.055  1.00 79.65  ? 108 PRO B CA  1 
ATOM   5877  C C   . PRO B 1 108 ? 11.849  17.102  10.793  1.00 82.14  ? 108 PRO B C   1 
ATOM   5878  O O   . PRO B 1 108 ? 11.402  17.858  9.921   1.00 80.88  ? 108 PRO B O   1 
ATOM   5879  C CB  . PRO B 1 108 ? 14.007  17.527  12.001  1.00 79.41  ? 108 PRO B CB  1 
ATOM   5880  C CG  . PRO B 1 108 ? 14.419  17.534  13.435  1.00 78.46  ? 108 PRO B CG  1 
ATOM   5881  C CD  . PRO B 1 108 ? 13.261  17.019  14.254  1.00 77.64  ? 108 PRO B CD  1 
ATOM   5882  N N   . ASN B 1 109 ? 11.798  15.773  10.715  1.00 83.96  ? 109 ASN B N   1 
ATOM   5883  C CA  . ASN B 1 109 ? 11.322  15.060  9.526   1.00 82.55  ? 109 ASN B CA  1 
ATOM   5884  C C   . ASN B 1 109 ? 9.844   15.305  9.218   1.00 76.49  ? 109 ASN B C   1 
ATOM   5885  O O   . ASN B 1 109 ? 9.451   15.379  8.051   1.00 73.89  ? 109 ASN B O   1 
ATOM   5886  C CB  . ASN B 1 109 ? 11.584  13.553  9.674   1.00 86.84  ? 109 ASN B CB  1 
ATOM   5887  C CG  . ASN B 1 109 ? 12.973  13.253  10.211  1.00 94.53  ? 109 ASN B CG  1 
ATOM   5888  O OD1 . ASN B 1 109 ? 13.968  13.366  9.490   1.00 97.84  ? 109 ASN B OD1 1 
ATOM   5889  N ND2 . ASN B 1 109 ? 13.049  12.879  11.489  1.00 94.63  ? 109 ASN B ND2 1 
ATOM   5890  N N   . LEU B 1 110 ? 9.031   15.430  10.265  1.00 71.79  ? 110 LEU B N   1 
ATOM   5891  C CA  . LEU B 1 110 ? 7.584   15.526  10.099  1.00 68.95  ? 110 LEU B CA  1 
ATOM   5892  C C   . LEU B 1 110 ? 7.102   16.969  9.950   1.00 64.14  ? 110 LEU B C   1 
ATOM   5893  O O   . LEU B 1 110 ? 5.907   17.212  9.768   1.00 65.92  ? 110 LEU B O   1 
ATOM   5894  C CB  . LEU B 1 110 ? 6.857   14.841  11.261  1.00 71.16  ? 110 LEU B CB  1 
ATOM   5895  C CG  . LEU B 1 110 ? 7.201   13.379  11.590  1.00 75.30  ? 110 LEU B CG  1 
ATOM   5896  C CD1 . LEU B 1 110 ? 6.170   12.813  12.556  1.00 75.64  ? 110 LEU B CD1 1 
ATOM   5897  C CD2 . LEU B 1 110 ? 7.305   12.507  10.342  1.00 73.17  ? 110 LEU B CD2 1 
ATOM   5898  N N   . ARG B 1 111 ? 8.039   17.912  10.000  1.00 58.89  ? 111 ARG B N   1 
ATOM   5899  C CA  . ARG B 1 111 ? 7.714   19.338  10.040  1.00 58.10  ? 111 ARG B CA  1 
ATOM   5900  C C   . ARG B 1 111 ? 7.081   19.875  8.744   1.00 58.01  ? 111 ARG B C   1 
ATOM   5901  O O   . ARG B 1 111 ? 6.006   20.477  8.798   1.00 58.93  ? 111 ARG B O   1 
ATOM   5902  C CB  . ARG B 1 111 ? 8.944   20.172  10.428  1.00 57.56  ? 111 ARG B CB  1 
ATOM   5903  C CG  . ARG B 1 111 ? 9.231   20.207  11.920  1.00 58.54  ? 111 ARG B CG  1 
ATOM   5904  C CD  . ARG B 1 111 ? 10.579  20.858  12.201  1.00 60.20  ? 111 ARG B CD  1 
ATOM   5905  N NE  . ARG B 1 111 ? 11.011  20.656  13.588  1.00 58.31  ? 111 ARG B NE  1 
ATOM   5906  C CZ  . ARG B 1 111 ? 12.037  21.284  14.152  1.00 56.15  ? 111 ARG B CZ  1 
ATOM   5907  N NH1 . ARG B 1 111 ? 12.750  22.162  13.457  1.00 56.32  ? 111 ARG B NH1 1 
ATOM   5908  N NH2 . ARG B 1 111 ? 12.355  21.031  15.411  1.00 56.24  ? 111 ARG B NH2 1 
ATOM   5909  N N   . PRO B 1 112 ? 7.744   19.666  7.579   1.00 55.29  ? 112 PRO B N   1 
ATOM   5910  C CA  . PRO B 1 112 ? 7.223   20.255  6.348   1.00 53.22  ? 112 PRO B CA  1 
ATOM   5911  C C   . PRO B 1 112 ? 5.781   19.869  6.034   1.00 52.83  ? 112 PRO B C   1 
ATOM   5912  O O   . PRO B 1 112 ? 5.014   20.718  5.573   1.00 53.98  ? 112 PRO B O   1 
ATOM   5913  C CB  . PRO B 1 112 ? 8.185   19.736  5.275   1.00 55.18  ? 112 PRO B CB  1 
ATOM   5914  C CG  . PRO B 1 112 ? 9.467   19.542  6.008   1.00 55.67  ? 112 PRO B CG  1 
ATOM   5915  C CD  . PRO B 1 112 ? 9.048   19.012  7.353   1.00 56.49  ? 112 PRO B CD  1 
ATOM   5916  N N   . LYS B 1 113 ? 5.411   18.617  6.300   1.00 52.00  ? 113 LYS B N   1 
ATOM   5917  C CA  . LYS B 1 113 ? 4.026   18.165  6.132   1.00 52.12  ? 113 LYS B CA  1 
ATOM   5918  C C   . LYS B 1 113 ? 3.082   18.868  7.090   1.00 49.10  ? 113 LYS B C   1 
ATOM   5919  O O   . LYS B 1 113 ? 1.931   19.146  6.742   1.00 47.01  ? 113 LYS B O   1 
ATOM   5920  C CB  . LYS B 1 113 ? 3.909   16.650  6.322   1.00 57.28  ? 113 LYS B CB  1 
ATOM   5921  C CG  . LYS B 1 113 ? 3.875   15.856  5.020   1.00 65.32  ? 113 LYS B CG  1 
ATOM   5922  C CD  . LYS B 1 113 ? 5.269   15.447  4.554   1.00 70.04  ? 113 LYS B CD  1 
ATOM   5923  C CE  . LYS B 1 113 ? 5.200   14.248  3.616   1.00 73.81  ? 113 LYS B CE  1 
ATOM   5924  N NZ  . LYS B 1 113 ? 6.484   14.002  2.899   1.00 76.49  ? 113 LYS B NZ  1 
ATOM   5925  N N   . LEU B 1 114 ? 3.558   19.149  8.303   1.00 48.71  ? 114 LEU B N   1 
ATOM   5926  C CA  . LEU B 1 114 ? 2.749   19.910  9.260   1.00 47.69  ? 114 LEU B CA  1 
ATOM   5927  C C   . LEU B 1 114 ? 2.588   21.371  8.836   1.00 44.20  ? 114 LEU B C   1 
ATOM   5928  O O   . LEU B 1 114 ? 1.476   21.895  8.845   1.00 43.44  ? 114 LEU B O   1 
ATOM   5929  C CB  . LEU B 1 114 ? 3.282   19.793  10.686  1.00 49.36  ? 114 LEU B CB  1 
ATOM   5930  C CG  . LEU B 1 114 ? 2.637   18.712  11.561  1.00 53.82  ? 114 LEU B CG  1 
ATOM   5931  C CD1 . LEU B 1 114 ? 3.020   18.905  13.024  1.00 55.51  ? 114 LEU B CD1 1 
ATOM   5932  C CD2 . LEU B 1 114 ? 1.118   18.690  11.404  1.00 54.72  ? 114 LEU B CD2 1 
ATOM   5933  N N   . LEU B 1 115 ? 3.678   22.013  8.418   1.00 41.95  ? 115 LEU B N   1 
ATOM   5934  C CA  . LEU B 1 115 ? 3.575   23.399  7.937   1.00 41.09  ? 115 LEU B CA  1 
ATOM   5935  C C   . LEU B 1 115 ? 2.653   23.493  6.725   1.00 40.08  ? 115 LEU B C   1 
ATOM   5936  O O   . LEU B 1 115 ? 1.869   24.450  6.601   1.00 42.40  ? 115 LEU B O   1 
ATOM   5937  C CB  . LEU B 1 115 ? 4.943   24.000  7.613   1.00 39.78  ? 115 LEU B CB  1 
ATOM   5938  C CG  . LEU B 1 115 ? 4.921   25.455  7.124   1.00 39.48  ? 115 LEU B CG  1 
ATOM   5939  C CD1 . LEU B 1 115 ? 4.579   26.456  8.234   1.00 37.72  ? 115 LEU B CD1 1 
ATOM   5940  C CD2 . LEU B 1 115 ? 6.246   25.815  6.478   1.00 39.89  ? 115 LEU B CD2 1 
ATOM   5941  N N   . LEU B 1 116 ? 2.731   22.497  5.847   1.00 38.09  ? 116 LEU B N   1 
ATOM   5942  C CA  . LEU B 1 116 ? 1.888   22.463  4.664   1.00 37.71  ? 116 LEU B CA  1 
ATOM   5943  C C   . LEU B 1 116 ? 0.424   22.395  5.083   1.00 38.49  ? 116 LEU B C   1 
ATOM   5944  O O   . LEU B 1 116 ? -0.403  23.218  4.649   1.00 35.62  ? 116 LEU B O   1 
ATOM   5945  C CB  . LEU B 1 116 ? 2.249   21.280  3.747   1.00 36.86  ? 116 LEU B CB  1 
ATOM   5946  C CG  . LEU B 1 116 ? 1.229   20.960  2.642   1.00 36.88  ? 116 LEU B CG  1 
ATOM   5947  C CD1 . LEU B 1 116 ? 1.329   21.981  1.513   1.00 35.48  ? 116 LEU B CD1 1 
ATOM   5948  C CD2 . LEU B 1 116 ? 1.352   19.529  2.105   1.00 36.35  ? 116 LEU B CD2 1 
ATOM   5949  N N   . LYS B 1 117 ? 0.114   21.421  5.937   1.00 39.92  ? 117 LYS B N   1 
ATOM   5950  C CA  . LYS B 1 117 ? -1.253  21.215  6.403   1.00 42.38  ? 117 LYS B CA  1 
ATOM   5951  C C   . LYS B 1 117 ? -1.824  22.480  7.056   1.00 41.82  ? 117 LYS B C   1 
ATOM   5952  O O   . LYS B 1 117 ? -2.985  22.839  6.824   1.00 42.21  ? 117 LYS B O   1 
ATOM   5953  C CB  . LYS B 1 117 ? -1.305  20.045  7.380   1.00 43.56  ? 117 LYS B CB  1 
ATOM   5954  C CG  . LYS B 1 117 ? -2.684  19.785  7.962   1.00 47.52  ? 117 LYS B CG  1 
ATOM   5955  C CD  . LYS B 1 117 ? -2.877  18.306  8.301   1.00 53.30  ? 117 LYS B CD  1 
ATOM   5956  C CE  . LYS B 1 117 ? -2.428  17.985  9.716   1.00 52.08  ? 117 LYS B CE  1 
ATOM   5957  N NZ  . LYS B 1 117 ? -3.582  17.836  10.639  1.00 57.99  ? 117 LYS B NZ  1 
ATOM   5958  N N   . HIS B 1 118 ? -1.004  23.146  7.871   1.00 41.31  ? 118 HIS B N   1 
ATOM   5959  C CA  . HIS B 1 118 ? -1.413  24.375  8.558   1.00 41.81  ? 118 HIS B CA  1 
ATOM   5960  C C   . HIS B 1 118 ? -1.436  25.581  7.660   1.00 40.02  ? 118 HIS B C   1 
ATOM   5961  O O   . HIS B 1 118 ? -2.276  26.453  7.841   1.00 42.69  ? 118 HIS B O   1 
ATOM   5962  C CB  . HIS B 1 118 ? -0.532  24.642  9.778   1.00 43.77  ? 118 HIS B CB  1 
ATOM   5963  C CG  . HIS B 1 118 ? -0.769  23.681  10.926  1.00 45.57  ? 118 HIS B CG  1 
ATOM   5964  N ND1 . HIS B 1 118 ? -1.052  24.098  12.177  1.00 44.91  ? 118 HIS B ND1 1 
ATOM   5965  C CD2 . HIS B 1 118 ? -0.779  22.284  10.967  1.00 46.92  ? 118 HIS B CD2 1 
ATOM   5966  C CE1 . HIS B 1 118 ? -1.221  23.028  12.975  1.00 46.02  ? 118 HIS B CE1 1 
ATOM   5967  N NE2 . HIS B 1 118 ? -1.059  21.921  12.234  1.00 46.43  ? 118 HIS B NE2 1 
ATOM   5968  N N   . ASN B 1 119 ? -0.506  25.668  6.705   1.00 37.35  ? 119 ASN B N   1 
ATOM   5969  C CA  . ASN B 1 119 ? -0.587  26.720  5.697   1.00 35.27  ? 119 ASN B CA  1 
ATOM   5970  C C   . ASN B 1 119 ? -1.881  26.585  4.908   1.00 34.91  ? 119 ASN B C   1 
ATOM   5971  O O   . ASN B 1 119 ? -2.618  27.560  4.752   1.00 35.46  ? 119 ASN B O   1 
ATOM   5972  C CB  . ASN B 1 119 ? 0.619   26.700  4.741   1.00 34.84  ? 119 ASN B CB  1 
ATOM   5973  C CG  . ASN B 1 119 ? 1.783   27.537  5.240   1.00 33.19  ? 119 ASN B CG  1 
ATOM   5974  O OD1 . ASN B 1 119 ? 2.907   27.424  4.736   1.00 35.03  ? 119 ASN B OD1 1 
ATOM   5975  N ND2 . ASN B 1 119 ? 1.534   28.355  6.232   1.00 30.31  ? 119 ASN B ND2 1 
ATOM   5976  N N   . LEU B 1 120 ? -2.154  25.371  4.424   1.00 33.02  ? 120 LEU B N   1 
ATOM   5977  C CA  . LEU B 1 120 ? -3.398  25.076  3.723   1.00 32.55  ? 120 LEU B CA  1 
ATOM   5978  C C   . LEU B 1 120 ? -4.635  25.518  4.564   1.00 33.95  ? 120 LEU B C   1 
ATOM   5979  O O   . LEU B 1 120 ? -5.501  26.256  4.071   1.00 34.60  ? 120 LEU B O   1 
ATOM   5980  C CB  . LEU B 1 120 ? -3.467  23.579  3.324   1.00 31.24  ? 120 LEU B CB  1 
ATOM   5981  C CG  . LEU B 1 120 ? -2.696  23.045  2.089   1.00 31.99  ? 120 LEU B CG  1 
ATOM   5982  C CD1 . LEU B 1 120 ? -2.859  21.528  1.923   1.00 31.08  ? 120 LEU B CD1 1 
ATOM   5983  C CD2 . LEU B 1 120 ? -3.079  23.753  0.787   1.00 29.51  ? 120 LEU B CD2 1 
ATOM   5984  N N   . PHE B 1 121 ? -4.699  25.115  5.834   1.00 34.30  ? 121 PHE B N   1 
ATOM   5985  C CA  . PHE B 1 121 ? -5.804  25.582  6.705   1.00 34.17  ? 121 PHE B CA  1 
ATOM   5986  C C   . PHE B 1 121 ? -5.984  27.100  6.635   1.00 33.14  ? 121 PHE B C   1 
ATOM   5987  O O   . PHE B 1 121 ? -7.092  27.593  6.381   1.00 32.64  ? 121 PHE B O   1 
ATOM   5988  C CB  . PHE B 1 121 ? -5.614  25.164  8.164   1.00 34.20  ? 121 PHE B CB  1 
ATOM   5989  C CG  . PHE B 1 121 ? -6.773  25.557  9.055   1.00 34.72  ? 121 PHE B CG  1 
ATOM   5990  C CD1 . PHE B 1 121 ? -6.855  26.838  9.591   1.00 33.47  ? 121 PHE B CD1 1 
ATOM   5991  C CD2 . PHE B 1 121 ? -7.798  24.661  9.313   1.00 34.25  ? 121 PHE B CD2 1 
ATOM   5992  C CE1 . PHE B 1 121 ? -7.926  27.204  10.376  1.00 34.83  ? 121 PHE B CE1 1 
ATOM   5993  C CE2 . PHE B 1 121 ? -8.868  25.019  10.090  1.00 35.13  ? 121 PHE B CE2 1 
ATOM   5994  C CZ  . PHE B 1 121 ? -8.932  26.290  10.631  1.00 35.23  ? 121 PHE B CZ  1 
ATOM   5995  N N   . LEU B 1 122 ? -4.906  27.841  6.889   1.00 33.13  ? 122 LEU B N   1 
ATOM   5996  C CA  . LEU B 1 122 ? -4.978  29.317  6.847   1.00 32.93  ? 122 LEU B CA  1 
ATOM   5997  C C   . LEU B 1 122 ? -5.483  29.843  5.493   1.00 32.59  ? 122 LEU B C   1 
ATOM   5998  O O   . LEU B 1 122 ? -6.358  30.707  5.452   1.00 32.95  ? 122 LEU B O   1 
ATOM   5999  C CB  . LEU B 1 122 ? -3.633  29.952  7.204   1.00 32.06  ? 122 LEU B CB  1 
ATOM   6000  C CG  . LEU B 1 122 ? -3.093  29.703  8.613   1.00 32.73  ? 122 LEU B CG  1 
ATOM   6001  C CD1 . LEU B 1 122 ? -1.630  30.112  8.680   1.00 31.44  ? 122 LEU B CD1 1 
ATOM   6002  C CD2 . LEU B 1 122 ? -3.920  30.473  9.647   1.00 32.41  ? 122 LEU B CD2 1 
ATOM   6003  N N   . LEU B 1 123 ? -4.953  29.298  4.390   1.00 33.32  ? 123 LEU B N   1 
ATOM   6004  C CA  . LEU B 1 123 ? -5.348  29.759  3.056   1.00 32.72  ? 123 LEU B CA  1 
ATOM   6005  C C   . LEU B 1 123 ? -6.823  29.435  2.769   1.00 32.98  ? 123 LEU B C   1 
ATOM   6006  O O   . LEU B 1 123 ? -7.531  30.242  2.156   1.00 33.54  ? 123 LEU B O   1 
ATOM   6007  C CB  . LEU B 1 123 ? -4.436  29.175  1.953   1.00 32.16  ? 123 LEU B CB  1 
ATOM   6008  C CG  . LEU B 1 123 ? -2.949  29.557  1.887   1.00 32.79  ? 123 LEU B CG  1 
ATOM   6009  C CD1 . LEU B 1 123 ? -2.199  28.633  0.940   1.00 30.94  ? 123 LEU B CD1 1 
ATOM   6010  C CD2 . LEU B 1 123 ? -2.727  31.010  1.487   1.00 31.38  ? 123 LEU B CD2 1 
ATOM   6011  N N   . ASP B 1 124 ? -7.272  28.262  3.216   1.00 32.64  ? 124 ASP B N   1 
ATOM   6012  C CA  . ASP B 1 124 ? -8.613  27.765  2.898   1.00 33.71  ? 124 ASP B CA  1 
ATOM   6013  C C   . ASP B 1 124 ? -9.677  28.386  3.799   1.00 33.81  ? 124 ASP B C   1 
ATOM   6014  O O   . ASP B 1 124 ? -10.820 28.518  3.390   1.00 35.49  ? 124 ASP B O   1 
ATOM   6015  C CB  . ASP B 1 124 ? -8.693  26.229  3.063   1.00 34.48  ? 124 ASP B CB  1 
ATOM   6016  C CG  . ASP B 1 124 ? -8.031  25.460  1.924   1.00 35.89  ? 124 ASP B CG  1 
ATOM   6017  O OD1 . ASP B 1 124 ? -8.013  25.945  0.770   1.00 36.05  ? 124 ASP B OD1 1 
ATOM   6018  O OD2 . ASP B 1 124 ? -7.548  24.331  2.186   1.00 37.52  ? 124 ASP B OD2 1 
ATOM   6019  N N   . ASN B 1 125 ? -9.318  28.700  5.040   1.00 32.97  ? 125 ASN B N   1 
ATOM   6020  C CA  . ASN B 1 125 ? -10.318 29.111  6.053   1.00 35.03  ? 125 ASN B CA  1 
ATOM   6021  C C   . ASN B 1 125 ? -10.299 30.598  6.414   1.00 34.52  ? 125 ASN B C   1 
ATOM   6022  O O   . ASN B 1 125 ? -11.266 31.114  6.955   1.00 36.67  ? 125 ASN B O   1 
ATOM   6023  C CB  . ASN B 1 125 ? -10.186 28.270  7.330   1.00 32.96  ? 125 ASN B CB  1 
ATOM   6024  C CG  . ASN B 1 125 ? -10.454 26.797  7.079   1.00 33.68  ? 125 ASN B CG  1 
ATOM   6025  O OD1 . ASN B 1 125 ? -11.595 26.355  7.075   1.00 32.53  ? 125 ASN B OD1 1 
ATOM   6026  N ND2 . ASN B 1 125 ? -9.399  26.040  6.837   1.00 34.10  ? 125 ASN B ND2 1 
ATOM   6027  N N   . ILE B 1 126 ? -9.196  31.270  6.129   1.00 33.71  ? 126 ILE B N   1 
ATOM   6028  C CA  . ILE B 1 126 ? -9.034  32.666  6.522   1.00 32.92  ? 126 ILE B CA  1 
ATOM   6029  C C   . ILE B 1 126 ? -8.676  33.574  5.348   1.00 31.19  ? 126 ILE B C   1 
ATOM   6030  O O   . ILE B 1 126 ? -9.277  34.646  5.186   1.00 31.89  ? 126 ILE B O   1 
ATOM   6031  C CB  . ILE B 1 126 ? -7.994  32.815  7.657   1.00 33.57  ? 126 ILE B CB  1 
ATOM   6032  C CG1 . ILE B 1 126 ? -8.507  32.093  8.923   1.00 34.63  ? 126 ILE B CG1 1 
ATOM   6033  C CG2 . ILE B 1 126 ? -7.716  34.289  7.939   1.00 32.73  ? 126 ILE B CG2 1 
ATOM   6034  C CD1 . ILE B 1 126 ? -7.571  32.153  10.113  1.00 33.97  ? 126 ILE B CD1 1 
ATOM   6035  N N   . VAL B 1 127 ? -7.729  33.137  4.513   1.00 28.47  ? 127 VAL B N   1 
ATOM   6036  C CA  . VAL B 1 127 ? -7.231  33.995  3.436   1.00 26.81  ? 127 VAL B CA  1 
ATOM   6037  C C   . VAL B 1 127 ? -8.255  34.126  2.331   1.00 26.56  ? 127 VAL B C   1 
ATOM   6038  O O   . VAL B 1 127 ? -8.745  35.204  2.074   1.00 28.09  ? 127 VAL B O   1 
ATOM   6039  C CB  . VAL B 1 127 ? -5.836  33.568  2.915   1.00 25.58  ? 127 VAL B CB  1 
ATOM   6040  C CG1 . VAL B 1 127 ? -5.437  34.411  1.732   1.00 24.53  ? 127 VAL B CG1 1 
ATOM   6041  C CG2 . VAL B 1 127 ? -4.782  33.699  4.031   1.00 24.74  ? 127 VAL B CG2 1 
ATOM   6042  N N   . LYS B 1 128 ? -8.615  33.023  1.710   1.00 27.33  ? 128 LYS B N   1 
ATOM   6043  C CA  . LYS B 1 128 ? -9.694  33.022  0.741   1.00 28.43  ? 128 LYS B CA  1 
ATOM   6044  C C   . LYS B 1 128 ? -11.030 33.580  1.312   1.00 30.35  ? 128 LYS B C   1 
ATOM   6045  O O   . LYS B 1 128 ? -11.622 34.484  0.708   1.00 32.11  ? 128 LYS B O   1 
ATOM   6046  C CB  . LYS B 1 128 ? -9.851  31.631  0.109   1.00 28.63  ? 128 LYS B CB  1 
ATOM   6047  C CG  . LYS B 1 128 ? -8.748  31.312  -0.903  1.00 28.51  ? 128 LYS B CG  1 
ATOM   6048  C CD  . LYS B 1 128 ? -8.894  29.922  -1.499  1.00 29.51  ? 128 LYS B CD  1 
ATOM   6049  C CE  . LYS B 1 128 ? -7.721  29.608  -2.411  1.00 29.18  ? 128 LYS B CE  1 
ATOM   6050  N NZ  . LYS B 1 128 ? -7.941  28.325  -3.136  1.00 30.08  ? 128 LYS B NZ  1 
ATOM   6051  N N   . PRO B 1 129 ? -11.490 33.082  2.493   1.00 31.00  ? 129 PRO B N   1 
ATOM   6052  C CA  . PRO B 1 129 ? -12.686 33.680  3.098   1.00 32.56  ? 129 PRO B CA  1 
ATOM   6053  C C   . PRO B 1 129 ? -12.646 35.193  3.355   1.00 32.92  ? 129 PRO B C   1 
ATOM   6054  O O   . PRO B 1 129 ? -13.671 35.849  3.156   1.00 33.13  ? 129 PRO B O   1 
ATOM   6055  C CB  . PRO B 1 129 ? -12.820 32.919  4.412   1.00 33.15  ? 129 PRO B CB  1 
ATOM   6056  C CG  . PRO B 1 129 ? -12.377 31.561  4.030   1.00 33.80  ? 129 PRO B CG  1 
ATOM   6057  C CD  . PRO B 1 129 ? -11.182 31.789  3.130   1.00 31.75  ? 129 PRO B CD  1 
ATOM   6058  N N   . ILE B 1 130 ? -11.505 35.749  3.797   1.00 32.68  ? 130 ILE B N   1 
ATOM   6059  C CA  . ILE B 1 130 ? -11.434 37.221  3.991   1.00 32.49  ? 130 ILE B CA  1 
ATOM   6060  C C   . ILE B 1 130 ? -11.610 38.022  2.687   1.00 32.80  ? 130 ILE B C   1 
ATOM   6061  O O   . ILE B 1 130 ? -12.309 39.033  2.664   1.00 34.84  ? 130 ILE B O   1 
ATOM   6062  C CB  . ILE B 1 130 ? -10.161 37.704  4.733   1.00 31.53  ? 130 ILE B CB  1 
ATOM   6063  C CG1 . ILE B 1 130 ? -10.386 39.105  5.265   1.00 31.47  ? 130 ILE B CG1 1 
ATOM   6064  C CG2 . ILE B 1 130 ? -8.921  37.702  3.831   1.00 30.31  ? 130 ILE B CG2 1 
ATOM   6065  C CD1 . ILE B 1 130 ? -11.426 39.148  6.363   1.00 36.30  ? 130 ILE B CD1 1 
ATOM   6066  N N   . ILE B 1 131 ? -10.953 37.580  1.621   1.00 31.87  ? 131 ILE B N   1 
ATOM   6067  C CA  . ILE B 1 131 ? -11.065 38.241  0.331   1.00 33.84  ? 131 ILE B CA  1 
ATOM   6068  C C   . ILE B 1 131 ? -12.517 38.195  -0.126  1.00 34.85  ? 131 ILE B C   1 
ATOM   6069  O O   . ILE B 1 131 ? -13.060 39.211  -0.582  1.00 36.14  ? 131 ILE B O   1 
ATOM   6070  C CB  . ILE B 1 131 ? -10.147 37.582  -0.734  1.00 33.53  ? 131 ILE B CB  1 
ATOM   6071  C CG1 . ILE B 1 131 ? -8.697  37.708  -0.313  1.00 31.76  ? 131 ILE B CG1 1 
ATOM   6072  C CG2 . ILE B 1 131 ? -10.348 38.206  -2.120  1.00 33.75  ? 131 ILE B CG2 1 
ATOM   6073  C CD1 . ILE B 1 131 ? -7.818  36.634  -0.906  1.00 31.59  ? 131 ILE B CD1 1 
ATOM   6074  N N   . ALA B 1 132 ? -13.149 37.032  0.029   1.00 33.78  ? 132 ALA B N   1 
ATOM   6075  C CA  . ALA B 1 132 ? -14.549 36.860  -0.370  1.00 35.71  ? 132 ALA B CA  1 
ATOM   6076  C C   . ALA B 1 132 ? -15.502 37.648  0.528   1.00 37.60  ? 132 ALA B C   1 
ATOM   6077  O O   . ALA B 1 132 ? -16.627 37.985  0.110   1.00 37.42  ? 132 ALA B O   1 
ATOM   6078  C CB  . ALA B 1 132 ? -14.924 35.391  -0.366  1.00 36.29  ? 132 ALA B CB  1 
ATOM   6079  N N   . PHE B 1 133 ? -15.066 37.932  1.764   1.00 36.59  ? 133 PHE B N   1 
ATOM   6080  C CA  . PHE B 1 133 ? -15.875 38.739  2.673   1.00 37.03  ? 133 PHE B CA  1 
ATOM   6081  C C   . PHE B 1 133 ? -15.928 40.195  2.226   1.00 37.25  ? 133 PHE B C   1 
ATOM   6082  O O   . PHE B 1 133 ? -16.963 40.845  2.370   1.00 39.39  ? 133 PHE B O   1 
ATOM   6083  C CB  . PHE B 1 133 ? -15.399 38.643  4.127   1.00 37.59  ? 133 PHE B CB  1 
ATOM   6084  C CG  . PHE B 1 133 ? -16.307 39.358  5.105   1.00 38.56  ? 133 PHE B CG  1 
ATOM   6085  C CD1 . PHE B 1 133 ? -17.525 38.791  5.494   1.00 39.22  ? 133 PHE B CD1 1 
ATOM   6086  C CD2 . PHE B 1 133 ? -15.961 40.608  5.614   1.00 38.65  ? 133 PHE B CD2 1 
ATOM   6087  C CE1 . PHE B 1 133 ? -18.365 39.450  6.374   1.00 38.82  ? 133 PHE B CE1 1 
ATOM   6088  C CE2 . PHE B 1 133 ? -16.800 41.270  6.502   1.00 39.10  ? 133 PHE B CE2 1 
ATOM   6089  C CZ  . PHE B 1 133 ? -18.000 40.690  6.883   1.00 39.72  ? 133 PHE B CZ  1 
ATOM   6090  N N   . TYR B 1 134 ? -14.829 40.696  1.665   1.00 36.19  ? 134 TYR B N   1 
ATOM   6091  C CA  . TYR B 1 134 ? -14.768 42.106  1.221   1.00 36.33  ? 134 TYR B CA  1 
ATOM   6092  C C   . TYR B 1 134 ? -14.966 42.335  -0.276  1.00 37.70  ? 134 TYR B C   1 
ATOM   6093  O O   . TYR B 1 134 ? -15.329 43.437  -0.685  1.00 37.70  ? 134 TYR B O   1 
ATOM   6094  C CB  . TYR B 1 134 ? -13.471 42.778  1.691   1.00 35.39  ? 134 TYR B CB  1 
ATOM   6095  C CG  . TYR B 1 134 ? -13.400 42.931  3.196   1.00 35.41  ? 134 TYR B CG  1 
ATOM   6096  C CD1 . TYR B 1 134 ? -14.320 43.721  3.875   1.00 36.13  ? 134 TYR B CD1 1 
ATOM   6097  C CD2 . TYR B 1 134 ? -12.436 42.250  3.938   1.00 34.47  ? 134 TYR B CD2 1 
ATOM   6098  C CE1 . TYR B 1 134 ? -14.282 43.845  5.256   1.00 37.49  ? 134 TYR B CE1 1 
ATOM   6099  C CE2 . TYR B 1 134 ? -12.374 42.372  5.313   1.00 34.93  ? 134 TYR B CE2 1 
ATOM   6100  C CZ  . TYR B 1 134 ? -13.291 43.178  5.975   1.00 36.68  ? 134 TYR B CZ  1 
ATOM   6101  O OH  . TYR B 1 134 ? -13.249 43.287  7.354   1.00 34.28  ? 134 TYR B OH  1 
ATOM   6102  N N   . TYR B 1 135 ? -14.729 41.297  -1.086  1.00 38.45  ? 135 TYR B N   1 
ATOM   6103  C CA  . TYR B 1 135 ? -14.725 41.434  -2.540  1.00 38.73  ? 135 TYR B CA  1 
ATOM   6104  C C   . TYR B 1 135 ? -15.552 40.392  -3.255  1.00 39.82  ? 135 TYR B C   1 
ATOM   6105  O O   . TYR B 1 135 ? -15.616 39.248  -2.835  1.00 40.87  ? 135 TYR B O   1 
ATOM   6106  C CB  . TYR B 1 135 ? -13.297 41.390  -3.078  1.00 35.77  ? 135 TYR B CB  1 
ATOM   6107  C CG  . TYR B 1 135 ? -12.476 42.523  -2.594  1.00 36.41  ? 135 TYR B CG  1 
ATOM   6108  C CD1 . TYR B 1 135 ? -12.496 43.752  -3.254  1.00 36.37  ? 135 TYR B CD1 1 
ATOM   6109  C CD2 . TYR B 1 135 ? -11.681 42.392  -1.453  1.00 35.40  ? 135 TYR B CD2 1 
ATOM   6110  C CE1 . TYR B 1 135 ? -11.739 44.812  -2.793  1.00 36.07  ? 135 TYR B CE1 1 
ATOM   6111  C CE2 . TYR B 1 135 ? -10.928 43.439  -0.993  1.00 34.11  ? 135 TYR B CE2 1 
ATOM   6112  C CZ  . TYR B 1 135 ? -10.963 44.646  -1.664  1.00 36.72  ? 135 TYR B CZ  1 
ATOM   6113  O OH  . TYR B 1 135 ? -10.213 45.694  -1.196  1.00 40.38  ? 135 TYR B OH  1 
ATOM   6114  N N   . LYS B 1 136 ? -16.181 40.812  -4.347  1.00 42.97  ? 136 LYS B N   1 
ATOM   6115  C CA  . LYS B 1 136 ? -16.766 39.901  -5.319  1.00 44.60  ? 136 LYS B CA  1 
ATOM   6116  C C   . LYS B 1 136 ? -15.783 39.717  -6.482  1.00 42.85  ? 136 LYS B C   1 
ATOM   6117  O O   . LYS B 1 136 ? -15.407 40.692  -7.134  1.00 44.18  ? 136 LYS B O   1 
ATOM   6118  C CB  . LYS B 1 136 ? -18.087 40.477  -5.826  1.00 49.64  ? 136 LYS B CB  1 
ATOM   6119  C CG  . LYS B 1 136 ? -18.937 39.529  -6.661  1.00 55.97  ? 136 LYS B CG  1 
ATOM   6120  C CD  . LYS B 1 136 ? -19.407 38.319  -5.860  1.00 62.49  ? 136 LYS B CD  1 
ATOM   6121  C CE  . LYS B 1 136 ? -20.815 37.901  -6.264  1.00 66.19  ? 136 LYS B CE  1 
ATOM   6122  N NZ  . LYS B 1 136 ? -21.068 38.143  -7.711  1.00 69.11  ? 136 LYS B NZ  1 
ATOM   6123  N N   . PRO B 1 137 ? -15.333 38.472  -6.725  1.00 42.11  ? 137 PRO B N   1 
ATOM   6124  C CA  . PRO B 1 137 ? -14.525 38.224  -7.922  1.00 42.37  ? 137 PRO B CA  1 
ATOM   6125  C C   . PRO B 1 137 ? -15.405 38.203  -9.175  1.00 44.44  ? 137 PRO B C   1 
ATOM   6126  O O   . PRO B 1 137 ? -16.473 37.584  -9.176  1.00 45.68  ? 137 PRO B O   1 
ATOM   6127  C CB  . PRO B 1 137 ? -13.924 36.841  -7.669  1.00 41.87  ? 137 PRO B CB  1 
ATOM   6128  C CG  . PRO B 1 137 ? -14.856 36.177  -6.714  1.00 41.60  ? 137 PRO B CG  1 
ATOM   6129  C CD  . PRO B 1 137 ? -15.506 37.261  -5.900  1.00 41.86  ? 137 PRO B CD  1 
ATOM   6130  N N   . ILE B 1 138 ? -14.985 38.918  -10.209 1.00 44.44  ? 138 ILE B N   1 
ATOM   6131  C CA  . ILE B 1 138 ? -15.723 38.938  -11.467 1.00 45.08  ? 138 ILE B CA  1 
ATOM   6132  C C   . ILE B 1 138 ? -14.806 38.533  -12.616 1.00 43.76  ? 138 ILE B C   1 
ATOM   6133  O O   . ILE B 1 138 ? -13.695 39.045  -12.743 1.00 42.21  ? 138 ILE B O   1 
ATOM   6134  C CB  . ILE B 1 138 ? -16.411 40.311  -11.714 1.00 45.38  ? 138 ILE B CB  1 
ATOM   6135  C CG1 . ILE B 1 138 ? -17.830 40.293  -11.148 1.00 44.95  ? 138 ILE B CG1 1 
ATOM   6136  C CG2 . ILE B 1 138 ? -16.517 40.631  -13.200 1.00 45.17  ? 138 ILE B CG2 1 
ATOM   6137  C CD1 . ILE B 1 138 ? -17.930 40.716  -9.720  1.00 46.05  ? 138 ILE B CD1 1 
ATOM   6138  N N   . LYS B 1 139 ? -15.258 37.556  -13.396 1.00 46.08  ? 139 LYS B N   1 
ATOM   6139  C CA  . LYS B 1 139 ? -14.588 37.150  -14.633 1.00 47.12  ? 139 LYS B CA  1 
ATOM   6140  C C   . LYS B 1 139 ? -14.988 38.121  -15.737 1.00 46.86  ? 139 LYS B C   1 
ATOM   6141  O O   . LYS B 1 139 ? -16.155 38.174  -16.127 1.00 46.75  ? 139 LYS B O   1 
ATOM   6142  C CB  . LYS B 1 139 ? -14.994 35.719  -15.016 1.00 48.89  ? 139 LYS B CB  1 
ATOM   6143  C CG  . LYS B 1 139 ? -14.591 34.651  -14.007 1.00 51.04  ? 139 LYS B CG  1 
ATOM   6144  C CD  . LYS B 1 139 ? -15.176 33.291  -14.377 1.00 55.34  ? 139 LYS B CD  1 
ATOM   6145  C CE  . LYS B 1 139 ? -15.183 32.323  -13.192 1.00 59.39  ? 139 LYS B CE  1 
ATOM   6146  N NZ  . LYS B 1 139 ? -13.813 31.858  -12.812 1.00 60.74  ? 139 LYS B NZ  1 
ATOM   6147  N N   . THR B 1 140 ? -14.025 38.908  -16.215 1.00 46.52  ? 140 THR B N   1 
ATOM   6148  C CA  . THR B 1 140 ? -14.301 39.955  -17.196 1.00 48.67  ? 140 THR B CA  1 
ATOM   6149  C C   . THR B 1 140 ? -14.518 39.353  -18.578 1.00 50.62  ? 140 THR B C   1 
ATOM   6150  O O   . THR B 1 140 ? -15.076 40.004  -19.466 1.00 50.14  ? 140 THR B O   1 
ATOM   6151  C CB  . THR B 1 140 ? -13.143 40.976  -17.289 1.00 50.05  ? 140 THR B CB  1 
ATOM   6152  O OG1 . THR B 1 140 ? -11.910 40.291  -17.575 1.00 46.83  ? 140 THR B OG1 1 
ATOM   6153  C CG2 . THR B 1 140 ? -13.007 41.783  -15.982 1.00 49.22  ? 140 THR B CG2 1 
ATOM   6154  N N   . LEU B 1 141 ? -14.062 38.108  -18.746 1.00 50.76  ? 141 LEU B N   1 
ATOM   6155  C CA  . LEU B 1 141 ? -14.118 37.384  -20.027 1.00 52.86  ? 141 LEU B CA  1 
ATOM   6156  C C   . LEU B 1 141 ? -13.103 37.878  -21.051 1.00 51.04  ? 141 LEU B C   1 
ATOM   6157  O O   . LEU B 1 141 ? -12.984 37.316  -22.139 1.00 53.12  ? 141 LEU B O   1 
ATOM   6158  C CB  . LEU B 1 141 ? -15.537 37.357  -20.633 1.00 54.47  ? 141 LEU B CB  1 
ATOM   6159  C CG  . LEU B 1 141 ? -16.637 36.543  -19.937 1.00 57.99  ? 141 LEU B CG  1 
ATOM   6160  C CD1 . LEU B 1 141 ? -17.726 36.217  -20.949 1.00 60.89  ? 141 LEU B CD1 1 
ATOM   6161  C CD2 . LEU B 1 141 ? -16.120 35.264  -19.281 1.00 56.42  ? 141 LEU B CD2 1 
ATOM   6162  N N   . ASN B 1 142 ? -12.367 38.924  -20.711 1.00 47.61  ? 142 ASN B N   1 
ATOM   6163  C CA  . ASN B 1 142 ? -11.161 39.204  -21.451 1.00 46.67  ? 142 ASN B CA  1 
ATOM   6164  C C   . ASN B 1 142 ? -10.070 38.233  -21.038 1.00 45.05  ? 142 ASN B C   1 
ATOM   6165  O O   . ASN B 1 142 ? -9.300  38.490  -20.093 1.00 42.40  ? 142 ASN B O   1 
ATOM   6166  C CB  . ASN B 1 142 ? -10.710 40.639  -21.280 1.00 48.44  ? 142 ASN B CB  1 
ATOM   6167  C CG  . ASN B 1 142 ? -9.840  41.096  -22.425 1.00 51.47  ? 142 ASN B CG  1 
ATOM   6168  O OD1 . ASN B 1 142 ? -9.041  40.319  -22.969 1.00 52.66  ? 142 ASN B OD1 1 
ATOM   6169  N ND2 . ASN B 1 142 ? -9.991  42.350  -22.811 1.00 52.26  ? 142 ASN B ND2 1 
ATOM   6170  N N   . GLY B 1 143 ? -10.021 37.108  -21.753 1.00 42.99  ? 143 GLY B N   1 
ATOM   6171  C CA  . GLY B 1 143 ? -9.263  35.941  -21.332 1.00 41.53  ? 143 GLY B CA  1 
ATOM   6172  C C   . GLY B 1 143 ? -9.641  35.520  -19.918 1.00 43.38  ? 143 GLY B C   1 
ATOM   6173  O O   . GLY B 1 143 ? -10.806 35.562  -19.535 1.00 43.83  ? 143 GLY B O   1 
ATOM   6174  N N   . HIS B 1 144 ? -8.640  35.159  -19.129 1.00 41.88  ? 144 HIS B N   1 
ATOM   6175  C CA  . HIS B 1 144 ? -8.875  34.600  -17.814 1.00 40.85  ? 144 HIS B CA  1 
ATOM   6176  C C   . HIS B 1 144 ? -8.754  35.654  -16.724 1.00 41.41  ? 144 HIS B C   1 
ATOM   6177  O O   . HIS B 1 144 ? -8.626  35.343  -15.547 1.00 41.41  ? 144 HIS B O   1 
ATOM   6178  C CB  . HIS B 1 144 ? -7.963  33.397  -17.591 1.00 38.60  ? 144 HIS B CB  1 
ATOM   6179  C CG  . HIS B 1 144 ? -8.084  32.338  -18.670 1.00 37.80  ? 144 HIS B CG  1 
ATOM   6180  N ND1 . HIS B 1 144 ? -7.187  32.216  -19.684 1.00 37.53  ? 144 HIS B ND1 1 
ATOM   6181  C CD2 . HIS B 1 144 ? -9.057  31.369  -18.895 1.00 38.56  ? 144 HIS B CD2 1 
ATOM   6182  C CE1 . HIS B 1 144 ? -7.563  31.217  -20.497 1.00 35.94  ? 144 HIS B CE1 1 
ATOM   6183  N NE2 . HIS B 1 144 ? -8.703  30.696  -20.020 1.00 37.75  ? 144 HIS B NE2 1 
ATOM   6184  N N   . GLU B 1 145 ? -8.870  36.917  -17.122 1.00 42.53  ? 145 GLU B N   1 
ATOM   6185  C CA  . GLU B 1 145 ? -8.783  38.031  -16.198 1.00 42.05  ? 145 GLU B CA  1 
ATOM   6186  C C   . GLU B 1 145 ? -9.850  37.921  -15.112 1.00 42.28  ? 145 GLU B C   1 
ATOM   6187  O O   . GLU B 1 145 ? -11.012 37.644  -15.401 1.00 43.72  ? 145 GLU B O   1 
ATOM   6188  C CB  . GLU B 1 145 ? -8.915  39.362  -16.950 1.00 42.39  ? 145 GLU B CB  1 
ATOM   6189  C CG  . GLU B 1 145 ? -9.027  40.586  -16.049 1.00 45.70  ? 145 GLU B CG  1 
ATOM   6190  C CD  . GLU B 1 145 ? -9.148  41.893  -16.822 1.00 47.96  ? 145 GLU B CD  1 
ATOM   6191  O OE1 . GLU B 1 145 ? -8.387  42.826  -16.509 1.00 50.26  ? 145 GLU B OE1 1 
ATOM   6192  O OE2 . GLU B 1 145 ? -9.996  41.993  -17.741 1.00 50.61  ? 145 GLU B OE2 1 
ATOM   6193  N N   . ILE B 1 146 ? -9.433  38.112  -13.861 1.00 39.33  ? 146 ILE B N   1 
ATOM   6194  C CA  . ILE B 1 146 ? -10.359 38.244  -12.756 1.00 39.90  ? 146 ILE B CA  1 
ATOM   6195  C C   . ILE B 1 146 ? -10.191 39.610  -12.124 1.00 40.13  ? 146 ILE B C   1 
ATOM   6196  O O   . ILE B 1 146 ? -9.075  40.049  -11.872 1.00 41.25  ? 146 ILE B O   1 
ATOM   6197  C CB  . ILE B 1 146 ? -10.161 37.142  -11.702 1.00 38.12  ? 146 ILE B CB  1 
ATOM   6198  C CG1 . ILE B 1 146 ? -10.705 35.818  -12.239 1.00 36.53  ? 146 ILE B CG1 1 
ATOM   6199  C CG2 . ILE B 1 146 ? -10.874 37.511  -10.405 1.00 38.49  ? 146 ILE B CG2 1 
ATOM   6200  C CD1 . ILE B 1 146 ? -10.421 34.626  -11.356 1.00 35.75  ? 146 ILE B CD1 1 
ATOM   6201  N N   . LYS B 1 147 ? -11.309 40.294  -11.916 1.00 41.79  ? 147 LYS B N   1 
ATOM   6202  C CA  . LYS B 1 147 ? -11.311 41.616  -11.305 1.00 44.01  ? 147 LYS B CA  1 
ATOM   6203  C C   . LYS B 1 147 ? -12.078 41.551  -9.973  1.00 43.47  ? 147 LYS B C   1 
ATOM   6204  O O   . LYS B 1 147 ? -13.158 40.950  -9.890  1.00 41.02  ? 147 LYS B O   1 
ATOM   6205  C CB  . LYS B 1 147 ? -11.913 42.639  -12.280 1.00 50.60  ? 147 LYS B CB  1 
ATOM   6206  C CG  . LYS B 1 147 ? -11.906 44.089  -11.813 1.00 57.49  ? 147 LYS B CG  1 
ATOM   6207  C CD  . LYS B 1 147 ? -12.061 45.052  -12.997 1.00 61.23  ? 147 LYS B CD  1 
ATOM   6208  C CE  . LYS B 1 147 ? -10.828 45.950  -13.153 1.00 65.53  ? 147 LYS B CE  1 
ATOM   6209  N NZ  . LYS B 1 147 ? -10.388 46.143  -14.568 1.00 60.26  ? 147 LYS B NZ  1 
ATOM   6210  N N   . PHE B 1 148 ? -11.480 42.102  -8.920  1.00 40.77  ? 148 PHE B N   1 
ATOM   6211  C CA  . PHE B 1 148 ? -12.093 42.044  -7.603  1.00 39.95  ? 148 PHE B CA  1 
ATOM   6212  C C   . PHE B 1 148 ? -12.793 43.347  -7.317  1.00 39.88  ? 148 PHE B C   1 
ATOM   6213  O O   . PHE B 1 148 ? -12.167 44.397  -7.272  1.00 40.08  ? 148 PHE B O   1 
ATOM   6214  C CB  . PHE B 1 148 ? -11.062 41.740  -6.510  1.00 38.09  ? 148 PHE B CB  1 
ATOM   6215  C CG  . PHE B 1 148 ? -10.561 40.323  -6.524  1.00 38.51  ? 148 PHE B CG  1 
ATOM   6216  C CD1 . PHE B 1 148 ? -11.345 39.289  -6.034  1.00 37.80  ? 148 PHE B CD1 1 
ATOM   6217  C CD2 . PHE B 1 148 ? -9.301  40.021  -7.035  1.00 38.83  ? 148 PHE B CD2 1 
ATOM   6218  C CE1 . PHE B 1 148 ? -10.889 37.979  -6.057  1.00 39.04  ? 148 PHE B CE1 1 
ATOM   6219  C CE2 . PHE B 1 148 ? -8.839  38.713  -7.055  1.00 37.71  ? 148 PHE B CE2 1 
ATOM   6220  C CZ  . PHE B 1 148 ? -9.636  37.692  -6.559  1.00 37.86  ? 148 PHE B CZ  1 
ATOM   6221  N N   . ILE B 1 149 ? -14.099 43.268  -7.119  1.00 40.73  ? 149 ILE B N   1 
ATOM   6222  C CA  . ILE B 1 149 ? -14.904 44.450  -6.895  1.00 44.83  ? 149 ILE B CA  1 
ATOM   6223  C C   . ILE B 1 149 ? -15.316 44.499  -5.434  1.00 45.16  ? 149 ILE B C   1 
ATOM   6224  O O   . ILE B 1 149 ? -15.696 43.484  -4.862  1.00 45.74  ? 149 ILE B O   1 
ATOM   6225  C CB  . ILE B 1 149 ? -16.136 44.469  -7.826  1.00 44.43  ? 149 ILE B CB  1 
ATOM   6226  C CG1 . ILE B 1 149 ? -15.678 44.476  -9.283  1.00 47.41  ? 149 ILE B CG1 1 
ATOM   6227  C CG2 . ILE B 1 149 ? -17.011 45.684  -7.563  1.00 45.41  ? 149 ILE B CG2 1 
ATOM   6228  C CD1 . ILE B 1 149 ? -14.524 45.423  -9.564  1.00 46.81  ? 149 ILE B CD1 1 
ATOM   6229  N N   . ARG B 1 150 ? -15.170 45.668  -4.830  1.00 47.89  ? 150 ARG B N   1 
ATOM   6230  C CA  . ARG B 1 150 ? -15.628 45.918  -3.464  1.00 53.25  ? 150 ARG B CA  1 
ATOM   6231  C C   . ARG B 1 150 ? -17.081 45.442  -3.350  1.00 53.89  ? 150 ARG B C   1 
ATOM   6232  O O   . ARG B 1 150 ? -17.923 45.796  -4.185  1.00 54.72  ? 150 ARG B O   1 
ATOM   6233  C CB  . ARG B 1 150 ? -15.514 47.416  -3.166  1.00 58.41  ? 150 ARG B CB  1 
ATOM   6234  C CG  . ARG B 1 150 ? -15.616 47.797  -1.708  1.00 66.75  ? 150 ARG B CG  1 
ATOM   6235  C CD  . ARG B 1 150 ? -14.249 47.850  -1.050  1.00 71.09  ? 150 ARG B CD  1 
ATOM   6236  N NE  . ARG B 1 150 ? -14.345 48.054  0.401   1.00 72.45  ? 150 ARG B NE  1 
ATOM   6237  C CZ  . ARG B 1 150 ? -14.618 47.091  1.285   1.00 73.47  ? 150 ARG B CZ  1 
ATOM   6238  N NH1 . ARG B 1 150 ? -14.830 45.841  0.878   1.00 67.61  ? 150 ARG B NH1 1 
ATOM   6239  N NH2 . ARG B 1 150 ? -14.689 47.381  2.584   1.00 73.84  ? 150 ARG B NH2 1 
ATOM   6240  N N   . LYS B 1 151 ? -17.362 44.615  -2.343  1.00 53.80  ? 151 LYS B N   1 
ATOM   6241  C CA  . LYS B 1 151 ? -18.640 43.897  -2.252  1.00 56.45  ? 151 LYS B CA  1 
ATOM   6242  C C   . LYS B 1 151 ? -19.852 44.827  -2.170  1.00 60.04  ? 151 LYS B C   1 
ATOM   6243  O O   . LYS B 1 151 ? -20.881 44.563  -2.791  1.00 61.05  ? 151 LYS B O   1 
ATOM   6244  C CB  . LYS B 1 151 ? -18.632 42.936  -1.065  1.00 57.54  ? 151 LYS B CB  1 
ATOM   6245  C CG  . LYS B 1 151 ? -19.486 41.695  -1.261  1.00 60.15  ? 151 LYS B CG  1 
ATOM   6246  C CD  . LYS B 1 151 ? -19.038 40.580  -0.329  1.00 62.43  ? 151 LYS B CD  1 
ATOM   6247  C CE  . LYS B 1 151 ? -20.034 39.431  -0.306  1.00 64.78  ? 151 LYS B CE  1 
ATOM   6248  N NZ  . LYS B 1 151 ? -19.478 38.237  0.390   1.00 66.94  ? 151 LYS B NZ  1 
ATOM   6249  N N   . GLU B 1 152 ? -19.720 45.914  -1.415  1.00 61.32  ? 152 GLU B N   1 
ATOM   6250  C CA  . GLU B 1 152 ? -20.790 46.905  -1.289  1.00 67.22  ? 152 GLU B CA  1 
ATOM   6251  C C   . GLU B 1 152 ? -21.054 47.634  -2.606  1.00 66.41  ? 152 GLU B C   1 
ATOM   6252  O O   . GLU B 1 152 ? -22.212 47.876  -2.964  1.00 66.58  ? 152 GLU B O   1 
ATOM   6253  C CB  . GLU B 1 152 ? -20.521 47.904  -0.141  1.00 70.51  ? 152 GLU B CB  1 
ATOM   6254  C CG  . GLU B 1 152 ? -19.065 48.010  0.306   1.00 76.07  ? 152 GLU B CG  1 
ATOM   6255  C CD  . GLU B 1 152 ? -18.591 46.786  1.082   1.00 79.67  ? 152 GLU B CD  1 
ATOM   6256  O OE1 . GLU B 1 152 ? -19.306 46.347  2.011   1.00 84.27  ? 152 GLU B OE1 1 
ATOM   6257  O OE2 . GLU B 1 152 ? -17.505 46.256  0.757   1.00 78.94  ? 152 GLU B OE2 1 
ATOM   6258  N N   . GLU B 1 153 ? -19.983 47.958  -3.331  1.00 66.17  ? 153 GLU B N   1 
ATOM   6259  C CA  . GLU B 1 153 ? -20.101 48.532  -4.674  1.00 64.74  ? 153 GLU B CA  1 
ATOM   6260  C C   . GLU B 1 153 ? -20.834 47.575  -5.599  1.00 63.16  ? 153 GLU B C   1 
ATOM   6261  O O   . GLU B 1 153 ? -21.685 47.991  -6.388  1.00 65.65  ? 153 GLU B O   1 
ATOM   6262  C CB  . GLU B 1 153 ? -18.727 48.841  -5.261  1.00 66.61  ? 153 GLU B CB  1 
ATOM   6263  C CG  . GLU B 1 153 ? -18.070 50.110  -4.746  1.00 71.95  ? 153 GLU B CG  1 
ATOM   6264  C CD  . GLU B 1 153 ? -16.627 50.239  -5.211  1.00 76.58  ? 153 GLU B CD  1 
ATOM   6265  O OE1 . GLU B 1 153 ? -16.353 49.950  -6.401  1.00 81.33  ? 153 GLU B OE1 1 
ATOM   6266  O OE2 . GLU B 1 153 ? -15.763 50.618  -4.390  1.00 79.01  ? 153 GLU B OE2 1 
ATOM   6267  N N   . TYR B 1 154 ? -20.506 46.291  -5.502  1.00 60.60  ? 154 TYR B N   1 
ATOM   6268  C CA  . TYR B 1 154 ? -21.134 45.302  -6.354  1.00 59.48  ? 154 TYR B CA  1 
ATOM   6269  C C   . TYR B 1 154 ? -22.609 45.117  -6.019  1.00 61.17  ? 154 TYR B C   1 
ATOM   6270  O O   . TYR B 1 154 ? -23.443 45.046  -6.920  1.00 63.59  ? 154 TYR B O   1 
ATOM   6271  C CB  . TYR B 1 154 ? -20.417 43.955  -6.299  1.00 57.25  ? 154 TYR B CB  1 
ATOM   6272  C CG  . TYR B 1 154 ? -21.219 42.875  -6.981  1.00 58.03  ? 154 TYR B CG  1 
ATOM   6273  C CD1 . TYR B 1 154 ? -21.266 42.795  -8.375  1.00 59.29  ? 154 TYR B CD1 1 
ATOM   6274  C CD2 . TYR B 1 154 ? -21.982 41.979  -6.243  1.00 57.23  ? 154 TYR B CD2 1 
ATOM   6275  C CE1 . TYR B 1 154 ? -22.029 41.829  -9.013  1.00 61.70  ? 154 TYR B CE1 1 
ATOM   6276  C CE2 . TYR B 1 154 ? -22.748 41.007  -6.867  1.00 61.89  ? 154 TYR B CE2 1 
ATOM   6277  C CZ  . TYR B 1 154 ? -22.772 40.935  -8.252  1.00 64.01  ? 154 TYR B CZ  1 
ATOM   6278  O OH  . TYR B 1 154 ? -23.531 39.967  -8.879  1.00 64.01  ? 154 TYR B OH  1 
ATOM   6279  N N   . ILE B 1 155 ? -22.923 45.006  -4.730  1.00 59.79  ? 155 ILE B N   1 
ATOM   6280  C CA  . ILE B 1 155 ? -24.311 44.859  -4.300  1.00 60.39  ? 155 ILE B CA  1 
ATOM   6281  C C   . ILE B 1 155 ? -25.127 46.103  -4.660  1.00 62.00  ? 155 ILE B C   1 
ATOM   6282  O O   . ILE B 1 155 ? -26.248 45.995  -5.153  1.00 63.12  ? 155 ILE B O   1 
ATOM   6283  C CB  . ILE B 1 155 ? -24.417 44.528  -2.801  1.00 59.87  ? 155 ILE B CB  1 
ATOM   6284  C CG1 . ILE B 1 155 ? -23.954 43.084  -2.554  1.00 58.12  ? 155 ILE B CG1 1 
ATOM   6285  C CG2 . ILE B 1 155 ? -25.847 44.722  -2.301  1.00 59.88  ? 155 ILE B CG2 1 
ATOM   6286  C CD1 . ILE B 1 155 ? -23.560 42.797  -1.122  1.00 57.53  ? 155 ILE B CD1 1 
ATOM   6287  N N   . SER B 1 156 ? -24.540 47.275  -4.443  1.00 62.06  ? 156 SER B N   1 
ATOM   6288  C CA  . SER B 1 156 ? -25.112 48.527  -4.917  1.00 64.11  ? 156 SER B CA  1 
ATOM   6289  C C   . SER B 1 156 ? -25.436 48.455  -6.415  1.00 67.60  ? 156 SER B C   1 
ATOM   6290  O O   . SER B 1 156 ? -26.526 48.858  -6.848  1.00 69.65  ? 156 SER B O   1 
ATOM   6291  C CB  . SER B 1 156 ? -24.153 49.685  -4.622  1.00 64.97  ? 156 SER B CB  1 
ATOM   6292  O OG  . SER B 1 156 ? -24.467 50.831  -5.390  1.00 68.10  ? 156 SER B OG  1 
ATOM   6293  N N   . PHE B 1 157 ? -24.491 47.927  -7.196  1.00 66.61  ? 157 PHE B N   1 
ATOM   6294  C CA  . PHE B 1 157 ? -24.673 47.754  -8.637  1.00 64.51  ? 157 PHE B CA  1 
ATOM   6295  C C   . PHE B 1 157 ? -25.724 46.686  -8.969  1.00 64.41  ? 157 PHE B C   1 
ATOM   6296  O O   . PHE B 1 157 ? -26.575 46.895  -9.836  1.00 66.37  ? 157 PHE B O   1 
ATOM   6297  C CB  . PHE B 1 157 ? -23.337 47.434  -9.314  1.00 62.81  ? 157 PHE B CB  1 
ATOM   6298  C CG  . PHE B 1 157 ? -23.479 46.871  -10.698 1.00 64.61  ? 157 PHE B CG  1 
ATOM   6299  C CD1 . PHE B 1 157 ? -23.563 47.718  -11.807 1.00 65.81  ? 157 PHE B CD1 1 
ATOM   6300  C CD2 . PHE B 1 157 ? -23.534 45.489  -10.901 1.00 62.92  ? 157 PHE B CD2 1 
ATOM   6301  C CE1 . PHE B 1 157 ? -23.701 47.200  -13.084 1.00 65.27  ? 157 PHE B CE1 1 
ATOM   6302  C CE2 . PHE B 1 157 ? -23.677 44.967  -12.176 1.00 63.78  ? 157 PHE B CE2 1 
ATOM   6303  C CZ  . PHE B 1 157 ? -23.756 45.823  -13.269 1.00 65.96  ? 157 PHE B CZ  1 
ATOM   6304  N N   . GLU B 1 158 ? -25.651 45.548  -8.281  1.00 61.77  ? 158 GLU B N   1 
ATOM   6305  C CA  . GLU B 1 158 ? -26.592 44.437  -8.467  1.00 63.03  ? 158 GLU B CA  1 
ATOM   6306  C C   . GLU B 1 158 ? -28.044 44.863  -8.195  1.00 65.69  ? 158 GLU B C   1 
ATOM   6307  O O   . GLU B 1 158 ? -28.973 44.367  -8.836  1.00 65.50  ? 158 GLU B O   1 
ATOM   6308  C CB  . GLU B 1 158 ? -26.202 43.271  -7.552  1.00 63.32  ? 158 GLU B CB  1 
ATOM   6309  C CG  . GLU B 1 158 ? -26.958 41.964  -7.760  1.00 62.58  ? 158 GLU B CG  1 
ATOM   6310  C CD  . GLU B 1 158 ? -26.699 40.953  -6.640  1.00 64.95  ? 158 GLU B CD  1 
ATOM   6311  O OE1 . GLU B 1 158 ? -26.823 39.735  -6.890  1.00 64.56  ? 158 GLU B OE1 1 
ATOM   6312  O OE2 . GLU B 1 158 ? -26.366 41.373  -5.503  1.00 64.68  ? 158 GLU B OE2 1 
ATOM   6313  N N   . SER B 1 159 ? -28.229 45.785  -7.252  1.00 65.62  ? 159 SER B N   1 
ATOM   6314  C CA  . SER B 1 159 ? -29.567 46.233  -6.873  1.00 68.52  ? 159 SER B CA  1 
ATOM   6315  C C   . SER B 1 159 ? -30.149 47.246  -7.853  1.00 71.23  ? 159 SER B C   1 
ATOM   6316  O O   . SER B 1 159 ? -31.341 47.194  -8.165  1.00 73.03  ? 159 SER B O   1 
ATOM   6317  C CB  . SER B 1 159 ? -29.573 46.796  -5.455  1.00 66.71  ? 159 SER B CB  1 
ATOM   6318  O OG  . SER B 1 159 ? -29.612 45.748  -4.505  1.00 66.24  ? 159 SER B OG  1 
ATOM   6319  N N   . LYS B 1 160 ? -29.307 48.164  -8.326  1.00 73.25  ? 160 LYS B N   1 
ATOM   6320  C CA  . LYS B 1 160 ? -29.700 49.139  -9.347  1.00 76.14  ? 160 LYS B CA  1 
ATOM   6321  C C   . LYS B 1 160 ? -30.227 48.440  -10.601 1.00 77.41  ? 160 LYS B C   1 
ATOM   6322  O O   . LYS B 1 160 ? -31.193 48.897  -11.222 1.00 80.60  ? 160 LYS B O   1 
ATOM   6323  C CB  . LYS B 1 160 ? -28.522 50.055  -9.707  1.00 78.13  ? 160 LYS B CB  1 
ATOM   6324  C CG  . LYS B 1 160 ? -28.798 51.008  -10.868 1.00 81.90  ? 160 LYS B CG  1 
ATOM   6325  C CD  . LYS B 1 160 ? -27.516 51.418  -11.579 1.00 85.01  ? 160 LYS B CD  1 
ATOM   6326  C CE  . LYS B 1 160 ? -27.781 51.759  -13.041 1.00 88.11  ? 160 LYS B CE  1 
ATOM   6327  N NZ  . LYS B 1 160 ? -26.520 51.952  -13.813 1.00 85.77  ? 160 LYS B NZ  1 
ATOM   6328  N N   . VAL B 1 161 ? -29.595 47.326  -10.957 1.00 76.39  ? 161 VAL B N   1 
ATOM   6329  C CA  . VAL B 1 161 ? -29.982 46.555  -12.134 1.00 77.15  ? 161 VAL B CA  1 
ATOM   6330  C C   . VAL B 1 161 ? -31.207 45.686  -11.828 1.00 79.28  ? 161 VAL B C   1 
ATOM   6331  O O   . VAL B 1 161 ? -32.096 45.523  -12.677 1.00 81.35  ? 161 VAL B O   1 
ATOM   6332  C CB  . VAL B 1 161 ? -28.799 45.704  -12.663 1.00 74.15  ? 161 VAL B CB  1 
ATOM   6333  C CG1 . VAL B 1 161 ? -29.252 44.738  -13.748 1.00 71.46  ? 161 VAL B CG1 1 
ATOM   6334  C CG2 . VAL B 1 161 ? -27.685 46.610  -13.180 1.00 72.23  ? 161 VAL B CG2 1 
ATOM   6335  N N   . PHE B 1 162 ? -31.259 45.151  -10.611 1.00 78.88  ? 162 PHE B N   1 
ATOM   6336  C CA  . PHE B 1 162 ? -32.426 44.411  -10.142 1.00 83.44  ? 162 PHE B CA  1 
ATOM   6337  C C   . PHE B 1 162 ? -33.682 45.285  -10.204 1.00 86.30  ? 162 PHE B C   1 
ATOM   6338  O O   . PHE B 1 162 ? -34.763 44.799  -10.531 1.00 84.55  ? 162 PHE B O   1 
ATOM   6339  C CB  . PHE B 1 162 ? -32.190 43.885  -8.719  1.00 85.76  ? 162 PHE B CB  1 
ATOM   6340  C CG  . PHE B 1 162 ? -33.427 43.344  -8.045  1.00 90.25  ? 162 PHE B CG  1 
ATOM   6341  C CD1 . PHE B 1 162 ? -34.137 42.277  -8.597  1.00 92.70  ? 162 PHE B CD1 1 
ATOM   6342  C CD2 . PHE B 1 162 ? -33.870 43.887  -6.838  1.00 92.43  ? 162 PHE B CD2 1 
ATOM   6343  C CE1 . PHE B 1 162 ? -35.273 41.780  -7.967  1.00 96.49  ? 162 PHE B CE1 1 
ATOM   6344  C CE2 . PHE B 1 162 ? -35.006 43.393  -6.206  1.00 93.47  ? 162 PHE B CE2 1 
ATOM   6345  C CZ  . PHE B 1 162 ? -35.707 42.338  -6.770  1.00 94.80  ? 162 PHE B CZ  1 
ATOM   6346  N N   . HIS B 1 163 ? -33.519 46.578  -9.924  1.00 88.79  ? 163 HIS B N   1 
ATOM   6347  C CA  . HIS B 1 163 ? -34.637 47.525  -9.916  1.00 92.88  ? 163 HIS B CA  1 
ATOM   6348  C C   . HIS B 1 163 ? -34.996 48.081  -11.275 1.00 93.58  ? 163 HIS B C   1 
ATOM   6349  O O   . HIS B 1 163 ? -36.004 48.780  -11.417 1.00 93.62  ? 163 HIS B O   1 
ATOM   6350  C CB  . HIS B 1 163 ? -34.384 48.650  -8.916  1.00 95.03  ? 163 HIS B CB  1 
ATOM   6351  C CG  . HIS B 1 163 ? -34.768 48.297  -7.499  1.00 99.13  ? 163 HIS B CG  1 
ATOM   6352  N ND1 . HIS B 1 163 ? -33.859 47.965  -6.561  1.00 99.17  ? 163 HIS B ND1 1 
ATOM   6353  C CD2 . HIS B 1 163 ? -36.018 48.213  -6.883  1.00 100.80 ? 163 HIS B CD2 1 
ATOM   6354  C CE1 . HIS B 1 163 ? -34.491 47.693  -5.404  1.00 99.91  ? 163 HIS B CE1 1 
ATOM   6355  N NE2 . HIS B 1 163 ? -35.812 47.842  -5.604  1.00 102.16 ? 163 HIS B NE2 1 
ATOM   6356  N N   . LYS B 1 164 ? -34.178 47.776  -12.284 1.00 92.37  ? 164 LYS B N   1 
ATOM   6357  C CA  . LYS B 1 164 ? -34.498 48.108  -13.676 1.00 92.56  ? 164 LYS B CA  1 
ATOM   6358  C C   . LYS B 1 164 ? -35.144 46.922  -14.393 1.00 92.12  ? 164 LYS B C   1 
ATOM   6359  O O   . LYS B 1 164 ? -36.074 47.093  -15.184 1.00 91.32  ? 164 LYS B O   1 
ATOM   6360  C CB  . LYS B 1 164 ? -33.248 48.563  -14.430 1.00 93.80  ? 164 LYS B CB  1 
ATOM   6361  C CG  . LYS B 1 164 ? -32.891 50.028  -14.238 1.00 95.67  ? 164 LYS B CG  1 
ATOM   6362  C CD  . LYS B 1 164 ? -31.753 50.425  -15.166 1.00 97.19  ? 164 LYS B CD  1 
ATOM   6363  C CE  . LYS B 1 164 ? -31.269 51.836  -14.884 1.00 99.40  ? 164 LYS B CE  1 
ATOM   6364  N NZ  . LYS B 1 164 ? -30.011 52.129  -15.625 1.00 100.58 ? 164 LYS B NZ  1 
ATOM   6365  N N   . LEU B 1 165 ? -34.629 45.723  -14.120 1.00 92.04  ? 165 LEU B N   1 
ATOM   6366  C CA  . LEU B 1 165 ? -35.265 44.477  -14.550 1.00 92.21  ? 165 LEU B CA  1 
ATOM   6367  C C   . LEU B 1 165 ? -36.625 44.347  -13.880 1.00 94.18  ? 165 LEU B C   1 
ATOM   6368  O O   . LEU B 1 165 ? -37.514 43.660  -14.382 1.00 95.13  ? 165 LEU B O   1 
ATOM   6369  C CB  . LEU B 1 165 ? -34.382 43.272  -14.190 1.00 90.13  ? 165 LEU B CB  1 
ATOM   6370  C CG  . LEU B 1 165 ? -33.453 42.649  -15.248 1.00 88.24  ? 165 LEU B CG  1 
ATOM   6371  C CD1 . LEU B 1 165 ? -32.808 43.685  -16.157 1.00 86.53  ? 165 LEU B CD1 1 
ATOM   6372  C CD2 . LEU B 1 165 ? -32.393 41.782  -14.580 1.00 83.05  ? 165 LEU B CD2 1 
ATOM   6373  N N   . LYS B 1 166 ? -36.762 45.021  -12.738 1.00 96.95  ? 166 LYS B N   1 
ATOM   6374  C CA  . LYS B 1 166 ? -38.027 45.162  -12.027 1.00 99.65  ? 166 LYS B CA  1 
ATOM   6375  C C   . LYS B 1 166 ? -38.992 46.037  -12.828 1.00 101.28 ? 166 LYS B C   1 
ATOM   6376  O O   . LYS B 1 166 ? -39.928 45.530  -13.446 1.00 99.87  ? 166 LYS B O   1 
ATOM   6377  C CB  . LYS B 1 166 ? -37.778 45.783  -10.647 1.00 102.16 ? 166 LYS B CB  1 
ATOM   6378  C CG  . LYS B 1 166 ? -38.860 45.542  -9.602  1.00 106.60 ? 166 LYS B CG  1 
ATOM   6379  C CD  . LYS B 1 166 ? -38.489 46.219  -8.286  1.00 105.61 ? 166 LYS B CD  1 
ATOM   6380  C CE  . LYS B 1 166 ? -39.179 45.573  -7.097  1.00 106.11 ? 166 LYS B CE  1 
ATOM   6381  N NZ  . LYS B 1 166 ? -38.620 46.062  -5.807  1.00 105.81 ? 166 LYS B NZ  1 
ATOM   6382  N N   . LYS B 1 167 ? -38.745 47.348  -12.834 1.00 102.64 ? 167 LYS B N   1 
ATOM   6383  C CA  . LYS B 1 167 ? -39.676 48.302  -13.441 1.00 106.07 ? 167 LYS B CA  1 
ATOM   6384  C C   . LYS B 1 167 ? -39.557 48.372  -14.962 1.00 108.66 ? 167 LYS B C   1 
ATOM   6385  O O   . LYS B 1 167 ? -39.771 49.420  -15.573 1.00 114.12 ? 167 LYS B O   1 
ATOM   6386  C CB  . LYS B 1 167 ? -39.566 49.689  -12.792 1.00 108.29 ? 167 LYS B CB  1 
ATOM   6387  C CG  . LYS B 1 167 ? -40.255 49.777  -11.432 1.00 107.93 ? 167 LYS B CG  1 
ATOM   6388  C CD  . LYS B 1 167 ? -40.951 51.113  -11.229 1.00 106.98 ? 167 LYS B CD  1 
ATOM   6389  C CE  . LYS B 1 167 ? -41.810 51.089  -9.976  1.00 106.30 ? 167 LYS B CE  1 
ATOM   6390  N NZ  . LYS B 1 167 ? -42.609 52.335  -9.827  1.00 105.26 ? 167 LYS B NZ  1 
ATOM   6391  N N   . MET B 1 168 ? -39.202 47.241  -15.558 1.00 108.45 ? 168 MET B N   1 
ATOM   6392  C CA  . MET B 1 168 ? -39.399 47.005  -16.976 1.00 107.98 ? 168 MET B CA  1 
ATOM   6393  C C   . MET B 1 168 ? -39.924 45.584  -17.126 1.00 108.69 ? 168 MET B C   1 
ATOM   6394  O O   . MET B 1 168 ? -40.018 44.849  -16.146 1.00 108.67 ? 168 MET B O   1 
ATOM   6395  C CB  . MET B 1 168 ? -38.095 47.199  -17.748 1.00 106.95 ? 168 MET B CB  1 
ATOM   6396  C CG  . MET B 1 168 ? -37.683 48.654  -17.902 1.00 108.69 ? 168 MET B CG  1 
ATOM   6397  S SD  . MET B 1 168 ? -36.051 48.860  -18.639 1.00 112.15 ? 168 MET B SD  1 
ATOM   6398  C CE  . MET B 1 168 ? -35.990 50.642  -18.829 1.00 112.98 ? 168 MET B CE  1 
ATOM   6399  N N   . LYS B 1 169 ? -40.272 45.202  -18.347 1.00 113.20 ? 169 LYS B N   1 
ATOM   6400  C CA  . LYS B 1 169 ? -40.943 43.922  -18.598 1.00 117.91 ? 169 LYS B CA  1 
ATOM   6401  C C   . LYS B 1 169 ? -40.164 42.709  -18.056 1.00 114.78 ? 169 LYS B C   1 
ATOM   6402  O O   . LYS B 1 169 ? -40.754 41.678  -17.719 1.00 114.91 ? 169 LYS B O   1 
ATOM   6403  C CB  . LYS B 1 169 ? -41.200 43.756  -20.106 1.00 120.90 ? 169 LYS B CB  1 
ATOM   6404  C CG  . LYS B 1 169 ? -42.334 42.801  -20.450 1.00 123.01 ? 169 LYS B CG  1 
ATOM   6405  C CD  . LYS B 1 169 ? -42.613 42.774  -21.944 1.00 122.24 ? 169 LYS B CD  1 
ATOM   6406  C CE  . LYS B 1 169 ? -43.847 41.940  -22.244 1.00 121.87 ? 169 LYS B CE  1 
ATOM   6407  N NZ  . LYS B 1 169 ? -44.174 41.948  -23.692 1.00 124.25 ? 169 LYS B NZ  1 
ATOM   6408  N N   . TYR B 1 170 ? -38.851 42.881  -17.919 1.00 110.24 ? 170 TYR B N   1 
ATOM   6409  C CA  . TYR B 1 170 ? -37.879 41.779  -17.894 1.00 104.99 ? 170 TYR B CA  1 
ATOM   6410  C C   . TYR B 1 170 ? -38.065 40.721  -16.799 1.00 100.83 ? 170 TYR B C   1 
ATOM   6411  O O   . TYR B 1 170 ? -37.947 39.521  -17.065 1.00 96.64  ? 170 TYR B O   1 
ATOM   6412  C CB  . TYR B 1 170 ? -36.455 42.350  -17.861 1.00 104.99 ? 170 TYR B CB  1 
ATOM   6413  C CG  . TYR B 1 170 ? -36.128 43.234  -19.051 1.00 106.33 ? 170 TYR B CG  1 
ATOM   6414  C CD1 . TYR B 1 170 ? -35.028 42.966  -19.858 1.00 105.59 ? 170 TYR B CD1 1 
ATOM   6415  C CD2 . TYR B 1 170 ? -36.932 44.329  -19.377 1.00 109.30 ? 170 TYR B CD2 1 
ATOM   6416  C CE1 . TYR B 1 170 ? -34.728 43.770  -20.948 1.00 106.79 ? 170 TYR B CE1 1 
ATOM   6417  C CE2 . TYR B 1 170 ? -36.646 45.131  -20.468 1.00 109.96 ? 170 TYR B CE2 1 
ATOM   6418  C CZ  . TYR B 1 170 ? -35.544 44.848  -21.250 1.00 110.64 ? 170 TYR B CZ  1 
ATOM   6419  O OH  . TYR B 1 170 ? -35.251 45.645  -22.333 1.00 112.90 ? 170 TYR B OH  1 
ATOM   6420  N N   . LEU B 1 171 ? -38.355 41.165  -15.579 1.00 98.98  ? 171 LEU B N   1 
ATOM   6421  C CA  . LEU B 1 171 ? -38.438 40.256  -14.439 1.00 99.86  ? 171 LEU B CA  1 
ATOM   6422  C C   . LEU B 1 171 ? -39.746 40.419  -13.656 1.00 102.79 ? 171 LEU B C   1 
ATOM   6423  O O   . LEU B 1 171 ? -39.995 41.466  -13.050 1.00 102.10 ? 171 LEU B O   1 
ATOM   6424  C CB  . LEU B 1 171 ? -37.226 40.458  -13.522 1.00 98.21  ? 171 LEU B CB  1 
ATOM   6425  C CG  . LEU B 1 171 ? -36.663 39.260  -12.748 1.00 97.09  ? 171 LEU B CG  1 
ATOM   6426  C CD1 . LEU B 1 171 ? -36.427 38.060  -13.654 1.00 95.36  ? 171 LEU B CD1 1 
ATOM   6427  C CD2 . LEU B 1 171 ? -35.375 39.654  -12.039 1.00 95.45  ? 171 LEU B CD2 1 
ATOM   6428  N N   . VAL B 1 172 ? -40.577 39.377  -13.679 1.00 105.64 ? 172 VAL B N   1 
ATOM   6429  C CA  . VAL B 1 172 ? -41.864 39.380  -12.973 1.00 107.26 ? 172 VAL B CA  1 
ATOM   6430  C C   . VAL B 1 172 ? -41.898 38.261  -11.924 1.00 110.09 ? 172 VAL B C   1 
ATOM   6431  O O   . VAL B 1 172 ? -41.810 37.081  -12.264 1.00 112.38 ? 172 VAL B O   1 
ATOM   6432  C CB  . VAL B 1 172 ? -43.059 39.216  -13.956 1.00 105.60 ? 172 VAL B CB  1 
ATOM   6433  C CG1 . VAL B 1 172 ? -44.389 39.282  -13.212 1.00 104.89 ? 172 VAL B CG1 1 
ATOM   6434  C CG2 . VAL B 1 172 ? -43.013 40.271  -15.056 1.00 101.98 ? 172 VAL B CG2 1 
ATOM   6435  N N   . GLU B 1 173 ? -42.021 38.637  -10.652 1.00 112.81 ? 173 GLU B N   1 
ATOM   6436  C CA  . GLU B 1 173 ? -42.120 37.663  -9.560  1.00 118.54 ? 173 GLU B CA  1 
ATOM   6437  C C   . GLU B 1 173 ? -43.424 36.863  -9.656  1.00 125.04 ? 173 GLU B C   1 
ATOM   6438  O O   . GLU B 1 173 ? -44.438 37.379  -10.130 1.00 125.76 ? 173 GLU B O   1 
ATOM   6439  C CB  . GLU B 1 173 ? -42.038 38.373  -8.202  1.00 118.68 ? 173 GLU B CB  1 
ATOM   6440  C CG  . GLU B 1 173 ? -41.581 37.482  -7.053  1.00 118.46 ? 173 GLU B CG  1 
ATOM   6441  C CD  . GLU B 1 173 ? -42.148 37.898  -5.704  1.00 120.71 ? 173 GLU B CD  1 
ATOM   6442  O OE1 . GLU B 1 173 ? -42.749 38.992  -5.606  1.00 121.11 ? 173 GLU B OE1 1 
ATOM   6443  O OE2 . GLU B 1 173 ? -41.991 37.124  -4.735  1.00 120.86 ? 173 GLU B OE2 1 
ATOM   6444  N N   . VAL B 1 174 ? -43.390 35.605  -9.212  1.00 133.60 ? 174 VAL B N   1 
ATOM   6445  C CA  . VAL B 1 174 ? -44.597 34.763  -9.177  1.00 144.91 ? 174 VAL B CA  1 
ATOM   6446  C C   . VAL B 1 174 ? -44.577 33.706  -8.046  1.00 151.31 ? 174 VAL B C   1 
ATOM   6447  O O   . VAL B 1 174 ? -44.240 32.539  -8.268  1.00 155.48 ? 174 VAL B O   1 
ATOM   6448  C CB  . VAL B 1 174 ? -44.913 34.141  -10.572 1.00 145.20 ? 174 VAL B CB  1 
ATOM   6449  C CG1 . VAL B 1 174 ? -43.772 33.257  -11.064 1.00 142.09 ? 174 VAL B CG1 1 
ATOM   6450  C CG2 . VAL B 1 174 ? -46.247 33.399  -10.557 1.00 148.22 ? 174 VAL B CG2 1 
ATOM   6451  N N   . GLN B 1 175 ? -44.935 34.144  -6.836  1.00 155.70 ? 175 GLN B N   1 
ATOM   6452  C CA  . GLN B 1 175 ? -45.032 33.273  -5.644  1.00 160.73 ? 175 GLN B CA  1 
ATOM   6453  C C   . GLN B 1 175 ? -43.752 32.490  -5.291  1.00 165.83 ? 175 GLN B C   1 
ATOM   6454  O O   . GLN B 1 175 ? -42.701 32.684  -5.907  1.00 166.87 ? 175 GLN B O   1 
ATOM   6455  C CB  . GLN B 1 175 ? -46.244 32.335  -5.738  1.00 159.62 ? 175 GLN B CB  1 
ATOM   6456  C CG  . GLN B 1 175 ? -47.577 33.017  -5.464  1.00 159.08 ? 175 GLN B CG  1 
ATOM   6457  C CD  . GLN B 1 175 ? -48.669 32.043  -5.057  1.00 159.16 ? 175 GLN B CD  1 
ATOM   6458  O OE1 . GLN B 1 175 ? -48.579 30.842  -5.313  1.00 159.43 ? 175 GLN B OE1 1 
ATOM   6459  N NE2 . GLN B 1 175 ? -49.712 32.561  -4.421  1.00 157.15 ? 175 GLN B NE2 1 
ATOM   6460  N N   . ASP B 1 176 ? -43.856 31.618  -4.286  1.00 170.60 ? 176 ASP B N   1 
ATOM   6461  C CA  . ASP B 1 176 ? -42.707 30.878  -3.752  1.00 174.38 ? 176 ASP B CA  1 
ATOM   6462  C C   . ASP B 1 176 ? -43.112 29.439  -3.391  1.00 178.64 ? 176 ASP B C   1 
ATOM   6463  O O   . ASP B 1 176 ? -44.255 29.213  -2.990  1.00 179.02 ? 176 ASP B O   1 
ATOM   6464  C CB  . ASP B 1 176 ? -42.167 31.582  -2.496  1.00 171.94 ? 176 ASP B CB  1 
ATOM   6465  C CG  . ASP B 1 176 ? -41.597 32.963  -2.790  1.00 170.73 ? 176 ASP B CG  1 
ATOM   6466  O OD1 . ASP B 1 176 ? -40.784 33.094  -3.730  1.00 173.23 ? 176 ASP B OD1 1 
ATOM   6467  O OD2 . ASP B 1 176 ? -41.952 33.915  -2.064  1.00 169.21 ? 176 ASP B OD2 1 
ATOM   6468  N N   . GLU B 1 177 ? -42.209 28.457  -3.536  1.00 182.17 ? 177 GLU B N   1 
ATOM   6469  C CA  . GLU B 1 177 ? -40.897 28.583  -4.204  1.00 180.50 ? 177 GLU B CA  1 
ATOM   6470  C C   . GLU B 1 177 ? -40.393 27.191  -4.627  1.00 180.41 ? 177 GLU B C   1 
ATOM   6471  O O   . GLU B 1 177 ? -39.203 27.007  -4.904  1.00 177.33 ? 177 GLU B O   1 
ATOM   6472  C CB  . GLU B 1 177 ? -39.854 29.232  -3.277  1.00 178.50 ? 177 GLU B CB  1 
ATOM   6473  C CG  . GLU B 1 177 ? -38.715 29.932  -4.017  1.00 174.06 ? 177 GLU B CG  1 
ATOM   6474  C CD  . GLU B 1 177 ? -37.338 29.580  -3.474  1.00 169.39 ? 177 GLU B CD  1 
ATOM   6475  O OE1 . GLU B 1 177 ? -37.173 29.522  -2.237  1.00 168.17 ? 177 GLU B OE1 1 
ATOM   6476  O OE2 . GLU B 1 177 ? -36.414 29.370  -4.290  1.00 165.06 ? 177 GLU B OE2 1 
ATOM   6477  N N   . VAL B 1 178 ? -41.305 26.222  -4.687  1.00 182.07 ? 178 VAL B N   1 
ATOM   6478  C CA  . VAL B 1 178 ? -40.929 24.800  -4.761  1.00 178.84 ? 178 VAL B CA  1 
ATOM   6479  C C   . VAL B 1 178 ? -40.538 24.316  -6.178  1.00 175.30 ? 178 VAL B C   1 
ATOM   6480  O O   . VAL B 1 178 ? -40.454 23.108  -6.425  1.00 174.39 ? 178 VAL B O   1 
ATOM   6481  C CB  . VAL B 1 178 ? -42.027 23.882  -4.151  1.00 180.93 ? 178 VAL B CB  1 
ATOM   6482  C CG1 . VAL B 1 178 ? -41.399 22.654  -3.502  1.00 177.83 ? 178 VAL B CG1 1 
ATOM   6483  C CG2 . VAL B 1 178 ? -42.864 24.640  -3.125  1.00 178.07 ? 178 VAL B CG2 1 
ATOM   6484  N N   . LYS B 1 179 ? -40.294 25.259  -7.095  1.00 168.02 ? 179 LYS B N   1 
ATOM   6485  C CA  . LYS B 1 179 ? -39.792 24.939  -8.449  1.00 157.72 ? 179 LYS B CA  1 
ATOM   6486  C C   . LYS B 1 179 ? -39.090 26.130  -9.136  1.00 155.66 ? 179 LYS B C   1 
ATOM   6487  O O   . LYS B 1 179 ? -39.693 26.816  -9.964  1.00 156.35 ? 179 LYS B O   1 
ATOM   6488  C CB  . LYS B 1 179 ? -40.908 24.359  -9.344  1.00 154.24 ? 179 LYS B CB  1 
ATOM   6489  C CG  . LYS B 1 179 ? -42.297 24.949  -9.119  1.00 151.79 ? 179 LYS B CG  1 
ATOM   6490  C CD  . LYS B 1 179 ? -42.620 26.045  -10.121 1.00 147.39 ? 179 LYS B CD  1 
ATOM   6491  C CE  . LYS B 1 179 ? -43.582 27.066  -9.536  1.00 145.18 ? 179 LYS B CE  1 
ATOM   6492  N NZ  . LYS B 1 179 ? -42.929 27.917  -8.501  1.00 139.96 ? 179 LYS B NZ  1 
ATOM   6493  N N   . PRO B 1 180 ? -37.803 26.368  -8.796  1.00 153.70 ? 180 PRO B N   1 
ATOM   6494  C CA  . PRO B 1 180 ? -37.073 27.536  -9.295  1.00 148.47 ? 180 PRO B CA  1 
ATOM   6495  C C   . PRO B 1 180 ? -36.282 27.285  -10.583 1.00 142.61 ? 180 PRO B C   1 
ATOM   6496  O O   . PRO B 1 180 ? -36.429 28.038  -11.542 1.00 141.57 ? 180 PRO B O   1 
ATOM   6497  C CB  . PRO B 1 180 ? -36.126 27.878  -8.136  1.00 149.83 ? 180 PRO B CB  1 
ATOM   6498  C CG  . PRO B 1 180 ? -36.002 26.617  -7.325  1.00 152.13 ? 180 PRO B CG  1 
ATOM   6499  C CD  . PRO B 1 180 ? -36.995 25.602  -7.831  1.00 154.88 ? 180 PRO B CD  1 
ATOM   6500  N N   . ARG B 1 181 ? -35.437 26.251  -10.579 1.00 140.10 ? 181 ARG B N   1 
ATOM   6501  C CA  . ARG B 1 181 ? -34.659 25.815  -11.758 1.00 138.37 ? 181 ARG B CA  1 
ATOM   6502  C C   . ARG B 1 181 ? -33.219 26.351  -11.822 1.00 132.28 ? 181 ARG B C   1 
ATOM   6503  O O   . ARG B 1 181 ? -32.265 25.574  -11.975 1.00 134.16 ? 181 ARG B O   1 
ATOM   6504  C CB  . ARG B 1 181 ? -35.404 26.085  -13.074 1.00 140.61 ? 181 ARG B CB  1 
ATOM   6505  C CG  . ARG B 1 181 ? -34.890 25.258  -14.238 1.00 141.81 ? 181 ARG B CG  1 
ATOM   6506  C CD  . ARG B 1 181 ? -36.024 24.829  -15.151 1.00 145.83 ? 181 ARG B CD  1 
ATOM   6507  N NE  . ARG B 1 181 ? -35.894 23.426  -15.543 1.00 147.71 ? 181 ARG B NE  1 
ATOM   6508  C CZ  . ARG B 1 181 ? -35.161 22.990  -16.566 1.00 147.15 ? 181 ARG B CZ  1 
ATOM   6509  N NH1 . ARG B 1 181 ? -34.480 23.845  -17.320 1.00 147.27 ? 181 ARG B NH1 1 
ATOM   6510  N NH2 . ARG B 1 181 ? -35.110 21.693  -16.836 1.00 147.59 ? 181 ARG B NH2 1 
ATOM   6511  N N   . GLY B 1 182 ? -33.070 27.674  -11.726 1.00 122.53 ? 182 GLY B N   1 
ATOM   6512  C CA  . GLY B 1 182 ? -31.749 28.295  -11.802 1.00 109.45 ? 182 GLY B CA  1 
ATOM   6513  C C   . GLY B 1 182 ? -31.660 29.620  -11.071 1.00 101.64 ? 182 GLY B C   1 
ATOM   6514  O O   . GLY B 1 182 ? -32.670 30.294  -10.872 1.00 100.46 ? 182 GLY B O   1 
ATOM   6515  N N   . VAL B 1 183 ? -30.446 29.997  -10.676 1.00 95.47  ? 183 VAL B N   1 
ATOM   6516  C CA  . VAL B 1 183 ? -30.225 31.260  -9.966  1.00 92.05  ? 183 VAL B CA  1 
ATOM   6517  C C   . VAL B 1 183 ? -29.755 32.380  -10.902 1.00 89.64  ? 183 VAL B C   1 
ATOM   6518  O O   . VAL B 1 183 ? -28.826 32.201  -11.694 1.00 91.88  ? 183 VAL B O   1 
ATOM   6519  C CB  . VAL B 1 183 ? -29.278 31.091  -8.740  1.00 90.45  ? 183 VAL B CB  1 
ATOM   6520  C CG1 . VAL B 1 183 ? -27.962 30.435  -9.139  1.00 91.36  ? 183 VAL B CG1 1 
ATOM   6521  C CG2 . VAL B 1 183 ? -29.039 32.424  -8.038  1.00 87.30  ? 183 VAL B CG2 1 
ATOM   6522  N N   . LEU B 1 184 ? -30.426 33.527  -10.813 1.00 86.68  ? 184 LEU B N   1 
ATOM   6523  C CA  . LEU B 1 184 ? -30.097 34.695  -11.626 1.00 83.72  ? 184 LEU B CA  1 
ATOM   6524  C C   . LEU B 1 184 ? -28.829 35.378  -11.122 1.00 81.69  ? 184 LEU B C   1 
ATOM   6525  O O   . LEU B 1 184 ? -28.713 35.689  -9.932  1.00 81.91  ? 184 LEU B O   1 
ATOM   6526  C CB  . LEU B 1 184 ? -31.264 35.693  -11.611 1.00 83.88  ? 184 LEU B CB  1 
ATOM   6527  C CG  . LEU B 1 184 ? -31.143 36.945  -12.485 1.00 84.15  ? 184 LEU B CG  1 
ATOM   6528  C CD1 . LEU B 1 184 ? -31.735 36.695  -13.862 1.00 85.26  ? 184 LEU B CD1 1 
ATOM   6529  C CD2 . LEU B 1 184 ? -31.818 38.137  -11.825 1.00 83.65  ? 184 LEU B CD2 1 
ATOM   6530  N N   . ASN B 1 185 ? -27.882 35.608  -12.030 1.00 78.57  ? 185 ASN B N   1 
ATOM   6531  C CA  . ASN B 1 185 ? -26.700 36.415  -11.720 1.00 77.92  ? 185 ASN B CA  1 
ATOM   6532  C C   . ASN B 1 185 ? -26.626 37.666  -12.573 1.00 74.87  ? 185 ASN B C   1 
ATOM   6533  O O   . ASN B 1 185 ? -26.779 37.606  -13.790 1.00 80.14  ? 185 ASN B O   1 
ATOM   6534  C CB  . ASN B 1 185 ? -25.411 35.600  -11.884 1.00 79.40  ? 185 ASN B CB  1 
ATOM   6535  C CG  . ASN B 1 185 ? -25.258 34.531  -10.821 1.00 81.75  ? 185 ASN B CG  1 
ATOM   6536  O OD1 . ASN B 1 185 ? -25.180 33.343  -11.131 1.00 84.87  ? 185 ASN B OD1 1 
ATOM   6537  N ND2 . ASN B 1 185 ? -25.224 34.946  -9.557  1.00 78.13  ? 185 ASN B ND2 1 
ATOM   6538  N N   . ILE B 1 186 ? -26.400 38.799  -11.926 1.00 70.97  ? 186 ILE B N   1 
ATOM   6539  C CA  . ILE B 1 186 ? -26.130 40.036  -12.630 1.00 70.11  ? 186 ILE B CA  1 
ATOM   6540  C C   . ILE B 1 186 ? -24.623 40.217  -12.679 1.00 70.30  ? 186 ILE B C   1 
ATOM   6541  O O   . ILE B 1 186 ? -24.001 40.559  -11.674 1.00 73.26  ? 186 ILE B O   1 
ATOM   6542  C CB  . ILE B 1 186 ? -26.761 41.259  -11.921 1.00 69.17  ? 186 ILE B CB  1 
ATOM   6543  C CG1 . ILE B 1 186 ? -28.242 41.013  -11.573 1.00 71.14  ? 186 ILE B CG1 1 
ATOM   6544  C CG2 . ILE B 1 186 ? -26.551 42.530  -12.737 1.00 67.62  ? 186 ILE B CG2 1 
ATOM   6545  C CD1 . ILE B 1 186 ? -29.144 40.749  -12.759 1.00 75.99  ? 186 ILE B CD1 1 
ATOM   6546  N N   . ILE B 1 187 ? -24.033 39.948  -13.838 1.00 70.57  ? 187 ILE B N   1 
ATOM   6547  C CA  . ILE B 1 187 ? -22.611 40.193  -14.048 1.00 69.99  ? 187 ILE B CA  1 
ATOM   6548  C C   . ILE B 1 187 ? -22.422 41.581  -14.664 1.00 70.65  ? 187 ILE B C   1 
ATOM   6549  O O   . ILE B 1 187 ? -23.080 41.913  -15.652 1.00 68.72  ? 187 ILE B O   1 
ATOM   6550  C CB  . ILE B 1 187 ? -21.971 39.120  -14.967 1.00 71.04  ? 187 ILE B CB  1 
ATOM   6551  C CG1 . ILE B 1 187 ? -22.304 37.698  -14.479 1.00 71.02  ? 187 ILE B CG1 1 
ATOM   6552  C CG2 . ILE B 1 187 ? -20.464 39.328  -15.089 1.00 69.63  ? 187 ILE B CG2 1 
ATOM   6553  C CD1 . ILE B 1 187 ? -21.848 37.383  -13.065 1.00 75.32  ? 187 ILE B CD1 1 
ATOM   6554  N N   . PRO B 1 188 ? -21.533 42.404  -14.071 1.00 72.75  ? 188 PRO B N   1 
ATOM   6555  C CA  . PRO B 1 188 ? -21.194 43.688  -14.684 1.00 76.24  ? 188 PRO B CA  1 
ATOM   6556  C C   . PRO B 1 188 ? -20.428 43.485  -15.985 1.00 81.09  ? 188 PRO B C   1 
ATOM   6557  O O   . PRO B 1 188 ? -19.693 42.502  -16.125 1.00 79.48  ? 188 PRO B O   1 
ATOM   6558  C CB  . PRO B 1 188 ? -20.283 44.359  -13.641 1.00 74.73  ? 188 PRO B CB  1 
ATOM   6559  C CG  . PRO B 1 188 ? -20.422 43.553  -12.394 1.00 72.14  ? 188 PRO B CG  1 
ATOM   6560  C CD  . PRO B 1 188 ? -20.773 42.168  -12.834 1.00 71.80  ? 188 PRO B CD  1 
ATOM   6561  N N   . LYS B 1 189 ? -20.622 44.401  -16.931 1.00 89.95  ? 189 LYS B N   1 
ATOM   6562  C CA  . LYS B 1 189 ? -19.909 44.376  -18.205 1.00 95.60  ? 189 LYS B CA  1 
ATOM   6563  C C   . LYS B 1 189 ? -19.316 45.761  -18.507 1.00 99.99  ? 189 LYS B C   1 
ATOM   6564  O O   . LYS B 1 189 ? -19.452 46.691  -17.705 1.00 100.27 ? 189 LYS B O   1 
ATOM   6565  C CB  . LYS B 1 189 ? -20.840 43.921  -19.337 1.00 97.46  ? 189 LYS B CB  1 
ATOM   6566  C CG  . LYS B 1 189 ? -20.169 43.017  -20.359 1.00 100.08 ? 189 LYS B CG  1 
ATOM   6567  C CD  . LYS B 1 189 ? -20.457 43.481  -21.780 1.00 106.15 ? 189 LYS B CD  1 
ATOM   6568  C CE  . LYS B 1 189 ? -19.303 43.137  -22.709 1.00 107.38 ? 189 LYS B CE  1 
ATOM   6569  N NZ  . LYS B 1 189 ? -19.301 43.978  -23.938 1.00 106.37 ? 189 LYS B NZ  1 
ATOM   6570  N N   . GLN B 1 190 ? -18.641 45.882  -19.650 1.00 106.27 ? 190 GLN B N   1 
ATOM   6571  C CA  . GLN B 1 190 ? -18.061 47.153  -20.088 1.00 111.04 ? 190 GLN B CA  1 
ATOM   6572  C C   . GLN B 1 190 ? -19.134 48.245  -20.167 1.00 112.20 ? 190 GLN B C   1 
ATOM   6573  O O   . GLN B 1 190 ? -19.834 48.369  -21.177 1.00 118.68 ? 190 GLN B O   1 
ATOM   6574  C CB  . GLN B 1 190 ? -17.362 46.986  -21.448 1.00 114.03 ? 190 GLN B CB  1 
ATOM   6575  C CG  . GLN B 1 190 ? -16.079 46.163  -21.406 1.00 115.06 ? 190 GLN B CG  1 
ATOM   6576  C CD  . GLN B 1 190 ? -14.854 46.991  -21.051 1.00 117.64 ? 190 GLN B CD  1 
ATOM   6577  O OE1 . GLN B 1 190 ? -14.814 48.200  -21.289 1.00 119.84 ? 190 GLN B OE1 1 
ATOM   6578  N NE2 . GLN B 1 190 ? -13.842 46.338  -20.487 1.00 114.58 ? 190 GLN B NE2 1 
ATOM   6579  N N   . ASP B 1 191 ? -19.269 49.012  -19.081 1.00 109.86 ? 191 ASP B N   1 
ATOM   6580  C CA  . ASP B 1 191 ? -20.245 50.115  -18.980 1.00 110.10 ? 191 ASP B CA  1 
ATOM   6581  C C   . ASP B 1 191 ? -21.712 49.644  -18.884 1.00 108.39 ? 191 ASP B C   1 
ATOM   6582  O O   . ASP B 1 191 ? -22.626 50.468  -18.778 1.00 112.89 ? 191 ASP B O   1 
ATOM   6583  C CB  . ASP B 1 191 ? -20.068 51.125  -20.133 1.00 112.45 ? 191 ASP B CB  1 
ATOM   6584  C CG  . ASP B 1 191 ? -20.306 52.567  -19.698 1.00 114.15 ? 191 ASP B CG  1 
ATOM   6585  O OD1 . ASP B 1 191 ? -19.444 53.125  -18.985 1.00 115.06 ? 191 ASP B OD1 1 
ATOM   6586  O OD2 . ASP B 1 191 ? -21.342 53.150  -20.088 1.00 109.58 ? 191 ASP B OD2 1 
ATOM   6587  N N   . ASN B 1 192 ? -21.929 48.328  -18.911 1.00 101.13 ? 192 ASN B N   1 
ATOM   6588  C CA  . ASN B 1 192 ? -23.279 47.759  -18.800 1.00 96.80  ? 192 ASN B CA  1 
ATOM   6589  C C   . ASN B 1 192 ? -23.367 46.511  -17.911 1.00 90.46  ? 192 ASN B C   1 
ATOM   6590  O O   . ASN B 1 192 ? -22.509 46.288  -17.055 1.00 87.12  ? 192 ASN B O   1 
ATOM   6591  C CB  . ASN B 1 192 ? -23.868 47.478  -20.189 1.00 98.68  ? 192 ASN B CB  1 
ATOM   6592  C CG  . ASN B 1 192 ? -24.959 48.462  -20.569 1.00 101.33 ? 192 ASN B CG  1 
ATOM   6593  O OD1 . ASN B 1 192 ? -25.766 48.870  -19.730 1.00 100.36 ? 192 ASN B OD1 1 
ATOM   6594  N ND2 . ASN B 1 192 ? -24.997 48.839  -21.843 1.00 103.19 ? 192 ASN B ND2 1 
ATOM   6595  N N   . PHE B 1 193 ? -24.421 45.715  -18.107 1.00 83.33  ? 193 PHE B N   1 
ATOM   6596  C CA  . PHE B 1 193 ? -24.612 44.485  -17.341 1.00 78.50  ? 193 PHE B CA  1 
ATOM   6597  C C   . PHE B 1 193 ? -24.988 43.298  -18.227 1.00 74.84  ? 193 PHE B C   1 
ATOM   6598  O O   . PHE B 1 193 ? -25.150 43.444  -19.428 1.00 75.43  ? 193 PHE B O   1 
ATOM   6599  C CB  . PHE B 1 193 ? -25.662 44.690  -16.240 1.00 76.76  ? 193 PHE B CB  1 
ATOM   6600  C CG  . PHE B 1 193 ? -27.075 44.707  -16.742 1.00 75.25  ? 193 PHE B CG  1 
ATOM   6601  C CD1 . PHE B 1 193 ? -27.798 43.522  -16.874 1.00 74.77  ? 193 PHE B CD1 1 
ATOM   6602  C CD2 . PHE B 1 193 ? -27.692 45.908  -17.069 1.00 75.49  ? 193 PHE B CD2 1 
ATOM   6603  C CE1 . PHE B 1 193 ? -29.102 43.535  -17.335 1.00 74.01  ? 193 PHE B CE1 1 
ATOM   6604  C CE2 . PHE B 1 193 ? -28.999 45.926  -17.527 1.00 76.11  ? 193 PHE B CE2 1 
ATOM   6605  C CZ  . PHE B 1 193 ? -29.703 44.739  -17.658 1.00 75.40  ? 193 PHE B CZ  1 
ATOM   6606  N N   . ARG B 1 194 ? -25.137 42.129  -17.610 1.00 74.30  ? 194 ARG B N   1 
ATOM   6607  C CA  . ARG B 1 194 ? -25.463 40.901  -18.318 1.00 74.60  ? 194 ARG B CA  1 
ATOM   6608  C C   . ARG B 1 194 ? -26.130 39.929  -17.341 1.00 75.61  ? 194 ARG B C   1 
ATOM   6609  O O   . ARG B 1 194 ? -25.537 39.544  -16.339 1.00 77.80  ? 194 ARG B O   1 
ATOM   6610  C CB  . ARG B 1 194 ? -24.187 40.300  -18.924 1.00 74.07  ? 194 ARG B CB  1 
ATOM   6611  C CG  . ARG B 1 194 ? -24.374 39.022  -19.731 1.00 77.77  ? 194 ARG B CG  1 
ATOM   6612  C CD  . ARG B 1 194 ? -23.040 38.441  -20.201 1.00 80.11  ? 194 ARG B CD  1 
ATOM   6613  N NE  . ARG B 1 194 ? -21.886 38.964  -19.450 1.00 83.29  ? 194 ARG B NE  1 
ATOM   6614  C CZ  . ARG B 1 194 ? -20.819 38.248  -19.088 1.00 80.14  ? 194 ARG B CZ  1 
ATOM   6615  N NH1 . ARG B 1 194 ? -20.748 36.954  -19.376 1.00 80.02  ? 194 ARG B NH1 1 
ATOM   6616  N NH2 . ARG B 1 194 ? -19.826 38.827  -18.419 1.00 77.90  ? 194 ARG B NH2 1 
ATOM   6617  N N   . ALA B 1 195 ? -27.379 39.571  -17.623 1.00 78.71  ? 195 ALA B N   1 
ATOM   6618  C CA  . ALA B 1 195 ? -28.157 38.687  -16.755 1.00 78.15  ? 195 ALA B CA  1 
ATOM   6619  C C   . ALA B 1 195 ? -28.073 37.224  -17.200 1.00 81.83  ? 195 ALA B C   1 
ATOM   6620  O O   . ALA B 1 195 ? -28.633 36.846  -18.231 1.00 83.34  ? 195 ALA B O   1 
ATOM   6621  C CB  . ALA B 1 195 ? -29.605 39.145  -16.710 1.00 78.00  ? 195 ALA B CB  1 
ATOM   6622  N N   . ILE B 1 196 ? -27.371 36.404  -16.419 1.00 86.21  ? 196 ILE B N   1 
ATOM   6623  C CA  . ILE B 1 196 ? -27.220 34.972  -16.732 1.00 89.86  ? 196 ILE B CA  1 
ATOM   6624  C C   . ILE B 1 196 ? -27.840 34.066  -15.659 1.00 94.43  ? 196 ILE B C   1 
ATOM   6625  O O   . ILE B 1 196 ? -28.143 34.520  -14.552 1.00 96.88  ? 196 ILE B O   1 
ATOM   6626  C CB  . ILE B 1 196 ? -25.737 34.574  -16.995 1.00 87.64  ? 196 ILE B CB  1 
ATOM   6627  C CG1 . ILE B 1 196 ? -24.869 34.764  -15.743 1.00 87.67  ? 196 ILE B CG1 1 
ATOM   6628  C CG2 . ILE B 1 196 ? -25.166 35.351  -18.173 1.00 88.37  ? 196 ILE B CG2 1 
ATOM   6629  C CD1 . ILE B 1 196 ? -24.610 33.486  -14.969 1.00 87.39  ? 196 ILE B CD1 1 
ATOM   6630  N N   . VAL B 1 197 ? -28.024 32.787  -15.995 1.00 96.52  ? 197 VAL B N   1 
ATOM   6631  C CA  . VAL B 1 197 ? -28.585 31.803  -15.058 1.00 97.94  ? 197 VAL B CA  1 
ATOM   6632  C C   . VAL B 1 197 ? -27.650 30.622  -14.791 1.00 99.94  ? 197 VAL B C   1 
ATOM   6633  O O   . VAL B 1 197 ? -26.860 30.233  -15.655 1.00 99.03  ? 197 VAL B O   1 
ATOM   6634  C CB  . VAL B 1 197 ? -29.965 31.274  -15.519 1.00 97.55  ? 197 VAL B CB  1 
ATOM   6635  C CG1 . VAL B 1 197 ? -30.979 32.402  -15.549 1.00 97.76  ? 197 VAL B CG1 1 
ATOM   6636  C CG2 . VAL B 1 197 ? -29.871 30.590  -16.877 1.00 96.24  ? 197 VAL B CG2 1 
ATOM   6637  N N   . SER B 1 198 ? -27.753 30.057  -13.588 1.00 103.37 ? 198 SER B N   1 
ATOM   6638  C CA  . SER B 1 198 ? -26.960 28.889  -13.209 1.00 107.32 ? 198 SER B CA  1 
ATOM   6639  C C   . SER B 1 198 ? -27.850 27.675  -12.946 1.00 112.20 ? 198 SER B C   1 
ATOM   6640  O O   . SER B 1 198 ? -28.902 27.791  -12.316 1.00 111.80 ? 198 SER B O   1 
ATOM   6641  C CB  . SER B 1 198 ? -26.095 29.197  -11.984 1.00 104.98 ? 198 SER B CB  1 
ATOM   6642  O OG  . SER B 1 198 ? -25.213 30.276  -12.245 1.00 100.57 ? 198 SER B OG  1 
ATOM   6643  N N   . ILE B 1 199 ? -27.412 26.515  -13.430 1.00 117.49 ? 199 ILE B N   1 
ATOM   6644  C CA  . ILE B 1 199 ? -28.203 25.281  -13.372 1.00 125.02 ? 199 ILE B CA  1 
ATOM   6645  C C   . ILE B 1 199 ? -27.915 24.501  -12.077 1.00 131.22 ? 199 ILE B C   1 
ATOM   6646  O O   . ILE B 1 199 ? -27.009 24.863  -11.323 1.00 131.80 ? 199 ILE B O   1 
ATOM   6647  C CB  . ILE B 1 199 ? -27.945 24.383  -14.612 1.00 125.15 ? 199 ILE B CB  1 
ATOM   6648  C CG1 . ILE B 1 199 ? -27.580 25.225  -15.845 1.00 122.48 ? 199 ILE B CG1 1 
ATOM   6649  C CG2 . ILE B 1 199 ? -29.156 23.508  -14.911 1.00 125.16 ? 199 ILE B CG2 1 
ATOM   6650  C CD1 . ILE B 1 199 ? -26.089 25.387  -16.074 1.00 119.52 ? 199 ILE B CD1 1 
ATOM   6651  N N   . PHE B 1 200 ? -28.686 23.437  -11.829 1.00 139.69 ? 200 PHE B N   1 
ATOM   6652  C CA  . PHE B 1 200 ? -28.601 22.669  -10.571 1.00 143.89 ? 200 PHE B CA  1 
ATOM   6653  C C   . PHE B 1 200 ? -27.256 21.958  -10.297 1.00 144.63 ? 200 PHE B C   1 
ATOM   6654  O O   . PHE B 1 200 ? -26.621 22.233  -9.277  1.00 143.28 ? 200 PHE B O   1 
ATOM   6655  C CB  . PHE B 1 200 ? -29.782 21.691  -10.425 1.00 150.01 ? 200 PHE B CB  1 
ATOM   6656  C CG  . PHE B 1 200 ? -31.037 22.317  -9.870  1.00 155.36 ? 200 PHE B CG  1 
ATOM   6657  C CD1 . PHE B 1 200 ? -30.991 23.140  -8.745  1.00 155.16 ? 200 PHE B CD1 1 
ATOM   6658  C CD2 . PHE B 1 200 ? -32.274 22.054  -10.453 1.00 159.18 ? 200 PHE B CD2 1 
ATOM   6659  C CE1 . PHE B 1 200 ? -32.148 23.707  -8.230  1.00 156.70 ? 200 PHE B CE1 1 
ATOM   6660  C CE2 . PHE B 1 200 ? -33.435 22.617  -9.939  1.00 161.56 ? 200 PHE B CE2 1 
ATOM   6661  C CZ  . PHE B 1 200 ? -33.372 23.443  -8.827  1.00 160.61 ? 200 PHE B CZ  1 
ATOM   6662  N N   . PRO B 1 201 ? -26.815 21.039  -11.193 1.00 148.28 ? 201 PRO B N   1 
ATOM   6663  C CA  . PRO B 1 201 ? -27.412 20.566  -12.439 1.00 154.06 ? 201 PRO B CA  1 
ATOM   6664  C C   . PRO B 1 201 ? -28.127 19.209  -12.305 1.00 158.84 ? 201 PRO B C   1 
ATOM   6665  O O   . PRO B 1 201 ? -28.312 18.708  -11.192 1.00 157.91 ? 201 PRO B O   1 
ATOM   6666  C CB  . PRO B 1 201 ? -26.194 20.423  -13.358 1.00 150.65 ? 201 PRO B CB  1 
ATOM   6667  C CG  . PRO B 1 201 ? -25.049 20.124  -12.431 1.00 146.65 ? 201 PRO B CG  1 
ATOM   6668  C CD  . PRO B 1 201 ? -25.459 20.487  -11.023 1.00 145.95 ? 201 PRO B CD  1 
ATOM   6669  N N   . ASP B 1 202 ? -28.534 18.652  -13.449 1.00 163.68 ? 202 ASP B N   1 
ATOM   6670  C CA  . ASP B 1 202 ? -29.092 17.292  -13.555 1.00 162.86 ? 202 ASP B CA  1 
ATOM   6671  C C   . ASP B 1 202 ? -30.529 17.138  -13.028 1.00 164.59 ? 202 ASP B C   1 
ATOM   6672  O O   . ASP B 1 202 ? -30.791 16.346  -12.118 1.00 163.12 ? 202 ASP B O   1 
ATOM   6673  C CB  . ASP B 1 202 ? -28.153 16.250  -12.928 1.00 157.90 ? 202 ASP B CB  1 
ATOM   6674  C CG  . ASP B 1 202 ? -28.116 14.955  -13.714 1.00 155.26 ? 202 ASP B CG  1 
ATOM   6675  O OD1 . ASP B 1 202 ? -27.535 14.945  -14.819 1.00 151.37 ? 202 ASP B OD1 1 
ATOM   6676  O OD2 . ASP B 1 202 ? -28.661 13.945  -13.223 1.00 154.84 ? 202 ASP B OD2 1 
ATOM   6677  N N   . SER B 1 203 ? -31.449 17.901  -13.615 1.00 167.34 ? 203 SER B N   1 
ATOM   6678  C CA  . SER B 1 203 ? -32.886 17.677  -13.444 1.00 171.99 ? 203 SER B CA  1 
ATOM   6679  C C   . SER B 1 203 ? -33.514 17.404  -14.809 1.00 177.43 ? 203 SER B C   1 
ATOM   6680  O O   . SER B 1 203 ? -33.279 18.149  -15.765 1.00 178.84 ? 203 SER B O   1 
ATOM   6681  C CB  . SER B 1 203 ? -33.555 18.884  -12.778 1.00 169.24 ? 203 SER B CB  1 
ATOM   6682  O OG  . SER B 1 203 ? -33.237 18.954  -11.398 1.00 162.24 ? 203 SER B OG  1 
ATOM   6683  N N   . ALA B 1 204 ? -34.306 16.333  -14.891 1.00 181.83 ? 204 ALA B N   1 
ATOM   6684  C CA  . ALA B 1 204 ? -34.794 15.789  -16.173 1.00 186.40 ? 204 ALA B CA  1 
ATOM   6685  C C   . ALA B 1 204 ? -33.644 15.361  -17.106 1.00 191.32 ? 204 ALA B C   1 
ATOM   6686  O O   . ALA B 1 204 ? -33.771 15.412  -18.334 1.00 194.35 ? 204 ALA B O   1 
ATOM   6687  C CB  . ALA B 1 204 ? -35.738 16.770  -16.867 1.00 181.78 ? 204 ALA B CB  1 
ATOM   6688  N N   . ARG B 1 205 ? -32.531 14.941  -16.494 1.00 193.37 ? 205 ARG B N   1 
ATOM   6689  C CA  . ARG B 1 205 ? -31.343 14.386  -17.187 1.00 189.63 ? 205 ARG B CA  1 
ATOM   6690  C C   . ARG B 1 205 ? -30.468 15.420  -17.916 1.00 184.46 ? 205 ARG B C   1 
ATOM   6691  O O   . ARG B 1 205 ? -30.973 16.373  -18.515 1.00 183.59 ? 205 ARG B O   1 
ATOM   6692  C CB  . ARG B 1 205 ? -31.709 13.211  -18.116 1.00 189.81 ? 205 ARG B CB  1 
ATOM   6693  C CG  . ARG B 1 205 ? -32.522 12.108  -17.445 1.00 188.90 ? 205 ARG B CG  1 
ATOM   6694  C CD  . ARG B 1 205 ? -32.048 10.720  -17.851 1.00 185.49 ? 205 ARG B CD  1 
ATOM   6695  N NE  . ARG B 1 205 ? -30.926 10.261  -17.031 1.00 181.60 ? 205 ARG B NE  1 
ATOM   6696  C CZ  . ARG B 1 205 ? -31.049 9.629   -15.865 1.00 179.66 ? 205 ARG B CZ  1 
ATOM   6697  N NH1 . ARG B 1 205 ? -32.250 9.372   -15.361 1.00 181.17 ? 205 ARG B NH1 1 
ATOM   6698  N NH2 . ARG B 1 205 ? -29.967 9.253   -15.198 1.00 177.54 ? 205 ARG B NH2 1 
ATOM   6699  N N   . LYS B 1 206 ? -29.152 15.212  -17.850 1.00 177.85 ? 206 LYS B N   1 
ATOM   6700  C CA  . LYS B 1 206 ? -28.176 16.078  -18.518 1.00 172.05 ? 206 LYS B CA  1 
ATOM   6701  C C   . LYS B 1 206 ? -27.866 15.644  -19.967 1.00 172.61 ? 206 LYS B C   1 
ATOM   6702  O O   . LYS B 1 206 ? -27.514 16.487  -20.797 1.00 170.62 ? 206 LYS B O   1 
ATOM   6703  C CB  . LYS B 1 206 ? -26.884 16.175  -17.693 1.00 164.05 ? 206 LYS B CB  1 
ATOM   6704  C CG  . LYS B 1 206 ? -26.039 17.404  -17.987 1.00 156.19 ? 206 LYS B CG  1 
ATOM   6705  C CD  . LYS B 1 206 ? -24.705 17.345  -17.263 1.00 150.18 ? 206 LYS B CD  1 
ATOM   6706  C CE  . LYS B 1 206 ? -23.752 18.404  -17.790 1.00 144.94 ? 206 LYS B CE  1 
ATOM   6707  N NZ  . LYS B 1 206 ? -22.388 18.258  -17.213 1.00 139.59 ? 206 LYS B NZ  1 
ATOM   6708  N N   . PRO B 1 207 ? -27.980 14.329  -20.272 1.00 174.20 ? 207 PRO B N   1 
ATOM   6709  C CA  . PRO B 1 207 ? -27.884 13.905  -21.677 1.00 173.65 ? 207 PRO B CA  1 
ATOM   6710  C C   . PRO B 1 207 ? -29.135 14.245  -22.502 1.00 174.53 ? 207 PRO B C   1 
ATOM   6711  O O   . PRO B 1 207 ? -29.087 14.212  -23.736 1.00 174.98 ? 207 PRO B O   1 
ATOM   6712  C CB  . PRO B 1 207 ? -27.705 12.383  -21.577 1.00 173.19 ? 207 PRO B CB  1 
ATOM   6713  C CG  . PRO B 1 207 ? -28.276 12.017  -20.251 1.00 173.32 ? 207 PRO B CG  1 
ATOM   6714  C CD  . PRO B 1 207 ? -27.957 13.174  -19.353 1.00 173.53 ? 207 PRO B CD  1 
ATOM   6715  N N   . PHE B 1 208 ? -30.236 14.567  -21.822 1.00 172.00 ? 208 PHE B N   1 
ATOM   6716  C CA  . PHE B 1 208 ? -31.485 14.959  -22.486 1.00 167.72 ? 208 PHE B CA  1 
ATOM   6717  C C   . PHE B 1 208 ? -31.373 16.342  -23.132 1.00 167.29 ? 208 PHE B C   1 
ATOM   6718  O O   . PHE B 1 208 ? -32.084 16.644  -24.092 1.00 168.15 ? 208 PHE B O   1 
ATOM   6719  C CB  . PHE B 1 208 ? -32.656 14.925  -21.495 1.00 163.53 ? 208 PHE B CB  1 
ATOM   6720  C CG  . PHE B 1 208 ? -34.011 14.979  -22.149 1.00 159.89 ? 208 PHE B CG  1 
ATOM   6721  C CD1 . PHE B 1 208 ? -34.581 13.835  -22.698 1.00 159.99 ? 208 PHE B CD1 1 
ATOM   6722  C CD2 . PHE B 1 208 ? -34.725 16.172  -22.204 1.00 157.35 ? 208 PHE B CD2 1 
ATOM   6723  C CE1 . PHE B 1 208 ? -35.831 13.882  -23.298 1.00 160.67 ? 208 PHE B CE1 1 
ATOM   6724  C CE2 . PHE B 1 208 ? -35.975 16.224  -22.802 1.00 156.65 ? 208 PHE B CE2 1 
ATOM   6725  C CZ  . PHE B 1 208 ? -36.529 15.078  -23.350 1.00 159.10 ? 208 PHE B CZ  1 
ATOM   6726  N N   . PHE B 1 209 ? -30.480 17.174  -22.596 1.00 167.38 ? 209 PHE B N   1 
ATOM   6727  C CA  . PHE B 1 209 ? -30.195 18.488  -23.175 1.00 164.04 ? 209 PHE B CA  1 
ATOM   6728  C C   . PHE B 1 209 ? -29.255 18.387  -24.375 1.00 160.11 ? 209 PHE B C   1 
ATOM   6729  O O   . PHE B 1 209 ? -29.356 19.178  -25.314 1.00 157.35 ? 209 PHE B O   1 
ATOM   6730  C CB  . PHE B 1 209 ? -29.602 19.431  -22.125 1.00 165.60 ? 209 PHE B CB  1 
ATOM   6731  C CG  . PHE B 1 209 ? -30.571 19.827  -21.046 1.00 169.86 ? 209 PHE B CG  1 
ATOM   6732  C CD1 . PHE B 1 209 ? -31.653 20.656  -21.332 1.00 171.02 ? 209 PHE B CD1 1 
ATOM   6733  C CD2 . PHE B 1 209 ? -30.394 19.386  -19.739 1.00 172.41 ? 209 PHE B CD2 1 
ATOM   6734  C CE1 . PHE B 1 209 ? -32.545 21.025  -20.338 1.00 174.42 ? 209 PHE B CE1 1 
ATOM   6735  C CE2 . PHE B 1 209 ? -31.282 19.753  -18.739 1.00 174.51 ? 209 PHE B CE2 1 
ATOM   6736  C CZ  . PHE B 1 209 ? -32.359 20.574  -19.039 1.00 176.05 ? 209 PHE B CZ  1 
ATOM   6737  N N   . LYS B 1 210 ? -28.342 17.417  -24.333 1.00 155.67 ? 210 LYS B N   1 
ATOM   6738  C CA  . LYS B 1 210 ? -27.419 17.178  -25.443 1.00 152.27 ? 210 LYS B CA  1 
ATOM   6739  C C   . LYS B 1 210 ? -28.111 16.458  -26.603 1.00 156.56 ? 210 LYS B C   1 
ATOM   6740  O O   . LYS B 1 210 ? -27.690 16.578  -27.756 1.00 157.69 ? 210 LYS B O   1 
ATOM   6741  C CB  . LYS B 1 210 ? -26.184 16.399  -24.974 1.00 145.33 ? 210 LYS B CB  1 
ATOM   6742  C CG  . LYS B 1 210 ? -24.969 16.566  -25.876 1.00 138.46 ? 210 LYS B CG  1 
ATOM   6743  C CD  . LYS B 1 210 ? -23.688 16.142  -25.178 1.00 131.44 ? 210 LYS B CD  1 
ATOM   6744  C CE  . LYS B 1 210 ? -22.470 16.489  -26.017 1.00 124.68 ? 210 LYS B CE  1 
ATOM   6745  N NZ  . LYS B 1 210 ? -21.205 16.272  -25.268 1.00 119.61 ? 210 LYS B NZ  1 
ATOM   6746  N N   . LEU B 1 211 ? -29.175 15.717  -26.288 1.00 160.01 ? 211 LEU B N   1 
ATOM   6747  C CA  . LEU B 1 211 ? -29.985 15.031  -27.301 1.00 162.91 ? 211 LEU B CA  1 
ATOM   6748  C C   . LEU B 1 211 ? -30.793 16.019  -28.148 1.00 163.24 ? 211 LEU B C   1 
ATOM   6749  O O   . LEU B 1 211 ? -30.814 15.921  -29.379 1.00 163.85 ? 211 LEU B O   1 
ATOM   6750  C CB  . LEU B 1 211 ? -30.916 13.999  -26.642 1.00 164.42 ? 211 LEU B CB  1 
ATOM   6751  C CG  . LEU B 1 211 ? -32.011 13.329  -27.488 1.00 165.56 ? 211 LEU B CG  1 
ATOM   6752  C CD1 . LEU B 1 211 ? -31.422 12.428  -28.565 1.00 166.87 ? 211 LEU B CD1 1 
ATOM   6753  C CD2 . LEU B 1 211 ? -32.975 12.549  -26.605 1.00 165.22 ? 211 LEU B CD2 1 
ATOM   6754  N N   . LEU B 1 212 ? -31.454 16.964  -27.480 1.00 161.44 ? 212 LEU B N   1 
ATOM   6755  C CA  . LEU B 1 212 ? -32.273 17.970  -28.156 1.00 156.65 ? 212 LEU B CA  1 
ATOM   6756  C C   . LEU B 1 212 ? -31.426 18.982  -28.921 1.00 152.15 ? 212 LEU B C   1 
ATOM   6757  O O   . LEU B 1 212 ? -31.774 19.364  -30.039 1.00 149.80 ? 212 LEU B O   1 
ATOM   6758  C CB  . LEU B 1 212 ? -33.181 18.695  -27.157 1.00 156.60 ? 212 LEU B CB  1 
ATOM   6759  C CG  . LEU B 1 212 ? -34.325 17.897  -26.524 1.00 159.36 ? 212 LEU B CG  1 
ATOM   6760  C CD1 . LEU B 1 212 ? -34.939 18.676  -25.371 1.00 160.29 ? 212 LEU B CD1 1 
ATOM   6761  C CD2 . LEU B 1 212 ? -35.383 17.537  -27.558 1.00 162.78 ? 212 LEU B CD2 1 
ATOM   6762  N N   . THR B 1 213 ? -30.316 19.407  -28.319 1.00 148.30 ? 213 THR B N   1 
ATOM   6763  C CA  . THR B 1 213 ? -29.442 20.405  -28.939 1.00 145.46 ? 213 THR B CA  1 
ATOM   6764  C C   . THR B 1 213 ? -28.813 19.899  -30.239 1.00 142.79 ? 213 THR B C   1 
ATOM   6765  O O   . THR B 1 213 ? -28.713 20.642  -31.215 1.00 140.49 ? 213 THR B O   1 
ATOM   6766  C CB  . THR B 1 213 ? -28.354 20.931  -27.965 1.00 142.34 ? 213 THR B CB  1 
ATOM   6767  O OG1 . THR B 1 213 ? -27.752 22.110  -28.511 1.00 142.80 ? 213 THR B OG1 1 
ATOM   6768  C CG2 . THR B 1 213 ? -27.269 19.887  -27.714 1.00 140.16 ? 213 THR B CG2 1 
ATOM   6769  N N   . SER B 1 214 ? -28.424 18.626  -30.252 1.00 142.19 ? 214 SER B N   1 
ATOM   6770  C CA  . SER B 1 214 ? -27.782 18.028  -31.416 1.00 140.81 ? 214 SER B CA  1 
ATOM   6771  C C   . SER B 1 214 ? -28.750 17.902  -32.586 1.00 142.05 ? 214 SER B C   1 
ATOM   6772  O O   . SER B 1 214 ? -28.379 18.161  -33.731 1.00 143.15 ? 214 SER B O   1 
ATOM   6773  C CB  . SER B 1 214 ? -27.194 16.661  -31.068 1.00 141.66 ? 214 SER B CB  1 
ATOM   6774  O OG  . SER B 1 214 ? -26.441 16.145  -32.152 1.00 142.86 ? 214 SER B OG  1 
ATOM   6775  N N   . LYS B 1 215 ? -29.989 17.509  -32.290 1.00 142.31 ? 215 LYS B N   1 
ATOM   6776  C CA  . LYS B 1 215 ? -31.017 17.344  -33.322 1.00 142.76 ? 215 LYS B CA  1 
ATOM   6777  C C   . LYS B 1 215 ? -31.509 18.681  -33.887 1.00 142.30 ? 215 LYS B C   1 
ATOM   6778  O O   . LYS B 1 215 ? -31.919 18.755  -35.048 1.00 143.15 ? 215 LYS B O   1 
ATOM   6779  C CB  . LYS B 1 215 ? -32.191 16.500  -32.806 1.00 142.72 ? 215 LYS B CB  1 
ATOM   6780  C CG  . LYS B 1 215 ? -31.930 14.998  -32.833 1.00 140.91 ? 215 LYS B CG  1 
ATOM   6781  C CD  . LYS B 1 215 ? -33.206 14.191  -32.636 1.00 139.55 ? 215 LYS B CD  1 
ATOM   6782  C CE  . LYS B 1 215 ? -32.947 12.702  -32.817 1.00 137.75 ? 215 LYS B CE  1 
ATOM   6783  N NZ  . LYS B 1 215 ? -34.197 11.897  -32.742 1.00 136.29 ? 215 LYS B NZ  1 
ATOM   6784  N N   . ILE B 1 216 ? -31.457 19.733  -33.069 1.00 138.84 ? 216 ILE B N   1 
ATOM   6785  C CA  . ILE B 1 216 ? -31.782 21.088  -33.529 1.00 134.46 ? 216 ILE B CA  1 
ATOM   6786  C C   . ILE B 1 216 ? -30.674 21.645  -34.429 1.00 131.59 ? 216 ILE B C   1 
ATOM   6787  O O   . ILE B 1 216 ? -30.942 22.442  -35.328 1.00 132.91 ? 216 ILE B O   1 
ATOM   6788  C CB  . ILE B 1 216 ? -32.077 22.048  -32.351 1.00 131.16 ? 216 ILE B CB  1 
ATOM   6789  C CG1 . ILE B 1 216 ? -33.386 21.655  -31.663 1.00 132.12 ? 216 ILE B CG1 1 
ATOM   6790  C CG2 . ILE B 1 216 ? -32.168 23.493  -32.830 1.00 129.42 ? 216 ILE B CG2 1 
ATOM   6791  C CD1 . ILE B 1 216 ? -33.574 22.271  -30.293 1.00 132.81 ? 216 ILE B CD1 1 
ATOM   6792  N N   . TYR B 1 217 ? -29.437 21.207  -34.196 1.00 129.14 ? 217 TYR B N   1 
ATOM   6793  C CA  . TYR B 1 217 ? -28.321 21.549  -35.081 1.00 128.81 ? 217 TYR B CA  1 
ATOM   6794  C C   . TYR B 1 217 ? -28.456 20.892  -36.460 1.00 133.77 ? 217 TYR B C   1 
ATOM   6795  O O   . TYR B 1 217 ? -27.889 21.376  -37.443 1.00 133.80 ? 217 TYR B O   1 
ATOM   6796  C CB  . TYR B 1 217 ? -26.972 21.196  -34.437 1.00 123.61 ? 217 TYR B CB  1 
ATOM   6797  C CG  . TYR B 1 217 ? -26.413 22.290  -33.550 1.00 118.95 ? 217 TYR B CG  1 
ATOM   6798  C CD1 . TYR B 1 217 ? -25.927 23.476  -34.097 1.00 117.61 ? 217 TYR B CD1 1 
ATOM   6799  C CD2 . TYR B 1 217 ? -26.364 22.138  -32.166 1.00 117.64 ? 217 TYR B CD2 1 
ATOM   6800  C CE1 . TYR B 1 217 ? -25.420 24.484  -33.290 1.00 114.59 ? 217 TYR B CE1 1 
ATOM   6801  C CE2 . TYR B 1 217 ? -25.858 23.140  -31.350 1.00 113.30 ? 217 TYR B CE2 1 
ATOM   6802  C CZ  . TYR B 1 217 ? -25.387 24.311  -31.917 1.00 111.63 ? 217 TYR B CZ  1 
ATOM   6803  O OH  . TYR B 1 217 ? -24.883 25.309  -31.115 1.00 107.60 ? 217 TYR B OH  1 
ATOM   6804  N N   . LYS B 1 218 ? -29.214 19.797  -36.521 1.00 138.65 ? 218 LYS B N   1 
ATOM   6805  C CA  . LYS B 1 218 ? -29.533 19.137  -37.791 1.00 142.09 ? 218 LYS B CA  1 
ATOM   6806  C C   . LYS B 1 218 ? -30.599 19.926  -38.558 1.00 143.76 ? 218 LYS B C   1 
ATOM   6807  O O   . LYS B 1 218 ? -30.489 20.114  -39.773 1.00 143.81 ? 218 LYS B O   1 
ATOM   6808  C CB  . LYS B 1 218 ? -30.012 17.693  -37.561 1.00 145.67 ? 218 LYS B CB  1 
ATOM   6809  C CG  . LYS B 1 218 ? -29.193 16.882  -36.562 1.00 145.71 ? 218 LYS B CG  1 
ATOM   6810  C CD  . LYS B 1 218 ? -27.979 16.220  -37.198 1.00 145.12 ? 218 LYS B CD  1 
ATOM   6811  C CE  . LYS B 1 218 ? -27.216 15.389  -36.176 1.00 142.85 ? 218 LYS B CE  1 
ATOM   6812  N NZ  . LYS B 1 218 ? -26.053 14.677  -36.775 1.00 140.74 ? 218 LYS B NZ  1 
ATOM   6813  N N   . VAL B 1 219 ? -31.626 20.380  -37.837 1.00 144.93 ? 219 VAL B N   1 
ATOM   6814  C CA  . VAL B 1 219 ? -32.684 21.224  -38.406 1.00 146.74 ? 219 VAL B CA  1 
ATOM   6815  C C   . VAL B 1 219 ? -32.132 22.604  -38.777 1.00 145.93 ? 219 VAL B C   1 
ATOM   6816  O O   . VAL B 1 219 ? -32.599 23.238  -39.731 1.00 146.36 ? 219 VAL B O   1 
ATOM   6817  C CB  . VAL B 1 219 ? -33.875 21.383  -37.425 1.00 149.18 ? 219 VAL B CB  1 
ATOM   6818  C CG1 . VAL B 1 219 ? -35.001 22.192  -38.059 1.00 150.39 ? 219 VAL B CG1 1 
ATOM   6819  C CG2 . VAL B 1 219 ? -34.393 20.022  -36.981 1.00 151.40 ? 219 VAL B CG2 1 
ATOM   6820  N N   . LEU B 1 220 ? -31.122 23.046  -38.026 1.00 145.51 ? 220 LEU B N   1 
ATOM   6821  C CA  . LEU B 1 220 ? -30.464 24.338  -38.246 1.00 143.67 ? 220 LEU B CA  1 
ATOM   6822  C C   . LEU B 1 220 ? -29.850 24.467  -39.644 1.00 142.10 ? 220 LEU B C   1 
ATOM   6823  O O   . LEU B 1 220 ? -29.651 25.577  -40.138 1.00 140.02 ? 220 LEU B O   1 
ATOM   6824  C CB  . LEU B 1 220 ? -29.395 24.581  -37.169 1.00 142.09 ? 220 LEU B CB  1 
ATOM   6825  C CG  . LEU B 1 220 ? -28.575 25.878  -37.202 1.00 142.57 ? 220 LEU B CG  1 
ATOM   6826  C CD1 . LEU B 1 220 ? -29.459 27.105  -37.035 1.00 142.20 ? 220 LEU B CD1 1 
ATOM   6827  C CD2 . LEU B 1 220 ? -27.491 25.855  -36.137 1.00 142.76 ? 220 LEU B CD2 1 
ATOM   6828  N N   . GLU B 1 221 ? -29.551 23.331  -40.273 1.00 141.75 ? 221 GLU B N   1 
ATOM   6829  C CA  . GLU B 1 221 ? -28.990 23.330  -41.625 1.00 141.23 ? 221 GLU B CA  1 
ATOM   6830  C C   . GLU B 1 221 ? -29.614 22.291  -42.571 1.00 143.33 ? 221 GLU B C   1 
ATOM   6831  O O   . GLU B 1 221 ? -28.970 21.844  -43.524 1.00 144.26 ? 221 GLU B O   1 
ATOM   6832  C CB  . GLU B 1 221 ? -27.455 23.212  -41.588 1.00 140.77 ? 221 GLU B CB  1 
ATOM   6833  C CG  . GLU B 1 221 ? -26.910 22.174  -40.615 1.00 140.28 ? 221 GLU B CG  1 
ATOM   6834  C CD  . GLU B 1 221 ? -27.002 20.758  -41.149 1.00 141.17 ? 221 GLU B CD  1 
ATOM   6835  O OE1 . GLU B 1 221 ? -26.557 20.517  -42.293 1.00 139.19 ? 221 GLU B OE1 1 
ATOM   6836  O OE2 . GLU B 1 221 ? -27.512 19.884  -40.419 1.00 142.61 ? 221 GLU B OE2 1 
ATOM   6837  N N   . GLU B 1 222 ? -30.865 21.914  -42.304 1.00 141.71 ? 222 GLU B N   1 
ATOM   6838  C CA  . GLU B 1 222 ? -31.643 21.116  -43.254 1.00 140.20 ? 222 GLU B CA  1 
ATOM   6839  C C   . GLU B 1 222 ? -32.591 22.028  -44.014 1.00 139.10 ? 222 GLU B C   1 
ATOM   6840  O O   . GLU B 1 222 ? -32.677 21.969  -45.241 1.00 140.07 ? 222 GLU B O   1 
ATOM   6841  C CB  . GLU B 1 222 ? -32.431 20.011  -42.540 1.00 142.14 ? 222 GLU B CB  1 
ATOM   6842  C CG  . GLU B 1 222 ? -32.788 18.819  -43.427 1.00 146.21 ? 222 GLU B CG  1 
ATOM   6843  C CD  . GLU B 1 222 ? -33.958 19.087  -44.366 1.00 147.92 ? 222 GLU B CD  1 
ATOM   6844  O OE1 . GLU B 1 222 ? -35.096 19.257  -43.878 1.00 150.07 ? 222 GLU B OE1 1 
ATOM   6845  O OE2 . GLU B 1 222 ? -33.741 19.108  -45.597 1.00 147.26 ? 222 GLU B OE2 1 
ATOM   6846  N N   . LYS B 1 223 ? -33.301 22.871  -43.271 1.00 137.39 ? 223 LYS B N   1 
ATOM   6847  C CA  . LYS B 1 223 ? -34.174 23.870  -43.862 1.00 135.76 ? 223 LYS B CA  1 
ATOM   6848  C C   . LYS B 1 223 ? -33.406 25.181  -44.036 1.00 129.94 ? 223 LYS B C   1 
ATOM   6849  O O   . LYS B 1 223 ? -33.990 26.223  -44.344 1.00 129.92 ? 223 LYS B O   1 
ATOM   6850  C CB  . LYS B 1 223 ? -35.408 24.074  -42.982 1.00 138.13 ? 223 LYS B CB  1 
ATOM   6851  C CG  . LYS B 1 223 ? -36.709 24.188  -43.757 1.00 140.34 ? 223 LYS B CG  1 
ATOM   6852  C CD  . LYS B 1 223 ? -37.907 24.135  -42.819 1.00 141.17 ? 223 LYS B CD  1 
ATOM   6853  C CE  . LYS B 1 223 ? -39.216 24.319  -43.575 1.00 143.20 ? 223 LYS B CE  1 
ATOM   6854  N NZ  . LYS B 1 223 ? -40.377 24.475  -42.639 1.00 145.52 ? 223 LYS B NZ  1 
ATOM   6855  N N   . TYR B 1 224 ? -32.088 25.111  -43.839 1.00 124.31 ? 224 TYR B N   1 
ATOM   6856  C CA  . TYR B 1 224 ? -31.211 26.283  -43.921 1.00 119.15 ? 224 TYR B CA  1 
ATOM   6857  C C   . TYR B 1 224 ? -29.903 25.958  -44.643 1.00 116.16 ? 224 TYR B C   1 
ATOM   6858  O O   . TYR B 1 224 ? -29.444 24.815  -44.636 1.00 115.02 ? 224 TYR B O   1 
ATOM   6859  C CB  . TYR B 1 224 ? -30.954 26.864  -42.524 1.00 113.99 ? 224 TYR B CB  1 
ATOM   6860  C CG  . TYR B 1 224 ? -32.231 27.236  -41.801 1.00 113.29 ? 224 TYR B CG  1 
ATOM   6861  C CD1 . TYR B 1 224 ? -32.903 28.418  -42.105 1.00 113.06 ? 224 TYR B CD1 1 
ATOM   6862  C CD2 . TYR B 1 224 ? -32.791 26.387  -40.847 1.00 113.47 ? 224 TYR B CD2 1 
ATOM   6863  C CE1 . TYR B 1 224 ? -34.084 28.756  -41.468 1.00 111.48 ? 224 TYR B CE1 1 
ATOM   6864  C CE2 . TYR B 1 224 ? -33.973 26.718  -40.202 1.00 112.08 ? 224 TYR B CE2 1 
ATOM   6865  C CZ  . TYR B 1 224 ? -34.614 27.904  -40.519 1.00 113.33 ? 224 TYR B CZ  1 
ATOM   6866  O OH  . TYR B 1 224 ? -35.788 28.244  -39.891 1.00 116.24 ? 224 TYR B OH  1 
ATOM   6867  N N   . LYS B 1 225 ? -29.309 26.974  -45.260 1.00 116.18 ? 225 LYS B N   1 
ATOM   6868  C CA  . LYS B 1 225 ? -28.286 26.767  -46.289 1.00 120.74 ? 225 LYS B CA  1 
ATOM   6869  C C   . LYS B 1 225 ? -26.832 26.852  -45.793 1.00 118.88 ? 225 LYS B C   1 
ATOM   6870  O O   . LYS B 1 225 ? -26.572 27.168  -44.626 1.00 111.76 ? 225 LYS B O   1 
ATOM   6871  C CB  . LYS B 1 225 ? -28.514 27.735  -47.460 1.00 124.02 ? 225 LYS B CB  1 
ATOM   6872  C CG  . LYS B 1 225 ? -28.711 29.186  -47.037 1.00 125.59 ? 225 LYS B CG  1 
ATOM   6873  C CD  . LYS B 1 225 ? -29.097 30.065  -48.214 1.00 125.36 ? 225 LYS B CD  1 
ATOM   6874  C CE  . LYS B 1 225 ? -29.470 31.461  -47.741 1.00 124.74 ? 225 LYS B CE  1 
ATOM   6875  N NZ  . LYS B 1 225 ? -29.693 32.377  -48.898 1.00 125.05 ? 225 LYS B NZ  1 
ATOM   6876  N N   . THR B 1 226 ? -25.899 26.562  -46.703 1.00 119.49 ? 226 THR B N   1 
ATOM   6877  C CA  . THR B 1 226 ? -24.460 26.614  -46.421 1.00 117.61 ? 226 THR B CA  1 
ATOM   6878  C C   . THR B 1 226 ? -23.940 28.049  -46.282 1.00 115.70 ? 226 THR B C   1 
ATOM   6879  O O   . THR B 1 226 ? -23.880 28.806  -47.261 1.00 109.88 ? 226 THR B O   1 
ATOM   6880  C CB  . THR B 1 226 ? -23.624 25.833  -47.480 1.00 117.04 ? 226 THR B CB  1 
ATOM   6881  O OG1 . THR B 1 226 ? -22.251 26.241  -47.416 1.00 112.70 ? 226 THR B OG1 1 
ATOM   6882  C CG2 . THR B 1 226 ? -24.155 26.067  -48.900 1.00 115.44 ? 226 THR B CG2 1 
ATOM   6883  N N   . SER B 1 227 ? -23.567 28.406  -45.051 1.00 116.73 ? 227 SER B N   1 
ATOM   6884  C CA  . SER B 1 227 ? -22.959 29.704  -44.750 1.00 114.02 ? 227 SER B CA  1 
ATOM   6885  C C   . SER B 1 227 ? -21.908 30.082  -45.784 1.00 109.16 ? 227 SER B C   1 
ATOM   6886  O O   . SER B 1 227 ? -21.959 31.162  -46.380 1.00 108.54 ? 227 SER B O   1 
ATOM   6887  C CB  . SER B 1 227 ? -22.303 29.680  -43.360 1.00 112.96 ? 227 SER B CB  1 
ATOM   6888  O OG  . SER B 1 227 ? -23.265 29.555  -42.328 1.00 117.19 ? 227 SER B OG  1 
ATOM   6889  N N   . GLY B 1 228 ? -20.973 29.165  -46.013 1.00 104.55 ? 228 GLY B N   1 
ATOM   6890  C CA  . GLY B 1 228 ? -19.697 29.510  -46.606 1.00 95.94  ? 228 GLY B CA  1 
ATOM   6891  C C   . GLY B 1 228 ? -18.837 30.092  -45.503 1.00 89.01  ? 228 GLY B C   1 
ATOM   6892  O O   . GLY B 1 228 ? -19.289 30.953  -44.738 1.00 88.36  ? 228 GLY B O   1 
ATOM   6893  N N   . SER B 1 229 ? -17.608 29.600  -45.392 1.00 83.22  ? 229 SER B N   1 
ATOM   6894  C CA  . SER B 1 229 ? -16.680 30.115  -44.401 1.00 75.29  ? 229 SER B CA  1 
ATOM   6895  C C   . SER B 1 229 ? -16.323 31.552  -44.746 1.00 71.42  ? 229 SER B C   1 
ATOM   6896  O O   . SER B 1 229 ? -16.303 31.936  -45.923 1.00 70.95  ? 229 SER B O   1 
ATOM   6897  C CB  . SER B 1 229 ? -15.422 29.251  -44.329 1.00 74.74  ? 229 SER B CB  1 
ATOM   6898  O OG  . SER B 1 229 ? -14.553 29.521  -45.416 1.00 78.25  ? 229 SER B OG  1 
ATOM   6899  N N   . LEU B 1 230 ? -16.065 32.342  -43.707 1.00 68.06  ? 230 LEU B N   1 
ATOM   6900  C CA  . LEU B 1 230 ? -15.651 33.734  -43.842 1.00 63.90  ? 230 LEU B CA  1 
ATOM   6901  C C   . LEU B 1 230 ? -14.521 33.860  -44.852 1.00 62.81  ? 230 LEU B C   1 
ATOM   6902  O O   . LEU B 1 230 ? -14.544 34.741  -45.711 1.00 65.22  ? 230 LEU B O   1 
ATOM   6903  C CB  . LEU B 1 230 ? -15.184 34.267  -42.485 1.00 61.00  ? 230 LEU B CB  1 
ATOM   6904  C CG  . LEU B 1 230 ? -15.538 35.687  -42.040 1.00 59.56  ? 230 LEU B CG  1 
ATOM   6905  C CD1 . LEU B 1 230 ? -14.635 36.063  -40.875 1.00 57.64  ? 230 LEU B CD1 1 
ATOM   6906  C CD2 . LEU B 1 230 ? -15.430 36.716  -43.163 1.00 58.06  ? 230 LEU B CD2 1 
ATOM   6907  N N   . TYR B 1 231 ? -13.539 32.967  -44.750 1.00 61.61  ? 231 TYR B N   1 
ATOM   6908  C CA  . TYR B 1 231 ? -12.411 32.953  -45.672 1.00 59.84  ? 231 TYR B CA  1 
ATOM   6909  C C   . TYR B 1 231 ? -12.883 32.862  -47.110 1.00 61.15  ? 231 TYR B C   1 
ATOM   6910  O O   . TYR B 1 231 ? -12.497 33.679  -47.941 1.00 62.39  ? 231 TYR B O   1 
ATOM   6911  C CB  . TYR B 1 231 ? -11.448 31.805  -45.351 1.00 56.16  ? 231 TYR B CB  1 
ATOM   6912  C CG  . TYR B 1 231 ? -10.209 31.785  -46.228 1.00 54.87  ? 231 TYR B CG  1 
ATOM   6913  C CD1 . TYR B 1 231 ? -9.112  32.617  -45.949 1.00 52.97  ? 231 TYR B CD1 1 
ATOM   6914  C CD2 . TYR B 1 231 ? -10.126 30.937  -47.332 1.00 54.18  ? 231 TYR B CD2 1 
ATOM   6915  C CE1 . TYR B 1 231 ? -7.980  32.598  -46.745 1.00 50.68  ? 231 TYR B CE1 1 
ATOM   6916  C CE2 . TYR B 1 231 ? -8.996  30.913  -48.133 1.00 53.37  ? 231 TYR B CE2 1 
ATOM   6917  C CZ  . TYR B 1 231 ? -7.927  31.744  -47.836 1.00 52.58  ? 231 TYR B CZ  1 
ATOM   6918  O OH  . TYR B 1 231 ? -6.806  31.717  -48.635 1.00 53.10  ? 231 TYR B OH  1 
ATOM   6919  N N   . THR B 1 232 ? -13.723 31.872  -47.397 1.00 63.49  ? 232 THR B N   1 
ATOM   6920  C CA  . THR B 1 232 ? -14.176 31.626  -48.768 1.00 66.79  ? 232 THR B CA  1 
ATOM   6921  C C   . THR B 1 232 ? -14.962 32.825  -49.292 1.00 65.29  ? 232 THR B C   1 
ATOM   6922  O O   . THR B 1 232 ? -14.758 33.264  -50.425 1.00 66.51  ? 232 THR B O   1 
ATOM   6923  C CB  . THR B 1 232 ? -15.037 30.352  -48.860 1.00 71.55  ? 232 THR B CB  1 
ATOM   6924  O OG1 . THR B 1 232 ? -14.456 29.326  -48.046 1.00 76.78  ? 232 THR B OG1 1 
ATOM   6925  C CG2 . THR B 1 232 ? -15.119 29.859  -50.297 1.00 73.55  ? 232 THR B CG2 1 
ATOM   6926  N N   . CYS B 1 233 ? -15.834 33.365  -48.443 1.00 65.28  ? 233 CYS B N   1 
ATOM   6927  C CA  . CYS B 1 233 ? -16.628 34.546  -48.777 1.00 64.95  ? 233 CYS B CA  1 
ATOM   6928  C C   . CYS B 1 233 ? -15.771 35.768  -49.105 1.00 62.94  ? 233 CYS B C   1 
ATOM   6929  O O   . CYS B 1 233 ? -16.039 36.466  -50.081 1.00 63.74  ? 233 CYS B O   1 
ATOM   6930  C CB  . CYS B 1 233 ? -17.595 34.878  -47.640 1.00 67.01  ? 233 CYS B CB  1 
ATOM   6931  S SG  . CYS B 1 233 ? -18.967 33.723  -47.464 1.00 73.16  ? 233 CYS B SG  1 
ATOM   6932  N N   . TRP B 1 234 ? -14.744 36.025  -48.289 1.00 59.59  ? 234 TRP B N   1 
ATOM   6933  C CA  . TRP B 1 234 ? -13.870 37.173  -48.506 1.00 55.78  ? 234 TRP B CA  1 
ATOM   6934  C C   . TRP B 1 234 ? -12.989 36.945  -49.693 1.00 56.22  ? 234 TRP B C   1 
ATOM   6935  O O   . TRP B 1 234 ? -12.696 37.877  -50.454 1.00 60.05  ? 234 TRP B O   1 
ATOM   6936  C CB  . TRP B 1 234 ? -13.031 37.480  -47.266 1.00 51.54  ? 234 TRP B CB  1 
ATOM   6937  C CG  . TRP B 1 234 ? -12.237 38.758  -47.397 1.00 48.28  ? 234 TRP B CG  1 
ATOM   6938  C CD1 . TRP B 1 234 ? -10.871 38.890  -47.635 1.00 46.38  ? 234 TRP B CD1 1 
ATOM   6939  C CD2 . TRP B 1 234 ? -12.749 40.130  -47.340 1.00 48.47  ? 234 TRP B CD2 1 
ATOM   6940  N NE1 . TRP B 1 234 ? -10.512 40.216  -47.711 1.00 44.98  ? 234 TRP B NE1 1 
ATOM   6941  C CE2 . TRP B 1 234 ? -11.593 41.011  -47.538 1.00 47.09  ? 234 TRP B CE2 1 
ATOM   6942  C CE3 . TRP B 1 234 ? -14.007 40.698  -47.146 1.00 49.30  ? 234 TRP B CE3 1 
ATOM   6943  C CZ2 . TRP B 1 234 ? -11.713 42.393  -47.551 1.00 46.78  ? 234 TRP B CZ2 1 
ATOM   6944  C CZ3 . TRP B 1 234 ? -14.115 42.098  -47.151 1.00 49.91  ? 234 TRP B CZ3 1 
ATOM   6945  C CH2 . TRP B 1 234 ? -12.990 42.922  -47.349 1.00 48.73  ? 234 TRP B CH2 1 
ATOM   6946  N N   . SER B 1 235 ? -12.569 35.701  -49.885 1.00 55.00  ? 235 SER B N   1 
ATOM   6947  C CA  . SER B 1 235 ? -11.712 35.371  -51.017 1.00 55.85  ? 235 SER B CA  1 
ATOM   6948  C C   . SER B 1 235 ? -12.448 35.563  -52.347 1.00 57.02  ? 235 SER B C   1 
ATOM   6949  O O   . SER B 1 235 ? -11.994 36.315  -53.214 1.00 54.93  ? 235 SER B O   1 
ATOM   6950  C CB  . SER B 1 235 ? -11.160 33.954  -50.893 1.00 54.58  ? 235 SER B CB  1 
ATOM   6951  O OG  . SER B 1 235 ? -10.122 33.746  -51.830 1.00 55.12  ? 235 SER B OG  1 
ATOM   6952  N N   . GLU B 1 236 ? -13.591 34.897  -52.498 1.00 59.30  ? 236 GLU B N   1 
ATOM   6953  C CA  . GLU B 1 236 ? -14.381 35.025  -53.725 1.00 61.77  ? 236 GLU B CA  1 
ATOM   6954  C C   . GLU B 1 236 ? -14.727 36.489  -53.998 1.00 59.20  ? 236 GLU B C   1 
ATOM   6955  O O   . GLU B 1 236 ? -14.508 36.993  -55.098 1.00 57.82  ? 236 GLU B O   1 
ATOM   6956  C CB  . GLU B 1 236 ? -15.653 34.175  -53.644 1.00 67.48  ? 236 GLU B CB  1 
ATOM   6957  C CG  . GLU B 1 236 ? -15.411 32.669  -53.711 1.00 71.40  ? 236 GLU B CG  1 
ATOM   6958  C CD  . GLU B 1 236 ? -16.690 31.849  -53.577 1.00 75.14  ? 236 GLU B CD  1 
ATOM   6959  O OE1 . GLU B 1 236 ? -16.636 30.623  -53.811 1.00 77.43  ? 236 GLU B OE1 1 
ATOM   6960  O OE2 . GLU B 1 236 ? -17.751 32.422  -53.235 1.00 76.26  ? 236 GLU B OE2 1 
ATOM   6961  N N   . PHE B 1 237 ? -15.233 37.170  -52.971 1.00 58.71  ? 237 PHE B N   1 
ATOM   6962  C CA  . PHE B 1 237 ? -15.642 38.569  -53.084 1.00 57.67  ? 237 PHE B CA  1 
ATOM   6963  C C   . PHE B 1 237 ? -14.540 39.494  -53.614 1.00 56.91  ? 237 PHE B C   1 
ATOM   6964  O O   . PHE B 1 237 ? -14.765 40.260  -54.547 1.00 56.35  ? 237 PHE B O   1 
ATOM   6965  C CB  . PHE B 1 237 ? -16.170 39.079  -51.743 1.00 57.22  ? 237 PHE B CB  1 
ATOM   6966  C CG  . PHE B 1 237 ? -16.594 40.516  -51.767 1.00 58.83  ? 237 PHE B CG  1 
ATOM   6967  C CD1 . PHE B 1 237 ? -17.721 40.914  -52.488 1.00 59.55  ? 237 PHE B CD1 1 
ATOM   6968  C CD2 . PHE B 1 237 ? -15.872 41.479  -51.068 1.00 57.80  ? 237 PHE B CD2 1 
ATOM   6969  C CE1 . PHE B 1 237 ? -18.113 42.240  -52.515 1.00 58.76  ? 237 PHE B CE1 1 
ATOM   6970  C CE2 . PHE B 1 237 ? -16.262 42.811  -51.096 1.00 57.89  ? 237 PHE B CE2 1 
ATOM   6971  C CZ  . PHE B 1 237 ? -17.383 43.189  -51.820 1.00 59.95  ? 237 PHE B CZ  1 
ATOM   6972  N N   . THR B 1 238 ? -13.349 39.415  -53.026 1.00 55.67  ? 238 THR B N   1 
ATOM   6973  C CA  . THR B 1 238 ? -12.270 40.337  -53.395 1.00 54.22  ? 238 THR B CA  1 
ATOM   6974  C C   . THR B 1 238 ? -11.707 40.097  -54.800 1.00 54.69  ? 238 THR B C   1 
ATOM   6975  O O   . THR B 1 238 ? -11.396 41.052  -55.516 1.00 53.63  ? 238 THR B O   1 
ATOM   6976  C CB  . THR B 1 238 ? -11.132 40.360  -52.353 1.00 52.95  ? 238 THR B CB  1 
ATOM   6977  O OG1 . THR B 1 238 ? -10.667 39.028  -52.109 1.00 53.58  ? 238 THR B OG1 1 
ATOM   6978  C CG2 . THR B 1 238 ? -11.618 40.969  -51.055 1.00 51.20  ? 238 THR B CG2 1 
ATOM   6979  N N   . GLN B 1 239 ? -11.603 38.827  -55.194 1.00 55.55  ? 239 GLN B N   1 
ATOM   6980  C CA  . GLN B 1 239 ? -11.047 38.454  -56.500 1.00 56.33  ? 239 GLN B CA  1 
ATOM   6981  C C   . GLN B 1 239 ? -11.935 38.864  -57.678 1.00 62.28  ? 239 GLN B C   1 
ATOM   6982  O O   . GLN B 1 239 ? -11.443 39.047  -58.802 1.00 65.20  ? 239 GLN B O   1 
ATOM   6983  C CB  . GLN B 1 239 ? -10.755 36.953  -56.563 1.00 55.89  ? 239 GLN B CB  1 
ATOM   6984  C CG  . GLN B 1 239 ? -9.821  36.444  -55.462 1.00 58.26  ? 239 GLN B CG  1 
ATOM   6985  C CD  . GLN B 1 239 ? -8.648  37.379  -55.192 1.00 57.46  ? 239 GLN B CD  1 
ATOM   6986  O OE1 . GLN B 1 239 ? -7.842  37.653  -56.083 1.00 59.96  ? 239 GLN B OE1 1 
ATOM   6987  N NE2 . GLN B 1 239 ? -8.559  37.882  -53.969 1.00 53.47  ? 239 GLN B NE2 1 
ATOM   6988  N N   . LYS B 1 240 ? -13.235 39.010  -57.426 1.00 63.14  ? 240 LYS B N   1 
ATOM   6989  C CA  . LYS B 1 240 ? -14.162 39.405  -58.478 1.00 65.70  ? 240 LYS B CA  1 
ATOM   6990  C C   . LYS B 1 240 ? -14.570 40.885  -58.420 1.00 67.18  ? 240 LYS B C   1 
ATOM   6991  O O   . LYS B 1 240 ? -15.338 41.349  -59.263 1.00 71.36  ? 240 LYS B O   1 
ATOM   6992  C CB  . LYS B 1 240 ? -15.398 38.491  -58.485 1.00 66.69  ? 240 LYS B CB  1 
ATOM   6993  C CG  . LYS B 1 240 ? -16.446 38.809  -57.433 1.00 66.97  ? 240 LYS B CG  1 
ATOM   6994  C CD  . LYS B 1 240 ? -17.467 37.686  -57.331 1.00 67.21  ? 240 LYS B CD  1 
ATOM   6995  C CE  . LYS B 1 240 ? -18.567 38.023  -56.335 1.00 66.88  ? 240 LYS B CE  1 
ATOM   6996  N NZ  . LYS B 1 240 ? -19.221 36.793  -55.805 1.00 65.23  ? 240 LYS B NZ  1 
ATOM   6997  N N   . THR B 1 241 ? -14.051 41.623  -57.439 1.00 64.38  ? 241 THR B N   1 
ATOM   6998  C CA  . THR B 1 241 ? -14.402 43.032  -57.282 1.00 62.02  ? 241 THR B CA  1 
ATOM   6999  C C   . THR B 1 241 ? -13.187 43.908  -57.498 1.00 62.02  ? 241 THR B C   1 
ATOM   7000  O O   . THR B 1 241 ? -12.291 43.955  -56.661 1.00 65.84  ? 241 THR B O   1 
ATOM   7001  C CB  . THR B 1 241 ? -14.999 43.309  -55.897 1.00 61.71  ? 241 THR B CB  1 
ATOM   7002  O OG1 . THR B 1 241 ? -15.953 42.293  -55.585 1.00 62.42  ? 241 THR B OG1 1 
ATOM   7003  C CG2 . THR B 1 241 ? -15.683 44.680  -55.854 1.00 62.00  ? 241 THR B CG2 1 
ATOM   7004  N N   . GLN B 1 242 ? -13.166 44.608  -58.624 1.00 63.72  ? 242 GLN B N   1 
ATOM   7005  C CA  . GLN B 1 242 ? -12.003 45.383  -59.039 1.00 63.52  ? 242 GLN B CA  1 
ATOM   7006  C C   . GLN B 1 242 ? -12.065 46.823  -58.535 1.00 61.88  ? 242 GLN B C   1 
ATOM   7007  O O   . GLN B 1 242 ? -11.037 47.457  -58.329 1.00 61.32  ? 242 GLN B O   1 
ATOM   7008  C CB  . GLN B 1 242 ? -11.866 45.364  -60.564 1.00 69.14  ? 242 GLN B CB  1 
ATOM   7009  C CG  . GLN B 1 242 ? -12.358 44.082  -61.236 1.00 74.02  ? 242 GLN B CG  1 
ATOM   7010  C CD  . GLN B 1 242 ? -11.905 43.973  -62.687 1.00 81.86  ? 242 GLN B CD  1 
ATOM   7011  O OE1 . GLN B 1 242 ? -12.669 44.250  -63.620 1.00 78.98  ? 242 GLN B OE1 1 
ATOM   7012  N NE2 . GLN B 1 242 ? -10.643 43.577  -62.885 1.00 85.48  ? 242 GLN B NE2 1 
ATOM   7013  N N   . GLY B 1 243 ? -13.274 47.334  -58.333 1.00 61.97  ? 243 GLY B N   1 
ATOM   7014  C CA  . GLY B 1 243 ? -13.448 48.692  -57.834 1.00 62.00  ? 243 GLY B CA  1 
ATOM   7015  C C   . GLY B 1 243 ? -13.286 48.824  -56.326 1.00 61.85  ? 243 GLY B C   1 
ATOM   7016  O O   . GLY B 1 243 ? -12.939 47.853  -55.630 1.00 58.99  ? 243 GLY B O   1 
ATOM   7017  N N   . GLN B 1 244 ? -13.528 50.038  -55.826 1.00 61.57  ? 244 GLN B N   1 
ATOM   7018  C CA  . GLN B 1 244 ? -13.509 50.323  -54.400 1.00 60.93  ? 244 GLN B CA  1 
ATOM   7019  C C   . GLN B 1 244 ? -14.619 49.542  -53.699 1.00 60.70  ? 244 GLN B C   1 
ATOM   7020  O O   . GLN B 1 244 ? -15.773 49.549  -54.147 1.00 64.01  ? 244 GLN B O   1 
ATOM   7021  C CB  . GLN B 1 244 ? -13.662 51.834  -54.149 1.00 61.48  ? 244 GLN B CB  1 
ATOM   7022  C CG  . GLN B 1 244 ? -13.634 52.251  -52.673 1.00 62.27  ? 244 GLN B CG  1 
ATOM   7023  C CD  . GLN B 1 244 ? -12.253 52.132  -52.027 1.00 61.81  ? 244 GLN B CD  1 
ATOM   7024  O OE1 . GLN B 1 244 ? -11.229 52.383  -52.666 1.00 62.33  ? 244 GLN B OE1 1 
ATOM   7025  N NE2 . GLN B 1 244 ? -12.226 51.763  -50.745 1.00 62.02  ? 244 GLN B NE2 1 
ATOM   7026  N N   . ILE B 1 245 ? -14.255 48.837  -52.630 1.00 56.61  ? 245 ILE B N   1 
ATOM   7027  C CA  . ILE B 1 245 ? -15.228 48.132  -51.800 1.00 55.27  ? 245 ILE B CA  1 
ATOM   7028  C C   . ILE B 1 245 ? -15.763 49.077  -50.733 1.00 55.89  ? 245 ILE B C   1 
ATOM   7029  O O   . ILE B 1 245 ? -14.997 49.808  -50.095 1.00 56.17  ? 245 ILE B O   1 
ATOM   7030  C CB  . ILE B 1 245 ? -14.614 46.884  -51.127 1.00 53.21  ? 245 ILE B CB  1 
ATOM   7031  C CG1 . ILE B 1 245 ? -14.336 45.797  -52.163 1.00 52.88  ? 245 ILE B CG1 1 
ATOM   7032  C CG2 . ILE B 1 245 ? -15.527 46.341  -50.035 1.00 53.09  ? 245 ILE B CG2 1 
ATOM   7033  C CD1 . ILE B 1 245 ? -13.284 44.799  -51.727 1.00 50.97  ? 245 ILE B CD1 1 
ATOM   7034  N N   . TYR B 1 246 ? -17.082 49.081  -50.566 1.00 56.24  ? 246 TYR B N   1 
ATOM   7035  C CA  . TYR B 1 246 ? -17.708 49.726  -49.422 1.00 56.20  ? 246 TYR B CA  1 
ATOM   7036  C C   . TYR B 1 246 ? -18.275 48.641  -48.542 1.00 55.26  ? 246 TYR B C   1 
ATOM   7037  O O   . TYR B 1 246 ? -18.598 47.557  -49.022 1.00 54.21  ? 246 TYR B O   1 
ATOM   7038  C CB  . TYR B 1 246 ? -18.792 50.713  -49.870 1.00 59.22  ? 246 TYR B CB  1 
ATOM   7039  C CG  . TYR B 1 246 ? -18.234 51.837  -50.716 1.00 59.29  ? 246 TYR B CG  1 
ATOM   7040  C CD1 . TYR B 1 246 ? -17.694 52.983  -50.124 1.00 59.36  ? 246 TYR B CD1 1 
ATOM   7041  C CD2 . TYR B 1 246 ? -18.196 51.732  -52.102 1.00 61.01  ? 246 TYR B CD2 1 
ATOM   7042  C CE1 . TYR B 1 246 ? -17.155 54.002  -50.892 1.00 60.80  ? 246 TYR B CE1 1 
ATOM   7043  C CE2 . TYR B 1 246 ? -17.659 52.745  -52.887 1.00 63.19  ? 246 TYR B CE2 1 
ATOM   7044  C CZ  . TYR B 1 246 ? -17.141 53.879  -52.279 1.00 63.00  ? 246 TYR B CZ  1 
ATOM   7045  O OH  . TYR B 1 246 ? -16.607 54.880  -53.061 1.00 64.11  ? 246 TYR B OH  1 
ATOM   7046  N N   . GLY B 1 247 ? -18.355 48.912  -47.246 1.00 55.65  ? 247 GLY B N   1 
ATOM   7047  C CA  . GLY B 1 247 ? -18.724 47.883  -46.289 1.00 55.04  ? 247 GLY B CA  1 
ATOM   7048  C C   . GLY B 1 247 ? -19.163 48.446  -44.964 1.00 56.24  ? 247 GLY B C   1 
ATOM   7049  O O   . GLY B 1 247 ? -18.833 49.581  -44.621 1.00 58.29  ? 247 GLY B O   1 
ATOM   7050  N N   . ILE B 1 248 ? -19.913 47.645  -44.218 1.00 55.92  ? 248 ILE B N   1 
ATOM   7051  C CA  . ILE B 1 248 ? -20.352 48.022  -42.887 1.00 58.17  ? 248 ILE B CA  1 
ATOM   7052  C C   . ILE B 1 248 ? -20.340 46.805  -41.970 1.00 57.70  ? 248 ILE B C   1 
ATOM   7053  O O   . ILE B 1 248 ? -20.617 45.683  -42.411 1.00 58.15  ? 248 ILE B O   1 
ATOM   7054  C CB  . ILE B 1 248 ? -21.763 48.669  -42.911 1.00 60.30  ? 248 ILE B CB  1 
ATOM   7055  C CG1 . ILE B 1 248 ? -22.133 49.221  -41.530 1.00 60.25  ? 248 ILE B CG1 1 
ATOM   7056  C CG2 . ILE B 1 248 ? -22.815 47.682  -43.407 1.00 59.73  ? 248 ILE B CG2 1 
ATOM   7057  C CD1 . ILE B 1 248 ? -23.196 50.291  -41.579 1.00 63.55  ? 248 ILE B CD1 1 
ATOM   7058  N N   . LYS B 1 249 ? -19.959 47.018  -40.714 1.00 58.16  ? 249 LYS B N   1 
ATOM   7059  C CA  . LYS B 1 249 ? -20.230 46.041  -39.668 1.00 58.65  ? 249 LYS B CA  1 
ATOM   7060  C C   . LYS B 1 249 ? -21.268 46.617  -38.726 1.00 60.12  ? 249 LYS B C   1 
ATOM   7061  O O   . LYS B 1 249 ? -21.204 47.794  -38.355 1.00 59.60  ? 249 LYS B O   1 
ATOM   7062  C CB  . LYS B 1 249 ? -18.969 45.655  -38.885 1.00 57.46  ? 249 LYS B CB  1 
ATOM   7063  C CG  . LYS B 1 249 ? -19.282 44.840  -37.624 1.00 57.61  ? 249 LYS B CG  1 
ATOM   7064  C CD  . LYS B 1 249 ? -18.101 44.726  -36.686 1.00 58.56  ? 249 LYS B CD  1 
ATOM   7065  C CE  . LYS B 1 249 ? -17.983 45.917  -35.748 1.00 59.34  ? 249 LYS B CE  1 
ATOM   7066  N NZ  . LYS B 1 249 ? -18.080 45.518  -34.316 1.00 58.21  ? 249 LYS B NZ  1 
ATOM   7067  N N   . VAL B 1 250 ? -22.228 45.784  -38.345 1.00 62.74  ? 250 VAL B N   1 
ATOM   7068  C CA  . VAL B 1 250 ? -23.268 46.194  -37.418 1.00 65.94  ? 250 VAL B CA  1 
ATOM   7069  C C   . VAL B 1 250 ? -23.306 45.233  -36.237 1.00 68.35  ? 250 VAL B C   1 
ATOM   7070  O O   . VAL B 1 250 ? -23.182 44.013  -36.406 1.00 67.40  ? 250 VAL B O   1 
ATOM   7071  C CB  . VAL B 1 250 ? -24.663 46.272  -38.091 1.00 66.43  ? 250 VAL B CB  1 
ATOM   7072  C CG1 . VAL B 1 250 ? -25.485 47.372  -37.449 1.00 66.91  ? 250 VAL B CG1 1 
ATOM   7073  C CG2 . VAL B 1 250 ? -24.534 46.550  -39.582 1.00 66.38  ? 250 VAL B CG2 1 
ATOM   7074  N N   . ASP B 1 251 ? -23.454 45.797  -35.042 1.00 73.29  ? 251 ASP B N   1 
ATOM   7075  C CA  . ASP B 1 251 ? -23.493 45.017  -33.818 1.00 76.88  ? 251 ASP B CA  1 
ATOM   7076  C C   . ASP B 1 251 ? -24.935 44.915  -33.350 1.00 78.33  ? 251 ASP B C   1 
ATOM   7077  O O   . ASP B 1 251 ? -25.573 45.925  -33.040 1.00 81.98  ? 251 ASP B O   1 
ATOM   7078  C CB  . ASP B 1 251 ? -22.622 45.675  -32.740 1.00 80.48  ? 251 ASP B CB  1 
ATOM   7079  C CG  . ASP B 1 251 ? -22.256 44.721  -31.608 1.00 85.94  ? 251 ASP B CG  1 
ATOM   7080  O OD1 . ASP B 1 251 ? -23.169 44.221  -30.908 1.00 87.06  ? 251 ASP B OD1 1 
ATOM   7081  O OD2 . ASP B 1 251 ? -21.044 44.489  -31.403 1.00 87.82  ? 251 ASP B OD2 1 
ATOM   7082  N N   . ILE B 1 252 ? -25.453 43.694  -33.322 1.00 76.81  ? 252 ILE B N   1 
ATOM   7083  C CA  . ILE B 1 252 ? -26.802 43.453  -32.836 1.00 77.95  ? 252 ILE B CA  1 
ATOM   7084  C C   . ILE B 1 252 ? -26.832 43.539  -31.308 1.00 79.15  ? 252 ILE B C   1 
ATOM   7085  O O   . ILE B 1 252 ? -26.127 42.794  -30.621 1.00 76.68  ? 252 ILE B O   1 
ATOM   7086  C CB  . ILE B 1 252 ? -27.338 42.089  -33.318 1.00 76.44  ? 252 ILE B CB  1 
ATOM   7087  C CG1 . ILE B 1 252 ? -27.263 42.009  -34.846 1.00 73.98  ? 252 ILE B CG1 1 
ATOM   7088  C CG2 . ILE B 1 252 ? -28.768 41.872  -32.829 1.00 76.54  ? 252 ILE B CG2 1 
ATOM   7089  C CD1 . ILE B 1 252 ? -27.278 40.599  -35.386 1.00 74.40  ? 252 ILE B CD1 1 
ATOM   7090  N N   . ARG B 1 253 ? -27.628 44.470  -30.782 1.00 81.02  ? 253 ARG B N   1 
ATOM   7091  C CA  . ARG B 1 253 ? -27.773 44.612  -29.336 1.00 81.24  ? 253 ARG B CA  1 
ATOM   7092  C C   . ARG B 1 253 ? -28.658 43.500  -28.777 1.00 80.38  ? 253 ARG B C   1 
ATOM   7093  O O   . ARG B 1 253 ? -29.741 43.236  -29.298 1.00 83.48  ? 253 ARG B O   1 
ATOM   7094  C CB  . ARG B 1 253 ? -28.312 46.003  -28.964 1.00 82.96  ? 253 ARG B CB  1 
ATOM   7095  C CG  . ARG B 1 253 ? -28.625 46.190  -27.481 1.00 86.09  ? 253 ARG B CG  1 
ATOM   7096  C CD  . ARG B 1 253 ? -28.399 47.622  -27.011 1.00 88.77  ? 253 ARG B CD  1 
ATOM   7097  N NE  . ARG B 1 253 ? -28.943 48.607  -27.945 1.00 96.98  ? 253 ARG B NE  1 
ATOM   7098  C CZ  . ARG B 1 253 ? -29.145 49.892  -27.662 1.00 98.88  ? 253 ARG B CZ  1 
ATOM   7099  N NH1 . ARG B 1 253 ? -28.854 50.368  -26.456 1.00 98.08  ? 253 ARG B NH1 1 
ATOM   7100  N NH2 . ARG B 1 253 ? -29.648 50.703  -28.590 1.00 97.40  ? 253 ARG B NH2 1 
ATOM   7101  N N   . ASP B 1 254 ? -28.148 42.828  -27.746 1.00 79.64  ? 254 ASP B N   1 
ATOM   7102  C CA  . ASP B 1 254 ? -28.861 41.773  -27.011 1.00 78.57  ? 254 ASP B CA  1 
ATOM   7103  C C   . ASP B 1 254 ? -29.637 40.814  -27.914 1.00 78.96  ? 254 ASP B C   1 
ATOM   7104  O O   . ASP B 1 254 ? -30.865 40.826  -27.930 1.00 80.71  ? 254 ASP B O   1 
ATOM   7105  C CB  . ASP B 1 254 ? -29.780 42.384  -25.935 1.00 78.97  ? 254 ASP B CB  1 
ATOM   7106  C CG  . ASP B 1 254 ? -30.082 41.410  -24.785 1.00 78.86  ? 254 ASP B CG  1 
ATOM   7107  O OD1 . ASP B 1 254 ? -29.703 40.219  -24.888 1.00 78.80  ? 254 ASP B OD1 1 
ATOM   7108  O OD2 . ASP B 1 254 ? -30.701 41.842  -23.778 1.00 77.20  ? 254 ASP B OD2 1 
ATOM   7109  N N   . ALA B 1 255 ? -28.911 39.981  -28.654 1.00 77.22  ? 255 ALA B N   1 
ATOM   7110  C CA  . ALA B 1 255 ? -29.531 39.014  -29.556 1.00 79.21  ? 255 ALA B CA  1 
ATOM   7111  C C   . ALA B 1 255 ? -30.460 38.061  -28.806 1.00 81.05  ? 255 ALA B C   1 
ATOM   7112  O O   . ALA B 1 255 ? -31.615 37.871  -29.200 1.00 85.67  ? 255 ALA B O   1 
ATOM   7113  C CB  . ALA B 1 255 ? -28.467 38.239  -30.317 1.00 77.71  ? 255 ALA B CB  1 
ATOM   7114  N N   . TYR B 1 256 ? -29.955 37.488  -27.715 1.00 82.23  ? 256 TYR B N   1 
ATOM   7115  C CA  . TYR B 1 256 ? -30.699 36.522  -26.905 1.00 83.60  ? 256 TYR B CA  1 
ATOM   7116  C C   . TYR B 1 256 ? -31.960 37.137  -26.314 1.00 83.68  ? 256 TYR B C   1 
ATOM   7117  O O   . TYR B 1 256 ? -33.023 36.518  -26.320 1.00 82.89  ? 256 TYR B O   1 
ATOM   7118  C CB  . TYR B 1 256 ? -29.812 35.966  -25.783 1.00 86.98  ? 256 TYR B CB  1 
ATOM   7119  C CG  . TYR B 1 256 ? -28.741 34.999  -26.258 1.00 92.34  ? 256 TYR B CG  1 
ATOM   7120  C CD1 . TYR B 1 256 ? -27.558 35.464  -26.835 1.00 93.68  ? 256 TYR B CD1 1 
ATOM   7121  C CD2 . TYR B 1 256 ? -28.908 33.621  -26.125 1.00 94.89  ? 256 TYR B CD2 1 
ATOM   7122  C CE1 . TYR B 1 256 ? -26.577 34.583  -27.274 1.00 96.86  ? 256 TYR B CE1 1 
ATOM   7123  C CE2 . TYR B 1 256 ? -27.930 32.733  -26.557 1.00 95.33  ? 256 TYR B CE2 1 
ATOM   7124  C CZ  . TYR B 1 256 ? -26.768 33.218  -27.130 1.00 96.75  ? 256 TYR B CZ  1 
ATOM   7125  O OH  . TYR B 1 256 ? -25.794 32.344  -27.560 1.00 96.99  ? 256 TYR B OH  1 
ATOM   7126  N N   . GLY B 1 257 ? -31.834 38.365  -25.821 1.00 82.92  ? 257 GLY B N   1 
ATOM   7127  C CA  . GLY B 1 257 ? -32.938 39.056  -25.167 1.00 82.24  ? 257 GLY B CA  1 
ATOM   7128  C C   . GLY B 1 257 ? -33.985 39.623  -26.108 1.00 84.76  ? 257 GLY B C   1 
ATOM   7129  O O   . GLY B 1 257 ? -35.124 39.861  -25.698 1.00 88.01  ? 257 GLY B O   1 
ATOM   7130  N N   . ASN B 1 258 ? -33.610 39.848  -27.366 1.00 82.96  ? 258 ASN B N   1 
ATOM   7131  C CA  . ASN B 1 258 ? -34.529 40.436  -28.341 1.00 83.47  ? 258 ASN B CA  1 
ATOM   7132  C C   . ASN B 1 258 ? -35.273 39.406  -29.191 1.00 85.04  ? 258 ASN B C   1 
ATOM   7133  O O   . ASN B 1 258 ? -36.028 39.762  -30.102 1.00 82.97  ? 258 ASN B O   1 
ATOM   7134  C CB  . ASN B 1 258 ? -33.813 41.467  -29.218 1.00 82.37  ? 258 ASN B CB  1 
ATOM   7135  C CG  . ASN B 1 258 ? -33.662 42.811  -28.528 1.00 83.05  ? 258 ASN B CG  1 
ATOM   7136  O OD1 . ASN B 1 258 ? -32.615 43.453  -28.621 1.00 83.78  ? 258 ASN B OD1 1 
ATOM   7137  N ND2 . ASN B 1 258 ? -34.706 43.239  -27.819 1.00 82.69  ? 258 ASN B ND2 1 
ATOM   7138  N N   . VAL B 1 259 ? -35.060 38.131  -28.879 1.00 86.32  ? 259 VAL B N   1 
ATOM   7139  C CA  . VAL B 1 259 ? -35.832 37.052  -29.478 1.00 87.58  ? 259 VAL B CA  1 
ATOM   7140  C C   . VAL B 1 259 ? -37.305 37.237  -29.121 1.00 90.92  ? 259 VAL B C   1 
ATOM   7141  O O   . VAL B 1 259 ? -37.693 37.126  -27.953 1.00 91.72  ? 259 VAL B O   1 
ATOM   7142  C CB  . VAL B 1 259 ? -35.345 35.667  -28.993 1.00 86.71  ? 259 VAL B CB  1 
ATOM   7143  C CG1 . VAL B 1 259 ? -36.220 34.557  -29.554 1.00 87.82  ? 259 VAL B CG1 1 
ATOM   7144  C CG2 . VAL B 1 259 ? -33.894 35.446  -29.390 1.00 85.27  ? 259 VAL B CG2 1 
ATOM   7145  N N   . LYS B 1 260 ? -38.107 37.573  -30.129 1.00 93.41  ? 260 LYS B N   1 
ATOM   7146  C CA  . LYS B 1 260 ? -39.556 37.606  -29.985 1.00 93.73  ? 260 LYS B CA  1 
ATOM   7147  C C   . LYS B 1 260 ? -40.060 36.180  -29.794 1.00 91.37  ? 260 LYS B C   1 
ATOM   7148  O O   . LYS B 1 260 ? -40.154 35.404  -30.755 1.00 87.74  ? 260 LYS B O   1 
ATOM   7149  C CB  . LYS B 1 260 ? -40.210 38.268  -31.206 1.00 98.29  ? 260 LYS B CB  1 
ATOM   7150  C CG  . LYS B 1 260 ? -39.974 39.771  -31.288 1.00 100.98 ? 260 LYS B CG  1 
ATOM   7151  C CD  . LYS B 1 260 ? -39.930 40.253  -32.730 1.00 103.19 ? 260 LYS B CD  1 
ATOM   7152  C CE  . LYS B 1 260 ? -39.173 41.568  -32.849 1.00 102.79 ? 260 LYS B CE  1 
ATOM   7153  N NZ  . LYS B 1 260 ? -38.845 41.891  -34.267 1.00 103.42 ? 260 LYS B NZ  1 
ATOM   7154  N N   . ILE B 1 261 ? -40.353 35.845  -28.537 1.00 89.93  ? 261 ILE B N   1 
ATOM   7155  C CA  . ILE B 1 261 ? -40.745 34.489  -28.135 1.00 92.30  ? 261 ILE B CA  1 
ATOM   7156  C C   . ILE B 1 261 ? -41.952 33.932  -28.917 1.00 95.16  ? 261 ILE B C   1 
ATOM   7157  O O   . ILE B 1 261 ? -41.888 32.801  -29.419 1.00 94.07  ? 261 ILE B O   1 
ATOM   7158  C CB  . ILE B 1 261 ? -41.000 34.400  -26.609 1.00 93.27  ? 261 ILE B CB  1 
ATOM   7159  C CG1 . ILE B 1 261 ? -39.799 34.948  -25.833 1.00 90.92  ? 261 ILE B CG1 1 
ATOM   7160  C CG2 . ILE B 1 261 ? -41.300 32.964  -26.194 1.00 93.86  ? 261 ILE B CG2 1 
ATOM   7161  C CD1 . ILE B 1 261 ? -40.152 35.489  -24.465 1.00 91.51  ? 261 ILE B CD1 1 
ATOM   7162  N N   . PRO B 1 262 ? -43.051 34.720  -29.035 1.00 96.85  ? 262 PRO B N   1 
ATOM   7163  C CA  . PRO B 1 262 ? -44.180 34.209  -29.814 1.00 100.72 ? 262 PRO B CA  1 
ATOM   7164  C C   . PRO B 1 262 ? -43.787 33.796  -31.238 1.00 100.79 ? 262 PRO B C   1 
ATOM   7165  O O   . PRO B 1 262 ? -44.303 32.802  -31.749 1.00 104.54 ? 262 PRO B O   1 
ATOM   7166  C CB  . PRO B 1 262 ? -45.156 35.391  -29.830 1.00 102.03 ? 262 PRO B CB  1 
ATOM   7167  C CG  . PRO B 1 262 ? -44.871 36.111  -28.556 1.00 99.50  ? 262 PRO B CG  1 
ATOM   7168  C CD  . PRO B 1 262 ? -43.379 36.008  -28.385 1.00 97.12  ? 262 PRO B CD  1 
ATOM   7169  N N   . VAL B 1 263 ? -42.863 34.536  -31.851 1.00 98.50  ? 263 VAL B N   1 
ATOM   7170  C CA  . VAL B 1 263 ? -42.396 34.230  -33.212 1.00 96.80  ? 263 VAL B CA  1 
ATOM   7171  C C   . VAL B 1 263 ? -41.503 32.975  -33.261 1.00 95.54  ? 263 VAL B C   1 
ATOM   7172  O O   . VAL B 1 263 ? -41.562 32.208  -34.226 1.00 94.16  ? 263 VAL B O   1 
ATOM   7173  C CB  . VAL B 1 263 ? -41.692 35.448  -33.875 1.00 95.64  ? 263 VAL B CB  1 
ATOM   7174  C CG1 . VAL B 1 263 ? -41.162 35.092  -35.257 1.00 93.40  ? 263 VAL B CG1 1 
ATOM   7175  C CG2 . VAL B 1 263 ? -42.646 36.635  -33.975 1.00 95.88  ? 263 VAL B CG2 1 
ATOM   7176  N N   . LEU B 1 264 ? -40.696 32.761  -32.219 1.00 94.51  ? 264 LEU B N   1 
ATOM   7177  C CA  . LEU B 1 264 ? -39.844 31.564  -32.135 1.00 94.40  ? 264 LEU B CA  1 
ATOM   7178  C C   . LEU B 1 264 ? -40.652 30.281  -31.921 1.00 97.39  ? 264 LEU B C   1 
ATOM   7179  O O   . LEU B 1 264 ? -40.270 29.215  -32.404 1.00 99.32  ? 264 LEU B O   1 
ATOM   7180  C CB  . LEU B 1 264 ? -38.773 31.712  -31.039 1.00 91.73  ? 264 LEU B CB  1 
ATOM   7181  C CG  . LEU B 1 264 ? -37.775 30.557  -30.818 1.00 89.87  ? 264 LEU B CG  1 
ATOM   7182  C CD1 . LEU B 1 264 ? -37.036 30.174  -32.096 1.00 89.06  ? 264 LEU B CD1 1 
ATOM   7183  C CD2 . LEU B 1 264 ? -36.783 30.895  -29.715 1.00 88.07  ? 264 LEU B CD2 1 
ATOM   7184  N N   . CYS B 1 265 ? -41.761 30.389  -31.196 1.00 99.51  ? 265 CYS B N   1 
ATOM   7185  C CA  . CYS B 1 265 ? -42.640 29.244  -30.973 1.00 103.74 ? 265 CYS B CA  1 
ATOM   7186  C C   . CYS B 1 265 ? -43.304 28.778  -32.267 1.00 105.97 ? 265 CYS B C   1 
ATOM   7187  O O   . CYS B 1 265 ? -43.425 27.575  -32.509 1.00 106.12 ? 265 CYS B O   1 
ATOM   7188  C CB  . CYS B 1 265 ? -43.690 29.565  -29.911 1.00 104.28 ? 265 CYS B CB  1 
ATOM   7189  S SG  . CYS B 1 265 ? -43.027 29.614  -28.230 1.00 105.78 ? 265 CYS B SG  1 
ATOM   7190  N N   . LYS B 1 266 ? -43.709 29.737  -33.100 1.00 108.82 ? 266 LYS B N   1 
ATOM   7191  C CA  . LYS B 1 266 ? -44.292 29.440  -34.415 1.00 113.55 ? 266 LYS B CA  1 
ATOM   7192  C C   . LYS B 1 266 ? -43.249 28.840  -35.359 1.00 115.51 ? 266 LYS B C   1 
ATOM   7193  O O   . LYS B 1 266 ? -43.581 28.392  -36.458 1.00 117.64 ? 266 LYS B O   1 
ATOM   7194  C CB  . LYS B 1 266 ? -44.891 30.706  -35.048 1.00 113.61 ? 266 LYS B CB  1 
ATOM   7195  C CG  . LYS B 1 266 ? -45.845 31.491  -34.157 1.00 113.56 ? 266 LYS B CG  1 
ATOM   7196  C CD  . LYS B 1 266 ? -47.242 30.898  -34.151 1.00 115.66 ? 266 LYS B CD  1 
ATOM   7197  C CE  . LYS B 1 266 ? -48.180 31.746  -33.313 1.00 116.07 ? 266 LYS B CE  1 
ATOM   7198  N NZ  . LYS B 1 266 ? -49.581 31.255  -33.392 1.00 118.77 ? 266 LYS B NZ  1 
ATOM   7199  N N   . LEU B 1 267 ? -41.992 28.838  -34.915 1.00 116.82 ? 267 LEU B N   1 
ATOM   7200  C CA  . LEU B 1 267 ? -40.870 28.329  -35.700 1.00 116.54 ? 267 LEU B CA  1 
ATOM   7201  C C   . LEU B 1 267 ? -40.538 26.891  -35.299 1.00 118.73 ? 267 LEU B C   1 
ATOM   7202  O O   . LEU B 1 267 ? -40.260 26.047  -36.153 1.00 118.44 ? 267 LEU B O   1 
ATOM   7203  C CB  . LEU B 1 267 ? -39.642 29.215  -35.484 1.00 113.77 ? 267 LEU B CB  1 
ATOM   7204  C CG  . LEU B 1 267 ? -38.779 29.656  -36.668 1.00 112.30 ? 267 LEU B CG  1 
ATOM   7205  C CD1 . LEU B 1 267 ? -37.545 30.358  -36.124 1.00 109.91 ? 267 LEU B CD1 1 
ATOM   7206  C CD2 . LEU B 1 267 ? -38.386 28.499  -37.580 1.00 111.08 ? 267 LEU B CD2 1 
ATOM   7207  N N   . ILE B 1 268 ? -40.557 26.629  -33.993 1.00 122.08 ? 268 ILE B N   1 
ATOM   7208  C CA  . ILE B 1 268 ? -40.320 25.287  -33.460 1.00 124.29 ? 268 ILE B CA  1 
ATOM   7209  C C   . ILE B 1 268 ? -41.496 24.365  -33.796 1.00 128.15 ? 268 ILE B C   1 
ATOM   7210  O O   . ILE B 1 268 ? -41.312 23.169  -34.038 1.00 129.64 ? 268 ILE B O   1 
ATOM   7211  C CB  . ILE B 1 268 ? -40.077 25.321  -31.935 1.00 122.68 ? 268 ILE B CB  1 
ATOM   7212  C CG1 . ILE B 1 268 ? -38.951 26.307  -31.599 1.00 120.50 ? 268 ILE B CG1 1 
ATOM   7213  C CG2 . ILE B 1 268 ? -39.731 23.932  -31.412 1.00 123.49 ? 268 ILE B CG2 1 
ATOM   7214  C CD1 . ILE B 1 268 ? -39.069 26.941  -30.229 1.00 120.09 ? 268 ILE B CD1 1 
ATOM   7215  N N   . GLN B 1 269 ? -42.697 24.940  -33.824 1.00 129.48 ? 269 GLN B N   1 
ATOM   7216  C CA  . GLN B 1 269 ? -43.897 24.234  -34.263 1.00 134.03 ? 269 GLN B CA  1 
ATOM   7217  C C   . GLN B 1 269 ? -43.832 23.900  -35.757 1.00 134.63 ? 269 GLN B C   1 
ATOM   7218  O O   . GLN B 1 269 ? -44.280 22.833  -36.184 1.00 133.90 ? 269 GLN B O   1 
ATOM   7219  C CB  . GLN B 1 269 ? -45.142 25.074  -33.956 1.00 135.97 ? 269 GLN B CB  1 
ATOM   7220  C CG  . GLN B 1 269 ? -46.465 24.346  -34.145 1.00 141.04 ? 269 GLN B CG  1 
ATOM   7221  C CD  . GLN B 1 269 ? -47.591 24.947  -33.320 1.00 143.31 ? 269 GLN B CD  1 
ATOM   7222  O OE1 . GLN B 1 269 ? -47.491 26.076  -32.832 1.00 143.55 ? 269 GLN B OE1 1 
ATOM   7223  N NE2 . GLN B 1 269 ? -48.671 24.189  -33.156 1.00 142.64 ? 269 GLN B NE2 1 
ATOM   7224  N N   . SER B 1 270 ? -43.259 24.814  -36.538 1.00 134.99 ? 270 SER B N   1 
ATOM   7225  C CA  . SER B 1 270 ? -43.137 24.647  -37.988 1.00 136.65 ? 270 SER B CA  1 
ATOM   7226  C C   . SER B 1 270 ? -42.224 23.486  -38.380 1.00 137.66 ? 270 SER B C   1 
ATOM   7227  O O   . SER B 1 270 ? -42.504 22.776  -39.348 1.00 138.74 ? 270 SER B O   1 
ATOM   7228  C CB  . SER B 1 270 ? -42.641 25.939  -38.639 1.00 134.86 ? 270 SER B CB  1 
ATOM   7229  O OG  . SER B 1 270 ? -43.652 26.929  -38.642 1.00 135.38 ? 270 SER B OG  1 
ATOM   7230  N N   . ILE B 1 271 ? -41.135 23.305  -37.629 1.00 137.63 ? 271 ILE B N   1 
ATOM   7231  C CA  . ILE B 1 271 ? -40.148 22.256  -37.913 1.00 137.07 ? 271 ILE B CA  1 
ATOM   7232  C C   . ILE B 1 271 ? -40.834 20.967  -38.361 1.00 138.61 ? 271 ILE B C   1 
ATOM   7233  O O   . ILE B 1 271 ? -41.608 20.382  -37.599 1.00 141.24 ? 271 ILE B O   1 
ATOM   7234  C CB  . ILE B 1 271 ? -39.241 21.965  -36.692 1.00 134.43 ? 271 ILE B CB  1 
ATOM   7235  C CG1 . ILE B 1 271 ? -38.401 23.198  -36.340 1.00 133.35 ? 271 ILE B CG1 1 
ATOM   7236  C CG2 . ILE B 1 271 ? -38.341 20.762  -36.962 1.00 134.22 ? 271 ILE B CG2 1 
ATOM   7237  C CD1 . ILE B 1 271 ? -37.662 23.094  -35.021 1.00 132.35 ? 271 ILE B CD1 1 
ATOM   7238  N N   . PRO B 1 272 ? -40.574 20.540  -39.613 1.00 139.32 ? 272 PRO B N   1 
ATOM   7239  C CA  . PRO B 1 272 ? -41.124 19.292  -40.130 1.00 142.91 ? 272 PRO B CA  1 
ATOM   7240  C C   . PRO B 1 272 ? -40.979 18.162  -39.111 1.00 144.34 ? 272 PRO B C   1 
ATOM   7241  O O   . PRO B 1 272 ? -39.868 17.875  -38.655 1.00 141.80 ? 272 PRO B O   1 
ATOM   7242  C CB  . PRO B 1 272 ? -40.262 19.025  -41.363 1.00 143.00 ? 272 PRO B CB  1 
ATOM   7243  C CG  . PRO B 1 272 ? -39.896 20.386  -41.851 1.00 140.30 ? 272 PRO B CG  1 
ATOM   7244  C CD  . PRO B 1 272 ? -39.776 21.256  -40.629 1.00 138.54 ? 272 PRO B CD  1 
ATOM   7245  N N   . THR B 1 273 ? -42.105 17.550  -38.745 1.00 148.40 ? 273 THR B N   1 
ATOM   7246  C CA  . THR B 1 273 ? -42.151 16.572  -37.652 1.00 148.12 ? 273 THR B CA  1 
ATOM   7247  C C   . THR B 1 273 ? -41.232 15.374  -37.881 1.00 147.59 ? 273 THR B C   1 
ATOM   7248  O O   . THR B 1 273 ? -40.747 14.767  -36.925 1.00 146.04 ? 273 THR B O   1 
ATOM   7249  C CB  . THR B 1 273 ? -43.589 16.078  -37.381 1.00 149.81 ? 273 THR B CB  1 
ATOM   7250  O OG1 . THR B 1 273 ? -44.283 15.909  -38.623 1.00 150.77 ? 273 THR B OG1 1 
ATOM   7251  C CG2 . THR B 1 273 ? -44.345 17.078  -36.514 1.00 149.30 ? 273 THR B CG2 1 
ATOM   7252  N N   . HIS B 1 274 ? -40.976 15.056  -39.148 1.00 148.92 ? 274 HIS B N   1 
ATOM   7253  C CA  . HIS B 1 274 ? -40.102 13.939  -39.503 1.00 151.78 ? 274 HIS B CA  1 
ATOM   7254  C C   . HIS B 1 274 ? -38.641 14.204  -39.211 1.00 149.79 ? 274 HIS B C   1 
ATOM   7255  O O   . HIS B 1 274 ? -37.758 13.497  -39.706 1.00 149.59 ? 274 HIS B O   1 
ATOM   7256  C CB  . HIS B 1 274 ? -40.314 13.521  -40.964 1.00 156.29 ? 274 HIS B CB  1 
ATOM   7257  C CG  . HIS B 1 274 ? -40.009 14.610  -41.971 1.00 158.43 ? 274 HIS B CG  1 
ATOM   7258  N ND1 . HIS B 1 274 ? -38.760 14.860  -42.417 1.00 158.80 ? 274 HIS B ND1 1 
ATOM   7259  C CD2 . HIS B 1 274 ? -40.849 15.502  -42.639 1.00 159.85 ? 274 HIS B CD2 1 
ATOM   7260  C CE1 . HIS B 1 274 ? -38.796 15.867  -43.310 1.00 158.06 ? 274 HIS B CE1 1 
ATOM   7261  N NE2 . HIS B 1 274 ? -40.073 16.258  -43.447 1.00 160.11 ? 274 HIS B NE2 1 
ATOM   7262  N N   . LEU B 1 275 ? -38.376 15.219  -38.388 1.00 148.07 ? 275 LEU B N   1 
ATOM   7263  C CA  . LEU B 1 275 ? -37.016 15.533  -37.956 1.00 145.29 ? 275 LEU B CA  1 
ATOM   7264  C C   . LEU B 1 275 ? -36.917 15.538  -36.435 1.00 143.78 ? 275 LEU B C   1 
ATOM   7265  O O   . LEU B 1 275 ? -36.288 14.659  -35.845 1.00 142.70 ? 275 LEU B O   1 
ATOM   7266  C CB  . LEU B 1 275 ? -36.555 16.882  -38.524 1.00 142.86 ? 275 LEU B CB  1 
ATOM   7267  C CG  . LEU B 1 275 ? -36.482 17.041  -40.046 1.00 143.38 ? 275 LEU B CG  1 
ATOM   7268  C CD1 . LEU B 1 275 ? -36.338 18.509  -40.418 1.00 141.94 ? 275 LEU B CD1 1 
ATOM   7269  C CD2 . LEU B 1 275 ? -35.348 16.216  -40.642 1.00 143.84 ? 275 LEU B CD2 1 
ATOM   7270  N N   . LEU B 1 276 ? -37.544 16.528  -35.804 1.00 143.92 ? 276 LEU B N   1 
ATOM   7271  C CA  . LEU B 1 276 ? -37.523 16.641  -34.350 1.00 146.41 ? 276 LEU B CA  1 
ATOM   7272  C C   . LEU B 1 276 ? -38.540 15.688  -33.722 1.00 148.82 ? 276 LEU B C   1 
ATOM   7273  O O   . LEU B 1 276 ? -38.264 14.497  -33.566 1.00 150.05 ? 276 LEU B O   1 
ATOM   7274  C CB  . LEU B 1 276 ? -37.776 18.093  -33.911 1.00 146.99 ? 276 LEU B CB  1 
ATOM   7275  C CG  . LEU B 1 276 ? -37.436 18.487  -32.465 1.00 143.43 ? 276 LEU B CG  1 
ATOM   7276  C CD1 . LEU B 1 276 ? -35.931 18.549  -32.243 1.00 140.84 ? 276 LEU B CD1 1 
ATOM   7277  C CD2 . LEU B 1 276 ? -38.085 19.816  -32.106 1.00 142.54 ? 276 LEU B CD2 1 
ATOM   7278  N N   . ASP B 1 277 ? -39.713 16.217  -33.377 1.00 150.64 ? 277 ASP B N   1 
ATOM   7279  C CA  . ASP B 1 277 ? -40.780 15.441  -32.742 1.00 152.81 ? 277 ASP B CA  1 
ATOM   7280  C C   . ASP B 1 277 ? -42.049 16.282  -32.632 1.00 155.66 ? 277 ASP B C   1 
ATOM   7281  O O   . ASP B 1 277 ? -41.983 17.512  -32.574 1.00 155.24 ? 277 ASP B O   1 
ATOM   7282  C CB  . ASP B 1 277 ? -40.348 14.962  -31.347 1.00 150.26 ? 277 ASP B CB  1 
ATOM   7283  C CG  . ASP B 1 277 ? -41.328 13.969  -30.735 1.00 149.13 ? 277 ASP B CG  1 
ATOM   7284  O OD1 . ASP B 1 277 ? -41.861 13.116  -31.477 1.00 151.93 ? 277 ASP B OD1 1 
ATOM   7285  O OD2 . ASP B 1 277 ? -41.559 14.038  -29.510 1.00 144.69 ? 277 ASP B OD2 1 
ATOM   7286  N N   . SER B 1 278 ? -43.198 15.612  -32.613 1.00 157.50 ? 278 SER B N   1 
ATOM   7287  C CA  . SER B 1 278 ? -44.485 16.276  -32.419 1.00 157.04 ? 278 SER B CA  1 
ATOM   7288  C C   . SER B 1 278 ? -44.654 16.754  -30.974 1.00 156.31 ? 278 SER B C   1 
ATOM   7289  O O   . SER B 1 278 ? -45.225 17.818  -30.730 1.00 155.70 ? 278 SER B O   1 
ATOM   7290  C CB  . SER B 1 278 ? -45.635 15.338  -32.807 1.00 156.28 ? 278 SER B CB  1 
ATOM   7291  O OG  . SER B 1 278 ? -46.894 15.961  -32.624 1.00 152.36 ? 278 SER B OG  1 
ATOM   7292  N N   . GLU B 1 279 ? -44.137 15.970  -30.028 1.00 155.94 ? 279 GLU B N   1 
ATOM   7293  C CA  . GLU B 1 279 ? -44.344 16.234  -28.601 1.00 155.25 ? 279 GLU B CA  1 
ATOM   7294  C C   . GLU B 1 279 ? -43.104 16.783  -27.888 1.00 154.01 ? 279 GLU B C   1 
ATOM   7295  O O   . GLU B 1 279 ? -43.228 17.497  -26.890 1.00 154.11 ? 279 GLU B O   1 
ATOM   7296  C CB  . GLU B 1 279 ? -44.857 14.980  -27.885 1.00 154.76 ? 279 GLU B CB  1 
ATOM   7297  C CG  . GLU B 1 279 ? -46.257 14.552  -28.305 1.00 155.98 ? 279 GLU B CG  1 
ATOM   7298  C CD  . GLU B 1 279 ? -46.949 13.682  -27.268 1.00 155.97 ? 279 GLU B CD  1 
ATOM   7299  O OE1 . GLU B 1 279 ? -46.277 13.210  -26.326 1.00 154.52 ? 279 GLU B OE1 1 
ATOM   7300  O OE2 . GLU B 1 279 ? -48.173 13.470  -27.395 1.00 156.23 ? 279 GLU B OE2 1 
ATOM   7301  N N   . LYS B 1 280 ? -41.917 16.445  -28.393 1.00 152.92 ? 280 LYS B N   1 
ATOM   7302  C CA  . LYS B 1 280 ? -40.669 17.012  -27.864 1.00 149.22 ? 280 LYS B CA  1 
ATOM   7303  C C   . LYS B 1 280 ? -40.480 18.453  -28.327 1.00 144.73 ? 280 LYS B C   1 
ATOM   7304  O O   . LYS B 1 280 ? -39.760 19.227  -27.694 1.00 142.84 ? 280 LYS B O   1 
ATOM   7305  C CB  . LYS B 1 280 ? -39.459 16.155  -28.245 1.00 148.74 ? 280 LYS B CB  1 
ATOM   7306  C CG  . LYS B 1 280 ? -39.297 14.909  -27.387 1.00 150.69 ? 280 LYS B CG  1 
ATOM   7307  C CD  . LYS B 1 280 ? -38.143 14.043  -27.863 1.00 149.52 ? 280 LYS B CD  1 
ATOM   7308  C CE  . LYS B 1 280 ? -38.000 12.804  -26.992 1.00 149.07 ? 280 LYS B CE  1 
ATOM   7309  N NZ  . LYS B 1 280 ? -36.768 12.032  -27.315 1.00 147.57 ? 280 LYS B NZ  1 
ATOM   7310  N N   . LYS B 1 281 ? -41.126 18.798  -29.438 1.00 143.78 ? 281 LYS B N   1 
ATOM   7311  C CA  . LYS B 1 281 ? -41.303 20.189  -29.839 1.00 143.01 ? 281 LYS B CA  1 
ATOM   7312  C C   . LYS B 1 281 ? -42.060 20.949  -28.745 1.00 141.80 ? 281 LYS B C   1 
ATOM   7313  O O   . LYS B 1 281 ? -41.631 22.022  -28.314 1.00 141.32 ? 281 LYS B O   1 
ATOM   7314  C CB  . LYS B 1 281 ? -42.056 20.266  -31.176 1.00 145.42 ? 281 LYS B CB  1 
ATOM   7315  C CG  . LYS B 1 281 ? -42.837 21.553  -31.405 1.00 145.66 ? 281 LYS B CG  1 
ATOM   7316  C CD  . LYS B 1 281 ? -44.232 21.252  -31.928 1.00 147.56 ? 281 LYS B CD  1 
ATOM   7317  C CE  . LYS B 1 281 ? -45.252 22.229  -31.367 1.00 145.62 ? 281 LYS B CE  1 
ATOM   7318  N NZ  . LYS B 1 281 ? -46.649 21.783  -31.623 1.00 149.00 ? 281 LYS B NZ  1 
ATOM   7319  N N   . ASN B 1 282 ? -43.168 20.368  -28.284 1.00 143.10 ? 282 ASN B N   1 
ATOM   7320  C CA  . ASN B 1 282 ? -44.002 20.981  -27.249 1.00 142.11 ? 282 ASN B CA  1 
ATOM   7321  C C   . ASN B 1 282 ? -43.300 21.120  -25.899 1.00 139.57 ? 282 ASN B C   1 
ATOM   7322  O O   . ASN B 1 282 ? -43.701 21.939  -25.069 1.00 138.84 ? 282 ASN B O   1 
ATOM   7323  C CB  . ASN B 1 282 ? -45.318 20.218  -27.092 1.00 145.20 ? 282 ASN B CB  1 
ATOM   7324  C CG  . ASN B 1 282 ? -46.288 20.491  -28.226 1.00 147.67 ? 282 ASN B CG  1 
ATOM   7325  O OD1 . ASN B 1 282 ? -46.717 21.627  -28.434 1.00 147.54 ? 282 ASN B OD1 1 
ATOM   7326  N ND2 . ASN B 1 282 ? -46.644 19.446  -28.962 1.00 149.17 ? 282 ASN B ND2 1 
ATOM   7327  N N   . PHE B 1 283 ? -42.255 20.320  -25.687 1.00 136.98 ? 283 PHE B N   1 
ATOM   7328  C CA  . PHE B 1 283 ? -41.396 20.467  -24.514 1.00 134.40 ? 283 PHE B CA  1 
ATOM   7329  C C   . PHE B 1 283 ? -40.610 21.775  -24.595 1.00 130.09 ? 283 PHE B C   1 
ATOM   7330  O O   . PHE B 1 283 ? -40.445 22.472  -23.594 1.00 127.63 ? 283 PHE B O   1 
ATOM   7331  C CB  . PHE B 1 283 ? -40.440 19.274  -24.380 1.00 137.13 ? 283 PHE B CB  1 
ATOM   7332  C CG  . PHE B 1 283 ? -39.703 19.227  -23.064 1.00 140.16 ? 283 PHE B CG  1 
ATOM   7333  C CD1 . PHE B 1 283 ? -40.281 18.627  -21.945 1.00 142.24 ? 283 PHE B CD1 1 
ATOM   7334  C CD2 . PHE B 1 283 ? -38.430 19.780  -22.941 1.00 138.29 ? 283 PHE B CD2 1 
ATOM   7335  C CE1 . PHE B 1 283 ? -39.606 18.585  -20.731 1.00 140.42 ? 283 PHE B CE1 1 
ATOM   7336  C CE2 . PHE B 1 283 ? -37.752 19.741  -21.729 1.00 138.03 ? 283 PHE B CE2 1 
ATOM   7337  C CZ  . PHE B 1 283 ? -38.340 19.142  -20.624 1.00 138.38 ? 283 PHE B CZ  1 
ATOM   7338  N N   . ILE B 1 284 ? -40.143 22.104  -25.797 1.00 127.16 ? 284 ILE B N   1 
ATOM   7339  C CA  . ILE B 1 284 ? -39.370 23.323  -26.029 1.00 123.61 ? 284 ILE B CA  1 
ATOM   7340  C C   . ILE B 1 284 ? -40.270 24.564  -26.088 1.00 124.81 ? 284 ILE B C   1 
ATOM   7341  O O   . ILE B 1 284 ? -39.891 25.632  -25.601 1.00 122.52 ? 284 ILE B O   1 
ATOM   7342  C CB  . ILE B 1 284 ? -38.520 23.215  -27.317 1.00 121.99 ? 284 ILE B CB  1 
ATOM   7343  C CG1 . ILE B 1 284 ? -37.560 22.023  -27.222 1.00 121.35 ? 284 ILE B CG1 1 
ATOM   7344  C CG2 . ILE B 1 284 ? -37.746 24.504  -27.569 1.00 119.06 ? 284 ILE B CG2 1 
ATOM   7345  C CD1 . ILE B 1 284 ? -37.067 21.515  -28.563 1.00 122.49 ? 284 ILE B CD1 1 
ATOM   7346  N N   . VAL B 1 285 ? -41.460 24.410  -26.671 1.00 126.91 ? 285 VAL B N   1 
ATOM   7347  C CA  . VAL B 1 285 ? -42.408 25.522  -26.838 1.00 130.43 ? 285 VAL B CA  1 
ATOM   7348  C C   . VAL B 1 285 ? -42.590 26.331  -25.547 1.00 132.51 ? 285 VAL B C   1 
ATOM   7349  O O   . VAL B 1 285 ? -42.360 27.543  -25.530 1.00 133.87 ? 285 VAL B O   1 
ATOM   7350  C CB  . VAL B 1 285 ? -43.784 25.035  -27.367 1.00 132.03 ? 285 VAL B CB  1 
ATOM   7351  C CG1 . VAL B 1 285 ? -44.813 26.159  -27.332 1.00 131.84 ? 285 VAL B CG1 1 
ATOM   7352  C CG2 . VAL B 1 285 ? -43.651 24.492  -28.781 1.00 132.18 ? 285 VAL B CG2 1 
ATOM   7353  N N   . ASP B 1 286 ? -42.980 25.653  -24.469 1.00 134.56 ? 286 ASP B N   1 
ATOM   7354  C CA  . ASP B 1 286 ? -43.260 26.324  -23.195 1.00 134.63 ? 286 ASP B CA  1 
ATOM   7355  C C   . ASP B 1 286 ? -42.064 26.370  -22.232 1.00 128.17 ? 286 ASP B C   1 
ATOM   7356  O O   . ASP B 1 286 ? -42.121 27.035  -21.196 1.00 123.72 ? 286 ASP B O   1 
ATOM   7357  C CB  . ASP B 1 286 ? -44.515 25.743  -22.517 1.00 139.59 ? 286 ASP B CB  1 
ATOM   7358  C CG  . ASP B 1 286 ? -44.866 24.351  -23.017 1.00 143.41 ? 286 ASP B CG  1 
ATOM   7359  O OD1 . ASP B 1 286 ? -44.327 23.367  -22.468 1.00 146.15 ? 286 ASP B OD1 1 
ATOM   7360  O OD2 . ASP B 1 286 ? -45.691 24.243  -23.951 1.00 142.25 ? 286 ASP B OD2 1 
ATOM   7361  N N   . HIS B 1 287 ? -40.982 25.681  -22.589 1.00 125.63 ? 287 HIS B N   1 
ATOM   7362  C CA  . HIS B 1 287 ? -39.713 25.814  -21.870 1.00 124.46 ? 287 HIS B CA  1 
ATOM   7363  C C   . HIS B 1 287 ? -39.136 27.194  -22.047 1.00 120.37 ? 287 HIS B C   1 
ATOM   7364  O O   . HIS B 1 287 ? -38.346 27.657  -21.222 1.00 119.30 ? 287 HIS B O   1 
ATOM   7365  C CB  . HIS B 1 287 ? -38.712 24.763  -22.341 1.00 126.65 ? 287 HIS B CB  1 
ATOM   7366  C CG  . HIS B 1 287 ? -37.393 24.807  -21.607 1.00 128.27 ? 287 HIS B CG  1 
ATOM   7367  N ND1 . HIS B 1 287 ? -36.319 25.464  -22.087 1.00 129.88 ? 287 HIS B ND1 1 
ATOM   7368  C CD2 . HIS B 1 287 ? -37.004 24.255  -20.387 1.00 127.91 ? 287 HIS B CD2 1 
ATOM   7369  C CE1 . HIS B 1 287 ? -35.294 25.334  -21.224 1.00 128.91 ? 287 HIS B CE1 1 
ATOM   7370  N NE2 . HIS B 1 287 ? -35.714 24.595  -20.185 1.00 129.28 ? 287 HIS B NE2 1 
ATOM   7371  N N   . ILE B 1 288 ? -39.535 27.860  -23.131 1.00 116.23 ? 288 ILE B N   1 
ATOM   7372  C CA  . ILE B 1 288 ? -39.088 29.220  -23.435 1.00 110.89 ? 288 ILE B CA  1 
ATOM   7373  C C   . ILE B 1 288 ? -40.083 30.253  -22.904 1.00 108.68 ? 288 ILE B C   1 
ATOM   7374  O O   . ILE B 1 288 ? -39.692 31.325  -22.437 1.00 105.69 ? 288 ILE B O   1 
ATOM   7375  C CB  . ILE B 1 288 ? -38.881 29.421  -24.958 1.00 112.46 ? 288 ILE B CB  1 
ATOM   7376  C CG1 . ILE B 1 288 ? -38.001 28.306  -25.548 1.00 111.14 ? 288 ILE B CG1 1 
ATOM   7377  C CG2 . ILE B 1 288 ? -38.303 30.799  -25.260 1.00 111.99 ? 288 ILE B CG2 1 
ATOM   7378  C CD1 . ILE B 1 288 ? -36.761 27.971  -24.739 1.00 106.23 ? 288 ILE B CD1 1 
ATOM   7379  N N   . SER B 1 289 ? -41.370 29.918  -22.974 1.00 109.05 ? 289 SER B N   1 
ATOM   7380  C CA  . SER B 1 289 ? -42.430 30.789  -22.470 1.00 108.17 ? 289 SER B CA  1 
ATOM   7381  C C   . SER B 1 289 ? -42.428 30.860  -20.942 1.00 107.77 ? 289 SER B C   1 
ATOM   7382  O O   . SER B 1 289 ? -42.729 31.905  -20.359 1.00 106.46 ? 289 SER B O   1 
ATOM   7383  C CB  . SER B 1 289 ? -43.791 30.309  -22.971 1.00 109.99 ? 289 SER B CB  1 
ATOM   7384  O OG  . SER B 1 289 ? -43.752 30.037  -24.361 1.00 108.42 ? 289 SER B OG  1 
ATOM   7385  N N   . ASN B 1 290 ? -42.081 29.744  -20.302 1.00 107.16 ? 290 ASN B N   1 
ATOM   7386  C CA  . ASN B 1 290 ? -42.048 29.667  -18.843 1.00 106.64 ? 290 ASN B CA  1 
ATOM   7387  C C   . ASN B 1 290 ? -40.623 29.537  -18.309 1.00 105.13 ? 290 ASN B C   1 
ATOM   7388  O O   . ASN B 1 290 ? -40.238 28.494  -17.773 1.00 104.91 ? 290 ASN B O   1 
ATOM   7389  C CB  . ASN B 1 290 ? -42.913 28.502  -18.339 1.00 106.24 ? 290 ASN B CB  1 
ATOM   7390  C CG  . ASN B 1 290 ? -44.284 28.467  -18.987 1.00 107.77 ? 290 ASN B CG  1 
ATOM   7391  O OD1 . ASN B 1 290 ? -45.033 29.443  -18.941 1.00 108.20 ? 290 ASN B OD1 1 
ATOM   7392  N ND2 . ASN B 1 290 ? -44.622 27.333  -19.590 1.00 107.85 ? 290 ASN B ND2 1 
ATOM   7393  N N   . GLN B 1 291 ? -39.840 30.599  -18.469 1.00 103.33 ? 291 GLN B N   1 
ATOM   7394  C CA  . GLN B 1 291 ? -38.496 30.648  -17.908 1.00 102.38 ? 291 GLN B CA  1 
ATOM   7395  C C   . GLN B 1 291 ? -38.520 31.341  -16.546 1.00 103.44 ? 291 GLN B C   1 
ATOM   7396  O O   . GLN B 1 291 ? -38.624 32.566  -16.460 1.00 102.92 ? 291 GLN B O   1 
ATOM   7397  C CB  . GLN B 1 291 ? -37.536 31.357  -18.865 1.00 100.47 ? 291 GLN B CB  1 
ATOM   7398  C CG  . GLN B 1 291 ? -37.189 30.551  -20.109 1.00 100.39 ? 291 GLN B CG  1 
ATOM   7399  C CD  . GLN B 1 291 ? -36.415 31.352  -21.146 1.00 98.60  ? 291 GLN B CD  1 
ATOM   7400  O OE1 . GLN B 1 291 ? -35.587 30.802  -21.878 1.00 96.53  ? 291 GLN B OE1 1 
ATOM   7401  N NE2 . GLN B 1 291 ? -36.687 32.655  -21.221 1.00 97.21  ? 291 GLN B NE2 1 
ATOM   7402  N N   . PHE B 1 292 ? -38.451 30.546  -15.482 1.00 105.30 ? 292 PHE B N   1 
ATOM   7403  C CA  . PHE B 1 292 ? -38.486 31.078  -14.120 1.00 106.55 ? 292 PHE B CA  1 
ATOM   7404  C C   . PHE B 1 292 ? -37.166 30.861  -13.385 1.00 105.22 ? 292 PHE B C   1 
ATOM   7405  O O   . PHE B 1 292 ? -36.541 29.802  -13.500 1.00 103.93 ? 292 PHE B O   1 
ATOM   7406  C CB  . PHE B 1 292 ? -39.663 30.500  -13.319 1.00 110.35 ? 292 PHE B CB  1 
ATOM   7407  C CG  . PHE B 1 292 ? -40.123 29.148  -13.794 1.00 113.85 ? 292 PHE B CG  1 
ATOM   7408  C CD1 . PHE B 1 292 ? -39.335 28.014  -13.596 1.00 115.26 ? 292 PHE B CD1 1 
ATOM   7409  C CD2 . PHE B 1 292 ? -41.352 29.006  -14.432 1.00 115.97 ? 292 PHE B CD2 1 
ATOM   7410  C CE1 . PHE B 1 292 ? -39.761 26.769  -14.037 1.00 118.30 ? 292 PHE B CE1 1 
ATOM   7411  C CE2 . PHE B 1 292 ? -41.784 27.762  -14.872 1.00 118.18 ? 292 PHE B CE2 1 
ATOM   7412  C CZ  . PHE B 1 292 ? -40.988 26.643  -14.674 1.00 119.16 ? 292 PHE B CZ  1 
ATOM   7413  N N   . VAL B 1 293 ? -36.745 31.880  -12.641 1.00 102.52 ? 293 VAL B N   1 
ATOM   7414  C CA  . VAL B 1 293 ? -35.441 31.877  -11.987 1.00 100.95 ? 293 VAL B CA  1 
ATOM   7415  C C   . VAL B 1 293 ? -35.541 32.297  -10.525 1.00 102.58 ? 293 VAL B C   1 
ATOM   7416  O O   . VAL B 1 293 ? -36.466 33.014  -10.136 1.00 104.03 ? 293 VAL B O   1 
ATOM   7417  C CB  . VAL B 1 293 ? -34.428 32.800  -12.712 1.00 99.89  ? 293 VAL B CB  1 
ATOM   7418  C CG1 . VAL B 1 293 ? -34.167 32.305  -14.127 1.00 100.33 ? 293 VAL B CG1 1 
ATOM   7419  C CG2 . VAL B 1 293 ? -34.912 34.246  -12.727 1.00 99.75  ? 293 VAL B CG2 1 
ATOM   7420  N N   . ALA B 1 294 ? -34.584 31.841  -9.723  1.00 101.45 ? 294 ALA B N   1 
ATOM   7421  C CA  . ALA B 1 294 ? -34.470 32.269  -8.335  1.00 100.80 ? 294 ALA B CA  1 
ATOM   7422  C C   . ALA B 1 294 ? -33.448 33.393  -8.220  1.00 97.97  ? 294 ALA B C   1 
ATOM   7423  O O   . ALA B 1 294 ? -32.369 33.323  -8.807  1.00 98.44  ? 294 ALA B O   1 
ATOM   7424  C CB  . ALA B 1 294 ? -34.080 31.098  -7.447  1.00 101.57 ? 294 ALA B CB  1 
ATOM   7425  N N   . PHE B 1 295 ? -33.799 34.438  -7.481  1.00 96.35  ? 295 PHE B N   1 
ATOM   7426  C CA  . PHE B 1 295 ? -32.870 35.529  -7.244  1.00 95.59  ? 295 PHE B CA  1 
ATOM   7427  C C   . PHE B 1 295 ? -32.509 35.620  -5.761  1.00 99.03  ? 295 PHE B C   1 
ATOM   7428  O O   . PHE B 1 295 ? -31.696 34.830  -5.268  1.00 100.90 ? 295 PHE B O   1 
ATOM   7429  C CB  . PHE B 1 295 ? -33.421 36.857  -7.784  1.00 91.97  ? 295 PHE B CB  1 
ATOM   7430  C CG  . PHE B 1 295 ? -32.434 37.996  -7.722  1.00 88.71  ? 295 PHE B CG  1 
ATOM   7431  C CD1 . PHE B 1 295 ? -31.132 37.838  -8.190  1.00 84.43  ? 295 PHE B CD1 1 
ATOM   7432  C CD2 . PHE B 1 295 ? -32.807 39.228  -7.194  1.00 86.83  ? 295 PHE B CD2 1 
ATOM   7433  C CE1 . PHE B 1 295 ? -30.222 38.883  -8.127  1.00 81.79  ? 295 PHE B CE1 1 
ATOM   7434  C CE2 . PHE B 1 295 ? -31.902 40.276  -7.133  1.00 84.05  ? 295 PHE B CE2 1 
ATOM   7435  C CZ  . PHE B 1 295 ? -30.609 40.104  -7.601  1.00 81.56  ? 295 PHE B CZ  1 
ATOM   7436  N N   . ARG B 1 296 ? -33.114 36.570  -5.053  1.00 99.35  ? 296 ARG B N   1 
ATOM   7437  C CA  . ARG B 1 296 ? -32.841 36.741  -3.628  1.00 97.84  ? 296 ARG B CA  1 
ATOM   7438  C C   . ARG B 1 296 ? -33.887 36.010  -2.796  1.00 100.91 ? 296 ARG B C   1 
ATOM   7439  O O   . ARG B 1 296 ? -34.799 36.626  -2.237  1.00 102.66 ? 296 ARG B O   1 
ATOM   7440  C CB  . ARG B 1 296 ? -32.754 38.226  -3.262  1.00 92.69  ? 296 ARG B CB  1 
ATOM   7441  C CG  . ARG B 1 296 ? -31.447 38.873  -3.699  1.00 88.05  ? 296 ARG B CG  1 
ATOM   7442  C CD  . ARG B 1 296 ? -31.518 40.390  -3.666  1.00 85.06  ? 296 ARG B CD  1 
ATOM   7443  N NE  . ARG B 1 296 ? -30.268 40.989  -4.131  1.00 81.64  ? 296 ARG B NE  1 
ATOM   7444  C CZ  . ARG B 1 296 ? -30.026 42.298  -4.173  1.00 80.19  ? 296 ARG B CZ  1 
ATOM   7445  N NH1 . ARG B 1 296 ? -30.951 43.165  -3.780  1.00 79.65  ? 296 ARG B NH1 1 
ATOM   7446  N NH2 . ARG B 1 296 ? -28.856 42.741  -4.609  1.00 77.08  ? 296 ARG B NH2 1 
ATOM   7447  N N   . ARG B 1 297 ? -33.748 34.681  -2.750  1.00 104.73 ? 297 ARG B N   1 
ATOM   7448  C CA  . ARG B 1 297 ? -34.667 33.786  -2.030  1.00 110.60 ? 297 ARG B CA  1 
ATOM   7449  C C   . ARG B 1 297 ? -36.098 33.792  -2.595  1.00 111.24 ? 297 ARG B C   1 
ATOM   7450  O O   . ARG B 1 297 ? -37.034 33.325  -1.940  1.00 112.37 ? 297 ARG B O   1 
ATOM   7451  C CB  . ARG B 1 297 ? -34.672 34.095  -0.523  1.00 112.96 ? 297 ARG B CB  1 
ATOM   7452  C CG  . ARG B 1 297 ? -33.421 33.649  0.222   1.00 112.85 ? 297 ARG B CG  1 
ATOM   7453  C CD  . ARG B 1 297 ? -33.361 34.290  1.600   1.00 116.52 ? 297 ARG B CD  1 
ATOM   7454  N NE  . ARG B 1 297 ? -32.839 33.379  2.618   1.00 120.02 ? 297 ARG B NE  1 
ATOM   7455  C CZ  . ARG B 1 297 ? -32.986 33.551  3.932   1.00 121.85 ? 297 ARG B CZ  1 
ATOM   7456  N NH1 . ARG B 1 297 ? -33.642 34.605  4.403   1.00 124.15 ? 297 ARG B NH1 1 
ATOM   7457  N NH2 . ARG B 1 297 ? -32.481 32.663  4.779   1.00 119.78 ? 297 ARG B NH2 1 
ATOM   7458  N N   . LYS B 1 298 ? -36.255 34.308  -3.815  1.00 111.56 ? 298 LYS B N   1 
ATOM   7459  C CA  . LYS B 1 298 ? -37.574 34.443  -4.446  1.00 111.12 ? 298 LYS B CA  1 
ATOM   7460  C C   . LYS B 1 298 ? -37.559 34.009  -5.914  1.00 110.65 ? 298 LYS B C   1 
ATOM   7461  O O   . LYS B 1 298 ? -36.532 34.114  -6.590  1.00 106.70 ? 298 LYS B O   1 
ATOM   7462  C CB  . LYS B 1 298 ? -38.084 35.885  -4.324  1.00 111.30 ? 298 LYS B CB  1 
ATOM   7463  C CG  . LYS B 1 298 ? -38.499 36.269  -2.913  1.00 113.09 ? 298 LYS B CG  1 
ATOM   7464  C CD  . LYS B 1 298 ? -38.886 37.732  -2.806  1.00 112.45 ? 298 LYS B CD  1 
ATOM   7465  C CE  . LYS B 1 298 ? -39.281 38.073  -1.379  1.00 112.44 ? 298 LYS B CE  1 
ATOM   7466  N NZ  . LYS B 1 298 ? -39.683 39.497  -1.228  1.00 113.78 ? 298 LYS B NZ  1 
ATOM   7467  N N   . ILE B 1 299 ? -38.706 33.523  -6.392  1.00 111.09 ? 299 ILE B N   1 
ATOM   7468  C CA  . ILE B 1 299 ? -38.861 33.078  -7.782  1.00 110.30 ? 299 ILE B CA  1 
ATOM   7469  C C   . ILE B 1 299 ? -39.370 34.200  -8.692  1.00 109.10 ? 299 ILE B C   1 
ATOM   7470  O O   . ILE B 1 299 ? -40.372 34.854  -8.392  1.00 111.25 ? 299 ILE B O   1 
ATOM   7471  C CB  . ILE B 1 299 ? -39.785 31.837  -7.884  1.00 113.61 ? 299 ILE B CB  1 
ATOM   7472  C CG1 . ILE B 1 299 ? -38.975 30.555  -7.678  1.00 115.39 ? 299 ILE B CG1 1 
ATOM   7473  C CG2 . ILE B 1 299 ? -40.508 31.787  -9.228  1.00 113.91 ? 299 ILE B CG2 1 
ATOM   7474  C CD1 . ILE B 1 299 ? -39.816 29.296  -7.654  1.00 121.96 ? 299 ILE B CD1 1 
ATOM   7475  N N   . TYR B 1 300 ? -38.665 34.411  -9.803  1.00 104.76 ? 300 TYR B N   1 
ATOM   7476  C CA  . TYR B 1 300 ? -39.051 35.401  -10.804 1.00 101.72 ? 300 TYR B CA  1 
ATOM   7477  C C   . TYR B 1 300 ? -39.211 34.750  -12.179 1.00 98.83  ? 300 TYR B C   1 
ATOM   7478  O O   . TYR B 1 300 ? -38.568 33.745  -12.475 1.00 95.26  ? 300 TYR B O   1 
ATOM   7479  C CB  . TYR B 1 300 ? -38.007 36.512  -10.880 1.00 101.47 ? 300 TYR B CB  1 
ATOM   7480  C CG  . TYR B 1 300 ? -37.895 37.367  -9.636  1.00 102.26 ? 300 TYR B CG  1 
ATOM   7481  C CD1 . TYR B 1 300 ? -37.093 36.973  -8.563  1.00 102.15 ? 300 TYR B CD1 1 
ATOM   7482  C CD2 . TYR B 1 300 ? -38.566 38.584  -9.543  1.00 103.87 ? 300 TYR B CD2 1 
ATOM   7483  C CE1 . TYR B 1 300 ? -36.983 37.757  -7.423  1.00 102.56 ? 300 TYR B CE1 1 
ATOM   7484  C CE2 . TYR B 1 300 ? -38.459 39.377  -8.409  1.00 105.45 ? 300 TYR B CE2 1 
ATOM   7485  C CZ  . TYR B 1 300 ? -37.668 38.959  -7.353  1.00 104.47 ? 300 TYR B CZ  1 
ATOM   7486  O OH  . TYR B 1 300 ? -37.562 39.742  -6.226  1.00 104.51 ? 300 TYR B OH  1 
ATOM   7487  N N   . LYS B 1 301 ? -40.076 35.330  -13.008 1.00 99.56  ? 301 LYS B N   1 
ATOM   7488  C CA  . LYS B 1 301 ? -40.269 34.873  -14.387 1.00 99.48  ? 301 LYS B CA  1 
ATOM   7489  C C   . LYS B 1 301 ? -39.512 35.761  -15.378 1.00 96.73  ? 301 LYS B C   1 
ATOM   7490  O O   . LYS B 1 301 ? -39.659 36.989  -15.372 1.00 97.33  ? 301 LYS B O   1 
ATOM   7491  C CB  . LYS B 1 301 ? -41.766 34.801  -14.737 1.00 101.74 ? 301 LYS B CB  1 
ATOM   7492  C CG  . LYS B 1 301 ? -42.109 35.185  -16.175 1.00 102.98 ? 301 LYS B CG  1 
ATOM   7493  C CD  . LYS B 1 301 ? -43.391 34.529  -16.667 1.00 102.44 ? 301 LYS B CD  1 
ATOM   7494  C CE  . LYS B 1 301 ? -43.089 33.237  -17.406 1.00 102.47 ? 301 LYS B CE  1 
ATOM   7495  N NZ  . LYS B 1 301 ? -44.174 32.870  -18.354 1.00 102.85 ? 301 LYS B NZ  1 
ATOM   7496  N N   . TRP B 1 302 ? -38.687 35.128  -16.208 1.00 92.95  ? 302 TRP B N   1 
ATOM   7497  C CA  . TRP B 1 302 ? -37.964 35.822  -17.270 1.00 90.61  ? 302 TRP B CA  1 
ATOM   7498  C C   . TRP B 1 302 ? -38.687 35.635  -18.570 1.00 90.55  ? 302 TRP B C   1 
ATOM   7499  O O   . TRP B 1 302 ? -38.770 34.522  -19.100 1.00 89.82  ? 302 TRP B O   1 
ATOM   7500  C CB  . TRP B 1 302 ? -36.530 35.304  -17.371 1.00 87.79  ? 302 TRP B CB  1 
ATOM   7501  C CG  . TRP B 1 302 ? -35.640 36.120  -18.286 1.00 86.96  ? 302 TRP B CG  1 
ATOM   7502  C CD1 . TRP B 1 302 ? -35.444 35.949  -19.656 1.00 86.19  ? 302 TRP B CD1 1 
ATOM   7503  C CD2 . TRP B 1 302 ? -34.780 37.253  -17.917 1.00 84.78  ? 302 TRP B CD2 1 
ATOM   7504  N NE1 . TRP B 1 302 ? -34.552 36.877  -20.142 1.00 84.84  ? 302 TRP B NE1 1 
ATOM   7505  C CE2 . TRP B 1 302 ? -34.119 37.687  -19.150 1.00 83.20  ? 302 TRP B CE2 1 
ATOM   7506  C CE3 . TRP B 1 302 ? -34.504 37.926  -16.731 1.00 82.54  ? 302 TRP B CE3 1 
ATOM   7507  C CZ2 . TRP B 1 302 ? -33.231 38.750  -19.174 1.00 81.55  ? 302 TRP B CZ2 1 
ATOM   7508  C CZ3 . TRP B 1 302 ? -33.604 38.998  -16.766 1.00 80.67  ? 302 TRP B CZ3 1 
ATOM   7509  C CH2 . TRP B 1 302 ? -32.984 39.399  -17.961 1.00 81.39  ? 302 TRP B CH2 1 
ATOM   7510  N N   . ASN B 1 303 ? -39.242 36.726  -19.084 1.00 92.22  ? 303 ASN B N   1 
ATOM   7511  C CA  . ASN B 1 303 ? -40.004 36.691  -20.329 1.00 96.39  ? 303 ASN B CA  1 
ATOM   7512  C C   . ASN B 1 303 ? -39.399 37.600  -21.399 1.00 95.53  ? 303 ASN B C   1 
ATOM   7513  O O   . ASN B 1 303 ? -40.019 37.869  -22.434 1.00 97.67  ? 303 ASN B O   1 
ATOM   7514  C CB  . ASN B 1 303 ? -41.485 37.029  -20.077 1.00 99.92  ? 303 ASN B CB  1 
ATOM   7515  C CG  . ASN B 1 303 ? -41.674 38.107  -19.019 1.00 100.66 ? 303 ASN B CG  1 
ATOM   7516  O OD1 . ASN B 1 303 ? -40.874 39.039  -18.909 1.00 100.90 ? 303 ASN B OD1 1 
ATOM   7517  N ND2 . ASN B 1 303 ? -42.738 37.981  -18.232 1.00 100.92 ? 303 ASN B ND2 1 
ATOM   7518  N N   . HIS B 1 304 ? -38.179 38.064  -21.142 1.00 92.57  ? 304 HIS B N   1 
ATOM   7519  C CA  . HIS B 1 304 ? -37.449 38.866  -22.109 1.00 90.69  ? 304 HIS B CA  1 
ATOM   7520  C C   . HIS B 1 304 ? -36.592 37.996  -22.985 1.00 88.40  ? 304 HIS B C   1 
ATOM   7521  O O   . HIS B 1 304 ? -35.390 37.828  -22.747 1.00 86.11  ? 304 HIS B O   1 
ATOM   7522  C CB  . HIS B 1 304 ? -36.620 39.937  -21.414 1.00 89.17  ? 304 HIS B CB  1 
ATOM   7523  C CG  . HIS B 1 304 ? -35.851 40.814  -22.366 1.00 90.50  ? 304 HIS B CG  1 
ATOM   7524  N ND1 . HIS B 1 304 ? -36.451 41.722  -23.160 1.00 92.56  ? 304 HIS B ND1 1 
ATOM   7525  C CD2 . HIS B 1 304 ? -34.487 40.888  -22.645 1.00 88.94  ? 304 HIS B CD2 1 
ATOM   7526  C CE1 . HIS B 1 304 ? -35.521 42.347  -23.905 1.00 92.27  ? 304 HIS B CE1 1 
ATOM   7527  N NE2 . HIS B 1 304 ? -34.320 41.837  -23.588 1.00 90.55  ? 304 HIS B NE2 1 
ATOM   7528  N N   . GLY B 1 305 ? -37.221 37.424  -24.007 1.00 89.53  ? 305 GLY B N   1 
ATOM   7529  C CA  . GLY B 1 305 ? -36.553 36.511  -24.925 1.00 89.02  ? 305 GLY B CA  1 
ATOM   7530  C C   . GLY B 1 305 ? -35.983 35.303  -24.218 1.00 88.21  ? 305 GLY B C   1 
ATOM   7531  O O   . GLY B 1 305 ? -36.522 34.845  -23.207 1.00 88.60  ? 305 GLY B O   1 
ATOM   7532  N N   . LEU B 1 306 ? -34.885 34.789  -24.756 1.00 88.37  ? 306 LEU B N   1 
ATOM   7533  C CA  . LEU B 1 306 ? -34.152 33.708  -24.123 1.00 89.47  ? 306 LEU B CA  1 
ATOM   7534  C C   . LEU B 1 306 ? -33.207 34.247  -23.057 1.00 88.62  ? 306 LEU B C   1 
ATOM   7535  O O   . LEU B 1 306 ? -32.776 35.404  -23.117 1.00 85.86  ? 306 LEU B O   1 
ATOM   7536  C CB  . LEU B 1 306 ? -33.363 32.919  -25.167 1.00 89.57  ? 306 LEU B CB  1 
ATOM   7537  C CG  . LEU B 1 306 ? -34.160 32.082  -26.167 1.00 91.10  ? 306 LEU B CG  1 
ATOM   7538  C CD1 . LEU B 1 306 ? -33.329 31.828  -27.413 1.00 89.36  ? 306 LEU B CD1 1 
ATOM   7539  C CD2 . LEU B 1 306 ? -34.607 30.769  -25.542 1.00 93.13  ? 306 LEU B CD2 1 
ATOM   7540  N N   . LEU B 1 307 ? -32.903 33.400  -22.078 1.00 90.99  ? 307 LEU B N   1 
ATOM   7541  C CA  . LEU B 1 307 ? -31.903 33.697  -21.062 1.00 91.84  ? 307 LEU B CA  1 
ATOM   7542  C C   . LEU B 1 307 ? -30.533 33.282  -21.549 1.00 93.55  ? 307 LEU B C   1 
ATOM   7543  O O   . LEU B 1 307 ? -30.348 32.149  -21.996 1.00 94.54  ? 307 LEU B O   1 
ATOM   7544  C CB  . LEU B 1 307 ? -32.205 32.916  -19.787 1.00 91.41  ? 307 LEU B CB  1 
ATOM   7545  C CG  . LEU B 1 307 ? -33.226 33.471  -18.810 1.00 91.17  ? 307 LEU B CG  1 
ATOM   7546  C CD1 . LEU B 1 307 ? -33.847 32.328  -18.028 1.00 94.04  ? 307 LEU B CD1 1 
ATOM   7547  C CD2 . LEU B 1 307 ? -32.572 34.483  -17.883 1.00 88.44  ? 307 LEU B CD2 1 
ATOM   7548  N N   . GLN B 1 308 ? -29.567 34.188  -21.454 1.00 97.24  ? 308 GLN B N   1 
ATOM   7549  C CA  . GLN B 1 308 ? -28.169 33.797  -21.584 1.00 99.70  ? 308 GLN B CA  1 
ATOM   7550  C C   . GLN B 1 308 ? -27.806 32.913  -20.388 1.00 102.17 ? 308 GLN B C   1 
ATOM   7551  O O   . GLN B 1 308 ? -27.709 33.397  -19.262 1.00 104.45 ? 308 GLN B O   1 
ATOM   7552  C CB  . GLN B 1 308 ? -27.253 35.025  -21.655 1.00 98.28  ? 308 GLN B CB  1 
ATOM   7553  C CG  . GLN B 1 308 ? -27.195 35.685  -23.026 1.00 98.15  ? 308 GLN B CG  1 
ATOM   7554  C CD  . GLN B 1 308 ? -25.807 36.199  -23.373 1.00 96.70  ? 308 GLN B CD  1 
ATOM   7555  O OE1 . GLN B 1 308 ? -25.323 37.167  -22.784 1.00 98.49  ? 308 GLN B OE1 1 
ATOM   7556  N NE2 . GLN B 1 308 ? -25.161 35.553  -24.342 1.00 94.69  ? 308 GLN B NE2 1 
ATOM   7557  N N   . GLY B 1 309 ? -27.660 31.611  -20.631 1.00 103.02 ? 309 GLY B N   1 
ATOM   7558  C CA  . GLY B 1 309 ? -27.321 30.665  -19.566 1.00 103.15 ? 309 GLY B CA  1 
ATOM   7559  C C   . GLY B 1 309 ? -27.948 29.289  -19.711 1.00 103.83 ? 309 GLY B C   1 
ATOM   7560  O O   . GLY B 1 309 ? -27.330 28.280  -19.365 1.00 102.25 ? 309 GLY B O   1 
ATOM   7561  N N   . ASP B 1 310 ? -29.184 29.248  -20.203 1.00 107.67 ? 310 ASP B N   1 
ATOM   7562  C CA  . ASP B 1 310 ? -29.864 27.982  -20.477 1.00 112.56 ? 310 ASP B CA  1 
ATOM   7563  C C   . ASP B 1 310 ? -29.124 27.203  -21.569 1.00 115.47 ? 310 ASP B C   1 
ATOM   7564  O O   . ASP B 1 310 ? -28.848 27.748  -22.642 1.00 113.69 ? 310 ASP B O   1 
ATOM   7565  C CB  . ASP B 1 310 ? -31.323 28.229  -20.886 1.00 114.22 ? 310 ASP B CB  1 
ATOM   7566  C CG  . ASP B 1 310 ? -32.050 26.950  -21.283 1.00 116.85 ? 310 ASP B CG  1 
ATOM   7567  O OD1 . ASP B 1 310 ? -32.023 25.977  -20.499 1.00 116.56 ? 310 ASP B OD1 1 
ATOM   7568  O OD2 . ASP B 1 310 ? -32.660 26.924  -22.376 1.00 118.68 ? 310 ASP B OD2 1 
ATOM   7569  N N   . PRO B 1 311 ? -28.783 25.927  -21.288 1.00 119.00 ? 311 PRO B N   1 
ATOM   7570  C CA  . PRO B 1 311 ? -28.063 25.065  -22.234 1.00 119.02 ? 311 PRO B CA  1 
ATOM   7571  C C   . PRO B 1 311 ? -28.701 24.976  -23.627 1.00 118.86 ? 311 PRO B C   1 
ATOM   7572  O O   . PRO B 1 311 ? -28.025 24.593  -24.582 1.00 117.34 ? 311 PRO B O   1 
ATOM   7573  C CB  . PRO B 1 311 ? -28.094 23.700  -21.545 1.00 119.35 ? 311 PRO B CB  1 
ATOM   7574  C CG  . PRO B 1 311 ? -28.102 24.031  -20.093 1.00 119.12 ? 311 PRO B CG  1 
ATOM   7575  C CD  . PRO B 1 311 ? -28.917 25.290  -19.962 1.00 119.24 ? 311 PRO B CD  1 
ATOM   7576  N N   . LEU B 1 312 ? -29.980 25.334  -23.738 1.00 120.19 ? 312 LEU B N   1 
ATOM   7577  C CA  . LEU B 1 312 ? -30.692 25.268  -25.019 1.00 121.98 ? 312 LEU B CA  1 
ATOM   7578  C C   . LEU B 1 312 ? -30.916 26.634  -25.681 1.00 118.70 ? 312 LEU B C   1 
ATOM   7579  O O   . LEU B 1 312 ? -31.668 26.743  -26.652 1.00 118.80 ? 312 LEU B O   1 
ATOM   7580  C CB  . LEU B 1 312 ? -32.029 24.529  -24.862 1.00 127.18 ? 312 LEU B CB  1 
ATOM   7581  C CG  . LEU B 1 312 ? -32.009 22.994  -24.848 1.00 130.42 ? 312 LEU B CG  1 
ATOM   7582  C CD1 . LEU B 1 312 ? -33.413 22.451  -24.624 1.00 132.98 ? 312 LEU B CD1 1 
ATOM   7583  C CD2 . LEU B 1 312 ? -31.410 22.420  -26.127 1.00 127.50 ? 312 LEU B CD2 1 
ATOM   7584  N N   . SER B 1 313 ? -30.254 27.667  -25.166 1.00 112.34 ? 313 SER B N   1 
ATOM   7585  C CA  . SER B 1 313 ? -30.420 29.017  -25.699 1.00 107.06 ? 313 SER B CA  1 
ATOM   7586  C C   . SER B 1 313 ? -29.549 29.274  -26.926 1.00 104.26 ? 313 SER B C   1 
ATOM   7587  O O   . SER B 1 313 ? -30.001 29.891  -27.893 1.00 104.11 ? 313 SER B O   1 
ATOM   7588  C CB  . SER B 1 313 ? -30.142 30.062  -24.619 1.00 104.49 ? 313 SER B CB  1 
ATOM   7589  O OG  . SER B 1 313 ? -31.197 30.098  -23.677 1.00 104.55 ? 313 SER B OG  1 
ATOM   7590  N N   . GLY B 1 314 ? -28.307 28.796  -26.881 1.00 100.00 ? 314 GLY B N   1 
ATOM   7591  C CA  . GLY B 1 314 ? -27.346 29.021  -27.960 1.00 96.81  ? 314 GLY B CA  1 
ATOM   7592  C C   . GLY B 1 314 ? -27.839 28.536  -29.310 1.00 96.06  ? 314 GLY B C   1 
ATOM   7593  O O   . GLY B 1 314 ? -27.705 29.232  -30.317 1.00 94.25  ? 314 GLY B O   1 
ATOM   7594  N N   . CYS B 1 315 ? -28.427 27.343  -29.316 1.00 96.08  ? 315 CYS B N   1 
ATOM   7595  C CA  . CYS B 1 315 ? -28.906 26.705  -30.542 1.00 98.17  ? 315 CYS B CA  1 
ATOM   7596  C C   . CYS B 1 315 ? -30.181 27.354  -31.078 1.00 98.67  ? 315 CYS B C   1 
ATOM   7597  O O   . CYS B 1 315 ? -30.320 27.553  -32.288 1.00 99.12  ? 315 CYS B O   1 
ATOM   7598  C CB  . CYS B 1 315 ? -29.155 25.221  -30.293 1.00 100.21 ? 315 CYS B CB  1 
ATOM   7599  S SG  . CYS B 1 315 ? -30.374 24.912  -28.996 1.00 107.82 ? 315 CYS B SG  1 
ATOM   7600  N N   . LEU B 1 316 ? -31.110 27.667  -30.173 1.00 96.43  ? 316 LEU B N   1 
ATOM   7601  C CA  . LEU B 1 316 ? -32.390 28.273  -30.544 1.00 94.22  ? 316 LEU B CA  1 
ATOM   7602  C C   . LEU B 1 316 ? -32.222 29.687  -31.082 1.00 92.22  ? 316 LEU B C   1 
ATOM   7603  O O   . LEU B 1 316 ? -32.944 30.101  -31.988 1.00 92.91  ? 316 LEU B O   1 
ATOM   7604  C CB  . LEU B 1 316 ? -33.355 28.277  -29.356 1.00 93.47  ? 316 LEU B CB  1 
ATOM   7605  C CG  . LEU B 1 316 ? -34.049 26.960  -29.003 1.00 95.42  ? 316 LEU B CG  1 
ATOM   7606  C CD1 . LEU B 1 316 ? -34.868 27.124  -27.732 1.00 94.97  ? 316 LEU B CD1 1 
ATOM   7607  C CD2 . LEU B 1 316 ? -34.924 26.460  -30.144 1.00 95.20  ? 316 LEU B CD2 1 
ATOM   7608  N N   . CYS B 1 317 ? -31.266 30.420  -30.518 1.00 90.47  ? 317 CYS B N   1 
ATOM   7609  C CA  . CYS B 1 317 ? -30.919 31.749  -31.008 1.00 88.23  ? 317 CYS B CA  1 
ATOM   7610  C C   . CYS B 1 317 ? -30.378 31.674  -32.434 1.00 86.38  ? 317 CYS B C   1 
ATOM   7611  O O   . CYS B 1 317 ? -30.686 32.527  -33.266 1.00 85.45  ? 317 CYS B O   1 
ATOM   7612  C CB  . CYS B 1 317 ? -29.897 32.414  -30.087 1.00 85.28  ? 317 CYS B CB  1 
ATOM   7613  S SG  . CYS B 1 317 ? -29.838 34.214  -30.232 1.00 83.71  ? 317 CYS B SG  1 
ATOM   7614  N N   . GLU B 1 318 ? -29.583 30.644  -32.711 1.00 86.25  ? 318 GLU B N   1 
ATOM   7615  C CA  . GLU B 1 318 ? -29.084 30.404  -34.062 1.00 89.34  ? 318 GLU B CA  1 
ATOM   7616  C C   . GLU B 1 318 ? -30.229 30.050  -35.004 1.00 90.65  ? 318 GLU B C   1 
ATOM   7617  O O   . GLU B 1 318 ? -30.306 30.568  -36.113 1.00 92.49  ? 318 GLU B O   1 
ATOM   7618  C CB  . GLU B 1 318 ? -28.024 29.301  -34.064 1.00 92.71  ? 318 GLU B CB  1 
ATOM   7619  C CG  . GLU B 1 318 ? -26.729 29.695  -33.365 1.00 98.04  ? 318 GLU B CG  1 
ATOM   7620  C CD  . GLU B 1 318 ? -25.706 28.574  -33.339 1.00 100.89 ? 318 GLU B CD  1 
ATOM   7621  O OE1 . GLU B 1 318 ? -25.357 28.115  -32.227 1.00 97.76  ? 318 GLU B OE1 1 
ATOM   7622  O OE2 . GLU B 1 318 ? -25.253 28.152  -34.430 1.00 102.89 ? 318 GLU B OE2 1 
ATOM   7623  N N   . LEU B 1 319 ? -31.119 29.175  -34.538 1.00 89.87  ? 319 LEU B N   1 
ATOM   7624  C CA  . LEU B 1 319 ? -32.301 28.757  -35.289 1.00 89.96  ? 319 LEU B CA  1 
ATOM   7625  C C   . LEU B 1 319 ? -33.195 29.949  -35.635 1.00 87.44  ? 319 LEU B C   1 
ATOM   7626  O O   . LEU B 1 319 ? -33.631 30.098  -36.777 1.00 85.94  ? 319 LEU B O   1 
ATOM   7627  C CB  . LEU B 1 319 ? -33.089 27.716  -34.479 1.00 94.63  ? 319 LEU B CB  1 
ATOM   7628  C CG  . LEU B 1 319 ? -34.094 26.757  -35.147 1.00 98.29  ? 319 LEU B CG  1 
ATOM   7629  C CD1 . LEU B 1 319 ? -35.400 27.449  -35.516 1.00 100.22 ? 319 LEU B CD1 1 
ATOM   7630  C CD2 . LEU B 1 319 ? -33.497 26.028  -36.349 1.00 97.38  ? 319 LEU B CD2 1 
ATOM   7631  N N   . TYR B 1 320 ? -33.461 30.789  -34.638 1.00 84.66  ? 320 TYR B N   1 
ATOM   7632  C CA  . TYR B 1 320 ? -34.223 32.018  -34.830 1.00 83.97  ? 320 TYR B CA  1 
ATOM   7633  C C   . TYR B 1 320 ? -33.505 32.927  -35.820 1.00 85.50  ? 320 TYR B C   1 
ATOM   7634  O O   . TYR B 1 320 ? -34.129 33.498  -36.726 1.00 83.55  ? 320 TYR B O   1 
ATOM   7635  C CB  . TYR B 1 320 ? -34.391 32.726  -33.489 1.00 81.95  ? 320 TYR B CB  1 
ATOM   7636  C CG  . TYR B 1 320 ? -35.227 33.992  -33.504 1.00 83.05  ? 320 TYR B CG  1 
ATOM   7637  C CD1 . TYR B 1 320 ? -36.595 33.953  -33.221 1.00 85.21  ? 320 TYR B CD1 1 
ATOM   7638  C CD2 . TYR B 1 320 ? -34.641 35.235  -33.731 1.00 81.68  ? 320 TYR B CD2 1 
ATOM   7639  C CE1 . TYR B 1 320 ? -37.357 35.113  -33.202 1.00 85.38  ? 320 TYR B CE1 1 
ATOM   7640  C CE2 . TYR B 1 320 ? -35.396 36.398  -33.717 1.00 82.38  ? 320 TYR B CE2 1 
ATOM   7641  C CZ  . TYR B 1 320 ? -36.751 36.333  -33.453 1.00 83.94  ? 320 TYR B CZ  1 
ATOM   7642  O OH  . TYR B 1 320 ? -37.496 37.489  -33.435 1.00 84.48  ? 320 TYR B OH  1 
ATOM   7643  N N   . MET B 1 321 ? -32.187 33.040  -35.649 1.00 84.71  ? 321 MET B N   1 
ATOM   7644  C CA  . MET B 1 321 ? -31.365 33.926  -36.471 1.00 85.83  ? 321 MET B CA  1 
ATOM   7645  C C   . MET B 1 321 ? -31.281 33.448  -37.917 1.00 85.45  ? 321 MET B C   1 
ATOM   7646  O O   . MET B 1 321 ? -31.457 34.238  -38.845 1.00 84.20  ? 321 MET B O   1 
ATOM   7647  C CB  . MET B 1 321 ? -29.962 34.049  -35.884 1.00 85.81  ? 321 MET B CB  1 
ATOM   7648  C CG  . MET B 1 321 ? -29.546 35.478  -35.597 1.00 86.74  ? 321 MET B CG  1 
ATOM   7649  S SD  . MET B 1 321 ? -30.195 36.048  -34.020 1.00 89.58  ? 321 MET B SD  1 
ATOM   7650  C CE  . MET B 1 321 ? -29.592 37.731  -34.013 1.00 91.15  ? 321 MET B CE  1 
ATOM   7651  N N   . ALA B 1 322 ? -31.011 32.153  -38.096 1.00 86.43  ? 322 ALA B N   1 
ATOM   7652  C CA  . ALA B 1 322 ? -30.993 31.526  -39.421 1.00 87.91  ? 322 ALA B CA  1 
ATOM   7653  C C   . ALA B 1 322 ? -32.346 31.644  -40.103 1.00 91.55  ? 322 ALA B C   1 
ATOM   7654  O O   . ALA B 1 322 ? -32.424 31.636  -41.328 1.00 96.14  ? 322 ALA B O   1 
ATOM   7655  C CB  . ALA B 1 322 ? -30.580 30.065  -39.319 1.00 87.40  ? 322 ALA B CB  1 
ATOM   7656  N N   . PHE B 1 323 ? -33.408 31.746  -39.302 1.00 93.44  ? 323 PHE B N   1 
ATOM   7657  C CA  . PHE B 1 323 ? -34.749 31.985  -39.824 1.00 94.98  ? 323 PHE B CA  1 
ATOM   7658  C C   . PHE B 1 323 ? -34.934 33.425  -40.293 1.00 94.89  ? 323 PHE B C   1 
ATOM   7659  O O   . PHE B 1 323 ? -35.503 33.664  -41.358 1.00 99.27  ? 323 PHE B O   1 
ATOM   7660  C CB  . PHE B 1 323 ? -35.816 31.626  -38.787 1.00 96.91  ? 323 PHE B CB  1 
ATOM   7661  C CG  . PHE B 1 323 ? -37.187 32.151  -39.120 1.00 98.93  ? 323 PHE B CG  1 
ATOM   7662  C CD1 . PHE B 1 323 ? -37.950 31.561  -40.122 1.00 99.34  ? 323 PHE B CD1 1 
ATOM   7663  C CD2 . PHE B 1 323 ? -37.716 33.240  -38.431 1.00 99.52  ? 323 PHE B CD2 1 
ATOM   7664  C CE1 . PHE B 1 323 ? -39.210 32.046  -40.432 1.00 101.55 ? 323 PHE B CE1 1 
ATOM   7665  C CE2 . PHE B 1 323 ? -38.977 33.728  -38.736 1.00 101.85 ? 323 PHE B CE2 1 
ATOM   7666  C CZ  . PHE B 1 323 ? -39.725 33.130  -39.737 1.00 102.64 ? 323 PHE B CZ  1 
ATOM   7667  N N   . MET B 1 324 ? -34.470 34.381  -39.493 1.00 92.29  ? 324 MET B N   1 
ATOM   7668  C CA  . MET B 1 324 ? -34.572 35.789  -39.866 1.00 94.30  ? 324 MET B CA  1 
ATOM   7669  C C   . MET B 1 324 ? -33.472 36.221  -40.844 1.00 93.69  ? 324 MET B C   1 
ATOM   7670  O O   . MET B 1 324 ? -33.465 37.360  -41.315 1.00 94.36  ? 324 MET B O   1 
ATOM   7671  C CB  . MET B 1 324 ? -34.606 36.691  -38.628 1.00 94.73  ? 324 MET B CB  1 
ATOM   7672  C CG  . MET B 1 324 ? -35.970 36.748  -37.957 1.00 98.53  ? 324 MET B CG  1 
ATOM   7673  S SD  . MET B 1 324 ? -36.286 38.331  -37.157 1.00 102.20 ? 324 MET B SD  1 
ATOM   7674  C CE  . MET B 1 324 ? -37.969 38.112  -36.572 1.00 101.26 ? 324 MET B CE  1 
ATOM   7675  N N   . ASP B 1 325 ? -32.561 35.302  -41.160 1.00 94.07  ? 325 ASP B N   1 
ATOM   7676  C CA  . ASP B 1 325 ? -31.541 35.539  -42.185 1.00 93.55  ? 325 ASP B CA  1 
ATOM   7677  C C   . ASP B 1 325 ? -32.028 35.067  -43.552 1.00 94.15  ? 325 ASP B C   1 
ATOM   7678  O O   . ASP B 1 325 ? -31.832 35.749  -44.561 1.00 93.99  ? 325 ASP B O   1 
ATOM   7679  C CB  . ASP B 1 325 ? -30.231 34.838  -41.822 1.00 94.20  ? 325 ASP B CB  1 
ATOM   7680  C CG  . ASP B 1 325 ? -29.043 35.394  -42.583 1.00 95.26  ? 325 ASP B CG  1 
ATOM   7681  O OD1 . ASP B 1 325 ? -28.568 36.492  -42.228 1.00 96.83  ? 325 ASP B OD1 1 
ATOM   7682  O OD2 . ASP B 1 325 ? -28.572 34.728  -43.526 1.00 95.53  ? 325 ASP B OD2 1 
ATOM   7683  N N   . ARG B 1 326 ? -32.656 33.891  -43.575 1.00 94.31  ? 326 ARG B N   1 
ATOM   7684  C CA  . ARG B 1 326 ? -33.325 33.374  -44.773 1.00 96.78  ? 326 ARG B CA  1 
ATOM   7685  C C   . ARG B 1 326 ? -34.443 34.328  -45.204 1.00 95.69  ? 326 ARG B C   1 
ATOM   7686  O O   . ARG B 1 326 ? -34.697 34.511  -46.393 1.00 94.25  ? 326 ARG B O   1 
ATOM   7687  C CB  . ARG B 1 326 ? -33.895 31.973  -44.495 1.00 99.76  ? 326 ARG B CB  1 
ATOM   7688  C CG  . ARG B 1 326 ? -34.605 31.311  -45.671 1.00 102.53 ? 326 ARG B CG  1 
ATOM   7689  C CD  . ARG B 1 326 ? -35.665 30.324  -45.192 1.00 105.22 ? 326 ARG B CD  1 
ATOM   7690  N NE  . ARG B 1 326 ? -36.858 30.992  -44.652 1.00 107.09 ? 326 ARG B NE  1 
ATOM   7691  C CZ  . ARG B 1 326 ? -38.083 30.904  -45.175 1.00 109.80 ? 326 ARG B CZ  1 
ATOM   7692  N NH1 . ARG B 1 326 ? -38.307 30.163  -46.256 1.00 108.61 ? 326 ARG B NH1 1 
ATOM   7693  N NH2 . ARG B 1 326 ? -39.094 31.551  -44.606 1.00 111.45 ? 326 ARG B NH2 1 
ATOM   7694  N N   . LEU B 1 327 ? -35.088 34.946  -44.217 1.00 93.87  ? 327 LEU B N   1 
ATOM   7695  C CA  . LEU B 1 327 ? -36.209 35.841  -44.457 1.00 93.25  ? 327 LEU B CA  1 
ATOM   7696  C C   . LEU B 1 327 ? -35.778 37.200  -45.010 1.00 91.19  ? 327 LEU B C   1 
ATOM   7697  O O   . LEU B 1 327 ? -36.339 37.667  -45.994 1.00 91.26  ? 327 LEU B O   1 
ATOM   7698  C CB  . LEU B 1 327 ? -37.024 36.024  -43.170 1.00 94.83  ? 327 LEU B CB  1 
ATOM   7699  C CG  . LEU B 1 327 ? -38.504 36.413  -43.288 1.00 97.61  ? 327 LEU B CG  1 
ATOM   7700  C CD1 . LEU B 1 327 ? -39.291 35.381  -44.089 1.00 98.64  ? 327 LEU B CD1 1 
ATOM   7701  C CD2 . LEU B 1 327 ? -39.113 36.604  -41.905 1.00 96.32  ? 327 LEU B CD2 1 
ATOM   7702  N N   . TYR B 1 328 ? -34.777 37.822  -44.383 1.00 89.21  ? 328 TYR B N   1 
ATOM   7703  C CA  . TYR B 1 328 ? -34.428 39.221  -44.676 1.00 86.61  ? 328 TYR B CA  1 
ATOM   7704  C C   . TYR B 1 328 ? -33.140 39.389  -45.481 1.00 84.52  ? 328 TYR B C   1 
ATOM   7705  O O   . TYR B 1 328 ? -32.991 40.356  -46.234 1.00 84.94  ? 328 TYR B O   1 
ATOM   7706  C CB  . TYR B 1 328 ? -34.323 40.037  -43.381 1.00 86.14  ? 328 TYR B CB  1 
ATOM   7707  C CG  . TYR B 1 328 ? -35.618 40.194  -42.615 1.00 86.66  ? 328 TYR B CG  1 
ATOM   7708  C CD1 . TYR B 1 328 ? -36.663 40.969  -43.119 1.00 88.47  ? 328 TYR B CD1 1 
ATOM   7709  C CD2 . TYR B 1 328 ? -35.790 39.587  -41.368 1.00 86.15  ? 328 TYR B CD2 1 
ATOM   7710  C CE1 . TYR B 1 328 ? -37.850 41.121  -42.411 1.00 89.55  ? 328 TYR B CE1 1 
ATOM   7711  C CE2 . TYR B 1 328 ? -36.973 39.736  -40.650 1.00 87.44  ? 328 TYR B CE2 1 
ATOM   7712  C CZ  . TYR B 1 328 ? -37.998 40.503  -41.177 1.00 90.10  ? 328 TYR B CZ  1 
ATOM   7713  O OH  . TYR B 1 328 ? -39.173 40.654  -40.473 1.00 93.26  ? 328 TYR B OH  1 
ATOM   7714  N N   . PHE B 1 329 ? -32.210 38.455  -45.320 1.00 80.88  ? 329 PHE B N   1 
ATOM   7715  C CA  . PHE B 1 329 ? -30.858 38.654  -45.832 1.00 79.92  ? 329 PHE B CA  1 
ATOM   7716  C C   . PHE B 1 329 ? -30.424 37.606  -46.863 1.00 79.66  ? 329 PHE B C   1 
ATOM   7717  O O   . PHE B 1 329 ? -29.328 37.692  -47.415 1.00 79.28  ? 329 PHE B O   1 
ATOM   7718  C CB  . PHE B 1 329 ? -29.852 38.745  -44.662 1.00 75.18  ? 329 PHE B CB  1 
ATOM   7719  C CG  . PHE B 1 329 ? -30.283 39.688  -43.562 1.00 73.57  ? 329 PHE B CG  1 
ATOM   7720  C CD1 . PHE B 1 329 ? -30.192 41.069  -43.730 1.00 72.64  ? 329 PHE B CD1 1 
ATOM   7721  C CD2 . PHE B 1 329 ? -30.790 39.196  -42.362 1.00 72.77  ? 329 PHE B CD2 1 
ATOM   7722  C CE1 . PHE B 1 329 ? -30.599 41.936  -42.725 1.00 72.07  ? 329 PHE B CE1 1 
ATOM   7723  C CE2 . PHE B 1 329 ? -31.195 40.060  -41.354 1.00 71.40  ? 329 PHE B CE2 1 
ATOM   7724  C CZ  . PHE B 1 329 ? -31.101 41.431  -41.537 1.00 70.56  ? 329 PHE B CZ  1 
ATOM   7725  N N   . SER B 1 330 ? -31.296 36.637  -47.128 1.00 82.22  ? 330 SER B N   1 
ATOM   7726  C CA  . SER B 1 330 ? -30.997 35.533  -48.050 1.00 85.13  ? 330 SER B CA  1 
ATOM   7727  C C   . SER B 1 330 ? -30.707 35.998  -49.495 1.00 85.63  ? 330 SER B C   1 
ATOM   7728  O O   . SER B 1 330 ? -29.628 35.723  -50.047 1.00 83.67  ? 330 SER B O   1 
ATOM   7729  C CB  . SER B 1 330 ? -32.142 34.501  -48.019 1.00 89.79  ? 330 SER B CB  1 
ATOM   7730  O OG  . SER B 1 330 ? -32.290 33.808  -49.252 1.00 93.00  ? 330 SER B OG  1 
ATOM   7731  N N   . ASN B 1 331 ? -31.660 36.721  -50.083 1.00 85.84  ? 331 ASN B N   1 
ATOM   7732  C CA  . ASN B 1 331 ? -31.625 37.048  -51.509 1.00 86.06  ? 331 ASN B CA  1 
ATOM   7733  C C   . ASN B 1 331 ? -31.128 38.474  -51.793 1.00 86.15  ? 331 ASN B C   1 
ATOM   7734  O O   . ASN B 1 331 ? -31.676 39.170  -52.651 1.00 87.69  ? 331 ASN B O   1 
ATOM   7735  C CB  . ASN B 1 331 ? -33.012 36.846  -52.129 1.00 88.03  ? 331 ASN B CB  1 
ATOM   7736  C CG  . ASN B 1 331 ? -33.791 35.718  -51.478 1.00 88.52  ? 331 ASN B CG  1 
ATOM   7737  O OD1 . ASN B 1 331 ? -34.696 35.958  -50.681 1.00 88.17  ? 331 ASN B OD1 1 
ATOM   7738  N ND2 . ASN B 1 331 ? -33.442 34.482  -51.816 1.00 89.57  ? 331 ASN B ND2 1 
ATOM   7739  N N   . LEU B 1 332 ? -30.070 38.887  -51.098 1.00 84.83  ? 332 LEU B N   1 
ATOM   7740  C CA  . LEU B 1 332 ? -29.676 40.303  -51.055 1.00 81.76  ? 332 LEU B CA  1 
ATOM   7741  C C   . LEU B 1 332 ? -28.903 40.832  -52.266 1.00 78.68  ? 332 LEU B C   1 
ATOM   7742  O O   . LEU B 1 332 ? -28.826 42.051  -52.469 1.00 77.74  ? 332 LEU B O   1 
ATOM   7743  C CB  . LEU B 1 332 ? -28.911 40.617  -49.763 1.00 79.58  ? 332 LEU B CB  1 
ATOM   7744  C CG  . LEU B 1 332 ? -29.701 41.407  -48.721 1.00 79.34  ? 332 LEU B CG  1 
ATOM   7745  C CD1 . LEU B 1 332 ? -28.835 41.651  -47.502 1.00 78.19  ? 332 LEU B CD1 1 
ATOM   7746  C CD2 . LEU B 1 332 ? -30.192 42.728  -49.296 1.00 79.17  ? 332 LEU B CD2 1 
ATOM   7747  N N   . ASP B 1 333 ? -28.344 39.921  -53.058 1.00 75.19  ? 333 ASP B N   1 
ATOM   7748  C CA  . ASP B 1 333 ? -27.458 40.271  -54.170 1.00 76.52  ? 333 ASP B CA  1 
ATOM   7749  C C   . ASP B 1 333 ? -26.370 39.216  -54.236 1.00 78.25  ? 333 ASP B C   1 
ATOM   7750  O O   . ASP B 1 333 ? -25.384 39.283  -53.497 1.00 79.33  ? 333 ASP B O   1 
ATOM   7751  C CB  . ASP B 1 333 ? -26.841 41.675  -53.981 1.00 72.54  ? 333 ASP B CB  1 
ATOM   7752  C CG  . ASP B 1 333 ? -25.997 42.128  -55.177 1.00 71.81  ? 333 ASP B CG  1 
ATOM   7753  O OD1 . ASP B 1 333 ? -25.462 41.276  -55.916 1.00 70.87  ? 333 ASP B OD1 1 
ATOM   7754  O OD2 . ASP B 1 333 ? -25.849 43.351  -55.369 1.00 71.70  ? 333 ASP B OD2 1 
ATOM   7755  N N   . LYS B 1 334 ? -26.561 38.230  -55.109 1.00 81.93  ? 334 LYS B N   1 
ATOM   7756  C CA  . LYS B 1 334 ? -25.597 37.139  -55.276 1.00 84.32  ? 334 LYS B CA  1 
ATOM   7757  C C   . LYS B 1 334 ? -24.141 37.631  -55.232 1.00 83.51  ? 334 LYS B C   1 
ATOM   7758  O O   . LYS B 1 334 ? -23.254 36.926  -54.740 1.00 82.65  ? 334 LYS B O   1 
ATOM   7759  C CB  . LYS B 1 334 ? -25.860 36.391  -56.590 1.00 87.10  ? 334 LYS B CB  1 
ATOM   7760  C CG  . LYS B 1 334 ? -26.953 35.339  -56.507 1.00 89.52  ? 334 LYS B CG  1 
ATOM   7761  C CD  . LYS B 1 334 ? -27.419 34.934  -57.899 1.00 95.08  ? 334 LYS B CD  1 
ATOM   7762  C CE  . LYS B 1 334 ? -28.256 33.664  -57.866 1.00 97.36  ? 334 LYS B CE  1 
ATOM   7763  N NZ  . LYS B 1 334 ? -27.409 32.438  -57.826 1.00 96.80  ? 334 LYS B NZ  1 
ATOM   7764  N N   . ASP B 1 335 ? -23.922 38.854  -55.719 1.00 82.93  ? 335 ASP B N   1 
ATOM   7765  C CA  . ASP B 1 335 ? -22.584 39.396  -55.938 1.00 80.81  ? 335 ASP B CA  1 
ATOM   7766  C C   . ASP B 1 335 ? -22.092 40.330  -54.827 1.00 77.10  ? 335 ASP B C   1 
ATOM   7767  O O   . ASP B 1 335 ? -21.016 40.929  -54.944 1.00 76.22  ? 335 ASP B O   1 
ATOM   7768  C CB  . ASP B 1 335 ? -22.526 40.118  -57.286 1.00 85.57  ? 335 ASP B CB  1 
ATOM   7769  C CG  . ASP B 1 335 ? -22.711 39.179  -58.462 1.00 90.04  ? 335 ASP B CG  1 
ATOM   7770  O OD1 . ASP B 1 335 ? -23.377 38.129  -58.300 1.00 92.09  ? 335 ASP B OD1 1 
ATOM   7771  O OD2 . ASP B 1 335 ? -22.197 39.499  -59.556 1.00 92.45  ? 335 ASP B OD2 1 
ATOM   7772  N N   . ALA B 1 336 ? -22.874 40.459  -53.760 1.00 72.56  ? 336 ALA B N   1 
ATOM   7773  C CA  . ALA B 1 336 ? -22.417 41.167  -52.569 1.00 68.81  ? 336 ALA B CA  1 
ATOM   7774  C C   . ALA B 1 336 ? -21.819 40.193  -51.559 1.00 66.38  ? 336 ALA B C   1 
ATOM   7775  O O   . ALA B 1 336 ? -22.101 38.990  -51.596 1.00 66.03  ? 336 ALA B O   1 
ATOM   7776  C CB  . ALA B 1 336 ? -23.558 41.953  -51.940 1.00 66.58  ? 336 ALA B CB  1 
ATOM   7777  N N   . PHE B 1 337 ? -20.985 40.721  -50.664 1.00 64.62  ? 337 PHE B N   1 
ATOM   7778  C CA  . PHE B 1 337 ? -20.441 39.947  -49.550 1.00 61.26  ? 337 PHE B CA  1 
ATOM   7779  C C   . PHE B 1 337 ? -21.304 40.131  -48.309 1.00 59.78  ? 337 PHE B C   1 
ATOM   7780  O O   . PHE B 1 337 ? -21.627 41.254  -47.929 1.00 60.36  ? 337 PHE B O   1 
ATOM   7781  C CB  . PHE B 1 337 ? -18.989 40.363  -49.252 1.00 60.76  ? 337 PHE B CB  1 
ATOM   7782  C CG  . PHE B 1 337 ? -18.450 39.809  -47.956 1.00 58.16  ? 337 PHE B CG  1 
ATOM   7783  C CD1 . PHE B 1 337 ? -18.700 40.454  -46.750 1.00 57.22  ? 337 PHE B CD1 1 
ATOM   7784  C CD2 . PHE B 1 337 ? -17.702 38.638  -47.942 1.00 57.51  ? 337 PHE B CD2 1 
ATOM   7785  C CE1 . PHE B 1 337 ? -18.220 39.938  -45.558 1.00 56.73  ? 337 PHE B CE1 1 
ATOM   7786  C CE2 . PHE B 1 337 ? -17.212 38.124  -46.749 1.00 56.82  ? 337 PHE B CE2 1 
ATOM   7787  C CZ  . PHE B 1 337 ? -17.470 38.775  -45.556 1.00 55.82  ? 337 PHE B CZ  1 
ATOM   7788  N N   . ILE B 1 338 ? -21.655 39.021  -47.670 1.00 58.35  ? 338 ILE B N   1 
ATOM   7789  C CA  . ILE B 1 338 ? -22.427 39.050  -46.432 1.00 57.25  ? 338 ILE B CA  1 
ATOM   7790  C C   . ILE B 1 338 ? -21.963 37.912  -45.543 1.00 56.22  ? 338 ILE B C   1 
ATOM   7791  O O   . ILE B 1 338 ? -21.727 36.808  -46.009 1.00 56.86  ? 338 ILE B O   1 
ATOM   7792  C CB  . ILE B 1 338 ? -23.947 38.913  -46.705 1.00 58.94  ? 338 ILE B CB  1 
ATOM   7793  C CG1 . ILE B 1 338 ? -24.767 39.104  -45.415 1.00 60.21  ? 338 ILE B CG1 1 
ATOM   7794  C CG2 . ILE B 1 338 ? -24.263 37.580  -47.374 1.00 58.39  ? 338 ILE B CG2 1 
ATOM   7795  C CD1 . ILE B 1 338 ? -26.237 39.416  -45.664 1.00 62.64  ? 338 ILE B CD1 1 
ATOM   7796  N N   . HIS B 1 339 ? -21.836 38.180  -44.259 1.00 56.88  ? 339 HIS B N   1 
ATOM   7797  C CA  . HIS B 1 339 ? -21.493 37.137  -43.321 1.00 58.46  ? 339 HIS B CA  1 
ATOM   7798  C C   . HIS B 1 339 ? -21.999 37.525  -41.987 1.00 60.13  ? 339 HIS B C   1 
ATOM   7799  O O   . HIS B 1 339 ? -22.025 38.715  -41.648 1.00 59.80  ? 339 HIS B O   1 
ATOM   7800  C CB  . HIS B 1 339 ? -19.974 36.912  -43.278 1.00 57.30  ? 339 HIS B CB  1 
ATOM   7801  C CG  . HIS B 1 339 ? -19.574 35.623  -42.605 1.00 55.76  ? 339 HIS B CG  1 
ATOM   7802  N ND1 . HIS B 1 339 ? -19.438 35.514  -41.263 1.00 54.96  ? 339 HIS B ND1 1 
ATOM   7803  C CD2 . HIS B 1 339 ? -19.310 34.359  -43.133 1.00 54.93  ? 339 HIS B CD2 1 
ATOM   7804  C CE1 . HIS B 1 339 ? -19.103 34.249  -40.951 1.00 54.59  ? 339 HIS B CE1 1 
ATOM   7805  N NE2 . HIS B 1 339 ? -19.024 33.543  -42.096 1.00 54.75  ? 339 HIS B NE2 1 
ATOM   7806  N N   . ARG B 1 340 ? -22.386 36.519  -41.203 1.00 64.45  ? 340 ARG B N   1 
ATOM   7807  C CA  . ARG B 1 340 ? -23.073 36.739  -39.937 1.00 67.17  ? 340 ARG B CA  1 
ATOM   7808  C C   . ARG B 1 340 ? -22.534 35.886  -38.783 1.00 67.90  ? 340 ARG B C   1 
ATOM   7809  O O   . ARG B 1 340 ? -22.007 34.780  -38.982 1.00 64.08  ? 340 ARG B O   1 
ATOM   7810  C CB  . ARG B 1 340 ? -24.572 36.467  -40.105 1.00 73.02  ? 340 ARG B CB  1 
ATOM   7811  C CG  . ARG B 1 340 ? -24.920 34.998  -40.298 1.00 77.76  ? 340 ARG B CG  1 
ATOM   7812  C CD  . ARG B 1 340 ? -26.397 34.808  -40.588 1.00 86.47  ? 340 ARG B CD  1 
ATOM   7813  N NE  . ARG B 1 340 ? -26.912 33.570  -40.000 1.00 90.70  ? 340 ARG B NE  1 
ATOM   7814  C CZ  . ARG B 1 340 ? -27.240 33.426  -38.716 1.00 91.32  ? 340 ARG B CZ  1 
ATOM   7815  N NH1 . ARG B 1 340 ? -27.110 34.443  -37.867 1.00 90.69  ? 340 ARG B NH1 1 
ATOM   7816  N NH2 . ARG B 1 340 ? -27.696 32.259  -38.277 1.00 91.57  ? 340 ARG B NH2 1 
ATOM   7817  N N   . THR B 1 341 ? -22.669 36.425  -37.577 1.00 68.35  ? 341 THR B N   1 
ATOM   7818  C CA  . THR B 1 341 ? -22.715 35.617  -36.370 1.00 72.39  ? 341 THR B CA  1 
ATOM   7819  C C   . THR B 1 341 ? -24.037 35.949  -35.676 1.00 78.10  ? 341 THR B C   1 
ATOM   7820  O O   . THR B 1 341 ? -24.910 36.597  -36.270 1.00 78.20  ? 341 THR B O   1 
ATOM   7821  C CB  . THR B 1 341 ? -21.514 35.894  -35.423 1.00 68.52  ? 341 THR B CB  1 
ATOM   7822  O OG1 . THR B 1 341 ? -21.490 37.277  -35.053 1.00 66.36  ? 341 THR B OG1 1 
ATOM   7823  C CG2 . THR B 1 341 ? -20.188 35.529  -36.095 1.00 66.26  ? 341 THR B CG2 1 
ATOM   7824  N N   . VAL B 1 342 ? -24.190 35.512  -34.430 1.00 83.37  ? 342 VAL B N   1 
ATOM   7825  C CA  . VAL B 1 342 ? -25.348 35.917  -33.635 1.00 89.21  ? 342 VAL B CA  1 
ATOM   7826  C C   . VAL B 1 342 ? -25.311 37.425  -33.366 1.00 89.86  ? 342 VAL B C   1 
ATOM   7827  O O   . VAL B 1 342 ? -26.347 38.097  -33.383 1.00 92.24  ? 342 VAL B O   1 
ATOM   7828  C CB  . VAL B 1 342 ? -25.466 35.129  -32.300 1.00 91.48  ? 342 VAL B CB  1 
ATOM   7829  C CG1 . VAL B 1 342 ? -26.067 33.748  -32.540 1.00 93.78  ? 342 VAL B CG1 1 
ATOM   7830  C CG2 . VAL B 1 342 ? -24.120 35.022  -31.594 1.00 90.04  ? 342 VAL B CG2 1 
ATOM   7831  N N   . ASP B 1 343 ? -24.104 37.950  -33.174 1.00 86.29  ? 343 ASP B N   1 
ATOM   7832  C CA  . ASP B 1 343 ? -23.914 39.313  -32.693 1.00 84.75  ? 343 ASP B CA  1 
ATOM   7833  C C   . ASP B 1 343 ? -23.551 40.296  -33.810 1.00 82.56  ? 343 ASP B C   1 
ATOM   7834  O O   . ASP B 1 343 ? -23.850 41.488  -33.710 1.00 81.58  ? 343 ASP B O   1 
ATOM   7835  C CB  . ASP B 1 343 ? -22.838 39.340  -31.597 1.00 85.50  ? 343 ASP B CB  1 
ATOM   7836  C CG  . ASP B 1 343 ? -22.977 38.183  -30.600 1.00 86.63  ? 343 ASP B CG  1 
ATOM   7837  O OD1 . ASP B 1 343 ? -24.069 38.018  -30.007 1.00 91.03  ? 343 ASP B OD1 1 
ATOM   7838  O OD2 . ASP B 1 343 ? -21.991 37.442  -30.407 1.00 82.96  ? 343 ASP B OD2 1 
ATOM   7839  N N   . ASP B 1 344 ? -22.907 39.792  -34.865 1.00 79.99  ? 344 ASP B N   1 
ATOM   7840  C CA  . ASP B 1 344 ? -22.336 40.649  -35.913 1.00 74.30  ? 344 ASP B CA  1 
ATOM   7841  C C   . ASP B 1 344 ? -22.921 40.363  -37.282 1.00 70.36  ? 344 ASP B C   1 
ATOM   7842  O O   . ASP B 1 344 ? -23.109 39.206  -37.663 1.00 69.51  ? 344 ASP B O   1 
ATOM   7843  C CB  . ASP B 1 344 ? -20.817 40.469  -36.020 1.00 74.39  ? 344 ASP B CB  1 
ATOM   7844  C CG  . ASP B 1 344 ? -20.146 40.267  -34.691 1.00 76.56  ? 344 ASP B CG  1 
ATOM   7845  O OD1 . ASP B 1 344 ? -20.168 41.205  -33.863 1.00 79.47  ? 344 ASP B OD1 1 
ATOM   7846  O OD2 . ASP B 1 344 ? -19.561 39.175  -34.492 1.00 77.14  ? 344 ASP B OD2 1 
ATOM   7847  N N   . TYR B 1 345 ? -23.163 41.428  -38.035 1.00 67.01  ? 345 TYR B N   1 
ATOM   7848  C CA  . TYR B 1 345 ? -23.364 41.321  -39.467 1.00 65.50  ? 345 TYR B CA  1 
ATOM   7849  C C   . TYR B 1 345 ? -22.305 42.130  -40.200 1.00 60.98  ? 345 TYR B C   1 
ATOM   7850  O O   . TYR B 1 345 ? -21.967 43.246  -39.801 1.00 60.52  ? 345 TYR B O   1 
ATOM   7851  C CB  . TYR B 1 345 ? -24.768 41.790  -39.866 1.00 70.18  ? 345 TYR B CB  1 
ATOM   7852  C CG  . TYR B 1 345 ? -25.790 40.675  -39.930 1.00 74.05  ? 345 TYR B CG  1 
ATOM   7853  C CD1 . TYR B 1 345 ? -25.826 39.797  -41.011 1.00 76.39  ? 345 TYR B CD1 1 
ATOM   7854  C CD2 . TYR B 1 345 ? -26.725 40.505  -38.917 1.00 75.88  ? 345 TYR B CD2 1 
ATOM   7855  C CE1 . TYR B 1 345 ? -26.764 38.777  -41.074 1.00 78.82  ? 345 TYR B CE1 1 
ATOM   7856  C CE2 . TYR B 1 345 ? -27.662 39.485  -38.969 1.00 78.25  ? 345 TYR B CE2 1 
ATOM   7857  C CZ  . TYR B 1 345 ? -27.675 38.623  -40.047 1.00 78.91  ? 345 TYR B CZ  1 
ATOM   7858  O OH  . TYR B 1 345 ? -28.608 37.613  -40.099 1.00 83.02  ? 345 TYR B OH  1 
ATOM   7859  N N   . PHE B 1 346 ? -21.787 41.557  -41.276 1.00 56.83  ? 346 PHE B N   1 
ATOM   7860  C CA  . PHE B 1 346 ? -20.757 42.194  -42.064 1.00 54.55  ? 346 PHE B CA  1 
ATOM   7861  C C   . PHE B 1 346 ? -21.164 42.096  -43.523 1.00 54.64  ? 346 PHE B C   1 
ATOM   7862  O O   . PHE B 1 346 ? -21.428 41.009  -44.030 1.00 56.95  ? 346 PHE B O   1 
ATOM   7863  C CB  . PHE B 1 346 ? -19.411 41.498  -41.803 1.00 52.70  ? 346 PHE B CB  1 
ATOM   7864  C CG  . PHE B 1 346 ? -18.226 42.143  -42.488 1.00 50.71  ? 346 PHE B CG  1 
ATOM   7865  C CD1 . PHE B 1 346 ? -18.129 43.524  -42.615 1.00 50.17  ? 346 PHE B CD1 1 
ATOM   7866  C CD2 . PHE B 1 346 ? -17.174 41.358  -42.942 1.00 49.36  ? 346 PHE B CD2 1 
ATOM   7867  C CE1 . PHE B 1 346 ? -17.037 44.101  -43.238 1.00 50.30  ? 346 PHE B CE1 1 
ATOM   7868  C CE2 . PHE B 1 346 ? -16.070 41.929  -43.550 1.00 50.23  ? 346 PHE B CE2 1 
ATOM   7869  C CZ  . PHE B 1 346 ? -16.004 43.303  -43.706 1.00 49.93  ? 346 PHE B CZ  1 
ATOM   7870  N N   . PHE B 1 347 ? -21.252 43.242  -44.183 1.00 53.70  ? 347 PHE B N   1 
ATOM   7871  C CA  . PHE B 1 347 ? -21.787 43.307  -45.537 1.00 55.24  ? 347 PHE B CA  1 
ATOM   7872  C C   . PHE B 1 347 ? -20.941 44.249  -46.393 1.00 54.24  ? 347 PHE B C   1 
ATOM   7873  O O   . PHE B 1 347 ? -20.607 45.343  -45.963 1.00 55.15  ? 347 PHE B O   1 
ATOM   7874  C CB  . PHE B 1 347 ? -23.262 43.771  -45.506 1.00 56.73  ? 347 PHE B CB  1 
ATOM   7875  C CG  . PHE B 1 347 ? -23.883 43.919  -46.872 1.00 58.27  ? 347 PHE B CG  1 
ATOM   7876  C CD1 . PHE B 1 347 ? -23.806 45.129  -47.561 1.00 58.83  ? 347 PHE B CD1 1 
ATOM   7877  C CD2 . PHE B 1 347 ? -24.523 42.843  -47.482 1.00 59.40  ? 347 PHE B CD2 1 
ATOM   7878  C CE1 . PHE B 1 347 ? -24.356 45.264  -48.827 1.00 61.22  ? 347 PHE B CE1 1 
ATOM   7879  C CE2 . PHE B 1 347 ? -25.081 42.974  -48.746 1.00 61.97  ? 347 PHE B CE2 1 
ATOM   7880  C CZ  . PHE B 1 347 ? -25.004 44.188  -49.417 1.00 62.26  ? 347 PHE B CZ  1 
ATOM   7881  N N   . CYS B 1 348 ? -20.598 43.820  -47.601 1.00 54.79  ? 348 CYS B N   1 
ATOM   7882  C CA  . CYS B 1 348 ? -19.794 44.648  -48.507 1.00 56.21  ? 348 CYS B CA  1 
ATOM   7883  C C   . CYS B 1 348 ? -20.309 44.638  -49.943 1.00 57.12  ? 348 CYS B C   1 
ATOM   7884  O O   . CYS B 1 348 ? -20.758 43.608  -50.439 1.00 57.70  ? 348 CYS B O   1 
ATOM   7885  C CB  . CYS B 1 348 ? -18.326 44.205  -48.486 1.00 55.64  ? 348 CYS B CB  1 
ATOM   7886  S SG  . CYS B 1 348 ? -17.535 44.393  -46.878 1.00 53.55  ? 348 CYS B SG  1 
ATOM   7887  N N   . SER B 1 349 ? -20.221 45.792  -50.602 1.00 57.65  ? 349 SER B N   1 
ATOM   7888  C CA  . SER B 1 349 ? -20.562 45.924  -52.020 1.00 60.01  ? 349 SER B CA  1 
ATOM   7889  C C   . SER B 1 349 ? -19.699 46.999  -52.688 1.00 59.24  ? 349 SER B C   1 
ATOM   7890  O O   . SER B 1 349 ? -19.322 47.983  -52.042 1.00 58.87  ? 349 SER B O   1 
ATOM   7891  C CB  . SER B 1 349 ? -22.059 46.264  -52.197 1.00 62.84  ? 349 SER B CB  1 
ATOM   7892  O OG  . SER B 1 349 ? -22.392 46.439  -53.570 1.00 63.35  ? 349 SER B OG  1 
ATOM   7893  N N   . PRO B 1 350 ? -19.370 46.807  -53.983 1.00 59.48  ? 350 PRO B N   1 
ATOM   7894  C CA  . PRO B 1 350 ? -18.777 47.890  -54.774 1.00 61.28  ? 350 PRO B CA  1 
ATOM   7895  C C   . PRO B 1 350 ? -19.772 49.040  -55.001 1.00 63.82  ? 350 PRO B C   1 
ATOM   7896  O O   . PRO B 1 350 ? -19.387 50.115  -55.464 1.00 65.33  ? 350 PRO B O   1 
ATOM   7897  C CB  . PRO B 1 350 ? -18.437 47.210  -56.109 1.00 59.77  ? 350 PRO B CB  1 
ATOM   7898  C CG  . PRO B 1 350 ? -19.270 45.975  -56.148 1.00 59.46  ? 350 PRO B CG  1 
ATOM   7899  C CD  . PRO B 1 350 ? -19.388 45.533  -54.724 1.00 58.81  ? 350 PRO B CD  1 
ATOM   7900  N N   . HIS B 1 351 ? -21.039 48.803  -54.667 1.00 65.99  ? 351 HIS B N   1 
ATOM   7901  C CA  . HIS B 1 351 ? -22.087 49.805  -54.817 1.00 65.53  ? 351 HIS B CA  1 
ATOM   7902  C C   . HIS B 1 351 ? -22.448 50.369  -53.474 1.00 64.90  ? 351 HIS B C   1 
ATOM   7903  O O   . HIS B 1 351 ? -23.074 49.688  -52.652 1.00 65.11  ? 351 HIS B O   1 
ATOM   7904  C CB  . HIS B 1 351 ? -23.294 49.202  -55.517 1.00 67.19  ? 351 HIS B CB  1 
ATOM   7905  C CG  . HIS B 1 351 ? -22.944 48.465  -56.786 1.00 68.13  ? 351 HIS B CG  1 
ATOM   7906  N ND1 . HIS B 1 351 ? -22.991 47.124  -56.880 1.00 68.26  ? 351 HIS B ND1 1 
ATOM   7907  C CD2 . HIS B 1 351 ? -22.492 48.930  -58.024 1.00 69.43  ? 351 HIS B CD2 1 
ATOM   7908  C CE1 . HIS B 1 351 ? -22.608 46.746  -58.117 1.00 68.26  ? 351 HIS B CE1 1 
ATOM   7909  N NE2 . HIS B 1 351 ? -22.299 47.852  -58.813 1.00 69.27  ? 351 HIS B NE2 1 
ATOM   7910  N N   . PRO B 1 352 ? -22.025 51.620  -53.211 1.00 64.38  ? 352 PRO B N   1 
ATOM   7911  C CA  . PRO B 1 352 ? -22.195 52.252  -51.901 1.00 64.60  ? 352 PRO B CA  1 
ATOM   7912  C C   . PRO B 1 352 ? -23.644 52.324  -51.447 1.00 67.06  ? 352 PRO B C   1 
ATOM   7913  O O   . PRO B 1 352 ? -23.915 52.169  -50.261 1.00 68.08  ? 352 PRO B O   1 
ATOM   7914  C CB  . PRO B 1 352 ? -21.631 53.666  -52.106 1.00 64.94  ? 352 PRO B CB  1 
ATOM   7915  C CG  . PRO B 1 352 ? -21.531 53.852  -53.584 1.00 66.42  ? 352 PRO B CG  1 
ATOM   7916  C CD  . PRO B 1 352 ? -21.293 52.488  -54.147 1.00 65.24  ? 352 PRO B CD  1 
ATOM   7917  N N   . HIS B 1 353 ? -24.567 52.546  -52.383 1.00 68.73  ? 353 HIS B N   1 
ATOM   7918  C CA  . HIS B 1 353 ? -25.980 52.661  -52.038 1.00 70.55  ? 353 HIS B CA  1 
ATOM   7919  C C   . HIS B 1 353 ? -26.529 51.367  -51.490 1.00 69.87  ? 353 HIS B C   1 
ATOM   7920  O O   . HIS B 1 353 ? -27.406 51.370  -50.624 1.00 70.39  ? 353 HIS B O   1 
ATOM   7921  C CB  . HIS B 1 353 ? -26.802 53.163  -53.232 1.00 73.13  ? 353 HIS B CB  1 
ATOM   7922  C CG  . HIS B 1 353 ? -27.021 52.126  -54.312 1.00 73.50  ? 353 HIS B CG  1 
ATOM   7923  N ND1 . HIS B 1 353 ? -28.082 51.291  -54.313 1.00 74.31  ? 353 HIS B ND1 1 
ATOM   7924  C CD2 . HIS B 1 353 ? -26.274 51.815  -55.452 1.00 74.67  ? 353 HIS B CD2 1 
ATOM   7925  C CE1 . HIS B 1 353 ? -28.016 50.485  -55.393 1.00 75.22  ? 353 HIS B CE1 1 
ATOM   7926  N NE2 . HIS B 1 353 ? -26.912 50.807  -56.090 1.00 74.89  ? 353 HIS B NE2 1 
ATOM   7927  N N   . LYS B 1 354 ? -25.999 50.251  -51.977 1.00 69.36  ? 354 LYS B N   1 
ATOM   7928  C CA  . LYS B 1 354 ? -26.414 48.932  -51.516 1.00 70.31  ? 354 LYS B CA  1 
ATOM   7929  C C   . LYS B 1 354 ? -25.992 48.697  -50.060 1.00 70.76  ? 354 LYS B C   1 
ATOM   7930  O O   . LYS B 1 354 ? -26.641 47.942  -49.327 1.00 73.01  ? 354 LYS B O   1 
ATOM   7931  C CB  . LYS B 1 354 ? -25.817 47.864  -52.419 1.00 70.49  ? 354 LYS B CB  1 
ATOM   7932  C CG  . LYS B 1 354 ? -26.733 46.693  -52.708 1.00 70.90  ? 354 LYS B CG  1 
ATOM   7933  C CD  . LYS B 1 354 ? -26.334 46.025  -54.014 1.00 70.59  ? 354 LYS B CD  1 
ATOM   7934  C CE  . LYS B 1 354 ? -26.848 46.810  -55.215 1.00 73.10  ? 354 LYS B CE  1 
ATOM   7935  N NZ  . LYS B 1 354 ? -26.199 46.374  -56.479 1.00 71.74  ? 354 LYS B NZ  1 
ATOM   7936  N N   . VAL B 1 355 ? -24.919 49.366  -49.642 1.00 68.95  ? 355 VAL B N   1 
ATOM   7937  C CA  . VAL B 1 355 ? -24.459 49.299  -48.256 1.00 67.35  ? 355 VAL B CA  1 
ATOM   7938  C C   . VAL B 1 355 ? -25.339 50.149  -47.325 1.00 68.67  ? 355 VAL B C   1 
ATOM   7939  O O   . VAL B 1 355 ? -25.625 49.742  -46.191 1.00 66.42  ? 355 VAL B O   1 
ATOM   7940  C CB  . VAL B 1 355 ? -22.959 49.672  -48.126 1.00 64.59  ? 355 VAL B CB  1 
ATOM   7941  C CG1 . VAL B 1 355 ? -22.484 49.507  -46.691 1.00 60.94  ? 355 VAL B CG1 1 
ATOM   7942  C CG2 . VAL B 1 355 ? -22.119 48.809  -49.058 1.00 62.80  ? 355 VAL B CG2 1 
ATOM   7943  N N   . TYR B 1 356 ? -25.777 51.318  -47.809 1.00 71.79  ? 356 TYR B N   1 
ATOM   7944  C CA  . TYR B 1 356 ? -26.778 52.136  -47.088 1.00 75.33  ? 356 TYR B CA  1 
ATOM   7945  C C   . TYR B 1 356 ? -28.068 51.351  -46.879 1.00 73.55  ? 356 TYR B C   1 
ATOM   7946  O O   . TYR B 1 356 ? -28.621 51.330  -45.780 1.00 72.23  ? 356 TYR B O   1 
ATOM   7947  C CB  . TYR B 1 356 ? -27.108 53.435  -47.848 1.00 81.70  ? 356 TYR B CB  1 
ATOM   7948  C CG  . TYR B 1 356 ? -26.037 54.504  -47.787 1.00 85.94  ? 356 TYR B CG  1 
ATOM   7949  C CD1 . TYR B 1 356 ? -25.828 55.248  -46.625 1.00 87.65  ? 356 TYR B CD1 1 
ATOM   7950  C CD2 . TYR B 1 356 ? -25.244 54.786  -48.905 1.00 88.18  ? 356 TYR B CD2 1 
ATOM   7951  C CE1 . TYR B 1 356 ? -24.844 56.224  -46.571 1.00 90.17  ? 356 TYR B CE1 1 
ATOM   7952  C CE2 . TYR B 1 356 ? -24.260 55.760  -48.862 1.00 89.14  ? 356 TYR B CE2 1 
ATOM   7953  C CZ  . TYR B 1 356 ? -24.065 56.478  -47.697 1.00 90.18  ? 356 TYR B CZ  1 
ATOM   7954  O OH  . TYR B 1 356 ? -23.085 57.442  -47.658 1.00 92.20  ? 356 TYR B OH  1 
ATOM   7955  N N   . ASP B 1 357 ? -28.539 50.714  -47.953 1.00 73.36  ? 357 ASP B N   1 
ATOM   7956  C CA  . ASP B 1 357 ? -29.801 49.973  -47.938 1.00 73.21  ? 357 ASP B CA  1 
ATOM   7957  C C   . ASP B 1 357 ? -29.758 48.830  -46.933 1.00 70.48  ? 357 ASP B C   1 
ATOM   7958  O O   . ASP B 1 357 ? -30.708 48.625  -46.179 1.00 71.12  ? 357 ASP B O   1 
ATOM   7959  C CB  . ASP B 1 357 ? -30.141 49.439  -49.339 1.00 72.73  ? 357 ASP B CB  1 
ATOM   7960  C CG  . ASP B 1 357 ? -30.476 50.549  -50.335 1.00 73.05  ? 357 ASP B CG  1 
ATOM   7961  O OD1 . ASP B 1 357 ? -30.690 51.706  -49.912 1.00 72.44  ? 357 ASP B OD1 1 
ATOM   7962  O OD2 . ASP B 1 357 ? -30.518 50.257  -51.549 1.00 73.14  ? 357 ASP B OD2 1 
ATOM   7963  N N   . PHE B 1 358 ? -28.647 48.096  -46.919 1.00 69.18  ? 358 PHE B N   1 
ATOM   7964  C CA  . PHE B 1 358 ? -28.442 47.043  -45.927 1.00 67.57  ? 358 PHE B CA  1 
ATOM   7965  C C   . PHE B 1 358 ? -28.519 47.595  -44.516 1.00 67.47  ? 358 PHE B C   1 
ATOM   7966  O O   . PHE B 1 358 ? -29.177 47.012  -43.653 1.00 69.19  ? 358 PHE B O   1 
ATOM   7967  C CB  . PHE B 1 358 ? -27.096 46.348  -46.114 1.00 64.58  ? 358 PHE B CB  1 
ATOM   7968  C CG  . PHE B 1 358 ? -26.767 45.392  -45.008 1.00 62.06  ? 358 PHE B CG  1 
ATOM   7969  C CD1 . PHE B 1 358 ? -27.257 44.094  -45.030 1.00 61.91  ? 358 PHE B CD1 1 
ATOM   7970  C CD2 . PHE B 1 358 ? -26.007 45.804  -43.919 1.00 60.60  ? 358 PHE B CD2 1 
ATOM   7971  C CE1 . PHE B 1 358 ? -26.975 43.214  -44.001 1.00 62.09  ? 358 PHE B CE1 1 
ATOM   7972  C CE2 . PHE B 1 358 ? -25.722 44.931  -42.886 1.00 59.57  ? 358 PHE B CE2 1 
ATOM   7973  C CZ  . PHE B 1 358 ? -26.208 43.633  -42.924 1.00 60.88  ? 358 PHE B CZ  1 
ATOM   7974  N N   . GLU B 1 359 ? -27.832 48.709  -44.280 1.00 67.73  ? 359 GLU B N   1 
ATOM   7975  C CA  . GLU B 1 359 ? -27.840 49.333  -42.966 1.00 70.32  ? 359 GLU B CA  1 
ATOM   7976  C C   . GLU B 1 359 ? -29.272 49.637  -42.541 1.00 71.36  ? 359 GLU B C   1 
ATOM   7977  O O   . GLU B 1 359 ? -29.676 49.329  -41.410 1.00 70.58  ? 359 GLU B O   1 
ATOM   7978  C CB  . GLU B 1 359 ? -26.984 50.603  -42.954 1.00 72.00  ? 359 GLU B CB  1 
ATOM   7979  C CG  . GLU B 1 359 ? -26.824 51.219  -41.569 1.00 72.98  ? 359 GLU B CG  1 
ATOM   7980  C CD  . GLU B 1 359 ? -26.160 52.584  -41.598 1.00 74.90  ? 359 GLU B CD  1 
ATOM   7981  O OE1 . GLU B 1 359 ? -26.010 53.162  -42.695 1.00 76.27  ? 359 GLU B OE1 1 
ATOM   7982  O OE2 . GLU B 1 359 ? -25.788 53.082  -40.515 1.00 75.57  ? 359 GLU B OE2 1 
ATOM   7983  N N   . LEU B 1 360 ? -30.037 50.228  -43.458 1.00 72.90  ? 360 LEU B N   1 
ATOM   7984  C CA  . LEU B 1 360 ? -31.459 50.469  -43.240 1.00 74.63  ? 360 LEU B CA  1 
ATOM   7985  C C   . LEU B 1 360 ? -32.205 49.179  -42.911 1.00 73.14  ? 360 LEU B C   1 
ATOM   7986  O O   . LEU B 1 360 ? -32.862 49.091  -41.876 1.00 70.98  ? 360 LEU B O   1 
ATOM   7987  C CB  . LEU B 1 360 ? -32.086 51.147  -44.458 1.00 79.95  ? 360 LEU B CB  1 
ATOM   7988  C CG  . LEU B 1 360 ? -31.994 52.674  -44.534 1.00 82.53  ? 360 LEU B CG  1 
ATOM   7989  C CD1 . LEU B 1 360 ? -32.887 53.193  -45.655 1.00 82.74  ? 360 LEU B CD1 1 
ATOM   7990  C CD2 . LEU B 1 360 ? -32.357 53.324  -43.200 1.00 81.70  ? 360 LEU B CD2 1 
ATOM   7991  N N   . LEU B 1 361 ? -32.064 48.176  -43.782 1.00 72.27  ? 361 LEU B N   1 
ATOM   7992  C CA  . LEU B 1 361 ? -32.708 46.872  -43.598 1.00 73.40  ? 361 LEU B CA  1 
ATOM   7993  C C   . LEU B 1 361 ? -32.459 46.275  -42.217 1.00 73.66  ? 361 LEU B C   1 
ATOM   7994  O O   . LEU B 1 361 ? -33.402 45.900  -41.518 1.00 76.19  ? 361 LEU B O   1 
ATOM   7995  C CB  . LEU B 1 361 ? -32.266 45.887  -44.694 1.00 73.96  ? 361 LEU B CB  1 
ATOM   7996  C CG  . LEU B 1 361 ? -32.708 44.416  -44.603 1.00 74.35  ? 361 LEU B CG  1 
ATOM   7997  C CD1 . LEU B 1 361 ? -34.221 44.267  -44.724 1.00 77.97  ? 361 LEU B CD1 1 
ATOM   7998  C CD2 . LEU B 1 361 ? -32.016 43.590  -45.673 1.00 73.77  ? 361 LEU B CD2 1 
ATOM   7999  N N   . ILE B 1 362 ? -31.190 46.202  -41.823 1.00 72.61  ? 362 ILE B N   1 
ATOM   8000  C CA  . ILE B 1 362 ? -30.807 45.564  -40.569 1.00 70.90  ? 362 ILE B CA  1 
ATOM   8001  C C   . ILE B 1 362 ? -31.313 46.344  -39.357 1.00 70.94  ? 362 ILE B C   1 
ATOM   8002  O O   . ILE B 1 362 ? -31.678 45.752  -38.337 1.00 70.50  ? 362 ILE B O   1 
ATOM   8003  C CB  . ILE B 1 362 ? -29.271 45.307  -40.504 1.00 70.23  ? 362 ILE B CB  1 
ATOM   8004  C CG1 . ILE B 1 362 ? -28.929 44.202  -39.489 1.00 68.66  ? 362 ILE B CG1 1 
ATOM   8005  C CG2 . ILE B 1 362 ? -28.490 46.599  -40.274 1.00 69.63  ? 362 ILE B CG2 1 
ATOM   8006  C CD1 . ILE B 1 362 ? -28.361 44.695  -38.175 1.00 68.96  ? 362 ILE B CD1 1 
ATOM   8007  N N   . LYS B 1 363 ? -31.366 47.667  -39.480 1.00 71.91  ? 363 LYS B N   1 
ATOM   8008  C CA  . LYS B 1 363 ? -31.849 48.513  -38.384 1.00 73.74  ? 363 LYS B CA  1 
ATOM   8009  C C   . LYS B 1 363 ? -33.348 48.340  -38.125 1.00 75.79  ? 363 LYS B C   1 
ATOM   8010  O O   . LYS B 1 363 ? -33.819 48.546  -37.010 1.00 75.85  ? 363 LYS B O   1 
ATOM   8011  C CB  . LYS B 1 363 ? -31.525 49.981  -38.647 1.00 76.19  ? 363 LYS B CB  1 
ATOM   8012  C CG  . LYS B 1 363 ? -30.127 50.387  -38.223 1.00 77.11  ? 363 LYS B CG  1 
ATOM   8013  C CD  . LYS B 1 363 ? -29.875 51.854  -38.523 1.00 80.49  ? 363 LYS B CD  1 
ATOM   8014  C CE  . LYS B 1 363 ? -28.501 52.280  -38.030 1.00 82.94  ? 363 LYS B CE  1 
ATOM   8015  N NZ  . LYS B 1 363 ? -27.982 53.438  -38.812 1.00 85.49  ? 363 LYS B NZ  1 
ATOM   8016  N N   . GLY B 1 364 ? -34.091 47.969  -39.166 1.00 78.17  ? 364 GLY B N   1 
ATOM   8017  C CA  . GLY B 1 364 ? -35.506 47.654  -39.024 1.00 77.81  ? 364 GLY B CA  1 
ATOM   8018  C C   . GLY B 1 364 ? -35.730 46.292  -38.395 1.00 77.73  ? 364 GLY B C   1 
ATOM   8019  O O   . GLY B 1 364 ? -36.730 46.078  -37.713 1.00 79.52  ? 364 GLY B O   1 
ATOM   8020  N N   . VAL B 1 365 ? -34.794 45.371  -38.616 1.00 76.14  ? 365 VAL B N   1 
ATOM   8021  C CA  . VAL B 1 365 ? -34.948 43.986  -38.167 1.00 75.35  ? 365 VAL B CA  1 
ATOM   8022  C C   . VAL B 1 365 ? -34.453 43.774  -36.744 1.00 75.78  ? 365 VAL B C   1 
ATOM   8023  O O   . VAL B 1 365 ? -35.125 43.137  -35.940 1.00 79.09  ? 365 VAL B O   1 
ATOM   8024  C CB  . VAL B 1 365 ? -34.239 42.990  -39.111 1.00 73.19  ? 365 VAL B CB  1 
ATOM   8025  C CG1 . VAL B 1 365 ? -34.360 41.567  -38.578 1.00 72.11  ? 365 VAL B CG1 1 
ATOM   8026  C CG2 . VAL B 1 365 ? -34.815 43.086  -40.516 1.00 74.18  ? 365 VAL B CG2 1 
ATOM   8027  N N   . TYR B 1 366 ? -33.272 44.300  -36.436 1.00 77.94  ? 366 TYR B N   1 
ATOM   8028  C CA  . TYR B 1 366 ? -32.669 44.102  -35.114 1.00 76.81  ? 366 TYR B CA  1 
ATOM   8029  C C   . TYR B 1 366 ? -32.434 45.422  -34.385 1.00 77.77  ? 366 TYR B C   1 
ATOM   8030  O O   . TYR B 1 366 ? -32.434 46.492  -34.998 1.00 78.65  ? 366 TYR B O   1 
ATOM   8031  C CB  . TYR B 1 366 ? -31.350 43.332  -35.236 1.00 73.64  ? 366 TYR B CB  1 
ATOM   8032  C CG  . TYR B 1 366 ? -31.480 41.922  -35.788 1.00 74.03  ? 366 TYR B CG  1 
ATOM   8033  C CD1 . TYR B 1 366 ? -32.174 40.941  -35.087 1.00 75.47  ? 366 TYR B CD1 1 
ATOM   8034  C CD2 . TYR B 1 366 ? -30.875 41.562  -36.994 1.00 73.93  ? 366 TYR B CD2 1 
ATOM   8035  C CE1 . TYR B 1 366 ? -32.284 39.650  -35.578 1.00 75.98  ? 366 TYR B CE1 1 
ATOM   8036  C CE2 . TYR B 1 366 ? -30.978 40.271  -37.491 1.00 74.27  ? 366 TYR B CE2 1 
ATOM   8037  C CZ  . TYR B 1 366 ? -31.686 39.320  -36.776 1.00 74.93  ? 366 TYR B CZ  1 
ATOM   8038  O OH  . TYR B 1 366 ? -31.799 38.035  -37.249 1.00 76.65  ? 366 TYR B OH  1 
ATOM   8039  N N   . GLN B 1 367 ? -32.257 45.344  -33.070 1.00 80.69  ? 367 GLN B N   1 
ATOM   8040  C CA  . GLN B 1 367 ? -31.721 46.469  -32.313 1.00 83.04  ? 367 GLN B CA  1 
ATOM   8041  C C   . GLN B 1 367 ? -30.224 46.520  -32.538 1.00 82.06  ? 367 GLN B C   1 
ATOM   8042  O O   . GLN B 1 367 ? -29.534 45.503  -32.405 1.00 81.68  ? 367 GLN B O   1 
ATOM   8043  C CB  . GLN B 1 367 ? -32.019 46.324  -30.818 1.00 85.83  ? 367 GLN B CB  1 
ATOM   8044  C CG  . GLN B 1 367 ? -32.027 47.647  -30.058 1.00 89.75  ? 367 GLN B CG  1 
ATOM   8045  C CD  . GLN B 1 367 ? -33.233 48.519  -30.405 1.00 94.44  ? 367 GLN B CD  1 
ATOM   8046  O OE1 . GLN B 1 367 ? -33.125 49.461  -31.192 1.00 97.41  ? 367 GLN B OE1 1 
ATOM   8047  N NE2 . GLN B 1 367 ? -34.389 48.197  -29.826 1.00 92.16  ? 367 GLN B NE2 1 
ATOM   8048  N N   . VAL B 1 368 ? -29.725 47.698  -32.899 1.00 82.03  ? 368 VAL B N   1 
ATOM   8049  C CA  . VAL B 1 368 ? -28.292 47.883  -33.130 1.00 81.15  ? 368 VAL B CA  1 
ATOM   8050  C C   . VAL B 1 368 ? -27.654 48.840  -32.119 1.00 82.70  ? 368 VAL B C   1 
ATOM   8051  O O   . VAL B 1 368 ? -28.329 49.698  -31.553 1.00 87.01  ? 368 VAL B O   1 
ATOM   8052  C CB  . VAL B 1 368 ? -28.003 48.367  -34.566 1.00 78.29  ? 368 VAL B CB  1 
ATOM   8053  C CG1 . VAL B 1 368 ? -28.486 47.341  -35.571 1.00 78.85  ? 368 VAL B CG1 1 
ATOM   8054  C CG2 . VAL B 1 368 ? -28.648 49.717  -34.827 1.00 79.14  ? 368 VAL B CG2 1 
ATOM   8055  N N   . ASN B 1 369 ? -26.360 48.667  -31.879 1.00 81.61  ? 369 ASN B N   1 
ATOM   8056  C CA  . ASN B 1 369 ? -25.576 49.677  -31.181 1.00 82.72  ? 369 ASN B CA  1 
ATOM   8057  C C   . ASN B 1 369 ? -24.879 50.582  -32.198 1.00 81.66  ? 369 ASN B C   1 
ATOM   8058  O O   . ASN B 1 369 ? -23.838 50.215  -32.731 1.00 79.82  ? 369 ASN B O   1 
ATOM   8059  C CB  . ASN B 1 369 ? -24.552 49.017  -30.254 1.00 85.11  ? 369 ASN B CB  1 
ATOM   8060  C CG  . ASN B 1 369 ? -25.168 48.526  -28.957 1.00 88.50  ? 369 ASN B CG  1 
ATOM   8061  O OD1 . ASN B 1 369 ? -25.835 49.283  -28.248 1.00 92.53  ? 369 ASN B OD1 1 
ATOM   8062  N ND2 . ASN B 1 369 ? -24.938 47.255  -28.633 1.00 86.60  ? 369 ASN B ND2 1 
ATOM   8063  N N   . PRO B 1 370 ? -25.463 51.768  -32.479 1.00 83.44  ? 370 PRO B N   1 
ATOM   8064  C CA  . PRO B 1 370 ? -24.984 52.650  -33.560 1.00 83.77  ? 370 PRO B CA  1 
ATOM   8065  C C   . PRO B 1 370 ? -23.537 53.111  -33.361 1.00 83.93  ? 370 PRO B C   1 
ATOM   8066  O O   . PRO B 1 370 ? -22.833 53.393  -34.339 1.00 84.43  ? 370 PRO B O   1 
ATOM   8067  C CB  . PRO B 1 370 ? -25.937 53.851  -33.490 1.00 83.60  ? 370 PRO B CB  1 
ATOM   8068  C CG  . PRO B 1 370 ? -27.101 53.386  -32.681 1.00 83.19  ? 370 PRO B CG  1 
ATOM   8069  C CD  . PRO B 1 370 ? -26.548 52.396  -31.711 1.00 81.83  ? 370 PRO B CD  1 
ATOM   8070  N N   . THR B 1 371 ? -23.113 53.177  -32.099 1.00 83.83  ? 371 THR B N   1 
ATOM   8071  C CA  . THR B 1 371 ? -21.732 53.489  -31.728 1.00 81.70  ? 371 THR B CA  1 
ATOM   8072  C C   . THR B 1 371 ? -20.760 52.367  -32.126 1.00 80.54  ? 371 THR B C   1 
ATOM   8073  O O   . THR B 1 371 ? -19.574 52.616  -32.368 1.00 79.03  ? 371 THR B O   1 
ATOM   8074  C CB  . THR B 1 371 ? -21.608 53.796  -30.208 1.00 84.99  ? 371 THR B CB  1 
ATOM   8075  O OG1 . THR B 1 371 ? -20.503 53.070  -29.645 1.00 83.38  ? 371 THR B OG1 1 
ATOM   8076  C CG2 . THR B 1 371 ? -22.888 53.400  -29.461 1.00 86.01  ? 371 THR B CG2 1 
ATOM   8077  N N   . LYS B 1 372 ? -21.272 51.139  -32.192 1.00 78.43  ? 372 LYS B N   1 
ATOM   8078  C CA  . LYS B 1 372 ? -20.465 49.970  -32.550 1.00 76.18  ? 372 LYS B CA  1 
ATOM   8079  C C   . LYS B 1 372 ? -20.364 49.762  -34.066 1.00 74.25  ? 372 LYS B C   1 
ATOM   8080  O O   . LYS B 1 372 ? -19.714 48.818  -34.527 1.00 75.73  ? 372 LYS B O   1 
ATOM   8081  C CB  . LYS B 1 372 ? -21.039 48.711  -31.892 1.00 79.04  ? 372 LYS B CB  1 
ATOM   8082  C CG  . LYS B 1 372 ? -20.515 48.417  -30.497 1.00 80.27  ? 372 LYS B CG  1 
ATOM   8083  C CD  . LYS B 1 372 ? -19.270 47.544  -30.553 1.00 80.70  ? 372 LYS B CD  1 
ATOM   8084  C CE  . LYS B 1 372 ? -19.063 46.794  -29.249 1.00 81.58  ? 372 LYS B CE  1 
ATOM   8085  N NZ  . LYS B 1 372 ? -17.967 45.792  -29.359 1.00 81.04  ? 372 LYS B NZ  1 
ATOM   8086  N N   . THR B 1 373 ? -21.008 50.639  -34.832 1.00 70.71  ? 373 THR B N   1 
ATOM   8087  C CA  . THR B 1 373 ? -21.023 50.535  -36.287 1.00 68.89  ? 373 THR B CA  1 
ATOM   8088  C C   . THR B 1 373 ? -19.700 51.021  -36.891 1.00 67.12  ? 373 THR B C   1 
ATOM   8089  O O   . THR B 1 373 ? -19.235 52.115  -36.569 1.00 68.50  ? 373 THR B O   1 
ATOM   8090  C CB  . THR B 1 373 ? -22.213 51.326  -36.884 1.00 69.43  ? 373 THR B CB  1 
ATOM   8091  O OG1 . THR B 1 373 ? -23.433 50.639  -36.588 1.00 68.28  ? 373 THR B OG1 1 
ATOM   8092  C CG2 . THR B 1 373 ? -22.078 51.474  -38.399 1.00 67.34  ? 373 THR B CG2 1 
ATOM   8093  N N   . ARG B 1 374 ? -19.096 50.194  -37.750 1.00 62.94  ? 374 ARG B N   1 
ATOM   8094  C CA  . ARG B 1 374 ? -17.900 50.587  -38.504 1.00 61.32  ? 374 ARG B CA  1 
ATOM   8095  C C   . ARG B 1 374 ? -18.147 50.502  -39.999 1.00 60.36  ? 374 ARG B C   1 
ATOM   8096  O O   . ARG B 1 374 ? -18.684 49.505  -40.491 1.00 58.57  ? 374 ARG B O   1 
ATOM   8097  C CB  . ARG B 1 374 ? -16.693 49.710  -38.141 1.00 61.15  ? 374 ARG B CB  1 
ATOM   8098  C CG  . ARG B 1 374 ? -16.418 49.591  -36.654 1.00 60.51  ? 374 ARG B CG  1 
ATOM   8099  C CD  . ARG B 1 374 ? -15.836 50.868  -36.076 1.00 60.79  ? 374 ARG B CD  1 
ATOM   8100  N NE  . ARG B 1 374 ? -15.643 50.744  -34.633 1.00 64.20  ? 374 ARG B NE  1 
ATOM   8101  C CZ  . ARG B 1 374 ? -16.486 51.211  -33.717 1.00 64.87  ? 374 ARG B CZ  1 
ATOM   8102  N NH1 . ARG B 1 374 ? -17.578 51.859  -34.082 1.00 67.28  ? 374 ARG B NH1 1 
ATOM   8103  N NH2 . ARG B 1 374 ? -16.231 51.034  -32.432 1.00 68.13  ? 374 ARG B NH2 1 
ATOM   8104  N N   . THR B 1 375 ? -17.728 51.543  -40.716 1.00 59.31  ? 375 THR B N   1 
ATOM   8105  C CA  . THR B 1 375 ? -17.962 51.646  -42.153 1.00 60.75  ? 375 THR B CA  1 
ATOM   8106  C C   . THR B 1 375 ? -17.010 52.636  -42.826 1.00 60.39  ? 375 THR B C   1 
ATOM   8107  O O   . THR B 1 375 ? -16.539 53.575  -42.191 1.00 60.54  ? 375 THR B O   1 
ATOM   8108  C CB  . THR B 1 375 ? -19.418 52.067  -42.453 1.00 62.39  ? 375 THR B CB  1 
ATOM   8109  O OG1 . THR B 1 375 ? -19.665 51.949  -43.855 1.00 61.72  ? 375 THR B OG1 1 
ATOM   8110  C CG2 . THR B 1 375 ? -19.677 53.509  -42.008 1.00 63.17  ? 375 THR B CG2 1 
ATOM   8111  N N   . ASN B 1 376 ? -16.737 52.430  -44.114 1.00 60.49  ? 376 ASN B N   1 
ATOM   8112  C CA  . ASN B 1 376 ? -15.980 53.417  -44.888 1.00 61.78  ? 376 ASN B CA  1 
ATOM   8113  C C   . ASN B 1 376 ? -16.880 54.365  -45.693 1.00 65.82  ? 376 ASN B C   1 
ATOM   8114  O O   . ASN B 1 376 ? -16.414 55.041  -46.620 1.00 67.67  ? 376 ASN B O   1 
ATOM   8115  C CB  . ASN B 1 376 ? -14.944 52.740  -45.799 1.00 59.16  ? 376 ASN B CB  1 
ATOM   8116  C CG  . ASN B 1 376 ? -15.579 51.918  -46.910 1.00 58.81  ? 376 ASN B CG  1 
ATOM   8117  O OD1 . ASN B 1 376 ? -16.698 51.430  -46.776 1.00 61.33  ? 376 ASN B OD1 1 
ATOM   8118  N ND2 . ASN B 1 376 ? -14.848 51.741  -48.004 1.00 57.78  ? 376 ASN B ND2 1 
ATOM   8119  N N   . LEU B 1 377 ? -18.165 54.409  -45.338 1.00 69.42  ? 377 LEU B N   1 
ATOM   8120  C CA  . LEU B 1 377 ? -19.129 55.262  -46.041 1.00 73.76  ? 377 LEU B CA  1 
ATOM   8121  C C   . LEU B 1 377 ? -18.906 56.753  -45.751 1.00 77.25  ? 377 LEU B C   1 
ATOM   8122  O O   . LEU B 1 377 ? -18.824 57.156  -44.590 1.00 75.29  ? 377 LEU B O   1 
ATOM   8123  C CB  . LEU B 1 377 ? -20.567 54.851  -45.708 1.00 73.41  ? 377 LEU B CB  1 
ATOM   8124  C CG  . LEU B 1 377 ? -21.092 53.567  -46.363 1.00 73.19  ? 377 LEU B CG  1 
ATOM   8125  C CD1 . LEU B 1 377 ? -22.445 53.192  -45.781 1.00 72.69  ? 377 LEU B CD1 1 
ATOM   8126  C CD2 . LEU B 1 377 ? -21.176 53.698  -47.881 1.00 73.64  ? 377 LEU B CD2 1 
ATOM   8127  N N   . PRO B 1 378 ? -18.802 57.573  -46.817 1.00 84.00  ? 378 PRO B N   1 
ATOM   8128  C CA  . PRO B 1 378 ? -18.546 59.016  -46.709 1.00 88.61  ? 378 PRO B CA  1 
ATOM   8129  C C   . PRO B 1 378 ? -19.531 59.737  -45.784 1.00 93.75  ? 378 PRO B C   1 
ATOM   8130  O O   . PRO B 1 378 ? -19.168 60.737  -45.161 1.00 96.32  ? 378 PRO B O   1 
ATOM   8131  C CB  . PRO B 1 378 ? -18.703 59.513  -48.156 1.00 90.38  ? 378 PRO B CB  1 
ATOM   8132  C CG  . PRO B 1 378 ? -19.445 58.429  -48.871 1.00 89.32  ? 378 PRO B CG  1 
ATOM   8133  C CD  . PRO B 1 378 ? -18.982 57.163  -48.220 1.00 86.32  ? 378 PRO B CD  1 
ATOM   8134  N N   . THR B 1 379 ? -20.758 59.218  -45.698 1.00 98.47  ? 379 THR B N   1 
ATOM   8135  C CA  . THR B 1 379 ? -21.787 59.729  -44.784 1.00 101.89 ? 379 THR B CA  1 
ATOM   8136  C C   . THR B 1 379 ? -21.276 59.938  -43.360 1.00 103.71 ? 379 THR B C   1 
ATOM   8137  O O   . THR B 1 379 ? -21.390 61.039  -42.814 1.00 109.05 ? 379 THR B O   1 
ATOM   8138  C CB  . THR B 1 379 ? -23.023 58.791  -44.752 1.00 101.87 ? 379 THR B CB  1 
ATOM   8139  O OG1 . THR B 1 379 ? -23.903 59.132  -45.824 1.00 104.80 ? 379 THR B OG1 1 
ATOM   8140  C CG2 . THR B 1 379 ? -23.794 58.905  -43.429 1.00 104.02 ? 379 THR B CG2 1 
ATOM   8141  N N   . HIS B 1 380 ? -20.695 58.886  -42.783 1.00 101.18 ? 380 HIS B N   1 
ATOM   8142  C CA  . HIS B 1 380 ? -20.502 58.791  -41.333 1.00 100.13 ? 380 HIS B CA  1 
ATOM   8143  C C   . HIS B 1 380 ? -19.514 59.774  -40.779 1.00 99.05  ? 380 HIS B C   1 
ATOM   8144  O O   . HIS B 1 380 ? -18.644 60.274  -41.497 1.00 97.76  ? 380 HIS B O   1 
ATOM   8145  C CB  . HIS B 1 380 ? -20.127 57.362  -40.936 1.00 99.97  ? 380 HIS B CB  1 
ATOM   8146  C CG  . HIS B 1 380 ? -21.296 56.396  -40.954 1.00 101.87 ? 380 HIS B CG  1 
ATOM   8147  N ND1 . HIS B 1 380 ? -22.007 56.132  -42.073 1.00 101.48 ? 380 HIS B ND1 1 
ATOM   8148  C CD2 . HIS B 1 380 ? -21.859 55.618  -39.939 1.00 100.76 ? 380 HIS B CD2 1 
ATOM   8149  C CE1 . HIS B 1 380 ? -22.976 55.241  -41.788 1.00 100.43 ? 380 HIS B CE1 1 
ATOM   8150  N NE2 . HIS B 1 380 ? -22.886 54.927  -40.485 1.00 100.97 ? 380 HIS B NE2 1 
ATOM   8151  N N   . ARG B 1 381 ? -19.665 60.075  -39.490 1.00 100.28 ? 381 ARG B N   1 
ATOM   8152  C CA  . ARG B 1 381 ? -18.770 60.990  -38.787 1.00 101.51 ? 381 ARG B CA  1 
ATOM   8153  C C   . ARG B 1 381 ? -17.316 60.557  -38.921 1.00 98.81  ? 381 ARG B C   1 
ATOM   8154  O O   . ARG B 1 381 ? -16.465 61.345  -39.340 1.00 98.81  ? 381 ARG B O   1 
ATOM   8155  C CB  . ARG B 1 381 ? -19.161 61.090  -37.311 1.00 103.47 ? 381 ARG B CB  1 
ATOM   8156  C CG  . ARG B 1 381 ? -20.348 62.000  -37.052 1.00 106.92 ? 381 ARG B CG  1 
ATOM   8157  C CD  . ARG B 1 381 ? -21.412 61.301  -36.222 1.00 109.45 ? 381 ARG B CD  1 
ATOM   8158  N NE  . ARG B 1 381 ? -22.725 61.922  -36.402 1.00 112.67 ? 381 ARG B NE  1 
ATOM   8159  C CZ  . ARG B 1 381 ? -23.882 61.264  -36.374 1.00 112.50 ? 381 ARG B CZ  1 
ATOM   8160  N NH1 . ARG B 1 381 ? -23.905 59.951  -36.180 1.00 111.20 ? 381 ARG B NH1 1 
ATOM   8161  N NH2 . ARG B 1 381 ? -25.019 61.923  -36.550 1.00 114.36 ? 381 ARG B NH2 1 
ATOM   8162  N N   . HIS B 1 382 ? -17.042 59.297  -38.588 1.00 95.26  ? 382 HIS B N   1 
ATOM   8163  C CA  . HIS B 1 382 ? -15.679 58.767  -38.648 1.00 92.23  ? 382 HIS B CA  1 
ATOM   8164  C C   . HIS B 1 382 ? -15.583 57.519  -39.502 1.00 86.20  ? 382 HIS B C   1 
ATOM   8165  O O   . HIS B 1 382 ? -15.565 56.400  -38.976 1.00 83.30  ? 382 HIS B O   1 
ATOM   8166  C CB  . HIS B 1 382 ? -15.134 58.514  -37.237 1.00 94.88  ? 382 HIS B CB  1 
ATOM   8167  C CG  . HIS B 1 382 ? -15.324 59.683  -36.287 1.00 100.76 ? 382 HIS B CG  1 
ATOM   8168  N ND1 . HIS B 1 382 ? -15.882 59.543  -35.066 1.00 101.82 ? 382 HIS B ND1 1 
ATOM   8169  C CD2 . HIS B 1 382 ? -15.018 61.040  -36.424 1.00 101.60 ? 382 HIS B CD2 1 
ATOM   8170  C CE1 . HIS B 1 382 ? -15.926 60.742  -34.453 1.00 101.30 ? 382 HIS B CE1 1 
ATOM   8171  N NE2 . HIS B 1 382 ? -15.401 61.656  -35.283 1.00 101.58 ? 382 HIS B NE2 1 
ATOM   8172  N N   . PRO B 1 383 ? -15.525 57.692  -40.842 1.00 82.78  ? 383 PRO B N   1 
ATOM   8173  C CA  . PRO B 1 383 ? -15.382 56.541  -41.739 1.00 78.79  ? 383 PRO B CA  1 
ATOM   8174  C C   . PRO B 1 383 ? -14.012 55.870  -41.610 1.00 75.12  ? 383 PRO B C   1 
ATOM   8175  O O   . PRO B 1 383 ? -13.008 56.553  -41.402 1.00 75.10  ? 383 PRO B O   1 
ATOM   8176  C CB  . PRO B 1 383 ? -15.557 57.151  -43.132 1.00 78.04  ? 383 PRO B CB  1 
ATOM   8177  C CG  . PRO B 1 383 ? -15.209 58.588  -42.971 1.00 78.83  ? 383 PRO B CG  1 
ATOM   8178  C CD  . PRO B 1 383 ? -15.629 58.963  -41.585 1.00 81.18  ? 383 PRO B CD  1 
ATOM   8179  N N   . GLN B 1 384 ? -13.991 54.542  -41.723 1.00 70.49  ? 384 GLN B N   1 
ATOM   8180  C CA  . GLN B 1 384 ? -12.780 53.746  -41.539 1.00 65.71  ? 384 GLN B CA  1 
ATOM   8181  C C   . GLN B 1 384 ? -12.622 52.760  -42.669 1.00 63.10  ? 384 GLN B C   1 
ATOM   8182  O O   . GLN B 1 384 ? -13.595 52.155  -43.108 1.00 62.13  ? 384 GLN B O   1 
ATOM   8183  C CB  . GLN B 1 384 ? -12.865 52.942  -40.255 1.00 63.96  ? 384 GLN B CB  1 
ATOM   8184  C CG  . GLN B 1 384 ? -12.917 53.753  -38.985 1.00 66.19  ? 384 GLN B CG  1 
ATOM   8185  C CD  . GLN B 1 384 ? -13.279 52.903  -37.788 1.00 64.97  ? 384 GLN B CD  1 
ATOM   8186  O OE1 . GLN B 1 384 ? -14.110 53.293  -36.969 1.00 64.71  ? 384 GLN B OE1 1 
ATOM   8187  N NE2 . GLN B 1 384 ? -12.670 51.719  -37.689 1.00 63.27  ? 384 GLN B NE2 1 
ATOM   8188  N N   . ASP B 1 385 ? -11.385 52.551  -43.097 1.00 61.79  ? 385 ASP B N   1 
ATOM   8189  C CA  . ASP B 1 385 ? -11.087 51.515  -44.077 1.00 60.43  ? 385 ASP B CA  1 
ATOM   8190  C C   . ASP B 1 385 ? -11.025 50.129  -43.436 1.00 57.60  ? 385 ASP B C   1 
ATOM   8191  O O   . ASP B 1 385 ? -11.357 49.123  -44.071 1.00 56.31  ? 385 ASP B O   1 
ATOM   8192  C CB  . ASP B 1 385 ? -9.776  51.826  -44.786 1.00 63.03  ? 385 ASP B CB  1 
ATOM   8193  C CG  . ASP B 1 385 ? -9.933  52.891  -45.844 1.00 67.34  ? 385 ASP B CG  1 
ATOM   8194  O OD1 . ASP B 1 385 ? -11.088 53.301  -46.114 1.00 70.98  ? 385 ASP B OD1 1 
ATOM   8195  O OD2 . ASP B 1 385 ? -8.905  53.311  -46.414 1.00 67.22  ? 385 ASP B OD2 1 
ATOM   8196  N N   . GLU B 1 386 ? -10.616 50.090  -42.174 1.00 53.95  ? 386 GLU B N   1 
ATOM   8197  C CA  . GLU B 1 386 ? -10.396 48.840  -41.475 1.00 53.35  ? 386 GLU B CA  1 
ATOM   8198  C C   . GLU B 1 386 ? -11.555 48.570  -40.538 1.00 53.21  ? 386 GLU B C   1 
ATOM   8199  O O   . GLU B 1 386 ? -11.861 49.385  -39.662 1.00 56.91  ? 386 GLU B O   1 
ATOM   8200  C CB  . GLU B 1 386 ? -9.072  48.894  -40.700 1.00 54.37  ? 386 GLU B CB  1 
ATOM   8201  C CG  . GLU B 1 386 ? -7.909  49.431  -41.528 1.00 57.59  ? 386 GLU B CG  1 
ATOM   8202  C CD  . GLU B 1 386 ? -6.539  49.108  -40.944 1.00 61.25  ? 386 GLU B CD  1 
ATOM   8203  O OE1 . GLU B 1 386 ? -6.411  49.012  -39.695 1.00 61.13  ? 386 GLU B OE1 1 
ATOM   8204  O OE2 . GLU B 1 386 ? -5.582  48.958  -41.747 1.00 62.33  ? 386 GLU B OE2 1 
ATOM   8205  N N   . ILE B 1 387 ? -12.224 47.442  -40.731 1.00 51.00  ? 387 ILE B N   1 
ATOM   8206  C CA  . ILE B 1 387 ? -13.339 47.086  -39.864 1.00 50.90  ? 387 ILE B CA  1 
ATOM   8207  C C   . ILE B 1 387 ? -13.066 45.765  -39.142 1.00 49.66  ? 387 ILE B C   1 
ATOM   8208  O O   . ILE B 1 387 ? -12.646 44.782  -39.762 1.00 48.20  ? 387 ILE B O   1 
ATOM   8209  C CB  . ILE B 1 387 ? -14.700 47.043  -40.619 1.00 52.96  ? 387 ILE B CB  1 
ATOM   8210  C CG1 . ILE B 1 387 ? -14.846 45.734  -41.371 1.00 52.97  ? 387 ILE B CG1 1 
ATOM   8211  C CG2 . ILE B 1 387 ? -14.860 48.239  -41.577 1.00 50.88  ? 387 ILE B CG2 1 
ATOM   8212  C CD1 . ILE B 1 387 ? -14.134 45.742  -42.704 1.00 55.25  ? 387 ILE B CD1 1 
ATOM   8213  N N   . PRO B 1 388 ? -13.275 45.747  -37.817 1.00 49.20  ? 388 PRO B N   1 
ATOM   8214  C CA  . PRO B 1 388 ? -13.034 44.530  -37.062 1.00 48.78  ? 388 PRO B CA  1 
ATOM   8215  C C   . PRO B 1 388 ? -14.238 43.600  -37.131 1.00 50.01  ? 388 PRO B C   1 
ATOM   8216  O O   . PRO B 1 388 ? -15.356 44.013  -36.835 1.00 53.50  ? 388 PRO B O   1 
ATOM   8217  C CB  . PRO B 1 388 ? -12.819 45.044  -35.634 1.00 47.76  ? 388 PRO B CB  1 
ATOM   8218  C CG  . PRO B 1 388 ? -13.632 46.292  -35.560 1.00 49.67  ? 388 PRO B CG  1 
ATOM   8219  C CD  . PRO B 1 388 ? -13.646 46.882  -36.948 1.00 49.68  ? 388 PRO B CD  1 
ATOM   8220  N N   . TYR B 1 389 ? -14.006 42.354  -37.523 1.00 48.67  ? 389 TYR B N   1 
ATOM   8221  C CA  . TYR B 1 389 ? -15.063 41.355  -37.583 1.00 49.00  ? 389 TYR B CA  1 
ATOM   8222  C C   . TYR B 1 389 ? -14.475 39.983  -37.299 1.00 47.99  ? 389 TYR B C   1 
ATOM   8223  O O   . TYR B 1 389 ? -13.436 39.626  -37.846 1.00 49.47  ? 389 TYR B O   1 
ATOM   8224  C CB  . TYR B 1 389 ? -15.734 41.373  -38.967 1.00 49.39  ? 389 TYR B CB  1 
ATOM   8225  C CG  . TYR B 1 389 ? -16.823 40.343  -39.144 1.00 48.95  ? 389 TYR B CG  1 
ATOM   8226  C CD1 . TYR B 1 389 ? -18.067 40.495  -38.527 1.00 50.19  ? 389 TYR B CD1 1 
ATOM   8227  C CD2 . TYR B 1 389 ? -16.615 39.221  -39.938 1.00 49.65  ? 389 TYR B CD2 1 
ATOM   8228  C CE1 . TYR B 1 389 ? -19.072 39.548  -38.692 1.00 51.32  ? 389 TYR B CE1 1 
ATOM   8229  C CE2 . TYR B 1 389 ? -17.613 38.273  -40.117 1.00 51.40  ? 389 TYR B CE2 1 
ATOM   8230  C CZ  . TYR B 1 389 ? -18.836 38.437  -39.486 1.00 52.27  ? 389 TYR B CZ  1 
ATOM   8231  O OH  . TYR B 1 389 ? -19.812 37.489  -39.657 1.00 52.93  ? 389 TYR B OH  1 
ATOM   8232  N N   . CYS B 1 390 ? -15.132 39.226  -36.431 1.00 48.80  ? 390 CYS B N   1 
ATOM   8233  C CA  . CYS B 1 390 ? -14.696 37.865  -36.081 1.00 50.96  ? 390 CYS B CA  1 
ATOM   8234  C C   . CYS B 1 390 ? -13.202 37.727  -35.784 1.00 47.55  ? 390 CYS B C   1 
ATOM   8235  O O   . CYS B 1 390 ? -12.533 36.845  -36.332 1.00 44.62  ? 390 CYS B O   1 
ATOM   8236  C CB  . CYS B 1 390 ? -15.103 36.878  -37.178 1.00 54.90  ? 390 CYS B CB  1 
ATOM   8237  S SG  . CYS B 1 390 ? -16.887 36.668  -37.303 1.00 63.74  ? 390 CYS B SG  1 
ATOM   8238  N N   . GLY B 1 391 ? -12.687 38.607  -34.926 1.00 46.92  ? 391 GLY B N   1 
ATOM   8239  C CA  . GLY B 1 391 ? -11.285 38.551  -34.491 1.00 44.89  ? 391 GLY B CA  1 
ATOM   8240  C C   . GLY B 1 391 ? -10.298 38.884  -35.588 1.00 45.57  ? 391 GLY B C   1 
ATOM   8241  O O   . GLY B 1 391 ? -9.102  38.600  -35.480 1.00 46.39  ? 391 GLY B O   1 
ATOM   8242  N N   . LYS B 1 392 ? -10.802 39.477  -36.658 1.00 45.77  ? 392 LYS B N   1 
ATOM   8243  C CA  . LYS B 1 392 ? -9.966  39.890  -37.765 1.00 44.30  ? 392 LYS B CA  1 
ATOM   8244  C C   . LYS B 1 392 ? -10.187 41.372  -38.027 1.00 44.53  ? 392 LYS B C   1 
ATOM   8245  O O   . LYS B 1 392 ? -11.214 41.940  -37.620 1.00 44.11  ? 392 LYS B O   1 
ATOM   8246  C CB  . LYS B 1 392 ? -10.309 39.076  -39.012 1.00 44.87  ? 392 LYS B CB  1 
ATOM   8247  C CG  . LYS B 1 392 ? -9.399  37.885  -39.277 1.00 47.03  ? 392 LYS B CG  1 
ATOM   8248  C CD  . LYS B 1 392 ? -9.577  36.733  -38.303 1.00 48.15  ? 392 LYS B CD  1 
ATOM   8249  C CE  . LYS B 1 392 ? -8.503  35.687  -38.549 1.00 50.00  ? 392 LYS B CE  1 
ATOM   8250  N NZ  . LYS B 1 392 ? -8.252  34.756  -37.409 1.00 51.35  ? 392 LYS B NZ  1 
ATOM   8251  N N   . ILE B 1 393 ? -9.213  42.000  -38.679 1.00 42.62  ? 393 ILE B N   1 
ATOM   8252  C CA  . ILE B 1 393 ? -9.400  43.322  -39.262 1.00 42.76  ? 393 ILE B CA  1 
ATOM   8253  C C   . ILE B 1 393 ? -9.346  43.253  -40.789 1.00 42.82  ? 393 ILE B C   1 
ATOM   8254  O O   . ILE B 1 393 ? -8.357  42.810  -41.364 1.00 42.20  ? 393 ILE B O   1 
ATOM   8255  C CB  . ILE B 1 393 ? -8.361  44.335  -38.751 1.00 42.42  ? 393 ILE B CB  1 
ATOM   8256  C CG1 . ILE B 1 393 ? -8.461  44.480  -37.226 1.00 42.60  ? 393 ILE B CG1 1 
ATOM   8257  C CG2 . ILE B 1 393 ? -8.560  45.682  -39.436 1.00 42.16  ? 393 ILE B CG2 1 
ATOM   8258  C CD1 . ILE B 1 393 ? -7.218  45.056  -36.571 1.00 40.89  ? 393 ILE B CD1 1 
ATOM   8259  N N   . PHE B 1 394 ? -10.427 43.693  -41.428 1.00 43.79  ? 394 PHE B N   1 
ATOM   8260  C CA  . PHE B 1 394 ? -10.532 43.731  -42.882 1.00 43.33  ? 394 PHE B CA  1 
ATOM   8261  C C   . PHE B 1 394 ? -10.321 45.156  -43.391 1.00 43.54  ? 394 PHE B C   1 
ATOM   8262  O O   . PHE B 1 394 ? -11.059 46.061  -43.021 1.00 44.45  ? 394 PHE B O   1 
ATOM   8263  C CB  . PHE B 1 394 ? -11.916 43.228  -43.327 1.00 42.81  ? 394 PHE B CB  1 
ATOM   8264  C CG  . PHE B 1 394 ? -12.171 41.778  -43.011 1.00 41.81  ? 394 PHE B CG  1 
ATOM   8265  C CD1 . PHE B 1 394 ? -12.494 41.375  -41.721 1.00 41.91  ? 394 PHE B CD1 1 
ATOM   8266  C CD2 . PHE B 1 394 ? -12.093 40.817  -44.006 1.00 41.29  ? 394 PHE B CD2 1 
ATOM   8267  C CE1 . PHE B 1 394 ? -12.723 40.031  -41.432 1.00 41.23  ? 394 PHE B CE1 1 
ATOM   8268  C CE2 . PHE B 1 394 ? -12.317 39.476  -43.721 1.00 40.44  ? 394 PHE B CE2 1 
ATOM   8269  C CZ  . PHE B 1 394 ? -12.632 39.084  -42.432 1.00 40.28  ? 394 PHE B CZ  1 
ATOM   8270  N N   . ASN B 1 395 ? -9.317  45.356  -44.237 1.00 42.38  ? 395 ASN B N   1 
ATOM   8271  C CA  . ASN B 1 395 ? -9.147  46.649  -44.888 1.00 43.64  ? 395 ASN B CA  1 
ATOM   8272  C C   . ASN B 1 395 ? -9.923  46.673  -46.211 1.00 44.05  ? 395 ASN B C   1 
ATOM   8273  O O   . ASN B 1 395 ? -9.630  45.902  -47.125 1.00 43.19  ? 395 ASN B O   1 
ATOM   8274  C CB  . ASN B 1 395 ? -7.659  46.975  -45.098 1.00 42.54  ? 395 ASN B CB  1 
ATOM   8275  C CG  . ASN B 1 395 ? -7.437  48.382  -45.651 1.00 44.33  ? 395 ASN B CG  1 
ATOM   8276  O OD1 . ASN B 1 395 ? -8.054  48.775  -46.643 1.00 47.17  ? 395 ASN B OD1 1 
ATOM   8277  N ND2 . ASN B 1 395 ? -6.531  49.134  -45.028 1.00 42.24  ? 395 ASN B ND2 1 
ATOM   8278  N N   . LEU B 1 396 ? -10.917 47.550  -46.305 1.00 44.96  ? 396 LEU B N   1 
ATOM   8279  C CA  . LEU B 1 396 ? -11.825 47.530  -47.456 1.00 46.97  ? 396 LEU B CA  1 
ATOM   8280  C C   . LEU B 1 396 ? -11.152 47.983  -48.751 1.00 48.13  ? 396 LEU B C   1 
ATOM   8281  O O   . LEU B 1 396 ? -11.534 47.555  -49.836 1.00 49.46  ? 396 LEU B O   1 
ATOM   8282  C CB  . LEU B 1 396 ? -13.089 48.342  -47.167 1.00 48.72  ? 396 LEU B CB  1 
ATOM   8283  C CG  . LEU B 1 396 ? -13.908 47.835  -45.971 1.00 48.98  ? 396 LEU B CG  1 
ATOM   8284  C CD1 . LEU B 1 396 ? -15.081 48.753  -45.685 1.00 49.52  ? 396 LEU B CD1 1 
ATOM   8285  C CD2 . LEU B 1 396 ? -14.376 46.396  -46.172 1.00 48.12  ? 396 LEU B CD2 1 
ATOM   8286  N N   . THR B 1 397 ? -10.115 48.807  -48.620 1.00 47.77  ? 397 THR B N   1 
ATOM   8287  C CA  . THR B 1 397 ? -9.404  49.343  -49.770 1.00 47.88  ? 397 THR B CA  1 
ATOM   8288  C C   . THR B 1 397 ? -8.330  48.374  -50.257 1.00 47.37  ? 397 THR B C   1 
ATOM   8289  O O   . THR B 1 397 ? -8.346  47.961  -51.411 1.00 47.90  ? 397 THR B O   1 
ATOM   8290  C CB  . THR B 1 397 ? -8.802  50.734  -49.458 1.00 48.37  ? 397 THR B CB  1 
ATOM   8291  O OG1 . THR B 1 397 ? -9.853  51.631  -49.065 1.00 50.06  ? 397 THR B OG1 1 
ATOM   8292  C CG2 . THR B 1 397 ? -8.073  51.307  -50.673 1.00 47.63  ? 397 THR B CG2 1 
ATOM   8293  N N   . THR B 1 398 ? -7.423  47.988  -49.361 1.00 47.29  ? 398 THR B N   1 
ATOM   8294  C CA  . THR B 1 398 ? -6.289  47.132  -49.721 1.00 45.56  ? 398 THR B CA  1 
ATOM   8295  C C   . THR B 1 398 ? -6.648  45.639  -49.738 1.00 44.97  ? 398 THR B C   1 
ATOM   8296  O O   . THR B 1 398 ? -5.897  44.818  -50.288 1.00 44.09  ? 398 THR B O   1 
ATOM   8297  C CB  . THR B 1 398 ? -5.099  47.350  -48.762 1.00 44.87  ? 398 THR B CB  1 
ATOM   8298  O OG1 . THR B 1 398 ? -5.446  46.861  -47.459 1.00 44.41  ? 398 THR B OG1 1 
ATOM   8299  C CG2 . THR B 1 398 ? -4.740  48.847  -48.670 1.00 42.99  ? 398 THR B CG2 1 
ATOM   8300  N N   . ARG B 1 399 ? -7.782  45.298  -49.114 1.00 43.90  ? 399 ARG B N   1 
ATOM   8301  C CA  . ARG B 1 399 ? -8.271  43.911  -49.023 1.00 43.85  ? 399 ARG B CA  1 
ATOM   8302  C C   . ARG B 1 399 ? -7.421  43.030  -48.111 1.00 44.91  ? 399 ARG B C   1 
ATOM   8303  O O   . ARG B 1 399 ? -7.642  41.814  -48.030 1.00 46.60  ? 399 ARG B O   1 
ATOM   8304  C CB  . ARG B 1 399 ? -8.403  43.263  -50.407 1.00 44.27  ? 399 ARG B CB  1 
ATOM   8305  C CG  . ARG B 1 399 ? -9.419  43.930  -51.315 1.00 46.01  ? 399 ARG B CG  1 
ATOM   8306  C CD  . ARG B 1 399 ? -8.755  44.835  -52.350 1.00 47.23  ? 399 ARG B CD  1 
ATOM   8307  N NE  . ARG B 1 399 ? -9.739  45.682  -53.021 1.00 47.96  ? 399 ARG B NE  1 
ATOM   8308  C CZ  . ARG B 1 399 ? -10.523 45.274  -54.012 1.00 49.16  ? 399 ARG B CZ  1 
ATOM   8309  N NH1 . ARG B 1 399 ? -10.435 44.036  -54.469 1.00 48.51  ? 399 ARG B NH1 1 
ATOM   8310  N NH2 . ARG B 1 399 ? -11.402 46.106  -54.548 1.00 53.03  ? 399 ARG B NH2 1 
ATOM   8311  N N   . GLN B 1 400 ? -6.440  43.643  -47.443 1.00 43.73  ? 400 GLN B N   1 
ATOM   8312  C CA  . GLN B 1 400 ? -5.581  42.942  -46.488 1.00 42.54  ? 400 GLN B CA  1 
ATOM   8313  C C   . GLN B 1 400 ? -6.342  42.558  -45.226 1.00 41.70  ? 400 GLN B C   1 
ATOM   8314  O O   . GLN B 1 400 ? -7.198  43.309  -44.760 1.00 44.49  ? 400 GLN B O   1 
ATOM   8315  C CB  . GLN B 1 400 ? -4.366  43.804  -46.123 1.00 41.90  ? 400 GLN B CB  1 
ATOM   8316  C CG  . GLN B 1 400 ? -3.487  44.171  -47.308 1.00 41.36  ? 400 GLN B CG  1 
ATOM   8317  C CD  . GLN B 1 400 ? -3.148  42.969  -48.171 1.00 42.72  ? 400 GLN B CD  1 
ATOM   8318  O OE1 . GLN B 1 400 ? -3.702  42.794  -49.266 1.00 43.85  ? 400 GLN B OE1 1 
ATOM   8319  N NE2 . GLN B 1 400 ? -2.252  42.120  -47.678 1.00 38.93  ? 400 GLN B NE2 1 
ATOM   8320  N N   . VAL B 1 401 ? -6.034  41.381  -44.688 1.00 39.40  ? 401 VAL B N   1 
ATOM   8321  C CA  . VAL B 1 401 ? -6.626  40.909  -43.442 1.00 38.13  ? 401 VAL B CA  1 
ATOM   8322  C C   . VAL B 1 401 ? -5.535  40.621  -42.390 1.00 38.91  ? 401 VAL B C   1 
ATOM   8323  O O   . VAL B 1 401 ? -4.558  39.904  -42.656 1.00 37.07  ? 401 VAL B O   1 
ATOM   8324  C CB  . VAL B 1 401 ? -7.541  39.678  -43.660 1.00 38.37  ? 401 VAL B CB  1 
ATOM   8325  C CG1 . VAL B 1 401 ? -8.183  39.225  -42.346 1.00 37.26  ? 401 VAL B CG1 1 
ATOM   8326  C CG2 . VAL B 1 401 ? -8.631  40.002  -44.677 1.00 39.96  ? 401 VAL B CG2 1 
ATOM   8327  N N   . ARG B 1 402 ? -5.713  41.225  -41.214 1.00 38.85  ? 402 ARG B N   1 
ATOM   8328  C CA  . ARG B 1 402 ? -4.806  41.101  -40.085 1.00 38.33  ? 402 ARG B CA  1 
ATOM   8329  C C   . ARG B 1 402 ? -5.597  40.513  -38.921 1.00 38.86  ? 402 ARG B C   1 
ATOM   8330  O O   . ARG B 1 402 ? -6.822  40.591  -38.895 1.00 39.20  ? 402 ARG B O   1 
ATOM   8331  C CB  . ARG B 1 402 ? -4.271  42.485  -39.686 1.00 38.42  ? 402 ARG B CB  1 
ATOM   8332  C CG  . ARG B 1 402 ? -3.505  43.232  -40.780 1.00 39.74  ? 402 ARG B CG  1 
ATOM   8333  C CD  . ARG B 1 402 ? -2.060  42.739  -40.932 1.00 40.03  ? 402 ARG B CD  1 
ATOM   8334  N NE  . ARG B 1 402 ? -1.293  42.799  -39.685 1.00 38.97  ? 402 ARG B NE  1 
ATOM   8335  C CZ  . ARG B 1 402 ? -0.523  43.828  -39.328 1.00 39.79  ? 402 ARG B CZ  1 
ATOM   8336  N NH1 . ARG B 1 402 ? -0.409  44.888  -40.122 1.00 42.22  ? 402 ARG B NH1 1 
ATOM   8337  N NH2 . ARG B 1 402 ? 0.146   43.798  -38.185 1.00 36.19  ? 402 ARG B NH2 1 
ATOM   8338  N N   . THR B 1 403 ? -4.900  39.926  -37.960 1.00 39.99  ? 403 THR B N   1 
ATOM   8339  C CA  . THR B 1 403 ? -5.539  39.427  -36.745 1.00 39.99  ? 403 THR B CA  1 
ATOM   8340  C C   . THR B 1 403 ? -5.844  40.609  -35.817 1.00 40.48  ? 403 THR B C   1 
ATOM   8341  O O   . THR B 1 403 ? -5.072  41.554  -35.736 1.00 41.10  ? 403 THR B O   1 
ATOM   8342  C CB  . THR B 1 403 ? -4.613  38.443  -36.026 1.00 41.39  ? 403 THR B CB  1 
ATOM   8343  O OG1 . THR B 1 403 ? -4.013  37.557  -36.984 1.00 42.38  ? 403 THR B OG1 1 
ATOM   8344  C CG2 . THR B 1 403 ? -5.358  37.650  -34.963 1.00 40.92  ? 403 THR B CG2 1 
ATOM   8345  N N   . LEU B 1 404 ? -6.978  40.552  -35.132 1.00 42.12  ? 404 LEU B N   1 
ATOM   8346  C CA  . LEU B 1 404 ? -7.365  41.600  -34.207 1.00 41.60  ? 404 LEU B CA  1 
ATOM   8347  C C   . LEU B 1 404 ? -6.839  41.271  -32.827 1.00 42.71  ? 404 LEU B C   1 
ATOM   8348  O O   . LEU B 1 404 ? -7.065  40.174  -32.297 1.00 39.41  ? 404 LEU B O   1 
ATOM   8349  C CB  . LEU B 1 404 ? -8.888  41.748  -34.162 1.00 41.64  ? 404 LEU B CB  1 
ATOM   8350  C CG  . LEU B 1 404 ? -9.526  42.714  -33.144 1.00 43.27  ? 404 LEU B CG  1 
ATOM   8351  C CD1 . LEU B 1 404 ? -9.054  44.152  -33.327 1.00 42.04  ? 404 LEU B CD1 1 
ATOM   8352  C CD2 . LEU B 1 404 ? -11.052 42.639  -33.202 1.00 42.82  ? 404 LEU B CD2 1 
ATOM   8353  N N   . TYR B 1 405 ? -6.144  42.220  -32.230 1.00 44.89  ? 405 TYR B N   1 
ATOM   8354  C CA  . TYR B 1 405 ? -5.693  42.002  -30.883 1.00 50.20  ? 405 TYR B CA  1 
ATOM   8355  C C   . TYR B 1 405 ? -6.397  42.880  -29.857 1.00 54.93  ? 405 TYR B C   1 
ATOM   8356  O O   . TYR B 1 405 ? -6.183  44.098  -29.811 1.00 56.28  ? 405 TYR B O   1 
ATOM   8357  C CB  . TYR B 1 405 ? -4.159  42.043  -30.786 1.00 46.21  ? 405 TYR B CB  1 
ATOM   8358  C CG  . TYR B 1 405 ? -3.488  40.844  -31.451 1.00 43.34  ? 405 TYR B CG  1 
ATOM   8359  C CD1 . TYR B 1 405 ? -3.392  39.620  -30.785 1.00 42.63  ? 405 TYR B CD1 1 
ATOM   8360  C CD2 . TYR B 1 405 ? -2.974  40.924  -32.753 1.00 41.43  ? 405 TYR B CD2 1 
ATOM   8361  C CE1 . TYR B 1 405 ? -2.789  38.519  -31.378 1.00 38.12  ? 405 TYR B CE1 1 
ATOM   8362  C CE2 . TYR B 1 405 ? -2.356  39.820  -33.348 1.00 39.82  ? 405 TYR B CE2 1 
ATOM   8363  C CZ  . TYR B 1 405 ? -2.266  38.626  -32.645 1.00 38.66  ? 405 TYR B CZ  1 
ATOM   8364  O OH  . TYR B 1 405 ? -1.674  37.521  -33.210 1.00 37.99  ? 405 TYR B OH  1 
ATOM   8365  N N   . LYS B 1 406 ? -7.316  42.241  -29.117 1.00 62.16  ? 406 LYS B N   1 
ATOM   8366  C CA  . LYS B 1 406 ? -7.794  42.694  -27.785 1.00 67.64  ? 406 LYS B CA  1 
ATOM   8367  C C   . LYS B 1 406 ? -7.716  44.238  -27.587 1.00 70.09  ? 406 LYS B C   1 
ATOM   8368  O O   . LYS B 1 406 ? -8.561  44.924  -28.168 1.00 78.42  ? 406 LYS B O   1 
ATOM   8369  C CB  . LYS B 1 406 ? -7.138  41.847  -26.693 1.00 70.58  ? 406 LYS B CB  1 
ATOM   8370  C CG  . LYS B 1 406 ? -5.987  40.980  -27.229 1.00 66.79  ? 406 LYS B CG  1 
ATOM   8371  C CD  . LYS B 1 406 ? -6.382  39.549  -27.575 1.00 64.71  ? 406 LYS B CD  1 
ATOM   8372  C CE  . LYS B 1 406 ? -5.117  38.743  -27.826 1.00 66.05  ? 406 LYS B CE  1 
ATOM   8373  N NZ  . LYS B 1 406 ? -5.056  37.477  -27.052 1.00 63.94  ? 406 LYS B NZ  1 
ATOM   8374  N N   . LEU B 1 407 ? -6.763  44.833  -26.838 1.00 69.96  ? 407 LEU B N   1 
ATOM   8375  C CA  . LEU B 1 407 ? -6.193  44.434  -25.537 1.00 70.27  ? 407 LEU B CA  1 
ATOM   8376  C C   . LEU B 1 407 ? -6.294  45.734  -24.697 1.00 69.70  ? 407 LEU B C   1 
ATOM   8377  O O   . LEU B 1 407 ? -5.474  46.642  -24.872 1.00 69.13  ? 407 LEU B O   1 
ATOM   8378  C CB  . LEU B 1 407 ? -4.691  44.122  -25.675 1.00 73.79  ? 407 LEU B CB  1 
ATOM   8379  C CG  . LEU B 1 407 ? -4.103  42.718  -25.808 1.00 71.78  ? 407 LEU B CG  1 
ATOM   8380  C CD1 . LEU B 1 407 ? -2.700  42.780  -26.380 1.00 71.27  ? 407 LEU B CD1 1 
ATOM   8381  C CD2 . LEU B 1 407 ? -4.111  41.997  -24.473 1.00 72.22  ? 407 LEU B CD2 1 
ATOM   8382  N N   . PRO B 1 408 ? -7.285  45.828  -23.786 1.00 67.97  ? 408 PRO B N   1 
ATOM   8383  C CA  . PRO B 1 408 ? -7.590  47.119  -23.138 1.00 65.44  ? 408 PRO B CA  1 
ATOM   8384  C C   . PRO B 1 408 ? -6.403  47.716  -22.360 1.00 64.90  ? 408 PRO B C   1 
ATOM   8385  O O   . PRO B 1 408 ? -5.470  46.986  -22.021 1.00 61.10  ? 408 PRO B O   1 
ATOM   8386  C CB  . PRO B 1 408 ? -8.741  46.768  -22.189 1.00 62.78  ? 408 PRO B CB  1 
ATOM   8387  C CG  . PRO B 1 408 ? -8.567  45.319  -21.906 1.00 62.83  ? 408 PRO B CG  1 
ATOM   8388  C CD  . PRO B 1 408 ? -8.043  44.721  -23.180 1.00 64.47  ? 408 PRO B CD  1 
ATOM   8389  N N   . PRO B 1 409 ? -6.443  49.043  -22.081 1.00 67.50  ? 409 PRO B N   1 
ATOM   8390  C CA  . PRO B 1 409 ? -5.367  49.768  -21.375 1.00 64.97  ? 409 PRO B CA  1 
ATOM   8391  C C   . PRO B 1 409 ? -4.952  49.123  -20.046 1.00 61.32  ? 409 PRO B C   1 
ATOM   8392  O O   . PRO B 1 409 ? -5.809  48.713  -19.257 1.00 57.88  ? 409 PRO B O   1 
ATOM   8393  C CB  . PRO B 1 409 ? -5.981  51.162  -21.121 1.00 67.14  ? 409 PRO B CB  1 
ATOM   8394  C CG  . PRO B 1 409 ? -7.451  51.010  -21.367 1.00 68.39  ? 409 PRO B CG  1 
ATOM   8395  C CD  . PRO B 1 409 ? -7.565  49.943  -22.414 1.00 69.00  ? 409 PRO B CD  1 
ATOM   8396  N N   . ASN B 1 410 ? -3.641  49.032  -19.819 1.00 59.77  ? 410 ASN B N   1 
ATOM   8397  C CA  . ASN B 1 410 ? -3.094  48.430  -18.595 1.00 57.08  ? 410 ASN B CA  1 
ATOM   8398  C C   . ASN B 1 410 ? -3.589  47.005  -18.337 1.00 54.17  ? 410 ASN B C   1 
ATOM   8399  O O   . ASN B 1 410 ? -3.685  46.565  -17.188 1.00 55.42  ? 410 ASN B O   1 
ATOM   8400  C CB  . ASN B 1 410 ? -3.358  49.331  -17.374 1.00 60.29  ? 410 ASN B CB  1 
ATOM   8401  C CG  . ASN B 1 410 ? -2.556  50.624  -17.418 1.00 65.92  ? 410 ASN B CG  1 
ATOM   8402  O OD1 . ASN B 1 410 ? -1.341  50.610  -17.643 1.00 65.84  ? 410 ASN B OD1 1 
ATOM   8403  N ND2 . ASN B 1 410 ? -3.234  51.750  -17.203 1.00 66.00  ? 410 ASN B ND2 1 
ATOM   8404  N N   . TYR B 1 411 ? -3.907  46.281  -19.407 1.00 50.61  ? 411 TYR B N   1 
ATOM   8405  C CA  . TYR B 1 411 ? -4.249  44.874  -19.270 1.00 46.10  ? 411 TYR B CA  1 
ATOM   8406  C C   . TYR B 1 411 ? -3.008  44.071  -18.901 1.00 41.36  ? 411 TYR B C   1 
ATOM   8407  O O   . TYR B 1 411 ? -1.926  44.316  -19.421 1.00 40.52  ? 411 TYR B O   1 
ATOM   8408  C CB  . TYR B 1 411 ? -4.853  44.352  -20.559 1.00 45.16  ? 411 TYR B CB  1 
ATOM   8409  C CG  . TYR B 1 411 ? -5.363  42.934  -20.500 1.00 43.42  ? 411 TYR B CG  1 
ATOM   8410  C CD1 . TYR B 1 411 ? -6.625  42.648  -20.006 1.00 44.34  ? 411 TYR B CD1 1 
ATOM   8411  C CD2 . TYR B 1 411 ? -4.600  41.884  -20.988 1.00 40.80  ? 411 TYR B CD2 1 
ATOM   8412  C CE1 . TYR B 1 411 ? -7.105  41.346  -19.984 1.00 42.89  ? 411 TYR B CE1 1 
ATOM   8413  C CE2 . TYR B 1 411 ? -5.069  40.584  -20.959 1.00 39.63  ? 411 TYR B CE2 1 
ATOM   8414  C CZ  . TYR B 1 411 ? -6.315  40.323  -20.459 1.00 39.29  ? 411 TYR B CZ  1 
ATOM   8415  O OH  . TYR B 1 411 ? -6.775  39.038  -20.444 1.00 39.01  ? 411 TYR B OH  1 
ATOM   8416  N N   . GLU B 1 412 ? -3.164  43.142  -17.971 1.00 38.05  ? 412 GLU B N   1 
ATOM   8417  C CA  . GLU B 1 412 ? -2.083  42.247  -17.624 1.00 36.45  ? 412 GLU B CA  1 
ATOM   8418  C C   . GLU B 1 412 ? -2.108  41.041  -18.545 1.00 35.72  ? 412 GLU B C   1 
ATOM   8419  O O   . GLU B 1 412 ? -3.020  40.212  -18.500 1.00 37.13  ? 412 GLU B O   1 
ATOM   8420  C CB  . GLU B 1 412 ? -2.136  41.849  -16.149 1.00 37.07  ? 412 GLU B CB  1 
ATOM   8421  C CG  . GLU B 1 412 ? -1.493  42.883  -15.244 1.00 39.51  ? 412 GLU B CG  1 
ATOM   8422  C CD  . GLU B 1 412 ? -1.591  42.534  -13.774 1.00 41.83  ? 412 GLU B CD  1 
ATOM   8423  O OE1 . GLU B 1 412 ? -0.909  41.585  -13.318 1.00 41.03  ? 412 GLU B OE1 1 
ATOM   8424  O OE2 . GLU B 1 412 ? -2.336  43.235  -13.065 1.00 44.62  ? 412 GLU B OE2 1 
ATOM   8425  N N   . ILE B 1 413 ? -1.086  40.949  -19.383 1.00 34.41  ? 413 ILE B N   1 
ATOM   8426  C CA  . ILE B 1 413 ? -1.123  40.055  -20.521 1.00 35.18  ? 413 ILE B CA  1 
ATOM   8427  C C   . ILE B 1 413 ? -1.126  38.572  -20.062 1.00 34.75  ? 413 ILE B C   1 
ATOM   8428  O O   . ILE B 1 413 ? -1.655  37.704  -20.747 1.00 33.83  ? 413 ILE B O   1 
ATOM   8429  C CB  . ILE B 1 413 ? -0.019  40.430  -21.570 1.00 34.35  ? 413 ILE B CB  1 
ATOM   8430  C CG1 . ILE B 1 413 ? -0.217  39.691  -22.893 1.00 36.94  ? 413 ILE B CG1 1 
ATOM   8431  C CG2 . ILE B 1 413 ? 1.379   40.195  -21.031 1.00 35.04  ? 413 ILE B CG2 1 
ATOM   8432  C CD1 . ILE B 1 413 ? -1.420  40.142  -23.670 1.00 36.92  ? 413 ILE B CD1 1 
ATOM   8433  N N   . ARG B 1 414 ? -0.611  38.317  -18.857 1.00 35.01  ? 414 ARG B N   1 
ATOM   8434  C CA  . ARG B 1 414 ? -0.621  36.967  -18.280 1.00 33.90  ? 414 ARG B CA  1 
ATOM   8435  C C   . ARG B 1 414 ? -2.029  36.390  -18.189 1.00 34.28  ? 414 ARG B C   1 
ATOM   8436  O O   . ARG B 1 414 ? -2.188  35.179  -18.206 1.00 35.87  ? 414 ARG B O   1 
ATOM   8437  C CB  . ARG B 1 414 ? 0.068   36.927  -16.912 1.00 33.16  ? 414 ARG B CB  1 
ATOM   8438  C CG  . ARG B 1 414 ? -0.723  37.585  -15.777 1.00 32.26  ? 414 ARG B CG  1 
ATOM   8439  C CD  . ARG B 1 414 ? 0.079   37.651  -14.477 1.00 31.69  ? 414 ARG B CD  1 
ATOM   8440  N NE  . ARG B 1 414 ? -0.491  38.636  -13.558 1.00 30.09  ? 414 ARG B NE  1 
ATOM   8441  C CZ  . ARG B 1 414 ? -1.590  38.445  -12.821 1.00 29.71  ? 414 ARG B CZ  1 
ATOM   8442  N NH1 . ARG B 1 414 ? -2.265  37.291  -12.852 1.00 29.97  ? 414 ARG B NH1 1 
ATOM   8443  N NH2 . ARG B 1 414 ? -2.028  39.418  -12.071 1.00 28.35  ? 414 ARG B NH2 1 
ATOM   8444  N N   . HIS B 1 415 ? -3.045  37.256  -18.100 1.00 37.51  ? 415 HIS B N   1 
ATOM   8445  C CA  . HIS B 1 415 ? -4.449  36.804  -18.074 1.00 37.85  ? 415 HIS B CA  1 
ATOM   8446  C C   . HIS B 1 415 ? -4.884  36.095  -19.335 1.00 37.76  ? 415 HIS B C   1 
ATOM   8447  O O   . HIS B 1 415 ? -5.796  35.276  -19.292 1.00 41.80  ? 415 HIS B O   1 
ATOM   8448  C CB  . HIS B 1 415 ? -5.394  37.957  -17.802 1.00 38.66  ? 415 HIS B CB  1 
ATOM   8449  C CG  . HIS B 1 415 ? -5.340  38.472  -16.395 1.00 42.02  ? 415 HIS B CG  1 
ATOM   8450  N ND1 . HIS B 1 415 ? -5.386  37.657  -15.320 1.00 41.88  ? 415 HIS B ND1 1 
ATOM   8451  C CD2 . HIS B 1 415 ? -5.291  39.778  -15.900 1.00 39.24  ? 415 HIS B CD2 1 
ATOM   8452  C CE1 . HIS B 1 415 ? -5.323  38.400  -14.201 1.00 42.94  ? 415 HIS B CE1 1 
ATOM   8453  N NE2 . HIS B 1 415 ? -5.273  39.697  -14.561 1.00 41.02  ? 415 HIS B NE2 1 
ATOM   8454  N N   . LYS B 1 416 ? -4.265  36.413  -20.471 1.00 37.99  ? 416 LYS B N   1 
ATOM   8455  C CA  . LYS B 1 416 ? -4.568  35.717  -21.739 1.00 38.55  ? 416 LYS B CA  1 
ATOM   8456  C C   . LYS B 1 416 ? -4.281  34.211  -21.726 1.00 37.08  ? 416 LYS B C   1 
ATOM   8457  O O   . LYS B 1 416 ? -4.845  33.466  -22.535 1.00 39.54  ? 416 LYS B O   1 
ATOM   8458  C CB  . LYS B 1 416 ? -3.813  36.350  -22.916 1.00 42.05  ? 416 LYS B CB  1 
ATOM   8459  C CG  . LYS B 1 416 ? -4.527  37.522  -23.581 1.00 46.64  ? 416 LYS B CG  1 
ATOM   8460  C CD  . LYS B 1 416 ? -5.949  37.169  -23.999 1.00 45.44  ? 416 LYS B CD  1 
ATOM   8461  C CE  . LYS B 1 416 ? -6.757  38.428  -24.277 1.00 51.44  ? 416 LYS B CE  1 
ATOM   8462  N NZ  . LYS B 1 416 ? -8.042  38.128  -24.984 1.00 59.04  ? 416 LYS B NZ  1 
ATOM   8463  N N   . PHE B 1 417 ? -3.430  33.757  -20.809 1.00 33.67  ? 417 PHE B N   1 
ATOM   8464  C CA  . PHE B 1 417 ? -2.852  32.427  -20.932 1.00 34.00  ? 417 PHE B CA  1 
ATOM   8465  C C   . PHE B 1 417 ? -3.317  31.463  -19.858 1.00 35.22  ? 417 PHE B C   1 
ATOM   8466  O O   . PHE B 1 417 ? -3.629  31.866  -18.744 1.00 39.35  ? 417 PHE B O   1 
ATOM   8467  C CB  . PHE B 1 417 ? -1.318  32.522  -20.979 1.00 33.93  ? 417 PHE B CB  1 
ATOM   8468  C CG  . PHE B 1 417 ? -0.810  33.501  -22.006 1.00 34.42  ? 417 PHE B CG  1 
ATOM   8469  C CD1 . PHE B 1 417 ? -1.120  33.331  -23.363 1.00 35.83  ? 417 PHE B CD1 1 
ATOM   8470  C CD2 . PHE B 1 417 ? -0.096  34.624  -21.623 1.00 33.63  ? 417 PHE B CD2 1 
ATOM   8471  C CE1 . PHE B 1 417 ? -0.672  34.237  -24.309 1.00 35.08  ? 417 PHE B CE1 1 
ATOM   8472  C CE2 . PHE B 1 417 ? 0.346   35.540  -22.562 1.00 32.43  ? 417 PHE B CE2 1 
ATOM   8473  C CZ  . PHE B 1 417 ? 0.055   35.349  -23.904 1.00 34.21  ? 417 PHE B CZ  1 
ATOM   8474  N N   . LYS B 1 418 ? -3.379  30.184  -20.209 1.00 35.46  ? 418 LYS B N   1 
ATOM   8475  C CA  . LYS B 1 418 ? -3.693  29.138  -19.267 1.00 35.45  ? 418 LYS B CA  1 
ATOM   8476  C C   . LYS B 1 418 ? -2.496  28.200  -19.124 1.00 36.08  ? 418 LYS B C   1 
ATOM   8477  O O   . LYS B 1 418 ? -2.331  27.255  -19.901 1.00 36.99  ? 418 LYS B O   1 
ATOM   8478  C CB  . LYS B 1 418 ? -4.925  28.361  -19.732 1.00 38.13  ? 418 LYS B CB  1 
ATOM   8479  C CG  . LYS B 1 418 ? -5.390  27.305  -18.748 1.00 39.44  ? 418 LYS B CG  1 
ATOM   8480  C CD  . LYS B 1 418 ? -6.630  26.573  -19.251 1.00 40.77  ? 418 LYS B CD  1 
ATOM   8481  C CE  . LYS B 1 418 ? -6.974  25.418  -18.313 1.00 40.97  ? 418 LYS B CE  1 
ATOM   8482  N NZ  . LYS B 1 418 ? -8.395  24.996  -18.420 1.00 43.49  ? 418 LYS B NZ  1 
ATOM   8483  N N   . LEU B 1 419 ? -1.673  28.446  -18.110 1.00 34.65  ? 419 LEU B N   1 
ATOM   8484  C CA  . LEU B 1 419 ? -0.467  27.664  -17.907 1.00 32.90  ? 419 LEU B CA  1 
ATOM   8485  C C   . LEU B 1 419 ? -0.690  26.430  -17.049 1.00 32.91  ? 419 LEU B C   1 
ATOM   8486  O O   . LEU B 1 419 ? 0.117   25.504  -17.075 1.00 33.16  ? 419 LEU B O   1 
ATOM   8487  C CB  . LEU B 1 419 ? 0.604   28.522  -17.254 1.00 34.36  ? 419 LEU B CB  1 
ATOM   8488  C CG  . LEU B 1 419 ? 1.021   29.806  -17.961 1.00 36.34  ? 419 LEU B CG  1 
ATOM   8489  C CD1 . LEU B 1 419 ? 2.147   30.458  -17.179 1.00 34.85  ? 419 LEU B CD1 1 
ATOM   8490  C CD2 . LEU B 1 419 ? 1.449   29.512  -19.392 1.00 35.87  ? 419 LEU B CD2 1 
ATOM   8491  N N   . TRP B 1 420 ? -1.757  26.455  -16.250 1.00 32.52  ? 420 TRP B N   1 
ATOM   8492  C CA  . TRP B 1 420 ? -2.025  25.426  -15.245 1.00 33.27  ? 420 TRP B CA  1 
ATOM   8493  C C   . TRP B 1 420 ? -3.262  24.705  -15.602 1.00 32.97  ? 420 TRP B C   1 
ATOM   8494  O O   . TRP B 1 420 ? -4.268  25.324  -15.891 1.00 31.89  ? 420 TRP B O   1 
ATOM   8495  C CB  . TRP B 1 420 ? -2.198  26.045  -13.855 1.00 32.94  ? 420 TRP B CB  1 
ATOM   8496  C CG  . TRP B 1 420 ? -1.095  26.996  -13.511 1.00 31.84  ? 420 TRP B CG  1 
ATOM   8497  C CD1 . TRP B 1 420 ? -1.021  28.344  -13.819 1.00 30.22  ? 420 TRP B CD1 1 
ATOM   8498  C CD2 . TRP B 1 420 ? 0.149   26.684  -12.831 1.00 31.59  ? 420 TRP B CD2 1 
ATOM   8499  N NE1 . TRP B 1 420 ? 0.165   28.867  -13.384 1.00 30.55  ? 420 TRP B NE1 1 
ATOM   8500  C CE2 . TRP B 1 420 ? 0.900   27.918  -12.764 1.00 32.08  ? 420 TRP B CE2 1 
ATOM   8501  C CE3 . TRP B 1 420 ? 0.678   25.547  -12.252 1.00 35.71  ? 420 TRP B CE3 1 
ATOM   8502  C CZ2 . TRP B 1 420 ? 2.137   27.991  -12.154 1.00 34.43  ? 420 TRP B CZ2 1 
ATOM   8503  C CZ3 . TRP B 1 420 ? 1.936   25.629  -11.639 1.00 36.28  ? 420 TRP B CZ3 1 
ATOM   8504  C CH2 . TRP B 1 420 ? 2.644   26.818  -11.601 1.00 35.57  ? 420 TRP B CH2 1 
ATOM   8505  N N   . ASN B 1 421 ? -3.183  23.379  -15.624 1.00 35.01  ? 421 ASN B N   1 
ATOM   8506  C CA  . ASN B 1 421 ? -4.344  22.558  -15.851 1.00 37.50  ? 421 ASN B CA  1 
ATOM   8507  C C   . ASN B 1 421 ? -4.459  21.576  -14.702 1.00 39.16  ? 421 ASN B C   1 
ATOM   8508  O O   . ASN B 1 421 ? -3.599  20.705  -14.522 1.00 39.58  ? 421 ASN B O   1 
ATOM   8509  C CB  . ASN B 1 421 ? -4.264  21.834  -17.213 1.00 38.62  ? 421 ASN B CB  1 
ATOM   8510  C CG  . ASN B 1 421 ? -5.433  20.864  -17.441 1.00 42.05  ? 421 ASN B CG  1 
ATOM   8511  O OD1 . ASN B 1 421 ? -6.398  20.826  -16.662 1.00 42.98  ? 421 ASN B OD1 1 
ATOM   8512  N ND2 . ASN B 1 421 ? -5.337  20.057  -18.501 1.00 43.83  ? 421 ASN B ND2 1 
ATOM   8513  N N   . PHE B 1 422 ? -5.525  21.724  -13.918 1.00 39.32  ? 422 PHE B N   1 
ATOM   8514  C CA  . PHE B 1 422 ? -5.696  20.943  -12.702 1.00 38.15  ? 422 PHE B CA  1 
ATOM   8515  C C   . PHE B 1 422 ? -5.935  19.459  -12.984 1.00 40.87  ? 422 PHE B C   1 
ATOM   8516  O O   . PHE B 1 422 ? -5.770  18.617  -12.095 1.00 41.78  ? 422 PHE B O   1 
ATOM   8517  C CB  . PHE B 1 422 ? -6.822  21.522  -11.843 1.00 36.90  ? 422 PHE B CB  1 
ATOM   8518  C CG  . PHE B 1 422 ? -6.818  21.023  -10.434 1.00 36.40  ? 422 PHE B CG  1 
ATOM   8519  C CD1 . PHE B 1 422 ? -5.887  21.496  -9.523  1.00 33.96  ? 422 PHE B CD1 1 
ATOM   8520  C CD2 . PHE B 1 422 ? -7.738  20.048  -10.021 1.00 38.13  ? 422 PHE B CD2 1 
ATOM   8521  C CE1 . PHE B 1 422 ? -5.867  21.022  -8.216  1.00 34.94  ? 422 PHE B CE1 1 
ATOM   8522  C CE2 . PHE B 1 422 ? -7.730  19.570  -8.713  1.00 37.38  ? 422 PHE B CE2 1 
ATOM   8523  C CZ  . PHE B 1 422 ? -6.786  20.059  -7.810  1.00 36.38  ? 422 PHE B CZ  1 
ATOM   8524  N N   . ASN B 1 423 ? -6.304  19.152  -14.225 1.00 42.86  ? 423 ASN B N   1 
ATOM   8525  C CA  . ASN B 1 423 ? -6.529  17.774  -14.670 1.00 44.01  ? 423 ASN B CA  1 
ATOM   8526  C C   . ASN B 1 423 ? -5.297  17.130  -15.308 1.00 42.28  ? 423 ASN B C   1 
ATOM   8527  O O   . ASN B 1 423 ? -5.319  15.950  -15.672 1.00 42.56  ? 423 ASN B O   1 
ATOM   8528  C CB  . ASN B 1 423 ? -7.708  17.725  -15.652 1.00 48.07  ? 423 ASN B CB  1 
ATOM   8529  C CG  . ASN B 1 423 ? -8.993  18.280  -15.053 1.00 53.19  ? 423 ASN B CG  1 
ATOM   8530  O OD1 . ASN B 1 423 ? -9.373  17.946  -13.916 1.00 55.47  ? 423 ASN B OD1 1 
ATOM   8531  N ND2 . ASN B 1 423 ? -9.669  19.139  -15.812 1.00 54.98  ? 423 ASN B ND2 1 
ATOM   8532  N N   . ASN B 1 424 ? -4.231  17.912  -15.466 1.00 40.06  ? 424 ASN B N   1 
ATOM   8533  C CA  . ASN B 1 424 ? -2.991  17.405  -16.052 1.00 36.95  ? 424 ASN B CA  1 
ATOM   8534  C C   . ASN B 1 424 ? -1.782  18.082  -15.417 1.00 34.59  ? 424 ASN B C   1 
ATOM   8535  O O   . ASN B 1 424 ? -1.125  18.893  -16.040 1.00 32.83  ? 424 ASN B O   1 
ATOM   8536  C CB  . ASN B 1 424 ? -3.004  17.584  -17.580 1.00 36.24  ? 424 ASN B CB  1 
ATOM   8537  C CG  . ASN B 1 424 ? -1.917  16.775  -18.281 1.00 36.38  ? 424 ASN B CG  1 
ATOM   8538  O OD1 . ASN B 1 424 ? -1.299  15.883  -17.691 1.00 37.10  ? 424 ASN B OD1 1 
ATOM   8539  N ND2 . ASN B 1 424 ? -1.697  17.071  -19.543 1.00 35.33  ? 424 ASN B ND2 1 
ATOM   8540  N N   . GLN B 1 425 ? -1.510  17.729  -14.163 1.00 35.70  ? 425 GLN B N   1 
ATOM   8541  C CA  . GLN B 1 425 ? -0.553  18.458  -13.302 1.00 34.56  ? 425 GLN B CA  1 
ATOM   8542  C C   . GLN B 1 425 ? 0.893   18.017  -13.531 1.00 34.91  ? 425 GLN B C   1 
ATOM   8543  O O   . GLN B 1 425 ? 1.169   16.838  -13.858 1.00 33.96  ? 425 GLN B O   1 
ATOM   8544  C CB  . GLN B 1 425 ? -0.926  18.317  -11.806 1.00 34.28  ? 425 GLN B CB  1 
ATOM   8545  C CG  . GLN B 1 425 ? -2.432  18.336  -11.541 1.00 35.62  ? 425 GLN B CG  1 
ATOM   8546  C CD  . GLN B 1 425 ? -2.837  18.575  -10.074 1.00 37.77  ? 425 GLN B CD  1 
ATOM   8547  O OE1 . GLN B 1 425 ? -2.009  18.610  -9.146  1.00 36.59  ? 425 GLN B OE1 1 
ATOM   8548  N NE2 . GLN B 1 425 ? -4.133  18.723  -9.868  1.00 38.23  ? 425 GLN B NE2 1 
ATOM   8549  N N   . ILE B 1 426 ? 1.806   18.966  -13.347 1.00 32.22  ? 426 ILE B N   1 
ATOM   8550  C CA  . ILE B 1 426 ? 3.216   18.780  -13.646 1.00 32.39  ? 426 ILE B CA  1 
ATOM   8551  C C   . ILE B 1 426 ? 4.005   19.018  -12.364 1.00 33.48  ? 426 ILE B C   1 
ATOM   8552  O O   . ILE B 1 426 ? 3.872   20.078  -11.748 1.00 31.86  ? 426 ILE B O   1 
ATOM   8553  C CB  . ILE B 1 426 ? 3.663   19.795  -14.723 1.00 31.72  ? 426 ILE B CB  1 
ATOM   8554  C CG1 . ILE B 1 426 ? 2.788   19.643  -15.975 1.00 30.96  ? 426 ILE B CG1 1 
ATOM   8555  C CG2 . ILE B 1 426 ? 5.154   19.655  -15.022 1.00 32.02  ? 426 ILE B CG2 1 
ATOM   8556  C CD1 . ILE B 1 426 ? 3.216   20.486  -17.155 1.00 31.64  ? 426 ILE B CD1 1 
ATOM   8557  N N   . SER B 1 427 ? 4.792   18.030  -11.929 1.00 35.29  ? 427 SER B N   1 
ATOM   8558  C CA  . SER B 1 427 ? 5.455   18.142  -10.619 1.00 36.92  ? 427 SER B CA  1 
ATOM   8559  C C   . SER B 1 427 ? 6.464   19.280  -10.630 1.00 36.72  ? 427 SER B C   1 
ATOM   8560  O O   . SER B 1 427 ? 6.912   19.713  -11.701 1.00 37.44  ? 427 SER B O   1 
ATOM   8561  C CB  . SER B 1 427 ? 6.102   16.821  -10.173 1.00 36.77  ? 427 SER B CB  1 
ATOM   8562  O OG  . SER B 1 427 ? 7.163   16.475  -11.020 1.00 39.45  ? 427 SER B OG  1 
ATOM   8563  N N   . ASP B 1 428 ? 6.806   19.772  -9.446  1.00 35.88  ? 428 ASP B N   1 
ATOM   8564  C CA  . ASP B 1 428 ? 7.646   20.954  -9.329  1.00 38.46  ? 428 ASP B CA  1 
ATOM   8565  C C   . ASP B 1 428 ? 9.072   20.764  -9.850  1.00 40.17  ? 428 ASP B C   1 
ATOM   8566  O O   . ASP B 1 428 ? 9.813   21.740  -9.984  1.00 44.01  ? 428 ASP B O   1 
ATOM   8567  C CB  . ASP B 1 428 ? 7.657   21.483  -7.885  1.00 39.22  ? 428 ASP B CB  1 
ATOM   8568  C CG  . ASP B 1 428 ? 8.146   20.446  -6.869  1.00 39.80  ? 428 ASP B CG  1 
ATOM   8569  O OD1 . ASP B 1 428 ? 8.776   19.441  -7.258  1.00 43.77  ? 428 ASP B OD1 1 
ATOM   8570  O OD2 . ASP B 1 428 ? 7.929   20.657  -5.667  1.00 39.37  ? 428 ASP B OD2 1 
ATOM   8571  N N   . ASP B 1 429 ? 9.450   19.520  -10.140 1.00 40.14  ? 429 ASP B N   1 
ATOM   8572  C CA  . ASP B 1 429 ? 10.795  19.220  -10.645 1.00 40.75  ? 429 ASP B CA  1 
ATOM   8573  C C   . ASP B 1 429 ? 10.843  18.948  -12.149 1.00 39.58  ? 429 ASP B C   1 
ATOM   8574  O O   . ASP B 1 429 ? 11.871  18.517  -12.680 1.00 40.36  ? 429 ASP B O   1 
ATOM   8575  C CB  . ASP B 1 429 ? 11.439  18.068  -9.855  1.00 45.43  ? 429 ASP B CB  1 
ATOM   8576  C CG  . ASP B 1 429 ? 10.704  16.738  -10.033 1.00 49.06  ? 429 ASP B CG  1 
ATOM   8577  O OD1 . ASP B 1 429 ? 9.990   16.553  -11.040 1.00 49.39  ? 429 ASP B OD1 1 
ATOM   8578  O OD2 . ASP B 1 429 ? 10.860  15.858  -9.160  1.00 55.82  ? 429 ASP B OD2 1 
ATOM   8579  N N   . ASN B 1 430 ? 9.732   19.206  -12.833 1.00 37.54  ? 430 ASN B N   1 
ATOM   8580  C CA  . ASN B 1 430 ? 9.703   19.167  -14.281 1.00 36.21  ? 430 ASN B CA  1 
ATOM   8581  C C   . ASN B 1 430 ? 9.353   20.515  -14.918 1.00 34.47  ? 430 ASN B C   1 
ATOM   8582  O O   . ASN B 1 430 ? 8.349   20.631  -15.611 1.00 34.12  ? 430 ASN B O   1 
ATOM   8583  C CB  . ASN B 1 430 ? 8.742   18.080  -14.764 1.00 38.69  ? 430 ASN B CB  1 
ATOM   8584  C CG  . ASN B 1 430 ? 9.126   17.523  -16.127 1.00 42.81  ? 430 ASN B CG  1 
ATOM   8585  O OD1 . ASN B 1 430 ? 9.852   18.168  -16.907 1.00 44.28  ? 430 ASN B OD1 1 
ATOM   8586  N ND2 . ASN B 1 430 ? 8.632   16.314  -16.434 1.00 45.59  ? 430 ASN B ND2 1 
ATOM   8587  N N   . PRO B 1 431 ? 10.188  21.541  -14.688 1.00 33.95  ? 431 PRO B N   1 
ATOM   8588  C CA  . PRO B 1 431 ? 9.961   22.836  -15.328 1.00 33.30  ? 431 PRO B CA  1 
ATOM   8589  C C   . PRO B 1 431 ? 10.009  22.801  -16.868 1.00 33.45  ? 431 PRO B C   1 
ATOM   8590  O O   . PRO B 1 431 ? 9.189   23.459  -17.527 1.00 33.27  ? 431 PRO B O   1 
ATOM   8591  C CB  . PRO B 1 431 ? 11.083  23.720  -14.750 1.00 33.99  ? 431 PRO B CB  1 
ATOM   8592  C CG  . PRO B 1 431 ? 12.114  22.767  -14.241 1.00 33.66  ? 431 PRO B CG  1 
ATOM   8593  C CD  . PRO B 1 431 ? 11.348  21.573  -13.776 1.00 33.51  ? 431 PRO B CD  1 
ATOM   8594  N N   . ALA B 1 432 ? 10.935  22.026  -17.438 1.00 33.31  ? 432 ALA B N   1 
ATOM   8595  C CA  . ALA B 1 432 ? 11.044  21.896  -18.898 1.00 32.07  ? 432 ALA B CA  1 
ATOM   8596  C C   . ALA B 1 432 ? 9.723   21.413  -19.547 1.00 32.04  ? 432 ALA B C   1 
ATOM   8597  O O   . ALA B 1 432 ? 9.289   21.939  -20.573 1.00 30.53  ? 432 ALA B O   1 
ATOM   8598  C CB  . ALA B 1 432 ? 12.204  20.973  -19.258 1.00 32.65  ? 432 ALA B CB  1 
ATOM   8599  N N   . ARG B 1 433 ? 9.069   20.440  -18.921 1.00 33.61  ? 433 ARG B N   1 
ATOM   8600  C CA  . ARG B 1 433 ? 7.773   19.976  -19.407 1.00 35.07  ? 433 ARG B CA  1 
ATOM   8601  C C   . ARG B 1 433 ? 6.714   21.098  -19.405 1.00 34.44  ? 433 ARG B C   1 
ATOM   8602  O O   . ARG B 1 433 ? 5.979   21.274  -20.372 1.00 33.75  ? 433 ARG B O   1 
ATOM   8603  C CB  . ARG B 1 433 ? 7.320   18.732  -18.625 1.00 36.07  ? 433 ARG B CB  1 
ATOM   8604  C CG  . ARG B 1 433 ? 5.808   18.520  -18.554 1.00 37.80  ? 433 ARG B CG  1 
ATOM   8605  C CD  . ARG B 1 433 ? 5.426   17.088  -18.867 1.00 37.39  ? 433 ARG B CD  1 
ATOM   8606  N NE  . ARG B 1 433 ? 4.548   16.514  -17.854 1.00 40.80  ? 433 ARG B NE  1 
ATOM   8607  C CZ  . ARG B 1 433 ? 3.215   16.499  -17.900 1.00 40.05  ? 433 ARG B CZ  1 
ATOM   8608  N NH1 . ARG B 1 433 ? 2.554   17.052  -18.909 1.00 42.35  ? 433 ARG B NH1 1 
ATOM   8609  N NH2 . ARG B 1 433 ? 2.547   15.912  -16.930 1.00 38.86  ? 433 ARG B NH2 1 
ATOM   8610  N N   . PHE B 1 434 ? 6.668   21.860  -18.315 1.00 34.14  ? 434 PHE B N   1 
ATOM   8611  C CA  . PHE B 1 434 ? 5.759   23.004  -18.179 1.00 32.41  ? 434 PHE B CA  1 
ATOM   8612  C C   . PHE B 1 434 ? 6.001   24.028  -19.288 1.00 31.41  ? 434 PHE B C   1 
ATOM   8613  O O   . PHE B 1 434 ? 5.061   24.470  -19.957 1.00 29.84  ? 434 PHE B O   1 
ATOM   8614  C CB  . PHE B 1 434 ? 5.954   23.636  -16.789 1.00 31.58  ? 434 PHE B CB  1 
ATOM   8615  C CG  . PHE B 1 434 ? 4.989   24.745  -16.455 1.00 30.70  ? 434 PHE B CG  1 
ATOM   8616  C CD1 . PHE B 1 434 ? 3.733   24.463  -15.926 1.00 30.53  ? 434 PHE B CD1 1 
ATOM   8617  C CD2 . PHE B 1 434 ? 5.380   26.076  -16.564 1.00 30.78  ? 434 PHE B CD2 1 
ATOM   8618  C CE1 . PHE B 1 434 ? 2.862   25.490  -15.566 1.00 31.06  ? 434 PHE B CE1 1 
ATOM   8619  C CE2 . PHE B 1 434 ? 4.513   27.110  -16.200 1.00 30.42  ? 434 PHE B CE2 1 
ATOM   8620  C CZ  . PHE B 1 434 ? 3.249   26.820  -15.720 1.00 29.98  ? 434 PHE B CZ  1 
ATOM   8621  N N   . LEU B 1 435 ? 7.263   24.396  -19.486 1.00 31.98  ? 435 LEU B N   1 
ATOM   8622  C CA  . LEU B 1 435 ? 7.616   25.336  -20.544 1.00 32.41  ? 435 LEU B CA  1 
ATOM   8623  C C   . LEU B 1 435 ? 7.270   24.796  -21.934 1.00 33.32  ? 435 LEU B C   1 
ATOM   8624  O O   . LEU B 1 435 ? 6.681   25.509  -22.765 1.00 33.78  ? 435 LEU B O   1 
ATOM   8625  C CB  . LEU B 1 435 ? 9.083   25.725  -20.460 1.00 32.13  ? 435 LEU B CB  1 
ATOM   8626  C CG  . LEU B 1 435 ? 9.528   26.725  -21.529 1.00 32.88  ? 435 LEU B CG  1 
ATOM   8627  C CD1 . LEU B 1 435 ? 8.768   28.043  -21.425 1.00 31.25  ? 435 LEU B CD1 1 
ATOM   8628  C CD2 . LEU B 1 435 ? 11.021  26.944  -21.410 1.00 32.96  ? 435 LEU B CD2 1 
ATOM   8629  N N   . GLN B 1 436 ? 7.604   23.531  -22.177 1.00 32.95  ? 436 GLN B N   1 
ATOM   8630  C CA  . GLN B 1 436 ? 7.268   22.907  -23.443 1.00 33.64  ? 436 GLN B CA  1 
ATOM   8631  C C   . GLN B 1 436 ? 5.771   22.881  -23.659 1.00 34.04  ? 436 GLN B C   1 
ATOM   8632  O O   . GLN B 1 436 ? 5.288   23.263  -24.727 1.00 35.02  ? 436 GLN B O   1 
ATOM   8633  C CB  . GLN B 1 436 ? 7.859   21.494  -23.549 1.00 35.48  ? 436 GLN B CB  1 
ATOM   8634  C CG  . GLN B 1 436 ? 9.361   21.472  -23.811 1.00 35.65  ? 436 GLN B CG  1 
ATOM   8635  C CD  . GLN B 1 436 ? 9.955   20.092  -23.664 1.00 38.41  ? 436 GLN B CD  1 
ATOM   8636  O OE1 . GLN B 1 436 ? 9.526   19.301  -22.828 1.00 41.70  ? 436 GLN B OE1 1 
ATOM   8637  N NE2 . GLN B 1 436 ? 10.933  19.785  -24.494 1.00 40.92  ? 436 GLN B NE2 1 
ATOM   8638  N N   . LYS B 1 437 ? 5.027   22.440  -22.647 1.00 34.88  ? 437 LYS B N   1 
ATOM   8639  C CA  . LYS B 1 437 ? 3.571   22.400  -22.746 1.00 34.59  ? 437 LYS B CA  1 
ATOM   8640  C C   . LYS B 1 437 ? 3.025   23.797  -23.087 1.00 32.49  ? 437 LYS B C   1 
ATOM   8641  O O   . LYS B 1 437 ? 2.121   23.932  -23.902 1.00 35.17  ? 437 LYS B O   1 
ATOM   8642  C CB  . LYS B 1 437 ? 2.949   21.855  -21.457 1.00 35.62  ? 437 LYS B CB  1 
ATOM   8643  C CG  . LYS B 1 437 ? 1.491   21.446  -21.585 1.00 39.49  ? 437 LYS B CG  1 
ATOM   8644  C CD  . LYS B 1 437 ? 0.857   21.321  -20.205 1.00 45.46  ? 437 LYS B CD  1 
ATOM   8645  C CE  . LYS B 1 437 ? -0.660  21.270  -20.282 1.00 50.70  ? 437 LYS B CE  1 
ATOM   8646  N NZ  . LYS B 1 437 ? -1.169  19.902  -20.604 1.00 54.55  ? 437 LYS B NZ  1 
ATOM   8647  N N   . ALA B 1 438 ? 3.618   24.833  -22.519 1.00 28.98  ? 438 ALA B N   1 
ATOM   8648  C CA  . ALA B 1 438 ? 3.128   26.183  -22.766 1.00 28.49  ? 438 ALA B CA  1 
ATOM   8649  C C   . ALA B 1 438 ? 3.451   26.710  -24.179 1.00 30.47  ? 438 ALA B C   1 
ATOM   8650  O O   . ALA B 1 438 ? 2.849   27.680  -24.629 1.00 31.12  ? 438 ALA B O   1 
ATOM   8651  C CB  . ALA B 1 438 ? 3.652   27.134  -21.709 1.00 26.04  ? 438 ALA B CB  1 
ATOM   8652  N N   . MET B 1 439 ? 4.422   26.101  -24.854 1.00 32.75  ? 439 MET B N   1 
ATOM   8653  C CA  . MET B 1 439 ? 4.777   26.518  -26.222 1.00 35.32  ? 439 MET B CA  1 
ATOM   8654  C C   . MET B 1 439 ? 4.061   25.716  -27.325 1.00 36.58  ? 439 MET B C   1 
ATOM   8655  O O   . MET B 1 439 ? 4.056   26.124  -28.485 1.00 36.60  ? 439 MET B O   1 
ATOM   8656  C CB  . MET B 1 439 ? 6.296   26.533  -26.413 1.00 34.63  ? 439 MET B CB  1 
ATOM   8657  C CG  . MET B 1 439 ? 7.008   27.566  -25.538 1.00 33.67  ? 439 MET B CG  1 
ATOM   8658  S SD  . MET B 1 439 ? 6.631   29.248  -26.078 1.00 37.37  ? 439 MET B SD  1 
ATOM   8659  C CE  . MET B 1 439 ? 5.453   29.827  -24.841 1.00 35.22  ? 439 MET B CE  1 
ATOM   8660  N N   . ASP B 1 440 ? 3.444   24.599  -26.942 1.00 37.94  ? 440 ASP B N   1 
ATOM   8661  C CA  . ASP B 1 440 ? 2.463   23.883  -27.785 1.00 43.04  ? 440 ASP B CA  1 
ATOM   8662  C C   . ASP B 1 440 ? 1.503   24.811  -28.558 1.00 47.79  ? 440 ASP B C   1 
ATOM   8663  O O   . ASP B 1 440 ? 1.032   25.828  -28.030 1.00 44.63  ? 440 ASP B O   1 
ATOM   8664  C CB  . ASP B 1 440 ? 1.626   22.900  -26.932 1.00 42.89  ? 440 ASP B CB  1 
ATOM   8665  C CG  . ASP B 1 440 ? 2.358   21.586  -26.633 1.00 42.59  ? 440 ASP B CG  1 
ATOM   8666  O OD1 . ASP B 1 440 ? 3.394   21.321  -27.258 1.00 43.12  ? 440 ASP B OD1 1 
ATOM   8667  O OD2 . ASP B 1 440 ? 1.873   20.799  -25.783 1.00 43.92  ? 440 ASP B OD2 1 
ATOM   8668  N N   . PHE B 1 441 ? 1.178   24.390  -29.783 1.00 53.23  ? 441 PHE B N   1 
ATOM   8669  C CA  . PHE B 1 441 ? 0.428   25.166  -30.794 1.00 59.94  ? 441 PHE B CA  1 
ATOM   8670  C C   . PHE B 1 441 ? -1.027  25.583  -30.448 1.00 62.81  ? 441 PHE B C   1 
ATOM   8671  O O   . PHE B 1 441 ? -1.398  26.736  -30.671 1.00 62.38  ? 441 PHE B O   1 
ATOM   8672  C CB  . PHE B 1 441 ? 0.474   24.387  -32.128 1.00 66.31  ? 441 PHE B CB  1 
ATOM   8673  C CG  . PHE B 1 441 ? -0.196  25.074  -33.292 1.00 72.25  ? 441 PHE B CG  1 
ATOM   8674  C CD1 . PHE B 1 441 ? 0.300   26.274  -33.804 1.00 73.76  ? 441 PHE B CD1 1 
ATOM   8675  C CD2 . PHE B 1 441 ? -1.278  24.466  -33.940 1.00 76.80  ? 441 PHE B CD2 1 
ATOM   8676  C CE1 . PHE B 1 441 ? -0.298  26.874  -34.907 1.00 72.69  ? 441 PHE B CE1 1 
ATOM   8677  C CE2 . PHE B 1 441 ? -1.878  25.066  -35.040 1.00 76.65  ? 441 PHE B CE2 1 
ATOM   8678  C CZ  . PHE B 1 441 ? -1.389  26.271  -35.522 1.00 75.51  ? 441 PHE B CZ  1 
ATOM   8679  N N   . PRO B 1 442 ? -1.858  24.649  -29.930 1.00 65.42  ? 442 PRO B N   1 
ATOM   8680  C CA  . PRO B 1 442 ? -3.306  24.886  -29.739 1.00 69.24  ? 442 PRO B CA  1 
ATOM   8681  C C   . PRO B 1 442 ? -3.747  26.305  -29.320 1.00 67.16  ? 442 PRO B C   1 
ATOM   8682  O O   . PRO B 1 442 ? -4.675  26.857  -29.923 1.00 70.04  ? 442 PRO B O   1 
ATOM   8683  C CB  . PRO B 1 442 ? -3.675  23.877  -28.651 1.00 69.05  ? 442 PRO B CB  1 
ATOM   8684  C CG  . PRO B 1 442 ? -2.736  22.734  -28.878 1.00 70.64  ? 442 PRO B CG  1 
ATOM   8685  C CD  . PRO B 1 442 ? -1.505  23.257  -29.592 1.00 67.93  ? 442 PRO B CD  1 
ATOM   8686  N N   . PHE B 1 443 ? -3.095  26.880  -28.309 1.00 65.08  ? 443 PHE B N   1 
ATOM   8687  C CA  . PHE B 1 443 ? -3.534  28.159  -27.707 1.00 67.41  ? 443 PHE B CA  1 
ATOM   8688  C C   . PHE B 1 443 ? -3.547  29.348  -28.690 1.00 67.61  ? 443 PHE B C   1 
ATOM   8689  O O   . PHE B 1 443 ? -4.325  30.296  -28.509 1.00 71.66  ? 443 PHE B O   1 
ATOM   8690  C CB  . PHE B 1 443 ? -2.690  28.510  -26.450 1.00 63.89  ? 443 PHE B CB  1 
ATOM   8691  C CG  . PHE B 1 443 ? -1.479  29.353  -26.754 1.00 61.11  ? 443 PHE B CG  1 
ATOM   8692  C CD1 . PHE B 1 443 ? -1.537  30.744  -26.648 1.00 58.43  ? 443 PHE B CD1 1 
ATOM   8693  C CD2 . PHE B 1 443 ? -0.296  28.761  -27.219 1.00 57.25  ? 443 PHE B CD2 1 
ATOM   8694  C CE1 . PHE B 1 443 ? -0.431  31.525  -26.969 1.00 58.25  ? 443 PHE B CE1 1 
ATOM   8695  C CE2 . PHE B 1 443 ? 0.811   29.536  -27.530 1.00 55.62  ? 443 PHE B CE2 1 
ATOM   8696  C CZ  . PHE B 1 443 ? 0.741   30.921  -27.410 1.00 55.74  ? 443 PHE B CZ  1 
ATOM   8697  N N   . ILE B 1 444 ? -2.675  29.310  -29.703 1.00 67.15  ? 444 ILE B N   1 
ATOM   8698  C CA  . ILE B 1 444 ? -2.566  30.417  -30.679 1.00 66.12  ? 444 ILE B CA  1 
ATOM   8699  C C   . ILE B 1 444 ? -2.899  30.016  -32.131 1.00 68.04  ? 444 ILE B C   1 
ATOM   8700  O O   . ILE B 1 444 ? -2.563  30.737  -33.077 1.00 66.46  ? 444 ILE B O   1 
ATOM   8701  C CB  . ILE B 1 444 ? -1.201  31.181  -30.578 1.00 62.02  ? 444 ILE B CB  1 
ATOM   8702  C CG1 . ILE B 1 444 ? -1.311  32.571  -31.236 1.00 60.81  ? 444 ILE B CG1 1 
ATOM   8703  C CG2 . ILE B 1 444 ? -0.033  30.355  -31.132 1.00 57.21  ? 444 ILE B CG2 1 
ATOM   8704  C CD1 . ILE B 1 444 ? -0.254  33.569  -30.806 1.00 54.47  ? 444 ILE B CD1 1 
ATOM   8705  N N   . CYS B 1 445 ? -3.597  28.887  -32.291 1.00 72.99  ? 445 CYS B N   1 
ATOM   8706  C CA  . CYS B 1 445 ? -3.982  28.390  -33.624 1.00 76.49  ? 445 CYS B CA  1 
ATOM   8707  C C   . CYS B 1 445 ? -4.901  29.355  -34.390 1.00 75.55  ? 445 CYS B C   1 
ATOM   8708  O O   . CYS B 1 445 ? -4.942  29.323  -35.623 1.00 73.86  ? 445 CYS B O   1 
ATOM   8709  C CB  . CYS B 1 445 ? -4.584  26.967  -33.559 1.00 81.46  ? 445 CYS B CB  1 
ATOM   8710  S SG  . CYS B 1 445 ? -6.325  26.829  -33.055 1.00 91.49  ? 445 CYS B SG  1 
ATOM   8711  N N   . ASN B 1 446 ? -5.608  30.223  -33.660 1.00 72.24  ? 446 ASN B N   1 
ATOM   8712  C CA  . ASN B 1 446 ? -6.452  31.251  -34.291 1.00 74.30  ? 446 ASN B CA  1 
ATOM   8713  C C   . ASN B 1 446 ? -5.693  32.492  -34.804 1.00 72.82  ? 446 ASN B C   1 
ATOM   8714  O O   . ASN B 1 446 ? -6.291  33.401  -35.387 1.00 73.62  ? 446 ASN B O   1 
ATOM   8715  C CB  . ASN B 1 446 ? -7.636  31.632  -33.389 1.00 75.07  ? 446 ASN B CB  1 
ATOM   8716  C CG  . ASN B 1 446 ? -8.908  30.865  -33.743 1.00 78.89  ? 446 ASN B CG  1 
ATOM   8717  O OD1 . ASN B 1 446 ? -9.321  30.833  -34.906 1.00 79.08  ? 446 ASN B OD1 1 
ATOM   8718  N ND2 . ASN B 1 446 ? -9.533  30.246  -32.740 1.00 75.03  ? 446 ASN B ND2 1 
ATOM   8719  N N   . SER B 1 447 ? -4.377  32.509  -34.591 1.00 69.25  ? 447 SER B N   1 
ATOM   8720  C CA  . SER B 1 447 ? -3.488  33.464  -35.253 1.00 65.77  ? 447 SER B CA  1 
ATOM   8721  C C   . SER B 1 447 ? -2.726  32.778  -36.394 1.00 63.17  ? 447 SER B C   1 
ATOM   8722  O O   . SER B 1 447 ? -1.869  33.391  -37.046 1.00 61.05  ? 447 SER B O   1 
ATOM   8723  C CB  . SER B 1 447 ? -2.494  34.061  -34.251 1.00 65.90  ? 447 SER B CB  1 
ATOM   8724  O OG  . SER B 1 447 ? -3.091  35.062  -33.446 1.00 69.44  ? 447 SER B OG  1 
ATOM   8725  N N   . PHE B 1 448 ? -3.052  31.507  -36.626 1.00 59.07  ? 448 PHE B N   1 
ATOM   8726  C CA  . PHE B 1 448 ? -2.350  30.671  -37.600 1.00 55.33  ? 448 PHE B CA  1 
ATOM   8727  C C   . PHE B 1 448 ? -3.293  30.048  -38.614 1.00 53.59  ? 448 PHE B C   1 
ATOM   8728  O O   . PHE B 1 448 ? -3.197  28.859  -38.937 1.00 55.65  ? 448 PHE B O   1 
ATOM   8729  C CB  . PHE B 1 448 ? -1.553  29.582  -36.883 1.00 58.11  ? 448 PHE B CB  1 
ATOM   8730  C CG  . PHE B 1 448 ? -0.136  29.961  -36.618 1.00 55.39  ? 448 PHE B CG  1 
ATOM   8731  C CD1 . PHE B 1 448 ? 0.899   29.304  -37.267 1.00 54.02  ? 448 PHE B CD1 1 
ATOM   8732  C CD2 . PHE B 1 448 ? 0.164   31.005  -35.751 1.00 55.61  ? 448 PHE B CD2 1 
ATOM   8733  C CE1 . PHE B 1 448 ? 2.210   29.663  -37.045 1.00 52.54  ? 448 PHE B CE1 1 
ATOM   8734  C CE2 . PHE B 1 448 ? 1.475   31.380  -35.535 1.00 54.86  ? 448 PHE B CE2 1 
ATOM   8735  C CZ  . PHE B 1 448 ? 2.498   30.704  -36.182 1.00 55.44  ? 448 PHE B CZ  1 
ATOM   8736  N N   . THR B 1 449 ? -4.205  30.858  -39.117 1.00 50.67  ? 449 THR B N   1 
ATOM   8737  C CA  . THR B 1 449 ? -5.214  30.377  -40.025 1.00 51.13  ? 449 THR B CA  1 
ATOM   8738  C C   . THR B 1 449 ? -4.844  30.769  -41.442 1.00 49.48  ? 449 THR B C   1 
ATOM   8739  O O   . THR B 1 449 ? -3.835  31.443  -41.675 1.00 45.87  ? 449 THR B O   1 
ATOM   8740  C CB  . THR B 1 449 ? -6.591  30.970  -39.678 1.00 52.68  ? 449 THR B CB  1 
ATOM   8741  O OG1 . THR B 1 449 ? -6.583  32.378  -39.942 1.00 53.28  ? 449 THR B OG1 1 
ATOM   8742  C CG2 . THR B 1 449 ? -6.920  30.741  -38.205 1.00 51.81  ? 449 THR B CG2 1 
ATOM   8743  N N   . LYS B 1 450 ? -5.672  30.342  -42.385 1.00 49.55  ? 450 LYS B N   1 
ATOM   8744  C CA  . LYS B 1 450 ? -5.554  30.762  -43.766 1.00 48.92  ? 450 LYS B CA  1 
ATOM   8745  C C   . LYS B 1 450 ? -5.666  32.287  -43.892 1.00 45.90  ? 450 LYS B C   1 
ATOM   8746  O O   . LYS B 1 450 ? -5.063  32.891  -44.776 1.00 44.78  ? 450 LYS B O   1 
ATOM   8747  C CB  . LYS B 1 450 ? -6.603  30.052  -44.640 1.00 51.61  ? 450 LYS B CB  1 
ATOM   8748  C CG  . LYS B 1 450 ? -7.918  29.738  -43.938 1.00 54.74  ? 450 LYS B CG  1 
ATOM   8749  C CD  . LYS B 1 450 ? -8.772  28.783  -44.767 1.00 59.00  ? 450 LYS B CD  1 
ATOM   8750  C CE  . LYS B 1 450 ? -9.559  27.805  -43.898 1.00 62.13  ? 450 LYS B CE  1 
ATOM   8751  N NZ  . LYS B 1 450 ? -10.602 28.461  -43.054 1.00 66.64  ? 450 LYS B NZ  1 
ATOM   8752  N N   . PHE B 1 451 ? -6.423  32.900  -42.992 1.00 44.28  ? 451 PHE B N   1 
ATOM   8753  C CA  . PHE B 1 451 ? -6.585  34.350  -42.986 1.00 44.74  ? 451 PHE B CA  1 
ATOM   8754  C C   . PHE B 1 451 ? -5.273  35.094  -42.800 1.00 42.19  ? 451 PHE B C   1 
ATOM   8755  O O   . PHE B 1 451 ? -5.095  36.182  -43.341 1.00 41.17  ? 451 PHE B O   1 
ATOM   8756  C CB  . PHE B 1 451 ? -7.561  34.772  -41.892 1.00 47.27  ? 451 PHE B CB  1 
ATOM   8757  C CG  . PHE B 1 451 ? -8.977  34.878  -42.356 1.00 50.48  ? 451 PHE B CG  1 
ATOM   8758  C CD1 . PHE B 1 451 ? -9.369  35.910  -43.202 1.00 51.88  ? 451 PHE B CD1 1 
ATOM   8759  C CD2 . PHE B 1 451 ? -9.927  33.953  -41.942 1.00 52.15  ? 451 PHE B CD2 1 
ATOM   8760  C CE1 . PHE B 1 451 ? -10.685 36.012  -43.633 1.00 54.96  ? 451 PHE B CE1 1 
ATOM   8761  C CE2 . PHE B 1 451 ? -11.245 34.054  -42.367 1.00 53.89  ? 451 PHE B CE2 1 
ATOM   8762  C CZ  . PHE B 1 451 ? -11.624 35.089  -43.206 1.00 53.62  ? 451 PHE B CZ  1 
ATOM   8763  N N   . GLU B 1 452 ? -4.368  34.516  -42.014 1.00 39.83  ? 452 GLU B N   1 
ATOM   8764  C CA  . GLU B 1 452 ? -3.088  35.146  -41.750 1.00 39.34  ? 452 GLU B CA  1 
ATOM   8765  C C   . GLU B 1 452 ? -2.044  34.840  -42.824 1.00 38.76  ? 452 GLU B C   1 
ATOM   8766  O O   . GLU B 1 452 ? -1.287  35.721  -43.218 1.00 38.24  ? 452 GLU B O   1 
ATOM   8767  C CB  . GLU B 1 452 ? -2.561  34.740  -40.379 1.00 40.26  ? 452 GLU B CB  1 
ATOM   8768  C CG  . GLU B 1 452 ? -3.156  35.538  -39.226 1.00 43.42  ? 452 GLU B CG  1 
ATOM   8769  C CD  . GLU B 1 452 ? -4.475  34.977  -38.722 1.00 43.74  ? 452 GLU B CD  1 
ATOM   8770  O OE1 . GLU B 1 452 ? -5.217  35.731  -38.072 1.00 46.34  ? 452 GLU B OE1 1 
ATOM   8771  O OE2 . GLU B 1 452 ? -4.774  33.788  -38.964 1.00 45.02  ? 452 GLU B OE2 1 
ATOM   8772  N N   . PHE B 1 453 ? -2.028  33.598  -43.308 1.00 38.02  ? 453 PHE B N   1 
ATOM   8773  C CA  . PHE B 1 453 ? -0.910  33.094  -44.094 1.00 38.13  ? 453 PHE B CA  1 
ATOM   8774  C C   . PHE B 1 453 ? -1.150  32.995  -45.602 1.00 38.44  ? 453 PHE B C   1 
ATOM   8775  O O   . PHE B 1 453 ? -0.221  32.709  -46.366 1.00 38.98  ? 453 PHE B O   1 
ATOM   8776  C CB  . PHE B 1 453 ? -0.417  31.757  -43.518 1.00 38.64  ? 453 PHE B CB  1 
ATOM   8777  C CG  . PHE B 1 453 ? 0.168   31.885  -42.148 1.00 41.04  ? 453 PHE B CG  1 
ATOM   8778  C CD1 . PHE B 1 453 ? 1.345   32.606  -41.945 1.00 39.86  ? 453 PHE B CD1 1 
ATOM   8779  C CD2 . PHE B 1 453 ? -0.469  31.331  -41.050 1.00 42.01  ? 453 PHE B CD2 1 
ATOM   8780  C CE1 . PHE B 1 453 ? 1.872   32.760  -40.681 1.00 40.26  ? 453 PHE B CE1 1 
ATOM   8781  C CE2 . PHE B 1 453 ? 0.061   31.477  -39.783 1.00 41.24  ? 453 PHE B CE2 1 
ATOM   8782  C CZ  . PHE B 1 453 ? 1.230   32.195  -39.597 1.00 42.14  ? 453 PHE B CZ  1 
ATOM   8783  N N   . ASN B 1 454 ? -2.378  33.233  -46.042 1.00 38.07  ? 454 ASN B N   1 
ATOM   8784  C CA  . ASN B 1 454 ? -2.675  33.153  -47.471 1.00 38.32  ? 454 ASN B CA  1 
ATOM   8785  C C   . ASN B 1 454 ? -1.953  34.234  -48.253 1.00 37.51  ? 454 ASN B C   1 
ATOM   8786  O O   . ASN B 1 454 ? -1.629  35.293  -47.715 1.00 36.84  ? 454 ASN B O   1 
ATOM   8787  C CB  . ASN B 1 454 ? -4.183  33.230  -47.745 1.00 38.84  ? 454 ASN B CB  1 
ATOM   8788  C CG  . ASN B 1 454 ? -4.697  34.654  -47.739 1.00 38.68  ? 454 ASN B CG  1 
ATOM   8789  O OD1 . ASN B 1 454 ? -4.711  35.322  -48.772 1.00 39.47  ? 454 ASN B OD1 1 
ATOM   8790  N ND2 . ASN B 1 454 ? -5.069  35.144  -46.565 1.00 37.77  ? 454 ASN B ND2 1 
ATOM   8791  N N   . THR B 1 455 ? -1.694  33.954  -49.523 1.00 37.00  ? 455 THR B N   1 
ATOM   8792  C CA  . THR B 1 455 ? -1.202  34.957  -50.433 1.00 37.57  ? 455 THR B CA  1 
ATOM   8793  C C   . THR B 1 455 ? -2.115  35.024  -51.654 1.00 39.10  ? 455 THR B C   1 
ATOM   8794  O O   . THR B 1 455 ? -1.658  35.234  -52.786 1.00 39.14  ? 455 THR B O   1 
ATOM   8795  C CB  . THR B 1 455 ? 0.273   34.712  -50.827 1.00 38.07  ? 455 THR B CB  1 
ATOM   8796  O OG1 . THR B 1 455 ? 0.489   33.311  -51.057 1.00 38.31  ? 455 THR B OG1 1 
ATOM   8797  C CG2 . THR B 1 455 ? 1.217   35.204  -49.708 1.00 36.54  ? 455 THR B CG2 1 
ATOM   8798  N N   . VAL B 1 456 ? -3.409  34.813  -51.402 1.00 40.12  ? 456 VAL B N   1 
ATOM   8799  C CA  . VAL B 1 456 ? -4.466  35.031  -52.393 1.00 41.36  ? 456 VAL B CA  1 
ATOM   8800  C C   . VAL B 1 456 ? -4.828  36.528  -52.382 1.00 40.81  ? 456 VAL B C   1 
ATOM   8801  O O   . VAL B 1 456 ? -4.433  37.272  -53.271 1.00 40.61  ? 456 VAL B O   1 
ATOM   8802  C CB  . VAL B 1 456 ? -5.718  34.158  -52.087 1.00 42.92  ? 456 VAL B CB  1 
ATOM   8803  C CG1 . VAL B 1 456 ? -6.819  34.408  -53.108 1.00 43.08  ? 456 VAL B CG1 1 
ATOM   8804  C CG2 . VAL B 1 456 ? -5.353  32.678  -52.061 1.00 42.98  ? 456 VAL B CG2 1 
ATOM   8805  N N   . PHE B 1 457 ? -5.522  36.971  -51.336 1.00 40.84  ? 457 PHE B N   1 
ATOM   8806  C CA  . PHE B 1 457 ? -5.787  38.398  -51.149 1.00 41.17  ? 457 PHE B CA  1 
ATOM   8807  C C   . PHE B 1 457 ? -4.688  39.139  -50.337 1.00 39.53  ? 457 PHE B C   1 
ATOM   8808  O O   . PHE B 1 457 ? -4.427  40.312  -50.574 1.00 39.29  ? 457 PHE B O   1 
ATOM   8809  C CB  . PHE B 1 457 ? -7.193  38.624  -50.561 1.00 41.41  ? 457 PHE B CB  1 
ATOM   8810  C CG  . PHE B 1 457 ? -7.479  37.815  -49.315 1.00 43.54  ? 457 PHE B CG  1 
ATOM   8811  C CD1 . PHE B 1 457 ? -7.171  38.322  -48.044 1.00 41.77  ? 457 PHE B CD1 1 
ATOM   8812  C CD2 . PHE B 1 457 ? -8.075  36.553  -49.404 1.00 44.37  ? 457 PHE B CD2 1 
ATOM   8813  C CE1 . PHE B 1 457 ? -7.438  37.579  -46.901 1.00 41.85  ? 457 PHE B CE1 1 
ATOM   8814  C CE2 . PHE B 1 457 ? -8.349  35.812  -48.257 1.00 43.77  ? 457 PHE B CE2 1 
ATOM   8815  C CZ  . PHE B 1 457 ? -8.031  36.327  -47.008 1.00 42.22  ? 457 PHE B CZ  1 
ATOM   8816  N N   . ASN B 1 458 ? -4.043  38.448  -49.400 1.00 38.54  ? 458 ASN B N   1 
ATOM   8817  C CA  . ASN B 1 458 ? -2.951  39.045  -48.605 1.00 37.23  ? 458 ASN B CA  1 
ATOM   8818  C C   . ASN B 1 458 ? -1.625  39.162  -49.347 1.00 36.52  ? 458 ASN B C   1 
ATOM   8819  O O   . ASN B 1 458 ? -1.191  38.230  -49.999 1.00 37.10  ? 458 ASN B O   1 
ATOM   8820  C CB  . ASN B 1 458 ? -2.717  38.246  -47.322 1.00 35.91  ? 458 ASN B CB  1 
ATOM   8821  C CG  . ASN B 1 458 ? -3.622  38.684  -46.181 1.00 36.38  ? 458 ASN B CG  1 
ATOM   8822  O OD1 . ASN B 1 458 ? -3.705  38.011  -45.138 1.00 36.46  ? 458 ASN B OD1 1 
ATOM   8823  N ND2 . ASN B 1 458 ? -4.301  39.810  -46.362 1.00 34.63  ? 458 ASN B ND2 1 
ATOM   8824  N N   . ASP B 1 459 ? -0.963  40.303  -49.216 1.00 37.72  ? 459 ASP B N   1 
ATOM   8825  C CA  . ASP B 1 459 ? 0.428   40.428  -49.661 1.00 37.72  ? 459 ASP B CA  1 
ATOM   8826  C C   . ASP B 1 459 ? 1.337   39.599  -48.734 1.00 36.34  ? 459 ASP B C   1 
ATOM   8827  O O   . ASP B 1 459 ? 0.971   39.283  -47.602 1.00 35.77  ? 459 ASP B O   1 
ATOM   8828  C CB  . ASP B 1 459 ? 0.869   41.894  -49.648 1.00 39.04  ? 459 ASP B CB  1 
ATOM   8829  C CG  . ASP B 1 459 ? 0.086   42.762  -50.650 1.00 42.82  ? 459 ASP B CG  1 
ATOM   8830  O OD1 . ASP B 1 459 ? -0.029  42.354  -51.825 1.00 47.01  ? 459 ASP B OD1 1 
ATOM   8831  O OD2 . ASP B 1 459 ? -0.376  43.867  -50.272 1.00 40.66  ? 459 ASP B OD2 1 
ATOM   8832  N N   . GLN B 1 460 ? 2.508   39.247  -49.234 1.00 35.44  ? 460 GLN B N   1 
ATOM   8833  C CA  . GLN B 1 460 ? 3.530   38.581  -48.462 1.00 34.51  ? 460 GLN B CA  1 
ATOM   8834  C C   . GLN B 1 460 ? 3.933   39.395  -47.231 1.00 33.45  ? 460 GLN B C   1 
ATOM   8835  O O   . GLN B 1 460 ? 4.119   38.840  -46.151 1.00 33.96  ? 460 GLN B O   1 
ATOM   8836  C CB  . GLN B 1 460 ? 4.746   38.337  -49.356 1.00 35.65  ? 460 GLN B CB  1 
ATOM   8837  C CG  . GLN B 1 460 ? 5.920   37.683  -48.655 1.00 34.49  ? 460 GLN B CG  1 
ATOM   8838  C CD  . GLN B 1 460 ? 6.984   37.236  -49.623 1.00 33.78  ? 460 GLN B CD  1 
ATOM   8839  O OE1 . GLN B 1 460 ? 6.721   36.460  -50.531 1.00 34.32  ? 460 GLN B OE1 1 
ATOM   8840  N NE2 . GLN B 1 460 ? 8.204   37.703  -49.411 1.00 34.49  ? 460 GLN B NE2 1 
ATOM   8841  N N   . ARG B 1 461 ? 4.034   40.712  -47.382 1.00 33.04  ? 461 ARG B N   1 
ATOM   8842  C CA  . ARG B 1 461 ? 4.422   41.563  -46.264 1.00 33.43  ? 461 ARG B CA  1 
ATOM   8843  C C   . ARG B 1 461 ? 3.367   41.598  -45.180 1.00 32.60  ? 461 ARG B C   1 
ATOM   8844  O O   . ARG B 1 461 ? 3.670   41.828  -44.016 1.00 33.78  ? 461 ARG B O   1 
ATOM   8845  C CB  . ARG B 1 461 ? 4.740   42.983  -46.733 1.00 35.66  ? 461 ARG B CB  1 
ATOM   8846  C CG  . ARG B 1 461 ? 3.624   43.670  -47.481 1.00 38.94  ? 461 ARG B CG  1 
ATOM   8847  C CD  . ARG B 1 461 ? 4.030   45.081  -47.834 1.00 41.62  ? 461 ARG B CD  1 
ATOM   8848  N NE  . ARG B 1 461 ? 3.121   45.686  -48.790 1.00 46.30  ? 461 ARG B NE  1 
ATOM   8849  C CZ  . ARG B 1 461 ? 2.331   46.722  -48.526 1.00 49.23  ? 461 ARG B CZ  1 
ATOM   8850  N NH1 . ARG B 1 461 ? 2.337   47.284  -47.324 1.00 50.55  ? 461 ARG B NH1 1 
ATOM   8851  N NH2 . ARG B 1 461 ? 1.542   47.210  -49.476 1.00 51.94  ? 461 ARG B NH2 1 
ATOM   8852  N N   . THR B 1 462 ? 2.123   41.361  -45.573 1.00 31.79  ? 462 THR B N   1 
ATOM   8853  C CA  . THR B 1 462 ? 1.022   41.276  -44.648 1.00 30.90  ? 462 THR B CA  1 
ATOM   8854  C C   . THR B 1 462 ? 1.104   39.971  -43.862 1.00 31.08  ? 462 THR B C   1 
ATOM   8855  O O   . THR B 1 462 ? 0.815   39.940  -42.670 1.00 30.38  ? 462 THR B O   1 
ATOM   8856  C CB  . THR B 1 462 ? -0.299  41.355  -45.416 1.00 31.42  ? 462 THR B CB  1 
ATOM   8857  O OG1 . THR B 1 462 ? -0.441  42.676  -45.961 1.00 31.97  ? 462 THR B OG1 1 
ATOM   8858  C CG2 . THR B 1 462 ? -1.506  41.024  -44.515 1.00 31.51  ? 462 THR B CG2 1 
ATOM   8859  N N   . VAL B 1 463 ? 1.496   38.899  -44.545 1.00 30.43  ? 463 VAL B N   1 
ATOM   8860  C CA  . VAL B 1 463 ? 1.672   37.609  -43.911 1.00 30.93  ? 463 VAL B CA  1 
ATOM   8861  C C   . VAL B 1 463 ? 2.814   37.684  -42.894 1.00 29.92  ? 463 VAL B C   1 
ATOM   8862  O O   . VAL B 1 463 ? 2.689   37.203  -41.778 1.00 29.48  ? 463 VAL B O   1 
ATOM   8863  C CB  . VAL B 1 463 ? 1.982   36.509  -44.957 1.00 32.28  ? 463 VAL B CB  1 
ATOM   8864  C CG1 . VAL B 1 463 ? 2.322   35.207  -44.261 1.00 31.93  ? 463 VAL B CG1 1 
ATOM   8865  C CG2 . VAL B 1 463 ? 0.799   36.315  -45.907 1.00 30.69  ? 463 VAL B CG2 1 
ATOM   8866  N N   . PHE B 1 464 ? 3.918   38.320  -43.276 1.00 29.82  ? 464 PHE B N   1 
ATOM   8867  C CA  . PHE B 1 464 ? 5.010   38.558  -42.328 1.00 28.17  ? 464 PHE B CA  1 
ATOM   8868  C C   . PHE B 1 464 ? 4.561   39.380  -41.079 1.00 28.68  ? 464 PHE B C   1 
ATOM   8869  O O   . PHE B 1 464 ? 4.900   39.037  -39.963 1.00 27.07  ? 464 PHE B O   1 
ATOM   8870  C CB  . PHE B 1 464 ? 6.195   39.208  -43.038 1.00 26.89  ? 464 PHE B CB  1 
ATOM   8871  C CG  . PHE B 1 464 ? 6.926   38.285  -43.982 1.00 27.26  ? 464 PHE B CG  1 
ATOM   8872  C CD1 . PHE B 1 464 ? 6.923   36.897  -43.787 1.00 26.42  ? 464 PHE B CD1 1 
ATOM   8873  C CD2 . PHE B 1 464 ? 7.652   38.801  -45.055 1.00 27.21  ? 464 PHE B CD2 1 
ATOM   8874  C CE1 . PHE B 1 464 ? 7.635   36.067  -44.630 1.00 26.32  ? 464 PHE B CE1 1 
ATOM   8875  C CE2 . PHE B 1 464 ? 8.341   37.965  -45.917 1.00 26.94  ? 464 PHE B CE2 1 
ATOM   8876  C CZ  . PHE B 1 464 ? 8.350   36.599  -45.698 1.00 26.29  ? 464 PHE B CZ  1 
ATOM   8877  N N   . ALA B 1 465 ? 3.771   40.435  -41.271 1.00 28.73  ? 465 ALA B N   1 
ATOM   8878  C CA  . ALA B 1 465 ? 3.222   41.179  -40.116 1.00 29.84  ? 465 ALA B CA  1 
ATOM   8879  C C   . ALA B 1 465 ? 2.358   40.282  -39.207 1.00 31.07  ? 465 ALA B C   1 
ATOM   8880  O O   . ALA B 1 465 ? 2.527   40.248  -37.969 1.00 30.46  ? 465 ALA B O   1 
ATOM   8881  C CB  . ALA B 1 465 ? 2.421   42.379  -40.577 1.00 27.94  ? 465 ALA B CB  1 
ATOM   8882  N N   . ASN B 1 466 ? 1.430   39.562  -39.827 1.00 30.95  ? 466 ASN B N   1 
ATOM   8883  C CA  . ASN B 1 466 ? 0.615   38.633  -39.094 1.00 31.30  ? 466 ASN B CA  1 
ATOM   8884  C C   . ASN B 1 466 ? 1.467   37.673  -38.287 1.00 29.63  ? 466 ASN B C   1 
ATOM   8885  O O   . ASN B 1 466 ? 1.195   37.434  -37.122 1.00 29.14  ? 466 ASN B O   1 
ATOM   8886  C CB  . ASN B 1 466 ? -0.330  37.882  -40.035 1.00 32.35  ? 466 ASN B CB  1 
ATOM   8887  C CG  . ASN B 1 466 ? -1.488  38.728  -40.455 1.00 33.45  ? 466 ASN B CG  1 
ATOM   8888  O OD1 . ASN B 1 466 ? -1.893  39.630  -39.726 1.00 36.01  ? 466 ASN B OD1 1 
ATOM   8889  N ND2 . ASN B 1 466 ? -2.011  38.478  -41.645 1.00 32.78  ? 466 ASN B ND2 1 
ATOM   8890  N N   . PHE B 1 467 ? 2.520   37.153  -38.905 1.00 29.25  ? 467 PHE B N   1 
ATOM   8891  C CA  . PHE B 1 467 ? 3.372   36.167  -38.245 1.00 27.85  ? 467 PHE B CA  1 
ATOM   8892  C C   . PHE B 1 467 ? 4.173   36.799  -37.099 1.00 26.97  ? 467 PHE B C   1 
ATOM   8893  O O   . PHE B 1 467 ? 4.270   36.245  -36.019 1.00 27.53  ? 467 PHE B O   1 
ATOM   8894  C CB  . PHE B 1 467 ? 4.277   35.498  -39.265 1.00 26.82  ? 467 PHE B CB  1 
ATOM   8895  C CG  . PHE B 1 467 ? 5.234   34.515  -38.672 1.00 27.15  ? 467 PHE B CG  1 
ATOM   8896  C CD1 . PHE B 1 467 ? 4.775   33.336  -38.090 1.00 26.51  ? 467 PHE B CD1 1 
ATOM   8897  C CD2 . PHE B 1 467 ? 6.599   34.756  -38.705 1.00 26.66  ? 467 PHE B CD2 1 
ATOM   8898  C CE1 . PHE B 1 467 ? 5.657   32.427  -37.538 1.00 25.68  ? 467 PHE B CE1 1 
ATOM   8899  C CE2 . PHE B 1 467 ? 7.485   33.842  -38.157 1.00 26.24  ? 467 PHE B CE2 1 
ATOM   8900  C CZ  . PHE B 1 467 ? 7.009   32.684  -37.576 1.00 25.15  ? 467 PHE B CZ  1 
ATOM   8901  N N   . TYR B 1 468 ? 4.718   37.981  -37.330 1.00 26.81  ? 468 TYR B N   1 
ATOM   8902  C CA  . TYR B 1 468 ? 5.411   38.711  -36.267 1.00 27.31  ? 468 TYR B CA  1 
ATOM   8903  C C   . TYR B 1 468 ? 4.475   38.917  -35.059 1.00 27.95  ? 468 TYR B C   1 
ATOM   8904  O O   . TYR B 1 468 ? 4.795   38.513  -33.938 1.00 28.34  ? 468 TYR B O   1 
ATOM   8905  C CB  . TYR B 1 468 ? 5.918   40.038  -36.818 1.00 25.21  ? 468 TYR B CB  1 
ATOM   8906  C CG  . TYR B 1 468 ? 6.767   40.840  -35.889 1.00 23.80  ? 468 TYR B CG  1 
ATOM   8907  C CD1 . TYR B 1 468 ? 8.032   40.394  -35.479 1.00 23.38  ? 468 TYR B CD1 1 
ATOM   8908  C CD2 . TYR B 1 468 ? 6.334   42.089  -35.462 1.00 23.56  ? 468 TYR B CD2 1 
ATOM   8909  C CE1 . TYR B 1 468 ? 8.811   41.176  -34.643 1.00 23.27  ? 468 TYR B CE1 1 
ATOM   8910  C CE2 . TYR B 1 468 ? 7.082   42.867  -34.633 1.00 22.74  ? 468 TYR B CE2 1 
ATOM   8911  C CZ  . TYR B 1 468 ? 8.304   42.435  -34.226 1.00 23.46  ? 468 TYR B CZ  1 
ATOM   8912  O OH  . TYR B 1 468 ? 9.016   43.275  -33.415 1.00 24.85  ? 468 TYR B OH  1 
ATOM   8913  N N   . ASP B 1 469 ? 3.285   39.463  -35.311 1.00 28.98  ? 469 ASP B N   1 
ATOM   8914  C CA  . ASP B 1 469 ? 2.291   39.678  -34.251 1.00 29.27  ? 469 ASP B CA  1 
ATOM   8915  C C   . ASP B 1 469 ? 2.026   38.387  -33.423 1.00 30.75  ? 469 ASP B C   1 
ATOM   8916  O O   . ASP B 1 469 ? 2.183   38.387  -32.192 1.00 31.22  ? 469 ASP B O   1 
ATOM   8917  C CB  . ASP B 1 469 ? 0.994   40.206  -34.848 1.00 29.95  ? 469 ASP B CB  1 
ATOM   8918  C CG  . ASP B 1 469 ? 1.091   41.668  -35.296 1.00 31.20  ? 469 ASP B CG  1 
ATOM   8919  O OD1 . ASP B 1 469 ? 2.083   42.347  -34.966 1.00 30.50  ? 469 ASP B OD1 1 
ATOM   8920  O OD2 . ASP B 1 469 ? 0.145   42.142  -35.959 1.00 31.76  ? 469 ASP B OD2 1 
ATOM   8921  N N   . ALA B 1 470 ? 1.641   37.298  -34.096 1.00 29.60  ? 470 ALA B N   1 
ATOM   8922  C CA  . ALA B 1 470 ? 1.419   36.013  -33.417 1.00 29.41  ? 470 ALA B CA  1 
ATOM   8923  C C   . ALA B 1 470 ? 2.628   35.583  -32.556 1.00 27.68  ? 470 ALA B C   1 
ATOM   8924  O O   . ALA B 1 470 ? 2.453   35.112  -31.451 1.00 28.71  ? 470 ALA B O   1 
ATOM   8925  C CB  . ALA B 1 470 ? 1.034   34.925  -34.425 1.00 29.32  ? 470 ALA B CB  1 
ATOM   8926  N N   . MET B 1 471 ? 3.850   35.809  -33.048 1.00 26.65  ? 471 MET B N   1 
ATOM   8927  C CA  . MET B 1 471 ? 5.067   35.442  -32.305 1.00 25.73  ? 471 MET B CA  1 
ATOM   8928  C C   . MET B 1 471 ? 5.361   36.362  -31.082 1.00 27.15  ? 471 MET B C   1 
ATOM   8929  O O   . MET B 1 471 ? 5.964   35.906  -30.069 1.00 25.35  ? 471 MET B O   1 
ATOM   8930  C CB  . MET B 1 471 ? 6.297   35.336  -33.234 1.00 25.80  ? 471 MET B CB  1 
ATOM   8931  C CG  . MET B 1 471 ? 6.261   34.185  -34.258 1.00 25.64  ? 471 MET B CG  1 
ATOM   8932  S SD  . MET B 1 471 ? 5.696   32.581  -33.604 1.00 26.60  ? 471 MET B SD  1 
ATOM   8933  C CE  . MET B 1 471 ? 7.022   32.147  -32.478 1.00 23.79  ? 471 MET B CE  1 
ATOM   8934  N N   . ILE B 1 472 ? 4.953   37.639  -31.171 1.00 26.49  ? 472 ILE B N   1 
ATOM   8935  C CA  . ILE B 1 472 ? 4.942   38.515  -30.011 1.00 26.82  ? 472 ILE B CA  1 
ATOM   8936  C C   . ILE B 1 472 ? 4.056   37.889  -28.901 1.00 28.66  ? 472 ILE B C   1 
ATOM   8937  O O   . ILE B 1 472 ? 4.486   37.788  -27.731 1.00 27.35  ? 472 ILE B O   1 
ATOM   8938  C CB  . ILE B 1 472 ? 4.395   39.927  -30.345 1.00 28.06  ? 472 ILE B CB  1 
ATOM   8939  C CG1 . ILE B 1 472 ? 5.318   40.696  -31.321 1.00 28.10  ? 472 ILE B CG1 1 
ATOM   8940  C CG2 . ILE B 1 472 ? 4.171   40.727  -29.065 1.00 27.34  ? 472 ILE B CG2 1 
ATOM   8941  C CD1 . ILE B 1 472 ? 6.621   41.185  -30.695 1.00 28.31  ? 472 ILE B CD1 1 
ATOM   8942  N N   . CYS B 1 473 ? 2.829   37.473  -29.261 1.00 28.14  ? 473 CYS B N   1 
ATOM   8943  C CA  . CYS B 1 473 ? 1.941   36.799  -28.304 1.00 29.18  ? 473 CYS B CA  1 
ATOM   8944  C C   . CYS B 1 473 ? 2.579   35.555  -27.697 1.00 28.58  ? 473 CYS B C   1 
ATOM   8945  O O   . CYS B 1 473 ? 2.465   35.333  -26.503 1.00 30.66  ? 473 CYS B O   1 
ATOM   8946  C CB  . CYS B 1 473 ? 0.611   36.407  -28.933 1.00 31.31  ? 473 CYS B CB  1 
ATOM   8947  S SG  . CYS B 1 473 ? -0.427  37.778  -29.438 1.00 39.34  ? 473 CYS B SG  1 
ATOM   8948  N N   . VAL B 1 474 ? 3.212   34.733  -28.529 1.00 27.58  ? 474 VAL B N   1 
ATOM   8949  C CA  . VAL B 1 474 ? 3.920   33.526  -28.052 1.00 27.98  ? 474 VAL B CA  1 
ATOM   8950  C C   . VAL B 1 474 ? 5.040   33.915  -27.096 1.00 27.37  ? 474 VAL B C   1 
ATOM   8951  O O   . VAL B 1 474 ? 5.300   33.220  -26.099 1.00 27.33  ? 474 VAL B O   1 
ATOM   8952  C CB  . VAL B 1 474 ? 4.527   32.714  -29.240 1.00 28.27  ? 474 VAL B CB  1 
ATOM   8953  C CG1 . VAL B 1 474 ? 5.514   31.662  -28.753 1.00 25.78  ? 474 VAL B CG1 1 
ATOM   8954  C CG2 . VAL B 1 474 ? 3.407   32.077  -30.065 1.00 28.51  ? 474 VAL B CG2 1 
ATOM   8955  N N   . ALA B 1 475 ? 5.696   35.030  -27.392 1.00 26.00  ? 475 ALA B N   1 
ATOM   8956  C CA  . ALA B 1 475 ? 6.787   35.496  -26.559 1.00 27.18  ? 475 ALA B CA  1 
ATOM   8957  C C   . ALA B 1 475 ? 6.274   36.010  -25.189 1.00 27.49  ? 475 ALA B C   1 
ATOM   8958  O O   . ALA B 1 475 ? 6.847   35.703  -24.147 1.00 29.80  ? 475 ALA B O   1 
ATOM   8959  C CB  . ALA B 1 475 ? 7.624   36.542  -27.290 1.00 25.07  ? 475 ALA B CB  1 
ATOM   8960  N N   . TYR B 1 476 ? 5.154   36.712  -25.192 1.00 28.15  ? 476 TYR B N   1 
ATOM   8961  C CA  . TYR B 1 476 ? 4.535   37.131  -23.942 1.00 27.40  ? 476 TYR B CA  1 
ATOM   8962  C C   . TYR B 1 476 ? 4.110   35.910  -23.095 1.00 27.94  ? 476 TYR B C   1 
ATOM   8963  O O   . TYR B 1 476 ? 4.267   35.918  -21.858 1.00 26.01  ? 476 TYR B O   1 
ATOM   8964  C CB  . TYR B 1 476 ? 3.357   38.027  -24.202 1.00 26.29  ? 476 TYR B CB  1 
ATOM   8965  C CG  . TYR B 1 476 ? 3.680   39.484  -24.339 1.00 27.29  ? 476 TYR B CG  1 
ATOM   8966  C CD1 . TYR B 1 476 ? 4.376   40.166  -23.334 1.00 27.74  ? 476 TYR B CD1 1 
ATOM   8967  C CD2 . TYR B 1 476 ? 3.214   40.218  -25.442 1.00 27.35  ? 476 TYR B CD2 1 
ATOM   8968  C CE1 . TYR B 1 476 ? 4.642   41.523  -23.445 1.00 28.90  ? 476 TYR B CE1 1 
ATOM   8969  C CE2 . TYR B 1 476 ? 3.461   41.580  -25.560 1.00 28.66  ? 476 TYR B CE2 1 
ATOM   8970  C CZ  . TYR B 1 476 ? 4.185   42.225  -24.561 1.00 29.32  ? 476 TYR B CZ  1 
ATOM   8971  O OH  . TYR B 1 476 ? 4.452   43.553  -24.675 1.00 30.35  ? 476 TYR B OH  1 
ATOM   8972  N N   . LYS B 1 477 ? 3.600   34.864  -23.754 1.00 26.43  ? 477 LYS B N   1 
ATOM   8973  C CA  . LYS B 1 477 ? 3.294   33.630  -23.034 1.00 28.08  ? 477 LYS B CA  1 
ATOM   8974  C C   . LYS B 1 477 ? 4.571   32.989  -22.480 1.00 28.18  ? 477 LYS B C   1 
ATOM   8975  O O   . LYS B 1 477 ? 4.577   32.499  -21.356 1.00 29.27  ? 477 LYS B O   1 
ATOM   8976  C CB  . LYS B 1 477 ? 2.509   32.639  -23.896 1.00 29.67  ? 477 LYS B CB  1 
ATOM   8977  C CG  . LYS B 1 477 ? 1.976   31.467  -23.081 1.00 31.72  ? 477 LYS B CG  1 
ATOM   8978  C CD  . LYS B 1 477 ? 1.030   30.578  -23.878 1.00 34.33  ? 477 LYS B CD  1 
ATOM   8979  C CE  . LYS B 1 477 ? 0.730   29.311  -23.093 1.00 34.98  ? 477 LYS B CE  1 
ATOM   8980  N NZ  . LYS B 1 477 ? -0.252  28.403  -23.752 1.00 35.24  ? 477 LYS B NZ  1 
ATOM   8981  N N   . PHE B 1 478 ? 5.653   33.033  -23.269 1.00 27.26  ? 478 PHE B N   1 
ATOM   8982  C CA  . PHE B 1 478 ? 6.961   32.566  -22.837 1.00 26.69  ? 478 PHE B CA  1 
ATOM   8983  C C   . PHE B 1 478 ? 7.384   33.283  -21.576 1.00 26.95  ? 478 PHE B C   1 
ATOM   8984  O O   . PHE B 1 478 ? 7.854   32.668  -20.629 1.00 24.95  ? 478 PHE B O   1 
ATOM   8985  C CB  . PHE B 1 478 ? 8.020   32.801  -23.928 1.00 26.42  ? 478 PHE B CB  1 
ATOM   8986  C CG  . PHE B 1 478 ? 9.408   32.374  -23.527 1.00 25.81  ? 478 PHE B CG  1 
ATOM   8987  C CD1 . PHE B 1 478 ? 9.830   31.070  -23.729 1.00 25.34  ? 478 PHE B CD1 1 
ATOM   8988  C CD2 . PHE B 1 478 ? 10.275  33.272  -22.911 1.00 26.06  ? 478 PHE B CD2 1 
ATOM   8989  C CE1 . PHE B 1 478 ? 11.097  30.670  -23.351 1.00 26.02  ? 478 PHE B CE1 1 
ATOM   8990  C CE2 . PHE B 1 478 ? 11.544  32.876  -22.512 1.00 26.84  ? 478 PHE B CE2 1 
ATOM   8991  C CZ  . PHE B 1 478 ? 11.957  31.573  -22.736 1.00 26.66  ? 478 PHE B CZ  1 
ATOM   8992  N N   . ASP B 1 479 ? 7.227   34.603  -21.575 1.00 28.09  ? 479 ASP B N   1 
ATOM   8993  C CA  . ASP B 1 479 ? 7.661   35.381  -20.456 1.00 27.07  ? 479 ASP B CA  1 
ATOM   8994  C C   . ASP B 1 479 ? 6.805   35.052  -19.215 1.00 27.87  ? 479 ASP B C   1 
ATOM   8995  O O   . ASP B 1 479 ? 7.337   34.963  -18.093 1.00 25.67  ? 479 ASP B O   1 
ATOM   8996  C CB  . ASP B 1 479 ? 7.586   36.852  -20.807 1.00 28.46  ? 479 ASP B CB  1 
ATOM   8997  C CG  . ASP B 1 479 ? 7.914   37.728  -19.638 1.00 28.89  ? 479 ASP B CG  1 
ATOM   8998  O OD1 . ASP B 1 479 ? 9.090   37.759  -19.198 1.00 29.32  ? 479 ASP B OD1 1 
ATOM   8999  O OD2 . ASP B 1 479 ? 6.981   38.371  -19.144 1.00 31.58  ? 479 ASP B OD2 1 
ATOM   9000  N N   . ALA B 1 480 ? 5.492   34.835  -19.435 1.00 27.77  ? 480 ALA B N   1 
ATOM   9001  C CA  . ALA B 1 480 ? 4.560   34.443  -18.365 1.00 28.91  ? 480 ALA B CA  1 
ATOM   9002  C C   . ALA B 1 480 ? 4.878   33.051  -17.771 1.00 30.54  ? 480 ALA B C   1 
ATOM   9003  O O   . ALA B 1 480 ? 4.785   32.844  -16.553 1.00 31.76  ? 480 ALA B O   1 
ATOM   9004  C CB  . ALA B 1 480 ? 3.117   34.497  -18.858 1.00 28.36  ? 480 ALA B CB  1 
ATOM   9005  N N   . ALA B 1 481 ? 5.240   32.108  -18.631 1.00 30.00  ? 481 ALA B N   1 
ATOM   9006  C CA  . ALA B 1 481 ? 5.751   30.814  -18.178 1.00 31.95  ? 481 ALA B CA  1 
ATOM   9007  C C   . ALA B 1 481 ? 7.037   31.008  -17.351 1.00 32.48  ? 481 ALA B C   1 
ATOM   9008  O O   . ALA B 1 481 ? 7.227   30.340  -16.332 1.00 35.48  ? 481 ALA B O   1 
ATOM   9009  C CB  . ALA B 1 481 ? 6.001   29.884  -19.374 1.00 29.16  ? 481 ALA B CB  1 
ATOM   9010  N N   . MET B 1 482 ? 7.892   31.936  -17.771 1.00 31.48  ? 482 MET B N   1 
ATOM   9011  C CA  . MET B 1 482 ? 9.161   32.167  -17.075 1.00 34.26  ? 482 MET B CA  1 
ATOM   9012  C C   . MET B 1 482 ? 8.905   32.603  -15.654 1.00 34.45  ? 482 MET B C   1 
ATOM   9013  O O   . MET B 1 482 ? 9.612   32.184  -14.754 1.00 35.46  ? 482 MET B O   1 
ATOM   9014  C CB  . MET B 1 482 ? 10.021  33.238  -17.769 1.00 33.98  ? 482 MET B CB  1 
ATOM   9015  C CG  . MET B 1 482 ? 10.690  32.815  -19.062 1.00 32.85  ? 482 MET B CG  1 
ATOM   9016  S SD  . MET B 1 482 ? 11.616  31.296  -18.866 1.00 34.20  ? 482 MET B SD  1 
ATOM   9017  C CE  . MET B 1 482 ? 10.420  30.183  -19.586 1.00 38.52  ? 482 MET B CE  1 
ATOM   9018  N N   . MET B 1 483 ? 7.910   33.474  -15.462 1.00 35.25  ? 483 MET B N   1 
ATOM   9019  C CA  . MET B 1 483 ? 7.619   34.013  -14.132 1.00 35.39  ? 483 MET B CA  1 
ATOM   9020  C C   . MET B 1 483 ? 7.121   32.882  -13.239 1.00 35.64  ? 483 MET B C   1 
ATOM   9021  O O   . MET B 1 483 ? 7.548   32.743  -12.094 1.00 34.31  ? 483 MET B O   1 
ATOM   9022  C CB  . MET B 1 483 ? 6.609   35.155  -14.201 1.00 36.39  ? 483 MET B CB  1 
ATOM   9023  C CG  . MET B 1 483 ? 7.123   36.425  -14.888 1.00 41.19  ? 483 MET B CG  1 
ATOM   9024  S SD  . MET B 1 483 ? 8.738   37.003  -14.293 1.00 43.14  ? 483 MET B SD  1 
ATOM   9025  C CE  . MET B 1 483 ? 9.773   36.571  -15.694 1.00 48.37  ? 483 MET B CE  1 
ATOM   9026  N N   . ALA B 1 484 ? 6.276   32.030  -13.809 1.00 35.92  ? 484 ALA B N   1 
ATOM   9027  C CA  . ALA B 1 484 ? 5.786   30.867  -13.113 1.00 36.14  ? 484 ALA B CA  1 
ATOM   9028  C C   . ALA B 1 484 ? 6.921   29.904  -12.766 1.00 36.55  ? 484 ALA B C   1 
ATOM   9029  O O   . ALA B 1 484 ? 6.867   29.239  -11.744 1.00 36.67  ? 484 ALA B O   1 
ATOM   9030  C CB  . ALA B 1 484 ? 4.714   30.165  -13.940 1.00 35.28  ? 484 ALA B CB  1 
ATOM   9031  N N   . LEU B 1 485 ? 7.921   29.798  -13.645 1.00 37.30  ? 485 LEU B N   1 
ATOM   9032  C CA  . LEU B 1 485 ? 9.041   28.891  -13.417 1.00 36.26  ? 485 LEU B CA  1 
ATOM   9033  C C   . LEU B 1 485 ? 9.801   29.385  -12.192 1.00 36.72  ? 485 LEU B C   1 
ATOM   9034  O O   . LEU B 1 485 ? 10.229  28.594  -11.340 1.00 35.10  ? 485 LEU B O   1 
ATOM   9035  C CB  . LEU B 1 485 ? 9.961   28.819  -14.650 1.00 34.54  ? 485 LEU B CB  1 
ATOM   9036  C CG  . LEU B 1 485 ? 10.111  27.550  -15.516 1.00 36.84  ? 485 LEU B CG  1 
ATOM   9037  C CD1 . LEU B 1 485 ? 8.855   26.696  -15.643 1.00 38.44  ? 485 LEU B CD1 1 
ATOM   9038  C CD2 . LEU B 1 485 ? 10.620  27.891  -16.904 1.00 34.71  ? 485 LEU B CD2 1 
ATOM   9039  N N   . ARG B 1 486 ? 9.937   30.705  -12.103 1.00 37.20  ? 486 ARG B N   1 
ATOM   9040  C CA  . ARG B 1 486 ? 10.617  31.342  -10.990 1.00 38.13  ? 486 ARG B CA  1 
ATOM   9041  C C   . ARG B 1 486 ? 9.846   31.226  -9.661  1.00 36.53  ? 486 ARG B C   1 
ATOM   9042  O O   . ARG B 1 486 ? 10.436  30.885  -8.639  1.00 37.47  ? 486 ARG B O   1 
ATOM   9043  C CB  . ARG B 1 486 ? 10.874  32.810  -11.313 1.00 41.68  ? 486 ARG B CB  1 
ATOM   9044  C CG  . ARG B 1 486 ? 11.616  33.568  -10.230 1.00 45.85  ? 486 ARG B CG  1 
ATOM   9045  C CD  . ARG B 1 486 ? 13.044  33.062  -10.091 1.00 55.22  ? 486 ARG B CD  1 
ATOM   9046  N NE  . ARG B 1 486 ? 13.782  33.762  -9.046  1.00 62.53  ? 486 ARG B NE  1 
ATOM   9047  C CZ  . ARG B 1 486 ? 15.086  33.622  -8.832  1.00 72.50  ? 486 ARG B CZ  1 
ATOM   9048  N NH1 . ARG B 1 486 ? 15.812  32.811  -9.597  1.00 76.47  ? 486 ARG B NH1 1 
ATOM   9049  N NH2 . ARG B 1 486 ? 15.673  34.301  -7.855  1.00 77.97  ? 486 ARG B NH2 1 
ATOM   9050  N N   . THR B 1 487 ? 8.540   31.500  -9.687  1.00 34.12  ? 487 THR B N   1 
ATOM   9051  C CA  . THR B 1 487 ? 7.752   31.671  -8.453  1.00 33.92  ? 487 THR B CA  1 
ATOM   9052  C C   . THR B 1 487 ? 7.134   30.384  -7.914  1.00 35.04  ? 487 THR B C   1 
ATOM   9053  O O   . THR B 1 487 ? 6.951   30.250  -6.714  1.00 37.45  ? 487 THR B O   1 
ATOM   9054  C CB  . THR B 1 487 ? 6.620   32.715  -8.599  1.00 33.22  ? 487 THR B CB  1 
ATOM   9055  O OG1 . THR B 1 487 ? 5.700   32.303  -9.619  1.00 32.76  ? 487 THR B OG1 1 
ATOM   9056  C CG2 . THR B 1 487 ? 7.175   34.107  -8.923  1.00 32.34  ? 487 THR B CG2 1 
ATOM   9057  N N   . SER B 1 488 ? 6.800   29.445  -8.786  1.00 34.67  ? 488 SER B N   1 
ATOM   9058  C CA  . SER B 1 488 ? 6.144   28.215  -8.332  1.00 34.41  ? 488 SER B CA  1 
ATOM   9059  C C   . SER B 1 488 ? 7.008   26.956  -8.441  1.00 36.01  ? 488 SER B C   1 
ATOM   9060  O O   . SER B 1 488 ? 6.936   26.079  -7.577  1.00 36.68  ? 488 SER B O   1 
ATOM   9061  C CB  . SER B 1 488 ? 4.812   28.025  -9.059  1.00 33.87  ? 488 SER B CB  1 
ATOM   9062  O OG  . SER B 1 488 ? 4.299   26.734  -8.833  1.00 36.12  ? 488 SER B OG  1 
ATOM   9063  N N   . PHE B 1 489 ? 7.805   26.843  -9.506  1.00 33.47  ? 489 PHE B N   1 
ATOM   9064  C CA  . PHE B 1 489 ? 8.711   25.699  -9.626  1.00 35.24  ? 489 PHE B CA  1 
ATOM   9065  C C   . PHE B 1 489 ? 10.013  26.009  -8.892  1.00 37.07  ? 489 PHE B C   1 
ATOM   9066  O O   . PHE B 1 489 ? 10.842  25.126  -8.661  1.00 36.81  ? 489 PHE B O   1 
ATOM   9067  C CB  . PHE B 1 489 ? 9.029   25.401  -11.098 1.00 32.75  ? 489 PHE B CB  1 
ATOM   9068  C CG  . PHE B 1 489 ? 7.872   24.833  -11.887 1.00 31.17  ? 489 PHE B CG  1 
ATOM   9069  C CD1 . PHE B 1 489 ? 6.848   25.664  -12.354 1.00 30.20  ? 489 PHE B CD1 1 
ATOM   9070  C CD2 . PHE B 1 489 ? 7.862   23.499  -12.250 1.00 30.34  ? 489 PHE B CD2 1 
ATOM   9071  C CE1 . PHE B 1 489 ? 5.808   25.156  -13.116 1.00 29.26  ? 489 PHE B CE1 1 
ATOM   9072  C CE2 . PHE B 1 489 ? 6.820   22.984  -13.013 1.00 31.83  ? 489 PHE B CE2 1 
ATOM   9073  C CZ  . PHE B 1 489 ? 5.785   23.808  -13.436 1.00 29.53  ? 489 PHE B CZ  1 
ATOM   9074  N N   . LEU B 1 490 ? 10.203  27.292  -8.599  1.00 39.60  ? 490 LEU B N   1 
ATOM   9075  C CA  . LEU B 1 490 ? 11.387  27.804  -7.920  1.00 43.43  ? 490 LEU B CA  1 
ATOM   9076  C C   . LEU B 1 490 ? 12.710  27.500  -8.655  1.00 45.23  ? 490 LEU B C   1 
ATOM   9077  O O   . LEU B 1 490 ? 13.608  26.893  -8.073  1.00 46.21  ? 490 LEU B O   1 
ATOM   9078  C CB  . LEU B 1 490 ? 11.432  27.300  -6.462  1.00 42.67  ? 490 LEU B CB  1 
ATOM   9079  C CG  . LEU B 1 490 ? 10.206  27.554  -5.557  1.00 43.92  ? 490 LEU B CG  1 
ATOM   9080  C CD1 . LEU B 1 490 ? 10.367  26.866  -4.197  1.00 41.01  ? 490 LEU B CD1 1 
ATOM   9081  C CD2 . LEU B 1 490 ? 9.944   29.051  -5.381  1.00 43.48  ? 490 LEU B CD2 1 
ATOM   9082  N N   . VAL B 1 491 ? 12.861  27.989  -9.892  1.00 46.15  ? 491 VAL B N   1 
ATOM   9083  C CA  . VAL B 1 491 ? 13.965  27.507  -10.765 1.00 49.59  ? 491 VAL B CA  1 
ATOM   9084  C C   . VAL B 1 491 ? 15.430  27.909  -10.416 1.00 53.63  ? 491 VAL B C   1 
ATOM   9085  O O   . VAL B 1 491 ? 16.266  27.027  -10.169 1.00 57.87  ? 491 VAL B O   1 
ATOM   9086  C CB  . VAL B 1 491 ? 13.630  27.608  -12.290 1.00 47.39  ? 491 VAL B CB  1 
ATOM   9087  C CG1 . VAL B 1 491 ? 14.889  27.579  -13.156 1.00 45.15  ? 491 VAL B CG1 1 
ATOM   9088  C CG2 . VAL B 1 491 ? 12.698  26.474  -12.687 1.00 44.29  ? 491 VAL B CG2 1 
ATOM   9089  N N   . ASN B 1 492 ? 15.741  29.205  -10.400 1.00 53.52  ? 492 ASN B N   1 
ATOM   9090  C CA  . ASN B 1 492 ? 17.146  29.682  -10.212 1.00 59.90  ? 492 ASN B CA  1 
ATOM   9091  C C   . ASN B 1 492 ? 18.069  29.522  -11.436 1.00 61.35  ? 492 ASN B C   1 
ATOM   9092  O O   . ASN B 1 492 ? 18.668  30.505  -11.883 1.00 65.59  ? 492 ASN B O   1 
ATOM   9093  C CB  . ASN B 1 492 ? 17.833  29.063  -8.971  1.00 60.97  ? 492 ASN B CB  1 
ATOM   9094  C CG  . ASN B 1 492 ? 17.035  29.249  -7.691  1.00 66.98  ? 492 ASN B CG  1 
ATOM   9095  O OD1 . ASN B 1 492 ? 16.280  30.219  -7.539  1.00 70.45  ? 492 ASN B OD1 1 
ATOM   9096  N ND2 . ASN B 1 492 ? 17.199  28.310  -6.754  1.00 66.38  ? 492 ASN B ND2 1 
ATOM   9097  N N   . ASP B 1 493 ? 18.202  28.288  -11.949 1.00 58.70  ? 493 ASP B N   1 
ATOM   9098  C CA  . ASP B 1 493 ? 19.091  27.992  -13.100 1.00 56.43  ? 493 ASP B CA  1 
ATOM   9099  C C   . ASP B 1 493 ? 18.325  27.803  -14.433 1.00 53.11  ? 493 ASP B C   1 
ATOM   9100  O O   . ASP B 1 493 ? 17.768  26.731  -14.707 1.00 50.32  ? 493 ASP B O   1 
ATOM   9101  C CB  . ASP B 1 493 ? 19.972  26.764  -12.801 1.00 57.62  ? 493 ASP B CB  1 
ATOM   9102  C CG  . ASP B 1 493 ? 20.999  26.472  -13.910 1.00 62.33  ? 493 ASP B CG  1 
ATOM   9103  O OD1 . ASP B 1 493 ? 21.126  27.266  -14.874 1.00 59.91  ? 493 ASP B OD1 1 
ATOM   9104  O OD2 . ASP B 1 493 ? 21.687  25.432  -13.810 1.00 66.72  ? 493 ASP B OD2 1 
ATOM   9105  N N   . PHE B 1 494 ? 18.347  28.832  -15.274 1.00 49.15  ? 494 PHE B N   1 
ATOM   9106  C CA  . PHE B 1 494 ? 17.491  28.854  -16.463 1.00 49.45  ? 494 PHE B CA  1 
ATOM   9107  C C   . PHE B 1 494 ? 18.147  28.324  -17.759 1.00 49.28  ? 494 PHE B C   1 
ATOM   9108  O O   . PHE B 1 494 ? 17.603  28.493  -18.847 1.00 47.70  ? 494 PHE B O   1 
ATOM   9109  C CB  . PHE B 1 494 ? 16.883  30.246  -16.663 1.00 49.01  ? 494 PHE B CB  1 
ATOM   9110  C CG  . PHE B 1 494 ? 15.848  30.604  -15.628 1.00 49.79  ? 494 PHE B CG  1 
ATOM   9111  C CD1 . PHE B 1 494 ? 14.503  30.297  -15.834 1.00 48.51  ? 494 PHE B CD1 1 
ATOM   9112  C CD2 . PHE B 1 494 ? 16.219  31.230  -14.437 1.00 49.55  ? 494 PHE B CD2 1 
ATOM   9113  C CE1 . PHE B 1 494 ? 13.548  30.615  -14.878 1.00 52.70  ? 494 PHE B CE1 1 
ATOM   9114  C CE2 . PHE B 1 494 ? 15.270  31.541  -13.477 1.00 51.55  ? 494 PHE B CE2 1 
ATOM   9115  C CZ  . PHE B 1 494 ? 13.932  31.235  -13.696 1.00 51.64  ? 494 PHE B CZ  1 
ATOM   9116  N N   . GLY B 1 495 ? 19.281  27.647  -17.617 1.00 47.96  ? 495 GLY B N   1 
ATOM   9117  C CA  . GLY B 1 495 ? 20.035  27.128  -18.749 1.00 50.05  ? 495 GLY B CA  1 
ATOM   9118  C C   . GLY B 1 495 ? 19.224  26.330  -19.760 1.00 48.92  ? 495 GLY B C   1 
ATOM   9119  O O   . GLY B 1 495 ? 19.328  26.578  -20.978 1.00 48.57  ? 495 GLY B O   1 
ATOM   9120  N N   . PHE B 1 496 ? 18.419  25.383  -19.260 1.00 43.83  ? 496 PHE B N   1 
ATOM   9121  C CA  . PHE B 1 496 ? 17.605  24.481  -20.102 1.00 38.56  ? 496 PHE B CA  1 
ATOM   9122  C C   . PHE B 1 496 ? 16.620  25.229  -20.998 1.00 36.38  ? 496 PHE B C   1 
ATOM   9123  O O   . PHE B 1 496 ? 16.106  24.671  -21.965 1.00 36.06  ? 496 PHE B O   1 
ATOM   9124  C CB  . PHE B 1 496 ? 16.838  23.467  -19.235 1.00 37.61  ? 496 PHE B CB  1 
ATOM   9125  C CG  . PHE B 1 496 ? 15.664  24.060  -18.494 1.00 35.13  ? 496 PHE B CG  1 
ATOM   9126  C CD1 . PHE B 1 496 ? 15.844  24.668  -17.252 1.00 34.33  ? 496 PHE B CD1 1 
ATOM   9127  C CD2 . PHE B 1 496 ? 14.384  24.028  -19.046 1.00 33.98  ? 496 PHE B CD2 1 
ATOM   9128  C CE1 . PHE B 1 496 ? 14.768  25.226  -16.568 1.00 35.14  ? 496 PHE B CE1 1 
ATOM   9129  C CE2 . PHE B 1 496 ? 13.304  24.598  -18.376 1.00 35.12  ? 496 PHE B CE2 1 
ATOM   9130  C CZ  . PHE B 1 496 ? 13.491  25.191  -17.132 1.00 34.85  ? 496 PHE B CZ  1 
ATOM   9131  N N   . ILE B 1 497 ? 16.353  26.489  -20.669 1.00 35.35  ? 497 ILE B N   1 
ATOM   9132  C CA  . ILE B 1 497 ? 15.420  27.311  -21.441 1.00 34.79  ? 497 ILE B CA  1 
ATOM   9133  C C   . ILE B 1 497 ? 15.893  27.548  -22.888 1.00 33.21  ? 497 ILE B C   1 
ATOM   9134  O O   . ILE B 1 497 ? 15.079  27.586  -23.828 1.00 31.27  ? 497 ILE B O   1 
ATOM   9135  C CB  . ILE B 1 497 ? 15.128  28.634  -20.706 1.00 36.11  ? 497 ILE B CB  1 
ATOM   9136  C CG1 . ILE B 1 497 ? 13.929  28.453  -19.791 1.00 35.39  ? 497 ILE B CG1 1 
ATOM   9137  C CG2 . ILE B 1 497 ? 14.932  29.806  -21.665 1.00 35.40  ? 497 ILE B CG2 1 
ATOM   9138  C CD1 . ILE B 1 497 ? 14.304  27.860  -18.461 1.00 36.74  ? 497 ILE B CD1 1 
ATOM   9139  N N   . TRP B 1 498 ? 17.208  27.661  -23.068 1.00 31.85  ? 498 TRP B N   1 
ATOM   9140  C CA  . TRP B 1 498 ? 17.769  27.946  -24.386 1.00 30.78  ? 498 TRP B CA  1 
ATOM   9141  C C   . TRP B 1 498 ? 17.302  26.964  -25.432 1.00 31.16  ? 498 TRP B C   1 
ATOM   9142  O O   . TRP B 1 498 ? 16.820  27.355  -26.480 1.00 28.19  ? 498 TRP B O   1 
ATOM   9143  C CB  . TRP B 1 498 ? 19.291  27.963  -24.337 1.00 31.55  ? 498 TRP B CB  1 
ATOM   9144  C CG  . TRP B 1 498 ? 19.878  28.249  -25.689 1.00 30.71  ? 498 TRP B CG  1 
ATOM   9145  C CD1 . TRP B 1 498 ? 20.782  27.476  -26.398 1.00 30.97  ? 498 TRP B CD1 1 
ATOM   9146  C CD2 . TRP B 1 498 ? 19.553  29.381  -26.569 1.00 29.92  ? 498 TRP B CD2 1 
ATOM   9147  N NE1 . TRP B 1 498 ? 21.042  28.045  -27.626 1.00 31.65  ? 498 TRP B NE1 1 
ATOM   9148  C CE2 . TRP B 1 498 ? 20.325  29.194  -27.781 1.00 30.76  ? 498 TRP B CE2 1 
ATOM   9149  C CE3 . TRP B 1 498 ? 18.719  30.501  -26.462 1.00 29.17  ? 498 TRP B CE3 1 
ATOM   9150  C CZ2 . TRP B 1 498 ? 20.271  30.105  -28.842 1.00 31.02  ? 498 TRP B CZ2 1 
ATOM   9151  C CZ3 . TRP B 1 498 ? 18.661  31.402  -27.533 1.00 29.18  ? 498 TRP B CZ3 1 
ATOM   9152  C CH2 . TRP B 1 498 ? 19.420  31.206  -28.696 1.00 29.18  ? 498 TRP B CH2 1 
ATOM   9153  N N   . LEU B 1 499 ? 17.433  25.668  -25.150 1.00 33.11  ? 499 LEU B N   1 
ATOM   9154  C CA  . LEU B 1 499 ? 17.102  24.668  -26.164 1.00 33.42  ? 499 LEU B CA  1 
ATOM   9155  C C   . LEU B 1 499 ? 15.615  24.555  -26.430 1.00 31.16  ? 499 LEU B C   1 
ATOM   9156  O O   . LEU B 1 499 ? 15.217  24.350  -27.575 1.00 31.66  ? 499 LEU B O   1 
ATOM   9157  C CB  . LEU B 1 499 ? 17.731  23.301  -25.854 1.00 36.50  ? 499 LEU B CB  1 
ATOM   9158  C CG  . LEU B 1 499 ? 19.206  23.185  -26.267 1.00 38.69  ? 499 LEU B CG  1 
ATOM   9159  C CD1 . LEU B 1 499 ? 19.860  21.962  -25.633 1.00 39.15  ? 499 LEU B CD1 1 
ATOM   9160  C CD2 . LEU B 1 499 ? 19.385  23.187  -27.788 1.00 37.81  ? 499 LEU B CD2 1 
ATOM   9161  N N   . VAL B 1 500 ? 14.791  24.706  -25.389 1.00 29.24  ? 500 VAL B N   1 
ATOM   9162  C CA  . VAL B 1 500 ? 13.330  24.745  -25.569 1.00 28.60  ? 500 VAL B CA  1 
ATOM   9163  C C   . VAL B 1 500 ? 12.939  25.949  -26.437 1.00 29.61  ? 500 VAL B C   1 
ATOM   9164  O O   . VAL B 1 500 ? 12.173  25.805  -27.424 1.00 30.20  ? 500 VAL B O   1 
ATOM   9165  C CB  . VAL B 1 500 ? 12.578  24.828  -24.213 1.00 29.21  ? 500 VAL B CB  1 
ATOM   9166  C CG1 . VAL B 1 500 ? 11.066  24.879  -24.422 1.00 26.70  ? 500 VAL B CG1 1 
ATOM   9167  C CG2 . VAL B 1 500 ? 12.968  23.664  -23.301 1.00 28.53  ? 500 VAL B CG2 1 
ATOM   9168  N N   . LEU B 1 501 ? 13.463  27.124  -26.069 1.00 27.71  ? 501 LEU B N   1 
ATOM   9169  C CA  . LEU B 1 501 ? 13.272  28.342  -26.838 1.00 28.50  ? 501 LEU B CA  1 
ATOM   9170  C C   . LEU B 1 501 ? 13.652  28.139  -28.314 1.00 29.04  ? 501 LEU B C   1 
ATOM   9171  O O   . LEU B 1 501 ? 12.838  28.411  -29.194 1.00 29.80  ? 501 LEU B O   1 
ATOM   9172  C CB  . LEU B 1 501 ? 14.052  29.559  -26.223 1.00 26.98  ? 501 LEU B CB  1 
ATOM   9173  C CG  . LEU B 1 501 ? 13.825  30.923  -26.948 1.00 27.60  ? 501 LEU B CG  1 
ATOM   9174  C CD1 . LEU B 1 501 ? 12.336  31.218  -27.168 1.00 27.35  ? 501 LEU B CD1 1 
ATOM   9175  C CD2 . LEU B 1 501 ? 14.505  32.117  -26.267 1.00 26.50  ? 501 LEU B CD2 1 
ATOM   9176  N N   . SER B 1 502 ? 14.870  27.654  -28.572 1.00 30.20  ? 502 SER B N   1 
ATOM   9177  C CA  . SER B 1 502 ? 15.318  27.345  -29.955 1.00 32.34  ? 502 SER B CA  1 
ATOM   9178  C C   . SER B 1 502 ? 14.391  26.407  -30.713 1.00 31.50  ? 502 SER B C   1 
ATOM   9179  O O   . SER B 1 502 ? 14.059  26.682  -31.862 1.00 31.87  ? 502 SER B O   1 
ATOM   9180  C CB  . SER B 1 502 ? 16.736  26.771  -29.978 1.00 34.24  ? 502 SER B CB  1 
ATOM   9181  O OG  . SER B 1 502 ? 17.682  27.763  -29.626 1.00 40.76  ? 502 SER B OG  1 
ATOM   9182  N N   . SER B 1 503 ? 14.020  25.280  -30.092 1.00 31.09  ? 503 SER B N   1 
ATOM   9183  C CA  . SER B 1 503 ? 13.002  24.369  -30.653 1.00 31.59  ? 503 SER B CA  1 
ATOM   9184  C C   . SER B 1 503 ? 11.691  25.048  -30.982 1.00 30.54  ? 503 SER B C   1 
ATOM   9185  O O   . SER B 1 503 ? 11.074  24.736  -31.986 1.00 29.94  ? 503 SER B O   1 
ATOM   9186  C CB  . SER B 1 503 ? 12.686  23.242  -29.691 1.00 34.15  ? 503 SER B CB  1 
ATOM   9187  O OG  . SER B 1 503 ? 13.590  22.189  -29.874 1.00 45.58  ? 503 SER B OG  1 
ATOM   9188  N N   . THR B 1 504 ? 11.249  25.949  -30.107 1.00 31.58  ? 504 THR B N   1 
ATOM   9189  C CA  . THR B 1 504 ? 9.981   26.647  -30.301 1.00 31.48  ? 504 THR B CA  1 
ATOM   9190  C C   . THR B 1 504 ? 10.041  27.498  -31.564 1.00 30.23  ? 504 THR B C   1 
ATOM   9191  O O   . THR B 1 504 ? 9.220   27.342  -32.467 1.00 31.80  ? 504 THR B O   1 
ATOM   9192  C CB  . THR B 1 504 ? 9.606   27.491  -29.061 1.00 32.21  ? 504 THR B CB  1 
ATOM   9193  O OG1 . THR B 1 504 ? 9.594   26.648  -27.913 1.00 31.66  ? 504 THR B OG1 1 
ATOM   9194  C CG2 . THR B 1 504 ? 8.224   28.107  -29.213 1.00 32.58  ? 504 THR B CG2 1 
ATOM   9195  N N   . VAL B 1 505 ? 11.048  28.354  -31.656 1.00 30.56  ? 505 VAL B N   1 
ATOM   9196  C CA  . VAL B 1 505 ? 11.255  29.175  -32.869 1.00 29.08  ? 505 VAL B CA  1 
ATOM   9197  C C   . VAL B 1 505 ? 11.288  28.291  -34.142 1.00 29.22  ? 505 VAL B C   1 
ATOM   9198  O O   . VAL B 1 505 ? 10.631  28.586  -35.153 1.00 27.33  ? 505 VAL B O   1 
ATOM   9199  C CB  . VAL B 1 505 ? 12.534  30.018  -32.754 1.00 29.08  ? 505 VAL B CB  1 
ATOM   9200  C CG1 . VAL B 1 505 ? 12.840  30.751  -34.073 1.00 29.47  ? 505 VAL B CG1 1 
ATOM   9201  C CG2 . VAL B 1 505 ? 12.436  31.001  -31.583 1.00 27.29  ? 505 VAL B CG2 1 
ATOM   9202  N N   . ARG B 1 506 ? 12.006  27.184  -34.069 1.00 28.88  ? 506 ARG B N   1 
ATOM   9203  C CA  . ARG B 1 506 ? 12.034  26.257  -35.189 1.00 29.59  ? 506 ARG B CA  1 
ATOM   9204  C C   . ARG B 1 506 ? 10.618  25.729  -35.515 1.00 28.21  ? 506 ARG B C   1 
ATOM   9205  O O   . ARG B 1 506 ? 10.203  25.737  -36.663 1.00 29.03  ? 506 ARG B O   1 
ATOM   9206  C CB  . ARG B 1 506 ? 13.040  25.131  -34.911 1.00 32.22  ? 506 ARG B CB  1 
ATOM   9207  C CG  . ARG B 1 506 ? 13.262  24.164  -36.077 1.00 34.59  ? 506 ARG B CG  1 
ATOM   9208  C CD  . ARG B 1 506 ? 12.546  22.856  -35.770 1.00 38.66  ? 506 ARG B CD  1 
ATOM   9209  N NE  . ARG B 1 506 ? 11.453  22.603  -36.690 1.00 40.59  ? 506 ARG B NE  1 
ATOM   9210  C CZ  . ARG B 1 506 ? 10.383  21.860  -36.434 1.00 42.08  ? 506 ARG B CZ  1 
ATOM   9211  N NH1 . ARG B 1 506 ? 10.179  21.316  -35.234 1.00 39.37  ? 506 ARG B NH1 1 
ATOM   9212  N NH2 . ARG B 1 506 ? 9.488   21.690  -37.396 1.00 46.68  ? 506 ARG B NH2 1 
ATOM   9213  N N   . ALA B 1 507 ? 9.853   25.367  -34.488 1.00 26.77  ? 507 ALA B N   1 
ATOM   9214  C CA  . ALA B 1 507 ? 8.518   24.778  -34.674 1.00 26.15  ? 507 ALA B CA  1 
ATOM   9215  C C   . ALA B 1 507 ? 7.540   25.748  -35.276 1.00 26.05  ? 507 ALA B C   1 
ATOM   9216  O O   . ALA B 1 507 ? 6.762   25.405  -36.166 1.00 26.05  ? 507 ALA B O   1 
ATOM   9217  C CB  . ALA B 1 507 ? 7.983   24.260  -33.354 1.00 25.21  ? 507 ALA B CB  1 
ATOM   9218  N N   . TYR B 1 508 ? 7.541   26.967  -34.757 1.00 26.69  ? 508 TYR B N   1 
ATOM   9219  C CA  . TYR B 1 508 ? 6.606   27.949  -35.222 1.00 26.28  ? 508 TYR B CA  1 
ATOM   9220  C C   . TYR B 1 508 ? 6.936   28.378  -36.631 1.00 26.25  ? 508 TYR B C   1 
ATOM   9221  O O   . TYR B 1 508 ? 6.049   28.484  -37.459 1.00 27.13  ? 508 TYR B O   1 
ATOM   9222  C CB  . TYR B 1 508 ? 6.535   29.113  -34.235 1.00 26.96  ? 508 TYR B CB  1 
ATOM   9223  C CG  . TYR B 1 508 ? 5.562   28.825  -33.099 1.00 28.52  ? 508 TYR B CG  1 
ATOM   9224  C CD1 . TYR B 1 508 ? 4.201   29.109  -33.232 1.00 29.75  ? 508 TYR B CD1 1 
ATOM   9225  C CD2 . TYR B 1 508 ? 5.986   28.223  -31.929 1.00 28.28  ? 508 TYR B CD2 1 
ATOM   9226  C CE1 . TYR B 1 508 ? 3.310   28.828  -32.214 1.00 29.42  ? 508 TYR B CE1 1 
ATOM   9227  C CE2 . TYR B 1 508 ? 5.097   27.940  -30.907 1.00 29.06  ? 508 TYR B CE2 1 
ATOM   9228  C CZ  . TYR B 1 508 ? 3.766   28.240  -31.052 1.00 29.36  ? 508 TYR B CZ  1 
ATOM   9229  O OH  . TYR B 1 508 ? 2.872   27.969  -30.029 1.00 29.31  ? 508 TYR B OH  1 
ATOM   9230  N N   . ALA B 1 509 ? 8.227   28.533  -36.923 1.00 26.74  ? 509 ALA B N   1 
ATOM   9231  C CA  . ALA B 1 509 ? 8.694   28.874  -38.271 1.00 28.09  ? 509 ALA B CA  1 
ATOM   9232  C C   . ALA B 1 509 ? 8.257   27.844  -39.285 1.00 30.10  ? 509 ALA B C   1 
ATOM   9233  O O   . ALA B 1 509 ? 7.877   28.187  -40.412 1.00 31.96  ? 509 ALA B O   1 
ATOM   9234  C CB  . ALA B 1 509 ? 10.211  29.011  -38.302 1.00 27.04  ? 509 ALA B CB  1 
ATOM   9235  N N   . SER B 1 510 ? 8.336   26.580  -38.886 1.00 30.59  ? 510 SER B N   1 
ATOM   9236  C CA  . SER B 1 510 ? 7.943   25.491  -39.728 1.00 32.75  ? 510 SER B CA  1 
ATOM   9237  C C   . SER B 1 510 ? 6.444   25.478  -39.967 1.00 34.44  ? 510 SER B C   1 
ATOM   9238  O O   . SER B 1 510 ? 6.004   25.281  -41.095 1.00 36.10  ? 510 SER B O   1 
ATOM   9239  C CB  . SER B 1 510 ? 8.386   24.170  -39.112 1.00 33.69  ? 510 SER B CB  1 
ATOM   9240  O OG  . SER B 1 510 ? 7.729   23.094  -39.741 1.00 35.26  ? 510 SER B OG  1 
ATOM   9241  N N   . ARG B 1 511 ? 5.652   25.672  -38.909 1.00 35.27  ? 511 ARG B N   1 
ATOM   9242  C CA  . ARG B 1 511 ? 4.204   25.684  -39.078 1.00 37.29  ? 511 ARG B CA  1 
ATOM   9243  C C   . ARG B 1 511 ? 3.801   26.835  -39.987 1.00 35.77  ? 511 ARG B C   1 
ATOM   9244  O O   . ARG B 1 511 ? 2.976   26.664  -40.870 1.00 36.91  ? 511 ARG B O   1 
ATOM   9245  C CB  . ARG B 1 511 ? 3.456   25.746  -37.734 1.00 39.88  ? 511 ARG B CB  1 
ATOM   9246  C CG  . ARG B 1 511 ? 3.545   24.457  -36.915 1.00 48.86  ? 511 ARG B CG  1 
ATOM   9247  C CD  . ARG B 1 511 ? 2.658   24.522  -35.670 1.00 53.80  ? 511 ARG B CD  1 
ATOM   9248  N NE  . ARG B 1 511 ? 3.113   23.659  -34.574 1.00 54.51  ? 511 ARG B NE  1 
ATOM   9249  C CZ  . ARG B 1 511 ? 3.645   24.103  -33.435 1.00 54.27  ? 511 ARG B CZ  1 
ATOM   9250  N NH1 . ARG B 1 511 ? 3.811   25.402  -33.238 1.00 53.29  ? 511 ARG B NH1 1 
ATOM   9251  N NH2 . ARG B 1 511 ? 4.011   23.244  -32.486 1.00 56.17  ? 511 ARG B NH2 1 
ATOM   9252  N N   . ALA B 1 512 ? 4.406   28.002  -39.787 1.00 33.69  ? 512 ALA B N   1 
ATOM   9253  C CA  . ALA B 1 512 ? 4.175   29.117  -40.699 1.00 33.73  ? 512 ALA B CA  1 
ATOM   9254  C C   . ALA B 1 512 ? 4.574   28.768  -42.138 1.00 34.25  ? 512 ALA B C   1 
ATOM   9255  O O   . ALA B 1 512 ? 3.860   29.116  -43.072 1.00 33.76  ? 512 ALA B O   1 
ATOM   9256  C CB  . ALA B 1 512 ? 4.908   30.358  -40.228 1.00 32.04  ? 512 ALA B CB  1 
ATOM   9257  N N   . PHE B 1 513 ? 5.714   28.089  -42.311 1.00 32.73  ? 513 PHE B N   1 
ATOM   9258  C CA  . PHE B 1 513 ? 6.180   27.753  -43.646 1.00 33.64  ? 513 PHE B CA  1 
ATOM   9259  C C   . PHE B 1 513 ? 5.157   26.875  -44.378 1.00 36.23  ? 513 PHE B C   1 
ATOM   9260  O O   . PHE B 1 513 ? 4.825   27.141  -45.539 1.00 35.84  ? 513 PHE B O   1 
ATOM   9261  C CB  . PHE B 1 513 ? 7.570   27.093  -43.622 1.00 32.58  ? 513 PHE B CB  1 
ATOM   9262  C CG  . PHE B 1 513 ? 8.160   26.859  -45.000 1.00 32.98  ? 513 PHE B CG  1 
ATOM   9263  C CD1 . PHE B 1 513 ? 7.832   25.713  -45.734 1.00 32.99  ? 513 PHE B CD1 1 
ATOM   9264  C CD2 . PHE B 1 513 ? 9.031   27.793  -45.572 1.00 32.73  ? 513 PHE B CD2 1 
ATOM   9265  C CE1 . PHE B 1 513 ? 8.367   25.499  -47.004 1.00 33.37  ? 513 PHE B CE1 1 
ATOM   9266  C CE2 . PHE B 1 513 ? 9.567   27.585  -46.841 1.00 33.27  ? 513 PHE B CE2 1 
ATOM   9267  C CZ  . PHE B 1 513 ? 9.228   26.435  -47.559 1.00 32.70  ? 513 PHE B CZ  1 
ATOM   9268  N N   . LYS B 1 514 ? 4.656   25.846  -43.688 1.00 39.35  ? 514 LYS B N   1 
ATOM   9269  C CA  . LYS B 1 514 ? 3.640   24.943  -44.245 1.00 42.64  ? 514 LYS B CA  1 
ATOM   9270  C C   . LYS B 1 514 ? 2.332   25.655  -44.599 1.00 41.84  ? 514 LYS B C   1 
ATOM   9271  O O   . LYS B 1 514 ? 1.782   25.446  -45.672 1.00 40.76  ? 514 LYS B O   1 
ATOM   9272  C CB  . LYS B 1 514 ? 3.374   23.766  -43.296 1.00 46.55  ? 514 LYS B CB  1 
ATOM   9273  C CG  . LYS B 1 514 ? 4.313   22.589  -43.529 1.00 53.37  ? 514 LYS B CG  1 
ATOM   9274  C CD  . LYS B 1 514 ? 4.389   21.627  -42.344 1.00 56.69  ? 514 LYS B CD  1 
ATOM   9275  C CE  . LYS B 1 514 ? 5.149   20.356  -42.738 1.00 61.98  ? 514 LYS B CE  1 
ATOM   9276  N NZ  . LYS B 1 514 ? 5.363   19.395  -41.614 1.00 61.70  ? 514 LYS B NZ  1 
ATOM   9277  N N   . LYS B 1 515 ? 1.848   26.503  -43.699 1.00 42.47  ? 515 LYS B N   1 
ATOM   9278  C CA  . LYS B 1 515 ? 0.598   27.224  -43.922 1.00 43.02  ? 515 LYS B CA  1 
ATOM   9279  C C   . LYS B 1 515 ? 0.710   28.138  -45.139 1.00 42.14  ? 515 LYS B C   1 
ATOM   9280  O O   . LYS B 1 515 ? -0.213  28.240  -45.948 1.00 43.44  ? 515 LYS B O   1 
ATOM   9281  C CB  . LYS B 1 515 ? 0.208   28.024  -42.670 1.00 45.24  ? 515 LYS B CB  1 
ATOM   9282  C CG  . LYS B 1 515 ? -0.945  27.434  -41.864 1.00 47.46  ? 515 LYS B CG  1 
ATOM   9283  C CD  . LYS B 1 515 ? -0.616  26.058  -41.303 1.00 51.23  ? 515 LYS B CD  1 
ATOM   9284  C CE  . LYS B 1 515 ? -1.544  25.682  -40.149 1.00 52.82  ? 515 LYS B CE  1 
ATOM   9285  N NZ  . LYS B 1 515 ? -2.953  25.455  -40.585 1.00 54.87  ? 515 LYS B NZ  1 
ATOM   9286  N N   . ILE B 1 516 ? 1.866   28.773  -45.278 1.00 40.15  ? 516 ILE B N   1 
ATOM   9287  C CA  . ILE B 1 516 ? 2.116   29.694  -46.364 1.00 37.93  ? 516 ILE B CA  1 
ATOM   9288  C C   . ILE B 1 516 ? 2.103   28.949  -47.697 1.00 39.43  ? 516 ILE B C   1 
ATOM   9289  O O   . ILE B 1 516 ? 1.556   29.450  -48.694 1.00 36.90  ? 516 ILE B O   1 
ATOM   9290  C CB  . ILE B 1 516 ? 3.441   30.467  -46.148 1.00 36.43  ? 516 ILE B CB  1 
ATOM   9291  C CG1 . ILE B 1 516 ? 3.234   31.548  -45.071 1.00 35.14  ? 516 ILE B CG1 1 
ATOM   9292  C CG2 . ILE B 1 516 ? 3.957   31.045  -47.463 1.00 35.82  ? 516 ILE B CG2 1 
ATOM   9293  C CD1 . ILE B 1 516 ? 4.462   32.337  -44.672 1.00 33.65  ? 516 ILE B CD1 1 
ATOM   9294  N N   . VAL B 1 517 ? 2.683   27.747  -47.706 1.00 39.07  ? 517 VAL B N   1 
ATOM   9295  C CA  . VAL B 1 517 ? 2.705   26.928  -48.918 1.00 41.17  ? 517 VAL B CA  1 
ATOM   9296  C C   . VAL B 1 517 ? 1.293   26.486  -49.278 1.00 42.28  ? 517 VAL B C   1 
ATOM   9297  O O   . VAL B 1 517 ? 0.844   26.693  -50.393 1.00 42.64  ? 517 VAL B O   1 
ATOM   9298  C CB  . VAL B 1 517 ? 3.675   25.720  -48.802 1.00 41.64  ? 517 VAL B CB  1 
ATOM   9299  C CG1 . VAL B 1 517 ? 3.355   24.647  -49.852 1.00 41.15  ? 517 VAL B CG1 1 
ATOM   9300  C CG2 . VAL B 1 517 ? 5.122   26.189  -48.949 1.00 38.13  ? 517 VAL B CG2 1 
ATOM   9301  N N   . THR B 1 518 ? 0.588   25.931  -48.302 1.00 44.25  ? 518 THR B N   1 
ATOM   9302  C CA  . THR B 1 518 ? -0.785  25.463  -48.480 1.00 46.82  ? 518 THR B CA  1 
ATOM   9303  C C   . THR B 1 518 ? -1.736  26.521  -49.060 1.00 47.41  ? 518 THR B C   1 
ATOM   9304  O O   . THR B 1 518 ? -2.553  26.221  -49.929 1.00 50.46  ? 518 THR B O   1 
ATOM   9305  C CB  . THR B 1 518 ? -1.347  24.930  -47.151 1.00 45.47  ? 518 THR B CB  1 
ATOM   9306  O OG1 . THR B 1 518 ? -0.549  23.827  -46.724 1.00 46.38  ? 518 THR B OG1 1 
ATOM   9307  C CG2 . THR B 1 518 ? -2.783  24.457  -47.312 1.00 48.19  ? 518 THR B CG2 1 
ATOM   9308  N N   . TYR B 1 519 ? -1.626  27.751  -48.579 1.00 46.68  ? 519 TYR B N   1 
ATOM   9309  C CA  . TYR B 1 519 ? -2.566  28.788  -48.951 1.00 44.26  ? 519 TYR B CA  1 
ATOM   9310  C C   . TYR B 1 519 ? -1.913  29.822  -49.836 1.00 42.30  ? 519 TYR B C   1 
ATOM   9311  O O   . TYR B 1 519 ? -2.275  31.000  -49.822 1.00 42.88  ? 519 TYR B O   1 
ATOM   9312  C CB  . TYR B 1 519 ? -3.174  29.403  -47.704 1.00 47.85  ? 519 TYR B CB  1 
ATOM   9313  C CG  . TYR B 1 519 ? -3.918  28.380  -46.875 1.00 51.23  ? 519 TYR B CG  1 
ATOM   9314  C CD1 . TYR B 1 519 ? -5.099  27.803  -47.351 1.00 54.18  ? 519 TYR B CD1 1 
ATOM   9315  C CD2 . TYR B 1 519 ? -3.426  27.956  -45.644 1.00 49.55  ? 519 TYR B CD2 1 
ATOM   9316  C CE1 . TYR B 1 519 ? -5.782  26.848  -46.612 1.00 56.29  ? 519 TYR B CE1 1 
ATOM   9317  C CE2 . TYR B 1 519 ? -4.104  27.005  -44.891 1.00 53.63  ? 519 TYR B CE2 1 
ATOM   9318  C CZ  . TYR B 1 519 ? -5.282  26.452  -45.381 1.00 56.53  ? 519 TYR B CZ  1 
ATOM   9319  O OH  . TYR B 1 519 ? -5.972  25.502  -44.652 1.00 58.84  ? 519 TYR B OH  1 
ATOM   9320  N N   . LYS B 1 520 ? -0.952  29.355  -50.623 1.00 40.51  ? 520 LYS B N   1 
ATOM   9321  C CA  . LYS B 1 520 ? -0.237  30.176  -51.587 1.00 40.06  ? 520 LYS B CA  1 
ATOM   9322  C C   . LYS B 1 520 ? -1.175  30.646  -52.690 1.00 40.95  ? 520 LYS B C   1 
ATOM   9323  O O   . LYS B 1 520 ? -2.013  29.886  -53.175 1.00 40.99  ? 520 LYS B O   1 
ATOM   9324  C CB  . LYS B 1 520 ? 0.912   29.370  -52.178 1.00 39.76  ? 520 LYS B CB  1 
ATOM   9325  C CG  . LYS B 1 520 ? 1.783   30.120  -53.173 1.00 41.92  ? 520 LYS B CG  1 
ATOM   9326  C CD  . LYS B 1 520 ? 2.957   29.272  -53.623 1.00 40.94  ? 520 LYS B CD  1 
ATOM   9327  C CE  . LYS B 1 520 ? 3.988   29.159  -52.517 1.00 41.42  ? 520 LYS B CE  1 
ATOM   9328  N NZ  . LYS B 1 520 ? 4.996   28.131  -52.873 1.00 44.88  ? 520 LYS B NZ  1 
ATOM   9329  N N   . GLY B 1 521 ? -1.043  31.910  -53.066 1.00 41.47  ? 521 GLY B N   1 
ATOM   9330  C CA  . GLY B 1 521 ? -1.834  32.472  -54.150 1.00 41.91  ? 521 GLY B CA  1 
ATOM   9331  C C   . GLY B 1 521 ? -1.001  33.352  -55.051 1.00 42.45  ? 521 GLY B C   1 
ATOM   9332  O O   . GLY B 1 521 ? 0.228   33.352  -54.968 1.00 42.44  ? 521 GLY B O   1 
ATOM   9333  N N   . GLY B 1 522 ? -1.671  34.114  -55.917 1.00 43.73  ? 522 GLY B N   1 
ATOM   9334  C CA  . GLY B 1 522 ? -0.982  34.899  -56.944 1.00 41.61  ? 522 GLY B CA  1 
ATOM   9335  C C   . GLY B 1 522 ? -0.052  35.981  -56.419 1.00 41.32  ? 522 GLY B C   1 
ATOM   9336  O O   . GLY B 1 522 ? 0.766   36.496  -57.162 1.00 41.98  ? 522 GLY B O   1 
ATOM   9337  N N   . LYS B 1 523 ? -0.165  36.315  -55.136 1.00 42.92  ? 523 LYS B N   1 
ATOM   9338  C CA  . LYS B 1 523 ? 0.584   37.438  -54.543 1.00 41.63  ? 523 LYS B CA  1 
ATOM   9339  C C   . LYS B 1 523 ? 1.849   36.974  -53.843 1.00 40.92  ? 523 LYS B C   1 
ATOM   9340  O O   . LYS B 1 523 ? 2.620   37.789  -53.313 1.00 40.58  ? 523 LYS B O   1 
ATOM   9341  C CB  . LYS B 1 523 ? -0.307  38.214  -53.568 1.00 41.87  ? 523 LYS B CB  1 
ATOM   9342  C CG  . LYS B 1 523 ? -1.386  39.032  -54.261 1.00 42.37  ? 523 LYS B CG  1 
ATOM   9343  C CD  . LYS B 1 523 ? -2.159  39.881  -53.279 1.00 42.51  ? 523 LYS B CD  1 
ATOM   9344  C CE  . LYS B 1 523 ? -3.155  40.763  -54.021 1.00 45.00  ? 523 LYS B CE  1 
ATOM   9345  N NZ  . LYS B 1 523 ? -4.225  41.273  -53.119 1.00 45.41  ? 523 LYS B NZ  1 
ATOM   9346  N N   . TYR B 1 524 ? 2.055   35.662  -53.834 1.00 40.42  ? 524 TYR B N   1 
ATOM   9347  C CA  . TYR B 1 524 ? 3.243   35.077  -53.225 1.00 41.66  ? 524 TYR B CA  1 
ATOM   9348  C C   . TYR B 1 524 ? 4.461   35.574  -53.983 1.00 42.86  ? 524 TYR B C   1 
ATOM   9349  O O   . TYR B 1 524 ? 4.440   35.633  -55.214 1.00 41.88  ? 524 TYR B O   1 
ATOM   9350  C CB  . TYR B 1 524 ? 3.172   33.547  -53.290 1.00 41.48  ? 524 TYR B CB  1 
ATOM   9351  C CG  . TYR B 1 524 ? 4.413   32.856  -52.776 1.00 41.59  ? 524 TYR B CG  1 
ATOM   9352  C CD1 . TYR B 1 524 ? 4.583   32.610  -51.409 1.00 40.66  ? 524 TYR B CD1 1 
ATOM   9353  C CD2 . TYR B 1 524 ? 5.419   32.443  -53.652 1.00 41.68  ? 524 TYR B CD2 1 
ATOM   9354  C CE1 . TYR B 1 524 ? 5.724   31.982  -50.927 1.00 40.19  ? 524 TYR B CE1 1 
ATOM   9355  C CE2 . TYR B 1 524 ? 6.557   31.810  -53.180 1.00 41.13  ? 524 TYR B CE2 1 
ATOM   9356  C CZ  . TYR B 1 524 ? 6.705   31.588  -51.814 1.00 41.34  ? 524 TYR B CZ  1 
ATOM   9357  O OH  . TYR B 1 524 ? 7.839   30.983  -51.335 1.00 40.25  ? 524 TYR B OH  1 
ATOM   9358  N N   . ARG B 1 525 ? 5.508   35.974  -53.262 1.00 44.25  ? 525 ARG B N   1 
ATOM   9359  C CA  . ARG B 1 525 ? 6.781   36.287  -53.929 1.00 42.81  ? 525 ARG B CA  1 
ATOM   9360  C C   . ARG B 1 525 ? 7.817   35.207  -53.637 1.00 42.04  ? 525 ARG B C   1 
ATOM   9361  O O   . ARG B 1 525 ? 8.193   34.437  -54.531 1.00 42.14  ? 525 ARG B O   1 
ATOM   9362  C CB  . ARG B 1 525 ? 7.341   37.687  -53.588 1.00 43.02  ? 525 ARG B CB  1 
ATOM   9363  C CG  . ARG B 1 525 ? 6.405   38.661  -52.895 1.00 48.12  ? 525 ARG B CG  1 
ATOM   9364  C CD  . ARG B 1 525 ? 5.766   39.690  -53.816 1.00 50.18  ? 525 ARG B CD  1 
ATOM   9365  N NE  . ARG B 1 525 ? 6.690   40.744  -54.208 1.00 53.21  ? 525 ARG B NE  1 
ATOM   9366  C CZ  . ARG B 1 525 ? 6.338   42.001  -54.476 1.00 53.07  ? 525 ARG B CZ  1 
ATOM   9367  N NH1 . ARG B 1 525 ? 5.076   42.392  -54.347 1.00 53.20  ? 525 ARG B NH1 1 
ATOM   9368  N NH2 . ARG B 1 525 ? 7.262   42.877  -54.848 1.00 52.95  ? 525 ARG B NH2 1 
ATOM   9369  N N   . LYS B 1 526 ? 8.279   35.156  -52.387 1.00 40.66  ? 526 LYS B N   1 
ATOM   9370  C CA  . LYS B 1 526 ? 9.307   34.211  -51.967 1.00 38.05  ? 526 LYS B CA  1 
ATOM   9371  C C   . LYS B 1 526 ? 9.478   34.232  -50.459 1.00 39.26  ? 526 LYS B C   1 
ATOM   9372  O O   . LYS B 1 526 ? 9.968   35.223  -49.888 1.00 40.50  ? 526 LYS B O   1 
ATOM   9373  C CB  . LYS B 1 526 ? 10.661  34.503  -52.639 1.00 38.19  ? 526 LYS B CB  1 
ATOM   9374  C CG  . LYS B 1 526 ? 11.751  33.495  -52.254 1.00 37.76  ? 526 LYS B CG  1 
ATOM   9375  C CD  . LYS B 1 526 ? 12.993  33.599  -53.136 1.00 39.82  ? 526 LYS B CD  1 
ATOM   9376  C CE  . LYS B 1 526 ? 14.199  32.909  -52.490 1.00 40.94  ? 526 LYS B CE  1 
ATOM   9377  N NZ  . LYS B 1 526 ? 15.391  32.952  -53.383 1.00 44.49  ? 526 LYS B NZ  1 
ATOM   9378  N N   . VAL B 1 527 ? 9.111   33.119  -49.826 1.00 36.16  ? 527 VAL B N   1 
ATOM   9379  C CA  . VAL B 1 527 ? 9.205   32.973  -48.401 1.00 34.34  ? 527 VAL B CA  1 
ATOM   9380  C C   . VAL B 1 527 ? 10.139  31.806  -48.082 1.00 33.89  ? 527 VAL B C   1 
ATOM   9381  O O   . VAL B 1 527 ? 9.851   30.677  -48.453 1.00 33.12  ? 527 VAL B O   1 
ATOM   9382  C CB  . VAL B 1 527 ? 7.803   32.723  -47.769 1.00 34.47  ? 527 VAL B CB  1 
ATOM   9383  C CG1 . VAL B 1 527 ? 7.934   32.311  -46.308 1.00 34.03  ? 527 VAL B CG1 1 
ATOM   9384  C CG2 . VAL B 1 527 ? 6.932   33.965  -47.879 1.00 32.56  ? 527 VAL B CG2 1 
ATOM   9385  N N   . THR B 1 528 ? 11.247  32.090  -47.392 1.00 33.47  ? 528 THR B N   1 
ATOM   9386  C CA  . THR B 1 528 ? 12.146  31.051  -46.880 1.00 34.37  ? 528 THR B CA  1 
ATOM   9387  C C   . THR B 1 528 ? 11.915  30.763  -45.399 1.00 33.72  ? 528 THR B C   1 
ATOM   9388  O O   . THR B 1 528 ? 11.398  31.601  -44.665 1.00 32.61  ? 528 THR B O   1 
ATOM   9389  C CB  . THR B 1 528 ? 13.620  31.451  -47.007 1.00 37.29  ? 528 THR B CB  1 
ATOM   9390  O OG1 . THR B 1 528 ? 13.878  32.567  -46.142 1.00 36.53  ? 528 THR B OG1 1 
ATOM   9391  C CG2 . THR B 1 528 ? 13.977  31.815  -48.470 1.00 38.37  ? 528 THR B CG2 1 
ATOM   9392  N N   . PHE B 1 529 ? 12.318  29.567  -44.974 1.00 32.40  ? 529 PHE B N   1 
ATOM   9393  C CA  . PHE B 1 529 ? 12.341  29.200  -43.580 1.00 31.27  ? 529 PHE B CA  1 
ATOM   9394  C C   . PHE B 1 529 ? 13.190  30.180  -42.765 1.00 31.97  ? 529 PHE B C   1 
ATOM   9395  O O   . PHE B 1 529 ? 12.778  30.624  -41.682 1.00 32.43  ? 529 PHE B O   1 
ATOM   9396  C CB  . PHE B 1 529 ? 12.887  27.780  -43.410 1.00 29.22  ? 529 PHE B CB  1 
ATOM   9397  C CG  . PHE B 1 529 ? 12.834  27.276  -41.993 1.00 28.57  ? 529 PHE B CG  1 
ATOM   9398  C CD1 . PHE B 1 529 ? 11.641  26.851  -41.437 1.00 27.86  ? 529 PHE B CD1 1 
ATOM   9399  C CD2 . PHE B 1 529 ? 13.986  27.248  -41.203 1.00 29.54  ? 529 PHE B CD2 1 
ATOM   9400  C CE1 . PHE B 1 529 ? 11.598  26.354  -40.143 1.00 27.31  ? 529 PHE B CE1 1 
ATOM   9401  C CE2 . PHE B 1 529 ? 13.946  26.765  -39.900 1.00 28.09  ? 529 PHE B CE2 1 
ATOM   9402  C CZ  . PHE B 1 529 ? 12.741  26.332  -39.367 1.00 26.85  ? 529 PHE B CZ  1 
ATOM   9403  N N   . GLN B 1 530 ? 14.378  30.476  -43.280 1.00 32.21  ? 530 GLN B N   1 
ATOM   9404  C CA  . GLN B 1 530 ? 15.305  31.422  -42.668 1.00 33.25  ? 530 GLN B CA  1 
ATOM   9405  C C   . GLN B 1 530 ? 14.638  32.753  -42.366 1.00 32.52  ? 530 GLN B C   1 
ATOM   9406  O O   . GLN B 1 530 ? 14.868  33.334  -41.295 1.00 32.16  ? 530 GLN B O   1 
ATOM   9407  C CB  . GLN B 1 530 ? 16.512  31.668  -43.593 1.00 34.28  ? 530 GLN B CB  1 
ATOM   9408  C CG  . GLN B 1 530 ? 17.491  30.505  -43.680 1.00 37.86  ? 530 GLN B CG  1 
ATOM   9409  C CD  . GLN B 1 530 ? 16.899  29.261  -44.349 1.00 38.23  ? 530 GLN B CD  1 
ATOM   9410  O OE1 . GLN B 1 530 ? 16.271  29.346  -45.406 1.00 37.29  ? 530 GLN B OE1 1 
ATOM   9411  N NE2 . GLN B 1 530 ? 17.093  28.102  -43.721 1.00 39.78  ? 530 GLN B NE2 1 
ATOM   9412  N N   . CYS B 1 531 ? 13.838  33.250  -43.311 1.00 31.24  ? 531 CYS B N   1 
ATOM   9413  C CA  . CYS B 1 531 ? 13.244  34.574  -43.163 1.00 32.92  ? 531 CYS B CA  1 
ATOM   9414  C C   . CYS B 1 531 ? 12.228  34.561  -42.016 1.00 31.99  ? 531 CYS B C   1 
ATOM   9415  O O   . CYS B 1 531 ? 12.222  35.454  -41.159 1.00 30.32  ? 531 CYS B O   1 
ATOM   9416  C CB  . CYS B 1 531 ? 12.576  35.055  -44.465 1.00 34.72  ? 531 CYS B CB  1 
ATOM   9417  S SG  . CYS B 1 531 ? 11.846  36.715  -44.296 1.00 40.37  ? 531 CYS B SG  1 
ATOM   9418  N N   . LEU B 1 532 ? 11.407  33.511  -42.002 1.00 31.29  ? 532 LEU B N   1 
ATOM   9419  C CA  . LEU B 1 532 ? 10.422  33.281  -40.968 1.00 30.18  ? 532 LEU B CA  1 
ATOM   9420  C C   . LEU B 1 532 ? 11.056  33.131  -39.601 1.00 30.37  ? 532 LEU B C   1 
ATOM   9421  O O   . LEU B 1 532 ? 10.548  33.672  -38.599 1.00 29.96  ? 532 LEU B O   1 
ATOM   9422  C CB  . LEU B 1 532 ? 9.579   32.041  -41.303 1.00 30.41  ? 532 LEU B CB  1 
ATOM   9423  C CG  . LEU B 1 532 ? 8.584   32.195  -42.466 1.00 30.05  ? 532 LEU B CG  1 
ATOM   9424  C CD1 . LEU B 1 532 ? 7.933   30.863  -42.839 1.00 29.92  ? 532 LEU B CD1 1 
ATOM   9425  C CD2 . LEU B 1 532 ? 7.531   33.240  -42.137 1.00 28.41  ? 532 LEU B CD2 1 
ATOM   9426  N N   . LYS B 1 533 ? 12.173  32.419  -39.547 1.00 29.92  ? 533 LYS B N   1 
ATOM   9427  C CA  . LYS B 1 533 ? 12.838  32.178  -38.278 1.00 28.98  ? 533 LYS B CA  1 
ATOM   9428  C C   . LYS B 1 533 ? 13.398  33.487  -37.725 1.00 28.90  ? 533 LYS B C   1 
ATOM   9429  O O   . LYS B 1 533 ? 13.401  33.710  -36.507 1.00 28.52  ? 533 LYS B O   1 
ATOM   9430  C CB  . LYS B 1 533 ? 13.925  31.134  -38.446 1.00 30.63  ? 533 LYS B CB  1 
ATOM   9431  C CG  . LYS B 1 533 ? 14.320  30.425  -37.153 1.00 35.03  ? 533 LYS B CG  1 
ATOM   9432  C CD  . LYS B 1 533 ? 15.015  29.099  -37.398 1.00 34.15  ? 533 LYS B CD  1 
ATOM   9433  C CE  . LYS B 1 533 ? 16.331  29.276  -38.157 1.00 35.90  ? 533 LYS B CE  1 
ATOM   9434  N NZ  . LYS B 1 533 ? 17.211  28.098  -37.917 1.00 39.54  ? 533 LYS B NZ  1 
ATOM   9435  N N   . SER B 1 534 ? 13.820  34.379  -38.621 1.00 28.32  ? 534 SER B N   1 
ATOM   9436  C CA  . SER B 1 534 ? 14.327  35.702  -38.202 1.00 29.55  ? 534 SER B CA  1 
ATOM   9437  C C   . SER B 1 534 ? 13.222  36.585  -37.639 1.00 28.59  ? 534 SER B C   1 
ATOM   9438  O O   . SER B 1 534 ? 13.438  37.319  -36.685 1.00 27.27  ? 534 SER B O   1 
ATOM   9439  C CB  . SER B 1 534 ? 15.024  36.429  -39.357 1.00 29.80  ? 534 SER B CB  1 
ATOM   9440  O OG  . SER B 1 534 ? 16.167  35.714  -39.750 1.00 31.41  ? 534 SER B OG  1 
ATOM   9441  N N   . ILE B 1 535 ? 12.049  36.530  -38.256 1.00 29.40  ? 535 ILE B N   1 
ATOM   9442  C CA  . ILE B 1 535 ? 10.882  37.249  -37.742 1.00 29.42  ? 535 ILE B CA  1 
ATOM   9443  C C   . ILE B 1 535 ? 10.511  36.728  -36.342 1.00 29.10  ? 535 ILE B C   1 
ATOM   9444  O O   . ILE B 1 535 ? 10.251  37.516  -35.446 1.00 30.42  ? 535 ILE B O   1 
ATOM   9445  C CB  . ILE B 1 535 ? 9.699   37.197  -38.749 1.00 29.40  ? 535 ILE B CB  1 
ATOM   9446  C CG1 . ILE B 1 535 ? 10.018  38.074  -39.956 1.00 29.71  ? 535 ILE B CG1 1 
ATOM   9447  C CG2 . ILE B 1 535 ? 8.373   37.611  -38.111 1.00 29.86  ? 535 ILE B CG2 1 
ATOM   9448  C CD1 . ILE B 1 535 ? 9.163   37.789  -41.180 1.00 30.49  ? 535 ILE B CD1 1 
ATOM   9449  N N   . ALA B 1 536 ? 10.569  35.408  -36.147 1.00 27.43  ? 536 ALA B N   1 
ATOM   9450  C CA  . ALA B 1 536 ? 10.273  34.808  -34.851 1.00 26.62  ? 536 ALA B CA  1 
ATOM   9451  C C   . ALA B 1 536 ? 11.240  35.265  -33.771 1.00 27.88  ? 536 ALA B C   1 
ATOM   9452  O O   . ALA B 1 536 ? 10.817  35.643  -32.688 1.00 27.33  ? 536 ALA B O   1 
ATOM   9453  C CB  . ALA B 1 536 ? 10.277  33.297  -34.943 1.00 24.76  ? 536 ALA B CB  1 
ATOM   9454  N N   . TRP B 1 537 ? 12.545  35.226  -34.060 1.00 28.37  ? 537 TRP B N   1 
ATOM   9455  C CA  . TRP B 1 537 ? 13.514  35.701  -33.092 1.00 28.76  ? 537 TRP B CA  1 
ATOM   9456  C C   . TRP B 1 537 ? 13.288  37.172  -32.762 1.00 30.16  ? 537 TRP B C   1 
ATOM   9457  O O   . TRP B 1 537 ? 13.496  37.607  -31.608 1.00 30.75  ? 537 TRP B O   1 
ATOM   9458  C CB  . TRP B 1 537 ? 14.941  35.456  -33.571 1.00 27.86  ? 537 TRP B CB  1 
ATOM   9459  C CG  . TRP B 1 537 ? 15.400  34.021  -33.438 1.00 26.47  ? 537 TRP B CG  1 
ATOM   9460  C CD1 . TRP B 1 537 ? 15.805  33.161  -34.465 1.00 25.77  ? 537 TRP B CD1 1 
ATOM   9461  C CD2 . TRP B 1 537 ? 15.530  33.236  -32.208 1.00 25.21  ? 537 TRP B CD2 1 
ATOM   9462  N NE1 . TRP B 1 537 ? 16.156  31.924  -33.956 1.00 25.74  ? 537 TRP B NE1 1 
ATOM   9463  C CE2 . TRP B 1 537 ? 16.000  31.900  -32.617 1.00 25.33  ? 537 TRP B CE2 1 
ATOM   9464  C CE3 . TRP B 1 537 ? 15.291  33.485  -30.852 1.00 24.74  ? 537 TRP B CE3 1 
ATOM   9465  C CZ2 . TRP B 1 537 ? 16.237  30.888  -31.696 1.00 25.13  ? 537 TRP B CZ2 1 
ATOM   9466  C CZ3 . TRP B 1 537 ? 15.526  32.454  -29.930 1.00 24.26  ? 537 TRP B CZ3 1 
ATOM   9467  C CH2 . TRP B 1 537 ? 15.985  31.184  -30.343 1.00 24.80  ? 537 TRP B CH2 1 
ATOM   9468  N N   . ARG B 1 538 ? 12.857  37.953  -33.753 1.00 29.78  ? 538 ARG B N   1 
ATOM   9469  C CA  . ARG B 1 538 ? 12.672  39.386  -33.519 1.00 31.21  ? 538 ARG B CA  1 
ATOM   9470  C C   . ARG B 1 538 ? 11.510  39.615  -32.586 1.00 29.72  ? 538 ARG B C   1 
ATOM   9471  O O   . ARG B 1 538 ? 11.553  40.532  -31.787 1.00 30.14  ? 538 ARG B O   1 
ATOM   9472  C CB  . ARG B 1 538 ? 12.450  40.167  -34.813 1.00 32.16  ? 538 ARG B CB  1 
ATOM   9473  C CG  . ARG B 1 538 ? 13.695  40.279  -35.636 1.00 34.73  ? 538 ARG B CG  1 
ATOM   9474  C CD  . ARG B 1 538 ? 13.854  41.677  -36.141 1.00 36.56  ? 538 ARG B CD  1 
ATOM   9475  N NE  . ARG B 1 538 ? 14.894  41.748  -37.158 1.00 38.34  ? 538 ARG B NE  1 
ATOM   9476  C CZ  . ARG B 1 538 ? 15.583  42.847  -37.436 1.00 39.38  ? 538 ARG B CZ  1 
ATOM   9477  N NH1 . ARG B 1 538 ? 15.353  43.973  -36.753 1.00 38.64  ? 538 ARG B NH1 1 
ATOM   9478  N NH2 . ARG B 1 538 ? 16.503  42.818  -38.387 1.00 38.12  ? 538 ARG B NH2 1 
ATOM   9479  N N   . ALA B 1 539 ? 10.465  38.791  -32.713 1.00 27.96  ? 539 ALA B N   1 
ATOM   9480  C CA  . ALA B 1 539 ? 9.285   38.914  -31.858 1.00 26.99  ? 539 ALA B CA  1 
ATOM   9481  C C   . ALA B 1 539 ? 9.650   38.611  -30.415 1.00 26.80  ? 539 ALA B C   1 
ATOM   9482  O O   . ALA B 1 539 ? 9.227   39.315  -29.528 1.00 28.31  ? 539 ALA B O   1 
ATOM   9483  C CB  . ALA B 1 539 ? 8.173   38.020  -32.335 1.00 24.52  ? 539 ALA B CB  1 
ATOM   9484  N N   . PHE B 1 540 ? 10.468  37.581  -30.196 1.00 27.86  ? 540 PHE B N   1 
ATOM   9485  C CA  . PHE B 1 540 ? 10.964  37.244  -28.856 1.00 28.33  ? 540 PHE B CA  1 
ATOM   9486  C C   . PHE B 1 540 ? 11.849  38.373  -28.304 1.00 31.13  ? 540 PHE B C   1 
ATOM   9487  O O   . PHE B 1 540 ? 11.717  38.753  -27.136 1.00 30.96  ? 540 PHE B O   1 
ATOM   9488  C CB  . PHE B 1 540 ? 11.705  35.894  -28.854 1.00 26.60  ? 540 PHE B CB  1 
ATOM   9489  C CG  . PHE B 1 540 ? 10.794  34.700  -28.664 1.00 29.13  ? 540 PHE B CG  1 
ATOM   9490  C CD1 . PHE B 1 540 ? 10.325  34.349  -27.391 1.00 28.52  ? 540 PHE B CD1 1 
ATOM   9491  C CD2 . PHE B 1 540 ? 10.364  33.949  -29.751 1.00 29.69  ? 540 PHE B CD2 1 
ATOM   9492  C CE1 . PHE B 1 540 ? 9.454   33.284  -27.216 1.00 28.92  ? 540 PHE B CE1 1 
ATOM   9493  C CE2 . PHE B 1 540 ? 9.499   32.861  -29.579 1.00 30.44  ? 540 PHE B CE2 1 
ATOM   9494  C CZ  . PHE B 1 540 ? 9.044   32.527  -28.306 1.00 29.56  ? 540 PHE B CZ  1 
ATOM   9495  N N   . LEU B 1 541 ? 12.737  38.916  -29.147 1.00 30.94  ? 541 LEU B N   1 
ATOM   9496  C CA  . LEU B 1 541 ? 13.613  40.012  -28.724 1.00 30.57  ? 541 LEU B CA  1 
ATOM   9497  C C   . LEU B 1 541 ? 12.840  41.207  -28.226 1.00 31.54  ? 541 LEU B C   1 
ATOM   9498  O O   . LEU B 1 541 ? 13.268  41.881  -27.288 1.00 31.81  ? 541 LEU B O   1 
ATOM   9499  C CB  . LEU B 1 541 ? 14.467  40.499  -29.877 1.00 30.66  ? 541 LEU B CB  1 
ATOM   9500  C CG  . LEU B 1 541 ? 15.929  40.132  -30.024 1.00 30.80  ? 541 LEU B CG  1 
ATOM   9501  C CD1 . LEU B 1 541 ? 16.572  39.524  -28.764 1.00 29.61  ? 541 LEU B CD1 1 
ATOM   9502  C CD2 . LEU B 1 541 ? 16.034  39.203  -31.201 1.00 31.62  ? 541 LEU B CD2 1 
ATOM   9503  N N   . ALA B 1 542 ? 11.732  41.519  -28.898 1.00 30.99  ? 542 ALA B N   1 
ATOM   9504  C CA  . ALA B 1 542 ? 11.032  42.761  -28.630 1.00 30.53  ? 542 ALA B CA  1 
ATOM   9505  C C   . ALA B 1 542 ? 10.307  42.657  -27.273 1.00 30.42  ? 542 ALA B C   1 
ATOM   9506  O O   . ALA B 1 542 ? 10.089  43.653  -26.572 1.00 29.46  ? 542 ALA B O   1 
ATOM   9507  C CB  . ALA B 1 542 ? 10.065  43.072  -29.759 1.00 29.86  ? 542 ALA B CB  1 
ATOM   9508  N N   . VAL B 1 543 ? 9.982   41.431  -26.899 1.00 29.84  ? 543 VAL B N   1 
ATOM   9509  C CA  . VAL B 1 543 ? 9.341   41.153  -25.620 1.00 30.68  ? 543 VAL B CA  1 
ATOM   9510  C C   . VAL B 1 543 ? 10.376  41.012  -24.507 1.00 31.38  ? 543 VAL B C   1 
ATOM   9511  O O   . VAL B 1 543 ? 10.217  41.574  -23.434 1.00 32.15  ? 543 VAL B O   1 
ATOM   9512  C CB  . VAL B 1 543 ? 8.464   39.892  -25.709 1.00 29.97  ? 543 VAL B CB  1 
ATOM   9513  C CG1 . VAL B 1 543 ? 8.097   39.395  -24.333 1.00 31.05  ? 543 VAL B CG1 1 
ATOM   9514  C CG2 . VAL B 1 543 ? 7.207   40.199  -26.499 1.00 29.71  ? 543 VAL B CG2 1 
ATOM   9515  N N   . LEU B 1 544 ? 11.456  40.291  -24.783 1.00 31.55  ? 544 LEU B N   1 
ATOM   9516  C CA  . LEU B 1 544 ? 12.443  40.016  -23.776 1.00 31.06  ? 544 LEU B CA  1 
ATOM   9517  C C   . LEU B 1 544 ? 13.103  41.315  -23.312 1.00 35.49  ? 544 LEU B C   1 
ATOM   9518  O O   . LEU B 1 544 ? 13.476  41.446  -22.139 1.00 36.38  ? 544 LEU B O   1 
ATOM   9519  C CB  . LEU B 1 544 ? 13.469  39.023  -24.300 1.00 28.75  ? 544 LEU B CB  1 
ATOM   9520  C CG  . LEU B 1 544 ? 12.989  37.574  -24.551 1.00 28.51  ? 544 LEU B CG  1 
ATOM   9521  C CD1 . LEU B 1 544 ? 14.029  36.783  -25.343 1.00 25.86  ? 544 LEU B CD1 1 
ATOM   9522  C CD2 . LEU B 1 544 ? 12.635  36.844  -23.253 1.00 26.82  ? 544 LEU B CD2 1 
ATOM   9523  N N   . LYS B 1 545 ? 13.202  42.282  -24.232 1.00 36.61  ? 545 LYS B N   1 
ATOM   9524  C CA  . LYS B 1 545 ? 13.794  43.602  -23.965 1.00 37.53  ? 545 LYS B CA  1 
ATOM   9525  C C   . LYS B 1 545 ? 13.062  44.380  -22.895 1.00 36.36  ? 545 LYS B C   1 
ATOM   9526  O O   . LYS B 1 545 ? 13.620  45.296  -22.311 1.00 35.69  ? 545 LYS B O   1 
ATOM   9527  C CB  . LYS B 1 545 ? 13.843  44.452  -25.247 1.00 37.51  ? 545 LYS B CB  1 
ATOM   9528  C CG  . LYS B 1 545 ? 15.136  44.323  -26.029 1.00 41.36  ? 545 LYS B CG  1 
ATOM   9529  C CD  . LYS B 1 545 ? 14.946  44.939  -27.398 1.00 45.54  ? 545 LYS B CD  1 
ATOM   9530  C CE  . LYS B 1 545 ? 16.262  45.347  -28.014 1.00 47.49  ? 545 LYS B CE  1 
ATOM   9531  N NZ  . LYS B 1 545 ? 15.999  46.369  -29.069 1.00 50.91  ? 545 LYS B NZ  1 
ATOM   9532  N N   . ARG B 1 546 ? 11.793  44.046  -22.676 1.00 36.54  ? 546 ARG B N   1 
ATOM   9533  C CA  . ARG B 1 546 ? 11.009  44.677  -21.604 1.00 34.98  ? 546 ARG B CA  1 
ATOM   9534  C C   . ARG B 1 546 ? 11.523  44.333  -20.209 1.00 34.19  ? 546 ARG B C   1 
ATOM   9535  O O   . ARG B 1 546 ? 11.142  44.978  -19.250 1.00 33.16  ? 546 ARG B O   1 
ATOM   9536  C CB  . ARG B 1 546 ? 9.543   44.311  -21.723 1.00 32.65  ? 546 ARG B CB  1 
ATOM   9537  C CG  . ARG B 1 546 ? 8.904   44.825  -22.990 1.00 34.00  ? 546 ARG B CG  1 
ATOM   9538  C CD  . ARG B 1 546 ? 7.392   44.737  -22.899 1.00 34.10  ? 546 ARG B CD  1 
ATOM   9539  N NE  . ARG B 1 546 ? 6.884   45.620  -21.858 1.00 33.08  ? 546 ARG B NE  1 
ATOM   9540  C CZ  . ARG B 1 546 ? 5.597   45.818  -21.609 1.00 34.21  ? 546 ARG B CZ  1 
ATOM   9541  N NH1 . ARG B 1 546 ? 4.659   45.211  -22.350 1.00 31.47  ? 546 ARG B NH1 1 
ATOM   9542  N NH2 . ARG B 1 546 ? 5.245   46.640  -20.628 1.00 34.87  ? 546 ARG B NH2 1 
ATOM   9543  N N   . ARG B 1 547 ? 12.358  43.292  -20.106 1.00 34.70  ? 547 ARG B N   1 
ATOM   9544  C CA  . ARG B 1 547 ? 13.051  42.954  -18.848 1.00 35.48  ? 547 ARG B CA  1 
ATOM   9545  C C   . ARG B 1 547 ? 14.535  42.751  -19.129 1.00 37.70  ? 547 ARG B C   1 
ATOM   9546  O O   . ARG B 1 547 ? 15.093  41.653  -18.880 1.00 37.88  ? 547 ARG B O   1 
ATOM   9547  C CB  . ARG B 1 547 ? 12.485  41.675  -18.208 1.00 35.36  ? 547 ARG B CB  1 
ATOM   9548  C CG  . ARG B 1 547 ? 10.969  41.611  -18.031 1.00 35.24  ? 547 ARG B CG  1 
ATOM   9549  C CD  . ARG B 1 547 ? 10.591  40.450  -17.106 1.00 36.27  ? 547 ARG B CD  1 
ATOM   9550  N NE  . ARG B 1 547 ? 9.221   39.997  -17.335 1.00 38.11  ? 547 ARG B NE  1 
ATOM   9551  C CZ  . ARG B 1 547 ? 8.157   40.398  -16.634 1.00 38.74  ? 547 ARG B CZ  1 
ATOM   9552  N NH1 . ARG B 1 547 ? 8.293   41.260  -15.628 1.00 41.57  ? 547 ARG B NH1 1 
ATOM   9553  N NH2 . ARG B 1 547 ? 6.950   39.938  -16.938 1.00 34.57  ? 547 ARG B NH2 1 
ATOM   9554  N N   . THR B 1 548 ? 15.178  43.785  -19.667 1.00 39.94  ? 548 THR B N   1 
ATOM   9555  C CA  . THR B 1 548 ? 16.582  43.666  -20.087 1.00 44.84  ? 548 THR B CA  1 
ATOM   9556  C C   . THR B 1 548 ? 17.468  43.227  -18.934 1.00 45.96  ? 548 THR B C   1 
ATOM   9557  O O   . THR B 1 548 ? 18.524  42.639  -19.151 1.00 51.79  ? 548 THR B O   1 
ATOM   9558  C CB  . THR B 1 548 ? 17.148  44.976  -20.686 1.00 45.79  ? 548 THR B CB  1 
ATOM   9559  O OG1 . THR B 1 548 ? 16.654  46.098  -19.939 1.00 53.74  ? 548 THR B OG1 1 
ATOM   9560  C CG2 . THR B 1 548 ? 16.739  45.131  -22.124 1.00 43.72  ? 548 THR B CG2 1 
ATOM   9561  N N   . GLU B 1 549 ? 17.036  43.509  -17.711 1.00 45.79  ? 549 GLU B N   1 
ATOM   9562  C CA  . GLU B 1 549 ? 17.804  43.137  -16.516 1.00 49.94  ? 549 GLU B CA  1 
ATOM   9563  C C   . GLU B 1 549 ? 17.796  41.618  -16.321 1.00 46.92  ? 549 GLU B C   1 
ATOM   9564  O O   . GLU B 1 549 ? 18.841  40.993  -16.230 1.00 49.34  ? 549 GLU B O   1 
ATOM   9565  C CB  . GLU B 1 549 ? 17.263  43.861  -15.262 1.00 52.82  ? 549 GLU B CB  1 
ATOM   9566  C CG  . GLU B 1 549 ? 15.830  43.474  -14.845 1.00 57.39  ? 549 GLU B CG  1 
ATOM   9567  C CD  . GLU B 1 549 ? 14.727  44.141  -15.681 1.00 57.45  ? 549 GLU B CD  1 
ATOM   9568  O OE1 . GLU B 1 549 ? 15.040  45.009  -16.521 1.00 58.93  ? 549 GLU B OE1 1 
ATOM   9569  O OE2 . GLU B 1 549 ? 13.537  43.805  -15.485 1.00 56.93  ? 549 GLU B OE2 1 
ATOM   9570  N N   . ILE B 1 550 ? 16.605  41.039  -16.285 1.00 42.40  ? 550 ILE B N   1 
ATOM   9571  C CA  . ILE B 1 550 ? 16.435  39.599  -16.170 1.00 41.37  ? 550 ILE B CA  1 
ATOM   9572  C C   . ILE B 1 550 ? 16.987  38.864  -17.425 1.00 41.94  ? 550 ILE B C   1 
ATOM   9573  O O   . ILE B 1 550 ? 17.746  37.915  -17.305 1.00 38.43  ? 550 ILE B O   1 
ATOM   9574  C CB  . ILE B 1 550 ? 14.940  39.249  -15.867 1.00 38.24  ? 550 ILE B CB  1 
ATOM   9575  C CG1 . ILE B 1 550 ? 14.671  39.389  -14.358 1.00 38.40  ? 550 ILE B CG1 1 
ATOM   9576  C CG2 . ILE B 1 550 ? 14.584  37.856  -16.340 1.00 37.00  ? 550 ILE B CG2 1 
ATOM   9577  C CD1 . ILE B 1 550 ? 13.253  39.764  -13.971 1.00 36.49  ? 550 ILE B CD1 1 
ATOM   9578  N N   . TYR B 1 551 ? 16.653  39.364  -18.616 1.00 41.57  ? 551 TYR B N   1 
ATOM   9579  C CA  . TYR B 1 551 ? 16.860  38.596  -19.850 1.00 40.04  ? 551 TYR B CA  1 
ATOM   9580  C C   . TYR B 1 551 ? 18.116  38.990  -20.669 1.00 41.89  ? 551 TYR B C   1 
ATOM   9581  O O   . TYR B 1 551 ? 18.378  38.407  -21.734 1.00 41.94  ? 551 TYR B O   1 
ATOM   9582  C CB  . TYR B 1 551 ? 15.634  38.711  -20.733 1.00 37.15  ? 551 TYR B CB  1 
ATOM   9583  C CG  . TYR B 1 551 ? 14.381  38.011  -20.239 1.00 35.15  ? 551 TYR B CG  1 
ATOM   9584  C CD1 . TYR B 1 551 ? 14.401  36.674  -19.837 1.00 35.24  ? 551 TYR B CD1 1 
ATOM   9585  C CD2 . TYR B 1 551 ? 13.165  38.658  -20.281 1.00 32.93  ? 551 TYR B CD2 1 
ATOM   9586  C CE1 . TYR B 1 551 ? 13.246  36.033  -19.424 1.00 34.07  ? 551 TYR B CE1 1 
ATOM   9587  C CE2 . TYR B 1 551 ? 12.013  38.023  -19.897 1.00 34.85  ? 551 TYR B CE2 1 
ATOM   9588  C CZ  . TYR B 1 551 ? 12.059  36.709  -19.472 1.00 36.11  ? 551 TYR B CZ  1 
ATOM   9589  O OH  . TYR B 1 551 ? 10.893  36.093  -19.111 1.00 37.83  ? 551 TYR B OH  1 
ATOM   9590  N N   . LYS B 1 552 ? 18.869  39.974  -20.172 1.00 41.37  ? 552 LYS B N   1 
ATOM   9591  C CA  . LYS B 1 552 ? 20.172  40.373  -20.745 1.00 43.50  ? 552 LYS B CA  1 
ATOM   9592  C C   . LYS B 1 552 ? 20.952  39.254  -21.453 1.00 39.11  ? 552 LYS B C   1 
ATOM   9593  O O   . LYS B 1 552 ? 21.233  39.342  -22.647 1.00 39.34  ? 552 LYS B O   1 
ATOM   9594  C CB  . LYS B 1 552 ? 21.055  41.022  -19.659 1.00 46.89  ? 552 LYS B CB  1 
ATOM   9595  C CG  . LYS B 1 552 ? 22.486  41.350  -20.090 1.00 52.60  ? 552 LYS B CG  1 
ATOM   9596  C CD  . LYS B 1 552 ? 22.530  42.395  -21.206 1.00 57.29  ? 552 LYS B CD  1 
ATOM   9597  C CE  . LYS B 1 552 ? 23.920  43.013  -21.351 1.00 59.05  ? 552 LYS B CE  1 
ATOM   9598  N NZ  . LYS B 1 552 ? 24.075  43.767  -22.632 1.00 60.01  ? 552 LYS B NZ  1 
ATOM   9599  N N   . GLY B 1 553 ? 21.309  38.223  -20.705 1.00 37.36  ? 553 GLY B N   1 
ATOM   9600  C CA  . GLY B 1 553 ? 22.150  37.140  -21.218 1.00 35.53  ? 553 GLY B CA  1 
ATOM   9601  C C   . GLY B 1 553 ? 21.480  36.360  -22.331 1.00 34.89  ? 553 GLY B C   1 
ATOM   9602  O O   . GLY B 1 553 ? 22.149  35.880  -23.250 1.00 35.35  ? 553 GLY B O   1 
ATOM   9603  N N   . LEU B 1 554 ? 20.157  36.227  -22.248 1.00 32.48  ? 554 LEU B N   1 
ATOM   9604  C CA  . LEU B 1 554 ? 19.393  35.502  -23.260 1.00 32.74  ? 554 LEU B CA  1 
ATOM   9605  C C   . LEU B 1 554 ? 19.310  36.352  -24.545 1.00 32.19  ? 554 LEU B C   1 
ATOM   9606  O O   . LEU B 1 554 ? 19.507  35.846  -25.638 1.00 33.65  ? 554 LEU B O   1 
ATOM   9607  C CB  . LEU B 1 554 ? 18.002  35.155  -22.728 1.00 31.30  ? 554 LEU B CB  1 
ATOM   9608  C CG  . LEU B 1 554 ? 17.018  34.418  -23.641 1.00 32.37  ? 554 LEU B CG  1 
ATOM   9609  C CD1 . LEU B 1 554 ? 17.626  33.107  -24.158 1.00 32.53  ? 554 LEU B CD1 1 
ATOM   9610  C CD2 . LEU B 1 554 ? 15.709  34.144  -22.908 1.00 28.90  ? 554 LEU B CD2 1 
ATOM   9611  N N   . ILE B 1 555 ? 19.066  37.650  -24.374 1.00 31.21  ? 555 ILE B N   1 
ATOM   9612  C CA  . ILE B 1 555 ? 19.072  38.624  -25.460 1.00 31.25  ? 555 ILE B CA  1 
ATOM   9613  C C   . ILE B 1 555 ? 20.396  38.623  -26.232 1.00 34.61  ? 555 ILE B C   1 
ATOM   9614  O O   . ILE B 1 555 ? 20.395  38.635  -27.469 1.00 35.73  ? 555 ILE B O   1 
ATOM   9615  C CB  . ILE B 1 555 ? 18.806  40.053  -24.927 1.00 29.51  ? 555 ILE B CB  1 
ATOM   9616  C CG1 . ILE B 1 555 ? 17.372  40.184  -24.432 1.00 27.21  ? 555 ILE B CG1 1 
ATOM   9617  C CG2 . ILE B 1 555 ? 19.068  41.091  -26.003 1.00 27.67  ? 555 ILE B CG2 1 
ATOM   9618  C CD1 . ILE B 1 555 ? 17.124  41.424  -23.608 1.00 26.26  ? 555 ILE B CD1 1 
ATOM   9619  N N   . ASP B 1 556 ? 21.514  38.621  -25.498 1.00 35.47  ? 556 ASP B N   1 
ATOM   9620  C CA  . ASP B 1 556 ? 22.846  38.606  -26.088 1.00 36.44  ? 556 ASP B CA  1 
ATOM   9621  C C   . ASP B 1 556 ? 23.134  37.305  -26.804 1.00 35.42  ? 556 ASP B C   1 
ATOM   9622  O O   . ASP B 1 556 ? 23.752  37.301  -27.867 1.00 36.49  ? 556 ASP B O   1 
ATOM   9623  C CB  . ASP B 1 556 ? 23.921  38.851  -25.016 1.00 39.29  ? 556 ASP B CB  1 
ATOM   9624  C CG  . ASP B 1 556 ? 23.985  40.305  -24.581 1.00 44.60  ? 556 ASP B CG  1 
ATOM   9625  O OD1 . ASP B 1 556 ? 23.405  41.174  -25.279 1.00 45.77  ? 556 ASP B OD1 1 
ATOM   9626  O OD2 . ASP B 1 556 ? 24.606  40.584  -23.534 1.00 48.82  ? 556 ASP B OD2 1 
ATOM   9627  N N   . ARG B 1 557 ? 22.731  36.193  -26.210 1.00 33.58  ? 557 ARG B N   1 
ATOM   9628  C CA  . ARG B 1 557 ? 22.853  34.925  -26.908 1.00 34.65  ? 557 ARG B CA  1 
ATOM   9629  C C   . ARG B 1 557 ? 22.077  34.933  -28.245 1.00 31.59  ? 557 ARG B C   1 
ATOM   9630  O O   . ARG B 1 557 ? 22.606  34.554  -29.265 1.00 32.45  ? 557 ARG B O   1 
ATOM   9631  C CB  . ARG B 1 557 ? 22.434  33.745  -26.019 1.00 35.39  ? 557 ARG B CB  1 
ATOM   9632  C CG  . ARG B 1 557 ? 22.589  32.410  -26.726 1.00 36.17  ? 557 ARG B CG  1 
ATOM   9633  C CD  . ARG B 1 557 ? 22.345  31.235  -25.804 1.00 37.67  ? 557 ARG B CD  1 
ATOM   9634  N NE  . ARG B 1 557 ? 23.350  31.121  -24.756 1.00 39.06  ? 557 ARG B NE  1 
ATOM   9635  C CZ  . ARG B 1 557 ? 23.412  30.112  -23.891 1.00 40.96  ? 557 ARG B CZ  1 
ATOM   9636  N NH1 . ARG B 1 557 ? 22.524  29.118  -23.952 1.00 39.15  ? 557 ARG B NH1 1 
ATOM   9637  N NH2 . ARG B 1 557 ? 24.354  30.101  -22.955 1.00 40.70  ? 557 ARG B NH2 1 
ATOM   9638  N N   . ILE B 1 558 ? 20.841  35.399  -28.243 1.00 30.38  ? 558 ILE B N   1 
ATOM   9639  C CA  . ILE B 1 558 ? 20.079  35.426  -29.493 1.00 29.13  ? 558 ILE B CA  1 
ATOM   9640  C C   . ILE B 1 558 ? 20.838  36.226  -30.554 1.00 30.53  ? 558 ILE B C   1 
ATOM   9641  O O   . ILE B 1 558 ? 20.993  35.776  -31.690 1.00 29.10  ? 558 ILE B O   1 
ATOM   9642  C CB  . ILE B 1 558 ? 18.647  35.962  -29.283 1.00 27.86  ? 558 ILE B CB  1 
ATOM   9643  C CG1 . ILE B 1 558 ? 17.877  35.038  -28.331 1.00 26.39  ? 558 ILE B CG1 1 
ATOM   9644  C CG2 . ILE B 1 558 ? 17.913  36.154  -30.623 1.00 27.17  ? 558 ILE B CG2 1 
ATOM   9645  C CD1 . ILE B 1 558 ? 16.541  35.576  -27.871 1.00 25.46  ? 558 ILE B CD1 1 
ATOM   9646  N N   . LYS B 1 559 ? 21.338  37.397  -30.164 1.00 31.89  ? 559 LYS B N   1 
ATOM   9647  C CA  . LYS B 1 559 ? 22.022  38.311  -31.105 1.00 32.99  ? 559 LYS B CA  1 
ATOM   9648  C C   . LYS B 1 559 ? 23.347  37.769  -31.640 1.00 33.17  ? 559 LYS B C   1 
ATOM   9649  O O   . LYS B 1 559 ? 23.728  38.057  -32.778 1.00 31.75  ? 559 LYS B O   1 
ATOM   9650  C CB  . LYS B 1 559 ? 22.277  39.665  -30.456 1.00 33.49  ? 559 LYS B CB  1 
ATOM   9651  C CG  . LYS B 1 559 ? 21.067  40.555  -30.402 1.00 34.81  ? 559 LYS B CG  1 
ATOM   9652  C CD  . LYS B 1 559 ? 21.476  41.883  -29.816 1.00 37.68  ? 559 LYS B CD  1 
ATOM   9653  C CE  . LYS B 1 559 ? 20.343  42.895  -29.839 1.00 39.12  ? 559 LYS B CE  1 
ATOM   9654  N NZ  . LYS B 1 559 ? 20.781  44.038  -28.976 1.00 42.60  ? 559 LYS B NZ  1 
ATOM   9655  N N   . SER B 1 560 ? 24.048  36.987  -30.831 1.00 33.77  ? 560 SER B N   1 
ATOM   9656  C CA  . SER B 1 560 ? 25.328  36.460  -31.268 1.00 36.56  ? 560 SER B CA  1 
ATOM   9657  C C   . SER B 1 560 ? 25.202  35.146  -32.010 1.00 36.85  ? 560 SER B C   1 
ATOM   9658  O O   . SER B 1 560 ? 26.110  34.788  -32.770 1.00 39.49  ? 560 SER B O   1 
ATOM   9659  C CB  . SER B 1 560 ? 26.300  36.303  -30.095 1.00 38.67  ? 560 SER B CB  1 
ATOM   9660  O OG  . SER B 1 560 ? 25.678  35.596  -29.042 1.00 42.79  ? 560 SER B OG  1 
ATOM   9661  N N   . ARG B 1 561 ? 24.100  34.421  -31.797 1.00 33.60  ? 561 ARG B N   1 
ATOM   9662  C CA  . ARG B 1 561 ? 23.997  33.052  -32.308 1.00 33.31  ? 561 ARG B CA  1 
ATOM   9663  C C   . ARG B 1 561 ? 23.006  32.915  -33.460 1.00 33.16  ? 561 ARG B C   1 
ATOM   9664  O O   . ARG B 1 561 ? 23.135  31.991  -34.288 1.00 32.30  ? 561 ARG B O   1 
ATOM   9665  C CB  . ARG B 1 561 ? 23.633  32.061  -31.191 1.00 35.29  ? 561 ARG B CB  1 
ATOM   9666  C CG  . ARG B 1 561 ? 24.712  31.838  -30.137 1.00 35.74  ? 561 ARG B CG  1 
ATOM   9667  C CD  . ARG B 1 561 ? 24.454  30.578  -29.304 1.00 36.86  ? 561 ARG B CD  1 
ATOM   9668  N NE  . ARG B 1 561 ? 25.304  30.535  -28.102 1.00 38.71  ? 561 ARG B NE  1 
ATOM   9669  C CZ  . ARG B 1 561 ? 25.404  29.499  -27.260 1.00 39.20  ? 561 ARG B CZ  1 
ATOM   9670  N NH1 . ARG B 1 561 ? 24.696  28.377  -27.450 1.00 38.20  ? 561 ARG B NH1 1 
ATOM   9671  N NH2 . ARG B 1 561 ? 26.206  29.591  -26.207 1.00 37.08  ? 561 ARG B NH2 1 
ATOM   9672  N N   . GLU B 1 562 ? 22.022  33.817  -33.511 1.00 31.04  ? 562 GLU B N   1 
ATOM   9673  C CA  . GLU B 1 562 ? 20.948  33.735  -34.503 1.00 30.59  ? 562 GLU B CA  1 
ATOM   9674  C C   . GLU B 1 562 ? 20.963  34.819  -35.567 1.00 30.93  ? 562 GLU B C   1 
ATOM   9675  O O   . GLU B 1 562 ? 21.331  35.979  -35.336 1.00 28.91  ? 562 GLU B O   1 
ATOM   9676  C CB  . GLU B 1 562 ? 19.545  33.726  -33.851 1.00 29.05  ? 562 GLU B CB  1 
ATOM   9677  C CG  . GLU B 1 562 ? 19.325  32.703  -32.749 1.00 30.11  ? 562 GLU B CG  1 
ATOM   9678  C CD  . GLU B 1 562 ? 19.738  31.293  -33.133 1.00 30.10  ? 562 GLU B CD  1 
ATOM   9679  O OE1 . GLU B 1 562 ? 19.511  30.861  -34.283 1.00 30.72  ? 562 GLU B OE1 1 
ATOM   9680  O OE2 . GLU B 1 562 ? 20.289  30.618  -32.270 1.00 30.35  ? 562 GLU B OE2 1 
ATOM   9681  N N   . LYS B 1 563 ? 20.479  34.424  -36.727 1.00 32.80  ? 563 LYS B N   1 
ATOM   9682  C CA  . LYS B 1 563 ? 20.302  35.312  -37.840 1.00 34.29  ? 563 LYS B CA  1 
ATOM   9683  C C   . LYS B 1 563 ? 19.045  36.161  -37.627 1.00 33.42  ? 563 LYS B C   1 
ATOM   9684  O O   . LYS B 1 563 ? 17.924  35.651  -37.693 1.00 35.37  ? 563 LYS B O   1 
ATOM   9685  C CB  . LYS B 1 563 ? 20.198  34.460  -39.112 1.00 35.63  ? 563 LYS B CB  1 
ATOM   9686  C CG  . LYS B 1 563 ? 20.087  35.236  -40.407 1.00 38.50  ? 563 LYS B CG  1 
ATOM   9687  C CD  . LYS B 1 563 ? 21.306  36.105  -40.623 1.00 39.10  ? 563 LYS B CD  1 
ATOM   9688  C CE  . LYS B 1 563 ? 21.727  36.056  -42.081 1.00 41.55  ? 563 LYS B CE  1 
ATOM   9689  N NZ  . LYS B 1 563 ? 22.881  36.957  -42.327 1.00 42.05  ? 563 LYS B NZ  1 
ATOM   9690  N N   . LEU B 1 564 ? 19.238  37.452  -37.364 1.00 33.52  ? 564 LEU B N   1 
ATOM   9691  C CA  . LEU B 1 564 ? 18.118  38.395  -37.151 1.00 32.90  ? 564 LEU B CA  1 
ATOM   9692  C C   . LEU B 1 564 ? 17.802  39.264  -38.361 1.00 32.91  ? 564 LEU B C   1 
ATOM   9693  O O   . LEU B 1 564 ? 16.740  39.899  -38.422 1.00 33.86  ? 564 LEU B O   1 
ATOM   9694  C CB  . LEU B 1 564 ? 18.390  39.296  -35.950 1.00 32.79  ? 564 LEU B CB  1 
ATOM   9695  C CG  . LEU B 1 564 ? 18.597  38.581  -34.620 1.00 33.11  ? 564 LEU B CG  1 
ATOM   9696  C CD1 . LEU B 1 564 ? 18.776  39.596  -33.509 1.00 33.68  ? 564 LEU B CD1 1 
ATOM   9697  C CD2 . LEU B 1 564 ? 17.434  37.648  -34.330 1.00 32.55  ? 564 LEU B CD2 1 
ATOM   9698  N N   . THR B 1 565 ? 18.718  39.308  -39.319 1.00 33.48  ? 565 THR B N   1 
ATOM   9699  C CA  . THR B 1 565 ? 18.498  40.094  -40.542 1.00 34.59  ? 565 THR B CA  1 
ATOM   9700  C C   . THR B 1 565 ? 17.833  39.232  -41.618 1.00 34.64  ? 565 THR B C   1 
ATOM   9701  O O   . THR B 1 565 ? 18.065  38.045  -41.685 1.00 36.33  ? 565 THR B O   1 
ATOM   9702  C CB  . THR B 1 565 ? 19.795  40.739  -41.077 1.00 32.29  ? 565 THR B CB  1 
ATOM   9703  O OG1 . THR B 1 565 ? 20.796  39.729  -41.285 1.00 31.18  ? 565 THR B OG1 1 
ATOM   9704  C CG2 . THR B 1 565 ? 20.308  41.777  -40.097 1.00 32.13  ? 565 THR B CG2 1 
ATOM   9705  N N   . MET B 1 566 ? 16.995  39.841  -42.440 1.00 35.36  ? 566 MET B N   1 
ATOM   9706  C CA  . MET B 1 566 ? 16.270  39.108  -43.454 1.00 36.59  ? 566 MET B CA  1 
ATOM   9707  C C   . MET B 1 566 ? 16.058  39.944  -44.709 1.00 37.17  ? 566 MET B C   1 
ATOM   9708  O O   . MET B 1 566 ? 15.943  41.171  -44.652 1.00 36.26  ? 566 MET B O   1 
ATOM   9709  C CB  . MET B 1 566 ? 14.923  38.624  -42.909 1.00 38.46  ? 566 MET B CB  1 
ATOM   9710  C CG  . MET B 1 566 ? 13.961  39.719  -42.478 1.00 40.77  ? 566 MET B CG  1 
ATOM   9711  S SD  . MET B 1 566 ? 14.091  40.125  -40.723 1.00 47.54  ? 566 MET B SD  1 
ATOM   9712  C CE  . MET B 1 566 ? 12.472  40.823  -40.414 1.00 41.35  ? 566 MET B CE  1 
ATOM   9713  N N   . LYS B 1 567 ? 16.015  39.263  -45.842 1.00 37.66  ? 567 LYS B N   1 
ATOM   9714  C CA  . LYS B 1 567 ? 15.801  39.902  -47.115 1.00 38.56  ? 567 LYS B CA  1 
ATOM   9715  C C   . LYS B 1 567 ? 14.307  39.971  -47.421 1.00 37.72  ? 567 LYS B C   1 
ATOM   9716  O O   . LYS B 1 567 ? 13.617  38.958  -47.377 1.00 36.75  ? 567 LYS B O   1 
ATOM   9717  C CB  . LYS B 1 567 ? 16.540  39.130  -48.219 1.00 38.75  ? 567 LYS B CB  1 
ATOM   9718  C CG  . LYS B 1 567 ? 16.363  39.727  -49.596 1.00 38.72  ? 567 LYS B CG  1 
ATOM   9719  C CD  . LYS B 1 567 ? 17.043  38.892  -50.663 1.00 41.15  ? 567 LYS B CD  1 
ATOM   9720  C CE  . LYS B 1 567 ? 16.776  39.503  -52.046 1.00 43.04  ? 567 LYS B CE  1 
ATOM   9721  N NZ  . LYS B 1 567 ? 17.861  39.243  -53.030 1.00 45.20  ? 567 LYS B NZ  1 
ATOM   9722  N N   . PHE B 1 568 ? 13.827  41.171  -47.736 1.00 37.71  ? 568 PHE B N   1 
ATOM   9723  C CA  . PHE B 1 568 ? 12.436  41.376  -48.164 1.00 39.18  ? 568 PHE B CA  1 
ATOM   9724  C C   . PHE B 1 568 ? 12.303  41.390  -49.688 1.00 39.48  ? 568 PHE B C   1 
ATOM   9725  O O   . PHE B 1 568 ? 13.275  41.630  -50.393 1.00 43.55  ? 568 PHE B O   1 
ATOM   9726  C CB  . PHE B 1 568 ? 11.876  42.682  -47.584 1.00 39.28  ? 568 PHE B CB  1 
ATOM   9727  C CG  . PHE B 1 568 ? 11.727  42.665  -46.093 1.00 40.39  ? 568 PHE B CG  1 
ATOM   9728  C CD1 . PHE B 1 568 ? 10.848  41.779  -45.478 1.00 39.15  ? 568 PHE B CD1 1 
ATOM   9729  C CD2 . PHE B 1 568 ? 12.462  43.546  -45.294 1.00 40.70  ? 568 PHE B CD2 1 
ATOM   9730  C CE1 . PHE B 1 568 ? 10.710  41.761  -44.100 1.00 38.33  ? 568 PHE B CE1 1 
ATOM   9731  C CE2 . PHE B 1 568 ? 12.330  43.522  -43.910 1.00 39.97  ? 568 PHE B CE2 1 
ATOM   9732  C CZ  . PHE B 1 568 ? 11.460  42.624  -43.316 1.00 38.51  ? 568 PHE B CZ  1 
ATOM   9733  N N   . HIS B 1 569 ? 11.095  41.146  -50.192 1.00 40.28  ? 569 HIS B N   1 
ATOM   9734  C CA  . HIS B 1 569 ? 10.860  41.094  -51.635 1.00 39.21  ? 569 HIS B CA  1 
ATOM   9735  C C   . HIS B 1 569 ? 9.775   42.001  -52.088 1.00 40.13  ? 569 HIS B C   1 
ATOM   9736  O O   . HIS B 1 569 ? 9.291   41.897  -53.220 1.00 40.49  ? 569 HIS B O   1 
ATOM   9737  C CB  . HIS B 1 569 ? 10.546  39.685  -52.055 1.00 39.40  ? 569 HIS B CB  1 
ATOM   9738  C CG  . HIS B 1 569 ? 11.674  38.749  -51.853 1.00 39.76  ? 569 HIS B CG  1 
ATOM   9739  N ND1 . HIS B 1 569 ? 11.915  38.163  -50.674 1.00 40.28  ? 569 HIS B ND1 1 
ATOM   9740  C CD2 . HIS B 1 569 ? 12.665  38.313  -52.720 1.00 41.93  ? 569 HIS B CD2 1 
ATOM   9741  C CE1 . HIS B 1 569 ? 12.992  37.374  -50.776 1.00 40.41  ? 569 HIS B CE1 1 
ATOM   9742  N NE2 . HIS B 1 569 ? 13.449  37.461  -52.030 1.00 43.51  ? 569 HIS B NE2 1 
ATOM   9743  N N   . ASP B 1 570 ? 9.364   42.898  -51.206 1.00 41.63  ? 570 ASP B N   1 
ATOM   9744  C CA  . ASP B 1 570 ? 8.375   43.899  -51.556 1.00 43.08  ? 570 ASP B CA  1 
ATOM   9745  C C   . ASP B 1 570 ? 8.884   45.269  -51.134 1.00 41.89  ? 570 ASP B C   1 
ATOM   9746  O O   . ASP B 1 570 ? 9.097   45.522  -49.942 1.00 40.62  ? 570 ASP B O   1 
ATOM   9747  C CB  . ASP B 1 570 ? 7.024   43.583  -50.894 1.00 44.38  ? 570 ASP B CB  1 
ATOM   9748  C CG  . ASP B 1 570 ? 5.900   44.525  -51.355 1.00 47.37  ? 570 ASP B CG  1 
ATOM   9749  O OD1 . ASP B 1 570 ? 6.202   45.564  -51.976 1.00 45.30  ? 570 ASP B OD1 1 
ATOM   9750  O OD2 . ASP B 1 570 ? 4.712   44.224  -51.081 1.00 49.75  ? 570 ASP B OD2 1 
ATOM   9751  N N   . GLY B 1 571 ? 9.082   46.148  -52.115 1.00 41.55  ? 571 GLY B N   1 
ATOM   9752  C CA  . GLY B 1 571 ? 9.516   47.522  -51.842 1.00 42.05  ? 571 GLY B CA  1 
ATOM   9753  C C   . GLY B 1 571 ? 8.551   48.288  -50.954 1.00 41.59  ? 571 GLY B C   1 
ATOM   9754  O O   . GLY B 1 571 ? 8.866   49.363  -50.468 1.00 42.29  ? 571 GLY B O   1 
ATOM   9755  N N   . GLU B 1 572 ? 7.375   47.721  -50.724 1.00 44.86  ? 572 GLU B N   1 
ATOM   9756  C CA  . GLU B 1 572 ? 6.331   48.417  -49.983 1.00 46.89  ? 572 GLU B CA  1 
ATOM   9757  C C   . GLU B 1 572 ? 6.279   47.994  -48.522 1.00 44.04  ? 572 GLU B C   1 
ATOM   9758  O O   . GLU B 1 572 ? 5.510   48.552  -47.735 1.00 45.68  ? 572 GLU B O   1 
ATOM   9759  C CB  . GLU B 1 572 ? 4.979   48.179  -50.634 1.00 53.13  ? 572 GLU B CB  1 
ATOM   9760  C CG  . GLU B 1 572 ? 4.147   49.437  -50.784 1.00 64.08  ? 572 GLU B CG  1 
ATOM   9761  C CD  . GLU B 1 572 ? 4.281   50.055  -52.158 1.00 67.12  ? 572 GLU B CD  1 
ATOM   9762  O OE1 . GLU B 1 572 ? 4.144   49.314  -53.153 1.00 69.86  ? 572 GLU B OE1 1 
ATOM   9763  O OE2 . GLU B 1 572 ? 4.515   51.281  -52.241 1.00 73.69  ? 572 GLU B OE2 1 
ATOM   9764  N N   . VAL B 1 573 ? 7.070   46.987  -48.166 1.00 40.31  ? 573 VAL B N   1 
ATOM   9765  C CA  . VAL B 1 573 ? 7.166   46.557  -46.782 1.00 37.45  ? 573 VAL B CA  1 
ATOM   9766  C C   . VAL B 1 573 ? 7.476   47.732  -45.884 1.00 37.03  ? 573 VAL B C   1 
ATOM   9767  O O   . VAL B 1 573 ? 8.230   48.634  -46.267 1.00 35.01  ? 573 VAL B O   1 
ATOM   9768  C CB  . VAL B 1 573 ? 8.259   45.490  -46.578 1.00 35.58  ? 573 VAL B CB  1 
ATOM   9769  C CG1 . VAL B 1 573 ? 9.642   46.060  -46.841 1.00 35.17  ? 573 VAL B CG1 1 
ATOM   9770  C CG2 . VAL B 1 573 ? 8.179   44.915  -45.174 1.00 35.06  ? 573 VAL B CG2 1 
ATOM   9771  N N   . ASP B 1 574 ? 6.897   47.710  -44.684 1.00 36.91  ? 574 ASP B N   1 
ATOM   9772  C CA  . ASP B 1 574 ? 7.367   48.559  -43.611 1.00 37.72  ? 574 ASP B CA  1 
ATOM   9773  C C   . ASP B 1 574 ? 8.375   47.760  -42.805 1.00 35.84  ? 574 ASP B C   1 
ATOM   9774  O O   . ASP B 1 574 ? 8.014   46.986  -41.913 1.00 35.72  ? 574 ASP B O   1 
ATOM   9775  C CB  . ASP B 1 574 ? 6.209   49.042  -42.730 1.00 40.15  ? 574 ASP B CB  1 
ATOM   9776  C CG  . ASP B 1 574 ? 6.665   50.004  -41.649 1.00 42.41  ? 574 ASP B CG  1 
ATOM   9777  O OD1 . ASP B 1 574 ? 7.852   50.372  -41.637 1.00 44.35  ? 574 ASP B OD1 1 
ATOM   9778  O OD2 . ASP B 1 574 ? 5.840   50.399  -40.809 1.00 47.83  ? 574 ASP B OD2 1 
ATOM   9779  N N   . ALA B 1 575 ? 9.642   47.925  -43.155 1.00 35.45  ? 575 ALA B N   1 
ATOM   9780  C CA  . ALA B 1 575 ? 10.733  47.216  -42.485 1.00 34.33  ? 575 ALA B CA  1 
ATOM   9781  C C   . ALA B 1 575 ? 10.748  47.561  -41.004 1.00 32.29  ? 575 ALA B C   1 
ATOM   9782  O O   . ALA B 1 575 ? 11.118  46.739  -40.174 1.00 29.14  ? 575 ALA B O   1 
ATOM   9783  C CB  . ALA B 1 575 ? 12.063  47.574  -43.125 1.00 33.71  ? 575 ALA B CB  1 
ATOM   9784  N N   . SER B 1 576 ? 10.300  48.770  -40.675 1.00 32.43  ? 576 SER B N   1 
ATOM   9785  C CA  . SER B 1 576 ? 10.404  49.256  -39.305 1.00 33.78  ? 576 SER B CA  1 
ATOM   9786  C C   . SER B 1 576 ? 9.499   48.497  -38.332 1.00 32.97  ? 576 SER B C   1 
ATOM   9787  O O   . SER B 1 576 ? 9.771   48.459  -37.131 1.00 33.19  ? 576 SER B O   1 
ATOM   9788  C CB  . SER B 1 576 ? 10.166  50.764  -39.226 1.00 34.02  ? 576 SER B CB  1 
ATOM   9789  O OG  . SER B 1 576 ? 8.793   51.056  -39.415 1.00 39.12  ? 576 SER B OG  1 
ATOM   9790  N N   . TYR B 1 577 ? 8.475   47.839  -38.864 1.00 32.52  ? 577 TYR B N   1 
ATOM   9791  C CA  . TYR B 1 577 ? 7.563   47.034  -38.060 1.00 33.81  ? 577 TYR B CA  1 
ATOM   9792  C C   . TYR B 1 577 ? 8.284   45.973  -37.245 1.00 34.02  ? 577 TYR B C   1 
ATOM   9793  O O   . TYR B 1 577 ? 7.832   45.607  -36.165 1.00 33.31  ? 577 TYR B O   1 
ATOM   9794  C CB  . TYR B 1 577 ? 6.491   46.367  -38.938 1.00 34.26  ? 577 TYR B CB  1 
ATOM   9795  C CG  . TYR B 1 577 ? 5.254   45.932  -38.168 1.00 34.44  ? 577 TYR B CG  1 
ATOM   9796  C CD1 . TYR B 1 577 ? 4.390   46.880  -37.605 1.00 34.13  ? 577 TYR B CD1 1 
ATOM   9797  C CD2 . TYR B 1 577 ? 4.944   44.576  -37.999 1.00 33.87  ? 577 TYR B CD2 1 
ATOM   9798  C CE1 . TYR B 1 577 ? 3.272   46.496  -36.898 1.00 32.59  ? 577 TYR B CE1 1 
ATOM   9799  C CE2 . TYR B 1 577 ? 3.818   44.186  -37.291 1.00 30.92  ? 577 TYR B CE2 1 
ATOM   9800  C CZ  . TYR B 1 577 ? 2.996   45.154  -36.745 1.00 31.70  ? 577 TYR B CZ  1 
ATOM   9801  O OH  . TYR B 1 577 ? 1.876   44.794  -36.043 1.00 32.01  ? 577 TYR B OH  1 
ATOM   9802  N N   . PHE B 1 578 ? 9.412   45.497  -37.749 1.00 32.93  ? 578 PHE B N   1 
ATOM   9803  C CA  . PHE B 1 578 ? 10.068  44.349  -37.137 1.00 35.08  ? 578 PHE B CA  1 
ATOM   9804  C C   . PHE B 1 578 ? 11.189  44.741  -36.165 1.00 36.13  ? 578 PHE B C   1 
ATOM   9805  O O   . PHE B 1 578 ? 11.806  43.881  -35.541 1.00 35.59  ? 578 PHE B O   1 
ATOM   9806  C CB  . PHE B 1 578 ? 10.571  43.384  -38.218 1.00 36.31  ? 578 PHE B CB  1 
ATOM   9807  C CG  . PHE B 1 578 ? 9.506   42.962  -39.194 1.00 35.82  ? 578 PHE B CG  1 
ATOM   9808  C CD1 . PHE B 1 578 ? 8.666   41.875  -38.914 1.00 36.58  ? 578 PHE B CD1 1 
ATOM   9809  C CD2 . PHE B 1 578 ? 9.330   43.646  -40.380 1.00 35.82  ? 578 PHE B CD2 1 
ATOM   9810  C CE1 . PHE B 1 578 ? 7.682   41.484  -39.810 1.00 35.89  ? 578 PHE B CE1 1 
ATOM   9811  C CE2 . PHE B 1 578 ? 8.329   43.269  -41.272 1.00 38.83  ? 578 PHE B CE2 1 
ATOM   9812  C CZ  . PHE B 1 578 ? 7.504   42.186  -40.984 1.00 36.65  ? 578 PHE B CZ  1 
ATOM   9813  N N   . CYS B 1 579 ? 11.386  46.048  -36.002 1.00 37.61  ? 579 CYS B N   1 
ATOM   9814  C CA  . CYS B 1 579 ? 12.416  46.609  -35.136 1.00 38.84  ? 579 CYS B CA  1 
ATOM   9815  C C   . CYS B 1 579 ? 11.976  46.679  -33.681 1.00 37.40  ? 579 CYS B C   1 
ATOM   9816  O O   . CYS B 1 579 ? 12.818  46.786  -32.788 1.00 35.00  ? 579 CYS B O   1 
ATOM   9817  C CB  . CYS B 1 579 ? 12.733  48.047  -35.574 1.00 44.58  ? 579 CYS B CB  1 
ATOM   9818  S SG  . CYS B 1 579 ? 13.796  48.224  -37.009 1.00 56.33  ? 579 CYS B SG  1 
ATOM   9819  N N   . LYS B 1 580 ? 10.657  46.680  -33.450 1.00 35.03  ? 580 LYS B N   1 
ATOM   9820  C CA  . LYS B 1 580 ? 10.084  47.126  -32.166 1.00 35.20  ? 580 LYS B CA  1 
ATOM   9821  C C   . LYS B 1 580 ? 8.798   46.381  -31.784 1.00 32.71  ? 580 LYS B C   1 
ATOM   9822  O O   . LYS B 1 580 ? 8.149   45.750  -32.635 1.00 32.56  ? 580 LYS B O   1 
ATOM   9823  C CB  . LYS B 1 580 ? 9.789   48.643  -32.243 1.00 36.97  ? 580 LYS B CB  1 
ATOM   9824  C CG  . LYS B 1 580 ? 8.757   49.003  -33.326 1.00 37.58  ? 580 LYS B CG  1 
ATOM   9825  C CD  . LYS B 1 580 ? 8.669   50.497  -33.640 1.00 39.43  ? 580 LYS B CD  1 
ATOM   9826  C CE  . LYS B 1 580 ? 7.837   50.755  -34.914 1.00 39.16  ? 580 LYS B CE  1 
ATOM   9827  N NZ  . LYS B 1 580 ? 6.408   50.303  -34.823 1.00 38.26  ? 580 LYS B NZ  1 
ATOM   9828  N N   . LEU B 1 581 ? 8.409   46.482  -30.518 1.00 31.58  ? 581 LEU B N   1 
ATOM   9829  C CA  . LEU B 1 581 ? 7.034   46.158  -30.124 1.00 32.13  ? 581 LEU B CA  1 
ATOM   9830  C C   . LEU B 1 581 ? 6.092   47.017  -30.933 1.00 33.50  ? 581 LEU B C   1 
ATOM   9831  O O   . LEU B 1 581 ? 6.221   48.241  -30.908 1.00 36.80  ? 581 LEU B O   1 
ATOM   9832  C CB  . LEU B 1 581 ? 6.814   46.470  -28.648 1.00 33.09  ? 581 LEU B CB  1 
ATOM   9833  C CG  . LEU B 1 581 ? 6.751   45.341  -27.615 1.00 34.07  ? 581 LEU B CG  1 
ATOM   9834  C CD1 . LEU B 1 581 ? 7.411   44.073  -28.094 1.00 33.07  ? 581 LEU B CD1 1 
ATOM   9835  C CD2 . LEU B 1 581 ? 7.341   45.775  -26.293 1.00 34.20  ? 581 LEU B CD2 1 
ATOM   9836  N N   . PRO B 1 582 ? 5.145   46.398  -31.663 1.00 32.70  ? 582 PRO B N   1 
ATOM   9837  C CA  . PRO B 1 582 ? 4.064   47.191  -32.234 1.00 33.85  ? 582 PRO B CA  1 
ATOM   9838  C C   . PRO B 1 582 ? 3.245   47.842  -31.125 1.00 37.94  ? 582 PRO B C   1 
ATOM   9839  O O   . PRO B 1 582 ? 2.986   47.209  -30.094 1.00 38.05  ? 582 PRO B O   1 
ATOM   9840  C CB  . PRO B 1 582 ? 3.198   46.155  -32.963 1.00 33.90  ? 582 PRO B CB  1 
ATOM   9841  C CG  . PRO B 1 582 ? 4.007   44.896  -33.040 1.00 32.28  ? 582 PRO B CG  1 
ATOM   9842  C CD  . PRO B 1 582 ? 4.962   44.955  -31.890 1.00 32.86  ? 582 PRO B CD  1 
ATOM   9843  N N   . GLU B 1 583 ? 2.801   49.073  -31.354 1.00 41.02  ? 583 GLU B N   1 
ATOM   9844  C CA  . GLU B 1 583 ? 2.073   49.844  -30.341 1.00 44.46  ? 583 GLU B CA  1 
ATOM   9845  C C   . GLU B 1 583 ? 0.887   49.111  -29.627 1.00 41.60  ? 583 GLU B C   1 
ATOM   9846  O O   . GLU B 1 583 ? 0.674   49.287  -28.427 1.00 38.24  ? 583 GLU B O   1 
ATOM   9847  C CB  . GLU B 1 583 ? 1.638   51.209  -30.914 1.00 51.51  ? 583 GLU B CB  1 
ATOM   9848  C CG  . GLU B 1 583 ? 2.782   52.004  -31.558 1.00 60.35  ? 583 GLU B CG  1 
ATOM   9849  C CD  . GLU B 1 583 ? 4.008   52.154  -30.647 1.00 67.20  ? 583 GLU B CD  1 
ATOM   9850  O OE1 . GLU B 1 583 ? 3.893   52.859  -29.614 1.00 67.28  ? 583 GLU B OE1 1 
ATOM   9851  O OE2 . GLU B 1 583 ? 5.089   51.572  -30.965 1.00 68.24  ? 583 GLU B OE2 1 
ATOM   9852  N N   . LYS B 1 584 ? 0.167   48.261  -30.347 1.00 38.09  ? 584 LYS B N   1 
ATOM   9853  C CA  . LYS B 1 584 ? -0.933  47.524  -29.738 1.00 38.06  ? 584 LYS B CA  1 
ATOM   9854  C C   . LYS B 1 584 ? -0.465  46.496  -28.700 1.00 38.34  ? 584 LYS B C   1 
ATOM   9855  O O   . LYS B 1 584 ? -1.260  46.022  -27.895 1.00 40.25  ? 584 LYS B O   1 
ATOM   9856  C CB  . LYS B 1 584 ? -1.794  46.855  -30.811 1.00 37.95  ? 584 LYS B CB  1 
ATOM   9857  C CG  . LYS B 1 584 ? -1.141  45.659  -31.478 1.00 38.57  ? 584 LYS B CG  1 
ATOM   9858  C CD  . LYS B 1 584 ? -1.811  45.350  -32.795 1.00 38.62  ? 584 LYS B CD  1 
ATOM   9859  C CE  . LYS B 1 584 ? -1.034  44.310  -33.564 1.00 37.56  ? 584 LYS B CE  1 
ATOM   9860  N NZ  . LYS B 1 584 ? -1.153  44.592  -35.017 1.00 36.63  ? 584 LYS B NZ  1 
ATOM   9861  N N   . PHE B 1 585 ? 0.829   46.170  -28.714 1.00 38.25  ? 585 PHE B N   1 
ATOM   9862  C CA  . PHE B 1 585 ? 1.418   45.218  -27.763 1.00 37.04  ? 585 PHE B CA  1 
ATOM   9863  C C   . PHE B 1 585 ? 2.397   45.919  -26.801 1.00 36.96  ? 585 PHE B C   1 
ATOM   9864  O O   . PHE B 1 585 ? 3.022   45.279  -25.946 1.00 33.84  ? 585 PHE B O   1 
ATOM   9865  C CB  . PHE B 1 585 ? 2.201   44.125  -28.526 1.00 36.40  ? 585 PHE B CB  1 
ATOM   9866  C CG  . PHE B 1 585 ? 1.337   43.126  -29.281 1.00 34.61  ? 585 PHE B CG  1 
ATOM   9867  C CD1 . PHE B 1 585 ? 0.404   42.343  -28.623 1.00 33.13  ? 585 PHE B CD1 1 
ATOM   9868  C CD2 . PHE B 1 585 ? 1.548   42.898  -30.643 1.00 32.92  ? 585 PHE B CD2 1 
ATOM   9869  C CE1 . PHE B 1 585 ? -0.340  41.388  -29.316 1.00 33.48  ? 585 PHE B CE1 1 
ATOM   9870  C CE2 . PHE B 1 585 ? 0.799   41.949  -31.340 1.00 31.45  ? 585 PHE B CE2 1 
ATOM   9871  C CZ  . PHE B 1 585 ? -0.145  41.197  -30.676 1.00 31.46  ? 585 PHE B CZ  1 
ATOM   9872  N N   . ARG B 1 586 ? 2.569   47.221  -26.972 1.00 40.12  ? 586 ARG B N   1 
ATOM   9873  C CA  . ARG B 1 586 ? 3.686   47.911  -26.331 1.00 43.22  ? 586 ARG B CA  1 
ATOM   9874  C C   . ARG B 1 586 ? 3.465   48.221  -24.846 1.00 44.31  ? 586 ARG B C   1 
ATOM   9875  O O   . ARG B 1 586 ? 4.437   48.288  -24.086 1.00 46.97  ? 586 ARG B O   1 
ATOM   9876  C CB  . ARG B 1 586 ? 4.081   49.172  -27.112 1.00 45.42  ? 586 ARG B CB  1 
ATOM   9877  C CG  . ARG B 1 586 ? 5.518   49.619  -26.884 1.00 49.92  ? 586 ARG B CG  1 
ATOM   9878  C CD  . ARG B 1 586 ? 6.139   50.230  -28.131 1.00 57.12  ? 586 ARG B CD  1 
ATOM   9879  N NE  . ARG B 1 586 ? 5.924   51.673  -28.227 1.00 62.74  ? 586 ARG B NE  1 
ATOM   9880  C CZ  . ARG B 1 586 ? 6.631   52.590  -27.561 1.00 69.20  ? 586 ARG B CZ  1 
ATOM   9881  N NH1 . ARG B 1 586 ? 7.602   52.216  -26.724 1.00 66.23  ? 586 ARG B NH1 1 
ATOM   9882  N NH2 . ARG B 1 586 ? 6.353   53.888  -27.717 1.00 65.92  ? 586 ARG B NH2 1 
ATOM   9883  N N   . PHE B 1 587 ? 2.203   48.367  -24.428 1.00 43.52  ? 587 PHE B N   1 
ATOM   9884  C CA  . PHE B 1 587 ? 1.897   48.871  -23.076 1.00 45.85  ? 587 PHE B CA  1 
ATOM   9885  C C   . PHE B 1 587 ? 1.049   47.930  -22.218 1.00 44.89  ? 587 PHE B C   1 
ATOM   9886  O O   . PHE B 1 587 ? 0.521   48.329  -21.181 1.00 42.63  ? 587 PHE B O   1 
ATOM   9887  C CB  . PHE B 1 587 ? 1.227   50.249  -23.146 1.00 48.03  ? 587 PHE B CB  1 
ATOM   9888  C CG  . PHE B 1 587 ? 1.935   51.227  -24.048 1.00 52.32  ? 587 PHE B CG  1 
ATOM   9889  C CD1 . PHE B 1 587 ? 3.188   51.738  -23.702 1.00 51.94  ? 587 PHE B CD1 1 
ATOM   9890  C CD2 . PHE B 1 587 ? 1.351   51.635  -25.251 1.00 52.45  ? 587 PHE B CD2 1 
ATOM   9891  C CE1 . PHE B 1 587 ? 3.844   52.635  -24.533 1.00 52.31  ? 587 PHE B CE1 1 
ATOM   9892  C CE2 . PHE B 1 587 ? 2.002   52.535  -26.083 1.00 54.88  ? 587 PHE B CE2 1 
ATOM   9893  C CZ  . PHE B 1 587 ? 3.248   53.039  -25.723 1.00 52.91  ? 587 PHE B CZ  1 
ATOM   9894  N N   . VAL B 1 588 ? 0.924   46.679  -22.646 1.00 43.31  ? 588 VAL B N   1 
ATOM   9895  C CA  . VAL B 1 588 ? 0.321   45.663  -21.799 1.00 40.53  ? 588 VAL B CA  1 
ATOM   9896  C C   . VAL B 1 588 ? 1.169   45.538  -20.551 1.00 38.04  ? 588 VAL B C   1 
ATOM   9897  O O   . VAL B 1 588 ? 2.397   45.626  -20.615 1.00 37.24  ? 588 VAL B O   1 
ATOM   9898  C CB  . VAL B 1 588 ? 0.176   44.302  -22.527 1.00 40.65  ? 588 VAL B CB  1 
ATOM   9899  C CG1 . VAL B 1 588 ? -0.607  44.485  -23.811 1.00 42.32  ? 588 VAL B CG1 1 
ATOM   9900  C CG2 . VAL B 1 588 ? 1.526   43.696  -22.840 1.00 37.43  ? 588 VAL B CG2 1 
ATOM   9901  N N   . LYS B 1 589 ? 0.518   45.426  -19.404 1.00 39.48  ? 589 LYS B N   1 
ATOM   9902  C CA  . LYS B 1 589 ? 1.249   45.275  -18.148 1.00 39.92  ? 589 LYS B CA  1 
ATOM   9903  C C   . LYS B 1 589 ? 1.867   43.898  -18.054 1.00 37.09  ? 589 LYS B C   1 
ATOM   9904  O O   . LYS B 1 589 ? 1.245   42.909  -18.406 1.00 36.42  ? 589 LYS B O   1 
ATOM   9905  C CB  . LYS B 1 589 ? 0.333   45.513  -16.950 1.00 41.81  ? 589 LYS B CB  1 
ATOM   9906  C CG  . LYS B 1 589 ? 0.248   46.967  -16.519 1.00 47.60  ? 589 LYS B CG  1 
ATOM   9907  C CD  . LYS B 1 589 ? 0.535   47.104  -15.026 1.00 51.47  ? 589 LYS B CD  1 
ATOM   9908  C CE  . LYS B 1 589 ? -0.654  46.682  -14.178 1.00 54.39  ? 589 LYS B CE  1 
ATOM   9909  N NZ  . LYS B 1 589 ? -0.231  46.033  -12.898 1.00 53.81  ? 589 LYS B NZ  1 
ATOM   9910  N N   . ILE B 1 590 ? 3.086   43.838  -17.550 1.00 37.48  ? 590 ILE B N   1 
ATOM   9911  C CA  . ILE B 1 590 ? 3.751   42.563  -17.330 1.00 36.81  ? 590 ILE B CA  1 
ATOM   9912  C C   . ILE B 1 590 ? 4.233   42.367  -15.885 1.00 37.67  ? 590 ILE B C   1 
ATOM   9913  O O   . ILE B 1 590 ? 4.933   41.403  -15.578 1.00 41.70  ? 590 ILE B O   1 
ATOM   9914  C CB  . ILE B 1 590 ? 4.911   42.363  -18.341 1.00 36.29  ? 590 ILE B CB  1 
ATOM   9915  C CG1 . ILE B 1 590 ? 6.109   43.253  -17.989 1.00 36.55  ? 590 ILE B CG1 1 
ATOM   9916  C CG2 . ILE B 1 590 ? 4.422   42.630  -19.765 1.00 34.93  ? 590 ILE B CG2 1 
ATOM   9917  C CD1 . ILE B 1 590 ? 7.332   43.029  -18.869 1.00 38.41  ? 590 ILE B CD1 1 
ATOM   9918  N N   . ASN B 1 591 ? 3.864   43.277  -14.997 1.00 39.00  ? 591 ASN B N   1 
ATOM   9919  C CA  . ASN B 1 591 ? 4.227   43.133  -13.590 1.00 40.04  ? 591 ASN B CA  1 
ATOM   9920  C C   . ASN B 1 591 ? 2.997   42.901  -12.715 1.00 39.24  ? 591 ASN B C   1 
ATOM   9921  O O   . ASN B 1 591 ? 2.052   43.694  -12.740 1.00 37.61  ? 591 ASN B O   1 
ATOM   9922  C CB  . ASN B 1 591 ? 4.999   44.361  -13.097 1.00 42.24  ? 591 ASN B CB  1 
ATOM   9923  C CG  . ASN B 1 591 ? 6.378   44.481  -13.726 1.00 46.00  ? 591 ASN B CG  1 
ATOM   9924  O OD1 . ASN B 1 591 ? 7.146   43.512  -13.779 1.00 48.00  ? 591 ASN B OD1 1 
ATOM   9925  N ND2 . ASN B 1 591 ? 6.709   45.682  -14.186 1.00 45.07  ? 591 ASN B ND2 1 
ATOM   9926  N N   . ARG B 1 592 ? 3.007   41.797  -11.970 1.00 37.03  ? 592 ARG B N   1 
ATOM   9927  C CA  . ARG B 1 592 ? 1.974   41.511  -10.959 1.00 38.35  ? 592 ARG B CA  1 
ATOM   9928  C C   . ARG B 1 592 ? 2.120   42.434  -9.766  1.00 39.31  ? 592 ARG B C   1 
ATOM   9929  O O   . ARG B 1 592 ? 3.212   42.594  -9.250  1.00 42.28  ? 592 ARG B O   1 
ATOM   9930  C CB  . ARG B 1 592 ? 2.165   40.089  -10.425 1.00 38.54  ? 592 ARG B CB  1 
ATOM   9931  C CG  . ARG B 1 592 ? 1.298   39.037  -11.050 1.00 35.49  ? 592 ARG B CG  1 
ATOM   9932  C CD  . ARG B 1 592 ? 1.435   37.740  -10.294 1.00 32.27  ? 592 ARG B CD  1 
ATOM   9933  N NE  . ARG B 1 592 ? 0.130   37.235  -9.849  1.00 31.59  ? 592 ARG B NE  1 
ATOM   9934  C CZ  . ARG B 1 592 ? -0.349  36.025  -10.135 1.00 32.60  ? 592 ARG B CZ  1 
ATOM   9935  N NH1 . ARG B 1 592 ? 0.349   35.201  -10.909 1.00 31.92  ? 592 ARG B NH1 1 
ATOM   9936  N NH2 . ARG B 1 592 ? -1.525  35.631  -9.642  1.00 30.96  ? 592 ARG B NH2 1 
ATOM   9937  N N   . LYS B 1 593 ? 1.023   42.986  -9.287  1.00 41.91  ? 593 LYS B N   1 
ATOM   9938  C CA  . LYS B 1 593 ? 0.994   43.522  -7.926  1.00 48.81  ? 593 LYS B CA  1 
ATOM   9939  C C   . LYS B 1 593 ? -0.431  43.553  -7.363  1.00 50.47  ? 593 LYS B C   1 
ATOM   9940  O O   . LYS B 1 593 ? -1.384  43.786  -8.098  1.00 50.03  ? 593 LYS B O   1 
ATOM   9941  C CB  . LYS B 1 593 ? 1.617   44.919  -7.872  1.00 52.21  ? 593 LYS B CB  1 
ATOM   9942  C CG  . LYS B 1 593 ? 2.167   45.285  -6.494  1.00 57.30  ? 593 LYS B CG  1 
ATOM   9943  C CD  . LYS B 1 593 ? 1.914   46.749  -6.151  1.00 59.39  ? 593 LYS B CD  1 
ATOM   9944  C CE  . LYS B 1 593 ? 1.944   46.970  -4.642  1.00 61.85  ? 593 LYS B CE  1 
ATOM   9945  N NZ  . LYS B 1 593 ? 1.294   48.247  -4.240  1.00 61.12  ? 593 LYS B NZ  1 
ATOM   9946  N N   . ALA B 1 594 ? -0.575  43.309  -6.062  1.00 52.68  ? 594 ALA B N   1 
ATOM   9947  C CA  . ALA B 1 594 ? -1.896  43.385  -5.420  1.00 49.73  ? 594 ALA B CA  1 
ATOM   9948  C C   . ALA B 1 594 ? -2.407  44.832  -5.324  1.00 52.80  ? 594 ALA B C   1 
ATOM   9949  O O   . ALA B 1 594 ? -1.677  45.737  -4.886  1.00 48.45  ? 594 ALA B O   1 
ATOM   9950  C CB  . ALA B 1 594 ? -1.855  42.754  -4.052  1.00 45.67  ? 594 ALA B CB  1 
ATOM   9951  N N   . SER B 1 595 ? -3.655  45.045  -5.744  1.00 52.27  ? 595 SER B N   1 
ATOM   9952  C CA  . SER B 1 595 ? -4.301  46.352  -5.564  1.00 58.29  ? 595 SER B CA  1 
ATOM   9953  C C   . SER B 1 595 ? -5.623  46.273  -4.775  1.00 55.81  ? 595 SER B C   1 
ATOM   9954  O O   . SER B 1 595 ? -6.506  47.121  -4.943  1.00 59.17  ? 595 SER B O   1 
ATOM   9955  C CB  . SER B 1 595 ? -4.498  47.065  -6.912  1.00 59.64  ? 595 SER B CB  1 
ATOM   9956  O OG  . SER B 1 595 ? -5.361  46.329  -7.760  1.00 64.79  ? 595 SER B OG  1 
ATOM   9957  N N   . ILE B 1 596 ? -5.746  45.255  -3.924  1.00 48.96  ? 596 ILE B N   1 
ATOM   9958  C CA  . ILE B 1 596 ? -6.878  45.140  -3.003  1.00 47.71  ? 596 ILE B CA  1 
ATOM   9959  C C   . ILE B 1 596 ? -6.449  44.567  -1.627  1.00 48.52  ? 596 ILE B C   1 
ATOM   9960  O O   . ILE B 1 596 ? -7.094  44.813  -0.592  1.00 45.91  ? 596 ILE B O   1 
ATOM   9961  C CB  . ILE B 1 596 ? -8.042  44.301  -3.602  1.00 44.67  ? 596 ILE B CB  1 
ATOM   9962  C CG1 . ILE B 1 596 ? -7.570  42.899  -4.007  1.00 40.59  ? 596 ILE B CG1 1 
ATOM   9963  C CG2 . ILE B 1 596 ? -8.674  45.018  -4.790  1.00 45.35  ? 596 ILE B CG2 1 
ATOM   9964  C CD1 . ILE B 1 596 ? -8.622  41.826  -3.816  1.00 38.76  ? 596 ILE B CD1 1 
HETATM 9965  C C5  . 55C C 2 .   ? 23.393  7.687   -27.103 1.00 45.67  ? 601 55C A C5  1 
HETATM 9966  C C3  . 55C C 2 .   ? 23.279  8.880   -25.002 1.00 42.96  ? 601 55C A C3  1 
HETATM 9967  C C2  . 55C C 2 .   ? 22.702  9.961   -25.669 1.00 46.11  ? 601 55C A C2  1 
HETATM 9968  C C4  . 55C C 2 .   ? 23.626  7.742   -25.724 1.00 47.79  ? 601 55C A C4  1 
HETATM 9969  N N1  . 55C C 2 .   ? 24.648  6.148   -34.078 1.00 51.71  ? 601 55C A N1  1 
HETATM 9970  O O21 . 55C C 2 .   ? 22.640  7.167   -34.299 1.00 50.41  ? 601 55C A O21 1 
HETATM 9971  C C13 . 55C C 2 .   ? 23.584  6.802   -33.616 1.00 52.65  ? 601 55C A C13 1 
HETATM 9972  C C15 . 55C C 2 .   ? 24.877  5.733   -35.395 1.00 56.66  ? 601 55C A C15 1 
HETATM 9973  C C17 . 55C C 2 .   ? 23.910  5.877   -36.393 1.00 51.36  ? 601 55C A C17 1 
HETATM 9974  C C16 . 55C C 2 .   ? 24.174  5.416   -37.677 1.00 51.23  ? 601 55C A C16 1 
HETATM 9975  C C20 . 55C C 2 .   ? 25.378  4.785   -37.968 1.00 52.22  ? 601 55C A C20 1 
HETATM 9976  C C19 . 55C C 2 .   ? 26.337  4.627   -36.974 1.00 55.05  ? 601 55C A C19 1 
HETATM 9977  C C18 . 55C C 2 .   ? 26.087  5.093   -35.682 1.00 57.44  ? 601 55C A C18 1 
HETATM 9978  C C21 . 55C C 2 .   ? 27.124  4.899   -34.604 1.00 60.92  ? 601 55C A C21 1 
HETATM 9979  O O22 . 55C C 2 .   ? 28.000  4.019   -34.757 1.00 67.00  ? 601 55C A O22 1 
HETATM 9980  O O23 . 55C C 2 .   ? 27.099  5.614   -33.578 1.00 63.88  ? 601 55C A O23 1 
HETATM 9981  C C12 . 55C C 2 .   ? 23.650  7.014   -32.145 1.00 50.33  ? 601 55C A C12 1 
HETATM 9982  C C11 . 55C C 2 .   ? 22.672  7.487   -31.350 1.00 48.91  ? 601 55C A C11 1 
HETATM 9983  C C14 . 55C C 2 .   ? 21.334  7.915   -31.903 1.00 48.34  ? 601 55C A C14 1 
HETATM 9984  C C10 . 55C C 2 .   ? 22.932  7.578   -29.866 1.00 48.23  ? 601 55C A C10 1 
HETATM 9985  C C9  . 55C C 2 .   ? 23.507  6.483   -29.196 1.00 48.28  ? 601 55C A C9  1 
HETATM 9986  C C8  . 55C C 2 .   ? 23.744  6.540   -27.823 1.00 48.28  ? 601 55C A C8  1 
HETATM 9987  C C6  . 55C C 2 .   ? 22.809  8.776   -27.764 1.00 45.97  ? 601 55C A C6  1 
HETATM 9988  C C7  . 55C C 2 .   ? 22.582  8.722   -29.146 1.00 45.44  ? 601 55C A C7  1 
HETATM 9989  C C1  . 55C C 2 .   ? 22.464  9.920   -27.045 1.00 43.13  ? 601 55C A C1  1 
HETATM 9990  C C5  . 55C D 2 .   ? 20.096  33.346  -20.109 1.00 46.51  ? 601 55C B C5  1 
HETATM 9991  C C3  . 55C D 2 .   ? 21.748  32.211  -21.464 1.00 44.76  ? 601 55C B C3  1 
HETATM 9992  C C2  . 55C D 2 .   ? 20.879  31.135  -21.618 1.00 45.99  ? 601 55C B C2  1 
HETATM 9993  C C4  . 55C D 2 .   ? 21.361  33.314  -20.704 1.00 46.25  ? 601 55C B C4  1 
HETATM 9994  N N1  . 55C D 2 .   ? 15.034  34.663  -15.131 1.00 50.36  ? 601 55C B N1  1 
HETATM 9995  O O21 . 55C D 2 .   ? 13.735  33.491  -16.597 1.00 49.82  ? 601 55C B O21 1 
HETATM 9996  C C13 . 55C D 2 .   ? 14.809  33.970  -16.245 1.00 53.61  ? 601 55C B C13 1 
HETATM 9997  C C15 . 55C D 2 .   ? 14.146  35.061  -14.129 1.00 55.30  ? 601 55C B C15 1 
HETATM 9998  C C17 . 55C D 2 .   ? 12.762  35.011  -14.299 1.00 50.60  ? 601 55C B C17 1 
HETATM 9999  C C16 . 55C D 2 .   ? 11.938  35.468  -13.281 1.00 49.16  ? 601 55C B C16 1 
HETATM 10000 C C20 . 55C D 2 .   ? 12.481  35.997  -12.111 1.00 49.56  ? 601 55C B C20 1 
HETATM 10001 C C19 . 55C D 2 .   ? 13.857  36.065  -11.950 1.00 52.50  ? 601 55C B C19 1 
HETATM 10002 C C18 . 55C D 2 .   ? 14.695  35.611  -12.967 1.00 55.98  ? 601 55C B C18 1 
HETATM 10003 C C21 . 55C D 2 .   ? 16.194  35.689  -12.802 1.00 60.21  ? 601 55C B C21 1 
HETATM 10004 O O22 . 55C D 2 .   ? 16.937  35.090  -13.619 1.00 58.43  ? 601 55C B O22 1 
HETATM 10005 O O23 . 55C D 2 .   ? 16.672  36.346  -11.848 1.00 63.04  ? 601 55C B O23 1 
HETATM 10006 C C12 . 55C D 2 .   ? 16.060  33.852  -17.039 1.00 52.46  ? 601 55C B C12 1 
HETATM 10007 C C11 . 55C D 2 .   ? 16.185  33.380  -18.289 1.00 52.51  ? 601 55C B C11 1 
HETATM 10008 C C14 . 55C D 2 .   ? 15.001  32.835  -19.050 1.00 52.24  ? 601 55C B C14 1 
HETATM 10009 C C10 . 55C D 2 .   ? 17.560  33.379  -18.921 1.00 49.69  ? 601 55C B C10 1 
HETATM 10010 C C9  . 55C D 2 .   ? 18.426  34.475  -18.759 1.00 49.95  ? 601 55C B C9  1 
HETATM 10011 C C8  . 55C D 2 .   ? 19.696  34.456  -19.346 1.00 48.98  ? 601 55C B C8  1 
HETATM 10012 C C6  . 55C D 2 .   ? 19.228  32.263  -20.276 1.00 46.34  ? 601 55C B C6  1 
HETATM 10013 C C7  . 55C D 2 .   ? 17.970  32.282  -19.679 1.00 47.87  ? 601 55C B C7  1 
HETATM 10014 C C1  . 55C D 2 .   ? 19.617  31.156  -21.027 1.00 44.93  ? 601 55C B C1  1 
HETATM 10015 O O   . HOH E 3 .   ? 20.948  13.940  -61.869 1.00 44.50  ? 701 HOH A O   1 
HETATM 10016 O O   . HOH E 3 .   ? -3.632  -6.009  -30.429 1.00 38.75  ? 702 HOH A O   1 
HETATM 10017 O O   . HOH E 3 .   ? 25.202  16.459  -69.877 1.00 37.74  ? 703 HOH A O   1 
HETATM 10018 O O   . HOH E 3 .   ? 29.024  18.936  -63.133 1.00 41.39  ? 704 HOH A O   1 
HETATM 10019 O O   . HOH E 3 .   ? 10.168  9.553   -17.435 1.00 30.77  ? 705 HOH A O   1 
HETATM 10020 O O   . HOH E 3 .   ? 19.031  -2.391  -55.091 1.00 54.90  ? 706 HOH A O   1 
HETATM 10021 O O   . HOH E 3 .   ? -7.537  4.293   -67.407 1.00 60.65  ? 707 HOH A O   1 
HETATM 10022 O O   . HOH E 3 .   ? 13.542  -1.639  -50.962 1.00 47.49  ? 708 HOH A O   1 
HETATM 10023 O O   . HOH E 3 .   ? 27.273  17.813  -39.940 1.00 52.60  ? 709 HOH A O   1 
HETATM 10024 O O   . HOH E 3 .   ? 13.672  1.312   -16.379 1.00 39.26  ? 710 HOH A O   1 
HETATM 10025 O O   . HOH E 3 .   ? 12.568  -8.344  -35.241 1.00 43.31  ? 711 HOH A O   1 
HETATM 10026 O O   . HOH E 3 .   ? -9.202  10.799  -15.524 1.00 41.58  ? 712 HOH A O   1 
HETATM 10027 O O   . HOH E 3 .   ? 3.853   -12.265 -29.616 1.00 47.84  ? 713 HOH A O   1 
HETATM 10028 O O   . HOH E 3 .   ? 37.125  5.981   -80.022 1.00 48.72  ? 714 HOH A O   1 
HETATM 10029 O O   . HOH E 3 .   ? 13.056  7.624   -45.079 1.00 32.01  ? 715 HOH A O   1 
HETATM 10030 O O   . HOH E 3 .   ? -35.897 -7.069  -41.100 1.00 57.66  ? 716 HOH A O   1 
HETATM 10031 O O   . HOH E 3 .   ? 1.349   -2.874  -15.213 1.00 39.30  ? 717 HOH A O   1 
HETATM 10032 O O   . HOH E 3 .   ? 19.445  18.713  -28.495 1.00 34.54  ? 718 HOH A O   1 
HETATM 10033 O O   . HOH E 3 .   ? -14.459 -8.260  -52.684 1.00 49.83  ? 719 HOH A O   1 
HETATM 10034 O O   . HOH E 3 .   ? 27.844  16.396  -45.834 1.00 41.78  ? 720 HOH A O   1 
HETATM 10035 O O   . HOH E 3 .   ? 8.373   21.790  -45.402 1.00 48.90  ? 721 HOH A O   1 
HETATM 10036 O O   . HOH E 3 .   ? 14.295  -4.491  -22.593 1.00 46.92  ? 722 HOH A O   1 
HETATM 10037 O O   . HOH E 3 .   ? -7.772  -10.038 -23.232 1.00 53.07  ? 723 HOH A O   1 
HETATM 10038 O O   . HOH E 3 .   ? 7.038   -7.328  -39.868 1.00 40.34  ? 724 HOH A O   1 
HETATM 10039 O O   . HOH E 3 .   ? -28.952 -5.869  -31.492 1.00 61.33  ? 725 HOH A O   1 
HETATM 10040 O O   . HOH E 3 .   ? 11.327  10.067  -49.465 1.00 37.11  ? 726 HOH A O   1 
HETATM 10041 O O   . HOH E 3 .   ? 30.745  10.674  -52.109 1.00 44.45  ? 727 HOH A O   1 
HETATM 10042 O O   . HOH E 3 .   ? 35.343  3.708   -60.534 1.00 24.00  ? 728 HOH A O   1 
HETATM 10043 O O   . HOH E 3 .   ? 14.967  5.912   -48.660 1.00 34.57  ? 729 HOH A O   1 
HETATM 10044 O O   . HOH E 3 .   ? 15.427  25.347  -49.184 1.00 32.09  ? 730 HOH A O   1 
HETATM 10045 O O   . HOH E 3 .   ? 29.158  6.713   -81.333 1.00 38.11  ? 731 HOH A O   1 
HETATM 10046 O O   . HOH E 3 .   ? 3.786   2.929   -41.772 1.00 44.77  ? 732 HOH A O   1 
HETATM 10047 O O   . HOH E 3 .   ? 13.448  2.609   -39.358 1.00 31.74  ? 733 HOH A O   1 
HETATM 10048 O O   . HOH E 3 .   ? 23.459  13.222  -24.498 1.00 44.71  ? 734 HOH A O   1 
HETATM 10049 O O   . HOH E 3 .   ? -11.056 8.640   -25.110 1.00 35.05  ? 735 HOH A O   1 
HETATM 10050 O O   . HOH E 3 .   ? 24.765  -3.971  -72.490 1.00 38.66  ? 736 HOH A O   1 
HETATM 10051 O O   . HOH E 3 .   ? 32.163  3.857   -78.808 1.00 28.96  ? 737 HOH A O   1 
HETATM 10052 O O   . HOH E 3 .   ? 9.020   -2.207  -25.643 1.00 32.10  ? 738 HOH A O   1 
HETATM 10053 O O   . HOH E 3 .   ? 30.223  18.760  -70.970 1.00 40.10  ? 739 HOH A O   1 
HETATM 10054 O O   . HOH E 3 .   ? -12.440 0.535   -21.144 1.00 34.20  ? 740 HOH A O   1 
HETATM 10055 O O   . HOH E 3 .   ? -2.250  3.336   -34.649 1.00 37.53  ? 741 HOH A O   1 
HETATM 10056 O O   . HOH E 3 .   ? 13.101  17.740  -44.414 1.00 34.52  ? 742 HOH A O   1 
HETATM 10057 O O   . HOH E 3 .   ? 14.330  18.995  -46.288 1.00 33.20  ? 743 HOH A O   1 
HETATM 10058 O O   . HOH E 3 .   ? 44.445  19.280  -50.978 1.00 65.32  ? 744 HOH A O   1 
HETATM 10059 O O   . HOH E 3 .   ? -3.521  -0.468  -33.965 1.00 43.14  ? 745 HOH A O   1 
HETATM 10060 O O   . HOH E 3 .   ? 25.230  20.302  -49.192 1.00 36.03  ? 746 HOH A O   1 
HETATM 10061 O O   . HOH E 3 .   ? 11.054  -2.197  -49.960 1.00 41.15  ? 747 HOH A O   1 
HETATM 10062 O O   . HOH E 3 .   ? 25.545  3.845   -49.226 1.00 31.29  ? 748 HOH A O   1 
HETATM 10063 O O   . HOH E 3 .   ? 3.948   5.251   -16.309 1.00 46.97  ? 749 HOH A O   1 
HETATM 10064 O O   . HOH E 3 .   ? 13.856  0.531   -43.977 1.00 30.46  ? 750 HOH A O   1 
HETATM 10065 O O   . HOH E 3 .   ? -2.979  -3.498  -36.941 1.00 49.56  ? 751 HOH A O   1 
HETATM 10066 O O   . HOH E 3 .   ? 34.302  -3.831  -61.452 1.00 35.55  ? 752 HOH A O   1 
HETATM 10067 O O   . HOH E 3 .   ? 14.621  1.513   -54.087 1.00 39.26  ? 753 HOH A O   1 
HETATM 10068 O O   . HOH E 3 .   ? 12.790  -5.455  -30.380 1.00 33.93  ? 754 HOH A O   1 
HETATM 10069 O O   . HOH E 3 .   ? -15.956 -2.644  -24.912 1.00 43.17  ? 755 HOH A O   1 
HETATM 10070 O O   . HOH E 3 .   ? 20.263  6.054   -70.170 1.00 35.95  ? 756 HOH A O   1 
HETATM 10071 O O   . HOH E 3 .   ? -10.984 -4.228  -14.549 1.00 47.23  ? 757 HOH A O   1 
HETATM 10072 O O   . HOH E 3 .   ? 42.556  3.508   -49.734 1.00 45.39  ? 758 HOH A O   1 
HETATM 10073 O O   . HOH E 3 .   ? 29.346  9.113   -49.653 1.00 38.36  ? 759 HOH A O   1 
HETATM 10074 O O   . HOH E 3 .   ? 31.673  12.312  -48.237 1.00 45.39  ? 760 HOH A O   1 
HETATM 10075 O O   . HOH E 3 .   ? 29.201  9.586   -74.471 1.00 37.01  ? 761 HOH A O   1 
HETATM 10076 O O   . HOH E 3 .   ? 13.712  -7.269  -62.974 1.00 55.64  ? 762 HOH A O   1 
HETATM 10077 O O   . HOH E 3 .   ? -15.548 9.282   -43.407 1.00 48.08  ? 763 HOH A O   1 
HETATM 10078 O O   . HOH E 3 .   ? 43.028  16.389  -73.574 1.00 45.20  ? 764 HOH A O   1 
HETATM 10079 O O   . HOH E 3 .   ? -10.805 -6.831  -30.003 1.00 38.88  ? 765 HOH A O   1 
HETATM 10080 O O   . HOH E 3 .   ? 14.036  9.724   -55.928 1.00 24.62  ? 766 HOH A O   1 
HETATM 10081 O O   . HOH E 3 .   ? 11.390  2.349   -15.495 1.00 33.68  ? 767 HOH A O   1 
HETATM 10082 O O   . HOH E 3 .   ? 18.978  -3.583  -22.291 1.00 40.86  ? 768 HOH A O   1 
HETATM 10083 O O   . HOH E 3 .   ? 24.629  10.179  -74.978 1.00 35.57  ? 769 HOH A O   1 
HETATM 10084 O O   . HOH E 3 .   ? -1.381  -2.808  -14.068 1.00 31.27  ? 770 HOH A O   1 
HETATM 10085 O O   . HOH E 3 .   ? -0.133  -6.042  -33.754 1.00 49.88  ? 771 HOH A O   1 
HETATM 10086 O O   . HOH E 3 .   ? 3.514   -6.278  -29.480 1.00 35.24  ? 772 HOH A O   1 
HETATM 10087 O O   . HOH E 3 .   ? 14.812  11.875  -55.570 1.00 23.84  ? 773 HOH A O   1 
HETATM 10088 O O   . HOH E 3 .   ? 23.764  5.189   -21.176 1.00 38.50  ? 774 HOH A O   1 
HETATM 10089 O O   . HOH E 3 .   ? 17.544  9.072   -46.497 1.00 40.14  ? 775 HOH A O   1 
HETATM 10090 O O   . HOH E 3 .   ? 4.010   -4.608  -20.203 1.00 30.35  ? 776 HOH A O   1 
HETATM 10091 O O   . HOH E 3 .   ? 26.699  18.390  -67.157 1.00 51.86  ? 777 HOH A O   1 
HETATM 10092 O O   . HOH E 3 .   ? 6.376   -5.270  -19.704 1.00 37.24  ? 778 HOH A O   1 
HETATM 10093 O O   . HOH E 3 .   ? 19.864  9.824   -48.506 1.00 36.87  ? 779 HOH A O   1 
HETATM 10094 O O   . HOH E 3 .   ? 23.672  -0.441  -77.538 1.00 49.46  ? 780 HOH A O   1 
HETATM 10095 O O   . HOH E 3 .   ? 15.685  -9.657  -62.915 1.00 72.71  ? 781 HOH A O   1 
HETATM 10096 O O   . HOH E 3 .   ? -2.238  4.451   -14.946 1.00 46.74  ? 782 HOH A O   1 
HETATM 10097 O O   . HOH E 3 .   ? 7.964   17.770  -47.892 1.00 48.94  ? 783 HOH A O   1 
HETATM 10098 O O   . HOH E 3 .   ? 29.598  6.965   -34.000 1.00 59.35  ? 784 HOH A O   1 
HETATM 10099 O O   . HOH E 3 .   ? 39.151  1.288   -62.747 1.00 40.03  ? 785 HOH A O   1 
HETATM 10100 O O   . HOH E 3 .   ? -3.432  5.808   -17.432 1.00 33.23  ? 786 HOH A O   1 
HETATM 10101 O O   . HOH E 3 .   ? -9.214  0.472   -66.958 1.00 61.61  ? 787 HOH A O   1 
HETATM 10102 O O   . HOH E 3 .   ? 24.793  21.977  -46.677 1.00 35.82  ? 788 HOH A O   1 
HETATM 10103 O O   . HOH E 3 .   ? 11.093  -4.230  -26.348 1.00 37.10  ? 789 HOH A O   1 
HETATM 10104 O O   . HOH E 3 .   ? 37.189  1.226   -60.260 1.00 27.93  ? 790 HOH A O   1 
HETATM 10105 O O   . HOH E 3 .   ? 31.131  2.634   -82.911 1.00 63.19  ? 791 HOH A O   1 
HETATM 10106 O O   . HOH E 3 .   ? 12.564  12.411  -48.839 1.00 33.98  ? 792 HOH A O   1 
HETATM 10107 O O   . HOH E 3 .   ? 20.325  8.122   -45.505 1.00 34.43  ? 793 HOH A O   1 
HETATM 10108 O O   . HOH E 3 .   ? 13.429  15.265  -42.087 1.00 25.14  ? 794 HOH A O   1 
HETATM 10109 O O   . HOH E 3 .   ? 22.323  6.436   -72.359 1.00 38.76  ? 795 HOH A O   1 
HETATM 10110 O O   . HOH E 3 .   ? -9.850  -0.859  -21.295 1.00 47.35  ? 796 HOH A O   1 
HETATM 10111 O O   . HOH E 3 .   ? 20.859  15.960  -25.503 1.00 43.02  ? 797 HOH A O   1 
HETATM 10112 O O   . HOH E 3 .   ? 17.837  13.488  -19.025 1.00 43.14  ? 798 HOH A O   1 
HETATM 10113 O O   . HOH E 3 .   ? 21.504  0.111   -43.633 1.00 45.64  ? 799 HOH A O   1 
HETATM 10114 O O   . HOH E 3 .   ? 12.976  9.169   -46.873 1.00 40.30  ? 800 HOH A O   1 
HETATM 10115 O O   . HOH E 3 .   ? -5.624  4.849   -40.875 1.00 45.75  ? 801 HOH A O   1 
HETATM 10116 O O   . HOH E 3 .   ? 4.636   -1.795  -16.439 1.00 40.99  ? 802 HOH A O   1 
HETATM 10117 O O   . HOH E 3 .   ? 24.559  -3.064  -57.994 1.00 49.49  ? 803 HOH A O   1 
HETATM 10118 O O   . HOH E 3 .   ? 23.135  13.854  -19.918 1.00 52.16  ? 804 HOH A O   1 
HETATM 10119 O O   . HOH E 3 .   ? 6.002   8.084   -17.163 1.00 31.56  ? 805 HOH A O   1 
HETATM 10120 O O   . HOH E 3 .   ? 14.250  3.458   -67.692 1.00 47.14  ? 806 HOH A O   1 
HETATM 10121 O O   . HOH E 3 .   ? 7.868   -4.798  -51.242 1.00 46.51  ? 807 HOH A O   1 
HETATM 10122 O O   . HOH E 3 .   ? 37.572  0.274   -68.986 1.00 44.87  ? 808 HOH A O   1 
HETATM 10123 O O   . HOH E 3 .   ? 42.025  18.102  -69.049 1.00 41.74  ? 809 HOH A O   1 
HETATM 10124 O O   . HOH E 3 .   ? 1.067   2.009   -48.149 1.00 45.07  ? 810 HOH A O   1 
HETATM 10125 O O   . HOH E 3 .   ? 12.531  16.077  -52.603 1.00 42.47  ? 811 HOH A O   1 
HETATM 10126 O O   . HOH E 3 .   ? 9.616   -3.033  -22.953 1.00 30.38  ? 812 HOH A O   1 
HETATM 10127 O O   . HOH E 3 .   ? 16.928  6.020   -43.616 1.00 28.69  ? 813 HOH A O   1 
HETATM 10128 O O   . HOH E 3 .   ? 27.722  -4.621  -58.442 1.00 57.62  ? 814 HOH A O   1 
HETATM 10129 O O   . HOH E 3 .   ? 22.743  -9.317  -68.774 1.00 47.90  ? 815 HOH A O   1 
HETATM 10130 O O   . HOH E 3 .   ? 20.589  19.100  -57.172 1.00 36.63  ? 816 HOH A O   1 
HETATM 10131 O O   . HOH E 3 .   ? 7.250   10.998  -43.570 1.00 30.90  ? 817 HOH A O   1 
HETATM 10132 O O   . HOH E 3 .   ? -4.317  -1.509  -11.233 1.00 44.84  ? 818 HOH A O   1 
HETATM 10133 O O   . HOH E 3 .   ? 20.210  -5.757  -32.580 1.00 46.80  ? 819 HOH A O   1 
HETATM 10134 O O   . HOH E 3 .   ? 26.534  18.101  -64.093 1.00 41.75  ? 820 HOH A O   1 
HETATM 10135 O O   . HOH E 3 .   ? -1.057  22.207  -24.005 1.00 47.53  ? 821 HOH A O   1 
HETATM 10136 O O   . HOH E 3 .   ? 0.890   -7.720  -35.118 1.00 29.33  ? 822 HOH A O   1 
HETATM 10137 O O   . HOH E 3 .   ? 26.375  -3.089  -80.343 1.00 42.07  ? 823 HOH A O   1 
HETATM 10138 O O   . HOH E 3 .   ? 8.150   7.987   -18.698 1.00 42.88  ? 824 HOH A O   1 
HETATM 10139 O O   . HOH E 3 .   ? -8.631  -7.184  -48.113 1.00 54.60  ? 825 HOH A O   1 
HETATM 10140 O O   . HOH E 3 .   ? -3.254  5.652   -12.482 1.00 58.40  ? 826 HOH A O   1 
HETATM 10141 O O   . HOH E 3 .   ? -3.259  3.485   -17.773 1.00 44.73  ? 827 HOH A O   1 
HETATM 10142 O O   . HOH E 3 .   ? 13.193  7.831   -65.269 1.00 62.26  ? 828 HOH A O   1 
HETATM 10143 O O   . HOH E 3 .   ? 39.408  2.836   -68.535 1.00 44.71  ? 829 HOH A O   1 
HETATM 10144 O O   . HOH E 3 .   ? 16.398  0.464   -45.007 1.00 38.87  ? 830 HOH A O   1 
HETATM 10145 O O   . HOH E 3 .   ? 43.660  15.807  -68.271 1.00 56.20  ? 831 HOH A O   1 
HETATM 10146 O O   . HOH E 3 .   ? 26.765  -2.381  -49.369 1.00 47.91  ? 832 HOH A O   1 
HETATM 10147 O O   . HOH E 3 .   ? 11.901  18.440  -57.213 1.00 45.93  ? 833 HOH A O   1 
HETATM 10148 O O   . HOH E 3 .   ? 10.513  14.906  -42.398 1.00 38.66  ? 834 HOH A O   1 
HETATM 10149 O O   . HOH E 3 .   ? 10.023  13.493  -21.861 1.00 39.55  ? 835 HOH A O   1 
HETATM 10150 O O   . HOH E 3 .   ? 27.305  -4.635  -70.871 1.00 42.07  ? 836 HOH A O   1 
HETATM 10151 O O   . HOH E 3 .   ? -10.356 -11.757 -37.565 1.00 43.17  ? 837 HOH A O   1 
HETATM 10152 O O   . HOH E 3 .   ? -19.644 -0.642  -28.224 1.00 33.20  ? 838 HOH A O   1 
HETATM 10153 O O   . HOH E 3 .   ? 9.860   17.732  -52.227 1.00 37.66  ? 839 HOH A O   1 
HETATM 10154 O O   . HOH E 3 .   ? 3.308   7.996   -42.074 1.00 54.18  ? 840 HOH A O   1 
HETATM 10155 O O   . HOH E 3 .   ? 18.004  -6.671  -36.275 1.00 39.03  ? 841 HOH A O   1 
HETATM 10156 O O   . HOH E 3 .   ? 19.531  8.789   -70.079 1.00 44.09  ? 842 HOH A O   1 
HETATM 10157 O O   . HOH E 3 .   ? 4.444   19.133  -34.830 1.00 44.21  ? 843 HOH A O   1 
HETATM 10158 O O   . HOH E 3 .   ? -3.236  -5.253  -58.411 1.00 59.20  ? 844 HOH A O   1 
HETATM 10159 O O   . HOH E 3 .   ? 25.130  26.561  -43.186 1.00 44.76  ? 845 HOH A O   1 
HETATM 10160 O O   . HOH E 3 .   ? 27.808  -7.078  -64.567 1.00 38.50  ? 846 HOH A O   1 
HETATM 10161 O O   . HOH E 3 .   ? 10.173  1.390   -13.175 1.00 43.65  ? 847 HOH A O   1 
HETATM 10162 O O   . HOH E 3 .   ? 17.263  -6.063  -42.157 1.00 27.45  ? 848 HOH A O   1 
HETATM 10163 O O   . HOH E 3 .   ? 2.306   -9.130  -31.356 1.00 45.36  ? 849 HOH A O   1 
HETATM 10164 O O   . HOH E 3 .   ? 9.988   -8.012  -30.942 1.00 38.47  ? 850 HOH A O   1 
HETATM 10165 O O   . HOH E 3 .   ? 15.340  -0.539  -52.040 1.00 33.56  ? 851 HOH A O   1 
HETATM 10166 O O   . HOH E 3 .   ? 14.181  7.203   -59.870 1.00 45.04  ? 852 HOH A O   1 
HETATM 10167 O O   . HOH E 3 .   ? 2.294   18.571  -29.018 1.00 39.47  ? 853 HOH A O   1 
HETATM 10168 O O   . HOH E 3 .   ? -11.420 10.193  -38.286 1.00 55.53  ? 854 HOH A O   1 
HETATM 10169 O O   . HOH E 3 .   ? -7.631  -4.939  -30.192 1.00 57.66  ? 855 HOH A O   1 
HETATM 10170 O O   . HOH E 3 .   ? 10.852  12.018  -56.887 1.00 37.24  ? 856 HOH A O   1 
HETATM 10171 O O   . HOH E 3 .   ? 5.948   3.452   -64.885 1.00 58.52  ? 857 HOH A O   1 
HETATM 10172 O O   . HOH E 3 .   ? -7.731  -0.552  -46.254 1.00 45.11  ? 858 HOH A O   1 
HETATM 10173 O O   . HOH E 3 .   ? 19.224  4.310   -45.298 1.00 47.53  ? 859 HOH A O   1 
HETATM 10174 O O   . HOH E 3 .   ? -14.332 9.712   -40.079 1.00 56.56  ? 860 HOH A O   1 
HETATM 10175 O O   . HOH E 3 .   ? 12.699  -1.963  -53.210 1.00 36.41  ? 861 HOH A O   1 
HETATM 10176 O O   . HOH E 3 .   ? 25.332  -0.502  -47.703 1.00 54.53  ? 862 HOH A O   1 
HETATM 10177 O O   . HOH E 3 .   ? 27.398  20.780  -37.685 1.00 45.99  ? 863 HOH A O   1 
HETATM 10178 O O   . HOH E 3 .   ? -10.293 -11.608 -56.609 1.00 75.21  ? 864 HOH A O   1 
HETATM 10179 O O   . HOH E 3 .   ? -9.351  13.158  -35.465 1.00 50.82  ? 865 HOH A O   1 
HETATM 10180 O O   . HOH E 3 .   ? 11.783  22.729  -40.553 1.00 30.13  ? 866 HOH A O   1 
HETATM 10181 O O   . HOH E 3 .   ? 14.388  2.606   -42.027 1.00 34.75  ? 867 HOH A O   1 
HETATM 10182 O O   . HOH E 3 .   ? 14.919  -3.205  -56.624 1.00 41.35  ? 868 HOH A O   1 
HETATM 10183 O O   . HOH E 3 .   ? -17.141 4.975   -75.056 1.00 66.61  ? 869 HOH A O   1 
HETATM 10184 O O   . HOH E 3 .   ? 19.800  24.957  -41.712 1.00 30.60  ? 870 HOH A O   1 
HETATM 10185 O O   . HOH E 3 .   ? 21.331  28.173  -45.727 1.00 46.02  ? 871 HOH A O   1 
HETATM 10186 O O   . HOH E 3 .   ? 9.680   -5.630  -21.879 1.00 52.91  ? 872 HOH A O   1 
HETATM 10187 O O   . HOH E 3 .   ? -15.190 0.382   -19.251 1.00 47.08  ? 873 HOH A O   1 
HETATM 10188 O O   . HOH E 3 .   ? 17.806  12.868  -70.356 1.00 51.78  ? 874 HOH A O   1 
HETATM 10189 O O   . HOH E 3 .   ? -19.896 -11.329 -59.590 1.00 60.83  ? 875 HOH A O   1 
HETATM 10190 O O   . HOH E 3 .   ? 6.271   13.331  -16.099 1.00 52.37  ? 876 HOH A O   1 
HETATM 10191 O O   . HOH E 3 .   ? 1.196   4.556   -48.198 1.00 42.28  ? 877 HOH A O   1 
HETATM 10192 O O   . HOH E 3 .   ? 24.069  1.320   -45.855 1.00 48.19  ? 878 HOH A O   1 
HETATM 10193 O O   . HOH E 3 .   ? 13.915  14.635  -60.042 1.00 53.21  ? 879 HOH A O   1 
HETATM 10194 O O   . HOH E 3 .   ? -21.792 11.133  -51.985 1.00 66.48  ? 880 HOH A O   1 
HETATM 10195 O O   . HOH E 3 .   ? 12.565  -2.923  -23.232 1.00 42.49  ? 881 HOH A O   1 
HETATM 10196 O O   . HOH E 3 .   ? -19.972 11.386  -34.091 1.00 59.56  ? 882 HOH A O   1 
HETATM 10197 O O   . HOH E 3 .   ? -5.908  -0.497  -19.486 1.00 27.62  ? 883 HOH A O   1 
HETATM 10198 O O   . HOH E 3 .   ? -19.862 2.442   -21.840 1.00 58.01  ? 884 HOH A O   1 
HETATM 10199 O O   . HOH E 3 .   ? 1.168   5.176   -14.814 1.00 40.04  ? 885 HOH A O   1 
HETATM 10200 O O   . HOH E 3 .   ? 8.461   15.141  -19.965 1.00 33.05  ? 886 HOH A O   1 
HETATM 10201 O O   . HOH E 3 .   ? 4.880   8.973   -53.146 1.00 60.81  ? 887 HOH A O   1 
HETATM 10202 O O   . HOH E 3 .   ? 12.263  1.272   -69.553 1.00 59.98  ? 888 HOH A O   1 
HETATM 10203 O O   . HOH E 3 .   ? 27.963  -3.436  -51.882 1.00 44.90  ? 889 HOH A O   1 
HETATM 10204 O O   . HOH E 3 .   ? -33.575 26.583  -65.818 1.00 70.93  ? 890 HOH A O   1 
HETATM 10205 O O   . HOH E 3 .   ? 40.240  -1.738  -56.633 1.00 63.78  ? 891 HOH A O   1 
HETATM 10206 O O   . HOH E 3 .   ? 6.366   12.989  -44.669 1.00 47.90  ? 892 HOH A O   1 
HETATM 10207 O O   . HOH E 3 .   ? 12.000  7.939   -61.092 1.00 48.36  ? 893 HOH A O   1 
HETATM 10208 O O   . HOH E 3 .   ? -7.736  -4.143  -47.033 1.00 47.93  ? 894 HOH A O   1 
HETATM 10209 O O   . HOH E 3 .   ? 26.308  -5.745  -68.928 1.00 41.74  ? 895 HOH A O   1 
HETATM 10210 O O   . HOH E 3 .   ? 15.555  7.146   -45.952 1.00 34.57  ? 896 HOH A O   1 
HETATM 10211 O O   . HOH E 3 .   ? 29.676  -1.834  -49.233 1.00 38.96  ? 897 HOH A O   1 
HETATM 10212 O O   . HOH E 3 .   ? 8.944   18.708  -29.910 1.00 34.94  ? 898 HOH A O   1 
HETATM 10213 O O   . HOH E 3 .   ? -0.029  -9.387  -30.434 1.00 45.87  ? 899 HOH A O   1 
HETATM 10214 O O   . HOH E 3 .   ? 13.203  5.468   -66.518 1.00 43.95  ? 900 HOH A O   1 
HETATM 10215 O O   . HOH E 3 .   ? 40.215  20.699  -64.077 1.00 51.68  ? 901 HOH A O   1 
HETATM 10216 O O   . HOH E 3 .   ? 13.190  13.914  -56.583 1.00 41.21  ? 902 HOH A O   1 
HETATM 10217 O O   . HOH E 3 .   ? -3.176  -6.050  -27.819 1.00 59.51  ? 903 HOH A O   1 
HETATM 10218 O O   . HOH E 3 .   ? 0.425   -12.329 -20.585 1.00 50.98  ? 904 HOH A O   1 
HETATM 10219 O O   . HOH E 3 .   ? 16.651  3.329   -42.727 1.00 30.48  ? 905 HOH A O   1 
HETATM 10220 O O   . HOH E 3 .   ? 24.189  2.236   -77.765 1.00 46.05  ? 906 HOH A O   1 
HETATM 10221 O O   . HOH E 3 .   ? -5.444  22.581  -26.425 1.00 55.79  ? 907 HOH A O   1 
HETATM 10222 O O   . HOH E 3 .   ? 17.815  20.324  -27.519 1.00 38.40  ? 908 HOH A O   1 
HETATM 10223 O O   . HOH E 3 .   ? 12.238  16.218  -55.352 1.00 48.06  ? 909 HOH A O   1 
HETATM 10224 O O   . HOH E 3 .   ? 23.357  19.645  -58.368 1.00 36.71  ? 910 HOH A O   1 
HETATM 10225 O O   . HOH F 3 .   ? -9.014  26.435  -1.168  1.00 35.53  ? 701 HOH B O   1 
HETATM 10226 O O   . HOH F 3 .   ? 9.319   30.524  -53.219 1.00 42.84  ? 702 HOH B O   1 
HETATM 10227 O O   . HOH F 3 .   ? -15.150 44.782  8.663   1.00 31.00  ? 703 HOH B O   1 
HETATM 10228 O O   . HOH F 3 .   ? -5.051  21.701  6.148   1.00 42.97  ? 704 HOH B O   1 
HETATM 10229 O O   . HOH F 3 .   ? -3.295  45.543  -13.166 1.00 46.96  ? 705 HOH B O   1 
HETATM 10230 O O   . HOH F 3 .   ? 0.013   23.090  -17.751 1.00 36.63  ? 706 HOH B O   1 
HETATM 10231 O O   . HOH F 3 .   ? -7.756  52.147  4.665   1.00 55.39  ? 707 HOH B O   1 
HETATM 10232 O O   . HOH F 3 .   ? -11.577 47.618  -0.299  1.00 43.59  ? 708 HOH B O   1 
HETATM 10233 O O   . HOH F 3 .   ? 0.629   31.953  -48.933 1.00 27.10  ? 709 HOH B O   1 
HETATM 10234 O O   . HOH F 3 .   ? 11.291  35.233  -47.724 1.00 31.26  ? 710 HOH B O   1 
HETATM 10235 O O   . HOH F 3 .   ? 7.734   24.409  -5.323  1.00 36.65  ? 711 HOH B O   1 
HETATM 10236 O O   . HOH F 3 .   ? -15.419 37.064  18.317  1.00 34.16  ? 712 HOH B O   1 
HETATM 10237 O O   . HOH F 3 .   ? 16.628  35.632  -42.256 1.00 45.96  ? 713 HOH B O   1 
HETATM 10238 O O   . HOH F 3 .   ? 19.709  31.677  -36.693 1.00 31.09  ? 714 HOH B O   1 
HETATM 10239 O O   . HOH F 3 .   ? 2.080   17.832  -21.293 1.00 33.75  ? 715 HOH B O   1 
HETATM 10240 O O   . HOH F 3 .   ? 0.071   44.759  -44.549 1.00 44.93  ? 716 HOH B O   1 
HETATM 10241 O O   . HOH F 3 .   ? 22.521  39.470  -34.560 1.00 29.01  ? 717 HOH B O   1 
HETATM 10242 O O   . HOH F 3 .   ? 20.196  44.362  -26.489 1.00 42.93  ? 718 HOH B O   1 
HETATM 10243 O O   . HOH F 3 .   ? 13.426  19.707  -29.186 1.00 37.50  ? 719 HOH B O   1 
HETATM 10244 O O   . HOH F 3 .   ? 18.850  28.191  -31.890 1.00 32.36  ? 720 HOH B O   1 
HETATM 10245 O O   . HOH F 3 .   ? 0.647   14.833  -15.408 1.00 29.79  ? 721 HOH B O   1 
HETATM 10246 O O   . HOH F 3 .   ? -10.127 30.360  -41.342 1.00 62.04  ? 722 HOH B O   1 
HETATM 10247 O O   . HOH F 3 .   ? 16.996  24.569  -10.637 1.00 46.18  ? 723 HOH B O   1 
HETATM 10248 O O   . HOH F 3 .   ? -0.661  33.214  -17.428 1.00 32.11  ? 724 HOH B O   1 
HETATM 10249 O O   . HOH F 3 .   ? 10.987  46.070  -26.982 1.00 31.30  ? 725 HOH B O   1 
HETATM 10250 O O   . HOH F 3 .   ? -9.953  50.423  -53.858 1.00 54.80  ? 726 HOH B O   1 
HETATM 10251 O O   . HOH F 3 .   ? -14.028 31.061  13.366  1.00 37.64  ? 727 HOH B O   1 
HETATM 10252 O O   . HOH F 3 .   ? -12.131 44.981  10.027  1.00 40.12  ? 728 HOH B O   1 
HETATM 10253 O O   . HOH F 3 .   ? -1.721  40.384  -37.209 1.00 58.32  ? 729 HOH B O   1 
HETATM 10254 O O   . HOH F 3 .   ? -12.305 35.996  -17.411 1.00 45.94  ? 730 HOH B O   1 
HETATM 10255 O O   . HOH F 3 .   ? -6.995  39.173  -10.507 1.00 39.40  ? 731 HOH B O   1 
HETATM 10256 O O   . HOH F 3 .   ? 15.254  46.119  -38.289 1.00 49.04  ? 732 HOH B O   1 
HETATM 10257 O O   . HOH F 3 .   ? -0.678  21.610  -15.737 1.00 31.91  ? 733 HOH B O   1 
HETATM 10258 O O   . HOH F 3 .   ? 4.339   30.568  -6.413  1.00 34.44  ? 734 HOH B O   1 
HETATM 10259 O O   . HOH F 3 .   ? 18.672  36.761  -15.103 1.00 44.66  ? 735 HOH B O   1 
HETATM 10260 O O   . HOH F 3 .   ? -16.872 40.374  -34.790 1.00 54.37  ? 736 HOH B O   1 
HETATM 10261 O O   . HOH F 3 .   ? -10.704 22.107  11.785  1.00 48.37  ? 737 HOH B O   1 
HETATM 10262 O O   . HOH F 3 .   ? 0.927   37.123  9.493   1.00 32.64  ? 738 HOH B O   1 
HETATM 10263 O O   . HOH F 3 .   ? 15.313  42.395  -51.926 1.00 39.23  ? 739 HOH B O   1 
HETATM 10264 O O   . HOH F 3 .   ? -12.566 54.098  -48.185 1.00 50.81  ? 740 HOH B O   1 
HETATM 10265 O O   . HOH F 3 .   ? 4.545   38.154  -20.405 1.00 27.89  ? 741 HOH B O   1 
HETATM 10266 O O   . HOH F 3 .   ? 13.170  27.831  -46.838 1.00 34.65  ? 742 HOH B O   1 
HETATM 10267 O O   . HOH F 3 .   ? 5.257   46.486  -54.319 1.00 46.71  ? 743 HOH B O   1 
HETATM 10268 O O   . HOH F 3 .   ? 0.928   31.441  -13.206 1.00 34.52  ? 744 HOH B O   1 
HETATM 10269 O O   . HOH F 3 .   ? 12.200  43.028  -32.579 1.00 23.50  ? 745 HOH B O   1 
HETATM 10270 O O   . HOH F 3 .   ? 9.748   47.967  -28.697 1.00 37.84  ? 746 HOH B O   1 
HETATM 10271 O O   . HOH F 3 .   ? 22.145  27.728  -21.663 1.00 43.79  ? 747 HOH B O   1 
HETATM 10272 O O   . HOH F 3 .   ? -3.676  19.073  -21.216 1.00 54.31  ? 748 HOH B O   1 
HETATM 10273 O O   . HOH F 3 .   ? -1.367  37.632  -36.258 1.00 36.07  ? 749 HOH B O   1 
HETATM 10274 O O   . HOH F 3 .   ? -6.820  23.321  -4.981  1.00 32.31  ? 750 HOH B O   1 
HETATM 10275 O O   . HOH F 3 .   ? -0.252  47.916  -25.495 1.00 40.52  ? 751 HOH B O   1 
HETATM 10276 O O   . HOH F 3 .   ? 5.702   38.721  0.667   1.00 32.74  ? 752 HOH B O   1 
HETATM 10277 O O   . HOH F 3 .   ? -19.716 41.366  10.464  1.00 50.92  ? 753 HOH B O   1 
HETATM 10278 O O   . HOH F 3 .   ? 5.290   40.365  -11.601 1.00 49.37  ? 754 HOH B O   1 
HETATM 10279 O O   . HOH F 3 .   ? -1.654  50.476  -20.993 1.00 49.26  ? 755 HOH B O   1 
HETATM 10280 O O   . HOH F 3 .   ? 21.605  38.682  -36.798 1.00 34.52  ? 756 HOH B O   1 
HETATM 10281 O O   . HOH F 3 .   ? -0.303  44.369  9.213   1.00 46.32  ? 757 HOH B O   1 
HETATM 10282 O O   . HOH F 3 .   ? -7.038  18.329  -19.761 1.00 44.15  ? 758 HOH B O   1 
HETATM 10283 O O   . HOH F 3 .   ? 3.631   20.429  -5.206  1.00 29.33  ? 759 HOH B O   1 
HETATM 10284 O O   . HOH F 3 .   ? -16.341 35.291  3.356   1.00 42.25  ? 760 HOH B O   1 
HETATM 10285 O O   . HOH F 3 .   ? -1.660  13.499  -16.398 1.00 34.68  ? 761 HOH B O   1 
HETATM 10286 O O   . HOH F 3 .   ? -20.143 43.977  14.709  1.00 51.23  ? 762 HOH B O   1 
HETATM 10287 O O   . HOH F 3 .   ? 0.877   40.335  -17.516 1.00 26.86  ? 763 HOH B O   1 
HETATM 10288 O O   . HOH F 3 .   ? 2.785   40.317  -52.247 1.00 44.40  ? 764 HOH B O   1 
HETATM 10289 O O   . HOH F 3 .   ? -14.004 30.886  6.852   1.00 39.16  ? 765 HOH B O   1 
HETATM 10290 O O   . HOH F 3 .   ? -7.696  28.826  -9.598  1.00 28.03  ? 766 HOH B O   1 
HETATM 10291 O O   . HOH F 3 .   ? 0.764   30.998  -9.941  1.00 41.95  ? 767 HOH B O   1 
HETATM 10292 O O   . HOH F 3 .   ? 4.722   30.174  0.719   1.00 40.86  ? 768 HOH B O   1 
HETATM 10293 O O   . HOH F 3 .   ? -10.677 22.620  -10.552 1.00 44.72  ? 769 HOH B O   1 
HETATM 10294 O O   . HOH F 3 .   ? 17.213  32.516  -40.078 1.00 38.05  ? 770 HOH B O   1 
HETATM 10295 O O   . HOH F 3 .   ? 16.518  25.731  -36.665 1.00 24.97  ? 771 HOH B O   1 
HETATM 10296 O O   . HOH F 3 .   ? 2.047   39.469  11.043  1.00 34.44  ? 772 HOH B O   1 
HETATM 10297 O O   . HOH F 3 .   ? -16.806 47.620  -33.042 1.00 60.43  ? 773 HOH B O   1 
HETATM 10298 O O   . HOH F 3 .   ? -11.305 33.466  -7.612  1.00 35.49  ? 774 HOH B O   1 
HETATM 10299 O O   . HOH F 3 .   ? 26.713  33.917  -27.083 1.00 42.94  ? 775 HOH B O   1 
HETATM 10300 O O   . HOH F 3 .   ? 2.034   32.136  -56.709 1.00 48.49  ? 776 HOH B O   1 
HETATM 10301 O O   . HOH F 3 .   ? 20.411  37.571  -18.138 1.00 48.03  ? 777 HOH B O   1 
HETATM 10302 O O   . HOH F 3 .   ? 22.696  39.156  -39.301 1.00 38.16  ? 778 HOH B O   1 
HETATM 10303 O O   . HOH F 3 .   ? -1.929  34.661  -13.803 1.00 37.27  ? 779 HOH B O   1 
HETATM 10304 O O   . HOH F 3 .   ? -5.530  42.906  -16.468 1.00 41.30  ? 780 HOH B O   1 
HETATM 10305 O O   . HOH F 3 .   ? 6.038   52.907  -33.817 1.00 38.02  ? 781 HOH B O   1 
HETATM 10306 O O   . HOH F 3 .   ? -10.733 30.489  18.016  1.00 36.88  ? 782 HOH B O   1 
HETATM 10307 O O   . HOH F 3 .   ? 16.032  43.962  -45.060 1.00 31.60  ? 783 HOH B O   1 
HETATM 10308 O O   . HOH F 3 .   ? 16.596  21.965  -22.609 1.00 43.37  ? 784 HOH B O   1 
HETATM 10309 O O   . HOH F 3 .   ? 3.619   37.074  -5.092  1.00 38.54  ? 785 HOH B O   1 
HETATM 10310 O O   . HOH F 3 .   ? -11.334 48.198  -52.640 1.00 44.72  ? 786 HOH B O   1 
HETATM 10311 O O   . HOH F 3 .   ? 12.411  22.882  -10.076 1.00 54.61  ? 787 HOH B O   1 
HETATM 10312 O O   . HOH F 3 .   ? -33.982 37.149  -47.894 1.00 69.59  ? 788 HOH B O   1 
HETATM 10313 O O   . HOH F 3 .   ? -8.434  30.916  -10.312 1.00 27.14  ? 789 HOH B O   1 
HETATM 10314 O O   . HOH F 3 .   ? -5.018  42.744  -13.872 1.00 48.45  ? 790 HOH B O   1 
HETATM 10315 O O   . HOH F 3 .   ? 2.038   25.296  -19.169 1.00 33.78  ? 791 HOH B O   1 
HETATM 10316 O O   . HOH F 3 .   ? -13.156 29.729  21.282  1.00 61.98  ? 792 HOH B O   1 
HETATM 10317 O O   . HOH F 3 .   ? 8.215   24.273  -28.695 1.00 41.57  ? 793 HOH B O   1 
HETATM 10318 O O   . HOH F 3 .   ? -16.499 32.440  2.617   1.00 34.30  ? 794 HOH B O   1 
HETATM 10319 O O   . HOH F 3 .   ? -4.778  30.499  -16.225 1.00 31.81  ? 795 HOH B O   1 
HETATM 10320 O O   . HOH F 3 .   ? 4.536   41.513  -50.181 1.00 41.49  ? 796 HOH B O   1 
HETATM 10321 O O   . HOH F 3 .   ? -0.350  26.259  -21.716 1.00 36.14  ? 797 HOH B O   1 
HETATM 10322 O O   . HOH F 3 .   ? -16.716 34.504  6.355   1.00 43.86  ? 798 HOH B O   1 
HETATM 10323 O O   . HOH F 3 .   ? -9.247  44.830  -18.394 1.00 58.37  ? 799 HOH B O   1 
HETATM 10324 O O   . HOH F 3 .   ? 14.201  32.940  8.556   1.00 43.88  ? 800 HOH B O   1 
HETATM 10325 O O   . HOH F 3 .   ? 2.991   34.484  -14.993 1.00 25.61  ? 801 HOH B O   1 
HETATM 10326 O O   . HOH F 3 .   ? 8.792   45.292  -55.311 1.00 45.17  ? 802 HOH B O   1 
HETATM 10327 O O   . HOH F 3 .   ? -3.829  28.258  -15.329 1.00 31.11  ? 803 HOH B O   1 
HETATM 10328 O O   . HOH F 3 .   ? -3.031  29.377  20.654  1.00 46.82  ? 804 HOH B O   1 
HETATM 10329 O O   . HOH F 3 .   ? -16.187 30.296  3.621   1.00 42.10  ? 805 HOH B O   1 
HETATM 10330 O O   . HOH F 3 .   ? 22.957  27.215  -29.644 1.00 39.46  ? 806 HOH B O   1 
HETATM 10331 O O   . HOH F 3 .   ? -6.321  29.675  -50.641 1.00 56.60  ? 807 HOH B O   1 
HETATM 10332 O O   . HOH F 3 .   ? -13.914 33.795  20.618  1.00 54.01  ? 808 HOH B O   1 
HETATM 10333 O O   . HOH F 3 .   ? -6.262  51.929  -45.814 1.00 44.78  ? 809 HOH B O   1 
HETATM 10334 O O   . HOH F 3 .   ? -3.347  47.744  -45.637 1.00 36.95  ? 810 HOH B O   1 
HETATM 10335 O O   . HOH F 3 .   ? -1.459  45.839  -42.677 1.00 41.21  ? 811 HOH B O   1 
HETATM 10336 O O   . HOH F 3 .   ? 25.569  33.022  -24.846 1.00 49.83  ? 812 HOH B O   1 
HETATM 10337 O O   . HOH F 3 .   ? 6.199   50.817  -37.937 1.00 48.80  ? 813 HOH B O   1 
HETATM 10338 O O   . HOH F 3 .   ? 5.891   47.394  -34.874 1.00 28.78  ? 814 HOH B O   1 
HETATM 10339 O O   . HOH F 3 .   ? -20.000 37.992  19.349  1.00 53.59  ? 815 HOH B O   1 
HETATM 10340 O O   . HOH F 3 .   ? 19.476  24.692  -23.275 1.00 36.77  ? 816 HOH B O   1 
HETATM 10341 O O   . HOH F 3 .   ? -3.929  14.958  -8.358  1.00 53.04  ? 817 HOH B O   1 
HETATM 10342 O O   . HOH F 3 .   ? -5.518  21.377  -4.280  1.00 38.06  ? 818 HOH B O   1 
HETATM 10343 O O   . HOH F 3 .   ? -4.583  33.823  -56.245 1.00 44.57  ? 819 HOH B O   1 
HETATM 10344 O O   . HOH F 3 .   ? -18.155 35.814  1.433   1.00 53.37  ? 820 HOH B O   1 
HETATM 10345 O O   . HOH F 3 .   ? 19.299  24.700  -16.512 1.00 62.64  ? 821 HOH B O   1 
HETATM 10346 O O   . HOH F 3 .   ? -6.343  37.814  -30.653 1.00 55.01  ? 822 HOH B O   1 
HETATM 10347 O O   . HOH F 3 .   ? 10.484  20.995  2.651   1.00 47.98  ? 823 HOH B O   1 
HETATM 10348 O O   . HOH F 3 .   ? -7.433  32.797  -23.828 1.00 52.77  ? 824 HOH B O   1 
HETATM 10349 O O   . HOH F 3 .   ? -2.156  31.258  -16.234 1.00 42.81  ? 825 HOH B O   1 
HETATM 10350 O O   . HOH F 3 .   ? -16.215 33.776  20.391  1.00 52.59  ? 826 HOH B O   1 
HETATM 10351 O O   . HOH F 3 .   ? 18.097  27.241  -40.628 1.00 40.42  ? 827 HOH B O   1 
HETATM 10352 O O   . HOH F 3 .   ? -23.819 35.149  -21.191 1.00 79.02  ? 828 HOH B O   1 
HETATM 10353 O O   . HOH F 3 .   ? -3.037  38.255  17.569  1.00 36.94  ? 829 HOH B O   1 
HETATM 10354 O O   . HOH F 3 .   ? 4.375   42.653  -4.293  1.00 49.38  ? 830 HOH B O   1 
HETATM 10355 O O   . HOH F 3 .   ? -7.142  41.245  -53.830 1.00 28.94  ? 831 HOH B O   1 
HETATM 10356 O O   . HOH F 3 .   ? 12.763  20.474  9.327   1.00 57.94  ? 832 HOH B O   1 
HETATM 10357 O O   . HOH F 3 .   ? 13.617  46.699  -19.329 1.00 57.11  ? 833 HOH B O   1 
HETATM 10358 O O   . HOH F 3 .   ? 17.013  32.776  -37.588 1.00 41.27  ? 834 HOH B O   1 
HETATM 10359 O O   . HOH F 3 .   ? 2.823   35.938  -12.474 1.00 35.36  ? 835 HOH B O   1 
HETATM 10360 O O   . HOH F 3 .   ? -17.359 30.721  9.645   1.00 45.72  ? 836 HOH B O   1 
HETATM 10361 O O   . HOH F 3 .   ? -8.133  23.109  -15.618 1.00 31.46  ? 837 HOH B O   1 
HETATM 10362 O O   . HOH F 3 .   ? 10.617  50.648  -44.136 1.00 31.18  ? 838 HOH B O   1 
HETATM 10363 O O   . HOH F 3 .   ? 5.323   18.640  -7.026  1.00 30.73  ? 839 HOH B O   1 
HETATM 10364 O O   . HOH F 3 .   ? -0.193  48.891  -33.318 1.00 35.98  ? 840 HOH B O   1 
HETATM 10365 O O   . HOH F 3 .   ? 18.423  34.003  -10.911 1.00 68.20  ? 841 HOH B O   1 
HETATM 10366 O O   . HOH F 3 .   ? -3.091  29.712  -23.239 1.00 36.20  ? 842 HOH B O   1 
HETATM 10367 O O   . HOH F 3 .   ? 13.354  44.688  -30.583 1.00 35.31  ? 843 HOH B O   1 
HETATM 10368 O O   . HOH F 3 .   ? 8.463   13.922  -8.834  1.00 44.99  ? 844 HOH B O   1 
HETATM 10369 O O   . HOH F 3 .   ? 2.557   21.355  -30.251 1.00 51.39  ? 845 HOH B O   1 
HETATM 10370 O O   . HOH F 3 .   ? 25.651  26.933  -24.678 1.00 52.92  ? 846 HOH B O   1 
HETATM 10371 O O   . HOH F 3 .   ? -10.960 28.595  -11.930 1.00 39.17  ? 847 HOH B O   1 
HETATM 10372 O O   . HOH F 3 .   ? 14.109  19.838  -10.912 1.00 49.93  ? 848 HOH B O   1 
HETATM 10373 O O   . HOH F 3 .   ? -6.960  47.806  5.936   1.00 38.09  ? 849 HOH B O   1 
HETATM 10374 O O   . HOH F 3 .   ? -22.445 42.636  -59.338 1.00 63.10  ? 850 HOH B O   1 
HETATM 10375 O O   . HOH F 3 .   ? -4.064  43.889  -0.662  1.00 69.92  ? 851 HOH B O   1 
HETATM 10376 O O   . HOH F 3 .   ? 1.170   32.356  19.971  1.00 36.21  ? 852 HOH B O   1 
HETATM 10377 O O   . HOH F 3 .   ? 1.946   40.547  -14.794 1.00 35.33  ? 853 HOH B O   1 
HETATM 10378 O O   . HOH F 3 .   ? -33.179 45.482  -3.778  1.00 60.11  ? 854 HOH B O   1 
HETATM 10379 O O   . HOH F 3 .   ? 3.227   49.791  -34.835 1.00 44.75  ? 855 HOH B O   1 
HETATM 10380 O O   . HOH F 3 .   ? 4.103   38.893  -13.729 1.00 46.14  ? 856 HOH B O   1 
HETATM 10381 O O   . HOH F 3 .   ? -1.280  20.199  17.547  1.00 55.31  ? 857 HOH B O   1 
HETATM 10382 O O   . HOH F 3 .   ? 16.699  43.896  -31.030 1.00 34.60  ? 858 HOH B O   1 
HETATM 10383 O O   . HOH F 3 .   ? 8.443   40.777  -48.299 1.00 27.20  ? 859 HOH B O   1 
HETATM 10384 O O   . HOH F 3 .   ? 3.539   33.451  -11.805 1.00 37.49  ? 860 HOH B O   1 
HETATM 10385 O O   . HOH F 3 .   ? -6.898  49.790  0.194   1.00 56.99  ? 861 HOH B O   1 
HETATM 10386 O O   . HOH F 3 .   ? 5.986   15.799  -14.030 1.00 36.71  ? 862 HOH B O   1 
HETATM 10387 O O   . HOH F 3 .   ? 13.616  21.387  -26.670 1.00 47.43  ? 863 HOH B O   1 
HETATM 10388 O O   . HOH F 3 .   ? 16.207  36.046  -45.107 1.00 40.07  ? 864 HOH B O   1 
HETATM 10389 O O   . HOH F 3 .   ? -13.064 30.563  -42.284 1.00 49.66  ? 865 HOH B O   1 
HETATM 10390 O O   . HOH F 3 .   ? 6.839   41.156  9.692   1.00 54.46  ? 866 HOH B O   1 
HETATM 10391 O O   . HOH F 3 .   ? -7.267  42.914  -12.503 1.00 37.51  ? 867 HOH B O   1 
HETATM 10392 O O   . HOH F 3 .   ? -11.723 25.960  -7.903  1.00 50.85  ? 868 HOH B O   1 
HETATM 10393 O O   . HOH F 3 .   ? -12.071 32.091  -17.768 1.00 55.62  ? 869 HOH B O   1 
HETATM 10394 O O   . HOH F 3 .   ? 4.012   46.944  -16.064 1.00 33.44  ? 870 HOH B O   1 
HETATM 10395 O O   . HOH F 3 .   ? 3.990   32.567  -4.441  1.00 33.35  ? 871 HOH B O   1 
HETATM 10396 O O   . HOH F 3 .   ? 10.004  21.799  -27.261 1.00 52.20  ? 872 HOH B O   1 
HETATM 10397 O O   . HOH F 3 .   ? -8.371  52.559  -40.895 1.00 48.70  ? 873 HOH B O   1 
HETATM 10398 O O   . HOH F 3 .   ? 3.394   12.398  -10.808 1.00 48.67  ? 874 HOH B O   1 
HETATM 10399 O O   . HOH F 3 .   ? 12.030  31.372  -4.079  1.00 53.54  ? 875 HOH B O   1 
HETATM 10400 O O   . HOH F 3 .   ? -14.316 41.394  -33.145 1.00 52.11  ? 876 HOH B O   1 
HETATM 10401 O O   . HOH F 3 .   ? 2.218   40.550  -55.799 1.00 46.34  ? 877 HOH B O   1 
HETATM 10402 O O   . HOH F 3 .   ? 4.132   16.419  1.300   1.00 62.71  ? 878 HOH B O   1 
HETATM 10403 O O   . HOH F 3 .   ? -17.446 35.334  -3.953  1.00 47.53  ? 879 HOH B O   1 
HETATM 10404 O O   . HOH F 3 .   ? 16.140  34.959  -50.248 1.00 41.23  ? 880 HOH B O   1 
HETATM 10405 O O   . HOH F 3 .   ? 2.809   45.479  -43.393 1.00 56.81  ? 881 HOH B O   1 
HETATM 10406 O O   . HOH F 3 .   ? 3.082   38.519  -17.957 1.00 42.41  ? 882 HOH B O   1 
HETATM 10407 O O   . HOH F 3 .   ? 0.368   33.665  -15.005 1.00 25.79  ? 883 HOH B O   1 
HETATM 10408 O O   . HOH F 3 .   ? 15.786  20.800  -25.128 1.00 44.87  ? 884 HOH B O   1 
HETATM 10409 O O   . HOH F 3 .   ? 5.068   41.273  3.101   1.00 53.27  ? 885 HOH B O   1 
HETATM 10410 O O   . HOH F 3 .   ? 11.072  19.166  -30.903 1.00 38.59  ? 886 HOH B O   1 
HETATM 10411 O O   . HOH F 3 .   ? 1.273   20.414  16.092  1.00 63.19  ? 887 HOH B O   1 
HETATM 10412 O O   . HOH F 3 .   ? -21.148 39.290  -3.187  1.00 69.85  ? 888 HOH B O   1 
HETATM 10413 O O   . HOH F 3 .   ? -13.795 32.988  -8.432  1.00 51.73  ? 889 HOH B O   1 
HETATM 10414 O O   . HOH F 3 .   ? 9.210   21.886  -29.646 1.00 36.20  ? 890 HOH B O   1 
HETATM 10415 O O   . HOH F 3 .   ? 3.900   37.270  -16.021 1.00 30.83  ? 891 HOH B O   1 
HETATM 10416 O O   . HOH F 3 .   ? -8.698  15.591  -18.158 1.00 47.63  ? 892 HOH B O   1 
HETATM 10417 O O   . HOH F 3 .   ? 3.274   46.793  -41.129 1.00 43.13  ? 893 HOH B O   1 
HETATM 10418 O O   . HOH F 3 .   ? 5.642   39.077  -8.518  1.00 52.44  ? 894 HOH B O   1 
HETATM 10419 O O   . HOH F 3 .   ? 4.919   37.737  -11.100 1.00 53.32  ? 895 HOH B O   1 
HETATM 10420 O O   . HOH F 3 .   ? 4.982   44.861  -5.410  1.00 51.26  ? 896 HOH B O   1 
HETATM 10421 O O   . HOH F 3 .   ? -4.941  21.235  -1.409  1.00 45.11  ? 897 HOH B O   1 
HETATM 10422 O O   . HOH F 3 .   ? 19.293  31.465  -40.626 1.00 40.24  ? 898 HOH B O   1 
HETATM 10423 O O   . HOH F 3 .   ? 21.440  34.969  -11.723 1.00 48.92  ? 899 HOH B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . MET A 1   ? 1.0060 0.7996 0.8772 0.0392  0.1875  0.0090  1   MET A N   
2    C CA  . MET A 1   ? 0.9630 0.7704 0.8345 0.0488  0.1783  0.0169  1   MET A CA  
3    C C   . MET A 1   ? 0.8784 0.7083 0.7588 0.0460  0.1607  0.0137  1   MET A C   
4    O O   . MET A 1   ? 0.8894 0.7290 0.7743 0.0440  0.1514  0.0117  1   MET A O   
5    C CB  . MET A 1   ? 1.0190 0.8232 0.8821 0.0626  0.1854  0.0292  1   MET A CB  
6    C CG  . MET A 1   ? 1.0748 0.8943 0.9378 0.0727  0.1772  0.0375  1   MET A CG  
7    S SD  . MET A 1   ? 1.1422 0.9606 0.9951 0.0901  0.1859  0.0527  1   MET A SD  
8    C CE  . MET A 1   ? 1.0249 0.8565 0.8789 0.0910  0.1795  0.0535  1   MET A CE  
9    N N   . VAL A 2   ? 0.8080 0.6451 0.6905 0.0457  0.1568  0.0129  2   VAL A N   
10   C CA  . VAL A 2   ? 0.7243 0.5819 0.6138 0.0453  0.1416  0.0115  2   VAL A CA  
11   C C   . VAL A 2   ? 0.6613 0.5257 0.5598 0.0343  0.1325  0.0012  2   VAL A C   
12   O O   . VAL A 2   ? 0.6982 0.5581 0.5993 0.0275  0.1356  -0.0051 2   VAL A O   
13   C CB  . VAL A 2   ? 0.7147 0.5787 0.6022 0.0507  0.1410  0.0159  2   VAL A CB  
14   C CG1 . VAL A 2   ? 0.6890 0.5729 0.5834 0.0495  0.1263  0.0137  2   VAL A CG1 
15   C CG2 . VAL A 2   ? 0.7550 0.6160 0.6334 0.0630  0.1485  0.0273  2   VAL A CG2 
16   N N   . HIS A 3   ? 0.5958 0.4721 0.4993 0.0331  0.1212  -0.0001 3   HIS A N   
17   C CA  . HIS A 3   ? 0.5448 0.4284 0.4566 0.0241  0.1121  -0.0087 3   HIS A CA  
18   C C   . HIS A 3   ? 0.4930 0.3926 0.4104 0.0247  0.0996  -0.0092 3   HIS A C   
19   O O   . HIS A 3   ? 0.4432 0.3487 0.3674 0.0184  0.0930  -0.0158 3   HIS A O   
20   C CB  . HIS A 3   ? 0.5719 0.4543 0.4846 0.0208  0.1102  -0.0107 3   HIS A CB  
21   C CG  . HIS A 3   ? 0.6118 0.4779 0.5195 0.0182  0.1227  -0.0121 3   HIS A CG  
22   N ND1 . HIS A 3   ? 0.6250 0.4832 0.5266 0.0237  0.1292  -0.0064 3   HIS A ND1 
23   C CD2 . HIS A 3   ? 0.6115 0.4678 0.5195 0.0101  0.1306  -0.0192 3   HIS A CD2 
24   C CE1 . HIS A 3   ? 0.6359 0.4786 0.5338 0.0193  0.1411  -0.0097 3   HIS A CE1 
25   N NE2 . HIS A 3   ? 0.6370 0.4789 0.5388 0.0105  0.1419  -0.0178 3   HIS A NE2 
26   N N   . TYR A 4   ? 0.4682 0.3751 0.3826 0.0324  0.0969  -0.0024 4   TYR A N   
27   C CA  . TYR A 4   ? 0.4541 0.3762 0.3729 0.0330  0.0853  -0.0027 4   TYR A CA  
28   C C   . TYR A 4   ? 0.4705 0.3988 0.3891 0.0357  0.0846  -0.0014 4   TYR A C   
29   O O   . TYR A 4   ? 0.4694 0.3940 0.3820 0.0414  0.0920  0.0037  4   TYR A O   
30   C CB  . TYR A 4   ? 0.4367 0.3660 0.3526 0.0387  0.0818  0.0032  4   TYR A CB  
31   C CG  . TYR A 4   ? 0.4140 0.3411 0.3306 0.0363  0.0799  0.0022  4   TYR A CG  
32   C CD1 . TYR A 4   ? 0.4205 0.3412 0.3408 0.0287  0.0798  -0.0042 4   TYR A CD1 
33   C CD2 . TYR A 4   ? 0.4042 0.3376 0.3182 0.0413  0.0778  0.0074  4   TYR A CD2 
34   C CE1 . TYR A 4   ? 0.4109 0.3303 0.3314 0.0263  0.0780  -0.0051 4   TYR A CE1 
35   C CE2 . TYR A 4   ? 0.4082 0.3397 0.3227 0.0391  0.0762  0.0065  4   TYR A CE2 
36   C CZ  . TYR A 4   ? 0.4158 0.3399 0.3333 0.0316  0.0763  0.0003  4   TYR A CZ  
37   O OH  . TYR A 4   ? 0.4048 0.3277 0.3223 0.0293  0.0748  -0.0005 4   TYR A OH  
38   N N   . TYR A 5   ? 0.4704 0.4084 0.3951 0.0322  0.0757  -0.0059 5   TYR A N   
39   C CA  . TYR A 5   ? 0.4662 0.4134 0.3907 0.0348  0.0729  -0.0047 5   TYR A CA  
40   C C   . TYR A 5   ? 0.4574 0.4173 0.3826 0.0367  0.0644  -0.0029 5   TYR A C   
41   O O   . TYR A 5   ? 0.4688 0.4313 0.3983 0.0328  0.0579  -0.0061 5   TYR A O   
42   C CB  . TYR A 5   ? 0.4728 0.4208 0.4037 0.0291  0.0701  -0.0118 5   TYR A CB  
43   C CG  . TYR A 5   ? 0.4806 0.4381 0.4122 0.0306  0.0669  -0.0120 5   TYR A CG  
44   C CD1 . TYR A 5   ? 0.4788 0.4360 0.4048 0.0351  0.0732  -0.0079 5   TYR A CD1 
45   C CD2 . TYR A 5   ? 0.4729 0.4392 0.4103 0.0275  0.0581  -0.0163 5   TYR A CD2 
46   C CE1 . TYR A 5   ? 0.4668 0.4335 0.3931 0.0359  0.0703  -0.0086 5   TYR A CE1 
47   C CE2 . TYR A 5   ? 0.4780 0.4525 0.4159 0.0281  0.0558  -0.0173 5   TYR A CE2 
48   C CZ  . TYR A 5   ? 0.4890 0.4644 0.4214 0.0321  0.0616  -0.0137 5   TYR A CZ  
49   O OH  . TYR A 5   ? 0.5229 0.5074 0.4555 0.0322  0.0593  -0.0151 5   TYR A OH  
50   N N   . ARG A 6   ? 0.4346 0.4028 0.3552 0.0426  0.0652  0.0024  6   ARG A N   
51   C CA  . ARG A 6   ? 0.4413 0.4227 0.3621 0.0438  0.0581  0.0038  6   ARG A CA  
52   C C   . ARG A 6   ? 0.4418 0.4314 0.3673 0.0394  0.0514  -0.0016 6   ARG A C   
53   O O   . ARG A 6   ? 0.4451 0.4346 0.3709 0.0390  0.0534  -0.0033 6   ARG A O   
54   C CB  . ARG A 6   ? 0.4741 0.4638 0.3880 0.0519  0.0617  0.0115  6   ARG A CB  
55   C CG  . ARG A 6   ? 0.4886 0.4727 0.3978 0.0573  0.0672  0.0177  6   ARG A CG  
56   C CD  . ARG A 6   ? 0.5372 0.5296 0.4395 0.0667  0.0717  0.0262  6   ARG A CD  
57   N NE  . ARG A 6   ? 0.6135 0.6025 0.5124 0.0692  0.0775  0.0279  6   ARG A NE  
58   C CZ  . ARG A 6   ? 0.6302 0.6210 0.5217 0.0781  0.0843  0.0361  6   ARG A CZ  
59   N NH1 . ARG A 6   ? 0.6636 0.6604 0.5509 0.0858  0.0862  0.0434  6   ARG A NH1 
60   N NH2 . ARG A 6   ? 0.6184 0.6056 0.5069 0.0797  0.0895  0.0372  6   ARG A NH2 
61   N N   . LEU A 7   ? 0.4189 0.4148 0.3478 0.0359  0.0439  -0.0045 7   LEU A N   
62   C CA  . LEU A 7   ? 0.4130 0.4151 0.3464 0.0314  0.0381  -0.0101 7   LEU A CA  
63   C C   . LEU A 7   ? 0.4259 0.4422 0.3562 0.0334  0.0367  -0.0088 7   LEU A C   
64   O O   . LEU A 7   ? 0.4310 0.4518 0.3640 0.0300  0.0338  -0.0135 7   LEU A O   
65   C CB  . LEU A 7   ? 0.3815 0.3827 0.3195 0.0266  0.0316  -0.0140 7   LEU A CB  
66   C CG  . LEU A 7   ? 0.3826 0.3728 0.3243 0.0236  0.0312  -0.0163 7   LEU A CG  
67   C CD1 . LEU A 7   ? 0.3720 0.3634 0.3176 0.0195  0.0244  -0.0196 7   LEU A CD1 
68   C CD2 . LEU A 7   ? 0.3722 0.3553 0.3175 0.0219  0.0342  -0.0197 7   LEU A CD2 
69   N N   . SER A 8   ? 0.4366 0.4604 0.3612 0.0390  0.0391  -0.0025 8   SER A N   
70   C CA  . SER A 8   ? 0.4603 0.5010 0.3816 0.0410  0.0376  -0.0010 8   SER A CA  
71   C C   . SER A 8   ? 0.4752 0.5191 0.3953 0.0412  0.0399  -0.0024 8   SER A C   
72   O O   . SER A 8   ? 0.4465 0.4818 0.3650 0.0440  0.0455  -0.0003 8   SER A O   
73   C CB  . SER A 8   ? 0.4901 0.5388 0.4053 0.0485  0.0407  0.0069  8   SER A CB  
74   O OG  . SER A 8   ? 0.5214 0.5894 0.4335 0.0503  0.0388  0.0082  8   SER A OG  
75   N N   . LEU A 9   ? 0.4882 0.5447 0.4091 0.0379  0.0359  -0.0064 9   LEU A N   
76   C CA  . LEU A 9   ? 0.5180 0.5804 0.4374 0.0376  0.0376  -0.0082 9   LEU A CA  
77   C C   . LEU A 9   ? 0.5680 0.6387 0.4801 0.0455  0.0427  -0.0004 9   LEU A C   
78   O O   . LEU A 9   ? 0.5913 0.6601 0.5011 0.0473  0.0468  0.0003  9   LEU A O   
79   C CB  . LEU A 9   ? 0.4807 0.5560 0.4017 0.0318  0.0326  -0.0143 9   LEU A CB  
80   C CG  . LEU A 9   ? 0.4697 0.5371 0.3968 0.0248  0.0304  -0.0227 9   LEU A CG  
81   C CD1 . LEU A 9   ? 0.4309 0.4812 0.3636 0.0230  0.0294  -0.0244 9   LEU A CD1 
82   C CD2 . LEU A 9   ? 0.4439 0.5223 0.3718 0.0188  0.0262  -0.0285 9   LEU A CD2 
83   N N   . LYS A 10  ? 0.6043 0.6837 0.5125 0.0506  0.0427  0.0056  10  LYS A N   
84   C CA  . LYS A 10  ? 0.6332 0.7222 0.5339 0.0596  0.0475  0.0143  10  LYS A CA  
85   C C   . LYS A 10  ? 0.6277 0.7025 0.5249 0.0647  0.0554  0.0190  10  LYS A C   
86   O O   . LYS A 10  ? 0.6563 0.7385 0.5471 0.0712  0.0597  0.0250  10  LYS A O   
87   C CB  . LYS A 10  ? 0.6855 0.7813 0.5838 0.0650  0.0472  0.0205  10  LYS A CB  
88   C CG  . LYS A 10  ? 0.7463 0.8627 0.6456 0.0617  0.0407  0.0175  10  LYS A CG  
89   C CD  . LYS A 10  ? 0.7770 0.8995 0.6749 0.0666  0.0404  0.0231  10  LYS A CD  
90   C CE  . LYS A 10  ? 0.8268 0.9682 0.7267 0.0611  0.0338  0.0184  10  LYS A CE  
91   N NZ  . LYS A 10  ? 0.8639 1.0172 0.7617 0.0670  0.0337  0.0244  10  LYS A NZ  
92   N N   . SER A 11  ? 0.6128 0.6678 0.5139 0.0616  0.0575  0.0162  11  SER A N   
93   C CA  . SER A 11  ? 0.6348 0.6747 0.5327 0.0651  0.0659  0.0197  11  SER A CA  
94   C C   . SER A 11  ? 0.6173 0.6523 0.5176 0.0604  0.0671  0.0141  11  SER A C   
95   O O   . SER A 11  ? 0.6131 0.6348 0.5116 0.0617  0.0741  0.0155  11  SER A O   
96   C CB  . SER A 11  ? 0.6033 0.6252 0.5032 0.0645  0.0691  0.0200  11  SER A CB  
97   O OG  . SER A 11  ? 0.6065 0.6259 0.5139 0.0568  0.0623  0.0127  11  SER A OG  
98   N N   . ARG A 12  ? 0.5939 0.6393 0.4981 0.0548  0.0609  0.0075  12  ARG A N   
99   C CA  . ARG A 12  ? 0.6058 0.6476 0.5128 0.0502  0.0618  0.0017  12  ARG A CA  
100  C C   . ARG A 12  ? 0.6409 0.6852 0.5407 0.0557  0.0685  0.0070  12  ARG A C   
101  O O   . ARG A 12  ? 0.6709 0.7257 0.5635 0.0627  0.0705  0.0145  12  ARG A O   
102  C CB  . ARG A 12  ? 0.5552 0.6083 0.4668 0.0438  0.0549  -0.0059 12  ARG A CB  
103  C CG  . ARG A 12  ? 0.5278 0.6015 0.4343 0.0457  0.0528  -0.0040 12  ARG A CG  
104  C CD  . ARG A 12  ? 0.5333 0.6160 0.4446 0.0386  0.0459  -0.0116 12  ARG A CD  
105  N NE  . ARG A 12  ? 0.5370 0.6405 0.4440 0.0382  0.0441  -0.0121 12  ARG A NE  
106  C CZ  . ARG A 12  ? 0.5164 0.6358 0.4202 0.0401  0.0414  -0.0092 12  ARG A CZ  
107  N NH1 . ARG A 12  ? 0.5017 0.6179 0.4059 0.0430  0.0403  -0.0051 12  ARG A NH1 
108  N NH2 . ARG A 12  ? 0.5148 0.6547 0.4151 0.0387  0.0399  -0.0108 12  ARG A NH2 
109  N N   . GLN A 13  ? 0.6404 0.6758 0.5418 0.0527  0.0721  0.0032  13  GLN A N   
110  C CA  . GLN A 13  ? 0.6594 0.6968 0.5539 0.0569  0.0785  0.0076  13  GLN A CA  
111  C C   . GLN A 13  ? 0.6546 0.7031 0.5507 0.0526  0.0755  0.0016  13  GLN A C   
112  O O   . GLN A 13  ? 0.6091 0.6580 0.5128 0.0455  0.0702  -0.0068 13  GLN A O   
113  C CB  . GLN A 13  ? 0.6964 0.7145 0.5898 0.0577  0.0871  0.0091  13  GLN A CB  
114  C CG  . GLN A 13  ? 0.7605 0.7694 0.6476 0.0649  0.0937  0.0180  13  GLN A CG  
115  C CD  . GLN A 13  ? 0.7794 0.7671 0.6684 0.0622  0.1004  0.0161  13  GLN A CD  
116  O OE1 . GLN A 13  ? 0.7787 0.7579 0.6687 0.0627  0.1013  0.0175  13  GLN A OE1 
117  N NE2 . GLN A 13  ? 0.7490 0.7288 0.6388 0.0586  0.1053  0.0124  13  GLN A NE2 
118  N N   . LYS A 14  ? 0.7033 0.7614 0.5916 0.0572  0.0793  0.0065  14  LYS A N   
119  C CA  . LYS A 14  ? 0.7215 0.7884 0.6097 0.0536  0.0787  0.0016  14  LYS A CA  
120  C C   . LYS A 14  ? 0.7203 0.7710 0.6112 0.0505  0.0843  -0.0019 14  LYS A C   
121  O O   . LYS A 14  ? 0.7667 0.8068 0.6523 0.0550  0.0922  0.0038  14  LYS A O   
122  C CB  . LYS A 14  ? 0.7589 0.8422 0.6370 0.0603  0.0812  0.0090  14  LYS A CB  
123  C CG  . LYS A 14  ? 0.7983 0.8916 0.6750 0.0567  0.0815  0.0043  14  LYS A CG  
124  C CD  . LYS A 14  ? 0.8455 0.9585 0.7120 0.0633  0.0830  0.0117  14  LYS A CD  
125  C CE  . LYS A 14  ? 0.8860 1.0098 0.7508 0.0591  0.0831  0.0065  14  LYS A CE  
126  N NZ  . LYS A 14  ? 0.9141 1.0608 0.7689 0.0651  0.0836  0.0133  14  LYS A NZ  
127  N N   . ALA A 15  ? 0.6895 0.7383 0.5887 0.0428  0.0807  -0.0117 15  ALA A N   
128  C CA  . ALA A 15  ? 0.6565 0.6915 0.5601 0.0391  0.0852  -0.0163 15  ALA A CA  
129  C C   . ALA A 15  ? 0.6474 0.6845 0.5445 0.0409  0.0917  -0.0143 15  ALA A C   
130  O O   . ALA A 15  ? 0.6461 0.6978 0.5397 0.0410  0.0898  -0.0148 15  ALA A O   
131  C CB  . ALA A 15  ? 0.6119 0.6464 0.5261 0.0316  0.0796  -0.0267 15  ALA A CB  
132  N N   . PRO A 16  ? 0.6444 0.6671 0.5399 0.0417  0.0996  -0.0125 16  PRO A N   
133  C CA  . PRO A 16  ? 0.6603 0.6827 0.5511 0.0417  0.1061  -0.0123 16  PRO A CA  
134  C C   . PRO A 16  ? 0.6762 0.7027 0.5751 0.0344  0.1025  -0.0228 16  PRO A C   
135  O O   . PRO A 16  ? 0.6259 0.6531 0.5341 0.0298  0.0958  -0.0296 16  PRO A O   
136  C CB  . PRO A 16  ? 0.6660 0.6694 0.5554 0.0422  0.1150  -0.0101 16  PRO A CB  
137  C CG  . PRO A 16  ? 0.6517 0.6466 0.5497 0.0388  0.1112  -0.0141 16  PRO A CG  
138  C CD  . PRO A 16  ? 0.6293 0.6352 0.5275 0.0414  0.1032  -0.0117 16  PRO A CD  
139  N N   . LYS A 17  ? 0.6874 0.7162 0.5828 0.0336  0.1073  -0.0239 17  LYS A N   
140  C CA  . LYS A 17  ? 0.6764 0.7071 0.5796 0.0268  0.1057  -0.0340 17  LYS A CA  
141  C C   . LYS A 17  ? 0.6551 0.6714 0.5667 0.0225  0.1085  -0.0393 17  LYS A C   
142  O O   . LYS A 17  ? 0.6513 0.6678 0.5733 0.0177  0.1037  -0.0474 17  LYS A O   
143  C CB  . LYS A 17  ? 0.7244 0.7629 0.6209 0.0270  0.1101  -0.0337 17  LYS A CB  
144  C CG  . LYS A 17  ? 0.7550 0.8123 0.6454 0.0289  0.1058  -0.0318 17  LYS A CG  
145  C CD  . LYS A 17  ? 0.7418 0.8070 0.6393 0.0255  0.0966  -0.0372 17  LYS A CD  
146  C CE  . LYS A 17  ? 0.7544 0.8387 0.6480 0.0239  0.0931  -0.0398 17  LYS A CE  
147  N NZ  . LYS A 17  ? 0.7476 0.8336 0.6452 0.0178  0.0944  -0.0488 17  LYS A NZ  
148  N N   . ILE A 18  ? 0.6729 0.6772 0.5799 0.0244  0.1169  -0.0349 18  ILE A N   
149  C CA  . ILE A 18  ? 0.6844 0.6758 0.5987 0.0200  0.1202  -0.0398 18  ILE A CA  
150  C C   . ILE A 18  ? 0.7153 0.6942 0.6248 0.0232  0.1253  -0.0331 18  ILE A C   
151  O O   . ILE A 18  ? 0.7016 0.6814 0.6019 0.0296  0.1267  -0.0243 18  ILE A O   
152  C CB  . ILE A 18  ? 0.7108 0.6986 0.6262 0.0160  0.1272  -0.0446 18  ILE A CB  
153  C CG1 . ILE A 18  ? 0.7167 0.6982 0.6193 0.0200  0.1375  -0.0367 18  ILE A CG1 
154  C CG2 . ILE A 18  ? 0.6697 0.6694 0.5905 0.0127  0.1224  -0.0519 18  ILE A CG2 
155  C CD1 . ILE A 18  ? 0.7075 0.6829 0.6106 0.0156  0.1457  -0.0411 18  ILE A CD1 
156  N N   . VAL A 19  ? 0.7474 0.7157 0.6631 0.0188  0.1280  -0.0376 19  VAL A N   
157  C CA  . VAL A 19  ? 0.8011 0.7566 0.7128 0.0206  0.1334  -0.0326 19  VAL A CA  
158  C C   . VAL A 19  ? 0.8792 0.8214 0.7830 0.0207  0.1463  -0.0295 19  VAL A C   
159  O O   . VAL A 19  ? 0.9483 0.8914 0.8515 0.0182  0.1506  -0.0325 19  VAL A O   
160  C CB  . VAL A 19  ? 0.7758 0.7277 0.6978 0.0157  0.1289  -0.0387 19  VAL A CB  
161  C CG1 . VAL A 19  ? 0.7626 0.7251 0.6900 0.0169  0.1173  -0.0396 19  VAL A CG1 
162  C CG2 . VAL A 19  ? 0.7481 0.6995 0.6796 0.0084  0.1302  -0.0485 19  VAL A CG2 
163  N N   . ASN A 20  ? 0.9416 0.8711 0.8392 0.0235  0.1530  -0.0236 20  ASN A N   
164  C CA  . ASN A 20  ? 1.0652 0.9792 0.9536 0.0240  0.1669  -0.0197 20  ASN A CA  
165  C C   . ASN A 20  ? 1.0993 1.0016 0.9937 0.0154  0.1733  -0.0278 20  ASN A C   
166  O O   . ASN A 20  ? 1.0847 0.9936 0.9910 0.0087  0.1667  -0.0372 20  ASN A O   
167  C CB  . ASN A 20  ? 1.1101 1.0156 0.9866 0.0328  0.1728  -0.0079 20  ASN A CB  
168  C CG  . ASN A 20  ? 1.1225 1.0255 1.0026 0.0335  0.1681  -0.0073 20  ASN A CG  
169  O OD1 . ASN A 20  ? 1.1461 1.0355 1.0272 0.0297  0.1743  -0.0095 20  ASN A OD1 
170  N ND2 . ASN A 20  ? 1.1509 1.0676 1.0329 0.0377  0.1576  -0.0047 20  ASN A ND2 
171  N N   . SER A 21  ? 1.1617 1.0470 1.0474 0.0155  0.1866  -0.0240 21  SER A N   
172  C CA  . SER A 21  ? 1.1814 1.0552 1.0713 0.0064  0.1945  -0.0320 21  SER A CA  
173  C C   . SER A 21  ? 1.1233 0.9974 1.0221 0.0018  0.1891  -0.0376 21  SER A C   
174  O O   . SER A 21  ? 1.1272 1.0016 1.0346 -0.0071 0.1898  -0.0474 21  SER A O   
175  C CB  . SER A 21  ? 1.2246 1.0780 1.1019 0.0079  0.2110  -0.0261 21  SER A CB  
176  O OG  . SER A 21  ? 1.2871 1.1387 1.1595 0.0071  0.2182  -0.0259 21  SER A OG  
177  N N   . LYS A 22  ? 1.0905 0.9659 0.9871 0.0078  0.1836  -0.0314 22  LYS A N   
178  C CA  . LYS A 22  ? 1.0407 0.9147 0.9435 0.0044  0.1795  -0.0351 22  LYS A CA  
179  C C   . LYS A 22  ? 0.9780 0.8676 0.8950 -0.0009 0.1667  -0.0443 22  LYS A C   
180  O O   . LYS A 22  ? 0.9753 0.8642 0.8996 -0.0080 0.1663  -0.0518 22  LYS A O   
181  C CB  . LYS A 22  ? 1.0722 0.9444 0.9686 0.0130  0.1768  -0.0256 22  LYS A CB  
182  C CG  . LYS A 22  ? 1.1302 0.9840 1.0135 0.0181  0.1906  -0.0168 22  LYS A CG  
183  C CD  . LYS A 22  ? 1.1157 0.9733 0.9912 0.0297  0.1875  -0.0052 22  LYS A CD  
184  C CE  . LYS A 22  ? 1.0720 0.9392 0.9541 0.0305  0.1758  -0.0060 22  LYS A CE  
185  N NZ  . LYS A 22  ? 1.0847 0.9650 0.9631 0.0398  0.1682  0.0021  22  LYS A NZ  
186  N N   . TYR A 23  ? 0.9050 0.8088 0.8254 0.0024  0.1569  -0.0438 23  TYR A N   
187  C CA  . TYR A 23  ? 0.8128 0.7305 0.7453 -0.0004 0.1444  -0.0504 23  TYR A CA  
188  C C   . TYR A 23  ? 0.7828 0.7082 0.7244 -0.0064 0.1432  -0.0594 23  TYR A C   
189  O O   . TYR A 23  ? 0.7885 0.7131 0.7267 -0.0065 0.1487  -0.0595 23  TYR A O   
190  C CB  . TYR A 23  ? 0.7646 0.6930 0.6961 0.0060  0.1347  -0.0454 23  TYR A CB  
191  C CG  . TYR A 23  ? 0.7664 0.6911 0.6910 0.0121  0.1338  -0.0372 23  TYR A CG  
192  C CD1 . TYR A 23  ? 0.7436 0.6675 0.6726 0.0106  0.1289  -0.0385 23  TYR A CD1 
193  C CD2 . TYR A 23  ? 0.7805 0.7040 0.6942 0.0196  0.1375  -0.0278 23  TYR A CD2 
194  C CE1 . TYR A 23  ? 0.7455 0.6668 0.6686 0.0162  0.1281  -0.0312 23  TYR A CE1 
195  C CE2 . TYR A 23  ? 0.7598 0.6816 0.6677 0.0258  0.1366  -0.0201 23  TYR A CE2 
196  C CZ  . TYR A 23  ? 0.7744 0.6947 0.6871 0.0239  0.1319  -0.0220 23  TYR A CZ  
197  O OH  . TYR A 23  ? 0.8164 0.7354 0.7237 0.0299  0.1311  -0.0146 23  TYR A OH  
198  N N   . ASN A 24  ? 0.7076 0.6412 0.6607 -0.0107 0.1357  -0.0667 24  ASN A N   
199  C CA  . ASN A 24  ? 0.6422 0.5857 0.6053 -0.0152 0.1329  -0.0751 24  ASN A CA  
200  C C   . ASN A 24  ? 0.6648 0.6178 0.6289 -0.0111 0.1264  -0.0740 24  ASN A C   
201  O O   . ASN A 24  ? 0.6383 0.5951 0.6004 -0.0061 0.1195  -0.0693 24  ASN A O   
202  C CB  . ASN A 24  ? 0.6255 0.5766 0.6001 -0.0194 0.1260  -0.0819 24  ASN A CB  
203  C CG  . ASN A 24  ? 0.6207 0.5824 0.6062 -0.0238 0.1243  -0.0906 24  ASN A CG  
204  O OD1 . ASN A 24  ? 0.6341 0.6039 0.6236 -0.0212 0.1190  -0.0917 24  ASN A OD1 
205  N ND2 . ASN A 24  ? 0.5997 0.5619 0.5902 -0.0306 0.1290  -0.0972 24  ASN A ND2 
206  N N   . SER A 25  ? 0.6455 0.6028 0.6131 -0.0137 0.1293  -0.0789 25  SER A N   
207  C CA  . SER A 25  ? 0.6168 0.5825 0.5850 -0.0109 0.1250  -0.0791 25  SER A CA  
208  C C   . SER A 25  ? 0.5604 0.5362 0.5368 -0.0091 0.1136  -0.0814 25  SER A C   
209  O O   . SER A 25  ? 0.5499 0.5314 0.5249 -0.0062 0.1097  -0.0803 25  SER A O   
210  C CB  . SER A 25  ? 0.6253 0.5939 0.5975 -0.0152 0.1303  -0.0855 25  SER A CB  
211  O OG  . SER A 25  ? 0.6881 0.6485 0.6495 -0.0146 0.1401  -0.0813 25  SER A OG  
212  N N   . ILE A 26  ? 0.5376 0.5158 0.5224 -0.0111 0.1087  -0.0850 26  ILE A N   
213  C CA  . ILE A 26  ? 0.5212 0.5074 0.5134 -0.0091 0.0985  -0.0866 26  ILE A CA  
214  C C   . ILE A 26  ? 0.5103 0.4961 0.4953 -0.0041 0.0938  -0.0800 26  ILE A C   
215  O O   . ILE A 26  ? 0.5198 0.5117 0.5079 -0.0024 0.0876  -0.0812 26  ILE A O   
216  C CB  . ILE A 26  ? 0.4960 0.4845 0.4967 -0.0113 0.0943  -0.0900 26  ILE A CB  
217  C CG1 . ILE A 26  ? 0.4981 0.4953 0.5079 -0.0092 0.0851  -0.0929 26  ILE A CG1 
218  C CG2 . ILE A 26  ? 0.4903 0.4714 0.4847 -0.0105 0.0946  -0.0846 26  ILE A CG2 
219  C CD1 . ILE A 26  ? 0.5120 0.5147 0.5316 -0.0112 0.0813  -0.0972 26  ILE A CD1 
220  N N   . LEU A 27  ? 0.5142 0.4930 0.4894 -0.0020 0.0976  -0.0732 27  LEU A N   
221  C CA  . LEU A 27  ? 0.5136 0.4937 0.4816 0.0026  0.0939  -0.0667 27  LEU A CA  
222  C C   . LEU A 27  ? 0.5170 0.5036 0.4809 0.0045  0.0937  -0.0659 27  LEU A C   
223  O O   . LEU A 27  ? 0.5296 0.5218 0.4912 0.0070  0.0883  -0.0637 27  LEU A O   
224  C CB  . LEU A 27  ? 0.5141 0.4858 0.4724 0.0053  0.0989  -0.0593 27  LEU A CB  
225  C CG  . LEU A 27  ? 0.5178 0.4832 0.4785 0.0036  0.0988  -0.0593 27  LEU A CG  
226  C CD1 . LEU A 27  ? 0.5192 0.4754 0.4693 0.0070  0.1053  -0.0515 27  LEU A CD1 
227  C CD2 . LEU A 27  ? 0.4958 0.4669 0.4629 0.0039  0.0889  -0.0606 27  LEU A CD2 
228  N N   . ASN A 28  ? 0.5114 0.4975 0.4739 0.0029  0.1000  -0.0682 28  ASN A N   
229  C CA  . ASN A 28  ? 0.5146 0.5079 0.4740 0.0038  0.1000  -0.0687 28  ASN A CA  
230  C C   . ASN A 28  ? 0.5030 0.5046 0.4707 0.0024  0.0927  -0.0749 28  ASN A C   
231  O O   . ASN A 28  ? 0.4862 0.4943 0.4502 0.0036  0.0904  -0.0744 28  ASN A O   
232  C CB  . ASN A 28  ? 0.5417 0.5326 0.4988 0.0017  0.1084  -0.0707 28  ASN A CB  
233  C CG  . ASN A 28  ? 0.5792 0.5610 0.5255 0.0039  0.1170  -0.0635 28  ASN A CG  
234  O OD1 . ASN A 28  ? 0.5817 0.5609 0.5209 0.0081  0.1166  -0.0562 28  ASN A OD1 
235  N ND2 . ASN A 28  ? 0.5991 0.5759 0.5439 0.0013  0.1254  -0.0654 28  ASN A ND2 
236  N N   . ILE A 29  ? 0.4802 0.4816 0.4588 0.0000  0.0898  -0.0808 29  ILE A N   
237  C CA  . ILE A 29  ? 0.4529 0.4600 0.4396 -0.0005 0.0837  -0.0863 29  ILE A CA  
238  C C   . ILE A 29  ? 0.4354 0.4443 0.4196 0.0015  0.0773  -0.0831 29  ILE A C   
239  O O   . ILE A 29  ? 0.4203 0.4342 0.4029 0.0015  0.0750  -0.0846 29  ILE A O   
240  C CB  . ILE A 29  ? 0.4549 0.4621 0.4536 -0.0023 0.0818  -0.0919 29  ILE A CB  
241  C CG1 . ILE A 29  ? 0.4557 0.4629 0.4574 -0.0052 0.0885  -0.0961 29  ILE A CG1 
242  C CG2 . ILE A 29  ? 0.4457 0.4573 0.4522 -0.0017 0.0764  -0.0966 29  ILE A CG2 
243  C CD1 . ILE A 29  ? 0.4600 0.4689 0.4723 -0.0072 0.0876  -0.1007 29  ILE A CD1 
244  N N   . ALA A 30  ? 0.4249 0.4296 0.4080 0.0028  0.0749  -0.0790 30  ALA A N   
245  C CA  . ALA A 30  ? 0.4252 0.4311 0.4055 0.0046  0.0693  -0.0755 30  ALA A CA  
246  C C   . ALA A 30  ? 0.4365 0.4473 0.4067 0.0064  0.0701  -0.0711 30  ALA A C   
247  O O   . ALA A 30  ? 0.4721 0.4880 0.4415 0.0062  0.0659  -0.0718 30  ALA A O   
248  C CB  . ALA A 30  ? 0.4062 0.4067 0.3863 0.0055  0.0680  -0.0716 30  ALA A CB  
249  N N   . LEU A 31  ? 0.4376 0.4473 0.4000 0.0080  0.0760  -0.0665 31  LEU A N   
250  C CA  . LEU A 31  ? 0.4464 0.4630 0.3990 0.0104  0.0773  -0.0620 31  LEU A CA  
251  C C   . LEU A 31  ? 0.4438 0.4688 0.3975 0.0079  0.0761  -0.0674 31  LEU A C   
252  O O   . LEU A 31  ? 0.4364 0.4700 0.3855 0.0082  0.0733  -0.0665 31  LEU A O   
253  C CB  . LEU A 31  ? 0.4478 0.4608 0.3920 0.0129  0.0853  -0.0564 31  LEU A CB  
254  C CG  . LEU A 31  ? 0.4738 0.4793 0.4124 0.0166  0.0882  -0.0488 31  LEU A CG  
255  C CD1 . LEU A 31  ? 0.4710 0.4703 0.4019 0.0187  0.0976  -0.0442 31  LEU A CD1 
256  C CD2 . LEU A 31  ? 0.4526 0.4647 0.3855 0.0204  0.0838  -0.0430 31  LEU A CD2 
257  N N   . LYS A 32  ? 0.4513 0.4743 0.4111 0.0053  0.0786  -0.0735 32  LYS A N   
258  C CA  . LYS A 32  ? 0.4710 0.5003 0.4329 0.0026  0.0787  -0.0797 32  LYS A CA  
259  C C   . LYS A 32  ? 0.4599 0.4918 0.4267 0.0009  0.0726  -0.0839 32  LYS A C   
260  O O   . LYS A 32  ? 0.4526 0.4921 0.4148 -0.0002 0.0711  -0.0848 32  LYS A O   
261  C CB  . LYS A 32  ? 0.5144 0.5398 0.4835 0.0004  0.0827  -0.0852 32  LYS A CB  
262  C CG  . LYS A 32  ? 0.5360 0.5657 0.5103 -0.0023 0.0827  -0.0930 32  LYS A CG  
263  C CD  . LYS A 32  ? 0.5719 0.6086 0.5381 -0.0032 0.0869  -0.0930 32  LYS A CD  
264  C CE  . LYS A 32  ? 0.5995 0.6398 0.5709 -0.0064 0.0877  -0.1014 32  LYS A CE  
265  N NZ  . LYS A 32  ? 0.6543 0.7030 0.6170 -0.0077 0.0913  -0.1015 32  LYS A NZ  
266  N N   . ASN A 33  ? 0.4579 0.4835 0.4335 0.0007  0.0694  -0.0862 33  ASN A N   
267  C CA  . ASN A 33  ? 0.4486 0.4738 0.4288 -0.0001 0.0641  -0.0893 33  ASN A CA  
268  C C   . ASN A 33  ? 0.4555 0.4845 0.4288 0.0002  0.0606  -0.0851 33  ASN A C   
269  O O   . ASN A 33  ? 0.4620 0.4936 0.4357 -0.0018 0.0580  -0.0884 33  ASN A O   
270  C CB  . ASN A 33  ? 0.4386 0.4569 0.4281 0.0008  0.0614  -0.0904 33  ASN A CB  
271  C CG  . ASN A 33  ? 0.4526 0.4693 0.4497 0.0003  0.0646  -0.0948 33  ASN A CG  
272  O OD1 . ASN A 33  ? 0.4631 0.4828 0.4609 -0.0010 0.0681  -0.0990 33  ASN A OD1 
273  N ND2 . ASN A 33  ? 0.4466 0.4598 0.4495 0.0013  0.0636  -0.0941 33  ASN A ND2 
274  N N   . PHE A 34  ? 0.4378 0.4673 0.4048 0.0029  0.0612  -0.0781 34  PHE A N   
275  C CA  . PHE A 34  ? 0.4454 0.4810 0.4053 0.0038  0.0584  -0.0737 34  PHE A CA  
276  C C   . PHE A 34  ? 0.4351 0.4824 0.3885 0.0021  0.0595  -0.0752 34  PHE A C   
277  O O   . PHE A 34  ? 0.4376 0.4909 0.3898 -0.0003 0.0564  -0.0776 34  PHE A O   
278  C CB  . PHE A 34  ? 0.4539 0.4874 0.4082 0.0079  0.0597  -0.0654 34  PHE A CB  
279  C CG  . PHE A 34  ? 0.4712 0.5122 0.4187 0.0096  0.0569  -0.0604 34  PHE A CG  
280  C CD1 . PHE A 34  ? 0.4846 0.5292 0.4339 0.0071  0.0519  -0.0633 34  PHE A CD1 
281  C CD2 . PHE A 34  ? 0.4848 0.5291 0.4240 0.0141  0.0597  -0.0527 34  PHE A CD2 
282  C CE1 . PHE A 34  ? 0.4812 0.5343 0.4246 0.0082  0.0494  -0.0592 34  PHE A CE1 
283  C CE2 . PHE A 34  ? 0.4584 0.5114 0.3918 0.0163  0.0572  -0.0480 34  PHE A CE2 
284  C CZ  . PHE A 34  ? 0.4675 0.5257 0.4033 0.0131  0.0518  -0.0515 34  PHE A CZ  
285  N N   . ARG A 35  ? 0.4334 0.4842 0.3824 0.0029  0.0643  -0.0743 35  ARG A N   
286  C CA  . ARG A 35  ? 0.4580 0.5213 0.4010 0.0009  0.0658  -0.0763 35  ARG A CA  
287  C C   . ARG A 35  ? 0.4465 0.5112 0.3948 -0.0045 0.0648  -0.0859 35  ARG A C   
288  O O   . ARG A 35  ? 0.4490 0.5241 0.3931 -0.0076 0.0638  -0.0887 35  ARG A O   
289  C CB  . ARG A 35  ? 0.4598 0.5253 0.3973 0.0029  0.0716  -0.0736 35  ARG A CB  
290  C CG  . ARG A 35  ? 0.4554 0.5191 0.3858 0.0087  0.0743  -0.0637 35  ARG A CG  
291  C CD  . ARG A 35  ? 0.4751 0.5424 0.3981 0.0107  0.0806  -0.0607 35  ARG A CD  
292  N NE  . ARG A 35  ? 0.4729 0.5319 0.4014 0.0081  0.0848  -0.0658 35  ARG A NE  
293  C CZ  . ARG A 35  ? 0.4853 0.5322 0.4163 0.0094  0.0887  -0.0639 35  ARG A CZ  
294  N NH1 . ARG A 35  ? 0.4867 0.5269 0.4150 0.0133  0.0894  -0.0570 35  ARG A NH1 
295  N NH2 . ARG A 35  ? 0.4734 0.5153 0.4097 0.0065  0.0924  -0.0693 35  ARG A NH2 
296  N N   . LEU A 36  ? 0.4469 0.5015 0.4042 -0.0055 0.0655  -0.0908 36  LEU A N   
297  C CA  . LEU A 36  ? 0.4238 0.4771 0.3866 -0.0098 0.0656  -0.0996 36  LEU A CA  
298  C C   . LEU A 36  ? 0.4090 0.4617 0.3729 -0.0119 0.0615  -0.1014 36  LEU A C   
299  O O   . LEU A 36  ? 0.4087 0.4664 0.3708 -0.0164 0.0620  -0.1070 36  LEU A O   
300  C CB  . LEU A 36  ? 0.4100 0.4533 0.3829 -0.0090 0.0671  -0.1032 36  LEU A CB  
301  C CG  . LEU A 36  ? 0.4396 0.4835 0.4152 -0.0103 0.0721  -0.1083 36  LEU A CG  
302  C CD1 . LEU A 36  ? 0.4332 0.4875 0.3998 -0.0120 0.0758  -0.1081 36  LEU A CD1 
303  C CD2 . LEU A 36  ? 0.4334 0.4706 0.4154 -0.0077 0.0738  -0.1070 36  LEU A CD2 
304  N N   . CYS A 37  ? 0.4159 0.4622 0.3823 -0.0093 0.0578  -0.0970 37  CYS A N   
305  C CA  . CYS A 37  ? 0.4304 0.4747 0.3973 -0.0110 0.0539  -0.0978 37  CYS A CA  
306  C C   . CYS A 37  ? 0.4392 0.4963 0.3975 -0.0139 0.0531  -0.0973 37  CYS A C   
307  O O   . CYS A 37  ? 0.4125 0.4712 0.3705 -0.0185 0.0523  -0.1024 37  CYS A O   
308  C CB  . CYS A 37  ? 0.4308 0.4679 0.4003 -0.0072 0.0504  -0.0918 37  CYS A CB  
309  S SG  . CYS A 37  ? 0.4931 0.5262 0.4635 -0.0089 0.0458  -0.0920 37  CYS A SG  
310  N N   . LYS A 38  ? 0.4435 0.5101 0.3947 -0.0112 0.0536  -0.0912 38  LYS A N   
311  C CA  . LYS A 38  ? 0.4671 0.5490 0.4101 -0.0130 0.0526  -0.0900 38  LYS A CA  
312  C C   . LYS A 38  ? 0.4849 0.5769 0.4252 -0.0188 0.0551  -0.0975 38  LYS A C   
313  O O   . LYS A 38  ? 0.5158 0.6190 0.4519 -0.0231 0.0539  -0.1003 38  LYS A O   
314  C CB  . LYS A 38  ? 0.4891 0.5789 0.4251 -0.0073 0.0532  -0.0809 38  LYS A CB  
315  C CG  . LYS A 38  ? 0.4906 0.5742 0.4271 -0.0029 0.0503  -0.0737 38  LYS A CG  
316  C CD  . LYS A 38  ? 0.4933 0.5848 0.4220 0.0029  0.0518  -0.0646 38  LYS A CD  
317  C CE  . LYS A 38  ? 0.4978 0.5810 0.4261 0.0070  0.0564  -0.0609 38  LYS A CE  
318  N NZ  . LYS A 38  ? 0.5157 0.6047 0.4356 0.0134  0.0587  -0.0513 38  LYS A NZ  
319  N N   . LYS A 39  ? 0.4859 0.5742 0.4287 -0.0195 0.0589  -0.1015 39  LYS A N   
320  C CA  . LYS A 39  ? 0.4945 0.5918 0.4347 -0.0251 0.0621  -0.1092 39  LYS A CA  
321  C C   . LYS A 39  ? 0.4909 0.5804 0.4366 -0.0311 0.0629  -0.1185 39  LYS A C   
322  O O   . LYS A 39  ? 0.5208 0.6188 0.4632 -0.0373 0.0650  -0.1255 39  LYS A O   
323  C CB  . LYS A 39  ? 0.5088 0.6053 0.4491 -0.0235 0.0664  -0.1096 39  LYS A CB  
324  C CG  . LYS A 39  ? 0.5283 0.6341 0.4609 -0.0186 0.0675  -0.1012 39  LYS A CG  
325  C CD  . LYS A 39  ? 0.5608 0.6634 0.4940 -0.0174 0.0724  -0.1020 39  LYS A CD  
326  C CE  . LYS A 39  ? 0.5785 0.6884 0.5030 -0.0121 0.0745  -0.0930 39  LYS A CE  
327  N NZ  . LYS A 39  ? 0.6236 0.7245 0.5503 -0.0100 0.0793  -0.0923 39  LYS A NZ  
328  N N   . HIS A 40  ? 0.4911 0.5645 0.4449 -0.0290 0.0618  -0.1187 40  HIS A N   
329  C CA  . HIS A 40  ? 0.5033 0.5667 0.4623 -0.0331 0.0631  -0.1263 40  HIS A CA  
330  C C   . HIS A 40  ? 0.5566 0.6234 0.5121 -0.0378 0.0612  -0.1282 40  HIS A C   
331  O O   . HIS A 40  ? 0.5751 0.6386 0.5309 -0.0353 0.0572  -0.1229 40  HIS A O   
332  C CB  . HIS A 40  ? 0.4637 0.5106 0.4320 -0.0283 0.0620  -0.1244 40  HIS A CB  
333  C CG  . HIS A 40  ? 0.4613 0.4962 0.4350 -0.0309 0.0641  -0.1312 40  HIS A CG  
334  N ND1 . HIS A 40  ? 0.4449 0.4672 0.4245 -0.0276 0.0619  -0.1290 40  HIS A ND1 
335  C CD2 . HIS A 40  ? 0.4471 0.4806 0.4207 -0.0366 0.0690  -0.1402 40  HIS A CD2 
336  C CE1 . HIS A 40  ? 0.4423 0.4549 0.4252 -0.0303 0.0653  -0.1355 40  HIS A CE1 
337  N NE2 . HIS A 40  ? 0.4386 0.4575 0.4179 -0.0360 0.0699  -0.1426 40  HIS A NE2 
338  N N   . LYS A 41  ? 0.6429 0.7160 0.5949 -0.0452 0.0644  -0.1364 41  LYS A N   
339  C CA  . LYS A 41  ? 0.7017 0.7775 0.6506 -0.0514 0.0638  -0.1402 41  LYS A CA  
340  C C   . LYS A 41  ? 0.7433 0.7998 0.6983 -0.0533 0.0664  -0.1455 41  LYS A C   
341  O O   . LYS A 41  ? 0.8079 0.8584 0.7650 -0.0570 0.0716  -0.1533 41  LYS A O   
342  C CB  . LYS A 41  ? 0.7401 0.8342 0.6815 -0.0594 0.0664  -0.1468 41  LYS A CB  
343  C CG  . LYS A 41  ? 0.7511 0.8651 0.6859 -0.0566 0.0648  -0.1414 41  LYS A CG  
344  C CD  . LYS A 41  ? 0.7698 0.8922 0.7012 -0.0517 0.0594  -0.1318 41  LYS A CD  
345  C CE  . LYS A 41  ? 0.7682 0.9076 0.6933 -0.0469 0.0585  -0.1249 41  LYS A CE  
346  N NZ  . LYS A 41  ? 0.7986 0.9394 0.7223 -0.0393 0.0543  -0.1139 41  LYS A NZ  
347  N N   . THR A 42  ? 0.7750 0.8217 0.7326 -0.0503 0.0630  -0.1408 42  THR A N   
348  C CA  . THR A 42  ? 0.8246 0.8524 0.7876 -0.0505 0.0650  -0.1438 42  THR A CA  
349  C C   . THR A 42  ? 0.9023 0.9297 0.8610 -0.0571 0.0653  -0.1469 42  THR A C   
350  O O   . THR A 42  ? 0.8351 0.8740 0.7892 -0.0580 0.0613  -0.1429 42  THR A O   
351  C CB  . THR A 42  ? 0.8409 0.8567 0.8106 -0.0416 0.0611  -0.1359 42  THR A CB  
352  O OG1 . THR A 42  ? 0.8097 0.8137 0.7805 -0.0419 0.0602  -0.1350 42  THR A OG1 
353  C CG2 . THR A 42  ? 0.7773 0.8033 0.7450 -0.0366 0.0559  -0.1272 42  THR A CG2 
354  N N   . LYS A 43  ? 0.9723 0.9859 0.9325 -0.0614 0.0707  -0.1539 43  LYS A N   
355  C CA  . LYS A 43  ? 1.0650 1.0754 1.0210 -0.0688 0.0725  -0.1581 43  LYS A CA  
356  C C   . LYS A 43  ? 1.0797 1.0803 1.0375 -0.0642 0.0681  -0.1507 43  LYS A C   
357  O O   . LYS A 43  ? 1.0653 1.0718 1.0184 -0.0688 0.0664  -0.1505 43  LYS A O   
358  C CB  . LYS A 43  ? 1.0959 1.0920 1.0525 -0.0748 0.0811  -0.1680 43  LYS A CB  
359  C CG  . LYS A 43  ? 1.1157 1.1182 1.0653 -0.0869 0.0854  -0.1768 43  LYS A CG  
360  C CD  . LYS A 43  ? 1.1433 1.1282 1.0933 -0.0928 0.0951  -0.1866 43  LYS A CD  
361  C CE  . LYS A 43  ? 1.1302 1.1287 1.0742 -0.1047 0.1008  -0.1981 43  LYS A CE  
362  N NZ  . LYS A 43  ? 1.1373 1.1546 1.0741 -0.1134 0.0985  -0.2004 43  LYS A NZ  
363  N N   . LYS A 44  ? 1.0978 1.0847 1.0623 -0.0554 0.0663  -0.1449 44  LYS A N   
364  C CA  . LYS A 44  ? 1.1119 1.0871 1.0785 -0.0509 0.0630  -0.1386 44  LYS A CA  
365  C C   . LYS A 44  ? 1.0581 1.0423 1.0249 -0.0451 0.0553  -0.1292 44  LYS A C   
366  O O   . LYS A 44  ? 0.9475 0.9380 0.9169 -0.0398 0.0528  -0.1252 44  LYS A O   
367  C CB  . LYS A 44  ? 1.1458 1.1012 1.1192 -0.0448 0.0657  -0.1378 44  LYS A CB  
368  C CG  . LYS A 44  ? 1.2060 1.1471 1.1784 -0.0501 0.0740  -0.1459 44  LYS A CG  
369  C CD  . LYS A 44  ? 1.2333 1.1647 1.2014 -0.0545 0.0755  -0.1463 44  LYS A CD  
370  C CE  . LYS A 44  ? 1.3005 1.2225 1.2646 -0.0637 0.0849  -0.1565 44  LYS A CE  
371  N NZ  . LYS A 44  ? 1.3259 1.2285 1.2947 -0.0593 0.0917  -0.1589 44  LYS A NZ  
372  N N   . PRO A 45  ? 1.0333 1.0174 0.9970 -0.0466 0.0523  -0.1259 45  PRO A N   
373  C CA  . PRO A 45  ? 0.9693 0.9620 0.9318 -0.0427 0.0459  -0.1178 45  PRO A CA  
374  C C   . PRO A 45  ? 0.8909 0.8823 0.8585 -0.0337 0.0421  -0.1106 45  PRO A C   
375  O O   . PRO A 45  ? 0.8649 0.8446 0.8385 -0.0291 0.0430  -0.1101 45  PRO A O   
376  C CB  . PRO A 45  ? 1.0284 1.0111 0.9896 -0.0442 0.0451  -0.1162 45  PRO A CB  
377  C CG  . PRO A 45  ? 1.0476 1.0261 1.0053 -0.0531 0.0513  -0.1251 45  PRO A CG  
378  C CD  . PRO A 45  ? 1.0638 1.0388 1.0241 -0.0534 0.0563  -0.1309 45  PRO A CD  
379  N N   . VAL A 46  ? 0.8281 0.8316 0.7932 -0.0314 0.0381  -0.1052 46  VAL A N   
380  C CA  . VAL A 46  ? 0.7841 0.7889 0.7526 -0.0245 0.0357  -0.0994 46  VAL A CA  
381  C C   . VAL A 46  ? 0.7656 0.7632 0.7365 -0.0197 0.0315  -0.0927 46  VAL A C   
382  O O   . VAL A 46  ? 0.8343 0.8358 0.8015 -0.0206 0.0288  -0.0893 46  VAL A O   
383  C CB  . VAL A 46  ? 0.7542 0.7755 0.7179 -0.0242 0.0351  -0.0971 46  VAL A CB  
384  C CG1 . VAL A 46  ? 0.6843 0.7152 0.6443 -0.0300 0.0389  -0.1039 46  VAL A CG1 
385  C CG2 . VAL A 46  ? 0.7011 0.7309 0.6601 -0.0239 0.0316  -0.0918 46  VAL A CG2 
386  N N   . GLN A 47  ? 0.6855 0.6735 0.6628 -0.0148 0.0311  -0.0911 47  GLN A N   
387  C CA  . GLN A 47  ? 0.6760 0.6597 0.6560 -0.0101 0.0271  -0.0849 47  GLN A CA  
388  C C   . GLN A 47  ? 0.5892 0.5790 0.5705 -0.0062 0.0261  -0.0811 47  GLN A C   
389  O O   . GLN A 47  ? 0.5546 0.5435 0.5405 -0.0040 0.0279  -0.0827 47  GLN A O   
390  C CB  . GLN A 47  ? 0.7323 0.7033 0.7182 -0.0070 0.0271  -0.0852 47  GLN A CB  
391  C CG  . GLN A 47  ? 0.8093 0.7715 0.7929 -0.0092 0.0269  -0.0853 47  GLN A CG  
392  C CD  . GLN A 47  ? 0.7939 0.7551 0.7763 -0.0072 0.0224  -0.0792 47  GLN A CD  
393  O OE1 . GLN A 47  ? 0.8273 0.7960 0.8087 -0.0057 0.0197  -0.0753 47  GLN A OE1 
394  N NE2 . GLN A 47  ? 0.7898 0.7409 0.7717 -0.0072 0.0222  -0.0782 47  GLN A NE2 
395  N N   . ILE A 48  ? 0.5363 0.5323 0.5133 -0.0055 0.0240  -0.0763 48  ILE A N   
396  C CA  . ILE A 48  ? 0.5060 0.5073 0.4826 -0.0025 0.0246  -0.0728 48  ILE A CA  
397  C C   . ILE A 48  ? 0.4867 0.4818 0.4699 0.0011  0.0242  -0.0717 48  ILE A C   
398  O O   . ILE A 48  ? 0.4617 0.4587 0.4471 0.0023  0.0267  -0.0727 48  ILE A O   
399  C CB  . ILE A 48  ? 0.4893 0.4977 0.4597 -0.0018 0.0232  -0.0675 48  ILE A CB  
400  C CG1 . ILE A 48  ? 0.5225 0.5428 0.4869 -0.0037 0.0253  -0.0684 48  ILE A CG1 
401  C CG2 . ILE A 48  ? 0.4514 0.4591 0.4223 0.0021  0.0239  -0.0628 48  ILE A CG2 
402  C CD1 . ILE A 48  ? 0.5553 0.5793 0.5177 -0.0090 0.0257  -0.0738 48  ILE A CD1 
403  N N   . LEU A 49  ? 0.4813 0.4699 0.4676 0.0025  0.0212  -0.0699 49  LEU A N   
404  C CA  . LEU A 49  ? 0.4816 0.4667 0.4744 0.0057  0.0204  -0.0691 49  LEU A CA  
405  C C   . LEU A 49  ? 0.4695 0.4537 0.4681 0.0065  0.0230  -0.0737 49  LEU A C   
406  O O   . LEU A 49  ? 0.4525 0.4392 0.4546 0.0078  0.0245  -0.0743 49  LEU A O   
407  C CB  . LEU A 49  ? 0.4658 0.4451 0.4609 0.0071  0.0167  -0.0669 49  LEU A CB  
408  C CG  . LEU A 49  ? 0.4742 0.4536 0.4679 0.0081  0.0139  -0.0621 49  LEU A CG  
409  C CD1 . LEU A 49  ? 0.4512 0.4354 0.4401 0.0076  0.0154  -0.0595 49  LEU A CD1 
410  C CD2 . LEU A 49  ? 0.4751 0.4502 0.4660 0.0073  0.0109  -0.0600 49  LEU A CD2 
411  N N   . ALA A 50  ? 0.4795 0.4600 0.4788 0.0052  0.0240  -0.0773 50  ALA A N   
412  C CA  . ALA A 50  ? 0.4641 0.4432 0.4686 0.0060  0.0271  -0.0822 50  ALA A CA  
413  C C   . ALA A 50  ? 0.4637 0.4493 0.4666 0.0043  0.0307  -0.0849 50  ALA A C   
414  O O   . ALA A 50  ? 0.4951 0.4815 0.5034 0.0058  0.0328  -0.0875 50  ALA A O   
415  C CB  . ALA A 50  ? 0.4785 0.4505 0.4828 0.0046  0.0285  -0.0855 50  ALA A CB  
416  N N   . LEU A 51  ? 0.4437 0.4349 0.4393 0.0012  0.0316  -0.0844 51  LEU A N   
417  C CA  . LEU A 51  ? 0.4380 0.4361 0.4312 0.0001  0.0350  -0.0861 51  LEU A CA  
418  C C   . LEU A 51  ? 0.4104 0.4102 0.4049 0.0026  0.0356  -0.0828 51  LEU A C   
419  O O   . LEU A 51  ? 0.4431 0.4448 0.4402 0.0030  0.0387  -0.0852 51  LEU A O   
420  C CB  . LEU A 51  ? 0.4173 0.4231 0.4018 -0.0029 0.0356  -0.0854 51  LEU A CB  
421  C CG  . LEU A 51  ? 0.4407 0.4481 0.4225 -0.0074 0.0369  -0.0905 51  LEU A CG  
422  C CD1 . LEU A 51  ? 0.4322 0.4511 0.4054 -0.0101 0.0368  -0.0890 51  LEU A CD1 
423  C CD2 . LEU A 51  ? 0.4512 0.4573 0.4365 -0.0087 0.0409  -0.0968 51  LEU A CD2 
424  N N   . LEU A 52  ? 0.4137 0.4126 0.4064 0.0040  0.0330  -0.0778 52  LEU A N   
425  C CA  . LEU A 52  ? 0.4042 0.4041 0.3966 0.0057  0.0344  -0.0746 52  LEU A CA  
426  C C   . LEU A 52  ? 0.3937 0.3913 0.3944 0.0069  0.0352  -0.0773 52  LEU A C   
427  O O   . LEU A 52  ? 0.3596 0.3588 0.3611 0.0069  0.0386  -0.0776 52  LEU A O   
428  C CB  . LEU A 52  ? 0.3850 0.3834 0.3740 0.0066  0.0318  -0.0693 52  LEU A CB  
429  C CG  . LEU A 52  ? 0.4204 0.4216 0.4020 0.0075  0.0340  -0.0643 52  LEU A CG  
430  C CD1 . LEU A 52  ? 0.3950 0.4025 0.3712 0.0071  0.0376  -0.0646 52  LEU A CD1 
431  C CD2 . LEU A 52  ? 0.3890 0.3902 0.3663 0.0079  0.0307  -0.0601 52  LEU A CD2 
432  N N   . GLN A 53  ? 0.3912 0.3856 0.3981 0.0079  0.0324  -0.0792 53  GLN A N   
433  C CA  . GLN A 53  ? 0.4117 0.4062 0.4272 0.0097  0.0325  -0.0817 53  GLN A CA  
434  C C   . GLN A 53  ? 0.4200 0.4169 0.4394 0.0094  0.0365  -0.0868 53  GLN A C   
435  O O   . GLN A 53  ? 0.3940 0.3934 0.4200 0.0105  0.0377  -0.0891 53  GLN A O   
436  C CB  . GLN A 53  ? 0.4233 0.4144 0.4435 0.0121  0.0284  -0.0811 53  GLN A CB  
437  C CG  . GLN A 53  ? 0.4666 0.4578 0.4867 0.0129  0.0251  -0.0771 53  GLN A CG  
438  C CD  . GLN A 53  ? 0.4874 0.4743 0.5074 0.0145  0.0209  -0.0745 53  GLN A CD  
439  O OE1 . GLN A 53  ? 0.5278 0.5117 0.5516 0.0167  0.0201  -0.0758 53  GLN A OE1 
440  N NE2 . GLN A 53  ? 0.5127 0.4987 0.5280 0.0135  0.0186  -0.0705 53  GLN A NE2 
441  N N   . GLU A 54  ? 0.4097 0.4070 0.4245 0.0075  0.0387  -0.0888 54  GLU A N   
442  C CA  . GLU A 54  ? 0.4307 0.4309 0.4473 0.0065  0.0430  -0.0933 54  GLU A CA  
443  C C   . GLU A 54  ? 0.4373 0.4416 0.4482 0.0049  0.0466  -0.0919 54  GLU A C   
444  O O   . GLU A 54  ? 0.4153 0.4221 0.4286 0.0043  0.0505  -0.0949 54  GLU A O   
445  C CB  . GLU A 54  ? 0.4599 0.4587 0.4743 0.0047  0.0442  -0.0969 54  GLU A CB  
446  C CG  . GLU A 54  ? 0.4905 0.4829 0.5095 0.0065  0.0421  -0.0981 54  GLU A CG  
447  C CD  . GLU A 54  ? 0.4986 0.4883 0.5137 0.0036  0.0438  -0.1016 54  GLU A CD  
448  O OE1 . GLU A 54  ? 0.5310 0.5257 0.5394 0.0000  0.0457  -0.1026 54  GLU A OE1 
449  O OE2 . GLU A 54  ? 0.5452 0.5279 0.5636 0.0049  0.0438  -0.1033 54  GLU A OE2 
450  N N   . ILE A 55  ? 0.4201 0.4250 0.4233 0.0045  0.0457  -0.0870 55  ILE A N   
451  C CA  . ILE A 55  ? 0.4109 0.4189 0.4073 0.0040  0.0494  -0.0844 55  ILE A CA  
452  C C   . ILE A 55  ? 0.4117 0.4176 0.4102 0.0047  0.0518  -0.0827 55  ILE A C   
453  O O   . ILE A 55  ? 0.4386 0.4457 0.4363 0.0039  0.0566  -0.0839 55  ILE A O   
454  C CB  . ILE A 55  ? 0.4152 0.4256 0.4026 0.0041  0.0480  -0.0794 55  ILE A CB  
455  C CG1 . ILE A 55  ? 0.3981 0.4134 0.3822 0.0020  0.0477  -0.0824 55  ILE A CG1 
456  C CG2 . ILE A 55  ? 0.4120 0.4239 0.3924 0.0054  0.0518  -0.0744 55  ILE A CG2 
457  C CD1 . ILE A 55  ? 0.3886 0.4063 0.3673 0.0015  0.0443  -0.0794 55  ILE A CD1 
458  N N   . ILE A 56  ? 0.4201 0.4229 0.4209 0.0055  0.0488  -0.0803 56  ILE A N   
459  C CA  . ILE A 56  ? 0.4003 0.4014 0.4037 0.0052  0.0510  -0.0798 56  ILE A CA  
460  C C   . ILE A 56  ? 0.3973 0.4004 0.4112 0.0050  0.0499  -0.0849 56  ILE A C   
461  O O   . ILE A 56  ? 0.3931 0.3963 0.4122 0.0063  0.0452  -0.0854 56  ILE A O   
462  C CB  . ILE A 56  ? 0.3953 0.3930 0.3953 0.0058  0.0489  -0.0749 56  ILE A CB  
463  C CG1 . ILE A 56  ? 0.3918 0.3891 0.3822 0.0070  0.0490  -0.0697 56  ILE A CG1 
464  C CG2 . ILE A 56  ? 0.3912 0.3865 0.3918 0.0043  0.0532  -0.0747 56  ILE A CG2 
465  C CD1 . ILE A 56  ? 0.3883 0.3824 0.3750 0.0079  0.0473  -0.0647 56  ILE A CD1 
466  N N   . PRO A 57  ? 0.4070 0.4124 0.4242 0.0035  0.0545  -0.0885 57  PRO A N   
467  C CA  . PRO A 57  ? 0.4056 0.4153 0.4334 0.0038  0.0537  -0.0936 57  PRO A CA  
468  C C   . PRO A 57  ? 0.4016 0.4130 0.4344 0.0037  0.0509  -0.0932 57  PRO A C   
469  O O   . PRO A 57  ? 0.4077 0.4165 0.4360 0.0019  0.0526  -0.0906 57  PRO A O   
470  C CB  . PRO A 57  ? 0.4136 0.4256 0.4421 0.0014  0.0601  -0.0971 57  PRO A CB  
471  C CG  . PRO A 57  ? 0.4092 0.4165 0.4283 -0.0002 0.0644  -0.0929 57  PRO A CG  
472  C CD  . PRO A 57  ? 0.4205 0.4244 0.4318 0.0017  0.0611  -0.0874 57  PRO A CD  
473  N N   . LYS A 58  ? 0.4060 0.4220 0.4478 0.0058  0.0473  -0.0958 58  LYS A N   
474  C CA  . LYS A 58  ? 0.4385 0.4581 0.4848 0.0061  0.0438  -0.0952 58  LYS A CA  
475  C C   . LYS A 58  ? 0.4537 0.4774 0.5017 0.0021  0.0479  -0.0978 58  LYS A C   
476  O O   . LYS A 58  ? 0.4866 0.5117 0.5347 0.0005  0.0464  -0.0968 58  LYS A O   
477  C CB  . LYS A 58  ? 0.4528 0.4782 0.5085 0.0100  0.0394  -0.0970 58  LYS A CB  
478  C CG  . LYS A 58  ? 0.4684 0.4958 0.5255 0.0113  0.0342  -0.0941 58  LYS A CG  
479  C CD  . LYS A 58  ? 0.4825 0.5186 0.5497 0.0156  0.0306  -0.0957 58  LYS A CD  
480  C CE  . LYS A 58  ? 0.4851 0.5253 0.5530 0.0160  0.0260  -0.0930 58  LYS A CE  
481  N NZ  . LYS A 58  ? 0.5023 0.5491 0.5779 0.0220  0.0215  -0.0924 58  LYS A NZ  
482  N N   . SER A 59  ? 0.4366 0.4621 0.4857 -0.0001 0.0535  -0.1015 59  SER A N   
483  C CA  . SER A 59  ? 0.4512 0.4796 0.5014 -0.0048 0.0589  -0.1047 59  SER A CA  
484  C C   . SER A 59  ? 0.4561 0.4758 0.4965 -0.0078 0.0625  -0.1009 59  SER A C   
485  O O   . SER A 59  ? 0.4584 0.4790 0.4991 -0.0123 0.0669  -0.1032 59  SER A O   
486  C CB  . SER A 59  ? 0.4401 0.4705 0.4920 -0.0067 0.0648  -0.1090 59  SER A CB  
487  O OG  . SER A 59  ? 0.4502 0.4730 0.4938 -0.0055 0.0670  -0.1060 59  SER A OG  
488  N N   . TYR A 60  ? 0.4450 0.4568 0.4769 -0.0054 0.0612  -0.0952 60  TYR A N   
489  C CA  . TYR A 60  ? 0.4435 0.4474 0.4665 -0.0069 0.0643  -0.0908 60  TYR A CA  
490  C C   . TYR A 60  ? 0.4346 0.4398 0.4597 -0.0080 0.0608  -0.0903 60  TYR A C   
491  O O   . TYR A 60  ? 0.4203 0.4212 0.4414 -0.0113 0.0654  -0.0898 60  TYR A O   
492  C CB  . TYR A 60  ? 0.4394 0.4368 0.4530 -0.0037 0.0637  -0.0848 60  TYR A CB  
493  C CG  . TYR A 60  ? 0.4364 0.4262 0.4415 -0.0041 0.0666  -0.0797 60  TYR A CG  
494  C CD1 . TYR A 60  ? 0.4484 0.4319 0.4470 -0.0060 0.0751  -0.0785 60  TYR A CD1 
495  C CD2 . TYR A 60  ? 0.4469 0.4354 0.4506 -0.0026 0.0614  -0.0763 60  TYR A CD2 
496  C CE1 . TYR A 60  ? 0.4560 0.4316 0.4470 -0.0057 0.0787  -0.0738 60  TYR A CE1 
497  C CE2 . TYR A 60  ? 0.4307 0.4123 0.4270 -0.0028 0.0645  -0.0719 60  TYR A CE2 
498  C CZ  . TYR A 60  ? 0.4418 0.4168 0.4319 -0.0042 0.0733  -0.0707 60  TYR A CZ  
499  O OH  . TYR A 60  ? 0.4648 0.4318 0.4474 -0.0037 0.0773  -0.0660 60  TYR A OH  
500  N N   . PHE A 61  ? 0.4280 0.4389 0.4591 -0.0054 0.0533  -0.0904 61  PHE A N   
501  C CA  . PHE A 61  ? 0.4402 0.4535 0.4730 -0.0061 0.0492  -0.0896 61  PHE A CA  
502  C C   . PHE A 61  ? 0.4614 0.4864 0.5041 -0.0082 0.0479  -0.0952 61  PHE A C   
503  O O   . PHE A 61  ? 0.5073 0.5359 0.5512 -0.0102 0.0459  -0.0956 61  PHE A O   
504  C CB  . PHE A 61  ? 0.4213 0.4334 0.4535 -0.0017 0.0418  -0.0855 61  PHE A CB  
505  C CG  . PHE A 61  ? 0.4092 0.4128 0.4326 0.0003  0.0421  -0.0805 61  PHE A CG  
506  C CD1 . PHE A 61  ? 0.3933 0.3904 0.4087 -0.0005 0.0439  -0.0763 61  PHE A CD1 
507  C CD2 . PHE A 61  ? 0.3926 0.3958 0.4160 0.0030  0.0407  -0.0804 61  PHE A CD2 
508  C CE1 . PHE A 61  ? 0.3901 0.3821 0.3979 0.0017  0.0438  -0.0717 61  PHE A CE1 
509  C CE2 . PHE A 61  ? 0.4001 0.3982 0.4157 0.0043  0.0408  -0.0764 61  PHE A CE2 
510  C CZ  . PHE A 61  ? 0.3899 0.3832 0.3977 0.0039  0.0421  -0.0718 61  PHE A CZ  
511  N N   . GLY A 62  ? 0.4765 0.5087 0.5264 -0.0074 0.0485  -0.0994 62  GLY A N   
512  C CA  . GLY A 62  ? 0.4739 0.5200 0.5340 -0.0088 0.0471  -0.1048 62  GLY A CA  
513  C C   . GLY A 62  ? 0.4929 0.5473 0.5595 -0.0037 0.0390  -0.1033 62  GLY A C   
514  O O   . GLY A 62  ? 0.5160 0.5805 0.5914 -0.0007 0.0370  -0.1061 62  GLY A O   
515  N N   . THR A 63  ? 0.4993 0.5495 0.5615 -0.0023 0.0346  -0.0987 63  THR A N   
516  C CA  . THR A 63  ? 0.4825 0.5397 0.5497 0.0026  0.0272  -0.0965 63  THR A CA  
517  C C   . THR A 63  ? 0.4795 0.5257 0.5404 0.0066  0.0233  -0.0903 63  THR A C   
518  O O   . THR A 63  ? 0.4644 0.4996 0.5167 0.0048  0.0255  -0.0875 63  THR A O   
519  C CB  . THR A 63  ? 0.4918 0.5587 0.5610 -0.0004 0.0249  -0.0977 63  THR A CB  
520  O OG1 . THR A 63  ? 0.5195 0.5765 0.5797 -0.0047 0.0273  -0.0955 63  THR A OG1 
521  C CG2 . THR A 63  ? 0.4692 0.5505 0.5459 -0.0049 0.0282  -0.1047 63  THR A CG2 
522  N N   . THR A 64  ? 0.4776 0.5271 0.5426 0.0123  0.0178  -0.0880 64  THR A N   
523  C CA  . THR A 64  ? 0.4852 0.5249 0.5446 0.0157  0.0141  -0.0825 64  THR A CA  
524  C C   . THR A 64  ? 0.4855 0.5211 0.5379 0.0125  0.0128  -0.0794 64  THR A C   
525  O O   . THR A 64  ? 0.4914 0.5165 0.5363 0.0123  0.0128  -0.0759 64  THR A O   
526  C CB  . THR A 64  ? 0.4988 0.5428 0.5640 0.0224  0.0092  -0.0805 64  THR A CB  
527  O OG1 . THR A 64  ? 0.5061 0.5552 0.5787 0.0255  0.0111  -0.0838 64  THR A OG1 
528  C CG2 . THR A 64  ? 0.5045 0.5364 0.5638 0.0255  0.0069  -0.0756 64  THR A CG2 
529  N N   . THR A 65  ? 0.4846 0.5293 0.5395 0.0095  0.0122  -0.0813 65  THR A N   
530  C CA  . THR A 65  ? 0.4698 0.5110 0.5183 0.0062  0.0113  -0.0788 65  THR A CA  
531  C C   . THR A 65  ? 0.4648 0.4955 0.5054 0.0019  0.0170  -0.0786 65  THR A C   
532  O O   . THR A 65  ? 0.4436 0.4657 0.4770 0.0020  0.0162  -0.0744 65  THR A O   
533  C CB  . THR A 65  ? 0.4902 0.5446 0.5430 0.0033  0.0097  -0.0816 65  THR A CB  
534  O OG1 . THR A 65  ? 0.5020 0.5683 0.5627 0.0084  0.0047  -0.0816 65  THR A OG1 
535  C CG2 . THR A 65  ? 0.4778 0.5284 0.5242 0.0011  0.0077  -0.0785 65  THR A CG2 
536  N N   . ASN A 66  ? 0.4352 0.4667 0.4769 -0.0015 0.0230  -0.0827 66  ASN A N   
537  C CA  . ASN A 66  ? 0.4478 0.4685 0.4816 -0.0041 0.0292  -0.0816 66  ASN A CA  
538  C C   . ASN A 66  ? 0.4660 0.4779 0.4946 -0.0001 0.0281  -0.0772 66  ASN A C   
539  O O   . ASN A 66  ? 0.4534 0.4573 0.4742 -0.0002 0.0291  -0.0731 66  ASN A O   
540  C CB  . ASN A 66  ? 0.4569 0.4795 0.4928 -0.0078 0.0361  -0.0865 66  ASN A CB  
541  C CG  . ASN A 66  ? 0.4908 0.5209 0.5300 -0.0137 0.0391  -0.0916 66  ASN A CG  
542  O OD1 . ASN A 66  ? 0.5081 0.5404 0.5462 -0.0156 0.0369  -0.0911 66  ASN A OD1 
543  N ND2 . ASN A 66  ? 0.4615 0.4957 0.5044 -0.0172 0.0446  -0.0969 66  ASN A ND2 
544  N N   . LEU A 67  ? 0.4525 0.4668 0.4856 0.0031  0.0261  -0.0782 67  LEU A N   
545  C CA  . LEU A 67  ? 0.4571 0.4644 0.4855 0.0058  0.0256  -0.0752 67  LEU A CA  
546  C C   . LEU A 67  ? 0.4621 0.4647 0.4856 0.0074  0.0210  -0.0704 67  LEU A C   
547  O O   . LEU A 67  ? 0.4576 0.4542 0.4739 0.0074  0.0220  -0.0673 67  LEU A O   
548  C CB  . LEU A 67  ? 0.4272 0.4376 0.4617 0.0089  0.0245  -0.0778 67  LEU A CB  
549  C CG  . LEU A 67  ? 0.4128 0.4174 0.4438 0.0111  0.0239  -0.0762 67  LEU A CG  
550  C CD1 . LEU A 67  ? 0.4121 0.4197 0.4488 0.0123  0.0260  -0.0804 67  LEU A CD1 
551  C CD2 . LEU A 67  ? 0.4187 0.4203 0.4492 0.0139  0.0186  -0.0731 67  LEU A CD2 
552  N N   . LYS A 68  ? 0.4787 0.4851 0.5060 0.0089  0.0161  -0.0697 68  LYS A N   
553  C CA  . LYS A 68  ? 0.5277 0.5298 0.5509 0.0104  0.0118  -0.0654 68  LYS A CA  
554  C C   . LYS A 68  ? 0.5039 0.5020 0.5200 0.0076  0.0132  -0.0627 68  LYS A C   
555  O O   . LYS A 68  ? 0.5156 0.5086 0.5261 0.0082  0.0114  -0.0590 68  LYS A O   
556  C CB  . LYS A 68  ? 0.5834 0.5908 0.6120 0.0132  0.0067  -0.0648 68  LYS A CB  
557  C CG  . LYS A 68  ? 0.6364 0.6407 0.6671 0.0177  0.0041  -0.0637 68  LYS A CG  
558  C CD  . LYS A 68  ? 0.7140 0.7260 0.7525 0.0218  0.0009  -0.0641 68  LYS A CD  
559  C CE  . LYS A 68  ? 0.7178 0.7235 0.7562 0.0267  -0.0012 -0.0613 68  LYS A CE  
560  N NZ  . LYS A 68  ? 0.7670 0.7684 0.8001 0.0270  -0.0048 -0.0566 68  LYS A NZ  
561  N N   . ARG A 69  ? 0.4885 0.4888 0.5048 0.0043  0.0170  -0.0649 69  ARG A N   
562  C CA  . ARG A 69  ? 0.4769 0.4726 0.4868 0.0017  0.0198  -0.0628 69  ARG A CA  
563  C C   . ARG A 69  ? 0.4690 0.4576 0.4717 0.0024  0.0238  -0.0600 69  ARG A C   
564  O O   . ARG A 69  ? 0.4854 0.4698 0.4821 0.0032  0.0230  -0.0559 69  ARG A O   
565  C CB  . ARG A 69  ? 0.5061 0.5054 0.5181 -0.0026 0.0240  -0.0668 69  ARG A CB  
566  C CG  . ARG A 69  ? 0.5831 0.5772 0.5889 -0.0056 0.0271  -0.0651 69  ARG A CG  
567  C CD  . ARG A 69  ? 0.6135 0.6116 0.6218 -0.0110 0.0314  -0.0701 69  ARG A CD  
568  N NE  . ARG A 69  ? 0.6981 0.7050 0.7105 -0.0124 0.0261  -0.0717 69  ARG A NE  
569  C CZ  . ARG A 69  ? 0.7228 0.7418 0.7432 -0.0133 0.0234  -0.0759 69  ARG A CZ  
570  N NH1 . ARG A 69  ? 0.7171 0.7402 0.7426 -0.0132 0.0258  -0.0795 69  ARG A NH1 
571  N NH2 . ARG A 69  ? 0.7010 0.7290 0.7242 -0.0140 0.0185  -0.0766 69  ARG A NH2 
572  N N   . PHE A 70  ? 0.4370 0.4255 0.4403 0.0025  0.0280  -0.0619 70  PHE A N   
573  C CA  . PHE A 70  ? 0.4258 0.4098 0.4223 0.0038  0.0316  -0.0590 70  PHE A CA  
574  C C   . PHE A 70  ? 0.4198 0.4035 0.4136 0.0064  0.0270  -0.0560 70  PHE A C   
575  O O   . PHE A 70  ? 0.4521 0.4333 0.4393 0.0073  0.0280  -0.0521 70  PHE A O   
576  C CB  . PHE A 70  ? 0.4119 0.3972 0.4103 0.0035  0.0362  -0.0621 70  PHE A CB  
577  C CG  . PHE A 70  ? 0.3927 0.3752 0.3839 0.0053  0.0399  -0.0590 70  PHE A CG  
578  C CD1 . PHE A 70  ? 0.4121 0.3899 0.3969 0.0051  0.0464  -0.0563 70  PHE A CD1 
579  C CD2 . PHE A 70  ? 0.3935 0.3787 0.3845 0.0070  0.0373  -0.0590 70  PHE A CD2 
580  C CE1 . PHE A 70  ? 0.3916 0.3685 0.3696 0.0076  0.0497  -0.0528 70  PHE A CE1 
581  C CE2 . PHE A 70  ? 0.3551 0.3404 0.3396 0.0084  0.0405  -0.0565 70  PHE A CE2 
582  C CZ  . PHE A 70  ? 0.3780 0.3600 0.3562 0.0091  0.0463  -0.0531 70  PHE A CZ  
583  N N   . TYR A 71  ? 0.4000 0.3863 0.3989 0.0074  0.0225  -0.0579 71  TYR A N   
584  C CA  . TYR A 71  ? 0.3971 0.3824 0.3935 0.0088  0.0194  -0.0564 71  TYR A CA  
585  C C   . TYR A 71  ? 0.4033 0.3865 0.3962 0.0090  0.0156  -0.0528 71  TYR A C   
586  O O   . TYR A 71  ? 0.3909 0.3734 0.3798 0.0092  0.0142  -0.0512 71  TYR A O   
587  C CB  . TYR A 71  ? 0.3846 0.3712 0.3871 0.0100  0.0173  -0.0598 71  TYR A CB  
588  C CG  . TYR A 71  ? 0.4120 0.4005 0.4157 0.0098  0.0212  -0.0629 71  TYR A CG  
589  C CD1 . TYR A 71  ? 0.4102 0.3985 0.4090 0.0095  0.0226  -0.0627 71  TYR A CD1 
590  C CD2 . TYR A 71  ? 0.4033 0.3947 0.4126 0.0095  0.0238  -0.0664 71  TYR A CD2 
591  C CE1 . TYR A 71  ? 0.4220 0.4126 0.4212 0.0091  0.0264  -0.0655 71  TYR A CE1 
592  C CE2 . TYR A 71  ? 0.4040 0.3969 0.4140 0.0091  0.0277  -0.0693 71  TYR A CE2 
593  C CZ  . TYR A 71  ? 0.4117 0.4039 0.4164 0.0091  0.0289  -0.0687 71  TYR A CZ  
594  O OH  . TYR A 71  ? 0.4402 0.4345 0.4451 0.0085  0.0328  -0.0716 71  TYR A OH  
595  N N   . LYS A 72  ? 0.4131 0.3960 0.4071 0.0083  0.0142  -0.0520 72  LYS A N   
596  C CA  . LYS A 72  ? 0.4376 0.4183 0.4272 0.0080  0.0116  -0.0484 72  LYS A CA  
597  C C   . LYS A 72  ? 0.4113 0.3906 0.3937 0.0081  0.0150  -0.0452 72  LYS A C   
598  O O   . LYS A 72  ? 0.4017 0.3805 0.3799 0.0085  0.0130  -0.0424 72  LYS A O   
599  C CB  . LYS A 72  ? 0.4615 0.4430 0.4532 0.0068  0.0102  -0.0484 72  LYS A CB  
600  C CG  . LYS A 72  ? 0.5057 0.4903 0.5036 0.0078  0.0057  -0.0500 72  LYS A CG  
601  C CD  . LYS A 72  ? 0.5568 0.5391 0.5524 0.0087  0.0010  -0.0469 72  LYS A CD  
602  C CE  . LYS A 72  ? 0.6364 0.6164 0.6334 0.0109  -0.0009 -0.0470 72  LYS A CE  
603  N NZ  . LYS A 72  ? 0.6820 0.6588 0.6738 0.0101  0.0008  -0.0463 72  LYS A NZ  
604  N N   . VAL A 73  ? 0.3818 0.3606 0.3627 0.0081  0.0204  -0.0454 73  VAL A N   
605  C CA  . VAL A 73  ? 0.3897 0.3676 0.3636 0.0095  0.0242  -0.0417 73  VAL A CA  
606  C C   . VAL A 73  ? 0.3858 0.3677 0.3572 0.0108  0.0229  -0.0411 73  VAL A C   
607  O O   . VAL A 73  ? 0.3890 0.3730 0.3558 0.0117  0.0217  -0.0380 73  VAL A O   
608  C CB  . VAL A 73  ? 0.3947 0.3701 0.3672 0.0095  0.0311  -0.0420 73  VAL A CB  
609  C CG1 . VAL A 73  ? 0.3764 0.3514 0.3413 0.0124  0.0353  -0.0373 73  VAL A CG1 
610  C CG2 . VAL A 73  ? 0.3810 0.3527 0.3552 0.0071  0.0332  -0.0434 73  VAL A CG2 
611  N N   . VAL A 74  ? 0.3544 0.3383 0.3293 0.0105  0.0233  -0.0445 74  VAL A N   
612  C CA  . VAL A 74  ? 0.3706 0.3586 0.3437 0.0106  0.0225  -0.0454 74  VAL A CA  
613  C C   . VAL A 74  ? 0.3810 0.3698 0.3533 0.0096  0.0178  -0.0450 74  VAL A C   
614  O O   . VAL A 74  ? 0.4023 0.3957 0.3703 0.0093  0.0175  -0.0441 74  VAL A O   
615  C CB  . VAL A 74  ? 0.3617 0.3504 0.3403 0.0098  0.0231  -0.0503 74  VAL A CB  
616  C CG1 . VAL A 74  ? 0.3642 0.3566 0.3413 0.0090  0.0222  -0.0523 74  VAL A CG1 
617  C CG2 . VAL A 74  ? 0.3552 0.3438 0.3338 0.0103  0.0284  -0.0510 74  VAL A CG2 
618  N N   . GLU A 75  ? 0.3789 0.3639 0.3551 0.0089  0.0144  -0.0458 75  GLU A N   
619  C CA  . GLU A 75  ? 0.4063 0.3902 0.3818 0.0079  0.0106  -0.0454 75  GLU A CA  
620  C C   . GLU A 75  ? 0.3982 0.3836 0.3679 0.0079  0.0099  -0.0413 75  GLU A C   
621  O O   . GLU A 75  ? 0.3922 0.3795 0.3591 0.0065  0.0081  -0.0409 75  GLU A O   
622  C CB  . GLU A 75  ? 0.4578 0.4373 0.4386 0.0081  0.0075  -0.0465 75  GLU A CB  
623  C CG  . GLU A 75  ? 0.5759 0.5523 0.5555 0.0073  0.0039  -0.0455 75  GLU A CG  
624  C CD  . GLU A 75  ? 0.6990 0.6714 0.6836 0.0082  0.0022  -0.0477 75  GLU A CD  
625  O OE1 . GLU A 75  ? 0.7532 0.7264 0.7434 0.0100  0.0022  -0.0491 75  GLU A OE1 
626  O OE2 . GLU A 75  ? 0.7079 0.6767 0.6909 0.0071  0.0013  -0.0482 75  GLU A OE2 
627  N N   . LYS A 76  ? 0.3777 0.3622 0.3456 0.0091  0.0120  -0.0384 76  LYS A N   
628  C CA  . LYS A 76  ? 0.3833 0.3696 0.3457 0.0098  0.0122  -0.0343 76  LYS A CA  
629  C C   . LYS A 76  ? 0.3895 0.3829 0.3473 0.0111  0.0142  -0.0328 76  LYS A C   
630  O O   . LYS A 76  ? 0.3686 0.3670 0.3230 0.0107  0.0127  -0.0311 76  LYS A O   
631  C CB  . LYS A 76  ? 0.3960 0.3788 0.3573 0.0111  0.0153  -0.0319 76  LYS A CB  
632  C CG  . LYS A 76  ? 0.4250 0.4034 0.3894 0.0094  0.0128  -0.0328 76  LYS A CG  
633  C CD  . LYS A 76  ? 0.4647 0.4398 0.4266 0.0097  0.0163  -0.0306 76  LYS A CD  
634  C CE  . LYS A 76  ? 0.4677 0.4405 0.4311 0.0076  0.0129  -0.0311 76  LYS A CE  
635  N NZ  . LYS A 76  ? 0.4599 0.4292 0.4205 0.0071  0.0167  -0.0296 76  LYS A NZ  
636  N N   . ILE A 77  ? 0.3905 0.3856 0.3483 0.0124  0.0178  -0.0336 77  ILE A N   
637  C CA  . ILE A 77  ? 0.3728 0.3759 0.3259 0.0141  0.0200  -0.0318 77  ILE A CA  
638  C C   . ILE A 77  ? 0.3856 0.3948 0.3387 0.0112  0.0168  -0.0349 77  ILE A C   
639  O O   . ILE A 77  ? 0.4196 0.4380 0.3683 0.0114  0.0166  -0.0333 77  ILE A O   
640  C CB  . ILE A 77  ? 0.3679 0.3708 0.3212 0.0157  0.0246  -0.0325 77  ILE A CB  
641  C CG1 . ILE A 77  ? 0.3580 0.3545 0.3095 0.0183  0.0293  -0.0290 77  ILE A CG1 
642  C CG2 . ILE A 77  ? 0.3323 0.3453 0.2811 0.0169  0.0260  -0.0316 77  ILE A CG2 
643  C CD1 . ILE A 77  ? 0.3616 0.3563 0.3126 0.0196  0.0347  -0.0294 77  ILE A CD1 
644  N N   . LEU A 78  ? 0.3598 0.3641 0.3179 0.0084  0.0146  -0.0395 78  LEU A N   
645  C CA  . LEU A 78  ? 0.3761 0.3837 0.3340 0.0048  0.0127  -0.0433 78  LEU A CA  
646  C C   . LEU A 78  ? 0.3864 0.3949 0.3420 0.0028  0.0098  -0.0421 78  LEU A C   
647  O O   . LEU A 78  ? 0.3912 0.4035 0.3453 -0.0007 0.0090  -0.0451 78  LEU A O   
648  C CB  . LEU A 78  ? 0.3507 0.3513 0.3142 0.0032  0.0122  -0.0481 78  LEU A CB  
649  C CG  . LEU A 78  ? 0.3474 0.3495 0.3130 0.0038  0.0152  -0.0509 78  LEU A CG  
650  C CD1 . LEU A 78  ? 0.3378 0.3324 0.3098 0.0032  0.0146  -0.0549 78  LEU A CD1 
651  C CD2 . LEU A 78  ? 0.3463 0.3578 0.3077 0.0017  0.0167  -0.0530 78  LEU A CD2 
652  N N   . THR A 79  ? 0.3766 0.3816 0.3317 0.0046  0.0087  -0.0382 79  THR A N   
653  C CA  . THR A 79  ? 0.3959 0.4004 0.3492 0.0026  0.0060  -0.0371 79  THR A CA  
654  C C   . THR A 79  ? 0.4000 0.4091 0.3493 0.0052  0.0066  -0.0320 79  THR A C   
655  O O   . THR A 79  ? 0.3712 0.3791 0.3193 0.0042  0.0047  -0.0304 79  THR A O   
656  C CB  . THR A 79  ? 0.4176 0.4115 0.3747 0.0019  0.0035  -0.0377 79  THR A CB  
657  O OG1 . THR A 79  ? 0.4354 0.4252 0.3946 0.0047  0.0044  -0.0356 79  THR A OG1 
658  C CG2 . THR A 79  ? 0.3917 0.3804 0.3526 0.0001  0.0031  -0.0422 79  THR A CG2 
659  N N   . GLN A 80  ? 0.4034 0.4178 0.3504 0.0089  0.0099  -0.0293 80  GLN A N   
660  C CA  . GLN A 80  ? 0.4072 0.4236 0.3507 0.0128  0.0120  -0.0239 80  GLN A CA  
661  C C   . GLN A 80  ? 0.4143 0.4394 0.3543 0.0123  0.0103  -0.0219 80  GLN A C   
662  O O   . GLN A 80  ? 0.4199 0.4529 0.3593 0.0090  0.0084  -0.0247 80  GLN A O   
663  C CB  . GLN A 80  ? 0.4001 0.4206 0.3410 0.0172  0.0165  -0.0210 80  GLN A CB  
664  C CG  . GLN A 80  ? 0.4330 0.4658 0.3717 0.0168  0.0166  -0.0224 80  GLN A CG  
665  C CD  . GLN A 80  ? 0.4447 0.4809 0.3805 0.0215  0.0212  -0.0193 80  GLN A CD  
666  O OE1 . GLN A 80  ? 0.4330 0.4734 0.3645 0.0267  0.0242  -0.0135 80  GLN A OE1 
667  N NE2 . GLN A 80  ? 0.4540 0.4878 0.3919 0.0202  0.0224  -0.0228 80  GLN A NE2 
668  N N   . SER A 81  ? 0.3892 0.4131 0.3272 0.0153  0.0115  -0.0174 81  SER A N   
669  C CA  . SER A 81  ? 0.4123 0.4468 0.3465 0.0167  0.0112  -0.0143 81  SER A CA  
670  C C   . SER A 81  ? 0.4338 0.4759 0.3643 0.0233  0.0157  -0.0091 81  SER A C   
671  O O   . SER A 81  ? 0.4782 0.5136 0.4087 0.0263  0.0193  -0.0077 81  SER A O   
672  C CB  . SER A 81  ? 0.3956 0.4238 0.3297 0.0164  0.0103  -0.0123 81  SER A CB  
673  O OG  . SER A 81  ? 0.3782 0.4025 0.3144 0.0109  0.0062  -0.0160 81  SER A OG  
674  N N   . SER A 82  ? 0.4196 0.4757 0.3467 0.0259  0.0158  -0.0060 82  SER A N   
675  C CA  . SER A 82  ? 0.4254 0.4880 0.3484 0.0338  0.0204  0.0004  82  SER A CA  
676  C C   . SER A 82  ? 0.4262 0.4749 0.3486 0.0376  0.0246  0.0043  82  SER A C   
677  O O   . SER A 82  ? 0.4504 0.4924 0.3741 0.0352  0.0231  0.0036  82  SER A O   
678  C CB  . SER A 82  ? 0.4373 0.5183 0.3573 0.0363  0.0195  0.0034  82  SER A CB  
679  O OG  . SER A 82  ? 0.4697 0.5660 0.3895 0.0329  0.0168  -0.0002 82  SER A OG  
680  N N   . PHE A 83  ? 0.4327 0.4764 0.3526 0.0431  0.0303  0.0082  83  PHE A N   
681  C CA  . PHE A 83  ? 0.4383 0.4689 0.3564 0.0472  0.0361  0.0122  83  PHE A CA  
682  C C   . PHE A 83  ? 0.4250 0.4387 0.3467 0.0421  0.0365  0.0077  83  PHE A C   
683  O O   . PHE A 83  ? 0.4235 0.4258 0.3438 0.0440  0.0418  0.0097  83  PHE A O   
684  C CB  . PHE A 83  ? 0.4908 0.5249 0.4070 0.0499  0.0364  0.0159  83  PHE A CB  
685  C CG  . PHE A 83  ? 0.5203 0.5709 0.4324 0.0572  0.0380  0.0221  83  PHE A CG  
686  C CD1 . PHE A 83  ? 0.5511 0.6012 0.4585 0.0660  0.0451  0.0289  83  PHE A CD1 
687  C CD2 . PHE A 83  ? 0.5380 0.6050 0.4506 0.0555  0.0329  0.0213  83  PHE A CD2 
688  C CE1 . PHE A 83  ? 0.5563 0.6234 0.4598 0.0738  0.0465  0.0353  83  PHE A CE1 
689  C CE2 . PHE A 83  ? 0.5454 0.6304 0.4546 0.0624  0.0342  0.0268  83  PHE A CE2 
690  C CZ  . PHE A 83  ? 0.5478 0.6336 0.4525 0.0720  0.0408  0.0342  83  PHE A CZ  
691  N N   . GLU A 84  ? 0.4010 0.4137 0.3273 0.0357  0.0312  0.0016  84  GLU A N   
692  C CA  . GLU A 84  ? 0.4133 0.4131 0.3435 0.0312  0.0307  -0.0025 84  GLU A CA  
693  C C   . GLU A 84  ? 0.4313 0.4231 0.3613 0.0326  0.0364  -0.0026 84  GLU A C   
694  O O   . GLU A 84  ? 0.4388 0.4355 0.3675 0.0349  0.0382  -0.0018 84  GLU A O   
695  C CB  . GLU A 84  ? 0.4214 0.4228 0.3565 0.0251  0.0240  -0.0083 84  GLU A CB  
696  C CG  . GLU A 84  ? 0.3914 0.3822 0.3309 0.0210  0.0228  -0.0123 84  GLU A CG  
697  C CD  . GLU A 84  ? 0.4069 0.3988 0.3505 0.0165  0.0165  -0.0167 84  GLU A CD  
698  O OE1 . GLU A 84  ? 0.4270 0.4263 0.3703 0.0157  0.0141  -0.0179 84  GLU A OE1 
699  O OE2 . GLU A 84  ? 0.4121 0.3976 0.3590 0.0136  0.0144  -0.0192 84  GLU A OE2 
700  N N   . CYS A 85  ? 0.4222 0.4024 0.3534 0.0308  0.0395  -0.0040 85  CYS A N   
701  C CA  . CYS A 85  ? 0.4115 0.3831 0.3432 0.0303  0.0450  -0.0056 85  CYS A CA  
702  C C   . CYS A 85  ? 0.4143 0.3805 0.3517 0.0241  0.0419  -0.0116 85  CYS A C   
703  O O   . CYS A 85  ? 0.4277 0.3953 0.3675 0.0211  0.0365  -0.0134 85  CYS A O   
704  C CB  . CYS A 85  ? 0.4113 0.3740 0.3379 0.0341  0.0538  -0.0013 85  CYS A CB  
705  S SG  . CYS A 85  ? 0.4179 0.3877 0.3373 0.0434  0.0581  0.0073  85  CYS A SG  
706  N N   . ILE A 86  ? 0.4299 0.3908 0.3694 0.0222  0.0455  -0.0147 86  ILE A N   
707  C CA  . ILE A 86  ? 0.4174 0.3726 0.3612 0.0170  0.0455  -0.0197 86  ILE A CA  
708  C C   . ILE A 86  ? 0.4388 0.3842 0.3792 0.0172  0.0552  -0.0192 86  ILE A C   
709  O O   . ILE A 86  ? 0.4541 0.3969 0.3892 0.0220  0.0614  -0.0146 86  ILE A O   
710  C CB  . ILE A 86  ? 0.4030 0.3614 0.3530 0.0139  0.0416  -0.0249 86  ILE A CB  
711  C CG1 . ILE A 86  ? 0.4085 0.3684 0.3573 0.0164  0.0452  -0.0242 86  ILE A CG1 
712  C CG2 . ILE A 86  ? 0.4249 0.3901 0.3784 0.0128  0.0329  -0.0262 86  ILE A CG2 
713  C CD1 . ILE A 86  ? 0.3906 0.3476 0.3434 0.0133  0.0481  -0.0290 86  ILE A CD1 
714  N N   . HIS A 87  ? 0.4502 0.3906 0.3934 0.0120  0.0571  -0.0239 87  HIS A N   
715  C CA  . HIS A 87  ? 0.4653 0.3959 0.4061 0.0102  0.0670  -0.0254 87  HIS A CA  
716  C C   . HIS A 87  ? 0.4816 0.4119 0.4243 0.0094  0.0702  -0.0280 87  HIS A C   
717  O O   . HIS A 87  ? 0.4654 0.4025 0.4144 0.0066  0.0644  -0.0324 87  HIS A O   
718  C CB  . HIS A 87  ? 0.4799 0.4073 0.4232 0.0036  0.0679  -0.0308 87  HIS A CB  
719  C CG  . HIS A 87  ? 0.4880 0.4123 0.4277 0.0040  0.0683  -0.0284 87  HIS A CG  
720  N ND1 . HIS A 87  ? 0.4839 0.4152 0.4257 0.0038  0.0596  -0.0278 87  HIS A ND1 
721  C CD2 . HIS A 87  ? 0.4739 0.3879 0.4077 0.0048  0.0772  -0.0262 87  HIS A CD2 
722  C CE1 . HIS A 87  ? 0.4876 0.4143 0.4252 0.0043  0.0625  -0.0255 87  HIS A CE1 
723  N NE2 . HIS A 87  ? 0.4840 0.4001 0.4169 0.0049  0.0733  -0.0247 87  HIS A NE2 
724  N N   . LEU A 88  ? 0.4823 0.4040 0.4194 0.0118  0.0801  -0.0253 88  LEU A N   
725  C CA  . LEU A 88  ? 0.4731 0.3925 0.4109 0.0106  0.0850  -0.0276 88  LEU A CA  
726  C C   . LEU A 88  ? 0.4967 0.4171 0.4413 0.0026  0.0846  -0.0362 88  LEU A C   
727  O O   . LEU A 88  ? 0.4956 0.4200 0.4443 0.0008  0.0838  -0.0397 88  LEU A O   
728  C CB  . LEU A 88  ? 0.4597 0.3668 0.3891 0.0142  0.0973  -0.0230 88  LEU A CB  
729  C CG  . LEU A 88  ? 0.4806 0.3893 0.4036 0.0230  0.0992  -0.0146 88  LEU A CG  
730  C CD1 . LEU A 88  ? 0.4849 0.3797 0.3991 0.0272  0.1121  -0.0092 88  LEU A CD1 
731  C CD2 . LEU A 88  ? 0.4650 0.3812 0.3900 0.0240  0.0964  -0.0153 88  LEU A CD2 
732  N N   . SER A 89  ? 0.4855 0.4036 0.4313 -0.0021 0.0851  -0.0396 89  SER A N   
733  C CA  . SER A 89  ? 0.4841 0.4059 0.4363 -0.0099 0.0844  -0.0479 89  SER A CA  
734  C C   . SER A 89  ? 0.4702 0.4056 0.4309 -0.0109 0.0730  -0.0511 89  SER A C   
735  O O   . SER A 89  ? 0.4742 0.4154 0.4411 -0.0159 0.0720  -0.0574 89  SER A O   
736  C CB  . SER A 89  ? 0.4898 0.4069 0.4405 -0.0151 0.0881  -0.0509 89  SER A CB  
737  O OG  . SER A 89  ? 0.4946 0.4175 0.4465 -0.0138 0.0796  -0.0489 89  SER A OG  
738  N N   . VAL A 90  ? 0.4787 0.4193 0.4397 -0.0061 0.0648  -0.0468 90  VAL A N   
739  C CA  . VAL A 90  ? 0.4865 0.4379 0.4547 -0.0061 0.0550  -0.0490 90  VAL A CA  
740  C C   . VAL A 90  ? 0.4936 0.4482 0.4657 -0.0060 0.0560  -0.0518 90  VAL A C   
741  O O   . VAL A 90  ? 0.5284 0.4913 0.5075 -0.0068 0.0499  -0.0552 90  VAL A O   
742  C CB  . VAL A 90  ? 0.5077 0.4624 0.4744 -0.0012 0.0478  -0.0440 90  VAL A CB  
743  C CG1 . VAL A 90  ? 0.4893 0.4524 0.4628 -0.0012 0.0393  -0.0464 90  VAL A CG1 
744  C CG2 . VAL A 90  ? 0.5081 0.4602 0.4711 -0.0011 0.0465  -0.0411 90  VAL A CG2 
745  N N   . LEU A 91  ? 0.4687 0.4166 0.4359 -0.0046 0.0639  -0.0500 91  LEU A N   
746  C CA  . LEU A 91  ? 0.4651 0.4156 0.4347 -0.0038 0.0651  -0.0516 91  LEU A CA  
747  C C   . LEU A 91  ? 0.5044 0.4546 0.4779 -0.0095 0.0706  -0.0581 91  LEU A C   
748  O O   . LEU A 91  ? 0.5244 0.4771 0.5006 -0.0098 0.0723  -0.0606 91  LEU A O   
749  C CB  . LEU A 91  ? 0.4579 0.4031 0.4199 0.0012  0.0701  -0.0457 91  LEU A CB  
750  C CG  . LEU A 91  ? 0.4462 0.3950 0.4047 0.0068  0.0646  -0.0397 91  LEU A CG  
751  C CD1 . LEU A 91  ? 0.4105 0.3564 0.3614 0.0120  0.0701  -0.0340 91  LEU A CD1 
752  C CD2 . LEU A 91  ? 0.4289 0.3871 0.3934 0.0070  0.0553  -0.0420 91  LEU A CD2 
753  N N   . HIS A 92  ? 0.5257 0.4738 0.4996 -0.0145 0.0736  -0.0615 92  HIS A N   
754  C CA  . HIS A 92  ? 0.5431 0.4934 0.5214 -0.0212 0.0785  -0.0689 92  HIS A CA  
755  C C   . HIS A 92  ? 0.5613 0.5197 0.5452 -0.0267 0.0747  -0.0743 92  HIS A C   
756  O O   . HIS A 92  ? 0.5787 0.5455 0.5691 -0.0315 0.0748  -0.0810 92  HIS A O   
757  C CB  . HIS A 92  ? 0.5425 0.4801 0.5140 -0.0236 0.0913  -0.0690 92  HIS A CB  
758  C CG  . HIS A 92  ? 0.5359 0.4627 0.5003 -0.0246 0.0974  -0.0666 92  HIS A CG  
759  N ND1 . HIS A 92  ? 0.5512 0.4778 0.5169 -0.0316 0.1004  -0.0722 92  HIS A ND1 
760  C CD2 . HIS A 92  ? 0.5413 0.4572 0.4969 -0.0190 0.1017  -0.0590 92  HIS A CD2 
761  C CE1 . HIS A 92  ? 0.5245 0.4392 0.4825 -0.0308 0.1066  -0.0686 92  HIS A CE1 
762  N NE2 . HIS A 92  ? 0.5284 0.4366 0.4804 -0.0226 0.1074  -0.0602 92  HIS A NE2 
763  N N   . LYS A 93  ? 0.5787 0.5361 0.5601 -0.0260 0.0711  -0.0717 93  LYS A N   
764  C CA  . LYS A 93  ? 0.6180 0.5839 0.6038 -0.0311 0.0674  -0.0765 93  LYS A CA  
765  C C   . LYS A 93  ? 0.6158 0.5969 0.6107 -0.0300 0.0574  -0.0788 93  LYS A C   
766  O O   . LYS A 93  ? 0.5958 0.5790 0.5921 -0.0240 0.0505  -0.0745 93  LYS A O   
767  C CB  . LYS A 93  ? 0.6482 0.6099 0.6291 -0.0299 0.0651  -0.0725 93  LYS A CB  
768  C CG  . LYS A 93  ? 0.7062 0.6565 0.6802 -0.0342 0.0752  -0.0735 93  LYS A CG  
769  C CD  . LYS A 93  ? 0.7182 0.6652 0.6878 -0.0321 0.0721  -0.0690 93  LYS A CD  
770  C CE  . LYS A 93  ? 0.7521 0.6941 0.7183 -0.0389 0.0791  -0.0732 93  LYS A CE  
771  N NZ  . LYS A 93  ? 0.7688 0.6945 0.7274 -0.0397 0.0923  -0.0723 93  LYS A NZ  
772  N N   . CYS A 94  ? 0.6401 0.6320 0.6411 -0.0358 0.0572  -0.0858 94  CYS A N   
773  C CA  . CYS A 94  ? 0.6306 0.6387 0.6403 -0.0345 0.0479  -0.0879 94  CYS A CA  
774  C C   . CYS A 94  ? 0.6487 0.6625 0.6646 -0.0304 0.0450  -0.0882 94  CYS A C   
775  O O   . CYS A 94  ? 0.6815 0.7067 0.7040 -0.0272 0.0372  -0.0883 94  CYS A O   
776  C CB  . CYS A 94  ? 0.6740 0.6840 0.6826 -0.0302 0.0392  -0.0827 94  CYS A CB  
777  S SG  . CYS A 94  ? 0.7050 0.7117 0.7077 -0.0350 0.0411  -0.0829 94  CYS A SG  
778  N N   . TYR A 95  ? 0.6207 0.6263 0.6341 -0.0301 0.0515  -0.0882 95  TYR A N   
779  C CA  . TYR A 95  ? 0.6281 0.6395 0.6475 -0.0276 0.0502  -0.0899 95  TYR A CA  
780  C C   . TYR A 95  ? 0.6362 0.6610 0.6637 -0.0330 0.0518  -0.0978 95  TYR A C   
781  O O   . TYR A 95  ? 0.6387 0.6636 0.6649 -0.0402 0.0582  -0.1027 95  TYR A O   
782  C CB  . TYR A 95  ? 0.5992 0.5988 0.6131 -0.0261 0.0572  -0.0876 95  TYR A CB  
783  C CG  . TYR A 95  ? 0.5894 0.5819 0.5984 -0.0194 0.0536  -0.0805 95  TYR A CG  
784  C CD1 . TYR A 95  ? 0.5919 0.5753 0.5930 -0.0177 0.0541  -0.0751 95  TYR A CD1 
785  C CD2 . TYR A 95  ? 0.5927 0.5882 0.6049 -0.0150 0.0501  -0.0796 95  TYR A CD2 
786  C CE1 . TYR A 95  ? 0.5638 0.5428 0.5607 -0.0120 0.0509  -0.0691 95  TYR A CE1 
787  C CE2 . TYR A 95  ? 0.5809 0.5711 0.5885 -0.0099 0.0472  -0.0740 95  TYR A CE2 
788  C CZ  . TYR A 95  ? 0.5824 0.5651 0.5824 -0.0085 0.0474  -0.0688 95  TYR A CZ  
789  O OH  . TYR A 95  ? 0.5742 0.5539 0.5699 -0.0040 0.0446  -0.0638 95  TYR A OH  
790  N N   . ASP A 96  ? 0.6287 0.6651 0.6645 -0.0296 0.0464  -0.0993 96  ASP A N   
791  C CA  . ASP A 96  ? 0.6317 0.6828 0.6760 -0.0338 0.0478  -0.1068 96  ASP A CA  
792  C C   . ASP A 96  ? 0.6248 0.6693 0.6675 -0.0373 0.0570  -0.1101 96  ASP A C   
793  O O   . ASP A 96  ? 0.6380 0.6806 0.6824 -0.0331 0.0567  -0.1088 96  ASP A O   
794  C CB  . ASP A 96  ? 0.6582 0.7230 0.7116 -0.0276 0.0394  -0.1064 96  ASP A CB  
795  C CG  . ASP A 96  ? 0.6803 0.7647 0.7436 -0.0312 0.0393  -0.1138 96  ASP A CG  
796  O OD1 . ASP A 96  ? 0.6746 0.7623 0.7378 -0.0396 0.0460  -0.1201 96  ASP A OD1 
797  O OD2 . ASP A 96  ? 0.6909 0.7877 0.7621 -0.0256 0.0329  -0.1133 96  ASP A OD2 
798  N N   . TYR A 97  ? 0.6086 0.6484 0.6474 -0.0451 0.0657  -0.1144 97  TYR A N   
799  C CA  . TYR A 97  ? 0.6433 0.6737 0.6786 -0.0485 0.0757  -0.1166 97  TYR A CA  
800  C C   . TYR A 97  ? 0.6618 0.7055 0.7060 -0.0517 0.0774  -0.1238 97  TYR A C   
801  O O   . TYR A 97  ? 0.7093 0.7471 0.7522 -0.0513 0.0827  -0.1242 97  TYR A O   
802  C CB  . TYR A 97  ? 0.6280 0.6459 0.6551 -0.0556 0.0860  -0.1183 97  TYR A CB  
803  C CG  . TYR A 97  ? 0.6440 0.6449 0.6608 -0.0510 0.0870  -0.1101 97  TYR A CG  
804  C CD1 . TYR A 97  ? 0.6494 0.6363 0.6592 -0.0466 0.0917  -0.1046 97  TYR A CD1 
805  C CD2 . TYR A 97  ? 0.6356 0.6357 0.6498 -0.0509 0.0832  -0.1078 97  TYR A CD2 
806  C CE1 . TYR A 97  ? 0.6589 0.6326 0.6597 -0.0418 0.0925  -0.0969 97  TYR A CE1 
807  C CE2 . TYR A 97  ? 0.6426 0.6283 0.6479 -0.0465 0.0841  -0.1003 97  TYR A CE2 
808  C CZ  . TYR A 97  ? 0.6851 0.6582 0.6839 -0.0418 0.0887  -0.0948 97  TYR A CZ  
809  O OH  . TYR A 97  ? 0.7018 0.6628 0.6921 -0.0369 0.0896  -0.0873 97  TYR A OH  
810  N N   . ASP A 98  ? 0.6477 0.7105 0.7009 -0.0545 0.0729  -0.1294 98  ASP A N   
811  C CA  . ASP A 98  ? 0.6838 0.7627 0.7467 -0.0573 0.0739  -0.1366 98  ASP A CA  
812  C C   . ASP A 98  ? 0.6745 0.7572 0.7429 -0.0487 0.0683  -0.1336 98  ASP A C   
813  O O   . ASP A 98  ? 0.6858 0.7786 0.7613 -0.0500 0.0703  -0.1387 98  ASP A O   
814  C CB  . ASP A 98  ? 0.7046 0.8058 0.7759 -0.0615 0.0695  -0.1428 98  ASP A CB  
815  C CG  . ASP A 98  ? 0.7529 0.8543 0.8209 -0.0732 0.0781  -0.1500 98  ASP A CG  
816  O OD1 . ASP A 98  ? 0.7580 0.8504 0.8227 -0.0796 0.0887  -0.1542 98  ASP A OD1 
817  O OD2 . ASP A 98  ? 0.7614 0.8717 0.8300 -0.0763 0.0748  -0.1516 98  ASP A OD2 
818  N N   . ALA A 99  ? 0.6386 0.7131 0.7037 -0.0405 0.0619  -0.1257 99  ALA A N   
819  C CA  . ALA A 99  ? 0.6018 0.6797 0.6720 -0.0325 0.0563  -0.1229 99  ALA A CA  
820  C C   . ALA A 99  ? 0.5888 0.6507 0.6521 -0.0296 0.0602  -0.1189 99  ALA A C   
821  O O   . ALA A 99  ? 0.6090 0.6717 0.6754 -0.0237 0.0568  -0.1171 99  ALA A O   
822  C CB  . ALA A 99  ? 0.5744 0.6566 0.6466 -0.0255 0.0463  -0.1176 99  ALA A CB  
823  N N   . ILE A 100 ? 0.5567 0.6042 0.6105 -0.0335 0.0676  -0.1174 100 ILE A N   
824  C CA  . ILE A 100 ? 0.5564 0.5900 0.6027 -0.0307 0.0717  -0.1132 100 ILE A CA  
825  C C   . ILE A 100 ? 0.5811 0.6149 0.6285 -0.0352 0.0802  -0.1183 100 ILE A C   
826  O O   . ILE A 100 ? 0.5989 0.6273 0.6422 -0.0418 0.0886  -0.1213 100 ILE A O   
827  C CB  . ILE A 100 ? 0.5536 0.5712 0.5881 -0.0305 0.0749  -0.1071 100 ILE A CB  
828  C CG1 . ILE A 100 ? 0.5433 0.5611 0.5768 -0.0261 0.0664  -0.1021 100 ILE A CG1 
829  C CG2 . ILE A 100 ? 0.5334 0.5393 0.5601 -0.0273 0.0792  -0.1025 100 ILE A CG2 
830  C CD1 . ILE A 100 ? 0.5352 0.5413 0.5594 -0.0274 0.0694  -0.0978 100 ILE A CD1 
831  N N   . PRO A 101 ? 0.5776 0.6168 0.6303 -0.0318 0.0785  -0.1197 101 PRO A N   
832  C CA  . PRO A 101 ? 0.5841 0.6263 0.6396 -0.0358 0.0857  -0.1254 101 PRO A CA  
833  C C   . PRO A 101 ? 0.5963 0.6232 0.6410 -0.0395 0.0960  -0.1237 101 PRO A C   
834  O O   . PRO A 101 ? 0.6539 0.6810 0.6988 -0.0465 0.1043  -0.1291 101 PRO A O   
835  C CB  . PRO A 101 ? 0.5790 0.6254 0.6392 -0.0296 0.0812  -0.1245 101 PRO A CB  
836  C CG  . PRO A 101 ? 0.5641 0.6162 0.6288 -0.0237 0.0712  -0.1214 101 PRO A CG  
837  C CD  . PRO A 101 ? 0.5700 0.6128 0.6265 -0.0242 0.0700  -0.1163 101 PRO A CD  
838  N N   . TRP A 102 ? 0.5902 0.6044 0.6255 -0.0347 0.0960  -0.1163 102 TRP A N   
839  C CA  . TRP A 102 ? 0.5943 0.5944 0.6188 -0.0363 0.1058  -0.1134 102 TRP A CA  
840  C C   . TRP A 102 ? 0.6316 0.6223 0.6499 -0.0418 0.1133  -0.1136 102 TRP A C   
841  O O   . TRP A 102 ? 0.6291 0.6066 0.6379 -0.0430 0.1228  -0.1109 102 TRP A O   
842  C CB  . TRP A 102 ? 0.5972 0.5889 0.6135 -0.0294 0.1036  -0.1053 102 TRP A CB  
843  C CG  . TRP A 102 ? 0.5823 0.5696 0.5940 -0.0253 0.0978  -0.0990 102 TRP A CG  
844  C CD1 . TRP A 102 ? 0.5845 0.5784 0.6010 -0.0211 0.0875  -0.0973 102 TRP A CD1 
845  C CD2 . TRP A 102 ? 0.6023 0.5770 0.6035 -0.0248 0.1024  -0.0931 102 TRP A CD2 
846  N NE1 . TRP A 102 ? 0.5829 0.5700 0.5928 -0.0186 0.0852  -0.0914 102 TRP A NE1 
847  C CE2 . TRP A 102 ? 0.5928 0.5689 0.5938 -0.0204 0.0937  -0.0887 102 TRP A CE2 
848  C CE3 . TRP A 102 ? 0.6032 0.5655 0.5955 -0.0272 0.1131  -0.0911 102 TRP A CE3 
849  C CZ2 . TRP A 102 ? 0.5923 0.5590 0.5848 -0.0186 0.0953  -0.0827 102 TRP A CZ2 
850  C CZ3 . TRP A 102 ? 0.6058 0.5577 0.5894 -0.0247 0.1150  -0.0847 102 TRP A CZ3 
851  C CH2 . TRP A 102 ? 0.6073 0.5621 0.5914 -0.0205 0.1061  -0.0807 102 TRP A CH2 
852  N N   . LEU A 103 ? 0.6642 0.6619 0.6877 -0.0451 0.1098  -0.1170 103 LEU A N   
853  C CA  . LEU A 103 ? 0.7133 0.7023 0.7310 -0.0507 0.1167  -0.1177 103 LEU A CA  
854  C C   . LEU A 103 ? 0.7730 0.7706 0.7969 -0.0605 0.1221  -0.1276 103 LEU A C   
855  O O   . LEU A 103 ? 0.7532 0.7433 0.7723 -0.0666 0.1293  -0.1297 103 LEU A O   
856  C CB  . LEU A 103 ? 0.6872 0.6752 0.7031 -0.0474 0.1095  -0.1131 103 LEU A CB  
857  C CG  . LEU A 103 ? 0.6857 0.6597 0.6911 -0.0406 0.1092  -0.1034 103 LEU A CG  
858  C CD1 . LEU A 103 ? 0.6551 0.6304 0.6602 -0.0381 0.1017  -0.0999 103 LEU A CD1 
859  C CD2 . LEU A 103 ? 0.6793 0.6361 0.6735 -0.0426 0.1218  -0.1006 103 LEU A CD2 
860  N N   . GLN A 104 ? 0.8453 0.8585 0.8796 -0.0621 0.1193  -0.1339 104 GLN A N   
861  C CA  . GLN A 104 ? 0.8927 0.9189 0.9346 -0.0714 0.1231  -0.1441 104 GLN A CA  
862  C C   . GLN A 104 ? 0.9062 0.9213 0.9419 -0.0802 0.1376  -0.1487 104 GLN A C   
863  O O   . GLN A 104 ? 0.8897 0.9088 0.9269 -0.0895 0.1432  -0.1559 104 GLN A O   
864  C CB  . GLN A 104 ? 0.9127 0.9596 0.9676 -0.0699 0.1166  -0.1493 104 GLN A CB  
865  C CG  . GLN A 104 ? 0.9791 1.0394 1.0417 -0.0625 0.1031  -0.1464 104 GLN A CG  
866  C CD  . GLN A 104 ? 1.0363 1.1040 1.1005 -0.0657 0.0992  -0.1480 104 GLN A CD  
867  O OE1 . GLN A 104 ? 1.0613 1.1169 1.1175 -0.0644 0.0987  -0.1426 104 GLN A OE1 
868  N NE2 . GLN A 104 ? 1.0412 1.1303 1.1160 -0.0696 0.0963  -0.1553 104 GLN A NE2 
869  N N   . ASN A 105 ? 0.9456 0.9467 0.9738 -0.0777 0.1443  -0.1445 105 ASN A N   
870  C CA  . ASN A 105 ? 1.0148 1.0024 1.0354 -0.0851 0.1592  -0.1476 105 ASN A CA  
871  C C   . ASN A 105 ? 1.0129 0.9798 1.0211 -0.0871 0.1681  -0.1433 105 ASN A C   
872  O O   . ASN A 105 ? 1.0241 0.9758 1.0240 -0.0922 0.1816  -0.1444 105 ASN A O   
873  C CB  . ASN A 105 ? 1.0891 1.0701 1.1060 -0.0814 0.1634  -0.1445 105 ASN A CB  
874  C CG  . ASN A 105 ? 1.1562 1.1300 1.1672 -0.0700 0.1567  -0.1337 105 ASN A CG  
875  O OD1 . ASN A 105 ? 1.0982 1.0675 1.1056 -0.0651 0.1512  -0.1275 105 ASN A OD1 
876  N ND2 . ASN A 105 ? 1.1589 1.1324 1.1689 -0.0663 0.1575  -0.1318 105 ASN A ND2 
877  N N   . VAL A 106 ? 0.9849 0.9506 0.9915 -0.0828 0.1609  -0.1384 106 VAL A N   
878  C CA  . VAL A 106 ? 0.9714 0.9188 0.9671 -0.0836 0.1682  -0.1342 106 VAL A CA  
879  C C   . VAL A 106 ? 0.9730 0.9292 0.9736 -0.0911 0.1665  -0.1410 106 VAL A C   
880  O O   . VAL A 106 ? 0.9380 0.9115 0.9475 -0.0889 0.1541  -0.1423 106 VAL A O   
881  C CB  . VAL A 106 ? 0.9503 0.8890 0.9393 -0.0722 0.1616  -0.1223 106 VAL A CB  
882  C CG1 . VAL A 106 ? 0.9467 0.8656 0.9239 -0.0721 0.1703  -0.1173 106 VAL A CG1 
883  C CG2 . VAL A 106 ? 0.9086 0.8439 0.8942 -0.0645 0.1607  -0.1160 106 VAL A CG2 
884  N N   . GLU A 107 ? 1.0094 0.9538 1.0039 -0.1000 0.1792  -0.1455 107 GLU A N   
885  C CA  . GLU A 107 ? 1.0588 1.0118 1.0571 -0.1082 0.1785  -0.1528 107 GLU A CA  
886  C C   . GLU A 107 ? 1.0119 0.9627 1.0076 -0.1017 0.1700  -0.1458 107 GLU A C   
887  O O   . GLU A 107 ? 0.9527 0.8856 0.9386 -0.0944 0.1723  -0.1363 107 GLU A O   
888  C CB  . GLU A 107 ? 1.1883 1.1290 1.1806 -0.1208 0.1953  -0.1607 107 GLU A CB  
889  C CG  . GLU A 107 ? 1.2892 1.2027 1.2675 -0.1195 0.2064  -0.1544 107 GLU A CG  
890  C CD  . GLU A 107 ? 1.3830 1.2748 1.3508 -0.1148 0.2173  -0.1474 107 GLU A CD  
891  O OE1 . GLU A 107 ? 1.4168 1.3106 1.3849 -0.1044 0.2100  -0.1395 107 GLU A OE1 
892  O OE2 . GLU A 107 ? 1.3949 1.2677 1.3538 -0.1215 0.2336  -0.1499 107 GLU A OE2 
893  N N   . PRO A 108 ? 0.9895 0.9596 0.9939 -0.1041 0.1599  -0.1504 108 PRO A N   
894  C CA  . PRO A 108 ? 0.9714 0.9456 0.9764 -0.0974 0.1486  -0.1445 108 PRO A CA  
895  C C   . PRO A 108 ? 0.9862 0.9387 0.9794 -0.0929 0.1531  -0.1361 108 PRO A C   
896  O O   . PRO A 108 ? 0.9441 0.8955 0.9360 -0.0833 0.1440  -0.1276 108 PRO A O   
897  C CB  . PRO A 108 ? 0.9675 0.9601 0.9798 -0.1064 0.1455  -0.1539 108 PRO A CB  
898  C CG  . PRO A 108 ? 0.9603 0.9692 0.9815 -0.1131 0.1475  -0.1633 108 PRO A CG  
899  C CD  . PRO A 108 ? 0.9675 0.9595 0.9826 -0.1137 0.1590  -0.1622 108 PRO A CD  
900  N N   . ASN A 109 ? 1.0263 0.9616 1.0109 -0.0997 0.1675  -0.1386 109 ASN A N   
901  C CA  . ASN A 109 ? 1.0459 0.9613 1.0196 -0.0961 0.1730  -0.1316 109 ASN A CA  
902  C C   . ASN A 109 ? 0.9995 0.8986 0.9647 -0.0843 0.1742  -0.1194 109 ASN A C   
903  O O   . ASN A 109 ? 1.0283 0.9164 0.9866 -0.0784 0.1741  -0.1118 109 ASN A O   
904  C CB  . ASN A 109 ? 1.0933 0.9945 1.0603 -0.1072 0.1889  -0.1384 109 ASN A CB  
905  C CG  . ASN A 109 ? 1.1886 1.0790 1.1521 -0.1130 0.2030  -0.1426 109 ASN A CG  
906  O OD1 . ASN A 109 ? 1.2090 1.0792 1.1629 -0.1074 0.2120  -0.1352 109 ASN A OD1 
907  N ND2 . ASN A 109 ? 1.1994 1.1040 1.1704 -0.1243 0.2054  -0.1545 109 ASN A ND2 
908  N N   . LEU A 110 ? 0.9229 0.8219 0.8886 -0.0811 0.1753  -0.1175 110 LEU A N   
909  C CA  . LEU A 110 ? 0.8588 0.7463 0.8170 -0.0699 0.1756  -0.1062 110 LEU A CA  
910  C C   . LEU A 110 ? 0.8233 0.7254 0.7876 -0.0609 0.1598  -0.1011 110 LEU A C   
911  O O   . LEU A 110 ? 0.8368 0.7327 0.7954 -0.0516 0.1579  -0.0918 110 LEU A O   
912  C CB  . LEU A 110 ? 0.8781 0.7555 0.8315 -0.0710 0.1868  -0.1063 110 LEU A CB  
913  C CG  . LEU A 110 ? 0.8924 0.7485 0.8359 -0.0772 0.2054  -0.1081 110 LEU A CG  
914  C CD1 . LEU A 110 ? 0.8866 0.7293 0.8216 -0.0714 0.2138  -0.1013 110 LEU A CD1 
915  C CD2 . LEU A 110 ? 0.8945 0.7356 0.8299 -0.0761 0.2110  -0.1042 110 LEU A CD2 
916  N N   . ARG A 111 ? 0.7538 0.6754 0.7294 -0.0637 0.1490  -0.1070 111 ARG A N   
917  C CA  . ARG A 111 ? 0.7207 0.6557 0.7026 -0.0562 0.1353  -0.1034 111 ARG A CA  
918  C C   . ARG A 111 ? 0.7221 0.6532 0.6996 -0.0476 0.1281  -0.0943 111 ARG A C   
919  O O   . ARG A 111 ? 0.7187 0.6486 0.6937 -0.0398 0.1242  -0.0876 111 ARG A O   
920  C CB  . ARG A 111 ? 0.6948 0.6507 0.6893 -0.0604 0.1261  -0.1112 111 ARG A CB  
921  C CG  . ARG A 111 ? 0.7078 0.6725 0.7088 -0.0654 0.1294  -0.1186 111 ARG A CG  
922  C CD  . ARG A 111 ? 0.7084 0.6948 0.7216 -0.0699 0.1218  -0.1265 111 ARG A CD  
923  N NE  . ARG A 111 ? 0.7253 0.7204 0.7445 -0.0763 0.1270  -0.1348 111 ARG A NE  
924  C CZ  . ARG A 111 ? 0.7093 0.7255 0.7398 -0.0801 0.1217  -0.1423 111 ARG A CZ  
925  N NH1 . ARG A 111 ? 0.7292 0.7595 0.7659 -0.0778 0.1110  -0.1422 111 ARG A NH1 
926  N NH2 . ARG A 111 ? 0.6573 0.6811 0.6930 -0.0860 0.1272  -0.1498 111 ARG A NH2 
927  N N   . PRO A 112 ? 0.6731 0.6031 0.6494 -0.0495 0.1265  -0.0944 112 PRO A N   
928  C CA  . PRO A 112 ? 0.6544 0.5820 0.6271 -0.0418 0.1195  -0.0863 112 PRO A CA  
929  C C   . PRO A 112 ? 0.6516 0.5657 0.6144 -0.0343 0.1246  -0.0772 112 PRO A C   
930  O O   . PRO A 112 ? 0.6700 0.5877 0.6323 -0.0268 0.1169  -0.0710 112 PRO A O   
931  C CB  . PRO A 112 ? 0.6864 0.6105 0.6570 -0.0466 0.1218  -0.0885 112 PRO A CB  
932  C CG  . PRO A 112 ? 0.6796 0.6153 0.6582 -0.0562 0.1222  -0.0990 112 PRO A CG  
933  C CD  . PRO A 112 ? 0.6807 0.6155 0.6606 -0.0589 0.1291  -0.1027 112 PRO A CD  
934  N N   . LYS A 113 ? 0.6886 0.5879 0.6438 -0.0361 0.1379  -0.0765 113 LYS A N   
935  C CA  . LYS A 113 ? 0.7122 0.5989 0.6572 -0.0281 0.1439  -0.0671 113 LYS A CA  
936  C C   . LYS A 113 ? 0.6752 0.5686 0.6214 -0.0227 0.1393  -0.0639 113 LYS A C   
937  O O   . LYS A 113 ? 0.6581 0.5507 0.5992 -0.0143 0.1365  -0.0557 113 LYS A O   
938  C CB  . LYS A 113 ? 0.7931 0.6617 0.7296 -0.0315 0.1603  -0.0674 113 LYS A CB  
939  C CG  . LYS A 113 ? 0.8777 0.7312 0.8024 -0.0228 0.1675  -0.0567 113 LYS A CG  
940  C CD  . LYS A 113 ? 0.9539 0.7942 0.8732 -0.0254 0.1755  -0.0567 113 LYS A CD  
941  C CE  . LYS A 113 ? 0.9725 0.8230 0.8970 -0.0252 0.1642  -0.0573 113 LYS A CE  
942  N NZ  . LYS A 113 ? 1.0363 0.8786 0.9594 -0.0325 0.1710  -0.0626 113 LYS A NZ  
943  N N   . LEU A 114 ? 0.6461 0.5471 0.5990 -0.0276 0.1389  -0.0708 114 LEU A N   
944  C CA  . LEU A 114 ? 0.6261 0.5340 0.5808 -0.0235 0.1350  -0.0691 114 LEU A CA  
945  C C   . LEU A 114 ? 0.5905 0.5121 0.5513 -0.0188 0.1208  -0.0675 114 LEU A C   
946  O O   . LEU A 114 ? 0.5824 0.5056 0.5397 -0.0121 0.1173  -0.0614 114 LEU A O   
947  C CB  . LEU A 114 ? 0.6380 0.5507 0.5987 -0.0303 0.1387  -0.0774 114 LEU A CB  
948  C CG  . LEU A 114 ? 0.6837 0.5824 0.6364 -0.0325 0.1532  -0.0769 114 LEU A CG  
949  C CD1 . LEU A 114 ? 0.6846 0.5891 0.6443 -0.0412 0.1571  -0.0868 114 LEU A CD1 
950  C CD2 . LEU A 114 ? 0.6996 0.5938 0.6444 -0.0242 0.1549  -0.0684 114 LEU A CD2 
951  N N   . LEU A 115 ? 0.5601 0.4916 0.5296 -0.0225 0.1130  -0.0728 115 LEU A N   
952  C CA  . LEU A 115 ? 0.5472 0.4898 0.5222 -0.0184 0.1005  -0.0713 115 LEU A CA  
953  C C   . LEU A 115 ? 0.5413 0.4793 0.5091 -0.0117 0.0977  -0.0628 115 LEU A C   
954  O O   . LEU A 115 ? 0.5898 0.5332 0.5575 -0.0066 0.0914  -0.0593 115 LEU A O   
955  C CB  . LEU A 115 ? 0.5371 0.4894 0.5208 -0.0227 0.0937  -0.0770 115 LEU A CB  
956  C CG  . LEU A 115 ? 0.5477 0.5105 0.5371 -0.0184 0.0815  -0.0756 115 LEU A CG  
957  C CD1 . LEU A 115 ? 0.5213 0.4913 0.5157 -0.0161 0.0780  -0.0772 115 LEU A CD1 
958  C CD2 . LEU A 115 ? 0.5472 0.5188 0.5437 -0.0219 0.0756  -0.0800 115 LEU A CD2 
959  N N   . LEU A 116 ? 0.5047 0.4329 0.4661 -0.0118 0.1032  -0.0598 116 LEU A N   
960  C CA  . LEU A 116 ? 0.5100 0.4340 0.4643 -0.0054 0.1018  -0.0516 116 LEU A CA  
961  C C   . LEU A 116 ? 0.5101 0.4319 0.4577 0.0007  0.1051  -0.0454 116 LEU A C   
962  O O   . LEU A 116 ? 0.4937 0.4213 0.4397 0.0062  0.0989  -0.0406 116 LEU A O   
963  C CB  . LEU A 116 ? 0.5024 0.4146 0.4506 -0.0066 0.1094  -0.0497 116 LEU A CB  
964  C CG  . LEU A 116 ? 0.5144 0.4212 0.4543 0.0007  0.1103  -0.0406 116 LEU A CG  
965  C CD1 . LEU A 116 ? 0.4940 0.4105 0.4378 0.0027  0.0987  -0.0394 116 LEU A CD1 
966  C CD2 . LEU A 116 ? 0.5068 0.3986 0.4393 0.0001  0.1215  -0.0384 116 LEU A CD2 
967  N N   . LYS A 117 ? 0.5432 0.4571 0.4867 -0.0004 0.1151  -0.0458 117 LYS A N   
968  C CA  . LYS A 117 ? 0.5756 0.4869 0.5117 0.0055  0.1196  -0.0394 117 LYS A CA  
969  C C   . LYS A 117 ? 0.5496 0.4738 0.4902 0.0073  0.1113  -0.0406 117 LYS A C   
970  O O   . LYS A 117 ? 0.5371 0.4656 0.4728 0.0134  0.1090  -0.0346 117 LYS A O   
971  C CB  . LYS A 117 ? 0.6090 0.5084 0.5401 0.0027  0.1325  -0.0405 117 LYS A CB  
972  C CG  . LYS A 117 ? 0.6650 0.5591 0.5863 0.0096  0.1394  -0.0326 117 LYS A CG  
973  C CD  . LYS A 117 ? 0.6914 0.5799 0.6117 0.0054  0.1484  -0.0364 117 LYS A CD  
974  C CE  . LYS A 117 ? 0.7571 0.6318 0.6648 0.0108  0.1609  -0.0283 117 LYS A CE  
975  N NZ  . LYS A 117 ? 0.8474 0.7110 0.7535 0.0045  0.1727  -0.0331 117 LYS A NZ  
976  N N   . HIS A 118 ? 0.5340 0.4653 0.4840 0.0019  0.1071  -0.0485 118 HIS A N   
977  C CA  . HIS A 118 ? 0.5411 0.4836 0.4960 0.0031  0.0999  -0.0506 118 HIS A CA  
978  C C   . HIS A 118 ? 0.5253 0.4764 0.4836 0.0056  0.0891  -0.0494 118 HIS A C   
979  O O   . HIS A 118 ? 0.5511 0.5086 0.5079 0.0091  0.0851  -0.0471 118 HIS A O   
980  C CB  . HIS A 118 ? 0.5436 0.4906 0.5073 -0.0026 0.1000  -0.0590 118 HIS A CB  
981  C CG  . HIS A 118 ? 0.5825 0.5222 0.5425 -0.0053 0.1110  -0.0605 118 HIS A CG  
982  N ND1 . HIS A 118 ? 0.6001 0.5441 0.5623 -0.0063 0.1125  -0.0636 118 HIS A ND1 
983  C CD2 . HIS A 118 ? 0.5931 0.5202 0.5465 -0.0073 0.1219  -0.0591 118 HIS A CD2 
984  C CE1 . HIS A 118 ? 0.6096 0.5445 0.5669 -0.0089 0.1235  -0.0641 118 HIS A CE1 
985  N NE2 . HIS A 118 ? 0.5901 0.5141 0.5417 -0.0095 0.1295  -0.0612 118 HIS A NE2 
986  N N   . ASN A 119 ? 0.4949 0.4461 0.4571 0.0035  0.0848  -0.0510 119 ASN A N   
987  C CA  . ASN A 119 ? 0.4695 0.4266 0.4334 0.0060  0.0757  -0.0490 119 ASN A CA  
988  C C   . ASN A 119 ? 0.4651 0.4214 0.4203 0.0117  0.0764  -0.0414 119 ASN A C   
989  O O   . ASN A 119 ? 0.4634 0.4274 0.4186 0.0141  0.0705  -0.0400 119 ASN A O   
990  C CB  . ASN A 119 ? 0.4738 0.4297 0.4413 0.0032  0.0725  -0.0508 119 ASN A CB  
991  C CG  . ASN A 119 ? 0.4542 0.4170 0.4318 -0.0006 0.0671  -0.0576 119 ASN A CG  
992  O OD1 . ASN A 119 ? 0.5080 0.4719 0.4890 -0.0031 0.0642  -0.0596 119 ASN A OD1 
993  N ND2 . ASN A 119 ? 0.4248 0.3929 0.4071 -0.0009 0.0659  -0.0611 119 ASN A ND2 
994  N N   . LEU A 120 ? 0.4356 0.3833 0.3834 0.0137  0.0839  -0.0365 120 LEU A N   
995  C CA  . LEU A 120 ? 0.4501 0.3984 0.3895 0.0202  0.0852  -0.0286 120 LEU A CA  
996  C C   . LEU A 120 ? 0.4710 0.4265 0.4076 0.0231  0.0852  -0.0269 120 LEU A C   
997  O O   . LEU A 120 ? 0.5025 0.4667 0.4365 0.0267  0.0805  -0.0235 120 LEU A O   
998  C CB  . LEU A 120 ? 0.4582 0.3946 0.3896 0.0228  0.0950  -0.0233 120 LEU A CB  
999  C CG  . LEU A 120 ? 0.4623 0.3926 0.3936 0.0217  0.0952  -0.0226 120 LEU A CG  
1000 C CD1 . LEU A 120 ? 0.4705 0.3867 0.3938 0.0238  0.1072  -0.0183 120 LEU A CD1 
1001 C CD2 . LEU A 120 ? 0.4305 0.3687 0.3612 0.0255  0.0873  -0.0186 120 LEU A CD2 
1002 N N   . PHE A 121 ? 0.4676 0.4203 0.4046 0.0210  0.0905  -0.0298 121 PHE A N   
1003 C CA  . PHE A 121 ? 0.4750 0.4347 0.4092 0.0234  0.0908  -0.0286 121 PHE A CA  
1004 C C   . PHE A 121 ? 0.4572 0.4288 0.3973 0.0221  0.0811  -0.0324 121 PHE A C   
1005 O O   . PHE A 121 ? 0.4647 0.4449 0.4006 0.0254  0.0782  -0.0290 121 PHE A O   
1006 C CB  . PHE A 121 ? 0.4778 0.4329 0.4126 0.0204  0.0978  -0.0322 121 PHE A CB  
1007 C CG  . PHE A 121 ? 0.4703 0.4330 0.4021 0.0224  0.0981  -0.0315 121 PHE A CG  
1008 C CD1 . PHE A 121 ? 0.4486 0.4210 0.3872 0.0197  0.0913  -0.0374 121 PHE A CD1 
1009 C CD2 . PHE A 121 ? 0.4807 0.4411 0.4024 0.0274  0.1055  -0.0246 121 PHE A CD2 
1010 C CE1 . PHE A 121 ? 0.4594 0.4392 0.3949 0.0209  0.0918  -0.0372 121 PHE A CE1 
1011 C CE2 . PHE A 121 ? 0.4637 0.4326 0.3821 0.0291  0.1055  -0.0238 121 PHE A CE2 
1012 C CZ  . PHE A 121 ? 0.4575 0.4363 0.3830 0.0254  0.0986  -0.0306 121 PHE A CZ  
1013 N N   . LEU A 122 ? 0.4565 0.4289 0.4058 0.0173  0.0764  -0.0394 122 LEU A N   
1014 C CA  . LEU A 122 ? 0.4387 0.4200 0.3937 0.0160  0.0680  -0.0432 122 LEU A CA  
1015 C C   . LEU A 122 ? 0.4471 0.4334 0.3989 0.0186  0.0625  -0.0392 122 LEU A C   
1016 O O   . LEU A 122 ? 0.4688 0.4635 0.4188 0.0195  0.0594  -0.0391 122 LEU A O   
1017 C CB  . LEU A 122 ? 0.4201 0.4006 0.3851 0.0119  0.0640  -0.0498 122 LEU A CB  
1018 C CG  . LEU A 122 ? 0.4278 0.4074 0.3980 0.0088  0.0679  -0.0554 122 LEU A CG  
1019 C CD1 . LEU A 122 ? 0.4017 0.3819 0.3815 0.0055  0.0642  -0.0609 122 LEU A CD1 
1020 C CD2 . LEU A 122 ? 0.4198 0.4055 0.3903 0.0091  0.0676  -0.0577 122 LEU A CD2 
1021 N N   . LEU A 123 ? 0.4630 0.4448 0.4138 0.0194  0.0618  -0.0363 123 LEU A N   
1022 C CA  . LEU A 123 ? 0.4478 0.4346 0.3961 0.0214  0.0568  -0.0329 123 LEU A CA  
1023 C C   . LEU A 123 ? 0.4556 0.4487 0.3954 0.0262  0.0593  -0.0268 123 LEU A C   
1024 O O   . LEU A 123 ? 0.4655 0.4679 0.4039 0.0270  0.0546  -0.0259 123 LEU A O   
1025 C CB  . LEU A 123 ? 0.4425 0.4229 0.3908 0.0215  0.0564  -0.0308 123 LEU A CB  
1026 C CG  . LEU A 123 ? 0.4503 0.4264 0.4062 0.0172  0.0532  -0.0358 123 LEU A CG  
1027 C CD1 . LEU A 123 ? 0.4456 0.4146 0.3990 0.0175  0.0559  -0.0329 123 LEU A CD1 
1028 C CD2 . LEU A 123 ? 0.4224 0.4040 0.3835 0.0155  0.0450  -0.0389 123 LEU A CD2 
1029 N N   . ASP A 124 ? 0.4575 0.4460 0.3913 0.0294  0.0669  -0.0225 124 ASP A N   
1030 C CA  . ASP A 124 ? 0.4621 0.4571 0.3872 0.0354  0.0698  -0.0153 124 ASP A CA  
1031 C C   . ASP A 124 ? 0.4545 0.4605 0.3783 0.0353  0.0686  -0.0169 124 ASP A C   
1032 O O   . ASP A 124 ? 0.4618 0.4799 0.3811 0.0382  0.0663  -0.0137 124 ASP A O   
1033 C CB  . ASP A 124 ? 0.4851 0.4700 0.4033 0.0399  0.0795  -0.0091 124 ASP A CB  
1034 C CG  . ASP A 124 ? 0.5192 0.4950 0.4360 0.0416  0.0816  -0.0056 124 ASP A CG  
1035 O OD1 . ASP A 124 ? 0.5042 0.4851 0.4222 0.0421  0.0759  -0.0046 124 ASP A OD1 
1036 O OD2 . ASP A 124 ? 0.5314 0.4944 0.4454 0.0422  0.0899  -0.0039 124 ASP A OD2 
1037 N N   . ASN A 125 ? 0.4444 0.4473 0.3721 0.0316  0.0702  -0.0224 125 ASN A N   
1038 C CA  . ASN A 125 ? 0.4454 0.4574 0.3711 0.0313  0.0707  -0.0242 125 ASN A CA  
1039 C C   . ASN A 125 ? 0.4367 0.4562 0.3691 0.0262  0.0641  -0.0319 125 ASN A C   
1040 O O   . ASN A 125 ? 0.4505 0.4801 0.3805 0.0257  0.0635  -0.0334 125 ASN A O   
1041 C CB  . ASN A 125 ? 0.4367 0.4410 0.3608 0.0312  0.0784  -0.0244 125 ASN A CB  
1042 C CG  . ASN A 125 ? 0.4526 0.4495 0.3680 0.0369  0.0865  -0.0161 125 ASN A CG  
1043 O OD1 . ASN A 125 ? 0.4763 0.4606 0.3926 0.0363  0.0908  -0.0156 125 ASN A OD1 
1044 N ND2 . ASN A 125 ? 0.4363 0.4418 0.3432 0.0426  0.0885  -0.0093 125 ASN A ND2 
1045 N N   . ILE A 126 ? 0.4256 0.4400 0.3658 0.0225  0.0597  -0.0367 126 ILE A N   
1046 C CA  . ILE A 126 ? 0.4103 0.4281 0.3571 0.0181  0.0551  -0.0441 126 ILE A CA  
1047 C C   . ILE A 126 ? 0.3973 0.4165 0.3472 0.0165  0.0486  -0.0453 126 ILE A C   
1048 O O   . ILE A 126 ? 0.4136 0.4405 0.3631 0.0146  0.0453  -0.0478 126 ILE A O   
1049 C CB  . ILE A 126 ? 0.4009 0.4109 0.3553 0.0152  0.0569  -0.0496 126 ILE A CB  
1050 C CG1 . ILE A 126 ? 0.3888 0.3970 0.3394 0.0163  0.0641  -0.0483 126 ILE A CG1 
1051 C CG2 . ILE A 126 ? 0.3814 0.3940 0.3430 0.0117  0.0527  -0.0567 126 ILE A CG2 
1052 C CD1 . ILE A 126 ? 0.3927 0.3986 0.3501 0.0130  0.0659  -0.0549 126 ILE A CD1 
1053 N N   . VAL A 127 ? 0.3812 0.3932 0.3333 0.0171  0.0473  -0.0433 127 VAL A N   
1054 C CA  . VAL A 127 ? 0.3758 0.3879 0.3308 0.0154  0.0413  -0.0444 127 VAL A CA  
1055 C C   . VAL A 127 ? 0.3577 0.3786 0.3066 0.0169  0.0393  -0.0406 127 VAL A C   
1056 O O   . VAL A 127 ? 0.3613 0.3882 0.3108 0.0143  0.0357  -0.0437 127 VAL A O   
1057 C CB  . VAL A 127 ? 0.3675 0.3707 0.3264 0.0153  0.0403  -0.0438 127 VAL A CB  
1058 C CG1 . VAL A 127 ? 0.3503 0.3538 0.3112 0.0138  0.0344  -0.0443 127 VAL A CG1 
1059 C CG2 . VAL A 127 ? 0.3646 0.3622 0.3306 0.0132  0.0415  -0.0486 127 VAL A CG2 
1060 N N   . LYS A 128 ? 0.3626 0.3847 0.3054 0.0211  0.0422  -0.0340 128 LYS A N   
1061 C CA  . LYS A 128 ? 0.3715 0.4047 0.3085 0.0233  0.0406  -0.0300 128 LYS A CA  
1062 C C   . LYS A 128 ? 0.3871 0.4339 0.3207 0.0224  0.0405  -0.0318 128 LYS A C   
1063 O O   . LYS A 128 ? 0.3898 0.4460 0.3229 0.0198  0.0367  -0.0340 128 LYS A O   
1064 C CB  . LYS A 128 ? 0.3717 0.4033 0.3030 0.0291  0.0444  -0.0221 128 LYS A CB  
1065 C CG  . LYS A 128 ? 0.3756 0.3980 0.3095 0.0287  0.0427  -0.0210 128 LYS A CG  
1066 C CD  . LYS A 128 ? 0.3852 0.4014 0.3143 0.0340  0.0484  -0.0142 128 LYS A CD  
1067 C CE  . LYS A 128 ? 0.3812 0.3899 0.3125 0.0331  0.0466  -0.0137 128 LYS A CE  
1068 N NZ  . LYS A 128 ? 0.3876 0.3927 0.3130 0.0387  0.0519  -0.0064 128 LYS A NZ  
1069 N N   . PRO A 129 ? 0.3969 0.4447 0.3281 0.0238  0.0450  -0.0316 129 PRO A N   
1070 C CA  . PRO A 129 ? 0.4063 0.4680 0.3343 0.0222  0.0447  -0.0340 129 PRO A CA  
1071 C C   . PRO A 129 ? 0.4125 0.4760 0.3459 0.0155  0.0411  -0.0429 129 PRO A C   
1072 O O   . PRO A 129 ? 0.4099 0.4864 0.3404 0.0129  0.0392  -0.0452 129 PRO A O   
1073 C CB  . PRO A 129 ? 0.4128 0.4724 0.3378 0.0248  0.0505  -0.0322 129 PRO A CB  
1074 C CG  . PRO A 129 ? 0.4130 0.4629 0.3354 0.0302  0.0546  -0.0251 129 PRO A CG  
1075 C CD  . PRO A 129 ? 0.4034 0.4428 0.3322 0.0277  0.0512  -0.0273 129 PRO A CD  
1076 N N   . ILE A 130 ? 0.4057 0.4568 0.3464 0.0126  0.0404  -0.0478 130 ILE A N   
1077 C CA  . ILE A 130 ? 0.3904 0.4413 0.3359 0.0070  0.0376  -0.0555 130 ILE A CA  
1078 C C   . ILE A 130 ? 0.3891 0.4445 0.3339 0.0044  0.0335  -0.0563 130 ILE A C   
1079 O O   . ILE A 130 ? 0.3962 0.4595 0.3398 0.0000  0.0326  -0.0611 130 ILE A O   
1080 C CB  . ILE A 130 ? 0.3828 0.4207 0.3366 0.0055  0.0375  -0.0599 130 ILE A CB  
1081 C CG1 . ILE A 130 ? 0.3804 0.4191 0.3375 0.0007  0.0369  -0.0676 130 ILE A CG1 
1082 C CG2 . ILE A 130 ? 0.3670 0.3957 0.3248 0.0062  0.0343  -0.0582 130 ILE A CG2 
1083 C CD1 . ILE A 130 ? 0.4018 0.4373 0.3629 0.0003  0.0403  -0.0717 130 ILE A CD1 
1084 N N   . ILE A 131 ? 0.3886 0.4392 0.3336 0.0067  0.0314  -0.0518 131 ILE A N   
1085 C CA  . ILE A 131 ? 0.4072 0.4620 0.3510 0.0045  0.0278  -0.0518 131 ILE A CA  
1086 C C   . ILE A 131 ? 0.4240 0.4966 0.3611 0.0043  0.0279  -0.0505 131 ILE A C   
1087 O O   . ILE A 131 ? 0.4423 0.5223 0.3787 -0.0008 0.0262  -0.0552 131 ILE A O   
1088 C CB  . ILE A 131 ? 0.4178 0.4647 0.3627 0.0075  0.0261  -0.0467 131 ILE A CB  
1089 C CG1 . ILE A 131 ? 0.3995 0.4316 0.3513 0.0069  0.0255  -0.0490 131 ILE A CG1 
1090 C CG2 . ILE A 131 ? 0.4268 0.4781 0.3702 0.0052  0.0225  -0.0465 131 ILE A CG2 
1091 C CD1 . ILE A 131 ? 0.4004 0.4249 0.3530 0.0097  0.0247  -0.0444 131 ILE A CD1 
1092 N N   . ALA A 132 ? 0.4178 0.4977 0.3499 0.0096  0.0305  -0.0444 132 ALA A N   
1093 C CA  . ALA A 132 ? 0.4277 0.5270 0.3530 0.0108  0.0306  -0.0419 132 ALA A CA  
1094 C C   . ALA A 132 ? 0.4444 0.5547 0.3685 0.0057  0.0312  -0.0485 132 ALA A C   
1095 O O   . ALA A 132 ? 0.4317 0.5594 0.3518 0.0032  0.0300  -0.0499 132 ALA A O   
1096 C CB  . ALA A 132 ? 0.4321 0.5350 0.3520 0.0189  0.0340  -0.0331 132 ALA A CB  
1097 N N   . PHE A 133 ? 0.4467 0.5476 0.3742 0.0038  0.0334  -0.0529 133 PHE A N   
1098 C CA  . PHE A 133 ? 0.4498 0.5594 0.3762 -0.0010 0.0348  -0.0596 133 PHE A CA  
1099 C C   . PHE A 133 ? 0.4490 0.5597 0.3778 -0.0089 0.0327  -0.0677 133 PHE A C   
1100 O O   . PHE A 133 ? 0.4849 0.6100 0.4104 -0.0138 0.0332  -0.0725 133 PHE A O   
1101 C CB  . PHE A 133 ? 0.4654 0.5634 0.3955 -0.0008 0.0381  -0.0623 133 PHE A CB  
1102 C CG  . PHE A 133 ? 0.4881 0.5950 0.4166 -0.0054 0.0403  -0.0689 133 PHE A CG  
1103 C CD1 . PHE A 133 ? 0.4935 0.6169 0.4148 -0.0036 0.0423  -0.0662 133 PHE A CD1 
1104 C CD2 . PHE A 133 ? 0.4900 0.5891 0.4239 -0.0115 0.0407  -0.0777 133 PHE A CD2 
1105 C CE1 . PHE A 133 ? 0.5052 0.6375 0.4247 -0.0084 0.0444  -0.0728 133 PHE A CE1 
1106 C CE2 . PHE A 133 ? 0.5193 0.6261 0.4515 -0.0162 0.0433  -0.0844 133 PHE A CE2 
1107 C CZ  . PHE A 133 ? 0.5073 0.6311 0.4324 -0.0151 0.0450  -0.0822 133 PHE A CZ  
1108 N N   . TYR A 134 ? 0.4499 0.5457 0.3842 -0.0103 0.0308  -0.0691 134 TYR A N   
1109 C CA  . TYR A 134 ? 0.4401 0.5328 0.3767 -0.0176 0.0298  -0.0765 134 TYR A CA  
1110 C C   . TYR A 134 ? 0.4547 0.5529 0.3893 -0.0194 0.0268  -0.0750 134 TYR A C   
1111 O O   . TYR A 134 ? 0.4557 0.5564 0.3900 -0.0264 0.0267  -0.0813 134 TYR A O   
1112 C CB  . TYR A 134 ? 0.4228 0.4954 0.3666 -0.0182 0.0302  -0.0798 134 TYR A CB  
1113 C CG  . TYR A 134 ? 0.4228 0.4910 0.3693 -0.0180 0.0336  -0.0834 134 TYR A CG  
1114 C CD1 . TYR A 134 ? 0.4183 0.4932 0.3633 -0.0235 0.0363  -0.0907 134 TYR A CD1 
1115 C CD2 . TYR A 134 ? 0.3987 0.4569 0.3493 -0.0128 0.0343  -0.0800 134 TYR A CD2 
1116 C CE1 . TYR A 134 ? 0.4382 0.5093 0.3857 -0.0234 0.0396  -0.0943 134 TYR A CE1 
1117 C CE2 . TYR A 134 ? 0.4029 0.4580 0.3563 -0.0128 0.0375  -0.0835 134 TYR A CE2 
1118 C CZ  . TYR A 134 ? 0.4316 0.4929 0.3835 -0.0179 0.0400  -0.0905 134 TYR A CZ  
1119 O OH  . TYR A 134 ? 0.4172 0.4759 0.3717 -0.0180 0.0435  -0.0942 134 TYR A OH  
1120 N N   . TYR A 135 ? 0.4620 0.5616 0.3952 -0.0135 0.0249  -0.0670 135 TYR A N   
1121 C CA  . TYR A 135 ? 0.4692 0.5732 0.4011 -0.0148 0.0220  -0.0653 135 TYR A CA  
1122 C C   . TYR A 135 ? 0.4805 0.6015 0.4071 -0.0100 0.0211  -0.0585 135 TYR A C   
1123 O O   . TYR A 135 ? 0.4812 0.6038 0.4057 -0.0030 0.0226  -0.0520 135 TYR A O   
1124 C CB  . TYR A 135 ? 0.4413 0.5271 0.3776 -0.0129 0.0202  -0.0628 135 TYR A CB  
1125 C CG  . TYR A 135 ? 0.4646 0.5348 0.4059 -0.0171 0.0207  -0.0689 135 TYR A CG  
1126 C CD1 . TYR A 135 ? 0.4695 0.5365 0.4112 -0.0234 0.0201  -0.0739 135 TYR A CD1 
1127 C CD2 . TYR A 135 ? 0.4682 0.5268 0.4140 -0.0146 0.0223  -0.0696 135 TYR A CD2 
1128 C CE1 . TYR A 135 ? 0.4964 0.5481 0.4423 -0.0263 0.0214  -0.0788 135 TYR A CE1 
1129 C CE2 . TYR A 135 ? 0.4728 0.5180 0.4234 -0.0174 0.0230  -0.0746 135 TYR A CE2 
1130 C CZ  . TYR A 135 ? 0.4937 0.5350 0.4441 -0.0228 0.0227  -0.0789 135 TYR A CZ  
1131 O OH  . TYR A 135 ? 0.5447 0.5716 0.4995 -0.0245 0.0241  -0.0831 135 TYR A OH  
1132 N N   . LYS A 136 ? 0.5162 0.6495 0.4405 -0.0138 0.0192  -0.0599 136 LYS A N   
1133 C CA  . LYS A 136 ? 0.5186 0.6675 0.4389 -0.0088 0.0179  -0.0531 136 LYS A CA  
1134 C C   . LYS A 136 ? 0.4950 0.6325 0.4177 -0.0070 0.0158  -0.0494 136 LYS A C   
1135 O O   . LYS A 136 ? 0.5133 0.6449 0.4380 -0.0133 0.0143  -0.0542 136 LYS A O   
1136 C CB  . LYS A 136 ? 0.5746 0.7478 0.4910 -0.0145 0.0172  -0.0575 136 LYS A CB  
1137 C CG  . LYS A 136 ? 0.6389 0.8342 0.5506 -0.0083 0.0163  -0.0503 136 LYS A CG  
1138 C CD  . LYS A 136 ? 0.7185 0.9188 0.6267 0.0009  0.0185  -0.0427 136 LYS A CD  
1139 C CE  . LYS A 136 ? 0.7512 0.9814 0.6536 0.0043  0.0182  -0.0391 136 LYS A CE  
1140 N NZ  . LYS A 136 ? 0.7863 1.0293 0.6882 0.0048  0.0157  -0.0367 136 LYS A NZ  
1141 N N   . PRO A 137 ? 0.4798 0.6128 0.4017 0.0013  0.0163  -0.0410 137 PRO A N   
1142 C CA  . PRO A 137 ? 0.4886 0.6134 0.4120 0.0031  0.0145  -0.0373 137 PRO A CA  
1143 C C   . PRO A 137 ? 0.5265 0.6703 0.4467 0.0029  0.0128  -0.0355 137 PRO A C   
1144 O O   . PRO A 137 ? 0.5601 0.7217 0.4762 0.0079  0.0137  -0.0309 137 PRO A O   
1145 C CB  . PRO A 137 ? 0.4742 0.5891 0.3973 0.0117  0.0168  -0.0295 137 PRO A CB  
1146 C CG  . PRO A 137 ? 0.4769 0.6022 0.3962 0.0159  0.0197  -0.0269 137 PRO A CG  
1147 C CD  . PRO A 137 ? 0.4701 0.6034 0.3896 0.0090  0.0192  -0.0348 137 PRO A CD  
1148 N N   . ILE A 138 ? 0.5538 0.6944 0.4758 -0.0026 0.0106  -0.0389 138 ILE A N   
1149 C CA  . ILE A 138 ? 0.5688 0.7275 0.4884 -0.0043 0.0090  -0.0386 138 ILE A CA  
1150 C C   . ILE A 138 ? 0.5690 0.7180 0.4899 -0.0016 0.0077  -0.0341 138 ILE A C   
1151 O O   . ILE A 138 ? 0.5651 0.6960 0.4891 -0.0053 0.0067  -0.0367 138 ILE A O   
1152 C CB  . ILE A 138 ? 0.5849 0.7513 0.5045 -0.0154 0.0083  -0.0484 138 ILE A CB  
1153 C CG1 . ILE A 138 ? 0.6188 0.8118 0.5347 -0.0170 0.0089  -0.0507 138 ILE A CG1 
1154 C CG2 . ILE A 138 ? 0.6199 0.7874 0.5399 -0.0202 0.0066  -0.0501 138 ILE A CG2 
1155 C CD1 . ILE A 138 ? 0.6043 0.7971 0.5194 -0.0164 0.0109  -0.0526 138 ILE A CD1 
1156 N N   . LYS A 139 ? 0.5507 0.7116 0.4691 0.0052  0.0079  -0.0271 139 LYS A N   
1157 C CA  . LYS A 139 ? 0.5619 0.7171 0.4811 0.0074  0.0069  -0.0232 139 LYS A CA  
1158 C C   . LYS A 139 ? 0.5456 0.7127 0.4647 -0.0002 0.0047  -0.0283 139 LYS A C   
1159 O O   . LYS A 139 ? 0.5404 0.7311 0.4571 -0.0005 0.0043  -0.0286 139 LYS A O   
1160 C CB  . LYS A 139 ? 0.5791 0.7421 0.4955 0.0180  0.0089  -0.0138 139 LYS A CB  
1161 C CG  . LYS A 139 ? 0.6089 0.7585 0.5248 0.0254  0.0123  -0.0086 139 LYS A CG  
1162 C CD  . LYS A 139 ? 0.6821 0.8356 0.5949 0.0359  0.0154  0.0008  139 LYS A CD  
1163 C CE  . LYS A 139 ? 0.7342 0.8796 0.6447 0.0433  0.0201  0.0061  139 LYS A CE  
1164 N NZ  . LYS A 139 ? 0.7414 0.8614 0.6549 0.0416  0.0215  0.0044  139 LYS A NZ  
1165 N N   . THR A 140 ? 0.5421 0.6935 0.4635 -0.0065 0.0034  -0.0324 140 THR A N   
1166 C CA  . THR A 140 ? 0.5775 0.7369 0.4986 -0.0148 0.0020  -0.0378 140 THR A CA  
1167 C C   . THR A 140 ? 0.6204 0.7931 0.5403 -0.0109 0.0013  -0.0328 140 THR A C   
1168 O O   . THR A 140 ? 0.6350 0.8235 0.5539 -0.0165 0.0005  -0.0365 140 THR A O   
1169 C CB  . THR A 140 ? 0.5850 0.7220 0.5083 -0.0215 0.0014  -0.0423 140 THR A CB  
1170 O OG1 . THR A 140 ? 0.5758 0.6969 0.5005 -0.0163 0.0007  -0.0366 140 THR A OG1 
1171 C CG2 . THR A 140 ? 0.5509 0.6747 0.4758 -0.0248 0.0026  -0.0472 140 THR A CG2 
1172 N N   . LEU A 141 ? 0.6499 0.8163 0.5698 -0.0015 0.0021  -0.0247 141 LEU A N   
1173 C CA  . LEU A 141 ? 0.6805 0.8567 0.5993 0.0040  0.0021  -0.0189 141 LEU A CA  
1174 C C   . LEU A 141 ? 0.6989 0.8623 0.6191 -0.0004 0.0008  -0.0203 141 LEU A C   
1175 O O   . LEU A 141 ? 0.7289 0.8953 0.6487 0.0038  0.0011  -0.0155 141 LEU A O   
1176 C CB  . LEU A 141 ? 0.6965 0.9036 0.6132 0.0046  0.0018  -0.0188 141 LEU A CB  
1177 C CG  . LEU A 141 ? 0.6979 0.9224 0.6123 0.0108  0.0031  -0.0156 141 LEU A CG  
1178 C CD1 . LEU A 141 ? 0.7358 0.9930 0.6484 0.0111  0.0022  -0.0157 141 LEU A CD1 
1179 C CD2 . LEU A 141 ? 0.6822 0.8973 0.5954 0.0229  0.0060  -0.0062 141 LEU A CD2 
1180 N N   . ASN A 142 ? 0.6356 0.7842 0.5572 -0.0087 -0.0001 -0.0265 142 ASN A N   
1181 C CA  . ASN A 142 ? 0.6474 0.7784 0.5700 -0.0115 -0.0011 -0.0266 142 ASN A CA  
1182 C C   . ASN A 142 ? 0.6275 0.7399 0.5514 -0.0047 -0.0003 -0.0213 142 ASN A C   
1183 O O   . ASN A 142 ? 0.6096 0.7061 0.5352 -0.0056 -0.0004 -0.0229 142 ASN A O   
1184 C CB  . ASN A 142 ? 0.6805 0.8004 0.6037 -0.0213 -0.0018 -0.0340 142 ASN A CB  
1185 C CG  . ASN A 142 ? 0.7447 0.8553 0.6676 -0.0258 -0.0027 -0.0348 142 ASN A CG  
1186 O OD1 . ASN A 142 ? 0.7433 0.8461 0.6665 -0.0212 -0.0032 -0.0298 142 ASN A OD1 
1187 N ND2 . ASN A 142 ? 0.7641 0.8753 0.6859 -0.0351 -0.0024 -0.0412 142 ASN A ND2 
1188 N N   . GLY A 143 ? 0.5885 0.7034 0.5115 0.0017  0.0006  -0.0152 143 GLY A N   
1189 C CA  . GLY A 143 ? 0.5703 0.6707 0.4938 0.0084  0.0026  -0.0102 143 GLY A CA  
1190 C C   . GLY A 143 ? 0.5450 0.6452 0.4684 0.0130  0.0046  -0.0088 143 GLY A C   
1191 O O   . GLY A 143 ? 0.5642 0.6807 0.4861 0.0153  0.0054  -0.0081 143 GLY A O   
1192 N N   . HIS A 144 ? 0.5431 0.6258 0.4683 0.0140  0.0055  -0.0086 144 HIS A N   
1193 C CA  . HIS A 144 ? 0.5455 0.6258 0.4706 0.0183  0.0080  -0.0072 144 HIS A CA  
1194 C C   . HIS A 144 ? 0.5533 0.6291 0.4806 0.0128  0.0063  -0.0132 144 HIS A C   
1195 O O   . HIS A 144 ? 0.5969 0.6676 0.5250 0.0150  0.0081  -0.0131 144 HIS A O   
1196 C CB  . HIS A 144 ? 0.5121 0.5774 0.4373 0.0232  0.0112  -0.0031 144 HIS A CB  
1197 C CG  . HIS A 144 ? 0.5006 0.5686 0.4234 0.0288  0.0139  0.0025  144 HIS A CG  
1198 N ND1 . HIS A 144 ? 0.5205 0.5814 0.4438 0.0268  0.0130  0.0025  144 HIS A ND1 
1199 C CD2 . HIS A 144 ? 0.5116 0.5897 0.4311 0.0368  0.0178  0.0087  144 HIS A CD2 
1200 C CE1 . HIS A 144 ? 0.5087 0.5740 0.4295 0.0329  0.0164  0.0080  144 HIS A CE1 
1201 N NE2 . HIS A 144 ? 0.4892 0.5649 0.4077 0.0395  0.0195  0.0120  144 HIS A NE2 
1202 N N   . GLU A 145 ? 0.5471 0.6249 0.4752 0.0055  0.0034  -0.0184 145 GLU A N   
1203 C CA  . GLU A 145 ? 0.5464 0.6192 0.4765 0.0000  0.0025  -0.0245 145 GLU A CA  
1204 C C   . GLU A 145 ? 0.5462 0.6299 0.4754 0.0014  0.0041  -0.0256 145 GLU A C   
1205 O O   . GLU A 145 ? 0.5376 0.6394 0.4641 0.0026  0.0046  -0.0245 145 GLU A O   
1206 C CB  . GLU A 145 ? 0.5548 0.6294 0.4847 -0.0079 0.0005  -0.0297 145 GLU A CB  
1207 C CG  . GLU A 145 ? 0.5810 0.6504 0.5123 -0.0137 0.0006  -0.0362 145 GLU A CG  
1208 C CD  . GLU A 145 ? 0.6145 0.6847 0.5447 -0.0221 0.0001  -0.0418 145 GLU A CD  
1209 O OE1 . GLU A 145 ? 0.6633 0.7189 0.5951 -0.0258 0.0002  -0.0452 145 GLU A OE1 
1210 O OE2 . GLU A 145 ? 0.6166 0.7023 0.5445 -0.0249 0.0000  -0.0427 145 GLU A OE2 
1211 N N   . ILE A 146 ? 0.5277 0.6013 0.4591 0.0013  0.0049  -0.0277 146 ILE A N   
1212 C CA  . ILE A 146 ? 0.5020 0.5843 0.4327 0.0008  0.0063  -0.0303 146 ILE A CA  
1213 C C   . ILE A 146 ? 0.5150 0.5906 0.4481 -0.0063 0.0056  -0.0378 146 ILE A C   
1214 O O   . ILE A 146 ? 0.5030 0.5623 0.4391 -0.0077 0.0048  -0.0393 146 ILE A O   
1215 C CB  . ILE A 146 ? 0.4977 0.5754 0.4285 0.0073  0.0091  -0.0265 146 ILE A CB  
1216 C CG1 . ILE A 146 ? 0.4510 0.5371 0.3783 0.0148  0.0112  -0.0190 146 ILE A CG1 
1217 C CG2 . ILE A 146 ? 0.4920 0.5762 0.4225 0.0058  0.0104  -0.0301 146 ILE A CG2 
1218 C CD1 . ILE A 146 ? 0.4204 0.4965 0.3475 0.0210  0.0149  -0.0145 146 ILE A CD1 
1219 N N   . LYS A 147 ? 0.5117 0.6004 0.4429 -0.0107 0.0061  -0.0424 147 LYS A N   
1220 C CA  . LYS A 147 ? 0.5268 0.6096 0.4596 -0.0174 0.0068  -0.0499 147 LYS A CA  
1221 C C   . LYS A 147 ? 0.5097 0.5982 0.4422 -0.0163 0.0089  -0.0517 147 LYS A C   
1222 O O   . LYS A 147 ? 0.4651 0.5699 0.3946 -0.0130 0.0096  -0.0490 147 LYS A O   
1223 C CB  . LYS A 147 ? 0.5921 0.6840 0.5227 -0.0255 0.0066  -0.0554 147 LYS A CB  
1224 C CG  . LYS A 147 ? 0.6588 0.7343 0.5913 -0.0319 0.0071  -0.0607 147 LYS A CG  
1225 C CD  . LYS A 147 ? 0.7401 0.8205 0.6701 -0.0383 0.0067  -0.0633 147 LYS A CD  
1226 C CE  . LYS A 147 ? 0.7749 0.8346 0.7062 -0.0419 0.0071  -0.0652 147 LYS A CE  
1227 N NZ  . LYS A 147 ? 0.7466 0.8058 0.6764 -0.0426 0.0053  -0.0622 147 LYS A NZ  
1228 N N   . PHE A 148 ? 0.4783 0.5537 0.4141 -0.0182 0.0100  -0.0557 148 PHE A N   
1229 C CA  . PHE A 148 ? 0.4565 0.5357 0.3923 -0.0175 0.0122  -0.0581 148 PHE A CA  
1230 C C   . PHE A 148 ? 0.4689 0.5519 0.4041 -0.0257 0.0138  -0.0665 148 PHE A C   
1231 O O   . PHE A 148 ? 0.4626 0.5313 0.4004 -0.0297 0.0146  -0.0710 148 PHE A O   
1232 C CB  . PHE A 148 ? 0.4486 0.5118 0.3888 -0.0135 0.0130  -0.0567 148 PHE A CB  
1233 C CG  . PHE A 148 ? 0.4288 0.4900 0.3689 -0.0059 0.0130  -0.0492 148 PHE A CG  
1234 C CD1 . PHE A 148 ? 0.4133 0.4856 0.3500 -0.0014 0.0149  -0.0453 148 PHE A CD1 
1235 C CD2 . PHE A 148 ? 0.4108 0.4587 0.3537 -0.0036 0.0116  -0.0461 148 PHE A CD2 
1236 C CE1 . PHE A 148 ? 0.4141 0.4825 0.3501 0.0052  0.0161  -0.0385 148 PHE A CE1 
1237 C CE2 . PHE A 148 ? 0.4005 0.4458 0.3429 0.0023  0.0125  -0.0401 148 PHE A CE2 
1238 C CZ  . PHE A 148 ? 0.4057 0.4602 0.3447 0.0067  0.0151  -0.0364 148 PHE A CZ  
1239 N N   . ILE A 149 ? 0.4714 0.5740 0.4027 -0.0279 0.0148  -0.0687 149 ILE A N   
1240 C CA  . ILE A 149 ? 0.5118 0.6213 0.4416 -0.0368 0.0169  -0.0776 149 ILE A CA  
1241 C C   . ILE A 149 ? 0.5271 0.6377 0.4572 -0.0364 0.0195  -0.0805 149 ILE A C   
1242 O O   . ILE A 149 ? 0.5088 0.6274 0.4376 -0.0301 0.0194  -0.0755 149 ILE A O   
1243 C CB  . ILE A 149 ? 0.5131 0.6472 0.4382 -0.0407 0.0162  -0.0790 149 ILE A CB  
1244 C CG1 . ILE A 149 ? 0.5194 0.6544 0.4441 -0.0396 0.0136  -0.0748 149 ILE A CG1 
1245 C CG2 . ILE A 149 ? 0.5187 0.6594 0.4421 -0.0517 0.0190  -0.0896 149 ILE A CG2 
1246 C CD1 . ILE A 149 ? 0.5208 0.6363 0.4478 -0.0446 0.0138  -0.0781 149 ILE A CD1 
1247 N N   . ARG A 150 ? 0.5757 0.6771 0.5075 -0.0427 0.0223  -0.0885 150 ARG A N   
1248 C CA  . ARG A 150 ? 0.6332 0.7363 0.5652 -0.0434 0.0252  -0.0925 150 ARG A CA  
1249 C C   . ARG A 150 ? 0.6525 0.7811 0.5792 -0.0447 0.0254  -0.0930 150 ARG A C   
1250 O O   . ARG A 150 ? 0.6761 0.8204 0.5993 -0.0503 0.0250  -0.0963 150 ARG A O   
1251 C CB  . ARG A 150 ? 0.6868 0.7776 0.6207 -0.0509 0.0289  -0.1017 150 ARG A CB  
1252 C CG  . ARG A 150 ? 0.7742 0.8402 0.7136 -0.0480 0.0291  -0.1004 150 ARG A CG  
1253 C CD  . ARG A 150 ? 0.8900 0.9434 0.8319 -0.0520 0.0337  -0.1080 150 ARG A CD  
1254 N NE  . ARG A 150 ? 0.9948 1.0539 0.9373 -0.0499 0.0355  -0.1093 150 ARG A NE  
1255 C CZ  . ARG A 150 ? 1.0417 1.0914 0.9869 -0.0519 0.0396  -0.1151 150 ARG A CZ  
1256 N NH1 . ARG A 150 ? 1.0763 1.1095 1.0237 -0.0553 0.0427  -0.1199 150 ARG A NH1 
1257 N NH2 . ARG A 150 ? 1.0933 1.1496 1.0388 -0.0500 0.0410  -0.1160 150 ARG A NH2 
1258 N N   . LYS A 151 ? 0.6532 0.7869 0.5792 -0.0391 0.0260  -0.0896 151 LYS A N   
1259 C CA  . LYS A 151 ? 0.6868 0.8451 0.6073 -0.0376 0.0259  -0.0874 151 LYS A CA  
1260 C C   . LYS A 151 ? 0.7145 0.8900 0.6314 -0.0474 0.0279  -0.0969 151 LYS A C   
1261 O O   . LYS A 151 ? 0.7358 0.9350 0.6482 -0.0488 0.0266  -0.0964 151 LYS A O   
1262 C CB  . LYS A 151 ? 0.7069 0.8638 0.6269 -0.0303 0.0273  -0.0824 151 LYS A CB  
1263 C CG  . LYS A 151 ? 0.7240 0.9022 0.6382 -0.0240 0.0267  -0.0752 151 LYS A CG  
1264 C CD  . LYS A 151 ? 0.7427 0.9103 0.6574 -0.0142 0.0277  -0.0665 151 LYS A CD  
1265 C CE  . LYS A 151 ? 0.7645 0.9508 0.6726 -0.0083 0.0291  -0.0605 151 LYS A CE  
1266 N NZ  . LYS A 151 ? 0.7558 0.9313 0.6635 0.0016  0.0306  -0.0506 151 LYS A NZ  
1267 N N   . GLU A 152 ? 0.7377 0.9019 0.6567 -0.0544 0.0312  -0.1058 152 GLU A N   
1268 C CA  . GLU A 152 ? 0.7898 0.9686 0.7055 -0.0651 0.0342  -0.1163 152 GLU A CA  
1269 C C   . GLU A 152 ? 0.7720 0.9582 0.6861 -0.0730 0.0336  -0.1208 152 GLU A C   
1270 O O   . GLU A 152 ? 0.7560 0.9652 0.6656 -0.0800 0.0343  -0.1263 152 GLU A O   
1271 C CB  . GLU A 152 ? 0.8186 0.9816 0.7368 -0.0706 0.0390  -0.1250 152 GLU A CB  
1272 C CG  . GLU A 152 ? 0.9315 1.0645 0.8560 -0.0686 0.0400  -0.1247 152 GLU A CG  
1273 C CD  . GLU A 152 ? 0.9900 1.1105 0.9186 -0.0579 0.0382  -0.1163 152 GLU A CD  
1274 O OE1 . GLU A 152 ? 1.0683 1.1965 0.9956 -0.0544 0.0390  -0.1147 152 GLU A OE1 
1275 O OE2 . GLU A 152 ? 1.0034 1.1069 0.9361 -0.0533 0.0363  -0.1116 152 GLU A OE2 
1276 N N   . GLU A 153 ? 0.7589 0.9266 0.6763 -0.0719 0.0324  -0.1184 153 GLU A N   
1277 C CA  . GLU A 153 ? 0.7780 0.9505 0.6939 -0.0789 0.0321  -0.1219 153 GLU A CA  
1278 C C   . GLU A 153 ? 0.7377 0.9356 0.6503 -0.0754 0.0280  -0.1159 153 GLU A C   
1279 O O   . GLU A 153 ? 0.7343 0.9517 0.6438 -0.0831 0.0283  -0.1213 153 GLU A O   
1280 C CB  . GLU A 153 ? 0.8239 0.9701 0.7438 -0.0773 0.0316  -0.1195 153 GLU A CB  
1281 C CG  . GLU A 153 ? 0.9246 1.0475 0.8469 -0.0829 0.0366  -0.1270 153 GLU A CG  
1282 C CD  . GLU A 153 ? 1.0016 1.0991 0.9278 -0.0792 0.0358  -0.1229 153 GLU A CD  
1283 O OE1 . GLU A 153 ? 1.0588 1.1581 0.9844 -0.0781 0.0327  -0.1185 153 GLU A OE1 
1284 O OE2 . GLU A 153 ? 1.0127 1.0895 0.9426 -0.0772 0.0382  -0.1239 153 GLU A OE2 
1285 N N   . TYR A 154 ? 0.6876 0.8857 0.6010 -0.0638 0.0247  -0.1050 154 TYR A N   
1286 C CA  . TYR A 154 ? 0.6568 0.8771 0.5673 -0.0583 0.0214  -0.0979 154 TYR A CA  
1287 C C   . TYR A 154 ? 0.6609 0.9117 0.5664 -0.0603 0.0218  -0.1002 154 TYR A C   
1288 O O   . TYR A 154 ? 0.6679 0.9431 0.5705 -0.0630 0.0203  -0.1009 154 TYR A O   
1289 C CB  . TYR A 154 ? 0.6339 0.8448 0.5459 -0.0453 0.0191  -0.0858 154 TYR A CB  
1290 C CG  . TYR A 154 ? 0.6458 0.8805 0.5541 -0.0382 0.0167  -0.0778 154 TYR A CG  
1291 C CD1 . TYR A 154 ? 0.6589 0.9024 0.5670 -0.0385 0.0144  -0.0756 154 TYR A CD1 
1292 C CD2 . TYR A 154 ? 0.6516 0.9008 0.5564 -0.0311 0.0172  -0.0724 154 TYR A CD2 
1293 C CE1 . TYR A 154 ? 0.6823 0.9488 0.5872 -0.0314 0.0126  -0.0681 154 TYR A CE1 
1294 C CE2 . TYR A 154 ? 0.6942 0.9655 0.5953 -0.0236 0.0156  -0.0643 154 TYR A CE2 
1295 C CZ  . TYR A 154 ? 0.7194 0.9996 0.6207 -0.0235 0.0133  -0.0622 154 TYR A CZ  
1296 O OH  . TYR A 154 ? 0.7378 1.0405 0.6357 -0.0151 0.0119  -0.0539 154 TYR A OH  
1297 N N   . ILE A 155 ? 0.6613 0.9120 0.5659 -0.0588 0.0238  -0.1013 155 ILE A N   
1298 C CA  . ILE A 155 ? 0.6769 0.9568 0.5762 -0.0604 0.0243  -0.1033 155 ILE A CA  
1299 C C   . ILE A 155 ? 0.7031 1.0002 0.6002 -0.0743 0.0261  -0.1157 155 ILE A C   
1300 O O   . ILE A 155 ? 0.7191 1.0475 0.6120 -0.0763 0.0248  -0.1165 155 ILE A O   
1301 C CB  . ILE A 155 ? 0.6691 0.9433 0.5677 -0.0569 0.0267  -0.1027 155 ILE A CB  
1302 C CG1 . ILE A 155 ? 0.6403 0.9062 0.5392 -0.0429 0.0252  -0.0897 155 ILE A CG1 
1303 C CG2 . ILE A 155 ? 0.6413 0.9450 0.5342 -0.0617 0.0279  -0.1078 155 ILE A CG2 
1304 C CD1 . ILE A 155 ? 0.6469 0.9030 0.5458 -0.0391 0.0279  -0.0886 155 ILE A CD1 
1305 N N   . SER A 156 ? 0.7155 0.9924 0.6153 -0.0839 0.0295  -0.1252 156 SER A N   
1306 C CA  . SER A 156 ? 0.7388 1.0266 0.6366 -0.0984 0.0325  -0.1379 156 SER A CA  
1307 C C   . SER A 156 ? 0.7744 1.0794 0.6711 -0.1008 0.0298  -0.1369 156 SER A C   
1308 O O   . SER A 156 ? 0.8229 1.1584 0.7158 -0.1076 0.0297  -0.1422 156 SER A O   
1309 C CB  . SER A 156 ? 0.7427 0.9995 0.6438 -0.1061 0.0374  -0.1462 156 SER A CB  
1310 O OG  . SER A 156 ? 0.7823 1.0399 0.6824 -0.1179 0.0400  -0.1552 156 SER A OG  
1311 N N   . PHE A 157 ? 0.7915 1.0784 0.6916 -0.0952 0.0275  -0.1301 157 PHE A N   
1312 C CA  . PHE A 157 ? 0.7549 1.0559 0.6544 -0.0954 0.0246  -0.1274 157 PHE A CA  
1313 C C   . PHE A 157 ? 0.7525 1.0882 0.6488 -0.0881 0.0209  -0.1203 157 PHE A C   
1314 O O   . PHE A 157 ? 0.7363 1.0997 0.6303 -0.0938 0.0200  -0.1241 157 PHE A O   
1315 C CB  . PHE A 157 ? 0.7478 1.0224 0.6515 -0.0881 0.0225  -0.1193 157 PHE A CB  
1316 C CG  . PHE A 157 ? 0.7369 1.0263 0.6402 -0.0843 0.0188  -0.1132 157 PHE A CG  
1317 C CD1 . PHE A 157 ? 0.7267 1.0286 0.6294 -0.0714 0.0152  -0.1014 157 PHE A CD1 
1318 C CD2 . PHE A 157 ? 0.7527 1.0428 0.6561 -0.0935 0.0197  -0.1190 157 PHE A CD2 
1319 C CE1 . PHE A 157 ? 0.7067 1.0225 0.6092 -0.0674 0.0123  -0.0958 157 PHE A CE1 
1320 C CE2 . PHE A 157 ? 0.7566 1.0611 0.6600 -0.0900 0.0164  -0.1136 157 PHE A CE2 
1321 C CZ  . PHE A 157 ? 0.7411 1.0588 0.6442 -0.0767 0.0127  -0.1020 157 PHE A CZ  
1322 N N   . GLU A 158 ? 0.7514 1.0855 0.6474 -0.0755 0.0191  -0.1101 158 GLU A N   
1323 C CA  . GLU A 158 ? 0.7570 1.1201 0.6496 -0.0658 0.0162  -0.1011 158 GLU A CA  
1324 C C   . GLU A 158 ? 0.7802 1.1782 0.6680 -0.0730 0.0169  -0.1083 158 GLU A C   
1325 O O   . GLU A 158 ? 0.7757 1.2056 0.6608 -0.0706 0.0145  -0.1053 158 GLU A O   
1326 C CB  . GLU A 158 ? 0.7580 1.1080 0.6505 -0.0520 0.0158  -0.0898 158 GLU A CB  
1327 C CG  . GLU A 158 ? 0.7720 1.1453 0.6609 -0.0393 0.0135  -0.0779 158 GLU A CG  
1328 C CD  . GLU A 158 ? 0.8045 1.1689 0.6915 -0.0285 0.0149  -0.0695 158 GLU A CD  
1329 O OE1 . GLU A 158 ? 0.8301 1.2088 0.7137 -0.0168 0.0141  -0.0586 158 GLU A OE1 
1330 O OE2 . GLU A 158 ? 0.8338 1.1768 0.7226 -0.0315 0.0173  -0.0736 158 GLU A OE2 
1331 N N   . SER A 159 ? 0.7789 1.1715 0.6659 -0.0818 0.0204  -0.1179 159 SER A N   
1332 C CA  . SER A 159 ? 0.8062 1.2307 0.6884 -0.0901 0.0217  -0.1263 159 SER A CA  
1333 C C   . SER A 159 ? 0.8098 1.2525 0.6914 -0.1043 0.0226  -0.1376 159 SER A C   
1334 O O   . SER A 159 ? 0.7836 1.2639 0.6616 -0.1073 0.0211  -0.1399 159 SER A O   
1335 C CB  . SER A 159 ? 0.7957 1.2070 0.6772 -0.0956 0.0259  -0.1337 159 SER A CB  
1336 O OG  . SER A 159 ? 0.8073 1.2152 0.6874 -0.0833 0.0250  -0.1239 159 SER A OG  
1337 N N   . LYS A 160 ? 0.8201 1.2365 0.7052 -0.1129 0.0253  -0.1446 160 LYS A N   
1338 C CA  . LYS A 160 ? 0.8487 1.2763 0.7332 -0.1277 0.0275  -0.1562 160 LYS A CA  
1339 C C   . LYS A 160 ? 0.8539 1.3090 0.7381 -0.1243 0.0231  -0.1509 160 LYS A C   
1340 O O   . LYS A 160 ? 0.8951 1.3772 0.7773 -0.1355 0.0240  -0.1599 160 LYS A O   
1341 C CB  . LYS A 160 ? 0.8602 1.2490 0.7481 -0.1347 0.0315  -0.1620 160 LYS A CB  
1342 C CG  . LYS A 160 ? 0.8999 1.2936 0.7872 -0.1495 0.0346  -0.1730 160 LYS A CG  
1343 C CD  . LYS A 160 ? 0.9467 1.3009 0.8374 -0.1508 0.0371  -0.1729 160 LYS A CD  
1344 C CE  . LYS A 160 ? 0.9749 1.3359 0.8658 -0.1566 0.0365  -0.1748 160 LYS A CE  
1345 N NZ  . LYS A 160 ? 0.9457 1.2742 0.8402 -0.1493 0.0352  -0.1666 160 LYS A NZ  
1346 N N   . VAL A 161 ? 0.8533 1.3020 0.7395 -0.1091 0.0188  -0.1367 161 VAL A N   
1347 C CA  . VAL A 161 ? 0.8350 1.3087 0.7212 -0.1034 0.0148  -0.1299 161 VAL A CA  
1348 C C   . VAL A 161 ? 0.8443 1.3582 0.7265 -0.0961 0.0120  -0.1245 161 VAL A C   
1349 O O   . VAL A 161 ? 0.8492 1.3982 0.7300 -0.0979 0.0099  -0.1254 161 VAL A O   
1350 C CB  . VAL A 161 ? 0.8078 1.2565 0.6977 -0.0901 0.0121  -0.1170 161 VAL A CB  
1351 C CG1 . VAL A 161 ? 0.7645 1.2406 0.6540 -0.0810 0.0081  -0.1079 161 VAL A CG1 
1352 C CG2 . VAL A 161 ? 0.7852 1.2008 0.6785 -0.0979 0.0143  -0.1223 161 VAL A CG2 
1353 N N   . PHE A 162 ? 0.8462 1.3552 0.7263 -0.0878 0.0122  -0.1189 162 PHE A N   
1354 C CA  . PHE A 162 ? 0.8869 1.4309 0.7623 -0.0800 0.0103  -0.1130 162 PHE A CA  
1355 C C   . PHE A 162 ? 0.9167 1.4997 0.7886 -0.0934 0.0110  -0.1253 162 PHE A C   
1356 O O   . PHE A 162 ? 0.8951 1.5178 0.7639 -0.0888 0.0082  -0.1213 162 PHE A O   
1357 C CB  . PHE A 162 ? 0.8830 1.4095 0.7566 -0.0716 0.0117  -0.1072 162 PHE A CB  
1358 C CG  . PHE A 162 ? 0.9040 1.4643 0.7718 -0.0650 0.0106  -0.1023 162 PHE A CG  
1359 C CD1 . PHE A 162 ? 0.8973 1.4835 0.7627 -0.0513 0.0074  -0.0896 162 PHE A CD1 
1360 C CD2 . PHE A 162 ? 0.9308 1.4961 0.7952 -0.0718 0.0132  -0.1098 162 PHE A CD2 
1361 C CE1 . PHE A 162 ? 0.9132 1.5302 0.7725 -0.0442 0.0067  -0.0842 162 PHE A CE1 
1362 C CE2 . PHE A 162 ? 0.9189 1.5155 0.7773 -0.0655 0.0123  -0.1050 162 PHE A CE2 
1363 C CZ  . PHE A 162 ? 0.9271 1.5496 0.7828 -0.0514 0.0089  -0.0918 162 PHE A CZ  
1364 N N   . HIS A 163 ? 0.9545 1.5264 0.8266 -0.1100 0.0152  -0.1404 163 HIS A N   
1365 C CA  . HIS A 163 ? 0.9989 1.6049 0.8675 -0.1252 0.0171  -0.1543 163 HIS A CA  
1366 C C   . HIS A 163 ? 0.9819 1.6105 0.8517 -0.1343 0.0163  -0.1606 163 HIS A C   
1367 O O   . HIS A 163 ? 0.9886 1.6593 0.8553 -0.1415 0.0156  -0.1671 163 HIS A O   
1368 C CB  . HIS A 163 ? 1.0380 1.6225 0.9061 -0.1398 0.0231  -0.1685 163 HIS A CB  
1369 C CG  . HIS A 163 ? 1.0888 1.6633 0.9546 -0.1332 0.0242  -0.1648 163 HIS A CG  
1370 N ND1 . HIS A 163 ? 1.1120 1.7199 0.9727 -0.1296 0.0226  -0.1626 163 HIS A ND1 
1371 C CD2 . HIS A 163 ? 1.0984 1.6325 0.9665 -0.1295 0.0268  -0.1629 163 HIS A CD2 
1372 C CE1 . HIS A 163 ? 1.1410 1.7297 1.0006 -0.1242 0.0244  -0.1595 163 HIS A CE1 
1373 N NE2 . HIS A 163 ? 1.1428 1.6868 1.0072 -0.1243 0.0269  -0.1599 163 HIS A NE2 
1374 N N   . LYS A 164 ? 0.9499 1.5519 0.8240 -0.1341 0.0164  -0.1587 164 LYS A N   
1375 C CA  . LYS A 164 ? 0.9283 1.5487 0.8040 -0.1415 0.0156  -0.1633 164 LYS A CA  
1376 C C   . LYS A 164 ? 0.9239 1.5818 0.7991 -0.1283 0.0098  -0.1516 164 LYS A C   
1377 O O   . LYS A 164 ? 0.9664 1.6628 0.8406 -0.1353 0.0088  -0.1574 164 LYS A O   
1378 C CB  . LYS A 164 ? 0.9258 1.5060 0.8059 -0.1427 0.0170  -0.1625 164 LYS A CB  
1379 C CG  . LYS A 164 ? 0.9384 1.5283 0.8194 -0.1573 0.0192  -0.1733 164 LYS A CG  
1380 C CD  . LYS A 164 ? 0.9436 1.4898 0.8280 -0.1593 0.0215  -0.1731 164 LYS A CD  
1381 C CE  . LYS A 164 ? 0.9682 1.4804 0.8519 -0.1708 0.0281  -0.1838 164 LYS A CE  
1382 N NZ  . LYS A 164 ? 0.9911 1.4569 0.8782 -0.1661 0.0292  -0.1785 164 LYS A NZ  
1383 N N   . LEU A 165 ? 0.9231 1.5699 0.7988 -0.1092 0.0067  -0.1353 165 LEU A N   
1384 C CA  . LEU A 165 ? 0.9123 1.5918 0.7869 -0.0940 0.0020  -0.1222 165 LEU A CA  
1385 C C   . LEU A 165 ? 0.9348 1.6591 0.8042 -0.0941 0.0009  -0.1239 165 LEU A C   
1386 O O   . LEU A 165 ? 0.9447 1.7108 0.8130 -0.0902 -0.0021 -0.1207 165 LEU A O   
1387 C CB  . LEU A 165 ? 0.8951 1.5478 0.7706 -0.0741 0.0005  -0.1050 165 LEU A CB  
1388 C CG  . LEU A 165 ? 0.8648 1.4765 0.7452 -0.0704 0.0008  -0.1002 165 LEU A CG  
1389 C CD1 . LEU A 165 ? 0.8064 1.3938 0.6867 -0.0522 0.0003  -0.0848 165 LEU A CD1 
1390 C CD2 . LEU A 165 ? 0.8211 1.4482 0.7042 -0.0709 -0.0011 -0.0993 165 LEU A CD2 
1391 N N   . LYS A 166 ? 0.9471 1.6632 0.8133 -0.0980 0.0034  -0.1285 166 LYS A N   
1392 C CA  . LYS A 166 ? 0.9687 1.7254 0.8295 -0.1012 0.0030  -0.1327 166 LYS A CA  
1393 C C   . LYS A 166 ? 0.9777 1.7702 0.8380 -0.1199 0.0039  -0.1489 166 LYS A C   
1394 O O   . LYS A 166 ? 0.9145 1.7542 0.7726 -0.1177 0.0007  -0.1473 166 LYS A O   
1395 C CB  . LYS A 166 ? 0.9897 1.7250 0.8478 -0.1048 0.0064  -0.1371 166 LYS A CB  
1396 C CG  . LYS A 166 ? 1.0154 1.7498 0.8698 -0.0868 0.0049  -0.1221 166 LYS A CG  
1397 C CD  . LYS A 166 ? 1.0577 1.7778 0.9091 -0.0931 0.0085  -0.1290 166 LYS A CD  
1398 C CE  . LYS A 166 ? 1.0719 1.8114 0.9172 -0.0794 0.0071  -0.1177 166 LYS A CE  
1399 N NZ  . LYS A 166 ? 1.0571 1.7965 0.8986 -0.0887 0.0105  -0.1274 166 LYS A NZ  
1400 N N   . LYS A 167 ? 1.0185 1.7882 0.8804 -0.1382 0.0086  -0.1643 167 LYS A N   
1401 C CA  . LYS A 167 ? 1.0552 1.8537 0.9162 -0.1585 0.0112  -0.1818 167 LYS A CA  
1402 C C   . LYS A 167 ? 1.0640 1.8754 0.9288 -0.1611 0.0094  -0.1824 167 LYS A C   
1403 O O   . LYS A 167 ? 1.1059 1.9232 0.9714 -0.1795 0.0130  -0.1974 167 LYS A O   
1404 C CB  . LYS A 167 ? 1.0985 1.8667 0.9591 -0.1772 0.0183  -0.1984 167 LYS A CB  
1405 C CG  . LYS A 167 ? 1.1248 1.9186 0.9801 -0.1892 0.0213  -0.2107 167 LYS A CG  
1406 C CD  . LYS A 167 ? 1.1269 1.9472 0.9781 -0.1740 0.0168  -0.1988 167 LYS A CD  
1407 C CE  . LYS A 167 ? 1.1206 1.9034 0.9709 -0.1660 0.0187  -0.1931 167 LYS A CE  
1408 N NZ  . LYS A 167 ? 1.1194 1.9018 0.9661 -0.1820 0.0244  -0.2087 167 LYS A NZ  
1409 N N   . MET A 168 ? 1.0492 1.8634 0.9162 -0.1426 0.0044  -0.1658 168 MET A N   
1410 C CA  . MET A 168 ? 1.0273 1.8691 0.8971 -0.1414 0.0015  -0.1638 168 MET A CA  
1411 C C   . MET A 168 ? 0.9973 1.8786 0.8652 -0.1227 -0.0039 -0.1489 168 MET A C   
1412 O O   . MET A 168 ? 0.9493 1.8453 0.8128 -0.1159 -0.0049 -0.1444 168 MET A O   
1413 C CB  . MET A 168 ? 1.0281 1.8297 0.9029 -0.1369 0.0017  -0.1580 168 MET A CB  
1414 C CG  . MET A 168 ? 1.0314 1.8022 0.9080 -0.1561 0.0072  -0.1731 168 MET A CG  
1415 S SD  . MET A 168 ? 1.0652 1.7843 0.9468 -0.1486 0.0073  -0.1644 168 MET A SD  
1416 C CE  . MET A 168 ? 1.0754 1.7629 0.9572 -0.1724 0.0149  -0.1833 168 MET A CE  
1417 N N   . LYS A 169 ? 1.0251 1.9233 0.8961 -0.1139 -0.0072 -0.1408 169 LYS A N   
1418 C CA  . LYS A 169 ? 1.0687 2.0033 0.9381 -0.0946 -0.0119 -0.1255 169 LYS A CA  
1419 C C   . LYS A 169 ? 1.0371 1.9362 0.9068 -0.0730 -0.0127 -0.1067 169 LYS A C   
1420 O O   . LYS A 169 ? 1.0334 1.9518 0.9000 -0.0553 -0.0151 -0.0926 169 LYS A O   
1421 C CB  . LYS A 169 ? 1.1154 2.0870 0.9882 -0.0942 -0.0146 -0.1251 169 LYS A CB  
1422 C CG  . LYS A 169 ? 1.1251 2.1051 1.0005 -0.1179 -0.0120 -0.1444 169 LYS A CG  
1423 C CD  . LYS A 169 ? 1.0951 2.1378 0.9708 -0.1223 -0.0147 -0.1492 169 LYS A CD  
1424 C CE  . LYS A 169 ? 1.0740 2.1264 0.9508 -0.1489 -0.0108 -0.1710 169 LYS A CE  
1425 N NZ  . LYS A 169 ? 1.0994 2.2138 0.9736 -0.1588 -0.0120 -0.1811 169 LYS A NZ  
1426 N N   . TYR A 170 ? 1.0347 1.8820 0.9077 -0.0749 -0.0104 -0.1069 170 TYR A N   
1427 C CA  . TYR A 170 ? 0.9939 1.8069 0.8686 -0.0565 -0.0110 -0.0906 170 TYR A CA  
1428 C C   . TYR A 170 ? 0.9600 1.7658 0.8304 -0.0401 -0.0110 -0.0775 170 TYR A C   
1429 O O   . TYR A 170 ? 0.9231 1.7287 0.7930 -0.0212 -0.0122 -0.0614 170 TYR A O   
1430 C CB  . TYR A 170 ? 1.0096 1.7698 0.8883 -0.0640 -0.0083 -0.0953 170 TYR A CB  
1431 C CG  . TYR A 170 ? 1.0560 1.8179 0.9386 -0.0792 -0.0075 -0.1069 170 TYR A CG  
1432 C CD1 . TYR A 170 ? 1.0617 1.8705 0.9448 -0.0853 -0.0092 -0.1125 170 TYR A CD1 
1433 C CD2 . TYR A 170 ? 1.0661 1.7834 0.9519 -0.0869 -0.0049 -0.1118 170 TYR A CD2 
1434 C CE1 . TYR A 170 ? 1.0623 1.8722 0.9486 -0.0997 -0.0079 -0.1234 170 TYR A CE1 
1435 C CE2 . TYR A 170 ? 1.0903 1.8077 0.9789 -0.1005 -0.0036 -0.1219 170 TYR A CE2 
1436 C CZ  . TYR A 170 ? 1.1025 1.8657 0.9913 -0.1072 -0.0049 -0.1278 170 TYR A CZ  
1437 O OH  . TYR A 170 ? 1.1042 1.8678 0.9956 -0.1213 -0.0031 -0.1382 170 TYR A OH  
1438 N N   . LEU A 171 ? 0.9742 1.7739 0.8412 -0.0477 -0.0091 -0.0845 171 LEU A N   
1439 C CA  . LEU A 171 ? 1.0024 1.7948 0.8648 -0.0342 -0.0085 -0.0736 171 LEU A CA  
1440 C C   . LEU A 171 ? 1.0161 1.8492 0.8727 -0.0391 -0.0090 -0.0791 171 LEU A C   
1441 O O   . LEU A 171 ? 1.0254 1.8587 0.8813 -0.0564 -0.0070 -0.0944 171 LEU A O   
1442 C CB  . LEU A 171 ? 1.0477 1.7870 0.9114 -0.0370 -0.0052 -0.0755 171 LEU A CB  
1443 C CG  . LEU A 171 ? 1.0767 1.7908 0.9379 -0.0199 -0.0040 -0.0609 171 LEU A CG  
1444 C CD1 . LEU A 171 ? 1.0676 1.7744 0.9302 -0.0019 -0.0050 -0.0448 171 LEU A CD1 
1445 C CD2 . LEU A 171 ? 1.0908 1.7568 0.9542 -0.0264 -0.0009 -0.0663 171 LEU A CD2 
1446 N N   . VAL A 172 ? 1.0213 1.8894 0.8737 -0.0237 -0.0113 -0.0667 172 VAL A N   
1447 C CA  . VAL A 172 ? 1.0429 1.9528 0.8890 -0.0258 -0.0122 -0.0696 172 VAL A CA  
1448 C C   . VAL A 172 ? 1.0742 1.9706 0.9146 -0.0108 -0.0107 -0.0568 172 VAL A C   
1449 O O   . VAL A 172 ? 1.0784 1.9616 0.9179 0.0084  -0.0105 -0.0399 172 VAL A O   
1450 C CB  . VAL A 172 ? 1.0257 1.9942 0.8704 -0.0202 -0.0160 -0.0657 172 VAL A CB  
1451 C CG1 . VAL A 172 ? 1.0200 2.0311 0.8572 -0.0182 -0.0171 -0.0651 172 VAL A CG1 
1452 C CG2 . VAL A 172 ? 1.0182 2.0062 0.8678 -0.0384 -0.0170 -0.0813 172 VAL A CG2 
1453 N N   . GLU A 173 ? 1.1110 2.0102 0.9472 -0.0201 -0.0090 -0.0653 173 GLU A N   
1454 C CA  . GLU A 173 ? 1.1476 2.0348 0.9778 -0.0081 -0.0071 -0.0550 173 GLU A CA  
1455 C C   . GLU A 173 ? 1.1895 2.1172 1.0134 0.0104  -0.0092 -0.0392 173 GLU A C   
1456 O O   . GLU A 173 ? 1.1755 2.1537 0.9973 0.0076  -0.0122 -0.0425 173 GLU A O   
1457 C CB  . GLU A 173 ? 1.1580 2.0443 0.9852 -0.0238 -0.0048 -0.0692 173 GLU A CB  
1458 C CG  . GLU A 173 ? 1.1588 2.0105 0.9827 -0.0163 -0.0015 -0.0626 173 GLU A CG  
1459 C CD  . GLU A 173 ? 1.1622 2.0226 0.9819 -0.0299 0.0005  -0.0753 173 GLU A CD  
1460 O OE1 . GLU A 173 ? 1.1568 2.0084 0.9800 -0.0493 0.0021  -0.0927 173 GLU A OE1 
1461 O OE2 . GLU A 173 ? 1.1863 2.0618 0.9988 -0.0211 0.0010  -0.0677 173 GLU A OE2 
1462 N N   . VAL A 174 ? 1.2366 2.1419 1.0573 0.0295  -0.0072 -0.0222 174 VAL A N   
1463 C CA  . VAL A 174 ? 1.2676 2.2045 1.0815 0.0498  -0.0080 -0.0048 174 VAL A CA  
1464 C C   . VAL A 174 ? 1.3260 2.2629 1.1313 0.0552  -0.0054 0.0002  174 VAL A C   
1465 O O   . VAL A 174 ? 1.3019 2.2042 1.1074 0.0469  -0.0025 -0.0065 174 VAL A O   
1466 C CB  . VAL A 174 ? 1.2396 2.1549 1.0554 0.0694  -0.0067 0.0125  174 VAL A CB  
1467 C CG1 . VAL A 174 ? 1.2703 2.1900 1.0779 0.0918  -0.0041 0.0323  174 VAL A CG1 
1468 C CG2 . VAL A 174 ? 1.2274 2.1735 1.0480 0.0704  -0.0104 0.0125  174 VAL A CG2 
1469 N N   . GLN A 175 ? 1.4279 2.4049 1.2257 0.0694  -0.0065 0.0122  175 GLN A N   
1470 C CA  . GLN A 175 ? 1.5007 2.4883 1.2892 0.0739  -0.0045 0.0165  175 GLN A CA  
1471 C C   . GLN A 175 ? 1.5960 2.5427 1.3802 0.0909  0.0006  0.0326  175 GLN A C   
1472 O O   . GLN A 175 ? 1.6133 2.5674 1.3889 0.0978  0.0028  0.0392  175 GLN A O   
1473 C CB  . GLN A 175 ? 1.4597 2.5100 1.2412 0.0822  -0.0078 0.0229  175 GLN A CB  
1474 C CG  . GLN A 175 ? 1.4269 2.5235 1.2117 0.0643  -0.0126 0.0061  175 GLN A CG  
1475 C CD  . GLN A 175 ? 1.3698 2.4805 1.1619 0.0661  -0.0157 0.0068  175 GLN A CD  
1476 O OE1 . GLN A 175 ? 1.3232 2.4115 1.1177 0.0820  -0.0144 0.0209  175 GLN A OE1 
1477 N NE2 . GLN A 175 ? 1.3417 2.4899 1.1372 0.0493  -0.0192 -0.0087 175 GLN A NE2 
1478 N N   . ASP A 176 ? 1.6628 2.5667 1.4526 0.0968  0.0029  0.0383  176 ASP A N   
1479 C CA  . ASP A 176 ? 1.6867 2.5490 1.4732 0.1125  0.0085  0.0531  176 ASP A CA  
1480 C C   . ASP A 176 ? 1.7489 2.6290 1.5283 0.1371  0.0106  0.0748  176 ASP A C   
1481 O O   . ASP A 176 ? 1.7412 2.5868 1.5182 0.1514  0.0160  0.0883  176 ASP A O   
1482 C CB  . ASP A 176 ? 1.6459 2.4869 1.4277 0.1068  0.0120  0.0490  176 ASP A CB  
1483 C CG  . ASP A 176 ? 1.6269 2.4456 1.4158 0.0841  0.0111  0.0287  176 ASP A CG  
1484 O OD1 . ASP A 176 ? 1.5950 2.3740 1.3915 0.0796  0.0121  0.0249  176 ASP A OD1 
1485 O OD2 . ASP A 176 ? 1.6102 2.4513 1.3968 0.0709  0.0097  0.0166  176 ASP A OD2 
1486 N N   . GLU A 177 ? 1.7906 2.7245 1.5666 0.1419  0.0067  0.0780  177 GLU A N   
1487 C CA  . GLU A 177 ? 1.7754 2.7326 1.5447 0.1659  0.0084  0.0986  177 GLU A CA  
1488 C C   . GLU A 177 ? 1.8049 2.7668 1.5809 0.1732  0.0067  0.1037  177 GLU A C   
1489 O O   . GLU A 177 ? 1.8110 2.8183 1.5854 0.1827  0.0038  0.1105  177 GLU A O   
1490 C CB  . GLU A 177 ? 1.7297 2.7462 1.4910 0.1687  0.0051  0.1005  177 GLU A CB  
1491 C CG  . GLU A 177 ? 1.7029 2.7435 1.4550 0.1951  0.0077  0.1234  177 GLU A CG  
1492 C CD  . GLU A 177 ? 1.6787 2.6945 1.4205 0.2075  0.0145  0.1361  177 GLU A CD  
1493 O OE1 . GLU A 177 ? 1.6933 2.6550 1.4364 0.2098  0.0202  0.1395  177 GLU A OE1 
1494 O OE2 . GLU A 177 ? 1.6372 2.6889 1.3692 0.2148  0.0142  0.1429  177 GLU A OE2 
1495 N N   . VAL A 178 ? 1.7918 2.7075 1.5755 0.1685  0.0086  0.1000  178 VAL A N   
1496 C CA  . VAL A 178 ? 1.7274 2.6404 1.5178 0.1745  0.0077  0.1042  178 VAL A CA  
1497 C C   . VAL A 178 ? 1.6590 2.5170 1.4509 0.1849  0.0141  0.1143  178 VAL A C   
1498 O O   . VAL A 178 ? 1.6294 2.4861 1.4218 0.2005  0.0164  0.1270  178 VAL A O   
1499 C CB  . VAL A 178 ? 1.7198 2.6428 1.5201 0.1532  0.0019  0.0849  178 VAL A CB  
1500 C CG1 . VAL A 178 ? 1.6856 2.5942 1.4932 0.1580  0.0019  0.0885  178 VAL A CG1 
1501 C CG2 . VAL A 178 ? 1.7201 2.7042 1.5191 0.1458  -0.0038 0.0772  178 VAL A CG2 
1502 N N   . LYS A 179 ? 1.5615 2.3755 1.3539 0.1762  0.0172  0.1082  179 LYS A N   
1503 C CA  . LYS A 179 ? 1.4994 2.2605 1.2924 0.1844  0.0239  0.1165  179 LYS A CA  
1504 C C   . LYS A 179 ? 1.4918 2.2285 1.2946 0.1791  0.0228  0.1114  179 LYS A C   
1505 O O   . LYS A 179 ? 1.4943 2.2453 1.2988 0.1895  0.0225  0.1194  179 LYS A O   
1506 C CB  . LYS A 179 ? 1.4950 2.2555 1.2788 0.2091  0.0306  0.1382  179 LYS A CB  
1507 C CG  . LYS A 179 ? 1.4662 2.1728 1.2479 0.2161  0.0390  0.1459  179 LYS A CG  
1508 C CD  . LYS A 179 ? 1.4321 2.1404 1.2025 0.2388  0.0467  0.1663  179 LYS A CD  
1509 C CE  . LYS A 179 ? 1.3960 2.0501 1.1638 0.2444  0.0560  0.1729  179 LYS A CE  
1510 N NZ  . LYS A 179 ? 1.3588 2.0120 1.1145 0.2654  0.0646  0.1922  179 LYS A NZ  
1511 N N   . PRO A 180 ? 1.4472 2.1468 1.2563 0.1634  0.0225  0.0986  180 PRO A N   
1512 C CA  . PRO A 180 ? 1.3762 2.0547 1.1947 0.1546  0.0205  0.0908  180 PRO A CA  
1513 C C   . PRO A 180 ? 1.3354 1.9801 1.1544 0.1684  0.0261  0.1031  180 PRO A C   
1514 O O   . PRO A 180 ? 1.3680 1.9956 1.1805 0.1822  0.0326  0.1158  180 PRO A O   
1515 C CB  . PRO A 180 ? 1.3614 2.0107 1.1843 0.1357  0.0194  0.0752  180 PRO A CB  
1516 C CG  . PRO A 180 ? 1.3923 2.0270 1.2082 0.1406  0.0240  0.0803  180 PRO A CG  
1517 C CD  . PRO A 180 ? 1.4190 2.0928 1.2260 0.1546  0.0247  0.0921  180 PRO A CD  
1518 N N   . ARG A 181 ? 1.2956 1.9307 1.1221 0.1641  0.0242  0.0990  181 ARG A N   
1519 C CA  . ARG A 181 ? 1.2877 1.8895 1.1155 0.1750  0.0296  0.1087  181 ARG A CA  
1520 C C   . ARG A 181 ? 1.2288 1.7959 1.0651 0.1609  0.0281  0.0973  181 ARG A C   
1521 O O   . ARG A 181 ? 1.2367 1.7937 1.0772 0.1642  0.0287  0.0998  181 ARG A O   
1522 C CB  . ARG A 181 ? 1.3196 1.9478 1.1462 0.1907  0.0303  0.1208  181 ARG A CB  
1523 C CG  . ARG A 181 ? 1.3581 2.0090 1.1750 0.2100  0.0344  0.1369  181 ARG A CG  
1524 C CD  . ARG A 181 ? 1.3811 2.0601 1.1975 0.2262  0.0351  0.1490  181 ARG A CD  
1525 N NE  . ARG A 181 ? 1.4084 2.1079 1.2149 0.2460  0.0397  0.1656  181 ARG A NE  
1526 C CZ  . ARG A 181 ? 1.4026 2.1287 1.2065 0.2641  0.0416  0.1793  181 ARG A CZ  
1527 N NH1 . ARG A 181 ? 1.3727 2.1090 1.1833 0.2647  0.0392  0.1781  181 ARG A NH1 
1528 N NH2 . ARG A 181 ? 1.4174 2.1601 1.2116 0.2821  0.0462  0.1946  181 ARG A NH2 
1529 N N   . GLY A 182 ? 1.1595 1.7086 0.9981 0.1459  0.0264  0.0851  182 GLY A N   
1530 C CA  . GLY A 182 ? 1.0848 1.6011 0.9309 0.1321  0.0249  0.0739  182 GLY A CA  
1531 C C   . GLY A 182 ? 1.0469 1.5648 0.8958 0.1140  0.0209  0.0584  182 GLY A C   
1532 O O   . GLY A 182 ? 1.0547 1.6060 0.9011 0.1096  0.0178  0.0539  182 GLY A O   
1533 N N   . VAL A 183 ? 1.0191 1.5016 0.8729 0.1037  0.0212  0.0501  183 VAL A N   
1534 C CA  . VAL A 183 ? 1.0268 1.5061 0.8833 0.0870  0.0184  0.0355  183 VAL A CA  
1535 C C   . VAL A 183 ? 1.0197 1.4978 0.8833 0.0723  0.0140  0.0228  183 VAL A C   
1536 O O   . VAL A 183 ? 1.0189 1.4746 0.8870 0.0721  0.0141  0.0234  183 VAL A O   
1537 C CB  . VAL A 183 ? 1.0301 1.4730 0.8863 0.0854  0.0222  0.0344  183 VAL A CB  
1538 C CG1 . VAL A 183 ? 1.0308 1.4355 0.8918 0.0862  0.0243  0.0359  183 VAL A CG1 
1539 C CG2 . VAL A 183 ? 1.0162 1.4591 0.8744 0.0699  0.0200  0.0204  183 VAL A CG2 
1540 N N   . LEU A 184 ? 0.9891 1.4912 0.8532 0.0597  0.0106  0.0115  184 LEU A N   
1541 C CA  . LEU A 184 ? 0.9567 1.4591 0.8265 0.0448  0.0073  -0.0011 184 LEU A CA  
1542 C C   . LEU A 184 ? 0.9300 1.3928 0.8046 0.0350  0.0082  -0.0092 184 LEU A C   
1543 O O   . LEU A 184 ? 0.9820 1.4329 0.8557 0.0299  0.0097  -0.0142 184 LEU A O   
1544 C CB  . LEU A 184 ? 0.9552 1.4939 0.8236 0.0333  0.0045  -0.0118 184 LEU A CB  
1545 C CG  . LEU A 184 ? 0.9482 1.4853 0.8217 0.0155  0.0024  -0.0268 184 LEU A CG  
1546 C CD1 . LEU A 184 ? 0.9291 1.4786 0.8057 0.0163  0.0003  -0.0253 184 LEU A CD1 
1547 C CD2 . LEU A 184 ? 0.9740 1.5387 0.8453 0.0024  0.0016  -0.0390 184 LEU A CD2 
1548 N N   . ASN A 185 ? 0.8886 1.3319 0.7680 0.0327  0.0075  -0.0102 185 ASN A N   
1549 C CA  . ASN A 185 ? 0.8340 1.2414 0.7181 0.0241  0.0081  -0.0172 185 ASN A CA  
1550 C C   . ASN A 185 ? 0.7953 1.2051 0.6834 0.0096  0.0056  -0.0292 185 ASN A C   
1551 O O   . ASN A 185 ? 0.8205 1.2431 0.7099 0.0094  0.0038  -0.0285 185 ASN A O   
1552 C CB  . ASN A 185 ? 0.8561 1.2339 0.7421 0.0336  0.0099  -0.0082 185 ASN A CB  
1553 C CG  . ASN A 185 ? 0.8939 1.2380 0.7815 0.0324  0.0123  -0.0095 185 ASN A CG  
1554 O OD1 . ASN A 185 ? 0.8724 1.2162 0.7571 0.0349  0.0144  -0.0083 185 ASN A OD1 
1555 N ND2 . ASN A 185 ? 0.9132 1.2297 0.8056 0.0286  0.0120  -0.0121 185 ASN A ND2 
1556 N N   . ILE A 186 ? 0.7352 1.1324 0.6249 -0.0024 0.0062  -0.0402 186 ILE A N   
1557 C CA  . ILE A 186 ? 0.7219 1.1162 0.6148 -0.0167 0.0052  -0.0519 186 ILE A CA  
1558 C C   . ILE A 186 ? 0.7368 1.0925 0.6343 -0.0187 0.0059  -0.0528 186 ILE A C   
1559 O O   . ILE A 186 ? 0.7514 1.0830 0.6499 -0.0181 0.0076  -0.0532 186 ILE A O   
1560 C CB  . ILE A 186 ? 0.6828 1.0899 0.5742 -0.0297 0.0062  -0.0644 186 ILE A CB  
1561 C CG1 . ILE A 186 ? 0.6750 1.1247 0.5619 -0.0286 0.0051  -0.0640 186 ILE A CG1 
1562 C CG2 . ILE A 186 ? 0.6701 1.0685 0.5644 -0.0448 0.0067  -0.0766 186 ILE A CG2 
1563 C CD1 . ILE A 186 ? 0.6692 1.1324 0.5533 -0.0387 0.0066  -0.0742 186 ILE A CD1 
1564 N N   . ILE A 187 ? 0.7762 1.1274 0.6762 -0.0206 0.0045  -0.0528 187 ILE A N   
1565 C CA  . ILE A 187 ? 0.7792 1.0965 0.6831 -0.0221 0.0048  -0.0529 187 ILE A CA  
1566 C C   . ILE A 187 ? 0.7719 1.0843 0.6775 -0.0365 0.0050  -0.0644 187 ILE A C   
1567 O O   . ILE A 187 ? 0.7867 1.1207 0.6915 -0.0422 0.0041  -0.0684 187 ILE A O   
1568 C CB  . ILE A 187 ? 0.8086 1.1212 0.7136 -0.0126 0.0037  -0.0433 187 ILE A CB  
1569 C CG1 . ILE A 187 ? 0.8026 1.1248 0.7048 0.0020  0.0045  -0.0314 187 ILE A CG1 
1570 C CG2 . ILE A 187 ? 0.7989 1.0768 0.7074 -0.0135 0.0039  -0.0429 187 ILE A CG2 
1571 C CD1 . ILE A 187 ? 0.8343 1.1355 0.7360 0.0079  0.0068  -0.0274 187 ILE A CD1 
1572 N N   . PRO A 188 ? 0.8040 1.0879 0.7120 -0.0421 0.0065  -0.0696 188 PRO A N   
1573 C CA  . PRO A 188 ? 0.8466 1.1213 0.7558 -0.0546 0.0076  -0.0792 188 PRO A CA  
1574 C C   . PRO A 188 ? 0.9025 1.1697 0.8133 -0.0533 0.0060  -0.0754 188 PRO A C   
1575 O O   . PRO A 188 ? 0.9142 1.1629 0.8269 -0.0448 0.0049  -0.0675 188 PRO A O   
1576 C CB  . PRO A 188 ? 0.8258 1.0700 0.7372 -0.0572 0.0098  -0.0827 188 PRO A CB  
1577 C CG  . PRO A 188 ? 0.8084 1.0517 0.7194 -0.0483 0.0099  -0.0772 188 PRO A CG  
1578 C CD  . PRO A 188 ? 0.7974 1.0566 0.7069 -0.0370 0.0077  -0.0667 188 PRO A CD  
1579 N N   . LYS A 189 ? 0.9908 1.2738 0.9007 -0.0619 0.0060  -0.0813 189 LYS A N   
1580 C CA  . LYS A 189 ? 1.0367 1.3140 0.9478 -0.0623 0.0049  -0.0789 189 LYS A CA  
1581 C C   . LYS A 189 ? 1.1136 1.3765 1.0249 -0.0755 0.0074  -0.0886 189 LYS A C   
1582 O O   . LYS A 189 ? 1.1158 1.3969 1.0254 -0.0859 0.0088  -0.0967 189 LYS A O   
1583 C CB  . LYS A 189 ? 1.0210 1.3310 0.9311 -0.0594 0.0029  -0.0758 189 LYS A CB  
1584 C CG  . LYS A 189 ? 1.0197 1.3355 0.9300 -0.0439 0.0009  -0.0632 189 LYS A CG  
1585 C CD  . LYS A 189 ? 0.9576 1.2451 0.8700 -0.0374 0.0004  -0.0563 189 LYS A CD  
1586 C CE  . LYS A 189 ? 0.9460 1.2328 0.8582 -0.0225 0.0001  -0.0446 189 LYS A CE  
1587 N NZ  . LYS A 189 ? 0.9147 1.1712 0.8288 -0.0175 0.0002  -0.0394 189 LYS A NZ  
1588 N N   . GLN A 190 ? 1.1744 1.4048 1.0874 -0.0750 0.0083  -0.0877 190 GLN A N   
1589 C CA  . GLN A 190 ? 1.2320 1.4431 1.1447 -0.0854 0.0111  -0.0947 190 GLN A CA  
1590 C C   . GLN A 190 ? 1.2571 1.4751 1.1675 -0.0988 0.0154  -0.1069 190 GLN A C   
1591 O O   . GLN A 190 ? 1.3108 1.5121 1.2213 -0.1016 0.0183  -0.1112 190 GLN A O   
1592 C CB  . GLN A 190 ? 1.2951 1.5085 1.2075 -0.0868 0.0099  -0.0926 190 GLN A CB  
1593 C CG  . GLN A 190 ? 1.3645 1.5678 1.2790 -0.0747 0.0065  -0.0814 190 GLN A CG  
1594 C CD  . GLN A 190 ? 1.3805 1.6029 1.2947 -0.0726 0.0045  -0.0777 190 GLN A CD  
1595 O OE1 . GLN A 190 ? 1.4312 1.6773 1.3440 -0.0796 0.0052  -0.0832 190 GLN A OE1 
1596 N NE2 . GLN A 190 ? 1.3803 1.5932 1.2959 -0.0629 0.0023  -0.0687 190 GLN A NE2 
1597 N N   . ASP A 191 ? 1.2549 1.4977 1.1632 -0.1072 0.0162  -0.1129 191 ASP A N   
1598 C CA  . ASP A 191 ? 1.2636 1.5164 1.1693 -0.1212 0.0209  -0.1256 191 ASP A CA  
1599 C C   . ASP A 191 ? 1.2486 1.5361 1.1531 -0.1211 0.0196  -0.1277 191 ASP A C   
1600 O O   . ASP A 191 ? 1.2952 1.5886 1.1978 -0.1298 0.0232  -0.1369 191 ASP A O   
1601 C CB  . ASP A 191 ? 1.2805 1.5371 1.1844 -0.1333 0.0238  -0.1328 191 ASP A CB  
1602 C CG  . ASP A 191 ? 1.3057 1.5620 1.2066 -0.1494 0.0305  -0.1469 191 ASP A CG  
1603 O OD1 . ASP A 191 ? 1.3256 1.5530 1.2260 -0.1525 0.0349  -0.1502 191 ASP A OD1 
1604 O OD2 . ASP A 191 ? 1.2825 1.5679 1.1815 -0.1589 0.0319  -0.1547 191 ASP A OD2 
1605 N N   . ASN A 192 ? 1.1834 1.4937 1.0886 -0.1110 0.0149  -0.1191 192 ASN A N   
1606 C CA  . ASN A 192 ? 1.1304 1.4760 1.0341 -0.1089 0.0133  -0.1193 192 ASN A CA  
1607 C C   . ASN A 192 ? 1.0267 1.3713 0.9311 -0.0937 0.0103  -0.1083 192 ASN A C   
1608 O O   . ASN A 192 ? 0.9890 1.3071 0.8945 -0.0900 0.0113  -0.1063 192 ASN A O   
1609 C CB  . ASN A 192 ? 1.1778 1.5575 1.0810 -0.1102 0.0112  -0.1192 192 ASN A CB  
1610 C CG  . ASN A 192 ? 1.2234 1.6250 1.1244 -0.1271 0.0146  -0.1332 192 ASN A CG  
1611 O OD1 . ASN A 192 ? 1.2545 1.6467 1.1538 -0.1376 0.0189  -0.1431 192 ASN A OD1 
1612 N ND2 . ASN A 192 ? 1.2589 1.6905 1.1599 -0.1299 0.0131  -0.1345 192 ASN A ND2 
1613 N N   . PHE A 193 ? 0.9237 1.2975 0.8274 -0.0849 0.0072  -0.1013 193 PHE A N   
1614 C CA  . PHE A 193 ? 0.8759 1.2510 0.7793 -0.0703 0.0052  -0.0904 193 PHE A CA  
1615 C C   . PHE A 193 ? 0.8622 1.2604 0.7654 -0.0587 0.0021  -0.0801 193 PHE A C   
1616 O O   . PHE A 193 ? 0.8747 1.2921 0.7782 -0.0626 0.0012  -0.0822 193 PHE A O   
1617 C CB  . PHE A 193 ? 0.8186 1.2101 0.7192 -0.0725 0.0063  -0.0947 193 PHE A CB  
1618 C CG  . PHE A 193 ? 0.7638 1.1984 0.6617 -0.0763 0.0053  -0.0984 193 PHE A CG  
1619 C CD1 . PHE A 193 ? 0.7467 1.2078 0.6431 -0.0636 0.0026  -0.0882 193 PHE A CD1 
1620 C CD2 . PHE A 193 ? 0.7591 1.2083 0.6559 -0.0925 0.0076  -0.1121 193 PHE A CD2 
1621 C CE1 . PHE A 193 ? 0.7443 1.2479 0.6383 -0.0664 0.0014  -0.0912 193 PHE A CE1 
1622 C CE2 . PHE A 193 ? 0.7610 1.2527 0.6554 -0.0966 0.0066  -0.1161 193 PHE A CE2 
1623 C CZ  . PHE A 193 ? 0.7579 1.2779 0.6511 -0.0832 0.0031  -0.1054 193 PHE A CZ  
1624 N N   . ARG A 194 ? 0.8860 1.2822 0.7885 -0.0445 0.0012  -0.0691 194 ARG A N   
1625 C CA  . ARG A 194 ? 0.9045 1.3216 0.8062 -0.0318 -0.0006 -0.0583 194 ARG A CA  
1626 C C   . ARG A 194 ? 0.8905 1.3221 0.7890 -0.0214 -0.0004 -0.0513 194 ARG A C   
1627 O O   . ARG A 194 ? 0.8892 1.2983 0.7872 -0.0164 0.0009  -0.0477 194 ARG A O   
1628 C CB  . ARG A 194 ? 0.9784 1.3698 0.8826 -0.0229 -0.0008 -0.0494 194 ARG A CB  
1629 C CG  . ARG A 194 ? 1.0808 1.4924 0.9850 -0.0133 -0.0021 -0.0409 194 ARG A CG  
1630 C CD  . ARG A 194 ? 1.1753 1.5595 1.0813 -0.0041 -0.0016 -0.0320 194 ARG A CD  
1631 N NE  . ARG A 194 ? 1.2850 1.6875 1.1904 0.0082  -0.0017 -0.0219 194 ARG A NE  
1632 C CZ  . ARG A 194 ? 1.3566 1.7415 1.2622 0.0200  -0.0002 -0.0117 194 ARG A CZ  
1633 N NH1 . ARG A 194 ? 1.4243 1.7744 1.3309 0.0206  0.0011  -0.0106 194 ARG A NH1 
1634 N NH2 . ARG A 194 ? 1.3895 1.7926 1.2942 0.0312  0.0002  -0.0029 194 ARG A NH2 
1635 N N   . ALA A 195 ? 0.8516 1.3216 0.7476 -0.0185 -0.0017 -0.0496 195 ALA A N   
1636 C CA  . ALA A 195 ? 0.8537 1.3414 0.7457 -0.0085 -0.0014 -0.0427 195 ALA A CA  
1637 C C   . ALA A 195 ? 0.8717 1.3675 0.7625 0.0091  -0.0015 -0.0277 195 ALA A C   
1638 O O   . ALA A 195 ? 0.8708 1.3996 0.7606 0.0135  -0.0030 -0.0243 195 ALA A O   
1639 C CB  . ALA A 195 ? 0.8604 1.3871 0.7497 -0.0167 -0.0023 -0.0507 195 ALA A CB  
1640 N N   . ILE A 196 ? 0.9193 1.3847 0.8100 0.0191  0.0004  -0.0190 196 ILE A N   
1641 C CA  . ILE A 196 ? 0.9284 1.3943 0.8177 0.0360  0.0018  -0.0047 196 ILE A CA  
1642 C C   . ILE A 196 ? 0.9586 1.4266 0.8428 0.0477  0.0043  0.0042  196 ILE A C   
1643 O O   . ILE A 196 ? 0.9487 1.4104 0.8314 0.0425  0.0050  -0.0005 196 ILE A O   
1644 C CB  . ILE A 196 ? 0.9257 1.3551 0.8183 0.0390  0.0032  -0.0009 196 ILE A CB  
1645 C CG1 . ILE A 196 ? 0.9472 1.3404 0.8407 0.0355  0.0050  -0.0036 196 ILE A CG1 
1646 C CG2 . ILE A 196 ? 0.9362 1.3655 0.8329 0.0290  0.0009  -0.0081 196 ILE A CG2 
1647 C CD1 . ILE A 196 ? 0.9373 1.2965 0.8332 0.0402  0.0068  0.0013  196 ILE A CD1 
1648 N N   . VAL A 197 ? 0.9663 1.4424 0.8477 0.0636  0.0063  0.0175  197 VAL A N   
1649 C CA  . VAL A 197 ? 0.9603 1.4368 0.8362 0.0762  0.0097  0.0276  197 VAL A CA  
1650 C C   . VAL A 197 ? 1.0154 1.4582 0.8906 0.0877  0.0145  0.0380  197 VAL A C   
1651 O O   . VAL A 197 ? 1.0104 1.4454 0.8875 0.0936  0.0156  0.0433  197 VAL A O   
1652 C CB  . VAL A 197 ? 0.9159 1.4341 0.7872 0.0870  0.0093  0.0357  197 VAL A CB  
1653 C CG1 . VAL A 197 ? 0.9151 1.4675 0.7858 0.0753  0.0053  0.0251  197 VAL A CG1 
1654 C CG2 . VAL A 197 ? 0.8851 1.4157 0.7581 0.0958  0.0092  0.0430  197 VAL A CG2 
1655 N N   . SER A 198 ? 1.1030 1.5261 0.9754 0.0902  0.0178  0.0402  198 SER A N   
1656 C CA  . SER A 198 ? 1.1996 1.5935 1.0701 0.1013  0.0235  0.0502  198 SER A CA  
1657 C C   . SER A 198 ? 1.2789 1.6887 1.1420 0.1171  0.0277  0.0632  198 SER A C   
1658 O O   . SER A 198 ? 1.2705 1.6946 1.1294 0.1173  0.0277  0.0630  198 SER A O   
1659 C CB  . SER A 198 ? 1.2110 1.5715 1.0832 0.0940  0.0251  0.0444  198 SER A CB  
1660 O OG  . SER A 198 ? 1.1458 1.4916 1.0244 0.0805  0.0214  0.0332  198 SER A OG  
1661 N N   . ILE A 199 ? 1.3525 1.7602 1.2137 0.1307  0.0316  0.0747  199 ILE A N   
1662 C CA  . ILE A 199 ? 1.4555 1.8765 1.3092 0.1477  0.0367  0.0888  199 ILE A CA  
1663 C C   . ILE A 199 ? 1.5466 1.9345 1.3960 0.1537  0.0440  0.0949  199 ILE A C   
1664 O O   . ILE A 199 ? 1.5434 1.8995 1.3964 0.1452  0.0449  0.0884  199 ILE A O   
1665 C CB  . ILE A 199 ? 1.4459 1.8783 1.2991 0.1608  0.0389  0.0993  199 ILE A CB  
1666 C CG1 . ILE A 199 ? 1.4020 1.8452 1.2625 0.1512  0.0329  0.0907  199 ILE A CG1 
1667 C CG2 . ILE A 199 ? 1.4509 1.9183 1.2974 0.1754  0.0403  0.1106  199 ILE A CG2 
1668 C CD1 . ILE A 199 ? 1.3870 1.8729 1.2488 0.1443  0.0261  0.0840  199 ILE A CD1 
1669 N N   . PHE A 200 ? 1.6601 2.0564 1.5015 0.1683  0.0495  0.1073  200 PHE A N   
1670 C CA  . PHE A 200 ? 1.7769 2.1448 1.6130 0.1740  0.0573  0.1132  200 PHE A CA  
1671 C C   . PHE A 200 ? 1.8586 2.1870 1.6955 0.1784  0.0646  0.1176  200 PHE A C   
1672 O O   . PHE A 200 ? 1.7843 2.0832 1.6210 0.1735  0.0683  0.1144  200 PHE A O   
1673 C CB  . PHE A 200 ? 1.8265 2.2145 1.6530 0.1887  0.0617  0.1258  200 PHE A CB  
1674 C CG  . PHE A 200 ? 1.8617 2.2811 1.6863 0.1826  0.0560  0.1202  200 PHE A CG  
1675 C CD1 . PHE A 200 ? 1.8858 2.2928 1.7093 0.1739  0.0563  0.1136  200 PHE A CD1 
1676 C CD2 . PHE A 200 ? 1.8787 2.3412 1.7028 0.1851  0.0505  0.1212  200 PHE A CD2 
1677 C CE1 . PHE A 200 ? 1.8786 2.3143 1.7001 0.1678  0.0515  0.1079  200 PHE A CE1 
1678 C CE2 . PHE A 200 ? 1.8659 2.3584 1.6880 0.1785  0.0456  0.1153  200 PHE A CE2 
1679 C CZ  . PHE A 200 ? 1.8594 2.3379 1.6800 0.1698  0.0462  0.1086  200 PHE A CZ  
1680 N N   . PRO A 201 ? 1.9962 2.3243 1.8335 0.1873  0.0671  0.1247  201 PRO A N   
1681 C CA  . PRO A 201 ? 2.0743 2.4356 1.9117 0.1952  0.0641  0.1301  201 PRO A CA  
1682 C C   . PRO A 201 ? 2.1466 2.5216 1.9751 0.2152  0.0712  0.1467  201 PRO A C   
1683 O O   . PRO A 201 ? 2.2045 2.6107 2.0287 0.2197  0.0688  0.1501  201 PRO A O   
1684 C CB  . PRO A 201 ? 2.0620 2.4064 1.9053 0.1930  0.0644  0.1280  201 PRO A CB  
1685 C CG  . PRO A 201 ? 2.0247 2.3254 1.8683 0.1896  0.0706  0.1263  201 PRO A CG  
1686 C CD  . PRO A 201 ? 2.0057 2.2966 1.8445 0.1887  0.0737  0.1265  201 PRO A CD  
1687 N N   . ASP A 202 ? 2.1498 2.5014 1.9754 0.2272  0.0803  0.1569  202 ASP A N   
1688 C CA  . ASP A 202 ? 2.1643 2.5245 1.9812 0.2479  0.0886  0.1739  202 ASP A CA  
1689 C C   . ASP A 202 ? 2.2596 2.6656 2.0763 0.2567  0.0835  0.1794  202 ASP A C   
1690 O O   . ASP A 202 ? 2.2886 2.7013 2.1091 0.2611  0.0832  0.1817  202 ASP A O   
1691 C CB  . ASP A 202 ? 2.0676 2.4196 1.8756 0.2536  0.0947  0.1802  202 ASP A CB  
1692 C CG  . ASP A 202 ? 2.0122 2.3607 1.8103 0.2754  0.1061  0.1987  202 ASP A CG  
1693 O OD1 . ASP A 202 ? 1.9659 2.2954 1.7639 0.2838  0.1132  0.2051  202 ASP A OD1 
1694 O OD2 . ASP A 202 ? 1.9736 2.3377 1.7637 0.2843  0.1084  0.2068  202 ASP A OD2 
1695 N N   . SER A 203 ? 2.3142 2.7528 2.1270 0.2585  0.0795  0.1809  203 SER A N   
1696 C CA  . SER A 203 ? 2.3103 2.7977 2.1224 0.2668  0.0744  0.1861  203 SER A CA  
1697 C C   . SER A 203 ? 2.3153 2.8087 2.1240 0.2874  0.0813  0.2019  203 SER A C   
1698 O O   . SER A 203 ? 2.2892 2.7836 2.1040 0.2871  0.0800  0.2002  203 SER A O   
1699 C CB  . SER A 203 ? 2.2867 2.7998 2.1080 0.2501  0.0628  0.1710  203 SER A CB  
1700 O OG  . SER A 203 ? 2.2721 2.7615 2.1009 0.2420  0.0621  0.1641  203 SER A OG  
1701 N N   . ALA A 204 ? 2.3259 2.8241 2.1247 0.3056  0.0890  0.2174  204 ALA A N   
1702 C CA  . ALA A 204 ? 2.3280 2.8212 2.1217 0.3273  0.0989  0.2344  204 ALA A CA  
1703 C C   . ALA A 204 ? 2.3420 2.7855 2.1376 0.3259  0.1074  0.2338  204 ALA A C   
1704 O O   . ALA A 204 ? 2.3938 2.8012 2.1833 0.3295  0.1171  0.2386  204 ALA A O   
1705 C CB  . ALA A 204 ? 2.2860 2.8227 2.0835 0.3354  0.0936  0.2383  204 ALA A CB  
1706 N N   . ARG A 205 ? 2.2803 2.7228 2.0844 0.3200  0.1038  0.2273  205 ARG A N   
1707 C CA  . ARG A 205 ? 2.1960 2.5943 2.0033 0.3148  0.1099  0.2235  205 ARG A CA  
1708 C C   . ARG A 205 ? 2.1150 2.5177 1.9335 0.2976  0.1001  0.2084  205 ARG A C   
1709 O O   . ARG A 205 ? 2.0765 2.5169 1.8997 0.2959  0.0917  0.2054  205 ARG A O   
1710 C CB  . ARG A 205 ? 2.2144 2.5991 2.0168 0.3350  0.1222  0.2390  205 ARG A CB  
1711 C CG  . ARG A 205 ? 2.2471 2.5985 2.0389 0.3467  0.1361  0.2504  205 ARG A CG  
1712 C CD  . ARG A 205 ? 2.2763 2.6327 2.0606 0.3717  0.1472  0.2695  205 ARG A CD  
1713 N NE  . ARG A 205 ? 2.3047 2.6356 2.0774 0.3838  0.1603  0.2815  205 ARG A NE  
1714 C CZ  . ARG A 205 ? 2.3136 2.6499 2.0770 0.4071  0.1707  0.3000  205 ARG A CZ  
1715 N NH1 . ARG A 205 ? 2.3086 2.6768 2.0735 0.4213  0.1692  0.3088  205 ARG A NH1 
1716 N NH2 . ARG A 205 ? 2.3017 2.6118 2.0542 0.4164  0.1831  0.3100  205 ARG A NH2 
1717 N N   . LYS A 206 ? 2.0725 2.4372 1.8949 0.2846  0.1014  0.1988  206 LYS A N   
1718 C CA  . LYS A 206 ? 2.0330 2.3968 1.8652 0.2684  0.0932  0.1850  206 LYS A CA  
1719 C C   . LYS A 206 ? 2.0611 2.4272 1.8966 0.2760  0.0958  0.1894  206 LYS A C   
1720 O O   . LYS A 206 ? 2.0736 2.4581 1.9164 0.2668  0.0876  0.1810  206 LYS A O   
1721 C CB  . LYS A 206 ? 1.9935 2.3181 1.8287 0.2523  0.0934  0.1736  206 LYS A CB  
1722 C CG  . LYS A 206 ? 1.9658 2.2948 1.8104 0.2333  0.0828  0.1579  206 LYS A CG  
1723 C CD  . LYS A 206 ? 1.9584 2.2491 1.8058 0.2193  0.0835  0.1480  206 LYS A CD  
1724 C CE  . LYS A 206 ? 1.9291 2.2231 1.7853 0.2020  0.0737  0.1337  206 LYS A CE  
1725 N NZ  . LYS A 206 ? 1.9220 2.1816 1.7812 0.1889  0.0739  0.1243  206 LYS A NZ  
1726 N N   . PRO A 207 ? 2.1018 2.4483 1.9316 0.2925  0.1080  0.2024  207 PRO A N   
1727 C CA  . PRO A 207 ? 2.0498 2.4008 1.8820 0.3019  0.1115  0.2080  207 PRO A CA  
1728 C C   . PRO A 207 ? 1.9671 2.3670 1.8003 0.3129  0.1065  0.2147  207 PRO A C   
1729 O O   . PRO A 207 ? 1.8975 2.3103 1.7356 0.3154  0.1050  0.2147  207 PRO A O   
1730 C CB  . PRO A 207 ? 2.1095 2.4274 1.9337 0.3178  0.1271  0.2211  207 PRO A CB  
1731 C CG  . PRO A 207 ? 2.1517 2.4629 1.9679 0.3218  0.1311  0.2262  207 PRO A CG  
1732 C CD  . PRO A 207 ? 2.1416 2.4556 1.9628 0.3012  0.1200  0.2110  207 PRO A CD  
1733 N N   . PHE A 208 ? 1.9285 2.3562 1.7569 0.3194  0.1041  0.2202  208 PHE A N   
1734 C CA  . PHE A 208 ? 1.8466 2.3257 1.6759 0.3282  0.0980  0.2252  208 PHE A CA  
1735 C C   . PHE A 208 ? 1.7649 2.2703 1.6040 0.3103  0.0851  0.2100  208 PHE A C   
1736 O O   . PHE A 208 ? 1.7340 2.2709 1.5773 0.3149  0.0817  0.2115  208 PHE A O   
1737 C CB  . PHE A 208 ? 1.8728 2.3754 1.6948 0.3358  0.0973  0.2323  208 PHE A CB  
1738 C CG  . PHE A 208 ? 1.8465 2.4060 1.6698 0.3418  0.0896  0.2352  208 PHE A CG  
1739 C CD1 . PHE A 208 ? 1.8727 2.4562 1.6938 0.3629  0.0943  0.2498  208 PHE A CD1 
1740 C CD2 . PHE A 208 ? 1.8101 2.4002 1.6369 0.3265  0.0781  0.2231  208 PHE A CD2 
1741 C CE1 . PHE A 208 ? 1.8631 2.5020 1.6858 0.3684  0.0870  0.2523  208 PHE A CE1 
1742 C CE2 . PHE A 208 ? 1.8189 2.4632 1.6468 0.3310  0.0712  0.2249  208 PHE A CE2 
1743 C CZ  . PHE A 208 ? 1.8398 2.5096 1.6658 0.3519  0.0753  0.2395  208 PHE A CZ  
1744 N N   . PHE A 209 ? 1.6788 2.1705 1.5212 0.2900  0.0786  0.1954  209 PHE A N   
1745 C CA  . PHE A 209 ? 1.6064 2.1159 1.4575 0.2712  0.0676  0.1798  209 PHE A CA  
1746 C C   . PHE A 209 ? 1.5802 2.0722 1.4376 0.2662  0.0682  0.1752  209 PHE A C   
1747 O O   . PHE A 209 ? 1.5686 2.0878 1.4320 0.2612  0.0619  0.1697  209 PHE A O   
1748 C CB  . PHE A 209 ? 1.5558 2.0508 1.4082 0.2519  0.0619  0.1663  209 PHE A CB  
1749 C CG  . PHE A 209 ? 1.5356 2.0606 1.3843 0.2511  0.0573  0.1658  209 PHE A CG  
1750 C CD1 . PHE A 209 ? 1.5202 2.0950 1.3702 0.2532  0.0511  0.1659  209 PHE A CD1 
1751 C CD2 . PHE A 209 ? 1.5384 2.0431 1.3826 0.2471  0.0593  0.1644  209 PHE A CD2 
1752 C CE1 . PHE A 209 ? 1.4837 2.0873 1.3301 0.2516  0.0469  0.1648  209 PHE A CE1 
1753 C CE2 . PHE A 209 ? 1.5102 2.0425 1.3508 0.2458  0.0553  0.1635  209 PHE A CE2 
1754 C CZ  . PHE A 209 ? 1.4686 2.0504 1.3101 0.2479  0.0491  0.1636  209 PHE A CZ  
1755 N N   . LYS A 210 ? 1.5637 2.0112 1.4196 0.2672  0.0760  0.1770  210 LYS A N   
1756 C CA  . LYS A 210 ? 1.5352 1.9621 1.3967 0.2611  0.0770  0.1717  210 LYS A CA  
1757 C C   . LYS A 210 ? 1.5512 1.9976 1.4139 0.2755  0.0805  0.1808  210 LYS A C   
1758 O O   . LYS A 210 ? 1.5057 1.9573 1.3747 0.2684  0.0767  0.1742  210 LYS A O   
1759 C CB  . LYS A 210 ? 1.5051 1.8813 1.3640 0.2588  0.0851  0.1714  210 LYS A CB  
1760 C CG  . LYS A 210 ? 1.4611 1.8150 1.3262 0.2470  0.0839  0.1621  210 LYS A CG  
1761 C CD  . LYS A 210 ? 1.4308 1.7427 1.2953 0.2355  0.0863  0.1549  210 LYS A CD  
1762 C CE  . LYS A 210 ? 1.3955 1.6894 1.2660 0.2225  0.0836  0.1450  210 LYS A CE  
1763 N NZ  . LYS A 210 ? 1.3531 1.6165 1.2249 0.2077  0.0819  0.1350  210 LYS A NZ  
1764 N N   . LEU A 211 ? 1.6057 2.0628 1.4622 0.2962  0.0879  0.1962  211 LEU A N   
1765 C CA  . LEU A 211 ? 1.6362 2.1169 1.4936 0.3122  0.0913  0.2062  211 LEU A CA  
1766 C C   . LEU A 211 ? 1.6069 2.1438 1.4663 0.3161  0.0831  0.2076  211 LEU A C   
1767 O O   . LEU A 211 ? 1.6405 2.2046 1.5009 0.3304  0.0850  0.2164  211 LEU A O   
1768 C CB  . LEU A 211 ? 1.6875 2.1465 1.5371 0.3341  0.1055  0.2230  211 LEU A CB  
1769 C CG  . LEU A 211 ? 1.6644 2.0794 1.5142 0.3347  0.1152  0.2234  211 LEU A CG  
1770 C CD1 . LEU A 211 ? 1.6305 1.9997 1.4766 0.3250  0.1200  0.2185  211 LEU A CD1 
1771 C CD2 . LEU A 211 ? 1.6513 2.0644 1.4961 0.3586  0.1277  0.2402  211 LEU A CD2 
1772 N N   . LEU A 212 ? 1.5262 2.0809 1.3862 0.3031  0.0742  0.1985  212 LEU A N   
1773 C CA  . LEU A 212 ? 1.4351 2.0433 1.2981 0.3011  0.0651  0.1955  212 LEU A CA  
1774 C C   . LEU A 212 ? 1.3813 1.9997 1.2533 0.2815  0.0562  0.1796  212 LEU A C   
1775 O O   . LEU A 212 ? 1.3370 1.9926 1.2137 0.2832  0.0522  0.1789  212 LEU A O   
1776 C CB  . LEU A 212 ? 1.3955 2.0183 1.2540 0.2966  0.0607  0.1933  212 LEU A CB  
1777 C CG  . LEU A 212 ? 1.3654 2.0453 1.2232 0.3013  0.0544  0.1956  212 LEU A CG  
1778 C CD1 . LEU A 212 ? 1.3261 2.0343 1.1914 0.2803  0.0432  0.1785  212 LEU A CD1 
1779 C CD2 . LEU A 212 ? 1.3883 2.0979 1.2447 0.3241  0.0589  0.2111  212 LEU A CD2 
1780 N N   . THR A 213 ? 1.3909 1.9760 1.2653 0.2630  0.0537  0.1671  213 THR A N   
1781 C CA  . THR A 213 ? 1.3919 1.9785 1.2741 0.2443  0.0467  0.1524  213 THR A CA  
1782 C C   . THR A 213 ? 1.3710 1.9463 1.2568 0.2495  0.0509  0.1553  213 THR A C   
1783 O O   . THR A 213 ? 1.3759 1.9690 1.2679 0.2402  0.0457  0.1472  213 THR A O   
1784 C CB  . THR A 213 ? 1.3891 1.9413 1.2724 0.2245  0.0435  0.1393  213 THR A CB  
1785 O OG1 . THR A 213 ? 1.3857 1.9364 1.2758 0.2082  0.0381  0.1267  213 THR A OG1 
1786 C CG2 . THR A 213 ? 1.4039 1.9069 1.2834 0.2292  0.0518  0.1444  213 THR A CG2 
1787 N N   . SER A 214 ? 1.3769 1.9225 1.2586 0.2639  0.0609  0.1666  214 SER A N   
1788 C CA  . SER A 214 ? 1.3841 1.9178 1.2683 0.2711  0.0665  0.1707  214 SER A CA  
1789 C C   . SER A 214 ? 1.3715 1.9503 1.2582 0.2842  0.0657  0.1780  214 SER A C   
1790 O O   . SER A 214 ? 1.3504 1.9351 1.2422 0.2832  0.0655  0.1758  214 SER A O   
1791 C CB  . SER A 214 ? 1.4086 1.9015 1.2868 0.2843  0.0786  0.1816  214 SER A CB  
1792 O OG  . SER A 214 ? 1.4180 1.8885 1.2990 0.2847  0.0836  0.1811  214 SER A OG  
1793 N N   . LYS A 215 ? 1.3542 1.9658 1.2371 0.2965  0.0652  0.1867  215 LYS A N   
1794 C CA  . LYS A 215 ? 1.3722 2.0335 1.2576 0.3085  0.0632  0.1932  215 LYS A CA  
1795 C C   . LYS A 215 ? 1.3359 2.0336 1.2288 0.2907  0.0519  0.1787  215 LYS A C   
1796 O O   . LYS A 215 ? 1.3404 2.0728 1.2379 0.2955  0.0500  0.1800  215 LYS A O   
1797 C CB  . LYS A 215 ? 1.3998 2.0874 1.2786 0.3261  0.0654  0.2064  215 LYS A CB  
1798 C CG  . LYS A 215 ? 1.4360 2.1056 1.3084 0.3511  0.0780  0.2250  215 LYS A CG  
1799 C CD  . LYS A 215 ? 1.4611 2.1685 1.3279 0.3706  0.0794  0.2391  215 LYS A CD  
1800 C CE  . LYS A 215 ? 1.4519 2.1522 1.3141 0.3973  0.0917  0.2581  215 LYS A CE  
1801 N NZ  . LYS A 215 ? 1.4681 2.2071 1.3245 0.4178  0.0931  0.2730  215 LYS A NZ  
1802 N N   . ILE A 216 ? 1.2538 1.9427 1.1476 0.2701  0.0451  0.1649  216 ILE A N   
1803 C CA  . ILE A 216 ? 1.1867 1.9054 1.0867 0.2511  0.0354  0.1499  216 ILE A CA  
1804 C C   . ILE A 216 ? 1.1851 1.8851 1.0913 0.2380  0.0343  0.1400  216 ILE A C   
1805 O O   . ILE A 216 ? 1.1946 1.9264 1.1064 0.2326  0.0300  0.1343  216 ILE A O   
1806 C CB  . ILE A 216 ? 1.1353 1.8531 1.0336 0.2345  0.0293  0.1389  216 ILE A CB  
1807 C CG1 . ILE A 216 ? 1.1458 1.8942 1.0386 0.2462  0.0290  0.1474  216 ILE A CG1 
1808 C CG2 . ILE A 216 ? 1.1014 1.8412 1.0058 0.2128  0.0208  0.1221  216 ILE A CG2 
1809 C CD1 . ILE A 216 ? 1.1553 1.8897 1.0442 0.2351  0.0263  0.1409  216 ILE A CD1 
1810 N N   . TYR A 217 ? 1.1692 1.8194 1.0743 0.2331  0.0383  0.1381  217 TYR A N   
1811 C CA  . TYR A 217 ? 1.1583 1.7879 1.0683 0.2212  0.0377  0.1295  217 TYR A CA  
1812 C C   . TYR A 217 ? 1.1918 1.8381 1.1052 0.2333  0.0413  0.1363  217 TYR A C   
1813 O O   . TYR A 217 ? 1.1888 1.8375 1.1075 0.2229  0.0387  0.1281  217 TYR A O   
1814 C CB  . TYR A 217 ? 1.1571 1.7318 1.0646 0.2162  0.0420  0.1279  217 TYR A CB  
1815 C CG  . TYR A 217 ? 1.1449 1.7024 1.0525 0.1967  0.0363  0.1153  217 TYR A CG  
1816 C CD1 . TYR A 217 ? 1.1500 1.7092 1.0623 0.1773  0.0299  0.1013  217 TYR A CD1 
1817 C CD2 . TYR A 217 ? 1.1697 1.7088 1.0722 0.1980  0.0377  0.1176  217 TYR A CD2 
1818 C CE1 . TYR A 217 ? 1.1367 1.6796 1.0489 0.1604  0.0253  0.0903  217 TYR A CE1 
1819 C CE2 . TYR A 217 ? 1.1451 1.6688 1.0478 0.1808  0.0328  0.1062  217 TYR A CE2 
1820 C CZ  . TYR A 217 ? 1.1136 1.6391 1.0212 0.1625  0.0267  0.0928  217 TYR A CZ  
1821 O OH  . TYR A 217 ? 1.0941 1.6038 1.0018 0.1464  0.0225  0.0821  217 TYR A OH  
1822 N N   . LYS A 218 ? 1.2447 1.9023 1.1548 0.2556  0.0478  0.1515  218 LYS A N   
1823 C CA  . LYS A 218 ? 1.2554 1.9393 1.1688 0.2695  0.0509  0.1592  218 LYS A CA  
1824 C C   . LYS A 218 ? 1.2421 1.9786 1.1613 0.2613  0.0423  0.1514  218 LYS A C   
1825 O O   . LYS A 218 ? 1.2559 2.0005 1.1809 0.2519  0.0397  0.1434  218 LYS A O   
1826 C CB  . LYS A 218 ? 1.3037 1.9954 1.2118 0.2957  0.0590  0.1776  218 LYS A CB  
1827 C CG  . LYS A 218 ? 1.3659 2.0069 1.2681 0.3059  0.0698  0.1866  218 LYS A CG  
1828 C CD  . LYS A 218 ? 1.3938 2.0448 1.2904 0.3325  0.0785  0.2052  218 LYS A CD  
1829 C CE  . LYS A 218 ? 1.4030 2.0027 1.2924 0.3410  0.0898  0.2133  218 LYS A CE  
1830 N NZ  . LYS A 218 ? 1.4260 2.0333 1.3090 0.3674  0.0994  0.2320  218 LYS A NZ  
1831 N N   . VAL A 219 ? 1.2292 2.0008 1.1463 0.2639  0.0380  0.1529  219 VAL A N   
1832 C CA  . VAL A 219 ? 1.2145 2.0413 1.1365 0.2568  0.0302  0.1457  219 VAL A CA  
1833 C C   . VAL A 219 ? 1.2098 2.0343 1.1374 0.2315  0.0238  0.1275  219 VAL A C   
1834 O O   . VAL A 219 ? 1.1982 2.0587 1.1315 0.2261  0.0201  0.1216  219 VAL A O   
1835 C CB  . VAL A 219 ? 1.1805 2.0376 1.0986 0.2577  0.0258  0.1465  219 VAL A CB  
1836 C CG1 . VAL A 219 ? 1.1436 2.0616 1.0665 0.2521  0.0187  0.1401  219 VAL A CG1 
1837 C CG2 . VAL A 219 ? 1.2045 2.0597 1.1158 0.2824  0.0326  0.1650  219 VAL A CG2 
1838 N N   . LEU A 220 ? 1.2144 1.9964 1.1401 0.2162  0.0229  0.1188  220 LEU A N   
1839 C CA  . LEU A 220 ? 1.2057 1.9789 1.1356 0.1924  0.0178  0.1022  220 LEU A CA  
1840 C C   . LEU A 220 ? 1.2154 1.9851 1.1503 0.1913  0.0197  0.1006  220 LEU A C   
1841 O O   . LEU A 220 ? 1.1965 1.9894 1.1362 0.1777  0.0153  0.0898  220 LEU A O   
1842 C CB  . LEU A 220 ? 1.2002 1.9241 1.1267 0.1802  0.0179  0.0961  220 LEU A CB  
1843 C CG  . LEU A 220 ? 1.1983 1.9231 1.1257 0.1570  0.0113  0.0801  220 LEU A CG  
1844 C CD1 . LEU A 220 ? 1.1950 1.8676 1.1196 0.1480  0.0125  0.0760  220 LEU A CD1 
1845 C CD2 . LEU A 220 ? 1.1904 1.9359 1.1235 0.1414  0.0073  0.0680  220 LEU A CD2 
1846 N N   . GLU A 221 ? 1.2618 2.0026 1.1953 0.2054  0.0269  0.1110  221 GLU A N   
1847 C CA  . GLU A 221 ? 1.2994 2.0351 1.2372 0.2062  0.0298  0.1106  221 GLU A CA  
1848 C C   . GLU A 221 ? 1.3310 2.1039 1.2714 0.2261  0.0332  0.1220  221 GLU A C   
1849 O O   . GLU A 221 ? 1.3815 2.1446 1.3242 0.2334  0.0383  0.1263  221 GLU A O   
1850 C CB  . GLU A 221 ? 1.3319 2.0118 1.2672 0.2065  0.0357  0.1127  221 GLU A CB  
1851 C CG  . GLU A 221 ? 1.3386 1.9904 1.2675 0.2227  0.0427  0.1252  221 GLU A CG  
1852 C CD  . GLU A 221 ? 1.3393 1.9906 1.2675 0.2449  0.0517  0.1395  221 GLU A CD  
1853 O OE1 . GLU A 221 ? 1.2998 1.9364 1.2307 0.2444  0.0553  0.1386  221 GLU A OE1 
1854 O OE2 . GLU A 221 ? 1.3500 2.0145 1.2746 0.2631  0.0557  0.1520  221 GLU A OE2 
1855 N N   . GLU A 222 ? 1.3493 2.1658 1.2893 0.2346  0.0305  0.1267  222 GLU A N   
1856 C CA  . GLU A 222 ? 1.3314 2.1900 1.2742 0.2538  0.0329  0.1374  222 GLU A CA  
1857 C C   . GLU A 222 ? 1.3046 2.2172 1.2537 0.2431  0.0256  0.1275  222 GLU A C   
1858 O O   . GLU A 222 ? 1.2940 2.2204 1.2488 0.2407  0.0258  0.1241  222 GLU A O   
1859 C CB  . GLU A 222 ? 1.3911 2.2626 1.3282 0.2750  0.0363  0.1526  222 GLU A CB  
1860 C CG  . GLU A 222 ? 1.4186 2.2414 1.3493 0.2897  0.0456  0.1648  222 GLU A CG  
1861 C CD  . GLU A 222 ? 1.4526 2.2625 1.3848 0.3058  0.0544  0.1748  222 GLU A CD  
1862 O OE1 . GLU A 222 ? 1.4695 2.3193 1.4063 0.3162  0.0545  0.1794  222 GLU A OE1 
1863 O OE2 . GLU A 222 ? 1.4340 2.1944 1.3628 0.3080  0.0615  0.1779  222 GLU A OE2 
1864 N N   . LYS A 223 ? 1.2866 2.2298 1.2345 0.2361  0.0195  0.1225  223 LYS A N   
1865 C CA  . LYS A 223 ? 1.2796 2.2776 1.2329 0.2253  0.0129  0.1125  223 LYS A CA  
1866 C C   . LYS A 223 ? 1.2605 2.2468 1.2164 0.1966  0.0078  0.0930  223 LYS A C   
1867 O O   . LYS A 223 ? 1.2771 2.3039 1.2372 0.1834  0.0028  0.0820  223 LYS A O   
1868 C CB  . LYS A 223 ? 1.2729 2.3135 1.2234 0.2314  0.0091  0.1160  223 LYS A CB  
1869 C CG  . LYS A 223 ? 1.2585 2.3154 1.2058 0.2608  0.0141  0.1360  223 LYS A CG  
1870 C CD  . LYS A 223 ? 1.2585 2.3406 1.2112 0.2767  0.0177  0.1445  223 LYS A CD  
1871 C CE  . LYS A 223 ? 1.2506 2.3372 1.1991 0.3073  0.0247  0.1658  223 LYS A CE  
1872 N NZ  . LYS A 223 ? 1.2048 2.2977 1.1578 0.3237  0.0306  0.1750  223 LYS A NZ  
1873 N N   . TYR A 224 ? 1.2478 2.1789 1.2011 0.1870  0.0098  0.0890  224 TYR A N   
1874 C CA  . TYR A 224 ? 1.2096 2.1216 1.1648 0.1617  0.0065  0.0723  224 TYR A CA  
1875 C C   . TYR A 224 ? 1.1936 2.0672 1.1504 0.1617  0.0109  0.0733  224 TYR A C   
1876 O O   . TYR A 224 ? 1.1711 1.9984 1.1240 0.1671  0.0150  0.0792  224 TYR A O   
1877 C CB  . TYR A 224 ? 1.1790 2.0612 1.1294 0.1480  0.0040  0.0650  224 TYR A CB  
1878 C CG  . TYR A 224 ? 1.1710 2.0873 1.1190 0.1487  0.0003  0.0646  224 TYR A CG  
1879 C CD1 . TYR A 224 ? 1.1510 2.0645 1.0940 0.1669  0.0026  0.0780  224 TYR A CD1 
1880 C CD2 . TYR A 224 ? 1.1647 2.1164 1.1149 0.1309  -0.0050 0.0507  224 TYR A CD2 
1881 C CE1 . TYR A 224 ? 1.1370 2.0829 1.0773 0.1678  -0.0007 0.0778  224 TYR A CE1 
1882 C CE2 . TYR A 224 ? 1.1241 2.1085 1.0718 0.1310  -0.0082 0.0498  224 TYR A CE2 
1883 C CZ  . TYR A 224 ? 1.1255 2.1074 1.0684 0.1496  -0.0064 0.0636  224 TYR A CZ  
1884 O OH  . TYR A 224 ? 1.0758 2.0909 1.0158 0.1496  -0.0096 0.0627  224 TYR A OH  
1885 N N   . LYS A 225 ? 1.2277 2.1220 1.1901 0.1554  0.0103  0.0674  225 LYS A N   
1886 C CA  . LYS A 225 ? 1.2575 2.1223 1.2218 0.1564  0.0146  0.0686  225 LYS A CA  
1887 C C   . LYS A 225 ? 1.2691 2.0852 1.2310 0.1375  0.0140  0.0584  225 LYS A C   
1888 O O   . LYS A 225 ? 1.2438 2.0431 1.2079 0.1308  0.0157  0.0543  225 LYS A O   
1889 C CB  . LYS A 225 ? 1.2302 2.1342 1.2012 0.1549  0.0141  0.0650  225 LYS A CB  
1890 C CG  . LYS A 225 ? 1.2290 2.1665 1.2027 0.1792  0.0177  0.0791  225 LYS A CG  
1891 C CD  . LYS A 225 ? 1.2169 2.1849 1.1976 0.1774  0.0181  0.0753  225 LYS A CD  
1892 C CE  . LYS A 225 ? 1.1876 2.1901 1.1713 0.2028  0.0220  0.0898  225 LYS A CE  
1893 N NZ  . LYS A 225 ? 1.1354 2.1723 1.1265 0.2008  0.0220  0.0855  225 LYS A NZ  
1894 N N   . THR A 226 ? 1.2659 2.0602 1.2234 0.1297  0.0117  0.0549  226 THR A N   
1895 C CA  . THR A 226 ? 1.2508 1.9995 1.2057 0.1133  0.0111  0.0462  226 THR A CA  
1896 C C   . THR A 226 ? 1.2610 1.9635 1.2133 0.1232  0.0166  0.0548  226 THR A C   
1897 O O   . THR A 226 ? 1.2216 1.9164 1.1714 0.1413  0.0207  0.0671  226 THR A O   
1898 C CB  . THR A 226 ? 1.2576 1.9969 1.2086 0.1037  0.0075  0.0408  226 THR A CB  
1899 O OG1 . THR A 226 ? 1.2369 2.0239 1.1893 0.1015  0.0037  0.0372  226 THR A OG1 
1900 C CG2 . THR A 226 ? 1.2517 1.9593 1.2016 0.0819  0.0054  0.0278  226 THR A CG2 
1901 N N   . SER A 227 ? 1.2708 1.9434 1.2234 0.1111  0.0171  0.0480  227 SER A N   
1902 C CA  . SER A 227 ? 1.2756 1.9017 1.2253 0.1163  0.0218  0.0534  227 SER A CA  
1903 C C   . SER A 227 ? 1.2580 1.8463 1.2044 0.1002  0.0193  0.0450  227 SER A C   
1904 O O   . SER A 227 ? 1.2642 1.8338 1.2070 0.1030  0.0193  0.0479  227 SER A O   
1905 C CB  . SER A 227 ? 1.2875 1.9098 1.2401 0.1180  0.0254  0.0541  227 SER A CB  
1906 O OG  . SER A 227 ? 1.2950 1.9278 1.2503 0.1000  0.0217  0.0420  227 SER A OG  
1907 N N   . GLY A 228 ? 1.1852 1.7630 1.1326 0.0838  0.0173  0.0349  228 GLY A N   
1908 C CA  . GLY A 228 ? 1.0918 1.6394 1.0365 0.0676  0.0145  0.0262  228 GLY A CA  
1909 C C   . GLY A 228 ? 1.0291 1.5297 0.9702 0.0700  0.0173  0.0299  228 GLY A C   
1910 O O   . GLY A 228 ? 1.0726 1.5592 1.0114 0.0817  0.0198  0.0379  228 GLY A O   
1911 N N   . SER A 229 ? 0.8888 1.3661 0.8294 0.0585  0.0172  0.0239  229 SER A N   
1912 C CA  . SER A 229 ? 0.8170 1.2509 0.7542 0.0550  0.0181  0.0238  229 SER A CA  
1913 C C   . SER A 229 ? 0.7119 1.1322 0.6481 0.0362  0.0147  0.0130  229 SER A C   
1914 O O   . SER A 229 ? 0.6977 1.1238 0.6352 0.0291  0.0149  0.0087  229 SER A O   
1915 C CB  . SER A 229 ? 0.8201 1.2338 0.7566 0.0650  0.0235  0.0308  229 SER A CB  
1916 O OG  . SER A 229 ? 0.8005 1.1755 0.7340 0.0585  0.0238  0.0286  229 SER A OG  
1917 N N   . LEU A 230 ? 0.6413 1.0438 0.5752 0.0284  0.0121  0.0089  230 LEU A N   
1918 C CA  . LEU A 230 ? 0.6188 1.0090 0.5512 0.0110  0.0093  -0.0010 230 LEU A CA  
1919 C C   . LEU A 230 ? 0.5940 0.9642 0.5255 0.0054  0.0108  -0.0027 230 LEU A C   
1920 O O   . LEU A 230 ? 0.5911 0.9676 0.5227 -0.0065 0.0098  -0.0098 230 LEU A O   
1921 C CB  . LEU A 230 ? 0.6095 0.9748 0.5393 0.0070  0.0076  -0.0028 230 LEU A CB  
1922 C CG  . LEU A 230 ? 0.6132 0.9817 0.5421 -0.0077 0.0046  -0.0125 230 LEU A CG  
1923 C CD1 . LEU A 230 ? 0.5872 0.9213 0.5133 -0.0119 0.0037  -0.0138 230 LEU A CD1 
1924 C CD2 . LEU A 230 ? 0.5952 0.9732 0.5243 -0.0212 0.0043  -0.0207 230 LEU A CD2 
1925 N N   . TYR A 231 ? 0.5801 0.9266 0.5103 0.0140  0.0135  0.0037  231 TYR A N   
1926 C CA  . TYR A 231 ? 0.5685 0.8946 0.4972 0.0096  0.0150  0.0027  231 TYR A CA  
1927 C C   . TYR A 231 ? 0.5829 0.9312 0.5140 0.0097  0.0168  0.0022  231 TYR A C   
1928 O O   . TYR A 231 ? 0.5999 0.9438 0.5301 -0.0012 0.0163  -0.0034 231 TYR A O   
1929 C CB  . TYR A 231 ? 0.5498 0.8485 0.4766 0.0191  0.0182  0.0096  231 TYR A CB  
1930 C CG  . TYR A 231 ? 0.5293 0.8074 0.4542 0.0144  0.0198  0.0084  231 TYR A CG  
1931 C CD1 . TYR A 231 ? 0.5168 0.7691 0.4385 0.0039  0.0175  0.0040  231 TYR A CD1 
1932 C CD2 . TYR A 231 ? 0.5237 0.8090 0.4499 0.0207  0.0237  0.0118  231 TYR A CD2 
1933 C CE1 . TYR A 231 ? 0.5038 0.7387 0.4233 -0.0002 0.0188  0.0031  231 TYR A CE1 
1934 C CE2 . TYR A 231 ? 0.5331 0.8002 0.4571 0.0159  0.0253  0.0104  231 TYR A CE2 
1935 C CZ  . TYR A 231 ? 0.5317 0.7740 0.4522 0.0052  0.0226  0.0061  231 TYR A CZ  
1936 O OH  . TYR A 231 ? 0.5532 0.7786 0.4711 0.0004  0.0240  0.0048  231 TYR A OH  
1937 N N   . THR A 232 ? 0.5994 0.9712 0.5335 0.0226  0.0192  0.0083  232 THR A N   
1938 C CA  . THR A 232 ? 0.6118 1.0080 0.5490 0.0246  0.0212  0.0084  232 THR A CA  
1939 C C   . THR A 232 ? 0.5905 1.0128 0.5295 0.0115  0.0180  -0.0004 232 THR A C   
1940 O O   . THR A 232 ? 0.6009 1.0276 0.5404 0.0035  0.0187  -0.0049 232 THR A O   
1941 C CB  . THR A 232 ? 0.6263 1.0451 0.5664 0.0424  0.0245  0.0175  232 THR A CB  
1942 O OG1 . THR A 232 ? 0.6712 1.0641 0.6090 0.0540  0.0283  0.0254  232 THR A OG1 
1943 C CG2 . THR A 232 ? 0.6262 1.0658 0.5695 0.0458  0.0273  0.0184  232 THR A CG2 
1944 N N   . CYS A 233 ? 0.5788 1.0176 0.5183 0.0086  0.0151  -0.0034 233 CYS A N   
1945 C CA  . CYS A 233 ? 0.5935 1.0578 0.5344 -0.0047 0.0127  -0.0128 233 CYS A CA  
1946 C C   . CYS A 233 ? 0.5803 1.0221 0.5181 -0.0219 0.0121  -0.0213 233 CYS A C   
1947 O O   . CYS A 233 ? 0.5779 1.0316 0.5166 -0.0303 0.0131  -0.0265 233 CYS A O   
1948 C CB  . CYS A 233 ? 0.6302 1.1108 0.5714 -0.0060 0.0099  -0.0152 233 CYS A CB  
1949 S SG  . CYS A 233 ? 0.6490 1.1661 0.5936 0.0123  0.0102  -0.0063 233 CYS A SG  
1950 N N   . TRP A 234 ? 0.5691 0.9780 0.5029 -0.0263 0.0110  -0.0222 234 TRP A N   
1951 C CA  . TRP A 234 ? 0.5505 0.9357 0.4805 -0.0414 0.0107  -0.0292 234 TRP A CA  
1952 C C   . TRP A 234 ? 0.5530 0.9263 0.4820 -0.0428 0.0128  -0.0282 234 TRP A C   
1953 O O   . TRP A 234 ? 0.5662 0.9368 0.4932 -0.0557 0.0134  -0.0348 234 TRP A O   
1954 C CB  . TRP A 234 ? 0.5323 0.8844 0.4587 -0.0426 0.0092  -0.0283 234 TRP A CB  
1955 C CG  . TRP A 234 ? 0.5098 0.8379 0.4319 -0.0571 0.0091  -0.0349 234 TRP A CG  
1956 C CD1 . TRP A 234 ? 0.4875 0.7842 0.4060 -0.0590 0.0096  -0.0331 234 TRP A CD1 
1957 C CD2 . TRP A 234 ? 0.5060 0.8391 0.4264 -0.0721 0.0090  -0.0443 234 TRP A CD2 
1958 N NE1 . TRP A 234 ? 0.4899 0.7719 0.4045 -0.0727 0.0097  -0.0397 234 TRP A NE1 
1959 C CE2 . TRP A 234 ? 0.5115 0.8130 0.4269 -0.0813 0.0097  -0.0468 234 TRP A CE2 
1960 C CE3 . TRP A 234 ? 0.5049 0.8648 0.4270 -0.0788 0.0088  -0.0510 234 TRP A CE3 
1961 C CZ2 . TRP A 234 ? 0.5160 0.8114 0.4282 -0.0960 0.0109  -0.0551 234 TRP A CZ2 
1962 C CZ3 . TRP A 234 ? 0.5075 0.8612 0.4264 -0.0948 0.0100  -0.0603 234 TRP A CZ3 
1963 C CH2 . TRP A 234 ? 0.5063 0.8273 0.4202 -0.1029 0.0114  -0.0621 234 TRP A CH2 
1964 N N   . SER A 235 ? 0.5520 0.9176 0.4819 -0.0299 0.0146  -0.0201 235 SER A N   
1965 C CA  . SER A 235 ? 0.5734 0.9260 0.5019 -0.0304 0.0171  -0.0188 235 SER A CA  
1966 C C   . SER A 235 ? 0.5969 0.9790 0.5285 -0.0334 0.0187  -0.0219 235 SER A C   
1967 O O   . SER A 235 ? 0.5862 0.9631 0.5159 -0.0445 0.0195  -0.0271 235 SER A O   
1968 C CB  . SER A 235 ? 0.5654 0.9031 0.4940 -0.0158 0.0195  -0.0098 235 SER A CB  
1969 O OG  . SER A 235 ? 0.5742 0.8980 0.5012 -0.0172 0.0220  -0.0092 235 SER A OG  
1970 N N   . GLU A 236 ? 0.6081 1.0220 0.5446 -0.0233 0.0193  -0.0186 236 GLU A N   
1971 C CA  . GLU A 236 ? 0.6233 1.0699 0.5637 -0.0250 0.0208  -0.0214 236 GLU A CA  
1972 C C   . GLU A 236 ? 0.5959 1.0566 0.5358 -0.0425 0.0192  -0.0322 236 GLU A C   
1973 O O   . GLU A 236 ? 0.5990 1.0682 0.5392 -0.0510 0.0209  -0.0372 236 GLU A O   
1974 C CB  . GLU A 236 ? 0.6683 1.1480 0.6140 -0.0097 0.0215  -0.0151 236 GLU A CB  
1975 C CG  . GLU A 236 ? 0.7276 1.2006 0.6745 0.0064  0.0256  -0.0055 236 GLU A CG  
1976 C CD  . GLU A 236 ? 0.7649 1.2599 0.7152 0.0242  0.0268  0.0031  236 GLU A CD  
1977 O OE1 . GLU A 236 ? 0.7878 1.2676 0.7375 0.0381  0.0306  0.0117  236 GLU A OE1 
1978 O OE2 . GLU A 236 ? 0.7720 1.2996 0.7252 0.0244  0.0244  0.0013  236 GLU A OE2 
1979 N N   . PHE A 237 ? 0.5826 1.0435 0.5212 -0.0485 0.0166  -0.0363 237 PHE A N   
1980 C CA  . PHE A 237 ? 0.5753 1.0464 0.5127 -0.0661 0.0161  -0.0472 237 PHE A CA  
1981 C C   . PHE A 237 ? 0.5945 1.0363 0.5266 -0.0802 0.0176  -0.0527 237 PHE A C   
1982 O O   . PHE A 237 ? 0.6427 1.0970 0.5746 -0.0918 0.0195  -0.0597 237 PHE A O   
1983 C CB  . PHE A 237 ? 0.5636 1.0373 0.5001 -0.0690 0.0136  -0.0502 237 PHE A CB  
1984 C CG  . PHE A 237 ? 0.5731 1.0528 0.5075 -0.0878 0.0141  -0.0620 237 PHE A CG  
1985 C CD1 . PHE A 237 ? 0.5873 1.1064 0.5252 -0.0950 0.0149  -0.0691 237 PHE A CD1 
1986 C CD2 . PHE A 237 ? 0.5709 1.0174 0.4998 -0.0985 0.0145  -0.0662 237 PHE A CD2 
1987 C CE1 . PHE A 237 ? 0.5855 1.1091 0.5210 -0.1133 0.0164  -0.0808 237 PHE A CE1 
1988 C CE2 . PHE A 237 ? 0.5842 1.0339 0.5106 -0.1158 0.0162  -0.0771 237 PHE A CE2 
1989 C CZ  . PHE A 237 ? 0.5942 1.0818 0.5237 -0.1237 0.0174  -0.0848 237 PHE A CZ  
1990 N N   . THR A 238 ? 0.5754 0.9792 0.5029 -0.0794 0.0169  -0.0494 238 THR A N   
1991 C CA  . THR A 238 ? 0.5672 0.9421 0.4889 -0.0919 0.0182  -0.0536 238 THR A CA  
1992 C C   . THR A 238 ? 0.5885 0.9634 0.5097 -0.0935 0.0208  -0.0531 238 THR A C   
1993 O O   . THR A 238 ? 0.5765 0.9453 0.4942 -0.1068 0.0228  -0.0594 238 THR A O   
1994 C CB  . THR A 238 ? 0.5589 0.8949 0.4761 -0.0891 0.0167  -0.0492 238 THR A CB  
1995 O OG1 . THR A 238 ? 0.5501 0.8767 0.4686 -0.0748 0.0165  -0.0403 238 THR A OG1 
1996 C CG2 . THR A 238 ? 0.5319 0.8652 0.4490 -0.0898 0.0146  -0.0509 238 THR A CG2 
1997 N N   . GLN A 239 ? 0.6087 0.9897 0.5332 -0.0800 0.0213  -0.0458 239 GLN A N   
1998 C CA  . GLN A 239 ? 0.6461 1.0250 0.5702 -0.0802 0.0240  -0.0448 239 GLN A CA  
1999 C C   . GLN A 239 ? 0.6832 1.0945 0.6104 -0.0878 0.0261  -0.0511 239 GLN A C   
2000 O O   . GLN A 239 ? 0.7034 1.1092 0.6282 -0.0958 0.0285  -0.0542 239 GLN A O   
2001 C CB  . GLN A 239 ? 0.6574 1.0320 0.5837 -0.0637 0.0251  -0.0355 239 GLN A CB  
2002 C CG  . GLN A 239 ? 0.7100 1.0510 0.6328 -0.0573 0.0238  -0.0298 239 GLN A CG  
2003 C CD  . GLN A 239 ? 0.7245 1.0330 0.6406 -0.0685 0.0231  -0.0328 239 GLN A CD  
2004 O OE1 . GLN A 239 ? 0.7559 1.0525 0.6689 -0.0730 0.0249  -0.0333 239 GLN A OE1 
2005 N NE2 . GLN A 239 ? 0.6872 0.9812 0.6008 -0.0727 0.0205  -0.0344 239 GLN A NE2 
2006 N N   . LYS A 240 ? 0.7016 1.1474 0.6340 -0.0859 0.0252  -0.0534 240 LYS A N   
2007 C CA  . LYS A 240 ? 0.7311 1.2108 0.6668 -0.0945 0.0269  -0.0606 240 LYS A CA  
2008 C C   . LYS A 240 ? 0.7457 1.2251 0.6779 -0.1140 0.0277  -0.0716 240 LYS A C   
2009 O O   . LYS A 240 ? 0.8387 1.3348 0.7713 -0.1250 0.0304  -0.0787 240 LYS A O   
2010 C CB  . LYS A 240 ? 0.7230 1.2452 0.6664 -0.0833 0.0261  -0.0581 240 LYS A CB  
2011 C CG  . LYS A 240 ? 0.7099 1.2442 0.6546 -0.0803 0.0230  -0.0581 240 LYS A CG  
2012 C CD  . LYS A 240 ? 0.7335 1.3053 0.6851 -0.0646 0.0223  -0.0522 240 LYS A CD  
2013 C CE  . LYS A 240 ? 0.7565 1.3419 0.7090 -0.0607 0.0193  -0.0515 240 LYS A CE  
2014 N NZ  . LYS A 240 ? 0.7355 1.3576 0.6940 -0.0442 0.0188  -0.0446 240 LYS A NZ  
2015 N N   . THR A 241 ? 0.7411 1.2003 0.6694 -0.1184 0.0261  -0.0732 241 THR A N   
2016 C CA  . THR A 241 ? 0.7432 1.1999 0.6677 -0.1364 0.0277  -0.0836 241 THR A CA  
2017 C C   . THR A 241 ? 0.7796 1.1981 0.6963 -0.1470 0.0302  -0.0855 241 THR A C   
2018 O O   . THR A 241 ? 0.8007 1.1856 0.7131 -0.1435 0.0288  -0.0808 241 THR A O   
2019 C CB  . THR A 241 ? 0.7470 1.2025 0.6712 -0.1366 0.0254  -0.0852 241 THR A CB  
2020 O OG1 . THR A 241 ? 0.7424 1.2279 0.6730 -0.1230 0.0226  -0.0804 241 THR A OG1 
2021 C CG2 . THR A 241 ? 0.7586 1.2234 0.6805 -0.1551 0.0281  -0.0973 241 THR A CG2 
2022 N N   . GLN A 242 ? 0.8082 1.2330 0.7229 -0.1599 0.0341  -0.0924 242 GLN A N   
2023 C CA  . GLN A 242 ? 0.8119 1.2028 0.7188 -0.1696 0.0372  -0.0937 242 GLN A CA  
2024 C C   . GLN A 242 ? 0.7736 1.1462 0.6742 -0.1847 0.0399  -0.1012 242 GLN A C   
2025 O O   . GLN A 242 ? 0.7557 1.0920 0.6492 -0.1877 0.0409  -0.0990 242 GLN A O   
2026 C CB  . GLN A 242 ? 0.8829 1.2867 0.7900 -0.1758 0.0407  -0.0967 242 GLN A CB  
2027 C CG  . GLN A 242 ? 0.9445 1.3605 0.8568 -0.1608 0.0390  -0.0888 242 GLN A CG  
2028 C CD  . GLN A 242 ? 1.0484 1.4765 0.9610 -0.1670 0.0428  -0.0920 242 GLN A CD  
2029 O OE1 . GLN A 242 ? 1.0922 1.5516 1.0083 -0.1754 0.0451  -0.0997 242 GLN A OE1 
2030 N NE2 . GLN A 242 ? 1.0705 1.4750 0.9793 -0.1631 0.0436  -0.0865 242 GLN A NE2 
2031 N N   . GLY A 243 ? 0.7303 1.1287 0.6334 -0.1939 0.0414  -0.1101 243 GLY A N   
2032 C CA  . GLY A 243 ? 0.7171 1.1005 0.6144 -0.2090 0.0452  -0.1184 243 GLY A CA  
2033 C C   . GLY A 243 ? 0.7202 1.0870 0.6166 -0.2036 0.0423  -0.1158 243 GLY A C   
2034 O O   . GLY A 243 ? 0.6998 1.0670 0.6001 -0.1881 0.0372  -0.1073 243 GLY A O   
2035 N N   . GLN A 244 ? 0.7037 1.0556 0.5948 -0.2169 0.0464  -0.1233 244 GLN A N   
2036 C CA  . GLN A 244 ? 0.6883 1.0226 0.5778 -0.2142 0.0449  -0.1223 244 GLN A CA  
2037 C C   . GLN A 244 ? 0.6817 1.0477 0.5787 -0.2056 0.0403  -0.1218 244 GLN A C   
2038 O O   . GLN A 244 ? 0.7367 1.1385 0.6376 -0.2121 0.0414  -0.1294 244 GLN A O   
2039 C CB  . GLN A 244 ? 0.6842 1.0023 0.5670 -0.2319 0.0517  -0.1323 244 GLN A CB  
2040 C CG  . GLN A 244 ? 0.6795 0.9819 0.5607 -0.2311 0.0512  -0.1331 244 GLN A CG  
2041 C CD  . GLN A 244 ? 0.6592 0.9238 0.5372 -0.2197 0.0481  -0.1227 244 GLN A CD  
2042 O OE1 . GLN A 244 ? 0.6487 0.8853 0.5210 -0.2206 0.0501  -0.1188 244 GLN A OE1 
2043 N NE2 . GLN A 244 ? 0.6519 0.9164 0.5334 -0.2092 0.0434  -0.1184 244 GLN A NE2 
2044 N N   . ILE A 245 ? 0.6413 0.9952 0.5400 -0.1911 0.0353  -0.1129 245 ILE A N   
2045 C CA  . ILE A 245 ? 0.6043 0.9843 0.5091 -0.1818 0.0311  -0.1113 245 ILE A CA  
2046 C C   . ILE A 245 ? 0.6206 0.9976 0.5233 -0.1908 0.0329  -0.1188 245 ILE A C   
2047 O O   . ILE A 245 ? 0.6638 1.0065 0.5610 -0.1946 0.0348  -0.1189 245 ILE A O   
2048 C CB  . ILE A 245 ? 0.5833 0.9508 0.4905 -0.1628 0.0259  -0.0988 245 ILE A CB  
2049 C CG1 . ILE A 245 ? 0.5737 0.9524 0.4843 -0.1528 0.0245  -0.0920 245 ILE A CG1 
2050 C CG2 . ILE A 245 ? 0.5749 0.9609 0.4865 -0.1541 0.0223  -0.0971 245 ILE A CG2 
2051 C CD1 . ILE A 245 ? 0.5569 0.9129 0.4677 -0.1371 0.0212  -0.0806 245 ILE A CD1 
2052 N N   . TYR A 246 ? 0.6015 1.0151 0.5083 -0.1945 0.0327  -0.1253 246 TYR A N   
2053 C CA  . TYR A 246 ? 0.5983 1.0138 0.5040 -0.2007 0.0336  -0.1317 246 TYR A CA  
2054 C C   . TYR A 246 ? 0.5830 1.0183 0.4941 -0.1854 0.0278  -0.1250 246 TYR A C   
2055 O O   . TYR A 246 ? 0.5837 1.0455 0.5001 -0.1744 0.0244  -0.1193 246 TYR A O   
2056 C CB  . TYR A 246 ? 0.6358 1.0785 0.5411 -0.2189 0.0387  -0.1458 246 TYR A CB  
2057 C CG  . TYR A 246 ? 0.6529 1.0714 0.5515 -0.2354 0.0459  -0.1533 246 TYR A CG  
2058 C CD1 . TYR A 246 ? 0.6792 1.0636 0.5711 -0.2448 0.0507  -0.1577 246 TYR A CD1 
2059 C CD2 . TYR A 246 ? 0.6623 1.0901 0.5610 -0.2408 0.0483  -0.1551 246 TYR A CD2 
2060 C CE1 . TYR A 246 ? 0.7102 1.0699 0.5952 -0.2589 0.0581  -0.1634 246 TYR A CE1 
2061 C CE2 . TYR A 246 ? 0.7014 1.1050 0.5931 -0.2556 0.0554  -0.1611 246 TYR A CE2 
2062 C CZ  . TYR A 246 ? 0.7222 1.0915 0.6069 -0.2645 0.0605  -0.1651 246 TYR A CZ  
2063 O OH  . TYR A 246 ? 0.7821 1.1259 0.6591 -0.2786 0.0683  -0.1705 246 TYR A OH  
2064 N N   . GLY A 247 ? 0.5782 1.0001 0.4878 -0.1842 0.0270  -0.1252 247 GLY A N   
2065 C CA  . GLY A 247 ? 0.5643 1.0010 0.4781 -0.1692 0.0217  -0.1180 247 GLY A CA  
2066 C C   . GLY A 247 ? 0.5803 1.0088 0.4924 -0.1721 0.0219  -0.1217 247 GLY A C   
2067 O O   . GLY A 247 ? 0.6113 1.0129 0.5185 -0.1831 0.0259  -0.1276 247 GLY A O   
2068 N N   . ILE A 248 ? 0.5617 1.0129 0.4776 -0.1616 0.0180  -0.1177 248 ILE A N   
2069 C CA  . ILE A 248 ? 0.5840 1.0316 0.4985 -0.1635 0.0179  -0.1210 248 ILE A CA  
2070 C C   . ILE A 248 ? 0.5606 1.0093 0.4779 -0.1451 0.0128  -0.1098 248 ILE A C   
2071 O O   . ILE A 248 ? 0.5648 1.0329 0.4859 -0.1323 0.0098  -0.1018 248 ILE A O   
2072 C CB  . ILE A 248 ? 0.6009 1.0850 0.5161 -0.1768 0.0202  -0.1334 248 ILE A CB  
2073 C CG1 . ILE A 248 ? 0.6172 1.0927 0.5299 -0.1814 0.0213  -0.1385 248 ILE A CG1 
2074 C CG2 . ILE A 248 ? 0.5769 1.1089 0.4975 -0.1686 0.0165  -0.1307 248 ILE A CG2 
2075 C CD1 . ILE A 248 ? 0.6574 1.1588 0.5689 -0.1993 0.0256  -0.1533 248 ILE A CD1 
2076 N N   . LYS A 249 ? 0.5649 0.9909 0.4802 -0.1436 0.0126  -0.1091 249 LYS A N   
2077 C CA  . LYS A 249 ? 0.5881 1.0179 0.5055 -0.1287 0.0087  -0.1006 249 LYS A CA  
2078 C C   . LYS A 249 ? 0.5877 1.0333 0.5044 -0.1351 0.0093  -0.1081 249 LYS A C   
2079 O O   . LYS A 249 ? 0.5709 0.9980 0.4843 -0.1472 0.0127  -0.1163 249 LYS A O   
2080 C CB  . LYS A 249 ? 0.5779 0.9666 0.4938 -0.1197 0.0076  -0.0922 249 LYS A CB  
2081 C CG  . LYS A 249 ? 0.5730 0.9637 0.4911 -0.1027 0.0040  -0.0820 249 LYS A CG  
2082 C CD  . LYS A 249 ? 0.5443 0.9245 0.4610 -0.1036 0.0039  -0.0841 249 LYS A CD  
2083 C CE  . LYS A 249 ? 0.5860 0.9244 0.4997 -0.1084 0.0056  -0.0854 249 LYS A CE  
2084 N NZ  . LYS A 249 ? 0.5920 0.9186 0.5049 -0.1078 0.0056  -0.0867 249 LYS A NZ  
2085 N N   . VAL A 250 ? 0.6166 1.0967 0.5361 -0.1269 0.0065  -0.1052 250 VAL A N   
2086 C CA  . VAL A 250 ? 0.6792 1.1794 0.5980 -0.1325 0.0067  -0.1120 250 VAL A CA  
2087 C C   . VAL A 250 ? 0.7152 1.2123 0.6346 -0.1172 0.0034  -0.1026 250 VAL A C   
2088 O O   . VAL A 250 ? 0.7421 1.2513 0.6640 -0.1016 0.0004  -0.0918 250 VAL A O   
2089 C CB  . VAL A 250 ? 0.6826 1.2327 0.6035 -0.1388 0.0067  -0.1190 250 VAL A CB  
2090 C CG1 . VAL A 250 ? 0.7082 1.2797 0.6279 -0.1448 0.0070  -0.1263 250 VAL A CG1 
2091 C CG2 . VAL A 250 ? 0.6934 1.2464 0.6134 -0.1554 0.0107  -0.1294 250 VAL A CG2 
2092 N N   . ASP A 251 ? 0.7392 1.2189 0.6563 -0.1218 0.0046  -0.1067 251 ASP A N   
2093 C CA  . ASP A 251 ? 0.7712 1.2454 0.6883 -0.1096 0.0022  -0.0993 251 ASP A CA  
2094 C C   . ASP A 251 ? 0.7689 1.2845 0.6864 -0.1093 0.0009  -0.1023 251 ASP A C   
2095 O O   . ASP A 251 ? 0.8046 1.3334 0.7205 -0.1236 0.0033  -0.1141 251 ASP A O   
2096 C CB  . ASP A 251 ? 0.8385 1.2756 0.7530 -0.1155 0.0045  -0.1031 251 ASP A CB  
2097 C CG  . ASP A 251 ? 0.9185 1.3239 0.8334 -0.1018 0.0026  -0.0920 251 ASP A CG  
2098 O OD1 . ASP A 251 ? 0.9584 1.3486 0.8743 -0.0956 0.0017  -0.0852 251 ASP A OD1 
2099 O OD2 . ASP A 251 ? 0.9607 1.3565 0.8749 -0.0981 0.0022  -0.0907 251 ASP A OD2 
2100 N N   . ILE A 252 ? 0.7238 1.2594 0.6431 -0.0932 -0.0022 -0.0917 252 ILE A N   
2101 C CA  . ILE A 252 ? 0.7176 1.2931 0.6367 -0.0909 -0.0037 -0.0928 252 ILE A CA  
2102 C C   . ILE A 252 ? 0.7187 1.2816 0.6354 -0.0890 -0.0037 -0.0927 252 ILE A C   
2103 O O   . ILE A 252 ? 0.6980 1.2372 0.6145 -0.0763 -0.0047 -0.0828 252 ILE A O   
2104 C CB  . ILE A 252 ? 0.7073 1.3121 0.6288 -0.0736 -0.0066 -0.0809 252 ILE A CB  
2105 C CG1 . ILE A 252 ? 0.6741 1.2892 0.5983 -0.0745 -0.0064 -0.0805 252 ILE A CG1 
2106 C CG2 . ILE A 252 ? 0.6790 1.3297 0.6001 -0.0722 -0.0082 -0.0828 252 ILE A CG2 
2107 C CD1 . ILE A 252 ? 0.6648 1.2982 0.5914 -0.0556 -0.0083 -0.0672 252 ILE A CD1 
2108 N N   . ARG A 253 ? 0.7540 1.3335 0.6689 -0.1023 -0.0022 -0.1043 253 ARG A N   
2109 C CA  . ARG A 253 ? 0.7643 1.3369 0.6768 -0.1017 -0.0019 -0.1055 253 ARG A CA  
2110 C C   . ARG A 253 ? 0.7356 1.3377 0.6480 -0.0864 -0.0052 -0.0958 253 ARG A C   
2111 O O   . ARG A 253 ? 0.7156 1.3594 0.6289 -0.0841 -0.0069 -0.0953 253 ARG A O   
2112 C CB  . ARG A 253 ? 0.7782 1.3595 0.6884 -0.1213 0.0014  -0.1216 253 ARG A CB  
2113 C CG  . ARG A 253 ? 0.8180 1.3865 0.7256 -0.1226 0.0025  -0.1242 253 ARG A CG  
2114 C CD  . ARG A 253 ? 0.8915 1.4593 0.7967 -0.1432 0.0074  -0.1408 253 ARG A CD  
2115 N NE  . ARG A 253 ? 0.9507 1.4745 0.8552 -0.1515 0.0114  -0.1452 253 ARG A NE  
2116 C CZ  . ARG A 253 ? 1.0112 1.5227 0.9132 -0.1688 0.0171  -0.1586 253 ARG A CZ  
2117 N NH1 . ARG A 253 ? 0.9999 1.5401 0.8999 -0.1812 0.0196  -0.1704 253 ARG A NH1 
2118 N NH2 . ARG A 253 ? 1.0479 1.5182 0.9492 -0.1737 0.0208  -0.1604 253 ARG A NH2 
2119 N N   . ASP A 254 ? 0.7198 1.2994 0.6309 -0.0756 -0.0057 -0.0878 254 ASP A N   
2120 C CA  . ASP A 254 ? 0.6705 1.2697 0.5805 -0.0600 -0.0078 -0.0773 254 ASP A CA  
2121 C C   . ASP A 254 ? 0.6778 1.3185 0.5891 -0.0498 -0.0101 -0.0703 254 ASP A C   
2122 O O   . ASP A 254 ? 0.7131 1.3943 0.6233 -0.0519 -0.0112 -0.0738 254 ASP A O   
2123 C CB  . ASP A 254 ? 0.6695 1.2802 0.5764 -0.0662 -0.0073 -0.0840 254 ASP A CB  
2124 C CG  . ASP A 254 ? 0.6985 1.3123 0.6033 -0.0498 -0.0085 -0.0723 254 ASP A CG  
2125 O OD1 . ASP A 254 ? 0.6841 1.2899 0.5897 -0.0336 -0.0094 -0.0590 254 ASP A OD1 
2126 O OD2 . ASP A 254 ? 0.7083 1.3320 0.6103 -0.0535 -0.0081 -0.0767 254 ASP A OD2 
2127 N N   . ALA A 255 ? 0.6754 1.3065 0.5889 -0.0386 -0.0105 -0.0605 255 ALA A N   
2128 C CA  . ALA A 255 ? 0.6511 1.3185 0.5661 -0.0267 -0.0121 -0.0523 255 ALA A CA  
2129 C C   . ALA A 255 ? 0.6689 1.3574 0.5814 -0.0108 -0.0132 -0.0417 255 ALA A C   
2130 O O   . ALA A 255 ? 0.6780 1.4109 0.5904 -0.0064 -0.0148 -0.0400 255 ALA A O   
2131 C CB  . ALA A 255 ? 0.6275 1.2751 0.5451 -0.0177 -0.0115 -0.0439 255 ALA A CB  
2132 N N   . TYR A 256 ? 0.6639 1.3214 0.5740 -0.0024 -0.0120 -0.0347 256 TYR A N   
2133 C CA  . TYR A 256 ? 0.7111 1.3833 0.6178 0.0121  -0.0121 -0.0245 256 TYR A CA  
2134 C C   . TYR A 256 ? 0.7060 1.4154 0.6103 0.0042  -0.0137 -0.0324 256 TYR A C   
2135 O O   . TYR A 256 ? 0.6763 1.4239 0.5790 0.0142  -0.0150 -0.0261 256 TYR A O   
2136 C CB  . TYR A 256 ? 0.7426 1.3725 0.6472 0.0188  -0.0101 -0.0184 256 TYR A CB  
2137 C CG  . TYR A 256 ? 0.8421 1.4434 0.7477 0.0323  -0.0081 -0.0066 256 TYR A CG  
2138 C CD1 . TYR A 256 ? 0.8396 1.4161 0.7486 0.0264  -0.0077 -0.0098 256 TYR A CD1 
2139 C CD2 . TYR A 256 ? 0.8946 1.4927 0.7974 0.0508  -0.0061 0.0074  256 TYR A CD2 
2140 C CE1 . TYR A 256 ? 0.8834 1.4345 0.7932 0.0379  -0.0056 0.0001  256 TYR A CE1 
2141 C CE2 . TYR A 256 ? 0.8967 1.4675 0.8002 0.0623  -0.0033 0.0173  256 TYR A CE2 
2142 C CZ  . TYR A 256 ? 0.9040 1.4521 0.8110 0.0556  -0.0032 0.0134  256 TYR A CZ  
2143 O OH  . TYR A 256 ? 0.9387 1.4605 0.8463 0.0661  -0.0002 0.0225  256 TYR A OH  
2144 N N   . GLY A 257 ? 0.7222 1.4206 0.6261 -0.0135 -0.0132 -0.0462 257 GLY A N   
2145 C CA  . GLY A 257 ? 0.7289 1.4567 0.6300 -0.0229 -0.0139 -0.0552 257 GLY A CA  
2146 C C   . GLY A 257 ? 0.7551 1.5283 0.6576 -0.0341 -0.0153 -0.0652 257 GLY A C   
2147 O O   . GLY A 257 ? 0.7504 1.5578 0.6505 -0.0400 -0.0161 -0.0715 257 GLY A O   
2148 N N   . ASN A 258 ? 0.7447 1.5190 0.6510 -0.0377 -0.0153 -0.0672 258 ASN A N   
2149 C CA  . ASN A 258 ? 0.7257 1.5438 0.6340 -0.0482 -0.0164 -0.0764 258 ASN A CA  
2150 C C   . ASN A 258 ? 0.7178 1.5760 0.6277 -0.0323 -0.0189 -0.0652 258 ASN A C   
2151 O O   . ASN A 258 ? 0.7378 1.6360 0.6500 -0.0390 -0.0201 -0.0716 258 ASN A O   
2152 C CB  . ASN A 258 ? 0.7097 1.5085 0.6208 -0.0652 -0.0143 -0.0881 258 ASN A CB  
2153 C CG  . ASN A 258 ? 0.7275 1.5042 0.6364 -0.0849 -0.0113 -0.1031 258 ASN A CG  
2154 O OD1 . ASN A 258 ? 0.7074 1.4440 0.6171 -0.0929 -0.0088 -0.1074 258 ASN A OD1 
2155 N ND2 . ASN A 258 ? 0.6950 1.4976 0.6010 -0.0923 -0.0113 -0.1108 258 ASN A ND2 
2156 N N   . VAL A 259 ? 0.6776 1.5257 0.5864 -0.0111 -0.0192 -0.0486 259 VAL A N   
2157 C CA  . VAL A 259 ? 0.6710 1.5586 0.5802 0.0064  -0.0209 -0.0365 259 VAL A CA  
2158 C C   . VAL A 259 ? 0.6702 1.6088 0.5766 0.0041  -0.0231 -0.0404 259 VAL A C   
2159 O O   . VAL A 259 ? 0.6650 1.6000 0.5670 0.0042  -0.0230 -0.0406 259 VAL A O   
2160 C CB  . VAL A 259 ? 0.6589 1.5220 0.5662 0.0294  -0.0195 -0.0180 259 VAL A CB  
2161 C CG1 . VAL A 259 ? 0.6681 1.5740 0.5746 0.0485  -0.0206 -0.0049 259 VAL A CG1 
2162 C CG2 . VAL A 259 ? 0.6967 1.5183 0.6071 0.0321  -0.0174 -0.0141 259 VAL A CG2 
2163 N N   . LYS A 260 ? 0.6696 1.6564 0.5788 0.0010  -0.0251 -0.0445 260 LYS A N   
2164 C CA  . LYS A 260 ? 0.6750 1.7172 0.5818 0.0017  -0.0276 -0.0462 260 LYS A CA  
2165 C C   . LYS A 260 ? 0.6554 1.7138 0.5601 0.0285  -0.0285 -0.0261 260 LYS A C   
2166 O O   . LYS A 260 ? 0.6245 1.6954 0.5323 0.0423  -0.0286 -0.0159 260 LYS A O   
2167 C CB  . LYS A 260 ? 0.7174 1.8063 0.6283 -0.0114 -0.0292 -0.0580 260 LYS A CB  
2168 C CG  . LYS A 260 ? 0.7718 1.8379 0.6852 -0.0362 -0.0270 -0.0761 260 LYS A CG  
2169 C CD  . LYS A 260 ? 0.8026 1.8805 0.7218 -0.0387 -0.0270 -0.0780 260 LYS A CD  
2170 C CE  . LYS A 260 ? 0.7921 1.8228 0.7131 -0.0546 -0.0238 -0.0879 260 LYS A CE  
2171 N NZ  . LYS A 260 ? 0.7967 1.8432 0.7182 -0.0808 -0.0220 -0.1084 260 LYS A NZ  
2172 N N   . ILE A 261 ? 0.6759 1.7311 0.5749 0.0360  -0.0283 -0.0201 261 ILE A N   
2173 C CA  . ILE A 261 ? 0.6911 1.7507 0.5865 0.0619  -0.0276 -0.0001 261 ILE A CA  
2174 C C   . ILE A 261 ? 0.6782 1.7967 0.5745 0.0759  -0.0300 0.0084  261 ILE A C   
2175 O O   . ILE A 261 ? 0.6843 1.8008 0.5814 0.0963  -0.0285 0.0242  261 ILE A O   
2176 C CB  . ILE A 261 ? 0.7027 1.7510 0.5913 0.0647  -0.0269 0.0026  261 ILE A CB  
2177 C CG1 . ILE A 261 ? 0.7157 1.7029 0.6037 0.0549  -0.0242 -0.0029 261 ILE A CG1 
2178 C CG2 . ILE A 261 ? 0.7217 1.7784 0.6055 0.0913  -0.0256 0.0233  261 ILE A CG2 
2179 C CD1 . ILE A 261 ? 0.7184 1.6598 0.6099 0.0621  -0.0215 0.0042  261 ILE A CD1 
2180 N N   . PRO A 262 ? 0.6567 1.8283 0.5530 0.0648  -0.0333 -0.0020 262 PRO A N   
2181 C CA  . PRO A 262 ? 0.6705 1.9022 0.5682 0.0772  -0.0359 0.0051  262 PRO A CA  
2182 C C   . PRO A 262 ? 0.6670 1.9008 0.5714 0.0845  -0.0353 0.0101  262 PRO A C   
2183 O O   . PRO A 262 ? 0.6736 1.9287 0.5781 0.1068  -0.0351 0.0263  262 PRO A O   
2184 C CB  . PRO A 262 ? 0.6716 1.9513 0.5698 0.0558  -0.0391 -0.0131 262 PRO A CB  
2185 C CG  . PRO A 262 ? 0.6635 1.9137 0.5572 0.0405  -0.0379 -0.0236 262 PRO A CG  
2186 C CD  . PRO A 262 ? 0.6573 1.8369 0.5508 0.0436  -0.0343 -0.0187 262 PRO A CD  
2187 N N   . VAL A 263 ? 0.6432 1.8542 0.5526 0.0662  -0.0347 -0.0032 263 VAL A N   
2188 C CA  . VAL A 263 ? 0.6294 1.8399 0.5451 0.0705  -0.0340 -0.0003 263 VAL A CA  
2189 C C   . VAL A 263 ? 0.6573 1.8267 0.5725 0.0929  -0.0305 0.0181  263 VAL A C   
2190 O O   . VAL A 263 ? 0.6373 1.8247 0.5554 0.1093  -0.0298 0.0294  263 VAL A O   
2191 C CB  . VAL A 263 ? 0.6192 1.8081 0.5394 0.0452  -0.0333 -0.0188 263 VAL A CB  
2192 C CG1 . VAL A 263 ? 0.5948 1.7704 0.5207 0.0505  -0.0318 -0.0145 263 VAL A CG1 
2193 C CG2 . VAL A 263 ? 0.5966 1.8338 0.5181 0.0241  -0.0358 -0.0368 263 VAL A CG2 
2194 N N   . LEU A 264 ? 0.6843 1.7994 0.5956 0.0934  -0.0278 0.0209  264 LEU A N   
2195 C CA  . LEU A 264 ? 0.7002 1.7728 0.6101 0.1129  -0.0237 0.0373  264 LEU A CA  
2196 C C   . LEU A 264 ? 0.7251 1.8228 0.6311 0.1397  -0.0224 0.0568  264 LEU A C   
2197 O O   . LEU A 264 ? 0.7525 1.8400 0.6597 0.1579  -0.0191 0.0705  264 LEU A O   
2198 C CB  . LEU A 264 ? 0.6981 1.7115 0.6046 0.1066  -0.0213 0.0351  264 LEU A CB  
2199 C CG  . LEU A 264 ? 0.6788 1.6419 0.5837 0.1227  -0.0164 0.0492  264 LEU A CG  
2200 C CD1 . LEU A 264 ? 0.6650 1.6183 0.5753 0.1275  -0.0147 0.0526  264 LEU A CD1 
2201 C CD2 . LEU A 264 ? 0.6941 1.6037 0.5968 0.1117  -0.0149 0.0431  264 LEU A CD2 
2202 N N   . CYS A 265 ? 0.7242 1.8546 0.6254 0.1422  -0.0245 0.0580  265 CYS A N   
2203 C CA  . CYS A 265 ? 0.7622 1.9212 0.6590 0.1675  -0.0233 0.0764  265 CYS A CA  
2204 C C   . CYS A 265 ? 0.7703 1.9742 0.6717 0.1804  -0.0241 0.0837  265 CYS A C   
2205 O O   . CYS A 265 ? 0.7888 1.9848 0.6894 0.2031  -0.0200 0.1009  265 CYS A O   
2206 C CB  . CYS A 265 ? 0.7754 1.9683 0.6663 0.1651  -0.0261 0.0743  265 CYS A CB  
2207 S SG  . CYS A 265 ? 0.7614 1.9030 0.6461 0.1547  -0.0243 0.0691  265 CYS A SG  
2208 N N   . LYS A 266 ? 0.7710 2.0215 0.6773 0.1656  -0.0288 0.0703  266 LYS A N   
2209 C CA  . LYS A 266 ? 0.7828 2.0811 0.6946 0.1755  -0.0301 0.0750  266 LYS A CA  
2210 C C   . LYS A 266 ? 0.8048 2.0687 0.7214 0.1833  -0.0261 0.0813  266 LYS A C   
2211 O O   . LYS A 266 ? 0.8316 2.1178 0.7504 0.2029  -0.0245 0.0943  266 LYS A O   
2212 C CB  . LYS A 266 ? 0.7675 2.1145 0.6842 0.1532  -0.0353 0.0560  266 LYS A CB  
2213 C CG  . LYS A 266 ? 0.7678 2.1499 0.6800 0.1418  -0.0391 0.0468  266 LYS A CG  
2214 C CD  . LYS A 266 ? 0.7826 2.2159 0.6906 0.1637  -0.0406 0.0619  266 LYS A CD  
2215 C CE  . LYS A 266 ? 0.8085 2.2708 0.7110 0.1523  -0.0439 0.0530  266 LYS A CE  
2216 N NZ  . LYS A 266 ? 0.8306 2.3572 0.7301 0.1699  -0.0466 0.0643  266 LYS A NZ  
2217 N N   . LEU A 267 ? 0.8130 2.0227 0.7309 0.1683  -0.0244 0.0721  267 LEU A N   
2218 C CA  . LEU A 267 ? 0.8206 1.9909 0.7421 0.1739  -0.0204 0.0770  267 LEU A CA  
2219 C C   . LEU A 267 ? 0.8340 1.9764 0.7509 0.2004  -0.0146 0.0979  267 LEU A C   
2220 O O   . LEU A 267 ? 0.8396 1.9794 0.7592 0.2160  -0.0110 0.1087  267 LEU A O   
2221 C CB  . LEU A 267 ? 0.8102 1.9279 0.7328 0.1521  -0.0199 0.0631  267 LEU A CB  
2222 C CG  . LEU A 267 ? 0.7927 1.8888 0.7215 0.1433  -0.0187 0.0566  267 LEU A CG  
2223 C CD1 . LEU A 267 ? 0.8083 1.8503 0.7362 0.1242  -0.0181 0.0450  267 LEU A CD1 
2224 C CD2 . LEU A 267 ? 0.8160 1.8959 0.7459 0.1655  -0.0139 0.0730  267 LEU A CD2 
2225 N N   . ILE A 268 ? 0.8515 1.9721 0.7612 0.2050  -0.0131 0.1033  268 ILE A N   
2226 C CA  . ILE A 268 ? 0.8849 1.9763 0.7892 0.2287  -0.0067 0.1224  268 ILE A CA  
2227 C C   . ILE A 268 ? 0.9182 2.0563 0.8209 0.2535  -0.0054 0.1389  268 ILE A C   
2228 O O   . ILE A 268 ? 0.9268 2.0527 0.8296 0.2734  0.0003  0.1534  268 ILE A O   
2229 C CB  . ILE A 268 ? 0.8804 1.9384 0.7773 0.2263  -0.0053 0.1232  268 ILE A CB  
2230 C CG1 . ILE A 268 ? 0.8479 1.8502 0.7465 0.2071  -0.0048 0.1108  268 ILE A CG1 
2231 C CG2 . ILE A 268 ? 0.8989 1.9384 0.7890 0.2524  0.0015  0.1439  268 ILE A CG2 
2232 C CD1 . ILE A 268 ? 0.8505 1.8382 0.7448 0.1926  -0.0070 0.1014  268 ILE A CD1 
2233 N N   . GLN A 269 ? 0.9350 2.1274 0.8363 0.2521  -0.0105 0.1364  269 GLN A N   
2234 C CA  . GLN A 269 ? 1.0120 2.2547 0.9113 0.2756  -0.0099 0.1520  269 GLN A CA  
2235 C C   . GLN A 269 ? 1.0515 2.3080 0.9569 0.2894  -0.0073 0.1600  269 GLN A C   
2236 O O   . GLN A 269 ? 1.0798 2.3304 0.9823 0.3149  -0.0012 0.1789  269 GLN A O   
2237 C CB  . GLN A 269 ? 0.9964 2.3039 0.8960 0.2662  -0.0173 0.1431  269 GLN A CB  
2238 C CG  . GLN A 269 ? 0.9847 2.2845 0.8789 0.2495  -0.0204 0.1324  269 GLN A CG  
2239 C CD  . GLN A 269 ? 0.9890 2.2953 0.8736 0.2679  -0.0182 0.1476  269 GLN A CD  
2240 O OE1 . GLN A 269 ? 0.9976 2.3014 0.8785 0.2940  -0.0130 0.1675  269 GLN A OE1 
2241 N NE2 . GLN A 269 ? 0.9774 2.2910 0.8574 0.2544  -0.0215 0.1384  269 GLN A NE2 
2242 N N   . SER A 270 ? 1.0845 2.3574 0.9983 0.2722  -0.0113 0.1454  270 SER A N   
2243 C CA  . SER A 270 ? 1.1445 2.4423 1.0651 0.2829  -0.0100 0.1506  270 SER A CA  
2244 C C   . SER A 270 ? 1.1459 2.4082 1.0731 0.2665  -0.0093 0.1387  270 SER A C   
2245 O O   . SER A 270 ? 1.1223 2.3693 1.0513 0.2410  -0.0129 0.1208  270 SER A O   
2246 C CB  . SER A 270 ? 1.1622 2.5367 1.0869 0.2807  -0.0164 0.1456  270 SER A CB  
2247 O OG  . SER A 270 ? 1.1590 2.5721 1.0794 0.3066  -0.0152 0.1637  270 SER A OG  
2248 N N   . ILE A 271 ? 1.1932 2.4411 1.1237 0.2813  -0.0040 0.1486  271 ILE A N   
2249 C CA  . ILE A 271 ? 1.2627 2.5154 1.1898 0.3127  0.0024  0.1711  271 ILE A CA  
2250 C C   . ILE A 271 ? 1.2479 2.4334 1.1725 0.3214  0.0109  0.1795  271 ILE A C   
2251 O O   . ILE A 271 ? 1.1944 2.3642 1.1243 0.3213  0.0138  0.1784  271 ILE A O   
2252 C CB  . ILE A 271 ? 1.2844 2.5934 1.2180 0.3268  0.0018  0.1774  271 ILE A CB  
2253 C CG1 . ILE A 271 ? 1.2760 2.6559 1.2123 0.3180  -0.0065 0.1686  271 ILE A CG1 
2254 C CG2 . ILE A 271 ? 1.2986 2.6087 1.2280 0.3605  0.0095  0.2015  271 ILE A CG2 
2255 C CD1 . ILE A 271 ? 1.2628 2.7023 1.2063 0.3297  -0.0078 0.1731  271 ILE A CD1 
2256 N N   . PRO A 272 ? 1.2781 2.4231 1.1946 0.3268  0.0149  0.1865  272 PRO A N   
2257 C CA  . PRO A 272 ? 1.3467 2.4358 1.2596 0.3404  0.0245  0.1981  272 PRO A CA  
2258 C C   . PRO A 272 ? 1.4067 2.4959 1.3113 0.3687  0.0317  0.2196  272 PRO A C   
2259 O O   . PRO A 272 ? 1.4453 2.5025 1.3424 0.3701  0.0346  0.2235  272 PRO A O   
2260 C CB  . PRO A 272 ? 1.3276 2.3628 1.2381 0.3195  0.0236  0.1859  272 PRO A CB  
2261 C CG  . PRO A 272 ? 1.3022 2.3668 1.2128 0.2999  0.0146  0.1717  272 PRO A CG  
2262 C CD  . PRO A 272 ? 1.2813 2.4150 1.1934 0.3095  0.0104  0.1761  272 PRO A CD  
2263 N N   . THR A 273 ? 1.4356 2.5609 1.3416 0.3912  0.0349  0.2334  273 THR A N   
2264 C CA  . THR A 273 ? 1.4602 2.5877 1.3582 0.4203  0.0428  0.2554  273 THR A CA  
2265 C C   . THR A 273 ? 1.4834 2.5552 1.3783 0.4356  0.0552  0.2675  273 THR A C   
2266 O O   . THR A 273 ? 1.4752 2.5134 1.3611 0.4483  0.0629  0.2793  273 THR A O   
2267 C CB  . THR A 273 ? 1.4504 2.6459 1.3506 0.4397  0.0409  0.2663  273 THR A CB  
2268 O OG1 . THR A 273 ? 1.4436 2.6521 1.3523 0.4435  0.0423  0.2658  273 THR A OG1 
2269 C CG2 . THR A 273 ? 1.4252 2.6782 1.3275 0.4250  0.0293  0.2547  273 THR A CG2 
2270 N N   . HIS A 274 ? 1.5263 2.5886 1.4283 0.4335  0.0573  0.2639  274 HIS A N   
2271 C CA  . HIS A 274 ? 1.5795 2.5886 1.4796 0.4444  0.0689  0.2723  274 HIS A CA  
2272 C C   . HIS A 274 ? 1.5540 2.5003 1.4499 0.4288  0.0714  0.2644  274 HIS A C   
2273 O O   . HIS A 274 ? 1.5610 2.4586 1.4526 0.4381  0.0820  0.2724  274 HIS A O   
2274 C CB  . HIS A 274 ? 1.6447 2.6619 1.5543 0.4409  0.0688  0.2665  274 HIS A CB  
2275 C CG  . HIS A 274 ? 1.7214 2.6870 1.6297 0.4512  0.0809  0.2740  274 HIS A CG  
2276 N ND1 . HIS A 274 ? 1.7630 2.7271 1.6678 0.4792  0.0919  0.2930  274 HIS A ND1 
2277 C CD2 . HIS A 274 ? 1.7231 2.6371 1.6332 0.4358  0.0836  0.2639  274 HIS A CD2 
2278 C CE1 . HIS A 274 ? 1.7695 2.6825 1.6736 0.4809  0.1016  0.2944  274 HIS A CE1 
2279 N NE2 . HIS A 274 ? 1.7320 2.6155 1.6395 0.4542  0.0962  0.2765  274 HIS A NE2 
2280 N N   . LEU A 275 ? 1.5088 2.4566 1.4057 0.4051  0.0620  0.2486  275 LEU A N   
2281 C CA  . LEU A 275 ? 1.5034 2.3958 1.3982 0.3868  0.0625  0.2382  275 LEU A CA  
2282 C C   . LEU A 275 ? 1.5516 2.4308 1.4381 0.3860  0.0624  0.2406  275 LEU A C   
2283 O O   . LEU A 275 ? 1.5919 2.4209 1.4726 0.3876  0.0695  0.2442  275 LEU A O   
2284 C CB  . LEU A 275 ? 1.4495 2.3454 1.3522 0.3586  0.0529  0.2171  275 LEU A CB  
2285 C CG  . LEU A 275 ? 1.4287 2.3470 1.3401 0.3571  0.0515  0.2131  275 LEU A CG  
2286 C CD1 . LEU A 275 ? 1.4156 2.3653 1.3340 0.3327  0.0403  0.1944  275 LEU A CD1 
2287 C CD2 . LEU A 275 ? 1.4238 2.2920 1.3364 0.3570  0.0591  0.2133  275 LEU A CD2 
2288 N N   . LEU A 276 ? 1.5611 2.4863 1.4469 0.3830  0.0545  0.2381  276 LEU A N   
2289 C CA  . LEU A 276 ? 1.5946 2.5133 1.4726 0.3819  0.0537  0.2399  276 LEU A CA  
2290 C C   . LEU A 276 ? 1.6238 2.5894 1.4966 0.4028  0.0541  0.2547  276 LEU A C   
2291 O O   . LEU A 276 ? 1.6160 2.5648 1.4798 0.4193  0.0614  0.2688  276 LEU A O   
2292 C CB  . LEU A 276 ? 1.5625 2.4880 1.4437 0.3538  0.0431  0.2199  276 LEU A CB  
2293 C CG  . LEU A 276 ? 1.5379 2.4130 1.4219 0.3316  0.0421  0.2051  276 LEU A CG  
2294 C CD1 . LEU A 276 ? 1.5300 2.4265 1.4188 0.3058  0.0313  0.1857  276 LEU A CD1 
2295 C CD2 . LEU A 276 ? 1.5296 2.3538 1.4060 0.3340  0.0486  0.2099  276 LEU A CD2 
2296 N N   . ASP A 277 ? 1.6490 2.6740 1.5273 0.4019  0.0465  0.2512  277 ASP A N   
2297 C CA  . ASP A 277 ? 1.6966 2.7763 1.5709 0.4175  0.0442  0.2619  277 ASP A CA  
2298 C C   . ASP A 277 ? 1.6922 2.7769 1.5603 0.4069  0.0392  0.2565  277 ASP A C   
2299 O O   . ASP A 277 ? 1.6395 2.7117 1.5104 0.3815  0.0328  0.2385  277 ASP A O   
2300 C CB  . ASP A 277 ? 1.7611 2.8391 1.6291 0.4503  0.0551  0.2860  277 ASP A CB  
2301 C CG  . ASP A 277 ? 1.7914 2.9385 1.6600 0.4682  0.0519  0.2965  277 ASP A CG  
2302 O OD1 . ASP A 277 ? 1.7741 2.9682 1.6513 0.4571  0.0430  0.2854  277 ASP A OD1 
2303 O OD2 . ASP A 277 ? 1.8064 2.9614 1.6669 0.4934  0.0587  0.3159  277 ASP A OD2 
2304 N N   . SER A 278 ? 1.7151 2.8155 1.5743 0.4269  0.0430  0.2725  278 SER A N   
2305 C CA  . SER A 278 ? 1.7001 2.8291 1.5541 0.4201  0.0367  0.2687  278 SER A CA  
2306 C C   . SER A 278 ? 1.6892 2.7691 1.5355 0.4124  0.0399  0.2667  278 SER A C   
2307 O O   . SER A 278 ? 1.6435 2.7219 1.4911 0.3895  0.0329  0.2505  278 SER A O   
2308 C CB  . SER A 278 ? 1.7196 2.9021 1.5682 0.4450  0.0375  0.2863  278 SER A CB  
2309 O OG  . SER A 278 ? 1.7369 2.9652 1.5837 0.4346  0.0286  0.2785  278 SER A OG  
2310 N N   . GLU A 279 ? 1.7350 2.7755 1.5734 0.4314  0.0509  0.2832  279 GLU A N   
2311 C CA  . GLU A 279 ? 1.7377 2.7341 1.5679 0.4273  0.0552  0.2837  279 GLU A CA  
2312 C C   . GLU A 279 ? 1.6733 2.6304 1.5088 0.3990  0.0510  0.2634  279 GLU A C   
2313 O O   . GLU A 279 ? 1.6540 2.5980 1.4860 0.3857  0.0482  0.2554  279 GLU A O   
2314 C CB  . GLU A 279 ? 1.8050 2.7569 1.6270 0.4500  0.0693  0.3027  279 GLU A CB  
2315 C CG  . GLU A 279 ? 1.8813 2.8545 1.7028 0.4770  0.0760  0.3208  279 GLU A CG  
2316 C CD  . GLU A 279 ? 1.9129 2.8664 1.7433 0.4739  0.0784  0.3162  279 GLU A CD  
2317 O OE1 . GLU A 279 ? 1.9257 2.8228 1.7542 0.4754  0.0877  0.3186  279 GLU A OE1 
2318 O OE2 . GLU A 279 ? 1.9242 2.9189 1.7633 0.4695  0.0710  0.3097  279 GLU A OE2 
2319 N N   . LYS A 280 ? 1.6126 2.5518 1.4565 0.3904  0.0507  0.2554  280 LYS A N   
2320 C CA  . LYS A 280 ? 1.5453 2.4496 1.3948 0.3643  0.0466  0.2366  280 LYS A CA  
2321 C C   . LYS A 280 ? 1.5041 2.4477 1.3593 0.3423  0.0346  0.2187  280 LYS A C   
2322 O O   . LYS A 280 ? 1.4981 2.4264 1.3525 0.3241  0.0307  0.2064  280 LYS A O   
2323 C CB  . LYS A 280 ? 1.5311 2.4067 1.3873 0.3627  0.0502  0.2342  280 LYS A CB  
2324 C CG  . LYS A 280 ? 1.5355 2.4116 1.3897 0.3890  0.0595  0.2527  280 LYS A CG  
2325 C CD  . LYS A 280 ? 1.5233 2.3479 1.3691 0.4033  0.0719  0.2659  280 LYS A CD  
2326 C CE  . LYS A 280 ? 1.5161 2.3376 1.3605 0.4278  0.0821  0.2828  280 LYS A CE  
2327 N NZ  . LYS A 280 ? 1.5059 2.2816 1.3405 0.4439  0.0956  0.2972  280 LYS A NZ  
2328 N N   . LYS A 281 ? 1.4581 2.4529 1.3188 0.3441  0.0294  0.2172  281 LYS A N   
2329 C CA  . LYS A 281 ? 1.4051 2.4390 1.2718 0.3223  0.0189  0.1993  281 LYS A CA  
2330 C C   . LYS A 281 ? 1.3652 2.4192 1.2261 0.3150  0.0145  0.1949  281 LYS A C   
2331 O O   . LYS A 281 ? 1.3136 2.3654 1.1771 0.2915  0.0086  0.1774  281 LYS A O   
2332 C CB  . LYS A 281 ? 1.4075 2.4983 1.2803 0.3282  0.0149  0.2003  281 LYS A CB  
2333 C CG  . LYS A 281 ? 1.4645 2.6163 1.3332 0.3416  0.0119  0.2092  281 LYS A CG  
2334 C CD  . LYS A 281 ? 1.4557 2.6679 1.3321 0.3398  0.0058  0.2042  281 LYS A CD  
2335 C CE  . LYS A 281 ? 1.4866 2.7196 1.3633 0.3680  0.0112  0.2234  281 LYS A CE  
2336 N NZ  . LYS A 281 ? 1.4414 2.7446 1.3243 0.3691  0.0048  0.2206  281 LYS A NZ  
2337 N N   . ASN A 282 ? 1.3583 2.4300 1.2110 0.3355  0.0180  0.2111  282 ASN A N   
2338 C CA  . ASN A 282 ? 1.3207 2.4120 1.1667 0.3312  0.0147  0.2091  282 ASN A CA  
2339 C C   . ASN A 282 ? 1.2992 2.3389 1.1424 0.3155  0.0159  0.1999  282 ASN A C   
2340 O O   . ASN A 282 ? 1.2850 2.3367 1.1278 0.2977  0.0102  0.1866  282 ASN A O   
2341 C CB  . ASN A 282 ? 1.3595 2.4716 1.1960 0.3588  0.0198  0.2307  282 ASN A CB  
2342 C CG  . ASN A 282 ? 1.3640 2.5328 1.2031 0.3757  0.0182  0.2406  282 ASN A CG  
2343 O OD1 . ASN A 282 ? 1.3371 2.5532 1.1827 0.3639  0.0101  0.2291  282 ASN A OD1 
2344 N ND2 . ASN A 282 ? 1.3775 2.5418 1.2113 0.4036  0.0265  0.2620  282 ASN A ND2 
2345 N N   . PHE A 283 ? 1.2868 2.2698 1.1282 0.3219  0.0238  0.2065  283 PHE A N   
2346 C CA  . PHE A 283 ? 1.2581 2.1897 1.0974 0.3082  0.0257  0.1986  283 PHE A CA  
2347 C C   . PHE A 283 ? 1.2237 2.1417 1.0714 0.2809  0.0194  0.1772  283 PHE A C   
2348 O O   . PHE A 283 ? 1.2263 2.1268 1.0731 0.2645  0.0169  0.1658  283 PHE A O   
2349 C CB  . PHE A 283 ? 1.2645 2.1409 1.1001 0.3217  0.0362  0.2108  283 PHE A CB  
2350 C CG  . PHE A 283 ? 1.2693 2.0938 1.1034 0.3077  0.0382  0.2024  283 PHE A CG  
2351 C CD1 . PHE A 283 ? 1.2664 2.0837 1.0926 0.3086  0.0399  0.2051  283 PHE A CD1 
2352 C CD2 . PHE A 283 ? 1.2557 2.0402 1.0963 0.2933  0.0383  0.1916  283 PHE A CD2 
2353 C CE1 . PHE A 283 ? 1.2716 2.0431 1.0970 0.2957  0.0417  0.1971  283 PHE A CE1 
2354 C CE2 . PHE A 283 ? 1.2419 1.9814 1.0815 0.2808  0.0399  0.1839  283 PHE A CE2 
2355 C CZ  . PHE A 283 ? 1.2522 1.9853 1.0845 0.2819  0.0416  0.1865  283 PHE A CZ  
2356 N N   . ILE A 284 ? 1.1606 2.0853 1.0162 0.2764  0.0173  0.1720  284 ILE A N   
2357 C CA  . ILE A 284 ? 1.1162 2.0304 0.9795 0.2513  0.0117  0.1523  284 ILE A CA  
2358 C C   . ILE A 284 ? 1.1155 2.0775 0.9807 0.2352  0.0034  0.1387  284 ILE A C   
2359 O O   . ILE A 284 ? 1.1018 2.0503 0.9686 0.2142  0.0000  0.1232  284 ILE A O   
2360 C CB  . ILE A 284 ? 1.1121 2.0185 0.9829 0.2510  0.0124  0.1509  284 ILE A CB  
2361 C CG1 . ILE A 284 ? 1.1120 1.9749 0.9802 0.2683  0.0216  0.1652  284 ILE A CG1 
2362 C CG2 . ILE A 284 ? 1.0890 1.9751 0.9664 0.2254  0.0079  0.1316  284 ILE A CG2 
2363 C CD1 . ILE A 284 ? 1.0962 1.9570 0.9707 0.2729  0.0234  0.1672  284 ILE A CD1 
2364 N N   . VAL A 285 ? 1.1076 2.1255 0.9723 0.2455  0.0007  0.1446  285 VAL A N   
2365 C CA  . VAL A 285 ? 1.0902 2.1594 0.9564 0.2310  -0.0066 0.1319  285 VAL A CA  
2366 C C   . VAL A 285 ? 1.0822 2.1437 0.9433 0.2185  -0.0084 0.1237  285 VAL A C   
2367 O O   . VAL A 285 ? 1.0714 2.1327 0.9357 0.1952  -0.0126 0.1055  285 VAL A O   
2368 C CB  . VAL A 285 ? 1.1090 2.2412 0.9739 0.2479  -0.0085 0.1426  285 VAL A CB  
2369 C CG1 . VAL A 285 ? 1.1057 2.2900 0.9699 0.2338  -0.0154 0.1305  285 VAL A CG1 
2370 C CG2 . VAL A 285 ? 1.1086 2.2581 0.9808 0.2536  -0.0087 0.1448  285 VAL A CG2 
2371 N N   . ASP A 286 ? 1.1023 2.1554 0.9550 0.2340  -0.0044 0.1371  286 ASP A N   
2372 C CA  . ASP A 286 ? 1.1090 2.1556 0.9562 0.2238  -0.0055 0.1305  286 ASP A CA  
2373 C C   . ASP A 286 ? 1.0803 2.0654 0.9286 0.2103  -0.0030 0.1220  286 ASP A C   
2374 O O   . ASP A 286 ? 1.0822 2.0578 0.9280 0.1969  -0.0044 0.1124  286 ASP A O   
2375 C CB  . ASP A 286 ? 1.1613 2.2230 0.9984 0.2447  -0.0021 0.1478  286 ASP A CB  
2376 C CG  . ASP A 286 ? 1.1896 2.2043 1.0221 0.2643  0.0065  0.1650  286 ASP A CG  
2377 O OD1 . ASP A 286 ? 1.1959 2.1733 1.0333 0.2644  0.0098  0.1653  286 ASP A OD1 
2378 O OD2 . ASP A 286 ? 1.1568 2.1722 0.9803 0.2794  0.0106  0.1782  286 ASP A OD2 
2379 N N   . HIS A 287 ? 1.1070 2.0515 0.9592 0.2138  0.0007  0.1254  287 HIS A N   
2380 C CA  . HIS A 287 ? 1.1022 1.9899 0.9561 0.2016  0.0030  0.1176  287 HIS A CA  
2381 C C   . HIS A 287 ? 1.0650 1.9506 0.9254 0.1758  -0.0023 0.0970  287 HIS A C   
2382 O O   . HIS A 287 ? 1.0519 1.9082 0.9119 0.1620  -0.0024 0.0873  287 HIS A O   
2383 C CB  . HIS A 287 ? 1.1169 1.9629 0.9724 0.2132  0.0091  0.1275  287 HIS A CB  
2384 C CG  . HIS A 287 ? 1.1484 1.9386 1.0009 0.2118  0.0142  0.1287  287 HIS A CG  
2385 N ND1 . HIS A 287 ? 1.1494 1.8977 1.0069 0.1998  0.0148  0.1201  287 HIS A ND1 
2386 C CD2 . HIS A 287 ? 1.1661 1.9378 1.0108 0.2212  0.0190  0.1376  287 HIS A CD2 
2387 C CE1 . HIS A 287 ? 1.1614 1.8680 1.0151 0.2014  0.0196  0.1231  287 HIS A CE1 
2388 N NE2 . HIS A 287 ? 1.1921 1.9125 1.0379 0.2141  0.0223  0.1336  287 HIS A NE2 
2389 N N   . ILE A 288 ? 1.0335 1.9506 0.8998 0.1694  -0.0062 0.0902  288 ILE A N   
2390 C CA  . ILE A 288 ? 1.0181 1.9358 0.8904 0.1446  -0.0106 0.0704  288 ILE A CA  
2391 C C   . ILE A 288 ? 0.9912 1.9354 0.8609 0.1297  -0.0143 0.0582  288 ILE A C   
2392 O O   . ILE A 288 ? 0.9883 1.9124 0.8599 0.1100  -0.0154 0.0432  288 ILE A O   
2393 C CB  . ILE A 288 ? 1.0310 1.9803 0.9098 0.1418  -0.0134 0.0666  288 ILE A CB  
2394 C CG1 . ILE A 288 ? 1.0420 1.9827 0.9220 0.1624  -0.0096 0.0825  288 ILE A CG1 
2395 C CG2 . ILE A 288 ? 1.0160 1.9463 0.9009 0.1185  -0.0155 0.0487  288 ILE A CG2 
2396 C CD1 . ILE A 288 ? 1.0608 1.9415 0.9421 0.1638  -0.0050 0.0854  288 ILE A CD1 
2397 N N   . SER A 289 ? 0.9704 1.9610 0.8356 0.1393  -0.0158 0.0646  289 SER A N   
2398 C CA  . SER A 289 ? 0.9879 2.0030 0.8488 0.1290  -0.0183 0.0562  289 SER A CA  
2399 C C   . SER A 289 ? 1.0253 2.0619 0.8785 0.1509  -0.0166 0.0735  289 SER A C   
2400 O O   . SER A 289 ? 1.0836 2.1596 0.9362 0.1657  -0.0174 0.0839  289 SER A O   
2401 C CB  . SER A 289 ? 0.9623 2.0277 0.8268 0.1131  -0.0234 0.0416  289 SER A CB  
2402 O OG  . SER A 289 ? 0.9173 2.0244 0.7839 0.1261  -0.0249 0.0503  289 SER A OG  
2403 N N   . ASN A 290 ? 1.0007 2.0126 0.8476 0.1533  -0.0138 0.0769  290 ASN A N   
2404 C CA  . ASN A 290 ? 0.9888 1.9707 0.8360 0.1335  -0.0140 0.0621  290 ASN A CA  
2405 C C   . ASN A 290 ? 0.9891 1.9076 0.8362 0.1364  -0.0092 0.0663  290 ASN A C   
2406 O O   . ASN A 290 ? 1.0015 1.9015 0.8440 0.1551  -0.0046 0.0823  290 ASN A O   
2407 C CB  . ASN A 290 ? 1.0058 2.0147 0.8458 0.1314  -0.0152 0.0602  290 ASN A CB  
2408 C CG  . ASN A 290 ? 1.0104 2.0726 0.8452 0.1491  -0.0165 0.0734  290 ASN A CG  
2409 O OD1 . ASN A 290 ? 1.0090 2.0670 0.8409 0.1716  -0.0131 0.0918  290 ASN A OD1 
2410 N ND2 . ASN A 290 ? 0.9889 2.1018 0.8223 0.1392  -0.0209 0.0640  290 ASN A ND2 
2411 N N   . GLN A 291 ? 0.9547 1.8409 0.8067 0.1176  -0.0097 0.0517  291 GLN A N   
2412 C CA  . GLN A 291 ? 0.9408 1.7688 0.7935 0.1176  -0.0057 0.0534  291 GLN A CA  
2413 C C   . GLN A 291 ? 0.9520 1.7633 0.8013 0.1074  -0.0050 0.0457  291 GLN A C   
2414 O O   . GLN A 291 ? 0.9514 1.7667 0.8032 0.0880  -0.0075 0.0295  291 GLN A O   
2415 C CB  . GLN A 291 ? 0.9046 1.7059 0.7653 0.1050  -0.0066 0.0435  291 GLN A CB  
2416 C CG  . GLN A 291 ? 0.8857 1.7012 0.7503 0.1137  -0.0072 0.0500  291 GLN A CG  
2417 C CD  . GLN A 291 ? 0.8604 1.6581 0.7324 0.0983  -0.0088 0.0379  291 GLN A CD  
2418 O OE1 . GLN A 291 ? 0.8444 1.6459 0.7189 0.0788  -0.0113 0.0220  291 GLN A OE1 
2419 N NE2 . GLN A 291 ? 0.8333 1.6112 0.7085 0.1071  -0.0068 0.0454  291 GLN A NE2 
2420 N N   . PHE A 292 ? 0.9698 1.7620 0.8132 0.1204  -0.0009 0.0573  292 PHE A N   
2421 C CA  . PHE A 292 ? 0.9925 1.7725 0.8318 0.1128  0.0001  0.0515  292 PHE A CA  
2422 C C   . PHE A 292 ? 0.9998 1.7232 0.8406 0.1113  0.0042  0.0517  292 PHE A C   
2423 O O   . PHE A 292 ? 1.0090 1.7059 0.8492 0.1251  0.0082  0.0639  292 PHE A O   
2424 C CB  . PHE A 292 ? 1.0538 1.8623 0.8842 0.1268  0.0015  0.0631  292 PHE A CB  
2425 C CG  . PHE A 292 ? 1.1053 1.9228 0.9320 0.1504  0.0044  0.0826  292 PHE A CG  
2426 C CD1 . PHE A 292 ? 1.1392 1.9143 0.9646 0.1635  0.0105  0.0947  292 PHE A CD1 
2427 C CD2 . PHE A 292 ? 1.1143 1.9833 0.9389 0.1595  0.0017  0.0888  292 PHE A CD2 
2428 C CE1 . PHE A 292 ? 1.1620 1.9435 0.9836 0.1853  0.0144  0.1127  292 PHE A CE1 
2429 C CE2 . PHE A 292 ? 1.1456 2.0226 0.9667 0.1823  0.0051  0.1075  292 PHE A CE2 
2430 C CZ  . PHE A 292 ? 1.1699 2.0019 0.9892 0.1953  0.0117  0.1195  292 PHE A CZ  
2431 N N   . VAL A 293 ? 0.9706 1.6763 0.8134 0.0945  0.0034  0.0378  293 VAL A N   
2432 C CA  . VAL A 293 ? 0.9546 1.6089 0.8001 0.0906  0.0065  0.0355  293 VAL A CA  
2433 C C   . VAL A 293 ? 0.9759 1.6164 0.8181 0.0844  0.0084  0.0304  293 VAL A C   
2434 O O   . VAL A 293 ? 0.9658 1.6303 0.8063 0.0735  0.0062  0.0204  293 VAL A O   
2435 C CB  . VAL A 293 ? 0.9330 1.5669 0.7867 0.0756  0.0043  0.0230  293 VAL A CB  
2436 C CG1 . VAL A 293 ? 0.9139 1.5504 0.7712 0.0833  0.0037  0.0297  293 VAL A CG1 
2437 C CG2 . VAL A 293 ? 0.9534 1.6112 0.8092 0.0568  0.0007  0.0064  293 VAL A CG2 
2438 N N   . ALA A 294 ? 0.9939 1.5957 0.8351 0.0910  0.0128  0.0368  294 ALA A N   
2439 C CA  . ALA A 294 ? 1.0149 1.5972 0.8540 0.0849  0.0150  0.0317  294 ALA A CA  
2440 C C   . ALA A 294 ? 1.0173 1.5784 0.8633 0.0662  0.0132  0.0153  294 ALA A C   
2441 O O   . ALA A 294 ? 1.0323 1.5757 0.8845 0.0614  0.0120  0.0116  294 ALA A O   
2442 C CB  . ALA A 294 ? 1.0142 1.5621 0.8504 0.0977  0.0208  0.0436  294 ALA A CB  
2443 N N   . PHE A 295 ? 1.0465 1.6097 0.8910 0.0558  0.0133  0.0058  295 PHE A N   
2444 C CA  . PHE A 295 ? 1.0592 1.5987 0.9095 0.0395  0.0129  -0.0087 295 PHE A CA  
2445 C C   . PHE A 295 ? 1.1368 1.6589 0.9848 0.0366  0.0160  -0.0117 295 PHE A C   
2446 O O   . PHE A 295 ? 1.1883 1.6938 1.0330 0.0481  0.0195  -0.0013 295 PHE A O   
2447 C CB  . PHE A 295 ? 0.9958 1.5621 0.8484 0.0241  0.0093  -0.0226 295 PHE A CB  
2448 C CG  . PHE A 295 ? 0.9517 1.4908 0.8112 0.0093  0.0091  -0.0355 295 PHE A CG  
2449 C CD1 . PHE A 295 ? 0.9302 1.4385 0.7951 0.0119  0.0092  -0.0324 295 PHE A CD1 
2450 C CD2 . PHE A 295 ? 0.9266 1.4708 0.7869 -0.0069 0.0093  -0.0506 295 PHE A CD2 
2451 C CE1 . PHE A 295 ? 0.9220 1.4056 0.7927 -0.0007 0.0092  -0.0434 295 PHE A CE1 
2452 C CE2 . PHE A 295 ? 0.8792 1.3971 0.7453 -0.0195 0.0099  -0.0617 295 PHE A CE2 
2453 C CZ  . PHE A 295 ? 0.9020 1.3900 0.7732 -0.0161 0.0097  -0.0577 295 PHE A CZ  
2454 N N   . ARG A 296 ? 1.1233 1.6486 0.9728 0.0213  0.0154  -0.0261 296 ARG A N   
2455 C CA  . ARG A 296 ? 1.0709 1.5804 0.9188 0.0173  0.0184  -0.0306 296 ARG A CA  
2456 C C   . ARG A 296 ? 1.1064 1.6432 0.9456 0.0244  0.0197  -0.0243 296 ARG A C   
2457 O O   . ARG A 296 ? 1.0935 1.6582 0.9297 0.0156  0.0186  -0.0328 296 ARG A O   
2458 C CB  . ARG A 296 ? 0.9846 1.4890 0.8366 -0.0010 0.0181  -0.0480 296 ARG A CB  
2459 C CG  . ARG A 296 ? 0.8941 1.3692 0.7541 -0.0077 0.0175  -0.0536 296 ARG A CG  
2460 C CD  . ARG A 296 ? 0.8372 1.3128 0.7002 -0.0255 0.0176  -0.0704 296 ARG A CD  
2461 N NE  . ARG A 296 ? 0.7804 1.2235 0.6504 -0.0310 0.0178  -0.0750 296 ARG A NE  
2462 C CZ  . ARG A 296 ? 0.7647 1.1999 0.6381 -0.0455 0.0188  -0.0885 296 ARG A CZ  
2463 N NH1 . ARG A 296 ? 0.7655 1.2226 0.6359 -0.0570 0.0201  -0.0997 296 ARG A NH1 
2464 N NH2 . ARG A 296 ? 0.7251 1.1304 0.6042 -0.0486 0.0191  -0.0909 296 ARG A NH2 
2465 N N   . ARG A 297 ? 1.1652 1.6938 1.0002 0.0403  0.0223  -0.0094 297 ARG A N   
2466 C CA  . ARG A 297 ? 1.2189 1.7714 1.0446 0.0504  0.0241  -0.0002 297 ARG A CA  
2467 C C   . ARG A 297 ? 1.2195 1.8187 1.0408 0.0548  0.0206  0.0036  297 ARG A C   
2468 O O   . ARG A 297 ? 1.2254 1.8455 1.0388 0.0675  0.0219  0.0154  297 ARG A O   
2469 C CB  . ARG A 297 ? 1.2321 1.7843 1.0549 0.0418  0.0261  -0.0086 297 ARG A CB  
2470 C CG  . ARG A 297 ? 1.2240 1.7342 1.0492 0.0421  0.0305  -0.0085 297 ARG A CG  
2471 C CD  . ARG A 297 ? 1.2505 1.7650 1.0710 0.0373  0.0331  -0.0135 297 ARG A CD  
2472 N NE  . ARG A 297 ? 1.2361 1.7448 1.0618 0.0199  0.0323  -0.0308 297 ARG A NE  
2473 C CZ  . ARG A 297 ? 1.2109 1.7274 1.0335 0.0120  0.0342  -0.0389 297 ARG A CZ  
2474 N NH1 . ARG A 297 ? 1.2155 1.7469 1.0295 0.0198  0.0365  -0.0313 297 ARG A NH1 
2475 N NH2 . ARG A 297 ? 1.1645 1.6734 0.9922 -0.0034 0.0342  -0.0546 297 ARG A NH2 
2476 N N   . LYS A 298 ? 1.2501 1.8652 1.0764 0.0445  0.0166  -0.0058 298 LYS A N   
2477 C CA  . LYS A 298 ? 1.2614 1.9243 1.0846 0.0453  0.0129  -0.0053 298 LYS A CA  
2478 C C   . LYS A 298 ? 1.2498 1.9184 1.0757 0.0555  0.0110  0.0040  298 LYS A C   
2479 O O   . LYS A 298 ? 1.2183 1.8538 1.0498 0.0569  0.0119  0.0057  298 LYS A O   
2480 C CB  . LYS A 298 ? 1.2787 1.9612 1.1049 0.0252  0.0102  -0.0239 298 LYS A CB  
2481 C CG  . LYS A 298 ? 1.3128 1.9973 1.1356 0.0145  0.0121  -0.0341 298 LYS A CG  
2482 C CD  . LYS A 298 ? 1.3346 2.0300 1.1611 -0.0065 0.0109  -0.0536 298 LYS A CD  
2483 C CE  . LYS A 298 ? 1.3578 2.0106 1.1925 -0.0164 0.0123  -0.0625 298 LYS A CE  
2484 N NZ  . LYS A 298 ? 1.3380 1.9986 1.1758 -0.0368 0.0124  -0.0813 298 LYS A NZ  
2485 N N   . ILE A 299 ? 1.2260 1.9382 1.0478 0.0625  0.0085  0.0098  299 ILE A N   
2486 C CA  . ILE A 299 ? 1.2029 1.9275 1.0268 0.0729  0.0068  0.0189  299 ILE A CA  
2487 C C   . ILE A 299 ? 1.1651 1.9256 0.9929 0.0603  0.0019  0.0072  299 ILE A C   
2488 O O   . ILE A 299 ? 1.1789 1.9765 1.0034 0.0524  0.0000  -0.0003 299 ILE A O   
2489 C CB  . ILE A 299 ? 1.2123 1.9587 1.0284 0.0945  0.0085  0.0378  299 ILE A CB  
2490 C CG1 . ILE A 299 ? 1.2311 1.9409 1.0427 0.1059  0.0144  0.0488  299 ILE A CG1 
2491 C CG2 . ILE A 299 ? 1.1869 1.9445 1.0056 0.1061  0.0074  0.0475  299 ILE A CG2 
2492 C CD1 . ILE A 299 ? 1.2776 2.0108 1.0788 0.1214  0.0169  0.0626  299 ILE A CD1 
2493 N N   . TYR A 300 ? 1.0750 1.8244 0.9096 0.0579  0.0005  0.0053  300 TYR A N   
2494 C CA  . TYR A 300 ? 1.0191 1.7971 0.8581 0.0446  -0.0033 -0.0067 300 TYR A CA  
2495 C C   . TYR A 300 ? 0.9683 1.7665 0.8094 0.0556  -0.0053 0.0025  300 TYR A C   
2496 O O   . TYR A 300 ? 0.9178 1.6920 0.7598 0.0698  -0.0033 0.0152  300 TYR A O   
2497 C CB  . TYR A 300 ? 1.0243 1.7695 0.8701 0.0264  -0.0029 -0.0219 300 TYR A CB  
2498 C CG  . TYR A 300 ? 1.0293 1.7649 0.8739 0.0112  -0.0014 -0.0355 300 TYR A CG  
2499 C CD1 . TYR A 300 ? 1.0417 1.7430 0.8845 0.0146  0.0018  -0.0324 300 TYR A CD1 
2500 C CD2 . TYR A 300 ? 1.0394 1.7992 0.8848 -0.0071 -0.0026 -0.0520 300 TYR A CD2 
2501 C CE1 . TYR A 300 ? 1.0439 1.7363 0.8861 0.0010  0.0035  -0.0448 300 TYR A CE1 
2502 C CE2 . TYR A 300 ? 1.0569 1.8067 0.9012 -0.0212 -0.0004 -0.0648 300 TYR A CE2 
2503 C CZ  . TYR A 300 ? 1.0456 1.7618 0.8884 -0.0166 0.0025  -0.0609 300 TYR A CZ  
2504 O OH  . TYR A 300 ? 1.0694 1.7758 0.9113 -0.0300 0.0050  -0.0735 300 TYR A OH  
2505 N N   . LYS A 301 ? 0.9622 1.8050 0.8041 0.0486  -0.0089 -0.0042 301 LYS A N   
2506 C CA  . LYS A 301 ? 0.9493 1.8126 0.7949 0.0554  -0.0110 0.0010  301 LYS A CA  
2507 C C   . LYS A 301 ? 0.8815 1.7283 0.7348 0.0390  -0.0121 -0.0123 301 LYS A C   
2508 O O   . LYS A 301 ? 0.8410 1.6932 0.6959 0.0194  -0.0128 -0.0290 301 LYS A O   
2509 C CB  . LYS A 301 ? 1.0242 1.9492 0.8665 0.0585  -0.0144 0.0023  301 LYS A CB  
2510 C CG  . LYS A 301 ? 1.0783 2.0227 0.9149 0.0831  -0.0136 0.0226  301 LYS A CG  
2511 C CD  . LYS A 301 ? 1.1397 2.1482 0.9740 0.0858  -0.0174 0.0233  301 LYS A CD  
2512 C CE  . LYS A 301 ? 1.1965 2.2275 1.0221 0.1066  -0.0162 0.0406  301 LYS A CE  
2513 N NZ  . LYS A 301 ? 1.1668 2.2637 0.9894 0.1077  -0.0203 0.0399  301 LYS A NZ  
2514 N N   . TRP A 302 ? 0.8282 1.6536 0.6857 0.0472  -0.0115 -0.0048 302 TRP A N   
2515 C CA  . TRP A 302 ? 0.7914 1.5996 0.6557 0.0339  -0.0122 -0.0153 302 TRP A CA  
2516 C C   . TRP A 302 ? 0.7837 1.6356 0.6505 0.0314  -0.0153 -0.0183 302 TRP A C   
2517 O O   . TRP A 302 ? 0.7622 1.6309 0.6293 0.0471  -0.0160 -0.0057 302 TRP A O   
2518 C CB  . TRP A 302 ? 0.7794 1.5413 0.6469 0.0430  -0.0100 -0.0065 302 TRP A CB  
2519 C CG  . TRP A 302 ? 0.7614 1.5014 0.6354 0.0294  -0.0104 -0.0170 302 TRP A CG  
2520 C CD1 . TRP A 302 ? 0.7420 1.4900 0.6204 0.0305  -0.0117 -0.0158 302 TRP A CD1 
2521 C CD2 . TRP A 302 ? 0.7524 1.4581 0.6291 0.0123  -0.0093 -0.0304 302 TRP A CD2 
2522 N NE1 . TRP A 302 ? 0.7382 1.4596 0.6212 0.0155  -0.0114 -0.0271 302 TRP A NE1 
2523 C CE2 . TRP A 302 ? 0.7343 1.4296 0.6165 0.0045  -0.0099 -0.0359 302 TRP A CE2 
2524 C CE3 . TRP A 302 ? 0.7444 1.4280 0.6195 0.0036  -0.0075 -0.0377 302 TRP A CE3 
2525 C CZ2 . TRP A 302 ? 0.7451 1.4087 0.6304 -0.0108 -0.0087 -0.0477 302 TRP A CZ2 
2526 C CZ3 . TRP A 302 ? 0.7398 1.3918 0.6186 -0.0115 -0.0063 -0.0497 302 TRP A CZ3 
2527 C CH2 . TRP A 302 ? 0.7266 1.3689 0.6102 -0.0184 -0.0069 -0.0543 302 TRP A CH2 
2528 N N   . ASN A 303 ? 0.7948 1.6662 0.6634 0.0114  -0.0167 -0.0353 303 ASN A N   
2529 C CA  . ASN A 303 ? 0.8080 1.7236 0.6792 0.0056  -0.0194 -0.0410 303 ASN A CA  
2530 C C   . ASN A 303 ? 0.7927 1.6904 0.6699 -0.0114 -0.0189 -0.0542 303 ASN A C   
2531 O O   . ASN A 303 ? 0.8081 1.7260 0.6861 -0.0303 -0.0191 -0.0702 303 ASN A O   
2532 C CB  . ASN A 303 ? 0.8138 1.7795 0.6811 -0.0027 -0.0212 -0.0495 303 ASN A CB  
2533 C CG  . ASN A 303 ? 0.8535 1.8566 0.7157 0.0171  -0.0230 -0.0341 303 ASN A CG  
2534 O OD1 . ASN A 303 ? 0.8715 1.8904 0.7351 0.0330  -0.0241 -0.0214 303 ASN A OD1 
2535 N ND2 . ASN A 303 ? 0.8510 1.8682 0.7071 0.0167  -0.0228 -0.0349 303 ASN A ND2 
2536 N N   . HIS A 304 ? 0.7653 1.6240 0.6460 -0.0051 -0.0177 -0.0477 304 HIS A N   
2537 C CA  . HIS A 304 ? 0.7565 1.5981 0.6425 -0.0182 -0.0172 -0.0574 304 HIS A CA  
2538 C C   . HIS A 304 ? 0.7073 1.5310 0.5966 -0.0044 -0.0172 -0.0452 304 HIS A C   
2539 O O   . HIS A 304 ? 0.6876 1.4652 0.5786 -0.0029 -0.0153 -0.0425 304 HIS A O   
2540 C CB  . HIS A 304 ? 0.7841 1.5824 0.6707 -0.0338 -0.0145 -0.0690 304 HIS A CB  
2541 C CG  . HIS A 304 ? 0.8252 1.6084 0.7162 -0.0492 -0.0134 -0.0803 304 HIS A CG  
2542 N ND1 . HIS A 304 ? 0.8347 1.5702 0.7282 -0.0503 -0.0116 -0.0795 304 HIS A ND1 
2543 C CD2 . HIS A 304 ? 0.8280 1.6402 0.7209 -0.0641 -0.0136 -0.0926 304 HIS A CD2 
2544 C CE1 . HIS A 304 ? 0.8263 1.5591 0.7228 -0.0649 -0.0106 -0.0903 304 HIS A CE1 
2545 N NE2 . HIS A 304 ? 0.8268 1.6059 0.7229 -0.0735 -0.0116 -0.0985 304 HIS A NE2 
2546 N N   . GLY A 305 ? 0.6856 1.5472 0.5759 0.0059  -0.0192 -0.0378 305 GLY A N   
2547 C CA  . GLY A 305 ? 0.6787 1.5284 0.5722 0.0196  -0.0188 -0.0262 305 GLY A CA  
2548 C C   . GLY A 305 ? 0.6732 1.4953 0.5638 0.0398  -0.0167 -0.0094 305 GLY A C   
2549 O O   . GLY A 305 ? 0.6741 1.5037 0.5598 0.0480  -0.0163 -0.0033 305 GLY A O   
2550 N N   . LEU A 306 ? 0.6990 1.4893 0.5924 0.0473  -0.0150 -0.0022 306 LEU A N   
2551 C CA  . LEU A 306 ? 0.7136 1.4708 0.6046 0.0643  -0.0119 0.0121  306 LEU A CA  
2552 C C   . LEU A 306 ? 0.7140 1.4268 0.6037 0.0564  -0.0101 0.0071  306 LEU A C   
2553 O O   . LEU A 306 ? 0.6925 1.3863 0.5850 0.0395  -0.0107 -0.0057 306 LEU A O   
2554 C CB  . LEU A 306 ? 0.6990 1.4379 0.5935 0.0734  -0.0102 0.0199  306 LEU A CB  
2555 C CG  . LEU A 306 ? 0.6888 1.4668 0.5848 0.0854  -0.0109 0.0279  306 LEU A CG  
2556 C CD1 . LEU A 306 ? 0.6869 1.4438 0.5874 0.0878  -0.0095 0.0306  306 LEU A CD1 
2557 C CD2 . LEU A 306 ? 0.7147 1.5077 0.6056 0.1072  -0.0088 0.0444  306 LEU A CD2 
2558 N N   . LEU A 307 ? 0.7386 1.4354 0.6240 0.0691  -0.0076 0.0174  307 LEU A N   
2559 C CA  . LEU A 307 ? 0.7737 1.4264 0.6582 0.0646  -0.0054 0.0149  307 LEU A CA  
2560 C C   . LEU A 307 ? 0.7446 1.3552 0.6322 0.0680  -0.0031 0.0191  307 LEU A C   
2561 O O   . LEU A 307 ? 0.7430 1.3464 0.6295 0.0838  -0.0004 0.0319  307 LEU A O   
2562 C CB  . LEU A 307 ? 0.7970 1.4481 0.6755 0.0768  -0.0030 0.0246  307 LEU A CB  
2563 C CG  . LEU A 307 ? 0.8069 1.4717 0.6820 0.0676  -0.0041 0.0165  307 LEU A CG  
2564 C CD1 . LEU A 307 ? 0.8186 1.4852 0.6872 0.0830  -0.0014 0.0290  307 LEU A CD1 
2565 C CD2 . LEU A 307 ? 0.8058 1.4363 0.6834 0.0512  -0.0039 0.0038  307 LEU A CD2 
2566 N N   . GLN A 308 ? 0.7506 1.3334 0.6416 0.0533  -0.0037 0.0082  308 GLN A N   
2567 C CA  . GLN A 308 ? 0.8045 1.3438 0.6978 0.0554  -0.0015 0.0113  308 GLN A CA  
2568 C C   . GLN A 308 ? 0.8283 1.3428 0.7180 0.0666  0.0019  0.0206  308 GLN A C   
2569 O O   . GLN A 308 ? 0.7956 1.3091 0.6827 0.0634  0.0022  0.0175  308 GLN A O   
2570 C CB  . GLN A 308 ? 0.8026 1.3178 0.6994 0.0377  -0.0028 -0.0019 308 GLN A CB  
2571 C CG  . GLN A 308 ? 0.8093 1.3275 0.7101 0.0299  -0.0043 -0.0074 308 GLN A CG  
2572 C CD  . GLN A 308 ? 0.8118 1.3190 0.7146 0.0107  -0.0054 -0.0222 308 GLN A CD  
2573 O OE1 . GLN A 308 ? 0.8089 1.3347 0.7105 0.0007  -0.0062 -0.0311 308 GLN A OE1 
2574 N NE2 . GLN A 308 ? 0.8019 1.2788 0.7076 0.0055  -0.0049 -0.0247 308 GLN A NE2 
2575 N N   . GLY A 309 ? 0.8774 1.3728 0.7669 0.0796  0.0053  0.0316  309 GLY A N   
2576 C CA  . GLY A 309 ? 0.9540 1.4254 0.8397 0.0907  0.0098  0.0409  309 GLY A CA  
2577 C C   . GLY A 309 ? 0.9825 1.4709 0.8636 0.1096  0.0133  0.0556  309 GLY A C   
2578 O O   . GLY A 309 ? 1.0272 1.4915 0.9056 0.1208  0.0186  0.0652  309 GLY A O   
2579 N N   . ASP A 310 ? 0.9602 1.4906 0.8401 0.1132  0.0110  0.0573  310 ASP A N   
2580 C CA  . ASP A 310 ? 0.9940 1.5445 0.8698 0.1322  0.0142  0.0719  310 ASP A CA  
2581 C C   . ASP A 310 ? 1.0089 1.5472 0.8874 0.1404  0.0170  0.0786  310 ASP A C   
2582 O O   . ASP A 310 ? 0.9990 1.5440 0.8826 0.1320  0.0137  0.0717  310 ASP A O   
2583 C CB  . ASP A 310 ? 0.9704 1.5724 0.8449 0.1330  0.0103  0.0712  310 ASP A CB  
2584 C CG  . ASP A 310 ? 0.9738 1.5982 0.8426 0.1539  0.0139  0.0872  310 ASP A CG  
2585 O OD1 . ASP A 310 ? 1.0072 1.6208 0.8756 0.1678  0.0183  0.0983  310 ASP A OD1 
2586 O OD2 . ASP A 310 ? 0.9927 1.6463 0.8571 0.1566  0.0125  0.0888  310 ASP A OD2 
2587 N N   . PRO A 311 ? 1.0504 1.5694 0.9251 0.1564  0.0236  0.0918  311 PRO A N   
2588 C CA  . PRO A 311 ? 1.0656 1.5692 0.9419 0.1656  0.0278  0.0991  311 PRO A CA  
2589 C C   . PRO A 311 ? 1.0632 1.6002 0.9430 0.1684  0.0250  0.0998  311 PRO A C   
2590 O O   . PRO A 311 ? 1.0713 1.5949 0.9548 0.1682  0.0263  0.0997  311 PRO A O   
2591 C CB  . PRO A 311 ? 1.0900 1.5826 0.9595 0.1850  0.0360  0.1146  311 PRO A CB  
2592 C CG  . PRO A 311 ? 1.0862 1.5912 0.9505 0.1858  0.0354  0.1156  311 PRO A CG  
2593 C CD  . PRO A 311 ? 1.0673 1.5735 0.9354 0.1656  0.0285  0.0998  311 PRO A CD  
2594 N N   . LEU A 312 ? 1.0531 1.6343 0.9319 0.1706  0.0214  0.1003  312 LEU A N   
2595 C CA  . LEU A 312 ? 1.0071 1.6246 0.8891 0.1745  0.0189  0.1017  312 LEU A CA  
2596 C C   . LEU A 312 ? 0.9523 1.5856 0.8405 0.1550  0.0121  0.0861  312 LEU A C   
2597 O O   . LEU A 312 ? 0.9340 1.5886 0.8261 0.1552  0.0105  0.0852  312 LEU A O   
2598 C CB  . LEU A 312 ? 1.0442 1.7051 0.9220 0.1886  0.0190  0.1115  312 LEU A CB  
2599 C CG  . LEU A 312 ? 1.0929 1.7480 0.9652 0.2124  0.0267  0.1300  312 LEU A CG  
2600 C CD1 . LEU A 312 ? 1.1117 1.8143 0.9799 0.2254  0.0257  0.1388  312 LEU A CD1 
2601 C CD2 . LEU A 312 ? 1.1121 1.7549 0.9877 0.2209  0.0308  0.1359  312 LEU A CD2 
2602 N N   . SER A 313 ? 0.9043 1.5264 0.7931 0.1383  0.0088  0.0739  313 SER A N   
2603 C CA  . SER A 313 ? 0.8733 1.5097 0.7667 0.1190  0.0032  0.0586  313 SER A CA  
2604 C C   . SER A 313 ? 0.8538 1.4775 0.7525 0.1137  0.0030  0.0548  313 SER A C   
2605 O O   . SER A 313 ? 0.8518 1.5056 0.7540 0.1084  0.0000  0.0498  313 SER A O   
2606 C CB  . SER A 313 ? 0.8501 1.4661 0.7430 0.1030  0.0014  0.0470  313 SER A CB  
2607 O OG  . SER A 313 ? 0.8718 1.5120 0.7606 0.1040  0.0002  0.0469  313 SER A OG  
2608 N N   . GLY A 314 ? 0.8465 1.4271 0.7458 0.1151  0.0063  0.0573  314 GLY A N   
2609 C CA  . GLY A 314 ? 0.8145 1.3785 0.7182 0.1095  0.0063  0.0536  314 GLY A CA  
2610 C C   . GLY A 314 ? 0.8127 1.4058 0.7188 0.1183  0.0067  0.0592  314 GLY A C   
2611 O O   . GLY A 314 ? 0.8181 1.4269 0.7283 0.1078  0.0035  0.0508  314 GLY A O   
2612 N N   . CYS A 315 ? 0.8161 1.4162 0.7194 0.1378  0.0110  0.0734  315 CYS A N   
2613 C CA  . CYS A 315 ? 0.8193 1.4448 0.7247 0.1494  0.0124  0.0807  315 CYS A CA  
2614 C C   . CYS A 315 ? 0.8184 1.4981 0.7254 0.1480  0.0079  0.0778  315 CYS A C   
2615 O O   . CYS A 315 ? 0.8180 1.5229 0.7288 0.1498  0.0069  0.0778  315 CYS A O   
2616 C CB  . CYS A 315 ? 0.8456 1.4611 0.7469 0.1716  0.0195  0.0974  315 CYS A CB  
2617 S SG  . CYS A 315 ? 0.8717 1.5148 0.7666 0.1860  0.0206  0.1077  315 CYS A SG  
2618 N N   . LEU A 316 ? 0.7826 1.4812 0.6864 0.1450  0.0052  0.0752  316 LEU A N   
2619 C CA  . LEU A 316 ? 0.7788 1.5300 0.6837 0.1418  0.0007  0.0710  316 LEU A CA  
2620 C C   . LEU A 316 ? 0.7774 1.5373 0.6868 0.1189  -0.0040 0.0535  316 LEU A C   
2621 O O   . LEU A 316 ? 0.7994 1.5997 0.7120 0.1147  -0.0069 0.0488  316 LEU A O   
2622 C CB  . LEU A 316 ? 0.7763 1.5455 0.6757 0.1465  0.0000  0.0743  316 LEU A CB  
2623 C CG  . LEU A 316 ? 0.7831 1.5572 0.6773 0.1708  0.0048  0.0926  316 LEU A CG  
2624 C CD1 . LEU A 316 ? 0.7794 1.5689 0.6679 0.1729  0.0038  0.0944  316 LEU A CD1 
2625 C CD2 . LEU A 316 ? 0.7873 1.6002 0.6836 0.1855  0.0054  0.1018  316 LEU A CD2 
2626 N N   . CYS A 317 ? 0.7630 1.4850 0.6726 0.1043  -0.0043 0.0441  317 CYS A N   
2627 C CA  . CYS A 317 ? 0.7486 1.4709 0.6619 0.0827  -0.0075 0.0280  317 CYS A CA  
2628 C C   . CYS A 317 ? 0.7518 1.4728 0.6697 0.0810  -0.0071 0.0269  317 CYS A C   
2629 O O   . CYS A 317 ? 0.7535 1.4989 0.6747 0.0683  -0.0096 0.0166  317 CYS A O   
2630 C CB  . CYS A 317 ? 0.7284 1.4077 0.6404 0.0698  -0.0073 0.0200  317 CYS A CB  
2631 S SG  . CYS A 317 ? 0.6990 1.3768 0.6141 0.0432  -0.0101 0.0003  317 CYS A SG  
2632 N N   . GLU A 318 ? 0.7580 1.4508 0.6760 0.0933  -0.0034 0.0370  318 GLU A N   
2633 C CA  . GLU A 318 ? 0.7653 1.4573 0.6874 0.0942  -0.0024 0.0376  318 GLU A CA  
2634 C C   . GLU A 318 ? 0.7477 1.4899 0.6723 0.1032  -0.0033 0.0420  318 GLU A C   
2635 O O   . GLU A 318 ? 0.7526 1.5138 0.6814 0.0950  -0.0049 0.0352  318 GLU A O   
2636 C CB  . GLU A 318 ? 0.8162 1.4686 0.7373 0.1067  0.0025  0.0482  318 GLU A CB  
2637 C CG  . GLU A 318 ? 0.8942 1.4977 0.8144 0.0961  0.0031  0.0425  318 GLU A CG  
2638 C CD  . GLU A 318 ? 0.9357 1.5043 0.8558 0.1056  0.0079  0.0506  318 GLU A CD  
2639 O OE1 . GLU A 318 ? 0.9584 1.4938 0.8755 0.1100  0.0107  0.0550  318 GLU A OE1 
2640 O OE2 . GLU A 318 ? 0.9310 1.5060 0.8540 0.1084  0.0091  0.0523  318 GLU A OE2 
2641 N N   . LEU A 319 ? 0.7269 1.4903 0.6485 0.1205  -0.0019 0.0537  319 LEU A N   
2642 C CA  . LEU A 319 ? 0.7047 1.5188 0.6280 0.1316  -0.0028 0.0596  319 LEU A CA  
2643 C C   . LEU A 319 ? 0.6710 1.5276 0.5970 0.1151  -0.0081 0.0459  319 LEU A C   
2644 O O   . LEU A 319 ? 0.6815 1.5685 0.6122 0.1121  -0.0095 0.0422  319 LEU A O   
2645 C CB  . LEU A 319 ? 0.7259 1.5523 0.6443 0.1520  -0.0004 0.0742  319 LEU A CB  
2646 C CG  . LEU A 319 ? 0.7249 1.5951 0.6437 0.1717  0.0006  0.0867  319 LEU A CG  
2647 C CD1 . LEU A 319 ? 0.7202 1.6444 0.6387 0.1680  -0.0043 0.0822  319 LEU A CD1 
2648 C CD2 . LEU A 319 ? 0.7331 1.6118 0.6576 0.1751  0.0020  0.0879  319 LEU A CD2 
2649 N N   . TYR A 320 ? 0.6305 1.4886 0.5536 0.1038  -0.0106 0.0379  320 TYR A N   
2650 C CA  . TYR A 320 ? 0.6219 1.5145 0.5467 0.0852  -0.0148 0.0229  320 TYR A CA  
2651 C C   . TYR A 320 ? 0.6474 1.5295 0.5766 0.0658  -0.0155 0.0091  320 TYR A C   
2652 O O   . TYR A 320 ? 0.6299 1.5505 0.5627 0.0576  -0.0174 0.0015  320 TYR A O   
2653 C CB  . TYR A 320 ? 0.6028 1.4866 0.5231 0.0760  -0.0161 0.0166  320 TYR A CB  
2654 C CG  . TYR A 320 ? 0.6122 1.5274 0.5333 0.0555  -0.0194 0.0001  320 TYR A CG  
2655 C CD1 . TYR A 320 ? 0.6020 1.5724 0.5224 0.0579  -0.0220 -0.0003 320 TYR A CD1 
2656 C CD2 . TYR A 320 ? 0.6135 1.5026 0.5354 0.0337  -0.0193 -0.0149 320 TYR A CD2 
2657 C CE1 . TYR A 320 ? 0.6029 1.6021 0.5237 0.0379  -0.0243 -0.0164 320 TYR A CE1 
2658 C CE2 . TYR A 320 ? 0.6124 1.5276 0.5345 0.0143  -0.0211 -0.0306 320 TYR A CE2 
2659 C CZ  . TYR A 320 ? 0.6158 1.5860 0.5374 0.0159  -0.0235 -0.0318 320 TYR A CZ  
2660 O OH  . TYR A 320 ? 0.6110 1.6068 0.5324 -0.0046 -0.0246 -0.0483 320 TYR A OH  
2661 N N   . MET A 321 ? 0.6469 1.4777 0.5756 0.0589  -0.0136 0.0063  321 MET A N   
2662 C CA  . MET A 321 ? 0.6460 1.4609 0.5777 0.0400  -0.0138 -0.0065 321 MET A CA  
2663 C C   . MET A 321 ? 0.6386 1.4674 0.5749 0.0438  -0.0130 -0.0042 321 MET A C   
2664 O O   . MET A 321 ? 0.6351 1.4729 0.5743 0.0281  -0.0137 -0.0157 321 MET A O   
2665 C CB  . MET A 321 ? 0.6992 1.4562 0.6289 0.0340  -0.0120 -0.0083 321 MET A CB  
2666 C CG  . MET A 321 ? 0.7277 1.4684 0.6537 0.0250  -0.0127 -0.0145 321 MET A CG  
2667 S SD  . MET A 321 ? 0.7717 1.5293 0.6982 -0.0015 -0.0143 -0.0347 321 MET A SD  
2668 C CE  . MET A 321 ? 0.7475 1.4549 0.6750 -0.0147 -0.0122 -0.0417 321 MET A CE  
2669 N N   . ALA A 322 ? 0.6204 1.4494 0.5572 0.0646  -0.0109 0.0106  322 ALA A N   
2670 C CA  . ALA A 322 ? 0.6263 1.4720 0.5676 0.0708  -0.0098 0.0141  322 ALA A CA  
2671 C C   . ALA A 322 ? 0.6446 1.5510 0.5891 0.0687  -0.0125 0.0098  322 ALA A C   
2672 O O   . ALA A 322 ? 0.6363 1.5615 0.5853 0.0618  -0.0128 0.0039  322 ALA A O   
2673 C CB  . ALA A 322 ? 0.6412 1.4726 0.5816 0.0943  -0.0059 0.0313  322 ALA A CB  
2674 N N   . PHE A 323 ? 0.6336 1.5710 0.5757 0.0745  -0.0145 0.0126  323 PHE A N   
2675 C CA  . PHE A 323 ? 0.6786 1.6769 0.6233 0.0726  -0.0174 0.0084  323 PHE A CA  
2676 C C   . PHE A 323 ? 0.6887 1.7006 0.6351 0.0461  -0.0196 -0.0112 323 PHE A C   
2677 O O   . PHE A 323 ? 0.6932 1.7452 0.6441 0.0395  -0.0208 -0.0178 323 PHE A O   
2678 C CB  . PHE A 323 ? 0.7056 1.7307 0.6463 0.0851  -0.0189 0.0164  323 PHE A CB  
2679 C CG  . PHE A 323 ? 0.6921 1.7832 0.6351 0.0838  -0.0223 0.0125  323 PHE A CG  
2680 C CD1 . PHE A 323 ? 0.7027 1.8326 0.6505 0.0945  -0.0224 0.0181  323 PHE A CD1 
2681 C CD2 . PHE A 323 ? 0.7055 1.8213 0.6456 0.0723  -0.0252 0.0033  323 PHE A CD2 
2682 C CE1 . PHE A 323 ? 0.7085 1.9022 0.6587 0.0935  -0.0257 0.0144  323 PHE A CE1 
2683 C CE2 . PHE A 323 ? 0.7161 1.8950 0.6580 0.0707  -0.0284 -0.0007 323 PHE A CE2 
2684 C CZ  . PHE A 323 ? 0.7185 1.9373 0.6657 0.0813  -0.0288 0.0048  323 PHE A CZ  
2685 N N   . MET A 324 ? 0.6779 1.6566 0.6209 0.0308  -0.0195 -0.0205 324 MET A N   
2686 C CA  . MET A 324 ? 0.6895 1.6729 0.6332 0.0049  -0.0201 -0.0394 324 MET A CA  
2687 C C   . MET A 324 ? 0.7016 1.6718 0.6492 -0.0042 -0.0184 -0.0451 324 MET A C   
2688 O O   . MET A 324 ? 0.7221 1.7160 0.6720 -0.0217 -0.0185 -0.0586 324 MET A O   
2689 C CB  . MET A 324 ? 0.6706 1.6132 0.6098 -0.0073 -0.0194 -0.0465 324 MET A CB  
2690 C CG  . MET A 324 ? 0.6824 1.6346 0.6172 -0.0009 -0.0208 -0.0427 324 MET A CG  
2691 S SD  . MET A 324 ? 0.6806 1.6884 0.6147 -0.0170 -0.0231 -0.0573 324 MET A SD  
2692 C CE  . MET A 324 ? 0.7014 1.7677 0.6369 0.0058  -0.0258 -0.0431 324 MET A CE  
2693 N N   . ASP A 325 ? 0.6838 1.6168 0.6318 0.0073  -0.0164 -0.0348 325 ASP A N   
2694 C CA  . ASP A 325 ? 0.7262 1.6426 0.6774 0.0006  -0.0145 -0.0385 325 ASP A CA  
2695 C C   . ASP A 325 ? 0.7155 1.6798 0.6721 0.0048  -0.0150 -0.0379 325 ASP A C   
2696 O O   . ASP A 325 ? 0.6948 1.6689 0.6542 -0.0105 -0.0143 -0.0490 325 ASP A O   
2697 C CB  . ASP A 325 ? 0.7580 1.6243 0.7078 0.0130  -0.0121 -0.0271 325 ASP A CB  
2698 C CG  . ASP A 325 ? 0.8176 1.6595 0.7695 0.0038  -0.0101 -0.0320 325 ASP A CG  
2699 O OD1 . ASP A 325 ? 0.8463 1.7109 0.8023 0.0089  -0.0094 -0.0294 325 ASP A OD1 
2700 O OD2 . ASP A 325 ? 0.9035 1.7035 0.8528 -0.0079 -0.0091 -0.0379 325 ASP A OD2 
2701 N N   . ARG A 326 ? 0.7063 1.6998 0.6643 0.0260  -0.0157 -0.0246 326 ARG A N   
2702 C CA  . ARG A 326 ? 0.7115 1.7545 0.6750 0.0326  -0.0162 -0.0226 326 ARG A CA  
2703 C C   . ARG A 326 ? 0.6840 1.7783 0.6493 0.0163  -0.0190 -0.0366 326 ARG A C   
2704 O O   . ARG A 326 ? 0.6626 1.7897 0.6326 0.0087  -0.0191 -0.0437 326 ARG A O   
2705 C CB  . ARG A 326 ? 0.7325 1.7937 0.6961 0.0603  -0.0159 -0.0042 326 ARG A CB  
2706 C CG  . ARG A 326 ? 0.7657 1.8640 0.7352 0.0725  -0.0151 0.0020  326 ARG A CG  
2707 C CD  . ARG A 326 ? 0.7980 1.8877 0.7666 0.1010  -0.0122 0.0221  326 ARG A CD  
2708 N NE  . ARG A 326 ? 0.7953 1.8850 0.7586 0.1131  -0.0129 0.0311  326 ARG A NE  
2709 C CZ  . ARG A 326 ? 0.8195 1.9543 0.7827 0.1291  -0.0141 0.0404  326 ARG A CZ  
2710 N NH1 . ARG A 326 ? 0.8110 1.9969 0.7798 0.1357  -0.0150 0.0420  326 ARG A NH1 
2711 N NH2 . ARG A 326 ? 0.8011 1.9308 0.7587 0.1390  -0.0143 0.0482  326 ARG A NH2 
2712 N N   . LEU A 327 ? 0.6937 1.7930 0.6548 0.0101  -0.0208 -0.0412 327 LEU A N   
2713 C CA  . LEU A 327 ? 0.6785 1.8245 0.6401 -0.0059 -0.0230 -0.0550 327 LEU A CA  
2714 C C   . LEU A 327 ? 0.6852 1.8229 0.6476 -0.0338 -0.0213 -0.0744 327 LEU A C   
2715 O O   . LEU A 327 ? 0.6833 1.8639 0.6496 -0.0448 -0.0216 -0.0844 327 LEU A O   
2716 C CB  . LEU A 327 ? 0.6692 1.8131 0.6253 -0.0055 -0.0246 -0.0547 327 LEU A CB  
2717 C CG  . LEU A 327 ? 0.6559 1.8593 0.6116 -0.0071 -0.0277 -0.0589 327 LEU A CG  
2718 C CD1 . LEU A 327 ? 0.6496 1.9052 0.6094 0.0127  -0.0296 -0.0471 327 LEU A CD1 
2719 C CD2 . LEU A 327 ? 0.6279 1.8159 0.5775 -0.0025 -0.0286 -0.0548 327 LEU A CD2 
2720 N N   . TYR A 328 ? 0.7030 1.7855 0.6617 -0.0449 -0.0190 -0.0794 328 TYR A N   
2721 C CA  . TYR A 328 ? 0.6745 1.7440 0.6323 -0.0717 -0.0165 -0.0977 328 TYR A CA  
2722 C C   . TYR A 328 ? 0.6870 1.7148 0.6456 -0.0780 -0.0134 -0.0994 328 TYR A C   
2723 O O   . TYR A 328 ? 0.6723 1.6931 0.6304 -0.0995 -0.0106 -0.1139 328 TYR A O   
2724 C CB  . TYR A 328 ? 0.6562 1.7002 0.6084 -0.0836 -0.0158 -0.1053 328 TYR A CB  
2725 C CG  . TYR A 328 ? 0.6274 1.7095 0.5778 -0.0796 -0.0186 -0.1050 328 TYR A CG  
2726 C CD1 . TYR A 328 ? 0.6033 1.7434 0.5556 -0.0901 -0.0197 -0.1157 328 TYR A CD1 
2727 C CD2 . TYR A 328 ? 0.6020 1.6625 0.5484 -0.0662 -0.0199 -0.0946 328 TYR A CD2 
2728 C CE1 . TYR A 328 ? 0.5833 1.7596 0.5335 -0.0868 -0.0224 -0.1156 328 TYR A CE1 
2729 C CE2 . TYR A 328 ? 0.6057 1.7005 0.5499 -0.0626 -0.0223 -0.0942 328 TYR A CE2 
2730 C CZ  . TYR A 328 ? 0.6096 1.7624 0.5555 -0.0727 -0.0237 -0.1045 328 TYR A CZ  
2731 O OH  . TYR A 328 ? 0.6035 1.7913 0.5468 -0.0692 -0.0262 -0.1040 328 TYR A OH  
2732 N N   . PHE A 329 ? 0.7108 1.7106 0.6701 -0.0598 -0.0133 -0.0848 329 PHE A N   
2733 C CA  . PHE A 329 ? 0.7472 1.7082 0.7071 -0.0640 -0.0105 -0.0851 329 PHE A CA  
2734 C C   . PHE A 329 ? 0.8245 1.8082 0.7898 -0.0505 -0.0105 -0.0765 329 PHE A C   
2735 O O   . PHE A 329 ? 0.8834 1.8401 0.8489 -0.0343 -0.0097 -0.0638 329 PHE A O   
2736 C CB  . PHE A 329 ? 0.7356 1.6368 0.6913 -0.0574 -0.0096 -0.0772 329 PHE A CB  
2737 C CG  . PHE A 329 ? 0.7105 1.5868 0.6613 -0.0707 -0.0092 -0.0856 329 PHE A CG  
2738 C CD1 . PHE A 329 ? 0.7094 1.5601 0.6579 -0.0918 -0.0063 -0.0988 329 PHE A CD1 
2739 C CD2 . PHE A 329 ? 0.7006 1.5794 0.6488 -0.0619 -0.0112 -0.0804 329 PHE A CD2 
2740 C CE1 . PHE A 329 ? 0.6919 1.5198 0.6359 -0.1036 -0.0053 -0.1065 329 PHE A CE1 
2741 C CE2 . PHE A 329 ? 0.6978 1.5545 0.6417 -0.0742 -0.0105 -0.0885 329 PHE A CE2 
2742 C CZ  . PHE A 329 ? 0.6954 1.5267 0.6375 -0.0948 -0.0075 -0.1015 329 PHE A CZ  
2743 N N   . SER A 330 ? 0.8468 1.8808 0.8163 -0.0578 -0.0109 -0.0843 330 SER A N   
2744 C CA  . SER A 330 ? 0.8571 1.9234 0.8324 -0.0448 -0.0111 -0.0771 330 SER A CA  
2745 C C   . SER A 330 ? 0.8629 1.9301 0.8411 -0.0604 -0.0084 -0.0875 330 SER A C   
2746 O O   . SER A 330 ? 0.8828 1.9547 0.8650 -0.0501 -0.0074 -0.0805 330 SER A O   
2747 C CB  . SER A 330 ? 0.8729 2.0040 0.8517 -0.0369 -0.0141 -0.0755 330 SER A CB  
2748 O OG  . SER A 330 ? 0.8631 2.0207 0.8405 -0.0570 -0.0150 -0.0910 330 SER A OG  
2749 N N   . ASN A 331 ? 0.8806 1.9426 0.8565 -0.0852 -0.0066 -0.1041 331 ASN A N   
2750 C CA  . ASN A 331 ? 0.9226 1.9859 0.9004 -0.1025 -0.0033 -0.1154 331 ASN A CA  
2751 C C   . ASN A 331 ? 0.9429 1.9455 0.9157 -0.1145 0.0001  -0.1195 331 ASN A C   
2752 O O   . ASN A 331 ? 0.9505 1.9481 0.9221 -0.1356 0.0036  -0.1331 331 ASN A O   
2753 C CB  . ASN A 331 ? 0.9328 2.0422 0.9121 -0.1230 -0.0027 -0.1324 331 ASN A CB  
2754 C CG  . ASN A 331 ? 0.9192 2.0935 0.9037 -0.1116 -0.0063 -0.1288 331 ASN A CG  
2755 O OD1 . ASN A 331 ? 0.9267 2.1269 0.9098 -0.1140 -0.0085 -0.1324 331 ASN A OD1 
2756 N ND2 . ASN A 331 ? 0.8953 2.0965 0.8859 -0.0982 -0.0069 -0.1210 331 ASN A ND2 
2757 N N   . LEU A 332 ? 0.9519 1.9092 0.9217 -0.1009 -0.0005 -0.1075 332 LEU A N   
2758 C CA  . LEU A 332 ? 0.9453 1.8443 0.9101 -0.1096 0.0021  -0.1095 332 LEU A CA  
2759 C C   . LEU A 332 ? 0.9145 1.7997 0.8806 -0.1142 0.0051  -0.1107 332 LEU A C   
2760 O O   . LEU A 332 ? 0.9310 1.8016 0.8945 -0.1339 0.0085  -0.1225 332 LEU A O   
2761 C CB  . LEU A 332 ? 0.9585 1.8171 0.9202 -0.0931 0.0005  -0.0962 332 LEU A CB  
2762 C CG  . LEU A 332 ? 0.9700 1.8296 0.9288 -0.0902 -0.0017 -0.0952 332 LEU A CG  
2763 C CD1 . LEU A 332 ? 0.9682 1.7921 0.9249 -0.0714 -0.0030 -0.0807 332 LEU A CD1 
2764 C CD2 . LEU A 332 ? 0.9660 1.8078 0.9203 -0.1121 0.0002  -0.1095 332 LEU A CD2 
2765 N N   . ASP A 333 ? 0.8669 1.7566 0.8367 -0.0959 0.0043  -0.0985 333 ASP A N   
2766 C CA  . ASP A 333 ? 0.8519 1.7266 0.8230 -0.0972 0.0071  -0.0976 333 ASP A CA  
2767 C C   . ASP A 333 ? 0.8766 1.7256 0.8481 -0.0753 0.0066  -0.0815 333 ASP A C   
2768 O O   . ASP A 333 ? 0.9129 1.7268 0.8805 -0.0677 0.0056  -0.0746 333 ASP A O   
2769 C CB  . ASP A 333 ? 0.8234 1.6573 0.7890 -0.1175 0.0105  -0.1077 333 ASP A CB  
2770 C CG  . ASP A 333 ? 0.8327 1.6572 0.7993 -0.1218 0.0136  -0.1089 333 ASP A CG  
2771 O OD1 . ASP A 333 ? 0.8245 1.6601 0.7954 -0.1065 0.0131  -0.0994 333 ASP A OD1 
2772 O OD2 . ASP A 333 ? 0.8297 1.6345 0.7925 -0.1407 0.0170  -0.1192 333 ASP A OD2 
2773 N N   . LYS A 334 ? 0.8991 1.7653 0.8752 -0.0657 0.0077  -0.0761 334 LYS A N   
2774 C CA  . LYS A 334 ? 0.9422 1.7835 0.9186 -0.0462 0.0086  -0.0619 334 LYS A CA  
2775 C C   . LYS A 334 ? 0.9438 1.7296 0.9151 -0.0530 0.0108  -0.0623 334 LYS A C   
2776 O O   . LYS A 334 ? 0.9405 1.6947 0.9100 -0.0395 0.0114  -0.0517 334 LYS A O   
2777 C CB  . LYS A 334 ? 0.9626 1.8392 0.9455 -0.0344 0.0099  -0.0566 334 LYS A CB  
2778 C CG  . LYS A 334 ? 0.9808 1.8447 0.9647 -0.0098 0.0111  -0.0405 334 LYS A CG  
2779 C CD  . LYS A 334 ? 1.0056 1.8734 0.9932 -0.0044 0.0144  -0.0374 334 LYS A CD  
2780 C CE  . LYS A 334 ? 1.0140 1.8369 0.9987 0.0089  0.0172  -0.0263 334 LYS A CE  
2781 N NZ  . LYS A 334 ? 0.9996 1.8224 0.9873 0.0123  0.0210  -0.0244 334 LYS A NZ  
2782 N N   . ASP A 335 ? 0.8999 1.6746 0.8685 -0.0741 0.0124  -0.0745 335 ASP A N   
2783 C CA  . ASP A 335 ? 0.8573 1.5840 0.8209 -0.0818 0.0146  -0.0756 335 ASP A CA  
2784 C C   . ASP A 335 ? 0.8072 1.4948 0.7643 -0.0913 0.0140  -0.0791 335 ASP A C   
2785 O O   . ASP A 335 ? 0.8223 1.4683 0.7748 -0.0960 0.0155  -0.0787 335 ASP A O   
2786 C CB  . ASP A 335 ? 0.8921 1.6280 0.8563 -0.0976 0.0177  -0.0854 335 ASP A CB  
2787 C CG  . ASP A 335 ? 0.9101 1.6769 0.8805 -0.0873 0.0188  -0.0809 335 ASP A CG  
2788 O OD1 . ASP A 335 ? 0.9280 1.6830 0.8997 -0.0695 0.0190  -0.0690 335 ASP A OD1 
2789 O OD2 . ASP A 335 ? 0.9137 1.7166 0.8877 -0.0974 0.0201  -0.0895 335 ASP A OD2 
2790 N N   . ALA A 336 ? 0.7311 1.4330 0.6878 -0.0938 0.0120  -0.0825 336 ALA A N   
2791 C CA  . ALA A 336 ? 0.6747 1.3419 0.6258 -0.1009 0.0115  -0.0852 336 ALA A CA  
2792 C C   . ALA A 336 ? 0.6441 1.2814 0.5937 -0.0838 0.0096  -0.0726 336 ALA A C   
2793 O O   . ALA A 336 ? 0.6205 1.2699 0.5735 -0.0660 0.0088  -0.0622 336 ALA A O   
2794 C CB  . ALA A 336 ? 0.6422 1.3361 0.5934 -0.1101 0.0104  -0.0938 336 ALA A CB  
2795 N N   . PHE A 337 ? 0.6215 1.2194 0.5660 -0.0893 0.0096  -0.0738 337 PHE A N   
2796 C CA  . PHE A 337 ? 0.6014 1.1725 0.5442 -0.0756 0.0079  -0.0639 337 PHE A CA  
2797 C C   . PHE A 337 ? 0.5733 1.1590 0.5161 -0.0741 0.0057  -0.0651 337 PHE A C   
2798 O O   . PHE A 337 ? 0.5728 1.1581 0.5134 -0.0886 0.0060  -0.0749 337 PHE A O   
2799 C CB  . PHE A 337 ? 0.5986 1.1204 0.5362 -0.0817 0.0088  -0.0642 337 PHE A CB  
2800 C CG  . PHE A 337 ? 0.5906 1.0851 0.5264 -0.0702 0.0072  -0.0559 337 PHE A CG  
2801 C CD1 . PHE A 337 ? 0.5730 1.0611 0.5068 -0.0737 0.0058  -0.0589 337 PHE A CD1 
2802 C CD2 . PHE A 337 ? 0.5848 1.0602 0.5208 -0.0563 0.0075  -0.0456 337 PHE A CD2 
2803 C CE1 . PHE A 337 ? 0.5773 1.0417 0.5098 -0.0634 0.0045  -0.0516 337 PHE A CE1 
2804 C CE2 . PHE A 337 ? 0.5686 1.0198 0.5029 -0.0466 0.0065  -0.0387 337 PHE A CE2 
2805 C CZ  . PHE A 337 ? 0.5654 1.0114 0.4981 -0.0501 0.0048  -0.0415 337 PHE A CZ  
2806 N N   . ILE A 338 ? 0.5547 1.1526 0.4997 -0.0566 0.0040  -0.0551 338 ILE A N   
2807 C CA  . ILE A 338 ? 0.5481 1.1565 0.4924 -0.0530 0.0019  -0.0544 338 ILE A CA  
2808 C C   . ILE A 338 ? 0.5358 1.1202 0.4789 -0.0359 0.0014  -0.0422 338 ILE A C   
2809 O O   . ILE A 338 ? 0.5477 1.1307 0.4926 -0.0215 0.0025  -0.0325 338 ILE A O   
2810 C CB  . ILE A 338 ? 0.5429 1.2047 0.4912 -0.0495 0.0005  -0.0556 338 ILE A CB  
2811 C CG1 . ILE A 338 ? 0.5731 1.2637 0.5234 -0.0653 0.0016  -0.0672 338 ILE A CG1 
2812 C CG2 . ILE A 338 ? 0.5533 1.2250 0.4999 -0.0506 -0.0013 -0.0578 338 ILE A CG2 
2813 C CD1 . ILE A 338 ? 0.5768 1.2935 0.5319 -0.0576 0.0025  -0.0631 338 ILE A CD1 
2814 N N   . HIS A 339 ? 0.5160 1.0811 0.4561 -0.0378 0.0003  -0.0431 339 HIS A N   
2815 C CA  . HIS A 339 ? 0.5353 1.0823 0.4743 -0.0224 0.0000  -0.0324 339 HIS A CA  
2816 C C   . HIS A 339 ? 0.5396 1.0877 0.4766 -0.0256 -0.0016 -0.0355 339 HIS A C   
2817 O O   . HIS A 339 ? 0.5523 1.0953 0.4876 -0.0412 -0.0019 -0.0459 339 HIS A O   
2818 C CB  . HIS A 339 ? 0.5457 1.0471 0.4824 -0.0203 0.0013  -0.0282 339 HIS A CB  
2819 C CG  . HIS A 339 ? 0.5306 1.0164 0.4667 -0.0027 0.0023  -0.0162 339 HIS A CG  
2820 N ND1 . HIS A 339 ? 0.5251 0.9955 0.4590 0.0008  0.0015  -0.0137 339 HIS A ND1 
2821 C CD2 . HIS A 339 ? 0.5103 0.9939 0.4476 0.0120  0.0048  -0.0062 339 HIS A CD2 
2822 C CE1 . HIS A 339 ? 0.5295 0.9881 0.4630 0.0167  0.0035  -0.0029 339 HIS A CE1 
2823 N NE2 . HIS A 339 ? 0.5317 0.9979 0.4672 0.0235  0.0058  0.0016  339 HIS A NE2 
2824 N N   . ARG A 340 ? 0.5615 1.1156 0.4983 -0.0107 -0.0021 -0.0265 340 ARG A N   
2825 C CA  . ARG A 340 ? 0.5739 1.1341 0.5089 -0.0123 -0.0036 -0.0288 340 ARG A CA  
2826 C C   . ARG A 340 ? 0.5646 1.1028 0.4976 0.0020  -0.0031 -0.0184 340 ARG A C   
2827 O O   . ARG A 340 ? 0.5405 1.0707 0.4740 0.0163  -0.0013 -0.0080 340 ARG A O   
2828 C CB  . ARG A 340 ? 0.5972 1.2079 0.5341 -0.0119 -0.0051 -0.0313 340 ARG A CB  
2829 C CG  . ARG A 340 ? 0.6248 1.2632 0.5642 0.0063  -0.0047 -0.0200 340 ARG A CG  
2830 C CD  . ARG A 340 ? 0.7015 1.3925 0.6429 0.0065  -0.0065 -0.0227 340 ARG A CD  
2831 N NE  . ARG A 340 ? 0.7024 1.4109 0.6433 0.0259  -0.0066 -0.0104 340 ARG A NE  
2832 C CZ  . ARG A 340 ? 0.7140 1.4143 0.6515 0.0306  -0.0071 -0.0071 340 ARG A CZ  
2833 N NH1 . ARG A 340 ? 0.7398 1.4161 0.6748 0.0172  -0.0079 -0.0155 340 ARG A NH1 
2834 N NH2 . ARG A 340 ? 0.7231 1.4389 0.6596 0.0490  -0.0065 0.0048  340 ARG A NH2 
2835 N N   . THR A 341 ? 0.5853 1.1124 0.5159 -0.0025 -0.0041 -0.0217 341 THR A N   
2836 C CA  . THR A 341 ? 0.6311 1.1486 0.5598 0.0104  -0.0037 -0.0130 341 THR A CA  
2837 C C   . THR A 341 ? 0.7040 1.2511 0.6318 0.0075  -0.0055 -0.0170 341 THR A C   
2838 O O   . THR A 341 ? 0.7433 1.3192 0.6723 -0.0032 -0.0068 -0.0259 341 THR A O   
2839 C CB  . THR A 341 ? 0.6189 1.0912 0.5454 0.0078  -0.0030 -0.0130 341 THR A CB  
2840 O OG1 . THR A 341 ? 0.6367 1.1018 0.5621 -0.0080 -0.0043 -0.0242 341 THR A OG1 
2841 C CG2 . THR A 341 ? 0.5975 1.0405 0.5244 0.0085  -0.0014 -0.0105 341 THR A CG2 
2842 N N   . VAL A 342 ? 0.7647 1.3052 0.6902 0.0163  -0.0053 -0.0112 342 VAL A N   
2843 C CA  . VAL A 342 ? 0.8147 1.3816 0.7387 0.0134  -0.0069 -0.0151 342 VAL A CA  
2844 C C   . VAL A 342 ? 0.8470 1.4066 0.7704 -0.0062 -0.0079 -0.0293 342 VAL A C   
2845 O O   . VAL A 342 ? 0.8457 1.4353 0.7687 -0.0145 -0.0090 -0.0369 342 VAL A O   
2846 C CB  . VAL A 342 ? 0.8288 1.3873 0.7499 0.0268  -0.0060 -0.0057 342 VAL A CB  
2847 C CG1 . VAL A 342 ? 0.8179 1.4059 0.7389 0.0447  -0.0051 0.0060  342 VAL A CG1 
2848 C CG2 . VAL A 342 ? 0.7943 1.3057 0.7143 0.0307  -0.0039 -0.0011 342 VAL A CG2 
2849 N N   . ASP A 343 ? 0.8448 1.3648 0.7677 -0.0137 -0.0069 -0.0328 343 ASP A N   
2850 C CA  . ASP A 343 ? 0.8318 1.3387 0.7536 -0.0312 -0.0068 -0.0452 343 ASP A CA  
2851 C C   . ASP A 343 ? 0.8182 1.3262 0.7412 -0.0453 -0.0060 -0.0543 343 ASP A C   
2852 O O   . ASP A 343 ? 0.8187 1.3256 0.7406 -0.0610 -0.0051 -0.0658 343 ASP A O   
2853 C CB  . ASP A 343 ? 0.8366 1.2997 0.7569 -0.0311 -0.0059 -0.0439 343 ASP A CB  
2854 C CG  . ASP A 343 ? 0.8541 1.3083 0.7733 -0.0150 -0.0058 -0.0326 343 ASP A CG  
2855 O OD1 . ASP A 343 ? 0.8749 1.3570 0.7935 -0.0064 -0.0063 -0.0279 343 ASP A OD1 
2856 O OD2 . ASP A 343 ? 0.8106 1.2299 0.7295 -0.0111 -0.0049 -0.0284 343 ASP A OD2 
2857 N N   . ASP A 344 ? 0.7792 1.2892 0.7042 -0.0399 -0.0058 -0.0493 344 ASP A N   
2858 C CA  . ASP A 344 ? 0.7021 1.1991 0.6276 -0.0516 -0.0046 -0.0558 344 ASP A CA  
2859 C C   . ASP A 344 ? 0.6684 1.1973 0.5964 -0.0523 -0.0046 -0.0568 344 ASP A C   
2860 O O   . ASP A 344 ? 0.6897 1.2367 0.6197 -0.0383 -0.0053 -0.0476 344 ASP A O   
2861 C CB  . ASP A 344 ? 0.6828 1.1396 0.6078 -0.0460 -0.0039 -0.0493 344 ASP A CB  
2862 C CG  . ASP A 344 ? 0.7073 1.1287 0.6300 -0.0504 -0.0035 -0.0515 344 ASP A CG  
2863 O OD1 . ASP A 344 ? 0.7041 1.1213 0.6253 -0.0643 -0.0026 -0.0615 344 ASP A OD1 
2864 O OD2 . ASP A 344 ? 0.7500 1.1473 0.6724 -0.0399 -0.0036 -0.0433 344 ASP A OD2 
2865 N N   . TYR A 345 ? 0.6433 1.1778 0.5712 -0.0687 -0.0033 -0.0679 345 TYR A N   
2866 C CA  . TYR A 345 ? 0.6284 1.1845 0.5588 -0.0715 -0.0027 -0.0698 345 TYR A CA  
2867 C C   . TYR A 345 ? 0.5717 1.0969 0.5006 -0.0828 -0.0004 -0.0748 345 TYR A C   
2868 O O   . TYR A 345 ? 0.5669 1.0698 0.4928 -0.0956 0.0012  -0.0827 345 TYR A O   
2869 C CB  . TYR A 345 ? 0.7060 1.3065 0.6376 -0.0817 -0.0028 -0.0794 345 TYR A CB  
2870 C CG  . TYR A 345 ? 0.7493 1.3934 0.6840 -0.0682 -0.0050 -0.0725 345 TYR A CG  
2871 C CD1 . TYR A 345 ? 0.7701 1.4434 0.7083 -0.0654 -0.0050 -0.0712 345 TYR A CD1 
2872 C CD2 . TYR A 345 ? 0.7793 1.4363 0.7131 -0.0582 -0.0068 -0.0672 345 TYR A CD2 
2873 C CE1 . TYR A 345 ? 0.7909 1.5053 0.7320 -0.0521 -0.0069 -0.0643 345 TYR A CE1 
2874 C CE2 . TYR A 345 ? 0.7892 1.4866 0.7253 -0.0450 -0.0086 -0.0600 345 TYR A CE2 
2875 C CZ  . TYR A 345 ? 0.8000 1.5261 0.7398 -0.0416 -0.0086 -0.0584 345 TYR A CZ  
2876 O OH  . TYR A 345 ? 0.8398 1.6069 0.7818 -0.0274 -0.0102 -0.0506 345 TYR A OH  
2877 N N   . PHE A 346 ? 0.5317 1.0557 0.4623 -0.0777 -0.0001 -0.0699 346 PHE A N   
2878 C CA  . PHE A 346 ? 0.5100 1.0059 0.4388 -0.0870 0.0020  -0.0734 346 PHE A CA  
2879 C C   . PHE A 346 ? 0.5021 1.0230 0.4335 -0.0900 0.0030  -0.0755 346 PHE A C   
2880 O O   . PHE A 346 ? 0.5165 1.0526 0.4509 -0.0769 0.0020  -0.0672 346 PHE A O   
2881 C CB  . PHE A 346 ? 0.5028 0.9599 0.4304 -0.0765 0.0016  -0.0637 346 PHE A CB  
2882 C CG  . PHE A 346 ? 0.4901 0.9163 0.4151 -0.0854 0.0035  -0.0665 346 PHE A CG  
2883 C CD1 . PHE A 346 ? 0.4896 0.9078 0.4118 -0.1027 0.0059  -0.0773 346 PHE A CD1 
2884 C CD2 . PHE A 346 ? 0.4736 0.8775 0.3985 -0.0763 0.0034  -0.0583 346 PHE A CD2 
2885 C CE1 . PHE A 346 ? 0.5084 0.8976 0.4274 -0.1099 0.0079  -0.0789 346 PHE A CE1 
2886 C CE2 . PHE A 346 ? 0.4918 0.8680 0.4138 -0.0840 0.0050  -0.0603 346 PHE A CE2 
2887 C CZ  . PHE A 346 ? 0.5019 0.8708 0.4209 -0.1004 0.0071  -0.0702 346 PHE A CZ  
2888 N N   . PHE A 347 ? 0.5018 1.0260 0.4317 -0.1074 0.0055  -0.0868 347 PHE A N   
2889 C CA  . PHE A 347 ? 0.4992 1.0533 0.4318 -0.1131 0.0068  -0.0912 347 PHE A CA  
2890 C C   . PHE A 347 ? 0.5026 1.0320 0.4321 -0.1269 0.0103  -0.0975 347 PHE A C   
2891 O O   . PHE A 347 ? 0.5253 1.0321 0.4506 -0.1400 0.0128  -0.1050 347 PHE A O   
2892 C CB  . PHE A 347 ? 0.5092 1.1067 0.4436 -0.1222 0.0069  -0.1008 347 PHE A CB  
2893 C CG  . PHE A 347 ? 0.5131 1.1450 0.4505 -0.1297 0.0084  -0.1069 347 PHE A CG  
2894 C CD1 . PHE A 347 ? 0.5311 1.1567 0.4660 -0.1491 0.0126  -0.1187 347 PHE A CD1 
2895 C CD2 . PHE A 347 ? 0.5086 1.1790 0.4511 -0.1172 0.0061  -0.1008 347 PHE A CD2 
2896 C CE1 . PHE A 347 ? 0.5342 1.1919 0.4720 -0.1567 0.0143  -0.1249 347 PHE A CE1 
2897 C CE2 . PHE A 347 ? 0.5356 1.2397 0.4814 -0.1240 0.0075  -0.1066 347 PHE A CE2 
2898 C CZ  . PHE A 347 ? 0.5380 1.2361 0.4816 -0.1442 0.0115  -0.1190 347 PHE A CZ  
2899 N N   . CYS A 348 ? 0.5007 1.0341 0.4320 -0.1235 0.0109  -0.0941 348 CYS A N   
2900 C CA  . CYS A 348 ? 0.5207 1.0332 0.4488 -0.1360 0.0144  -0.0993 348 CYS A CA  
2901 C C   . CYS A 348 ? 0.5347 1.0794 0.4661 -0.1401 0.0158  -0.1030 348 CYS A C   
2902 O O   . CYS A 348 ? 0.5250 1.0994 0.4616 -0.1278 0.0137  -0.0970 348 CYS A O   
2903 C CB  . CYS A 348 ? 0.5169 0.9884 0.4424 -0.1278 0.0139  -0.0904 348 CYS A CB  
2904 S SG  . CYS A 348 ? 0.5278 0.9614 0.4500 -0.1218 0.0121  -0.0853 348 CYS A SG  
2905 N N   . SER A 349 ? 0.5368 1.0749 0.4652 -0.1572 0.0200  -0.1126 349 SER A N   
2906 C CA  . SER A 349 ? 0.5520 1.1154 0.4829 -0.1635 0.0222  -0.1171 349 SER A CA  
2907 C C   . SER A 349 ? 0.5764 1.1118 0.5014 -0.1804 0.0273  -0.1247 349 SER A C   
2908 O O   . SER A 349 ? 0.5794 1.0893 0.4991 -0.1908 0.0298  -0.1301 349 SER A O   
2909 C CB  . SER A 349 ? 0.5584 1.1717 0.4934 -0.1703 0.0224  -0.1258 349 SER A CB  
2910 O OG  . SER A 349 ? 0.5520 1.1874 0.4885 -0.1815 0.0257  -0.1334 349 SER A OG  
2911 N N   . PRO A 350 ? 0.5957 1.1353 0.5213 -0.1829 0.0294  -0.1248 350 PRO A N   
2912 C CA  . PRO A 350 ? 0.6306 1.1490 0.5504 -0.2002 0.0350  -0.1329 350 PRO A CA  
2913 C C   . PRO A 350 ? 0.6631 1.2051 0.5821 -0.2196 0.0396  -0.1476 350 PRO A C   
2914 O O   . PRO A 350 ? 0.6822 1.2045 0.5953 -0.2359 0.0454  -0.1556 350 PRO A O   
2915 C CB  . PRO A 350 ? 0.6186 1.1446 0.5406 -0.1963 0.0356  -0.1291 350 PRO A CB  
2916 C CG  . PRO A 350 ? 0.5913 1.1578 0.5216 -0.1818 0.0314  -0.1237 350 PRO A CG  
2917 C CD  . PRO A 350 ? 0.5859 1.1484 0.5173 -0.1693 0.0271  -0.1172 350 PRO A CD  
2918 N N   . HIS A 351 ? 0.6807 1.2646 0.6053 -0.2179 0.0373  -0.1511 351 HIS A N   
2919 C CA  . HIS A 351 ? 0.6943 1.3069 0.6188 -0.2363 0.0414  -0.1658 351 HIS A CA  
2920 C C   . HIS A 351 ? 0.7115 1.3145 0.6330 -0.2416 0.0418  -0.1706 351 HIS A C   
2921 O O   . HIS A 351 ? 0.7146 1.3378 0.6398 -0.2311 0.0371  -0.1668 351 HIS A O   
2922 C CB  . HIS A 351 ? 0.6787 1.3486 0.6112 -0.2327 0.0389  -0.1679 351 HIS A CB  
2923 C CG  . HIS A 351 ? 0.6808 1.3620 0.6171 -0.2258 0.0385  -0.1626 351 HIS A CG  
2924 N ND1 . HIS A 351 ? 0.6970 1.3659 0.6302 -0.2387 0.0437  -0.1683 351 HIS A ND1 
2925 C CD2 . HIS A 351 ? 0.6714 1.3741 0.6143 -0.2065 0.0337  -0.1515 351 HIS A CD2 
2926 C CE1 . HIS A 351 ? 0.6861 1.3687 0.6238 -0.2284 0.0421  -0.1615 351 HIS A CE1 
2927 N NE2 . HIS A 351 ? 0.6862 1.3893 0.6299 -0.2085 0.0362  -0.1513 351 HIS A NE2 
2928 N N   . PRO A 352 ? 0.7307 1.3015 0.6448 -0.2577 0.0481  -0.1788 352 PRO A N   
2929 C CA  . PRO A 352 ? 0.7265 1.2791 0.6367 -0.2624 0.0495  -0.1827 352 PRO A CA  
2930 C C   . PRO A 352 ? 0.7428 1.3387 0.6568 -0.2677 0.0487  -0.1914 352 PRO A C   
2931 O O   . PRO A 352 ? 0.7230 1.3167 0.6372 -0.2615 0.0458  -0.1891 352 PRO A O   
2932 C CB  . PRO A 352 ? 0.7524 1.2712 0.6544 -0.2815 0.0584  -0.1921 352 PRO A CB  
2933 C CG  . PRO A 352 ? 0.7558 1.2636 0.6565 -0.2821 0.0602  -0.1888 352 PRO A CG  
2934 C CD  . PRO A 352 ? 0.7427 1.2952 0.6516 -0.2731 0.0552  -0.1856 352 PRO A CD  
2935 N N   . HIS A 353 ? 0.7536 1.3902 0.6706 -0.2790 0.0511  -0.2013 353 HIS A N   
2936 C CA  . HIS A 353 ? 0.7744 1.4565 0.6948 -0.2858 0.0506  -0.2108 353 HIS A CA  
2937 C C   . HIS A 353 ? 0.7613 1.4717 0.6880 -0.2654 0.0421  -0.2002 353 HIS A C   
2938 O O   . HIS A 353 ? 0.7742 1.5043 0.7016 -0.2665 0.0406  -0.2042 353 HIS A O   
2939 C CB  . HIS A 353 ? 0.7813 1.5034 0.7040 -0.3023 0.0551  -0.2238 353 HIS A CB  
2940 C CG  . HIS A 353 ? 0.7862 1.5479 0.7168 -0.2899 0.0499  -0.2171 353 HIS A CG  
2941 N ND1 . HIS A 353 ? 0.8095 1.5607 0.7407 -0.2877 0.0510  -0.2128 353 HIS A ND1 
2942 C CD2 . HIS A 353 ? 0.7513 1.5649 0.6896 -0.2785 0.0438  -0.2138 353 HIS A CD2 
2943 C CE1 . HIS A 353 ? 0.7947 1.5879 0.7336 -0.2755 0.0461  -0.2072 353 HIS A CE1 
2944 N NE2 . HIS A 353 ? 0.7643 1.5956 0.7076 -0.2695 0.0418  -0.2075 353 HIS A NE2 
2945 N N   . LYS A 354 ? 0.7384 1.4492 0.6692 -0.2467 0.0369  -0.1865 354 LYS A N   
2946 C CA  . LYS A 354 ? 0.7385 1.4703 0.6744 -0.2253 0.0295  -0.1745 354 LYS A CA  
2947 C C   . LYS A 354 ? 0.7374 1.4365 0.6700 -0.2167 0.0272  -0.1680 354 LYS A C   
2948 O O   . LYS A 354 ? 0.7142 1.4338 0.6495 -0.2049 0.0226  -0.1627 354 LYS A O   
2949 C CB  . LYS A 354 ? 0.7349 1.4686 0.6751 -0.2075 0.0260  -0.1614 354 LYS A CB  
2950 C CG  . LYS A 354 ? 0.7251 1.5016 0.6706 -0.2109 0.0268  -0.1656 354 LYS A CG  
2951 C CD  . LYS A 354 ? 0.7307 1.5127 0.6811 -0.1897 0.0229  -0.1512 354 LYS A CD  
2952 C CE  . LYS A 354 ? 0.7686 1.5611 0.7211 -0.1957 0.0259  -0.1543 354 LYS A CE  
2953 N NZ  . LYS A 354 ? 0.8008 1.6487 0.7583 -0.2056 0.0270  -0.1648 354 LYS A NZ  
2954 N N   . VAL A 355 ? 0.7412 1.3903 0.6679 -0.2224 0.0305  -0.1682 355 VAL A N   
2955 C CA  . VAL A 355 ? 0.7506 1.3671 0.6741 -0.2156 0.0288  -0.1630 355 VAL A CA  
2956 C C   . VAL A 355 ? 0.7564 1.3838 0.6777 -0.2285 0.0314  -0.1745 355 VAL A C   
2957 O O   . VAL A 355 ? 0.7588 1.3780 0.6795 -0.2209 0.0287  -0.1705 355 VAL A O   
2958 C CB  . VAL A 355 ? 0.7271 1.2879 0.6453 -0.2155 0.0311  -0.1583 355 VAL A CB  
2959 C CG1 . VAL A 355 ? 0.7070 1.2377 0.6230 -0.2063 0.0287  -0.1518 355 VAL A CG1 
2960 C CG2 . VAL A 355 ? 0.7081 1.2607 0.6284 -0.2037 0.0288  -0.1478 355 VAL A CG2 
2961 N N   . TYR A 356 ? 0.8027 1.4494 0.7226 -0.2485 0.0370  -0.1893 356 TYR A N   
2962 C CA  . TYR A 356 ? 0.8216 1.4895 0.7401 -0.2617 0.0397  -0.2017 356 TYR A CA  
2963 C C   . TYR A 356 ? 0.7887 1.5114 0.7132 -0.2533 0.0341  -0.2003 356 TYR A C   
2964 O O   . TYR A 356 ? 0.7760 1.5080 0.7006 -0.2485 0.0314  -0.1994 356 TYR A O   
2965 C CB  . TYR A 356 ? 0.8916 1.5631 0.8063 -0.2870 0.0485  -0.2189 356 TYR A CB  
2966 C CG  . TYR A 356 ? 0.9650 1.5824 0.8726 -0.2966 0.0553  -0.2211 356 TYR A CG  
2967 C CD1 . TYR A 356 ? 1.0117 1.5943 0.9138 -0.3022 0.0593  -0.2246 356 TYR A CD1 
2968 C CD2 . TYR A 356 ? 1.0054 1.6066 0.9116 -0.2995 0.0581  -0.2194 356 TYR A CD2 
2969 C CE1 . TYR A 356 ? 1.0582 1.5913 0.9535 -0.3097 0.0658  -0.2256 356 TYR A CE1 
2970 C CE2 . TYR A 356 ? 1.0594 1.6114 0.9585 -0.3074 0.0644  -0.2206 356 TYR A CE2 
2971 C CZ  . TYR A 356 ? 1.0790 1.5971 0.9726 -0.3121 0.0683  -0.2234 356 TYR A CZ  
2972 O OH  . TYR A 356 ? 1.0911 1.5608 0.9774 -0.3188 0.0749  -0.2236 356 TYR A OH  
2973 N N   . ASP A 357 ? 0.7779 1.5379 0.7074 -0.2512 0.0324  -0.1999 357 ASP A N   
2974 C CA  . ASP A 357 ? 0.7623 1.5774 0.6978 -0.2413 0.0270  -0.1971 357 ASP A CA  
2975 C C   . ASP A 357 ? 0.7262 1.5341 0.6631 -0.2185 0.0204  -0.1819 357 ASP A C   
2976 O O   . ASP A 357 ? 0.7240 1.5680 0.6633 -0.2119 0.0167  -0.1806 357 ASP A O   
2977 C CB  . ASP A 357 ? 0.7651 1.6137 0.7063 -0.2373 0.0256  -0.1949 357 ASP A CB  
2978 C CG  . ASP A 357 ? 0.7839 1.6443 0.7240 -0.2606 0.0324  -0.2107 357 ASP A CG  
2979 O OD1 . ASP A 357 ? 0.7913 1.6409 0.7264 -0.2804 0.0383  -0.2244 357 ASP A OD1 
2980 O OD2 . ASP A 357 ? 0.7656 1.6450 0.7095 -0.2593 0.0324  -0.2096 357 ASP A OD2 
2981 N N   . PHE A 358 ? 0.6851 1.4463 0.6201 -0.2071 0.0194  -0.1706 358 PHE A N   
2982 C CA  . PHE A 358 ? 0.6438 1.3922 0.5792 -0.1870 0.0143  -0.1569 358 PHE A CA  
2983 C C   . PHE A 358 ? 0.6428 1.3699 0.5740 -0.1920 0.0153  -0.1609 358 PHE A C   
2984 O O   . PHE A 358 ? 0.6434 1.3878 0.5755 -0.1820 0.0116  -0.1562 358 PHE A O   
2985 C CB  . PHE A 358 ? 0.6211 1.3311 0.5565 -0.1722 0.0128  -0.1433 358 PHE A CB  
2986 C CG  . PHE A 358 ? 0.5804 1.2823 0.5169 -0.1511 0.0080  -0.1292 358 PHE A CG  
2987 C CD1 . PHE A 358 ? 0.5573 1.2236 0.4900 -0.1493 0.0079  -0.1269 358 PHE A CD1 
2988 C CD2 . PHE A 358 ? 0.5565 1.2881 0.4977 -0.1332 0.0043  -0.1184 358 PHE A CD2 
2989 C CE1 . PHE A 358 ? 0.5576 1.2174 0.4910 -0.1309 0.0041  -0.1146 358 PHE A CE1 
2990 C CE2 . PHE A 358 ? 0.5374 1.2607 0.4788 -0.1142 0.0010  -0.1056 358 PHE A CE2 
2991 C CZ  . PHE A 358 ? 0.5488 1.2363 0.4863 -0.1135 0.0009  -0.1039 358 PHE A CZ  
2992 N N   . GLU A 359 ? 0.6714 1.3603 0.5975 -0.2067 0.0205  -0.1689 359 GLU A N   
2993 C CA  . GLU A 359 ? 0.7287 1.3965 0.6506 -0.2126 0.0223  -0.1736 359 GLU A CA  
2994 C C   . GLU A 359 ? 0.7460 1.4569 0.6686 -0.2213 0.0225  -0.1838 359 GLU A C   
2995 O O   . GLU A 359 ? 0.7627 1.4786 0.6850 -0.2133 0.0195  -0.1801 359 GLU A O   
2996 C CB  . GLU A 359 ? 0.7582 1.3818 0.6744 -0.2284 0.0292  -0.1818 359 GLU A CB  
2997 C CG  . GLU A 359 ? 0.7889 1.3863 0.7011 -0.2321 0.0312  -0.1851 359 GLU A CG  
2998 C CD  . GLU A 359 ? 0.8366 1.3879 0.7429 -0.2454 0.0384  -0.1916 359 GLU A CD  
2999 O OE1 . GLU A 359 ? 0.8634 1.4099 0.7678 -0.2575 0.0433  -0.1980 359 GLU A OE1 
3000 O OE2 . GLU A 359 ? 0.8628 1.3826 0.7662 -0.2435 0.0394  -0.1901 359 GLU A OE2 
3001 N N   . LEU A 360 ? 0.7668 1.5092 0.6898 -0.2379 0.0262  -0.1969 360 LEU A N   
3002 C CA  . LEU A 360 ? 0.7944 1.5814 0.7180 -0.2483 0.0268  -0.2082 360 LEU A CA  
3003 C C   . LEU A 360 ? 0.7539 1.5838 0.6822 -0.2299 0.0192  -0.1981 360 LEU A C   
3004 O O   . LEU A 360 ? 0.7529 1.5974 0.6801 -0.2282 0.0175  -0.1993 360 LEU A O   
3005 C CB  . LEU A 360 ? 0.8480 1.6637 0.7718 -0.2693 0.0322  -0.2239 360 LEU A CB  
3006 C CG  . LEU A 360 ? 0.8863 1.6718 0.8039 -0.2934 0.0418  -0.2394 360 LEU A CG  
3007 C CD1 . LEU A 360 ? 0.8988 1.6298 0.8133 -0.2925 0.0451  -0.2340 360 LEU A CD1 
3008 C CD2 . LEU A 360 ? 0.9068 1.7329 0.8252 -0.3139 0.0468  -0.2558 360 LEU A CD2 
3009 N N   . LEU A 361 ? 0.7360 1.5837 0.6690 -0.2156 0.0152  -0.1876 361 LEU A N   
3010 C CA  . LEU A 361 ? 0.7067 1.5930 0.6440 -0.1959 0.0086  -0.1761 361 LEU A CA  
3011 C C   . LEU A 361 ? 0.7179 1.5815 0.6533 -0.1793 0.0051  -0.1641 361 LEU A C   
3012 O O   . LEU A 361 ? 0.7196 1.6144 0.6554 -0.1726 0.0019  -0.1621 361 LEU A O   
3013 C CB  . LEU A 361 ? 0.7001 1.5983 0.6423 -0.1820 0.0060  -0.1655 361 LEU A CB  
3014 C CG  . LEU A 361 ? 0.6956 1.6159 0.6416 -0.1562 0.0001  -0.1486 361 LEU A CG  
3015 C CD1 . LEU A 361 ? 0.7021 1.6819 0.6504 -0.1541 -0.0027 -0.1511 361 LEU A CD1 
3016 C CD2 . LEU A 361 ? 0.6847 1.6066 0.6350 -0.1450 -0.0005 -0.1396 361 LEU A CD2 
3017 N N   . ILE A 362 ? 0.7006 1.5111 0.6338 -0.1727 0.0057  -0.1563 362 ILE A N   
3018 C CA  . ILE A 362 ? 0.6837 1.4702 0.6156 -0.1561 0.0026  -0.1441 362 ILE A CA  
3019 C C   . ILE A 362 ? 0.6885 1.4705 0.6165 -0.1653 0.0040  -0.1521 362 ILE A C   
3020 O O   . ILE A 362 ? 0.6920 1.4763 0.6193 -0.1528 0.0009  -0.1444 362 ILE A O   
3021 C CB  . ILE A 362 ? 0.7068 1.4388 0.6374 -0.1479 0.0031  -0.1346 362 ILE A CB  
3022 C CG1 . ILE A 362 ? 0.6883 1.4122 0.6203 -0.1240 -0.0010 -0.1175 362 ILE A CG1 
3023 C CG2 . ILE A 362 ? 0.7001 1.3871 0.6261 -0.1610 0.0071  -0.1421 362 ILE A CG2 
3024 C CD1 . ILE A 362 ? 0.6924 1.3860 0.6212 -0.1192 -0.0016 -0.1138 362 ILE A CD1 
3025 N N   . LYS A 363 ? 0.7166 1.4915 0.6417 -0.1871 0.0092  -0.1678 363 LYS A N   
3026 C CA  . LYS A 363 ? 0.7763 1.5499 0.6976 -0.1983 0.0116  -0.1776 363 LYS A CA  
3027 C C   . LYS A 363 ? 0.7855 1.6160 0.7082 -0.1994 0.0092  -0.1822 363 LYS A C   
3028 O O   . LYS A 363 ? 0.8344 1.6699 0.7547 -0.1995 0.0087  -0.1842 363 LYS A O   
3029 C CB  . LYS A 363 ? 0.8141 1.5642 0.7316 -0.2217 0.0192  -0.1935 363 LYS A CB  
3030 C CG  . LYS A 363 ? 0.8610 1.5512 0.7749 -0.2218 0.0222  -0.1908 363 LYS A CG  
3031 C CD  . LYS A 363 ? 0.8958 1.5609 0.8060 -0.2423 0.0302  -0.2037 363 LYS A CD  
3032 C CE  . LYS A 363 ? 0.9113 1.5186 0.8178 -0.2415 0.0332  -0.2006 363 LYS A CE  
3033 N NZ  . LYS A 363 ? 0.9358 1.5138 0.8392 -0.2545 0.0397  -0.2067 363 LYS A NZ  
3034 N N   . GLY A 364 ? 0.7908 1.6652 0.7172 -0.2002 0.0077  -0.1840 364 GLY A N   
3035 C CA  . GLY A 364 ? 0.7717 1.7060 0.6999 -0.1996 0.0047  -0.1872 364 GLY A CA  
3036 C C   . GLY A 364 ? 0.7679 1.7175 0.6977 -0.1749 -0.0015 -0.1703 364 GLY A C   
3037 O O   . GLY A 364 ? 0.7937 1.7766 0.7224 -0.1729 -0.0037 -0.1715 364 GLY A O   
3038 N N   . VAL A 365 ? 0.7293 1.6538 0.6609 -0.1564 -0.0039 -0.1548 365 VAL A N   
3039 C CA  . VAL A 365 ? 0.7176 1.6512 0.6503 -0.1319 -0.0088 -0.1376 365 VAL A CA  
3040 C C   . VAL A 365 ? 0.7469 1.6464 0.6753 -0.1263 -0.0090 -0.1330 365 VAL A C   
3041 O O   . VAL A 365 ? 0.7945 1.7169 0.7216 -0.1171 -0.0116 -0.1280 365 VAL A O   
3042 C CB  . VAL A 365 ? 0.6794 1.5971 0.6153 -0.1144 -0.0103 -0.1231 365 VAL A CB  
3043 C CG1 . VAL A 365 ? 0.6517 1.5758 0.5879 -0.0892 -0.0139 -0.1053 365 VAL A CG1 
3044 C CG2 . VAL A 365 ? 0.6583 1.6120 0.5988 -0.1188 -0.0101 -0.1272 365 VAL A CG2 
3045 N N   . TYR A 366 ? 0.7685 1.6145 0.6948 -0.1320 -0.0060 -0.1346 366 TYR A N   
3046 C CA  . TYR A 366 ? 0.7577 1.5662 0.6809 -0.1244 -0.0063 -0.1283 366 TYR A CA  
3047 C C   . TYR A 366 ? 0.7653 1.5479 0.6847 -0.1433 -0.0020 -0.1421 366 TYR A C   
3048 O O   . TYR A 366 ? 0.7461 1.5275 0.6650 -0.1622 0.0019  -0.1555 366 TYR A O   
3049 C CB  . TYR A 366 ? 0.7363 1.5004 0.6604 -0.1106 -0.0067 -0.1154 366 TYR A CB  
3050 C CG  . TYR A 366 ? 0.7265 1.5068 0.6537 -0.0898 -0.0098 -0.1001 366 TYR A CG  
3051 C CD1 . TYR A 366 ? 0.7031 1.5009 0.6298 -0.0720 -0.0126 -0.0884 366 TYR A CD1 
3052 C CD2 . TYR A 366 ? 0.7056 1.4804 0.6358 -0.0876 -0.0093 -0.0970 366 TYR A CD2 
3053 C CE1 . TYR A 366 ? 0.6942 1.5042 0.6233 -0.0524 -0.0143 -0.0741 366 TYR A CE1 
3054 C CE2 . TYR A 366 ? 0.6827 1.4700 0.6156 -0.0684 -0.0113 -0.0832 366 TYR A CE2 
3055 C CZ  . TYR A 366 ? 0.6778 1.4822 0.6101 -0.0507 -0.0136 -0.0717 366 TYR A CZ  
3056 O OH  . TYR A 366 ? 0.6895 1.5046 0.6240 -0.0311 -0.0145 -0.0577 366 TYR A OH  
3057 N N   . GLN A 367 ? 0.7955 1.5569 0.7122 -0.1381 -0.0023 -0.1386 367 GLN A N   
3058 C CA  . GLN A 367 ? 0.8490 1.5714 0.7624 -0.1515 0.0019  -0.1478 367 GLN A CA  
3059 C C   . GLN A 367 ? 0.8790 1.5499 0.7929 -0.1447 0.0025  -0.1397 367 GLN A C   
3060 O O   . GLN A 367 ? 0.8900 1.5476 0.8050 -0.1265 -0.0006 -0.1255 367 GLN A O   
3061 C CB  . GLN A 367 ? 0.8585 1.5815 0.7691 -0.1487 0.0013  -0.1477 367 GLN A CB  
3062 C CG  . GLN A 367 ? 0.8973 1.6112 0.8045 -0.1691 0.0066  -0.1640 367 GLN A CG  
3063 C CD  . GLN A 367 ? 0.9124 1.6759 0.8188 -0.1838 0.0078  -0.1775 367 GLN A CD  
3064 O OE1 . GLN A 367 ? 0.9054 1.6901 0.8135 -0.1929 0.0090  -0.1839 367 GLN A OE1 
3065 N NE2 . GLN A 367 ? 0.8801 1.6630 0.7839 -0.1866 0.0078  -0.1821 367 GLN A NE2 
3066 N N   . VAL A 368 ? 0.8919 1.5348 0.8046 -0.1594 0.0070  -0.1488 368 VAL A N   
3067 C CA  . VAL A 368 ? 0.8749 1.4723 0.7879 -0.1544 0.0077  -0.1420 368 VAL A CA  
3068 C C   . VAL A 368 ? 0.9062 1.4607 0.8159 -0.1654 0.0125  -0.1491 368 VAL A C   
3069 O O   . VAL A 368 ? 0.9463 1.5046 0.8535 -0.1826 0.0172  -0.1628 368 VAL A O   
3070 C CB  . VAL A 368 ? 0.8227 1.4259 0.7377 -0.1579 0.0083  -0.1425 368 VAL A CB  
3071 C CG1 . VAL A 368 ? 0.7957 1.4406 0.7143 -0.1455 0.0039  -0.1346 368 VAL A CG1 
3072 C CG2 . VAL A 368 ? 0.8182 1.4279 0.7312 -0.1802 0.0139  -0.1588 368 VAL A CG2 
3073 N N   . ASN A 369 ? 0.9033 1.4177 0.8129 -0.1554 0.0115  -0.1399 369 ASN A N   
3074 C CA  . ASN A 369 ? 0.9468 1.4188 0.8537 -0.1635 0.0159  -0.1449 369 ASN A CA  
3075 C C   . ASN A 369 ? 0.9580 1.4118 0.8633 -0.1763 0.0204  -0.1516 369 ASN A C   
3076 O O   . ASN A 369 ? 0.9155 1.3472 0.8216 -0.1698 0.0193  -0.1440 369 ASN A O   
3077 C CB  . ASN A 369 ? 0.9407 1.3780 0.8483 -0.1484 0.0132  -0.1327 369 ASN A CB  
3078 C CG  . ASN A 369 ? 0.9653 1.4167 0.8739 -0.1355 0.0094  -0.1255 369 ASN A CG  
3079 O OD1 . ASN A 369 ? 0.9933 1.4709 0.9009 -0.1402 0.0098  -0.1315 369 ASN A OD1 
3080 N ND2 . ASN A 369 ? 0.9460 1.3800 0.8563 -0.1195 0.0062  -0.1127 369 ASN A ND2 
3081 N N   . PRO A 370 ? 0.9936 1.4558 0.8962 -0.1949 0.0262  -0.1661 370 PRO A N   
3082 C CA  . PRO A 370 ? 1.0025 1.4542 0.9032 -0.2082 0.0313  -0.1733 370 PRO A CA  
3083 C C   . PRO A 370 ? 1.0064 1.4070 0.9041 -0.2098 0.0351  -0.1715 370 PRO A C   
3084 O O   . PRO A 370 ? 1.0481 1.4355 0.9443 -0.2164 0.0383  -0.1733 370 PRO A O   
3085 C CB  . PRO A 370 ? 0.9888 1.4639 0.8870 -0.2277 0.0371  -0.1898 370 PRO A CB  
3086 C CG  . PRO A 370 ? 0.9871 1.4614 0.8843 -0.2264 0.0372  -0.1919 370 PRO A CG  
3087 C CD  . PRO A 370 ? 0.9707 1.4483 0.8712 -0.2052 0.0293  -0.1769 370 PRO A CD  
3088 N N   . THR A 371 ? 0.9753 1.3489 0.8724 -0.2035 0.0350  -0.1677 371 THR A N   
3089 C CA  . THR A 371 ? 0.9566 1.2834 0.8514 -0.2021 0.0377  -0.1640 371 THR A CA  
3090 C C   . THR A 371 ? 0.9528 1.2663 0.8503 -0.1857 0.0317  -0.1495 371 THR A C   
3091 O O   . THR A 371 ? 0.9644 1.2452 0.8602 -0.1845 0.0332  -0.1457 371 THR A O   
3092 C CB  . THR A 371 ? 0.9772 1.2802 0.8706 -0.2012 0.0400  -0.1655 371 THR A CB  
3093 O OG1 . THR A 371 ? 0.9477 1.2497 0.8445 -0.1840 0.0333  -0.1539 371 THR A OG1 
3094 C CG2 . THR A 371 ? 0.9585 1.2819 0.8499 -0.2148 0.0447  -0.1789 371 THR A CG2 
3095 N N   . LYS A 372 ? 0.9158 1.2548 0.8172 -0.1730 0.0253  -0.1415 372 LYS A N   
3096 C CA  . LYS A 372 ? 0.8775 1.2066 0.7814 -0.1573 0.0201  -0.1282 372 LYS A CA  
3097 C C   . LYS A 372 ? 0.8149 1.1609 0.7201 -0.1577 0.0190  -0.1264 372 LYS A C   
3098 O O   . LYS A 372 ? 0.7961 1.1383 0.7035 -0.1453 0.0152  -0.1160 372 LYS A O   
3099 C CB  . LYS A 372 ? 0.9349 1.2772 0.8418 -0.1422 0.0149  -0.1194 372 LYS A CB  
3100 C CG  . LYS A 372 ? 0.9781 1.2921 0.8846 -0.1367 0.0148  -0.1163 372 LYS A CG  
3101 C CD  . LYS A 372 ? 0.9829 1.2912 0.8920 -0.1189 0.0098  -0.1032 372 LYS A CD  
3102 C CE  . LYS A 372 ? 1.0211 1.2918 0.9299 -0.1144 0.0102  -0.0994 372 LYS A CE  
3103 N NZ  . LYS A 372 ? 0.9927 1.2523 0.9036 -0.0994 0.0063  -0.0872 372 LYS A NZ  
3104 N N   . THR A 373 ? 0.7442 1.1082 0.6478 -0.1723 0.0230  -0.1370 373 THR A N   
3105 C CA  . THR A 373 ? 0.7298 1.1085 0.6344 -0.1747 0.0228  -0.1368 373 THR A CA  
3106 C C   . THR A 373 ? 0.7227 1.0650 0.6246 -0.1772 0.0254  -0.1345 373 THR A C   
3107 O O   . THR A 373 ? 0.7603 1.0736 0.6581 -0.1860 0.0303  -0.1396 373 THR A O   
3108 C CB  . THR A 373 ? 0.7010 1.1123 0.6049 -0.1906 0.0266  -0.1498 373 THR A CB  
3109 O OG1 . THR A 373 ? 0.6858 1.1337 0.5921 -0.1875 0.0237  -0.1512 373 THR A OG1 
3110 C CG2 . THR A 373 ? 0.6704 1.0983 0.5758 -0.1926 0.0264  -0.1493 373 THR A CG2 
3111 N N   . ARG A 374 ? 0.6700 1.0137 0.5738 -0.1689 0.0224  -0.1265 374 ARG A N   
3112 C CA  . ARG A 374 ? 0.6656 0.9789 0.5666 -0.1709 0.0244  -0.1239 374 ARG A CA  
3113 C C   . ARG A 374 ? 0.6419 0.9750 0.5435 -0.1761 0.0254  -0.1261 374 ARG A C   
3114 O O   . ARG A 374 ? 0.6277 0.9880 0.5335 -0.1674 0.0214  -0.1211 374 ARG A O   
3115 C CB  . ARG A 374 ? 0.6768 0.9653 0.5789 -0.1551 0.0201  -0.1111 374 ARG A CB  
3116 C CG  . ARG A 374 ? 0.6955 0.9627 0.5973 -0.1495 0.0191  -0.1085 374 ARG A CG  
3117 C CD  . ARG A 374 ? 0.7296 0.9672 0.6267 -0.1607 0.0246  -0.1152 374 ARG A CD  
3118 N NE  . ARG A 374 ? 0.7486 0.9641 0.6457 -0.1542 0.0237  -0.1118 374 ARG A NE  
3119 C CZ  . ARG A 374 ? 0.7487 0.9706 0.6461 -0.1570 0.0249  -0.1170 374 ARG A CZ  
3120 N NH1 . ARG A 374 ? 0.7357 0.9861 0.6332 -0.1665 0.0271  -0.1262 374 ARG A NH1 
3121 N NH2 . ARG A 374 ? 0.7512 0.9520 0.6489 -0.1505 0.0241  -0.1134 374 ARG A NH2 
3122 N N   . THR A 375 ? 0.6376 0.9564 0.5349 -0.1901 0.0311  -0.1334 375 THR A N   
3123 C CA  . THR A 375 ? 0.6387 0.9754 0.5360 -0.1979 0.0331  -0.1374 375 THR A CA  
3124 C C   . THR A 375 ? 0.6545 0.9581 0.5461 -0.2074 0.0387  -0.1397 375 THR A C   
3125 O O   . THR A 375 ? 0.6553 0.9270 0.5424 -0.2113 0.0422  -0.1411 375 THR A O   
3126 C CB  . THR A 375 ? 0.6452 1.0198 0.5436 -0.2111 0.0361  -0.1497 375 THR A CB  
3127 O OG1 . THR A 375 ? 0.6490 1.0396 0.5474 -0.2196 0.0386  -0.1541 375 THR A OG1 
3128 C CG2 . THR A 375 ? 0.6602 1.0203 0.5539 -0.2261 0.0427  -0.1609 375 THR A CG2 
3129 N N   . ASN A 376 ? 0.6669 0.9780 0.5582 -0.2105 0.0396  -0.1395 376 ASN A N   
3130 C CA  . ASN A 376 ? 0.6977 0.9812 0.5828 -0.2210 0.0456  -0.1425 376 ASN A CA  
3131 C C   . ASN A 376 ? 0.7329 1.0341 0.6157 -0.2401 0.0527  -0.1559 376 ASN A C   
3132 O O   . ASN A 376 ? 0.7679 1.0513 0.6455 -0.2498 0.0583  -0.1589 376 ASN A O   
3133 C CB  . ASN A 376 ? 0.6761 0.9488 0.5615 -0.2118 0.0425  -0.1327 376 ASN A CB  
3134 C CG  . ASN A 376 ? 0.6546 0.9644 0.5453 -0.2088 0.0396  -0.1320 376 ASN A CG  
3135 O OD1 . ASN A 376 ? 0.6514 0.9959 0.5472 -0.2065 0.0370  -0.1344 376 ASN A OD1 
3136 N ND2 . ASN A 376 ? 0.6349 0.9378 0.5244 -0.2080 0.0400  -0.1283 376 ASN A ND2 
3137 N N   . LEU A 377 ? 0.7528 1.0897 0.6391 -0.2456 0.0526  -0.1640 377 LEU A N   
3138 C CA  . LEU A 377 ? 0.7807 1.1385 0.6651 -0.2649 0.0595  -0.1782 377 LEU A CA  
3139 C C   . LEU A 377 ? 0.8177 1.1424 0.6943 -0.2802 0.0690  -0.1870 377 LEU A C   
3140 O O   . LEU A 377 ? 0.8131 1.1205 0.6879 -0.2792 0.0701  -0.1877 377 LEU A O   
3141 C CB  . LEU A 377 ? 0.7442 1.1477 0.6338 -0.2669 0.0571  -0.1848 377 LEU A CB  
3142 C CG  . LEU A 377 ? 0.7162 1.1603 0.6133 -0.2549 0.0497  -0.1786 377 LEU A CG  
3143 C CD1 . LEU A 377 ? 0.6875 1.1704 0.5891 -0.2527 0.0463  -0.1821 377 LEU A CD1 
3144 C CD2 . LEU A 377 ? 0.7173 1.1820 0.6152 -0.2638 0.0525  -0.1836 377 LEU A CD2 
3145 N N   . PRO A 378 ? 0.8662 1.1810 0.7377 -0.2942 0.0765  -0.1935 378 PRO A N   
3146 C CA  . PRO A 378 ? 0.9208 1.1986 0.7836 -0.3077 0.0867  -0.2002 378 PRO A CA  
3147 C C   . PRO A 378 ? 0.9644 1.2516 0.8253 -0.3226 0.0935  -0.2143 378 PRO A C   
3148 O O   . PRO A 378 ? 1.0029 1.2564 0.8570 -0.3309 0.1018  -0.2186 378 PRO A O   
3149 C CB  . PRO A 378 ? 0.9315 1.2056 0.7901 -0.3191 0.0928  -0.2041 378 PRO A CB  
3150 C CG  . PRO A 378 ? 0.9076 1.2035 0.7724 -0.3062 0.0841  -0.1947 378 PRO A CG  
3151 C CD  . PRO A 378 ? 0.8834 1.2177 0.7566 -0.2966 0.0761  -0.1934 378 PRO A CD  
3152 N N   . THR A 379 ? 0.9712 1.3035 0.8379 -0.3256 0.0904  -0.2210 379 THR A N   
3153 C CA  . THR A 379 ? 1.0167 1.3630 0.8819 -0.3405 0.0965  -0.2352 379 THR A CA  
3154 C C   . THR A 379 ? 0.9973 1.3307 0.8631 -0.3318 0.0938  -0.2319 379 THR A C   
3155 O O   . THR A 379 ? 1.0042 1.3361 0.8670 -0.3441 0.1005  -0.2431 379 THR A O   
3156 C CB  . THR A 379 ? 1.0324 1.4355 0.9033 -0.3477 0.0942  -0.2443 379 THR A CB  
3157 O OG1 . THR A 379 ? 1.0209 1.4520 0.8998 -0.3286 0.0823  -0.2332 379 THR A OG1 
3158 C CG2 . THR A 379 ? 1.0308 1.4478 0.9005 -0.3611 0.0994  -0.2515 379 THR A CG2 
3159 N N   . HIS A 380 ? 0.9813 1.3058 0.8510 -0.3113 0.0844  -0.2172 380 HIS A N   
3160 C CA  . HIS A 380 ? 0.9999 1.3113 0.8706 -0.3016 0.0813  -0.2128 380 HIS A CA  
3161 C C   . HIS A 380 ? 1.0190 1.2812 0.8829 -0.3047 0.0884  -0.2127 380 HIS A C   
3162 O O   . HIS A 380 ? 1.0300 1.2636 0.8886 -0.3093 0.0939  -0.2116 380 HIS A O   
3163 C CB  . HIS A 380 ? 0.9946 1.3112 0.8714 -0.2792 0.0698  -0.1973 380 HIS A CB  
3164 C CG  . HIS A 380 ? 1.0055 1.3700 0.8891 -0.2730 0.0627  -0.1969 380 HIS A CG  
3165 N ND1 . HIS A 380 ? 0.9972 1.3705 0.8840 -0.2621 0.0572  -0.1924 380 HIS A ND1 
3166 C CD2 . HIS A 380 ? 0.9911 1.3984 0.8787 -0.2759 0.0604  -0.2002 380 HIS A CD2 
3167 C CE1 . HIS A 380 ? 0.9903 1.4091 0.8825 -0.2579 0.0519  -0.1924 380 HIS A CE1 
3168 N NE2 . HIS A 380 ? 0.9837 1.4238 0.8766 -0.2660 0.0537  -0.1971 380 HIS A NE2 
3169 N N   . ARG A 381 ? 1.0552 1.3078 0.9191 -0.3019 0.0887  -0.2137 381 ARG A N   
3170 C CA  . ARG A 381 ? 1.1049 1.3114 0.9631 -0.3026 0.0951  -0.2126 381 ARG A CA  
3171 C C   . ARG A 381 ? 1.1192 1.2930 0.9762 -0.2889 0.0915  -0.1984 381 ARG A C   
3172 O O   . ARG A 381 ? 1.1147 1.2585 0.9654 -0.2949 0.0986  -0.1987 381 ARG A O   
3173 C CB  . ARG A 381 ? 1.1332 1.3386 0.9936 -0.2963 0.0928  -0.2124 381 ARG A CB  
3174 C CG  . ARG A 381 ? 1.1942 1.4237 1.0539 -0.3115 0.0985  -0.2277 381 ARG A CG  
3175 C CD  . ARG A 381 ? 1.1955 1.4437 1.0603 -0.3012 0.0913  -0.2248 381 ARG A CD  
3176 N NE  . ARG A 381 ? 1.2507 1.5101 1.1135 -0.3151 0.0980  -0.2388 381 ARG A NE  
3177 C CZ  . ARG A 381 ? 1.2700 1.5701 1.1338 -0.3277 0.0994  -0.2506 381 ARG A CZ  
3178 N NH1 . ARG A 381 ? 1.2613 1.5956 1.1286 -0.3278 0.0946  -0.2498 381 ARG A NH1 
3179 N NH2 . ARG A 381 ? 1.2653 1.5730 1.1267 -0.3404 0.1059  -0.2635 381 ARG A NH2 
3180 N N   . HIS A 382 ? 1.1044 1.2853 0.9673 -0.2707 0.0809  -0.1862 382 HIS A N   
3181 C CA  . HIS A 382 ? 1.0793 1.2322 0.9417 -0.2567 0.0765  -0.1725 382 HIS A CA  
3182 C C   . HIS A 382 ? 1.0108 1.1869 0.8786 -0.2458 0.0675  -0.1639 382 HIS A C   
3183 O O   . HIS A 382 ? 0.9493 1.1355 0.8225 -0.2312 0.0592  -0.1556 382 HIS A O   
3184 C CB  . HIS A 382 ? 1.1333 1.2631 0.9969 -0.2447 0.0736  -0.1655 382 HIS A CB  
3185 C CG  . HIS A 382 ? 1.2271 1.3335 1.0857 -0.2542 0.0828  -0.1737 382 HIS A CG  
3186 N ND1 . HIS A 382 ? 1.2549 1.3741 1.1155 -0.2570 0.0835  -0.1803 382 HIS A ND1 
3187 C CD2 . HIS A 382 ? 1.2636 1.3333 1.1149 -0.2616 0.0923  -0.1760 382 HIS A CD2 
3188 C CE1 . HIS A 382 ? 1.2653 1.3571 1.1205 -0.2659 0.0932  -0.1870 382 HIS A CE1 
3189 N NE2 . HIS A 382 ? 1.3071 1.3682 1.1565 -0.2684 0.0988  -0.1841 382 HIS A NE2 
3190 N N   . PRO A 383 ? 0.9737 1.1580 0.8398 -0.2529 0.0697  -0.1661 383 PRO A N   
3191 C CA  . PRO A 383 ? 0.9509 1.1542 0.8215 -0.2430 0.0623  -0.1579 383 PRO A CA  
3192 C C   . PRO A 383 ? 0.9298 1.1068 0.8007 -0.2269 0.0568  -0.1440 383 PRO A C   
3193 O O   . PRO A 383 ? 0.9352 1.0763 0.8012 -0.2264 0.0601  -0.1410 383 PRO A O   
3194 C CB  . PRO A 383 ? 0.9656 1.1730 0.8324 -0.2564 0.0683  -0.1643 383 PRO A CB  
3195 C CG  . PRO A 383 ? 0.9858 1.1622 0.8446 -0.2701 0.0787  -0.1719 383 PRO A CG  
3196 C CD  . PRO A 383 ? 0.9857 1.1617 0.8454 -0.2714 0.0801  -0.1769 383 PRO A CD  
3197 N N   . GLN A 384 ? 0.8983 1.0940 0.7750 -0.2139 0.0488  -0.1356 384 GLN A N   
3198 C CA  . GLN A 384 ? 0.8562 1.0325 0.7343 -0.1980 0.0429  -0.1230 384 GLN A CA  
3199 C C   . GLN A 384 ? 0.8122 1.0042 0.6937 -0.1897 0.0379  -0.1161 384 GLN A C   
3200 O O   . GLN A 384 ? 0.7981 1.0237 0.6844 -0.1876 0.0350  -0.1172 384 GLN A O   
3201 C CB  . GLN A 384 ? 0.8445 1.0256 0.7268 -0.1877 0.0382  -0.1196 384 GLN A CB  
3202 C CG  . GLN A 384 ? 0.9048 1.0520 0.7857 -0.1786 0.0366  -0.1120 384 GLN A CG  
3203 C CD  . GLN A 384 ? 0.9087 1.0609 0.7936 -0.1701 0.0330  -0.1100 384 GLN A CD  
3204 O OE1 . GLN A 384 ? 0.9356 1.0735 0.8187 -0.1739 0.0362  -0.1140 384 GLN A OE1 
3205 N NE2 . GLN A 384 ? 0.8837 1.0557 0.7738 -0.1584 0.0267  -0.1036 384 GLN A NE2 
3206 N N   . ASP A 385 ? 0.7974 0.9652 0.6761 -0.1845 0.0370  -0.1086 385 ASP A N   
3207 C CA  . ASP A 385 ? 0.7679 0.9467 0.6493 -0.1763 0.0328  -0.1016 385 ASP A CA  
3208 C C   . ASP A 385 ? 0.7202 0.9079 0.6074 -0.1600 0.0258  -0.0928 385 ASP A C   
3209 O O   . ASP A 385 ? 0.6921 0.9012 0.5832 -0.1534 0.0228  -0.0892 385 ASP A O   
3210 C CB  . ASP A 385 ? 0.7886 0.9389 0.6646 -0.1770 0.0345  -0.0971 385 ASP A CB  
3211 C CG  . ASP A 385 ? 0.8192 0.9720 0.6907 -0.1912 0.0406  -0.1041 385 ASP A CG  
3212 O OD1 . ASP A 385 ? 0.8382 1.0168 0.7114 -0.2007 0.0433  -0.1130 385 ASP A OD1 
3213 O OD2 . ASP A 385 ? 0.8344 0.9645 0.7005 -0.1930 0.0428  -0.1009 385 ASP A OD2 
3214 N N   . GLU A 386 ? 0.6837 0.8544 0.5712 -0.1535 0.0240  -0.0894 386 GLU A N   
3215 C CA  . GLU A 386 ? 0.6611 0.8341 0.5530 -0.1384 0.0183  -0.0807 386 GLU A CA  
3216 C C   . GLU A 386 ? 0.6429 0.8396 0.5392 -0.1351 0.0165  -0.0829 386 GLU A C   
3217 O O   . GLU A 386 ? 0.6683 0.8621 0.5636 -0.1409 0.0186  -0.0885 386 GLU A O   
3218 C CB  . GLU A 386 ? 0.6628 0.8026 0.5525 -0.1322 0.0170  -0.0746 386 GLU A CB  
3219 C CG  . GLU A 386 ? 0.6974 0.8136 0.5817 -0.1362 0.0192  -0.0727 386 GLU A CG  
3220 C CD  . GLU A 386 ? 0.7461 0.8395 0.6299 -0.1259 0.0158  -0.0639 386 GLU A CD  
3221 O OE1 . GLU A 386 ? 0.7699 0.8505 0.6546 -0.1209 0.0144  -0.0619 386 GLU A OE1 
3222 O OE2 . GLU A 386 ? 0.7169 0.8059 0.5993 -0.1234 0.0149  -0.0595 386 GLU A OE2 
3223 N N   . ILE A 387 ? 0.5837 0.8042 0.4845 -0.1258 0.0131  -0.0783 387 ILE A N   
3224 C CA  . ILE A 387 ? 0.5663 0.8141 0.4708 -0.1223 0.0115  -0.0798 387 ILE A CA  
3225 C C   . ILE A 387 ? 0.5469 0.7912 0.4545 -0.1068 0.0075  -0.0705 387 ILE A C   
3226 O O   . ILE A 387 ? 0.5663 0.8122 0.4755 -0.0973 0.0057  -0.0633 387 ILE A O   
3227 C CB  . ILE A 387 ? 0.5576 0.8423 0.4650 -0.1245 0.0117  -0.0827 387 ILE A CB  
3228 C CG1 . ILE A 387 ? 0.5584 0.8466 0.4627 -0.1407 0.0162  -0.0923 387 ILE A CG1 
3229 C CG2 . ILE A 387 ? 0.5274 0.8426 0.4383 -0.1205 0.0099  -0.0840 387 ILE A CG2 
3230 C CD1 . ILE A 387 ? 0.5557 0.8375 0.4567 -0.1542 0.0203  -0.1023 387 ILE A CD1 
3231 N N   . PRO A 388 ? 0.5407 0.7793 0.4487 -0.1044 0.0068  -0.0709 388 PRO A N   
3232 C CA  . PRO A 388 ? 0.5477 0.7845 0.4583 -0.0903 0.0037  -0.0625 388 PRO A CA  
3233 C C   . PRO A 388 ? 0.5583 0.8294 0.4723 -0.0834 0.0023  -0.0605 388 PRO A C   
3234 O O   . PRO A 388 ? 0.5950 0.8892 0.5095 -0.0896 0.0030  -0.0669 388 PRO A O   
3235 C CB  . PRO A 388 ? 0.5515 0.7708 0.4611 -0.0917 0.0039  -0.0647 388 PRO A CB  
3236 C CG  . PRO A 388 ? 0.5726 0.7995 0.4802 -0.1057 0.0071  -0.0751 388 PRO A CG  
3237 C CD  . PRO A 388 ? 0.5730 0.8065 0.4789 -0.1146 0.0093  -0.0791 388 PRO A CD  
3238 N N   . TYR A 389 ? 0.5463 0.8209 0.4624 -0.0707 0.0007  -0.0517 389 TYR A N   
3239 C CA  . TYR A 389 ? 0.5240 0.8291 0.4430 -0.0614 -0.0001 -0.0478 389 TYR A CA  
3240 C C   . TYR A 389 ? 0.5189 0.8145 0.4390 -0.0462 -0.0008 -0.0371 389 TYR A C   
3241 O O   . TYR A 389 ? 0.5156 0.7963 0.4353 -0.0432 -0.0002 -0.0332 389 TYR A O   
3242 C CB  . TYR A 389 ? 0.5244 0.8581 0.4447 -0.0657 0.0006  -0.0509 389 TYR A CB  
3243 C CG  . TYR A 389 ? 0.5288 0.8955 0.4521 -0.0549 -0.0002 -0.0459 389 TYR A CG  
3244 C CD1 . TYR A 389 ? 0.5365 0.9305 0.4607 -0.0557 -0.0010 -0.0491 389 TYR A CD1 
3245 C CD2 . TYR A 389 ? 0.5186 0.8899 0.4436 -0.0437 0.0000  -0.0379 389 TYR A CD2 
3246 C CE1 . TYR A 389 ? 0.5194 0.9453 0.4460 -0.0448 -0.0017 -0.0437 389 TYR A CE1 
3247 C CE2 . TYR A 389 ? 0.5372 0.9388 0.4648 -0.0325 -0.0001 -0.0324 389 TYR A CE2 
3248 C CZ  . TYR A 389 ? 0.5371 0.9663 0.4655 -0.0328 -0.0012 -0.0350 389 TYR A CZ  
3249 O OH  . TYR A 389 ? 0.5390 0.9990 0.4695 -0.0207 -0.0014 -0.0287 389 TYR A OH  
3250 N N   . CYS A 390 ? 0.5275 0.8310 0.4485 -0.0370 -0.0014 -0.0328 390 CYS A N   
3251 C CA  . CYS A 390 ? 0.5513 0.8463 0.4730 -0.0225 -0.0009 -0.0229 390 CYS A CA  
3252 C C   . CYS A 390 ? 0.5284 0.7877 0.4489 -0.0209 -0.0006 -0.0199 390 CYS A C   
3253 O O   . CYS A 390 ? 0.4604 0.7114 0.3810 -0.0132 0.0006  -0.0138 390 CYS A O   
3254 C CB  . CYS A 390 ? 0.5876 0.9034 0.5109 -0.0139 0.0002  -0.0174 390 CYS A CB  
3255 S SG  . CYS A 390 ? 0.6850 1.0451 0.6101 -0.0099 -0.0003 -0.0175 390 CYS A SG  
3256 N N   . GLY A 391 ? 0.5469 0.7862 0.4660 -0.0280 -0.0015 -0.0243 391 GLY A N   
3257 C CA  . GLY A 391 ? 0.5272 0.7348 0.4453 -0.0272 -0.0016 -0.0221 391 GLY A CA  
3258 C C   . GLY A 391 ? 0.5460 0.7413 0.4627 -0.0327 -0.0013 -0.0232 391 GLY A C   
3259 O O   . GLY A 391 ? 0.5832 0.7567 0.4991 -0.0301 -0.0013 -0.0199 391 GLY A O   
3260 N N   . LYS A 392 ? 0.5138 0.7239 0.4301 -0.0406 -0.0010 -0.0280 392 LYS A N   
3261 C CA  . LYS A 392 ? 0.5165 0.7166 0.4311 -0.0464 -0.0004 -0.0293 392 LYS A CA  
3262 C C   . LYS A 392 ? 0.5255 0.7264 0.4381 -0.0602 0.0001  -0.0377 392 LYS A C   
3263 O O   . LYS A 392 ? 0.5549 0.7730 0.4681 -0.0652 0.0004  -0.0430 392 LYS A O   
3264 C CB  . LYS A 392 ? 0.5219 0.7393 0.4379 -0.0409 0.0006  -0.0256 392 LYS A CB  
3265 C CG  . LYS A 392 ? 0.5702 0.7724 0.4861 -0.0318 0.0014  -0.0185 392 LYS A CG  
3266 C CD  . LYS A 392 ? 0.5815 0.7825 0.4989 -0.0197 0.0021  -0.0122 392 LYS A CD  
3267 C CE  . LYS A 392 ? 0.5970 0.7786 0.5136 -0.0132 0.0037  -0.0068 392 LYS A CE  
3268 N NZ  . LYS A 392 ? 0.5914 0.7702 0.5089 -0.0015 0.0057  -0.0006 392 LYS A NZ  
3269 N N   . ILE A 393 ? 0.5122 0.6939 0.4219 -0.0664 0.0007  -0.0390 393 ILE A N   
3270 C CA  . ILE A 393 ? 0.5129 0.6937 0.4198 -0.0795 0.0025  -0.0464 393 ILE A CA  
3271 C C   . ILE A 393 ? 0.5083 0.6981 0.4144 -0.0830 0.0038  -0.0469 393 ILE A C   
3272 O O   . ILE A 393 ? 0.5006 0.6765 0.4054 -0.0799 0.0035  -0.0425 393 ILE A O   
3273 C CB  . ILE A 393 ? 0.5285 0.6791 0.4319 -0.0847 0.0030  -0.0477 393 ILE A CB  
3274 C CG1 . ILE A 393 ? 0.5455 0.6879 0.4500 -0.0816 0.0020  -0.0478 393 ILE A CG1 
3275 C CG2 . ILE A 393 ? 0.5433 0.6907 0.4428 -0.0982 0.0062  -0.0550 393 ILE A CG2 
3276 C CD1 . ILE A 393 ? 0.5508 0.6633 0.4532 -0.0807 0.0015  -0.0455 393 ILE A CD1 
3277 N N   . PHE A 394 ? 0.5011 0.7158 0.4081 -0.0897 0.0052  -0.0525 394 PHE A N   
3278 C CA  . PHE A 394 ? 0.5116 0.7382 0.4181 -0.0945 0.0068  -0.0544 394 PHE A CA  
3279 C C   . PHE A 394 ? 0.5288 0.7443 0.4309 -0.1093 0.0099  -0.0619 394 PHE A C   
3280 O O   . PHE A 394 ? 0.5751 0.7954 0.4762 -0.1179 0.0116  -0.0689 394 PHE A O   
3281 C CB  . PHE A 394 ? 0.4822 0.7464 0.3929 -0.0925 0.0068  -0.0560 394 PHE A CB  
3282 C CG  . PHE A 394 ? 0.4604 0.7365 0.3749 -0.0773 0.0048  -0.0480 394 PHE A CG  
3283 C CD1 . PHE A 394 ? 0.4511 0.7277 0.3669 -0.0708 0.0033  -0.0458 394 PHE A CD1 
3284 C CD2 . PHE A 394 ? 0.4554 0.7417 0.3719 -0.0693 0.0052  -0.0426 394 PHE A CD2 
3285 C CE1 . PHE A 394 ? 0.4511 0.7371 0.3697 -0.0567 0.0023  -0.0380 394 PHE A CE1 
3286 C CE2 . PHE A 394 ? 0.4408 0.7360 0.3603 -0.0548 0.0045  -0.0349 394 PHE A CE2 
3287 C CZ  . PHE A 394 ? 0.4344 0.7290 0.3546 -0.0485 0.0032  -0.0324 394 PHE A CZ  
3288 N N   . ASN A 395 ? 0.5410 0.7403 0.4397 -0.1124 0.0111  -0.0606 395 ASN A N   
3289 C CA  . ASN A 395 ? 0.5560 0.7462 0.4500 -0.1263 0.0150  -0.0673 395 ASN A CA  
3290 C C   . ASN A 395 ? 0.5418 0.7577 0.4369 -0.1326 0.0170  -0.0716 395 ASN A C   
3291 O O   . ASN A 395 ? 0.5220 0.7427 0.4181 -0.1279 0.0164  -0.0675 395 ASN A O   
3292 C CB  . ASN A 395 ? 0.5535 0.7112 0.4423 -0.1267 0.0154  -0.0633 395 ASN A CB  
3293 C CG  . ASN A 395 ? 0.5625 0.7071 0.4452 -0.1403 0.0202  -0.0693 395 ASN A CG  
3294 O OD1 . ASN A 395 ? 0.5873 0.7474 0.4693 -0.1491 0.0233  -0.0748 395 ASN A OD1 
3295 N ND2 . ASN A 395 ? 0.5409 0.6566 0.4190 -0.1420 0.0214  -0.0681 395 ASN A ND2 
3296 N N   . LEU A 396 ? 0.5478 0.7814 0.4430 -0.1433 0.0198  -0.0804 396 LEU A N   
3297 C CA  . LEU A 396 ? 0.5609 0.8247 0.4582 -0.1493 0.0216  -0.0855 396 LEU A CA  
3298 C C   . LEU A 396 ? 0.5841 0.8369 0.4771 -0.1575 0.0249  -0.0871 396 LEU A C   
3299 O O   . LEU A 396 ? 0.5841 0.8589 0.4794 -0.1590 0.0257  -0.0885 396 LEU A O   
3300 C CB  . LEU A 396 ? 0.5640 0.8497 0.4621 -0.1602 0.0241  -0.0956 396 LEU A CB  
3301 C CG  . LEU A 396 ? 0.5627 0.8653 0.4650 -0.1527 0.0208  -0.0946 396 LEU A CG  
3302 C CD1 . LEU A 396 ? 0.5570 0.8824 0.4594 -0.1653 0.0238  -0.1057 396 LEU A CD1 
3303 C CD2 . LEU A 396 ? 0.5395 0.8662 0.4477 -0.1378 0.0166  -0.0868 396 LEU A CD2 
3304 N N   . THR A 397 ? 0.5991 0.8180 0.4859 -0.1620 0.0270  -0.0864 397 THR A N   
3305 C CA  . THR A 397 ? 0.6067 0.8117 0.4881 -0.1703 0.0308  -0.0876 397 THR A CA  
3306 C C   . THR A 397 ? 0.5938 0.7870 0.4750 -0.1599 0.0278  -0.0784 397 THR A C   
3307 O O   . THR A 397 ? 0.6107 0.8149 0.4923 -0.1611 0.0287  -0.0783 397 THR A O   
3308 C CB  . THR A 397 ? 0.6338 0.8083 0.5076 -0.1808 0.0356  -0.0914 397 THR A CB  
3309 O OG1 . THR A 397 ? 0.6448 0.8312 0.5183 -0.1924 0.0397  -0.1014 397 THR A OG1 
3310 C CG2 . THR A 397 ? 0.6129 0.7715 0.4802 -0.1884 0.0396  -0.0915 397 THR A CG2 
3311 N N   . THR A 398 ? 0.5809 0.7533 0.4618 -0.1499 0.0243  -0.0713 398 THR A N   
3312 C CA  . THR A 398 ? 0.5693 0.7283 0.4494 -0.1408 0.0219  -0.0631 398 THR A CA  
3313 C C   . THR A 398 ? 0.5499 0.7291 0.4366 -0.1284 0.0185  -0.0581 398 THR A C   
3314 O O   . THR A 398 ? 0.5436 0.7179 0.4301 -0.1222 0.0175  -0.0528 398 THR A O   
3315 C CB  . THR A 398 ? 0.5892 0.7166 0.4656 -0.1362 0.0201  -0.0578 398 THR A CB  
3316 O OG1 . THR A 398 ? 0.5682 0.6977 0.4486 -0.1292 0.0173  -0.0566 398 THR A OG1 
3317 C CG2 . THR A 398 ? 0.5890 0.6935 0.4580 -0.1470 0.0242  -0.0613 398 THR A CG2 
3318 N N   . ARG A 399 ? 0.5358 0.7368 0.4277 -0.1246 0.0171  -0.0597 399 ARG A N   
3319 C CA  . ARG A 399 ? 0.5255 0.7469 0.4235 -0.1120 0.0147  -0.0547 399 ARG A CA  
3320 C C   . ARG A 399 ? 0.5375 0.7411 0.4363 -0.0998 0.0118  -0.0468 399 ARG A C   
3321 O O   . ARG A 399 ? 0.5608 0.7769 0.4639 -0.0887 0.0105  -0.0420 399 ARG A O   
3322 C CB  . ARG A 399 ? 0.5213 0.7595 0.4211 -0.1108 0.0160  -0.0537 399 ARG A CB  
3323 C CG  . ARG A 399 ? 0.5321 0.7965 0.4330 -0.1211 0.0187  -0.0615 399 ARG A CG  
3324 C CD  . ARG A 399 ? 0.5521 0.8026 0.4474 -0.1337 0.0221  -0.0658 399 ARG A CD  
3325 N NE  . ARG A 399 ? 0.5743 0.8483 0.4702 -0.1458 0.0253  -0.0746 399 ARG A NE  
3326 C CZ  . ARG A 399 ? 0.5512 0.8538 0.4511 -0.1456 0.0263  -0.0763 399 ARG A CZ  
3327 N NH1 . ARG A 399 ? 0.5388 0.8492 0.4424 -0.1334 0.0246  -0.0694 399 ARG A NH1 
3328 N NH2 . ARG A 399 ? 0.5706 0.8944 0.4709 -0.1579 0.0294  -0.0852 399 ARG A NH2 
3329 N N   . GLN A 400 ? 0.5347 0.7093 0.4291 -0.1019 0.0113  -0.0455 400 GLN A N   
3330 C CA  . GLN A 400 ? 0.5121 0.6688 0.4068 -0.0922 0.0087  -0.0393 400 GLN A CA  
3331 C C   . GLN A 400 ? 0.4974 0.6638 0.3963 -0.0859 0.0070  -0.0387 400 GLN A C   
3332 O O   . GLN A 400 ? 0.5065 0.6832 0.4060 -0.0917 0.0076  -0.0440 400 GLN A O   
3333 C CB  . GLN A 400 ? 0.5234 0.6505 0.4127 -0.0968 0.0085  -0.0390 400 GLN A CB  
3334 C CG  . GLN A 400 ? 0.5232 0.6384 0.4072 -0.1033 0.0103  -0.0391 400 GLN A CG  
3335 C CD  . GLN A 400 ? 0.5482 0.6688 0.4334 -0.0972 0.0101  -0.0349 400 GLN A CD  
3336 O OE1 . GLN A 400 ? 0.5880 0.7272 0.4747 -0.0991 0.0119  -0.0368 400 GLN A OE1 
3337 N NE2 . GLN A 400 ? 0.5163 0.6214 0.4008 -0.0900 0.0083  -0.0295 400 GLN A NE2 
3338 N N   . VAL A 401 ? 0.4832 0.6459 0.3845 -0.0745 0.0054  -0.0326 401 VAL A N   
3339 C CA  . VAL A 401 ? 0.4621 0.6299 0.3665 -0.0679 0.0040  -0.0312 401 VAL A CA  
3340 C C   . VAL A 401 ? 0.4675 0.6106 0.3709 -0.0627 0.0024  -0.0272 401 VAL A C   
3341 O O   . VAL A 401 ? 0.4612 0.5927 0.3638 -0.0574 0.0024  -0.0226 401 VAL A O   
3342 C CB  . VAL A 401 ? 0.4444 0.6365 0.3533 -0.0580 0.0044  -0.0277 401 VAL A CB  
3343 C CG1 . VAL A 401 ? 0.4257 0.6226 0.3370 -0.0515 0.0032  -0.0260 401 VAL A CG1 
3344 C CG2 . VAL A 401 ? 0.4455 0.6653 0.3560 -0.0631 0.0057  -0.0319 401 VAL A CG2 
3345 N N   . ARG A 402 ? 0.4749 0.6111 0.3782 -0.0647 0.0013  -0.0294 402 ARG A N   
3346 C CA  . ARG A 402 ? 0.4960 0.6110 0.3989 -0.0603 -0.0001 -0.0263 402 ARG A CA  
3347 C C   . ARG A 402 ? 0.4950 0.6189 0.4015 -0.0532 -0.0009 -0.0249 402 ARG A C   
3348 O O   . ARG A 402 ? 0.4822 0.6262 0.3905 -0.0542 -0.0005 -0.0276 402 ARG A O   
3349 C CB  . ARG A 402 ? 0.4953 0.5916 0.3946 -0.0686 -0.0003 -0.0298 402 ARG A CB  
3350 C CG  . ARG A 402 ? 0.5194 0.6048 0.4141 -0.0759 0.0008  -0.0309 402 ARG A CG  
3351 C CD  . ARG A 402 ? 0.5515 0.6195 0.4443 -0.0714 -0.0004 -0.0257 402 ARG A CD  
3352 N NE  . ARG A 402 ? 0.5536 0.6046 0.4466 -0.0675 -0.0023 -0.0234 402 ARG A NE  
3353 C CZ  . ARG A 402 ? 0.5607 0.5942 0.4504 -0.0717 -0.0025 -0.0241 402 ARG A CZ  
3354 N NH1 . ARG A 402 ? 0.5950 0.6234 0.4801 -0.0800 -0.0004 -0.0268 402 ARG A NH1 
3355 N NH2 . ARG A 402 ? 0.5232 0.5439 0.4138 -0.0672 -0.0043 -0.0220 402 ARG A NH2 
3356 N N   . THR A 403 ? 0.5074 0.6171 0.4146 -0.0463 -0.0018 -0.0209 403 THR A N   
3357 C CA  . THR A 403 ? 0.5202 0.6347 0.4301 -0.0403 -0.0023 -0.0197 403 THR A CA  
3358 C C   . THR A 403 ? 0.5166 0.6263 0.4261 -0.0468 -0.0031 -0.0247 403 THR A C   
3359 O O   . THR A 403 ? 0.5206 0.6135 0.4277 -0.0527 -0.0034 -0.0268 403 THR A O   
3360 C CB  . THR A 403 ? 0.5232 0.6226 0.4339 -0.0324 -0.0025 -0.0148 403 THR A CB  
3361 O OG1 . THR A 403 ? 0.5645 0.6657 0.4750 -0.0272 -0.0008 -0.0107 403 THR A OG1 
3362 C CG2 . THR A 403 ? 0.5126 0.6172 0.4258 -0.0260 -0.0023 -0.0133 403 THR A CG2 
3363 N N   . LEU A 404 ? 0.5398 0.6645 0.4513 -0.0455 -0.0030 -0.0264 404 LEU A N   
3364 C CA  . LEU A 404 ? 0.5523 0.6731 0.4634 -0.0514 -0.0031 -0.0315 404 LEU A CA  
3365 C C   . LEU A 404 ? 0.5587 0.6654 0.4711 -0.0457 -0.0041 -0.0291 404 LEU A C   
3366 O O   . LEU A 404 ? 0.5387 0.6501 0.4532 -0.0370 -0.0042 -0.0247 404 LEU A O   
3367 C CB  . LEU A 404 ? 0.5608 0.7069 0.4730 -0.0543 -0.0023 -0.0357 404 LEU A CB  
3368 C CG  . LEU A 404 ? 0.5657 0.7135 0.4779 -0.0591 -0.0019 -0.0411 404 LEU A CG  
3369 C CD1 . LEU A 404 ? 0.5614 0.6963 0.4708 -0.0707 -0.0002 -0.0477 404 LEU A CD1 
3370 C CD2 . LEU A 404 ? 0.5427 0.7203 0.4565 -0.0588 -0.0017 -0.0434 404 LEU A CD2 
3371 N N   . TYR A 405 ? 0.6111 0.7001 0.5224 -0.0505 -0.0043 -0.0318 405 TYR A N   
3372 C CA  . TYR A 405 ? 0.6284 0.7056 0.5412 -0.0469 -0.0050 -0.0312 405 TYR A CA  
3373 C C   . TYR A 405 ? 0.6956 0.7672 0.6071 -0.0552 -0.0038 -0.0375 405 TYR A C   
3374 O O   . TYR A 405 ? 0.7976 0.8567 0.7064 -0.0614 -0.0028 -0.0395 405 TYR A O   
3375 C CB  . TYR A 405 ? 0.5644 0.6209 0.4770 -0.0432 -0.0063 -0.0270 405 TYR A CB  
3376 C CG  . TYR A 405 ? 0.5205 0.5771 0.4330 -0.0380 -0.0066 -0.0220 405 TYR A CG  
3377 C CD1 . TYR A 405 ? 0.5086 0.5658 0.4232 -0.0296 -0.0064 -0.0178 405 TYR A CD1 
3378 C CD2 . TYR A 405 ? 0.5024 0.5562 0.4122 -0.0417 -0.0065 -0.0217 405 TYR A CD2 
3379 C CE1 . TYR A 405 ? 0.4787 0.5341 0.3929 -0.0253 -0.0057 -0.0137 405 TYR A CE1 
3380 C CE2 . TYR A 405 ? 0.4871 0.5401 0.3966 -0.0373 -0.0064 -0.0175 405 TYR A CE2 
3381 C CZ  . TYR A 405 ? 0.4914 0.5451 0.4032 -0.0292 -0.0058 -0.0137 405 TYR A CZ  
3382 O OH  . TYR A 405 ? 0.4924 0.5442 0.4036 -0.0252 -0.0047 -0.0101 405 TYR A OH  
3383 N N   . LYS A 406 ? 0.7660 0.8453 0.6790 -0.0555 -0.0032 -0.0406 406 LYS A N   
3384 C CA  . LYS A 406 ? 0.8233 0.9136 0.7391 -0.0477 -0.0039 -0.0378 406 LYS A CA  
3385 C C   . LYS A 406 ? 0.7967 0.8732 0.7140 -0.0458 -0.0040 -0.0385 406 LYS A C   
3386 O O   . LYS A 406 ? 0.7746 0.8547 0.6939 -0.0390 -0.0045 -0.0357 406 LYS A O   
3387 C CB  . LYS A 406 ? 0.8053 0.8978 0.7221 -0.0387 -0.0049 -0.0308 406 LYS A CB  
3388 C CG  . LYS A 406 ? 0.8137 0.9260 0.7319 -0.0320 -0.0044 -0.0280 406 LYS A CG  
3389 C CD  . LYS A 406 ? 0.8383 0.9464 0.7572 -0.0226 -0.0041 -0.0210 406 LYS A CD  
3390 C CE  . LYS A 406 ? 0.7906 0.8769 0.7104 -0.0199 -0.0046 -0.0192 406 LYS A CE  
3391 N NZ  . LYS A 406 ? 0.8471 0.9301 0.7674 -0.0113 -0.0032 -0.0133 406 LYS A NZ  
3392 N N   . LEU A 407 ? 0.7401 0.8002 0.6562 -0.0515 -0.0032 -0.0420 407 LEU A N   
3393 C CA  . LEU A 407 ? 0.7750 0.8202 0.6929 -0.0490 -0.0033 -0.0420 407 LEU A CA  
3394 C C   . LEU A 407 ? 0.8059 0.8462 0.7227 -0.0563 -0.0006 -0.0486 407 LEU A C   
3395 O O   . LEU A 407 ? 0.8041 0.8325 0.7183 -0.0622 0.0010  -0.0511 407 LEU A O   
3396 C CB  . LEU A 407 ? 0.7985 0.8241 0.7165 -0.0455 -0.0048 -0.0377 407 LEU A CB  
3397 C CG  . LEU A 407 ? 0.7562 0.7806 0.6755 -0.0381 -0.0069 -0.0315 407 LEU A CG  
3398 C CD1 . LEU A 407 ? 0.7774 0.8118 0.6993 -0.0314 -0.0069 -0.0292 407 LEU A CD1 
3399 C CD2 . LEU A 407 ? 0.7456 0.7749 0.6626 -0.0394 -0.0072 -0.0295 407 LEU A CD2 
3400 N N   . PRO A 408 ? 0.8078 0.8563 0.7262 -0.0558 0.0001  -0.0515 408 PRO A N   
3401 C CA  . PRO A 408 ? 0.8073 0.8483 0.7252 -0.0616 0.0030  -0.0577 408 PRO A CA  
3402 C C   . PRO A 408 ? 0.8521 0.8686 0.7705 -0.0596 0.0033  -0.0560 408 PRO A C   
3403 O O   . PRO A 408 ? 0.8148 0.8238 0.7352 -0.0524 0.0006  -0.0501 408 PRO A O   
3404 C CB  . PRO A 408 ? 0.7957 0.8485 0.7159 -0.0580 0.0028  -0.0586 408 PRO A CB  
3405 C CG  . PRO A 408 ? 0.7936 0.8662 0.7141 -0.0533 0.0007  -0.0546 408 PRO A CG  
3406 C CD  . PRO A 408 ? 0.7938 0.8586 0.7142 -0.0493 -0.0011 -0.0487 408 PRO A CD  
3407 N N   . PRO A 409 ? 0.9066 0.9110 0.8233 -0.0659 0.0071  -0.0611 409 PRO A N   
3408 C CA  . PRO A 409 ? 0.8911 0.8737 0.8087 -0.0626 0.0078  -0.0592 409 PRO A CA  
3409 C C   . PRO A 409 ? 0.8695 0.8524 0.7917 -0.0555 0.0061  -0.0575 409 PRO A C   
3410 O O   . PRO A 409 ? 0.8665 0.8627 0.7899 -0.0561 0.0066  -0.0605 409 PRO A O   
3411 C CB  . PRO A 409 ? 0.9288 0.9015 0.8433 -0.0710 0.0135  -0.0660 409 PRO A CB  
3412 C CG  . PRO A 409 ? 0.9104 0.9025 0.8237 -0.0783 0.0155  -0.0727 409 PRO A CG  
3413 C CD  . PRO A 409 ? 0.9036 0.9145 0.8173 -0.0760 0.0115  -0.0691 409 PRO A CD  
3414 N N   . ASN A 410 ? 0.8623 0.8320 0.7869 -0.0490 0.0042  -0.0528 410 ASN A N   
3415 C CA  . ASN A 410 ? 0.8459 0.8152 0.7750 -0.0426 0.0028  -0.0514 410 ASN A CA  
3416 C C   . ASN A 410 ? 0.8180 0.8017 0.7492 -0.0376 -0.0001 -0.0480 410 ASN A C   
3417 O O   . ASN A 410 ? 0.8228 0.8084 0.7572 -0.0331 -0.0005 -0.0475 410 ASN A O   
3418 C CB  . ASN A 410 ? 0.9010 0.8703 0.8310 -0.0457 0.0064  -0.0574 410 ASN A CB  
3419 C CG  . ASN A 410 ? 0.9575 0.9107 0.8854 -0.0503 0.0108  -0.0610 410 ASN A CG  
3420 O OD1 . ASN A 410 ? 1.0149 0.9533 0.9421 -0.0480 0.0106  -0.0575 410 ASN A OD1 
3421 N ND2 . ASN A 410 ? 1.0162 0.9718 0.9426 -0.0567 0.0151  -0.0680 410 ASN A ND2 
3422 N N   . TYR A 411 ? 0.7155 0.7090 0.6445 -0.0383 -0.0015 -0.0458 411 TYR A N   
3423 C CA  . TYR A 411 ? 0.6266 0.6323 0.5569 -0.0329 -0.0033 -0.0420 411 TYR A CA  
3424 C C   . TYR A 411 ? 0.6035 0.5999 0.5362 -0.0267 -0.0054 -0.0370 411 TYR A C   
3425 O O   . TYR A 411 ? 0.6163 0.6029 0.5482 -0.0268 -0.0066 -0.0349 411 TYR A O   
3426 C CB  . TYR A 411 ? 0.5775 0.5965 0.5050 -0.0349 -0.0036 -0.0410 411 TYR A CB  
3427 C CG  . TYR A 411 ? 0.5357 0.5674 0.4639 -0.0288 -0.0044 -0.0369 411 TYR A CG  
3428 C CD1 . TYR A 411 ? 0.5170 0.5642 0.4453 -0.0277 -0.0033 -0.0381 411 TYR A CD1 
3429 C CD2 . TYR A 411 ? 0.4849 0.5134 0.4134 -0.0240 -0.0057 -0.0316 411 TYR A CD2 
3430 C CE1 . TYR A 411 ? 0.4775 0.5354 0.4058 -0.0212 -0.0033 -0.0334 411 TYR A CE1 
3431 C CE2 . TYR A 411 ? 0.4550 0.4931 0.3837 -0.0181 -0.0052 -0.0276 411 TYR A CE2 
3432 C CZ  . TYR A 411 ? 0.4543 0.5065 0.3828 -0.0163 -0.0039 -0.0282 411 TYR A CZ  
3433 O OH  . TYR A 411 ? 0.4616 0.5220 0.3896 -0.0096 -0.0027 -0.0233 411 TYR A OH  
3434 N N   . GLU A 412 ? 0.5301 0.5301 0.4655 -0.0215 -0.0055 -0.0354 412 GLU A N   
3435 C CA  . GLU A 412 ? 0.5003 0.4936 0.4380 -0.0163 -0.0068 -0.0315 412 GLU A CA  
3436 C C   . GLU A 412 ? 0.4795 0.4797 0.4155 -0.0137 -0.0071 -0.0275 412 GLU A C   
3437 O O   . GLU A 412 ? 0.5298 0.5403 0.4652 -0.0110 -0.0056 -0.0262 412 GLU A O   
3438 C CB  . GLU A 412 ? 0.5070 0.4995 0.4482 -0.0127 -0.0059 -0.0321 412 GLU A CB  
3439 C CG  . GLU A 412 ? 0.5234 0.5054 0.4675 -0.0134 -0.0060 -0.0347 412 GLU A CG  
3440 C CD  . GLU A 412 ? 0.5346 0.5171 0.4824 -0.0102 -0.0049 -0.0359 412 GLU A CD  
3441 O OE1 . GLU A 412 ? 0.5160 0.4949 0.4666 -0.0065 -0.0056 -0.0338 412 GLU A OE1 
3442 O OE2 . GLU A 412 ? 0.5363 0.5234 0.4840 -0.0118 -0.0030 -0.0392 412 GLU A OE2 
3443 N N   . ILE A 413 ? 0.4615 0.4557 0.3964 -0.0140 -0.0085 -0.0252 413 ILE A N   
3444 C CA  . ILE A 413 ? 0.4460 0.4458 0.3787 -0.0128 -0.0084 -0.0220 413 ILE A CA  
3445 C C   . ILE A 413 ? 0.4318 0.4340 0.3657 -0.0072 -0.0066 -0.0191 413 ILE A C   
3446 O O   . ILE A 413 ? 0.4286 0.4380 0.3606 -0.0049 -0.0051 -0.0165 413 ILE A O   
3447 C CB  . ILE A 413 ? 0.4332 0.4248 0.3642 -0.0150 -0.0102 -0.0207 413 ILE A CB  
3448 C CG1 . ILE A 413 ? 0.4449 0.4428 0.3732 -0.0147 -0.0097 -0.0181 413 ILE A CG1 
3449 C CG2 . ILE A 413 ? 0.4173 0.3985 0.3507 -0.0128 -0.0116 -0.0196 413 ILE A CG2 
3450 C CD1 . ILE A 413 ? 0.4319 0.4381 0.3575 -0.0190 -0.0094 -0.0196 413 ILE A CD1 
3451 N N   . ARG A 414 ? 0.4244 0.4205 0.3612 -0.0050 -0.0063 -0.0196 414 ARG A N   
3452 C CA  . ARG A 414 ? 0.4009 0.3976 0.3386 -0.0005 -0.0037 -0.0175 414 ARG A CA  
3453 C C   . ARG A 414 ? 0.4119 0.4193 0.3479 0.0023  -0.0010 -0.0161 414 ARG A C   
3454 O O   . ARG A 414 ? 0.4093 0.4174 0.3445 0.0066  0.0021  -0.0132 414 ARG A O   
3455 C CB  . ARG A 414 ? 0.3952 0.3851 0.3367 0.0004  -0.0036 -0.0193 414 ARG A CB  
3456 C CG  . ARG A 414 ? 0.3723 0.3652 0.3154 0.0002  -0.0032 -0.0220 414 ARG A CG  
3457 C CD  . ARG A 414 ? 0.3630 0.3498 0.3103 0.0013  -0.0029 -0.0238 414 ARG A CD  
3458 N NE  . ARG A 414 ? 0.3458 0.3333 0.2948 0.0000  -0.0033 -0.0271 414 ARG A NE  
3459 C CZ  . ARG A 414 ? 0.3487 0.3424 0.2974 0.0008  -0.0011 -0.0282 414 ARG A CZ  
3460 N NH1 . ARG A 414 ? 0.3368 0.3366 0.2833 0.0039  0.0015  -0.0255 414 ARG A NH1 
3461 N NH2 . ARG A 414 ? 0.3450 0.3387 0.2951 -0.0012 -0.0012 -0.0319 414 ARG A NH2 
3462 N N   . HIS A 415 ? 0.4353 0.4511 0.3704 0.0000  -0.0018 -0.0182 415 HIS A N   
3463 C CA  . HIS A 415 ? 0.4488 0.4782 0.3821 0.0024  0.0001  -0.0171 415 HIS A CA  
3464 C C   . HIS A 415 ? 0.4684 0.5069 0.3988 0.0045  0.0010  -0.0136 415 HIS A C   
3465 O O   . HIS A 415 ? 0.5028 0.5530 0.4314 0.0087  0.0031  -0.0109 415 HIS A O   
3466 C CB  . HIS A 415 ? 0.4819 0.5189 0.4150 -0.0020 -0.0009 -0.0216 415 HIS A CB  
3467 C CG  . HIS A 415 ? 0.5036 0.5356 0.4393 -0.0026 -0.0006 -0.0247 415 HIS A CG  
3468 N ND1 . HIS A 415 ? 0.4908 0.5238 0.4272 0.0018  0.0016  -0.0231 415 HIS A ND1 
3469 C CD2 . HIS A 415 ? 0.5053 0.5305 0.4428 -0.0071 -0.0017 -0.0295 415 HIS A CD2 
3470 C CE1 . HIS A 415 ? 0.5028 0.5306 0.4417 0.0000  0.0015  -0.0269 415 HIS A CE1 
3471 N NE2 . HIS A 415 ? 0.4910 0.5141 0.4307 -0.0052 -0.0004 -0.0307 415 HIS A NE2 
3472 N N   . LYS A 416 ? 0.4608 0.4952 0.3905 0.0018  -0.0005 -0.0133 416 LYS A N   
3473 C CA  . LYS A 416 ? 0.4614 0.5038 0.3887 0.0039  0.0004  -0.0100 416 LYS A CA  
3474 C C   . LYS A 416 ? 0.4516 0.4903 0.3781 0.0105  0.0042  -0.0052 416 LYS A C   
3475 O O   . LYS A 416 ? 0.4628 0.5100 0.3873 0.0147  0.0065  -0.0015 416 LYS A O   
3476 C CB  . LYS A 416 ? 0.5063 0.5442 0.4328 -0.0011 -0.0019 -0.0114 416 LYS A CB  
3477 C CG  . LYS A 416 ? 0.5492 0.6006 0.4739 -0.0048 -0.0028 -0.0128 416 LYS A CG  
3478 C CD  . LYS A 416 ? 0.5539 0.6195 0.4786 -0.0056 -0.0025 -0.0151 416 LYS A CD  
3479 C CE  . LYS A 416 ? 0.5953 0.6762 0.5184 -0.0100 -0.0031 -0.0174 416 LYS A CE  
3480 N NZ  . LYS A 416 ? 0.6004 0.6783 0.5234 -0.0188 -0.0045 -0.0236 416 LYS A NZ  
3481 N N   . PHE A 417 ? 0.4017 0.4281 0.3298 0.0115  0.0053  -0.0054 417 PHE A N   
3482 C CA  . PHE A 417 ? 0.4097 0.4287 0.3369 0.0157  0.0093  -0.0021 417 PHE A CA  
3483 C C   . PHE A 417 ? 0.4322 0.4503 0.3589 0.0212  0.0139  0.0000  417 PHE A C   
3484 O O   . PHE A 417 ? 0.4768 0.4966 0.4050 0.0208  0.0132  -0.0018 417 PHE A O   
3485 C CB  . PHE A 417 ? 0.4002 0.4061 0.3290 0.0119  0.0077  -0.0044 417 PHE A CB  
3486 C CG  . PHE A 417 ? 0.3898 0.3956 0.3183 0.0069  0.0035  -0.0061 417 PHE A CG  
3487 C CD1 . PHE A 417 ? 0.3918 0.4032 0.3178 0.0071  0.0040  -0.0041 417 PHE A CD1 
3488 C CD2 . PHE A 417 ? 0.3961 0.3964 0.3265 0.0023  -0.0003 -0.0094 417 PHE A CD2 
3489 C CE1 . PHE A 417 ? 0.3902 0.4012 0.3155 0.0021  0.0006  -0.0056 417 PHE A CE1 
3490 C CE2 . PHE A 417 ? 0.4016 0.4008 0.3309 -0.0019 -0.0035 -0.0104 417 PHE A CE2 
3491 C CZ  . PHE A 417 ? 0.3938 0.3982 0.3204 -0.0024 -0.0029 -0.0086 417 PHE A CZ  
3492 N N   . LYS A 418 ? 0.4542 0.4694 0.3786 0.0263  0.0192  0.0042  418 LYS A N   
3493 C CA  . LYS A 418 ? 0.4613 0.4730 0.3844 0.0317  0.0250  0.0069  418 LYS A CA  
3494 C C   . LYS A 418 ? 0.4691 0.4656 0.3921 0.0312  0.0294  0.0065  418 LYS A C   
3495 O O   . LYS A 418 ? 0.4805 0.4733 0.4009 0.0339  0.0337  0.0094  418 LYS A O   
3496 C CB  . LYS A 418 ? 0.4713 0.4937 0.3907 0.0393  0.0290  0.0128  418 LYS A CB  
3497 C CG  . LYS A 418 ? 0.5006 0.5176 0.4174 0.0459  0.0362  0.0169  418 LYS A CG  
3498 C CD  . LYS A 418 ? 0.5092 0.5377 0.4221 0.0548  0.0403  0.0239  418 LYS A CD  
3499 C CE  . LYS A 418 ? 0.5417 0.5660 0.4516 0.0611  0.0469  0.0278  418 LYS A CE  
3500 N NZ  . LYS A 418 ? 0.5831 0.6121 0.4881 0.0715  0.0536  0.0361  418 LYS A NZ  
3501 N N   . LEU A 419 ? 0.4644 0.4530 0.3902 0.0276  0.0287  0.0026  419 LEU A N   
3502 C CA  . LEU A 419 ? 0.4508 0.4269 0.3770 0.0254  0.0323  0.0008  419 LEU A CA  
3503 C C   . LEU A 419 ? 0.4715 0.4406 0.3956 0.0294  0.0404  0.0028  419 LEU A C   
3504 O O   . LEU A 419 ? 0.4724 0.4311 0.3955 0.0282  0.0458  0.0018  419 LEU A O   
3505 C CB  . LEU A 419 ? 0.4819 0.4546 0.4126 0.0192  0.0272  -0.0045 419 LEU A CB  
3506 C CG  . LEU A 419 ? 0.5170 0.4944 0.4496 0.0152  0.0195  -0.0065 419 LEU A CG  
3507 C CD1 . LEU A 419 ? 0.4906 0.4641 0.4274 0.0107  0.0155  -0.0110 419 LEU A CD1 
3508 C CD2 . LEU A 419 ? 0.5314 0.5083 0.4615 0.0142  0.0193  -0.0051 419 LEU A CD2 
3509 N N   . TRP A 420 ? 0.4737 0.4486 0.3967 0.0337  0.0417  0.0053  420 TRP A N   
3510 C CA  . TRP A 420 ? 0.4928 0.4609 0.4135 0.0373  0.0493  0.0071  420 TRP A CA  
3511 C C   . TRP A 420 ? 0.4870 0.4597 0.4026 0.0458  0.0546  0.0142  420 TRP A C   
3512 O O   . TRP A 420 ? 0.4896 0.4758 0.4046 0.0488  0.0510  0.0167  420 TRP A O   
3513 C CB  . TRP A 420 ? 0.4872 0.4578 0.4109 0.0353  0.0466  0.0039  420 TRP A CB  
3514 C CG  . TRP A 420 ? 0.4731 0.4413 0.4023 0.0280  0.0407  -0.0024 420 TRP A CG  
3515 C CD1 . TRP A 420 ? 0.4555 0.4305 0.3881 0.0244  0.0325  -0.0053 420 TRP A CD1 
3516 C CD2 . TRP A 420 ? 0.4695 0.4284 0.4015 0.0236  0.0429  -0.0068 420 TRP A CD2 
3517 N NE1 . TRP A 420 ? 0.4384 0.4087 0.3754 0.0193  0.0295  -0.0102 420 TRP A NE1 
3518 C CE2 . TRP A 420 ? 0.4614 0.4233 0.3986 0.0184  0.0351  -0.0115 420 TRP A CE2 
3519 C CE3 . TRP A 420 ? 0.5021 0.4508 0.4325 0.0233  0.0507  -0.0075 420 TRP A CE3 
3520 C CZ2 . TRP A 420 ? 0.4844 0.4417 0.4254 0.0138  0.0345  -0.0163 420 TRP A CZ2 
3521 C CZ3 . TRP A 420 ? 0.5140 0.4581 0.4485 0.0173  0.0503  -0.0133 420 TRP A CZ3 
3522 C CH2 . TRP A 420 ? 0.5002 0.4496 0.4400 0.0130  0.0420  -0.0175 420 TRP A CH2 
3523 N N   . ASN A 421 ? 0.4907 0.4526 0.4023 0.0497  0.0639  0.0175  421 ASN A N   
3524 C CA  . ASN A 421 ? 0.5243 0.4893 0.4304 0.0593  0.0702  0.0254  421 ASN A CA  
3525 C C   . ASN A 421 ? 0.5265 0.4807 0.4292 0.0628  0.0793  0.0276  421 ASN A C   
3526 O O   . ASN A 421 ? 0.5337 0.4722 0.4342 0.0619  0.0875  0.0270  421 ASN A O   
3527 C CB  . ASN A 421 ? 0.5517 0.5142 0.4550 0.0631  0.0742  0.0292  421 ASN A CB  
3528 C CG  . ASN A 421 ? 0.5952 0.5620 0.4928 0.0745  0.0812  0.0383  421 ASN A CG  
3529 O OD1 . ASN A 421 ? 0.6032 0.5749 0.4985 0.0797  0.0831  0.0420  421 ASN A OD1 
3530 N ND2 . ASN A 421 ? 0.6114 0.5768 0.5066 0.0790  0.0852  0.0422  421 ASN A ND2 
3531 N N   . PHE A 422 ? 0.5087 0.4712 0.4104 0.0663  0.0784  0.0299  422 PHE A N   
3532 C CA  . PHE A 422 ? 0.5102 0.4632 0.4084 0.0691  0.0865  0.0318  422 PHE A CA  
3533 C C   . PHE A 422 ? 0.5232 0.4640 0.4145 0.0769  0.0987  0.0387  422 PHE A C   
3534 O O   . PHE A 422 ? 0.5219 0.4485 0.4102 0.0772  0.1075  0.0389  422 PHE A O   
3535 C CB  . PHE A 422 ? 0.5034 0.4695 0.4008 0.0724  0.0834  0.0340  422 PHE A CB  
3536 C CG  . PHE A 422 ? 0.4985 0.4552 0.3944 0.0719  0.0893  0.0330  422 PHE A CG  
3537 C CD1 . PHE A 422 ? 0.4600 0.4111 0.3612 0.0630  0.0863  0.0248  422 PHE A CD1 
3538 C CD2 . PHE A 422 ? 0.5126 0.4659 0.4014 0.0806  0.0984  0.0407  422 PHE A CD2 
3539 C CE1 . PHE A 422 ? 0.4736 0.4168 0.3737 0.0620  0.0919  0.0235  422 PHE A CE1 
3540 C CE2 . PHE A 422 ? 0.5204 0.4641 0.4073 0.0797  0.1045  0.0397  422 PHE A CE2 
3541 C CZ  . PHE A 422 ? 0.4891 0.4281 0.3820 0.0699  0.1011  0.0307  422 PHE A CZ  
3542 N N   . ASN A 423 ? 0.5448 0.4906 0.4337 0.0831  0.0998  0.0442  423 ASN A N   
3543 C CA  . ASN A 423 ? 0.5966 0.5302 0.4788 0.0914  0.1119  0.0513  423 ASN A CA  
3544 C C   . ASN A 423 ? 0.5860 0.5017 0.4684 0.0861  0.1177  0.0471  423 ASN A C   
3545 O O   . ASN A 423 ? 0.5784 0.4797 0.4551 0.0915  0.1295  0.0517  423 ASN A O   
3546 C CB  . ASN A 423 ? 0.6485 0.5970 0.5281 0.1015  0.1109  0.0595  423 ASN A CB  
3547 C CG  . ASN A 423 ? 0.7563 0.7256 0.6356 0.1065  0.1050  0.0633  423 ASN A CG  
3548 O OD1 . ASN A 423 ? 0.8233 0.7912 0.6986 0.1113  0.1097  0.0672  423 ASN A OD1 
3549 N ND2 . ASN A 423 ? 0.7847 0.7738 0.6679 0.1048  0.0948  0.0618  423 ASN A ND2 
3550 N N   . ASN A 424 ? 0.5384 0.4553 0.4268 0.0757  0.1098  0.0388  424 ASN A N   
3551 C CA  . ASN A 424 ? 0.5033 0.4063 0.3922 0.0695  0.1140  0.0340  424 ASN A CA  
3552 C C   . ASN A 424 ? 0.4834 0.3847 0.3781 0.0578  0.1078  0.0242  424 ASN A C   
3553 O O   . ASN A 424 ? 0.4683 0.3779 0.3679 0.0520  0.0983  0.0198  424 ASN A O   
3554 C CB  . ASN A 424 ? 0.4998 0.4095 0.3891 0.0714  0.1107  0.0358  424 ASN A CB  
3555 C CG  . ASN A 424 ? 0.5057 0.3993 0.3929 0.0682  0.1189  0.0333  424 ASN A CG  
3556 O OD1 . ASN A 424 ? 0.5192 0.3963 0.4041 0.0647  0.1279  0.0303  424 ASN A OD1 
3557 N ND2 . ASN A 424 ? 0.4918 0.3904 0.3795 0.0689  0.1162  0.0342  424 ASN A ND2 
3558 N N   . GLN A 425 ? 0.4946 0.3858 0.3888 0.0546  0.1135  0.0212  425 GLN A N   
3559 C CA  . GLN A 425 ? 0.4989 0.3916 0.3991 0.0449  0.1074  0.0127  425 GLN A CA  
3560 C C   . GLN A 425 ? 0.4991 0.3814 0.4008 0.0359  0.1106  0.0053  425 GLN A C   
3561 O O   . GLN A 425 ? 0.4969 0.3649 0.3938 0.0362  0.1218  0.0059  425 GLN A O   
3562 C CB  . GLN A 425 ? 0.4902 0.3801 0.3896 0.0456  0.1111  0.0126  425 GLN A CB  
3563 C CG  . GLN A 425 ? 0.4906 0.3889 0.3865 0.0553  0.1110  0.0206  425 GLN A CG  
3564 C CD  . GLN A 425 ? 0.4941 0.3958 0.3914 0.0543  0.1097  0.0190  425 GLN A CD  
3565 O OE1 . GLN A 425 ? 0.4822 0.3780 0.3828 0.0470  0.1106  0.0123  425 GLN A OE1 
3566 N NE2 . GLN A 425 ? 0.4837 0.3961 0.3785 0.0617  0.1077  0.0251  425 GLN A NE2 
3567 N N   . ILE A 426 ? 0.4751 0.3648 0.3832 0.0279  0.1012  -0.0014 426 ILE A N   
3568 C CA  . ILE A 426 ? 0.4621 0.3468 0.3723 0.0190  0.1019  -0.0086 426 ILE A CA  
3569 C C   . ILE A 426 ? 0.4738 0.3586 0.3885 0.0118  0.1008  -0.0157 426 ILE A C   
3570 O O   . ILE A 426 ? 0.4647 0.3598 0.3841 0.0115  0.0924  -0.0167 426 ILE A O   
3571 C CB  . ILE A 426 ? 0.4538 0.3491 0.3676 0.0165  0.0911  -0.0099 426 ILE A CB  
3572 C CG1 . ILE A 426 ? 0.4481 0.3449 0.3578 0.0238  0.0919  -0.0029 426 ILE A CG1 
3573 C CG2 . ILE A 426 ? 0.4568 0.3496 0.3728 0.0071  0.0905  -0.0174 426 ILE A CG2 
3574 C CD1 . ILE A 426 ? 0.4668 0.3739 0.3792 0.0219  0.0820  -0.0035 426 ILE A CD1 
3575 N N   . SER A 427 ? 0.4988 0.3728 0.4121 0.0057  0.1099  -0.0209 427 SER A N   
3576 C CA  . SER A 427 ? 0.5230 0.3985 0.4407 -0.0008 0.1098  -0.0277 427 SER A CA  
3577 C C   . SER A 427 ? 0.5029 0.3922 0.4281 -0.0067 0.0975  -0.0333 427 SER A C   
3578 O O   . SER A 427 ? 0.4826 0.3770 0.4086 -0.0076 0.0914  -0.0331 427 SER A O   
3579 C CB  . SER A 427 ? 0.5451 0.4067 0.4596 -0.0071 0.1229  -0.0330 427 SER A CB  
3580 O OG  . SER A 427 ? 0.5779 0.4411 0.4946 -0.0160 0.1220  -0.0404 427 SER A OG  
3581 N N   . ASP A 428 ? 0.5003 0.3953 0.4307 -0.0105 0.0944  -0.0380 428 ASP A N   
3582 C CA  . ASP A 428 ? 0.5393 0.4479 0.4770 -0.0143 0.0829  -0.0421 428 ASP A CA  
3583 C C   . ASP A 428 ? 0.5574 0.4690 0.4971 -0.0222 0.0818  -0.0484 428 ASP A C   
3584 O O   . ASP A 428 ? 0.5961 0.5194 0.5412 -0.0246 0.0721  -0.0510 428 ASP A O   
3585 C CB  . ASP A 428 ? 0.5405 0.4552 0.4836 -0.0153 0.0802  -0.0451 428 ASP A CB  
3586 C CG  . ASP A 428 ? 0.5536 0.4624 0.4969 -0.0214 0.0896  -0.0512 428 ASP A CG  
3587 O OD1 . ASP A 428 ? 0.5893 0.4889 0.5285 -0.0257 0.0986  -0.0537 428 ASP A OD1 
3588 O OD2 . ASP A 428 ? 0.5421 0.4556 0.4896 -0.0225 0.0885  -0.0539 428 ASP A OD2 
3589 N N   . ASP A 429 ? 0.5627 0.4639 0.4978 -0.0262 0.0920  -0.0509 429 ASP A N   
3590 C CA  . ASP A 429 ? 0.5862 0.4910 0.5225 -0.0345 0.0917  -0.0576 429 ASP A CA  
3591 C C   . ASP A 429 ? 0.5774 0.4773 0.5087 -0.0336 0.0930  -0.0549 429 ASP A C   
3592 O O   . ASP A 429 ? 0.6133 0.5129 0.5436 -0.0407 0.0960  -0.0603 429 ASP A O   
3593 C CB  . ASP A 429 ? 0.6398 0.5397 0.5760 -0.0432 0.1018  -0.0657 429 ASP A CB  
3594 C CG  . ASP A 429 ? 0.7197 0.6005 0.6479 -0.0428 0.1170  -0.0645 429 ASP A CG  
3595 O OD1 . ASP A 429 ? 0.7061 0.5782 0.6290 -0.0350 0.1197  -0.0568 429 ASP A OD1 
3596 O OD2 . ASP A 429 ? 0.7889 0.6636 0.7161 -0.0504 0.1268  -0.0714 429 ASP A OD2 
3597 N N   . ASN A 430 ? 0.5403 0.4376 0.4686 -0.0251 0.0910  -0.0468 430 ASN A N   
3598 C CA  . ASN A 430 ? 0.5274 0.4226 0.4520 -0.0233 0.0905  -0.0436 430 ASN A CA  
3599 C C   . ASN A 430 ? 0.4895 0.3957 0.4167 -0.0186 0.0781  -0.0389 430 ASN A C   
3600 O O   . ASN A 430 ? 0.5016 0.4059 0.4256 -0.0117 0.0780  -0.0323 430 ASN A O   
3601 C CB  . ASN A 430 ? 0.5690 0.4496 0.4865 -0.0176 0.1020  -0.0384 430 ASN A CB  
3602 C CG  . ASN A 430 ? 0.6238 0.4990 0.5370 -0.0191 0.1060  -0.0384 430 ASN A CG  
3603 O OD1 . ASN A 430 ? 0.6052 0.4892 0.5204 -0.0222 0.0979  -0.0400 430 ASN A OD1 
3604 N ND2 . ASN A 430 ? 0.6232 0.4833 0.5301 -0.0167 0.1191  -0.0364 430 ASN A ND2 
3605 N N   . PRO A 431 ? 0.4559 0.3739 0.3886 -0.0222 0.0681  -0.0422 431 PRO A N   
3606 C CA  . PRO A 431 ? 0.4402 0.3669 0.3748 -0.0185 0.0573  -0.0381 431 PRO A CA  
3607 C C   . PRO A 431 ? 0.4431 0.3687 0.3738 -0.0179 0.0564  -0.0355 431 PRO A C   
3608 O O   . PRO A 431 ? 0.4673 0.3958 0.3972 -0.0129 0.0516  -0.0302 431 PRO A O   
3609 C CB  . PRO A 431 ? 0.4429 0.3806 0.3836 -0.0230 0.0489  -0.0426 431 PRO A CB  
3610 C CG  . PRO A 431 ? 0.4453 0.3820 0.3867 -0.0303 0.0548  -0.0497 431 PRO A CG  
3611 C CD  . PRO A 431 ? 0.4468 0.3711 0.3843 -0.0294 0.0666  -0.0495 431 PRO A CD  
3612 N N   . ALA A 432 ? 0.4358 0.3574 0.3641 -0.0234 0.0617  -0.0394 432 ALA A N   
3613 C CA  . ALA A 432 ? 0.4236 0.3443 0.3482 -0.0236 0.0612  -0.0377 432 ALA A CA  
3614 C C   . ALA A 432 ? 0.4216 0.3355 0.3419 -0.0160 0.0662  -0.0309 432 ALA A C   
3615 O O   . ALA A 432 ? 0.3980 0.3161 0.3172 -0.0126 0.0610  -0.0267 432 ALA A O   
3616 C CB  . ALA A 432 ? 0.4289 0.3460 0.3513 -0.0315 0.0674  -0.0439 432 ALA A CB  
3617 N N   . ARG A 433 ? 0.4255 0.3295 0.3431 -0.0130 0.0762  -0.0296 433 ARG A N   
3618 C CA  . ARG A 433 ? 0.4466 0.3456 0.3602 -0.0044 0.0810  -0.0224 433 ARG A CA  
3619 C C   . ARG A 433 ? 0.4421 0.3515 0.3582 0.0016  0.0719  -0.0172 433 ARG A C   
3620 O O   . ARG A 433 ? 0.4658 0.3788 0.3801 0.0064  0.0699  -0.0123 433 ARG A O   
3621 C CB  . ARG A 433 ? 0.4703 0.3570 0.3806 -0.0018 0.0932  -0.0216 433 ARG A CB  
3622 C CG  . ARG A 433 ? 0.4899 0.3727 0.3959 0.0084  0.0984  -0.0132 433 ARG A CG  
3623 C CD  . ARG A 433 ? 0.5286 0.3987 0.4306 0.0122  0.1106  -0.0112 433 ARG A CD  
3624 N NE  . ARG A 433 ? 0.5491 0.4208 0.4481 0.0234  0.1125  -0.0021 433 ARG A NE  
3625 C CZ  . ARG A 433 ? 0.5583 0.4237 0.4542 0.0294  0.1198  0.0021  433 ARG A CZ  
3626 N NH1 . ARG A 433 ? 0.5579 0.4133 0.4531 0.0250  0.1268  -0.0020 433 ARG A NH1 
3627 N NH2 . ARG A 433 ? 0.5812 0.4512 0.4744 0.0398  0.1204  0.0106  433 ARG A NH2 
3628 N N   . PHE A 434 ? 0.4309 0.3453 0.3511 0.0009  0.0670  -0.0187 434 PHE A N   
3629 C CA  . PHE A 434 ? 0.4320 0.3562 0.3547 0.0051  0.0585  -0.0152 434 PHE A CA  
3630 C C   . PHE A 434 ? 0.4178 0.3497 0.3415 0.0035  0.0499  -0.0148 434 PHE A C   
3631 O O   . PHE A 434 ? 0.3954 0.3325 0.3179 0.0079  0.0471  -0.0103 434 PHE A O   
3632 C CB  . PHE A 434 ? 0.4232 0.3511 0.3507 0.0029  0.0545  -0.0185 434 PHE A CB  
3633 C CG  . PHE A 434 ? 0.4126 0.3495 0.3426 0.0063  0.0467  -0.0159 434 PHE A CG  
3634 C CD1 . PHE A 434 ? 0.4202 0.3582 0.3487 0.0122  0.0492  -0.0118 434 PHE A CD1 
3635 C CD2 . PHE A 434 ? 0.4268 0.3710 0.3608 0.0033  0.0373  -0.0180 434 PHE A CD2 
3636 C CE1 . PHE A 434 ? 0.4218 0.3685 0.3525 0.0143  0.0425  -0.0105 434 PHE A CE1 
3637 C CE2 . PHE A 434 ? 0.4044 0.3554 0.3405 0.0056  0.0312  -0.0165 434 PHE A CE2 
3638 C CZ  . PHE A 434 ? 0.3883 0.3409 0.3228 0.0106  0.0338  -0.0131 434 PHE A CZ  
3639 N N   . LEU A 435 ? 0.4283 0.3616 0.3541 -0.0029 0.0461  -0.0195 435 LEU A N   
3640 C CA  . LEU A 435 ? 0.4362 0.3754 0.3621 -0.0047 0.0387  -0.0189 435 LEU A CA  
3641 C C   . LEU A 435 ? 0.4396 0.3770 0.3611 -0.0020 0.0421  -0.0153 435 LEU A C   
3642 O O   . LEU A 435 ? 0.4543 0.3976 0.3754 0.0006  0.0375  -0.0119 435 LEU A O   
3643 C CB  . LEU A 435 ? 0.4566 0.3975 0.3841 -0.0116 0.0354  -0.0240 435 LEU A CB  
3644 C CG  . LEU A 435 ? 0.4747 0.4235 0.4046 -0.0131 0.0252  -0.0238 435 LEU A CG  
3645 C CD1 . LEU A 435 ? 0.4535 0.4042 0.3826 -0.0188 0.0233  -0.0270 435 LEU A CD1 
3646 C CD2 . LEU A 435 ? 0.4524 0.4041 0.3806 -0.0093 0.0215  -0.0190 435 LEU A CD2 
3647 N N   . GLN A 436 ? 0.4361 0.3652 0.3542 -0.0029 0.0508  -0.0164 436 GLN A N   
3648 C CA  . GLN A 436 ? 0.4525 0.3792 0.3665 -0.0001 0.0551  -0.0132 436 GLN A CA  
3649 C C   . GLN A 436 ? 0.4619 0.3914 0.3746 0.0082  0.0568  -0.0068 436 GLN A C   
3650 O O   . GLN A 436 ? 0.4925 0.4275 0.4039 0.0109  0.0545  -0.0035 436 GLN A O   
3651 C CB  . GLN A 436 ? 0.4742 0.3898 0.3847 -0.0024 0.0657  -0.0157 436 GLN A CB  
3652 C CG  . GLN A 436 ? 0.4968 0.4119 0.4079 -0.0114 0.0645  -0.0224 436 GLN A CG  
3653 C CD  . GLN A 436 ? 0.5574 0.4613 0.4659 -0.0151 0.0757  -0.0268 436 GLN A CD  
3654 O OE1 . GLN A 436 ? 0.6129 0.5075 0.5190 -0.0105 0.0848  -0.0244 436 GLN A OE1 
3655 N NE2 . GLN A 436 ? 0.5512 0.4558 0.4599 -0.0237 0.0755  -0.0334 436 GLN A NE2 
3656 N N   . LYS A 437 ? 0.4468 0.3735 0.3595 0.0124  0.0609  -0.0049 437 LYS A N   
3657 C CA  . LYS A 437 ? 0.4714 0.4030 0.3826 0.0209  0.0623  0.0013  437 LYS A CA  
3658 C C   . LYS A 437 ? 0.4375 0.3826 0.3515 0.0210  0.0519  0.0025  437 LYS A C   
3659 O O   . LYS A 437 ? 0.4670 0.4197 0.3797 0.0255  0.0509  0.0066  437 LYS A O   
3660 C CB  . LYS A 437 ? 0.4961 0.4229 0.4067 0.0250  0.0682  0.0030  437 LYS A CB  
3661 C CG  . LYS A 437 ? 0.5278 0.4594 0.4357 0.0347  0.0715  0.0103  437 LYS A CG  
3662 C CD  . LYS A 437 ? 0.6010 0.5281 0.5079 0.0382  0.0766  0.0118  437 LYS A CD  
3663 C CE  . LYS A 437 ? 0.6651 0.6041 0.5714 0.0459  0.0742  0.0177  437 LYS A CE  
3664 N NZ  . LYS A 437 ? 0.7463 0.6846 0.6476 0.0556  0.0823  0.0252  437 LYS A NZ  
3665 N N   . ALA A 438 ? 0.4126 0.3606 0.3303 0.0157  0.0445  -0.0014 438 ALA A N   
3666 C CA  . ALA A 438 ? 0.3989 0.3573 0.3188 0.0149  0.0357  -0.0011 438 ALA A CA  
3667 C C   . ALA A 438 ? 0.4178 0.3801 0.3365 0.0127  0.0322  -0.0007 438 ALA A C   
3668 O O   . ALA A 438 ? 0.4151 0.3864 0.3339 0.0138  0.0278  0.0010  438 ALA A O   
3669 C CB  . ALA A 438 ? 0.3777 0.3365 0.3016 0.0103  0.0297  -0.0052 438 ALA A CB  
3670 N N   . MET A 439 ? 0.4323 0.3885 0.3496 0.0091  0.0344  -0.0027 439 MET A N   
3671 C CA  . MET A 439 ? 0.4636 0.4230 0.3793 0.0067  0.0314  -0.0025 439 MET A CA  
3672 C C   . MET A 439 ? 0.4863 0.4469 0.3987 0.0116  0.0372  0.0013  439 MET A C   
3673 O O   . MET A 439 ? 0.4929 0.4570 0.4040 0.0099  0.0352  0.0017  439 MET A O   
3674 C CB  . MET A 439 ? 0.4271 0.3816 0.3426 0.0000  0.0297  -0.0067 439 MET A CB  
3675 C CG  . MET A 439 ? 0.4346 0.3912 0.3534 -0.0039 0.0224  -0.0095 439 MET A CG  
3676 S SD  . MET A 439 ? 0.4536 0.4183 0.3731 -0.0045 0.0138  -0.0078 439 MET A SD  
3677 C CE  . MET A 439 ? 0.4136 0.3824 0.3361 -0.0005 0.0126  -0.0067 439 MET A CE  
3678 N N   . ASP A 440 ? 0.5018 0.4595 0.4128 0.0178  0.0445  0.0044  440 ASP A N   
3679 C CA  . ASP A 440 ? 0.5630 0.5234 0.4713 0.0247  0.0503  0.0094  440 ASP A CA  
3680 C C   . ASP A 440 ? 0.5925 0.5677 0.5017 0.0269  0.0445  0.0121  440 ASP A C   
3681 O O   . ASP A 440 ? 0.5368 0.5200 0.4482 0.0261  0.0385  0.0116  440 ASP A O   
3682 C CB  . ASP A 440 ? 0.5699 0.5258 0.4766 0.0323  0.0584  0.0133  440 ASP A CB  
3683 C CG  . ASP A 440 ? 0.5981 0.5381 0.5021 0.0316  0.0682  0.0117  440 ASP A CG  
3684 O OD1 . ASP A 440 ? 0.6233 0.5572 0.5263 0.0262  0.0696  0.0081  440 ASP A OD1 
3685 O OD2 . ASP A 440 ? 0.6429 0.5764 0.5453 0.0364  0.0753  0.0140  440 ASP A OD2 
3686 N N   . PHE A 441 ? 0.6500 0.6290 0.5573 0.0297  0.0473  0.0146  441 PHE A N   
3687 C CA  . PHE A 441 ? 0.7465 0.7400 0.6544 0.0303  0.0424  0.0162  441 PHE A CA  
3688 C C   . PHE A 441 ? 0.7925 0.8008 0.7016 0.0360  0.0406  0.0197  441 PHE A C   
3689 O O   . PHE A 441 ? 0.8099 0.8294 0.7206 0.0325  0.0338  0.0181  441 PHE A O   
3690 C CB  . PHE A 441 ? 0.8287 0.8222 0.7343 0.0325  0.0472  0.0180  441 PHE A CB  
3691 C CG  . PHE A 441 ? 0.8966 0.9062 0.8030 0.0336  0.0436  0.0198  441 PHE A CG  
3692 C CD1 . PHE A 441 ? 0.8951 0.9090 0.8022 0.0258  0.0366  0.0162  441 PHE A CD1 
3693 C CD2 . PHE A 441 ? 0.9331 0.9537 0.8390 0.0427  0.0478  0.0252  441 PHE A CD2 
3694 C CE1 . PHE A 441 ? 0.9049 0.9335 0.8125 0.0259  0.0340  0.0172  441 PHE A CE1 
3695 C CE2 . PHE A 441 ? 0.9371 0.9745 0.8440 0.0433  0.0446  0.0263  441 PHE A CE2 
3696 C CZ  . PHE A 441 ? 0.9229 0.9641 0.8307 0.0344  0.0378  0.0219  441 PHE A CZ  
3697 N N   . PRO A 442 ? 0.8071 0.8157 0.7149 0.0446  0.0469  0.0244  442 PRO A N   
3698 C CA  . PRO A 442 ? 0.8374 0.8634 0.7456 0.0511  0.0458  0.0286  442 PRO A CA  
3699 C C   . PRO A 442 ? 0.8236 0.8612 0.7344 0.0461  0.0374  0.0254  442 PRO A C   
3700 O O   . PRO A 442 ? 0.8667 0.9218 0.7782 0.0473  0.0344  0.0265  442 PRO A O   
3701 C CB  . PRO A 442 ? 0.8109 0.8310 0.7170 0.0597  0.0534  0.0334  442 PRO A CB  
3702 C CG  . PRO A 442 ? 0.8252 0.8271 0.7289 0.0600  0.0612  0.0333  442 PRO A CG  
3703 C CD  . PRO A 442 ? 0.8408 0.8344 0.7462 0.0489  0.0560  0.0263  442 PRO A CD  
3704 N N   . PHE A 443 ? 0.7975 0.8261 0.7097 0.0404  0.0341  0.0213  443 PHE A N   
3705 C CA  . PHE A 443 ? 0.8333 0.8705 0.7478 0.0357  0.0272  0.0180  443 PHE A CA  
3706 C C   . PHE A 443 ? 0.8172 0.8624 0.7326 0.0290  0.0213  0.0147  443 PHE A C   
3707 O O   . PHE A 443 ? 0.8408 0.8987 0.7572 0.0267  0.0173  0.0131  443 PHE A O   
3708 C CB  . PHE A 443 ? 0.8082 0.8325 0.7242 0.0312  0.0254  0.0142  443 PHE A CB  
3709 C CG  . PHE A 443 ? 0.7639 0.7794 0.6811 0.0231  0.0211  0.0096  443 PHE A CG  
3710 C CD1 . PHE A 443 ? 0.7335 0.7375 0.6496 0.0217  0.0240  0.0091  443 PHE A CD1 
3711 C CD2 . PHE A 443 ? 0.7439 0.7630 0.6629 0.0170  0.0146  0.0059  443 PHE A CD2 
3712 C CE1 . PHE A 443 ? 0.7096 0.7072 0.6262 0.0147  0.0198  0.0054  443 PHE A CE1 
3713 C CE2 . PHE A 443 ? 0.7202 0.7312 0.6395 0.0106  0.0110  0.0027  443 PHE A CE2 
3714 C CZ  . PHE A 443 ? 0.7371 0.7383 0.6553 0.0096  0.0132  0.0027  443 PHE A CZ  
3715 N N   . ILE A 444 ? 0.8024 0.8402 0.7171 0.0253  0.0212  0.0134  444 ILE A N   
3716 C CA  . ILE A 444 ? 0.8425 0.8848 0.7574 0.0181  0.0161  0.0102  444 ILE A CA  
3717 C C   . ILE A 444 ? 0.8690 0.9234 0.7828 0.0206  0.0179  0.0126  444 ILE A C   
3718 O O   . ILE A 444 ? 0.8762 0.9339 0.7896 0.0150  0.0149  0.0103  444 ILE A O   
3719 C CB  . ILE A 444 ? 0.7684 0.7954 0.6829 0.0115  0.0139  0.0070  444 ILE A CB  
3720 C CG1 . ILE A 444 ? 0.7708 0.8005 0.6848 0.0041  0.0088  0.0040  444 ILE A CG1 
3721 C CG2 . ILE A 444 ? 0.7658 0.7836 0.6786 0.0136  0.0189  0.0085  444 ILE A CG2 
3722 C CD1 . ILE A 444 ? 0.6780 0.7072 0.5933 -0.0007 0.0040  0.0007  444 ILE A CD1 
3723 N N   . CYS A 445 ? 0.8858 0.9471 0.7990 0.0295  0.0231  0.0175  445 CYS A N   
3724 C CA  . CYS A 445 ? 0.9302 1.0024 0.8427 0.0338  0.0261  0.0206  445 CYS A CA  
3725 C C   . CYS A 445 ? 0.9260 1.0175 0.8396 0.0300  0.0217  0.0187  445 CYS A C   
3726 O O   . CYS A 445 ? 0.9032 0.9999 0.8164 0.0286  0.0221  0.0186  445 CYS A O   
3727 C CB  . CYS A 445 ? 0.9963 1.0721 0.9077 0.0455  0.0332  0.0271  445 CYS A CB  
3728 S SG  . CYS A 445 ? 1.0300 1.1262 0.9421 0.0528  0.0327  0.0308  445 CYS A SG  
3729 N N   . ASN A 446 ? 0.8906 0.9925 0.8055 0.0276  0.0178  0.0166  446 ASN A N   
3730 C CA  . ASN A 446 ? 0.8678 0.9887 0.7836 0.0226  0.0141  0.0136  446 ASN A CA  
3731 C C   . ASN A 446 ? 0.8469 0.9605 0.7624 0.0112  0.0097  0.0076  446 ASN A C   
3732 O O   . ASN A 446 ? 0.8502 0.9764 0.7661 0.0051  0.0068  0.0039  446 ASN A O   
3733 C CB  . ASN A 446 ? 0.8656 1.0030 0.7825 0.0248  0.0127  0.0135  446 ASN A CB  
3734 C CG  . ASN A 446 ? 0.8817 1.0399 0.7987 0.0347  0.0159  0.0190  446 ASN A CG  
3735 O OD1 . ASN A 446 ? 0.8509 1.0225 0.7683 0.0358  0.0167  0.0200  446 ASN A OD1 
3736 N ND2 . ASN A 446 ? 0.8338 0.9958 0.7504 0.0423  0.0180  0.0229  446 ASN A ND2 
3737 N N   . SER A 447 ? 0.8183 0.9117 0.7327 0.0083  0.0095  0.0069  447 SER A N   
3738 C CA  . SER A 447 ? 0.7759 0.8605 0.6892 -0.0009 0.0063  0.0028  447 SER A CA  
3739 C C   . SER A 447 ? 0.7853 0.8649 0.6969 -0.0005 0.0086  0.0044  447 SER A C   
3740 O O   . SER A 447 ? 0.8079 0.8813 0.7178 -0.0073 0.0066  0.0019  447 SER A O   
3741 C CB  . SER A 447 ? 0.7958 0.8624 0.7090 -0.0040 0.0041  0.0009  447 SER A CB  
3742 O OG  . SER A 447 ? 0.8134 0.8779 0.7262 -0.0119 0.0004  -0.0032 447 SER A OG  
3743 N N   . PHE A 448 ? 0.7439 0.8259 0.6556 0.0077  0.0133  0.0086  448 PHE A N   
3744 C CA  . PHE A 448 ? 0.7288 0.8045 0.6389 0.0091  0.0167  0.0102  448 PHE A CA  
3745 C C   . PHE A 448 ? 0.6637 0.7560 0.5744 0.0151  0.0203  0.0134  448 PHE A C   
3746 O O   . PHE A 448 ? 0.6744 0.7636 0.5846 0.0224  0.0259  0.0172  448 PHE A O   
3747 C CB  . PHE A 448 ? 0.7859 0.8451 0.6952 0.0134  0.0207  0.0122  448 PHE A CB  
3748 C CG  . PHE A 448 ? 0.7575 0.8000 0.6653 0.0066  0.0186  0.0091  448 PHE A CG  
3749 C CD1 . PHE A 448 ? 0.7793 0.8165 0.6875 0.0006  0.0133  0.0060  448 PHE A CD1 
3750 C CD2 . PHE A 448 ? 0.7639 0.7963 0.6697 0.0065  0.0223  0.0094  448 PHE A CD2 
3751 C CE1 . PHE A 448 ? 0.7472 0.7709 0.6540 -0.0046 0.0112  0.0038  448 PHE A CE1 
3752 C CE2 . PHE A 448 ? 0.7528 0.7721 0.6570 0.0003  0.0202  0.0065  448 PHE A CE2 
3753 C CZ  . PHE A 448 ? 0.7589 0.7745 0.6636 -0.0048 0.0144  0.0040  448 PHE A CZ  
3754 N N   . THR A 449 ? 0.6062 0.7164 0.5181 0.0119  0.0176  0.0116  449 THR A N   
3755 C CA  . THR A 449 ? 0.5906 0.7209 0.5038 0.0178  0.0203  0.0144  449 THR A CA  
3756 C C   . THR A 449 ? 0.5874 0.7226 0.4999 0.0117  0.0198  0.0119  449 THR A C   
3757 O O   . THR A 449 ? 0.5766 0.6985 0.4871 0.0031  0.0174  0.0083  449 THR A O   
3758 C CB  . THR A 449 ? 0.5808 0.7329 0.4961 0.0191  0.0181  0.0140  449 THR A CB  
3759 O OG1 . THR A 449 ? 0.5717 0.7294 0.4870 0.0080  0.0134  0.0080  449 THR A OG1 
3760 C CG2 . THR A 449 ? 0.5715 0.7182 0.4870 0.0233  0.0179  0.0157  449 THR A CG2 
3761 N N   . LYS A 450 ? 0.5824 0.7377 0.4966 0.0164  0.0221  0.0139  450 LYS A N   
3762 C CA  . LYS A 450 ? 0.5641 0.7279 0.4780 0.0110  0.0219  0.0114  450 LYS A CA  
3763 C C   . LYS A 450 ? 0.5236 0.6928 0.4372 -0.0008 0.0168  0.0052  450 LYS A C   
3764 O O   . LYS A 450 ? 0.5131 0.6804 0.4251 -0.0086 0.0160  0.0020  450 LYS A O   
3765 C CB  . LYS A 450 ? 0.6186 0.8066 0.5352 0.0193  0.0252  0.0149  450 LYS A CB  
3766 C CG  . LYS A 450 ? 0.6788 0.8705 0.5964 0.0333  0.0299  0.0218  450 LYS A CG  
3767 C CD  . LYS A 450 ? 0.6978 0.9152 0.6181 0.0420  0.0331  0.0257  450 LYS A CD  
3768 C CE  . LYS A 450 ? 0.7127 0.9564 0.6355 0.0453  0.0305  0.0265  450 LYS A CE  
3769 N NZ  . LYS A 450 ? 0.7734 1.0123 0.6955 0.0548  0.0323  0.0317  450 LYS A NZ  
3770 N N   . PHE A 451 ? 0.5056 0.6814 0.4203 -0.0023 0.0140  0.0035  451 PHE A N   
3771 C CA  . PHE A 451 ? 0.5108 0.6900 0.4248 -0.0138 0.0102  -0.0027 451 PHE A CA  
3772 C C   . PHE A 451 ? 0.5085 0.6625 0.4191 -0.0218 0.0083  -0.0053 451 PHE A C   
3773 O O   . PHE A 451 ? 0.5026 0.6551 0.4113 -0.0314 0.0071  -0.0095 451 PHE A O   
3774 C CB  . PHE A 451 ? 0.5258 0.7154 0.4414 -0.0135 0.0082  -0.0041 451 PHE A CB  
3775 C CG  . PHE A 451 ? 0.5648 0.7852 0.4829 -0.0129 0.0083  -0.0055 451 PHE A CG  
3776 C CD1 . PHE A 451 ? 0.5721 0.8055 0.4901 -0.0227 0.0076  -0.0111 451 PHE A CD1 
3777 C CD2 . PHE A 451 ? 0.5793 0.8166 0.4997 -0.0030 0.0092  -0.0014 451 PHE A CD2 
3778 C CE1 . PHE A 451 ? 0.5912 0.8556 0.5119 -0.0229 0.0076  -0.0131 451 PHE A CE1 
3779 C CE2 . PHE A 451 ? 0.5677 0.8362 0.4905 -0.0023 0.0089  -0.0027 451 PHE A CE2 
3780 C CZ  . PHE A 451 ? 0.5732 0.8560 0.4964 -0.0126 0.0079  -0.0089 451 PHE A CZ  
3781 N N   . GLU A 452 ? 0.5007 0.6356 0.4105 -0.0178 0.0085  -0.0026 452 GLU A N   
3782 C CA  . GLU A 452 ? 0.5063 0.6190 0.4131 -0.0241 0.0065  -0.0044 452 GLU A CA  
3783 C C   . GLU A 452 ? 0.4881 0.5918 0.3923 -0.0259 0.0080  -0.0037 452 GLU A C   
3784 O O   . GLU A 452 ? 0.4600 0.5536 0.3611 -0.0337 0.0062  -0.0061 452 GLU A O   
3785 C CB  . GLU A 452 ? 0.5304 0.6281 0.4376 -0.0200 0.0058  -0.0026 452 GLU A CB  
3786 C CG  . GLU A 452 ? 0.5879 0.6892 0.4966 -0.0216 0.0034  -0.0049 452 GLU A CG  
3787 C CD  . GLU A 452 ? 0.5941 0.7134 0.5056 -0.0142 0.0049  -0.0027 452 GLU A CD  
3788 O OE1 . GLU A 452 ? 0.6327 0.7593 0.5453 -0.0162 0.0032  -0.0051 452 GLU A OE1 
3789 O OE2 . GLU A 452 ? 0.5792 0.7054 0.4916 -0.0061 0.0081  0.0014  452 GLU A OE2 
3790 N N   . PHE A 453 ? 0.4772 0.5845 0.3823 -0.0185 0.0117  -0.0001 453 PHE A N   
3791 C CA  . PHE A 453 ? 0.4697 0.5652 0.3722 -0.0194 0.0138  0.0006  453 PHE A CA  
3792 C C   . PHE A 453 ? 0.4670 0.5740 0.3690 -0.0209 0.0160  0.0002  453 PHE A C   
3793 O O   . PHE A 453 ? 0.4853 0.5830 0.3847 -0.0231 0.0176  0.0001  453 PHE A O   
3794 C CB  . PHE A 453 ? 0.4775 0.5625 0.3802 -0.0112 0.0175  0.0042  453 PHE A CB  
3795 C CG  . PHE A 453 ? 0.5037 0.5730 0.4059 -0.0119 0.0153  0.0038  453 PHE A CG  
3796 C CD1 . PHE A 453 ? 0.5163 0.5703 0.4156 -0.0183 0.0129  0.0019  453 PHE A CD1 
3797 C CD2 . PHE A 453 ? 0.5202 0.5912 0.4249 -0.0060 0.0158  0.0056  453 PHE A CD2 
3798 C CE1 . PHE A 453 ? 0.5262 0.5678 0.4255 -0.0187 0.0108  0.0015  453 PHE A CE1 
3799 C CE2 . PHE A 453 ? 0.5248 0.5822 0.4293 -0.0069 0.0139  0.0049  453 PHE A CE2 
3800 C CZ  . PHE A 453 ? 0.5323 0.5755 0.4344 -0.0132 0.0114  0.0028  453 PHE A CZ  
3801 N N   . ASN A 454 ? 0.4442 0.5726 0.3489 -0.0201 0.0163  -0.0004 454 ASN A N   
3802 C CA  . ASN A 454 ? 0.4424 0.5840 0.3473 -0.0216 0.0185  -0.0011 454 ASN A CA  
3803 C C   . ASN A 454 ? 0.4475 0.5817 0.3486 -0.0332 0.0165  -0.0052 454 ASN A C   
3804 O O   . ASN A 454 ? 0.4331 0.5592 0.3321 -0.0404 0.0132  -0.0081 454 ASN A O   
3805 C CB  . ASN A 454 ? 0.4499 0.6189 0.3588 -0.0187 0.0188  -0.0014 454 ASN A CB  
3806 C CG  . ASN A 454 ? 0.4346 0.6124 0.3432 -0.0292 0.0153  -0.0069 454 ASN A CG  
3807 O OD1 . ASN A 454 ? 0.4448 0.6289 0.3521 -0.0369 0.0155  -0.0104 454 ASN A OD1 
3808 N ND2 . ASN A 454 ? 0.4209 0.5975 0.3301 -0.0301 0.0127  -0.0081 454 ASN A ND2 
3809 N N   . THR A 455 ? 0.4572 0.5934 0.3569 -0.0346 0.0191  -0.0053 455 THR A N   
3810 C CA  . THR A 455 ? 0.4838 0.6182 0.3800 -0.0454 0.0180  -0.0092 455 THR A CA  
3811 C C   . THR A 455 ? 0.5010 0.6582 0.3994 -0.0468 0.0202  -0.0110 455 THR A C   
3812 O O   . THR A 455 ? 0.5273 0.6838 0.4232 -0.0521 0.0217  -0.0126 455 THR A O   
3813 C CB  . THR A 455 ? 0.4738 0.5879 0.3649 -0.0488 0.0184  -0.0087 455 THR A CB  
3814 O OG1 . THR A 455 ? 0.4948 0.6071 0.3869 -0.0409 0.0222  -0.0055 455 THR A OG1 
3815 C CG2 . THR A 455 ? 0.4805 0.5745 0.3687 -0.0512 0.0149  -0.0084 455 THR A CG2 
3816 N N   . VAL A 456 ? 0.5019 0.6804 0.4052 -0.0420 0.0204  -0.0108 456 VAL A N   
3817 C CA  . VAL A 456 ? 0.4931 0.6977 0.3993 -0.0437 0.0219  -0.0131 456 VAL A CA  
3818 C C   . VAL A 456 ? 0.4805 0.6910 0.3854 -0.0558 0.0194  -0.0193 456 VAL A C   
3819 O O   . VAL A 456 ? 0.4440 0.6535 0.3460 -0.0655 0.0201  -0.0231 456 VAL A O   
3820 C CB  . VAL A 456 ? 0.5185 0.7456 0.4304 -0.0319 0.0234  -0.0095 456 VAL A CB  
3821 C CG1 . VAL A 456 ? 0.5052 0.7624 0.4207 -0.0332 0.0248  -0.0119 456 VAL A CG1 
3822 C CG2 . VAL A 456 ? 0.5221 0.7396 0.4346 -0.0198 0.0271  -0.0032 456 VAL A CG2 
3823 N N   . PHE A 457 ? 0.4634 0.6784 0.3699 -0.0557 0.0170  -0.0204 457 PHE A N   
3824 C CA  . PHE A 457 ? 0.4762 0.6913 0.3806 -0.0676 0.0154  -0.0266 457 PHE A CA  
3825 C C   . PHE A 457 ? 0.4945 0.6800 0.3937 -0.0731 0.0135  -0.0271 457 PHE A C   
3826 O O   . PHE A 457 ? 0.5206 0.6987 0.4160 -0.0840 0.0136  -0.0315 457 PHE A O   
3827 C CB  . PHE A 457 ? 0.4587 0.6973 0.3672 -0.0668 0.0144  -0.0291 457 PHE A CB  
3828 C CG  . PHE A 457 ? 0.4603 0.6980 0.3714 -0.0557 0.0130  -0.0242 457 PHE A CG  
3829 C CD1 . PHE A 457 ? 0.4538 0.6746 0.3632 -0.0575 0.0107  -0.0249 457 PHE A CD1 
3830 C CD2 . PHE A 457 ? 0.4597 0.7140 0.3751 -0.0432 0.0144  -0.0190 457 PHE A CD2 
3831 C CE1 . PHE A 457 ? 0.4494 0.6696 0.3610 -0.0477 0.0098  -0.0207 457 PHE A CE1 
3832 C CE2 . PHE A 457 ? 0.4553 0.7081 0.3724 -0.0331 0.0138  -0.0143 457 PHE A CE2 
3833 C CZ  . PHE A 457 ? 0.4451 0.6811 0.3604 -0.0357 0.0114  -0.0154 457 PHE A CZ  
3834 N N   . ASN A 458 ? 0.4856 0.6550 0.3848 -0.0653 0.0121  -0.0224 458 ASN A N   
3835 C CA  . ASN A 458 ? 0.4873 0.6303 0.3822 -0.0689 0.0102  -0.0222 458 ASN A CA  
3836 C C   . ASN A 458 ? 0.4850 0.6103 0.3749 -0.0725 0.0108  -0.0210 458 ASN A C   
3837 O O   . ASN A 458 ? 0.5140 0.6397 0.4042 -0.0674 0.0123  -0.0181 458 ASN A O   
3838 C CB  . ASN A 458 ? 0.4575 0.5912 0.3544 -0.0596 0.0087  -0.0180 458 ASN A CB  
3839 C CG  . ASN A 458 ? 0.4631 0.6028 0.3624 -0.0594 0.0070  -0.0198 458 ASN A CG  
3840 O OD1 . ASN A 458 ? 0.4759 0.6252 0.3750 -0.0670 0.0069  -0.0247 458 ASN A OD1 
3841 N ND2 . ASN A 458 ? 0.4264 0.5605 0.3277 -0.0512 0.0061  -0.0164 458 ASN A ND2 
3842 N N   . ASP A 459 ? 0.4931 0.6022 0.3780 -0.0807 0.0099  -0.0230 459 ASP A N   
3843 C CA  . ASP A 459 ? 0.5068 0.5965 0.3862 -0.0828 0.0097  -0.0208 459 ASP A CA  
3844 C C   . ASP A 459 ? 0.4937 0.5690 0.3734 -0.0752 0.0078  -0.0164 459 ASP A C   
3845 O O   . ASP A 459 ? 0.4805 0.5565 0.3638 -0.0695 0.0064  -0.0154 459 ASP A O   
3846 C CB  . ASP A 459 ? 0.5332 0.6085 0.4066 -0.0925 0.0096  -0.0231 459 ASP A CB  
3847 C CG  . ASP A 459 ? 0.5832 0.6697 0.4549 -0.1018 0.0125  -0.0278 459 ASP A CG  
3848 O OD1 . ASP A 459 ? 0.5993 0.6913 0.4696 -0.1036 0.0144  -0.0278 459 ASP A OD1 
3849 O OD2 . ASP A 459 ? 0.5972 0.6868 0.4688 -0.1079 0.0134  -0.0319 459 ASP A OD2 
3850 N N   . GLN A 460 ? 0.4878 0.5505 0.3634 -0.0757 0.0078  -0.0143 460 GLN A N   
3851 C CA  . GLN A 460 ? 0.4847 0.5340 0.3599 -0.0702 0.0063  -0.0111 460 GLN A CA  
3852 C C   . GLN A 460 ? 0.4672 0.5029 0.3410 -0.0713 0.0032  -0.0108 460 GLN A C   
3853 O O   . GLN A 460 ? 0.4551 0.4863 0.3316 -0.0656 0.0017  -0.0091 460 GLN A O   
3854 C CB  . GLN A 460 ? 0.5036 0.5445 0.3740 -0.0720 0.0072  -0.0097 460 GLN A CB  
3855 C CG  . GLN A 460 ? 0.4936 0.5224 0.3632 -0.0677 0.0059  -0.0072 460 GLN A CG  
3856 C CD  . GLN A 460 ? 0.5008 0.5251 0.3659 -0.0698 0.0074  -0.0066 460 GLN A CD  
3857 O OE1 . GLN A 460 ? 0.5048 0.5381 0.3705 -0.0697 0.0107  -0.0074 460 GLN A OE1 
3858 N NE2 . GLN A 460 ? 0.4833 0.4946 0.3439 -0.0716 0.0052  -0.0053 460 GLN A NE2 
3859 N N   . ARG A 461 ? 0.4734 0.5026 0.3431 -0.0786 0.0028  -0.0124 461 ARG A N   
3860 C CA  . ARG A 461 ? 0.4877 0.5039 0.3561 -0.0793 0.0006  -0.0120 461 ARG A CA  
3861 C C   . ARG A 461 ? 0.4727 0.4964 0.3468 -0.0757 0.0000  -0.0135 461 ARG A C   
3862 O O   . ARG A 461 ? 0.4915 0.5065 0.3668 -0.0724 -0.0019 -0.0123 461 ARG A O   
3863 C CB  . ARG A 461 ? 0.5197 0.5265 0.3819 -0.0877 0.0017  -0.0133 461 ARG A CB  
3864 C CG  . ARG A 461 ? 0.5557 0.5741 0.4184 -0.0945 0.0046  -0.0180 461 ARG A CG  
3865 C CD  . ARG A 461 ? 0.5843 0.5918 0.4395 -0.1033 0.0070  -0.0190 461 ARG A CD  
3866 N NE  . ARG A 461 ? 0.6426 0.6527 0.4972 -0.1105 0.0099  -0.0239 461 ARG A NE  
3867 C CZ  . ARG A 461 ? 0.6685 0.6891 0.5219 -0.1183 0.0134  -0.0282 461 ARG A CZ  
3868 N NH1 . ARG A 461 ? 0.7148 0.7443 0.5676 -0.1193 0.0143  -0.0279 461 ARG A NH1 
3869 N NH2 . ARG A 461 ? 0.6696 0.6920 0.5224 -0.1257 0.0164  -0.0334 461 ARG A NH2 
3870 N N   . THR A 462 ? 0.4558 0.4970 0.3334 -0.0761 0.0017  -0.0161 462 THR A N   
3871 C CA  . THR A 462 ? 0.4410 0.4928 0.3239 -0.0723 0.0013  -0.0173 462 THR A CA  
3872 C C   . THR A 462 ? 0.4156 0.4682 0.3025 -0.0625 0.0005  -0.0138 462 THR A C   
3873 O O   . THR A 462 ? 0.4002 0.4496 0.2896 -0.0589 -0.0008 -0.0134 462 THR A O   
3874 C CB  . THR A 462 ? 0.4404 0.5135 0.3257 -0.0754 0.0034  -0.0209 462 THR A CB  
3875 O OG1 . THR A 462 ? 0.4585 0.5286 0.3398 -0.0856 0.0048  -0.0250 462 THR A OG1 
3876 C CG2 . THR A 462 ? 0.4259 0.5129 0.3164 -0.0707 0.0029  -0.0218 462 THR A CG2 
3877 N N   . VAL A 463 ? 0.3973 0.4532 0.2845 -0.0586 0.0019  -0.0116 463 VAL A N   
3878 C CA  . VAL A 463 ? 0.3965 0.4507 0.2865 -0.0500 0.0025  -0.0085 463 VAL A CA  
3879 C C   . VAL A 463 ? 0.3986 0.4354 0.2874 -0.0490 0.0001  -0.0072 463 VAL A C   
3880 O O   . VAL A 463 ? 0.3863 0.4217 0.2782 -0.0440 -0.0004 -0.0063 463 VAL A O   
3881 C CB  . VAL A 463 ? 0.3979 0.4548 0.2872 -0.0473 0.0054  -0.0067 463 VAL A CB  
3882 C CG1 . VAL A 463 ? 0.4147 0.4650 0.3056 -0.0398 0.0068  -0.0040 463 VAL A CG1 
3883 C CG2 . VAL A 463 ? 0.4007 0.4777 0.2927 -0.0458 0.0079  -0.0074 463 VAL A CG2 
3884 N N   . PHE A 464 ? 0.4043 0.4289 0.2884 -0.0539 -0.0012 -0.0071 464 PHE A N   
3885 C CA  . PHE A 464 ? 0.4090 0.4190 0.2917 -0.0534 -0.0038 -0.0059 464 PHE A CA  
3886 C C   . PHE A 464 ? 0.4173 0.4244 0.3022 -0.0531 -0.0057 -0.0068 464 PHE A C   
3887 O O   . PHE A 464 ? 0.4032 0.4048 0.2904 -0.0489 -0.0070 -0.0059 464 PHE A O   
3888 C CB  . PHE A 464 ? 0.4129 0.4126 0.2896 -0.0587 -0.0050 -0.0051 464 PHE A CB  
3889 C CG  . PHE A 464 ? 0.4304 0.4301 0.3047 -0.0585 -0.0035 -0.0041 464 PHE A CG  
3890 C CD1 . PHE A 464 ? 0.4285 0.4323 0.3059 -0.0531 -0.0014 -0.0036 464 PHE A CD1 
3891 C CD2 . PHE A 464 ? 0.4430 0.4378 0.3114 -0.0640 -0.0036 -0.0036 464 PHE A CD2 
3892 C CE1 . PHE A 464 ? 0.4302 0.4331 0.3052 -0.0534 0.0006  -0.0032 464 PHE A CE1 
3893 C CE2 . PHE A 464 ? 0.4447 0.4399 0.3107 -0.0642 -0.0021 -0.0031 464 PHE A CE2 
3894 C CZ  . PHE A 464 ? 0.4447 0.4438 0.3141 -0.0591 0.0000  -0.0031 464 PHE A CZ  
3895 N N   . ALA A 465 ? 0.4152 0.4260 0.2994 -0.0579 -0.0054 -0.0093 465 ALA A N   
3896 C CA  . ALA A 465 ? 0.4185 0.4270 0.3046 -0.0582 -0.0064 -0.0109 465 ALA A CA  
3897 C C   . ALA A 465 ? 0.4113 0.4299 0.3030 -0.0521 -0.0061 -0.0110 465 ALA A C   
3898 O O   . ALA A 465 ? 0.3952 0.4083 0.2891 -0.0488 -0.0074 -0.0106 465 ALA A O   
3899 C CB  . ALA A 465 ? 0.4107 0.4222 0.2946 -0.0656 -0.0049 -0.0145 465 ALA A CB  
3900 N N   . ASN A 466 ? 0.4204 0.4545 0.3141 -0.0503 -0.0042 -0.0114 466 ASN A N   
3901 C CA  . ASN A 466 ? 0.4137 0.4575 0.3119 -0.0433 -0.0034 -0.0103 466 ASN A CA  
3902 C C   . ASN A 466 ? 0.3981 0.4314 0.2973 -0.0373 -0.0037 -0.0074 466 ASN A C   
3903 O O   . ASN A 466 ? 0.4092 0.4409 0.3110 -0.0336 -0.0042 -0.0071 466 ASN A O   
3904 C CB  . ASN A 466 ? 0.4130 0.4745 0.3127 -0.0407 -0.0009 -0.0097 466 ASN A CB  
3905 C CG  . ASN A 466 ? 0.4248 0.5016 0.3249 -0.0461 -0.0006 -0.0134 466 ASN A CG  
3906 O OD1 . ASN A 466 ? 0.4563 0.5333 0.3568 -0.0495 -0.0017 -0.0163 466 ASN A OD1 
3907 N ND2 . ASN A 466 ? 0.4119 0.5024 0.3120 -0.0471 0.0011  -0.0138 466 ASN A ND2 
3908 N N   . PHE A 467 ? 0.3811 0.4073 0.2781 -0.0372 -0.0031 -0.0057 467 PHE A N   
3909 C CA  . PHE A 467 ? 0.3649 0.3824 0.2627 -0.0325 -0.0026 -0.0038 467 PHE A CA  
3910 C C   . PHE A 467 ? 0.3708 0.3769 0.2689 -0.0333 -0.0056 -0.0043 467 PHE A C   
3911 O O   . PHE A 467 ? 0.3692 0.3724 0.2700 -0.0290 -0.0053 -0.0038 467 PHE A O   
3912 C CB  . PHE A 467 ? 0.3647 0.3778 0.2596 -0.0335 -0.0011 -0.0029 467 PHE A CB  
3913 C CG  . PHE A 467 ? 0.3727 0.3779 0.2681 -0.0298 0.0002  -0.0019 467 PHE A CG  
3914 C CD1 . PHE A 467 ? 0.3647 0.3729 0.2630 -0.0235 0.0038  -0.0008 467 PHE A CD1 
3915 C CD2 . PHE A 467 ? 0.3785 0.3738 0.2712 -0.0330 -0.0014 -0.0022 467 PHE A CD2 
3916 C CE1 . PHE A 467 ? 0.3758 0.3758 0.2743 -0.0211 0.0060  -0.0006 467 PHE A CE1 
3917 C CE2 . PHE A 467 ? 0.3673 0.3568 0.2605 -0.0307 0.0002  -0.0023 467 PHE A CE2 
3918 C CZ  . PHE A 467 ? 0.3765 0.3678 0.2726 -0.0252 0.0042  -0.0018 467 PHE A CZ  
3919 N N   . TYR A 468 ? 0.3590 0.3585 0.2541 -0.0386 -0.0080 -0.0051 468 TYR A N   
3920 C CA  . TYR A 468 ? 0.3620 0.3509 0.2571 -0.0390 -0.0107 -0.0050 468 TYR A CA  
3921 C C   . TYR A 468 ? 0.3667 0.3580 0.2656 -0.0366 -0.0110 -0.0063 468 TYR A C   
3922 O O   . TYR A 468 ? 0.3741 0.3606 0.2756 -0.0334 -0.0120 -0.0060 468 TYR A O   
3923 C CB  . TYR A 468 ? 0.3580 0.3395 0.2485 -0.0446 -0.0123 -0.0050 468 TYR A CB  
3924 C CG  . TYR A 468 ? 0.3536 0.3241 0.2436 -0.0443 -0.0148 -0.0043 468 TYR A CG  
3925 C CD1 . TYR A 468 ? 0.3418 0.3064 0.2315 -0.0419 -0.0167 -0.0024 468 TYR A CD1 
3926 C CD2 . TYR A 468 ? 0.3518 0.3183 0.2414 -0.0467 -0.0148 -0.0056 468 TYR A CD2 
3927 C CE1 . TYR A 468 ? 0.3482 0.3044 0.2375 -0.0410 -0.0191 -0.0012 468 TYR A CE1 
3928 C CE2 . TYR A 468 ? 0.3425 0.2984 0.2314 -0.0458 -0.0165 -0.0044 468 TYR A CE2 
3929 C CZ  . TYR A 468 ? 0.3595 0.3108 0.2486 -0.0424 -0.0188 -0.0019 468 TYR A CZ  
3930 O OH  . TYR A 468 ? 0.3484 0.2908 0.2373 -0.0406 -0.0205 -0.0004 468 TYR A OH  
3931 N N   . ASP A 469 ? 0.3681 0.3685 0.2677 -0.0384 -0.0099 -0.0081 469 ASP A N   
3932 C CA  . ASP A 469 ? 0.3710 0.3758 0.2738 -0.0369 -0.0098 -0.0098 469 ASP A CA  
3933 C C   . ASP A 469 ? 0.3772 0.3866 0.2837 -0.0300 -0.0086 -0.0083 469 ASP A C   
3934 O O   . ASP A 469 ? 0.3694 0.3756 0.2784 -0.0276 -0.0093 -0.0087 469 ASP A O   
3935 C CB  . ASP A 469 ? 0.3784 0.3956 0.2810 -0.0407 -0.0085 -0.0124 469 ASP A CB  
3936 C CG  . ASP A 469 ? 0.3888 0.3995 0.2880 -0.0481 -0.0088 -0.0150 469 ASP A CG  
3937 O OD1 . ASP A 469 ? 0.3922 0.3886 0.2895 -0.0491 -0.0100 -0.0142 469 ASP A OD1 
3938 O OD2 . ASP A 469 ? 0.4048 0.4252 0.3031 -0.0529 -0.0073 -0.0179 469 ASP A OD2 
3939 N N   . ALA A 470 ? 0.3833 0.3994 0.2899 -0.0267 -0.0063 -0.0064 470 ALA A N   
3940 C CA  . ALA A 470 ? 0.3704 0.3893 0.2796 -0.0199 -0.0039 -0.0045 470 ALA A CA  
3941 C C   . ALA A 470 ? 0.3752 0.3815 0.2850 -0.0185 -0.0045 -0.0041 470 ALA A C   
3942 O O   . ALA A 470 ? 0.4179 0.4229 0.3301 -0.0146 -0.0035 -0.0038 470 ALA A O   
3943 C CB  . ALA A 470 ? 0.3547 0.3812 0.2633 -0.0163 -0.0004 -0.0022 470 ALA A CB  
3944 N N   . MET A 471 ? 0.3647 0.3626 0.2721 -0.0220 -0.0061 -0.0042 471 MET A N   
3945 C CA  . MET A 471 ? 0.3625 0.3510 0.2705 -0.0211 -0.0068 -0.0042 471 MET A CA  
3946 C C   . MET A 471 ? 0.3607 0.3439 0.2708 -0.0217 -0.0099 -0.0053 471 MET A C   
3947 O O   . MET A 471 ? 0.3413 0.3205 0.2536 -0.0194 -0.0097 -0.0057 471 MET A O   
3948 C CB  . MET A 471 ? 0.3605 0.3440 0.2651 -0.0242 -0.0073 -0.0038 471 MET A CB  
3949 C CG  . MET A 471 ? 0.3615 0.3484 0.2645 -0.0230 -0.0033 -0.0030 471 MET A CG  
3950 S SD  . MET A 471 ? 0.3772 0.3652 0.2828 -0.0165 0.0023  -0.0022 471 MET A SD  
3951 C CE  . MET A 471 ? 0.3536 0.3320 0.2602 -0.0175 0.0016  -0.0040 471 MET A CE  
3952 N N   . ILE A 472 ? 0.3645 0.3478 0.2737 -0.0247 -0.0119 -0.0063 472 ILE A N   
3953 C CA  . ILE A 472 ? 0.3680 0.3469 0.2793 -0.0247 -0.0138 -0.0075 472 ILE A CA  
3954 C C   . ILE A 472 ? 0.3843 0.3683 0.2994 -0.0208 -0.0121 -0.0082 472 ILE A C   
3955 O O   . ILE A 472 ? 0.3694 0.3494 0.2873 -0.0185 -0.0127 -0.0087 472 ILE A O   
3956 C CB  . ILE A 472 ? 0.4009 0.3789 0.3100 -0.0292 -0.0147 -0.0088 472 ILE A CB  
3957 C CG1 . ILE A 472 ? 0.3849 0.3552 0.2897 -0.0328 -0.0162 -0.0076 472 ILE A CG1 
3958 C CG2 . ILE A 472 ? 0.3877 0.3631 0.2994 -0.0288 -0.0151 -0.0108 472 ILE A CG2 
3959 C CD1 . ILE A 472 ? 0.3905 0.3509 0.2955 -0.0316 -0.0185 -0.0064 472 ILE A CD1 
3960 N N   . CYS A 473 ? 0.3930 0.3870 0.3082 -0.0195 -0.0099 -0.0081 473 CYS A N   
3961 C CA  . CYS A 473 ? 0.4118 0.4111 0.3298 -0.0150 -0.0079 -0.0080 473 CYS A CA  
3962 C C   . CYS A 473 ? 0.3973 0.3916 0.3168 -0.0110 -0.0060 -0.0067 473 CYS A C   
3963 O O   . CYS A 473 ? 0.3927 0.3845 0.3147 -0.0089 -0.0058 -0.0074 473 CYS A O   
3964 C CB  . CYS A 473 ? 0.4291 0.4416 0.3466 -0.0133 -0.0057 -0.0072 473 CYS A CB  
3965 S SG  . CYS A 473 ? 0.5363 0.5573 0.4527 -0.0189 -0.0073 -0.0103 473 CYS A SG  
3966 N N   . VAL A 474 ? 0.3924 0.3853 0.3100 -0.0102 -0.0040 -0.0051 474 VAL A N   
3967 C CA  . VAL A 474 ? 0.3697 0.3567 0.2881 -0.0076 -0.0011 -0.0046 474 VAL A CA  
3968 C C   . VAL A 474 ? 0.3630 0.3422 0.2832 -0.0096 -0.0037 -0.0065 474 VAL A C   
3969 O O   . VAL A 474 ? 0.3632 0.3394 0.2854 -0.0076 -0.0017 -0.0073 474 VAL A O   
3970 C CB  . VAL A 474 ? 0.3744 0.3599 0.2900 -0.0082 0.0014  -0.0036 474 VAL A CB  
3971 C CG1 . VAL A 474 ? 0.3485 0.3265 0.2642 -0.0077 0.0045  -0.0044 474 VAL A CG1 
3972 C CG2 . VAL A 474 ? 0.3656 0.3593 0.2799 -0.0047 0.0050  -0.0012 474 VAL A CG2 
3973 N N   . ALA A 475 ? 0.3537 0.3302 0.2730 -0.0133 -0.0079 -0.0072 475 ALA A N   
3974 C CA  . ALA A 475 ? 0.3488 0.3198 0.2697 -0.0144 -0.0108 -0.0084 475 ALA A CA  
3975 C C   . ALA A 475 ? 0.3676 0.3384 0.2924 -0.0124 -0.0116 -0.0096 475 ALA A C   
3976 O O   . ALA A 475 ? 0.3887 0.3570 0.3163 -0.0114 -0.0119 -0.0108 475 ALA A O   
3977 C CB  . ALA A 475 ? 0.3524 0.3204 0.2707 -0.0177 -0.0145 -0.0078 475 ALA A CB  
3978 N N   . TYR A 476 ? 0.3560 0.3303 0.2808 -0.0123 -0.0116 -0.0098 476 TYR A N   
3979 C CA  . TYR A 476 ? 0.3638 0.3386 0.2916 -0.0108 -0.0117 -0.0112 476 TYR A CA  
3980 C C   . TYR A 476 ? 0.3643 0.3416 0.2942 -0.0071 -0.0082 -0.0112 476 TYR A C   
3981 O O   . TYR A 476 ? 0.3689 0.3440 0.3020 -0.0058 -0.0082 -0.0125 476 TYR A O   
3982 C CB  . TYR A 476 ? 0.3677 0.3471 0.2944 -0.0125 -0.0120 -0.0120 476 TYR A CB  
3983 C CG  . TYR A 476 ? 0.3772 0.3513 0.3030 -0.0160 -0.0145 -0.0132 476 TYR A CG  
3984 C CD1 . TYR A 476 ? 0.3959 0.3633 0.3241 -0.0152 -0.0160 -0.0141 476 TYR A CD1 
3985 C CD2 . TYR A 476 ? 0.3946 0.3703 0.3169 -0.0198 -0.0146 -0.0134 476 TYR A CD2 
3986 C CE1 . TYR A 476 ? 0.4174 0.3784 0.3443 -0.0176 -0.0173 -0.0146 476 TYR A CE1 
3987 C CE2 . TYR A 476 ? 0.4088 0.3776 0.3295 -0.0232 -0.0157 -0.0144 476 TYR A CE2 
3988 C CZ  . TYR A 476 ? 0.4201 0.3809 0.3428 -0.0217 -0.0169 -0.0147 476 TYR A CZ  
3989 O OH  . TYR A 476 ? 0.4270 0.3796 0.3476 -0.0242 -0.0170 -0.0151 476 TYR A OH  
3990 N N   . LYS A 477 ? 0.3536 0.3349 0.2816 -0.0052 -0.0049 -0.0094 477 LYS A N   
3991 C CA  . LYS A 477 ? 0.3686 0.3498 0.2974 -0.0013 -0.0004 -0.0087 477 LYS A CA  
3992 C C   . LYS A 477 ? 0.3775 0.3517 0.3079 -0.0022 0.0002  -0.0102 477 LYS A C   
3993 O O   . LYS A 477 ? 0.3814 0.3537 0.3140 -0.0006 0.0024  -0.0112 477 LYS A O   
3994 C CB  . LYS A 477 ? 0.3639 0.3492 0.2899 0.0016  0.0037  -0.0058 477 LYS A CB  
3995 C CG  . LYS A 477 ? 0.3859 0.3735 0.3121 0.0068  0.0086  -0.0041 477 LYS A CG  
3996 C CD  . LYS A 477 ? 0.4079 0.3946 0.3314 0.0108  0.0147  -0.0009 477 LYS A CD  
3997 C CE  . LYS A 477 ? 0.4182 0.4123 0.3407 0.0170  0.0182  0.0023  477 LYS A CE  
3998 N NZ  . LYS A 477 ? 0.3958 0.3852 0.3162 0.0226  0.0259  0.0055  477 LYS A NZ  
3999 N N   . PHE A 478 ? 0.3772 0.3485 0.3062 -0.0053 -0.0015 -0.0105 478 PHE A N   
4000 C CA  . PHE A 478 ? 0.3761 0.3432 0.3064 -0.0069 -0.0009 -0.0125 478 PHE A CA  
4001 C C   . PHE A 478 ? 0.3880 0.3547 0.3224 -0.0071 -0.0040 -0.0145 478 PHE A C   
4002 O O   . PHE A 478 ? 0.3647 0.3302 0.3017 -0.0069 -0.0020 -0.0165 478 PHE A O   
4003 C CB  . PHE A 478 ? 0.3624 0.3285 0.2901 -0.0104 -0.0032 -0.0125 478 PHE A CB  
4004 C CG  . PHE A 478 ? 0.3569 0.3216 0.2861 -0.0129 -0.0040 -0.0150 478 PHE A CG  
4005 C CD1 . PHE A 478 ? 0.3673 0.3331 0.2986 -0.0138 -0.0091 -0.0156 478 PHE A CD1 
4006 C CD2 . PHE A 478 ? 0.3641 0.3269 0.2921 -0.0143 0.0008  -0.0167 478 PHE A CD2 
4007 C CE1 . PHE A 478 ? 0.3797 0.3472 0.3125 -0.0160 -0.0103 -0.0179 478 PHE A CE1 
4008 C CE2 . PHE A 478 ? 0.3795 0.3432 0.3088 -0.0176 0.0001  -0.0198 478 PHE A CE2 
4009 C CZ  . PHE A 478 ? 0.3711 0.3384 0.3030 -0.0183 -0.0057 -0.0204 478 PHE A CZ  
4010 N N   . ASP A 479 ? 0.4060 0.3733 0.3408 -0.0075 -0.0084 -0.0140 479 ASP A N   
4011 C CA  . ASP A 479 ? 0.4024 0.3689 0.3409 -0.0072 -0.0113 -0.0155 479 ASP A CA  
4012 C C   . ASP A 479 ? 0.3958 0.3634 0.3375 -0.0047 -0.0086 -0.0168 479 ASP A C   
4013 O O   . ASP A 479 ? 0.3560 0.3232 0.3014 -0.0043 -0.0087 -0.0188 479 ASP A O   
4014 C CB  . ASP A 479 ? 0.4036 0.3688 0.3410 -0.0081 -0.0150 -0.0145 479 ASP A CB  
4015 C CG  . ASP A 479 ? 0.4100 0.3735 0.3511 -0.0068 -0.0170 -0.0157 479 ASP A CG  
4016 O OD1 . ASP A 479 ? 0.3917 0.3549 0.3353 -0.0062 -0.0188 -0.0162 479 ASP A OD1 
4017 O OD2 . ASP A 479 ? 0.4381 0.4014 0.3796 -0.0064 -0.0166 -0.0163 479 ASP A OD2 
4018 N N   . ALA A 480 ? 0.3855 0.3554 0.3254 -0.0032 -0.0061 -0.0157 480 ALA A N   
4019 C CA  . ALA A 480 ? 0.3935 0.3651 0.3353 -0.0007 -0.0033 -0.0164 480 ALA A CA  
4020 C C   . ALA A 480 ? 0.4021 0.3716 0.3446 0.0005  0.0014  -0.0169 480 ALA A C   
4021 O O   . ALA A 480 ? 0.4127 0.3816 0.3581 0.0014  0.0029  -0.0187 480 ALA A O   
4022 C CB  . ALA A 480 ? 0.4051 0.3821 0.3443 0.0007  -0.0020 -0.0147 480 ALA A CB  
4023 N N   . ALA A 481 ? 0.3785 0.3463 0.3180 0.0002  0.0044  -0.0156 481 ALA A N   
4024 C CA  . ALA A 481 ? 0.4063 0.3700 0.3459 -0.0001 0.0094  -0.0170 481 ALA A CA  
4025 C C   . ALA A 481 ? 0.4304 0.3934 0.3739 -0.0031 0.0071  -0.0208 481 ALA A C   
4026 O O   . ALA A 481 ? 0.4421 0.4038 0.3879 -0.0033 0.0106  -0.0231 481 ALA A O   
4027 C CB  . ALA A 481 ? 0.3883 0.3496 0.3240 -0.0008 0.0128  -0.0157 481 ALA A CB  
4028 N N   . MET A 482 ? 0.4267 0.3915 0.3711 -0.0053 0.0016  -0.0212 482 MET A N   
4029 C CA  . MET A 482 ? 0.4444 0.4111 0.3927 -0.0073 -0.0009 -0.0242 482 MET A CA  
4030 C C   . MET A 482 ? 0.4489 0.4168 0.4017 -0.0055 -0.0014 -0.0257 482 MET A C   
4031 O O   . MET A 482 ? 0.4971 0.4670 0.4536 -0.0066 -0.0007 -0.0288 482 MET A O   
4032 C CB  . MET A 482 ? 0.4331 0.4019 0.3811 -0.0086 -0.0071 -0.0233 482 MET A CB  
4033 C CG  . MET A 482 ? 0.4352 0.4040 0.3794 -0.0114 -0.0072 -0.0227 482 MET A CG  
4034 S SD  . MET A 482 ? 0.4636 0.4319 0.4070 -0.0148 -0.0009 -0.0262 482 MET A SD  
4035 C CE  . MET A 482 ? 0.4677 0.4302 0.4067 -0.0125 0.0052  -0.0235 482 MET A CE  
4036 N N   . MET A 483 ? 0.4450 0.4128 0.3977 -0.0030 -0.0026 -0.0241 483 MET A N   
4037 C CA  . MET A 483 ? 0.4685 0.4374 0.4254 -0.0014 -0.0034 -0.0258 483 MET A CA  
4038 C C   . MET A 483 ? 0.4475 0.4156 0.4051 -0.0007 0.0023  -0.0271 483 MET A C   
4039 O O   . MET A 483 ? 0.4226 0.3919 0.3842 -0.0010 0.0031  -0.0300 483 MET A O   
4040 C CB  . MET A 483 ? 0.4905 0.4595 0.4468 0.0000  -0.0056 -0.0244 483 MET A CB  
4041 C CG  . MET A 483 ? 0.5526 0.5205 0.5084 -0.0006 -0.0106 -0.0233 483 MET A CG  
4042 S SD  . MET A 483 ? 0.5961 0.5649 0.5566 -0.0003 -0.0143 -0.0246 483 MET A SD  
4043 C CE  . MET A 483 ? 0.5885 0.5585 0.5459 -0.0027 -0.0155 -0.0234 483 MET A CE  
4044 N N   . ALA A 484 ? 0.4569 0.4232 0.4102 0.0004  0.0065  -0.0249 484 ALA A N   
4045 C CA  . ALA A 484 ? 0.4711 0.4349 0.4235 0.0016  0.0131  -0.0252 484 ALA A CA  
4046 C C   . ALA A 484 ? 0.4663 0.4277 0.4201 -0.0014 0.0165  -0.0284 484 ALA A C   
4047 O O   . ALA A 484 ? 0.5071 0.4672 0.4628 -0.0018 0.0206  -0.0307 484 ALA A O   
4048 C CB  . ALA A 484 ? 0.4518 0.4144 0.3989 0.0045  0.0173  -0.0212 484 ALA A CB  
4049 N N   . LEU A 485 ? 0.4801 0.4414 0.4327 -0.0042 0.0152  -0.0290 485 LEU A N   
4050 C CA  . LEU A 485 ? 0.4880 0.4480 0.4415 -0.0084 0.0191  -0.0329 485 LEU A CA  
4051 C C   . LEU A 485 ? 0.4760 0.4414 0.4355 -0.0103 0.0164  -0.0371 485 LEU A C   
4052 O O   . LEU A 485 ? 0.4579 0.4229 0.4191 -0.0131 0.0212  -0.0410 485 LEU A O   
4053 C CB  . LEU A 485 ? 0.4557 0.4158 0.4065 -0.0116 0.0182  -0.0332 485 LEU A CB  
4054 C CG  . LEU A 485 ? 0.4804 0.4350 0.4254 -0.0108 0.0226  -0.0303 485 LEU A CG  
4055 C CD1 . LEU A 485 ? 0.4719 0.4281 0.4152 -0.0148 0.0206  -0.0317 485 LEU A CD1 
4056 C CD2 . LEU A 485 ? 0.5023 0.4493 0.4443 -0.0102 0.0325  -0.0306 485 LEU A CD2 
4057 N N   . ARG A 486 ? 0.4729 0.4432 0.4358 -0.0086 0.0093  -0.0363 486 ARG A N   
4058 C CA  . ARG A 486 ? 0.5048 0.4812 0.4739 -0.0091 0.0062  -0.0396 486 ARG A CA  
4059 C C   . ARG A 486 ? 0.4968 0.4726 0.4690 -0.0073 0.0091  -0.0410 486 ARG A C   
4060 O O   . ARG A 486 ? 0.4957 0.4754 0.4723 -0.0091 0.0107  -0.0451 486 ARG A O   
4061 C CB  . ARG A 486 ? 0.5610 0.5413 0.5320 -0.0071 -0.0013 -0.0376 486 ARG A CB  
4062 C CG  . ARG A 486 ? 0.5893 0.5743 0.5664 -0.0048 -0.0045 -0.0390 486 ARG A CG  
4063 C CD  . ARG A 486 ? 0.6781 0.6709 0.6603 -0.0073 -0.0038 -0.0436 486 ARG A CD  
4064 N NE  . ARG A 486 ? 0.7205 0.7207 0.7037 -0.0087 -0.0081 -0.0439 486 ARG A NE  
4065 C CZ  . ARG A 486 ? 0.7810 0.7917 0.7695 -0.0097 -0.0098 -0.0472 486 ARG A CZ  
4066 N NH1 . ARG A 486 ? 0.7907 0.8052 0.7845 -0.0098 -0.0074 -0.0509 486 ARG A NH1 
4067 N NH2 . ARG A 486 ? 0.8257 0.8445 0.8142 -0.0108 -0.0139 -0.0470 486 ARG A NH2 
4068 N N   . THR A 487 ? 0.5010 0.4730 0.4707 -0.0039 0.0099  -0.0380 487 THR A N   
4069 C CA  . THR A 487 ? 0.4759 0.4481 0.4482 -0.0019 0.0116  -0.0390 487 THR A CA  
4070 C C   . THR A 487 ? 0.4830 0.4510 0.4527 -0.0020 0.0193  -0.0393 487 THR A C   
4071 O O   . THR A 487 ? 0.5010 0.4696 0.4732 -0.0013 0.0215  -0.0411 487 THR A O   
4072 C CB  . THR A 487 ? 0.4748 0.4466 0.4457 0.0012  0.0085  -0.0361 487 THR A CB  
4073 O OG1 . THR A 487 ? 0.4642 0.4332 0.4291 0.0023  0.0105  -0.0324 487 THR A OG1 
4074 C CG2 . THR A 487 ? 0.4813 0.4555 0.4547 0.0017  0.0018  -0.0357 487 THR A CG2 
4075 N N   . SER A 488 ? 0.4654 0.4284 0.4298 -0.0025 0.0239  -0.0374 488 SER A N   
4076 C CA  . SER A 488 ? 0.4595 0.4165 0.4202 -0.0017 0.0323  -0.0367 488 SER A CA  
4077 C C   . SER A 488 ? 0.4864 0.4384 0.4455 -0.0059 0.0389  -0.0394 488 SER A C   
4078 O O   . SER A 488 ? 0.5290 0.4769 0.4877 -0.0075 0.0459  -0.0418 488 SER A O   
4079 C CB  . SER A 488 ? 0.4338 0.3884 0.3888 0.0027  0.0339  -0.0310 488 SER A CB  
4080 O OG  . SER A 488 ? 0.4453 0.3932 0.3958 0.0044  0.0427  -0.0292 488 SER A OG  
4081 N N   . PHE A 489 ? 0.4500 0.4018 0.4074 -0.0081 0.0374  -0.0394 489 PHE A N   
4082 C CA  . PHE A 489 ? 0.4844 0.4318 0.4400 -0.0131 0.0438  -0.0429 489 PHE A CA  
4083 C C   . PHE A 489 ? 0.5039 0.4591 0.4655 -0.0183 0.0408  -0.0491 489 PHE A C   
4084 O O   . PHE A 489 ? 0.4940 0.4484 0.4556 -0.0239 0.0459  -0.0539 489 PHE A O   
4085 C CB  . PHE A 489 ? 0.4407 0.3860 0.3922 -0.0137 0.0432  -0.0408 489 PHE A CB  
4086 C CG  . PHE A 489 ? 0.4271 0.3651 0.3724 -0.0088 0.0479  -0.0351 489 PHE A CG  
4087 C CD1 . PHE A 489 ? 0.4028 0.3442 0.3473 -0.0034 0.0429  -0.0300 489 PHE A CD1 
4088 C CD2 . PHE A 489 ? 0.4233 0.3517 0.3635 -0.0096 0.0575  -0.0350 489 PHE A CD2 
4089 C CE1 . PHE A 489 ? 0.3813 0.3188 0.3205 0.0014  0.0469  -0.0247 489 PHE A CE1 
4090 C CE2 . PHE A 489 ? 0.4192 0.3420 0.3540 -0.0039 0.0620  -0.0290 489 PHE A CE2 
4091 C CZ  . PHE A 489 ? 0.4009 0.3293 0.3353 0.0017  0.0563  -0.0238 489 PHE A CZ  
4092 N N   . LEU A 490 ? 0.5384 0.5018 0.5052 -0.0163 0.0328  -0.0490 490 LEU A N   
4093 C CA  . LEU A 490 ? 0.5686 0.5421 0.5419 -0.0196 0.0284  -0.0538 490 LEU A CA  
4094 C C   . LEU A 490 ? 0.5653 0.5433 0.5382 -0.0246 0.0274  -0.0567 490 LEU A C   
4095 O O   . LEU A 490 ? 0.6199 0.6033 0.5956 -0.0300 0.0300  -0.0625 490 LEU A O   
4096 C CB  . LEU A 490 ? 0.5583 0.5333 0.5355 -0.0219 0.0333  -0.0586 490 LEU A CB  
4097 C CG  . LEU A 490 ? 0.5921 0.5633 0.5697 -0.0177 0.0354  -0.0566 490 LEU A CG  
4098 C CD1 . LEU A 490 ? 0.5586 0.5330 0.5407 -0.0210 0.0397  -0.0622 490 LEU A CD1 
4099 C CD2 . LEU A 490 ? 0.5639 0.5388 0.5438 -0.0124 0.0274  -0.0529 490 LEU A CD2 
4100 N N   . VAL A 491 ? 0.5814 0.5582 0.5507 -0.0234 0.0236  -0.0531 491 VAL A N   
4101 C CA  . VAL A 491 ? 0.6171 0.5993 0.5856 -0.0280 0.0218  -0.0555 491 VAL A CA  
4102 C C   . VAL A 491 ? 0.6295 0.6248 0.6036 -0.0277 0.0131  -0.0565 491 VAL A C   
4103 O O   . VAL A 491 ? 0.6722 0.6691 0.6484 -0.0225 0.0071  -0.0527 491 VAL A O   
4104 C CB  . VAL A 491 ? 0.6156 0.5917 0.5779 -0.0268 0.0212  -0.0511 491 VAL A CB  
4105 C CG1 . VAL A 491 ? 0.5857 0.5683 0.5470 -0.0315 0.0185  -0.0534 491 VAL A CG1 
4106 C CG2 . VAL A 491 ? 0.5868 0.5510 0.5437 -0.0266 0.0304  -0.0499 491 VAL A CG2 
4107 N N   . ASN A 492 ? 0.6748 0.6797 0.6509 -0.0331 0.0129  -0.0615 492 ASN A N   
4108 C CA  . ASN A 492 ? 0.7739 0.7928 0.7544 -0.0321 0.0046  -0.0616 492 ASN A CA  
4109 C C   . ASN A 492 ? 0.8004 0.8249 0.7775 -0.0354 0.0018  -0.0616 492 ASN A C   
4110 O O   . ASN A 492 ? 0.8132 0.8451 0.7913 -0.0322 -0.0056 -0.0583 492 ASN A O   
4111 C CB  . ASN A 492 ? 0.8036 0.8351 0.7914 -0.0343 0.0046  -0.0671 492 ASN A CB  
4112 C CG  . ASN A 492 ? 0.9077 0.9355 0.8953 -0.0405 0.0140  -0.0734 492 ASN A CG  
4113 O OD1 . ASN A 492 ? 0.9702 0.9933 0.9530 -0.0463 0.0200  -0.0764 492 ASN A OD1 
4114 N ND2 . ASN A 492 ? 0.8974 0.9264 0.8897 -0.0394 0.0161  -0.0755 492 ASN A ND2 
4115 N N   . ASP A 493 ? 0.7698 0.7901 0.7425 -0.0416 0.0083  -0.0652 493 ASP A N   
4116 C CA  . ASP A 493 ? 0.7648 0.7883 0.7330 -0.0451 0.0066  -0.0652 493 ASP A CA  
4117 C C   . ASP A 493 ? 0.7186 0.7282 0.6801 -0.0430 0.0087  -0.0603 493 ASP A C   
4118 O O   . ASP A 493 ? 0.6909 0.6895 0.6486 -0.0452 0.0169  -0.0616 493 ASP A O   
4119 C CB  . ASP A 493 ? 0.7870 0.8175 0.7548 -0.0544 0.0122  -0.0734 493 ASP A CB  
4120 C CG  . ASP A 493 ? 0.8277 0.8661 0.7919 -0.0582 0.0089  -0.0740 493 ASP A CG  
4121 O OD1 . ASP A 493 ? 0.8000 0.8304 0.7590 -0.0556 0.0073  -0.0689 493 ASP A OD1 
4122 O OD2 . ASP A 493 ? 0.8843 0.9379 0.8506 -0.0641 0.0081  -0.0799 493 ASP A OD2 
4123 N N   . PHE A 494 ? 0.6582 0.6684 0.6180 -0.0386 0.0017  -0.0546 494 PHE A N   
4124 C CA  . PHE A 494 ? 0.6733 0.6724 0.6275 -0.0361 0.0027  -0.0497 494 PHE A CA  
4125 C C   . PHE A 494 ? 0.6615 0.6611 0.6104 -0.0406 0.0038  -0.0506 494 PHE A C   
4126 O O   . PHE A 494 ? 0.6929 0.6873 0.6377 -0.0384 0.0020  -0.0461 494 PHE A O   
4127 C CB  . PHE A 494 ? 0.6877 0.6856 0.6426 -0.0294 -0.0042 -0.0434 494 PHE A CB  
4128 C CG  . PHE A 494 ? 0.6946 0.6891 0.6534 -0.0249 -0.0038 -0.0422 494 PHE A CG  
4129 C CD1 . PHE A 494 ? 0.6842 0.6687 0.6407 -0.0223 0.0000  -0.0397 494 PHE A CD1 
4130 C CD2 . PHE A 494 ? 0.6983 0.7007 0.6633 -0.0232 -0.0073 -0.0437 494 PHE A CD2 
4131 C CE1 . PHE A 494 ? 0.7218 0.7040 0.6814 -0.0185 0.0004  -0.0389 494 PHE A CE1 
4132 C CE2 . PHE A 494 ? 0.7259 0.7250 0.6943 -0.0195 -0.0066 -0.0430 494 PHE A CE2 
4133 C CZ  . PHE A 494 ? 0.7341 0.7230 0.6995 -0.0174 -0.0027 -0.0407 494 PHE A CZ  
4134 N N   . GLY A 495 ? 0.6026 0.6085 0.5516 -0.0475 0.0072  -0.0569 495 GLY A N   
4135 C CA  . GLY A 495 ? 0.5916 0.5999 0.5357 -0.0528 0.0082  -0.0588 495 GLY A CA  
4136 C C   . GLY A 495 ? 0.5751 0.5696 0.5132 -0.0532 0.0150  -0.0574 495 GLY A C   
4137 O O   . GLY A 495 ? 0.5610 0.5542 0.4949 -0.0525 0.0123  -0.0540 495 GLY A O   
4138 N N   . PHE A 496 ? 0.5463 0.5308 0.4838 -0.0542 0.0242  -0.0598 496 PHE A N   
4139 C CA  . PHE A 496 ? 0.5122 0.4827 0.4444 -0.0529 0.0318  -0.0577 496 PHE A CA  
4140 C C   . PHE A 496 ? 0.4856 0.4520 0.4157 -0.0460 0.0271  -0.0500 496 PHE A C   
4141 O O   . PHE A 496 ? 0.4721 0.4309 0.3977 -0.0451 0.0315  -0.0479 496 PHE A O   
4142 C CB  . PHE A 496 ? 0.5233 0.4833 0.4558 -0.0520 0.0413  -0.0592 496 PHE A CB  
4143 C CG  . PHE A 496 ? 0.5190 0.4765 0.4545 -0.0444 0.0384  -0.0540 496 PHE A CG  
4144 C CD1 . PHE A 496 ? 0.5267 0.4763 0.4594 -0.0378 0.0394  -0.0476 496 PHE A CD1 
4145 C CD2 . PHE A 496 ? 0.5127 0.4772 0.4539 -0.0440 0.0347  -0.0558 496 PHE A CD2 
4146 C CE1 . PHE A 496 ? 0.5569 0.5058 0.4921 -0.0315 0.0366  -0.0434 496 PHE A CE1 
4147 C CE2 . PHE A 496 ? 0.5401 0.5023 0.4838 -0.0376 0.0324  -0.0516 496 PHE A CE2 
4148 C CZ  . PHE A 496 ? 0.5520 0.5067 0.4925 -0.0316 0.0333  -0.0455 496 PHE A CZ  
4149 N N   . ILE A 497 ? 0.4768 0.4486 0.4104 -0.0414 0.0188  -0.0461 497 ILE A N   
4150 C CA  . ILE A 497 ? 0.4789 0.4479 0.4107 -0.0358 0.0143  -0.0396 497 ILE A CA  
4151 C C   . ILE A 497 ? 0.4691 0.4393 0.3964 -0.0378 0.0119  -0.0380 497 ILE A C   
4152 O O   . ILE A 497 ? 0.4597 0.4243 0.3836 -0.0352 0.0134  -0.0343 497 ILE A O   
4153 C CB  . ILE A 497 ? 0.4995 0.4735 0.4356 -0.0315 0.0064  -0.0366 497 ILE A CB  
4154 C CG1 . ILE A 497 ? 0.5035 0.4723 0.4419 -0.0271 0.0092  -0.0351 497 ILE A CG1 
4155 C CG2 . ILE A 497 ? 0.4998 0.4748 0.4337 -0.0290 0.0000  -0.0317 497 ILE A CG2 
4156 C CD1 . ILE A 497 ? 0.5384 0.5096 0.4813 -0.0285 0.0116  -0.0393 497 ILE A CD1 
4157 N N   . TRP A 498 ? 0.4399 0.4185 0.3669 -0.0426 0.0085  -0.0410 498 TRP A N   
4158 C CA  . TRP A 498 ? 0.4263 0.4071 0.3487 -0.0446 0.0056  -0.0394 498 TRP A CA  
4159 C C   . TRP A 498 ? 0.4248 0.3973 0.3424 -0.0458 0.0124  -0.0393 498 TRP A C   
4160 O O   . TRP A 498 ? 0.3992 0.3691 0.3137 -0.0434 0.0106  -0.0351 498 TRP A O   
4161 C CB  . TRP A 498 ? 0.4223 0.4143 0.3445 -0.0502 0.0024  -0.0434 498 TRP A CB  
4162 C CG  . TRP A 498 ? 0.4149 0.4089 0.3319 -0.0520 -0.0005 -0.0412 498 TRP A CG  
4163 C CD1 . TRP A 498 ? 0.4265 0.4226 0.3392 -0.0582 0.0029  -0.0451 498 TRP A CD1 
4164 C CD2 . TRP A 498 ? 0.4190 0.4117 0.3337 -0.0478 -0.0066 -0.0348 498 TRP A CD2 
4165 N NE1 . TRP A 498 ? 0.4145 0.4114 0.3226 -0.0579 -0.0010 -0.0413 498 TRP A NE1 
4166 C CE2 . TRP A 498 ? 0.4277 0.4224 0.3368 -0.0518 -0.0067 -0.0350 498 TRP A CE2 
4167 C CE3 . TRP A 498 ? 0.4004 0.3904 0.3170 -0.0419 -0.0113 -0.0295 498 TRP A CE3 
4168 C CZ2 . TRP A 498 ? 0.4169 0.4108 0.3224 -0.0498 -0.0114 -0.0298 498 TRP A CZ2 
4169 C CZ3 . TRP A 498 ? 0.4132 0.4020 0.3261 -0.0403 -0.0156 -0.0247 498 TRP A CZ3 
4170 C CH2 . TRP A 498 ? 0.4125 0.4031 0.3199 -0.0441 -0.0157 -0.0247 498 TRP A CH2 
4171 N N   . LEU A 499 ? 0.4335 0.4015 0.3501 -0.0496 0.0211  -0.0442 499 LEU A N   
4172 C CA  . LEU A 499 ? 0.4393 0.3987 0.3512 -0.0505 0.0288  -0.0444 499 LEU A CA  
4173 C C   . LEU A 499 ? 0.4162 0.3669 0.3277 -0.0434 0.0322  -0.0391 499 LEU A C   
4174 O O   . LEU A 499 ? 0.4219 0.3682 0.3297 -0.0418 0.0352  -0.0367 499 LEU A O   
4175 C CB  . LEU A 499 ? 0.4664 0.4222 0.3766 -0.0572 0.0382  -0.0515 499 LEU A CB  
4176 C CG  . LEU A 499 ? 0.4903 0.4565 0.3993 -0.0655 0.0357  -0.0573 499 LEU A CG  
4177 C CD1 . LEU A 499 ? 0.5072 0.4725 0.4167 -0.0727 0.0441  -0.0656 499 LEU A CD1 
4178 C CD2 . LEU A 499 ? 0.4865 0.4531 0.3902 -0.0680 0.0353  -0.0567 499 LEU A CD2 
4179 N N   . VAL A 500 ? 0.3988 0.3483 0.3140 -0.0390 0.0316  -0.0373 500 VAL A N   
4180 C CA  . VAL A 500 ? 0.4065 0.3507 0.3213 -0.0318 0.0338  -0.0320 500 VAL A CA  
4181 C C   . VAL A 500 ? 0.4077 0.3568 0.3220 -0.0289 0.0259  -0.0272 500 VAL A C   
4182 O O   . VAL A 500 ? 0.3956 0.3425 0.3073 -0.0258 0.0280  -0.0237 500 VAL A O   
4183 C CB  . VAL A 500 ? 0.4351 0.3779 0.3537 -0.0281 0.0346  -0.0313 500 VAL A CB  
4184 C CG1 . VAL A 500 ? 0.4039 0.3433 0.3217 -0.0207 0.0369  -0.0257 500 VAL A CG1 
4185 C CG2 . VAL A 500 ? 0.4209 0.3586 0.3399 -0.0317 0.0427  -0.0365 500 VAL A CG2 
4186 N N   . LEU A 501 ? 0.3939 0.3498 0.3107 -0.0300 0.0174  -0.0270 501 LEU A N   
4187 C CA  . LEU A 501 ? 0.3959 0.3554 0.3116 -0.0286 0.0104  -0.0231 501 LEU A CA  
4188 C C   . LEU A 501 ? 0.3977 0.3569 0.3086 -0.0313 0.0115  -0.0227 501 LEU A C   
4189 O O   . LEU A 501 ? 0.3856 0.3441 0.2946 -0.0287 0.0115  -0.0193 501 LEU A O   
4190 C CB  . LEU A 501 ? 0.3973 0.3627 0.3156 -0.0296 0.0023  -0.0232 501 LEU A CB  
4191 C CG  . LEU A 501 ? 0.4018 0.3690 0.3186 -0.0282 -0.0041 -0.0192 501 LEU A CG  
4192 C CD1 . LEU A 501 ? 0.3970 0.3617 0.3140 -0.0241 -0.0032 -0.0160 501 LEU A CD1 
4193 C CD2 . LEU A 501 ? 0.3931 0.3644 0.3123 -0.0279 -0.0108 -0.0187 501 LEU A CD2 
4194 N N   . SER A 502 ? 0.4116 0.3723 0.3206 -0.0367 0.0127  -0.0265 502 SER A N   
4195 C CA  . SER A 502 ? 0.4259 0.3861 0.3301 -0.0401 0.0147  -0.0271 502 SER A CA  
4196 C C   . SER A 502 ? 0.4300 0.3836 0.3317 -0.0376 0.0226  -0.0259 502 SER A C   
4197 O O   . SER A 502 ? 0.4517 0.4058 0.3506 -0.0369 0.0219  -0.0232 502 SER A O   
4198 C CB  . SER A 502 ? 0.4504 0.4139 0.3530 -0.0469 0.0160  -0.0325 502 SER A CB  
4199 O OG  . SER A 502 ? 0.5007 0.4725 0.4052 -0.0484 0.0082  -0.0328 502 SER A OG  
4200 N N   . SER A 503 ? 0.4103 0.3578 0.3128 -0.0363 0.0306  -0.0277 503 SER A N   
4201 C CA  . SER A 503 ? 0.4244 0.3653 0.3249 -0.0319 0.0386  -0.0254 503 SER A CA  
4202 C C   . SER A 503 ? 0.4162 0.3602 0.3177 -0.0254 0.0352  -0.0195 503 SER A C   
4203 O O   . SER A 503 ? 0.4252 0.3694 0.3243 -0.0231 0.0376  -0.0169 503 SER A O   
4204 C CB  . SER A 503 ? 0.4677 0.4010 0.3692 -0.0300 0.0471  -0.0270 503 SER A CB  
4205 O OG  . SER A 503 ? 0.6273 0.5577 0.5275 -0.0369 0.0515  -0.0332 503 SER A OG  
4206 N N   . THR A 504 ? 0.4003 0.3477 0.3054 -0.0227 0.0301  -0.0178 504 THR A N   
4207 C CA  . THR A 504 ? 0.3972 0.3491 0.3034 -0.0177 0.0264  -0.0132 504 THR A CA  
4208 C C   . THR A 504 ? 0.3904 0.3474 0.2946 -0.0196 0.0212  -0.0116 504 THR A C   
4209 O O   . THR A 504 ? 0.4160 0.3757 0.3191 -0.0165 0.0227  -0.0088 504 THR A O   
4210 C CB  . THR A 504 ? 0.4048 0.3594 0.3150 -0.0162 0.0213  -0.0129 504 THR A CB  
4211 O OG1 . THR A 504 ? 0.4105 0.3604 0.3223 -0.0149 0.0264  -0.0146 504 THR A OG1 
4212 C CG2 . THR A 504 ? 0.3999 0.3596 0.3110 -0.0115 0.0189  -0.0090 504 THR A CG2 
4213 N N   . VAL A 505 ? 0.3899 0.3486 0.2935 -0.0245 0.0153  -0.0133 505 VAL A N   
4214 C CA  . VAL A 505 ? 0.3825 0.3448 0.2833 -0.0269 0.0109  -0.0117 505 VAL A CA  
4215 C C   . VAL A 505 ? 0.3731 0.3343 0.2703 -0.0278 0.0163  -0.0119 505 VAL A C   
4216 O O   . VAL A 505 ? 0.3641 0.3285 0.2599 -0.0267 0.0159  -0.0096 505 VAL A O   
4217 C CB  . VAL A 505 ? 0.3841 0.3478 0.2839 -0.0315 0.0046  -0.0130 505 VAL A CB  
4218 C CG1 . VAL A 505 ? 0.3794 0.3451 0.2750 -0.0344 0.0017  -0.0115 505 VAL A CG1 
4219 C CG2 . VAL A 505 ? 0.3676 0.3325 0.2709 -0.0298 -0.0007 -0.0121 505 VAL A CG2 
4220 N N   . ARG A 506 ? 0.3810 0.3376 0.2769 -0.0300 0.0218  -0.0151 506 ARG A N   
4221 C CA  . ARG A 506 ? 0.3895 0.3435 0.2821 -0.0305 0.0284  -0.0156 506 ARG A CA  
4222 C C   . ARG A 506 ? 0.3741 0.3283 0.2675 -0.0235 0.0334  -0.0119 506 ARG A C   
4223 O O   . ARG A 506 ? 0.3616 0.3192 0.2533 -0.0225 0.0340  -0.0100 506 ARG A O   
4224 C CB  . ARG A 506 ? 0.4171 0.3652 0.3082 -0.0345 0.0348  -0.0204 506 ARG A CB  
4225 C CG  . ARG A 506 ? 0.4439 0.3877 0.3312 -0.0354 0.0429  -0.0217 506 ARG A CG  
4226 C CD  . ARG A 506 ? 0.4868 0.4228 0.3748 -0.0298 0.0528  -0.0208 506 ARG A CD  
4227 N NE  . ARG A 506 ? 0.4907 0.4258 0.3770 -0.0248 0.0582  -0.0175 506 ARG A NE  
4228 C CZ  . ARG A 506 ? 0.5068 0.4382 0.3938 -0.0172 0.0651  -0.0141 506 ARG A CZ  
4229 N NH1 . ARG A 506 ? 0.4731 0.4003 0.3622 -0.0137 0.0678  -0.0133 506 ARG A NH1 
4230 N NH2 . ARG A 506 ? 0.5159 0.4485 0.4015 -0.0126 0.0696  -0.0110 506 ARG A NH2 
4231 N N   . ALA A 507 ? 0.3719 0.3240 0.2680 -0.0185 0.0365  -0.0106 507 ALA A N   
4232 C CA  . ALA A 507 ? 0.3782 0.3312 0.2747 -0.0109 0.0418  -0.0066 507 ALA A CA  
4233 C C   . ALA A 507 ? 0.3830 0.3463 0.2808 -0.0081 0.0365  -0.0030 507 ALA A C   
4234 O O   . ALA A 507 ? 0.4076 0.3751 0.3046 -0.0036 0.0400  -0.0001 507 ALA A O   
4235 C CB  . ALA A 507 ? 0.3722 0.3206 0.2707 -0.0064 0.0461  -0.0058 507 ALA A CB  
4236 N N   . TYR A 508 ? 0.3745 0.3421 0.2742 -0.0105 0.0285  -0.0033 508 TYR A N   
4237 C CA  . TYR A 508 ? 0.3768 0.3540 0.2775 -0.0091 0.0238  -0.0009 508 TYR A CA  
4238 C C   . TYR A 508 ? 0.3962 0.3770 0.2942 -0.0131 0.0218  -0.0012 508 TYR A C   
4239 O O   . TYR A 508 ? 0.3929 0.3817 0.2909 -0.0108 0.0224  0.0008  508 TYR A O   
4240 C CB  . TYR A 508 ? 0.3800 0.3590 0.2832 -0.0106 0.0172  -0.0015 508 TYR A CB  
4241 C CG  . TYR A 508 ? 0.3981 0.3787 0.3041 -0.0050 0.0192  0.0000  508 TYR A CG  
4242 C CD1 . TYR A 508 ? 0.3986 0.3885 0.3056 -0.0004 0.0197  0.0027  508 TYR A CD1 
4243 C CD2 . TYR A 508 ? 0.4062 0.3799 0.3137 -0.0045 0.0209  -0.0014 508 TYR A CD2 
4244 C CE1 . TYR A 508 ? 0.4098 0.4021 0.3188 0.0047  0.0215  0.0043  508 TYR A CE1 
4245 C CE2 . TYR A 508 ? 0.4240 0.3988 0.3336 0.0005  0.0230  0.0000  508 TYR A CE2 
4246 C CZ  . TYR A 508 ? 0.4205 0.4045 0.3306 0.0053  0.0233  0.0032  508 TYR A CZ  
4247 O OH  . TYR A 508 ? 0.4109 0.3971 0.3225 0.0106  0.0255  0.0051  508 TYR A OH  
4248 N N   . ALA A 509 ? 0.3992 0.3749 0.2949 -0.0190 0.0197  -0.0037 509 ALA A N   
4249 C CA  . ALA A 509 ? 0.4205 0.3981 0.3128 -0.0232 0.0187  -0.0041 509 ALA A CA  
4250 C C   . ALA A 509 ? 0.4213 0.4002 0.3123 -0.0202 0.0258  -0.0032 509 ALA A C   
4251 O O   . ALA A 509 ? 0.4013 0.3861 0.2909 -0.0210 0.0256  -0.0023 509 ALA A O   
4252 C CB  . ALA A 509 ? 0.4160 0.3884 0.3056 -0.0294 0.0161  -0.0067 509 ALA A CB  
4253 N N   . SER A 510 ? 0.4247 0.3976 0.3160 -0.0167 0.0327  -0.0036 510 SER A N   
4254 C CA  . SER A 510 ? 0.4624 0.4344 0.3523 -0.0129 0.0407  -0.0025 510 SER A CA  
4255 C C   . SER A 510 ? 0.4756 0.4570 0.3678 -0.0052 0.0424  0.0018  510 SER A C   
4256 O O   . SER A 510 ? 0.4992 0.4865 0.3906 -0.0034 0.0449  0.0032  510 SER A O   
4257 C CB  . SER A 510 ? 0.4696 0.4308 0.3586 -0.0116 0.0488  -0.0042 510 SER A CB  
4258 O OG  . SER A 510 ? 0.4856 0.4454 0.3737 -0.0056 0.0575  -0.0019 510 SER A OG  
4259 N N   . ARG A 511 ? 0.5032 0.4873 0.3982 -0.0009 0.0410  0.0037  511 ARG A N   
4260 C CA  . ARG A 511 ? 0.5094 0.5054 0.4066 0.0061  0.0416  0.0078  511 ARG A CA  
4261 C C   . ARG A 511 ? 0.4799 0.4880 0.3775 0.0024  0.0356  0.0075  511 ARG A C   
4262 O O   . ARG A 511 ? 0.4729 0.4917 0.3711 0.0064  0.0377  0.0098  511 ARG A O   
4263 C CB  . ARG A 511 ? 0.5407 0.5381 0.4404 0.0106  0.0406  0.0096  511 ARG A CB  
4264 C CG  . ARG A 511 ? 0.6457 0.6333 0.5449 0.0165  0.0488  0.0112  511 ARG A CG  
4265 C CD  . ARG A 511 ? 0.6888 0.6789 0.5901 0.0215  0.0482  0.0135  511 ARG A CD  
4266 N NE  . ARG A 511 ? 0.7441 0.7206 0.6446 0.0225  0.0537  0.0126  511 ARG A NE  
4267 C CZ  . ARG A 511 ? 0.7262 0.6971 0.6280 0.0178  0.0499  0.0094  511 ARG A CZ  
4268 N NH1 . ARG A 511 ? 0.6610 0.6374 0.5647 0.0124  0.0410  0.0071  511 ARG A NH1 
4269 N NH2 . ARG A 511 ? 0.7277 0.6871 0.6288 0.0185  0.0557  0.0083  511 ARG A NH2 
4270 N N   . ALA A 512 ? 0.4472 0.4535 0.3442 -0.0049 0.0287  0.0048  512 ALA A N   
4271 C CA  . ALA A 512 ? 0.4429 0.4579 0.3394 -0.0096 0.0238  0.0040  512 ALA A CA  
4272 C C   . ALA A 512 ? 0.4517 0.4687 0.3457 -0.0113 0.0269  0.0038  512 ALA A C   
4273 O O   . ALA A 512 ? 0.4445 0.4734 0.3392 -0.0102 0.0272  0.0048  512 ALA A O   
4274 C CB  . ALA A 512 ? 0.4180 0.4275 0.3134 -0.0168 0.0171  0.0016  512 ALA A CB  
4275 N N   . PHE A 513 ? 0.4513 0.4575 0.3424 -0.0144 0.0293  0.0020  513 PHE A N   
4276 C CA  . PHE A 513 ? 0.4613 0.4680 0.3497 -0.0165 0.0326  0.0013  513 PHE A CA  
4277 C C   . PHE A 513 ? 0.4739 0.4892 0.3640 -0.0090 0.0389  0.0040  513 PHE A C   
4278 O O   . PHE A 513 ? 0.4740 0.4986 0.3638 -0.0100 0.0390  0.0043  513 PHE A O   
4279 C CB  . PHE A 513 ? 0.4729 0.4670 0.3581 -0.0200 0.0358  -0.0012 513 PHE A CB  
4280 C CG  . PHE A 513 ? 0.4661 0.4599 0.3476 -0.0239 0.0385  -0.0027 513 PHE A CG  
4281 C CD1 . PHE A 513 ? 0.4721 0.4662 0.3535 -0.0192 0.0467  -0.0019 513 PHE A CD1 
4282 C CD2 . PHE A 513 ? 0.4741 0.4671 0.3522 -0.0319 0.0334  -0.0047 513 PHE A CD2 
4283 C CE1 . PHE A 513 ? 0.4752 0.4691 0.3534 -0.0229 0.0496  -0.0037 513 PHE A CE1 
4284 C CE2 . PHE A 513 ? 0.4763 0.4694 0.3507 -0.0357 0.0360  -0.0062 513 PHE A CE2 
4285 C CZ  . PHE A 513 ? 0.4717 0.4654 0.3463 -0.0315 0.0440  -0.0060 513 PHE A CZ  
4286 N N   . LYS A 514 ? 0.5002 0.5127 0.3920 -0.0013 0.0444  0.0064  514 LYS A N   
4287 C CA  . LYS A 514 ? 0.5207 0.5407 0.4140 0.0077  0.0512  0.0101  514 LYS A CA  
4288 C C   . LYS A 514 ? 0.4989 0.5376 0.3953 0.0109  0.0476  0.0125  514 LYS A C   
4289 O O   . LYS A 514 ? 0.4938 0.5435 0.3910 0.0140  0.0503  0.0140  514 LYS A O   
4290 C CB  . LYS A 514 ? 0.5884 0.5998 0.4821 0.0155  0.0579  0.0126  514 LYS A CB  
4291 C CG  . LYS A 514 ? 0.6961 0.6915 0.5867 0.0144  0.0657  0.0106  514 LYS A CG  
4292 C CD  . LYS A 514 ? 0.7855 0.7714 0.6760 0.0221  0.0737  0.0132  514 LYS A CD  
4293 C CE  . LYS A 514 ? 0.8273 0.7965 0.7142 0.0199  0.0826  0.0102  514 LYS A CE  
4294 N NZ  . LYS A 514 ? 0.8567 0.8196 0.7415 0.0082  0.0777  0.0040  514 LYS A NZ  
4295 N N   . LYS A 515 ? 0.4928 0.5358 0.3910 0.0098  0.0418  0.0124  515 LYS A N   
4296 C CA  . LYS A 515 ? 0.5024 0.5642 0.4035 0.0113  0.0382  0.0135  515 LYS A CA  
4297 C C   . LYS A 515 ? 0.4961 0.5663 0.3963 0.0038  0.0348  0.0108  515 LYS A C   
4298 O O   . LYS A 515 ? 0.5129 0.5999 0.4149 0.0063  0.0355  0.0118  515 LYS A O   
4299 C CB  . LYS A 515 ? 0.5292 0.5917 0.4318 0.0098  0.0329  0.0128  515 LYS A CB  
4300 C CG  . LYS A 515 ? 0.5708 0.6411 0.4758 0.0194  0.0355  0.0168  515 LYS A CG  
4301 C CD  . LYS A 515 ? 0.6257 0.6808 0.5297 0.0252  0.0415  0.0191  515 LYS A CD  
4302 C CE  . LYS A 515 ? 0.6570 0.7170 0.5626 0.0329  0.0427  0.0226  515 LYS A CE  
4303 N NZ  . LYS A 515 ? 0.6830 0.7594 0.5899 0.0432  0.0469  0.0279  515 LYS A NZ  
4304 N N   . ILE A 516 ? 0.4817 0.5405 0.3788 -0.0049 0.0314  0.0074  516 ILE A N   
4305 C CA  . ILE A 516 ? 0.4730 0.5367 0.3683 -0.0127 0.0286  0.0048  516 ILE A CA  
4306 C C   . ILE A 516 ? 0.4995 0.5684 0.3941 -0.0105 0.0340  0.0055  516 ILE A C   
4307 O O   . ILE A 516 ? 0.4844 0.5667 0.3796 -0.0129 0.0333  0.0047  516 ILE A O   
4308 C CB  . ILE A 516 ? 0.4627 0.5118 0.3540 -0.0217 0.0242  0.0020  516 ILE A CB  
4309 C CG1 . ILE A 516 ? 0.4486 0.4969 0.3408 -0.0249 0.0184  0.0009  516 ILE A CG1 
4310 C CG2 . ILE A 516 ? 0.4532 0.5038 0.3411 -0.0288 0.0235  0.0000  516 ILE A CG2 
4311 C CD1 . ILE A 516 ? 0.4344 0.4680 0.3233 -0.0312 0.0145  -0.0006 516 ILE A CD1 
4312 N N   . VAL A 517 ? 0.5013 0.5598 0.3948 -0.0060 0.0399  0.0068  517 VAL A N   
4313 C CA  . VAL A 517 ? 0.5133 0.5750 0.4063 -0.0028 0.0462  0.0076  517 VAL A CA  
4314 C C   . VAL A 517 ? 0.5461 0.6258 0.4431 0.0065  0.0496  0.0113  517 VAL A C   
4315 O O   . VAL A 517 ? 0.5669 0.6599 0.4649 0.0063  0.0506  0.0111  517 VAL A O   
4316 C CB  . VAL A 517 ? 0.5228 0.5674 0.4132 -0.0005 0.0528  0.0075  517 VAL A CB  
4317 C CG1 . VAL A 517 ? 0.5270 0.5750 0.4177 0.0058  0.0613  0.0093  517 VAL A CG1 
4318 C CG2 . VAL A 517 ? 0.4958 0.5274 0.3818 -0.0106 0.0498  0.0034  517 VAL A CG2 
4319 N N   . THR A 518 ? 0.5765 0.6578 0.4759 0.0148  0.0513  0.0147  518 THR A N   
4320 C CA  . THR A 518 ? 0.6071 0.7064 0.5102 0.0252  0.0545  0.0192  518 THR A CA  
4321 C C   . THR A 518 ? 0.6073 0.7296 0.5131 0.0221  0.0491  0.0180  518 THR A C   
4322 O O   . THR A 518 ? 0.6282 0.7684 0.5366 0.0278  0.0520  0.0202  518 THR A O   
4323 C CB  . THR A 518 ? 0.5986 0.6951 0.5029 0.0335  0.0561  0.0231  518 THR A CB  
4324 O OG1 . THR A 518 ? 0.6143 0.6904 0.5160 0.0368  0.0627  0.0241  518 THR A OG1 
4325 C CG2 . THR A 518 ? 0.6114 0.7284 0.5191 0.0450  0.0591  0.0284  518 THR A CG2 
4326 N N   . TYR A 519 ? 0.5691 0.6911 0.4744 0.0130  0.0419  0.0143  519 TYR A N   
4327 C CA  . TYR A 519 ? 0.5436 0.6862 0.4512 0.0088  0.0373  0.0122  519 TYR A CA  
4328 C C   . TYR A 519 ? 0.5327 0.6733 0.4378 -0.0031 0.0340  0.0073  519 TYR A C   
4329 O O   . TYR A 519 ? 0.5273 0.6769 0.4327 -0.0105 0.0295  0.0039  519 TYR A O   
4330 C CB  . TYR A 519 ? 0.5475 0.6933 0.4565 0.0083  0.0327  0.0118  519 TYR A CB  
4331 C CG  . TYR A 519 ? 0.5666 0.7158 0.4776 0.0204  0.0362  0.0171  519 TYR A CG  
4332 C CD1 . TYR A 519 ? 0.5893 0.7582 0.5032 0.0304  0.0402  0.0214  519 TYR A CD1 
4333 C CD2 . TYR A 519 ? 0.5609 0.6938 0.4708 0.0224  0.0360  0.0183  519 TYR A CD2 
4334 C CE1 . TYR A 519 ? 0.6204 0.7919 0.5354 0.0424  0.0441  0.0271  519 TYR A CE1 
4335 C CE2 . TYR A 519 ? 0.5868 0.7219 0.4979 0.0335  0.0400  0.0234  519 TYR A CE2 
4336 C CZ  . TYR A 519 ? 0.6065 0.7604 0.5199 0.0437  0.0441  0.0281  519 TYR A CZ  
4337 O OH  . TYR A 519 ? 0.6558 0.8118 0.5697 0.0556  0.0486  0.0341  519 TYR A OH  
4338 N N   . LYS A 520 ? 0.5309 0.6591 0.4330 -0.0052 0.0370  0.0067  520 LYS A N   
4339 C CA  . LYS A 520 ? 0.5372 0.6625 0.4361 -0.0157 0.0350  0.0028  520 LYS A CA  
4340 C C   . LYS A 520 ? 0.5288 0.6769 0.4301 -0.0177 0.0351  0.0013  520 LYS A C   
4341 O O   . LYS A 520 ? 0.5273 0.6909 0.4322 -0.0096 0.0391  0.0038  520 LYS A O   
4342 C CB  . LYS A 520 ? 0.5374 0.6479 0.4329 -0.0158 0.0392  0.0030  520 LYS A CB  
4343 C CG  . LYS A 520 ? 0.5557 0.6613 0.4469 -0.0264 0.0374  -0.0005 520 LYS A CG  
4344 C CD  . LYS A 520 ? 0.5486 0.6394 0.4360 -0.0268 0.0416  -0.0006 520 LYS A CD  
4345 C CE  . LYS A 520 ? 0.5677 0.6391 0.4524 -0.0280 0.0399  -0.0007 520 LYS A CE  
4346 N NZ  . LYS A 520 ? 0.5963 0.6548 0.4774 -0.0287 0.0445  -0.0016 520 LYS A NZ  
4347 N N   . GLY A 521 ? 0.5267 0.6769 0.4261 -0.0285 0.0310  -0.0028 521 GLY A N   
4348 C CA  . GLY A 521 ? 0.5456 0.7161 0.4465 -0.0329 0.0314  -0.0055 521 GLY A CA  
4349 C C   . GLY A 521 ? 0.5495 0.7113 0.4454 -0.0447 0.0303  -0.0094 521 GLY A C   
4350 O O   . GLY A 521 ? 0.5589 0.6995 0.4500 -0.0487 0.0291  -0.0094 521 GLY A O   
4351 N N   . GLY A 522 ? 0.5547 0.7339 0.4516 -0.0506 0.0306  -0.0127 522 GLY A N   
4352 C CA  . GLY A 522 ? 0.5315 0.7046 0.4235 -0.0616 0.0307  -0.0162 522 GLY A CA  
4353 C C   . GLY A 522 ? 0.5439 0.6959 0.4298 -0.0707 0.0271  -0.0179 522 GLY A C   
4354 O O   . GLY A 522 ? 0.5516 0.6936 0.4321 -0.0784 0.0275  -0.0194 522 GLY A O   
4355 N N   . LYS A 523 ? 0.5640 0.7095 0.4505 -0.0696 0.0239  -0.0174 523 LYS A N   
4356 C CA  . LYS A 523 ? 0.5441 0.6701 0.4251 -0.0773 0.0208  -0.0186 523 LYS A CA  
4357 C C   . LYS A 523 ? 0.5622 0.6662 0.4399 -0.0739 0.0195  -0.0152 523 LYS A C   
4358 O O   . LYS A 523 ? 0.5796 0.6670 0.4526 -0.0789 0.0169  -0.0153 523 LYS A O   
4359 C CB  . LYS A 523 ? 0.5317 0.6623 0.4148 -0.0794 0.0183  -0.0207 523 LYS A CB  
4360 C CG  . LYS A 523 ? 0.5238 0.6753 0.4089 -0.0859 0.0196  -0.0254 523 LYS A CG  
4361 C CD  . LYS A 523 ? 0.5079 0.6629 0.3942 -0.0896 0.0177  -0.0285 523 LYS A CD  
4362 C CE  . LYS A 523 ? 0.5328 0.7097 0.4206 -0.0976 0.0196  -0.0342 523 LYS A CE  
4363 N NZ  . LYS A 523 ? 0.5123 0.6967 0.4018 -0.1015 0.0185  -0.0381 523 LYS A NZ  
4364 N N   . TYR A 524 ? 0.5273 0.6315 0.4073 -0.0655 0.0217  -0.0124 524 TYR A N   
4365 C CA  . TYR A 524 ? 0.5399 0.6257 0.4171 -0.0628 0.0213  -0.0101 524 TYR A CA  
4366 C C   . TYR A 524 ? 0.5559 0.6293 0.4263 -0.0705 0.0208  -0.0109 524 TYR A C   
4367 O O   . TYR A 524 ? 0.5720 0.6520 0.4406 -0.0747 0.0231  -0.0124 524 TYR A O   
4368 C CB  . TYR A 524 ? 0.5373 0.6260 0.4176 -0.0535 0.0255  -0.0077 524 TYR A CB  
4369 C CG  . TYR A 524 ? 0.5322 0.6031 0.4096 -0.0517 0.0259  -0.0063 524 TYR A CG  
4370 C CD1 . TYR A 524 ? 0.5224 0.5838 0.4009 -0.0484 0.0236  -0.0051 524 TYR A CD1 
4371 C CD2 . TYR A 524 ? 0.5334 0.5976 0.4069 -0.0539 0.0288  -0.0068 524 TYR A CD2 
4372 C CE1 . TYR A 524 ? 0.5314 0.5782 0.4074 -0.0475 0.0241  -0.0045 524 TYR A CE1 
4373 C CE2 . TYR A 524 ? 0.5455 0.5950 0.4162 -0.0533 0.0293  -0.0064 524 TYR A CE2 
4374 C CZ  . TYR A 524 ? 0.5462 0.5875 0.4183 -0.0502 0.0270  -0.0054 524 TYR A CZ  
4375 O OH  . TYR A 524 ? 0.5549 0.5834 0.4245 -0.0502 0.0277  -0.0056 524 TYR A OH  
4376 N N   . ARG A 525 ? 0.5706 0.6271 0.4370 -0.0722 0.0179  -0.0098 525 ARG A N   
4377 C CA  . ARG A 525 ? 0.5765 0.6215 0.4358 -0.0784 0.0175  -0.0098 525 ARG A CA  
4378 C C   . ARG A 525 ? 0.5634 0.5994 0.4214 -0.0746 0.0184  -0.0085 525 ARG A C   
4379 O O   . ARG A 525 ? 0.5934 0.6304 0.4494 -0.0752 0.0218  -0.0090 525 ARG A O   
4380 C CB  . ARG A 525 ? 0.5920 0.6255 0.4464 -0.0845 0.0136  -0.0095 525 ARG A CB  
4381 C CG  . ARG A 525 ? 0.6515 0.6907 0.5078 -0.0874 0.0127  -0.0112 525 ARG A CG  
4382 C CD  . ARG A 525 ? 0.7009 0.7468 0.5543 -0.0954 0.0149  -0.0138 525 ARG A CD  
4383 N NE  . ARG A 525 ? 0.7967 0.8281 0.6421 -0.1027 0.0140  -0.0132 525 ARG A NE  
4384 C CZ  . ARG A 525 ? 0.7714 0.7989 0.6141 -0.1089 0.0142  -0.0148 525 ARG A CZ  
4385 N NH1 . ARG A 525 ? 0.7204 0.7586 0.5680 -0.1097 0.0148  -0.0178 525 ARG A NH1 
4386 N NH2 . ARG A 525 ? 0.7623 0.7751 0.5969 -0.1145 0.0142  -0.0133 525 ARG A NH2 
4387 N N   . LYS A 526 ? 0.5564 0.5839 0.4154 -0.0713 0.0159  -0.0072 526 LYS A N   
4388 C CA  . LYS A 526 ? 0.5301 0.5493 0.3882 -0.0684 0.0168  -0.0066 526 LYS A CA  
4389 C C   . LYS A 526 ? 0.5095 0.5219 0.3698 -0.0652 0.0134  -0.0056 526 LYS A C   
4390 O O   . LYS A 526 ? 0.4867 0.4927 0.3444 -0.0684 0.0091  -0.0048 526 LYS A O   
4391 C CB  . LYS A 526 ? 0.5677 0.5789 0.4185 -0.0744 0.0160  -0.0069 526 LYS A CB  
4392 C CG  . LYS A 526 ? 0.5764 0.5801 0.4259 -0.0729 0.0167  -0.0072 526 LYS A CG  
4393 C CD  . LYS A 526 ? 0.6025 0.6004 0.4443 -0.0791 0.0153  -0.0074 526 LYS A CD  
4394 C CE  . LYS A 526 ? 0.6031 0.5955 0.4437 -0.0783 0.0158  -0.0085 526 LYS A CE  
4395 N NZ  . LYS A 526 ? 0.6478 0.6362 0.4808 -0.0842 0.0132  -0.0083 526 LYS A NZ  
4396 N N   . VAL A 527 ? 0.4902 0.5036 0.3551 -0.0586 0.0160  -0.0054 527 VAL A N   
4397 C CA  . VAL A 527 ? 0.4543 0.4616 0.3216 -0.0552 0.0136  -0.0047 527 VAL A CA  
4398 C C   . VAL A 527 ? 0.4469 0.4472 0.3135 -0.0535 0.0164  -0.0055 527 VAL A C   
4399 O O   . VAL A 527 ? 0.4681 0.4703 0.3363 -0.0498 0.0220  -0.0059 527 VAL A O   
4400 C CB  . VAL A 527 ? 0.4501 0.4650 0.3236 -0.0489 0.0147  -0.0038 527 VAL A CB  
4401 C CG1 . VAL A 527 ? 0.4586 0.4668 0.3346 -0.0453 0.0130  -0.0033 527 VAL A CG1 
4402 C CG2 . VAL A 527 ? 0.4565 0.4796 0.3309 -0.0515 0.0121  -0.0040 527 VAL A CG2 
4403 N N   . THR A 528 ? 0.4068 0.3992 0.2709 -0.0562 0.0129  -0.0058 528 THR A N   
4404 C CA  . THR A 528 ? 0.4263 0.4133 0.2900 -0.0554 0.0154  -0.0074 528 THR A CA  
4405 C C   . THR A 528 ? 0.4241 0.4083 0.2923 -0.0508 0.0149  -0.0072 528 THR A C   
4406 O O   . THR A 528 ? 0.4261 0.4112 0.2967 -0.0494 0.0109  -0.0058 528 THR A O   
4407 C CB  . THR A 528 ? 0.4273 0.4098 0.2856 -0.0611 0.0122  -0.0083 528 THR A CB  
4408 O OG1 . THR A 528 ? 0.4224 0.4024 0.2810 -0.0613 0.0061  -0.0066 528 THR A OG1 
4409 C CG2 . THR A 528 ? 0.4276 0.4121 0.2803 -0.0663 0.0122  -0.0082 528 THR A CG2 
4410 N N   . PHE A 529 ? 0.4220 0.4025 0.2912 -0.0489 0.0197  -0.0090 529 PHE A N   
4411 C CA  . PHE A 529 ? 0.4285 0.4051 0.3011 -0.0458 0.0197  -0.0095 529 PHE A CA  
4412 C C   . PHE A 529 ? 0.4438 0.4183 0.3155 -0.0491 0.0128  -0.0096 529 PHE A C   
4413 O O   . PHE A 529 ? 0.4363 0.4103 0.3115 -0.0464 0.0099  -0.0087 529 PHE A O   
4414 C CB  . PHE A 529 ? 0.3995 0.3708 0.2716 -0.0455 0.0268  -0.0124 529 PHE A CB  
4415 C CG  . PHE A 529 ? 0.3900 0.3570 0.2654 -0.0427 0.0280  -0.0133 529 PHE A CG  
4416 C CD1 . PHE A 529 ? 0.3732 0.3402 0.2526 -0.0358 0.0314  -0.0112 529 PHE A CD1 
4417 C CD2 . PHE A 529 ? 0.3862 0.3502 0.2607 -0.0470 0.0258  -0.0163 529 PHE A CD2 
4418 C CE1 . PHE A 529 ? 0.3651 0.3276 0.2472 -0.0335 0.0330  -0.0121 529 PHE A CE1 
4419 C CE2 . PHE A 529 ? 0.3855 0.3462 0.2633 -0.0449 0.0273  -0.0175 529 PHE A CE2 
4420 C CZ  . PHE A 529 ? 0.3680 0.3271 0.2494 -0.0382 0.0310  -0.0154 529 PHE A CZ  
4421 N N   . GLN A 530 ? 0.4639 0.4378 0.3307 -0.0546 0.0104  -0.0105 530 GLN A N   
4422 C CA  . GLN A 530 ? 0.5033 0.4764 0.3685 -0.0571 0.0039  -0.0099 530 GLN A CA  
4423 C C   . GLN A 530 ? 0.4846 0.4579 0.3511 -0.0554 -0.0011 -0.0066 530 GLN A C   
4424 O O   . GLN A 530 ? 0.4533 0.4251 0.3222 -0.0536 -0.0047 -0.0058 530 GLN A O   
4425 C CB  . GLN A 530 ? 0.5319 0.5059 0.3907 -0.0628 0.0024  -0.0105 530 GLN A CB  
4426 C CG  . GLN A 530 ? 0.6085 0.5824 0.4654 -0.0660 0.0068  -0.0148 530 GLN A CG  
4427 C CD  . GLN A 530 ? 0.6371 0.6096 0.4948 -0.0649 0.0150  -0.0169 530 GLN A CD  
4428 O OE1 . GLN A 530 ? 0.5978 0.5718 0.4544 -0.0644 0.0167  -0.0153 530 GLN A OE1 
4429 N NE2 . GLN A 530 ? 0.6383 0.6078 0.4976 -0.0646 0.0207  -0.0205 530 GLN A NE2 
4430 N N   . CYS A 531 ? 0.4605 0.4358 0.3254 -0.0563 -0.0007 -0.0051 531 CYS A N   
4431 C CA  . CYS A 531 ? 0.4604 0.4355 0.3259 -0.0559 -0.0044 -0.0028 531 CYS A CA  
4432 C C   . CYS A 531 ? 0.4425 0.4184 0.3142 -0.0510 -0.0044 -0.0028 531 CYS A C   
4433 O O   . CYS A 531 ? 0.4227 0.3958 0.2956 -0.0502 -0.0081 -0.0018 531 CYS A O   
4434 C CB  . CYS A 531 ? 0.4816 0.4600 0.3446 -0.0585 -0.0029 -0.0023 531 CYS A CB  
4435 S SG  . CYS A 531 ? 0.5662 0.5436 0.4291 -0.0598 -0.0062 -0.0006 531 CYS A SG  
4436 N N   . LEU A 532 ? 0.4181 0.3976 0.2934 -0.0474 0.0000  -0.0038 532 LEU A N   
4437 C CA  . LEU A 532 ? 0.3909 0.3720 0.2714 -0.0425 0.0007  -0.0036 532 LEU A CA  
4438 C C   . LEU A 532 ? 0.3976 0.3739 0.2802 -0.0411 -0.0010 -0.0043 532 LEU A C   
4439 O O   . LEU A 532 ? 0.3944 0.3702 0.2801 -0.0390 -0.0035 -0.0037 532 LEU A O   
4440 C CB  . LEU A 532 ? 0.4140 0.3993 0.2968 -0.0382 0.0066  -0.0037 532 LEU A CB  
4441 C CG  . LEU A 532 ? 0.4067 0.4004 0.2894 -0.0378 0.0085  -0.0028 532 LEU A CG  
4442 C CD1 . LEU A 532 ? 0.4024 0.3994 0.2866 -0.0329 0.0151  -0.0024 532 LEU A CD1 
4443 C CD2 . LEU A 532 ? 0.4079 0.4077 0.2934 -0.0368 0.0058  -0.0021 532 LEU A CD2 
4444 N N   . LYS A 533 ? 0.3917 0.3650 0.2726 -0.0428 0.0003  -0.0059 533 LYS A N   
4445 C CA  . LYS A 533 ? 0.3824 0.3530 0.2655 -0.0421 -0.0010 -0.0072 533 LYS A CA  
4446 C C   . LYS A 533 ? 0.3744 0.3439 0.2572 -0.0431 -0.0074 -0.0057 533 LYS A C   
4447 O O   . LYS A 533 ? 0.3560 0.3245 0.2425 -0.0406 -0.0092 -0.0058 533 LYS A O   
4448 C CB  . LYS A 533 ? 0.4127 0.3820 0.2934 -0.0452 0.0015  -0.0099 533 LYS A CB  
4449 C CG  . LYS A 533 ? 0.4468 0.4143 0.3306 -0.0443 0.0031  -0.0125 533 LYS A CG  
4450 C CD  . LYS A 533 ? 0.4419 0.4074 0.3241 -0.0464 0.0099  -0.0160 533 LYS A CD  
4451 C CE  . LYS A 533 ? 0.4697 0.4373 0.3469 -0.0524 0.0086  -0.0179 533 LYS A CE  
4452 N NZ  . LYS A 533 ? 0.4867 0.4565 0.3640 -0.0558 0.0065  -0.0210 533 LYS A NZ  
4453 N N   . SER A 534 ? 0.3792 0.3483 0.2574 -0.0463 -0.0103 -0.0041 534 SER A N   
4454 C CA  . SER A 534 ? 0.3963 0.3629 0.2732 -0.0467 -0.0156 -0.0018 534 SER A CA  
4455 C C   . SER A 534 ? 0.4010 0.3660 0.2807 -0.0444 -0.0167 -0.0006 534 SER A C   
4456 O O   . SER A 534 ? 0.4226 0.3850 0.3040 -0.0426 -0.0197 0.0003  534 SER A O   
4457 C CB  . SER A 534 ? 0.3943 0.3597 0.2645 -0.0506 -0.0174 0.0002  534 SER A CB  
4458 O OG  . SER A 534 ? 0.4205 0.3881 0.2877 -0.0530 -0.0173 -0.0009 534 SER A OG  
4459 N N   . ILE A 535 ? 0.4090 0.3763 0.2889 -0.0447 -0.0142 -0.0007 535 ILE A N   
4460 C CA  . ILE A 535 ? 0.4006 0.3685 0.2834 -0.0433 -0.0146 -0.0006 535 ILE A CA  
4461 C C   . ILE A 535 ? 0.4056 0.3740 0.2940 -0.0389 -0.0144 -0.0016 535 ILE A C   
4462 O O   . ILE A 535 ? 0.3981 0.3639 0.2885 -0.0377 -0.0165 -0.0014 535 ILE A O   
4463 C CB  . ILE A 535 ? 0.3952 0.3691 0.2776 -0.0445 -0.0116 -0.0012 535 ILE A CB  
4464 C CG1 . ILE A 535 ? 0.3970 0.3693 0.2736 -0.0496 -0.0120 -0.0004 535 ILE A CG1 
4465 C CG2 . ILE A 535 ? 0.3961 0.3737 0.2820 -0.0430 -0.0113 -0.0020 535 ILE A CG2 
4466 C CD1 . ILE A 535 ? 0.3999 0.3794 0.2760 -0.0516 -0.0092 -0.0013 535 ILE A CD1 
4467 N N   . ALA A 536 ? 0.3767 0.3474 0.2673 -0.0367 -0.0113 -0.0028 536 ALA A N   
4468 C CA  . ALA A 536 ? 0.3753 0.3460 0.2706 -0.0328 -0.0102 -0.0038 536 ALA A CA  
4469 C C   . ALA A 536 ? 0.3763 0.3433 0.2729 -0.0327 -0.0138 -0.0041 536 ALA A C   
4470 O O   . ALA A 536 ? 0.3514 0.3177 0.2516 -0.0303 -0.0150 -0.0043 536 ALA A O   
4471 C CB  . ALA A 536 ? 0.3568 0.3287 0.2529 -0.0310 -0.0051 -0.0049 536 ALA A CB  
4472 N N   . TRP A 537 ? 0.3747 0.3406 0.2686 -0.0351 -0.0153 -0.0042 537 TRP A N   
4473 C CA  . TRP A 537 ? 0.3872 0.3522 0.2824 -0.0346 -0.0190 -0.0042 537 TRP A CA  
4474 C C   . TRP A 537 ? 0.4123 0.3741 0.3074 -0.0335 -0.0226 -0.0018 537 TRP A C   
4475 O O   . TRP A 537 ? 0.4041 0.3650 0.3025 -0.0310 -0.0247 -0.0017 537 TRP A O   
4476 C CB  . TRP A 537 ? 0.3714 0.3381 0.2628 -0.0377 -0.0204 -0.0044 537 TRP A CB  
4477 C CG  . TRP A 537 ? 0.3582 0.3274 0.2506 -0.0391 -0.0167 -0.0080 537 TRP A CG  
4478 C CD1 . TRP A 537 ? 0.3529 0.3232 0.2417 -0.0424 -0.0133 -0.0096 537 TRP A CD1 
4479 C CD2 . TRP A 537 ? 0.3395 0.3099 0.2366 -0.0376 -0.0150 -0.0108 537 TRP A CD2 
4480 N NE1 . TRP A 537 ? 0.3545 0.3256 0.2453 -0.0433 -0.0092 -0.0135 537 TRP A NE1 
4481 C CE2 . TRP A 537 ? 0.3493 0.3205 0.2450 -0.0407 -0.0099 -0.0144 537 TRP A CE2 
4482 C CE3 . TRP A 537 ? 0.3323 0.3027 0.2344 -0.0345 -0.0164 -0.0111 537 TRP A CE3 
4483 C CZ2 . TRP A 537 ? 0.3408 0.3123 0.2397 -0.0410 -0.0063 -0.0181 537 TRP A CZ2 
4484 C CZ3 . TRP A 537 ? 0.3254 0.2970 0.2310 -0.0346 -0.0132 -0.0146 537 TRP A CZ3 
4485 C CH2 . TRP A 537 ? 0.3432 0.3150 0.2471 -0.0379 -0.0081 -0.0181 537 TRP A CH2 
4486 N N   . ARG A 538 ? 0.4118 0.3714 0.3030 -0.0355 -0.0227 -0.0001 538 ARG A N   
4487 C CA  . ARG A 538 ? 0.4534 0.4080 0.3434 -0.0352 -0.0249 0.0018  538 ARG A CA  
4488 C C   . ARG A 538 ? 0.4323 0.3867 0.3270 -0.0330 -0.0239 0.0004  538 ARG A C   
4489 O O   . ARG A 538 ? 0.4403 0.3905 0.3362 -0.0315 -0.0254 0.0011  538 ARG A O   
4490 C CB  . ARG A 538 ? 0.4582 0.4100 0.3424 -0.0390 -0.0244 0.0034  538 ARG A CB  
4491 C CG  . ARG A 538 ? 0.5000 0.4502 0.3786 -0.0408 -0.0263 0.0059  538 ARG A CG  
4492 C CD  . ARG A 538 ? 0.5533 0.4981 0.4259 -0.0441 -0.0258 0.0080  538 ARG A CD  
4493 N NE  . ARG A 538 ? 0.6012 0.5445 0.4674 -0.0459 -0.0272 0.0108  538 ARG A NE  
4494 C CZ  . ARG A 538 ? 0.6085 0.5451 0.4701 -0.0451 -0.0290 0.0148  538 ARG A CZ  
4495 N NH1 . ARG A 538 ? 0.6190 0.5489 0.4821 -0.0425 -0.0292 0.0161  538 ARG A NH1 
4496 N NH2 . ARG A 538 ? 0.5669 0.5031 0.4221 -0.0467 -0.0301 0.0177  538 ARG A NH2 
4497 N N   . ALA A 539 ? 0.4267 0.3861 0.3239 -0.0325 -0.0209 -0.0014 539 ALA A N   
4498 C CA  . ALA A 539 ? 0.3946 0.3557 0.2956 -0.0306 -0.0197 -0.0028 539 ALA A CA  
4499 C C   . ALA A 539 ? 0.4012 0.3614 0.3068 -0.0271 -0.0206 -0.0036 539 ALA A C   
4500 O O   . ALA A 539 ? 0.4310 0.3895 0.3392 -0.0257 -0.0212 -0.0042 539 ALA A O   
4501 C CB  . ALA A 539 ? 0.3562 0.3242 0.2581 -0.0301 -0.0164 -0.0038 539 ALA A CB  
4502 N N   . PHE A 540 ? 0.3887 0.3501 0.2952 -0.0263 -0.0203 -0.0041 540 PHE A N   
4503 C CA  . PHE A 540 ? 0.3963 0.3579 0.3072 -0.0237 -0.0209 -0.0053 540 PHE A CA  
4504 C C   . PHE A 540 ? 0.4270 0.3855 0.3382 -0.0229 -0.0248 -0.0041 540 PHE A C   
4505 O O   . PHE A 540 ? 0.4514 0.4090 0.3665 -0.0204 -0.0256 -0.0047 540 PHE A O   
4506 C CB  . PHE A 540 ? 0.3763 0.3403 0.2876 -0.0242 -0.0188 -0.0070 540 PHE A CB  
4507 C CG  . PHE A 540 ? 0.3764 0.3419 0.2895 -0.0225 -0.0139 -0.0083 540 PHE A CG  
4508 C CD1 . PHE A 540 ? 0.3743 0.3399 0.2918 -0.0199 -0.0123 -0.0098 540 PHE A CD1 
4509 C CD2 . PHE A 540 ? 0.3874 0.3542 0.2979 -0.0231 -0.0104 -0.0078 540 PHE A CD2 
4510 C CE1 . PHE A 540 ? 0.3844 0.3506 0.3029 -0.0176 -0.0073 -0.0102 540 PHE A CE1 
4511 C CE2 . PHE A 540 ? 0.3898 0.3576 0.3016 -0.0202 -0.0053 -0.0081 540 PHE A CE2 
4512 C CZ  . PHE A 540 ? 0.3817 0.3489 0.2972 -0.0174 -0.0037 -0.0091 540 PHE A CZ  
4513 N N   . LEU A 541 ? 0.4508 0.4078 0.3576 -0.0247 -0.0271 -0.0019 541 LEU A N   
4514 C CA  . LEU A 541 ? 0.4425 0.3964 0.3487 -0.0230 -0.0305 0.0004  541 LEU A CA  
4515 C C   . LEU A 541 ? 0.4635 0.4111 0.3703 -0.0216 -0.0303 0.0012  541 LEU A C   
4516 O O   . LEU A 541 ? 0.5028 0.4479 0.4119 -0.0185 -0.0318 0.0022  541 LEU A O   
4517 C CB  . LEU A 541 ? 0.4710 0.4237 0.3711 -0.0250 -0.0322 0.0033  541 LEU A CB  
4518 C CG  . LEU A 541 ? 0.4649 0.4241 0.3640 -0.0262 -0.0334 0.0027  541 LEU A CG  
4519 C CD1 . LEU A 541 ? 0.4823 0.4399 0.3747 -0.0281 -0.0352 0.0061  541 LEU A CD1 
4520 C CD2 . LEU A 541 ? 0.4733 0.4375 0.3770 -0.0232 -0.0357 0.0019  541 LEU A CD2 
4521 N N   . ALA A 542 ? 0.4471 0.3926 0.3518 -0.0242 -0.0280 0.0006  542 ALA A N   
4522 C CA  . ALA A 542 ? 0.4373 0.3767 0.3416 -0.0243 -0.0272 0.0007  542 ALA A CA  
4523 C C   . ALA A 542 ? 0.4231 0.3639 0.3334 -0.0215 -0.0264 -0.0017 542 ALA A C   
4524 O O   . ALA A 542 ? 0.3932 0.3285 0.3043 -0.0206 -0.0260 -0.0019 542 ALA A O   
4525 C CB  . ALA A 542 ? 0.4213 0.3601 0.3219 -0.0287 -0.0248 -0.0001 542 ALA A CB  
4526 N N   . VAL A 543 ? 0.4213 0.3689 0.3354 -0.0204 -0.0258 -0.0037 543 VAL A N   
4527 C CA  . VAL A 543 ? 0.4226 0.3722 0.3419 -0.0179 -0.0247 -0.0060 543 VAL A CA  
4528 C C   . VAL A 543 ? 0.4288 0.3787 0.3519 -0.0146 -0.0266 -0.0059 543 VAL A C   
4529 O O   . VAL A 543 ? 0.4418 0.3897 0.3683 -0.0123 -0.0268 -0.0066 543 VAL A O   
4530 C CB  . VAL A 543 ? 0.4364 0.3926 0.3572 -0.0179 -0.0221 -0.0077 543 VAL A CB  
4531 C CG1 . VAL A 543 ? 0.4367 0.3949 0.3626 -0.0150 -0.0211 -0.0096 543 VAL A CG1 
4532 C CG2 . VAL A 543 ? 0.4255 0.3843 0.3438 -0.0204 -0.0202 -0.0082 543 VAL A CG2 
4533 N N   . LEU A 544 ? 0.4278 0.3812 0.3505 -0.0148 -0.0278 -0.0054 544 LEU A N   
4534 C CA  . LEU A 544 ? 0.4216 0.3782 0.3482 -0.0123 -0.0296 -0.0059 544 LEU A CA  
4535 C C   . LEU A 544 ? 0.4685 0.4214 0.3953 -0.0095 -0.0323 -0.0033 544 LEU A C   
4536 O O   . LEU A 544 ? 0.4564 0.4117 0.3880 -0.0062 -0.0334 -0.0040 544 LEU A O   
4537 C CB  . LEU A 544 ? 0.3936 0.3554 0.3187 -0.0142 -0.0301 -0.0062 544 LEU A CB  
4538 C CG  . LEU A 544 ? 0.3882 0.3527 0.3134 -0.0164 -0.0263 -0.0088 544 LEU A CG  
4539 C CD1 . LEU A 544 ? 0.3536 0.3219 0.2760 -0.0193 -0.0264 -0.0093 544 LEU A CD1 
4540 C CD2 . LEU A 544 ? 0.3487 0.3152 0.2792 -0.0147 -0.0240 -0.0117 544 LEU A CD2 
4541 N N   . LYS A 545 ? 0.4826 0.4297 0.4042 -0.0104 -0.0330 -0.0003 545 LYS A N   
4542 C CA  . LYS A 545 ? 0.5178 0.4594 0.4382 -0.0070 -0.0347 0.0031  545 LYS A CA  
4543 C C   . LYS A 545 ? 0.5242 0.4607 0.4484 -0.0044 -0.0332 0.0019  545 LYS A C   
4544 O O   . LYS A 545 ? 0.5161 0.4493 0.4415 0.0000  -0.0341 0.0043  545 LYS A O   
4545 C CB  . LYS A 545 ? 0.5270 0.4612 0.4402 -0.0091 -0.0344 0.0064  545 LYS A CB  
4546 C CG  . LYS A 545 ? 0.5702 0.5076 0.4792 -0.0090 -0.0371 0.0099  545 LYS A CG  
4547 C CD  . LYS A 545 ? 0.6063 0.5372 0.5080 -0.0127 -0.0357 0.0120  545 LYS A CD  
4548 C CE  . LYS A 545 ? 0.6654 0.5933 0.5617 -0.0104 -0.0377 0.0175  545 LYS A CE  
4549 N NZ  . LYS A 545 ? 0.7412 0.6589 0.6301 -0.0137 -0.0352 0.0197  545 LYS A NZ  
4550 N N   . ARG A 546 ? 0.5009 0.4372 0.4266 -0.0068 -0.0305 -0.0015 546 ARG A N   
4551 C CA  . ARG A 546 ? 0.4878 0.4203 0.4170 -0.0052 -0.0286 -0.0035 546 ARG A CA  
4552 C C   . ARG A 546 ? 0.4770 0.4142 0.4128 -0.0010 -0.0297 -0.0047 546 ARG A C   
4553 O O   . ARG A 546 ? 0.4674 0.4011 0.4062 0.0011  -0.0284 -0.0060 546 ARG A O   
4554 C CB  . ARG A 546 ? 0.4416 0.3756 0.3707 -0.0088 -0.0257 -0.0070 546 ARG A CB  
4555 C CG  . ARG A 546 ? 0.4552 0.3845 0.3785 -0.0132 -0.0240 -0.0067 546 ARG A CG  
4556 C CD  . ARG A 546 ? 0.4584 0.3908 0.3824 -0.0162 -0.0212 -0.0104 546 ARG A CD  
4557 N NE  . ARG A 546 ? 0.4138 0.3422 0.3405 -0.0152 -0.0194 -0.0128 546 ARG A NE  
4558 C CZ  . ARG A 546 ? 0.4248 0.3558 0.3519 -0.0181 -0.0168 -0.0164 546 ARG A CZ  
4559 N NH1 . ARG A 546 ? 0.4045 0.3430 0.3295 -0.0216 -0.0159 -0.0178 546 ARG A NH1 
4560 N NH2 . ARG A 546 ? 0.4084 0.3350 0.3377 -0.0174 -0.0149 -0.0188 546 ARG A NH2 
4561 N N   . ARG A 547 ? 0.4592 0.4047 0.3971 -0.0004 -0.0317 -0.0049 547 ARG A N   
4562 C CA  . ARG A 547 ? 0.4854 0.4371 0.4294 0.0031  -0.0331 -0.0060 547 ARG A CA  
4563 C C   . ARG A 547 ? 0.4965 0.4547 0.4401 0.0045  -0.0364 -0.0037 547 ARG A C   
4564 O O   . ARG A 547 ? 0.4678 0.4348 0.4135 0.0029  -0.0370 -0.0060 547 ARG A O   
4565 C CB  . ARG A 547 ? 0.4893 0.4471 0.4372 0.0014  -0.0311 -0.0102 547 ARG A CB  
4566 C CG  . ARG A 547 ? 0.5087 0.4631 0.4570 0.0001  -0.0279 -0.0126 547 ARG A CG  
4567 C CD  . ARG A 547 ? 0.5170 0.4770 0.4693 -0.0001 -0.0258 -0.0159 547 ARG A CD  
4568 N NE  . ARG A 547 ? 0.5136 0.4729 0.4642 -0.0019 -0.0226 -0.0172 547 ARG A NE  
4569 C CZ  . ARG A 547 ? 0.5410 0.4988 0.4929 -0.0014 -0.0209 -0.0187 547 ARG A CZ  
4570 N NH1 . ARG A 547 ? 0.5504 0.5054 0.5054 0.0007  -0.0215 -0.0195 547 ARG A NH1 
4571 N NH2 . ARG A 547 ? 0.5138 0.4734 0.4637 -0.0028 -0.0183 -0.0195 547 ARG A NH2 
4572 N N   . THR A 548 ? 0.5232 0.4770 0.4634 0.0073  -0.0382 0.0007  548 THR A N   
4573 C CA  . THR A 548 ? 0.5794 0.5402 0.5176 0.0087  -0.0417 0.0039  548 THR A CA  
4574 C C   . THR A 548 ? 0.5950 0.5684 0.5395 0.0113  -0.0439 0.0021  548 THR A C   
4575 O O   . THR A 548 ? 0.6693 0.6529 0.6134 0.0096  -0.0460 0.0016  548 THR A O   
4576 C CB  . THR A 548 ? 0.5955 0.5489 0.5288 0.0126  -0.0427 0.0100  548 THR A CB  
4577 O OG1 . THR A 548 ? 0.6520 0.5958 0.5870 0.0164  -0.0405 0.0108  548 THR A OG1 
4578 C CG2 . THR A 548 ? 0.5686 0.5144 0.4939 0.0084  -0.0417 0.0120  548 THR A CG2 
4579 N N   . GLU A 549 ? 0.5969 0.5706 0.5474 0.0150  -0.0431 0.0007  549 GLU A N   
4580 C CA  . GLU A 549 ? 0.6352 0.6219 0.5926 0.0173  -0.0448 -0.0016 549 GLU A CA  
4581 C C   . GLU A 549 ? 0.5875 0.5820 0.5473 0.0116  -0.0433 -0.0074 549 GLU A C   
4582 O O   . GLU A 549 ? 0.6392 0.6461 0.6011 0.0103  -0.0450 -0.0092 549 GLU A O   
4583 C CB  . GLU A 549 ? 0.6767 0.6610 0.6400 0.0225  -0.0437 -0.0020 549 GLU A CB  
4584 C CG  . GLU A 549 ? 0.7615 0.7388 0.7270 0.0198  -0.0398 -0.0064 549 GLU A CG  
4585 C CD  . GLU A 549 ? 0.7621 0.7263 0.7216 0.0168  -0.0373 -0.0054 549 GLU A CD  
4586 O OE1 . GLU A 549 ? 0.8233 0.7795 0.7780 0.0186  -0.0376 -0.0012 549 GLU A OE1 
4587 O OE2 . GLU A 549 ? 0.7075 0.6696 0.6668 0.0128  -0.0346 -0.0089 549 GLU A OE2 
4588 N N   . ILE A 550 ? 0.5384 0.5258 0.4977 0.0082  -0.0397 -0.0102 550 ILE A N   
4589 C CA  . ILE A 550 ? 0.5177 0.5096 0.4782 0.0033  -0.0370 -0.0150 550 ILE A CA  
4590 C C   . ILE A 550 ? 0.5170 0.5110 0.4721 -0.0012 -0.0372 -0.0148 550 ILE A C   
4591 O O   . ILE A 550 ? 0.5052 0.5073 0.4614 -0.0045 -0.0365 -0.0182 550 ILE A O   
4592 C CB  . ILE A 550 ? 0.4977 0.4817 0.4585 0.0020  -0.0329 -0.0171 550 ILE A CB  
4593 C CG1 . ILE A 550 ? 0.5064 0.4923 0.4738 0.0048  -0.0319 -0.0196 550 ILE A CG1 
4594 C CG2 . ILE A 550 ? 0.4897 0.4743 0.4485 -0.0026 -0.0294 -0.0200 550 ILE A CG2 
4595 C CD1 . ILE A 550 ? 0.4598 0.4371 0.4272 0.0061  -0.0296 -0.0196 550 ILE A CD1 
4596 N N   . TYR A 551 ? 0.5091 0.4958 0.4582 -0.0016 -0.0378 -0.0112 551 TYR A N   
4597 C CA  . TYR A 551 ? 0.4813 0.4682 0.4251 -0.0061 -0.0370 -0.0114 551 TYR A CA  
4598 C C   . TYR A 551 ? 0.4911 0.4832 0.4310 -0.0061 -0.0409 -0.0083 551 TYR A C   
4599 O O   . TYR A 551 ? 0.4810 0.4734 0.4160 -0.0100 -0.0404 -0.0082 551 TYR A O   
4600 C CB  . TYR A 551 ? 0.4509 0.4279 0.3905 -0.0074 -0.0347 -0.0100 551 TYR A CB  
4601 C CG  . TYR A 551 ? 0.4183 0.3924 0.3602 -0.0083 -0.0305 -0.0130 551 TYR A CG  
4602 C CD1 . TYR A 551 ? 0.4168 0.3948 0.3606 -0.0106 -0.0272 -0.0167 551 TYR A CD1 
4603 C CD2 . TYR A 551 ? 0.3949 0.3625 0.3362 -0.0071 -0.0292 -0.0121 551 TYR A CD2 
4604 C CE1 . TYR A 551 ? 0.3966 0.3714 0.3416 -0.0106 -0.0229 -0.0185 551 TYR A CE1 
4605 C CE2 . TYR A 551 ? 0.4001 0.3666 0.3429 -0.0075 -0.0256 -0.0142 551 TYR A CE2 
4606 C CZ  . TYR A 551 ? 0.4106 0.3804 0.3550 -0.0087 -0.0225 -0.0170 551 TYR A CZ  
4607 O OH  . TYR A 551 ? 0.4251 0.3935 0.3702 -0.0083 -0.0185 -0.0182 551 TYR A OH  
4608 N N   . LYS A 552 ? 0.4994 0.4961 0.4414 -0.0014 -0.0444 -0.0055 552 LYS A N   
4609 C CA  . LYS A 552 ? 0.5384 0.5426 0.4774 0.0000  -0.0484 -0.0020 552 LYS A CA  
4610 C C   . LYS A 552 ? 0.4954 0.5085 0.4315 -0.0058 -0.0485 -0.0047 552 LYS A C   
4611 O O   . LYS A 552 ? 0.4951 0.5064 0.4247 -0.0076 -0.0494 -0.0021 552 LYS A O   
4612 C CB  . LYS A 552 ? 0.6014 0.6155 0.5459 0.0056  -0.0514 -0.0008 552 LYS A CB  
4613 C CG  . LYS A 552 ? 0.6871 0.7114 0.6287 0.0085  -0.0559 0.0035  552 LYS A CG  
4614 C CD  . LYS A 552 ? 0.7450 0.7611 0.6841 0.0161  -0.0574 0.0109  552 LYS A CD  
4615 C CE  . LYS A 552 ? 0.8112 0.8387 0.7473 0.0202  -0.0618 0.0162  552 LYS A CE  
4616 N NZ  . LYS A 552 ? 0.8074 0.8360 0.7357 0.0151  -0.0626 0.0172  552 LYS A NZ  
4617 N N   . GLY A 553 ? 0.4620 0.4847 0.4027 -0.0089 -0.0470 -0.0104 553 GLY A N   
4618 C CA  . GLY A 553 ? 0.4487 0.4806 0.3871 -0.0151 -0.0463 -0.0143 553 GLY A CA  
4619 C C   . GLY A 553 ? 0.4475 0.4698 0.3804 -0.0200 -0.0424 -0.0154 553 GLY A C   
4620 O O   . GLY A 553 ? 0.4609 0.4871 0.3891 -0.0241 -0.0426 -0.0159 553 GLY A O   
4621 N N   . LEU A 554 ? 0.4287 0.4394 0.3624 -0.0195 -0.0388 -0.0157 554 LEU A N   
4622 C CA  . LEU A 554 ? 0.4203 0.4229 0.3497 -0.0232 -0.0346 -0.0166 554 LEU A CA  
4623 C C   . LEU A 554 ? 0.4313 0.4286 0.3544 -0.0227 -0.0367 -0.0117 554 LEU A C   
4624 O O   . LEU A 554 ? 0.4201 0.4178 0.3384 -0.0267 -0.0355 -0.0122 554 LEU A O   
4625 C CB  . LEU A 554 ? 0.4016 0.3957 0.3338 -0.0217 -0.0306 -0.0177 554 LEU A CB  
4626 C CG  . LEU A 554 ? 0.4128 0.3997 0.3418 -0.0241 -0.0255 -0.0185 554 LEU A CG  
4627 C CD1 . LEU A 554 ? 0.4065 0.3967 0.3333 -0.0293 -0.0218 -0.0225 554 LEU A CD1 
4628 C CD2 . LEU A 554 ? 0.3889 0.3708 0.3215 -0.0218 -0.0219 -0.0196 554 LEU A CD2 
4629 N N   . ILE A 555 ? 0.4487 0.4407 0.3716 -0.0182 -0.0394 -0.0071 555 ILE A N   
4630 C CA  . ILE A 555 ? 0.4673 0.4539 0.3840 -0.0175 -0.0414 -0.0022 555 ILE A CA  
4631 C C   . ILE A 555 ? 0.4840 0.4786 0.3964 -0.0191 -0.0444 -0.0006 555 ILE A C   
4632 O O   . ILE A 555 ? 0.5367 0.5287 0.4431 -0.0221 -0.0439 0.0007  555 ILE A O   
4633 C CB  . ILE A 555 ? 0.4642 0.4443 0.3818 -0.0122 -0.0433 0.0020  555 ILE A CB  
4634 C CG1 . ILE A 555 ? 0.4406 0.4133 0.3617 -0.0113 -0.0403 0.0001  555 ILE A CG1 
4635 C CG2 . ILE A 555 ? 0.4384 0.4118 0.3488 -0.0119 -0.0446 0.0072  555 ILE A CG2 
4636 C CD1 . ILE A 555 ? 0.4431 0.4104 0.3665 -0.0063 -0.0413 0.0026  555 ILE A CD1 
4637 N N   . ASP A 556 ? 0.4953 0.5010 0.4106 -0.0172 -0.0475 -0.0008 556 ASP A N   
4638 C CA  . ASP A 556 ? 0.4920 0.5084 0.4033 -0.0186 -0.0507 0.0004  556 ASP A CA  
4639 C C   . ASP A 556 ? 0.4901 0.5109 0.3988 -0.0260 -0.0478 -0.0047 556 ASP A C   
4640 O O   . ASP A 556 ? 0.5176 0.5405 0.4201 -0.0287 -0.0488 -0.0031 556 ASP A O   
4641 C CB  . ASP A 556 ? 0.5299 0.5603 0.4458 -0.0150 -0.0544 0.0005  556 ASP A CB  
4642 C CG  . ASP A 556 ? 0.6036 0.6298 0.5204 -0.0068 -0.0573 0.0069  556 ASP A CG  
4643 O OD1 . ASP A 556 ? 0.6335 0.6468 0.5454 -0.0047 -0.0568 0.0119  556 ASP A OD1 
4644 O OD2 . ASP A 556 ? 0.6380 0.6734 0.5605 -0.0024 -0.0595 0.0068  556 ASP A OD2 
4645 N N   . ARG A 557 ? 0.4536 0.4754 0.3668 -0.0292 -0.0438 -0.0108 557 ARG A N   
4646 C CA  . ARG A 557 ? 0.4653 0.4882 0.3758 -0.0361 -0.0395 -0.0159 557 ARG A CA  
4647 C C   . ARG A 557 ? 0.4521 0.4641 0.3569 -0.0376 -0.0371 -0.0135 557 ARG A C   
4648 O O   . ARG A 557 ? 0.4681 0.4823 0.3680 -0.0421 -0.0359 -0.0148 557 ARG A O   
4649 C CB  . ARG A 557 ? 0.4638 0.4861 0.3795 -0.0388 -0.0341 -0.0223 557 ARG A CB  
4650 C CG  . ARG A 557 ? 0.4856 0.5079 0.3984 -0.0458 -0.0283 -0.0278 557 ARG A CG  
4651 C CD  . ARG A 557 ? 0.5056 0.5276 0.4230 -0.0487 -0.0224 -0.0342 557 ARG A CD  
4652 N NE  . ARG A 557 ? 0.5386 0.5744 0.4602 -0.0504 -0.0245 -0.0381 557 ARG A NE  
4653 C CZ  . ARG A 557 ? 0.5679 0.6068 0.4931 -0.0547 -0.0195 -0.0449 557 ARG A CZ  
4654 N NH1 . ARG A 557 ? 0.5365 0.5642 0.4612 -0.0571 -0.0115 -0.0481 557 ARG A NH1 
4655 N NH2 . ARG A 557 ? 0.5547 0.6086 0.4840 -0.0563 -0.0222 -0.0483 557 ARG A NH2 
4656 N N   . ILE A 558 ? 0.4243 0.4255 0.3297 -0.0340 -0.0365 -0.0104 558 ILE A N   
4657 C CA  . ILE A 558 ? 0.4212 0.4140 0.3219 -0.0357 -0.0340 -0.0088 558 ILE A CA  
4658 C C   . ILE A 558 ? 0.4370 0.4307 0.3310 -0.0363 -0.0374 -0.0045 558 ILE A C   
4659 O O   . ILE A 558 ? 0.4179 0.4112 0.3071 -0.0403 -0.0355 -0.0052 558 ILE A O   
4660 C CB  . ILE A 558 ? 0.4013 0.3847 0.3042 -0.0323 -0.0324 -0.0070 558 ILE A CB  
4661 C CG1 . ILE A 558 ? 0.3782 0.3608 0.2867 -0.0318 -0.0284 -0.0110 558 ILE A CG1 
4662 C CG2 . ILE A 558 ? 0.3988 0.3761 0.2968 -0.0342 -0.0302 -0.0054 558 ILE A CG2 
4663 C CD1 . ILE A 558 ? 0.3594 0.3354 0.2706 -0.0282 -0.0274 -0.0095 558 ILE A CD1 
4664 N N   . LYS A 559 ? 0.4609 0.4560 0.3547 -0.0322 -0.0420 0.0000  559 LYS A N   
4665 C CA  . LYS A 559 ? 0.4772 0.4720 0.3641 -0.0318 -0.0450 0.0050  559 LYS A CA  
4666 C C   . LYS A 559 ? 0.4713 0.4777 0.3545 -0.0355 -0.0466 0.0035  559 LYS A C   
4667 O O   . LYS A 559 ? 0.4515 0.4574 0.3279 -0.0377 -0.0471 0.0061  559 LYS A O   
4668 C CB  . LYS A 559 ? 0.4945 0.4870 0.3818 -0.0254 -0.0486 0.0106  559 LYS A CB  
4669 C CG  . LYS A 559 ? 0.5013 0.4812 0.3905 -0.0227 -0.0467 0.0121  559 LYS A CG  
4670 C CD  . LYS A 559 ? 0.5339 0.5088 0.4216 -0.0168 -0.0492 0.0181  559 LYS A CD  
4671 C CE  . LYS A 559 ? 0.5700 0.5313 0.4579 -0.0160 -0.0462 0.0189  559 LYS A CE  
4672 N NZ  . LYS A 559 ? 0.6329 0.5875 0.5203 -0.0101 -0.0473 0.0240  559 LYS A NZ  
4673 N N   . SER A 560 ? 0.4571 0.4748 0.3446 -0.0368 -0.0470 -0.0008 560 SER A N   
4674 C CA  . SER A 560 ? 0.4799 0.5106 0.3639 -0.0413 -0.0483 -0.0031 560 SER A CA  
4675 C C   . SER A 560 ? 0.4725 0.5026 0.3545 -0.0487 -0.0430 -0.0093 560 SER A C   
4676 O O   . SER A 560 ? 0.4817 0.5189 0.3584 -0.0532 -0.0433 -0.0105 560 SER A O   
4677 C CB  . SER A 560 ? 0.4803 0.5267 0.3687 -0.0399 -0.0517 -0.0050 560 SER A CB  
4678 O OG  . SER A 560 ? 0.5179 0.5643 0.4139 -0.0400 -0.0490 -0.0100 560 SER A OG  
4679 N N   . ARG A 561 ? 0.4550 0.4766 0.3410 -0.0496 -0.0379 -0.0129 561 ARG A N   
4680 C CA  . ARG A 561 ? 0.4635 0.4840 0.3485 -0.0559 -0.0316 -0.0192 561 ARG A CA  
4681 C C   . ARG A 561 ? 0.4617 0.4708 0.3433 -0.0565 -0.0277 -0.0178 561 ARG A C   
4682 O O   . ARG A 561 ? 0.4498 0.4584 0.3282 -0.0615 -0.0232 -0.0214 561 ARG A O   
4683 C CB  . ARG A 561 ? 0.4822 0.5026 0.3736 -0.0567 -0.0272 -0.0248 561 ARG A CB  
4684 C CG  . ARG A 561 ? 0.5025 0.5370 0.3968 -0.0597 -0.0287 -0.0296 561 ARG A CG  
4685 C CD  . ARG A 561 ? 0.5107 0.5431 0.4099 -0.0626 -0.0222 -0.0363 561 ARG A CD  
4686 N NE  . ARG A 561 ? 0.5462 0.5923 0.4499 -0.0642 -0.0242 -0.0404 561 ARG A NE  
4687 C CZ  . ARG A 561 ? 0.5642 0.6114 0.4720 -0.0679 -0.0187 -0.0471 561 ARG A CZ  
4688 N NH1 . ARG A 561 ? 0.5480 0.5822 0.4557 -0.0698 -0.0105 -0.0501 561 ARG A NH1 
4689 N NH2 . ARG A 561 ? 0.5425 0.6041 0.4545 -0.0695 -0.0212 -0.0508 561 ARG A NH2 
4690 N N   . GLU A 562 ? 0.4500 0.4504 0.3324 -0.0518 -0.0289 -0.0130 562 GLU A N   
4691 C CA  . GLU A 562 ? 0.4520 0.4436 0.3318 -0.0522 -0.0254 -0.0118 562 GLU A CA  
4692 C C   . GLU A 562 ? 0.4626 0.4518 0.3367 -0.0519 -0.0286 -0.0067 562 GLU A C   
4693 O O   . GLU A 562 ? 0.4495 0.4400 0.3223 -0.0491 -0.0335 -0.0025 562 GLU A O   
4694 C CB  . GLU A 562 ? 0.4500 0.4342 0.3348 -0.0481 -0.0230 -0.0113 562 GLU A CB  
4695 C CG  . GLU A 562 ? 0.4629 0.4476 0.3534 -0.0476 -0.0191 -0.0157 562 GLU A CG  
4696 C CD  . GLU A 562 ? 0.4409 0.4271 0.3297 -0.0525 -0.0134 -0.0209 562 GLU A CD  
4697 O OE1 . GLU A 562 ? 0.4463 0.4290 0.3315 -0.0545 -0.0096 -0.0211 562 GLU A OE1 
4698 O OE2 . GLU A 562 ? 0.4410 0.4321 0.3323 -0.0547 -0.0124 -0.0250 562 GLU A OE2 
4699 N N   . LYS A 563 ? 0.4738 0.4590 0.3443 -0.0544 -0.0252 -0.0069 563 LYS A N   
4700 C CA  . LYS A 563 ? 0.4812 0.4628 0.3461 -0.0550 -0.0267 -0.0028 563 LYS A CA  
4701 C C   . LYS A 563 ? 0.4796 0.4539 0.3469 -0.0514 -0.0268 0.0000  563 LYS A C   
4702 O O   . LYS A 563 ? 0.4833 0.4551 0.3540 -0.0507 -0.0230 -0.0019 563 LYS A O   
4703 C CB  . LYS A 563 ? 0.4859 0.4675 0.3470 -0.0596 -0.0221 -0.0053 563 LYS A CB  
4704 C CG  . LYS A 563 ? 0.5059 0.4836 0.3617 -0.0610 -0.0221 -0.0021 563 LYS A CG  
4705 C CD  . LYS A 563 ? 0.5063 0.4858 0.3556 -0.0621 -0.0267 0.0018  563 LYS A CD  
4706 C CE  . LYS A 563 ? 0.5345 0.5183 0.3777 -0.0675 -0.0251 0.0000  563 LYS A CE  
4707 N NZ  . LYS A 563 ? 0.5128 0.4975 0.3483 -0.0684 -0.0290 0.0049  563 LYS A NZ  
4708 N N   . LEU A 564 ? 0.5099 0.4810 0.3751 -0.0492 -0.0306 0.0045  564 LEU A N   
4709 C CA  . LEU A 564 ? 0.5198 0.4838 0.3868 -0.0467 -0.0304 0.0066  564 LEU A CA  
4710 C C   . LEU A 564 ? 0.5268 0.4853 0.3877 -0.0491 -0.0297 0.0095  564 LEU A C   
4711 O O   . LEU A 564 ? 0.5268 0.4802 0.3887 -0.0486 -0.0285 0.0101  564 LEU A O   
4712 C CB  . LEU A 564 ? 0.5382 0.5005 0.4080 -0.0421 -0.0338 0.0090  564 LEU A CB  
4713 C CG  . LEU A 564 ? 0.5514 0.5189 0.4279 -0.0395 -0.0345 0.0062  564 LEU A CG  
4714 C CD1 . LEU A 564 ? 0.5523 0.5190 0.4304 -0.0349 -0.0383 0.0094  564 LEU A CD1 
4715 C CD2 . LEU A 564 ? 0.5322 0.4982 0.4144 -0.0388 -0.0310 0.0028  564 LEU A CD2 
4716 N N   . THR A 565 ? 0.5341 0.4942 0.3886 -0.0522 -0.0303 0.0109  565 THR A N   
4717 C CA  . THR A 565 ? 0.5351 0.4903 0.3832 -0.0552 -0.0292 0.0135  565 THR A CA  
4718 C C   . THR A 565 ? 0.5469 0.5049 0.3949 -0.0590 -0.0251 0.0100  565 THR A C   
4719 O O   . THR A 565 ? 0.5622 0.5256 0.4119 -0.0600 -0.0236 0.0068  565 THR A O   
4720 C CB  . THR A 565 ? 0.5239 0.4794 0.3643 -0.0562 -0.0319 0.0174  565 THR A CB  
4721 O OG1 . THR A 565 ? 0.4969 0.4612 0.3366 -0.0583 -0.0322 0.0148  565 THR A OG1 
4722 C CG2 . THR A 565 ? 0.5228 0.4755 0.3629 -0.0512 -0.0355 0.0220  565 THR A CG2 
4723 N N   . MET A 566 ? 0.5542 0.5086 0.4006 -0.0611 -0.0229 0.0104  566 MET A N   
4724 C CA  . MET A 566 ? 0.5659 0.5242 0.4122 -0.0641 -0.0191 0.0076  566 MET A CA  
4725 C C   . MET A 566 ? 0.5796 0.5348 0.4194 -0.0685 -0.0179 0.0094  566 MET A C   
4726 O O   . MET A 566 ? 0.5912 0.5398 0.4276 -0.0690 -0.0190 0.0123  566 MET A O   
4727 C CB  . MET A 566 ? 0.5754 0.5365 0.4287 -0.0619 -0.0165 0.0049  566 MET A CB  
4728 C CG  . MET A 566 ? 0.6082 0.5656 0.4632 -0.0611 -0.0170 0.0058  566 MET A CG  
4729 S SD  . MET A 566 ? 0.7095 0.6633 0.5692 -0.0560 -0.0202 0.0067  566 MET A SD  
4730 C CE  . MET A 566 ? 0.5650 0.5179 0.4285 -0.0557 -0.0186 0.0054  566 MET A CE  
4731 N N   . LYS A 567 ? 0.5785 0.5381 0.4164 -0.0718 -0.0149 0.0074  567 LYS A N   
4732 C CA  . LYS A 567 ? 0.5824 0.5405 0.4147 -0.0765 -0.0130 0.0082  567 LYS A CA  
4733 C C   . LYS A 567 ? 0.5613 0.5225 0.3978 -0.0772 -0.0101 0.0059  567 LYS A C   
4734 O O   . LYS A 567 ? 0.5204 0.4884 0.3629 -0.0748 -0.0081 0.0033  567 LYS A O   
4735 C CB  . LYS A 567 ? 0.5791 0.5416 0.4076 -0.0797 -0.0111 0.0069  567 LYS A CB  
4736 C CG  . LYS A 567 ? 0.5846 0.5458 0.4064 -0.0851 -0.0091 0.0077  567 LYS A CG  
4737 C CD  . LYS A 567 ? 0.5875 0.5538 0.4064 -0.0880 -0.0068 0.0057  567 LYS A CD  
4738 C CE  . LYS A 567 ? 0.6238 0.5886 0.4351 -0.0937 -0.0051 0.0069  567 LYS A CE  
4739 N NZ  . LYS A 567 ? 0.6325 0.6000 0.4383 -0.0966 -0.0044 0.0063  567 LYS A NZ  
4740 N N   . PHE A 568 ? 0.5458 0.5025 0.3788 -0.0805 -0.0095 0.0070  568 PHE A N   
4741 C CA  . PHE A 568 ? 0.5403 0.5018 0.3766 -0.0825 -0.0066 0.0043  568 PHE A CA  
4742 C C   . PHE A 568 ? 0.5476 0.5129 0.3797 -0.0882 -0.0034 0.0031  568 PHE A C   
4743 O O   . PHE A 568 ? 0.6015 0.5616 0.4264 -0.0915 -0.0035 0.0052  568 PHE A O   
4744 C CB  . PHE A 568 ? 0.5398 0.4942 0.3757 -0.0835 -0.0070 0.0050  568 PHE A CB  
4745 C CG  . PHE A 568 ? 0.5571 0.5096 0.3985 -0.0781 -0.0094 0.0053  568 PHE A CG  
4746 C CD1 . PHE A 568 ? 0.5437 0.5050 0.3928 -0.0747 -0.0089 0.0025  568 PHE A CD1 
4747 C CD2 . PHE A 568 ? 0.5641 0.5064 0.4029 -0.0759 -0.0120 0.0086  568 PHE A CD2 
4748 C CE1 . PHE A 568 ? 0.5477 0.5071 0.4017 -0.0700 -0.0109 0.0026  568 PHE A CE1 
4749 C CE2 . PHE A 568 ? 0.5679 0.5088 0.4120 -0.0710 -0.0140 0.0086  568 PHE A CE2 
4750 C CZ  . PHE A 568 ? 0.5400 0.4893 0.3917 -0.0684 -0.0135 0.0054  568 PHE A CZ  
4751 N N   . HIS A 569 ? 0.5434 0.5188 0.3799 -0.0891 -0.0006 0.0000  569 HIS A N   
4752 C CA  . HIS A 569 ? 0.5349 0.5164 0.3686 -0.0942 0.0026  -0.0016 569 HIS A CA  
4753 C C   . HIS A 569 ? 0.5398 0.5248 0.3732 -0.0994 0.0049  -0.0039 569 HIS A C   
4754 O O   . HIS A 569 ? 0.5436 0.5358 0.3757 -0.1039 0.0079  -0.0059 569 HIS A O   
4755 C CB  . HIS A 569 ? 0.5170 0.5096 0.3555 -0.0908 0.0047  -0.0034 569 HIS A CB  
4756 C CG  . HIS A 569 ? 0.5268 0.5155 0.3637 -0.0881 0.0038  -0.0022 569 HIS A CG  
4757 N ND1 . HIS A 569 ? 0.5335 0.5214 0.3748 -0.0825 0.0025  -0.0019 569 HIS A ND1 
4758 C CD2 . HIS A 569 ? 0.5426 0.5284 0.3733 -0.0913 0.0044  -0.0015 569 HIS A CD2 
4759 C CE1 . HIS A 569 ? 0.5249 0.5099 0.3633 -0.0824 0.0025  -0.0017 569 HIS A CE1 
4760 N NE2 . HIS A 569 ? 0.5580 0.5422 0.3899 -0.0877 0.0035  -0.0014 569 HIS A NE2 
4761 N N   . ASP A 570 ? 0.5498 0.5304 0.3847 -0.0993 0.0040  -0.0042 570 ASP A N   
4762 C CA  . ASP A 570 ? 0.5922 0.5750 0.4262 -0.1056 0.0067  -0.0071 570 ASP A CA  
4763 C C   . ASP A 570 ? 0.5950 0.5609 0.4228 -0.1085 0.0066  -0.0050 570 ASP A C   
4764 O O   . ASP A 570 ? 0.6117 0.5701 0.4411 -0.1039 0.0040  -0.0030 570 ASP A O   
4765 C CB  . ASP A 570 ? 0.5884 0.5845 0.4307 -0.1031 0.0070  -0.0106 570 ASP A CB  
4766 C CG  . ASP A 570 ? 0.6244 0.6254 0.4663 -0.1105 0.0101  -0.0148 570 ASP A CG  
4767 O OD1 . ASP A 570 ? 0.6213 0.6106 0.4564 -0.1171 0.0121  -0.0148 570 ASP A OD1 
4768 O OD2 . ASP A 570 ? 0.6511 0.6680 0.4993 -0.1098 0.0109  -0.0182 570 ASP A OD2 
4769 N N   . GLY A 571 ? 0.6106 0.5702 0.4313 -0.1159 0.0098  -0.0053 571 GLY A N   
4770 C CA  . GLY A 571 ? 0.6411 0.5827 0.4548 -0.1184 0.0110  -0.0027 571 GLY A CA  
4771 C C   . GLY A 571 ? 0.6257 0.5649 0.4422 -0.1204 0.0129  -0.0060 571 GLY A C   
4772 O O   . GLY A 571 ? 0.6489 0.5724 0.4603 -0.1219 0.0146  -0.0041 571 GLY A O   
4773 N N   . GLU A 572 ? 0.6392 0.5944 0.4637 -0.1202 0.0129  -0.0107 572 GLU A N   
4774 C CA  . GLU A 572 ? 0.6415 0.5984 0.4691 -0.1231 0.0149  -0.0150 572 GLU A CA  
4775 C C   . GLU A 572 ? 0.6091 0.5652 0.4427 -0.1149 0.0110  -0.0135 572 GLU A C   
4776 O O   . GLU A 572 ? 0.5896 0.5451 0.4259 -0.1160 0.0121  -0.0165 572 GLU A O   
4777 C CB  . GLU A 572 ? 0.6840 0.6621 0.5169 -0.1273 0.0168  -0.0210 572 GLU A CB  
4778 C CG  . GLU A 572 ? 0.7657 0.7456 0.5977 -0.1362 0.0215  -0.0270 572 GLU A CG  
4779 C CD  . GLU A 572 ? 0.7938 0.7702 0.6187 -0.1462 0.0266  -0.0292 572 GLU A CD  
4780 O OE1 . GLU A 572 ? 0.8068 0.7819 0.6283 -0.1458 0.0262  -0.0261 572 GLU A OE1 
4781 O OE2 . GLU A 572 ? 0.9029 0.8777 0.7254 -0.1551 0.0316  -0.0344 572 GLU A OE2 
4782 N N   . VAL A 573 ? 0.5764 0.5331 0.4122 -0.1073 0.0068  -0.0095 573 VAL A N   
4783 C CA  . VAL A 573 ? 0.5609 0.5168 0.4021 -0.0995 0.0032  -0.0079 573 VAL A CA  
4784 C C   . VAL A 573 ? 0.5699 0.5096 0.4082 -0.0994 0.0035  -0.0063 573 VAL A C   
4785 O O   . VAL A 573 ? 0.5543 0.4795 0.3849 -0.1021 0.0053  -0.0035 573 VAL A O   
4786 C CB  . VAL A 573 ? 0.5570 0.5128 0.3990 -0.0929 -0.0004 -0.0038 573 VAL A CB  
4787 C CG1 . VAL A 573 ? 0.5402 0.4806 0.3750 -0.0924 -0.0016 0.0010  573 VAL A CG1 
4788 C CG2 . VAL A 573 ? 0.5399 0.5012 0.3894 -0.0855 -0.0033 -0.0039 573 VAL A CG2 
4789 N N   . ASP A 574 ? 0.5748 0.5166 0.4188 -0.0959 0.0024  -0.0080 574 ASP A N   
4790 C CA  . ASP A 574 ? 0.5803 0.5071 0.4228 -0.0933 0.0021  -0.0058 574 ASP A CA  
4791 C C   . ASP A 574 ? 0.5484 0.4737 0.3936 -0.0848 -0.0026 -0.0014 574 ASP A C   
4792 O O   . ASP A 574 ? 0.5178 0.4519 0.3698 -0.0800 -0.0050 -0.0025 574 ASP A O   
4793 C CB  . ASP A 574 ? 0.5926 0.5221 0.4396 -0.0945 0.0037  -0.0103 574 ASP A CB  
4794 C CG  . ASP A 574 ? 0.6308 0.5436 0.4760 -0.0919 0.0043  -0.0082 574 ASP A CG  
4795 O OD1 . ASP A 574 ? 0.6341 0.5356 0.4757 -0.0875 0.0025  -0.0026 574 ASP A OD1 
4796 O OD2 . ASP A 574 ? 0.6920 0.6035 0.5392 -0.0943 0.0068  -0.0121 574 ASP A OD2 
4797 N N   . ALA A 575 ? 0.5555 0.4703 0.3949 -0.0831 -0.0038 0.0035  575 ALA A N   
4798 C CA  . ALA A 575 ? 0.5393 0.4545 0.3805 -0.0760 -0.0084 0.0073  575 ALA A CA  
4799 C C   . ALA A 575 ? 0.5128 0.4223 0.3579 -0.0706 -0.0100 0.0083  575 ALA A C   
4800 O O   . ALA A 575 ? 0.4778 0.3918 0.3275 -0.0649 -0.0136 0.0095  575 ALA A O   
4801 C CB  . ALA A 575 ? 0.5256 0.4333 0.3591 -0.0761 -0.0092 0.0124  575 ALA A CB  
4802 N N   . SER A 576 ? 0.4929 0.3926 0.3362 -0.0728 -0.0069 0.0075  576 SER A N   
4803 C CA  . SER A 576 ? 0.5042 0.3972 0.3506 -0.0678 -0.0077 0.0084  576 SER A CA  
4804 C C   . SER A 576 ? 0.4990 0.4035 0.3543 -0.0654 -0.0093 0.0043  576 SER A C   
4805 O O   . SER A 576 ? 0.5170 0.4206 0.3766 -0.0596 -0.0117 0.0054  576 SER A O   
4806 C CB  . SER A 576 ? 0.5236 0.4017 0.3654 -0.0712 -0.0027 0.0080  576 SER A CB  
4807 O OG  . SER A 576 ? 0.5417 0.4243 0.3843 -0.0787 0.0013  0.0018  576 SER A OG  
4808 N N   . TYR A 577 ? 0.4905 0.4067 0.3483 -0.0694 -0.0080 0.0000  577 TYR A N   
4809 C CA  . TYR A 577 ? 0.4823 0.4098 0.3477 -0.0667 -0.0091 -0.0033 577 TYR A CA  
4810 C C   . TYR A 577 ? 0.4740 0.4050 0.3439 -0.0596 -0.0131 -0.0008 577 TYR A C   
4811 O O   . TYR A 577 ? 0.4757 0.4091 0.3509 -0.0557 -0.0141 -0.0020 577 TYR A O   
4812 C CB  . TYR A 577 ? 0.4684 0.4106 0.3357 -0.0706 -0.0075 -0.0071 577 TYR A CB  
4813 C CG  . TYR A 577 ? 0.4708 0.4242 0.3447 -0.0688 -0.0075 -0.0106 577 TYR A CG  
4814 C CD1 . TYR A 577 ? 0.4735 0.4248 0.3483 -0.0717 -0.0053 -0.0141 577 TYR A CD1 
4815 C CD2 . TYR A 577 ? 0.4578 0.4234 0.3366 -0.0641 -0.0091 -0.0103 577 TYR A CD2 
4816 C CE1 . TYR A 577 ? 0.4709 0.4339 0.3513 -0.0700 -0.0054 -0.0172 577 TYR A CE1 
4817 C CE2 . TYR A 577 ? 0.4408 0.4170 0.3250 -0.0618 -0.0088 -0.0128 577 TYR A CE2 
4818 C CZ  . TYR A 577 ? 0.4560 0.4314 0.3409 -0.0648 -0.0073 -0.0162 577 TYR A CZ  
4819 O OH  . TYR A 577 ? 0.4704 0.4573 0.3602 -0.0626 -0.0072 -0.0186 577 TYR A OH  
4820 N N   . PHE A 578 ? 0.4630 0.3935 0.3301 -0.0583 -0.0150 0.0023  578 PHE A N   
4821 C CA  . PHE A 578 ? 0.4797 0.4154 0.3507 -0.0530 -0.0180 0.0035  578 PHE A CA  
4822 C C   . PHE A 578 ? 0.5032 0.4319 0.3746 -0.0483 -0.0208 0.0066  578 PHE A C   
4823 O O   . PHE A 578 ? 0.4995 0.4328 0.3742 -0.0445 -0.0231 0.0070  578 PHE A O   
4824 C CB  . PHE A 578 ? 0.4767 0.4183 0.3453 -0.0545 -0.0181 0.0041  578 PHE A CB  
4825 C CG  . PHE A 578 ? 0.4671 0.4174 0.3361 -0.0581 -0.0152 0.0012  578 PHE A CG  
4826 C CD1 . PHE A 578 ? 0.4651 0.4258 0.3399 -0.0555 -0.0143 -0.0010 578 PHE A CD1 
4827 C CD2 . PHE A 578 ? 0.4516 0.4001 0.3154 -0.0639 -0.0131 0.0009  578 PHE A CD2 
4828 C CE1 . PHE A 578 ? 0.4637 0.4344 0.3393 -0.0579 -0.0118 -0.0032 578 PHE A CE1 
4829 C CE2 . PHE A 578 ? 0.4578 0.4165 0.3227 -0.0672 -0.0105 -0.0020 578 PHE A CE2 
4830 C CZ  . PHE A 578 ? 0.4435 0.4140 0.3145 -0.0639 -0.0101 -0.0039 578 PHE A CZ  
4831 N N   . CYS A 579 ? 0.5428 0.4608 0.4111 -0.0485 -0.0200 0.0083  579 CYS A N   
4832 C CA  . CYS A 579 ? 0.5916 0.5023 0.4593 -0.0435 -0.0222 0.0122  579 CYS A CA  
4833 C C   . CYS A 579 ? 0.5947 0.5054 0.4689 -0.0395 -0.0226 0.0105  579 CYS A C   
4834 O O   . CYS A 579 ? 0.6013 0.5107 0.4775 -0.0343 -0.0251 0.0129  579 CYS A O   
4835 C CB  . CYS A 579 ? 0.6482 0.5454 0.5088 -0.0450 -0.0198 0.0155  579 CYS A CB  
4836 S SG  . CYS A 579 ? 0.7680 0.6616 0.6194 -0.0476 -0.0199 0.0200  579 CYS A SG  
4837 N N   . LYS A 580 ? 0.5628 0.4753 0.4398 -0.0421 -0.0200 0.0063  580 LYS A N   
4838 C CA  . LYS A 580 ? 0.5618 0.4714 0.4433 -0.0395 -0.0193 0.0045  580 LYS A CA  
4839 C C   . LYS A 580 ? 0.5239 0.4435 0.4106 -0.0409 -0.0183 -0.0002 580 LYS A C   
4840 O O   . LYS A 580 ? 0.4986 0.4261 0.3847 -0.0444 -0.0173 -0.0021 580 LYS A O   
4841 C CB  . LYS A 580 ? 0.5884 0.4849 0.4654 -0.0420 -0.0156 0.0049  580 LYS A CB  
4842 C CG  . LYS A 580 ? 0.6032 0.4994 0.4759 -0.0497 -0.0118 0.0019  580 LYS A CG  
4843 C CD  . LYS A 580 ? 0.6354 0.5160 0.5017 -0.0530 -0.0073 0.0028  580 LYS A CD  
4844 C CE  . LYS A 580 ? 0.6510 0.5323 0.5124 -0.0617 -0.0034 -0.0002 580 LYS A CE  
4845 N NZ  . LYS A 580 ? 0.6498 0.5426 0.5153 -0.0665 -0.0016 -0.0069 580 LYS A NZ  
4846 N N   . LEU A 581 ? 0.4978 0.4176 0.3895 -0.0378 -0.0184 -0.0018 581 LEU A N   
4847 C CA  . LEU A 581 ? 0.5230 0.4504 0.4185 -0.0394 -0.0167 -0.0062 581 LEU A CA  
4848 C C   . LEU A 581 ? 0.5269 0.4526 0.4185 -0.0460 -0.0131 -0.0090 581 LEU A C   
4849 O O   . LEU A 581 ? 0.5688 0.4829 0.4568 -0.0481 -0.0108 -0.0088 581 LEU A O   
4850 C CB  . LEU A 581 ? 0.5256 0.4501 0.4257 -0.0357 -0.0167 -0.0075 581 LEU A CB  
4851 C CG  . LEU A 581 ? 0.5476 0.4809 0.4539 -0.0315 -0.0183 -0.0086 581 LEU A CG  
4852 C CD1 . LEU A 581 ? 0.5359 0.4778 0.4429 -0.0303 -0.0198 -0.0074 581 LEU A CD1 
4853 C CD2 . LEU A 581 ? 0.5585 0.4867 0.4685 -0.0264 -0.0198 -0.0075 581 LEU A CD2 
4854 N N   . PRO A 582 ? 0.5180 0.4556 0.4102 -0.0493 -0.0121 -0.0118 582 PRO A N   
4855 C CA  . PRO A 582 ? 0.5246 0.4643 0.4144 -0.0562 -0.0085 -0.0159 582 PRO A CA  
4856 C C   . PRO A 582 ? 0.5506 0.4885 0.4431 -0.0567 -0.0066 -0.0196 582 PRO A C   
4857 O O   . PRO A 582 ? 0.5424 0.4848 0.4399 -0.0518 -0.0083 -0.0197 582 PRO A O   
4858 C CB  . PRO A 582 ? 0.5056 0.4625 0.3975 -0.0572 -0.0087 -0.0176 582 PRO A CB  
4859 C CG  . PRO A 582 ? 0.4960 0.4553 0.3893 -0.0518 -0.0116 -0.0137 582 PRO A CG  
4860 C CD  . PRO A 582 ? 0.5004 0.4507 0.3958 -0.0466 -0.0137 -0.0114 582 PRO A CD  
4861 N N   . GLU A 583 ? 0.5930 0.5244 0.4820 -0.0630 -0.0026 -0.0229 583 GLU A N   
4862 C CA  . GLU A 583 ? 0.6392 0.5666 0.5298 -0.0641 0.0000  -0.0268 583 GLU A CA  
4863 C C   . GLU A 583 ? 0.5847 0.5289 0.4807 -0.0635 -0.0007 -0.0307 583 GLU A C   
4864 O O   . GLU A 583 ? 0.5641 0.5064 0.4634 -0.0607 -0.0006 -0.0320 583 GLU A O   
4865 C CB  . GLU A 583 ? 0.7092 0.6255 0.5944 -0.0721 0.0057  -0.0304 583 GLU A CB  
4866 C CG  . GLU A 583 ? 0.8181 0.7172 0.6970 -0.0724 0.0071  -0.0259 583 GLU A CG  
4867 C CD  . GLU A 583 ? 0.9084 0.7983 0.7884 -0.0632 0.0033  -0.0190 583 GLU A CD  
4868 O OE1 . GLU A 583 ? 0.9000 0.7761 0.7794 -0.0602 0.0053  -0.0176 583 GLU A OE1 
4869 O OE2 . GLU A 583 ? 0.8984 0.7952 0.7796 -0.0591 -0.0011 -0.0151 583 GLU A OE2 
4870 N N   . LYS A 584 ? 0.5489 0.5096 0.4457 -0.0652 -0.0015 -0.0318 584 LYS A N   
4871 C CA  . LYS A 584 ? 0.5430 0.5203 0.4444 -0.0630 -0.0024 -0.0340 584 LYS A CA  
4872 C C   . LYS A 584 ? 0.5413 0.5181 0.4472 -0.0543 -0.0056 -0.0303 584 LYS A C   
4873 O O   . LYS A 584 ? 0.5966 0.5816 0.5059 -0.0520 -0.0056 -0.0321 584 LYS A O   
4874 C CB  . LYS A 584 ? 0.5076 0.5035 0.4089 -0.0650 -0.0026 -0.0349 584 LYS A CB  
4875 C CG  . LYS A 584 ? 0.5244 0.5218 0.4256 -0.0605 -0.0051 -0.0297 584 LYS A CG  
4876 C CD  . LYS A 584 ? 0.5361 0.5490 0.4362 -0.0640 -0.0042 -0.0309 584 LYS A CD  
4877 C CE  . LYS A 584 ? 0.5476 0.5627 0.4480 -0.0588 -0.0060 -0.0260 584 LYS A CE  
4878 N NZ  . LYS A 584 ? 0.5508 0.5713 0.4480 -0.0639 -0.0048 -0.0267 584 LYS A NZ  
4879 N N   . PHE A 585 ? 0.5326 0.5002 0.4383 -0.0498 -0.0079 -0.0255 585 PHE A N   
4880 C CA  . PHE A 585 ? 0.5116 0.4781 0.4213 -0.0425 -0.0104 -0.0226 585 PHE A CA  
4881 C C   . PHE A 585 ? 0.5266 0.4787 0.4372 -0.0399 -0.0110 -0.0215 585 PHE A C   
4882 O O   . PHE A 585 ? 0.4981 0.4494 0.4124 -0.0345 -0.0128 -0.0198 585 PHE A O   
4883 C CB  . PHE A 585 ? 0.4875 0.4566 0.3970 -0.0392 -0.0125 -0.0185 585 PHE A CB  
4884 C CG  . PHE A 585 ? 0.4564 0.4402 0.3662 -0.0391 -0.0118 -0.0187 585 PHE A CG  
4885 C CD1 . PHE A 585 ? 0.4234 0.4181 0.3366 -0.0356 -0.0112 -0.0193 585 PHE A CD1 
4886 C CD2 . PHE A 585 ? 0.4256 0.4125 0.3323 -0.0417 -0.0115 -0.0176 585 PHE A CD2 
4887 C CE1 . PHE A 585 ? 0.4257 0.4340 0.3390 -0.0341 -0.0103 -0.0185 585 PHE A CE1 
4888 C CE2 . PHE A 585 ? 0.4266 0.4274 0.3339 -0.0406 -0.0106 -0.0172 585 PHE A CE2 
4889 C CZ  . PHE A 585 ? 0.4048 0.4163 0.3154 -0.0364 -0.0099 -0.0174 585 PHE A CZ  
4890 N N   . ARG A 586 ? 0.5657 0.5063 0.4727 -0.0437 -0.0090 -0.0222 586 ARG A N   
4891 C CA  . ARG A 586 ? 0.5939 0.5202 0.5007 -0.0402 -0.0095 -0.0196 586 ARG A CA  
4892 C C   . ARG A 586 ? 0.6107 0.5342 0.5217 -0.0374 -0.0086 -0.0217 586 ARG A C   
4893 O O   . ARG A 586 ? 0.6621 0.5786 0.5752 -0.0321 -0.0101 -0.0189 586 ARG A O   
4894 C CB  . ARG A 586 ? 0.6297 0.5430 0.5304 -0.0444 -0.0067 -0.0188 586 ARG A CB  
4895 C CG  . ARG A 586 ? 0.6905 0.5896 0.5901 -0.0394 -0.0073 -0.0143 586 ARG A CG  
4896 C CD  . ARG A 586 ? 0.7767 0.6641 0.6691 -0.0423 -0.0052 -0.0115 586 ARG A CD  
4897 N NE  . ARG A 586 ? 0.8767 0.7509 0.7654 -0.0464 0.0005  -0.0139 586 ARG A NE  
4898 C CZ  . ARG A 586 ? 0.9534 0.8122 0.8404 -0.0426 0.0028  -0.0111 586 ARG A CZ  
4899 N NH1 . ARG A 586 ? 0.9695 0.8263 0.8587 -0.0343 -0.0008 -0.0057 586 ARG A NH1 
4900 N NH2 . ARG A 586 ? 0.8891 0.7348 0.7720 -0.0472 0.0094  -0.0140 586 ARG A NH2 
4901 N N   . PHE A 587 ? 0.5816 0.5117 0.4939 -0.0407 -0.0063 -0.0266 587 PHE A N   
4902 C CA  . PHE A 587 ? 0.6419 0.5685 0.5576 -0.0390 -0.0047 -0.0293 587 PHE A CA  
4903 C C   . PHE A 587 ? 0.6507 0.5909 0.5708 -0.0372 -0.0056 -0.0315 587 PHE A C   
4904 O O   . PHE A 587 ? 0.6601 0.6010 0.5818 -0.0384 -0.0034 -0.0355 587 PHE A O   
4905 C CB  . PHE A 587 ? 0.6820 0.6003 0.5943 -0.0453 0.0004  -0.0339 587 PHE A CB  
4906 C CG  . PHE A 587 ? 0.7175 0.6209 0.6242 -0.0478 0.0028  -0.0318 587 PHE A CG  
4907 C CD1 . PHE A 587 ? 0.7326 0.6218 0.6390 -0.0421 0.0024  -0.0272 587 PHE A CD1 
4908 C CD2 . PHE A 587 ? 0.7311 0.6352 0.6327 -0.0556 0.0057  -0.0344 587 PHE A CD2 
4909 C CE1 . PHE A 587 ? 0.7525 0.6274 0.6530 -0.0437 0.0051  -0.0245 587 PHE A CE1 
4910 C CE2 . PHE A 587 ? 0.7504 0.6395 0.6461 -0.0581 0.0087  -0.0324 587 PHE A CE2 
4911 C CZ  . PHE A 587 ? 0.7648 0.6387 0.6597 -0.0519 0.0085  -0.0271 587 PHE A CZ  
4912 N N   . VAL A 588 ? 0.6306 0.5812 0.5521 -0.0343 -0.0083 -0.0290 588 VAL A N   
4913 C CA  . VAL A 588 ? 0.5509 0.5124 0.4763 -0.0311 -0.0089 -0.0298 588 VAL A CA  
4914 C C   . VAL A 588 ? 0.5208 0.4756 0.4504 -0.0259 -0.0099 -0.0288 588 VAL A C   
4915 O O   . VAL A 588 ? 0.5062 0.4522 0.4361 -0.0233 -0.0115 -0.0258 588 VAL A O   
4916 C CB  . VAL A 588 ? 0.5391 0.5113 0.4646 -0.0286 -0.0105 -0.0268 588 VAL A CB  
4917 C CG1 . VAL A 588 ? 0.5389 0.5186 0.4606 -0.0332 -0.0097 -0.0275 588 VAL A CG1 
4918 C CG2 . VAL A 588 ? 0.4840 0.4502 0.4103 -0.0245 -0.0128 -0.0227 588 VAL A CG2 
4919 N N   . LYS A 589 ? 0.5247 0.4843 0.4573 -0.0245 -0.0088 -0.0312 589 LYS A N   
4920 C CA  . LYS A 589 ? 0.5298 0.4844 0.4669 -0.0197 -0.0095 -0.0307 589 LYS A CA  
4921 C C   . LYS A 589 ? 0.5151 0.4739 0.4545 -0.0152 -0.0116 -0.0274 589 LYS A C   
4922 O O   . LYS A 589 ? 0.4812 0.4492 0.4201 -0.0147 -0.0112 -0.0268 589 LYS A O   
4923 C CB  . LYS A 589 ? 0.5797 0.5380 0.5191 -0.0202 -0.0073 -0.0348 589 LYS A CB  
4924 C CG  . LYS A 589 ? 0.6370 0.5850 0.5766 -0.0221 -0.0049 -0.0380 589 LYS A CG  
4925 C CD  . LYS A 589 ? 0.6588 0.6078 0.6027 -0.0197 -0.0035 -0.0406 589 LYS A CD  
4926 C CE  . LYS A 589 ? 0.7265 0.6805 0.6688 -0.0248 -0.0001 -0.0462 589 LYS A CE  
4927 N NZ  . LYS A 589 ? 0.7182 0.6802 0.6636 -0.0227 0.0004  -0.0482 589 LYS A NZ  
4928 N N   . ILE A 590 ? 0.4936 0.4461 0.4354 -0.0119 -0.0134 -0.0254 590 ILE A N   
4929 C CA  . ILE A 590 ? 0.4775 0.4338 0.4218 -0.0085 -0.0147 -0.0234 590 ILE A CA  
4930 C C   . ILE A 590 ? 0.4808 0.4360 0.4303 -0.0051 -0.0146 -0.0246 590 ILE A C   
4931 O O   . ILE A 590 ? 0.4774 0.4349 0.4293 -0.0029 -0.0153 -0.0238 590 ILE A O   
4932 C CB  . ILE A 590 ? 0.4791 0.4327 0.4214 -0.0084 -0.0170 -0.0202 590 ILE A CB  
4933 C CG1 . ILE A 590 ? 0.4845 0.4303 0.4279 -0.0067 -0.0188 -0.0190 590 ILE A CG1 
4934 C CG2 . ILE A 590 ? 0.4680 0.4228 0.4052 -0.0120 -0.0167 -0.0193 590 ILE A CG2 
4935 C CD1 . ILE A 590 ? 0.4814 0.4258 0.4226 -0.0063 -0.0213 -0.0157 590 ILE A CD1 
4936 N N   . ASN A 591 ? 0.5013 0.4529 0.4525 -0.0051 -0.0135 -0.0270 591 ASN A N   
4937 C CA  . ASN A 591 ? 0.5341 0.4852 0.4907 -0.0017 -0.0133 -0.0284 591 ASN A CA  
4938 C C   . ASN A 591 ? 0.5367 0.4927 0.4947 -0.0022 -0.0107 -0.0315 591 ASN A C   
4939 O O   . ASN A 591 ? 0.5202 0.4762 0.4762 -0.0049 -0.0089 -0.0339 591 ASN A O   
4940 C CB  . ASN A 591 ? 0.5688 0.5115 0.5270 0.0000  -0.0137 -0.0283 591 ASN A CB  
4941 C CG  . ASN A 591 ? 0.5922 0.5316 0.5497 0.0019  -0.0166 -0.0244 591 ASN A CG  
4942 O OD1 . ASN A 591 ? 0.6273 0.5719 0.5858 0.0029  -0.0186 -0.0229 591 ASN A OD1 
4943 N ND2 . ASN A 591 ? 0.5706 0.5013 0.5260 0.0024  -0.0163 -0.0230 591 ASN A ND2 
4944 N N   . ARG A 592 ? 0.4950 0.4554 0.4561 0.0000  -0.0102 -0.0317 592 ARG A N   
4945 C CA  . ARG A 592 ? 0.5315 0.4970 0.4935 0.0001  -0.0075 -0.0339 592 ARG A CA  
4946 C C   . ARG A 592 ? 0.5356 0.4985 0.5021 0.0015  -0.0065 -0.0369 592 ARG A C   
4947 O O   . ARG A 592 ? 0.5927 0.5545 0.5637 0.0041  -0.0074 -0.0369 592 ARG A O   
4948 C CB  . ARG A 592 ? 0.4992 0.4693 0.4616 0.0018  -0.0064 -0.0324 592 ARG A CB  
4949 C CG  . ARG A 592 ? 0.4517 0.4278 0.4123 0.0022  -0.0034 -0.0329 592 ARG A CG  
4950 C CD  . ARG A 592 ? 0.4189 0.3970 0.3789 0.0041  -0.0011 -0.0308 592 ARG A CD  
4951 N NE  . ARG A 592 ? 0.3869 0.3705 0.3448 0.0054  0.0021  -0.0306 592 ARG A NE  
4952 C CZ  . ARG A 592 ? 0.3932 0.3788 0.3484 0.0076  0.0052  -0.0278 592 ARG A CZ  
4953 N NH1 . ARG A 592 ? 0.4062 0.3886 0.3604 0.0078  0.0056  -0.0257 592 ARG A NH1 
4954 N NH2 . ARG A 592 ? 0.3837 0.3747 0.3367 0.0095  0.0084  -0.0269 592 ARG A NH2 
4955 N N   . LYS A 593 ? 0.5566 0.5196 0.5223 -0.0002 -0.0046 -0.0399 593 LYS A N   
4956 C CA  . LYS A 593 ? 0.6475 0.6091 0.6175 0.0010  -0.0028 -0.0432 593 LYS A CA  
4957 C C   . LYS A 593 ? 0.6418 0.6084 0.6102 -0.0012 0.0001  -0.0467 593 LYS A C   
4958 O O   . LYS A 593 ? 0.6144 0.5837 0.5784 -0.0048 0.0008  -0.0477 593 LYS A O   
4959 C CB  . LYS A 593 ? 0.7150 0.6675 0.6873 0.0021  -0.0032 -0.0438 593 LYS A CB  
4960 C CG  . LYS A 593 ? 0.7881 0.7396 0.7668 0.0059  -0.0026 -0.0454 593 LYS A CG  
4961 C CD  . LYS A 593 ? 0.8382 0.7810 0.8191 0.0086  -0.0029 -0.0447 593 LYS A CD  
4962 C CE  . LYS A 593 ? 0.8768 0.8122 0.8556 0.0062  0.0006  -0.0479 593 LYS A CE  
4963 N NZ  . LYS A 593 ? 0.9207 0.8581 0.9029 0.0063  0.0037  -0.0524 593 LYS A NZ  
4964 N N   . ALA A 594 ? 0.6674 0.6360 0.6394 0.0004  0.0018  -0.0488 594 ALA A N   
4965 C CA  . ALA A 594 ? 0.6639 0.6382 0.6346 -0.0014 0.0048  -0.0522 594 ALA A CA  
4966 C C   . ALA A 594 ? 0.6793 0.6497 0.6490 -0.0049 0.0066  -0.0565 594 ALA A C   
4967 O O   . ALA A 594 ? 0.6644 0.6258 0.6371 -0.0039 0.0069  -0.0578 594 ALA A O   
4968 C CB  . ALA A 594 ? 0.6546 0.6308 0.6293 0.0011  0.0065  -0.0535 594 ALA A CB  
4969 N N   . SER A 595 ? 0.6939 0.6715 0.6592 -0.0089 0.0082  -0.0588 595 SER A N   
4970 C CA  . SER A 595 ? 0.7503 0.7252 0.7135 -0.0139 0.0106  -0.0638 595 SER A CA  
4971 C C   . SER A 595 ? 0.7299 0.7135 0.6918 -0.0167 0.0137  -0.0685 595 SER A C   
4972 O O   . SER A 595 ? 0.7458 0.7299 0.7052 -0.0221 0.0163  -0.0736 595 SER A O   
4973 C CB  . SER A 595 ? 0.7641 0.7404 0.7223 -0.0180 0.0097  -0.0631 595 SER A CB  
4974 O OG  . SER A 595 ? 0.7862 0.7593 0.7419 -0.0239 0.0129  -0.0685 595 SER A OG  
4975 N N   . ILE A 596 ? 0.6815 0.6721 0.6446 -0.0135 0.0137  -0.0670 596 ILE A N   
4976 C CA  . ILE A 596 ? 0.6765 0.6753 0.6386 -0.0152 0.0166  -0.0710 596 ILE A CA  
4977 C C   . ILE A 596 ? 0.6825 0.6797 0.6492 -0.0109 0.0177  -0.0706 596 ILE A C   
4978 O O   . ILE A 596 ? 0.6590 0.6585 0.6264 -0.0123 0.0206  -0.0749 596 ILE A O   
4979 C CB  . ILE A 596 ? 0.6464 0.6611 0.6027 -0.0171 0.0165  -0.0699 596 ILE A CB  
4980 C CG1 . ILE A 596 ? 0.6205 0.6408 0.5760 -0.0115 0.0151  -0.0634 596 ILE A CG1 
4981 C CG2 . ILE A 596 ? 0.6657 0.6840 0.6181 -0.0220 0.0157  -0.0711 596 ILE A CG2 
4982 C CD1 . ILE A 596 ? 0.6116 0.6266 0.5674 -0.0091 0.0123  -0.0582 596 ILE A CD1 
4983 N N   . MET B 1   ? 1.2249 0.7942 0.7695 -0.0334 0.1181  -0.0304 1   MET B N   
4984 C CA  . MET B 1   ? 1.1672 0.7589 0.7295 -0.0446 0.1142  -0.0336 1   MET B CA  
4985 C C   . MET B 1   ? 1.0603 0.6911 0.6562 -0.0457 0.1032  -0.0341 1   MET B C   
4986 O O   . MET B 1   ? 1.0857 0.7381 0.6999 -0.0493 0.0982  -0.0350 1   MET B O   
4987 C CB  . MET B 1   ? 1.2522 0.8304 0.7965 -0.0647 0.1229  -0.0392 1   MET B CB  
4988 C CG  . MET B 1   ? 1.3134 0.8992 0.8582 -0.0785 0.1244  -0.0429 1   MET B CG  
4989 S SD  . MET B 1   ? 1.4191 1.0167 0.9632 -0.1040 0.1282  -0.0500 1   MET B SD  
4990 C CE  . MET B 1   ? 1.3665 0.9759 0.9134 -0.1148 0.1289  -0.0526 1   MET B CE  
4991 N N   . VAL B 2   ? 0.9531 0.5920 0.5562 -0.0422 0.0999  -0.0333 2   VAL B N   
4992 C CA  . VAL B 2   ? 0.8757 0.5489 0.5083 -0.0424 0.0902  -0.0336 2   VAL B CA  
4993 C C   . VAL B 2   ? 0.8155 0.5022 0.4660 -0.0260 0.0815  -0.0294 2   VAL B C   
4994 O O   . VAL B 2   ? 0.8115 0.4884 0.4556 -0.0145 0.0812  -0.0265 2   VAL B O   
4995 C CB  . VAL B 2   ? 0.8887 0.5673 0.5218 -0.0486 0.0906  -0.0356 2   VAL B CB  
4996 C CG1 . VAL B 2   ? 0.8462 0.5592 0.5064 -0.0533 0.0828  -0.0371 2   VAL B CG1 
4997 C CG2 . VAL B 2   ? 0.9474 0.6050 0.5559 -0.0633 0.1010  -0.0392 2   VAL B CG2 
4998 N N   . HIS B 3   ? 0.7190 0.4291 0.3917 -0.0254 0.0747  -0.0291 3   HIS B N   
4999 C CA  . HIS B 3   ? 0.6652 0.3894 0.3553 -0.0119 0.0666  -0.0255 3   HIS B CA  
5000 C C   . HIS B 3   ? 0.6058 0.3582 0.3214 -0.0126 0.0582  -0.0260 3   HIS B C   
5001 O O   . HIS B 3   ? 0.5440 0.3061 0.2717 -0.0025 0.0519  -0.0237 3   HIS B O   
5002 C CB  . HIS B 3   ? 0.6911 0.4163 0.3842 -0.0083 0.0660  -0.0238 3   HIS B CB  
5003 C CG  . HIS B 3   ? 0.7495 0.4457 0.4167 -0.0049 0.0743  -0.0227 3   HIS B CG  
5004 N ND1 . HIS B 3   ? 0.7797 0.4649 0.4351 -0.0138 0.0802  -0.0248 3   HIS B ND1 
5005 C CD2 . HIS B 3   ? 0.7525 0.4285 0.4026 0.0074  0.0778  -0.0194 3   HIS B CD2 
5006 C CE1 . HIS B 3   ? 0.7932 0.4502 0.4242 -0.0075 0.0875  -0.0231 3   HIS B CE1 
5007 N NE2 . HIS B 3   ? 0.7872 0.4389 0.4149 0.0059  0.0860  -0.0195 3   HIS B NE2 
5008 N N   . TYR B 4   ? 0.5639 0.3291 0.2862 -0.0247 0.0585  -0.0292 4   TYR B N   
5009 C CA  . TYR B 4   ? 0.5481 0.3399 0.2935 -0.0258 0.0514  -0.0297 4   TYR B CA  
5010 C C   . TYR B 4   ? 0.5682 0.3666 0.3160 -0.0285 0.0507  -0.0313 4   TYR B C   
5011 O O   . TYR B 4   ? 0.5718 0.3592 0.3047 -0.0359 0.0566  -0.0334 4   TYR B O   
5012 C CB  . TYR B 4   ? 0.5311 0.3375 0.2844 -0.0359 0.0517  -0.0316 4   TYR B CB  
5013 C CG  . TYR B 4   ? 0.5295 0.3354 0.2851 -0.0339 0.0512  -0.0302 4   TYR B CG  
5014 C CD1 . TYR B 4   ? 0.5266 0.3222 0.2798 -0.0226 0.0499  -0.0269 4   TYR B CD1 
5015 C CD2 . TYR B 4   ? 0.5209 0.3386 0.2815 -0.0429 0.0519  -0.0320 4   TYR B CD2 
5016 C CE1 . TYR B 4   ? 0.5229 0.3191 0.2784 -0.0205 0.0496  -0.0255 4   TYR B CE1 
5017 C CE2 . TYR B 4   ? 0.5188 0.3363 0.2814 -0.0410 0.0516  -0.0306 4   TYR B CE2 
5018 C CZ  . TYR B 4   ? 0.5165 0.3227 0.2765 -0.0297 0.0505  -0.0274 4   TYR B CZ  
5019 O OH  . TYR B 4   ? 0.5167 0.3233 0.2786 -0.0276 0.0504  -0.0259 4   TYR B OH  
5020 N N   . TYR B 5   ? 0.5511 0.3673 0.3173 -0.0230 0.0436  -0.0303 5   TYR B N   
5021 C CA  . TYR B 5   ? 0.5483 0.3759 0.3204 -0.0258 0.0421  -0.0319 5   TYR B CA  
5022 C C   . TYR B 5   ? 0.5361 0.3873 0.3258 -0.0298 0.0384  -0.0326 5   TYR B C   
5023 O O   . TYR B 5   ? 0.5408 0.4016 0.3442 -0.0241 0.0332  -0.0307 5   TYR B O   
5024 C CB  . TYR B 5   ? 0.5333 0.3606 0.3105 -0.0152 0.0373  -0.0304 5   TYR B CB  
5025 C CG  . TYR B 5   ? 0.5287 0.3677 0.3123 -0.0169 0.0355  -0.0320 5   TYR B CG  
5026 C CD1 . TYR B 5   ? 0.5336 0.3661 0.3046 -0.0234 0.0408  -0.0340 5   TYR B CD1 
5027 C CD2 . TYR B 5   ? 0.5086 0.3645 0.3098 -0.0123 0.0290  -0.0315 5   TYR B CD2 
5028 C CE1 . TYR B 5   ? 0.5339 0.3783 0.3107 -0.0246 0.0395  -0.0353 5   TYR B CE1 
5029 C CE2 . TYR B 5   ? 0.5083 0.3741 0.3141 -0.0129 0.0278  -0.0328 5   TYR B CE2 
5030 C CZ  . TYR B 5   ? 0.5220 0.3830 0.3162 -0.0188 0.0329  -0.0346 5   TYR B CZ  
5031 O OH  . TYR B 5   ? 0.5301 0.4019 0.3287 -0.0190 0.0320  -0.0358 5   TYR B OH  
5032 N N   . ARG B 6   ? 0.5341 0.3951 0.3227 -0.0395 0.0414  -0.0351 6   ARG B N   
5033 C CA  . ARG B 6   ? 0.5302 0.4152 0.3344 -0.0423 0.0383  -0.0353 6   ARG B CA  
5034 C C   . ARG B 6   ? 0.5112 0.4091 0.3295 -0.0344 0.0325  -0.0341 6   ARG B C   
5035 O O   . ARG B 6   ? 0.5135 0.4064 0.3278 -0.0317 0.0326  -0.0346 6   ARG B O   
5036 C CB  . ARG B 6   ? 0.5476 0.4421 0.3461 -0.0549 0.0432  -0.0384 6   ARG B CB  
5037 C CG  . ARG B 6   ? 0.5769 0.4628 0.3638 -0.0644 0.0485  -0.0401 6   ARG B CG  
5038 C CD  . ARG B 6   ? 0.6351 0.5300 0.4145 -0.0785 0.0538  -0.0438 6   ARG B CD  
5039 N NE  . ARG B 6   ? 0.7012 0.5889 0.4711 -0.0808 0.0569  -0.0451 6   ARG B NE  
5040 C CZ  . ARG B 6   ? 0.7179 0.6038 0.4746 -0.0937 0.0634  -0.0485 6   ARG B CZ  
5041 N NH1 . ARG B 6   ? 0.7473 0.6382 0.4984 -0.1062 0.0674  -0.0513 6   ARG B NH1 
5042 N NH2 . ARG B 6   ? 0.7298 0.6092 0.4786 -0.0947 0.0659  -0.0493 6   ARG B NH2 
5043 N N   . LEU B 7   ? 0.4800 0.3931 0.3136 -0.0305 0.0279  -0.0325 7   LEU B N   
5044 C CA  . LEU B 7   ? 0.4649 0.3881 0.3103 -0.0230 0.0230  -0.0314 7   LEU B CA  
5045 C C   . LEU B 7   ? 0.4789 0.4206 0.3287 -0.0263 0.0239  -0.0326 7   LEU B C   
5046 O O   . LEU B 7   ? 0.4915 0.4399 0.3482 -0.0201 0.0209  -0.0320 7   LEU B O   
5047 C CB  . LEU B 7   ? 0.4307 0.3595 0.2891 -0.0166 0.0181  -0.0289 7   LEU B CB  
5048 C CG  . LEU B 7   ? 0.4356 0.3515 0.2934 -0.0119 0.0161  -0.0272 7   LEU B CG  
5049 C CD1 . LEU B 7   ? 0.4300 0.3549 0.3020 -0.0064 0.0112  -0.0250 7   LEU B CD1 
5050 C CD2 . LEU B 7   ? 0.4279 0.3289 0.2778 -0.0072 0.0156  -0.0276 7   LEU B CD2 
5051 N N   . SER B 8   ? 0.4804 0.4304 0.3255 -0.0359 0.0282  -0.0343 8   SER B N   
5052 C CA  . SER B 8   ? 0.5154 0.4874 0.3650 -0.0397 0.0293  -0.0353 8   SER B CA  
5053 C C   . SER B 8   ? 0.5370 0.5097 0.3831 -0.0382 0.0301  -0.0364 8   SER B C   
5054 O O   . SER B 8   ? 0.5192 0.4766 0.3533 -0.0415 0.0332  -0.0380 8   SER B O   
5055 C CB  . SER B 8   ? 0.5441 0.5237 0.3868 -0.0524 0.0342  -0.0377 8   SER B CB  
5056 O OG  . SER B 8   ? 0.5587 0.5639 0.4069 -0.0562 0.0351  -0.0385 8   SER B OG  
5057 N N   . LEU B 9   ? 0.5268 0.5165 0.3824 -0.0325 0.0277  -0.0354 9   LEU B N   
5058 C CA  . LEU B 9   ? 0.5561 0.5507 0.4090 -0.0314 0.0289  -0.0365 9   LEU B CA  
5059 C C   . LEU B 9   ? 0.5985 0.5993 0.4415 -0.0435 0.0347  -0.0394 9   LEU B C   
5060 O O   . LEU B 9   ? 0.6057 0.5998 0.4407 -0.0449 0.0370  -0.0407 9   LEU B O   
5061 C CB  . LEU B 9   ? 0.5204 0.5347 0.3845 -0.0233 0.0262  -0.0347 9   LEU B CB  
5062 C CG  . LEU B 9   ? 0.5116 0.5161 0.3801 -0.0114 0.0219  -0.0331 9   LEU B CG  
5063 C CD1 . LEU B 9   ? 0.4957 0.4797 0.3643 -0.0082 0.0188  -0.0323 9   LEU B CD1 
5064 C CD2 . LEU B 9   ? 0.4957 0.5177 0.3741 -0.0034 0.0199  -0.0309 9   LEU B CD2 
5065 N N   . LYS B 10  ? 0.6180 0.6314 0.4609 -0.0527 0.0373  -0.0404 10  LYS B N   
5066 C CA  . LYS B 10  ? 0.6517 0.6744 0.4855 -0.0665 0.0431  -0.0436 10  LYS B CA  
5067 C C   . LYS B 10  ? 0.6546 0.6534 0.4717 -0.0733 0.0478  -0.0458 10  LYS B C   
5068 O O   . LYS B 10  ? 0.6771 0.6817 0.4862 -0.0825 0.0525  -0.0483 10  LYS B O   
5069 C CB  . LYS B 10  ? 0.7002 0.7347 0.5346 -0.0761 0.0449  -0.0448 10  LYS B CB  
5070 C CG  . LYS B 10  ? 0.7506 0.8120 0.6001 -0.0704 0.0411  -0.0426 10  LYS B CG  
5071 C CD  . LYS B 10  ? 0.7938 0.8684 0.6429 -0.0808 0.0431  -0.0441 10  LYS B CD  
5072 C CE  . LYS B 10  ? 0.8168 0.9133 0.6805 -0.0724 0.0389  -0.0410 10  LYS B CE  
5073 N NZ  . LYS B 10  ? 0.8534 0.9764 0.7185 -0.0825 0.0411  -0.0428 10  LYS B NZ  
5074 N N   . SER B 11  ? 0.6786 0.6511 0.4900 -0.0686 0.0468  -0.0448 11  SER B N   
5075 C CA  . SER B 11  ? 0.7216 0.6688 0.5160 -0.0727 0.0514  -0.0461 11  SER B CA  
5076 C C   . SER B 11  ? 0.7128 0.6499 0.5059 -0.0632 0.0494  -0.0450 11  SER B C   
5077 O O   . SER B 11  ? 0.7724 0.6862 0.5524 -0.0626 0.0519  -0.0451 11  SER B O   
5078 C CB  . SER B 11  ? 0.7135 0.6377 0.4996 -0.0729 0.0524  -0.0456 11  SER B CB  
5079 O OG  . SER B 11  ? 0.6776 0.6015 0.4758 -0.0615 0.0462  -0.0427 11  SER B OG  
5080 N N   . ARG B 12  ? 0.6706 0.6250 0.4761 -0.0556 0.0453  -0.0439 12  ARG B N   
5081 C CA  . ARG B 12  ? 0.6717 0.6186 0.4755 -0.0475 0.0436  -0.0434 12  ARG B CA  
5082 C C   . ARG B 12  ? 0.7168 0.6618 0.5082 -0.0555 0.0495  -0.0455 12  ARG B C   
5083 O O   . ARG B 12  ? 0.7138 0.6708 0.5012 -0.0673 0.0541  -0.0476 12  ARG B O   
5084 C CB  . ARG B 12  ? 0.6300 0.5948 0.4485 -0.0376 0.0385  -0.0420 12  ARG B CB  
5085 C CG  . ARG B 12  ? 0.5970 0.5891 0.4209 -0.0417 0.0403  -0.0427 12  ARG B CG  
5086 C CD  . ARG B 12  ? 0.5834 0.5900 0.4206 -0.0302 0.0355  -0.0406 12  ARG B CD  
5087 N NE  . ARG B 12  ? 0.5738 0.6084 0.4161 -0.0320 0.0373  -0.0408 12  ARG B NE  
5088 C CZ  . ARG B 12  ? 0.5483 0.6041 0.3977 -0.0351 0.0374  -0.0402 12  ARG B CZ  
5089 N NH1 . ARG B 12  ? 0.5464 0.5974 0.3988 -0.0371 0.0360  -0.0395 12  ARG B NH1 
5090 N NH2 . ARG B 12  ? 0.5521 0.6352 0.4058 -0.0357 0.0391  -0.0402 12  ARG B NH2 
5091 N N   . GLN B 13  ? 0.7194 0.6501 0.5043 -0.0496 0.0492  -0.0452 13  GLN B N   
5092 C CA  . GLN B 13  ? 0.7334 0.6607 0.5059 -0.0563 0.0548  -0.0469 13  GLN B CA  
5093 C C   . GLN B 13  ? 0.7183 0.6571 0.4965 -0.0490 0.0526  -0.0466 13  GLN B C   
5094 O O   . GLN B 13  ? 0.7159 0.6573 0.5044 -0.0375 0.0467  -0.0452 13  GLN B O   
5095 C CB  . GLN B 13  ? 0.7565 0.6537 0.5114 -0.0574 0.0586  -0.0468 13  GLN B CB  
5096 C CG  . GLN B 13  ? 0.8114 0.6974 0.5539 -0.0695 0.0646  -0.0482 13  GLN B CG  
5097 C CD  . GLN B 13  ? 0.8395 0.6936 0.5653 -0.0670 0.0676  -0.0471 13  GLN B CD  
5098 O OE1 . GLN B 13  ? 0.8720 0.7139 0.5909 -0.0710 0.0700  -0.0472 13  GLN B OE1 
5099 N NE2 . GLN B 13  ? 0.8121 0.6530 0.5309 -0.0594 0.0675  -0.0460 13  GLN B NE2 
5100 N N   . LYS B 14  ? 0.7633 0.7091 0.5341 -0.0563 0.0576  -0.0482 14  LYS B N   
5101 C CA  . LYS B 14  ? 0.7646 0.7184 0.5379 -0.0495 0.0564  -0.0481 14  LYS B CA  
5102 C C   . LYS B 14  ? 0.7614 0.6898 0.5233 -0.0438 0.0566  -0.0476 14  LYS B C   
5103 O O   . LYS B 14  ? 0.7957 0.7079 0.5421 -0.0511 0.0622  -0.0484 14  LYS B O   
5104 C CB  . LYS B 14  ? 0.7960 0.7700 0.5664 -0.0594 0.0617  -0.0498 14  LYS B CB  
5105 C CG  . LYS B 14  ? 0.8349 0.8164 0.6066 -0.0518 0.0609  -0.0495 14  LYS B CG  
5106 C CD  . LYS B 14  ? 0.8554 0.8645 0.6287 -0.0594 0.0650  -0.0508 14  LYS B CD  
5107 C CE  . LYS B 14  ? 0.8641 0.8793 0.6384 -0.0502 0.0640  -0.0503 14  LYS B CE  
5108 N NZ  . LYS B 14  ? 0.8978 0.9372 0.6704 -0.0583 0.0691  -0.0515 14  LYS B NZ  
5109 N N   . ALA B 15  ? 0.7140 0.6384 0.4827 -0.0309 0.0507  -0.0464 15  ALA B N   
5110 C CA  . ALA B 15  ? 0.7302 0.6343 0.4897 -0.0240 0.0499  -0.0459 15  ALA B CA  
5111 C C   . ALA B 15  ? 0.7491 0.6534 0.4982 -0.0275 0.0548  -0.0470 15  ALA B C   
5112 O O   . ALA B 15  ? 0.7269 0.6512 0.4817 -0.0284 0.0555  -0.0477 15  ALA B O   
5113 C CB  . ALA B 15  ? 0.6886 0.5936 0.4585 -0.0109 0.0426  -0.0452 15  ALA B CB  
5114 N N   . PRO B 16  ? 0.7609 0.6431 0.4941 -0.0289 0.0586  -0.0467 16  PRO B N   
5115 C CA  . PRO B 16  ? 0.7765 0.6558 0.4992 -0.0300 0.0626  -0.0473 16  PRO B CA  
5116 C C   . PRO B 16  ? 0.8229 0.7045 0.5516 -0.0170 0.0570  -0.0470 16  PRO B C   
5117 O O   . PRO B 16  ? 0.7846 0.6672 0.5238 -0.0081 0.0504  -0.0465 16  PRO B O   
5118 C CB  . PRO B 16  ? 0.7962 0.6477 0.4997 -0.0328 0.0677  -0.0466 16  PRO B CB  
5119 C CG  . PRO B 16  ? 0.8076 0.6469 0.5140 -0.0267 0.0634  -0.0452 16  PRO B CG  
5120 C CD  . PRO B 16  ? 0.7738 0.6325 0.4972 -0.0286 0.0595  -0.0456 16  PRO B CD  
5121 N N   . LYS B 17  ? 0.8398 0.7217 0.5610 -0.0165 0.0599  -0.0475 17  LYS B N   
5122 C CA  . LYS B 17  ? 0.8458 0.7274 0.5697 -0.0048 0.0554  -0.0476 17  LYS B CA  
5123 C C   . LYS B 17  ? 0.8265 0.6858 0.5432 0.0030  0.0523  -0.0466 17  LYS B C   
5124 O O   . LYS B 17  ? 0.8120 0.6713 0.5364 0.0128  0.0458  -0.0467 17  LYS B O   
5125 C CB  . LYS B 17  ? 0.8939 0.7810 0.6100 -0.0068 0.0599  -0.0483 17  LYS B CB  
5126 C CG  . LYS B 17  ? 0.9627 0.8582 0.6851 0.0040  0.0555  -0.0488 17  LYS B CG  
5127 C CD  . LYS B 17  ? 0.9820 0.8723 0.6920 0.0046  0.0596  -0.0491 17  LYS B CD  
5128 C CE  . LYS B 17  ? 1.0070 0.9077 0.7229 0.0147  0.0558  -0.0500 17  LYS B CE  
5129 N NZ  . LYS B 17  ? 1.0541 0.9418 0.7715 0.0258  0.0492  -0.0503 17  LYS B NZ  
5130 N N   . ILE B 18  ? 0.8303 0.6710 0.5316 -0.0011 0.0574  -0.0456 18  ILE B N   
5131 C CA  . ILE B 18  ? 0.8473 0.6678 0.5404 0.0065  0.0553  -0.0442 18  ILE B CA  
5132 C C   . ILE B 18  ? 0.8718 0.6763 0.5540 0.0001  0.0602  -0.0428 18  ILE B C   
5133 O O   . ILE B 18  ? 0.8611 0.6665 0.5379 -0.0113 0.0665  -0.0433 18  ILE B O   
5134 C CB  . ILE B 18  ? 0.8799 0.6892 0.5600 0.0126  0.0567  -0.0438 18  ILE B CB  
5135 C CG1 . ILE B 18  ? 0.8905 0.6895 0.5530 0.0036  0.0662  -0.0433 18  ILE B CG1 
5136 C CG2 . ILE B 18  ? 0.8499 0.6735 0.5396 0.0193  0.0520  -0.0454 18  ILE B CG2 
5137 C CD1 . ILE B 18  ? 0.8959 0.6777 0.5416 0.0098  0.0687  -0.0420 18  ILE B CD1 
5138 N N   . VAL B 19  ? 0.8961 0.6864 0.5745 0.0075  0.0575  -0.0411 19  VAL B N   
5139 C CA  . VAL B 19  ? 0.9317 0.7047 0.5981 0.0034  0.0624  -0.0395 19  VAL B CA  
5140 C C   . VAL B 19  ? 0.9935 0.7445 0.6365 0.0017  0.0705  -0.0382 19  VAL B C   
5141 O O   . VAL B 19  ? 0.9928 0.7405 0.6291 0.0069  0.0708  -0.0379 19  VAL B O   
5142 C CB  . VAL B 19  ? 0.9047 0.6728 0.5764 0.0121  0.0568  -0.0379 19  VAL B CB  
5143 C CG1 . VAL B 19  ? 0.8923 0.6795 0.5850 0.0111  0.0507  -0.0391 19  VAL B CG1 
5144 C CG2 . VAL B 19  ? 0.8805 0.6436 0.5497 0.0249  0.0522  -0.0369 19  VAL B CG2 
5145 N N   . ASN B 20  ? 1.0456 0.7810 0.6752 -0.0058 0.0774  -0.0374 20  ASN B N   
5146 C CA  . ASN B 20  ? 1.1609 0.8706 0.7652 -0.0075 0.0862  -0.0357 20  ASN B CA  
5147 C C   . ASN B 20  ? 1.2083 0.8990 0.8017 0.0059  0.0850  -0.0324 20  ASN B C   
5148 O O   . ASN B 20  ? 1.2148 0.9136 0.8211 0.0152  0.0773  -0.0317 20  ASN B O   
5149 C CB  . ASN B 20  ? 1.1806 0.8795 0.7725 -0.0224 0.0951  -0.0367 20  ASN B CB  
5150 C CG  . ASN B 20  ? 1.2050 0.9042 0.8037 -0.0242 0.0932  -0.0366 20  ASN B CG  
5151 O OD1 . ASN B 20  ? 1.2377 0.9145 0.8195 -0.0266 0.0993  -0.0354 20  ASN B OD1 
5152 N ND2 . ASN B 20  ? 1.1885 0.9120 0.8110 -0.0226 0.0850  -0.0379 20  ASN B ND2 
5153 N N   . SER B 21  ? 1.2592 0.9252 0.8283 0.0071  0.0928  -0.0302 21  SER B N   
5154 C CA  . SER B 21  ? 1.2685 0.9158 0.8239 0.0212  0.0929  -0.0265 21  SER B CA  
5155 C C   . SER B 21  ? 1.2482 0.8924 0.8076 0.0261  0.0901  -0.0250 21  SER B C   
5156 O O   . SER B 21  ? 1.2931 0.9325 0.8497 0.0398  0.0867  -0.0222 21  SER B O   
5157 C CB  . SER B 21  ? 1.2909 0.9086 0.8163 0.0195  0.1041  -0.0242 21  SER B CB  
5158 O OG  . SER B 21  ? 1.2435 0.8640 0.7645 0.0153  0.1069  -0.0253 21  SER B OG  
5159 N N   . LYS B 22  ? 1.2276 0.8760 0.7935 0.0149  0.0917  -0.0269 22  LYS B N   
5160 C CA  . LYS B 22  ? 1.1986 0.8450 0.7690 0.0180  0.0894  -0.0257 22  LYS B CA  
5161 C C   . LYS B 22  ? 1.1320 0.7992 0.7245 0.0291  0.0781  -0.0254 22  LYS B C   
5162 O O   . LYS B 22  ? 1.1529 0.8155 0.7448 0.0375  0.0760  -0.0231 22  LYS B O   
5163 C CB  . LYS B 22  ? 1.2213 0.8727 0.7971 0.0028  0.0924  -0.0285 22  LYS B CB  
5164 C CG  . LYS B 22  ? 1.3040 0.9278 0.8545 -0.0060 0.1038  -0.0281 22  LYS B CG  
5165 C CD  . LYS B 22  ? 1.3130 0.9461 0.8691 -0.0239 0.1069  -0.0318 22  LYS B CD  
5166 C CE  . LYS B 22  ? 1.2622 0.9192 0.8433 -0.0239 0.0985  -0.0331 22  LYS B CE  
5167 N NZ  . LYS B 22  ? 1.2517 0.9272 0.8434 -0.0398 0.0995  -0.0369 22  LYS B NZ  
5168 N N   . TYR B 23  ? 1.0631 0.7526 0.6741 0.0288  0.0713  -0.0277 23  TYR B N   
5169 C CA  . TYR B 23  ? 0.9698 0.6795 0.6025 0.0363  0.0609  -0.0282 23  TYR B CA  
5170 C C   . TYR B 23  ? 0.9204 0.6353 0.5546 0.0473  0.0557  -0.0279 23  TYR B C   
5171 O O   . TYR B 23  ? 0.9090 0.6197 0.5343 0.0469  0.0586  -0.0283 23  TYR B O   
5172 C CB  . TYR B 23  ? 0.9332 0.6648 0.5867 0.0276  0.0568  -0.0314 23  TYR B CB  
5173 C CG  . TYR B 23  ? 0.9637 0.6955 0.6194 0.0168  0.0604  -0.0322 23  TYR B CG  
5174 C CD1 . TYR B 23  ? 0.9299 0.6643 0.5937 0.0190  0.0572  -0.0313 23  TYR B CD1 
5175 C CD2 . TYR B 23  ? 0.9778 0.7090 0.6277 0.0039  0.0669  -0.0341 23  TYR B CD2 
5176 C CE1 . TYR B 23  ? 0.9234 0.6588 0.5893 0.0091  0.0603  -0.0322 23  TYR B CE1 
5177 C CE2 . TYR B 23  ? 0.9554 0.6887 0.6073 -0.0066 0.0700  -0.0352 23  TYR B CE2 
5178 C CZ  . TYR B 23  ? 0.9569 0.6919 0.6167 -0.0037 0.0666  -0.0342 23  TYR B CZ  
5179 O OH  . TYR B 23  ? 0.9878 0.7250 0.6491 -0.0140 0.0695  -0.0355 23  TYR B OH  
5180 N N   . ASN B 24  ? 0.8585 0.5834 0.5038 0.0565  0.0480  -0.0273 24  ASN B N   
5181 C CA  . ASN B 24  ? 0.7977 0.5325 0.4484 0.0652  0.0416  -0.0279 24  ASN B CA  
5182 C C   . ASN B 24  ? 0.8070 0.5572 0.4715 0.0592  0.0384  -0.0316 24  ASN B C   
5183 O O   . ASN B 24  ? 0.7863 0.5478 0.4650 0.0519  0.0366  -0.0334 24  ASN B O   
5184 C CB  . ASN B 24  ? 0.7791 0.5245 0.4410 0.0735  0.0340  -0.0272 24  ASN B CB  
5185 C CG  . ASN B 24  ? 0.7872 0.5418 0.4518 0.0826  0.0277  -0.0280 24  ASN B CG  
5186 O OD1 . ASN B 24  ? 0.8000 0.5663 0.4753 0.0802  0.0234  -0.0312 24  ASN B OD1 
5187 N ND2 . ASN B 24  ? 0.8081 0.5580 0.4626 0.0933  0.0272  -0.0252 24  ASN B ND2 
5188 N N   . SER B 25  ? 0.7809 0.5311 0.4400 0.0630  0.0380  -0.0323 25  SER B N   
5189 C CA  . SER B 25  ? 0.7711 0.5338 0.4400 0.0585  0.0360  -0.0355 25  SER B CA  
5190 C C   . SER B 25  ? 0.7196 0.5001 0.4085 0.0606  0.0271  -0.0380 25  SER B C   
5191 O O   . SER B 25  ? 0.7014 0.4923 0.3988 0.0582  0.0251  -0.0406 25  SER B O   
5192 C CB  . SER B 25  ? 0.7732 0.5303 0.4298 0.0624  0.0382  -0.0356 25  SER B CB  
5193 O OG  . SER B 25  ? 0.7906 0.5490 0.4458 0.0733  0.0329  -0.0352 25  SER B OG  
5194 N N   . ILE B 26  ? 0.6878 0.4712 0.3831 0.0651  0.0223  -0.0372 26  ILE B N   
5195 C CA  . ILE B 26  ? 0.6491 0.4475 0.3626 0.0653  0.0147  -0.0395 26  ILE B CA  
5196 C C   . ILE B 26  ? 0.6271 0.4336 0.3526 0.0567  0.0156  -0.0407 26  ILE B C   
5197 O O   . ILE B 26  ? 0.6190 0.4361 0.3561 0.0561  0.0116  -0.0431 26  ILE B O   
5198 C CB  . ILE B 26  ? 0.6355 0.4365 0.3535 0.0705  0.0102  -0.0381 26  ILE B CB  
5199 C CG1 . ILE B 26  ? 0.6105 0.4257 0.3444 0.0713  0.0022  -0.0410 26  ILE B CG1 
5200 C CG2 . ILE B 26  ? 0.6118 0.4073 0.3290 0.0669  0.0138  -0.0356 26  ILE B CG2 
5201 C CD1 . ILE B 26  ? 0.5794 0.4000 0.3174 0.0764  -0.0028 -0.0401 26  ILE B CD1 
5202 N N   . LEU B 27  ? 0.6467 0.4473 0.3675 0.0504  0.0215  -0.0391 27  LEU B N   
5203 C CA  . LEU B 27  ? 0.6442 0.4535 0.3744 0.0419  0.0233  -0.0401 27  LEU B CA  
5204 C C   . LEU B 27  ? 0.6565 0.4740 0.3890 0.0393  0.0243  -0.0421 27  LEU B C   
5205 O O   . LEU B 27  ? 0.6525 0.4825 0.3965 0.0356  0.0231  -0.0433 27  LEU B O   
5206 C CB  . LEU B 27  ? 0.6365 0.4368 0.3576 0.0348  0.0303  -0.0384 27  LEU B CB  
5207 C CG  . LEU B 27  ? 0.6648 0.4574 0.3839 0.0366  0.0301  -0.0363 27  LEU B CG  
5208 C CD1 . LEU B 27  ? 0.6682 0.4499 0.3761 0.0283  0.0380  -0.0353 27  LEU B CD1 
5209 C CD2 . LEU B 27  ? 0.6296 0.4356 0.3669 0.0374  0.0236  -0.0368 27  LEU B CD2 
5210 N N   . ASN B 28  ? 0.6665 0.4773 0.3872 0.0418  0.0268  -0.0423 28  ASN B N   
5211 C CA  . ASN B 28  ? 0.6940 0.5127 0.4160 0.0410  0.0276  -0.0442 28  ASN B CA  
5212 C C   . ASN B 28  ? 0.6742 0.5045 0.4095 0.0456  0.0210  -0.0464 28  ASN B C   
5213 O O   . ASN B 28  ? 0.7097 0.5506 0.4513 0.0435  0.0215  -0.0476 28  ASN B O   
5214 C CB  . ASN B 28  ? 0.7103 0.5186 0.4166 0.0440  0.0311  -0.0438 28  ASN B CB  
5215 C CG  . ASN B 28  ? 0.7460 0.5415 0.4371 0.0379  0.0393  -0.0419 28  ASN B CG  
5216 O OD1 . ASN B 28  ? 0.7337 0.5308 0.4263 0.0294  0.0431  -0.0416 28  ASN B OD1 
5217 N ND2 . ASN B 28  ? 0.7873 0.5692 0.4625 0.0420  0.0424  -0.0406 28  ASN B ND2 
5218 N N   . ILE B 29  ? 0.6569 0.4851 0.3952 0.0519  0.0151  -0.0469 29  ILE B N   
5219 C CA  . ILE B 29  ? 0.6301 0.4663 0.3792 0.0556  0.0090  -0.0494 29  ILE B CA  
5220 C C   . ILE B 29  ? 0.6196 0.4652 0.3821 0.0516  0.0080  -0.0493 29  ILE B C   
5221 O O   . ILE B 29  ? 0.6088 0.4620 0.3777 0.0523  0.0069  -0.0508 29  ILE B O   
5222 C CB  . ILE B 29  ? 0.6154 0.4484 0.3649 0.0612  0.0031  -0.0500 29  ILE B CB  
5223 C CG1 . ILE B 29  ? 0.6104 0.4362 0.3466 0.0664  0.0038  -0.0501 29  ILE B CG1 
5224 C CG2 . ILE B 29  ? 0.5973 0.4368 0.3568 0.0631  -0.0025 -0.0530 29  ILE B CG2 
5225 C CD1 . ILE B 29  ? 0.6099 0.4335 0.3437 0.0717  -0.0003 -0.0496 29  ILE B CD1 
5226 N N   . ALA B 30  ? 0.5886 0.4331 0.3540 0.0479  0.0089  -0.0474 30  ALA B N   
5227 C CA  . ALA B 30  ? 0.5757 0.4289 0.3530 0.0443  0.0080  -0.0469 30  ALA B CA  
5228 C C   . ALA B 30  ? 0.5596 0.4216 0.3382 0.0395  0.0127  -0.0468 30  ALA B C   
5229 O O   . ALA B 30  ? 0.5728 0.4449 0.3608 0.0395  0.0115  -0.0472 30  ALA B O   
5230 C CB  . ALA B 30  ? 0.5687 0.4184 0.3475 0.0417  0.0082  -0.0449 30  ALA B CB  
5231 N N   . LEU B 31  ? 0.5614 0.4200 0.3297 0.0354  0.0183  -0.0462 31  LEU B N   
5232 C CA  . LEU B 31  ? 0.5611 0.4303 0.3295 0.0299  0.0231  -0.0464 31  LEU B CA  
5233 C C   . LEU B 31  ? 0.5560 0.4342 0.3280 0.0348  0.0216  -0.0479 31  LEU B C   
5234 O O   . LEU B 31  ? 0.5443 0.4366 0.3232 0.0334  0.0228  -0.0479 31  LEU B O   
5235 C CB  . LEU B 31  ? 0.5628 0.4244 0.3172 0.0242  0.0297  -0.0458 31  LEU B CB  
5236 C CG  . LEU B 31  ? 0.5713 0.4243 0.3199 0.0173  0.0335  -0.0444 31  LEU B CG  
5237 C CD1 . LEU B 31  ? 0.6078 0.4484 0.3392 0.0126  0.0404  -0.0440 31  LEU B CD1 
5238 C CD2 . LEU B 31  ? 0.5350 0.4012 0.2927 0.0100  0.0348  -0.0443 31  LEU B CD2 
5239 N N   . LYS B 32  ? 0.5576 0.4279 0.3242 0.0410  0.0192  -0.0491 32  LYS B N   
5240 C CA  . LYS B 32  ? 0.5628 0.4383 0.3296 0.0462  0.0184  -0.0508 32  LYS B CA  
5241 C C   . LYS B 32  ? 0.5506 0.4326 0.3287 0.0500  0.0142  -0.0514 32  LYS B C   
5242 O O   . LYS B 32  ? 0.5474 0.4408 0.3301 0.0511  0.0157  -0.0513 32  LYS B O   
5243 C CB  . LYS B 32  ? 0.6149 0.4790 0.3724 0.0516  0.0164  -0.0522 32  LYS B CB  
5244 C CG  . LYS B 32  ? 0.6180 0.4843 0.3747 0.0580  0.0145  -0.0544 32  LYS B CG  
5245 C CD  . LYS B 32  ? 0.6655 0.5387 0.4165 0.0569  0.0198  -0.0543 32  LYS B CD  
5246 C CE  . LYS B 32  ? 0.7125 0.5894 0.4637 0.0639  0.0182  -0.0564 32  LYS B CE  
5247 N NZ  . LYS B 32  ? 0.7232 0.6146 0.4757 0.0630  0.0229  -0.0557 32  LYS B NZ  
5248 N N   . ASN B 33  ? 0.5439 0.4191 0.3263 0.0517  0.0095  -0.0517 33  ASN B N   
5249 C CA  . ASN B 33  ? 0.5141 0.3923 0.3060 0.0546  0.0058  -0.0522 33  ASN B CA  
5250 C C   . ASN B 33  ? 0.5113 0.4014 0.3115 0.0517  0.0080  -0.0503 33  ASN B C   
5251 O O   . ASN B 33  ? 0.5266 0.4220 0.3318 0.0556  0.0073  -0.0504 33  ASN B O   
5252 C CB  . ASN B 33  ? 0.4981 0.3680 0.2927 0.0552  0.0008  -0.0527 33  ASN B CB  
5253 C CG  . ASN B 33  ? 0.5137 0.3747 0.3007 0.0589  -0.0019 -0.0549 33  ASN B CG  
5254 O OD1 . ASN B 33  ? 0.5197 0.3795 0.3007 0.0623  -0.0012 -0.0566 33  ASN B OD1 
5255 N ND2 . ASN B 33  ? 0.4991 0.3550 0.2860 0.0586  -0.0052 -0.0548 33  ASN B ND2 
5256 N N   . PHE B 34  ? 0.5119 0.4057 0.3125 0.0452  0.0109  -0.0485 34  PHE B N   
5257 C CA  . PHE B 34  ? 0.5111 0.4186 0.3189 0.0415  0.0134  -0.0469 34  PHE B CA  
5258 C C   . PHE B 34  ? 0.5125 0.4338 0.3202 0.0435  0.0166  -0.0469 34  PHE B C   
5259 O O   . PHE B 34  ? 0.5095 0.4401 0.3238 0.0477  0.0160  -0.0462 34  PHE B O   
5260 C CB  . PHE B 34  ? 0.5291 0.4367 0.3345 0.0330  0.0167  -0.0456 34  PHE B CB  
5261 C CG  . PHE B 34  ? 0.5293 0.4521 0.3418 0.0281  0.0191  -0.0443 34  PHE B CG  
5262 C CD1 . PHE B 34  ? 0.5373 0.4685 0.3599 0.0320  0.0165  -0.0433 34  PHE B CD1 
5263 C CD2 . PHE B 34  ? 0.5462 0.4740 0.3542 0.0192  0.0240  -0.0440 34  PHE B CD2 
5264 C CE1 . PHE B 34  ? 0.5377 0.4845 0.3666 0.0281  0.0186  -0.0419 34  PHE B CE1 
5265 C CE2 . PHE B 34  ? 0.5329 0.4764 0.3474 0.0140  0.0260  -0.0431 34  PHE B CE2 
5266 C CZ  . PHE B 34  ? 0.5273 0.4813 0.3526 0.0189  0.0231  -0.0419 34  PHE B CZ  
5267 N N   . ARG B 35  ? 0.5088 0.4314 0.3084 0.0410  0.0203  -0.0476 35  ARG B N   
5268 C CA  . ARG B 35  ? 0.5370 0.4731 0.3355 0.0436  0.0234  -0.0478 35  ARG B CA  
5269 C C   . ARG B 35  ? 0.5252 0.4602 0.3259 0.0540  0.0204  -0.0485 35  ARG B C   
5270 O O   . ARG B 35  ? 0.5373 0.4860 0.3421 0.0581  0.0218  -0.0476 35  ARG B O   
5271 C CB  . ARG B 35  ? 0.5407 0.4739 0.3284 0.0405  0.0272  -0.0487 35  ARG B CB  
5272 C CG  . ARG B 35  ? 0.5648 0.4990 0.3475 0.0295  0.0319  -0.0481 35  ARG B CG  
5273 C CD  . ARG B 35  ? 0.6022 0.5355 0.3739 0.0264  0.0367  -0.0488 35  ARG B CD  
5274 N NE  . ARG B 35  ? 0.6301 0.5453 0.3929 0.0316  0.0348  -0.0497 35  ARG B NE  
5275 C CZ  . ARG B 35  ? 0.6897 0.5880 0.4438 0.0288  0.0355  -0.0494 35  ARG B CZ  
5276 N NH1 . ARG B 35  ? 0.7323 0.6270 0.4842 0.0207  0.0383  -0.0484 35  ARG B NH1 
5277 N NH2 . ARG B 35  ? 0.7021 0.5870 0.4485 0.0347  0.0335  -0.0500 35  ARG B NH2 
5278 N N   . LEU B 36  ? 0.5130 0.4316 0.3097 0.0582  0.0166  -0.0503 36  LEU B N   
5279 C CA  . LEU B 36  ? 0.5086 0.4219 0.3048 0.0670  0.0140  -0.0517 36  LEU B CA  
5280 C C   . LEU B 36  ? 0.5074 0.4237 0.3117 0.0702  0.0124  -0.0504 36  LEU B C   
5281 O O   . LEU B 36  ? 0.5104 0.4300 0.3146 0.0774  0.0131  -0.0503 36  LEU B O   
5282 C CB  . LEU B 36  ? 0.5139 0.4099 0.3045 0.0688  0.0100  -0.0542 36  LEU B CB  
5283 C CG  . LEU B 36  ? 0.5439 0.4338 0.3250 0.0734  0.0102  -0.0566 36  LEU B CG  
5284 C CD1 . LEU B 36  ? 0.5253 0.4257 0.3015 0.0731  0.0153  -0.0559 36  LEU B CD1 
5285 C CD2 . LEU B 36  ? 0.5321 0.4085 0.3076 0.0724  0.0068  -0.0584 36  LEU B CD2 
5286 N N   . CYS B 37  ? 0.5002 0.4145 0.3107 0.0653  0.0105  -0.0493 37  CYS B N   
5287 C CA  . CYS B 37  ? 0.5087 0.4253 0.3268 0.0677  0.0091  -0.0478 37  CYS B CA  
5288 C C   . CYS B 37  ? 0.5111 0.4469 0.3334 0.0696  0.0129  -0.0453 37  CYS B C   
5289 O O   . CYS B 37  ? 0.4769 0.4150 0.3008 0.0770  0.0132  -0.0442 37  CYS B O   
5290 C CB  . CYS B 37  ? 0.5190 0.4311 0.3426 0.0615  0.0066  -0.0470 37  CYS B CB  
5291 S SG  . CYS B 37  ? 0.5691 0.4812 0.4013 0.0638  0.0046  -0.0451 37  CYS B SG  
5292 N N   . LYS B 38  ? 0.5139 0.4632 0.3369 0.0631  0.0161  -0.0444 38  LYS B N   
5293 C CA  . LYS B 38  ? 0.5293 0.5007 0.3564 0.0637  0.0198  -0.0423 38  LYS B CA  
5294 C C   . LYS B 38  ? 0.5440 0.5232 0.3672 0.0727  0.0220  -0.0422 38  LYS B C   
5295 O O   . LYS B 38  ? 0.5503 0.5441 0.3771 0.0786  0.0237  -0.0401 38  LYS B O   
5296 C CB  . LYS B 38  ? 0.5351 0.5185 0.3620 0.0530  0.0231  -0.0421 38  LYS B CB  
5297 C CG  . LYS B 38  ? 0.5315 0.5119 0.3629 0.0450  0.0220  -0.0414 38  LYS B CG  
5298 C CD  . LYS B 38  ? 0.5364 0.5282 0.3658 0.0341  0.0261  -0.0415 38  LYS B CD  
5299 C CE  . LYS B 38  ? 0.5518 0.5289 0.3713 0.0287  0.0276  -0.0433 38  LYS B CE  
5300 N NZ  . LYS B 38  ? 0.5598 0.5447 0.3757 0.0168  0.0322  -0.0436 38  LYS B NZ  
5301 N N   . LYS B 39  ? 0.5439 0.5133 0.3593 0.0746  0.0220  -0.0444 39  LYS B N   
5302 C CA  . LYS B 39  ? 0.5589 0.5336 0.3692 0.0837  0.0242  -0.0447 39  LYS B CA  
5303 C C   . LYS B 39  ? 0.5565 0.5196 0.3652 0.0946  0.0223  -0.0447 39  LYS B C   
5304 O O   . LYS B 39  ? 0.5709 0.5411 0.3764 0.1039  0.0248  -0.0438 39  LYS B O   
5305 C CB  . LYS B 39  ? 0.5896 0.5562 0.3912 0.0822  0.0248  -0.0471 39  LYS B CB  
5306 C CG  . LYS B 39  ? 0.6235 0.6032 0.4238 0.0731  0.0285  -0.0469 39  LYS B CG  
5307 C CD  . LYS B 39  ? 0.6785 0.6470 0.4692 0.0720  0.0291  -0.0491 39  LYS B CD  
5308 C CE  . LYS B 39  ? 0.7234 0.7017 0.5109 0.0619  0.0335  -0.0488 39  LYS B CE  
5309 N NZ  . LYS B 39  ? 0.7690 0.7305 0.5467 0.0592  0.0335  -0.0506 39  LYS B NZ  
5310 N N   . HIS B 40  ? 0.5645 0.5097 0.3744 0.0934  0.0184  -0.0456 40  HIS B N   
5311 C CA  . HIS B 40  ? 0.5848 0.5150 0.3913 0.1018  0.0169  -0.0462 40  HIS B CA  
5312 C C   . HIS B 40  ? 0.6230 0.5606 0.4345 0.1071  0.0182  -0.0429 40  HIS B C   
5313 O O   . HIS B 40  ? 0.6174 0.5566 0.4361 0.1022  0.0167  -0.0414 40  HIS B O   
5314 C CB  . HIS B 40  ? 0.5662 0.4751 0.3714 0.0975  0.0123  -0.0490 40  HIS B CB  
5315 C CG  . HIS B 40  ? 0.5986 0.4897 0.3985 0.1041  0.0110  -0.0503 40  HIS B CG  
5316 N ND1 . HIS B 40  ? 0.5983 0.4764 0.4008 0.1008  0.0078  -0.0510 40  HIS B ND1 
5317 C CD2 . HIS B 40  ? 0.5845 0.4683 0.3756 0.1140  0.0131  -0.0511 40  HIS B CD2 
5318 C CE1 . HIS B 40  ? 0.5779 0.4401 0.3730 0.1071  0.0080  -0.0524 40  HIS B CE1 
5319 N NE2 . HIS B 40  ? 0.5884 0.4533 0.3760 0.1155  0.0114  -0.0525 40  HIS B NE2 
5320 N N   . LYS B 41  ? 0.7218 0.6630 0.5285 0.1182  0.0212  -0.0415 41  LYS B N   
5321 C CA  . LYS B 41  ? 0.7741 0.7211 0.5831 0.1258  0.0230  -0.0379 41  LYS B CA  
5322 C C   . LYS B 41  ? 0.8253 0.7462 0.6277 0.1314  0.0217  -0.0390 41  LYS B C   
5323 O O   . LYS B 41  ? 0.8616 0.7706 0.6536 0.1404  0.0235  -0.0401 41  LYS B O   
5324 C CB  . LYS B 41  ? 0.8071 0.7745 0.6137 0.1362  0.0278  -0.0352 41  LYS B CB  
5325 C CG  . LYS B 41  ? 0.8158 0.8066 0.6252 0.1309  0.0297  -0.0354 41  LYS B CG  
5326 C CD  . LYS B 41  ? 0.8600 0.8721 0.6802 0.1212  0.0297  -0.0335 41  LYS B CD  
5327 C CE  . LYS B 41  ? 0.8666 0.8997 0.6881 0.1139  0.0321  -0.0342 41  LYS B CE  
5328 N NZ  . LYS B 41  ? 0.8350 0.8842 0.6651 0.1019  0.0321  -0.0334 41  LYS B NZ  
5329 N N   . THR B 42  ? 0.8741 0.7853 0.6816 0.1253  0.0188  -0.0389 42  THR B N   
5330 C CA  . THR B 42  ? 0.9608 0.8504 0.7630 0.1296  0.0184  -0.0390 42  THR B CA  
5331 C C   . THR B 42  ? 1.0397 0.9382 0.8461 0.1351  0.0207  -0.0341 42  THR B C   
5332 O O   . THR B 42  ? 0.9671 0.8842 0.7839 0.1301  0.0203  -0.0317 42  THR B O   
5333 C CB  . THR B 42  ? 0.9748 0.8477 0.7797 0.1192  0.0137  -0.0419 42  THR B CB  
5334 O OG1 . THR B 42  ? 0.8857 0.7719 0.7001 0.1090  0.0112  -0.0421 42  THR B OG1 
5335 C CG2 . THR B 42  ? 1.0054 0.8572 0.8002 0.1187  0.0119  -0.0468 42  THR B CG2 
5336 N N   . LYS B 43  ? 1.1475 1.0313 0.9446 0.1456  0.0235  -0.0328 43  LYS B N   
5337 C CA  . LYS B 43  ? 1.2238 1.1087 1.0227 0.1508  0.0255  -0.0283 43  LYS B CA  
5338 C C   . LYS B 43  ? 1.2055 1.0708 1.0067 0.1421  0.0223  -0.0298 43  LYS B C   
5339 O O   . LYS B 43  ? 1.1955 1.0556 0.9965 0.1455  0.0238  -0.0266 43  LYS B O   
5340 C CB  . LYS B 43  ? 1.2813 1.1578 1.0675 0.1669  0.0308  -0.0257 43  LYS B CB  
5341 C CG  . LYS B 43  ? 1.2977 1.2003 1.0839 0.1769  0.0344  -0.0228 43  LYS B CG  
5342 C CD  . LYS B 43  ? 1.3245 1.2207 1.0981 0.1946  0.0401  -0.0190 43  LYS B CD  
5343 C CE  . LYS B 43  ? 1.3278 1.2550 1.1029 0.2048  0.0436  -0.0157 43  LYS B CE  
5344 N NZ  . LYS B 43  ? 1.3299 1.2526 1.0922 0.2240  0.0495  -0.0113 43  LYS B NZ  
5345 N N   . LYS B 44  ? 1.1675 1.0232 0.9703 0.1313  0.0180  -0.0344 44  LYS B N   
5346 C CA  . LYS B 44  ? 1.1153 0.9586 0.9226 0.1211  0.0142  -0.0361 44  LYS B CA  
5347 C C   . LYS B 44  ? 1.0421 0.9053 0.8636 0.1134  0.0121  -0.0337 44  LYS B C   
5348 O O   . LYS B 44  ? 1.0325 0.9095 0.8598 0.1075  0.0104  -0.0348 44  LYS B O   
5349 C CB  . LYS B 44  ? 1.1431 0.9721 0.9464 0.1136  0.0106  -0.0418 44  LYS B CB  
5350 C CG  . LYS B 44  ? 1.1688 0.9900 0.9779 0.1023  0.0062  -0.0438 44  LYS B CG  
5351 C CD  . LYS B 44  ? 1.2484 1.0556 1.0518 0.0964  0.0028  -0.0495 44  LYS B CD  
5352 C CE  . LYS B 44  ? 1.2642 1.0849 1.0746 0.0895  -0.0006 -0.0510 44  LYS B CE  
5353 N NZ  . LYS B 44  ? 1.2550 1.0868 1.0628 0.0943  0.0013  -0.0509 44  LYS B NZ  
5354 N N   . PRO B 45  ? 0.9820 0.8452 0.8080 0.1135  0.0126  -0.0303 45  PRO B N   
5355 C CA  . PRO B 45  ? 0.9223 0.8032 0.7606 0.1070  0.0111  -0.0279 45  PRO B CA  
5356 C C   . PRO B 45  ? 0.8497 0.7341 0.6948 0.0952  0.0069  -0.0309 45  PRO B C   
5357 O O   . PRO B 45  ? 0.8053 0.6747 0.6474 0.0902  0.0040  -0.0346 45  PRO B O   
5358 C CB  . PRO B 45  ? 0.9202 0.7897 0.7592 0.1073  0.0113  -0.0256 45  PRO B CB  
5359 C CG  . PRO B 45  ? 0.9963 0.8512 0.8231 0.1187  0.0154  -0.0243 45  PRO B CG  
5360 C CD  . PRO B 45  ? 1.0152 0.8607 0.8329 0.1207  0.0155  -0.0285 45  PRO B CD  
5361 N N   . VAL B 46  ? 0.7781 0.6824 0.6314 0.0910  0.0069  -0.0292 46  VAL B N   
5362 C CA  . VAL B 46  ? 0.7382 0.6471 0.5959 0.0814  0.0042  -0.0315 46  VAL B CA  
5363 C C   . VAL B 46  ? 0.7327 0.6368 0.5971 0.0737  0.0012  -0.0312 46  VAL B C   
5364 O O   . VAL B 46  ? 0.7498 0.6620 0.6202 0.0732  0.0019  -0.0281 46  VAL B O   
5365 C CB  . VAL B 46  ? 0.6675 0.5989 0.5288 0.0799  0.0065  -0.0301 46  VAL B CB  
5366 C CG1 . VAL B 46  ? 0.6152 0.5513 0.4813 0.0695  0.0048  -0.0311 46  VAL B CG1 
5367 C CG2 . VAL B 46  ? 0.6366 0.5709 0.4910 0.0845  0.0085  -0.0318 46  VAL B CG2 
5368 N N   . GLN B 47  ? 0.6686 0.5605 0.5314 0.0684  -0.0020 -0.0344 47  GLN B N   
5369 C CA  . GLN B 47  ? 0.6780 0.5682 0.5469 0.0609  -0.0049 -0.0344 47  GLN B CA  
5370 C C   . GLN B 47  ? 0.6361 0.5308 0.5053 0.0552  -0.0062 -0.0361 47  GLN B C   
5371 O O   . GLN B 47  ? 0.6220 0.5090 0.4862 0.0544  -0.0080 -0.0391 47  GLN B O   
5372 C CB  . GLN B 47  ? 0.7321 0.6059 0.5992 0.0593  -0.0076 -0.0363 47  GLN B CB  
5373 C CG  . GLN B 47  ? 0.8277 0.6947 0.6952 0.0622  -0.0063 -0.0340 47  GLN B CG  
5374 C CD  . GLN B 47  ? 0.8451 0.7168 0.7212 0.0574  -0.0074 -0.0315 47  GLN B CD  
5375 O OE1 . GLN B 47  ? 0.9146 0.7999 0.7963 0.0574  -0.0061 -0.0286 47  GLN B OE1 
5376 N NE2 . GLN B 47  ? 0.8412 0.7019 0.7177 0.0531  -0.0097 -0.0328 47  GLN B NE2 
5377 N N   . ILE B 48  ? 0.5846 0.4911 0.4586 0.0514  -0.0051 -0.0342 48  ILE B N   
5378 C CA  . ILE B 48  ? 0.5597 0.4690 0.4314 0.0466  -0.0049 -0.0355 48  ILE B CA  
5379 C C   . ILE B 48  ? 0.5411 0.4397 0.4107 0.0438  -0.0082 -0.0376 48  ILE B C   
5380 O O   . ILE B 48  ? 0.5353 0.4307 0.3990 0.0436  -0.0083 -0.0395 48  ILE B O   
5381 C CB  . ILE B 48  ? 0.5274 0.4491 0.4031 0.0420  -0.0026 -0.0333 48  ILE B CB  
5382 C CG1 . ILE B 48  ? 0.5537 0.4888 0.4278 0.0434  0.0010  -0.0327 48  ILE B CG1 
5383 C CG2 . ILE B 48  ? 0.4919 0.4102 0.3646 0.0363  -0.0028 -0.0343 48  ILE B CG2 
5384 C CD1 . ILE B 48  ? 0.5631 0.5054 0.4403 0.0498  0.0021  -0.0307 48  ILE B CD1 
5385 N N   . LEU B 49  ? 0.5311 0.4253 0.4053 0.0421  -0.0109 -0.0371 49  LEU B N   
5386 C CA  . LEU B 49  ? 0.5604 0.4478 0.4331 0.0397  -0.0142 -0.0388 49  LEU B CA  
5387 C C   . LEU B 49  ? 0.5805 0.4598 0.4469 0.0421  -0.0160 -0.0421 49  LEU B C   
5388 O O   . LEU B 49  ? 0.5820 0.4593 0.4435 0.0418  -0.0171 -0.0438 49  LEU B O   
5389 C CB  . LEU B 49  ? 0.5545 0.4405 0.4337 0.0373  -0.0167 -0.0378 49  LEU B CB  
5390 C CG  . LEU B 49  ? 0.5504 0.4437 0.4359 0.0347  -0.0155 -0.0346 49  LEU B CG  
5391 C CD1 . LEU B 49  ? 0.5649 0.4565 0.4566 0.0330  -0.0177 -0.0336 49  LEU B CD1 
5392 C CD2 . LEU B 49  ? 0.5095 0.4053 0.3926 0.0322  -0.0147 -0.0342 49  LEU B CD2 
5393 N N   . ALA B 50  ? 0.5627 0.4366 0.4280 0.0450  -0.0160 -0.0431 50  ALA B N   
5394 C CA  . ALA B 50  ? 0.5544 0.4192 0.4126 0.0470  -0.0176 -0.0467 50  ALA B CA  
5395 C C   . ALA B 50  ? 0.5617 0.4286 0.4135 0.0499  -0.0157 -0.0478 50  ALA B C   
5396 O O   . ALA B 50  ? 0.5912 0.4529 0.4370 0.0504  -0.0174 -0.0507 50  ALA B O   
5397 C CB  . ALA B 50  ? 0.5362 0.3927 0.3926 0.0498  -0.0168 -0.0472 50  ALA B CB  
5398 N N   . LEU B 51  ? 0.5277 0.4030 0.3804 0.0515  -0.0120 -0.0455 51  LEU B N   
5399 C CA  . LEU B 51  ? 0.5395 0.4182 0.3862 0.0538  -0.0095 -0.0462 51  LEU B CA  
5400 C C   . LEU B 51  ? 0.5336 0.4131 0.3774 0.0503  -0.0098 -0.0466 51  LEU B C   
5401 O O   . LEU B 51  ? 0.5538 0.4296 0.3905 0.0518  -0.0099 -0.0487 51  LEU B O   
5402 C CB  . LEU B 51  ? 0.5409 0.4314 0.3903 0.0555  -0.0055 -0.0436 51  LEU B CB  
5403 C CG  . LEU B 51  ? 0.5664 0.4608 0.4112 0.0614  -0.0026 -0.0438 51  LEU B CG  
5404 C CD1 . LEU B 51  ? 0.5724 0.4542 0.4122 0.0669  -0.0039 -0.0458 51  LEU B CD1 
5405 C CD2 . LEU B 51  ? 0.5412 0.4503 0.3909 0.0629  0.0006  -0.0406 51  LEU B CD2 
5406 N N   . LEU B 52  ? 0.5156 0.3989 0.3639 0.0462  -0.0097 -0.0446 52  LEU B N   
5407 C CA  . LEU B 52  ? 0.4941 0.3762 0.3383 0.0433  -0.0092 -0.0444 52  LEU B CA  
5408 C C   . LEU B 52  ? 0.4851 0.3594 0.3252 0.0446  -0.0130 -0.0465 52  LEU B C   
5409 O O   . LEU B 52  ? 0.4563 0.3277 0.2893 0.0451  -0.0122 -0.0470 52  LEU B O   
5410 C CB  . LEU B 52  ? 0.4717 0.3579 0.3210 0.0392  -0.0084 -0.0419 52  LEU B CB  
5411 C CG  . LEU B 52  ? 0.4908 0.3825 0.3377 0.0353  -0.0038 -0.0403 52  LEU B CG  
5412 C CD1 . LEU B 52  ? 0.4805 0.3780 0.3237 0.0358  -0.0004 -0.0410 52  LEU B CD1 
5413 C CD2 . LEU B 52  ? 0.4627 0.3611 0.3173 0.0321  -0.0031 -0.0381 52  LEU B CD2 
5414 N N   . GLN B 53  ? 0.4892 0.3606 0.3334 0.0451  -0.0167 -0.0477 53  GLN B N   
5415 C CA  . GLN B 53  ? 0.5201 0.3871 0.3610 0.0457  -0.0206 -0.0501 53  GLN B CA  
5416 C C   . GLN B 53  ? 0.5279 0.3901 0.3607 0.0489  -0.0211 -0.0532 53  GLN B C   
5417 O O   . GLN B 53  ? 0.5576 0.4176 0.3863 0.0496  -0.0241 -0.0553 53  GLN B O   
5418 C CB  . GLN B 53  ? 0.5115 0.3781 0.3589 0.0435  -0.0243 -0.0508 53  GLN B CB  
5419 C CG  . GLN B 53  ? 0.5330 0.4046 0.3867 0.0409  -0.0247 -0.0479 53  GLN B CG  
5420 C CD  . GLN B 53  ? 0.5362 0.4085 0.3975 0.0381  -0.0272 -0.0479 53  GLN B CD  
5421 O OE1 . GLN B 53  ? 0.5775 0.4471 0.4382 0.0368  -0.0303 -0.0507 53  GLN B OE1 
5422 N NE2 . GLN B 53  ? 0.5465 0.4224 0.4141 0.0364  -0.0255 -0.0449 53  GLN B NE2 
5423 N N   . GLU B 54  ? 0.5090 0.3710 0.3394 0.0510  -0.0181 -0.0534 54  GLU B N   
5424 C CA  . GLU B 54  ? 0.5393 0.3976 0.3613 0.0544  -0.0176 -0.0559 54  GLU B CA  
5425 C C   . GLU B 54  ? 0.5254 0.3865 0.3419 0.0547  -0.0140 -0.0544 54  GLU B C   
5426 O O   . GLU B 54  ? 0.5107 0.3685 0.3192 0.0568  -0.0141 -0.0560 54  GLU B O   
5427 C CB  . GLU B 54  ? 0.5567 0.4129 0.3778 0.0575  -0.0160 -0.0569 54  GLU B CB  
5428 C CG  . GLU B 54  ? 0.5877 0.4376 0.4116 0.0569  -0.0187 -0.0586 54  GLU B CG  
5429 C CD  . GLU B 54  ? 0.6359 0.4826 0.4585 0.0608  -0.0161 -0.0584 54  GLU B CD  
5430 O OE1 . GLU B 54  ? 0.6805 0.5337 0.5024 0.0640  -0.0124 -0.0565 54  GLU B OE1 
5431 O OE2 . GLU B 54  ? 0.6787 0.5167 0.5004 0.0608  -0.0174 -0.0602 54  GLU B OE2 
5432 N N   . ILE B 55  ? 0.4936 0.3605 0.3137 0.0519  -0.0107 -0.0515 55  ILE B N   
5433 C CA  . ILE B 55  ? 0.4843 0.3535 0.2987 0.0504  -0.0064 -0.0502 55  ILE B CA  
5434 C C   . ILE B 55  ? 0.4978 0.3617 0.3064 0.0494  -0.0065 -0.0494 55  ILE B C   
5435 O O   . ILE B 55  ? 0.5244 0.3841 0.3237 0.0509  -0.0050 -0.0500 55  ILE B O   
5436 C CB  . ILE B 55  ? 0.4719 0.3501 0.2914 0.0470  -0.0026 -0.0478 55  ILE B CB  
5437 C CG1 . ILE B 55  ? 0.4558 0.3405 0.2776 0.0501  -0.0012 -0.0483 55  ILE B CG1 
5438 C CG2 . ILE B 55  ? 0.4582 0.3377 0.2715 0.0428  0.0020  -0.0466 55  ILE B CG2 
5439 C CD1 . ILE B 55  ? 0.4286 0.3238 0.2583 0.0483  0.0005  -0.0460 55  ILE B CD1 
5440 N N   . ILE B 56  ? 0.5052 0.3689 0.3182 0.0475  -0.0081 -0.0479 56  ILE B N   
5441 C CA  . ILE B 56  ? 0.5089 0.3673 0.3155 0.0482  -0.0081 -0.0468 56  ILE B CA  
5442 C C   . ILE B 56  ? 0.5116 0.3683 0.3175 0.0521  -0.0133 -0.0488 56  ILE B C   
5443 O O   . ILE B 56  ? 0.5223 0.3821 0.3360 0.0515  -0.0172 -0.0495 56  ILE B O   
5444 C CB  . ILE B 56  ? 0.5060 0.3653 0.3166 0.0452  -0.0072 -0.0442 56  ILE B CB  
5445 C CG1 . ILE B 56  ? 0.5122 0.3756 0.3253 0.0401  -0.0027 -0.0428 56  ILE B CG1 
5446 C CG2 . ILE B 56  ? 0.4978 0.3501 0.2988 0.0471  -0.0057 -0.0425 56  ILE B CG2 
5447 C CD1 . ILE B 56  ? 0.4977 0.3625 0.3154 0.0368  -0.0019 -0.0406 56  ILE B CD1 
5448 N N   . PRO B 57  ? 0.5331 0.3857 0.3293 0.0557  -0.0133 -0.0497 57  PRO B N   
5449 C CA  . PRO B 57  ? 0.5429 0.3963 0.3385 0.0589  -0.0186 -0.0522 57  PRO B CA  
5450 C C   . PRO B 57  ? 0.5435 0.3999 0.3418 0.0597  -0.0215 -0.0508 57  PRO B C   
5451 O O   . PRO B 57  ? 0.5452 0.3995 0.3402 0.0603  -0.0187 -0.0477 57  PRO B O   
5452 C CB  . PRO B 57  ? 0.5566 0.4052 0.3401 0.0629  -0.0170 -0.0528 57  PRO B CB  
5453 C CG  . PRO B 57  ? 0.5531 0.3969 0.3297 0.0620  -0.0111 -0.0496 57  PRO B CG  
5454 C CD  . PRO B 57  ? 0.5415 0.3882 0.3261 0.0566  -0.0085 -0.0483 57  PRO B CD  
5455 N N   . LYS B 58  ? 0.5574 0.4188 0.3608 0.0597  -0.0268 -0.0532 58  LYS B N   
5456 C CA  . LYS B 58  ? 0.5723 0.4399 0.3802 0.0599  -0.0298 -0.0519 58  LYS B CA  
5457 C C   . LYS B 58  ? 0.5921 0.4593 0.3906 0.0656  -0.0290 -0.0496 58  LYS B C   
5458 O O   . LYS B 58  ? 0.6004 0.4712 0.4003 0.0672  -0.0292 -0.0470 58  LYS B O   
5459 C CB  . LYS B 58  ? 0.5793 0.4534 0.3931 0.0578  -0.0356 -0.0554 58  LYS B CB  
5460 C CG  . LYS B 58  ? 0.5639 0.4466 0.3845 0.0568  -0.0383 -0.0539 58  LYS B CG  
5461 C CD  . LYS B 58  ? 0.5753 0.4665 0.3995 0.0544  -0.0440 -0.0575 58  LYS B CD  
5462 C CE  . LYS B 58  ? 0.5877 0.4893 0.4195 0.0530  -0.0463 -0.0556 58  LYS B CE  
5463 N NZ  . LYS B 58  ? 0.5983 0.5051 0.4378 0.0461  -0.0502 -0.0591 58  LYS B NZ  
5464 N N   . SER B 59  ? 0.5894 0.4521 0.3775 0.0694  -0.0277 -0.0505 59  SER B N   
5465 C CA  . SER B 59  ? 0.6201 0.4809 0.3970 0.0760  -0.0263 -0.0480 59  SER B CA  
5466 C C   . SER B 59  ? 0.6134 0.4661 0.3848 0.0768  -0.0204 -0.0436 59  SER B C   
5467 O O   . SER B 59  ? 0.6380 0.4884 0.4007 0.0827  -0.0190 -0.0407 59  SER B O   
5468 C CB  . SER B 59  ? 0.6256 0.4817 0.3918 0.0796  -0.0253 -0.0496 59  SER B CB  
5469 O OG  . SER B 59  ? 0.6451 0.4928 0.4086 0.0765  -0.0206 -0.0496 59  SER B OG  
5470 N N   . TYR B 60  ? 0.5856 0.4339 0.3612 0.0710  -0.0168 -0.0431 60  TYR B N   
5471 C CA  . TYR B 60  ? 0.5809 0.4219 0.3519 0.0698  -0.0113 -0.0396 60  TYR B CA  
5472 C C   . TYR B 60  ? 0.5814 0.4276 0.3582 0.0711  -0.0134 -0.0374 60  TYR B C   
5473 O O   . TYR B 60  ? 0.5668 0.4064 0.3354 0.0741  -0.0096 -0.0342 60  TYR B O   
5474 C CB  . TYR B 60  ? 0.5543 0.3922 0.3286 0.0626  -0.0072 -0.0399 60  TYR B CB  
5475 C CG  . TYR B 60  ? 0.5566 0.3879 0.3268 0.0599  -0.0020 -0.0369 60  TYR B CG  
5476 C CD1 . TYR B 60  ? 0.5571 0.3757 0.3118 0.0607  0.0042  -0.0351 60  TYR B CD1 
5477 C CD2 . TYR B 60  ? 0.5406 0.3772 0.3210 0.0568  -0.0032 -0.0360 60  TYR B CD2 
5478 C CE1 . TYR B 60  ? 0.5563 0.3668 0.3053 0.0578  0.0094  -0.0327 60  TYR B CE1 
5479 C CE2 . TYR B 60  ? 0.5438 0.3737 0.3194 0.0544  0.0014  -0.0335 60  TYR B CE2 
5480 C CZ  . TYR B 60  ? 0.5437 0.3602 0.3033 0.0548  0.0078  -0.0321 60  TYR B CZ  
5481 O OH  . TYR B 60  ? 0.5589 0.3669 0.3122 0.0517  0.0130  -0.0301 60  TYR B OH  
5482 N N   . PHE B 61  ? 0.5792 0.4367 0.3691 0.0689  -0.0190 -0.0393 61  PHE B N   
5483 C CA  . PHE B 61  ? 0.5762 0.4409 0.3729 0.0697  -0.0212 -0.0374 61  PHE B CA  
5484 C C   . PHE B 61  ? 0.6170 0.4913 0.4124 0.0759  -0.0258 -0.0374 61  PHE B C   
5485 O O   . PHE B 61  ? 0.6345 0.5142 0.4311 0.0790  -0.0264 -0.0349 61  PHE B O   
5486 C CB  . PHE B 61  ? 0.5462 0.4175 0.3576 0.0629  -0.0238 -0.0389 61  PHE B CB  
5487 C CG  . PHE B 61  ? 0.5433 0.4085 0.3568 0.0575  -0.0195 -0.0385 61  PHE B CG  
5488 C CD1 . PHE B 61  ? 0.5311 0.3911 0.3416 0.0563  -0.0149 -0.0355 61  PHE B CD1 
5489 C CD2 . PHE B 61  ? 0.5300 0.3954 0.3478 0.0538  -0.0200 -0.0411 61  PHE B CD2 
5490 C CE1 . PHE B 61  ? 0.5306 0.3877 0.3431 0.0507  -0.0112 -0.0355 61  PHE B CE1 
5491 C CE2 . PHE B 61  ? 0.5317 0.3948 0.3517 0.0494  -0.0161 -0.0405 61  PHE B CE2 
5492 C CZ  . PHE B 61  ? 0.5133 0.3733 0.3311 0.0474  -0.0119 -0.0378 61  PHE B CZ  
5493 N N   . GLY B 62  ? 0.6201 0.4980 0.4130 0.0776  -0.0290 -0.0403 62  GLY B N   
5494 C CA  . GLY B 62  ? 0.6439 0.5341 0.4360 0.0829  -0.0338 -0.0408 62  GLY B CA  
5495 C C   . GLY B 62  ? 0.6546 0.5593 0.4604 0.0778  -0.0397 -0.0434 62  GLY B C   
5496 O O   . GLY B 62  ? 0.6901 0.6034 0.4981 0.0763  -0.0444 -0.0471 62  GLY B O   
5497 N N   . THR B 63  ? 0.6563 0.5635 0.4707 0.0745  -0.0391 -0.0415 63  THR B N   
5498 C CA  . THR B 63  ? 0.6267 0.5470 0.4538 0.0689  -0.0440 -0.0435 63  THR B CA  
5499 C C   . THR B 63  ? 0.6204 0.5354 0.4571 0.0611  -0.0428 -0.0439 63  THR B C   
5500 O O   . THR B 63  ? 0.6037 0.5084 0.4389 0.0606  -0.0381 -0.0416 63  THR B O   
5501 C CB  . THR B 63  ? 0.6312 0.5646 0.4607 0.0731  -0.0456 -0.0405 63  THR B CB  
5502 O OG1 . THR B 63  ? 0.6543 0.5796 0.4817 0.0756  -0.0407 -0.0361 63  THR B OG1 
5503 C CG2 . THR B 63  ? 0.6297 0.5718 0.4500 0.0820  -0.0473 -0.0398 63  THR B CG2 
5504 N N   . THR B 64  ? 0.6078 0.5304 0.4539 0.0547  -0.0468 -0.0469 64  THR B N   
5505 C CA  . THR B 64  ? 0.5920 0.5110 0.4472 0.0480  -0.0459 -0.0470 64  THR B CA  
5506 C C   . THR B 64  ? 0.5739 0.4942 0.4332 0.0489  -0.0433 -0.0425 64  THR B C   
5507 O O   . THR B 64  ? 0.5809 0.4942 0.4438 0.0459  -0.0403 -0.0413 64  THR B O   
5508 C CB  . THR B 64  ? 0.6047 0.5313 0.4674 0.0411  -0.0504 -0.0507 64  THR B CB  
5509 O OG1 . THR B 64  ? 0.6330 0.5595 0.4902 0.0407  -0.0531 -0.0551 64  THR B OG1 
5510 C CG2 . THR B 64  ? 0.6148 0.5333 0.4840 0.0348  -0.0488 -0.0512 64  THR B CG2 
5511 N N   . THR B 65  ? 0.5786 0.5083 0.4368 0.0537  -0.0442 -0.0401 65  THR B N   
5512 C CA  . THR B 65  ? 0.5890 0.5195 0.4500 0.0552  -0.0416 -0.0360 65  THR B CA  
5513 C C   . THR B 65  ? 0.5672 0.4832 0.4199 0.0579  -0.0357 -0.0334 65  THR B C   
5514 O O   . THR B 65  ? 0.5643 0.4758 0.4212 0.0545  -0.0330 -0.0319 65  THR B O   
5515 C CB  . THR B 65  ? 0.5806 0.5253 0.4416 0.0607  -0.0436 -0.0337 65  THR B CB  
5516 O OG1 . THR B 65  ? 0.5936 0.5535 0.4635 0.0557  -0.0490 -0.0365 65  THR B OG1 
5517 C CG2 . THR B 65  ? 0.5577 0.5023 0.4213 0.0622  -0.0407 -0.0296 65  THR B CG2 
5518 N N   . ASN B 66  ? 0.5504 0.4595 0.3912 0.0635  -0.0336 -0.0330 66  ASN B N   
5519 C CA  . ASN B 66  ? 0.5592 0.4534 0.3907 0.0644  -0.0276 -0.0314 66  ASN B CA  
5520 C C   . ASN B 66  ? 0.5577 0.4459 0.3941 0.0573  -0.0261 -0.0334 66  ASN B C   
5521 O O   . ASN B 66  ? 0.5531 0.4349 0.3888 0.0546  -0.0220 -0.0318 66  ASN B O   
5522 C CB  . ASN B 66  ? 0.5812 0.4684 0.3985 0.0709  -0.0256 -0.0311 66  ASN B CB  
5523 C CG  . ASN B 66  ? 0.6001 0.4905 0.4091 0.0800  -0.0253 -0.0280 66  ASN B CG  
5524 O OD1 . ASN B 66  ? 0.6330 0.5305 0.4464 0.0817  -0.0259 -0.0257 66  ASN B OD1 
5525 N ND2 . ASN B 66  ? 0.6012 0.4865 0.3975 0.0866  -0.0239 -0.0275 66  ASN B ND2 
5526 N N   . LEU B 67  ? 0.5604 0.4512 0.4008 0.0546  -0.0294 -0.0368 67  LEU B N   
5527 C CA  . LEU B 67  ? 0.5651 0.4509 0.4089 0.0497  -0.0278 -0.0384 67  LEU B CA  
5528 C C   . LEU B 67  ? 0.5506 0.4394 0.4047 0.0450  -0.0274 -0.0371 67  LEU B C   
5529 O O   . LEU B 67  ? 0.5509 0.4356 0.4055 0.0425  -0.0238 -0.0361 67  LEU B O   
5530 C CB  . LEU B 67  ? 0.5568 0.4438 0.4018 0.0485  -0.0313 -0.0424 67  LEU B CB  
5531 C CG  . LEU B 67  ? 0.5531 0.4358 0.4015 0.0448  -0.0302 -0.0442 67  LEU B CG  
5532 C CD1 . LEU B 67  ? 0.5671 0.4467 0.4102 0.0460  -0.0318 -0.0478 67  LEU B CD1 
5533 C CD2 . LEU B 67  ? 0.5396 0.4259 0.3987 0.0403  -0.0320 -0.0444 67  LEU B CD2 
5534 N N   . LYS B 68  ? 0.5600 0.4570 0.4219 0.0438  -0.0309 -0.0369 68  LYS B N   
5535 C CA  . LYS B 68  ? 0.6125 0.5124 0.4841 0.0396  -0.0306 -0.0355 68  LYS B CA  
5536 C C   . LYS B 68  ? 0.5822 0.4801 0.4525 0.0401  -0.0266 -0.0320 68  LYS B C   
5537 O O   . LYS B 68  ? 0.5532 0.4510 0.4291 0.0366  -0.0249 -0.0309 68  LYS B O   
5538 C CB  . LYS B 68  ? 0.6589 0.5682 0.5389 0.0371  -0.0351 -0.0363 68  LYS B CB  
5539 C CG  . LYS B 68  ? 0.7096 0.6172 0.5944 0.0323  -0.0371 -0.0393 68  LYS B CG  
5540 C CD  . LYS B 68  ? 0.7383 0.6537 0.6270 0.0293  -0.0417 -0.0417 68  LYS B CD  
5541 C CE  . LYS B 68  ? 0.7854 0.6945 0.6749 0.0247  -0.0427 -0.0453 68  LYS B CE  
5542 N NZ  . LYS B 68  ? 0.8343 0.7500 0.7271 0.0194  -0.0468 -0.0482 68  LYS B NZ  
5543 N N   . ARG B 69  ? 0.5624 0.4578 0.4241 0.0448  -0.0248 -0.0303 69  ARG B N   
5544 C CA  . ARG B 69  ? 0.5635 0.4540 0.4208 0.0453  -0.0203 -0.0274 69  ARG B CA  
5545 C C   . ARG B 69  ? 0.5545 0.4368 0.4072 0.0418  -0.0157 -0.0278 69  ARG B C   
5546 O O   . ARG B 69  ? 0.5362 0.4188 0.3928 0.0379  -0.0135 -0.0268 69  ARG B O   
5547 C CB  . ARG B 69  ? 0.6262 0.5133 0.4726 0.0521  -0.0186 -0.0253 69  ARG B CB  
5548 C CG  . ARG B 69  ? 0.6555 0.5536 0.5066 0.0560  -0.0222 -0.0238 69  ARG B CG  
5549 C CD  . ARG B 69  ? 0.7089 0.6029 0.5479 0.0642  -0.0193 -0.0208 69  ARG B CD  
5550 N NE  . ARG B 69  ? 0.7543 0.6367 0.5862 0.0636  -0.0134 -0.0186 69  ARG B NE  
5551 C CZ  . ARG B 69  ? 0.8060 0.6912 0.6428 0.0624  -0.0124 -0.0166 69  ARG B CZ  
5552 N NH1 . ARG B 69  ? 0.7324 0.6322 0.5819 0.0617  -0.0170 -0.0163 69  ARG B NH1 
5553 N NH2 . ARG B 69  ? 0.7435 0.6166 0.5719 0.0611  -0.0066 -0.0151 69  ARG B NH2 
5554 N N   . PHE B 70  ? 0.5321 0.4085 0.3767 0.0430  -0.0145 -0.0294 70  PHE B N   
5555 C CA  . PHE B 70  ? 0.5154 0.3863 0.3555 0.0393  -0.0101 -0.0301 70  PHE B CA  
5556 C C   . PHE B 70  ? 0.4963 0.3737 0.3472 0.0345  -0.0109 -0.0309 70  PHE B C   
5557 O O   . PHE B 70  ? 0.5266 0.4042 0.3776 0.0305  -0.0074 -0.0302 70  PHE B O   
5558 C CB  . PHE B 70  ? 0.5089 0.3745 0.3401 0.0415  -0.0095 -0.0320 70  PHE B CB  
5559 C CG  . PHE B 70  ? 0.4935 0.3553 0.3199 0.0374  -0.0050 -0.0328 70  PHE B CG  
5560 C CD1 . PHE B 70  ? 0.5123 0.3651 0.3270 0.0356  0.0007  -0.0317 70  PHE B CD1 
5561 C CD2 . PHE B 70  ? 0.4845 0.3515 0.3168 0.0354  -0.0061 -0.0348 70  PHE B CD2 
5562 C CE1 . PHE B 70  ? 0.5012 0.3525 0.3115 0.0306  0.0050  -0.0328 70  PHE B CE1 
5563 C CE2 . PHE B 70  ? 0.4551 0.3215 0.2832 0.0319  -0.0019 -0.0354 70  PHE B CE2 
5564 C CZ  . PHE B 70  ? 0.4801 0.3397 0.2977 0.0289  0.0034  -0.0345 70  PHE B CZ  
5565 N N   . TYR B 71  ? 0.4612 0.3439 0.3203 0.0350  -0.0153 -0.0323 71  TYR B N   
5566 C CA  . TYR B 71  ? 0.4671 0.3540 0.3344 0.0321  -0.0157 -0.0329 71  TYR B CA  
5567 C C   . TYR B 71  ? 0.4667 0.3588 0.3425 0.0295  -0.0156 -0.0308 71  TYR B C   
5568 O O   . TYR B 71  ? 0.4833 0.3788 0.3637 0.0275  -0.0143 -0.0304 71  TYR B O   
5569 C CB  . TYR B 71  ? 0.4544 0.3416 0.3246 0.0335  -0.0196 -0.0354 71  TYR B CB  
5570 C CG  . TYR B 71  ? 0.4814 0.3644 0.3442 0.0353  -0.0186 -0.0376 71  TYR B CG  
5571 C CD1 . TYR B 71  ? 0.4949 0.3786 0.3572 0.0346  -0.0159 -0.0379 71  TYR B CD1 
5572 C CD2 . TYR B 71  ? 0.4911 0.3709 0.3469 0.0383  -0.0203 -0.0391 71  TYR B CD2 
5573 C CE1 . TYR B 71  ? 0.5130 0.3936 0.3684 0.0365  -0.0148 -0.0398 71  TYR B CE1 
5574 C CE2 . TYR B 71  ? 0.4970 0.3728 0.3455 0.0402  -0.0192 -0.0410 71  TYR B CE2 
5575 C CZ  . TYR B 71  ? 0.5158 0.3918 0.3642 0.0391  -0.0164 -0.0414 71  TYR B CZ  
5576 O OH  . TYR B 71  ? 0.5372 0.4102 0.3786 0.0410  -0.0152 -0.0432 71  TYR B OH  
5577 N N   . LYS B 72  ? 0.4944 0.3879 0.3720 0.0301  -0.0168 -0.0292 72  LYS B N   
5578 C CA  . LYS B 72  ? 0.5136 0.4113 0.3976 0.0276  -0.0158 -0.0269 72  LYS B CA  
5579 C C   . LYS B 72  ? 0.5081 0.4044 0.3875 0.0248  -0.0109 -0.0261 72  LYS B C   
5580 O O   . LYS B 72  ? 0.4895 0.3910 0.3747 0.0220  -0.0098 -0.0250 72  LYS B O   
5581 C CB  . LYS B 72  ? 0.5377 0.4376 0.4233 0.0293  -0.0173 -0.0252 72  LYS B CB  
5582 C CG  . LYS B 72  ? 0.5885 0.4942 0.4819 0.0296  -0.0221 -0.0258 72  LYS B CG  
5583 C CD  . LYS B 72  ? 0.6464 0.5563 0.5499 0.0261  -0.0230 -0.0250 72  LYS B CD  
5584 C CE  . LYS B 72  ? 0.7043 0.6116 0.6095 0.0249  -0.0238 -0.0270 72  LYS B CE  
5585 N NZ  . LYS B 72  ? 0.7006 0.6098 0.6123 0.0228  -0.0226 -0.0254 72  LYS B NZ  
5586 N N   . VAL B 73  ? 0.4617 0.3512 0.3302 0.0252  -0.0078 -0.0267 73  VAL B N   
5587 C CA  . VAL B 73  ? 0.4833 0.3714 0.3463 0.0209  -0.0029 -0.0267 73  VAL B CA  
5588 C C   . VAL B 73  ? 0.4851 0.3801 0.3522 0.0185  -0.0023 -0.0279 73  VAL B C   
5589 O O   . VAL B 73  ? 0.4690 0.3708 0.3392 0.0146  0.0000  -0.0273 73  VAL B O   
5590 C CB  . VAL B 73  ? 0.4896 0.3670 0.3381 0.0212  0.0009  -0.0273 73  VAL B CB  
5591 C CG1 . VAL B 73  ? 0.4682 0.3450 0.3110 0.0147  0.0062  -0.0279 73  VAL B CG1 
5592 C CG2 . VAL B 73  ? 0.4810 0.3511 0.3234 0.0249  0.0012  -0.0255 73  VAL B CG2 
5593 N N   . VAL B 74  ? 0.4475 0.3415 0.3140 0.0213  -0.0042 -0.0295 74  VAL B N   
5594 C CA  . VAL B 74  ? 0.4542 0.3544 0.3239 0.0210  -0.0038 -0.0305 74  VAL B CA  
5595 C C   . VAL B 74  ? 0.4734 0.3814 0.3536 0.0211  -0.0054 -0.0290 74  VAL B C   
5596 O O   . VAL B 74  ? 0.5112 0.4278 0.3942 0.0196  -0.0033 -0.0285 74  VAL B O   
5597 C CB  . VAL B 74  ? 0.4570 0.3535 0.3243 0.0250  -0.0060 -0.0325 74  VAL B CB  
5598 C CG1 . VAL B 74  ? 0.4247 0.3277 0.2948 0.0259  -0.0052 -0.0331 74  VAL B CG1 
5599 C CG2 . VAL B 74  ? 0.4268 0.3153 0.2827 0.0256  -0.0042 -0.0336 74  VAL B CG2 
5600 N N   . GLU B 75  ? 0.4655 0.3717 0.3511 0.0229  -0.0088 -0.0283 75  GLU B N   
5601 C CA  . GLU B 75  ? 0.5035 0.4152 0.3981 0.0229  -0.0100 -0.0267 75  GLU B CA  
5602 C C   . GLU B 75  ? 0.4859 0.4045 0.3830 0.0195  -0.0073 -0.0247 75  GLU B C   
5603 O O   . GLU B 75  ? 0.4733 0.3993 0.3756 0.0196  -0.0066 -0.0233 75  GLU B O   
5604 C CB  . GLU B 75  ? 0.5682 0.4766 0.4672 0.0240  -0.0138 -0.0265 75  GLU B CB  
5605 C CG  . GLU B 75  ? 0.7005 0.6120 0.6076 0.0240  -0.0149 -0.0248 75  GLU B CG  
5606 C CD  . GLU B 75  ? 0.8323 0.7383 0.7407 0.0254  -0.0179 -0.0263 75  GLU B CD  
5607 O OE1 . GLU B 75  ? 0.8428 0.7448 0.7479 0.0256  -0.0202 -0.0285 75  GLU B OE1 
5608 O OE2 . GLU B 75  ? 0.8541 0.7595 0.7660 0.0261  -0.0177 -0.0254 75  GLU B OE2 
5609 N N   . LYS B 76  ? 0.4555 0.3712 0.3478 0.0169  -0.0055 -0.0244 76  LYS B N   
5610 C CA  . LYS B 76  ? 0.4501 0.3713 0.3431 0.0130  -0.0027 -0.0231 76  LYS B CA  
5611 C C   . LYS B 76  ? 0.4350 0.3640 0.3259 0.0100  0.0004  -0.0239 76  LYS B C   
5612 O O   . LYS B 76  ? 0.4155 0.3549 0.3114 0.0083  0.0014  -0.0227 76  LYS B O   
5613 C CB  . LYS B 76  ? 0.4693 0.3829 0.3547 0.0110  -0.0007 -0.0230 76  LYS B CB  
5614 C CG  . LYS B 76  ? 0.4813 0.3925 0.3707 0.0136  -0.0033 -0.0213 76  LYS B CG  
5615 C CD  . LYS B 76  ? 0.5289 0.4348 0.4112 0.0119  -0.0003 -0.0205 76  LYS B CD  
5616 C CE  . LYS B 76  ? 0.5144 0.4220 0.4026 0.0143  -0.0026 -0.0183 76  LYS B CE  
5617 N NZ  . LYS B 76  ? 0.5277 0.4289 0.4074 0.0134  0.0009  -0.0174 76  LYS B NZ  
5618 N N   . ILE B 77  ? 0.4655 0.3910 0.3492 0.0096  0.0019  -0.0258 77  ILE B N   
5619 C CA  . ILE B 77  ? 0.4341 0.3684 0.3151 0.0064  0.0051  -0.0269 77  ILE B CA  
5620 C C   . ILE B 77  ? 0.4361 0.3819 0.3255 0.0102  0.0037  -0.0258 77  ILE B C   
5621 O O   . ILE B 77  ? 0.4606 0.4198 0.3524 0.0080  0.0058  -0.0253 77  ILE B O   
5622 C CB  . ILE B 77  ? 0.4516 0.3787 0.3232 0.0063  0.0067  -0.0290 77  ILE B CB  
5623 C CG1 . ILE B 77  ? 0.4591 0.3738 0.3199 0.0027  0.0094  -0.0297 77  ILE B CG1 
5624 C CG2 . ILE B 77  ? 0.4239 0.3624 0.2941 0.0038  0.0096  -0.0301 77  ILE B CG2 
5625 C CD1 . ILE B 77  ? 0.4977 0.4022 0.3487 0.0042  0.0105  -0.0312 77  ILE B CD1 
5626 N N   . LEU B 78  ? 0.4188 0.3593 0.3117 0.0161  0.0004  -0.0255 78  LEU B N   
5627 C CA  . LEU B 78  ? 0.4437 0.3912 0.3422 0.0210  -0.0004 -0.0244 78  LEU B CA  
5628 C C   . LEU B 78  ? 0.4427 0.3980 0.3487 0.0216  -0.0006 -0.0216 78  LEU B C   
5629 O O   . LEU B 78  ? 0.4578 0.4198 0.3672 0.0261  -0.0003 -0.0200 78  LEU B O   
5630 C CB  . LEU B 78  ? 0.4284 0.3651 0.3265 0.0262  -0.0034 -0.0253 78  LEU B CB  
5631 C CG  . LEU B 78  ? 0.4270 0.3584 0.3182 0.0278  -0.0032 -0.0278 78  LEU B CG  
5632 C CD1 . LEU B 78  ? 0.4305 0.3503 0.3212 0.0314  -0.0066 -0.0290 78  LEU B CD1 
5633 C CD2 . LEU B 78  ? 0.4190 0.3605 0.3091 0.0304  -0.0006 -0.0277 78  LEU B CD2 
5634 N N   . THR B 79  ? 0.4435 0.3974 0.3512 0.0177  -0.0008 -0.0208 79  THR B N   
5635 C CA  . THR B 79  ? 0.4434 0.4035 0.3581 0.0181  -0.0012 -0.0181 79  THR B CA  
5636 C C   . THR B 79  ? 0.4463 0.4133 0.3600 0.0119  0.0010  -0.0179 79  THR B C   
5637 O O   . THR B 79  ? 0.4260 0.3957 0.3442 0.0112  0.0006  -0.0159 79  THR B O   
5638 C CB  . THR B 79  ? 0.4461 0.3958 0.3644 0.0198  -0.0044 -0.0171 79  THR B CB  
5639 O OG1 . THR B 79  ? 0.4515 0.3936 0.3661 0.0167  -0.0050 -0.0184 79  THR B OG1 
5640 C CG2 . THR B 79  ? 0.4543 0.3957 0.3725 0.0246  -0.0065 -0.0178 79  THR B CG2 
5641 N N   . GLN B 80  ? 0.4426 0.4116 0.3495 0.0070  0.0037  -0.0201 80  GLN B N   
5642 C CA  . GLN B 80  ? 0.4551 0.4262 0.3578 0.0000  0.0065  -0.0208 80  GLN B CA  
5643 C C   . GLN B 80  ? 0.4521 0.4398 0.3600 -0.0023 0.0078  -0.0194 80  GLN B C   
5644 O O   . GLN B 80  ? 0.4635 0.4637 0.3766 0.0016  0.0074  -0.0179 80  GLN B O   
5645 C CB  . GLN B 80  ? 0.4453 0.4147 0.3384 -0.0054 0.0098  -0.0236 80  GLN B CB  
5646 C CG  . GLN B 80  ? 0.4600 0.4443 0.3542 -0.0053 0.0112  -0.0243 80  GLN B CG  
5647 C CD  . GLN B 80  ? 0.4856 0.4677 0.3701 -0.0109 0.0146  -0.0271 80  GLN B CD  
5648 O OE1 . GLN B 80  ? 0.4783 0.4664 0.3575 -0.0193 0.0182  -0.0287 80  GLN B OE1 
5649 N NE2 . GLN B 80  ? 0.4843 0.4568 0.3654 -0.0068 0.0136  -0.0279 80  GLN B NE2 
5650 N N   . SER B 81  ? 0.4351 0.4226 0.3405 -0.0080 0.0095  -0.0196 81  SER B N   
5651 C CA  . SER B 81  ? 0.4469 0.4516 0.3545 -0.0125 0.0114  -0.0193 81  SER B CA  
5652 C C   . SER B 81  ? 0.4560 0.4626 0.3538 -0.0219 0.0156  -0.0228 81  SER B C   
5653 O O   . SER B 81  ? 0.4600 0.4513 0.3488 -0.0245 0.0171  -0.0248 81  SER B O   
5654 C CB  . SER B 81  ? 0.4251 0.4286 0.3357 -0.0134 0.0109  -0.0176 81  SER B CB  
5655 O OG  . SER B 81  ? 0.4104 0.4059 0.3274 -0.0065 0.0075  -0.0150 81  SER B OG  
5656 N N   . SER B 82  ? 0.4488 0.4740 0.3473 -0.0274 0.0177  -0.0235 82  SER B N   
5657 C CA  . SER B 82  ? 0.4546 0.4821 0.3430 -0.0386 0.0221  -0.0272 82  SER B CA  
5658 C C   . SER B 82  ? 0.4442 0.4519 0.3232 -0.0437 0.0242  -0.0285 82  SER B C   
5659 O O   . SER B 82  ? 0.4867 0.4900 0.3691 -0.0411 0.0227  -0.0267 82  SER B O   
5660 C CB  . SER B 82  ? 0.4506 0.5034 0.3423 -0.0441 0.0236  -0.0277 82  SER B CB  
5661 O OG  . SER B 82  ? 0.4526 0.5245 0.3523 -0.0376 0.0220  -0.0260 82  SER B OG  
5662 N N   . PHE B 83  ? 0.4606 0.4556 0.3269 -0.0504 0.0280  -0.0315 83  PHE B N   
5663 C CA  . PHE B 83  ? 0.4904 0.4642 0.3438 -0.0555 0.0313  -0.0330 83  PHE B CA  
5664 C C   . PHE B 83  ? 0.4818 0.4344 0.3337 -0.0467 0.0292  -0.0309 83  PHE B C   
5665 O O   . PHE B 83  ? 0.5138 0.4472 0.3533 -0.0489 0.0323  -0.0318 83  PHE B O   
5666 C CB  . PHE B 83  ? 0.5276 0.5071 0.3803 -0.0614 0.0328  -0.0335 83  PHE B CB  
5667 C CG  . PHE B 83  ? 0.5580 0.5586 0.4099 -0.0718 0.0355  -0.0362 83  PHE B CG  
5668 C CD1 . PHE B 83  ? 0.5901 0.5867 0.4281 -0.0839 0.0410  -0.0404 83  PHE B CD1 
5669 C CD2 . PHE B 83  ? 0.5602 0.5854 0.4245 -0.0700 0.0329  -0.0345 83  PHE B CD2 
5670 C CE1 . PHE B 83  ? 0.6135 0.6324 0.4509 -0.0948 0.0435  -0.0433 83  PHE B CE1 
5671 C CE2 . PHE B 83  ? 0.5783 0.6263 0.4422 -0.0794 0.0351  -0.0370 83  PHE B CE2 
5672 C CZ  . PHE B 83  ? 0.5963 0.6423 0.4471 -0.0924 0.0403  -0.0416 83  PHE B CZ  
5673 N N   . GLU B 84  ? 0.4520 0.4080 0.3155 -0.0368 0.0241  -0.0282 84  GLU B N   
5674 C CA  . GLU B 84  ? 0.4557 0.3951 0.3187 -0.0290 0.0217  -0.0264 84  GLU B CA  
5675 C C   . GLU B 84  ? 0.4645 0.3864 0.3142 -0.0296 0.0244  -0.0280 84  GLU B C   
5676 O O   . GLU B 84  ? 0.4667 0.3911 0.3131 -0.0319 0.0257  -0.0297 84  GLU B O   
5677 C CB  . GLU B 84  ? 0.4726 0.4188 0.3492 -0.0199 0.0161  -0.0239 84  GLU B CB  
5678 C CG  . GLU B 84  ? 0.4699 0.4030 0.3476 -0.0128 0.0131  -0.0222 84  GLU B CG  
5679 C CD  . GLU B 84  ? 0.4933 0.4330 0.3839 -0.0059 0.0081  -0.0200 84  GLU B CD  
5680 O OE1 . GLU B 84  ? 0.4813 0.4321 0.3783 -0.0048 0.0071  -0.0197 84  GLU B OE1 
5681 O OE2 . GLU B 84  ? 0.5301 0.4634 0.4236 -0.0015 0.0056  -0.0184 84  GLU B OE2 
5682 N N   . CYS B 85  ? 0.4686 0.3734 0.3101 -0.0270 0.0255  -0.0273 85  CYS B N   
5683 C CA  . CYS B 85  ? 0.4755 0.3625 0.3045 -0.0246 0.0276  -0.0279 85  CYS B CA  
5684 C C   . CYS B 85  ? 0.4704 0.3513 0.3040 -0.0145 0.0234  -0.0253 85  CYS B C   
5685 O O   . CYS B 85  ? 0.4732 0.3619 0.3180 -0.0109 0.0198  -0.0234 85  CYS B O   
5686 C CB  . CYS B 85  ? 0.4768 0.3469 0.2875 -0.0307 0.0342  -0.0294 85  CYS B CB  
5687 S SG  . CYS B 85  ? 0.4863 0.3640 0.2900 -0.0454 0.0398  -0.0331 85  CYS B SG  
5688 N N   . ILE B 86  ? 0.4871 0.3544 0.3112 -0.0101 0.0243  -0.0253 86  ILE B N   
5689 C CA  . ILE B 86  ? 0.4889 0.3484 0.3124 -0.0012 0.0218  -0.0230 86  ILE B CA  
5690 C C   . ILE B 86  ? 0.4971 0.3364 0.3008 -0.0007 0.0276  -0.0232 86  ILE B C   
5691 O O   . ILE B 86  ? 0.5191 0.3508 0.3111 -0.0078 0.0328  -0.0253 86  ILE B O   
5692 C CB  . ILE B 86  ? 0.4751 0.3388 0.3057 0.0051  0.0169  -0.0228 86  ILE B CB  
5693 C CG1 . ILE B 86  ? 0.5013 0.3609 0.3241 0.0023  0.0192  -0.0249 86  ILE B CG1 
5694 C CG2 . ILE B 86  ? 0.4973 0.3774 0.3455 0.0056  0.0116  -0.0223 86  ILE B CG2 
5695 C CD1 . ILE B 86  ? 0.5114 0.3664 0.3323 0.0094  0.0166  -0.0248 86  ILE B CD1 
5696 N N   . HIS B 87  ? 0.5050 0.3357 0.3039 0.0075  0.0270  -0.0209 87  HIS B N   
5697 C CA  . HIS B 87  ? 0.5569 0.3666 0.3352 0.0108  0.0325  -0.0204 87  HIS B CA  
5698 C C   . HIS B 87  ? 0.5655 0.3692 0.3370 0.0132  0.0328  -0.0211 87  HIS B C   
5699 O O   . HIS B 87  ? 0.5780 0.3923 0.3607 0.0182  0.0272  -0.0208 87  HIS B O   
5700 C CB  . HIS B 87  ? 0.5664 0.3707 0.3414 0.0207  0.0319  -0.0172 87  HIS B CB  
5701 C CG  . HIS B 87  ? 0.5744 0.3772 0.3483 0.0186  0.0342  -0.0164 87  HIS B CG  
5702 N ND1 . HIS B 87  ? 0.5686 0.3875 0.3593 0.0194  0.0294  -0.0152 87  HIS B ND1 
5703 C CD2 . HIS B 87  ? 0.5758 0.3611 0.3321 0.0153  0.0414  -0.0167 87  HIS B CD2 
5704 C CE1 . HIS B 87  ? 0.5825 0.3958 0.3674 0.0172  0.0330  -0.0147 87  HIS B CE1 
5705 N NE2 . HIS B 87  ? 0.5737 0.3661 0.3372 0.0147  0.0404  -0.0158 87  HIS B NE2 
5706 N N   . LEU B 88  ? 0.5771 0.3627 0.3292 0.0097  0.0398  -0.0222 88  LEU B N   
5707 C CA  . LEU B 88  ? 0.5827 0.3593 0.3248 0.0124  0.0414  -0.0225 88  LEU B CA  
5708 C C   . LEU B 88  ? 0.5987 0.3731 0.3398 0.0257  0.0380  -0.0197 88  LEU B C   
5709 O O   . LEU B 88  ? 0.6139 0.3916 0.3570 0.0296  0.0352  -0.0199 88  LEU B O   
5710 C CB  . LEU B 88  ? 0.5844 0.3387 0.3031 0.0061  0.0506  -0.0238 88  LEU B CB  
5711 C CG  . LEU B 88  ? 0.5975 0.3552 0.3146 -0.0076 0.0541  -0.0274 88  LEU B CG  
5712 C CD1 . LEU B 88  ? 0.6078 0.3424 0.3009 -0.0156 0.0639  -0.0288 88  LEU B CD1 
5713 C CD2 . LEU B 88  ? 0.5746 0.3401 0.2965 -0.0076 0.0518  -0.0286 88  LEU B CD2 
5714 N N   . SER B 89  ? 0.5863 0.3573 0.3251 0.0325  0.0380  -0.0171 89  SER B N   
5715 C CA  . SER B 89  ? 0.6145 0.3860 0.3518 0.0455  0.0351  -0.0141 89  SER B CA  
5716 C C   . SER B 89  ? 0.6108 0.4047 0.3691 0.0493  0.0260  -0.0142 89  SER B C   
5717 O O   . SER B 89  ? 0.6013 0.3985 0.3589 0.0588  0.0230  -0.0125 89  SER B O   
5718 C CB  . SER B 89  ? 0.6249 0.3891 0.3546 0.0520  0.0378  -0.0112 89  SER B CB  
5719 O OG  . SER B 89  ? 0.6214 0.4020 0.3687 0.0493  0.0333  -0.0111 89  SER B OG  
5720 N N   . VAL B 90  ? 0.5899 0.3989 0.3657 0.0419  0.0219  -0.0161 90  VAL B N   
5721 C CA  . VAL B 90  ? 0.6005 0.4277 0.3943 0.0440  0.0142  -0.0165 90  VAL B CA  
5722 C C   . VAL B 90  ? 0.6104 0.4377 0.4027 0.0450  0.0125  -0.0183 90  VAL B C   
5723 O O   . VAL B 90  ? 0.6572 0.4966 0.4608 0.0475  0.0065  -0.0190 90  VAL B O   
5724 C CB  . VAL B 90  ? 0.6070 0.4481 0.4181 0.0365  0.0110  -0.0178 90  VAL B CB  
5725 C CG1 . VAL B 90  ? 0.5731 0.4166 0.3870 0.0298  0.0113  -0.0205 90  VAL B CG1 
5726 C CG2 . VAL B 90  ? 0.5901 0.4467 0.4171 0.0400  0.0041  -0.0171 90  VAL B CG2 
5727 N N   . LEU B 91  ? 0.6165 0.4298 0.3942 0.0424  0.0180  -0.0192 91  LEU B N   
5728 C CA  . LEU B 91  ? 0.5969 0.4096 0.3721 0.0428  0.0171  -0.0209 91  LEU B CA  
5729 C C   . LEU B 91  ? 0.6043 0.4085 0.3669 0.0526  0.0178  -0.0191 91  LEU B C   
5730 O O   . LEU B 91  ? 0.6170 0.4187 0.3747 0.0542  0.0176  -0.0202 91  LEU B O   
5731 C CB  . LEU B 91  ? 0.5831 0.3879 0.3504 0.0340  0.0226  -0.0229 91  LEU B CB  
5732 C CG  . LEU B 91  ? 0.5574 0.3747 0.3380 0.0247  0.0215  -0.0249 91  LEU B CG  
5733 C CD1 . LEU B 91  ? 0.5454 0.3561 0.3160 0.0161  0.0276  -0.0268 91  LEU B CD1 
5734 C CD2 . LEU B 91  ? 0.5334 0.3668 0.3307 0.0261  0.0147  -0.0261 91  LEU B CD2 
5735 N N   . HIS B 92  ? 0.6275 0.4280 0.3844 0.0600  0.0186  -0.0162 92  HIS B N   
5736 C CA  . HIS B 92  ? 0.6775 0.4724 0.4224 0.0713  0.0190  -0.0139 92  HIS B CA  
5737 C C   . HIS B 92  ? 0.6890 0.4944 0.4388 0.0804  0.0152  -0.0112 92  HIS B C   
5738 O O   . HIS B 92  ? 0.7300 0.5392 0.4756 0.0898  0.0131  -0.0097 92  HIS B O   
5739 C CB  . HIS B 92  ? 0.6827 0.4532 0.4031 0.0733  0.0278  -0.0124 92  HIS B CB  
5740 C CG  . HIS B 92  ? 0.6895 0.4462 0.3988 0.0729  0.0339  -0.0105 92  HIS B CG  
5741 N ND1 . HIS B 92  ? 0.7034 0.4584 0.4071 0.0831  0.0345  -0.0070 92  HIS B ND1 
5742 C CD2 . HIS B 92  ? 0.7017 0.4453 0.4033 0.0629  0.0402  -0.0119 92  HIS B CD2 
5743 C CE1 . HIS B 92  ? 0.6973 0.4371 0.3898 0.0803  0.0409  -0.0062 92  HIS B CE1 
5744 N NE2 . HIS B 92  ? 0.6924 0.4252 0.3836 0.0674  0.0444  -0.0093 92  HIS B NE2 
5745 N N   . LYS B 93  ? 0.7129 0.5250 0.4721 0.0777  0.0143  -0.0105 93  LYS B N   
5746 C CA  . LYS B 93  ? 0.7194 0.5421 0.4828 0.0862  0.0114  -0.0077 93  LYS B CA  
5747 C C   . LYS B 93  ? 0.7047 0.5504 0.4865 0.0866  0.0029  -0.0090 93  LYS B C   
5748 O O   . LYS B 93  ? 0.6725 0.5266 0.4682 0.0782  -0.0008 -0.0119 93  LYS B O   
5749 C CB  . LYS B 93  ? 0.7533 0.5741 0.5188 0.0834  0.0139  -0.0063 93  LYS B CB  
5750 C CG  . LYS B 93  ? 0.7794 0.5773 0.5229 0.0870  0.0226  -0.0041 93  LYS B CG  
5751 C CD  . LYS B 93  ? 0.7862 0.5842 0.5317 0.0864  0.0244  -0.0025 93  LYS B CD  
5752 C CE  . LYS B 93  ? 0.7871 0.5600 0.5081 0.0909  0.0335  -0.0003 93  LYS B CE  
5753 N NZ  . LYS B 93  ? 0.7619 0.5331 0.4842 0.0881  0.0358  0.0003  93  LYS B NZ  
5754 N N   . CYS B 94  ? 0.7392 0.5949 0.5198 0.0966  0.0002  -0.0067 94  CYS B N   
5755 C CA  . CYS B 94  ? 0.7398 0.6188 0.5369 0.0967  -0.0076 -0.0080 94  CYS B CA  
5756 C C   . CYS B 94  ? 0.7478 0.6315 0.5495 0.0931  -0.0117 -0.0116 94  CYS B C   
5757 O O   . CYS B 94  ? 0.7613 0.6619 0.5768 0.0900  -0.0180 -0.0137 94  CYS B O   
5758 C CB  . CYS B 94  ? 0.7577 0.6485 0.5721 0.0892  -0.0106 -0.0086 94  CYS B CB  
5759 S SG  . CYS B 94  ? 0.8019 0.6885 0.6122 0.0929  -0.0061 -0.0046 94  CYS B SG  
5760 N N   . TYR B 95  ? 0.7326 0.6006 0.5220 0.0929  -0.0079 -0.0124 95  TYR B N   
5761 C CA  . TYR B 95  ? 0.7315 0.6023 0.5217 0.0918  -0.0110 -0.0154 95  TYR B CA  
5762 C C   . TYR B 95  ? 0.7540 0.6331 0.5374 0.1026  -0.0134 -0.0139 95  TYR B C   
5763 O O   . TYR B 95  ? 0.7263 0.5989 0.4961 0.1124  -0.0095 -0.0102 95  TYR B O   
5764 C CB  . TYR B 95  ? 0.7312 0.5833 0.5098 0.0884  -0.0056 -0.0164 95  TYR B CB  
5765 C CG  . TYR B 95  ? 0.7075 0.5586 0.4961 0.0771  -0.0057 -0.0193 95  TYR B CG  
5766 C CD1 . TYR B 95  ? 0.6981 0.5565 0.4957 0.0726  -0.0099 -0.0228 95  TYR B CD1 
5767 C CD2 . TYR B 95  ? 0.6932 0.5364 0.4813 0.0713  -0.0012 -0.0186 95  TYR B CD2 
5768 C CE1 . TYR B 95  ? 0.6592 0.5174 0.4651 0.0638  -0.0097 -0.0250 95  TYR B CE1 
5769 C CE2 . TYR B 95  ? 0.6581 0.5029 0.4553 0.0618  -0.0013 -0.0210 95  TYR B CE2 
5770 C CZ  . TYR B 95  ? 0.6542 0.5067 0.4603 0.0587  -0.0055 -0.0240 95  TYR B CZ  
5771 O OH  . TYR B 95  ? 0.6378 0.4925 0.4520 0.0510  -0.0052 -0.0259 95  TYR B OH  
5772 N N   . ASP B 96  ? 0.7499 0.6428 0.5415 0.1011  -0.0195 -0.0170 96  ASP B N   
5773 C CA  . ASP B 96  ? 0.7524 0.6561 0.5384 0.1105  -0.0224 -0.0163 96  ASP B CA  
5774 C C   . ASP B 96  ? 0.7688 0.6571 0.5387 0.1150  -0.0186 -0.0161 96  ASP B C   
5775 O O   . ASP B 96  ? 0.7702 0.6570 0.5422 0.1099  -0.0205 -0.0197 96  ASP B O   
5776 C CB  . ASP B 96  ? 0.7814 0.7063 0.5823 0.1056  -0.0304 -0.0202 96  ASP B CB  
5777 C CG  . ASP B 96  ? 0.8154 0.7548 0.6112 0.1143  -0.0341 -0.0201 96  ASP B CG  
5778 O OD1 . ASP B 96  ? 0.8371 0.7723 0.6185 0.1260  -0.0308 -0.0162 96  ASP B OD1 
5779 O OD2 . ASP B 96  ? 0.8210 0.7758 0.6264 0.1094  -0.0402 -0.0241 96  ASP B OD2 
5780 N N   . TYR B 97  ? 0.7973 0.6729 0.5499 0.1248  -0.0128 -0.0118 97  TYR B N   
5781 C CA  . TYR B 97  ? 0.8307 0.6876 0.5653 0.1288  -0.0075 -0.0110 97  TYR B CA  
5782 C C   . TYR B 97  ? 0.8570 0.7231 0.5863 0.1366  -0.0110 -0.0115 97  TYR B C   
5783 O O   . TYR B 97  ? 0.8933 0.7478 0.6128 0.1366  -0.0086 -0.0125 97  TYR B O   
5784 C CB  . TYR B 97  ? 0.8362 0.6722 0.5515 0.1359  0.0010  -0.0063 97  TYR B CB  
5785 C CG  . TYR B 97  ? 0.8487 0.6695 0.5648 0.1259  0.0059  -0.0069 97  TYR B CG  
5786 C CD1 . TYR B 97  ? 0.8474 0.6515 0.5571 0.1178  0.0105  -0.0089 97  TYR B CD1 
5787 C CD2 . TYR B 97  ? 0.8362 0.6613 0.5598 0.1242  0.0060  -0.0056 97  TYR B CD2 
5788 C CE1 . TYR B 97  ? 0.8431 0.6361 0.5537 0.1080  0.0148  -0.0098 97  TYR B CE1 
5789 C CE2 . TYR B 97  ? 0.8537 0.6666 0.5781 0.1147  0.0102  -0.0064 97  TYR B CE2 
5790 C CZ  . TYR B 97  ? 0.8707 0.6681 0.5887 0.1065  0.0145  -0.0086 97  TYR B CZ  
5791 O OH  . TYR B 97  ? 0.8755 0.6633 0.5943 0.0966  0.0186  -0.0096 97  TYR B OH  
5792 N N   . ASP B 98  ? 0.8688 0.7570 0.6043 0.1431  -0.0165 -0.0108 98  ASP B N   
5793 C CA  . ASP B 98  ? 0.9132 0.8144 0.6451 0.1501  -0.0207 -0.0117 98  ASP B CA  
5794 C C   . ASP B 98  ? 0.8868 0.7920 0.6282 0.1399  -0.0253 -0.0175 98  ASP B C   
5795 O O   . ASP B 98  ? 0.8924 0.7969 0.6259 0.1437  -0.0260 -0.0186 98  ASP B O   
5796 C CB  . ASP B 98  ? 0.9574 0.8862 0.6969 0.1568  -0.0265 -0.0105 98  ASP B CB  
5797 C CG  . ASP B 98  ? 1.0113 0.9377 0.7370 0.1715  -0.0218 -0.0041 98  ASP B CG  
5798 O OD1 . ASP B 98  ? 1.0477 0.9568 0.7534 0.1816  -0.0159 -0.0006 98  ASP B OD1 
5799 O OD2 . ASP B 98  ? 1.0239 0.9656 0.7580 0.1734  -0.0238 -0.0024 98  ASP B OD2 
5800 N N   . ALA B 99  ? 0.8534 0.7618 0.6108 0.1275  -0.0279 -0.0210 99  ALA B N   
5801 C CA  . ALA B 99  ? 0.8242 0.7381 0.5915 0.1183  -0.0327 -0.0266 99  ALA B CA  
5802 C C   . ALA B 99  ? 0.8043 0.6988 0.5673 0.1121  -0.0286 -0.0284 99  ALA B C   
5803 O O   . ALA B 99  ? 0.8192 0.7161 0.5889 0.1052  -0.0318 -0.0329 99  ALA B O   
5804 C CB  . ALA B 99  ? 0.7827 0.7114 0.5685 0.1090  -0.0380 -0.0295 99  ALA B CB  
5805 N N   . ILE B 100 ? 0.7591 0.6346 0.5101 0.1144  -0.0213 -0.0251 100 ILE B N   
5806 C CA  . ILE B 100 ? 0.7583 0.6172 0.5046 0.1083  -0.0168 -0.0266 100 ILE B CA  
5807 C C   . ILE B 100 ? 0.7843 0.6338 0.5142 0.1150  -0.0139 -0.0258 100 ILE B C   
5808 O O   . ILE B 100 ? 0.8080 0.6449 0.5218 0.1225  -0.0083 -0.0218 100 ILE B O   
5809 C CB  . ILE B 100 ? 0.7447 0.5885 0.4875 0.1041  -0.0102 -0.0242 100 ILE B CB  
5810 C CG1 . ILE B 100 ? 0.7324 0.5860 0.4918 0.0974  -0.0131 -0.0249 100 ILE B CG1 
5811 C CG2 . ILE B 100 ? 0.7433 0.5731 0.4810 0.0974  -0.0056 -0.0258 100 ILE B CG2 
5812 C CD1 . ILE B 100 ? 0.7011 0.5434 0.4568 0.0953  -0.0074 -0.0221 100 ILE B CD1 
5813 N N   . PRO B 101 ? 0.7728 0.6273 0.5055 0.1126  -0.0176 -0.0297 101 PRO B N   
5814 C CA  . PRO B 101 ? 0.7786 0.6282 0.4972 0.1195  -0.0162 -0.0294 101 PRO B CA  
5815 C C   . PRO B 101 ? 0.7885 0.6159 0.4898 0.1214  -0.0075 -0.0263 101 PRO B C   
5816 O O   . PRO B 101 ? 0.8366 0.6568 0.5218 0.1312  -0.0042 -0.0229 101 PRO B O   
5817 C CB  . PRO B 101 ? 0.7737 0.6295 0.5008 0.1130  -0.0207 -0.0348 101 PRO B CB  
5818 C CG  . PRO B 101 ? 0.7594 0.6294 0.5045 0.1061  -0.0265 -0.0377 101 PRO B CG  
5819 C CD  . PRO B 101 ? 0.7548 0.6198 0.5037 0.1036  -0.0231 -0.0346 101 PRO B CD  
5820 N N   . TRP B 102 ? 0.7591 0.5760 0.4628 0.1121  -0.0035 -0.0274 102 TRP B N   
5821 C CA  . TRP B 102 ? 0.7719 0.5684 0.4592 0.1113  0.0049  -0.0254 102 TRP B CA  
5822 C C   . TRP B 102 ? 0.8139 0.5959 0.4875 0.1158  0.0115  -0.0207 102 TRP B C   
5823 O O   . TRP B 102 ? 0.7957 0.5584 0.4535 0.1145  0.0194  -0.0189 102 TRP B O   
5824 C CB  . TRP B 102 ? 0.7656 0.5587 0.4601 0.0995  0.0070  -0.0282 102 TRP B CB  
5825 C CG  . TRP B 102 ? 0.7402 0.5370 0.4474 0.0921  0.0067  -0.0285 102 TRP B CG  
5826 C CD1 . TRP B 102 ? 0.7177 0.5301 0.4438 0.0879  0.0003  -0.0309 102 TRP B CD1 
5827 C CD2 . TRP B 102 ? 0.7602 0.5444 0.4613 0.0874  0.0134  -0.0263 102 TRP B CD2 
5828 N NE1 . TRP B 102 ? 0.6980 0.5090 0.4304 0.0820  0.0024  -0.0301 102 TRP B NE1 
5829 C CE2 . TRP B 102 ? 0.7404 0.5355 0.4587 0.0811  0.0100  -0.0275 102 TRP B CE2 
5830 C CE3 . TRP B 102 ? 0.7592 0.5239 0.4418 0.0873  0.0220  -0.0237 102 TRP B CE3 
5831 C CZ2 . TRP B 102 ? 0.7094 0.4976 0.4270 0.0754  0.0146  -0.0262 102 TRP B CZ2 
5832 C CZ3 . TRP B 102 ? 0.7704 0.5272 0.4518 0.0806  0.0268  -0.0228 102 TRP B CZ3 
5833 C CH2 . TRP B 102 ? 0.7436 0.5127 0.4425 0.0750  0.0229  -0.0241 102 TRP B CH2 
5834 N N   . LEU B 103 ? 0.8165 0.6071 0.4950 0.1209  0.0086  -0.0188 103 LEU B N   
5835 C CA  . LEU B 103 ? 0.8824 0.6595 0.5476 0.1265  0.0147  -0.0142 103 LEU B CA  
5836 C C   . LEU B 103 ? 0.9496 0.7294 0.6029 0.1418  0.0141  -0.0104 103 LEU B C   
5837 O O   . LEU B 103 ? 0.9502 0.7174 0.5890 0.1494  0.0197  -0.0059 103 LEU B O   
5838 C CB  . LEU B 103 ? 0.8630 0.6467 0.5417 0.1212  0.0131  -0.0143 103 LEU B CB  
5839 C CG  . LEU B 103 ? 0.8607 0.6334 0.5420 0.1087  0.0178  -0.0157 103 LEU B CG  
5840 C CD1 . LEU B 103 ? 0.8118 0.5940 0.5076 0.1044  0.0151  -0.0159 103 LEU B CD1 
5841 C CD2 . LEU B 103 ? 0.8561 0.6027 0.5145 0.1090  0.0280  -0.0130 103 LEU B CD2 
5842 N N   . GLN B 104 ? 0.9974 0.7934 0.6556 0.1465  0.0077  -0.0121 104 GLN B N   
5843 C CA  . GLN B 104 ? 1.0721 0.8778 0.7223 0.1611  0.0055  -0.0088 104 GLN B CA  
5844 C C   . GLN B 104 ? 1.1231 0.9083 0.7468 0.1728  0.0135  -0.0039 104 GLN B C   
5845 O O   . GLN B 104 ? 1.1139 0.9003 0.7269 0.1860  0.0149  0.0006  104 GLN B O   
5846 C CB  . GLN B 104 ? 1.0790 0.9092 0.7416 0.1617  -0.0036 -0.0126 104 GLN B CB  
5847 C CG  . GLN B 104 ? 1.0845 0.9366 0.7706 0.1538  -0.0114 -0.0163 104 GLN B CG  
5848 C CD  . GLN B 104 ? 1.1170 0.9723 0.8066 0.1562  -0.0104 -0.0130 104 GLN B CD  
5849 O OE1 . GLN B 104 ? 1.1543 1.0185 0.8379 0.1679  -0.0109 -0.0093 104 GLN B OE1 
5850 N NE2 . GLN B 104 ? 1.0830 0.9320 0.7822 0.1458  -0.0089 -0.0142 104 GLN B NE2 
5851 N N   . ASN B 105 ? 1.1694 0.9358 0.7819 0.1682  0.0190  -0.0047 105 ASN B N   
5852 C CA  . ASN B 105 ? 1.2288 0.9713 0.8142 0.1777  0.0279  0.0000  105 ASN B CA  
5853 C C   . ASN B 105 ? 1.2490 0.9642 0.8195 0.1746  0.0379  0.0029  105 ASN B C   
5854 O O   . ASN B 105 ? 1.3067 0.9964 0.8544 0.1771  0.0470  0.0056  105 ASN B O   
5855 C CB  . ASN B 105 ? 1.2750 1.0106 0.8529 0.1754  0.0294  -0.0018 105 ASN B CB  
5856 C CG  . ASN B 105 ? 1.3384 1.0699 0.9269 0.1586  0.0301  -0.0066 105 ASN B CG  
5857 O OD1 . ASN B 105 ? 1.3523 1.0823 0.9508 0.1486  0.0309  -0.0080 105 ASN B OD1 
5858 N ND2 . ASN B 105 ? 1.2864 1.0172 0.8726 0.1561  0.0299  -0.0089 105 ASN B ND2 
5859 N N   . VAL B 106 ? 1.1808 0.9012 0.7638 0.1686  0.0365  0.0022  106 VAL B N   
5860 C CA  . VAL B 106 ? 1.1412 0.8381 0.7115 0.1653  0.0452  0.0045  106 VAL B CA  
5861 C C   . VAL B 106 ? 1.1383 0.8400 0.7065 0.1767  0.0448  0.0085  106 VAL B C   
5862 O O   . VAL B 106 ? 1.0665 0.7944 0.6544 0.1783  0.0363  0.0074  106 VAL B O   
5863 C CB  . VAL B 106 ? 1.1025 0.8001 0.6884 0.1473  0.0449  0.0000  106 VAL B CB  
5864 C CG1 . VAL B 106 ? 1.0964 0.7782 0.6751 0.1442  0.0512  0.0018  106 VAL B CG1 
5865 C CG2 . VAL B 106 ? 1.0735 0.7595 0.6542 0.1369  0.0489  -0.0027 106 VAL B CG2 
5866 N N   . GLU B 107 ? 1.2245 0.9003 0.7679 0.1847  0.0544  0.0133  107 GLU B N   
5867 C CA  . GLU B 107 ? 1.2798 0.9576 0.8168 0.1984  0.0553  0.0181  107 GLU B CA  
5868 C C   . GLU B 107 ? 1.2446 0.9337 0.8000 0.1902  0.0520  0.0162  107 GLU B C   
5869 O O   . GLU B 107 ? 1.2072 0.8816 0.7630 0.1771  0.0563  0.0139  107 GLU B O   
5870 C CB  . GLU B 107 ? 1.3838 1.0271 0.8867 0.2091  0.0675  0.0237  107 GLU B CB  
5871 C CG  . GLU B 107 ? 1.4706 1.1067 0.9542 0.2228  0.0702  0.0272  107 GLU B CG  
5872 C CD  . GLU B 107 ? 1.5461 1.1480 0.9944 0.2363  0.0825  0.0337  107 GLU B CD  
5873 O OE1 . GLU B 107 ? 1.6210 1.2085 1.0603 0.2384  0.0879  0.0360  107 GLU B OE1 
5874 O OE2 . GLU B 107 ? 1.5444 1.1327 0.9727 0.2453  0.0870  0.0366  107 GLU B OE2 
5875 N N   . PRO B 108 ? 1.2320 0.9488 0.8032 0.1977  0.0441  0.0170  108 PRO B N   
5876 C CA  . PRO B 108 ? 1.2330 0.9674 0.8258 0.1906  0.0388  0.0151  108 PRO B CA  
5877 C C   . PRO B 108 ? 1.2737 0.9864 0.8607 0.1814  0.0458  0.0149  108 PRO B C   
5878 O O   . PRO B 108 ? 1.2480 0.9705 0.8544 0.1681  0.0421  0.0111  108 PRO B O   
5879 C CB  . PRO B 108 ? 1.2242 0.9766 0.8165 0.2071  0.0358  0.0195  108 PRO B CB  
5880 C CG  . PRO B 108 ? 1.2115 0.9728 0.7966 0.2184  0.0333  0.0209  108 PRO B CG  
5881 C CD  . PRO B 108 ? 1.2158 0.9503 0.7838 0.2142  0.0399  0.0202  108 PRO B CD  
5882 N N   . ASN B 109 ? 1.3158 0.9988 0.8754 0.1887  0.0562  0.0189  109 ASN B N   
5883 C CA  . ASN B 109 ? 1.3088 0.9689 0.8588 0.1815  0.0639  0.0190  109 ASN B CA  
5884 C C   . ASN B 109 ? 1.2337 0.8835 0.7890 0.1615  0.0660  0.0138  109 ASN B C   
5885 O O   . ASN B 109 ? 1.1990 0.8467 0.7615 0.1508  0.0671  0.0117  109 ASN B O   
5886 C CB  . ASN B 109 ? 1.3856 1.0127 0.9012 0.1941  0.0755  0.0245  109 ASN B CB  
5887 C CG  . ASN B 109 ? 1.4821 1.1198 0.9897 0.2161  0.0740  0.0302  109 ASN B CG  
5888 O OD1 . ASN B 109 ? 1.5162 1.1693 1.0316 0.2239  0.0709  0.0324  109 ASN B OD1 
5889 N ND2 . ASN B 109 ? 1.4908 1.1217 0.9828 0.2265  0.0761  0.0328  109 ASN B ND2 
5890 N N   . LEU B 110 ? 1.1770 0.8221 0.7286 0.1569  0.0667  0.0119  110 LEU B N   
5891 C CA  . LEU B 110 ? 1.1440 0.7786 0.6971 0.1391  0.0699  0.0074  110 LEU B CA  
5892 C C   . LEU B 110 ? 1.0636 0.7264 0.6470 0.1275  0.0602  0.0024  110 LEU B C   
5893 O O   . LEU B 110 ? 1.0854 0.7454 0.6738 0.1131  0.0616  -0.0012 110 LEU B O   
5894 C CB  . LEU B 110 ? 1.1864 0.7993 0.7179 0.1394  0.0768  0.0080  110 LEU B CB  
5895 C CG  . LEU B 110 ? 1.2612 0.8414 0.7584 0.1509  0.0878  0.0132  110 LEU B CG  
5896 C CD1 . LEU B 110 ? 1.2792 0.8372 0.7574 0.1454  0.0952  0.0125  110 LEU B CD1 
5897 C CD2 . LEU B 110 ? 1.2457 0.8049 0.7295 0.1489  0.0954  0.0145  110 LEU B CD2 
5898 N N   . ARG B 111 ? 0.9816 0.6715 0.5845 0.1338  0.0507  0.0024  111 ARG B N   
5899 C CA  . ARG B 111 ? 0.9542 0.6695 0.5836 0.1249  0.0415  -0.0019 111 ARG B CA  
5900 C C   . ARG B 111 ? 0.9458 0.6669 0.5913 0.1112  0.0402  -0.0050 111 ARG B C   
5901 O O   . ARG B 111 ? 0.9530 0.6781 0.6079 0.0996  0.0391  -0.0087 111 ARG B O   
5902 C CB  . ARG B 111 ? 0.9338 0.6753 0.5778 0.1345  0.0323  -0.0013 111 ARG B CB  
5903 C CG  . ARG B 111 ? 0.9474 0.6926 0.5841 0.1437  0.0303  -0.0006 111 ARG B CG  
5904 C CD  . ARG B 111 ? 0.9558 0.7272 0.6043 0.1534  0.0220  0.0002  111 ARG B CD  
5905 N NE  . ARG B 111 ? 0.9346 0.7087 0.5722 0.1647  0.0210  0.0018  111 ARG B NE  
5906 C CZ  . ARG B 111 ? 0.8959 0.6947 0.5427 0.1721  0.0134  0.0017  111 ARG B CZ  
5907 N NH1 . ARG B 111 ? 0.8835 0.7057 0.5505 0.1690  0.0063  0.0000  111 ARG B NH1 
5908 N NH2 . ARG B 111 ? 0.9002 0.7008 0.5358 0.1823  0.0131  0.0032  111 ARG B NH2 
5909 N N   . PRO B 112 ? 0.9098 0.6326 0.5583 0.1129  0.0405  -0.0032 112 PRO B N   
5910 C CA  . PRO B 112 ? 0.8755 0.6063 0.5403 0.1008  0.0386  -0.0060 112 PRO B CA  
5911 C C   . PRO B 112 ? 0.8779 0.5935 0.5359 0.0873  0.0449  -0.0086 112 PRO B C   
5912 O O   . PRO B 112 ? 0.8827 0.6108 0.5573 0.0764  0.0415  -0.0120 112 PRO B O   
5913 C CB  . PRO B 112 ? 0.9019 0.6307 0.5637 0.1069  0.0403  -0.0028 112 PRO B CB  
5914 C CG  . PRO B 112 ? 0.9079 0.6429 0.5641 0.1228  0.0379  0.0007  112 PRO B CG  
5915 C CD  . PRO B 112 ? 0.9287 0.6496 0.5677 0.1270  0.0418  0.0013  112 PRO B CD  
5916 N N   . LYS B 113 ? 0.8843 0.5738 0.5176 0.0881  0.0542  -0.0071 113 LYS B N   
5917 C CA  . LYS B 113 ? 0.8936 0.5685 0.5181 0.0744  0.0608  -0.0098 113 LYS B CA  
5918 C C   . LYS B 113 ? 0.8495 0.5339 0.4820 0.0682  0.0580  -0.0128 113 LYS B C   
5919 O O   . LYS B 113 ? 0.8197 0.5077 0.4585 0.0552  0.0591  -0.0161 113 LYS B O   
5920 C CB  . LYS B 113 ? 0.9800 0.6225 0.5735 0.0766  0.0720  -0.0075 113 LYS B CB  
5921 C CG  . LYS B 113 ? 1.0904 0.7175 0.6738 0.0713  0.0784  -0.0073 113 LYS B CG  
5922 C CD  . LYS B 113 ? 1.1533 0.7769 0.7310 0.0857  0.0783  -0.0030 113 LYS B CD  
5923 C CE  . LYS B 113 ? 1.2172 0.8138 0.7732 0.0828  0.0881  -0.0022 113 LYS B CE  
5924 N NZ  . LYS B 113 ? 1.2514 0.8488 0.8059 0.0954  0.0874  0.0015  113 LYS B NZ  
5925 N N   . LEU B 114 ? 0.8433 0.5325 0.4750 0.0779  0.0545  -0.0117 114 LEU B N   
5926 C CA  . LEU B 114 ? 0.8241 0.5235 0.4640 0.0733  0.0513  -0.0145 114 LEU B CA  
5927 C C   . LEU B 114 ? 0.7621 0.4877 0.4294 0.0680  0.0424  -0.0176 114 LEU B C   
5928 O O   . LEU B 114 ? 0.7477 0.4797 0.4229 0.0581  0.0421  -0.0207 114 LEU B O   
5929 C CB  . LEU B 114 ? 0.8493 0.5462 0.4797 0.0849  0.0502  -0.0127 114 LEU B CB  
5930 C CG  . LEU B 114 ? 0.9222 0.5949 0.5277 0.0848  0.0592  -0.0115 114 LEU B CG  
5931 C CD1 . LEU B 114 ? 0.9439 0.6200 0.5450 0.0952  0.0564  -0.0104 114 LEU B CD1 
5932 C CD2 . LEU B 114 ? 0.9351 0.6035 0.5404 0.0692  0.0636  -0.0149 114 LEU B CD2 
5933 N N   . LEU B 115 ? 0.7241 0.4646 0.4049 0.0743  0.0357  -0.0167 115 LEU B N   
5934 C CA  . LEU B 115 ? 0.6978 0.4605 0.4028 0.0691  0.0279  -0.0194 115 LEU B CA  
5935 C C   . LEU B 115 ? 0.6823 0.4461 0.3943 0.0573  0.0303  -0.0211 115 LEU B C   
5936 O O   . LEU B 115 ? 0.7028 0.4793 0.4289 0.0503  0.0270  -0.0238 115 LEU B O   
5937 C CB  . LEU B 115 ? 0.6722 0.4498 0.3892 0.0767  0.0211  -0.0181 115 LEU B CB  
5938 C CG  . LEU B 115 ? 0.6538 0.4520 0.3941 0.0713  0.0136  -0.0207 115 LEU B CG  
5939 C CD1 . LEU B 115 ? 0.6259 0.4336 0.3734 0.0709  0.0088  -0.0236 115 LEU B CD1 
5940 C CD2 . LEU B 115 ? 0.6516 0.4621 0.4017 0.0766  0.0088  -0.0191 115 LEU B CD2 
5941 N N   . LEU B 116 ? 0.6652 0.4155 0.3662 0.0555  0.0362  -0.0195 116 LEU B N   
5942 C CA  . LEU B 116 ? 0.6585 0.4097 0.3643 0.0442  0.0388  -0.0211 116 LEU B CA  
5943 C C   . LEU B 116 ? 0.6706 0.4192 0.3724 0.0341  0.0427  -0.0239 116 LEU B C   
5944 O O   . LEU B 116 ? 0.6244 0.3880 0.3408 0.0263  0.0401  -0.0263 116 LEU B O   
5945 C CB  . LEU B 116 ? 0.6584 0.3926 0.3495 0.0441  0.0453  -0.0191 116 LEU B CB  
5946 C CG  . LEU B 116 ? 0.6599 0.3911 0.3502 0.0309  0.0500  -0.0213 116 LEU B CG  
5947 C CD1 . LEU B 116 ? 0.6279 0.3797 0.3403 0.0276  0.0439  -0.0222 116 LEU B CD1 
5948 C CD2 . LEU B 116 ? 0.6689 0.3755 0.3366 0.0297  0.0589  -0.0200 116 LEU B CD2 
5949 N N   . LYS B 117 ? 0.7016 0.4319 0.3833 0.0347  0.0491  -0.0233 117 LYS B N   
5950 C CA  . LYS B 117 ? 0.7358 0.4627 0.4114 0.0249  0.0538  -0.0257 117 LYS B CA  
5951 C C   . LYS B 117 ? 0.7165 0.4634 0.4090 0.0240  0.0475  -0.0279 117 LYS B C   
5952 O O   . LYS B 117 ? 0.7160 0.4725 0.4151 0.0144  0.0484  -0.0304 117 LYS B O   
5953 C CB  . LYS B 117 ? 0.7670 0.4703 0.4177 0.0276  0.0613  -0.0243 117 LYS B CB  
5954 C CG  . LYS B 117 ? 0.8209 0.5204 0.4640 0.0172  0.0665  -0.0267 117 LYS B CG  
5955 C CD  . LYS B 117 ? 0.9133 0.5837 0.5279 0.0149  0.0771  -0.0254 117 LYS B CD  
5956 C CE  . LYS B 117 ? 0.9063 0.5648 0.5074 0.0257  0.0783  -0.0231 117 LYS B CE  
5957 N NZ  . LYS B 117 ? 0.9848 0.6403 0.5782 0.0182  0.0826  -0.0249 117 LYS B NZ  
5958 N N   . HIS B 118 ? 0.7057 0.4593 0.4045 0.0342  0.0414  -0.0271 118 HIS B N   
5959 C CA  . HIS B 118 ? 0.7018 0.4719 0.4148 0.0347  0.0355  -0.0292 118 HIS B CA  
5960 C C   . HIS B 118 ? 0.6657 0.4548 0.4000 0.0320  0.0293  -0.0305 118 HIS B C   
5961 O O   . HIS B 118 ? 0.6922 0.4932 0.4364 0.0283  0.0271  -0.0326 118 HIS B O   
5962 C CB  . HIS B 118 ? 0.7275 0.4974 0.4381 0.0457  0.0314  -0.0283 118 HIS B CB  
5963 C CG  . HIS B 118 ? 0.7625 0.5160 0.4529 0.0486  0.0371  -0.0273 118 HIS B CG  
5964 N ND1 . HIS B 118 ? 0.7535 0.5100 0.4428 0.0517  0.0353  -0.0284 118 HIS B ND1 
5965 C CD2 . HIS B 118 ? 0.7939 0.5257 0.4628 0.0486  0.0454  -0.0251 118 HIS B CD2 
5966 C CE1 . HIS B 118 ? 0.7803 0.5191 0.4491 0.0538  0.0419  -0.0268 118 HIS B CE1 
5967 N NE2 . HIS B 118 ? 0.7950 0.5179 0.4509 0.0519  0.0482  -0.0247 118 HIS B NE2 
5968 N N   . ASN B 119 ? 0.6288 0.4207 0.3696 0.0345  0.0267  -0.0291 119 ASN B N   
5969 C CA  . ASN B 119 ? 0.5909 0.3989 0.3504 0.0310  0.0220  -0.0300 119 ASN B CA  
5970 C C   . ASN B 119 ? 0.5846 0.3961 0.3457 0.0205  0.0261  -0.0314 119 ASN B C   
5971 O O   . ASN B 119 ? 0.5828 0.4083 0.3562 0.0173  0.0234  -0.0330 119 ASN B O   
5972 C CB  . ASN B 119 ? 0.5831 0.3927 0.3479 0.0349  0.0194  -0.0280 119 ASN B CB  
5973 C CG  . ASN B 119 ? 0.5564 0.3746 0.3299 0.0431  0.0124  -0.0276 119 ASN B CG  
5974 O OD1 . ASN B 119 ? 0.5784 0.3983 0.3542 0.0478  0.0104  -0.0257 119 ASN B OD1 
5975 N ND2 . ASN B 119 ? 0.5164 0.3406 0.2943 0.0446  0.0089  -0.0295 119 ASN B ND2 
5976 N N   . LEU B 120 ? 0.5694 0.3681 0.3170 0.0154  0.0328  -0.0309 120 LEU B N   
5977 C CA  . LEU B 120 ? 0.5626 0.3648 0.3092 0.0041  0.0374  -0.0326 120 LEU B CA  
5978 C C   . LEU B 120 ? 0.5769 0.3877 0.3252 0.0000  0.0381  -0.0347 120 LEU B C   
5979 O O   . LEU B 120 ? 0.5756 0.4031 0.3359 -0.0049 0.0366  -0.0361 120 LEU B O   
5980 C CB  . LEU B 120 ? 0.5589 0.3418 0.2863 -0.0012 0.0456  -0.0322 120 LEU B CB  
5981 C CG  . LEU B 120 ? 0.5713 0.3475 0.2965 -0.0011 0.0468  -0.0307 120 LEU B CG  
5982 C CD1 . LEU B 120 ? 0.5752 0.3282 0.2773 -0.0064 0.0560  -0.0307 120 LEU B CD1 
5983 C CD2 . LEU B 120 ? 0.5285 0.3226 0.2701 -0.0071 0.0439  -0.0317 120 LEU B CD2 
5984 N N   . PHE B 121 ? 0.5886 0.3891 0.3253 0.0030  0.0403  -0.0347 121 PHE B N   
5985 C CA  . PHE B 121 ? 0.5834 0.3927 0.3219 0.0003  0.0407  -0.0366 121 PHE B CA  
5986 C C   . PHE B 121 ? 0.5574 0.3866 0.3151 0.0036  0.0338  -0.0374 121 PHE B C   
5987 O O   . PHE B 121 ? 0.5439 0.3874 0.3087 -0.0016 0.0344  -0.0388 121 PHE B O   
5988 C CB  . PHE B 121 ? 0.5924 0.3891 0.3177 0.0058  0.0424  -0.0361 121 PHE B CB  
5989 C CG  . PHE B 121 ? 0.5961 0.4012 0.3220 0.0027  0.0435  -0.0380 121 PHE B CG  
5990 C CD1 . PHE B 121 ? 0.5712 0.3903 0.3102 0.0083  0.0374  -0.0389 121 PHE B CD1 
5991 C CD2 . PHE B 121 ? 0.5964 0.3955 0.3092 -0.0061 0.0510  -0.0389 121 PHE B CD2 
5992 C CE1 . PHE B 121 ? 0.5857 0.4128 0.3248 0.0063  0.0387  -0.0404 121 PHE B CE1 
5993 C CE2 . PHE B 121 ? 0.6040 0.4128 0.3179 -0.0089 0.0522  -0.0404 121 PHE B CE2 
5994 C CZ  . PHE B 121 ? 0.5961 0.4191 0.3231 -0.0020 0.0460  -0.0411 121 PHE B CZ  
5995 N N   . LEU B 122 ? 0.5544 0.3846 0.3195 0.0126  0.0276  -0.0366 122 LEU B N   
5996 C CA  . LEU B 122 ? 0.5415 0.3869 0.3228 0.0159  0.0215  -0.0375 122 LEU B CA  
5997 C C   . LEU B 122 ? 0.5287 0.3875 0.3221 0.0110  0.0208  -0.0375 122 LEU B C   
5998 O O   . LEU B 122 ? 0.5260 0.3979 0.3277 0.0100  0.0198  -0.0384 122 LEU B O   
5999 C CB  . LEU B 122 ? 0.5294 0.3730 0.3157 0.0245  0.0154  -0.0369 122 LEU B CB  
6000 C CG  . LEU B 122 ? 0.5441 0.3787 0.3207 0.0309  0.0146  -0.0371 122 LEU B CG  
6001 C CD1 . LEU B 122 ? 0.5263 0.3609 0.3073 0.0379  0.0090  -0.0364 122 LEU B CD1 
6002 C CD2 . LEU B 122 ? 0.5377 0.3779 0.3157 0.0320  0.0136  -0.0392 122 LEU B CD2 
6003 N N   . LEU B 123 ? 0.5389 0.3944 0.3325 0.0084  0.0218  -0.0362 123 LEU B N   
6004 C CA  . LEU B 123 ? 0.5234 0.3916 0.3280 0.0040  0.0211  -0.0360 123 LEU B CA  
6005 C C   . LEU B 123 ? 0.5243 0.4019 0.3269 -0.0046 0.0259  -0.0373 123 LEU B C   
6006 O O   . LEU B 123 ? 0.5223 0.4162 0.3356 -0.0060 0.0245  -0.0375 123 LEU B O   
6007 C CB  . LEU B 123 ? 0.5186 0.3807 0.3227 0.0032  0.0214  -0.0344 123 LEU B CB  
6008 C CG  . LEU B 123 ? 0.5262 0.3844 0.3352 0.0109  0.0164  -0.0329 123 LEU B CG  
6009 C CD1 . LEU B 123 ? 0.5072 0.3572 0.3110 0.0097  0.0187  -0.0313 123 LEU B CD1 
6010 C CD2 . LEU B 123 ? 0.4986 0.3696 0.3237 0.0139  0.0106  -0.0327 123 LEU B CD2 
6011 N N   . ASP B 124 ? 0.5281 0.3956 0.3161 -0.0103 0.0318  -0.0381 124 ASP B N   
6012 C CA  . ASP B 124 ? 0.5401 0.4163 0.3243 -0.0206 0.0371  -0.0397 124 ASP B CA  
6013 C C   . ASP B 124 ? 0.5363 0.4249 0.3233 -0.0202 0.0371  -0.0409 124 ASP B C   
6014 O O   . ASP B 124 ? 0.5507 0.4560 0.3416 -0.0265 0.0392  -0.0419 124 ASP B O   
6015 C CB  . ASP B 124 ? 0.5621 0.4204 0.3273 -0.0281 0.0443  -0.0404 124 ASP B CB  
6016 C CG  . ASP B 124 ? 0.5848 0.4331 0.3454 -0.0315 0.0463  -0.0397 124 ASP B CG  
6017 O OD1 . ASP B 124 ? 0.5790 0.4397 0.3510 -0.0329 0.0437  -0.0394 124 ASP B OD1 
6018 O OD2 . ASP B 124 ? 0.6181 0.4451 0.3620 -0.0325 0.0510  -0.0393 124 ASP B OD2 
6019 N N   . ASN B 125 ? 0.5291 0.4103 0.3133 -0.0128 0.0351  -0.0408 125 ASN B N   
6020 C CA  . ASN B 125 ? 0.5524 0.4424 0.3360 -0.0123 0.0361  -0.0419 125 ASN B CA  
6021 C C   . ASN B 125 ? 0.5383 0.4390 0.3342 -0.0031 0.0303  -0.0418 125 ASN B C   
6022 O O   . ASN B 125 ? 0.5609 0.4733 0.3589 -0.0024 0.0310  -0.0426 125 ASN B O   
6023 C CB  . ASN B 125 ? 0.5369 0.4102 0.3050 -0.0118 0.0395  -0.0423 125 ASN B CB  
6024 C CG  . ASN B 125 ? 0.5550 0.4163 0.3080 -0.0218 0.0468  -0.0427 125 ASN B CG  
6025 O OD1 . ASN B 125 ? 0.5396 0.4083 0.2879 -0.0311 0.0519  -0.0441 125 ASN B OD1 
6026 N ND2 . ASN B 125 ? 0.5694 0.4122 0.3139 -0.0202 0.0477  -0.0415 125 ASN B ND2 
6027 N N   . ILE B 126 ? 0.5271 0.4233 0.3302 0.0035  0.0250  -0.0408 126 ILE B N   
6028 C CA  . ILE B 126 ? 0.5122 0.4142 0.3245 0.0118  0.0199  -0.0409 126 ILE B CA  
6029 C C   . ILE B 126 ? 0.4835 0.3933 0.3083 0.0139  0.0162  -0.0398 126 ILE B C   
6030 O O   . ILE B 126 ? 0.4859 0.4072 0.3184 0.0172  0.0147  -0.0396 126 ILE B O   
6031 C CB  . ILE B 126 ? 0.5265 0.4147 0.3340 0.0186  0.0166  -0.0414 126 ILE B CB  
6032 C CG1 . ILE B 126 ? 0.5463 0.4280 0.3413 0.0178  0.0203  -0.0424 126 ILE B CG1 
6033 C CG2 . ILE B 126 ? 0.5117 0.4038 0.3279 0.0259  0.0114  -0.0420 126 ILE B CG2 
6034 C CD1 . ILE B 126 ? 0.5441 0.4136 0.3330 0.0246  0.0175  -0.0429 126 ILE B CD1 
6035 N N   . VAL B 127 ? 0.4506 0.3540 0.2767 0.0123  0.0151  -0.0387 127 VAL B N   
6036 C CA  . VAL B 127 ? 0.4240 0.3331 0.2615 0.0145  0.0115  -0.0374 127 VAL B CA  
6037 C C   . VAL B 127 ? 0.4135 0.3384 0.2570 0.0101  0.0138  -0.0367 127 VAL B C   
6038 O O   . VAL B 127 ? 0.4268 0.3623 0.2780 0.0139  0.0122  -0.0361 127 VAL B O   
6039 C CB  . VAL B 127 ? 0.4118 0.3107 0.2494 0.0150  0.0094  -0.0363 127 VAL B CB  
6040 C CG1 . VAL B 127 ? 0.3924 0.2981 0.2415 0.0162  0.0064  -0.0349 127 VAL B CG1 
6041 C CG2 . VAL B 127 ? 0.4063 0.2938 0.2398 0.0208  0.0062  -0.0370 127 VAL B CG2 
6042 N N   . LYS B 128 ? 0.4244 0.3506 0.2631 0.0022  0.0178  -0.0368 128 LYS B N   
6043 C CA  . LYS B 128 ? 0.4310 0.3747 0.2743 -0.0031 0.0203  -0.0366 128 LYS B CA  
6044 C C   . LYS B 128 ? 0.4498 0.4089 0.2944 -0.0020 0.0218  -0.0372 128 LYS B C   
6045 O O   . LYS B 128 ? 0.4638 0.4388 0.3172 0.0011  0.0207  -0.0361 128 LYS B O   
6046 C CB  . LYS B 128 ? 0.4373 0.3778 0.2726 -0.0132 0.0249  -0.0373 128 LYS B CB  
6047 C CG  . LYS B 128 ? 0.4382 0.3699 0.2751 -0.0136 0.0235  -0.0361 128 LYS B CG  
6048 C CD  . LYS B 128 ? 0.4562 0.3820 0.2829 -0.0234 0.0286  -0.0371 128 LYS B CD  
6049 C CE  . LYS B 128 ? 0.4552 0.3709 0.2826 -0.0223 0.0273  -0.0357 128 LYS B CE  
6050 N NZ  . LYS B 128 ? 0.4719 0.3818 0.2888 -0.0321 0.0327  -0.0369 128 LYS B NZ  
6051 N N   . PRO B 129 ? 0.4624 0.4173 0.2982 -0.0035 0.0244  -0.0388 129 PRO B N   
6052 C CA  . PRO B 129 ? 0.4765 0.4465 0.3138 -0.0012 0.0257  -0.0392 129 PRO B CA  
6053 C C   . PRO B 129 ? 0.4771 0.4513 0.3222 0.0098  0.0217  -0.0381 129 PRO B C   
6054 O O   . PRO B 129 ? 0.4722 0.4644 0.3220 0.0124  0.0226  -0.0374 129 PRO B O   
6055 C CB  . PRO B 129 ? 0.4915 0.4507 0.3172 -0.0034 0.0285  -0.0409 129 PRO B CB  
6056 C CG  . PRO B 129 ? 0.5067 0.4536 0.3236 -0.0122 0.0317  -0.0414 129 PRO B CG  
6057 C CD  . PRO B 129 ? 0.4815 0.4205 0.3043 -0.0090 0.0278  -0.0400 129 PRO B CD  
6058 N N   . ILE B 130 ? 0.4792 0.4374 0.3249 0.0163  0.0176  -0.0381 130 ILE B N   
6059 C CA  . ILE B 130 ? 0.4745 0.4339 0.3258 0.0259  0.0143  -0.0374 130 ILE B CA  
6060 C C   . ILE B 130 ? 0.4715 0.4423 0.3322 0.0283  0.0133  -0.0351 130 ILE B C   
6061 O O   . ILE B 130 ? 0.4931 0.4735 0.3569 0.0349  0.0135  -0.0341 130 ILE B O   
6062 C CB  . ILE B 130 ? 0.4692 0.4100 0.3187 0.0310  0.0102  -0.0383 130 ILE B CB  
6063 C CG1 . ILE B 130 ? 0.4680 0.4086 0.3191 0.0397  0.0084  -0.0385 130 ILE B CG1 
6064 C CG2 . ILE B 130 ? 0.4547 0.3877 0.3090 0.0299  0.0072  -0.0373 130 ILE B CG2 
6065 C CD1 . ILE B 130 ? 0.5293 0.4752 0.3746 0.0422  0.0110  -0.0396 130 ILE B CD1 
6066 N N   . ILE B 131 ? 0.4592 0.4280 0.3234 0.0238  0.0125  -0.0342 131 ILE B N   
6067 C CA  . ILE B 131 ? 0.4779 0.4571 0.3505 0.0257  0.0117  -0.0319 131 ILE B CA  
6068 C C   . ILE B 131 ? 0.4824 0.4846 0.3570 0.0242  0.0151  -0.0311 131 ILE B C   
6069 O O   . ILE B 131 ? 0.4932 0.5068 0.3728 0.0309  0.0149  -0.0291 131 ILE B O   
6070 C CB  . ILE B 131 ? 0.4749 0.4489 0.3501 0.0201  0.0108  -0.0312 131 ILE B CB  
6071 C CG1 . ILE B 131 ? 0.4592 0.4140 0.3334 0.0224  0.0073  -0.0317 131 ILE B CG1 
6072 C CG2 . ILE B 131 ? 0.4708 0.4570 0.3543 0.0217  0.0103  -0.0286 131 ILE B CG2 
6073 C CD1 . ILE B 131 ? 0.4601 0.4075 0.3326 0.0165  0.0073  -0.0316 131 ILE B CD1 
6074 N N   . ALA B 132 ? 0.4681 0.4772 0.3378 0.0155  0.0186  -0.0327 132 ALA B N   
6075 C CA  . ALA B 132 ? 0.4839 0.5176 0.3551 0.0121  0.0220  -0.0325 132 ALA B CA  
6076 C C   . ALA B 132 ? 0.5045 0.5488 0.3750 0.0197  0.0230  -0.0322 132 ALA B C   
6077 O O   . ALA B 132 ? 0.4932 0.5612 0.3673 0.0214  0.0249  -0.0310 132 ALA B O   
6078 C CB  . ALA B 132 ? 0.4927 0.5289 0.3573 -0.0006 0.0259  -0.0348 132 ALA B CB  
6079 N N   . PHE B 133 ? 0.4989 0.5268 0.3644 0.0246  0.0217  -0.0334 133 PHE B N   
6080 C CA  . PHE B 133 ? 0.5026 0.5376 0.3664 0.0328  0.0226  -0.0332 133 PHE B CA  
6081 C C   . PHE B 133 ? 0.5027 0.5410 0.3716 0.0445  0.0208  -0.0306 133 PHE B C   
6082 O O   . PHE B 133 ? 0.5242 0.5786 0.3936 0.0514  0.0227  -0.0293 133 PHE B O   
6083 C CB  . PHE B 133 ? 0.5185 0.5348 0.3746 0.0347  0.0218  -0.0353 133 PHE B CB  
6084 C CG  . PHE B 133 ? 0.5292 0.5532 0.3824 0.0426  0.0233  -0.0354 133 PHE B CG  
6085 C CD1 . PHE B 133 ? 0.5324 0.5748 0.3829 0.0386  0.0274  -0.0360 133 PHE B CD1 
6086 C CD2 . PHE B 133 ? 0.5343 0.5472 0.3867 0.0537  0.0210  -0.0350 133 PHE B CD2 
6087 C CE1 . PHE B 133 ? 0.5255 0.5762 0.3733 0.0465  0.0289  -0.0359 133 PHE B CE1 
6088 C CE2 . PHE B 133 ? 0.5393 0.5583 0.3879 0.0616  0.0227  -0.0351 133 PHE B CE2 
6089 C CZ  . PHE B 133 ? 0.5413 0.5797 0.3879 0.0586  0.0266  -0.0353 133 PHE B CZ  
6090 N N   . TYR B 134 ? 0.4933 0.5165 0.3653 0.0470  0.0176  -0.0297 134 TYR B N   
6091 C CA  . TYR B 134 ? 0.4944 0.5164 0.3695 0.0578  0.0164  -0.0271 134 TYR B CA  
6092 C C   . TYR B 134 ? 0.5048 0.5406 0.3869 0.0582  0.0166  -0.0241 134 TYR B C   
6093 O O   . TYR B 134 ? 0.5026 0.5435 0.3861 0.0679  0.0171  -0.0213 134 TYR B O   
6094 C CB  . TYR B 134 ? 0.4919 0.4878 0.3646 0.0613  0.0129  -0.0281 134 TYR B CB  
6095 C CG  . TYR B 134 ? 0.4988 0.4824 0.3640 0.0642  0.0126  -0.0307 134 TYR B CG  
6096 C CD1 . TYR B 134 ? 0.5075 0.4965 0.3686 0.0729  0.0147  -0.0303 134 TYR B CD1 
6097 C CD2 . TYR B 134 ? 0.4934 0.4612 0.3551 0.0586  0.0105  -0.0334 134 TYR B CD2 
6098 C CE1 . TYR B 134 ? 0.5307 0.5089 0.3846 0.0755  0.0145  -0.0329 134 TYR B CE1 
6099 C CE2 . TYR B 134 ? 0.5049 0.4626 0.3596 0.0612  0.0101  -0.0358 134 TYR B CE2 
6100 C CZ  . TYR B 134 ? 0.5268 0.4891 0.3776 0.0694  0.0121  -0.0357 134 TYR B CZ  
6101 O OH  . TYR B 134 ? 0.5022 0.4546 0.3456 0.0720  0.0118  -0.0383 134 TYR B OH  
6102 N N   . TYR B 135 ? 0.5114 0.5526 0.3968 0.0481  0.0166  -0.0245 135 TYR B N   
6103 C CA  . TYR B 135 ? 0.5091 0.5612 0.4010 0.0475  0.0164  -0.0220 135 TYR B CA  
6104 C C   . TYR B 135 ? 0.5147 0.5894 0.4088 0.0383  0.0189  -0.0224 135 TYR B C   
6105 O O   . TYR B 135 ? 0.5297 0.6032 0.4198 0.0284  0.0203  -0.0252 135 TYR B O   
6106 C CB  . TYR B 135 ? 0.4774 0.5100 0.3715 0.0448  0.0134  -0.0219 135 TYR B CB  
6107 C CG  . TYR B 135 ? 0.4926 0.5054 0.3851 0.0528  0.0110  -0.0214 135 TYR B CG  
6108 C CD1 . TYR B 135 ? 0.4913 0.5042 0.3862 0.0616  0.0109  -0.0183 135 TYR B CD1 
6109 C CD2 . TYR B 135 ? 0.4879 0.4814 0.3755 0.0516  0.0092  -0.0242 135 TYR B CD2 
6110 C CE1 . TYR B 135 ? 0.4953 0.4879 0.3870 0.0678  0.0093  -0.0182 135 TYR B CE1 
6111 C CE2 . TYR B 135 ? 0.4781 0.4541 0.3637 0.0577  0.0071  -0.0243 135 TYR B CE2 
6112 C CZ  . TYR B 135 ? 0.5109 0.4857 0.3982 0.0652  0.0073  -0.0215 135 TYR B CZ  
6113 O OH  . TYR B 135 ? 0.5650 0.5204 0.4486 0.0700  0.0058  -0.0221 135 TYR B OH  
6114 N N   . LYS B 136 ? 0.5462 0.6410 0.4455 0.0414  0.0197  -0.0197 136 LYS B N   
6115 C CA  . LYS B 136 ? 0.5588 0.6748 0.4610 0.0318  0.0215  -0.0202 136 LYS B CA  
6116 C C   . LYS B 136 ? 0.5383 0.6453 0.4444 0.0282  0.0195  -0.0192 136 LYS B C   
6117 O O   . LYS B 136 ? 0.5548 0.6589 0.4648 0.0366  0.0178  -0.0161 136 LYS B O   
6118 C CB  . LYS B 136 ? 0.6110 0.7581 0.5168 0.0380  0.0235  -0.0176 136 LYS B CB  
6119 C CG  . LYS B 136 ? 0.6812 0.8558 0.5893 0.0271  0.0257  -0.0188 136 LYS B CG  
6120 C CD  . LYS B 136 ? 0.7647 0.9424 0.6671 0.0145  0.0283  -0.0230 136 LYS B CD  
6121 C CE  . LYS B 136 ? 0.7988 1.0131 0.7029 0.0084  0.0314  -0.0237 136 LYS B CE  
6122 N NZ  . LYS B 136 ? 0.8266 1.0619 0.7372 0.0093  0.0308  -0.0214 136 LYS B NZ  
6123 N N   . PRO B 137 ? 0.5318 0.6324 0.4356 0.0159  0.0199  -0.0219 137 PRO B N   
6124 C CA  . PRO B 137 ? 0.5357 0.6312 0.4429 0.0123  0.0185  -0.0210 137 PRO B CA  
6125 C C   . PRO B 137 ? 0.5511 0.6742 0.4631 0.0103  0.0199  -0.0195 137 PRO B C   
6126 O O   . PRO B 137 ? 0.5603 0.7043 0.4708 0.0035  0.0226  -0.0213 137 PRO B O   
6127 C CB  . PRO B 137 ? 0.5364 0.6170 0.4374 0.0005  0.0195  -0.0244 137 PRO B CB  
6128 C CG  . PRO B 137 ? 0.5325 0.6205 0.4272 -0.0051 0.0226  -0.0271 137 PRO B CG  
6129 C CD  . PRO B 137 ? 0.5328 0.6284 0.4293 0.0055  0.0221  -0.0257 137 PRO B CD  
6130 N N   . ILE B 138 ? 0.5489 0.6731 0.4665 0.0162  0.0182  -0.0163 138 ILE B N   
6131 C CA  . ILE B 138 ? 0.5467 0.6971 0.4688 0.0151  0.0192  -0.0146 138 ILE B CA  
6132 C C   . ILE B 138 ? 0.5321 0.6742 0.4565 0.0100  0.0179  -0.0142 138 ILE B C   
6133 O O   . ILE B 138 ? 0.5187 0.6405 0.4447 0.0150  0.0156  -0.0124 138 ILE B O   
6134 C CB  . ILE B 138 ? 0.5439 0.7101 0.4700 0.0295  0.0191  -0.0101 138 ILE B CB  
6135 C CG1 . ILE B 138 ? 0.5303 0.7222 0.4552 0.0307  0.0217  -0.0107 138 ILE B CG1 
6136 C CG2 . ILE B 138 ? 0.5341 0.7163 0.4656 0.0320  0.0188  -0.0069 138 ILE B CG2 
6137 C CD1 . ILE B 138 ? 0.5498 0.7295 0.4703 0.0367  0.0220  -0.0114 138 ILE B CD1 
6138 N N   . LYS B 139 ? 0.5565 0.7140 0.4802 -0.0007 0.0196  -0.0163 139 LYS B N   
6139 C CA  . LYS B 139 ? 0.5701 0.7247 0.4956 -0.0056 0.0189  -0.0159 139 LYS B CA  
6140 C C   . LYS B 139 ? 0.5577 0.7322 0.4902 0.0030  0.0181  -0.0116 139 LYS B C   
6141 O O   . LYS B 139 ? 0.5462 0.7497 0.4804 0.0027  0.0196  -0.0113 139 LYS B O   
6142 C CB  . LYS B 139 ? 0.5915 0.7544 0.5117 -0.0212 0.0217  -0.0203 139 LYS B CB  
6143 C CG  . LYS B 139 ? 0.6289 0.7701 0.5400 -0.0301 0.0234  -0.0243 139 LYS B CG  
6144 C CD  . LYS B 139 ? 0.6830 0.8329 0.5867 -0.0460 0.0271  -0.0288 139 LYS B CD  
6145 C CE  . LYS B 139 ? 0.7434 0.8766 0.6365 -0.0541 0.0300  -0.0325 139 LYS B CE  
6146 N NZ  . LYS B 139 ? 0.7736 0.8731 0.6610 -0.0533 0.0293  -0.0328 139 LYS B NZ  
6147 N N   . THR B 140 ? 0.5573 0.7170 0.4933 0.0110  0.0159  -0.0082 140 THR B N   
6148 C CA  . THR B 140 ? 0.5778 0.7520 0.5191 0.0211  0.0154  -0.0034 140 THR B CA  
6149 C C   . THR B 140 ? 0.5957 0.7880 0.5393 0.0142  0.0159  -0.0035 140 THR B C   
6150 O O   . THR B 140 ? 0.5816 0.7943 0.5290 0.0210  0.0161  0.0000  140 THR B O   
6151 C CB  . THR B 140 ? 0.6026 0.7530 0.5458 0.0306  0.0134  0.0001  140 THR B CB  
6152 O OG1 . THR B 140 ? 0.5686 0.6992 0.5115 0.0230  0.0120  -0.0015 140 THR B OG1 
6153 C CG2 . THR B 140 ? 0.5986 0.7325 0.5390 0.0386  0.0130  0.0005  140 THR B CG2 
6154 N N   . LEU B 141 ? 0.6015 0.7854 0.5417 0.0011  0.0164  -0.0076 141 LEU B N   
6155 C CA  . LEU B 141 ? 0.6237 0.8202 0.5643 -0.0073 0.0171  -0.0087 141 LEU B CA  
6156 C C   . LEU B 141 ? 0.6028 0.7888 0.5474 -0.0020 0.0153  -0.0052 141 LEU B C   
6157 O O   . LEU B 141 ? 0.6267 0.8199 0.5714 -0.0083 0.0157  -0.0059 141 LEU B O   
6158 C CB  . LEU B 141 ? 0.6312 0.8648 0.5736 -0.0092 0.0187  -0.0089 141 LEU B CB  
6159 C CG  . LEU B 141 ? 0.6717 0.9220 0.6096 -0.0193 0.0211  -0.0134 141 LEU B CG  
6160 C CD1 . LEU B 141 ? 0.6958 0.9824 0.6353 -0.0255 0.0225  -0.0145 141 LEU B CD1 
6161 C CD2 . LEU B 141 ? 0.6621 0.8896 0.5917 -0.0328 0.0227  -0.0188 141 LEU B CD2 
6162 N N   . ASN B 142 ? 0.5642 0.7329 0.5115 0.0088  0.0135  -0.0015 142 ASN B N   
6163 C CA  . ASN B 142 ? 0.5569 0.7093 0.5067 0.0113  0.0120  0.0009  142 ASN B CA  
6164 C C   . ASN B 142 ? 0.5457 0.6743 0.4916 0.0029  0.0115  -0.0025 142 ASN B C   
6165 O O   . ASN B 142 ? 0.5195 0.6271 0.4644 0.0058  0.0103  -0.0026 142 ASN B O   
6166 C CB  . ASN B 142 ? 0.5821 0.7235 0.5349 0.0244  0.0108  0.0057  142 ASN B CB  
6167 C CG  . ASN B 142 ? 0.6212 0.7566 0.5776 0.0276  0.0099  0.0093  142 ASN B CG  
6168 O OD1 . ASN B 142 ? 0.6388 0.7665 0.5952 0.0203  0.0094  0.0077  142 ASN B OD1 
6169 N ND2 . ASN B 142 ? 0.6295 0.7680 0.5880 0.0390  0.0101  0.0143  142 ASN B ND2 
6170 N N   . GLY B 143 ? 0.5193 0.6518 0.4622 -0.0072 0.0128  -0.0052 143 GLY B N   
6171 C CA  . GLY B 143 ? 0.5096 0.6224 0.4459 -0.0160 0.0135  -0.0090 143 GLY B CA  
6172 C C   . GLY B 143 ? 0.5373 0.6428 0.4680 -0.0190 0.0146  -0.0123 143 GLY B C   
6173 O O   . GLY B 143 ? 0.5375 0.6601 0.4676 -0.0204 0.0158  -0.0135 143 GLY B O   
6174 N N   . HIS B 144 ? 0.5276 0.6091 0.4545 -0.0194 0.0139  -0.0134 144 HIS B N   
6175 C CA  . HIS B 144 ? 0.5199 0.5919 0.4400 -0.0228 0.0152  -0.0165 144 HIS B CA  
6176 C C   . HIS B 144 ? 0.5280 0.5936 0.4517 -0.0134 0.0130  -0.0147 144 HIS B C   
6177 O O   . HIS B 144 ? 0.5337 0.5870 0.4524 -0.0142 0.0133  -0.0167 144 HIS B O   
6178 C CB  . HIS B 144 ? 0.5015 0.5521 0.4129 -0.0293 0.0166  -0.0191 144 HIS B CB  
6179 C CG  . HIS B 144 ? 0.4919 0.5463 0.3978 -0.0389 0.0194  -0.0212 144 HIS B CG  
6180 N ND1 . HIS B 144 ? 0.4900 0.5385 0.3973 -0.0381 0.0187  -0.0196 144 HIS B ND1 
6181 C CD2 . HIS B 144 ? 0.5008 0.5651 0.3989 -0.0501 0.0232  -0.0250 144 HIS B CD2 
6182 C CE1 . HIS B 144 ? 0.4706 0.5238 0.3710 -0.0479 0.0219  -0.0224 144 HIS B CE1 
6183 N NE2 . HIS B 144 ? 0.4924 0.5550 0.3869 -0.0558 0.0247  -0.0258 144 HIS B NE2 
6184 N N   . GLU B 145 ? 0.5369 0.6109 0.4680 -0.0043 0.0112  -0.0110 145 GLU B N   
6185 C CA  . GLU B 145 ? 0.5324 0.5994 0.4658 0.0048  0.0095  -0.0092 145 GLU B CA  
6186 C C   . GLU B 145 ? 0.5340 0.6086 0.4636 0.0043  0.0110  -0.0114 145 GLU B C   
6187 O O   . GLU B 145 ? 0.5454 0.6411 0.4746 0.0011  0.0130  -0.0122 145 GLU B O   
6188 C CB  . GLU B 145 ? 0.5317 0.6072 0.4715 0.0144  0.0085  -0.0047 145 GLU B CB  
6189 C CG  . GLU B 145 ? 0.5758 0.6447 0.5159 0.0242  0.0077  -0.0029 145 GLU B CG  
6190 C CD  . GLU B 145 ? 0.6014 0.6755 0.5454 0.0341  0.0077  0.0018  145 GLU B CD  
6191 O OE1 . GLU B 145 ? 0.6361 0.6933 0.5802 0.0399  0.0065  0.0035  145 GLU B OE1 
6192 O OE2 . GLU B 145 ? 0.6272 0.7223 0.5733 0.0359  0.0090  0.0038  145 GLU B OE2 
6193 N N   . ILE B 146 ? 0.5031 0.5615 0.4298 0.0070  0.0100  -0.0125 146 ILE B N   
6194 C CA  . ILE B 146 ? 0.5094 0.5734 0.4330 0.0087  0.0112  -0.0140 146 ILE B CA  
6195 C C   . ILE B 146 ? 0.5142 0.5708 0.4398 0.0198  0.0095  -0.0117 146 ILE B C   
6196 O O   . ILE B 146 ? 0.5343 0.5722 0.4605 0.0228  0.0072  -0.0111 146 ILE B O   
6197 C CB  . ILE B 146 ? 0.4937 0.5450 0.4096 0.0014  0.0123  -0.0178 146 ILE B CB  
6198 C CG1 . ILE B 146 ? 0.4719 0.5326 0.3832 -0.0101 0.0154  -0.0205 146 ILE B CG1 
6199 C CG2 . ILE B 146 ? 0.4988 0.5517 0.4119 0.0052  0.0129  -0.0189 146 ILE B CG2 
6200 C CD1 . ILE B 146 ? 0.4705 0.5155 0.3720 -0.0176 0.0173  -0.0240 146 ILE B CD1 
6201 N N   . LYS B 147 ? 0.5298 0.6017 0.4560 0.0259  0.0107  -0.0104 147 LYS B N   
6202 C CA  . LYS B 147 ? 0.5605 0.6250 0.4865 0.0371  0.0100  -0.0082 147 LYS B CA  
6203 C C   . LYS B 147 ? 0.5546 0.6211 0.4758 0.0384  0.0112  -0.0105 147 LYS B C   
6204 O O   . LYS B 147 ? 0.5176 0.6032 0.4378 0.0345  0.0134  -0.0117 147 LYS B O   
6205 C CB  . LYS B 147 ? 0.6378 0.7171 0.5674 0.0460  0.0109  -0.0038 147 LYS B CB  
6206 C CG  . LYS B 147 ? 0.7293 0.7984 0.6567 0.0584  0.0110  -0.0011 147 LYS B CG  
6207 C CD  . LYS B 147 ? 0.7733 0.8497 0.7032 0.0669  0.0119  0.0038  147 LYS B CD  
6208 C CE  . LYS B 147 ? 0.8364 0.8877 0.7656 0.0705  0.0106  0.0056  147 LYS B CE  
6209 N NZ  . LYS B 147 ? 0.7671 0.8217 0.7005 0.0707  0.0105  0.0089  147 LYS B NZ  
6210 N N   . PHE B 148 ? 0.5280 0.5748 0.4459 0.0427  0.0098  -0.0113 148 PHE B N   
6211 C CA  . PHE B 148 ? 0.5195 0.5660 0.4324 0.0441  0.0109  -0.0135 148 PHE B CA  
6212 C C   . PHE B 148 ? 0.5176 0.5684 0.4292 0.0562  0.0119  -0.0110 148 PHE B C   
6213 O O   . PHE B 148 ? 0.5257 0.5608 0.4363 0.0633  0.0109  -0.0094 148 PHE B O   
6214 C CB  . PHE B 148 ? 0.5050 0.5282 0.4138 0.0411  0.0089  -0.0164 148 PHE B CB  
6215 C CG  . PHE B 148 ? 0.5123 0.5313 0.4194 0.0304  0.0088  -0.0190 148 PHE B CG  
6216 C CD1 . PHE B 148 ? 0.5019 0.5296 0.4047 0.0237  0.0113  -0.0214 148 PHE B CD1 
6217 C CD2 . PHE B 148 ? 0.5201 0.5259 0.4290 0.0270  0.0067  -0.0189 148 PHE B CD2 
6218 C CE1 . PHE B 148 ? 0.5211 0.5420 0.4201 0.0142  0.0120  -0.0236 148 PHE B CE1 
6219 C CE2 . PHE B 148 ? 0.5088 0.5094 0.4145 0.0185  0.0072  -0.0209 148 PHE B CE2 
6220 C CZ  . PHE B 148 ? 0.5105 0.5173 0.4105 0.0122  0.0101  -0.0233 148 PHE B CZ  
6221 N N   . ILE B 149 ? 0.5215 0.5935 0.4323 0.0585  0.0144  -0.0107 149 ILE B N   
6222 C CA  . ILE B 149 ? 0.5718 0.6509 0.4804 0.0713  0.0162  -0.0079 149 ILE B CA  
6223 C C   . ILE B 149 ? 0.5796 0.6537 0.4823 0.0737  0.0170  -0.0103 149 ILE B C   
6224 O O   . ILE B 149 ? 0.5849 0.6663 0.4866 0.0655  0.0177  -0.0133 149 ILE B O   
6225 C CB  . ILE B 149 ? 0.5550 0.6659 0.4672 0.0744  0.0185  -0.0051 149 ILE B CB  
6226 C CG1 . ILE B 149 ? 0.5897 0.7044 0.5072 0.0726  0.0176  -0.0026 149 ILE B CG1 
6227 C CG2 . ILE B 149 ? 0.5659 0.6849 0.4746 0.0896  0.0208  -0.0017 149 ILE B CG2 
6228 C CD1 . ILE B 149 ? 0.5908 0.6800 0.5076 0.0783  0.0160  -0.0005 149 ILE B CD1 
6229 N N   . ARG B 150 ? 0.6209 0.6800 0.5187 0.0844  0.0172  -0.0092 150 ARG B N   
6230 C CA  . ARG B 150 ? 0.6924 0.7469 0.5838 0.0889  0.0183  -0.0110 150 ARG B CA  
6231 C C   . ARG B 150 ? 0.6903 0.7748 0.5825 0.0893  0.0211  -0.0107 150 ARG B C   
6232 O O   . ARG B 150 ? 0.6924 0.7990 0.5874 0.0952  0.0230  -0.0073 150 ARG B O   
6233 C CB  . ARG B 150 ? 0.7653 0.8037 0.6504 0.1023  0.0192  -0.0088 150 ARG B CB  
6234 C CG  . ARG B 150 ? 0.8780 0.9030 0.7551 0.1067  0.0197  -0.0113 150 ARG B CG  
6235 C CD  . ARG B 150 ? 0.9437 0.9395 0.8178 0.1014  0.0165  -0.0147 150 ARG B CD  
6236 N NE  . ARG B 150 ? 0.9672 0.9518 0.8337 0.1041  0.0168  -0.0177 150 ARG B NE  
6237 C CZ  . ARG B 150 ? 0.9783 0.9689 0.8443 0.0980  0.0165  -0.0207 150 ARG B CZ  
6238 N NH1 . ARG B 150 ? 0.8967 0.9033 0.7686 0.0883  0.0163  -0.0212 150 ARG B NH1 
6239 N NH2 . ARG B 150 ? 0.9890 0.9687 0.8476 0.1014  0.0167  -0.0232 150 ARG B NH2 
6240 N N   . LYS B 151 ? 0.6893 0.7756 0.5790 0.0826  0.0216  -0.0141 151 LYS B N   
6241 C CA  . LYS B 151 ? 0.7128 0.8283 0.6037 0.0788  0.0243  -0.0147 151 LYS B CA  
6242 C C   . LYS B 151 ? 0.7519 0.8879 0.6414 0.0922  0.0272  -0.0114 151 LYS B C   
6243 O O   . LYS B 151 ? 0.7531 0.9199 0.6465 0.0916  0.0292  -0.0099 151 LYS B O   
6244 C CB  . LYS B 151 ? 0.7302 0.8393 0.6167 0.0699  0.0247  -0.0188 151 LYS B CB  
6245 C CG  . LYS B 151 ? 0.7546 0.8879 0.6429 0.0580  0.0270  -0.0206 151 LYS B CG  
6246 C CD  . LYS B 151 ? 0.7903 0.9083 0.6733 0.0468  0.0271  -0.0246 151 LYS B CD  
6247 C CE  . LYS B 151 ? 0.8129 0.9534 0.6949 0.0351  0.0306  -0.0267 151 LYS B CE  
6248 N NZ  . LYS B 151 ? 0.8484 0.9707 0.7240 0.0234  0.0312  -0.0302 151 LYS B NZ  
6249 N N   . GLU B 152 ? 0.7758 0.8949 0.6590 0.1043  0.0275  -0.0105 152 GLU B N   
6250 C CA  . GLU B 152 ? 0.8466 0.9811 0.7263 0.1195  0.0306  -0.0070 152 GLU B CA  
6251 C C   . GLU B 152 ? 0.8311 0.9783 0.7139 0.1284  0.0316  -0.0021 152 GLU B C   
6252 O O   . GLU B 152 ? 0.8230 0.9995 0.7069 0.1363  0.0343  0.0009  152 GLU B O   
6253 C CB  . GLU B 152 ? 0.8998 1.0091 0.7699 0.1302  0.0312  -0.0075 152 GLU B CB  
6254 C CG  . GLU B 152 ? 0.9834 1.0563 0.8504 0.1250  0.0279  -0.0105 152 GLU B CG  
6255 C CD  . GLU B 152 ? 1.0307 1.0975 0.8989 0.1110  0.0258  -0.0153 152 GLU B CD  
6256 O OE1 . GLU B 152 ? 1.0866 1.1633 0.9520 0.1099  0.0275  -0.0170 152 GLU B OE1 
6257 O OE2 . GLU B 152 ? 1.0251 1.0774 0.8965 0.1014  0.0229  -0.0170 152 GLU B OE2 
6258 N N   . GLU B 153 ? 0.8344 0.9609 0.7185 0.1272  0.0294  -0.0012 153 GLU B N   
6259 C CA  . GLU B 153 ? 0.8119 0.9486 0.6991 0.1340  0.0302  0.0034  153 GLU B CA  
6260 C C   . GLU B 153 ? 0.7775 0.9492 0.6732 0.1258  0.0303  0.0038  153 GLU B C   
6261 O O   . GLU B 153 ? 0.7999 0.9969 0.6974 0.1345  0.0324  0.0079  153 GLU B O   
6262 C CB  . GLU B 153 ? 0.8448 0.9532 0.7325 0.1308  0.0276  0.0036  153 GLU B CB  
6263 C CG  . GLU B 153 ? 0.9263 1.0026 0.8048 0.1410  0.0283  0.0045  153 GLU B CG  
6264 C CD  . GLU B 153 ? 0.9934 1.0429 0.8732 0.1344  0.0255  0.0037  153 GLU B CD  
6265 O OE1 . GLU B 153 ? 1.0486 1.1064 0.9350 0.1302  0.0245  0.0056  153 GLU B OE1 
6266 O OE2 . GLU B 153 ? 1.0354 1.0568 0.9096 0.1330  0.0243  0.0010  153 GLU B OE2 
6267 N N   . TYR B 154 ? 0.7431 0.9162 0.6431 0.1092  0.0285  -0.0004 154 TYR B N   
6268 C CA  . TYR B 154 ? 0.7166 0.9200 0.6232 0.0990  0.0289  -0.0010 154 TYR B CA  
6269 C C   . TYR B 154 ? 0.7263 0.9647 0.6331 0.1015  0.0318  -0.0007 154 TYR B C   
6270 O O   . TYR B 154 ? 0.7448 1.0152 0.6560 0.1026  0.0331  0.0014  154 TYR B O   
6271 C CB  . TYR B 154 ? 0.6911 0.8842 0.5998 0.0808  0.0270  -0.0058 154 TYR B CB  
6272 C CG  . TYR B 154 ? 0.6892 0.9134 0.6022 0.0689  0.0282  -0.0074 154 TYR B CG  
6273 C CD1 . TYR B 154 ? 0.6981 0.9380 0.6165 0.0670  0.0278  -0.0054 154 TYR B CD1 
6274 C CD2 . TYR B 154 ? 0.6747 0.9137 0.5859 0.0596  0.0302  -0.0108 154 TYR B CD2 
6275 C CE1 . TYR B 154 ? 0.7177 0.9871 0.6395 0.0554  0.0291  -0.0072 154 TYR B CE1 
6276 C CE2 . TYR B 154 ? 0.7232 0.9909 0.6374 0.0474  0.0318  -0.0127 154 TYR B CE2 
6277 C CZ  . TYR B 154 ? 0.7432 1.0262 0.6625 0.0452  0.0312  -0.0111 154 TYR B CZ  
6278 O OH  . TYR B 154 ? 0.7329 1.0447 0.6543 0.0320  0.0328  -0.0134 154 TYR B OH  
6279 N N   . ILE B 155 ? 0.7119 0.9457 0.6139 0.1017  0.0330  -0.0031 155 ILE B N   
6280 C CA  . ILE B 155 ? 0.7085 0.9755 0.6104 0.1042  0.0360  -0.0028 155 ILE B CA  
6281 C C   . ILE B 155 ? 0.7231 1.0085 0.6238 0.1238  0.0382  0.0028  155 ILE B C   
6282 O O   . ILE B 155 ? 0.7234 1.0471 0.6277 0.1259  0.0402  0.0047  155 ILE B O   
6283 C CB  . ILE B 155 ? 0.7074 0.9634 0.6038 0.1011  0.0369  -0.0063 155 ILE B CB  
6284 C CG1 . ILE B 155 ? 0.6876 0.9357 0.5848 0.0810  0.0359  -0.0115 155 ILE B CG1 
6285 C CG2 . ILE B 155 ? 0.6970 0.9858 0.5923 0.1082  0.0403  -0.0050 155 ILE B CG2 
6286 C CD1 . ILE B 155 ? 0.6902 0.9146 0.5809 0.0780  0.0358  -0.0149 155 ILE B CD1 
6287 N N   . SER B 156 ? 0.7351 0.9928 0.6298 0.1379  0.0381  0.0055  156 SER B N   
6288 C CA  . SER B 156 ? 0.7590 1.0266 0.6503 0.1577  0.0406  0.0115  156 SER B CA  
6289 C C   . SER B 156 ? 0.7921 1.0862 0.6901 0.1580  0.0405  0.0149  156 SER B C   
6290 O O   . SER B 156 ? 0.8067 1.1340 0.7054 0.1691  0.0430  0.0189  156 SER B O   
6291 C CB  . SER B 156 ? 0.7864 1.0128 0.6692 0.1688  0.0404  0.0131  156 SER B CB  
6292 O OG  . SER B 156 ? 0.8260 1.0564 0.7048 0.1863  0.0429  0.0193  156 SER B OG  
6293 N N   . PHE B 157 ? 0.7823 1.0631 0.6852 0.1461  0.0376  0.0133  157 PHE B N   
6294 C CA  . PHE B 157 ? 0.7460 1.0496 0.6554 0.1443  0.0371  0.0158  157 PHE B CA  
6295 C C   . PHE B 157 ? 0.7281 1.0749 0.6442 0.1329  0.0377  0.0137  157 PHE B C   
6296 O O   . PHE B 157 ? 0.7403 1.1215 0.6597 0.1393  0.0390  0.0172  157 PHE B O   
6297 C CB  . PHE B 157 ? 0.7326 1.0090 0.6449 0.1341  0.0339  0.0143  157 PHE B CB  
6298 C CG  . PHE B 157 ? 0.7450 1.0452 0.6646 0.1268  0.0330  0.0152  157 PHE B CG  
6299 C CD1 . PHE B 157 ? 0.7573 1.0656 0.6774 0.1391  0.0337  0.0209  157 PHE B CD1 
6300 C CD2 . PHE B 157 ? 0.7172 1.0311 0.6421 0.1076  0.0317  0.0103  157 PHE B CD2 
6301 C CE1 . PHE B 157 ? 0.7408 1.0719 0.6673 0.1325  0.0328  0.0215  157 PHE B CE1 
6302 C CE2 . PHE B 157 ? 0.7190 1.0546 0.6497 0.1004  0.0310  0.0106  157 PHE B CE2 
6303 C CZ  . PHE B 157 ? 0.7430 1.0881 0.6751 0.1128  0.0313  0.0162  157 PHE B CZ  
6304 N N   . GLU B 158 ? 0.6949 1.0397 0.6123 0.1160  0.0369  0.0079  158 GLU B N   
6305 C CA  . GLU B 158 ? 0.6969 1.0787 0.6189 0.1021  0.0380  0.0048  158 GLU B CA  
6306 C C   . GLU B 158 ? 0.7175 1.1388 0.6394 0.1129  0.0411  0.0075  158 GLU B C   
6307 O O   . GLU B 158 ? 0.6999 1.1619 0.6268 0.1072  0.0421  0.0073  158 GLU B O   
6308 C CB  . GLU B 158 ? 0.7069 1.0719 0.6270 0.0841  0.0375  -0.0014 158 GLU B CB  
6309 C CG  . GLU B 158 ? 0.6866 1.0816 0.6095 0.0655  0.0389  -0.0057 158 GLU B CG  
6310 C CD  . GLU B 158 ? 0.7243 1.1010 0.6425 0.0509  0.0396  -0.0112 158 GLU B CD  
6311 O OE1 . GLU B 158 ? 0.7164 1.1015 0.6348 0.0323  0.0405  -0.0155 158 GLU B OE1 
6312 O OE2 . GLU B 158 ? 0.7304 1.0833 0.6438 0.0580  0.0396  -0.0112 158 GLU B OE2 
6313 N N   . SER B 159 ? 0.7223 1.1324 0.6382 0.1286  0.0427  0.0099  159 SER B N   
6314 C CA  . SER B 159 ? 0.7476 1.1933 0.6624 0.1407  0.0459  0.0127  159 SER B CA  
6315 C C   . SER B 159 ? 0.7738 1.2434 0.6891 0.1595  0.0473  0.0196  159 SER B C   
6316 O O   . SER B 159 ? 0.7804 1.2954 0.6989 0.1634  0.0493  0.0215  159 SER B O   
6317 C CB  . SER B 159 ? 0.7345 1.1587 0.6413 0.1505  0.0475  0.0125  159 SER B CB  
6318 O OG  . SER B 159 ? 0.7294 1.1511 0.6364 0.1340  0.0474  0.0068  159 SER B OG  
6319 N N   . LYS B 160 ? 0.8108 1.2502 0.7222 0.1712  0.0465  0.0233  160 LYS B N   
6320 C CA  . LYS B 160 ? 0.8421 1.2982 0.7525 0.1894  0.0481  0.0303  160 LYS B CA  
6321 C C   . LYS B 160 ? 0.8415 1.3384 0.7611 0.1802  0.0470  0.0304  160 LYS B C   
6322 O O   . LYS B 160 ? 0.8689 1.4036 0.7897 0.1929  0.0490  0.0352  160 LYS B O   
6323 C CB  . LYS B 160 ? 0.8840 1.2959 0.7886 0.1985  0.0473  0.0332  160 LYS B CB  
6324 C CG  . LYS B 160 ? 0.9282 1.3529 0.8307 0.2163  0.0491  0.0406  160 LYS B CG  
6325 C CD  . LYS B 160 ? 0.9809 1.3676 0.8816 0.2156  0.0474  0.0418  160 LYS B CD  
6326 C CE  . LYS B 160 ? 1.0116 1.4211 0.9150 0.2237  0.0480  0.0474  160 LYS B CE  
6327 N NZ  . LYS B 160 ? 0.9931 1.3691 0.8964 0.2195  0.0460  0.0480  160 LYS B NZ  
6328 N N   . VAL B 161 ? 0.8291 1.3187 0.7546 0.1583  0.0441  0.0250  161 VAL B N   
6329 C CA  . VAL B 161 ? 0.8246 1.3487 0.7579 0.1465  0.0430  0.0239  161 VAL B CA  
6330 C C   . VAL B 161 ? 0.8350 1.4045 0.7725 0.1355  0.0444  0.0204  161 VAL B C   
6331 O O   . VAL B 161 ? 0.8446 1.4591 0.7870 0.1352  0.0450  0.0219  161 VAL B O   
6332 C CB  . VAL B 161 ? 0.7948 1.2912 0.7311 0.1277  0.0398  0.0194  161 VAL B CB  
6333 C CG1 . VAL B 161 ? 0.7467 1.2785 0.6899 0.1125  0.0389  0.0169  161 VAL B CG1 
6334 C CG2 . VAL B 161 ? 0.7838 1.2433 0.7171 0.1389  0.0385  0.0235  161 VAL B CG2 
6335 N N   . PHE B 162 ? 0.8345 1.3931 0.7695 0.1264  0.0452  0.0159  162 PHE B N   
6336 C CA  . PHE B 162 ? 0.8780 1.4768 0.8155 0.1165  0.0472  0.0127  162 PHE B CA  
6337 C C   . PHE B 162 ? 0.9000 1.5414 0.8377 0.1364  0.0499  0.0185  162 PHE B C   
6338 O O   . PHE B 162 ? 0.8598 1.5502 0.8024 0.1302  0.0511  0.0176  162 PHE B O   
6339 C CB  . PHE B 162 ? 0.9170 1.4910 0.8501 0.1071  0.0479  0.0080  162 PHE B CB  
6340 C CG  . PHE B 162 ? 0.9608 1.5735 0.8949 0.1005  0.0508  0.0056  162 PHE B CG  
6341 C CD1 . PHE B 162 ? 0.9773 1.6282 0.9165 0.0814  0.0514  0.0016  162 PHE B CD1 
6342 C CD2 . PHE B 162 ? 0.9907 1.6012 0.9201 0.1125  0.0530  0.0070  162 PHE B CD2 
6343 C CE1 . PHE B 162 ? 1.0129 1.7002 0.9528 0.0742  0.0544  -0.0007 162 PHE B CE1 
6344 C CE2 . PHE B 162 ? 0.9913 1.6383 0.9217 0.1063  0.0558  0.0049  162 PHE B CE2 
6345 C CZ  . PHE B 162 ? 0.9933 1.6793 0.9292 0.0868  0.0565  0.0011  162 PHE B CZ  
6346 N N   . HIS B 163 ? 0.9397 1.5622 0.8714 0.1604  0.0511  0.0245  163 HIS B N   
6347 C CA  . HIS B 163 ? 0.9806 1.6382 0.9101 0.1829  0.0542  0.0308  163 HIS B CA  
6348 C C   . HIS B 163 ? 0.9791 1.6652 0.9113 0.1953  0.0543  0.0367  163 HIS B C   
6349 O O   . HIS B 163 ? 0.9680 1.6900 0.8988 0.2140  0.0570  0.0423  163 HIS B O   
6350 C CB  . HIS B 163 ? 1.0224 1.6462 0.9418 0.2035  0.0563  0.0344  163 HIS B CB  
6351 C CG  . HIS B 163 ? 1.0757 1.6980 0.9924 0.1986  0.0579  0.0306  163 HIS B CG  
6352 N ND1 . HIS B 163 ? 1.0922 1.6704 1.0052 0.1884  0.0566  0.0259  163 HIS B ND1 
6353 C CD2 . HIS B 163 ? 1.0831 1.7461 1.0004 0.2028  0.0609  0.0311  163 HIS B CD2 
6354 C CE1 . HIS B 163 ? 1.0989 1.6875 1.0098 0.1864  0.0586  0.0235  163 HIS B CE1 
6355 N NE2 . HIS B 163 ? 1.1091 1.7495 1.0228 0.1949  0.0613  0.0266  163 HIS B NE2 
6356 N N   . LYS B 164 ? 0.9676 1.6387 0.9033 0.1858  0.0514  0.0357  164 LYS B N   
6357 C CA  . LYS B 164 ? 0.9591 1.6597 0.8981 0.1940  0.0511  0.0404  164 LYS B CA  
6358 C C   . LYS B 164 ? 0.9350 1.6818 0.8834 0.1730  0.0497  0.0357  164 LYS B C   
6359 O O   . LYS B 164 ? 0.9074 1.7028 0.8595 0.1803  0.0505  0.0392  164 LYS B O   
6360 C CB  . LYS B 164 ? 0.9896 1.6479 0.9262 0.1973  0.0492  0.0427  164 LYS B CB  
6361 C CG  . LYS B 164 ? 1.0271 1.6542 0.9535 0.2236  0.0515  0.0498  164 LYS B CG  
6362 C CD  . LYS B 164 ? 1.0582 1.6511 0.9831 0.2253  0.0499  0.0521  164 LYS B CD  
6363 C CE  . LYS B 164 ? 1.1031 1.6574 1.0160 0.2484  0.0527  0.0583  164 LYS B CE  
6364 N NZ  . LYS B 164 ? 1.1317 1.6468 1.0428 0.2463  0.0510  0.0594  164 LYS B NZ  
6365 N N   . LEU B 165 ? 0.9383 1.6691 0.8896 0.1471  0.0478  0.0279  165 LEU B N   
6366 C CA  . LEU B 165 ? 0.9252 1.6953 0.8830 0.1239  0.0473  0.0219  165 LEU B CA  
6367 C C   . LEU B 165 ? 0.9341 1.7508 0.8933 0.1250  0.0501  0.0215  165 LEU B C   
6368 O O   . LEU B 165 ? 0.9282 1.7935 0.8928 0.1125  0.0505  0.0188  165 LEU B O   
6369 C CB  . LEU B 165 ? 0.9106 1.6458 0.8679 0.0978  0.0458  0.0138  165 LEU B CB  
6370 C CG  . LEU B 165 ? 0.8924 1.6086 0.8517 0.0833  0.0430  0.0110  165 LEU B CG  
6371 C CD1 . LEU B 165 ? 0.8761 1.5761 0.8352 0.1018  0.0415  0.0176  165 LEU B CD1 
6372 C CD2 . LEU B 165 ? 0.8436 1.5124 0.7994 0.0653  0.0421  0.0048  165 LEU B CD2 
6373 N N   . LYS B 166 ? 0.9760 1.7777 0.9300 0.1397  0.0522  0.0240  166 LYS B N   
6374 C CA  . LYS B 166 ? 0.9961 1.8396 0.9503 0.1467  0.0552  0.0252  166 LYS B CA  
6375 C C   . LYS B 166 ? 1.0000 1.8918 0.9562 0.1686  0.0566  0.0327  166 LYS B C   
6376 O O   . LYS B 166 ? 0.9618 1.9082 0.9244 0.1604  0.0568  0.0315  166 LYS B O   
6377 C CB  . LYS B 166 ? 1.0422 1.8504 0.9889 0.1595  0.0570  0.0266  166 LYS B CB  
6378 C CG  . LYS B 166 ? 1.0877 1.9279 1.0344 0.1583  0.0601  0.0250  166 LYS B CG  
6379 C CD  . LYS B 166 ? 1.0914 1.8916 1.0296 0.1719  0.0617  0.0264  166 LYS B CD  
6380 C CE  . LYS B 166 ? 1.0925 1.9086 1.0304 0.1611  0.0639  0.0221  166 LYS B CE  
6381 N NZ  . LYS B 166 ? 1.1068 1.8771 1.0363 0.1702  0.0649  0.0221  166 LYS B NZ  
6382 N N   . LYS B 167 ? 1.0264 1.8975 0.9760 0.1963  0.0578  0.0403  167 LYS B N   
6383 C CA  . LYS B 167 ? 1.0559 1.9693 1.0047 0.2214  0.0600  0.0485  167 LYS B CA  
6384 C C   . LYS B 167 ? 1.0814 2.0129 1.0343 0.2228  0.0580  0.0514  167 LYS B C   
6385 O O   . LYS B 167 ? 1.1487 2.0895 1.0975 0.2477  0.0596  0.0595  167 LYS B O   
6386 C CB  . LYS B 167 ? 1.0973 1.9820 1.0350 0.2516  0.0632  0.0558  167 LYS B CB  
6387 C CG  . LYS B 167 ? 1.0912 1.9843 1.0253 0.2568  0.0662  0.0550  167 LYS B CG  
6388 C CD  . LYS B 167 ? 1.0777 1.9839 1.0029 0.2907  0.0705  0.0641  167 LYS B CD  
6389 C CE  . LYS B 167 ? 1.0634 1.9891 0.9864 0.2948  0.0736  0.0632  167 LYS B CE  
6390 N NZ  . LYS B 167 ? 1.0469 1.9916 0.9609 0.3286  0.0783  0.0723  167 LYS B NZ  
6391 N N   . MET B 168 ? 1.0753 2.0101 1.0351 0.1960  0.0550  0.0446  168 MET B N   
6392 C CA  . MET B 168 ? 1.0563 2.0245 1.0219 0.1918  0.0531  0.0455  168 MET B CA  
6393 C C   . MET B 168 ? 1.0505 2.0551 1.0238 0.1613  0.0519  0.0368  168 MET B C   
6394 O O   . MET B 168 ? 1.0526 2.0502 1.0260 0.1448  0.0527  0.0307  168 MET B O   
6395 C CB  . MET B 168 ? 1.0597 1.9804 1.0233 0.1912  0.0506  0.0464  168 MET B CB  
6396 C CG  . MET B 168 ? 1.0940 1.9863 1.0493 0.2215  0.0523  0.0557  168 MET B CG  
6397 S SD  . MET B 168 ? 1.1590 1.9905 1.1115 0.2186  0.0497  0.0561  168 MET B SD  
6398 C CE  . MET B 168 ? 1.1794 1.9925 1.1206 0.2562  0.0533  0.0678  168 MET B CE  
6399 N N   . LYS B 169 ? 1.0930 2.1360 1.0719 0.1536  0.0503  0.0362  169 LYS B N   
6400 C CA  . LYS B 169 ? 1.1364 2.2220 1.1217 0.1255  0.0497  0.0282  169 LYS B CA  
6401 C C   . LYS B 169 ? 1.1107 2.1558 1.0946 0.0956  0.0489  0.0186  169 LYS B C   
6402 O O   . LYS B 169 ? 1.1032 2.1735 1.0892 0.0726  0.0500  0.0116  169 LYS B O   
6403 C CB  . LYS B 169 ? 1.1599 2.2837 1.1500 0.1220  0.0478  0.0289  169 LYS B CB  
6404 C CG  . LYS B 169 ? 1.1630 2.3515 1.1593 0.1012  0.0480  0.0230  169 LYS B CG  
6405 C CD  . LYS B 169 ? 1.1384 2.3667 1.1391 0.1008  0.0460  0.0244  169 LYS B CD  
6406 C CE  . LYS B 169 ? 1.1086 2.4069 1.1150 0.0817  0.0465  0.0189  169 LYS B CE  
6407 N NZ  . LYS B 169 ? 1.1230 2.4640 1.1336 0.0822  0.0445  0.0203  169 LYS B NZ  
6408 N N   . TYR B 170 ? 1.0754 2.0578 1.0551 0.0971  0.0474  0.0188  170 TYR B N   
6409 C CA  . TYR B 170 ? 1.0228 1.9651 1.0010 0.0711  0.0459  0.0110  170 TYR B CA  
6410 C C   . TYR B 170 ? 0.9731 1.9086 0.9491 0.0485  0.0477  0.0032  170 TYR B C   
6411 O O   . TYR B 170 ? 0.9201 1.8558 0.8958 0.0220  0.0476  -0.0043 170 TYR B O   
6412 C CB  . TYR B 170 ? 1.0455 1.9239 1.0195 0.0813  0.0441  0.0139  170 TYR B CB  
6413 C CG  . TYR B 170 ? 1.0617 1.9413 1.0368 0.0993  0.0426  0.0208  170 TYR B CG  
6414 C CD1 . TYR B 170 ? 1.0635 1.9101 1.0383 0.0914  0.0401  0.0194  170 TYR B CD1 
6415 C CD2 . TYR B 170 ? 1.0877 2.0019 1.0632 0.1247  0.0439  0.0289  170 TYR B CD2 
6416 C CE1 . TYR B 170 ? 1.0782 1.9255 1.0536 0.1076  0.0390  0.0258  170 TYR B CE1 
6417 C CE2 . TYR B 170 ? 1.0961 2.0106 1.0713 0.1415  0.0429  0.0354  170 TYR B CE2 
6418 C CZ  . TYR B 170 ? 1.1157 1.9966 1.0911 0.1324  0.0405  0.0338  170 TYR B CZ  
6419 O OH  . TYR B 170 ? 1.1447 2.0252 1.1195 0.1488  0.0398  0.0405  170 TYR B OH  
6420 N N   . LEU B 171 ? 0.9529 1.8814 0.9263 0.0593  0.0497  0.0051  171 LEU B N   
6421 C CA  . LEU B 171 ? 0.9693 1.8852 0.9395 0.0403  0.0517  -0.0015 171 LEU B CA  
6422 C C   . LEU B 171 ? 0.9908 1.9522 0.9625 0.0453  0.0548  -0.0005 171 LEU B C   
6423 O O   . LEU B 171 ? 0.9827 1.9437 0.9529 0.0695  0.0558  0.0056  171 LEU B O   
6424 C CB  . LEU B 171 ? 0.9726 1.8222 0.9367 0.0445  0.0510  -0.0015 171 LEU B CB  
6425 C CG  . LEU B 171 ? 0.9714 1.7869 0.9306 0.0199  0.0519  -0.0093 171 LEU B CG  
6426 C CD1 . LEU B 171 ? 0.9484 1.7670 0.9078 -0.0058 0.0513  -0.0158 171 LEU B CD1 
6427 C CD2 . LEU B 171 ? 0.9733 1.7258 0.9273 0.0284  0.0504  -0.0080 171 LEU B CD2 
6428 N N   . VAL B 172 ? 1.0132 2.0134 0.9869 0.0221  0.0565  -0.0068 172 VAL B N   
6429 C CA  . VAL B 172 ? 1.0171 2.0653 0.9927 0.0231  0.0597  -0.0068 172 VAL B CA  
6430 C C   . VAL B 172 ? 1.0596 2.0924 1.0306 -0.0016 0.0624  -0.0145 172 VAL B C   
6431 O O   . VAL B 172 ? 1.0893 2.1219 1.0586 -0.0294 0.0630  -0.0219 172 VAL B O   
6432 C CB  . VAL B 172 ? 0.9696 2.0906 0.9520 0.0184  0.0600  -0.0069 172 VAL B CB  
6433 C CG1 . VAL B 172 ? 0.9424 2.1157 0.9273 0.0209  0.0633  -0.0063 172 VAL B CG1 
6434 C CG2 . VAL B 172 ? 0.9174 2.0537 0.9035 0.0429  0.0575  0.0009  172 VAL B CG2 
6435 N N   . GLU B 173 ? 1.1000 2.1184 1.0677 0.0085  0.0643  -0.0127 173 GLU B N   
6436 C CA  . GLU B 173 ? 1.1788 2.1837 1.1414 -0.0124 0.0674  -0.0192 173 GLU B CA  
6437 C C   . GLU B 173 ? 1.2398 2.3057 1.2054 -0.0323 0.0705  -0.0239 173 GLU B C   
6438 O O   . GLU B 173 ? 1.2276 2.3508 1.1998 -0.0216 0.0707  -0.0203 173 GLU B O   
6439 C CB  . GLU B 173 ? 1.1900 2.1705 1.1488 0.0057  0.0687  -0.0156 173 GLU B CB  
6440 C CG  . GLU B 173 ? 1.2029 2.1440 1.1541 -0.0124 0.0708  -0.0215 173 GLU B CG  
6441 C CD  . GLU B 173 ? 1.2304 2.1768 1.1792 -0.0012 0.0737  -0.0194 173 GLU B CD  
6442 O OE1 . GLU B 173 ? 1.2257 2.1983 1.1776 0.0235  0.0738  -0.0129 173 GLU B OE1 
6443 O OE2 . GLU B 173 ? 1.2418 2.1654 1.1846 -0.0168 0.0760  -0.0242 173 GLU B OE2 
6444 N N   . VAL B 174 ? 1.3541 2.4079 1.3142 -0.0613 0.0732  -0.0319 174 VAL B N   
6445 C CA  . VAL B 174 ? 1.4789 2.5867 1.4402 -0.0836 0.0769  -0.0373 174 VAL B CA  
6446 C C   . VAL B 174 ? 1.5710 2.6546 1.5234 -0.1068 0.0813  -0.0439 174 VAL B C   
6447 O O   . VAL B 174 ? 1.6324 2.6968 1.5781 -0.1343 0.0830  -0.0512 174 VAL B O   
6448 C CB  . VAL B 174 ? 1.4696 2.6130 1.4341 -0.1020 0.0760  -0.0415 174 VAL B CB  
6449 C CG1 . VAL B 174 ? 1.4499 2.5414 1.4072 -0.1215 0.0751  -0.0470 174 VAL B CG1 
6450 C CG2 . VAL B 174 ? 1.4865 2.6922 1.4528 -0.1239 0.0798  -0.0467 174 VAL B CG2 
6451 N N   . GLN B 175 ? 1.6270 2.7104 1.5784 -0.0947 0.0833  -0.0411 175 GLN B N   
6452 C CA  . GLN B 175 ? 1.6997 2.7642 1.6427 -0.1133 0.0879  -0.0463 175 GLN B CA  
6453 C C   . GLN B 175 ? 1.7915 2.7853 1.7238 -0.1271 0.0880  -0.0506 175 GLN B C   
6454 O O   . GLN B 175 ? 1.8174 2.7735 1.7492 -0.1209 0.0843  -0.0493 175 GLN B O   
6455 C CB  . GLN B 175 ? 1.6675 2.7866 1.6106 -0.1399 0.0924  -0.0524 175 GLN B CB  
6456 C CG  . GLN B 175 ? 1.6359 2.8210 1.5873 -0.1263 0.0938  -0.0483 175 GLN B CG  
6457 C CD  . GLN B 175 ? 1.6234 2.8512 1.5727 -0.1535 0.0993  -0.0546 175 GLN B CD  
6458 O OE1 . GLN B 175 ? 1.6323 2.8509 1.5745 -0.1847 0.1021  -0.0625 175 GLN B OE1 
6459 N NE2 . GLN B 175 ? 1.5808 2.8550 1.5351 -0.1420 0.1015  -0.0512 175 GLN B NE2 
6460 N N   . ASP B 176 ? 1.8604 2.8375 1.7838 -0.1453 0.0926  -0.0554 176 ASP B N   
6461 C CA  . ASP B 176 ? 1.9342 2.8451 1.8460 -0.1565 0.0936  -0.0589 176 ASP B CA  
6462 C C   . ASP B 176 ? 1.9917 2.9030 1.8926 -0.1898 0.0998  -0.0670 176 ASP B C   
6463 O O   . ASP B 176 ? 1.9814 2.9370 1.8835 -0.1992 0.1038  -0.0687 176 ASP B O   
6464 C CB  . ASP B 176 ? 1.9167 2.7899 1.8261 -0.1354 0.0927  -0.0545 176 ASP B CB  
6465 C CG  . ASP B 176 ? 1.9028 2.7642 1.8197 -0.1040 0.0871  -0.0470 176 ASP B CG  
6466 O OD1 . ASP B 176 ? 1.9409 2.7815 1.8595 -0.1010 0.0834  -0.0463 176 ASP B OD1 
6467 O OD2 . ASP B 176 ? 1.8793 2.7506 1.7993 -0.0823 0.0868  -0.0420 176 ASP B OD2 
6468 N N   . GLU B 177 ? 2.0562 2.9195 1.9457 -0.2079 0.1013  -0.0718 177 GLU B N   
6469 C CA  . GLU B 177 ? 2.0510 2.8678 1.9393 -0.2005 0.0969  -0.0705 177 GLU B CA  
6470 C C   . GLU B 177 ? 2.0645 2.8506 1.9394 -0.2291 0.1005  -0.0778 177 GLU B C   
6471 O O   . GLU B 177 ? 2.0435 2.7809 1.9132 -0.2270 0.0984  -0.0778 177 GLU B O   
6472 C CB  . GLU B 177 ? 2.0436 2.8086 1.9299 -0.1788 0.0942  -0.0658 177 GLU B CB  
6473 C CG  . GLU B 177 ? 1.9959 2.7303 1.8870 -0.1610 0.0881  -0.0618 177 GLU B CG  
6474 C CD  . GLU B 177 ? 1.9622 2.6302 1.8436 -0.1605 0.0875  -0.0624 177 GLU B CD  
6475 O OE1 . GLU B 177 ? 1.9567 2.6008 1.8319 -0.1574 0.0894  -0.0621 177 GLU B OE1 
6476 O OE2 . GLU B 177 ? 1.9169 2.5576 1.7967 -0.1626 0.0850  -0.0631 177 GLU B OE2 
6477 N N   . VAL B 178 ? 2.0780 2.8931 1.9466 -0.2558 0.1062  -0.0841 178 VAL B N   
6478 C CA  . VAL B 178 ? 2.0541 2.8352 1.9056 -0.2847 0.1117  -0.0914 178 VAL B CA  
6479 C C   . VAL B 178 ? 2.0109 2.7890 1.8604 -0.2973 0.1104  -0.0951 178 VAL B C   
6480 O O   . VAL B 178 ? 2.0103 2.7703 1.8451 -0.3238 0.1157  -0.1019 178 VAL B O   
6481 C CB  . VAL B 178 ? 2.0748 2.8821 1.9173 -0.3107 0.1195  -0.0973 178 VAL B CB  
6482 C CG1 . VAL B 178 ? 2.0614 2.8125 1.8829 -0.3307 0.1259  -0.1022 178 VAL B CG1 
6483 C CG2 . VAL B 178 ? 2.0247 2.8651 1.8759 -0.2962 0.1197  -0.0930 178 VAL B CG2 
6484 N N   . LYS B 179 ? 1.9089 2.7030 1.7719 -0.2780 0.1038  -0.0904 179 LYS B N   
6485 C CA  . LYS B 179 ? 1.7808 2.5687 1.6428 -0.2858 0.1018  -0.0929 179 LYS B CA  
6486 C C   . LYS B 179 ? 1.7518 2.5353 1.6271 -0.2576 0.0941  -0.0858 179 LYS B C   
6487 O O   . LYS B 179 ? 1.7408 2.5712 1.6285 -0.2488 0.0907  -0.0832 179 LYS B O   
6488 C CB  . LYS B 179 ? 1.7184 2.5609 1.5809 -0.3093 0.1046  -0.0988 179 LYS B CB  
6489 C CG  . LYS B 179 ? 1.6607 2.5712 1.5352 -0.3050 0.1046  -0.0970 179 LYS B CG  
6490 C CD  . LYS B 179 ? 1.5843 2.5400 1.4758 -0.2847 0.0984  -0.0917 179 LYS B CD  
6491 C CE  . LYS B 179 ? 1.5359 2.5401 1.4401 -0.2649 0.0970  -0.0859 179 LYS B CE  
6492 N NZ  . LYS B 179 ? 1.4817 2.4483 1.3879 -0.2383 0.0948  -0.0791 179 LYS B NZ  
6493 N N   . PRO B 180 ? 1.7469 2.4740 1.6189 -0.2435 0.0915  -0.0825 180 PRO B N   
6494 C CA  . PRO B 180 ? 1.6799 2.3978 1.5633 -0.2165 0.0847  -0.0756 180 PRO B CA  
6495 C C   . PRO B 180 ? 1.6116 2.3127 1.4940 -0.2206 0.0822  -0.0769 180 PRO B C   
6496 O O   . PRO B 180 ? 1.5853 2.3146 1.4788 -0.2086 0.0780  -0.0734 180 PRO B O   
6497 C CB  . PRO B 180 ? 1.7153 2.3824 1.5949 -0.2012 0.0837  -0.0721 180 PRO B CB  
6498 C CG  . PRO B 180 ? 1.7601 2.3966 1.6235 -0.2231 0.0898  -0.0779 180 PRO B CG  
6499 C CD  . PRO B 180 ? 1.7855 2.4560 1.6429 -0.2512 0.0951  -0.0848 180 PRO B CD  
6500 N N   . ARG B 181 ? 1.5999 2.2547 1.4685 -0.2363 0.0850  -0.0814 181 ARG B N   
6501 C CA  . ARG B 181 ? 1.5858 2.2207 1.4506 -0.2432 0.0837  -0.0835 181 ARG B CA  
6502 C C   . ARG B 181 ? 1.5241 2.1112 1.3906 -0.2239 0.0791  -0.0786 181 ARG B C   
6503 O O   . ARG B 181 ? 1.5663 2.1097 1.4215 -0.2328 0.0807  -0.0813 181 ARG B O   
6504 C CB  . ARG B 181 ? 1.5939 2.2805 1.4682 -0.2462 0.0815  -0.0841 181 ARG B CB  
6505 C CG  . ARG B 181 ? 1.6166 2.2883 1.4830 -0.2626 0.0823  -0.0889 181 ARG B CG  
6506 C CD  . ARG B 181 ? 1.6492 2.3745 1.5168 -0.2817 0.0842  -0.0940 181 ARG B CD  
6507 N NE  . ARG B 181 ? 1.6857 2.3907 1.5359 -0.3109 0.0898  -0.1026 181 ARG B NE  
6508 C CZ  . ARG B 181 ? 1.6879 2.3709 1.5323 -0.3171 0.0891  -0.1049 181 ARG B CZ  
6509 N NH1 . ARG B 181 ? 1.6869 2.3663 1.5424 -0.2966 0.0830  -0.0992 181 ARG B NH1 
6510 N NH2 . ARG B 181 ? 1.7059 2.3694 1.5325 -0.3441 0.0951  -0.1130 181 ARG B NH2 
6511 N N   . GLY B 182 ? 1.3933 1.9890 1.2732 -0.1978 0.0738  -0.0715 182 GLY B N   
6512 C CA  . GLY B 182 ? 1.2405 1.7950 1.1230 -0.1793 0.0693  -0.0667 182 GLY B CA  
6513 C C   . GLY B 182 ? 1.1382 1.6929 1.0304 -0.1531 0.0656  -0.0598 182 GLY B C   
6514 O O   . GLY B 182 ? 1.1072 1.7023 1.0073 -0.1448 0.0653  -0.0573 182 GLY B O   
6515 N N   . VAL B 183 ? 1.0754 1.5853 0.9665 -0.1400 0.0629  -0.0567 183 VAL B N   
6516 C CA  . VAL B 183 ? 1.0318 1.5355 0.9302 -0.1157 0.0595  -0.0505 183 VAL B CA  
6517 C C   . VAL B 183 ? 0.9967 1.5039 0.9051 -0.0967 0.0545  -0.0449 183 VAL B C   
6518 O O   . VAL B 183 ? 1.0330 1.5175 0.9406 -0.0982 0.0526  -0.0449 183 VAL B O   
6519 C CB  . VAL B 183 ? 1.0304 1.4854 0.9210 -0.1122 0.0599  -0.0505 183 VAL B CB  
6520 C CG1 . VAL B 183 ? 1.0585 1.4702 0.9422 -0.1185 0.0591  -0.0523 183 VAL B CG1 
6521 C CG2 . VAL B 183 ? 0.9905 1.4385 0.8877 -0.0879 0.0564  -0.0447 183 VAL B CG2 
6522 N N   . LEU B 184 ? 0.9468 1.4829 0.8638 -0.0787 0.0529  -0.0399 184 LEU B N   
6523 C CA  . LEU B 184 ? 0.9050 1.4457 0.8303 -0.0590 0.0489  -0.0339 184 LEU B CA  
6524 C C   . LEU B 184 ? 0.8952 1.3889 0.8194 -0.0441 0.0461  -0.0304 184 LEU B C   
6525 O O   . LEU B 184 ? 0.9049 1.3811 0.8262 -0.0369 0.0465  -0.0297 184 LEU B O   
6526 C CB  . LEU B 184 ? 0.8897 1.4750 0.8221 -0.0435 0.0490  -0.0293 184 LEU B CB  
6527 C CG  . LEU B 184 ? 0.8872 1.4831 0.8268 -0.0221 0.0459  -0.0226 184 LEU B CG  
6528 C CD1 . LEU B 184 ? 0.8865 1.5219 0.8309 -0.0290 0.0456  -0.0231 184 LEU B CD1 
6529 C CD2 . LEU B 184 ? 0.8741 1.4874 0.8165 -0.0002 0.0462  -0.0170 184 LEU B CD2 
6530 N N   . ASN B 185 ? 0.8614 1.3359 0.7877 -0.0401 0.0432  -0.0286 185 ASN B N   
6531 C CA  . ASN B 185 ? 0.8663 1.3015 0.7928 -0.0250 0.0403  -0.0249 185 ASN B CA  
6532 C C   . ASN B 185 ? 0.8219 1.2675 0.7553 -0.0062 0.0377  -0.0187 185 ASN B C   
6533 O O   . ASN B 185 ? 0.8807 1.3460 0.8180 -0.0087 0.0370  -0.0180 185 ASN B O   
6534 C CB  . ASN B 185 ? 0.9001 1.2951 0.8214 -0.0358 0.0394  -0.0280 185 ASN B CB  
6535 C CG  . ASN B 185 ? 0.9400 1.3139 0.8522 -0.0499 0.0421  -0.0330 185 ASN B CG  
6536 O OD1 . ASN B 185 ? 0.9830 1.3524 0.8891 -0.0680 0.0444  -0.0377 185 ASN B OD1 
6537 N ND2 . ASN B 185 ? 0.8994 1.2596 0.8094 -0.0416 0.0423  -0.0320 185 ASN B ND2 
6538 N N   . ILE B 186 ? 0.7770 1.2086 0.7109 0.0122  0.0366  -0.0143 186 ILE B N   
6539 C CA  . ILE B 186 ? 0.7649 1.1960 0.7028 0.0308  0.0347  -0.0081 186 ILE B CA  
6540 C C   . ILE B 186 ? 0.7831 1.1688 0.7192 0.0327  0.0321  -0.0077 186 ILE B C   
6541 O O   . ILE B 186 ? 0.8318 1.1873 0.7642 0.0380  0.0316  -0.0076 186 ILE B O   
6542 C CB  . ILE B 186 ? 0.7502 1.1904 0.6875 0.0510  0.0357  -0.0034 186 ILE B CB  
6543 C CG1 . ILE B 186 ? 0.7601 1.2443 0.6986 0.0489  0.0385  -0.0043 186 ILE B CG1 
6544 C CG2 . ILE B 186 ? 0.7299 1.1699 0.6694 0.0702  0.0346  0.0031  186 ILE B CG2 
6545 C CD1 . ILE B 186 ? 0.8044 1.3344 0.7482 0.0444  0.0390  -0.0038 186 ILE B CD1 
6546 N N   . ILE B 187 ? 0.7869 1.1689 0.7255 0.0275  0.0306  -0.0075 187 ILE B N   
6547 C CA  . ILE B 187 ? 0.7926 1.1359 0.7305 0.0301  0.0282  -0.0065 187 ILE B CA  
6548 C C   . ILE B 187 ? 0.8003 1.1428 0.7410 0.0490  0.0271  0.0000  187 ILE B C   
6549 O O   . ILE B 187 ? 0.7650 1.1367 0.7094 0.0542  0.0275  0.0030  187 ILE B O   
6550 C CB  . ILE B 187 ? 0.8081 1.1447 0.7462 0.0143  0.0275  -0.0098 187 ILE B CB  
6551 C CG1 . ILE B 187 ? 0.8086 1.1480 0.7417 -0.0050 0.0297  -0.0163 187 ILE B CG1 
6552 C CG2 . ILE B 187 ? 0.8036 1.1010 0.7410 0.0169  0.0250  -0.0088 187 ILE B CG2 
6553 C CD1 . ILE B 187 ? 0.8745 1.1854 0.8018 -0.0075 0.0302  -0.0188 187 ILE B CD1 
6554 N N   . PRO B 188 ? 0.8389 1.1480 0.7770 0.0593  0.0259  0.0021  188 PRO B N   
6555 C CA  . PRO B 188 ? 0.8854 1.1871 0.8243 0.0757  0.0254  0.0081  188 PRO B CA  
6556 C C   . PRO B 188 ? 0.9473 1.2438 0.8897 0.0710  0.0238  0.0090  188 PRO B C   
6557 O O   . PRO B 188 ? 0.9313 1.2141 0.8742 0.0568  0.0225  0.0050  188 PRO B O   
6558 C CB  . PRO B 188 ? 0.8807 1.1439 0.8148 0.0824  0.0247  0.0083  188 PRO B CB  
6559 C CG  . PRO B 188 ? 0.8508 1.1081 0.7820 0.0728  0.0250  0.0032  188 PRO B CG  
6560 C CD  . PRO B 188 ? 0.8393 1.1156 0.7730 0.0555  0.0253  -0.0009 188 PRO B CD  
6561 N N   . LYS B 189 ? 1.0553 1.3631 0.9993 0.0836  0.0242  0.0146  189 LYS B N   
6562 C CA  . LYS B 189 ? 1.1274 1.4305 1.0744 0.0815  0.0228  0.0163  189 LYS B CA  
6563 C C   . LYS B 189 ? 1.1906 1.4734 1.1352 0.0979  0.0231  0.0224  189 LYS B C   
6564 O O   . LYS B 189 ? 1.1996 1.4706 1.1394 0.1102  0.0245  0.0247  189 LYS B O   
6565 C CB  . LYS B 189 ? 1.1361 1.4795 1.0873 0.0778  0.0234  0.0168  189 LYS B CB  
6566 C CG  . LYS B 189 ? 1.1693 1.5099 1.1234 0.0640  0.0218  0.0142  189 LYS B CG  
6567 C CD  . LYS B 189 ? 1.2376 1.6007 1.1949 0.0711  0.0219  0.0188  189 LYS B CD  
6568 C CE  . LYS B 189 ? 1.2591 1.6027 1.2179 0.0642  0.0202  0.0184  189 LYS B CE  
6569 N NZ  . LYS B 189 ? 1.2422 1.5963 1.2028 0.0760  0.0204  0.0245  189 LYS B NZ  
6570 N N   . GLN B 190 ? 1.2711 1.5484 1.2182 0.0976  0.0222  0.0247  190 GLN B N   
6571 C CA  . GLN B 190 ? 1.3390 1.5971 1.2830 0.1118  0.0229  0.0306  190 GLN B CA  
6572 C C   . GLN B 190 ? 1.3485 1.6258 1.2886 0.1304  0.0259  0.0364  190 GLN B C   
6573 O O   . GLN B 190 ? 1.4203 1.7265 1.3624 0.1360  0.0269  0.0399  190 GLN B O   
6574 C CB  . GLN B 190 ? 1.3759 1.6327 1.3237 0.1078  0.0218  0.0323  190 GLN B CB  
6575 C CG  . GLN B 190 ? 1.3966 1.6281 1.3467 0.0932  0.0192  0.0279  190 GLN B CG  
6576 C CD  . GLN B 190 ? 1.4430 1.6367 1.3899 0.0980  0.0188  0.0296  190 GLN B CD  
6577 O OE1 . GLN B 190 ? 1.4750 1.6602 1.4180 0.1114  0.0206  0.0349  190 GLN B OE1 
6578 N NE2 . GLN B 190 ? 1.4116 1.5826 1.3593 0.0868  0.0167  0.0252  190 GLN B NE2 
6579 N N   . ASP B 191 ? 1.3263 1.5878 1.2600 0.1403  0.0276  0.0373  191 ASP B N   
6580 C CA  . ASP B 191 ? 1.3269 1.6017 1.2545 0.1598  0.0311  0.0430  191 ASP B CA  
6581 C C   . ASP B 191 ? 1.2894 1.6087 1.2200 0.1610  0.0321  0.0425  191 ASP B C   
6582 O O   . ASP B 191 ? 1.3425 1.6781 1.2683 0.1777  0.0351  0.0472  191 ASP B O   
6583 C CB  . ASP B 191 ? 1.3588 1.6307 1.2830 0.1736  0.0330  0.0502  191 ASP B CB  
6584 C CG  . ASP B 191 ? 1.3897 1.6449 1.3024 0.1942  0.0372  0.0558  191 ASP B CG  
6585 O OD1 . ASP B 191 ? 1.4163 1.6328 1.3226 0.1949  0.0376  0.0549  191 ASP B OD1 
6586 O OD2 . ASP B 191 ? 1.3245 1.6052 1.2337 0.2098  0.0402  0.0612  191 ASP B OD2 
6587 N N   . ASN B 192 ? 1.1887 1.5273 1.1263 0.1433  0.0299  0.0368  192 ASN B N   
6588 C CA  . ASN B 192 ? 1.1184 1.5002 1.0591 0.1409  0.0308  0.0353  192 ASN B CA  
6589 C C   . ASN B 192 ? 1.0367 1.4203 0.9799 0.1222  0.0295  0.0277  192 ASN B C   
6590 O O   . ASN B 192 ? 1.0064 1.3563 0.9473 0.1156  0.0284  0.0243  192 ASN B O   
6591 C CB  . ASN B 192 ? 1.1281 1.5472 1.0740 0.1399  0.0306  0.0374  192 ASN B CB  
6592 C CG  . ASN B 192 ? 1.1524 1.6020 1.0957 0.1603  0.0334  0.0443  192 ASN B CG  
6593 O OD1 . ASN B 192 ? 1.1374 1.5985 1.0772 0.1701  0.0355  0.0455  192 ASN B OD1 
6594 N ND2 . ASN B 192 ? 1.1708 1.6345 1.1153 0.1676  0.0336  0.0490  192 ASN B ND2 
6595 N N   . PHE B 193 ? 0.9319 1.3552 0.8791 0.1139  0.0300  0.0252  193 PHE B N   
6596 C CA  . PHE B 193 ? 0.8690 1.2961 0.8173 0.0954  0.0296  0.0181  193 PHE B CA  
6597 C C   . PHE B 193 ? 0.8117 1.2671 0.7646 0.0778  0.0290  0.0140  193 PHE B C   
6598 O O   . PHE B 193 ? 0.8116 1.2866 0.7676 0.0804  0.0285  0.0167  193 PHE B O   
6599 C CB  . PHE B 193 ? 0.8418 1.2870 0.7877 0.1014  0.0318  0.0179  193 PHE B CB  
6600 C CG  . PHE B 193 ? 0.8042 1.3014 0.7533 0.1056  0.0335  0.0199  193 PHE B CG  
6601 C CD1 . PHE B 193 ? 0.7864 1.3154 0.7391 0.0876  0.0337  0.0146  193 PHE B CD1 
6602 C CD2 . PHE B 193 ? 0.8019 1.3166 0.7494 0.1276  0.0352  0.0270  193 PHE B CD2 
6603 C CE1 . PHE B 193 ? 0.7586 1.3386 0.7145 0.0906  0.0352  0.0161  193 PHE B CE1 
6604 C CE2 . PHE B 193 ? 0.7918 1.3575 0.7424 0.1324  0.0367  0.0291  193 PHE B CE2 
6605 C CZ  . PHE B 193 ? 0.7698 1.3697 0.7252 0.1135  0.0365  0.0235  193 PHE B CZ  
6606 N N   . ARG B 194 ? 0.8048 1.2614 0.7569 0.0598  0.0293  0.0075  194 ARG B N   
6607 C CA  . ARG B 194 ? 0.8004 1.2791 0.7546 0.0405  0.0293  0.0024  194 ARG B CA  
6608 C C   . ARG B 194 ? 0.8107 1.2998 0.7622 0.0258  0.0312  -0.0034 194 ARG B C   
6609 O O   . ARG B 194 ? 0.8502 1.3082 0.7975 0.0201  0.0314  -0.0064 194 ARG B O   
6610 C CB  . ARG B 194 ? 0.8045 1.2516 0.7580 0.0298  0.0275  0.0001  194 ARG B CB  
6611 C CG  . ARG B 194 ? 0.8459 1.3095 0.7994 0.0097  0.0279  -0.0052 194 ARG B CG  
6612 C CD  . ARG B 194 ? 0.8881 1.3163 0.8395 0.0008  0.0264  -0.0073 194 ARG B CD  
6613 N NE  . ARG B 194 ? 0.9431 1.3287 0.8927 0.0091  0.0251  -0.0054 194 ARG B NE  
6614 C CZ  . ARG B 194 ? 0.9160 1.2671 0.8618 -0.0004 0.0245  -0.0089 194 ARG B CZ  
6615 N NH1 . ARG B 194 ? 0.9160 1.2664 0.8578 -0.0184 0.0257  -0.0143 194 ARG B NH1 
6616 N NH2 . ARG B 194 ? 0.8993 1.2163 0.8440 0.0080  0.0231  -0.0069 194 ARG B NH2 
6617 N N   . ALA B 195 ? 0.8342 1.3684 0.7879 0.0201  0.0329  -0.0048 195 ALA B N   
6618 C CA  . ALA B 195 ? 0.8230 1.3723 0.7740 0.0058  0.0353  -0.0102 195 ALA B CA  
6619 C C   . ALA B 195 ? 0.8702 1.4208 0.8182 -0.0195 0.0362  -0.0174 195 ALA B C   
6620 O O   . ALA B 195 ? 0.8778 1.4606 0.8282 -0.0276 0.0364  -0.0188 195 ALA B O   
6621 C CB  . ALA B 195 ? 0.8032 1.4025 0.7577 0.0137  0.0369  -0.0078 195 ALA B CB  
6622 N N   . ILE B 196 ? 0.9396 1.4547 0.8813 -0.0318 0.0371  -0.0219 196 ILE B N   
6623 C CA  . ILE B 196 ? 0.9897 1.4989 0.9254 -0.0557 0.0389  -0.0288 196 ILE B CA  
6624 C C   . ILE B 196 ? 1.0487 1.5610 0.9779 -0.0708 0.0425  -0.0342 196 ILE B C   
6625 O O   . ILE B 196 ? 1.0804 1.5909 1.0095 -0.0622 0.0432  -0.0326 196 ILE B O   
6626 C CB  . ILE B 196 ? 0.9785 1.4411 0.9102 -0.0594 0.0374  -0.0298 196 ILE B CB  
6627 C CG1 . ILE B 196 ? 0.9940 1.4151 0.9218 -0.0529 0.0370  -0.0291 196 ILE B CG1 
6628 C CG2 . ILE B 196 ? 0.9859 1.4481 0.9236 -0.0473 0.0343  -0.0250 196 ILE B CG2 
6629 C CD1 . ILE B 196 ? 1.0015 1.3993 0.9193 -0.0706 0.0399  -0.0351 196 ILE B CD1 
6630 N N   . VAL B 197 ? 1.0763 1.5919 0.9988 -0.0933 0.0453  -0.0406 197 VAL B N   
6631 C CA  . VAL B 197 ? 1.0968 1.6131 1.0111 -0.1103 0.0495  -0.0462 197 VAL B CA  
6632 C C   . VAL B 197 ? 1.1409 1.6132 1.0432 -0.1261 0.0518  -0.0512 197 VAL B C   
6633 O O   . VAL B 197 ? 1.1364 1.5902 1.0361 -0.1308 0.0510  -0.0522 197 VAL B O   
6634 C CB  . VAL B 197 ? 1.0751 1.6415 0.9899 -0.1255 0.0523  -0.0501 197 VAL B CB  
6635 C CG1 . VAL B 197 ? 1.0591 1.6706 0.9846 -0.1088 0.0508  -0.0450 197 VAL B CG1 
6636 C CG2 . VAL B 197 ? 1.0561 1.6318 0.9688 -0.1398 0.0525  -0.0537 197 VAL B CG2 
6637 N N   . SER B 198 ? 1.1925 1.6483 1.0867 -0.1335 0.0550  -0.0540 198 SER B N   
6638 C CA  . SER B 198 ? 1.2608 1.6752 1.1414 -0.1479 0.0582  -0.0584 198 SER B CA  
6639 C C   . SER B 198 ? 1.3220 1.7493 1.1917 -0.1717 0.0642  -0.0651 198 SER B C   
6640 O O   . SER B 198 ? 1.3068 1.7626 1.1783 -0.1741 0.0661  -0.0658 198 SER B O   
6641 C CB  . SER B 198 ? 1.2450 1.6206 1.1230 -0.1361 0.0571  -0.0559 198 SER B CB  
6642 O OG  . SER B 198 ? 1.1909 1.5524 1.0776 -0.1162 0.0519  -0.0503 198 SER B OG  
6643 N N   . ILE B 199 ? 1.4004 1.8057 1.2578 -0.1893 0.0675  -0.0701 199 ILE B N   
6644 C CA  . ILE B 199 ? 1.4969 1.9117 1.3415 -0.2146 0.0740  -0.0772 199 ILE B CA  
6645 C C   . ILE B 199 ? 1.5923 1.9708 1.4225 -0.2219 0.0787  -0.0795 199 ILE B C   
6646 O O   . ILE B 199 ? 1.6107 1.9560 1.4409 -0.2075 0.0766  -0.0758 199 ILE B O   
6647 C CB  . ILE B 199 ? 1.5033 1.9124 1.3394 -0.2312 0.0760  -0.0819 199 ILE B CB  
6648 C CG1 . ILE B 199 ? 1.4601 1.8843 1.3093 -0.2179 0.0702  -0.0779 199 ILE B CG1 
6649 C CG2 . ILE B 199 ? 1.4953 1.9363 1.3238 -0.2559 0.0814  -0.0887 199 ILE B CG2 
6650 C CD1 . ILE B 199 ? 1.4374 1.8179 1.2856 -0.2057 0.0673  -0.0746 199 ILE B CD1 
6651 N N   . PHE B 200 ? 1.7016 2.0868 1.5190 -0.2444 0.0853  -0.0856 200 PHE B N   
6652 C CA  . PHE B 200 ? 1.7699 2.1248 1.5725 -0.2526 0.0907  -0.0878 200 PHE B CA  
6653 C C   . PHE B 200 ? 1.8036 2.1001 1.5914 -0.2521 0.0927  -0.0880 200 PHE B C   
6654 O O   . PHE B 200 ? 1.7959 2.0653 1.5827 -0.2392 0.0915  -0.0847 200 PHE B O   
6655 C CB  . PHE B 200 ? 1.8439 2.2205 1.6352 -0.2783 0.0980  -0.0945 200 PHE B CB  
6656 C CG  . PHE B 200 ? 1.8922 2.3159 1.6946 -0.2760 0.0975  -0.0935 200 PHE B CG  
6657 C CD1 . PHE B 200 ? 1.8881 2.3090 1.6981 -0.2575 0.0949  -0.0884 200 PHE B CD1 
6658 C CD2 . PHE B 200 ? 1.9242 2.3954 1.7285 -0.2929 0.1000  -0.0977 200 PHE B CD2 
6659 C CE1 . PHE B 200 ? 1.8901 2.3540 1.7095 -0.2546 0.0948  -0.0873 200 PHE B CE1 
6660 C CE2 . PHE B 200 ? 1.9358 2.4525 1.7503 -0.2902 0.0997  -0.0966 200 PHE B CE2 
6661 C CZ  . PHE B 200 ? 1.9227 2.4352 1.7445 -0.2706 0.0973  -0.0912 200 PHE B CZ  
6662 N N   . PRO B 201 ? 1.8603 2.1377 1.6358 -0.2658 0.0958  -0.0920 201 PRO B N   
6663 C CA  . PRO B 201 ? 1.9257 2.2285 1.6991 -0.2829 0.0977  -0.0968 201 PRO B CA  
6664 C C   . PRO B 201 ? 1.9943 2.2933 1.7472 -0.3113 0.1068  -0.1045 201 PRO B C   
6665 O O   . PRO B 201 ? 1.9921 2.2738 1.7337 -0.3174 0.1118  -0.1058 201 PRO B O   
6666 C CB  . PRO B 201 ? 1.8937 2.1660 1.6642 -0.2772 0.0955  -0.0957 201 PRO B CB  
6667 C CG  . PRO B 201 ? 1.8637 2.0846 1.6238 -0.2681 0.0968  -0.0933 201 PRO B CG  
6668 C CD  . PRO B 201 ? 1.8529 2.0768 1.6157 -0.2616 0.0971  -0.0911 201 PRO B CD  
6669 N N   . ASP B 202 ? 2.0518 2.3675 1.7997 -0.3287 0.1091  -0.1097 202 ASP B N   
6670 C CA  . ASP B 202 ? 2.0515 2.3593 1.7772 -0.3580 0.1183  -0.1180 202 ASP B CA  
6671 C C   . ASP B 202 ? 2.0599 2.4079 1.7859 -0.3741 0.1221  -0.1218 202 ASP B C   
6672 O O   . ASP B 202 ? 2.0533 2.3815 1.7629 -0.3875 0.1292  -0.1249 202 ASP B O   
6673 C CB  . ASP B 202 ? 2.0174 2.2630 1.7190 -0.3629 0.1248  -0.1194 202 ASP B CB  
6674 C CG  . ASP B 202 ? 1.9989 2.2231 1.6772 -0.3871 0.1325  -0.1268 202 ASP B CG  
6675 O OD1 . ASP B 202 ? 1.9513 2.1695 1.6305 -0.3848 0.1301  -0.1270 202 ASP B OD1 
6676 O OD2 . ASP B 202 ? 2.0043 2.2162 1.6623 -0.4086 0.1413  -0.1324 202 ASP B OD2 
6677 N N   . SER B 203 ? 2.0695 2.4744 1.8139 -0.3722 0.1176  -0.1212 203 SER B N   
6678 C CA  . SER B 203 ? 2.1128 2.5643 1.8577 -0.3908 0.1212  -0.1258 203 SER B CA  
6679 C C   . SER B 203 ? 2.1690 2.6575 1.9149 -0.4077 0.1214  -0.1312 203 SER B C   
6680 O O   . SER B 203 ? 2.1753 2.6835 1.9360 -0.3942 0.1147  -0.1280 203 SER B O   
6681 C CB  . SER B 203 ? 2.0572 2.5498 1.8234 -0.3721 0.1159  -0.1200 203 SER B CB  
6682 O OG  . SER B 203 ? 1.9796 2.4428 1.7418 -0.3626 0.1174  -0.1168 203 SER B OG  
6683 N N   . ALA B 204 ? 2.2273 2.7248 1.9567 -0.4378 0.1292  -0.1396 204 ALA B N   
6684 C CA  . ALA B 204 ? 2.2784 2.8014 2.0026 -0.4591 0.1310  -0.1466 204 ALA B CA  
6685 C C   . ALA B 204 ? 2.3583 2.8386 2.0722 -0.4580 0.1308  -0.1475 204 ALA B C   
6686 O O   . ALA B 204 ? 2.3874 2.8914 2.1055 -0.4631 0.1283  -0.1499 204 ALA B O   
6687 C CB  . ALA B 204 ? 2.1883 2.7822 1.9363 -0.4521 0.1244  -0.1446 204 ALA B CB  
6688 N N   . ARG B 205 ? 2.4095 2.8279 2.1096 -0.4507 0.1335  -0.1454 205 ARG B N   
6689 C CA  . ARG B 205 ? 2.3830 2.7525 2.0692 -0.4497 0.1347  -0.1462 205 ARG B CA  
6690 C C   . ARG B 205 ? 2.3105 2.6820 2.0161 -0.4229 0.1253  -0.1391 205 ARG B C   
6691 O O   . ARG B 205 ? 2.2761 2.6961 2.0031 -0.4132 0.1185  -0.1363 205 ARG B O   
6692 C CB  . ARG B 205 ? 2.3932 2.7600 2.0584 -0.4801 0.1420  -0.1559 205 ARG B CB  
6693 C CG  . ARG B 205 ? 2.3914 2.7514 2.0343 -0.5090 0.1524  -0.1636 205 ARG B CG  
6694 C CD  . ARG B 205 ? 2.3758 2.6855 1.9865 -0.5310 0.1620  -0.1709 205 ARG B CD  
6695 N NE  . ARG B 205 ? 2.3542 2.5976 1.9481 -0.5202 0.1660  -0.1674 205 ARG B NE  
6696 C CZ  . ARG B 205 ? 2.3451 2.5594 1.9217 -0.5284 0.1735  -0.1685 205 ARG B CZ  
6697 N NH1 . ARG B 205 ? 2.3550 2.5999 1.9288 -0.5483 0.1781  -0.1731 205 ARG B NH1 
6698 N NH2 . ARG B 205 ? 2.3427 2.4982 1.9046 -0.5163 0.1766  -0.1647 205 ARG B NH2 
6699 N N   . LYS B 206 ? 2.2474 2.5657 1.9444 -0.4110 0.1254  -0.1361 206 LYS B N   
6700 C CA  . LYS B 206 ? 2.1706 2.4833 1.8830 -0.3871 0.1174  -0.1296 206 LYS B CA  
6701 C C   . LYS B 206 ? 2.1805 2.4912 1.8864 -0.3963 0.1177  -0.1334 206 LYS B C   
6702 O O   . LYS B 206 ? 2.1438 2.4723 1.8667 -0.3806 0.1106  -0.1291 206 LYS B O   
6703 C CB  . LYS B 206 ? 2.0879 2.3485 1.7964 -0.3679 0.1165  -0.1238 206 LYS B CB  
6704 C CG  . LYS B 206 ? 1.9803 2.2438 1.7102 -0.3395 0.1072  -0.1156 206 LYS B CG  
6705 C CD  . LYS B 206 ? 1.9238 2.1350 1.6473 -0.3237 0.1070  -0.1110 206 LYS B CD  
6706 C CE  . LYS B 206 ? 1.8516 2.0621 1.5932 -0.2994 0.0986  -0.1040 206 LYS B CE  
6707 N NZ  . LYS B 206 ? 1.8028 1.9636 1.5371 -0.2857 0.0986  -0.1002 206 LYS B NZ  
6708 N N   . PRO B 207 ? 2.2169 2.5044 1.8973 -0.4216 0.1264  -0.1416 207 PRO B N   
6709 C CA  . PRO B 207 ? 2.2105 2.5026 1.8845 -0.4331 0.1271  -0.1463 207 PRO B CA  
6710 C C   . PRO B 207 ? 2.1961 2.5525 1.8826 -0.4455 0.1244  -0.1501 207 PRO B C   
6711 O O   . PRO B 207 ? 2.1966 2.5673 1.8844 -0.4499 0.1226  -0.1525 207 PRO B O   
6712 C CB  . PRO B 207 ? 2.2314 2.4770 1.8718 -0.4571 0.1382  -0.1541 207 PRO B CB  
6713 C CG  . PRO B 207 ? 2.2383 2.4769 1.8699 -0.4658 0.1437  -0.1554 207 PRO B CG  
6714 C CD  . PRO B 207 ? 2.2310 2.4770 1.8851 -0.4379 0.1361  -0.1460 207 PRO B CD  
6715 N N   . PHE B 208 ? 2.1478 2.5436 1.8435 -0.4504 0.1243  -0.1505 208 PHE B N   
6716 C CA  . PHE B 208 ? 2.0671 2.5293 1.7761 -0.4603 0.1216  -0.1534 208 PHE B CA  
6717 C C   . PHE B 208 ? 2.0401 2.5391 1.7768 -0.4343 0.1113  -0.1456 208 PHE B C   
6718 O O   . PHE B 208 ? 2.0316 2.5793 1.7781 -0.4394 0.1083  -0.1475 208 PHE B O   
6719 C CB  . PHE B 208 ? 2.0030 2.4963 1.7138 -0.4713 0.1246  -0.1555 208 PHE B CB  
6720 C CG  . PHE B 208 ? 1.9326 2.4918 1.6507 -0.4887 0.1243  -0.1607 208 PHE B CG  
6721 C CD1 . PHE B 208 ? 1.9391 2.5024 1.6372 -0.5215 0.1316  -0.1713 208 PHE B CD1 
6722 C CD2 . PHE B 208 ? 1.8724 2.4898 1.6164 -0.4723 0.1169  -0.1552 208 PHE B CD2 
6723 C CE1 . PHE B 208 ? 1.9241 2.5511 1.6292 -0.5383 0.1311  -0.1764 208 PHE B CE1 
6724 C CE2 . PHE B 208 ? 1.8399 2.5211 1.5908 -0.4874 0.1165  -0.1597 208 PHE B CE2 
6725 C CZ  . PHE B 208 ? 1.8752 2.5625 1.6072 -0.5208 0.1234  -0.1704 208 PHE B CZ  
6726 N N   . PHE B 209 ? 2.0453 2.5207 1.7937 -0.4067 0.1061  -0.1369 209 PHE B N   
6727 C CA  . PHE B 209 ? 1.9867 2.4870 1.7587 -0.3806 0.0970  -0.1289 209 PHE B CA  
6728 C C   . PHE B 209 ? 1.9447 2.4244 1.7140 -0.3765 0.0950  -0.1285 209 PHE B C   
6729 O O   . PHE B 209 ? 1.8938 2.4063 1.6785 -0.3655 0.0891  -0.1252 209 PHE B O   
6730 C CB  . PHE B 209 ? 2.0084 2.4906 1.7928 -0.3539 0.0927  -0.1201 209 PHE B CB  
6731 C CG  . PHE B 209 ? 2.0502 2.5614 1.8421 -0.3526 0.0931  -0.1188 209 PHE B CG  
6732 C CD1 . PHE B 209 ? 2.0390 2.6109 1.8481 -0.3477 0.0892  -0.1169 209 PHE B CD1 
6733 C CD2 . PHE B 209 ? 2.0971 2.5751 1.8784 -0.3551 0.0974  -0.1192 209 PHE B CD2 
6734 C CE1 . PHE B 209 ? 2.0706 2.6699 1.8864 -0.3456 0.0897  -0.1156 209 PHE B CE1 
6735 C CE2 . PHE B 209 ? 2.1125 2.6172 1.9006 -0.3537 0.0979  -0.1180 209 PHE B CE2 
6736 C CZ  . PHE B 209 ? 2.1060 2.6714 1.9114 -0.3489 0.0941  -0.1162 209 PHE B CZ  
6737 N N   . LYS B 210 ? 1.9135 2.3388 1.6625 -0.3847 0.1001  -0.1317 210 LYS B N   
6738 C CA  . LYS B 210 ? 1.8800 2.2819 1.6235 -0.3825 0.0992  -0.1320 210 LYS B CA  
6739 C C   . LYS B 210 ? 1.9293 2.3563 1.6628 -0.4067 0.1025  -0.1405 210 LYS B C   
6740 O O   . LYS B 210 ? 1.9417 2.3719 1.6777 -0.4033 0.0997  -0.1402 210 LYS B O   
6741 C CB  . LYS B 210 ? 1.8206 2.1559 1.5451 -0.3811 0.1039  -0.1321 210 LYS B CB  
6742 C CG  . LYS B 210 ? 1.7418 2.0514 1.4674 -0.3675 0.1007  -0.1286 210 LYS B CG  
6743 C CD  . LYS B 210 ? 1.6772 1.9266 1.3902 -0.3578 0.1034  -0.1258 210 LYS B CD  
6744 C CE  . LYS B 210 ? 1.5967 1.8259 1.3146 -0.3413 0.0993  -0.1212 210 LYS B CE  
6745 N NZ  . LYS B 210 ? 1.5527 1.7297 1.2623 -0.3280 0.1007  -0.1171 210 LYS B NZ  
6746 N N   . LEU B 211 ? 1.9707 2.4160 1.6928 -0.4316 0.1084  -0.1481 211 LEU B N   
6747 C CA  . LEU B 211 ? 2.0010 2.4755 1.7134 -0.4575 0.1117  -0.1570 211 LEU B CA  
6748 C C   . LEU B 211 ? 1.9751 2.5166 1.7107 -0.4502 0.1044  -0.1546 211 LEU B C   
6749 O O   . LEU B 211 ? 1.9774 2.5357 1.7124 -0.4562 0.1029  -0.1575 211 LEU B O   
6750 C CB  . LEU B 211 ? 2.0257 2.5020 1.7194 -0.4867 0.1204  -0.1658 211 LEU B CB  
6751 C CG  . LEU B 211 ? 2.0300 2.5458 1.7145 -0.5168 0.1243  -0.1759 211 LEU B CG  
6752 C CD1 . LEU B 211 ? 2.0638 2.5484 1.7278 -0.5313 0.1284  -0.1823 211 LEU B CD1 
6753 C CD2 . LEU B 211 ? 2.0284 2.5504 1.6986 -0.5422 0.1321  -0.1828 211 LEU B CD2 
6754 N N   . LEU B 212 ? 1.9332 2.5124 1.6882 -0.4367 0.1000  -0.1492 212 LEU B N   
6755 C CA  . LEU B 212 ? 1.8436 2.4879 1.6205 -0.4270 0.0933  -0.1458 212 LEU B CA  
6756 C C   . LEU B 212 ? 1.7822 2.4241 1.5747 -0.3998 0.0858  -0.1374 212 LEU B C   
6757 O O   . LEU B 212 ? 1.7366 2.4171 1.5379 -0.3983 0.0820  -0.1373 212 LEU B O   
6758 C CB  . LEU B 212 ? 1.8257 2.5073 1.6171 -0.4184 0.0914  -0.1419 212 LEU B CB  
6759 C CG  . LEU B 212 ? 1.8567 2.5606 1.6375 -0.4452 0.0979  -0.1498 212 LEU B CG  
6760 C CD1 . LEU B 212 ? 1.8556 2.5840 1.6506 -0.4314 0.0959  -0.1442 212 LEU B CD1 
6761 C CD2 . LEU B 212 ? 1.8823 2.6406 1.6619 -0.4673 0.0988  -0.1572 212 LEU B CD2 
6762 N N   . THR B 213 ? 1.7474 2.3443 1.5429 -0.3787 0.0838  -0.1305 213 THR B N   
6763 C CA  . THR B 213 ? 1.7086 2.2996 1.5185 -0.3526 0.0770  -0.1221 213 THR B CA  
6764 C C   . THR B 213 ? 1.6826 2.2587 1.4837 -0.3596 0.0775  -0.1254 213 THR B C   
6765 O O   . THR B 213 ? 1.6412 2.2416 1.4551 -0.3467 0.0721  -0.1212 213 THR B O   
6766 C CB  . THR B 213 ? 1.6829 2.2283 1.4970 -0.3303 0.0751  -0.1146 213 THR B CB  
6767 O OG1 . THR B 213 ? 1.6811 2.2324 1.5122 -0.3045 0.0682  -0.1060 213 THR B OG1 
6768 C CG2 . THR B 213 ? 1.6830 2.1656 1.4767 -0.3387 0.0803  -0.1180 213 THR B CG2 
6769 N N   . SER B 214 ? 1.6959 2.2323 1.4742 -0.3800 0.0842  -0.1329 214 SER B N   
6770 C CA  . SER B 214 ? 1.6888 2.2054 1.4556 -0.3878 0.0856  -0.1366 214 SER B CA  
6771 C C   . SER B 214 ? 1.6870 2.2549 1.4552 -0.4034 0.0849  -0.1422 214 SER B C   
6772 O O   . SER B 214 ? 1.6968 2.2727 1.4693 -0.3973 0.0816  -0.1408 214 SER B O   
6773 C CB  . SER B 214 ? 1.7276 2.1878 1.4670 -0.4059 0.0940  -0.1433 214 SER B CB  
6774 O OG  . SER B 214 ? 1.7546 2.1908 1.4826 -0.4100 0.0953  -0.1460 214 SER B OG  
6775 N N   . LYS B 215 ? 1.6793 2.2834 1.4441 -0.4235 0.0881  -0.1485 215 LYS B N   
6776 C CA  . LYS B 215 ? 1.6667 2.3247 1.4325 -0.4406 0.0877  -0.1546 215 LYS B CA  
6777 C C   . LYS B 215 ? 1.6333 2.3485 1.4249 -0.4194 0.0793  -0.1470 215 LYS B C   
6778 O O   . LYS B 215 ? 1.6307 2.3830 1.4254 -0.4248 0.0771  -0.1494 215 LYS B O   
6779 C CB  . LYS B 215 ? 1.6628 2.3432 1.4164 -0.4698 0.0940  -0.1639 215 LYS B CB  
6780 C CG  . LYS B 215 ? 1.6652 2.3002 1.3886 -0.4985 0.1033  -0.1743 215 LYS B CG  
6781 C CD  . LYS B 215 ? 1.6413 2.3080 1.3528 -0.5306 0.1093  -0.1845 215 LYS B CD  
6782 C CE  . LYS B 215 ? 1.6447 2.2652 1.3237 -0.5600 0.1191  -0.1953 215 LYS B CE  
6783 N NZ  . LYS B 215 ? 1.6199 2.2724 1.2861 -0.5940 0.1254  -0.2061 215 LYS B NZ  
6784 N N   . ILE B 216 ? 1.5818 2.3029 1.3906 -0.3950 0.0750  -0.1379 216 ILE B N   
6785 C CA  . ILE B 216 ? 1.5033 2.2703 1.3351 -0.3707 0.0675  -0.1292 216 ILE B CA  
6786 C C   . ILE B 216 ? 1.4724 2.2172 1.3099 -0.3511 0.0631  -0.1230 216 ILE B C   
6787 O O   . ILE B 216 ? 1.4719 2.2554 1.3225 -0.3386 0.0582  -0.1187 216 ILE B O   
6788 C CB  . ILE B 216 ? 1.4530 2.2308 1.2996 -0.3506 0.0649  -0.1215 216 ILE B CB  
6789 C CG1 . ILE B 216 ? 1.4531 2.2692 1.2976 -0.3687 0.0684  -0.1270 216 ILE B CG1 
6790 C CG2 . ILE B 216 ? 1.4122 2.2249 1.2800 -0.3218 0.0577  -0.1114 216 ILE B CG2 
6791 C CD1 . ILE B 216 ? 1.4601 2.2730 1.3130 -0.3541 0.0679  -0.1213 216 ILE B CD1 
6792 N N   . TYR B 217 ? 1.4655 2.1488 1.2924 -0.3487 0.0652  -0.1226 217 TYR B N   
6793 C CA  . TYR B 217 ? 1.4687 2.1273 1.2982 -0.3338 0.0621  -0.1180 217 TYR B CA  
6794 C C   . TYR B 217 ? 1.5299 2.2028 1.3499 -0.3506 0.0633  -0.1247 217 TYR B C   
6795 O O   . TYR B 217 ? 1.5277 2.2019 1.3540 -0.3379 0.0596  -0.1205 217 TYR B O   
6796 C CB  . TYR B 217 ? 1.4285 2.0196 1.2484 -0.3274 0.0643  -0.1161 217 TYR B CB  
6797 C CG  . TYR B 217 ? 1.3693 1.9458 1.2041 -0.3004 0.0601  -0.1061 217 TYR B CG  
6798 C CD1 . TYR B 217 ? 1.3439 1.9295 1.1950 -0.2758 0.0541  -0.0971 217 TYR B CD1 
6799 C CD2 . TYR B 217 ? 1.3619 1.9144 1.1934 -0.3001 0.0626  -0.1057 217 TYR B CD2 
6800 C CE1 . TYR B 217 ? 1.3064 1.8775 1.1697 -0.2524 0.0507  -0.0885 217 TYR B CE1 
6801 C CE2 . TYR B 217 ? 1.3071 1.8463 1.1513 -0.2762 0.0588  -0.0971 217 TYR B CE2 
6802 C CZ  . TYR B 217 ? 1.2777 1.8260 1.1375 -0.2529 0.0529  -0.0887 217 TYR B CZ  
6803 O OH  . TYR B 217 ? 1.2278 1.7616 1.0988 -0.2305 0.0496  -0.0806 217 TYR B OH  
6804 N N   . LYS B 218 ? 1.5933 2.2770 1.3977 -0.3797 0.0688  -0.1352 218 LYS B N   
6805 C CA  . LYS B 218 ? 1.6336 2.3369 1.4280 -0.3990 0.0703  -0.1429 218 LYS B CA  
6806 C C   . LYS B 218 ? 1.6253 2.4005 1.4364 -0.3945 0.0651  -0.1411 218 LYS B C   
6807 O O   . LYS B 218 ? 1.6189 2.4125 1.4327 -0.3919 0.0623  -0.1408 218 LYS B O   
6808 C CB  . LYS B 218 ? 1.6916 2.3813 1.4619 -0.4331 0.0786  -0.1553 218 LYS B CB  
6809 C CG  . LYS B 218 ? 1.7202 2.3433 1.4726 -0.4384 0.0848  -0.1572 218 LYS B CG  
6810 C CD  . LYS B 218 ? 1.7360 2.3056 1.4721 -0.4395 0.0877  -0.1590 218 LYS B CD  
6811 C CE  . LYS B 218 ? 1.7349 2.2405 1.4521 -0.4441 0.0943  -0.1607 218 LYS B CE  
6812 N NZ  . LYS B 218 ? 1.7316 2.1849 1.4308 -0.4453 0.0979  -0.1625 218 LYS B NZ  
6813 N N   . VAL B 219 ? 1.6229 2.4389 1.4446 -0.3931 0.0640  -0.1396 219 VAL B N   
6814 C CA  . VAL B 219 ? 1.6166 2.5035 1.4551 -0.3855 0.0591  -0.1365 219 VAL B CA  
6815 C C   . VAL B 219 ? 1.5983 2.4907 1.4557 -0.3510 0.0523  -0.1241 219 VAL B C   
6816 O O   . VAL B 219 ? 1.5846 2.5237 1.4525 -0.3423 0.0481  -0.1211 219 VAL B O   
6817 C CB  . VAL B 219 ? 1.6322 2.5589 1.4771 -0.3907 0.0601  -0.1374 219 VAL B CB  
6818 C CG1 . VAL B 219 ? 1.6167 2.6196 1.4776 -0.3831 0.0554  -0.1345 219 VAL B CG1 
6819 C CG2 . VAL B 219 ? 1.6699 2.5876 1.4950 -0.4254 0.0675  -0.1495 219 VAL B CG2 
6820 N N   . LEU B 220 ? 1.6080 2.4518 1.4686 -0.3320 0.0515  -0.1171 220 LEU B N   
6821 C CA  . LEU B 220 ? 1.5810 2.4204 1.4573 -0.2999 0.0459  -0.1054 220 LEU B CA  
6822 C C   . LEU B 220 ? 1.5616 2.3994 1.4379 -0.2947 0.0434  -0.1039 220 LEU B C   
6823 O O   . LEU B 220 ? 1.5257 2.3788 1.4156 -0.2707 0.0386  -0.0949 220 LEU B O   
6824 C CB  . LEU B 220 ? 1.5802 2.3620 1.4565 -0.2855 0.0463  -0.1000 220 LEU B CB  
6825 C CG  . LEU B 220 ? 1.5863 2.3537 1.4768 -0.2537 0.0413  -0.0883 220 LEU B CG  
6826 C CD1 . LEU B 220 ? 1.5600 2.3759 1.4670 -0.2344 0.0375  -0.0808 220 LEU B CD1 
6827 C CD2 . LEU B 220 ? 1.6095 2.3179 1.4967 -0.2456 0.0426  -0.0854 220 LEU B CD2 
6828 N N   . GLU B 221 ? 1.5691 2.3873 1.4291 -0.3169 0.0470  -0.1127 221 GLU B N   
6829 C CA  . GLU B 221 ? 1.5638 2.3802 1.4220 -0.3144 0.0452  -0.1124 221 GLU B CA  
6830 C C   . GLU B 221 ? 1.5868 2.4275 1.4314 -0.3425 0.0481  -0.1235 221 GLU B C   
6831 O O   . GLU B 221 ? 1.6081 2.4293 1.4436 -0.3478 0.0488  -0.1263 221 GLU B O   
6832 C CB  . GLU B 221 ? 1.5816 2.3330 1.4339 -0.3045 0.0459  -0.1091 221 GLU B CB  
6833 C CG  . GLU B 221 ? 1.5987 2.2965 1.4346 -0.3191 0.0517  -0.1148 221 GLU B CG  
6834 C CD  . GLU B 221 ? 1.6217 2.3062 1.4356 -0.3486 0.0575  -0.1266 221 GLU B CD  
6835 O OE1 . GLU B 221 ? 1.5999 2.2801 1.4083 -0.3511 0.0572  -0.1284 221 GLU B OE1 
6836 O OE2 . GLU B 221 ? 1.6467 2.3238 1.4478 -0.3694 0.0627  -0.1341 221 GLU B OE2 
6837 N N   . GLU B 222 ? 1.5526 2.4361 1.3953 -0.3609 0.0499  -0.1300 222 GLU B N   
6838 C CA  . GLU B 222 ? 1.5250 2.4444 1.3575 -0.3868 0.0519  -0.1402 222 GLU B CA  
6839 C C   . GLU B 222 ? 1.4817 2.4726 1.3307 -0.3757 0.0463  -0.1359 222 GLU B C   
6840 O O   . GLU B 222 ? 1.4863 2.5014 1.3340 -0.3795 0.0446  -0.1381 222 GLU B O   
6841 C CB  . GLU B 222 ? 1.5537 2.4757 1.3713 -0.4176 0.0581  -0.1513 222 GLU B CB  
6842 C CG  . GLU B 222 ? 1.6090 2.5388 1.4072 -0.4498 0.0625  -0.1641 222 GLU B CG  
6843 C CD  . GLU B 222 ? 1.6026 2.6083 1.4091 -0.4571 0.0591  -0.1670 222 GLU B CD  
6844 O OE1 . GLU B 222 ? 1.6112 2.6658 1.4249 -0.4636 0.0588  -0.1684 222 GLU B OE1 
6845 O OE2 . GLU B 222 ? 1.5909 2.6084 1.3960 -0.4566 0.0569  -0.1679 222 GLU B OE2 
6846 N N   . LYS B 223 ? 1.4437 2.4686 1.3078 -0.3613 0.0438  -0.1297 223 LYS B N   
6847 C CA  . LYS B 223 ? 1.3954 2.4870 1.2758 -0.3457 0.0387  -0.1237 223 LYS B CA  
6848 C C   . LYS B 223 ? 1.3214 2.3995 1.2163 -0.3096 0.0338  -0.1101 223 LYS B C   
6849 O O   . LYS B 223 ? 1.3007 2.4256 1.2099 -0.2895 0.0296  -0.1024 223 LYS B O   
6850 C CB  . LYS B 223 ? 1.4075 2.5455 1.2953 -0.3492 0.0391  -0.1243 223 LYS B CB  
6851 C CG  . LYS B 223 ? 1.4071 2.6243 1.3005 -0.3572 0.0370  -0.1273 223 LYS B CG  
6852 C CD  . LYS B 223 ? 1.4023 2.6615 1.2998 -0.3664 0.0386  -0.1299 223 LYS B CD  
6853 C CE  . LYS B 223 ? 1.3977 2.7409 1.3022 -0.3724 0.0363  -0.1322 223 LYS B CE  
6854 N NZ  . LYS B 223 ? 1.4097 2.7983 1.3211 -0.3757 0.0373  -0.1326 223 LYS B NZ  
6855 N N   . TYR B 224 ? 1.2732 2.2866 1.1632 -0.3017 0.0346  -0.1073 224 TYR B N   
6856 C CA  . TYR B 224 ? 1.2113 2.2028 1.1130 -0.2697 0.0308  -0.0950 224 TYR B CA  
6857 C C   . TYR B 224 ? 1.1924 2.1347 1.0863 -0.2688 0.0312  -0.0951 224 TYR B C   
6858 O O   . TYR B 224 ? 1.1951 2.1017 1.0734 -0.2901 0.0352  -0.1037 224 TYR B O   
6859 C CB  . TYR B 224 ? 1.1528 2.1171 1.0611 -0.2541 0.0309  -0.0887 224 TYR B CB  
6860 C CG  . TYR B 224 ? 1.1249 2.1380 1.0412 -0.2531 0.0306  -0.0880 224 TYR B CG  
6861 C CD1 . TYR B 224 ? 1.1010 2.1631 1.0317 -0.2305 0.0267  -0.0794 224 TYR B CD1 
6862 C CD2 . TYR B 224 ? 1.1304 2.1419 1.0389 -0.2747 0.0347  -0.0959 224 TYR B CD2 
6863 C CE1 . TYR B 224 ? 1.0630 2.1719 1.0006 -0.2286 0.0266  -0.0785 224 TYR B CE1 
6864 C CE2 . TYR B 224 ? 1.0947 2.1532 1.0107 -0.2740 0.0345  -0.0953 224 TYR B CE2 
6865 C CZ  . TYR B 224 ? 1.0891 2.1969 1.0199 -0.2506 0.0304  -0.0866 224 TYR B CZ  
6866 O OH  . TYR B 224 ? 1.1075 2.2636 1.0455 -0.2486 0.0304  -0.0856 224 TYR B OH  
6867 N N   . LYS B 225 ? 1.1901 2.1301 1.0940 -0.2437 0.0273  -0.0853 225 LYS B N   
6868 C CA  . LYS B 225 ? 1.2594 2.1704 1.1576 -0.2424 0.0270  -0.0851 225 LYS B CA  
6869 C C   . LYS B 225 ? 1.2588 2.1030 1.1549 -0.2312 0.0278  -0.0806 225 LYS B C   
6870 O O   . LYS B 225 ? 1.1758 1.9950 1.0756 -0.2225 0.0283  -0.0770 225 LYS B O   
6871 C CB  . LYS B 225 ? 1.2839 2.2355 1.1927 -0.2240 0.0226  -0.0777 225 LYS B CB  
6872 C CG  . LYS B 225 ? 1.2928 2.2616 1.2175 -0.1940 0.0193  -0.0654 225 LYS B CG  
6873 C CD  . LYS B 225 ? 1.2721 2.2857 1.2050 -0.1773 0.0157  -0.0587 225 LYS B CD  
6874 C CE  . LYS B 225 ? 1.2532 2.2870 1.1994 -0.1486 0.0134  -0.0470 225 LYS B CE  
6875 N NZ  . LYS B 225 ? 1.2428 2.3129 1.1955 -0.1293 0.0104  -0.0391 225 LYS B NZ  
6876 N N   . THR B 226 ? 1.2775 2.0951 1.1673 -0.2317 0.0280  -0.0811 226 THR B N   
6877 C CA  . THR B 226 ? 1.2743 2.0322 1.1620 -0.2214 0.0287  -0.0770 226 THR B CA  
6878 C C   . THR B 226 ? 1.2466 1.9997 1.1497 -0.1910 0.0248  -0.0642 226 THR B C   
6879 O O   . THR B 226 ? 1.1634 1.9375 1.0737 -0.1767 0.0219  -0.0581 226 THR B O   
6880 C CB  . THR B 226 ? 1.2798 2.0119 1.1553 -0.2314 0.0305  -0.0815 226 THR B CB  
6881 O OG1 . THR B 226 ? 1.2393 1.9251 1.1173 -0.2147 0.0298  -0.0746 226 THR B OG1 
6882 C CG2 . THR B 226 ? 1.2435 2.0209 1.1216 -0.2314 0.0280  -0.0816 226 THR B CG2 
6883 N N   . SER B 227 ? 1.2678 1.9924 1.1749 -0.1817 0.0251  -0.0603 227 SER B N   
6884 C CA  . SER B 227 ? 1.2339 1.9450 1.1532 -0.1547 0.0222  -0.0489 227 SER B CA  
6885 C C   . SER B 227 ? 1.1782 1.8704 1.0988 -0.1432 0.0208  -0.0438 227 SER B C   
6886 O O   . SER B 227 ? 1.1605 1.8727 1.0906 -0.1242 0.0180  -0.0355 227 SER B O   
6887 C CB  . SER B 227 ? 1.2354 1.9025 1.1540 -0.1515 0.0236  -0.0478 227 SER B CB  
6888 O OG  . SER B 227 ? 1.2827 1.9678 1.2020 -0.1579 0.0247  -0.0507 227 SER B OG  
6889 N N   . GLY B 228 ? 1.1362 1.7900 1.0462 -0.1548 0.0231  -0.0487 228 GLY B N   
6890 C CA  . GLY B 228 ? 1.0372 1.6594 0.9484 -0.1427 0.0223  -0.0433 228 GLY B CA  
6891 C C   . GLY B 228 ? 0.9604 1.5443 0.8769 -0.1287 0.0219  -0.0373 228 GLY B C   
6892 O O   . GLY B 228 ? 0.9454 1.5409 0.8709 -0.1166 0.0204  -0.0322 228 GLY B O   
6893 N N   . SER B 229 ? 0.9043 1.4429 0.8146 -0.1307 0.0235  -0.0382 229 SER B N   
6894 C CA  . SER B 229 ? 0.8146 1.3164 0.7295 -0.1182 0.0231  -0.0329 229 SER B CA  
6895 C C   . SER B 229 ? 0.7593 1.2671 0.6869 -0.0952 0.0199  -0.0222 229 SER B C   
6896 O O   . SER B 229 ? 0.7465 1.2722 0.6767 -0.0894 0.0187  -0.0190 229 SER B O   
6897 C CB  . SER B 229 ? 0.8264 1.2819 0.7314 -0.1248 0.0255  -0.0360 229 SER B CB  
6898 O OG  . SER B 229 ? 0.8730 1.3203 0.7795 -0.1170 0.0246  -0.0320 229 SER B OG  
6899 N N   . LEU B 230 ? 0.7196 1.2121 0.6541 -0.0826 0.0189  -0.0169 230 LEU B N   
6900 C CA  . LEU B 230 ? 0.6641 1.1551 0.6088 -0.0611 0.0167  -0.0069 230 LEU B CA  
6901 C C   . LEU B 230 ? 0.6565 1.1290 0.6010 -0.0559 0.0165  -0.0034 230 LEU B C   
6902 O O   . LEU B 230 ? 0.6798 1.1684 0.6297 -0.0432 0.0151  0.0030  230 LEU B O   
6903 C CB  . LEU B 230 ? 0.6353 1.0986 0.5837 -0.0525 0.0165  -0.0037 230 LEU B CB  
6904 C CG  . LEU B 230 ? 0.6105 1.0844 0.5679 -0.0334 0.0150  0.0045  230 LEU B CG  
6905 C CD1 . LEU B 230 ? 0.5984 1.0340 0.5575 -0.0270 0.0149  0.0069  230 LEU B CD1 
6906 C CD2 . LEU B 230 ? 0.5850 1.0734 0.5474 -0.0181 0.0138  0.0124  230 LEU B CD2 
6907 N N   . TYR B 231 ? 0.6549 1.0937 0.5922 -0.0653 0.0181  -0.0076 231 TYR B N   
6908 C CA  . TYR B 231 ? 0.6391 1.0592 0.5754 -0.0616 0.0182  -0.0050 231 TYR B CA  
6909 C C   . TYR B 231 ? 0.6461 1.0961 0.5810 -0.0639 0.0179  -0.0055 231 TYR B C   
6910 O O   . TYR B 231 ? 0.6584 1.1134 0.5987 -0.0514 0.0167  0.0012  231 TYR B O   
6911 C CB  . TYR B 231 ? 0.6078 0.9913 0.5344 -0.0730 0.0205  -0.0107 231 TYR B CB  
6912 C CG  . TYR B 231 ? 0.5986 0.9618 0.5242 -0.0685 0.0208  -0.0077 231 TYR B CG  
6913 C CD1 . TYR B 231 ? 0.5798 0.9199 0.5126 -0.0548 0.0197  -0.0007 231 TYR B CD1 
6914 C CD2 . TYR B 231 ? 0.5914 0.9588 0.5083 -0.0783 0.0224  -0.0122 231 TYR B CD2 
6915 C CE1 . TYR B 231 ? 0.5567 0.8801 0.4888 -0.0509 0.0201  0.0020  231 TYR B CE1 
6916 C CE2 . TYR B 231 ? 0.5874 0.9370 0.5032 -0.0737 0.0229  -0.0094 231 TYR B CE2 
6917 C CZ  . TYR B 231 ? 0.5818 0.9102 0.5057 -0.0599 0.0217  -0.0021 231 TYR B CZ  
6918 O OH  . TYR B 231 ? 0.5940 0.9066 0.5170 -0.0557 0.0223  0.0006  231 TYR B OH  
6919 N N   . THR B 232 ? 0.6719 1.1416 0.5987 -0.0804 0.0192  -0.0136 232 THR B N   
6920 C CA  . THR B 232 ? 0.7051 1.2035 0.6289 -0.0853 0.0190  -0.0155 232 THR B CA  
6921 C C   . THR B 232 ? 0.6700 1.2068 0.6038 -0.0705 0.0165  -0.0083 232 THR B C   
6922 O O   . THR B 232 ? 0.6808 1.2295 0.6167 -0.0628 0.0156  -0.0040 232 THR B O   
6923 C CB  . THR B 232 ? 0.7640 1.2779 0.6766 -0.1075 0.0211  -0.0263 232 THR B CB  
6924 O OG1 . THR B 232 ? 0.8460 1.3225 0.7485 -0.1197 0.0241  -0.0324 232 THR B OG1 
6925 C CG2 . THR B 232 ? 0.7857 1.3167 0.6919 -0.1151 0.0215  -0.0296 232 THR B CG2 
6926 N N   . CYS B 233 ? 0.6620 1.2169 0.6013 -0.0656 0.0156  -0.0066 233 CYS B N   
6927 C CA  . CYS B 233 ? 0.6431 1.2335 0.5909 -0.0494 0.0136  0.0007  233 CYS B CA  
6928 C C   . CYS B 233 ? 0.6211 1.1949 0.5754 -0.0286 0.0128  0.0113  233 CYS B C   
6929 O O   . CYS B 233 ? 0.6223 1.2200 0.5795 -0.0175 0.0120  0.0169  233 CYS B O   
6930 C CB  . CYS B 233 ? 0.6626 1.2692 0.6141 -0.0472 0.0134  0.0007  233 CYS B CB  
6931 S SG  . CYS B 233 ? 0.7305 1.3733 0.6759 -0.0695 0.0142  -0.0101 233 CYS B SG  
6932 N N   . TRP B 234 ? 0.5916 1.1249 0.5475 -0.0236 0.0133  0.0139  234 TRP B N   
6933 C CA  . TRP B 234 ? 0.5479 1.0621 0.5091 -0.0056 0.0130  0.0233  234 TRP B CA  
6934 C C   . TRP B 234 ? 0.5576 1.0620 0.5164 -0.0066 0.0133  0.0244  234 TRP B C   
6935 O O   . TRP B 234 ? 0.6037 1.1118 0.5659 0.0074  0.0131  0.0322  234 TRP B O   
6936 C CB  . TRP B 234 ? 0.5064 0.9821 0.4697 -0.0016 0.0133  0.0251  234 TRP B CB  
6937 C CG  . TRP B 234 ? 0.4694 0.9272 0.4376 0.0161  0.0133  0.0347  234 TRP B CG  
6938 C CD1 . TRP B 234 ? 0.4560 0.8815 0.4246 0.0186  0.0138  0.0375  234 TRP B CD1 
6939 C CD2 . TRP B 234 ? 0.4661 0.9370 0.4385 0.0344  0.0133  0.0432  234 TRP B CD2 
6940 N NE1 . TRP B 234 ? 0.4396 0.8571 0.4122 0.0353  0.0141  0.0465  234 TRP B NE1 
6941 C CE2 . TRP B 234 ? 0.4577 0.8996 0.4319 0.0457  0.0141  0.0503  234 TRP B CE2 
6942 C CE3 . TRP B 234 ? 0.4656 0.9681 0.4394 0.0425  0.0132  0.0455  234 TRP B CE3 
6943 C CZ2 . TRP B 234 ? 0.4530 0.8952 0.4290 0.0637  0.0150  0.0593  234 TRP B CZ2 
6944 C CZ3 . TRP B 234 ? 0.4725 0.9755 0.4482 0.0623  0.0140  0.0550  234 TRP B CZ3 
6945 C CH2 . TRP B 234 ? 0.4678 0.9398 0.4440 0.0724  0.0151  0.0616  234 TRP B CH2 
6946 N N   . SER B 235 ? 0.5489 1.0402 0.5007 -0.0229 0.0142  0.0166  235 SER B N   
6947 C CA  . SER B 235 ? 0.5640 1.0452 0.5126 -0.0247 0.0149  0.0169  235 SER B CA  
6948 C C   . SER B 235 ? 0.5662 1.0856 0.5145 -0.0223 0.0141  0.0183  235 SER B C   
6949 O O   . SER B 235 ? 0.5383 1.0590 0.4896 -0.0101 0.0139  0.0254  235 SER B O   
6950 C CB  . SER B 235 ? 0.5588 1.0169 0.4978 -0.0423 0.0166  0.0080  235 SER B CB  
6951 O OG  . SER B 235 ? 0.5720 1.0138 0.5083 -0.0414 0.0174  0.0093  235 SER B OG  
6952 N N   . GLU B 236 ? 0.5859 1.1370 0.5301 -0.0341 0.0139  0.0116  236 GLU B N   
6953 C CA  . GLU B 236 ? 0.6037 1.1955 0.5475 -0.0329 0.0130  0.0123  236 GLU B CA  
6954 C C   . GLU B 236 ? 0.5619 1.1735 0.5138 -0.0110 0.0118  0.0231  236 GLU B C   
6955 O O   . GLU B 236 ? 0.5409 1.1625 0.4936 -0.0016 0.0116  0.0286  236 GLU B O   
6956 C CB  . GLU B 236 ? 0.6664 1.2920 0.6054 -0.0492 0.0129  0.0034  236 GLU B CB  
6957 C CG  . GLU B 236 ? 0.7252 1.3350 0.6527 -0.0720 0.0149  -0.0076 236 GLU B CG  
6958 C CD  . GLU B 236 ? 0.7634 1.4061 0.6853 -0.0898 0.0152  -0.0168 236 GLU B CD  
6959 O OE1 . GLU B 236 ? 0.7991 1.4333 0.7096 -0.1093 0.0174  -0.0262 236 GLU B OE1 
6960 O OE2 . GLU B 236 ? 0.7641 1.4410 0.6923 -0.0845 0.0138  -0.0146 236 GLU B OE2 
6961 N N   . PHE B 237 ? 0.5530 1.1678 0.5099 -0.0025 0.0114  0.0265  237 PHE B N   
6962 C CA  . PHE B 237 ? 0.5323 1.1637 0.4949 0.0189  0.0110  0.0367  237 PHE B CA  
6963 C C   . PHE B 237 ? 0.5307 1.1361 0.4953 0.0343  0.0119  0.0459  237 PHE B C   
6964 O O   . PHE B 237 ? 0.5168 1.1419 0.4821 0.0475  0.0120  0.0528  237 PHE B O   
6965 C CB  . PHE B 237 ? 0.5261 1.1556 0.4923 0.0249  0.0110  0.0383  237 PHE B CB  
6966 C CG  . PHE B 237 ? 0.5407 1.1838 0.5108 0.0477  0.0113  0.0488  237 PHE B CG  
6967 C CD1 . PHE B 237 ? 0.5341 1.2237 0.5046 0.0560  0.0108  0.0519  237 PHE B CD1 
6968 C CD2 . PHE B 237 ? 0.5382 1.1474 0.5104 0.0612  0.0125  0.0557  237 PHE B CD2 
6969 C CE1 . PHE B 237 ? 0.5199 1.2204 0.4920 0.0785  0.0117  0.0621  237 PHE B CE1 
6970 C CE2 . PHE B 237 ? 0.5359 1.1543 0.5092 0.0825  0.0136  0.0654  237 PHE B CE2 
6971 C CZ  . PHE B 237 ? 0.5472 1.2105 0.5201 0.0918  0.0134  0.0689  237 PHE B CZ  
6972 N N   . THR B 238 ? 0.5294 1.0914 0.4943 0.0323  0.0127  0.0459  238 THR B N   
6973 C CA  . THR B 238 ? 0.5190 1.0549 0.4859 0.0459  0.0138  0.0544  238 THR B CA  
6974 C C   . THR B 238 ? 0.5249 1.0638 0.4893 0.0447  0.0141  0.0555  238 THR B C   
6975 O O   . THR B 238 ? 0.5110 1.0500 0.4766 0.0591  0.0150  0.0641  238 THR B O   
6976 C CB  . THR B 238 ? 0.5173 1.0085 0.4858 0.0441  0.0144  0.0542  238 THR B CB  
6977 O OG1 . THR B 238 ? 0.5315 1.0075 0.4964 0.0261  0.0142  0.0451  238 THR B OG1 
6978 C CG2 . THR B 238 ? 0.4957 0.9827 0.4669 0.0504  0.0144  0.0558  238 THR B CG2 
6979 N N   . GLN B 239 ? 0.5366 1.0777 0.4964 0.0277  0.0137  0.0468  239 GLN B N   
6980 C CA  . GLN B 239 ? 0.5470 1.0896 0.5034 0.0249  0.0142  0.0467  239 GLN B CA  
6981 C C   . GLN B 239 ? 0.6089 1.1928 0.5647 0.0321  0.0135  0.0501  239 GLN B C   
6982 O O   . GLN B 239 ? 0.6458 1.2311 0.6002 0.0369  0.0141  0.0539  239 GLN B O   
6983 C CB  . GLN B 239 ? 0.5471 1.0796 0.4966 0.0046  0.0145  0.0360  239 GLN B CB  
6984 C CG  . GLN B 239 ? 0.5910 1.0827 0.5397 -0.0022 0.0154  0.0325  239 GLN B CG  
6985 C CD  . GLN B 239 ? 0.5894 1.0502 0.5436 0.0108  0.0160  0.0408  239 GLN B CD  
6986 O OE1 . GLN B 239 ? 0.6237 1.0763 0.5781 0.0163  0.0168  0.0452  239 GLN B OE1 
6987 N NE2 . GLN B 239 ? 0.5429 0.9874 0.5013 0.0154  0.0158  0.0427  239 GLN B NE2 
6988 N N   . LYS B 240 ? 0.6078 1.2266 0.5646 0.0334  0.0124  0.0491  240 LYS B N   
6989 C CA  . LYS B 240 ? 0.6259 1.2881 0.5822 0.0411  0.0116  0.0524  240 LYS B CA  
6990 C C   . LYS B 240 ? 0.6395 1.3131 0.5997 0.0643  0.0122  0.0639  240 LYS B C   
6991 O O   . LYS B 240 ? 0.6807 1.3905 0.6402 0.0740  0.0118  0.0682  240 LYS B O   
6992 C CB  . LYS B 240 ? 0.6264 1.3274 0.5799 0.0261  0.0101  0.0433  240 LYS B CB  
6993 C CG  . LYS B 240 ? 0.6223 1.3425 0.5794 0.0290  0.0095  0.0431  240 LYS B CG  
6994 C CD  . LYS B 240 ? 0.6162 1.3677 0.5698 0.0092  0.0084  0.0321  240 LYS B CD  
6995 C CE  . LYS B 240 ? 0.6028 1.3779 0.5603 0.0126  0.0078  0.0323  240 LYS B CE  
6996 N NZ  . LYS B 240 ? 0.5791 1.3665 0.5327 -0.0104 0.0076  0.0204  240 LYS B NZ  
6997 N N   . THR B 241 ? 0.6136 1.2558 0.5767 0.0734  0.0134  0.0688  241 THR B N   
6998 C CA  . THR B 241 ? 0.5815 1.2287 0.5462 0.0954  0.0148  0.0795  241 THR B CA  
6999 C C   . THR B 241 ? 0.5940 1.2038 0.5584 0.1070  0.0171  0.0878  241 THR B C   
7000 O O   . THR B 241 ? 0.6546 1.2262 0.6206 0.1039  0.0179  0.0872  241 THR B O   
7001 C CB  . THR B 241 ? 0.5775 1.2226 0.5445 0.0977  0.0147  0.0787  241 THR B CB  
7002 O OG1 . THR B 241 ? 0.5767 1.2508 0.5439 0.0824  0.0127  0.0693  241 THR B OG1 
7003 C CG2 . THR B 241 ? 0.5763 1.2365 0.5427 0.1208  0.0163  0.0891  241 THR B CG2 
7004 N N   . GLN B 242 ? 0.6123 1.2342 0.5743 0.1202  0.0184  0.0956  242 GLN B N   
7005 C CA  . GLN B 242 ? 0.6211 1.2102 0.5819 0.1298  0.0211  0.1034  242 GLN B CA  
7006 C C   . GLN B 242 ? 0.6057 1.1805 0.5647 0.1496  0.0240  0.1136  242 GLN B C   
7007 O O   . GLN B 242 ? 0.6112 1.1490 0.5695 0.1544  0.0264  0.1184  242 GLN B O   
7008 C CB  . GLN B 242 ? 0.6875 1.2939 0.6454 0.1332  0.0215  0.1066  242 GLN B CB  
7009 C CG  . GLN B 242 ? 0.7394 1.3763 0.6967 0.1171  0.0186  0.0972  242 GLN B CG  
7010 C CD  . GLN B 242 ? 0.8371 1.4816 0.7914 0.1183  0.0192  0.0996  242 GLN B CD  
7011 O OE1 . GLN B 242 ? 0.7896 1.4697 0.7414 0.1267  0.0189  0.1031  242 GLN B OE1 
7012 N NE2 . GLN B 242 ? 0.8940 1.5056 0.8483 0.1105  0.0200  0.0979  242 GLN B NE2 
7013 N N   . GLY B 243 ? 0.5976 1.2017 0.5551 0.1611  0.0242  0.1167  243 GLY B N   
7014 C CA  . GLY B 243 ? 0.6036 1.1948 0.5573 0.1809  0.0275  0.1262  243 GLY B CA  
7015 C C   . GLY B 243 ? 0.6101 1.1740 0.5658 0.1777  0.0277  0.1235  243 GLY B C   
7016 O O   . GLY B 243 ? 0.5762 1.1285 0.5366 0.1600  0.0252  0.1144  243 GLY B O   
7017 N N   . GLN B 244 ? 0.6119 1.1645 0.5628 0.1955  0.0310  0.1316  244 GLN B N   
7018 C CA  . GLN B 244 ? 0.6115 1.1406 0.5629 0.1954  0.0316  0.1300  244 GLN B CA  
7019 C C   . GLN B 244 ? 0.5966 1.1572 0.5523 0.1872  0.0284  0.1224  244 GLN B C   
7020 O O   . GLN B 244 ? 0.6248 1.2275 0.5796 0.1943  0.0277  0.1237  244 GLN B O   
7021 C CB  . GLN B 244 ? 0.6265 1.1397 0.5695 0.2178  0.0365  0.1408  244 GLN B CB  
7022 C CG  . GLN B 244 ? 0.6457 1.1326 0.5876 0.2191  0.0376  0.1397  244 GLN B CG  
7023 C CD  . GLN B 244 ? 0.6546 1.0950 0.5989 0.2068  0.0377  0.1363  244 GLN B CD  
7024 O OE1 . GLN B 244 ? 0.6692 1.0870 0.6121 0.2059  0.0393  0.1395  244 GLN B OE1 
7025 N NE2 . GLN B 244 ? 0.6604 1.0877 0.6083 0.1977  0.0359  0.1300  244 GLN B NE2 
7026 N N   . ILE B 245 ? 0.5497 1.0911 0.5099 0.1720  0.0264  0.1144  245 ILE B N   
7027 C CA  . ILE B 245 ? 0.5236 1.0890 0.4872 0.1634  0.0239  0.1072  245 ILE B CA  
7028 C C   . ILE B 245 ? 0.5347 1.0932 0.4953 0.1775  0.0261  0.1117  245 ILE B C   
7029 O O   . ILE B 245 ? 0.5523 1.0717 0.5102 0.1832  0.0284  0.1153  245 ILE B O   
7030 C CB  . ILE B 245 ? 0.5020 1.0493 0.4703 0.1406  0.0212  0.0964  245 ILE B CB  
7031 C CG1 . ILE B 245 ? 0.4930 1.0534 0.4627 0.1259  0.0192  0.0908  245 ILE B CG1 
7032 C CG2 . ILE B 245 ? 0.4943 1.0579 0.4649 0.1331  0.0196  0.0899  245 ILE B CG2 
7033 C CD1 . ILE B 245 ? 0.4784 1.0079 0.4502 0.1074  0.0179  0.0830  245 ILE B CD1 
7034 N N   . TYR B 246 ? 0.5261 1.1237 0.4868 0.1833  0.0255  0.1115  246 TYR B N   
7035 C CA  . TYR B 246 ? 0.5272 1.1224 0.4857 0.1938  0.0270  0.1137  246 TYR B CA  
7036 C C   . TYR B 246 ? 0.5080 1.1192 0.4721 0.1766  0.0239  0.1036  246 TYR B C   
7037 O O   . TYR B 246 ? 0.4846 1.1225 0.4526 0.1613  0.0211  0.0965  246 TYR B O   
7038 C CB  . TYR B 246 ? 0.5568 1.1838 0.5095 0.2169  0.0296  0.1228  246 TYR B CB  
7039 C CG  . TYR B 246 ? 0.5665 1.1744 0.5116 0.2349  0.0336  0.1334  246 TYR B CG  
7040 C CD1 . TYR B 246 ? 0.5836 1.1506 0.5211 0.2485  0.0379  0.1402  246 TYR B CD1 
7041 C CD2 . TYR B 246 ? 0.5817 1.2099 0.5262 0.2370  0.0333  0.1363  246 TYR B CD2 
7042 C CE1 . TYR B 246 ? 0.6114 1.1581 0.5404 0.2637  0.0422  0.1498  246 TYR B CE1 
7043 C CE2 . TYR B 246 ? 0.6183 1.2276 0.5550 0.2530  0.0373  0.1462  246 TYR B CE2 
7044 C CZ  . TYR B 246 ? 0.6322 1.2003 0.5609 0.2662  0.0419  0.1530  246 TYR B CZ  
7045 O OH  . TYR B 246 ? 0.6561 1.2037 0.5757 0.2811  0.0466  0.1627  246 TYR B OH  
7046 N N   . GLY B 247 ? 0.5192 1.1121 0.4829 0.1783  0.0246  0.1026  247 GLY B N   
7047 C CA  . GLY B 247 ? 0.5074 1.1076 0.4759 0.1610  0.0221  0.0929  247 GLY B CA  
7048 C C   . GLY B 247 ? 0.5263 1.1173 0.4931 0.1692  0.0235  0.0941  247 GLY B C   
7049 O O   . GLY B 247 ? 0.5628 1.1276 0.5243 0.1853  0.0265  0.1013  247 GLY B O   
7050 N N   . ILE B 248 ? 0.5142 1.1260 0.4845 0.1576  0.0216  0.0868  248 ILE B N   
7051 C CA  . ILE B 248 ? 0.5455 1.1498 0.5147 0.1630  0.0227  0.0867  248 ILE B CA  
7052 C C   . ILE B 248 ? 0.5394 1.1399 0.5129 0.1411  0.0203  0.0762  248 ILE B C   
7053 O O   . ILE B 248 ? 0.5364 1.1599 0.5131 0.1242  0.0182  0.0692  248 ILE B O   
7054 C CB  . ILE B 248 ? 0.5590 1.2060 0.5260 0.1802  0.0242  0.0920  248 ILE B CB  
7055 C CG1 . ILE B 248 ? 0.5633 1.1979 0.5278 0.1887  0.0260  0.0930  248 ILE B CG1 
7056 C CG2 . ILE B 248 ? 0.5325 1.2324 0.5043 0.1684  0.0217  0.0861  248 ILE B CG2 
7057 C CD1 . ILE B 248 ? 0.5978 1.2596 0.5570 0.2130  0.0289  0.1016  248 ILE B CD1 
7058 N N   . LYS B 249 ? 0.5561 1.1250 0.5286 0.1410  0.0210  0.0749  249 LYS B N   
7059 C CA  . LYS B 249 ? 0.5609 1.1311 0.5362 0.1244  0.0195  0.0662  249 LYS B CA  
7060 C C   . LYS B 249 ? 0.5744 1.1614 0.5482 0.1359  0.0209  0.0684  249 LYS B C   
7061 O O   . LYS B 249 ? 0.5748 1.1455 0.5443 0.1545  0.0233  0.0756  249 LYS B O   
7062 C CB  . LYS B 249 ? 0.5619 1.0840 0.5372 0.1132  0.0188  0.0620  249 LYS B CB  
7063 C CG  . LYS B 249 ? 0.5642 1.0840 0.5407 0.0998  0.0180  0.0543  249 LYS B CG  
7064 C CD  . LYS B 249 ? 0.5922 1.0647 0.5679 0.0938  0.0177  0.0518  249 LYS B CD  
7065 C CE  . LYS B 249 ? 0.6106 1.0606 0.5834 0.1096  0.0194  0.0572  249 LYS B CE  
7066 N NZ  . LYS B 249 ? 0.6006 1.0378 0.5731 0.1024  0.0191  0.0520  249 LYS B NZ  
7067 N N   . VAL B 250 ? 0.5958 1.2153 0.5724 0.1246  0.0198  0.0622  250 VAL B N   
7068 C CA  . VAL B 250 ? 0.6301 1.2694 0.6059 0.1337  0.0211  0.0635  250 VAL B CA  
7069 C C   . VAL B 250 ? 0.6631 1.2930 0.6407 0.1157  0.0201  0.0548  250 VAL B C   
7070 O O   . VAL B 250 ? 0.6489 1.2832 0.6286 0.0946  0.0185  0.0468  250 VAL B O   
7071 C CB  . VAL B 250 ? 0.6162 1.3142 0.5934 0.1408  0.0213  0.0657  250 VAL B CB  
7072 C CG1 . VAL B 250 ? 0.6193 1.3299 0.5932 0.1629  0.0239  0.0726  250 VAL B CG1 
7073 C CG2 . VAL B 250 ? 0.6106 1.3242 0.5874 0.1476  0.0210  0.0705  250 VAL B CG2 
7074 N N   . ASP B 251 ? 0.7315 1.3461 0.7070 0.1244  0.0215  0.0564  251 ASP B N   
7075 C CA  . ASP B 251 ? 0.7804 1.3840 0.7567 0.1098  0.0210  0.0491  251 ASP B CA  
7076 C C   . ASP B 251 ? 0.7836 1.4311 0.7612 0.1115  0.0218  0.0479  251 ASP B C   
7077 O O   . ASP B 251 ? 0.8266 1.4863 0.8020 0.1311  0.0236  0.0543  251 ASP B O   
7078 C CB  . ASP B 251 ? 0.8430 1.3987 0.8160 0.1171  0.0219  0.0510  251 ASP B CB  
7079 C CG  . ASP B 251 ? 0.9191 1.4532 0.8927 0.0993  0.0209  0.0430  251 ASP B CG  
7080 O OD1 . ASP B 251 ? 0.9255 1.4825 0.8998 0.0929  0.0212  0.0389  251 ASP B OD1 
7081 O OD2 . ASP B 251 ? 0.9565 1.4508 0.9293 0.0923  0.0200  0.0410  251 ASP B OD2 
7082 N N   . ILE B 252 ? 0.7555 1.4270 0.7356 0.0911  0.0207  0.0398  252 ILE B N   
7083 C CA  . ILE B 252 ? 0.7551 1.4697 0.7367 0.0891  0.0215  0.0376  252 ILE B CA  
7084 C C   . ILE B 252 ? 0.7781 1.4712 0.7579 0.0897  0.0226  0.0359  252 ILE B C   
7085 O O   . ILE B 252 ? 0.7580 1.4185 0.7367 0.0744  0.0221  0.0299  252 ILE B O   
7086 C CB  . ILE B 252 ? 0.7248 1.4711 0.7084 0.0649  0.0204  0.0289  252 ILE B CB  
7087 C CG1 . ILE B 252 ? 0.6866 1.4530 0.6713 0.0643  0.0192  0.0304  252 ILE B CG1 
7088 C CG2 . ILE B 252 ? 0.7094 1.5037 0.6948 0.0623  0.0214  0.0266  252 ILE B CG2 
7089 C CD1 . ILE B 252 ? 0.6881 1.4660 0.6726 0.0378  0.0183  0.0210  252 ILE B CD1 
7090 N N   . ARG B 253 ? 0.7962 1.5068 0.7751 0.1083  0.0243  0.0414  253 ARG B N   
7091 C CA  . ARG B 253 ? 0.8052 1.4994 0.7821 0.1103  0.0256  0.0401  253 ARG B CA  
7092 C C   . ARG B 253 ? 0.7834 1.5078 0.7626 0.0912  0.0256  0.0322  253 ARG B C   
7093 O O   . ARG B 253 ? 0.8050 1.5798 0.7871 0.0886  0.0258  0.0315  253 ARG B O   
7094 C CB  . ARG B 253 ? 0.8260 1.5265 0.7994 0.1375  0.0280  0.0489  253 ARG B CB  
7095 C CG  . ARG B 253 ? 0.8702 1.5596 0.8411 0.1408  0.0295  0.0477  253 ARG B CG  
7096 C CD  . ARG B 253 ? 0.9150 1.5784 0.8793 0.1662  0.0320  0.0558  253 ARG B CD  
7097 N NE  . ARG B 253 ? 1.0114 1.7001 0.9733 0.1880  0.0337  0.0644  253 ARG B NE  
7098 C CZ  . ARG B 253 ? 1.0410 1.7206 0.9954 0.2130  0.0369  0.0725  253 ARG B CZ  
7099 N NH1 . ARG B 253 ? 1.0439 1.6898 0.9928 0.2189  0.0386  0.0725  253 ARG B NH1 
7100 N NH2 . ARG B 253 ? 1.0151 1.7189 0.9665 0.2326  0.0388  0.0804  253 ARG B NH2 
7101 N N   . ASP B 254 ? 0.7851 1.4780 0.7626 0.0772  0.0256  0.0263  254 ASP B N   
7102 C CA  . ASP B 254 ? 0.7650 1.4771 0.7429 0.0584  0.0263  0.0187  254 ASP B CA  
7103 C C   . ASP B 254 ? 0.7543 1.5111 0.7347 0.0411  0.0260  0.0135  254 ASP B C   
7104 O O   . ASP B 254 ? 0.7596 1.5646 0.7424 0.0423  0.0269  0.0135  254 ASP B O   
7105 C CB  . ASP B 254 ? 0.7644 1.4940 0.7420 0.0711  0.0282  0.0213  254 ASP B CB  
7106 C CG  . ASP B 254 ? 0.7643 1.4913 0.7405 0.0528  0.0293  0.0138  254 ASP B CG  
7107 O OD1 . ASP B 254 ? 0.7677 1.4836 0.7426 0.0298  0.0288  0.0064  254 ASP B OD1 
7108 O OD2 . ASP B 254 ? 0.7409 1.4759 0.7163 0.0618  0.0309  0.0154  254 ASP B OD2 
7109 N N   . ALA B 255 ? 0.7379 1.4787 0.7172 0.0248  0.0248  0.0089  255 ALA B N   
7110 C CA  . ALA B 255 ? 0.7504 1.5285 0.7304 0.0064  0.0246  0.0031  255 ALA B CA  
7111 C C   . ALA B 255 ? 0.7660 1.5687 0.7446 -0.0125 0.0265  -0.0043 255 ALA B C   
7112 O O   . ALA B 255 ? 0.8063 1.6612 0.7874 -0.0171 0.0269  -0.0058 255 ALA B O   
7113 C CB  . ALA B 255 ? 0.7424 1.4904 0.7196 -0.0081 0.0236  -0.0009 255 ALA B CB  
7114 N N   . TYR B 256 ? 0.7947 1.5605 0.7690 -0.0230 0.0276  -0.0087 256 TYR B N   
7115 C CA  . TYR B 256 ? 0.8081 1.5888 0.7793 -0.0424 0.0300  -0.0160 256 TYR B CA  
7116 C C   . TYR B 256 ? 0.7935 1.6171 0.7689 -0.0313 0.0310  -0.0129 256 TYR B C   
7117 O O   . TYR B 256 ? 0.7693 1.6351 0.7451 -0.0452 0.0325  -0.0177 256 TYR B O   
7118 C CB  . TYR B 256 ? 0.8703 1.5987 0.8356 -0.0512 0.0311  -0.0198 256 TYR B CB  
7119 C CG  . TYR B 256 ? 0.9525 1.6439 0.9118 -0.0678 0.0311  -0.0249 256 TYR B CG  
7120 C CD1 . TYR B 256 ? 0.9804 1.6383 0.9406 -0.0573 0.0289  -0.0208 256 TYR B CD1 
7121 C CD2 . TYR B 256 ? 0.9882 1.6772 0.9399 -0.0937 0.0336  -0.0338 256 TYR B CD2 
7122 C CE1 . TYR B 256 ? 1.0335 1.6587 0.9879 -0.0713 0.0290  -0.0252 256 TYR B CE1 
7123 C CE2 . TYR B 256 ? 1.0079 1.6617 0.9524 -0.1076 0.0342  -0.0383 256 TYR B CE2 
7124 C CZ  . TYR B 256 ? 1.0356 1.6584 0.9819 -0.0959 0.0317  -0.0339 256 TYR B CZ  
7125 O OH  . TYR B 256 ? 1.0523 1.6413 0.9913 -0.1085 0.0324  -0.0380 256 TYR B OH  
7126 N N   . GLY B 257 ? 0.7866 1.5994 0.7643 -0.0063 0.0305  -0.0050 257 GLY B N   
7127 C CA  . GLY B 257 ? 0.7654 1.6135 0.7459 0.0076  0.0319  -0.0012 257 GLY B CA  
7128 C C   . GLY B 257 ? 0.7762 1.6825 0.7617 0.0192  0.0315  0.0033  257 GLY B C   
7129 O O   . GLY B 257 ? 0.8025 1.7510 0.7904 0.0247  0.0329  0.0045  257 GLY B O   
7130 N N   . ASN B 258 ? 0.7517 1.6617 0.7386 0.0238  0.0296  0.0060  258 ASN B N   
7131 C CA  . ASN B 258 ? 0.7386 1.7029 0.7297 0.0368  0.0291  0.0110  258 ASN B CA  
7132 C C   . ASN B 258 ? 0.7422 1.7536 0.7352 0.0144  0.0287  0.0041  258 ASN B C   
7133 O O   . ASN B 258 ? 0.6984 1.7587 0.6951 0.0225  0.0280  0.0074  258 ASN B O   
7134 C CB  . ASN B 258 ? 0.7310 1.6767 0.7220 0.0586  0.0278  0.0194  258 ASN B CB  
7135 C CG  . ASN B 258 ? 0.7473 1.6717 0.7363 0.0869  0.0290  0.0284  258 ASN B CG  
7136 O OD1 . ASN B 258 ? 0.7726 1.6519 0.7587 0.0984  0.0286  0.0328  258 ASN B OD1 
7137 N ND2 . ASN B 258 ? 0.7318 1.6883 0.7215 0.0978  0.0309  0.0309  258 ASN B ND2 
7138 N N   . VAL B 259 ? 0.7645 1.7609 0.7541 -0.0136 0.0295  -0.0055 259 VAL B N   
7139 C CA  . VAL B 259 ? 0.7664 1.8052 0.7559 -0.0384 0.0300  -0.0136 259 VAL B CA  
7140 C C   . VAL B 259 ? 0.7867 1.8873 0.7804 -0.0356 0.0313  -0.0131 259 VAL B C   
7141 O O   . VAL B 259 ? 0.7977 1.8964 0.7906 -0.0382 0.0333  -0.0146 259 VAL B O   
7142 C CB  . VAL B 259 ? 0.7690 1.7740 0.7513 -0.0685 0.0317  -0.0240 259 VAL B CB  
7143 C CG1 . VAL B 259 ? 0.7691 1.8182 0.7495 -0.0955 0.0329  -0.0329 259 VAL B CG1 
7144 C CG2 . VAL B 259 ? 0.7715 1.7187 0.7495 -0.0709 0.0305  -0.0244 259 VAL B CG2 
7145 N N   . LYS B 260 ? 0.7983 1.9542 0.7965 -0.0288 0.0301  -0.0103 260 LYS B N   
7146 C CA  . LYS B 260 ? 0.7785 2.0016 0.7811 -0.0291 0.0312  -0.0106 260 LYS B CA  
7147 C C   . LYS B 260 ? 0.7436 1.9848 0.7432 -0.0646 0.0329  -0.0226 260 LYS B C   
7148 O O   . LYS B 260 ? 0.6918 1.9520 0.6898 -0.0844 0.0323  -0.0288 260 LYS B O   
7149 C CB  . LYS B 260 ? 0.8163 2.0942 0.8239 -0.0135 0.0293  -0.0048 260 LYS B CB  
7150 C CG  . LYS B 260 ? 0.8531 2.1211 0.8623 0.0238  0.0287  0.0077  260 LYS B CG  
7151 C CD  . LYS B 260 ? 0.8728 2.1641 0.8837 0.0360  0.0265  0.0129  260 LYS B CD  
7152 C CE  . LYS B 260 ? 0.8808 2.1347 0.8898 0.0680  0.0263  0.0241  260 LYS B CE  
7153 N NZ  . LYS B 260 ? 0.8860 2.1482 0.8952 0.0763  0.0244  0.0282  260 LYS B NZ  
7154 N N   . ILE B 261 ? 0.7288 1.9613 0.7264 -0.0727 0.0356  -0.0258 261 ILE B N   
7155 C CA  . ILE B 261 ? 0.7583 1.9977 0.7508 -0.1067 0.0383  -0.0371 261 ILE B CA  
7156 C C   . ILE B 261 ? 0.7698 2.0809 0.7648 -0.1243 0.0386  -0.0425 261 ILE B C   
7157 O O   . ILE B 261 ? 0.7582 2.0685 0.7473 -0.1533 0.0396  -0.0520 261 ILE B O   
7158 C CB  . ILE B 261 ? 0.7761 2.0010 0.7668 -0.1082 0.0412  -0.0381 261 ILE B CB  
7159 C CG1 . ILE B 261 ? 0.7703 1.9257 0.7583 -0.0915 0.0407  -0.0331 261 ILE B CG1 
7160 C CG2 . ILE B 261 ? 0.7861 2.0107 0.7695 -0.1441 0.0447  -0.0497 261 ILE B CG2 
7161 C CD1 . ILE B 261 ? 0.7789 1.9301 0.7679 -0.0781 0.0426  -0.0294 261 ILE B CD1 
7162 N N   . PRO B 262 ? 0.7677 2.1412 0.7707 -0.1067 0.0379  -0.0367 262 PRO B N   
7163 C CA  . PRO B 262 ? 0.7920 2.2369 0.7977 -0.1234 0.0379  -0.0420 262 PRO B CA  
7164 C C   . PRO B 262 ? 0.7924 2.2409 0.7962 -0.1344 0.0356  -0.0454 262 PRO B C   
7165 O O   . PRO B 262 ? 0.8305 2.3103 0.8312 -0.1630 0.0365  -0.0548 262 PRO B O   
7166 C CB  . PRO B 262 ? 0.7863 2.2893 0.8011 -0.0938 0.0369  -0.0322 262 PRO B CB  
7167 C CG  . PRO B 262 ? 0.7666 2.2326 0.7812 -0.0731 0.0383  -0.0259 262 PRO B CG  
7168 C CD  . PRO B 262 ? 0.7659 2.1496 0.7744 -0.0734 0.0377  -0.0261 262 PRO B CD  
7169 N N   . VAL B 263 ? 0.7743 2.1890 0.7789 -0.1129 0.0329  -0.0381 263 VAL B N   
7170 C CA  . VAL B 263 ? 0.7537 2.1677 0.7564 -0.1205 0.0306  -0.0404 263 VAL B CA  
7171 C C   . VAL B 263 ? 0.7586 2.1201 0.7513 -0.1507 0.0321  -0.0506 263 VAL B C   
7172 O O   . VAL B 263 ? 0.7372 2.1143 0.7260 -0.1714 0.0318  -0.0576 263 VAL B O   
7173 C CB  . VAL B 263 ? 0.7441 2.1390 0.7504 -0.0875 0.0277  -0.0290 263 VAL B CB  
7174 C CG1 . VAL B 263 ? 0.7177 2.1093 0.7216 -0.0961 0.0255  -0.0315 263 VAL B CG1 
7175 C CG2 . VAL B 263 ? 0.7261 2.1767 0.7402 -0.0580 0.0268  -0.0190 263 VAL B CG2 
7176 N N   . LEU B 264 ? 0.7678 2.0677 0.7553 -0.1529 0.0340  -0.0515 264 LEU B N   
7177 C CA  . LEU B 264 ? 0.7876 2.0349 0.7641 -0.1798 0.0362  -0.0607 264 LEU B CA  
7178 C C   . LEU B 264 ? 0.8191 2.0924 0.7885 -0.2150 0.0399  -0.0725 264 LEU B C   
7179 O O   . LEU B 264 ? 0.8537 2.1066 0.8132 -0.2405 0.0416  -0.0812 264 LEU B O   
7180 C CB  . LEU B 264 ? 0.7785 1.9553 0.7513 -0.1711 0.0372  -0.0579 264 LEU B CB  
7181 C CG  . LEU B 264 ? 0.7793 1.8953 0.7398 -0.1945 0.0397  -0.0659 264 LEU B CG  
7182 C CD1 . LEU B 264 ? 0.7760 1.8756 0.7322 -0.2016 0.0382  -0.0683 264 LEU B CD1 
7183 C CD2 . LEU B 264 ? 0.7778 1.8318 0.7366 -0.1812 0.0401  -0.0617 264 LEU B CD2 
7184 N N   . CYS B 265 ? 0.8298 2.1474 0.8035 -0.2163 0.0415  -0.0728 265 CYS B N   
7185 C CA  . CYS B 265 ? 0.8753 2.2236 0.8427 -0.2497 0.0453  -0.0837 265 CYS B CA  
7186 C C   . CYS B 265 ? 0.8856 2.2880 0.8527 -0.2670 0.0444  -0.0896 265 CYS B C   
7187 O O   . CYS B 265 ? 0.8918 2.2920 0.8482 -0.3000 0.0475  -0.1007 265 CYS B O   
7188 C CB  . CYS B 265 ? 0.8672 2.2543 0.8404 -0.2450 0.0471  -0.0818 265 CYS B CB  
7189 S SG  . CYS B 265 ? 0.9093 2.2315 0.8782 -0.2383 0.0499  -0.0796 265 CYS B SG  
7190 N N   . LYS B 266 ? 0.9026 2.3517 0.8803 -0.2444 0.0403  -0.0821 266 LYS B N   
7191 C CA  . LYS B 266 ? 0.9443 2.4471 0.9228 -0.2567 0.0386  -0.0864 266 LYS B CA  
7192 C C   . LYS B 266 ? 0.9870 2.4453 0.9565 -0.2688 0.0379  -0.0910 266 LYS B C   
7193 O O   . LYS B 266 ? 1.0033 2.4958 0.9705 -0.2839 0.0370  -0.0964 266 LYS B O   
7194 C CB  . LYS B 266 ? 0.9219 2.4814 0.9134 -0.2252 0.0344  -0.0758 266 LYS B CB  
7195 C CG  . LYS B 266 ? 0.9041 2.5058 0.9047 -0.2065 0.0348  -0.0693 266 LYS B CG  
7196 C CD  . LYS B 266 ? 0.9053 2.5815 0.9076 -0.2289 0.0366  -0.0766 266 LYS B CD  
7197 C CE  . LYS B 266 ? 0.8926 2.6130 0.9043 -0.2073 0.0370  -0.0692 266 LYS B CE  
7198 N NZ  . LYS B 266 ? 0.8991 2.6997 0.9139 -0.2272 0.0384  -0.0756 266 LYS B NZ  
7199 N N   . LEU B 267 ? 1.0304 2.4135 0.9947 -0.2618 0.0385  -0.0887 267 LEU B N   
7200 C CA  . LEU B 267 ? 1.0461 2.3800 1.0018 -0.2700 0.0381  -0.0918 267 LEU B CA  
7201 C C   . LEU B 267 ? 1.0929 2.3857 1.0325 -0.3045 0.0432  -0.1038 267 LEU B C   
7202 O O   . LEU B 267 ? 1.0956 2.3791 1.0252 -0.3255 0.0443  -0.1114 267 LEU B O   
7203 C CB  . LEU B 267 ? 1.0289 2.3055 0.9882 -0.2408 0.0358  -0.0818 267 LEU B CB  
7204 C CG  . LEU B 267 ? 1.0157 2.2747 0.9763 -0.2267 0.0323  -0.0770 267 LEU B CG  
7205 C CD1 . LEU B 267 ? 1.0062 2.2014 0.9684 -0.2033 0.0313  -0.0688 267 LEU B CD1 
7206 C CD2 . LEU B 267 ? 1.0090 2.2532 0.9580 -0.2543 0.0338  -0.0870 267 LEU B CD2 
7207 N N   . ILE B 268 ? 1.1451 2.4120 1.0813 -0.3095 0.0466  -0.1051 268 ILE B N   
7208 C CA  . ILE B 268 ? 1.1916 2.4193 1.1113 -0.3411 0.0523  -0.1158 268 ILE B CA  
7209 C C   . ILE B 268 ? 1.2250 2.5056 1.1383 -0.3736 0.0555  -0.1266 268 ILE B C   
7210 O O   . ILE B 268 ? 1.2571 2.5143 1.1543 -0.4036 0.0599  -0.1371 268 ILE B O   
7211 C CB  . ILE B 268 ? 1.1847 2.3735 1.1027 -0.3360 0.0550  -0.1135 268 ILE B CB  
7212 C CG1 . ILE B 268 ? 1.1710 2.3115 1.0958 -0.3037 0.0516  -0.1028 268 ILE B CG1 
7213 C CG2 . ILE B 268 ? 1.2169 2.3592 1.1159 -0.3670 0.0614  -0.1239 268 ILE B CG2 
7214 C CD1 . ILE B 268 ? 1.1672 2.2975 1.0979 -0.2868 0.0520  -0.0967 268 ILE B CD1 
7215 N N   . GLN B 269 ? 1.2140 2.5662 1.1393 -0.3673 0.0536  -0.1241 269 GLN B N   
7216 C CA  . GLN B 269 ? 1.2519 2.6665 1.1740 -0.3957 0.0558  -0.1336 269 GLN B CA  
7217 C C   . GLN B 269 ? 1.2542 2.6886 1.1725 -0.4069 0.0538  -0.1384 269 GLN B C   
7218 O O   . GLN B 269 ? 1.2435 2.6939 1.1500 -0.4404 0.0574  -0.1500 269 GLN B O   
7219 C CB  . GLN B 269 ? 1.2465 2.7355 1.1841 -0.3811 0.0536  -0.1281 269 GLN B CB  
7220 C CG  . GLN B 269 ? 1.2892 2.8454 1.2242 -0.4113 0.0563  -0.1379 269 GLN B CG  
7221 C CD  . GLN B 269 ? 1.2950 2.9080 1.2419 -0.4009 0.0563  -0.1335 269 GLN B CD  
7222 O OE1 . GLN B 269 ? 1.2941 2.9071 1.2529 -0.3669 0.0533  -0.1220 269 GLN B OE1 
7223 N NE2 . GLN B 269 ? 1.2716 2.9331 1.2146 -0.4304 0.0600  -0.1428 269 GLN B NE2 
7224 N N   . SER B 270 ? 1.2565 2.6882 1.1840 -0.3791 0.0485  -0.1294 270 SER B N   
7225 C CA  . SER B 270 ? 1.2721 2.7225 1.1974 -0.3850 0.0460  -0.1324 270 SER B CA  
7226 C C   . SER B 270 ? 1.3109 2.7019 1.2176 -0.4100 0.0497  -0.1417 270 SER B C   
7227 O O   . SER B 270 ? 1.3199 2.7331 1.2183 -0.4330 0.0505  -0.1504 270 SER B O   
7228 C CB  . SER B 270 ? 1.2439 2.6977 1.1825 -0.3474 0.0400  -0.1196 270 SER B CB  
7229 O OG  . SER B 270 ? 1.2228 2.7445 1.1764 -0.3268 0.0369  -0.1122 270 SER B OG  
7230 N N   . ILE B 271 ? 1.3377 2.6540 1.2373 -0.4050 0.0519  -0.1398 271 ILE B N   
7231 C CA  . ILE B 271 ? 1.3578 2.6111 1.2390 -0.4247 0.0557  -0.1473 271 ILE B CA  
7232 C C   . ILE B 271 ? 1.3755 2.6501 1.2407 -0.4649 0.0606  -0.1616 271 ILE B C   
7233 O O   . ILE B 271 ? 1.4056 2.6959 1.2650 -0.4859 0.0651  -0.1680 271 ILE B O   
7234 C CB  . ILE B 271 ? 1.3515 2.5315 1.2247 -0.4221 0.0593  -0.1460 271 ILE B CB  
7235 C CG1 . ILE B 271 ? 1.3424 2.4947 1.2295 -0.3839 0.0545  -0.1326 271 ILE B CG1 
7236 C CG2 . ILE B 271 ? 1.3764 2.4951 1.2281 -0.4447 0.0643  -0.1545 271 ILE B CG2 
7237 C CD1 . ILE B 271 ? 1.3516 2.4430 1.2340 -0.3782 0.0573  -0.1301 271 ILE B CD1 
7238 N N   . PRO B 272 ? 1.3865 2.6630 1.2440 -0.4761 0.0600  -0.1667 272 PRO B N   
7239 C CA  . PRO B 272 ? 1.4329 2.7241 1.2727 -0.5153 0.0650  -0.1810 272 PRO B CA  
7240 C C   . PRO B 272 ? 1.4742 2.7156 1.2944 -0.5414 0.0732  -0.1894 272 PRO B C   
7241 O O   . PRO B 272 ? 1.4693 2.6386 1.2798 -0.5361 0.0758  -0.1877 272 PRO B O   
7242 C CB  . PRO B 272 ? 1.4461 2.7097 1.2775 -0.5162 0.0639  -0.1829 272 PRO B CB  
7243 C CG  . PRO B 272 ? 1.3997 2.6797 1.2514 -0.4780 0.0562  -0.1696 272 PRO B CG  
7244 C CD  . PRO B 272 ? 1.3773 2.6442 1.2423 -0.4521 0.0546  -0.1592 272 PRO B CD  
7245 N N   . THR B 273 ? 1.5141 2.7955 1.3287 -0.5687 0.0773  -0.1981 273 THR B N   
7246 C CA  . THR B 273 ? 1.5297 2.7714 1.3268 -0.5927 0.0854  -0.2053 273 THR B CA  
7247 C C   . THR B 273 ? 1.5559 2.7257 1.3262 -0.6144 0.0921  -0.2138 273 THR B C   
7248 O O   . THR B 273 ? 1.5601 2.6725 1.3162 -0.6218 0.0980  -0.2156 273 THR B O   
7249 C CB  . THR B 273 ? 1.5314 2.8345 1.3261 -0.6216 0.0890  -0.2141 273 THR B CB  
7250 O OG1 . THR B 273 ? 1.5240 2.8855 1.3189 -0.6375 0.0871  -0.2207 273 THR B OG1 
7251 C CG2 . THR B 273 ? 1.5019 2.8523 1.3184 -0.6004 0.0853  -0.2053 273 THR B CG2 
7252 N N   . HIS B 274 ? 1.5743 2.7467 1.3372 -0.6231 0.0911  -0.2186 274 HIS B N   
7253 C CA  . HIS B 274 ? 1.6415 2.7474 1.3778 -0.6425 0.0975  -0.2266 274 HIS B CA  
7254 C C   . HIS B 274 ? 1.6410 2.6736 1.3764 -0.6167 0.0965  -0.2181 274 HIS B C   
7255 O O   . HIS B 274 ? 1.6624 2.6420 1.3792 -0.6247 0.1002  -0.2223 274 HIS B O   
7256 C CB  . HIS B 274 ? 1.6922 2.8256 1.4205 -0.6601 0.0969  -0.2346 274 HIS B CB  
7257 C CG  . HIS B 274 ? 1.7024 2.8659 1.4512 -0.6305 0.0877  -0.2254 274 HIS B CG  
7258 N ND1 . HIS B 274 ? 1.7241 2.8372 1.4722 -0.6099 0.0854  -0.2193 274 HIS B ND1 
7259 C CD2 . HIS B 274 ? 1.6872 2.9291 1.4571 -0.6186 0.0805  -0.2213 274 HIS B CD2 
7260 C CE1 . HIS B 274 ? 1.6942 2.8496 1.4618 -0.5866 0.0774  -0.2117 274 HIS B CE1 
7261 N NE2 . HIS B 274 ? 1.6898 2.9233 1.4703 -0.5914 0.0745  -0.2128 274 HIS B NE2 
7262 N N   . LEU B 275 ? 1.6140 2.6432 1.3686 -0.5859 0.0919  -0.2062 275 LEU B N   
7263 C CA  . LEU B 275 ? 1.6010 2.5632 1.3561 -0.5610 0.0909  -0.1978 275 LEU B CA  
7264 C C   . LEU B 275 ? 1.5923 2.5234 1.3469 -0.5556 0.0939  -0.1944 275 LEU B C   
7265 O O   . LEU B 275 ? 1.6057 2.4759 1.3402 -0.5674 0.1006  -0.1984 275 LEU B O   
7266 C CB  . LEU B 275 ? 1.5562 2.5368 1.3350 -0.5246 0.0817  -0.1855 275 LEU B CB  
7267 C CG  . LEU B 275 ? 1.5530 2.5603 1.3343 -0.5236 0.0777  -0.1866 275 LEU B CG  
7268 C CD1 . LEU B 275 ? 1.5159 2.5540 1.3228 -0.4874 0.0690  -0.1737 275 LEU B CD1 
7269 C CD2 . LEU B 275 ? 1.5863 2.5312 1.3476 -0.5321 0.0815  -0.1911 275 LEU B CD2 
7270 N N   . LEU B 276 ? 1.5731 2.5462 1.3490 -0.5373 0.0893  -0.1868 276 LEU B N   
7271 C CA  . LEU B 276 ? 1.6120 2.5615 1.3894 -0.5305 0.0916  -0.1831 276 LEU B CA  
7272 C C   . LEU B 276 ? 1.6417 2.6078 1.4050 -0.5634 0.0990  -0.1932 276 LEU B C   
7273 O O   . LEU B 276 ? 1.6802 2.6018 1.4189 -0.5886 0.1068  -0.2020 276 LEU B O   
7274 C CB  . LEU B 276 ? 1.5984 2.5838 1.4027 -0.4972 0.0842  -0.1709 276 LEU B CB  
7275 C CG  . LEU B 276 ? 1.5626 2.5153 1.3716 -0.4806 0.0848  -0.1642 276 LEU B CG  
7276 C CD1 . LEU B 276 ? 1.5557 2.4358 1.3597 -0.4632 0.0843  -0.1589 276 LEU B CD1 
7277 C CD2 . LEU B 276 ? 1.5262 2.5299 1.3595 -0.4545 0.0786  -0.1547 276 LEU B CD2 
7278 N N   . ASP B 277 ? 1.6383 2.6684 1.4166 -0.5628 0.0967  -0.1919 277 ASP B N   
7279 C CA  . ASP B 277 ? 1.6612 2.7157 1.4290 -0.5928 0.1033  -0.2008 277 ASP B CA  
7280 C C   . ASP B 277 ? 1.6625 2.7996 1.4520 -0.5855 0.0987  -0.1974 277 ASP B C   
7281 O O   . ASP B 277 ? 1.6423 2.8021 1.4537 -0.5527 0.0916  -0.1863 277 ASP B O   
7282 C CB  . ASP B 277 ? 1.6522 2.6491 1.4079 -0.5955 0.1093  -0.2005 277 ASP B CB  
7283 C CG  . ASP B 277 ? 1.6384 2.6495 1.3783 -0.6305 0.1176  -0.2108 277 ASP B CG  
7284 O OD1 . ASP B 277 ? 1.6724 2.7023 1.3977 -0.6615 0.1219  -0.2217 277 ASP B OD1 
7285 O OD2 . ASP B 277 ? 1.5844 2.5873 1.3257 -0.6276 0.1201  -0.2082 277 ASP B OD2 
7286 N N   . SER B 278 ? 1.6734 2.8551 1.4557 -0.6163 0.1032  -0.2070 278 SER B N   
7287 C CA  . SER B 278 ? 1.6344 2.8969 1.4352 -0.6127 0.1000  -0.2047 278 SER B CA  
7288 C C   . SER B 278 ? 1.6248 2.8801 1.4341 -0.5974 0.1007  -0.1979 278 SER B C   
7289 O O   . SER B 278 ? 1.5935 2.8982 1.4241 -0.5740 0.0954  -0.1896 278 SER B O   
7290 C CB  . SER B 278 ? 1.6125 2.9237 1.4017 -0.6529 0.1052  -0.2178 278 SER B CB  
7291 O OG  . SER B 278 ? 1.5296 2.9225 1.3369 -0.6495 0.1022  -0.2156 278 SER B OG  
7292 N N   . GLU B 279 ? 1.6470 2.8393 1.4386 -0.6098 0.1076  -0.2012 279 GLU B N   
7293 C CA  . GLU B 279 ? 1.6397 2.8230 1.4358 -0.6006 0.1095  -0.1966 279 GLU B CA  
7294 C C   . GLU B 279 ? 1.6448 2.7624 1.4442 -0.5702 0.1072  -0.1867 279 GLU B C   
7295 O O   . GLU B 279 ? 1.6408 2.7625 1.4522 -0.5500 0.1053  -0.1792 279 GLU B O   
7296 C CB  . GLU B 279 ? 1.6459 2.8142 1.4200 -0.6377 0.1195  -0.2074 279 GLU B CB  
7297 C CG  . GLU B 279 ? 1.6371 2.8788 1.4105 -0.6676 0.1221  -0.2165 279 GLU B CG  
7298 C CD  . GLU B 279 ? 1.6427 2.8817 1.4014 -0.6965 0.1310  -0.2239 279 GLU B CD  
7299 O OE1 . GLU B 279 ? 1.6513 2.8239 1.3956 -0.6976 0.1364  -0.2235 279 GLU B OE1 
7300 O OE2 . GLU B 279 ? 1.6234 2.9280 1.3844 -0.7184 0.1329  -0.2302 279 GLU B OE2 
7301 N N   . LYS B 280 ? 1.6546 2.7127 1.4428 -0.5672 0.1074  -0.1870 280 LYS B N   
7302 C CA  . LYS B 280 ? 1.6260 2.6250 1.4183 -0.5376 0.1044  -0.1775 280 LYS B CA  
7303 C C   . LYS B 280 ? 1.5511 2.5793 1.3683 -0.5014 0.0949  -0.1662 280 LYS B C   
7304 O O   . LYS B 280 ? 1.5344 2.5321 1.3607 -0.4735 0.0915  -0.1570 280 LYS B O   
7305 C CB  . LYS B 280 ? 1.6507 2.5781 1.4224 -0.5462 0.1082  -0.1814 280 LYS B CB  
7306 C CG  . LYS B 280 ? 1.7011 2.5772 1.4472 -0.5715 0.1179  -0.1890 280 LYS B CG  
7307 C CD  . LYS B 280 ? 1.7161 2.5244 1.4404 -0.5795 0.1221  -0.1929 280 LYS B CD  
7308 C CE  . LYS B 280 ? 1.7371 2.4929 1.4339 -0.6036 0.1325  -0.1999 280 LYS B CE  
7309 N NZ  . LYS B 280 ? 1.7492 2.4333 1.4244 -0.6062 0.1367  -0.2020 280 LYS B NZ  
7310 N N   . LYS B 281 ? 1.5164 2.6031 1.3434 -0.5025 0.0909  -0.1672 281 LYS B N   
7311 C CA  . LYS B 281 ? 1.4844 2.6142 1.3351 -0.4702 0.0827  -0.1567 281 LYS B CA  
7312 C C   . LYS B 281 ? 1.4535 2.6162 1.3179 -0.4551 0.0817  -0.1506 281 LYS B C   
7313 O O   . LYS B 281 ? 1.4466 2.5987 1.3243 -0.4232 0.0771  -0.1401 281 LYS B O   
7314 C CB  . LYS B 281 ? 1.4918 2.6853 1.3481 -0.4786 0.0798  -0.1602 281 LYS B CB  
7315 C CG  . LYS B 281 ? 1.4645 2.7260 1.3438 -0.4528 0.0733  -0.1514 281 LYS B CG  
7316 C CD  . LYS B 281 ? 1.4616 2.8016 1.3432 -0.4742 0.0741  -0.1583 281 LYS B CD  
7317 C CE  . LYS B 281 ? 1.4104 2.8123 1.3102 -0.4552 0.0713  -0.1511 281 LYS B CE  
7318 N NZ  . LYS B 281 ? 1.4280 2.9047 1.3283 -0.4801 0.0733  -0.1588 281 LYS B NZ  
7319 N N   . ASN B 282 ? 1.4588 2.6596 1.3187 -0.4790 0.0862  -0.1575 282 ASN B N   
7320 C CA  . ASN B 282 ? 1.4303 2.6671 1.3019 -0.4679 0.0860  -0.1528 282 ASN B CA  
7321 C C   . ASN B 282 ? 1.4185 2.5972 1.2872 -0.4545 0.0879  -0.1479 282 ASN B C   
7322 O O   . ASN B 282 ? 1.3984 2.5973 1.2795 -0.4348 0.0860  -0.1409 282 ASN B O   
7323 C CB  . ASN B 282 ? 1.4536 2.7436 1.3198 -0.4999 0.0911  -0.1622 282 ASN B CB  
7324 C CG  . ASN B 282 ? 1.4552 2.8240 1.3315 -0.5045 0.0876  -0.1641 282 ASN B CG  
7325 O OD1 . ASN B 282 ? 1.4312 2.8480 1.3265 -0.4775 0.0818  -0.1555 282 ASN B OD1 
7326 N ND2 . ASN B 282 ? 1.4741 2.8566 1.3368 -0.5387 0.0914  -0.1756 282 ASN B ND2 
7327 N N   . PHE B 283 ? 1.4151 2.5224 1.2669 -0.4648 0.0917  -0.1515 283 PHE B N   
7328 C CA  . PHE B 283 ? 1.4037 2.4507 1.2522 -0.4500 0.0928  -0.1464 283 PHE B CA  
7329 C C   . PHE B 283 ? 1.3483 2.3815 1.2130 -0.4113 0.0854  -0.1346 283 PHE B C   
7330 O O   . PHE B 283 ? 1.3190 2.3391 1.1912 -0.3905 0.0840  -0.1276 283 PHE B O   
7331 C CB  . PHE B 283 ? 1.4698 2.4452 1.2951 -0.4696 0.0988  -0.1530 283 PHE B CB  
7332 C CG  . PHE B 283 ? 1.5296 2.4470 1.3488 -0.4595 0.1012  -0.1492 283 PHE B CG  
7333 C CD1 . PHE B 283 ? 1.5601 2.4745 1.3698 -0.4760 0.1075  -0.1533 283 PHE B CD1 
7334 C CD2 . PHE B 283 ? 1.5216 2.3885 1.3443 -0.4340 0.0973  -0.1418 283 PHE B CD2 
7335 C CE1 . PHE B 283 ? 1.5565 2.4185 1.3603 -0.4663 0.1097  -0.1497 283 PHE B CE1 
7336 C CE2 . PHE B 283 ? 1.5370 2.3530 1.3542 -0.4248 0.0993  -0.1385 283 PHE B CE2 
7337 C CZ  . PHE B 283 ? 1.5455 2.3589 1.3532 -0.4405 0.1054  -0.1424 283 PHE B CZ  
7338 N N   . ILE B 284 ? 1.3085 2.3450 1.1778 -0.4024 0.0810  -0.1326 284 ILE B N   
7339 C CA  . ILE B 284 ? 1.2634 2.2865 1.1467 -0.3675 0.0743  -0.1219 284 ILE B CA  
7340 C C   . ILE B 284 ? 1.2511 2.3370 1.1539 -0.3446 0.0696  -0.1142 284 ILE B C   
7341 O O   . ILE B 284 ? 1.2225 2.2968 1.1359 -0.3151 0.0660  -0.1047 284 ILE B O   
7342 C CB  . ILE B 284 ? 1.2506 2.2533 1.1310 -0.3663 0.0717  -0.1223 284 ILE B CB  
7343 C CG1 . ILE B 284 ? 1.2712 2.2081 1.1312 -0.3861 0.0768  -0.1291 284 ILE B CG1 
7344 C CG2 . ILE B 284 ? 1.2129 2.2032 1.1074 -0.3309 0.0652  -0.1111 284 ILE B CG2 
7345 C CD1 . ILE B 284 ? 1.2913 2.2189 1.1436 -0.3967 0.0764  -0.1335 284 ILE B CD1 
7346 N N   . VAL B 285 ? 1.2544 2.4067 1.1609 -0.3582 0.0699  -0.1184 285 VAL B N   
7347 C CA  . VAL B 285 ? 1.2711 2.4896 1.1950 -0.3373 0.0658  -0.1113 285 VAL B CA  
7348 C C   . VAL B 285 ? 1.2958 2.5114 1.2276 -0.3153 0.0655  -0.1039 285 VAL B C   
7349 O O   . VAL B 285 ? 1.3082 2.5264 1.2515 -0.2833 0.0611  -0.0938 285 VAL B O   
7350 C CB  . VAL B 285 ? 1.2664 2.5587 1.1912 -0.3603 0.0675  -0.1185 285 VAL B CB  
7351 C CG1 . VAL B 285 ? 1.2354 2.5964 1.1773 -0.3375 0.0640  -0.1108 285 VAL B CG1 
7352 C CG2 . VAL B 285 ? 1.2664 2.5697 1.1859 -0.3765 0.0665  -0.1244 285 VAL B CG2 
7353 N N   . ASP B 286 ? 1.3269 2.5345 1.2511 -0.3328 0.0706  -0.1089 286 ASP B N   
7354 C CA  . ASP B 286 ? 1.3256 2.5337 1.2560 -0.3149 0.0710  -0.1029 286 ASP B CA  
7355 C C   . ASP B 286 ? 1.2711 2.4033 1.1953 -0.3042 0.0717  -0.0997 286 ASP B C   
7356 O O   . ASP B 286 ? 1.2152 2.3407 1.1446 -0.2859 0.0714  -0.0939 286 ASP B O   
7357 C CB  . ASP B 286 ? 1.3741 2.6271 1.3023 -0.3364 0.0758  -0.1088 286 ASP B CB  
7358 C CG  . ASP B 286 ? 1.4245 2.6852 1.3389 -0.3762 0.0807  -0.1211 286 ASP B CG  
7359 O OD1 . ASP B 286 ? 1.4820 2.6902 1.3807 -0.3963 0.0857  -0.1272 286 ASP B OD1 
7360 O OD2 . ASP B 286 ? 1.3889 2.7084 1.3074 -0.3873 0.0798  -0.1246 286 ASP B OD2 
7361 N N   . HIS B 287 ? 1.2612 2.3378 1.1741 -0.3148 0.0726  -0.1035 287 HIS B N   
7362 C CA  . HIS B 287 ? 1.2715 2.2775 1.1797 -0.3016 0.0722  -0.0997 287 HIS B CA  
7363 C C   . HIS B 287 ? 1.2176 2.2168 1.1389 -0.2663 0.0662  -0.0890 287 HIS B C   
7364 O O   . HIS B 287 ? 1.2187 2.1737 1.1402 -0.2494 0.0652  -0.0840 287 HIS B O   
7365 C CB  . HIS B 287 ? 1.3220 2.2750 1.2149 -0.3203 0.0746  -0.1059 287 HIS B CB  
7366 C CG  . HIS B 287 ? 1.3680 2.2501 1.2552 -0.3082 0.0745  -0.1025 287 HIS B CG  
7367 N ND1 . HIS B 287 ? 1.3971 2.2485 1.2893 -0.2875 0.0699  -0.0965 287 HIS B ND1 
7368 C CD2 . HIS B 287 ? 1.3818 2.2197 1.2582 -0.3147 0.0787  -0.1044 287 HIS B CD2 
7369 C CE1 . HIS B 287 ? 1.4067 2.1990 1.2922 -0.2814 0.0709  -0.0948 287 HIS B CE1 
7370 N NE2 . HIS B 287 ? 1.4174 2.2015 1.2932 -0.2975 0.0762  -0.0995 287 HIS B NE2 
7371 N N   . ILE B 288 ? 1.1471 2.1903 1.0786 -0.2552 0.0622  -0.0855 288 ILE B N   
7372 C CA  . ILE B 288 ? 1.0762 2.1177 1.0194 -0.2215 0.0570  -0.0750 288 ILE B CA  
7373 C C   . ILE B 288 ? 1.0285 2.1177 0.9829 -0.2009 0.0559  -0.0684 288 ILE B C   
7374 O O   . ILE B 288 ? 0.9946 2.0663 0.9548 -0.1733 0.0535  -0.0600 288 ILE B O   
7375 C CB  . ILE B 288 ? 1.0890 2.1481 1.0359 -0.2183 0.0535  -0.0740 288 ILE B CB  
7376 C CG1 . ILE B 288 ? 1.0905 2.1070 1.0250 -0.2408 0.0551  -0.0814 288 ILE B CG1 
7377 C CG2 . ILE B 288 ? 1.0830 2.1324 1.0397 -0.1841 0.0487  -0.0631 288 ILE B CG2 
7378 C CD1 . ILE B 288 ? 1.0556 1.9991 0.9814 -0.2402 0.0566  -0.0815 288 ILE B CD1 
7379 N N   . SER B 289 ? 1.0124 2.1617 0.9690 -0.2149 0.0579  -0.0724 289 SER B N   
7380 C CA  . SER B 289 ? 0.9811 2.1815 0.9475 -0.1972 0.0575  -0.0667 289 SER B CA  
7381 C C   . SER B 289 ? 0.9854 2.1600 0.9492 -0.1929 0.0603  -0.0656 289 SER B C   
7382 O O   . SER B 289 ? 0.9621 2.1496 0.9331 -0.1673 0.0591  -0.0579 289 SER B O   
7383 C CB  . SER B 289 ? 0.9788 2.2525 0.9478 -0.2159 0.0591  -0.0721 289 SER B CB  
7384 O OG  . SER B 289 ? 0.9520 2.2459 0.9213 -0.2249 0.0571  -0.0749 289 SER B OG  
7385 N N   . ASN B 290 ? 0.9940 2.1310 0.9463 -0.2177 0.0642  -0.0732 290 ASN B N   
7386 C CA  . ASN B 290 ? 0.9977 2.1079 0.9460 -0.2166 0.0672  -0.0730 290 ASN B CA  
7387 C C   . ASN B 290 ? 1.0072 2.0395 0.9478 -0.2120 0.0669  -0.0721 290 ASN B C   
7388 O O   . ASN B 290 ? 1.0206 2.0160 0.9492 -0.2333 0.0708  -0.0786 290 ASN B O   
7389 C CB  . ASN B 290 ? 0.9880 2.1203 0.9284 -0.2482 0.0729  -0.0821 290 ASN B CB  
7390 C CG  . ASN B 290 ? 0.9786 2.1901 0.9258 -0.2577 0.0733  -0.0844 290 ASN B CG  
7391 O OD1 . ASN B 290 ? 0.9646 2.2232 0.9233 -0.2364 0.0712  -0.0779 290 ASN B OD1 
7392 N ND2 . ASN B 290 ? 0.9773 2.2039 0.9166 -0.2896 0.0763  -0.0939 290 ASN B ND2 
7393 N N   . GLN B 291 ? 0.9905 1.9984 0.9371 -0.1842 0.0626  -0.0641 291 GLN B N   
7394 C CA  . GLN B 291 ? 1.0034 1.9419 0.9444 -0.1765 0.0618  -0.0623 291 GLN B CA  
7395 C C   . GLN B 291 ? 1.0213 1.9450 0.9640 -0.1586 0.0622  -0.0574 291 GLN B C   
7396 O O   . GLN B 291 ? 1.0079 1.9434 0.9589 -0.1317 0.0594  -0.0495 291 GLN B O   
7397 C CB  . GLN B 291 ? 0.9851 1.9016 0.9305 -0.1586 0.0571  -0.0569 291 GLN B CB  
7398 C CG  . GLN B 291 ? 0.9863 1.9005 0.9273 -0.1770 0.0568  -0.0622 291 GLN B CG  
7399 C CD  . GLN B 291 ? 0.9654 1.8685 0.9124 -0.1581 0.0522  -0.0563 291 GLN B CD  
7400 O OE1 . GLN B 291 ? 0.9505 1.8249 0.8923 -0.1678 0.0516  -0.0592 291 GLN B OE1 
7401 N NE2 . GLN B 291 ? 0.9371 1.8623 0.8939 -0.1308 0.0493  -0.0478 291 GLN B NE2 
7402 N N   . PHE B 292 ? 1.0564 1.9542 0.9902 -0.1739 0.0661  -0.0621 292 PHE B N   
7403 C CA  . PHE B 292 ? 1.0772 1.9600 1.0112 -0.1596 0.0669  -0.0585 292 PHE B CA  
7404 C C   . PHE B 292 ? 1.0862 1.8995 1.0120 -0.1576 0.0668  -0.0585 292 PHE B C   
7405 O O   . PHE B 292 ? 1.0843 1.8642 1.0001 -0.1773 0.0689  -0.0642 292 PHE B O   
7406 C CB  . PHE B 292 ? 1.1145 2.0322 1.0459 -0.1755 0.0717  -0.0628 292 PHE B CB  
7407 C CG  . PHE B 292 ? 1.1563 2.0898 1.0796 -0.2090 0.0758  -0.0719 292 PHE B CG  
7408 C CD1 . PHE B 292 ? 1.1953 2.0789 1.1049 -0.2298 0.0789  -0.0781 292 PHE B CD1 
7409 C CD2 . PHE B 292 ? 1.1596 2.1582 1.0882 -0.2197 0.0768  -0.0744 292 PHE B CD2 
7410 C CE1 . PHE B 292 ? 1.2333 2.1284 1.1332 -0.2611 0.0833  -0.0868 292 PHE B CE1 
7411 C CE2 . PHE B 292 ? 1.1858 2.1987 1.1058 -0.2521 0.0809  -0.0835 292 PHE B CE2 
7412 C CZ  . PHE B 292 ? 1.2209 2.1804 1.1260 -0.2731 0.0843  -0.0897 292 PHE B CZ  
7413 N N   . VAL B 293 ? 1.0578 1.8502 0.9873 -0.1332 0.0646  -0.0521 293 VAL B N   
7414 C CA  . VAL B 293 ? 1.0607 1.7904 0.9843 -0.1274 0.0635  -0.0512 293 VAL B CA  
7415 C C   . VAL B 293 ? 1.0866 1.8024 1.0085 -0.1164 0.0648  -0.0489 293 VAL B C   
7416 O O   . VAL B 293 ? 1.0909 1.8428 1.0187 -0.1041 0.0651  -0.0455 293 VAL B O   
7417 C CB  . VAL B 293 ? 1.0534 1.7593 0.9823 -0.1071 0.0586  -0.0455 293 VAL B CB  
7418 C CG1 . VAL B 293 ? 1.0568 1.7692 0.9860 -0.1186 0.0574  -0.0480 293 VAL B CG1 
7419 C CG2 . VAL B 293 ? 1.0395 1.7724 0.9780 -0.0799 0.0561  -0.0377 293 VAL B CG2 
7420 N N   . ALA B 294 ? 1.0924 1.7564 1.0057 -0.1204 0.0656  -0.0507 294 ALA B N   
7421 C CA  . ALA B 294 ? 1.0917 1.7353 1.0028 -0.1089 0.0662  -0.0484 294 ALA B CA  
7422 C C   . ALA B 294 ? 1.0658 1.6760 0.9806 -0.0844 0.0617  -0.0424 294 ALA B C   
7423 O O   . ALA B 294 ? 1.0828 1.6609 0.9965 -0.0838 0.0592  -0.0422 294 ALA B O   
7424 C CB  . ALA B 294 ? 1.1174 1.7259 1.0159 -0.1277 0.0701  -0.0539 294 ALA B CB  
7425 N N   . PHE B 295 ? 1.0411 1.6598 0.9598 -0.0643 0.0609  -0.0376 295 PHE B N   
7426 C CA  . PHE B 295 ? 1.0420 1.6275 0.9623 -0.0420 0.0573  -0.0324 295 PHE B CA  
7427 C C   . PHE B 295 ? 1.0982 1.6519 1.0124 -0.0371 0.0583  -0.0326 295 PHE B C   
7428 O O   . PHE B 295 ? 1.1370 1.6529 1.0437 -0.0486 0.0589  -0.0361 295 PHE B O   
7429 C CB  . PHE B 295 ? 0.9831 1.5995 0.9116 -0.0193 0.0554  -0.0258 295 PHE B CB  
7430 C CG  . PHE B 295 ? 0.9534 1.5346 0.8825 0.0022  0.0521  -0.0206 295 PHE B CG  
7431 C CD1 . PHE B 295 ? 0.9131 1.4541 0.8407 -0.0005 0.0494  -0.0212 295 PHE B CD1 
7432 C CD2 . PHE B 295 ? 0.9268 1.5150 0.8571 0.0252  0.0521  -0.0152 295 PHE B CD2 
7433 C CE1 . PHE B 295 ? 0.8901 1.3996 0.8178 0.0177  0.0466  -0.0168 295 PHE B CE1 
7434 C CE2 . PHE B 295 ? 0.9033 1.4575 0.8325 0.0436  0.0496  -0.0108 295 PHE B CE2 
7435 C CZ  . PHE B 295 ? 0.8851 1.4004 0.8133 0.0393  0.0468  -0.0117 295 PHE B CZ  
7436 N N   . ARG B 296 ? 1.0965 1.6653 1.0129 -0.0196 0.0586  -0.0287 296 ARG B N   
7437 C CA  . ARG B 296 ? 1.0885 1.6298 0.9990 -0.0137 0.0595  -0.0287 296 ARG B CA  
7438 C C   . ARG B 296 ? 1.1202 1.6865 1.0273 -0.0265 0.0641  -0.0321 296 ARG B C   
7439 O O   . ARG B 296 ? 1.1324 1.7264 1.0416 -0.0153 0.0656  -0.0296 296 ARG B O   
7440 C CB  . ARG B 296 ? 1.0244 1.5600 0.9371 0.0131  0.0576  -0.0227 296 ARG B CB  
7441 C CG  . ARG B 296 ? 0.9788 1.4748 0.8916 0.0238  0.0536  -0.0202 296 ARG B CG  
7442 C CD  . ARG B 296 ? 0.9401 1.4370 0.8546 0.0497  0.0524  -0.0140 296 ARG B CD  
7443 N NE  . ARG B 296 ? 0.9093 1.3689 0.8235 0.0580  0.0489  -0.0119 296 ARG B NE  
7444 C CZ  . ARG B 296 ? 0.8948 1.3434 0.8083 0.0791  0.0478  -0.0068 296 ARG B CZ  
7445 N NH1 . ARG B 296 ? 0.8809 1.3520 0.7934 0.0956  0.0500  -0.0030 296 ARG B NH1 
7446 N NH2 . ARG B 296 ? 0.8671 1.2815 0.7800 0.0837  0.0449  -0.0055 296 ARG B NH2 
7447 N N   . ARG B 297 ? 1.1740 1.7301 1.0750 -0.0502 0.0665  -0.0378 297 ARG B N   
7448 C CA  . ARG B 297 ? 1.2433 1.8196 1.1393 -0.0669 0.0716  -0.0420 297 ARG B CA  
7449 C C   . ARG B 297 ? 1.2288 1.8663 1.1313 -0.0717 0.0738  -0.0421 297 ARG B C   
7450 O O   . ARG B 297 ? 1.2356 1.8980 1.1356 -0.0816 0.0779  -0.0444 297 ARG B O   
7451 C CB  . ARG B 297 ? 1.2807 1.8393 1.1717 -0.0578 0.0729  -0.0409 297 ARG B CB  
7452 C CG  . ARG B 297 ? 1.3010 1.8035 1.1829 -0.0609 0.0722  -0.0427 297 ARG B CG  
7453 C CD  . ARG B 297 ? 1.3539 1.8405 1.2326 -0.0462 0.0723  -0.0406 297 ARG B CD  
7454 N NE  . ARG B 297 ? 1.4135 1.8656 1.2811 -0.0579 0.0748  -0.0441 297 ARG B NE  
7455 C CZ  . ARG B 297 ? 1.4415 1.8840 1.3041 -0.0520 0.0764  -0.0438 297 ARG B CZ  
7456 N NH1 . ARG B 297 ? 1.4619 1.9258 1.3292 -0.0344 0.0759  -0.0402 297 ARG B NH1 
7457 N NH2 . ARG B 297 ? 1.4294 1.8403 1.2813 -0.0630 0.0787  -0.0468 297 ARG B NH2 
7458 N N   . LYS B 298 ? 1.2219 1.8842 1.1325 -0.0648 0.0711  -0.0395 298 LYS B N   
7459 C CA  . LYS B 298 ? 1.1935 1.9172 1.1113 -0.0664 0.0725  -0.0389 298 LYS B CA  
7460 C C   . LYS B 298 ? 1.1803 1.9220 1.1017 -0.0782 0.0712  -0.0409 298 LYS B C   
7461 O O   . LYS B 298 ? 1.1408 1.8511 1.0621 -0.0751 0.0680  -0.0400 298 LYS B O   
7462 C CB  . LYS B 298 ? 1.1854 1.9333 1.1102 -0.0379 0.0708  -0.0317 298 LYS B CB  
7463 C CG  . LYS B 298 ? 1.2097 1.9558 1.1313 -0.0279 0.0732  -0.0302 298 LYS B CG  
7464 C CD  . LYS B 298 ? 1.1945 1.9575 1.1206 0.0018  0.0718  -0.0229 298 LYS B CD  
7465 C CE  . LYS B 298 ? 1.1969 1.9564 1.1188 0.0112  0.0744  -0.0218 298 LYS B CE  
7466 N NZ  . LYS B 298 ? 1.2083 1.9823 1.1325 0.0408  0.0739  -0.0148 298 LYS B NZ  
7467 N N   . ILE B 299 ? 1.1677 1.9611 1.0921 -0.0922 0.0738  -0.0436 299 ILE B N   
7468 C CA  . ILE B 299 ? 1.1486 1.9662 1.0761 -0.1049 0.0729  -0.0461 299 ILE B CA  
7469 C C   . ILE B 299 ? 1.1161 1.9748 1.0545 -0.0841 0.0697  -0.0399 299 ILE B C   
7470 O O   . ILE B 299 ? 1.1275 2.0282 1.0711 -0.0714 0.0707  -0.0364 299 ILE B O   
7471 C CB  . ILE B 299 ? 1.1807 2.0315 1.1041 -0.1347 0.0776  -0.0534 299 ILE B CB  
7472 C CG1 . ILE B 299 ? 1.2233 2.0266 1.1341 -0.1586 0.0803  -0.0600 299 ILE B CG1 
7473 C CG2 . ILE B 299 ? 1.1651 2.0675 1.0955 -0.1413 0.0767  -0.0544 299 ILE B CG2 
7474 C CD1 . ILE B 299 ? 1.3008 2.1287 1.2044 -0.1892 0.0859  -0.0677 299 ILE B CD1 
7475 N N   . TYR B 300 ? 1.0644 1.9103 1.0054 -0.0800 0.0662  -0.0385 300 TYR B N   
7476 C CA  . TYR B 300 ? 1.0111 1.8926 0.9611 -0.0612 0.0634  -0.0326 300 TYR B CA  
7477 C C   . TYR B 300 ? 0.9654 1.8722 0.9175 -0.0780 0.0627  -0.0363 300 TYR B C   
7478 O O   . TYR B 300 ? 0.9315 1.8102 0.8777 -0.0989 0.0632  -0.0421 300 TYR B O   
7479 C CB  . TYR B 300 ? 1.0211 1.8623 0.9720 -0.0360 0.0597  -0.0261 300 TYR B CB  
7480 C CG  . TYR B 300 ? 1.0389 1.8587 0.9877 -0.0161 0.0602  -0.0218 300 TYR B CG  
7481 C CD1 . TYR B 300 ? 1.0564 1.8268 0.9980 -0.0219 0.0609  -0.0245 300 TYR B CD1 
7482 C CD2 . TYR B 300 ? 1.0485 1.8965 1.0015 0.0093  0.0601  -0.0148 300 TYR B CD2 
7483 C CE1 . TYR B 300 ? 1.0689 1.8198 1.0080 -0.0042 0.0613  -0.0210 300 TYR B CE1 
7484 C CE2 . TYR B 300 ? 1.0768 1.9034 1.0264 0.0276  0.0609  -0.0111 300 TYR B CE2 
7485 C CZ  . TYR B 300 ? 1.0827 1.8611 1.0256 0.0202  0.0613  -0.0145 300 TYR B CZ  
7486 O OH  . TYR B 300 ? 1.0913 1.8490 1.0304 0.0377  0.0620  -0.0112 300 TYR B OH  
7487 N N   . LYS B 301 ? 0.9542 1.9145 0.9142 -0.0681 0.0616  -0.0327 301 LYS B N   
7488 C CA  . LYS B 301 ? 0.9426 1.9315 0.9055 -0.0809 0.0604  -0.0355 301 LYS B CA  
7489 C C   . LYS B 301 ? 0.9116 1.8852 0.8785 -0.0608 0.0562  -0.0294 301 LYS B C   
7490 O O   . LYS B 301 ? 0.9144 1.8978 0.8858 -0.0333 0.0547  -0.0214 301 LYS B O   
7491 C CB  . LYS B 301 ? 0.9444 2.0079 0.9132 -0.0862 0.0621  -0.0363 301 LYS B CB  
7492 C CG  . LYS B 301 ? 0.9441 2.0489 0.9197 -0.0798 0.0594  -0.0337 301 LYS B CG  
7493 C CD  . LYS B 301 ? 0.9136 2.0860 0.8924 -0.0990 0.0614  -0.0386 301 LYS B CD  
7494 C CE  . LYS B 301 ? 0.9188 2.0824 0.8920 -0.1311 0.0621  -0.0478 301 LYS B CE  
7495 N NZ  . LYS B 301 ? 0.8995 2.1310 0.8772 -0.1449 0.0624  -0.0512 301 LYS B NZ  
7496 N N   . TRP B 302 ? 0.8734 1.8209 0.8374 -0.0746 0.0548  -0.0330 302 TRP B N   
7497 C CA  . TRP B 302 ? 0.8469 1.7815 0.8143 -0.0594 0.0511  -0.0281 302 TRP B CA  
7498 C C   . TRP B 302 ? 0.8272 1.8138 0.7995 -0.0662 0.0502  -0.0291 302 TRP B C   
7499 O O   . TRP B 302 ? 0.8164 1.8108 0.7853 -0.0921 0.0513  -0.0366 302 TRP B O   
7500 C CB  . TRP B 302 ? 0.8340 1.7063 0.7953 -0.0682 0.0498  -0.0309 302 TRP B CB  
7501 C CG  . TRP B 302 ? 0.8295 1.6808 0.7939 -0.0506 0.0462  -0.0251 302 TRP B CG  
7502 C CD1 . TRP B 302 ? 0.8149 1.6782 0.7815 -0.0553 0.0443  -0.0256 302 TRP B CD1 
7503 C CD2 . TRP B 302 ? 0.8144 1.6272 0.7794 -0.0257 0.0442  -0.0181 302 TRP B CD2 
7504 N NE1 . TRP B 302 ? 0.8063 1.6422 0.7749 -0.0352 0.0414  -0.0192 302 TRP B NE1 
7505 C CE2 . TRP B 302 ? 0.7963 1.6011 0.7638 -0.0174 0.0413  -0.0145 302 TRP B CE2 
7506 C CE3 . TRP B 302 ? 0.7960 1.5811 0.7590 -0.0107 0.0446  -0.0147 302 TRP B CE3 
7507 C CZ2 . TRP B 302 ? 0.7867 1.5571 0.7546 0.0042  0.0393  -0.0079 302 TRP B CZ2 
7508 C CZ3 . TRP B 302 ? 0.7839 1.5342 0.7469 0.0109  0.0424  -0.0083 302 TRP B CZ3 
7509 C CH2 . TRP B 302 ? 0.7946 1.5377 0.7600 0.0179  0.0400  -0.0050 302 TRP B CH2 
7510 N N   . ASN B 303 ? 0.8339 1.8571 0.8130 -0.0429 0.0487  -0.0217 303 ASN B N   
7511 C CA  . ASN B 303 ? 0.8664 1.9450 0.8507 -0.0458 0.0476  -0.0217 303 ASN B CA  
7512 C C   . ASN B 303 ? 0.8575 1.9273 0.8448 -0.0249 0.0443  -0.0147 303 ASN B C   
7513 O O   . ASN B 303 ? 0.8675 1.9839 0.8596 -0.0197 0.0432  -0.0123 303 ASN B O   
7514 C CB  . ASN B 303 ? 0.8871 2.0325 0.8767 -0.0392 0.0494  -0.0196 303 ASN B CB  
7515 C CG  . ASN B 303 ? 0.8986 2.0370 0.8888 -0.0125 0.0504  -0.0123 303 ASN B CG  
7516 O OD1 . ASN B 303 ? 0.9153 2.0142 0.9041 0.0099  0.0489  -0.0058 303 ASN B OD1 
7517 N ND2 . ASN B 303 ? 0.8888 2.0653 0.8804 -0.0154 0.0531  -0.0135 303 ASN B ND2 
7518 N N   . HIS B 304 ? 0.8409 1.8512 0.8250 -0.0133 0.0430  -0.0114 304 HIS B N   
7519 C CA  . HIS B 304 ? 0.8221 1.8157 0.8078 0.0043  0.0403  -0.0052 304 HIS B CA  
7520 C C   . HIS B 304 ? 0.8020 1.7710 0.7854 -0.0151 0.0387  -0.0106 304 HIS B C   
7521 O O   . HIS B 304 ? 0.7932 1.7060 0.7724 -0.0179 0.0380  -0.0116 304 HIS B O   
7522 C CB  . HIS B 304 ? 0.8197 1.7654 0.8029 0.0282  0.0399  0.0015  304 HIS B CB  
7523 C CG  . HIS B 304 ? 0.8428 1.7690 0.8266 0.0464  0.0376  0.0082  304 HIS B CG  
7524 N ND1 . HIS B 304 ? 0.8556 1.8186 0.8425 0.0667  0.0373  0.0154  304 HIS B ND1 
7525 C CD2 . HIS B 304 ? 0.8419 1.7142 0.8230 0.0468  0.0359  0.0087  304 HIS B CD2 
7526 C CE1 . HIS B 304 ? 0.8626 1.7951 0.8482 0.0790  0.0357  0.0202  304 HIS B CE1 
7527 N NE2 . HIS B 304 ? 0.8600 1.7378 0.8426 0.0664  0.0347  0.0160  304 HIS B NE2 
7528 N N   . GLY B 305 ? 0.8012 1.8137 0.7869 -0.0289 0.0384  -0.0142 305 GLY B N   
7529 C CA  . GLY B 305 ? 0.8014 1.7969 0.7840 -0.0492 0.0374  -0.0201 305 GLY B CA  
7530 C C   . GLY B 305 ? 0.8071 1.7622 0.7821 -0.0744 0.0394  -0.0286 305 GLY B C   
7531 O O   . GLY B 305 ? 0.8109 1.7719 0.7835 -0.0846 0.0420  -0.0324 305 GLY B O   
7532 N N   . LEU B 306 ? 0.8244 1.7383 0.7949 -0.0838 0.0384  -0.0313 306 LEU B N   
7533 C CA  . LEU B 306 ? 0.8566 1.7244 0.8182 -0.1043 0.0404  -0.0383 306 LEU B CA  
7534 C C   . LEU B 306 ? 0.8639 1.6791 0.8239 -0.0896 0.0400  -0.0343 306 LEU B C   
7535 O O   . LEU B 306 ? 0.8313 1.6349 0.7960 -0.0653 0.0376  -0.0265 306 LEU B O   
7536 C CB  . LEU B 306 ? 0.8668 1.7131 0.8233 -0.1196 0.0399  -0.0429 306 LEU B CB  
7537 C CG  . LEU B 306 ? 0.8723 1.7619 0.8270 -0.1409 0.0409  -0.0494 306 LEU B CG  
7538 C CD1 . LEU B 306 ? 0.8568 1.7289 0.8093 -0.1447 0.0391  -0.0503 306 LEU B CD1 
7539 C CD2 . LEU B 306 ? 0.9014 1.7904 0.8467 -0.1699 0.0453  -0.0590 306 LEU B CD2 
7540 N N   . LEU B 307 ? 0.9069 1.6909 0.8594 -0.1049 0.0426  -0.0397 307 LEU B N   
7541 C CA  . LEU B 307 ? 0.9362 1.6674 0.8858 -0.0950 0.0422  -0.0373 307 LEU B CA  
7542 C C   . LEU B 307 ? 0.9755 1.6587 0.9202 -0.0998 0.0410  -0.0386 307 LEU B C   
7543 O O   . LEU B 307 ? 0.9930 1.6684 0.9307 -0.1211 0.0428  -0.0452 307 LEU B O   
7544 C CB  . LEU B 307 ? 0.9368 1.6569 0.8794 -0.1095 0.0458  -0.0425 307 LEU B CB  
7545 C CG  . LEU B 307 ? 0.9227 1.6721 0.8692 -0.1002 0.0471  -0.0401 307 LEU B CG  
7546 C CD1 . LEU B 307 ? 0.9593 1.7151 0.8983 -0.1237 0.0514  -0.0475 307 LEU B CD1 
7547 C CD2 . LEU B 307 ? 0.8988 1.6143 0.8469 -0.0774 0.0455  -0.0339 307 LEU B CD2 
7548 N N   . GLN B 308 ? 1.0320 1.6827 0.9797 -0.0802 0.0383  -0.0325 308 GLN B N   
7549 C CA  . GLN B 308 ? 1.0818 1.6818 1.0245 -0.0839 0.0374  -0.0336 308 GLN B CA  
7550 C C   . GLN B 308 ? 1.1272 1.6935 1.0610 -0.0969 0.0401  -0.0387 308 GLN B C   
7551 O O   . GLN B 308 ? 1.1611 1.7120 1.0953 -0.0868 0.0401  -0.0363 308 GLN B O   
7552 C CB  . GLN B 308 ? 1.0704 1.6451 1.0183 -0.0604 0.0342  -0.0260 308 GLN B CB  
7553 C CG  . GLN B 308 ? 1.0607 1.6541 1.0144 -0.0500 0.0318  -0.0215 308 GLN B CG  
7554 C CD  . GLN B 308 ? 1.0558 1.6080 1.0101 -0.0393 0.0295  -0.0175 308 GLN B CD  
7555 O OE1 . GLN B 308 ? 1.0850 1.6158 1.0412 -0.0222 0.0283  -0.0123 308 GLN B OE1 
7556 N NE2 . GLN B 308 ? 1.0347 1.5760 0.9868 -0.0497 0.0289  -0.0200 308 GLN B NE2 
7557 N N   . GLY B 309 ? 1.1445 1.7002 1.0693 -0.1194 0.0428  -0.0457 309 GLY B N   
7558 C CA  . GLY B 309 ? 1.1609 1.6834 1.0750 -0.1326 0.0461  -0.0505 309 GLY B CA  
7559 C C   . GLY B 309 ? 1.1693 1.7029 1.0729 -0.1594 0.0508  -0.0588 309 GLY B C   
7560 O O   . GLY B 309 ? 1.1653 1.6629 1.0568 -0.1729 0.0538  -0.0633 309 GLY B O   
7561 N N   . ASP B 310 ? 1.2000 1.7836 1.1073 -0.1670 0.0517  -0.0607 310 ASP B N   
7562 C CA  . ASP B 310 ? 1.2601 1.8591 1.1573 -0.1941 0.0563  -0.0690 310 ASP B CA  
7563 C C   . ASP B 310 ? 1.3066 1.8847 1.1960 -0.2063 0.0569  -0.0728 310 ASP B C   
7564 O O   . ASP B 310 ? 1.2780 1.8670 1.1746 -0.1969 0.0533  -0.0696 310 ASP B O   
7565 C CB  . ASP B 310 ? 1.2576 1.9199 1.1621 -0.1981 0.0565  -0.0699 310 ASP B CB  
7566 C CG  . ASP B 310 ? 1.2880 1.9696 1.1820 -0.2278 0.0612  -0.0790 310 ASP B CG  
7567 O OD1 . ASP B 310 ? 1.2967 1.9539 1.1780 -0.2450 0.0660  -0.0844 310 ASP B OD1 
7568 O OD2 . ASP B 310 ? 1.2967 2.0180 1.1943 -0.2343 0.0603  -0.0808 310 ASP B OD2 
7569 N N   . PRO B 311 ? 1.3672 1.9134 1.2406 -0.2267 0.0618  -0.0795 311 PRO B N   
7570 C CA  . PRO B 311 ? 1.3792 1.9008 1.2420 -0.2393 0.0634  -0.0836 311 PRO B CA  
7571 C C   . PRO B 311 ? 1.3626 1.9248 1.2285 -0.2484 0.0625  -0.0863 311 PRO B C   
7572 O O   . PRO B 311 ? 1.3506 1.8960 1.2115 -0.2527 0.0623  -0.0879 311 PRO B O   
7573 C CB  . PRO B 311 ? 1.3991 1.8928 1.2428 -0.2621 0.0703  -0.0910 311 PRO B CB  
7574 C CG  . PRO B 311 ? 1.4003 1.8800 1.2455 -0.2528 0.0707  -0.0881 311 PRO B CG  
7575 C CD  . PRO B 311 ? 1.3808 1.9055 1.2441 -0.2360 0.0663  -0.0825 311 PRO B CD  
7576 N N   . LEU B 312 ? 1.3587 1.9749 1.2327 -0.2509 0.0620  -0.0868 312 LEU B N   
7577 C CA  . LEU B 312 ? 1.3654 2.0263 1.2428 -0.2596 0.0611  -0.0894 312 LEU B CA  
7578 C C   . LEU B 312 ? 1.3059 2.0030 1.2011 -0.2358 0.0551  -0.0814 312 LEU B C   
7579 O O   . LEU B 312 ? 1.2904 2.0330 1.1904 -0.2400 0.0539  -0.0826 312 LEU B O   
7580 C CB  . LEU B 312 ? 1.4198 2.1207 1.2915 -0.2833 0.0655  -0.0968 312 LEU B CB  
7581 C CG  . LEU B 312 ? 1.4758 2.1525 1.3269 -0.3139 0.0723  -0.1068 312 LEU B CG  
7582 C CD1 . LEU B 312 ? 1.4944 2.2161 1.3421 -0.3357 0.0763  -0.1134 312 LEU B CD1 
7583 C CD2 . LEU B 312 ? 1.4464 2.1086 1.2894 -0.3235 0.0725  -0.1105 312 LEU B CD2 
7584 N N   . SER B 313 ? 1.2294 1.9056 1.1332 -0.2109 0.0516  -0.0734 313 SER B N   
7585 C CA  . SER B 313 ? 1.1481 1.8528 1.0667 -0.1866 0.0467  -0.0651 313 SER B CA  
7586 C C   . SER B 313 ? 1.1163 1.8078 1.0370 -0.1792 0.0437  -0.0624 313 SER B C   
7587 O O   . SER B 313 ? 1.0993 1.8281 1.0281 -0.1708 0.0410  -0.0592 313 SER B O   
7588 C CB  . SER B 313 ? 1.1186 1.8070 1.0443 -0.1636 0.0447  -0.0578 313 SER B CB  
7589 O OG  . SER B 313 ? 1.1098 1.8256 1.0368 -0.1662 0.0468  -0.0589 313 SER B OG  
7590 N N   . GLY B 314 ? 1.0824 1.7218 0.9954 -0.1819 0.0443  -0.0635 314 GLY B N   
7591 C CA  . GLY B 314 ? 1.0474 1.6691 0.9619 -0.1744 0.0417  -0.0608 314 GLY B CA  
7592 C C   . GLY B 314 ? 1.0278 1.6816 0.9403 -0.1878 0.0419  -0.0650 314 GLY B C   
7593 O O   . GLY B 314 ? 0.9967 1.6671 0.9170 -0.1754 0.0386  -0.0604 314 GLY B O   
7594 N N   . CYS B 315 ? 1.0287 1.6914 0.9302 -0.2133 0.0461  -0.0739 315 CYS B N   
7595 C CA  . CYS B 315 ? 1.0474 1.7384 0.9442 -0.2303 0.0471  -0.0796 315 CYS B CA  
7596 C C   . CYS B 315 ? 1.0281 1.7848 0.9360 -0.2260 0.0448  -0.0778 315 CYS B C   
7597 O O   . CYS B 315 ? 1.0238 1.8068 0.9354 -0.2245 0.0426  -0.0772 315 CYS B O   
7598 C CB  . CYS B 315 ? 1.0834 1.7610 0.9629 -0.2601 0.0530  -0.0901 315 CYS B CB  
7599 S SG  . CYS B 315 ? 1.1724 1.8742 1.0500 -0.2723 0.0567  -0.0939 315 CYS B SG  
7600 N N   . LEU B 316 ? 0.9890 1.7730 0.9019 -0.2238 0.0454  -0.0769 316 LEU B N   
7601 C CA  . LEU B 316 ? 0.9358 1.7850 0.8588 -0.2189 0.0437  -0.0750 316 LEU B CA  
7602 C C   . LEU B 316 ? 0.9008 1.7657 0.8373 -0.1892 0.0387  -0.0646 316 LEU B C   
7603 O O   . LEU B 316 ? 0.8911 1.8048 0.8342 -0.1847 0.0367  -0.0628 316 LEU B O   
7604 C CB  . LEU B 316 ? 0.9183 1.7898 0.8430 -0.2224 0.0459  -0.0761 316 LEU B CB  
7605 C CG  . LEU B 316 ? 0.9441 1.8247 0.8567 -0.2540 0.0512  -0.0867 316 LEU B CG  
7606 C CD1 . LEU B 316 ? 0.9317 1.8296 0.8470 -0.2533 0.0531  -0.0862 316 LEU B CD1 
7607 C CD2 . LEU B 316 ? 0.9250 1.8559 0.8361 -0.2722 0.0516  -0.0928 316 LEU B CD2 
7608 N N   . CYS B 317 ? 0.8914 1.7147 0.8312 -0.1690 0.0370  -0.0577 317 CYS B N   
7609 C CA  . CYS B 317 ? 0.8582 1.6856 0.8083 -0.1411 0.0331  -0.0478 317 CYS B CA  
7610 C C   . CYS B 317 ? 0.8351 1.6619 0.7847 -0.1418 0.0312  -0.0476 317 CYS B C   
7611 O O   . CYS B 317 ? 0.8104 1.6686 0.7676 -0.1261 0.0286  -0.0417 317 CYS B O   
7612 C CB  . CYS B 317 ? 0.8371 1.6145 0.7886 -0.1234 0.0322  -0.0419 317 CYS B CB  
7613 S SG  . CYS B 317 ? 0.8100 1.5977 0.7729 -0.0879 0.0288  -0.0294 317 CYS B SG  
7614 N N   . GLU B 318 ? 0.8488 1.6397 0.7884 -0.1595 0.0329  -0.0538 318 GLU B N   
7615 C CA  . GLU B 318 ? 0.8891 1.6787 0.8265 -0.1633 0.0317  -0.0548 318 GLU B CA  
7616 C C   . GLU B 318 ? 0.8865 1.7335 0.8242 -0.1764 0.0318  -0.0594 318 GLU B C   
7617 O O   . GLU B 318 ? 0.8997 1.7718 0.8426 -0.1670 0.0292  -0.0557 318 GLU B O   
7618 C CB  . GLU B 318 ? 0.9533 1.6912 0.8781 -0.1799 0.0342  -0.0610 318 GLU B CB  
7619 C CG  . GLU B 318 ? 1.0390 1.7216 0.9642 -0.1655 0.0335  -0.0559 318 GLU B CG  
7620 C CD  . GLU B 318 ? 1.0958 1.7294 1.0079 -0.1808 0.0363  -0.0617 318 GLU B CD  
7621 O OE1 . GLU B 318 ? 1.0694 1.6699 0.9751 -0.1858 0.0388  -0.0639 318 GLU B OE1 
7622 O OE2 . GLU B 318 ? 1.1246 1.7527 1.0320 -0.1872 0.0363  -0.0639 318 GLU B OE2 
7623 N N   . LEU B 319 ? 0.8716 1.7397 0.8033 -0.1983 0.0350  -0.0674 319 LEU B N   
7624 C CA  . LEU B 319 ? 0.8535 1.7794 0.7848 -0.2139 0.0355  -0.0729 319 LEU B CA  
7625 C C   . LEU B 319 ? 0.7984 1.7805 0.7434 -0.1927 0.0320  -0.0652 319 LEU B C   
7626 O O   . LEU B 319 ? 0.7651 1.7868 0.7132 -0.1924 0.0301  -0.0649 319 LEU B O   
7627 C CB  . LEU B 319 ? 0.9125 1.8480 0.8351 -0.2399 0.0399  -0.0822 319 LEU B CB  
7628 C CG  . LEU B 319 ? 0.9464 1.9259 0.8621 -0.2679 0.0423  -0.0921 319 LEU B CG  
7629 C CD1 . LEU B 319 ? 0.9423 1.9957 0.8698 -0.2605 0.0398  -0.0893 319 LEU B CD1 
7630 C CD2 . LEU B 319 ? 0.9435 1.9069 0.8495 -0.2819 0.0428  -0.0975 319 LEU B CD2 
7631 N N   . TYR B 320 ? 0.7598 1.7447 0.7121 -0.1745 0.0315  -0.0587 320 TYR B N   
7632 C CA  . TYR B 320 ? 0.7316 1.7630 0.6956 -0.1504 0.0288  -0.0501 320 TYR B CA  
7633 C C   . TYR B 320 ? 0.7525 1.7746 0.7213 -0.1282 0.0255  -0.0418 320 TYR B C   
7634 O O   . TYR B 320 ? 0.7104 1.7790 0.6850 -0.1177 0.0235  -0.0378 320 TYR B O   
7635 C CB  . TYR B 320 ? 0.7079 1.7295 0.6763 -0.1342 0.0294  -0.0447 320 TYR B CB  
7636 C CG  . TYR B 320 ? 0.7033 1.7703 0.6819 -0.1082 0.0276  -0.0356 320 TYR B CG  
7637 C CD1 . TYR B 320 ? 0.7101 1.8351 0.6921 -0.1125 0.0286  -0.0373 320 TYR B CD1 
7638 C CD2 . TYR B 320 ? 0.6899 1.7399 0.6734 -0.0788 0.0254  -0.0251 320 TYR B CD2 
7639 C CE1 . TYR B 320 ? 0.6958 1.8619 0.6860 -0.0870 0.0274  -0.0286 320 TYR B CE1 
7640 C CE2 . TYR B 320 ? 0.6838 1.7718 0.6742 -0.0537 0.0245  -0.0164 320 TYR B CE2 
7641 C CZ  . TYR B 320 ? 0.6831 1.8292 0.6769 -0.0572 0.0255  -0.0180 320 TYR B CZ  
7642 O OH  . TYR B 320 ? 0.6755 1.8592 0.6752 -0.0307 0.0250  -0.0090 320 TYR B OH  
7643 N N   . MET B 321 ? 0.7634 1.7258 0.7294 -0.1215 0.0252  -0.0393 321 MET B N   
7644 C CA  . MET B 321 ? 0.7818 1.7275 0.7517 -0.1006 0.0226  -0.0312 321 MET B CA  
7645 C C   . MET B 321 ? 0.7722 1.7350 0.7395 -0.1109 0.0215  -0.0345 321 MET B C   
7646 O O   . MET B 321 ? 0.7455 1.7353 0.7182 -0.0946 0.0193  -0.0281 321 MET B O   
7647 C CB  . MET B 321 ? 0.8049 1.6834 0.7720 -0.0941 0.0227  -0.0288 321 MET B CB  
7648 C CG  . MET B 321 ? 0.8195 1.6830 0.7931 -0.0641 0.0211  -0.0177 321 MET B CG  
7649 S SD  . MET B 321 ? 0.8532 1.7206 0.8298 -0.0534 0.0224  -0.0149 321 MET B SD  
7650 C CE  . MET B 321 ? 0.8782 1.7252 0.8598 -0.0188 0.0209  -0.0021 321 MET B CE  
7651 N N   . ALA B 322 ? 0.7933 1.7391 0.7512 -0.1377 0.0235  -0.0444 322 ALA B N   
7652 C CA  . ALA B 322 ? 0.8083 1.7702 0.7617 -0.1516 0.0231  -0.0494 322 ALA B CA  
7653 C C   . ALA B 322 ? 0.8292 1.8622 0.7870 -0.1545 0.0220  -0.0505 322 ALA B C   
7654 O O   . ALA B 322 ? 0.8792 1.9363 0.8371 -0.1554 0.0204  -0.0507 322 ALA B O   
7655 C CB  . ALA B 322 ? 0.8168 1.7470 0.7569 -0.1809 0.0264  -0.0605 322 ALA B CB  
7656 N N   . PHE B 323 ? 0.8403 1.9081 0.8017 -0.1559 0.0229  -0.0513 323 PHE B N   
7657 C CA  . PHE B 323 ? 0.8339 1.9740 0.8009 -0.1556 0.0218  -0.0512 323 PHE B CA  
7658 C C   . PHE B 323 ? 0.8205 1.9869 0.7977 -0.1227 0.0187  -0.0390 323 PHE B C   
7659 O O   . PHE B 323 ? 0.8593 2.0729 0.8396 -0.1188 0.0169  -0.0375 323 PHE B O   
7660 C CB  . PHE B 323 ? 0.8484 2.0179 0.8158 -0.1676 0.0241  -0.0558 323 PHE B CB  
7661 C CG  . PHE B 323 ? 0.8460 2.0913 0.8215 -0.1602 0.0227  -0.0532 323 PHE B CG  
7662 C CD1 . PHE B 323 ? 0.8346 2.1313 0.8084 -0.1780 0.0222  -0.0598 323 PHE B CD1 
7663 C CD2 . PHE B 323 ? 0.8436 2.1097 0.8278 -0.1350 0.0220  -0.0442 323 PHE B CD2 
7664 C CE1 . PHE B 323 ? 0.8357 2.2054 0.8172 -0.1706 0.0208  -0.0572 323 PHE B CE1 
7665 C CE2 . PHE B 323 ? 0.8471 2.1844 0.8382 -0.1266 0.0209  -0.0413 323 PHE B CE2 
7666 C CZ  . PHE B 323 ? 0.8397 2.2301 0.8299 -0.1443 0.0202  -0.0477 323 PHE B CZ  
7667 N N   . MET B 324 ? 0.7963 1.9324 0.7776 -0.0990 0.0185  -0.0303 324 MET B N   
7668 C CA  . MET B 324 ? 0.8137 1.9670 0.8023 -0.0666 0.0166  -0.0182 324 MET B CA  
7669 C C   . MET B 324 ? 0.8170 1.9379 0.8046 -0.0546 0.0149  -0.0130 324 MET B C   
7670 O O   . MET B 324 ? 0.8206 1.9523 0.8124 -0.0284 0.0137  -0.0029 324 MET B O   
7671 C CB  . MET B 324 ? 0.8237 1.9599 0.8157 -0.0459 0.0175  -0.0111 324 MET B CB  
7672 C CG  . MET B 324 ? 0.8531 2.0416 0.8488 -0.0465 0.0186  -0.0120 324 MET B CG  
7673 S SD  . MET B 324 ? 0.8965 2.0889 0.8974 -0.0094 0.0190  0.0008  324 MET B SD  
7674 C CE  . MET B 324 ? 0.8598 2.1227 0.8646 -0.0158 0.0203  -0.0023 324 MET B CE  
7675 N N   . ASP B 325 ? 0.8370 1.9189 0.8182 -0.0737 0.0153  -0.0197 325 ASP B N   
7676 C CA  . ASP B 325 ? 0.8400 1.8947 0.8198 -0.0662 0.0139  -0.0161 325 ASP B CA  
7677 C C   . ASP B 325 ? 0.8336 1.9314 0.8119 -0.0774 0.0127  -0.0202 325 ASP B C   
7678 O O   . ASP B 325 ? 0.8271 1.9360 0.8079 -0.0613 0.0109  -0.0135 325 ASP B O   
7679 C CB  . ASP B 325 ? 0.8723 1.8612 0.8456 -0.0788 0.0151  -0.0206 325 ASP B CB  
7680 C CG  . ASP B 325 ? 0.8974 1.8510 0.8709 -0.0643 0.0138  -0.0143 325 ASP B CG  
7681 O OD1 . ASP B 325 ? 0.9232 1.8551 0.9008 -0.0409 0.0133  -0.0050 325 ASP B OD1 
7682 O OD2 . ASP B 325 ? 0.9048 1.8512 0.8736 -0.0769 0.0136  -0.0187 325 ASP B OD2 
7683 N N   . ARG B 326 ? 0.8296 1.9504 0.8030 -0.1055 0.0138  -0.0313 326 ARG B N   
7684 C CA  . ARG B 326 ? 0.8454 2.0149 0.8169 -0.1192 0.0128  -0.0366 326 ARG B CA  
7685 C C   . ARG B 326 ? 0.8069 2.0420 0.7868 -0.0998 0.0108  -0.0294 326 ARG B C   
7686 O O   . ARG B 326 ? 0.7768 2.0464 0.7578 -0.0957 0.0089  -0.0277 326 ARG B O   
7687 C CB  . ARG B 326 ? 0.8816 2.0634 0.8451 -0.1539 0.0152  -0.0502 326 ARG B CB  
7688 C CG  . ARG B 326 ? 0.9013 2.1327 0.8613 -0.1725 0.0145  -0.0575 326 ARG B CG  
7689 C CD  . ARG B 326 ? 0.9255 2.1913 0.8809 -0.2008 0.0169  -0.0685 326 ARG B CD  
7690 N NE  . ARG B 326 ? 0.9277 2.2483 0.8926 -0.1894 0.0161  -0.0642 326 ARG B NE  
7691 C CZ  . ARG B 326 ? 0.9374 2.3290 0.9053 -0.1969 0.0151  -0.0673 326 ARG B CZ  
7692 N NH1 . ARG B 326 ? 0.9159 2.3330 0.8778 -0.2172 0.0147  -0.0752 326 ARG B NH1 
7693 N NH2 . ARG B 326 ? 0.9398 2.3782 0.9163 -0.1841 0.0146  -0.0625 326 ARG B NH2 
7694 N N   . LEU B 327 ? 0.7766 2.0279 0.7621 -0.0868 0.0114  -0.0248 327 LEU B N   
7695 C CA  . LEU B 327 ? 0.7455 2.0593 0.7382 -0.0671 0.0101  -0.0177 327 LEU B CA  
7696 C C   . LEU B 327 ? 0.7205 2.0272 0.7169 -0.0329 0.0087  -0.0043 327 LEU B C   
7697 O O   . LEU B 327 ? 0.7050 2.0585 0.7039 -0.0213 0.0071  0.0001  327 LEU B O   
7698 C CB  . LEU B 327 ? 0.7585 2.0896 0.7547 -0.0645 0.0117  -0.0173 327 LEU B CB  
7699 C CG  . LEU B 327 ? 0.7657 2.1749 0.7678 -0.0570 0.0111  -0.0150 327 LEU B CG  
7700 C CD1 . LEU B 327 ? 0.7620 2.2235 0.7621 -0.0848 0.0104  -0.0255 327 LEU B CD1 
7701 C CD2 . LEU B 327 ? 0.7465 2.1616 0.7514 -0.0534 0.0131  -0.0142 327 LEU B CD2 
7702 N N   . TYR B 328 ? 0.7151 1.9631 0.7110 -0.0172 0.0096  0.0019  328 TYR B N   
7703 C CA  . TYR B 328 ? 0.6849 1.9228 0.6831 0.0164  0.0092  0.0152  328 TYR B CA  
7704 C C   . TYR B 328 ? 0.6748 1.8665 0.6700 0.0212  0.0086  0.0183  328 TYR B C   
7705 O O   . TYR B 328 ? 0.6778 1.8757 0.6737 0.0444  0.0081  0.0279  328 TYR B O   
7706 C CB  . TYR B 328 ? 0.6878 1.8975 0.6874 0.0346  0.0110  0.0216  328 TYR B CB  
7707 C CG  . TYR B 328 ? 0.6772 1.9349 0.6804 0.0381  0.0119  0.0217  328 TYR B CG  
7708 C CD1 . TYR B 328 ? 0.6793 1.9963 0.6856 0.0581  0.0116  0.0288  328 TYR B CD1 
7709 C CD2 . TYR B 328 ? 0.6755 1.9193 0.6784 0.0226  0.0133  0.0151  328 TYR B CD2 
7710 C CE1 . TYR B 328 ? 0.6767 2.0395 0.6863 0.0621  0.0125  0.0291  328 TYR B CE1 
7711 C CE2 . TYR B 328 ? 0.6758 1.9641 0.6820 0.0259  0.0143  0.0153  328 TYR B CE2 
7712 C CZ  . TYR B 328 ? 0.6884 2.0367 0.6982 0.0456  0.0139  0.0223  328 TYR B CZ  
7713 O OH  . TYR B 328 ? 0.7118 2.1064 0.7249 0.0496  0.0150  0.0227  328 TYR B OH  
7714 N N   . PHE B 329 ? 0.6454 1.7910 0.6365 -0.0001 0.0089  0.0105  329 PHE B N   
7715 C CA  . PHE B 329 ? 0.6514 1.7452 0.6398 0.0054  0.0086  0.0138  329 PHE B CA  
7716 C C   . PHE B 329 ? 0.6506 1.7414 0.6345 -0.0166 0.0078  0.0057  329 PHE B C   
7717 O O   . PHE B 329 ? 0.6594 1.7119 0.6410 -0.0133 0.0076  0.0080  329 PHE B O   
7718 C CB  . PHE B 329 ? 0.6131 1.6432 0.6002 0.0068  0.0100  0.0144  329 PHE B CB  
7719 C CG  . PHE B 329 ? 0.5915 1.6220 0.5818 0.0261  0.0112  0.0211  329 PHE B CG  
7720 C CD1 . PHE B 329 ? 0.5800 1.6082 0.5717 0.0561  0.0116  0.0330  329 PHE B CD1 
7721 C CD2 . PHE B 329 ? 0.5806 1.6130 0.5712 0.0145  0.0123  0.0155  329 PHE B CD2 
7722 C CE1 . PHE B 329 ? 0.5727 1.5999 0.5657 0.0741  0.0131  0.0390  329 PHE B CE1 
7723 C CE2 . PHE B 329 ? 0.5623 1.5953 0.5552 0.0326  0.0134  0.0215  329 PHE B CE2 
7724 C CZ  . PHE B 329 ? 0.5523 1.5825 0.5462 0.0625  0.0138  0.0332  329 PHE B CZ  
7725 N N   . SER B 330 ? 0.6698 1.8019 0.6519 -0.0391 0.0075  -0.0037 330 SER B N   
7726 C CA  . SER B 330 ? 0.7093 1.8402 0.6851 -0.0629 0.0073  -0.0128 330 SER B CA  
7727 C C   . SER B 330 ? 0.7109 1.8557 0.6869 -0.0509 0.0055  -0.0074 330 SER B C   
7728 O O   . SER B 330 ? 0.7007 1.8058 0.6725 -0.0547 0.0056  -0.0082 330 SER B O   
7729 C CB  . SER B 330 ? 0.7535 1.9315 0.7266 -0.0890 0.0077  -0.0238 330 SER B CB  
7730 O OG  . SER B 330 ? 0.7873 1.9904 0.7556 -0.1049 0.0068  -0.0302 330 SER B OG  
7731 N N   . ASN B 331 ? 0.6932 1.8942 0.6740 -0.0354 0.0040  -0.0016 331 ASN B N   
7732 C CA  . ASN B 331 ? 0.6878 1.9136 0.6682 -0.0265 0.0023  0.0024  331 ASN B CA  
7733 C C   . ASN B 331 ? 0.6930 1.9034 0.6766 0.0072  0.0022  0.0167  331 ASN B C   
7734 O O   . ASN B 331 ? 0.6981 1.9500 0.6835 0.0243  0.0012  0.0236  331 ASN B O   
7735 C CB  . ASN B 331 ? 0.6868 1.9890 0.6689 -0.0325 0.0008  -0.0008 331 ASN B CB  
7736 C CG  . ASN B 331 ? 0.6863 2.0105 0.6664 -0.0616 0.0016  -0.0132 331 ASN B CG  
7737 O OD1 . ASN B 331 ? 0.6702 2.0249 0.6546 -0.0580 0.0020  -0.0124 331 ASN B OD1 
7738 N ND2 . ASN B 331 ? 0.7075 2.0155 0.6799 -0.0906 0.0022  -0.0248 331 ASN B ND2 
7739 N N   . LEU B 332 ? 0.6965 1.8467 0.6797 0.0163  0.0036  0.0211  332 LEU B N   
7740 C CA  . LEU B 332 ? 0.6631 1.7949 0.6484 0.0479  0.0045  0.0346  332 LEU B CA  
7741 C C   . LEU B 332 ? 0.6294 1.7476 0.6125 0.0610  0.0042  0.0414  332 LEU B C   
7742 O O   . LEU B 332 ? 0.6180 1.7341 0.6015 0.0882  0.0051  0.0531  332 LEU B O   
7743 C CB  . LEU B 332 ? 0.6542 1.7297 0.6397 0.0527  0.0062  0.0366  332 LEU B CB  
7744 C CG  . LEU B 332 ? 0.6449 1.7359 0.6334 0.0691  0.0074  0.0420  332 LEU B CG  
7745 C CD1 . LEU B 332 ? 0.6502 1.6824 0.6382 0.0719  0.0089  0.0432  332 LEU B CD1 
7746 C CD2 . LEU B 332 ? 0.6332 1.7527 0.6222 0.0998  0.0080  0.0545  332 LEU B CD2 
7747 N N   . ASP B 333 ? 0.5896 1.6976 0.5694 0.0420  0.0032  0.0343  333 ASP B N   
7748 C CA  . ASP B 333 ? 0.6137 1.7024 0.5912 0.0510  0.0031  0.0395  333 ASP B CA  
7749 C C   . ASP B 333 ? 0.6520 1.6955 0.6256 0.0286  0.0033  0.0309  333 ASP B C   
7750 O O   . ASP B 333 ? 0.6836 1.6737 0.6568 0.0291  0.0045  0.0318  333 ASP B O   
7751 C CB  . ASP B 333 ? 0.5735 1.6306 0.5518 0.0804  0.0048  0.0529  333 ASP B CB  
7752 C CG  . ASP B 333 ? 0.5707 1.6115 0.5463 0.0912  0.0051  0.0593  333 ASP B CG  
7753 O OD1 . ASP B 333 ? 0.5622 1.5949 0.5354 0.0742  0.0041  0.0528  333 ASP B OD1 
7754 O OD2 . ASP B 333 ? 0.5716 1.6058 0.5466 0.1170  0.0067  0.0710  333 ASP B OD2 
7755 N N   . LYS B 334 ? 0.6925 1.7581 0.6623 0.0089  0.0022  0.0224  334 LYS B N   
7756 C CA  . LYS B 334 ? 0.7380 1.7637 0.7019 -0.0128 0.0028  0.0137  334 LYS B CA  
7757 C C   . LYS B 334 ? 0.7475 1.7140 0.7113 -0.0012 0.0039  0.0201  334 LYS B C   
7758 O O   . LYS B 334 ? 0.7527 1.6743 0.7131 -0.0148 0.0050  0.0146  334 LYS B O   
7759 C CB  . LYS B 334 ? 0.7644 1.8213 0.7233 -0.0273 0.0016  0.0073  334 LYS B CB  
7760 C CG  . LYS B 334 ? 0.7824 1.8807 0.7381 -0.0519 0.0012  -0.0043 334 LYS B CG  
7761 C CD  . LYS B 334 ? 0.8398 1.9810 0.7916 -0.0603 -0.0002 -0.0082 334 LYS B CD  
7762 C CE  . LYS B 334 ? 0.8607 2.0318 0.8065 -0.0908 0.0000  -0.0222 334 LYS B CE  
7763 N NZ  . LYS B 334 ? 0.8726 1.9973 0.8080 -0.1154 0.0022  -0.0326 334 LYS B NZ  
7764 N N   . ASP B 335 ? 0.7388 1.7063 0.7056 0.0241  0.0039  0.0319  335 ASP B N   
7765 C CA  . ASP B 335 ? 0.7285 1.6470 0.6948 0.0355  0.0051  0.0386  335 ASP B CA  
7766 C C   . ASP B 335 ? 0.6928 1.5743 0.6624 0.0515  0.0066  0.0460  335 ASP B C   
7767 O O   . ASP B 335 ? 0.6947 1.5370 0.6641 0.0625  0.0077  0.0524  335 ASP B O   
7768 C CB  . ASP B 335 ? 0.7824 1.7205 0.7480 0.0518  0.0048  0.0468  335 ASP B CB  
7769 C CG  . ASP B 335 ? 0.8316 1.7963 0.7931 0.0353  0.0034  0.0394  335 ASP B CG  
7770 O OD1 . ASP B 335 ? 0.8507 1.8382 0.8100 0.0138  0.0025  0.0286  335 ASP B OD1 
7771 O OD2 . ASP B 335 ? 0.8635 1.8261 0.8231 0.0437  0.0035  0.0442  335 ASP B OD2 
7772 N N   . ALA B 336 ? 0.6302 1.5245 0.6023 0.0526  0.0067  0.0450  336 ALA B N   
7773 C CA  . ALA B 336 ? 0.5944 1.4515 0.5686 0.0639  0.0081  0.0499  336 ALA B CA  
7774 C C   . ALA B 336 ? 0.5763 1.3962 0.5495 0.0438  0.0083  0.0409  336 ALA B C   
7775 O O   . ALA B 336 ? 0.5690 1.4000 0.5397 0.0216  0.0077  0.0307  336 ALA B O   
7776 C CB  . ALA B 336 ? 0.5546 1.4438 0.5314 0.0790  0.0085  0.0549  336 ALA B CB  
7777 N N   . PHE B 337 ? 0.5685 1.3439 0.5429 0.0517  0.0095  0.0448  337 PHE B N   
7778 C CA  . PHE B 337 ? 0.5380 1.2779 0.5115 0.0363  0.0098  0.0377  337 PHE B CA  
7779 C C   . PHE B 337 ? 0.5145 1.2663 0.4902 0.0381  0.0101  0.0368  337 PHE B C   
7780 O O   . PHE B 337 ? 0.5196 1.2759 0.4976 0.0579  0.0108  0.0448  337 PHE B O   
7781 C CB  . PHE B 337 ? 0.5498 1.2352 0.5233 0.0426  0.0107  0.0418  337 PHE B CB  
7782 C CG  . PHE B 337 ? 0.5291 1.1785 0.5021 0.0316  0.0112  0.0364  337 PHE B CG  
7783 C CD1 . PHE B 337 ? 0.5196 1.1596 0.4949 0.0407  0.0117  0.0393  337 PHE B CD1 
7784 C CD2 . PHE B 337 ? 0.5304 1.1550 0.4996 0.0127  0.0113  0.0285  337 PHE B CD2 
7785 C CE1 . PHE B 337 ? 0.5242 1.1324 0.4988 0.0308  0.0120  0.0343  337 PHE B CE1 
7786 C CE2 . PHE B 337 ? 0.5329 1.1249 0.5008 0.0037  0.0119  0.0239  337 PHE B CE2 
7787 C CZ  . PHE B 337 ? 0.5218 1.1061 0.4927 0.0126  0.0121  0.0268  337 PHE B CZ  
7788 N N   . ILE B 338 ? 0.4960 1.2508 0.4699 0.0176  0.0100  0.0270  338 ILE B N   
7789 C CA  . ILE B 338 ? 0.4785 1.2425 0.4541 0.0166  0.0104  0.0251  338 ILE B CA  
7790 C C   . ILE B 338 ? 0.4770 1.2100 0.4489 -0.0043 0.0111  0.0158  338 ILE B C   
7791 O O   . ILE B 338 ? 0.4880 1.2172 0.4550 -0.0233 0.0114  0.0081  338 ILE B O   
7792 C CB  . ILE B 338 ? 0.4793 1.3037 0.4562 0.0140  0.0098  0.0229  338 ILE B CB  
7793 C CG1 . ILE B 338 ? 0.4909 1.3266 0.4701 0.0161  0.0105  0.0223  338 ILE B CG1 
7794 C CG2 . ILE B 338 ? 0.4669 1.3120 0.4395 -0.0109 0.0094  0.0124  338 ILE B CG2 
7795 C CD1 . ILE B 338 ? 0.5003 1.3973 0.4823 0.0223  0.0100  0.0239  338 ILE B CD1 
7796 N N   . HIS B 339 ? 0.4926 1.2026 0.4659 -0.0005 0.0118  0.0166  339 HIS B N   
7797 C CA  . HIS B 339 ? 0.5231 1.2057 0.4923 -0.0189 0.0128  0.0083  339 HIS B CA  
7798 C C   . HIS B 339 ? 0.5437 1.2254 0.5153 -0.0135 0.0133  0.0094  339 HIS B C   
7799 O O   . HIS B 339 ? 0.5391 1.2184 0.5147 0.0067  0.0132  0.0176  339 HIS B O   
7800 C CB  . HIS B 339 ? 0.5267 1.1568 0.4933 -0.0209 0.0131  0.0084  339 HIS B CB  
7801 C CG  . HIS B 339 ? 0.5182 1.1220 0.4783 -0.0417 0.0145  -0.0007 339 HIS B CG  
7802 N ND1 . HIS B 339 ? 0.5160 1.0965 0.4755 -0.0436 0.0153  -0.0024 339 HIS B ND1 
7803 C CD2 . HIS B 339 ? 0.5126 1.1094 0.4648 -0.0614 0.0156  -0.0088 339 HIS B CD2 
7804 C CE1 . HIS B 339 ? 0.5208 1.0808 0.4724 -0.0630 0.0169  -0.0107 339 HIS B CE1 
7805 N NE2 . HIS B 339 ? 0.5214 1.0905 0.4682 -0.0739 0.0173  -0.0147 339 HIS B NE2 
7806 N N   . ARG B 340 ? 0.5998 1.2813 0.5677 -0.0318 0.0144  0.0010  340 ARG B N   
7807 C CA  . ARG B 340 ? 0.6315 1.3194 0.6012 -0.0294 0.0151  0.0008  340 ARG B CA  
7808 C C   . ARG B 340 ? 0.6549 1.3051 0.6198 -0.0437 0.0165  -0.0055 340 ARG B C   
7809 O O   . ARG B 340 ? 0.6153 1.2459 0.5735 -0.0615 0.0175  -0.0123 340 ARG B O   
7810 C CB  . ARG B 340 ? 0.6867 1.4302 0.6574 -0.0363 0.0152  -0.0025 340 ARG B CB  
7811 C CG  . ARG B 340 ? 0.7455 1.4994 0.7094 -0.0640 0.0165  -0.0136 340 ARG B CG  
7812 C CD  . ARG B 340 ? 0.8356 1.6489 0.8010 -0.0708 0.0165  -0.0167 340 ARG B CD  
7813 N NE  . ARG B 340 ? 0.8897 1.7076 0.8486 -0.0962 0.0187  -0.0271 340 ARG B NE  
7814 C CZ  . ARG B 340 ? 0.9003 1.7105 0.8587 -0.0997 0.0202  -0.0291 340 ARG B CZ  
7815 N NH1 . ARG B 340 ? 0.8947 1.6923 0.8589 -0.0795 0.0195  -0.0217 340 ARG B NH1 
7816 N NH2 . ARG B 340 ? 0.9047 1.7185 0.8558 -0.1239 0.0227  -0.0387 340 ARG B NH2 
7817 N N   . THR B 341 ? 0.6634 1.3029 0.6305 -0.0348 0.0168  -0.0028 341 THR B N   
7818 C CA  . THR B 341 ? 0.7219 1.3435 0.6847 -0.0487 0.0184  -0.0093 341 THR B CA  
7819 C C   . THR B 341 ? 0.7810 1.4395 0.7469 -0.0453 0.0189  -0.0089 341 THR B C   
7820 O O   . THR B 341 ? 0.7668 1.4669 0.7374 -0.0351 0.0181  -0.0048 341 THR B O   
7821 C CB  . THR B 341 ? 0.6904 1.2602 0.6526 -0.0420 0.0184  -0.0069 341 THR B CB  
7822 O OG1 . THR B 341 ? 0.6618 1.2296 0.6298 -0.0196 0.0174  0.0015  341 THR B OG1 
7823 C CG2 . THR B 341 ? 0.6744 1.2095 0.6335 -0.0455 0.0180  -0.0073 341 THR B CG2 
7824 N N   . VAL B 342 ? 0.8531 1.4980 0.8164 -0.0531 0.0204  -0.0129 342 VAL B N   
7825 C CA  . VAL B 342 ? 0.9157 1.5916 0.8821 -0.0479 0.0210  -0.0118 342 VAL B CA  
7826 C C   . VAL B 342 ? 0.9224 1.5971 0.8948 -0.0209 0.0199  -0.0019 342 VAL B C   
7827 O O   . VAL B 342 ? 0.9383 1.6518 0.9146 -0.0095 0.0199  0.0019  342 VAL B O   
7828 C CB  . VAL B 342 ? 0.9520 1.6103 0.9135 -0.0619 0.0231  -0.0180 342 VAL B CB  
7829 C CG1 . VAL B 342 ? 0.9772 1.6539 0.9321 -0.0882 0.0252  -0.0277 342 VAL B CG1 
7830 C CG2 . VAL B 342 ? 0.9539 1.5551 0.9120 -0.0607 0.0232  -0.0178 342 VAL B CG2 
7831 N N   . ASP B 343 ? 0.8919 1.5225 0.8642 -0.0108 0.0191  0.0021  343 ASP B N   
7832 C CA  . ASP B 343 ? 0.8755 1.4938 0.8508 0.0125  0.0188  0.0106  343 ASP B CA  
7833 C C   . ASP B 343 ? 0.8461 1.4670 0.8237 0.0295  0.0179  0.0184  343 ASP B C   
7834 O O   . ASP B 343 ? 0.8309 1.4587 0.8100 0.0501  0.0183  0.0259  343 ASP B O   
7835 C CB  . ASP B 343 ? 0.9027 1.4700 0.8756 0.0127  0.0189  0.0100  343 ASP B CB  
7836 C CG  . ASP B 343 ? 0.9216 1.4796 0.8904 -0.0062 0.0201  0.0018  343 ASP B CG  
7837 O OD1 . ASP B 343 ? 0.9678 1.5539 0.9369 -0.0096 0.0213  -0.0003 343 ASP B OD1 
7838 O OD2 . ASP B 343 ? 0.8881 1.4108 0.8530 -0.0175 0.0202  -0.0021 343 ASP B OD2 
7839 N N   . ASP B 344 ? 0.8161 1.4301 0.7929 0.0212  0.0170  0.0166  344 ASP B N   
7840 C CA  . ASP B 344 ? 0.7454 1.3539 0.7237 0.0359  0.0163  0.0238  344 ASP B CA  
7841 C C   . ASP B 344 ? 0.6820 1.3298 0.6614 0.0323  0.0157  0.0234  344 ASP B C   
7842 O O   . ASP B 344 ? 0.6678 1.3279 0.6452 0.0126  0.0155  0.0158  344 ASP B O   
7843 C CB  . ASP B 344 ? 0.7630 1.3236 0.7398 0.0321  0.0158  0.0235  344 ASP B CB  
7844 C CG  . ASP B 344 ? 0.8040 1.3261 0.7789 0.0279  0.0161  0.0208  344 ASP B CG  
7845 O OD1 . ASP B 344 ? 0.8444 1.3551 0.8200 0.0419  0.0166  0.0253  344 ASP B OD1 
7846 O OD2 . ASP B 344 ? 0.8189 1.3210 0.7909 0.0110  0.0160  0.0141  344 ASP B OD2 
7847 N N   . TYR B 345 ? 0.6332 1.2985 0.6144 0.0514  0.0157  0.0316  345 TYR B N   
7848 C CA  . TYR B 345 ? 0.6046 1.2977 0.5863 0.0510  0.0149  0.0327  345 TYR B CA  
7849 C C   . TYR B 345 ? 0.5569 1.2218 0.5382 0.0646  0.0149  0.0399  345 TYR B C   
7850 O O   . TYR B 345 ? 0.5582 1.2022 0.5390 0.0827  0.0159  0.0472  345 TYR B O   
7851 C CB  . TYR B 345 ? 0.6446 1.3933 0.6284 0.0613  0.0151  0.0361  345 TYR B CB  
7852 C CG  . TYR B 345 ? 0.6797 1.4695 0.6640 0.0414  0.0146  0.0275  345 TYR B CG  
7853 C CD1 . TYR B 345 ? 0.7036 1.5119 0.6867 0.0256  0.0136  0.0221  345 TYR B CD1 
7854 C CD2 . TYR B 345 ? 0.6958 1.5060 0.6810 0.0379  0.0154  0.0246  345 TYR B CD2 
7855 C CE1 . TYR B 345 ? 0.7223 1.5677 0.7046 0.0059  0.0135  0.0137  345 TYR B CE1 
7856 C CE2 . TYR B 345 ? 0.7133 1.5615 0.6984 0.0184  0.0153  0.0165  345 TYR B CE2 
7857 C CZ  . TYR B 345 ? 0.7166 1.5817 0.6999 0.0019  0.0145  0.0109  345 TYR B CZ  
7858 O OH  . TYR B 345 ? 0.7567 1.6589 0.7387 -0.0188 0.0148  0.0023  345 TYR B OH  
7859 N N   . PHE B 346 ? 0.5050 1.1688 0.4856 0.0553  0.0140  0.0376  346 PHE B N   
7860 C CA  . PHE B 346 ? 0.4847 1.1233 0.4648 0.0657  0.0141  0.0438  346 PHE B CA  
7861 C C   . PHE B 346 ? 0.4741 1.1476 0.4543 0.0663  0.0134  0.0451  346 PHE B C   
7862 O O   . PHE B 346 ? 0.4974 1.1895 0.4768 0.0485  0.0124  0.0377  346 PHE B O   
7863 C CB  . PHE B 346 ? 0.4770 1.0696 0.4557 0.0524  0.0137  0.0392  346 PHE B CB  
7864 C CG  . PHE B 346 ? 0.4617 1.0246 0.4401 0.0620  0.0140  0.0452  346 PHE B CG  
7865 C CD1 . PHE B 346 ? 0.4568 1.0139 0.4352 0.0834  0.0152  0.0549  346 PHE B CD1 
7866 C CD2 . PHE B 346 ? 0.4531 0.9918 0.4304 0.0493  0.0134  0.0412  346 PHE B CD2 
7867 C CE1 . PHE B 346 ? 0.4680 0.9976 0.4456 0.0908  0.0159  0.0602  346 PHE B CE1 
7868 C CE2 . PHE B 346 ? 0.4728 0.9854 0.4502 0.0573  0.0138  0.0466  346 PHE B CE2 
7869 C CZ  . PHE B 346 ? 0.4702 0.9787 0.4480 0.0775  0.0150  0.0560  346 PHE B CZ  
7870 N N   . PHE B 347 ? 0.4592 1.1416 0.4393 0.0870  0.0142  0.0545  347 PHE B N   
7871 C CA  . PHE B 347 ? 0.4659 1.1867 0.4460 0.0911  0.0136  0.0570  347 PHE B CA  
7872 C C   . PHE B 347 ? 0.4609 1.1607 0.4392 0.1072  0.0147  0.0659  347 PHE B C   
7873 O O   . PHE B 347 ? 0.4808 1.1571 0.4574 0.1245  0.0166  0.0735  347 PHE B O   
7874 C CB  . PHE B 347 ? 0.4676 1.2392 0.4486 0.1024  0.0139  0.0601  347 PHE B CB  
7875 C CG  . PHE B 347 ? 0.4726 1.2877 0.4535 0.1087  0.0133  0.0633  347 PHE B CG  
7876 C CD1 . PHE B 347 ? 0.4798 1.2968 0.4584 0.1326  0.0149  0.0743  347 PHE B CD1 
7877 C CD2 . PHE B 347 ? 0.4739 1.3272 0.4559 0.0903  0.0115  0.0553  347 PHE B CD2 
7878 C CE1 . PHE B 347 ? 0.4969 1.3543 0.4749 0.1391  0.0143  0.0776  347 PHE B CE1 
7879 C CE2 . PHE B 347 ? 0.4927 1.3873 0.4743 0.0958  0.0107  0.0581  347 PHE B CE2 
7880 C CZ  . PHE B 347 ? 0.4959 1.3935 0.4760 0.1208  0.0120  0.0694  347 PHE B CZ  
7881 N N   . CYS B 348 ? 0.4654 1.1730 0.4433 0.1011  0.0138  0.0648  348 CYS B N   
7882 C CA  . CYS B 348 ? 0.4901 1.1795 0.4659 0.1151  0.0150  0.0731  348 CYS B CA  
7883 C C   . CYS B 348 ? 0.4889 1.2175 0.4639 0.1190  0.0144  0.0755  348 CYS B C   
7884 O O   . CYS B 348 ? 0.4866 1.2431 0.4624 0.1027  0.0125  0.0679  348 CYS B O   
7885 C CB  . CYS B 348 ? 0.4987 1.1408 0.4744 0.1041  0.0149  0.0702  348 CYS B CB  
7886 S SG  . CYS B 348 ? 0.4884 1.0815 0.4647 0.1024  0.0157  0.0689  348 CYS B SG  
7887 N N   . SER B 349 ? 0.4963 1.2253 0.4686 0.1403  0.0163  0.0859  349 SER B N   
7888 C CA  . SER B 349 ? 0.5158 1.2776 0.4866 0.1468  0.0161  0.0897  349 SER B CA  
7889 C C   . SER B 349 ? 0.5166 1.2507 0.4834 0.1645  0.0187  0.1000  349 SER B C   
7890 O O   . SER B 349 ? 0.5231 1.2266 0.4871 0.1786  0.0214  0.1066  349 SER B O   
7891 C CB  . SER B 349 ? 0.5333 1.3504 0.5039 0.1582  0.0159  0.0926  349 SER B CB  
7892 O OG  . SER B 349 ? 0.5293 1.3796 0.4981 0.1658  0.0156  0.0967  349 SER B OG  
7893 N N   . PRO B 350 ? 0.5169 1.2605 0.4825 0.1631  0.0182  0.1012  350 PRO B N   
7894 C CA  . PRO B 350 ? 0.5469 1.2736 0.5078 0.1819  0.0212  0.1120  350 PRO B CA  
7895 C C   . PRO B 350 ? 0.5711 1.3264 0.5272 0.2071  0.0236  0.1221  350 PRO B C   
7896 O O   . PRO B 350 ? 0.5980 1.3362 0.5481 0.2258  0.0271  0.1322  350 PRO B O   
7897 C CB  . PRO B 350 ? 0.5231 1.2635 0.4843 0.1722  0.0195  0.1093  350 PRO B CB  
7898 C CG  . PRO B 350 ? 0.5052 1.2840 0.4698 0.1534  0.0161  0.0987  350 PRO B CG  
7899 C CD  . PRO B 350 ? 0.5010 1.2648 0.4687 0.1425  0.0154  0.0921  350 PRO B CD  
7900 N N   . HIS B 351 ? 0.5836 1.3819 0.5416 0.2076  0.0221  0.1194  351 HIS B N   
7901 C CA  . HIS B 351 ? 0.5685 1.3991 0.5220 0.2319  0.0244  0.1286  351 HIS B CA  
7902 C C   . HIS B 351 ? 0.5655 1.3824 0.5177 0.2406  0.0262  0.1303  351 HIS B C   
7903 O O   . HIS B 351 ? 0.5606 1.3952 0.5178 0.2284  0.0240  0.1227  351 HIS B O   
7904 C CB  . HIS B 351 ? 0.5673 1.4618 0.5235 0.2280  0.0215  0.1251  351 HIS B CB  
7905 C CG  . HIS B 351 ? 0.5742 1.4825 0.5316 0.2155  0.0192  0.1212  351 HIS B CG  
7906 N ND1 . HIS B 351 ? 0.5695 1.4920 0.5319 0.1895  0.0156  0.1093  351 HIS B ND1 
7907 C CD2 . HIS B 351 ? 0.5926 1.4995 0.5457 0.2262  0.0206  0.1282  351 HIS B CD2 
7908 C CE1 . HIS B 351 ? 0.5672 1.4977 0.5285 0.1840  0.0146  0.1084  351 HIS B CE1 
7909 N NE2 . HIS B 351 ? 0.5847 1.5063 0.5408 0.2065  0.0174  0.1201  351 HIS B NE2 
7910 N N   . PRO B 352 ? 0.5730 1.3557 0.5175 0.2611  0.0308  0.1402  352 PRO B N   
7911 C CA  . PRO B 352 ? 0.5841 1.3447 0.5257 0.2700  0.0332  0.1423  352 PRO B CA  
7912 C C   . PRO B 352 ? 0.5994 1.4071 0.5416 0.2790  0.0329  0.1426  352 PRO B C   
7913 O O   . PRO B 352 ? 0.6137 1.4147 0.5582 0.2742  0.0325  0.1384  352 PRO B O   
7914 C CB  . PRO B 352 ? 0.6042 1.3285 0.5346 0.2932  0.0389  0.1542  352 PRO B CB  
7915 C CG  . PRO B 352 ? 0.6182 1.3596 0.5455 0.3008  0.0395  0.1599  352 PRO B CG  
7916 C CD  . PRO B 352 ? 0.5940 1.3536 0.5312 0.2757  0.0342  0.1497  352 PRO B CD  
7917 N N   . HIS B 353 ? 0.6050 1.4613 0.5451 0.2921  0.0330  0.1476  353 HIS B N   
7918 C CA  . HIS B 353 ? 0.6112 1.5177 0.5517 0.3024  0.0328  0.1487  353 HIS B CA  
7919 C C   . HIS B 353 ? 0.5894 1.5251 0.5402 0.2774  0.0281  0.1362  353 HIS B C   
7920 O O   . HIS B 353 ? 0.5880 1.5458 0.5405 0.2800  0.0281  0.1347  353 HIS B O   
7921 C CB  . HIS B 353 ? 0.6293 1.5838 0.5652 0.3220  0.0339  0.1569  353 HIS B CB  
7922 C CG  . HIS B 353 ? 0.6180 1.6137 0.5608 0.3047  0.0293  0.1503  353 HIS B CG  
7923 N ND1 . HIS B 353 ? 0.6073 1.6589 0.5571 0.2929  0.0256  0.1431  353 HIS B ND1 
7924 C CD2 . HIS B 353 ? 0.6355 1.6229 0.5784 0.2972  0.0281  0.1498  353 HIS B CD2 
7925 C CE1 . HIS B 353 ? 0.6093 1.6860 0.5627 0.2781  0.0223  0.1379  353 HIS B CE1 
7926 N NE2 . HIS B 353 ? 0.6195 1.6569 0.5688 0.2813  0.0238  0.1421  353 HIS B NE2 
7927 N N   . LYS B 354 ? 0.5813 1.5156 0.5383 0.2527  0.0244  0.1271  354 LYS B N   
7928 C CA  . LYS B 354 ? 0.5832 1.5399 0.5482 0.2263  0.0205  0.1145  354 LYS B CA  
7929 C C   . LYS B 354 ? 0.6014 1.5187 0.5684 0.2159  0.0208  0.1092  354 LYS B C   
7930 O O   . LYS B 354 ? 0.6214 1.5595 0.5930 0.2015  0.0189  0.1013  354 LYS B O   
7931 C CB  . LYS B 354 ? 0.5845 1.5410 0.5527 0.2039  0.0175  0.1068  354 LYS B CB  
7932 C CG  . LYS B 354 ? 0.5708 1.5790 0.5439 0.1837  0.0140  0.0968  354 LYS B CG  
7933 C CD  . LYS B 354 ? 0.5636 1.5817 0.5366 0.1714  0.0120  0.0932  354 LYS B CD  
7934 C CE  . LYS B 354 ? 0.5841 1.6394 0.5537 0.1926  0.0127  0.1026  354 LYS B CE  
7935 N NZ  . LYS B 354 ? 0.5682 1.6207 0.5366 0.1843  0.0115  0.1010  354 LYS B NZ  
7936 N N   . VAL B 355 ? 0.5985 1.4597 0.5615 0.2233  0.0232  0.1137  355 VAL B N   
7937 C CA  . VAL B 355 ? 0.5911 1.4126 0.5551 0.2163  0.0238  0.1099  355 VAL B CA  
7938 C C   . VAL B 355 ? 0.6053 1.4378 0.5659 0.2351  0.0263  0.1152  355 VAL B C   
7939 O O   . VAL B 355 ? 0.5768 1.4064 0.5403 0.2258  0.0256  0.1094  355 VAL B O   
7940 C CB  . VAL B 355 ? 0.5780 1.3369 0.5391 0.2158  0.0253  0.1121  355 VAL B CB  
7941 C CG1 . VAL B 355 ? 0.5440 1.2650 0.5064 0.2069  0.0254  0.1072  355 VAL B CG1 
7942 C CG2 . VAL B 355 ? 0.5570 1.3076 0.5213 0.1981  0.0229  0.1070  355 VAL B CG2 
7943 N N   . TYR B 356 ? 0.6432 1.4879 0.5965 0.2618  0.0297  0.1264  356 TYR B N   
7944 C CA  . TYR B 356 ? 0.6833 1.5467 0.6320 0.2824  0.0326  0.1322  356 TYR B CA  
7945 C C   . TYR B 356 ? 0.6388 1.5614 0.5944 0.2734  0.0297  0.1260  356 TYR B C   
7946 O O   . TYR B 356 ? 0.6199 1.5476 0.5766 0.2734  0.0301  0.1237  356 TYR B O   
7947 C CB  . TYR B 356 ? 0.7644 1.6369 0.7027 0.3133  0.0370  0.1455  356 TYR B CB  
7948 C CG  . TYR B 356 ? 0.8414 1.6543 0.7696 0.3272  0.0416  0.1533  356 TYR B CG  
7949 C CD1 . TYR B 356 ? 0.8781 1.6525 0.7996 0.3369  0.0451  0.1560  356 TYR B CD1 
7950 C CD2 . TYR B 356 ? 0.8768 1.6721 0.8013 0.3304  0.0427  0.1580  356 TYR B CD2 
7951 C CE1 . TYR B 356 ? 0.9317 1.6511 0.8429 0.3480  0.0496  0.1626  356 TYR B CE1 
7952 C CE2 . TYR B 356 ? 0.9103 1.6513 0.8250 0.3418  0.0472  0.1649  356 TYR B CE2 
7953 C CZ  . TYR B 356 ? 0.9384 1.6416 0.8462 0.3501  0.0507  0.1670  356 TYR B CZ  
7954 O OH  . TYR B 356 ? 0.9855 1.6347 0.8827 0.3597  0.0556  0.1734  356 TYR B OH  
7955 N N   . ASP B 357 ? 0.6198 1.5877 0.5796 0.2654  0.0269  0.1233  357 ASP B N   
7956 C CA  . ASP B 357 ? 0.5951 1.6252 0.5611 0.2560  0.0243  0.1175  357 ASP B CA  
7957 C C   . ASP B 357 ? 0.5610 1.5830 0.5338 0.2285  0.0217  0.1052  357 ASP B C   
7958 O O   . ASP B 357 ? 0.5580 1.6106 0.5335 0.2266  0.0215  0.1023  357 ASP B O   
7959 C CB  . ASP B 357 ? 0.5733 1.6481 0.5419 0.2494  0.0217  0.1158  357 ASP B CB  
7960 C CG  . ASP B 357 ? 0.5725 1.6686 0.5342 0.2785  0.0242  0.1284  357 ASP B CG  
7961 O OD1 . ASP B 357 ? 0.5710 1.6560 0.5254 0.3047  0.0284  0.1383  357 ASP B OD1 
7962 O OD2 . ASP B 357 ? 0.5646 1.6873 0.5270 0.2754  0.0225  0.1283  357 ASP B OD2 
7963 N N   . PHE B 358 ? 0.5577 1.5381 0.5325 0.2077  0.0201  0.0984  358 PHE B N   
7964 C CA  . PHE B 358 ? 0.5415 1.5050 0.5207 0.1827  0.0184  0.0874  358 PHE B CA  
7965 C C   . PHE B 358 ? 0.5489 1.4880 0.5265 0.1917  0.0205  0.0894  358 PHE B C   
7966 O O   . PHE B 358 ? 0.5636 1.5205 0.5446 0.1804  0.0198  0.0831  358 PHE B O   
7967 C CB  . PHE B 358 ? 0.5193 1.4351 0.4991 0.1639  0.0171  0.0816  358 PHE B CB  
7968 C CG  . PHE B 358 ? 0.4949 1.3855 0.4774 0.1415  0.0160  0.0717  358 PHE B CG  
7969 C CD1 . PHE B 358 ? 0.4831 1.4005 0.4686 0.1166  0.0139  0.0611  358 PHE B CD1 
7970 C CD2 . PHE B 358 ? 0.4936 1.3343 0.4744 0.1455  0.0175  0.0731  358 PHE B CD2 
7971 C CE1 . PHE B 358 ? 0.4932 1.3863 0.4795 0.0968  0.0136  0.0524  358 PHE B CE1 
7972 C CE2 . PHE B 358 ? 0.4874 1.3059 0.4700 0.1261  0.0167  0.0644  358 PHE B CE2 
7973 C CZ  . PHE B 358 ? 0.4946 1.3387 0.4798 0.1021  0.0148  0.0542  358 PHE B CZ  
7974 N N   . GLU B 359 ? 0.5681 1.4653 0.5398 0.2114  0.0234  0.0979  359 GLU B N   
7975 C CA  . GLU B 359 ? 0.6109 1.4813 0.5796 0.2214  0.0258  0.1002  359 GLU B CA  
7976 C C   . GLU B 359 ? 0.6077 1.5273 0.5764 0.2338  0.0269  0.1027  359 GLU B C   
7977 O O   . GLU B 359 ? 0.5965 1.5175 0.5675 0.2270  0.0268  0.0981  359 GLU B O   
7978 C CB  . GLU B 359 ? 0.6509 1.4736 0.6112 0.2425  0.0295  0.1099  359 GLU B CB  
7979 C CG  . GLU B 359 ? 0.6765 1.4638 0.6325 0.2506  0.0320  0.1114  359 GLU B CG  
7980 C CD  . GLU B 359 ? 0.7184 1.4636 0.6639 0.2732  0.0364  0.1214  359 GLU B CD  
7981 O OE1 . GLU B 359 ? 0.7360 1.4850 0.6769 0.2861  0.0381  0.1286  359 GLU B OE1 
7982 O OE2 . GLU B 359 ? 0.7408 1.4484 0.6818 0.2776  0.0385  0.1220  359 GLU B OE2 
7983 N N   . LEU B 360 ? 0.6140 1.5753 0.5802 0.2523  0.0280  0.1101  360 LEU B N   
7984 C CA  . LEU B 360 ? 0.6173 1.6343 0.5839 0.2647  0.0288  0.1128  360 LEU B CA  
7985 C C   . LEU B 360 ? 0.5818 1.6395 0.5574 0.2390  0.0254  0.1015  360 LEU B C   
7986 O O   . LEU B 360 ? 0.5498 1.6201 0.5269 0.2381  0.0260  0.0991  360 LEU B O   
7987 C CB  . LEU B 360 ? 0.6721 1.7307 0.6350 0.2861  0.0300  0.1219  360 LEU B CB  
7988 C CG  . LEU B 360 ? 0.7158 1.7529 0.6670 0.3203  0.0352  0.1354  360 LEU B CG  
7989 C CD1 . LEU B 360 ? 0.7016 1.7925 0.6494 0.3410  0.0362  0.1437  360 LEU B CD1 
7990 C CD2 . LEU B 360 ? 0.7120 1.7336 0.6583 0.3339  0.0385  0.1383  360 LEU B CD2 
7991 N N   . LEU B 361 ? 0.5632 1.6388 0.5437 0.2175  0.0221  0.0944  361 LEU B N   
7992 C CA  . LEU B 361 ? 0.5632 1.6751 0.5505 0.1902  0.0193  0.0829  361 LEU B CA  
7993 C C   . LEU B 361 ? 0.5762 1.6570 0.5652 0.1735  0.0193  0.0752  361 LEU B C   
7994 O O   . LEU B 361 ? 0.5962 1.7102 0.5883 0.1669  0.0193  0.0711  361 LEU B O   
7995 C CB  . LEU B 361 ? 0.5676 1.6852 0.5572 0.1682  0.0164  0.0759  361 LEU B CB  
7996 C CG  . LEU B 361 ? 0.5621 1.7065 0.5563 0.1357  0.0139  0.0627  361 LEU B CG  
7997 C CD1 . LEU B 361 ? 0.5823 1.8001 0.5799 0.1360  0.0133  0.0615  361 LEU B CD1 
7998 C CD2 . LEU B 361 ? 0.5579 1.6932 0.5518 0.1169  0.0118  0.0569  361 LEU B CD2 
7999 N N   . ILE B 362 ? 0.5844 1.6027 0.5714 0.1670  0.0195  0.0736  362 ILE B N   
8000 C CA  . ILE B 362 ? 0.5736 1.5584 0.5618 0.1500  0.0194  0.0662  362 ILE B CA  
8001 C C   . ILE B 362 ? 0.5759 1.5573 0.5622 0.1667  0.0219  0.0707  362 ILE B C   
8002 O O   . ILE B 362 ? 0.5686 1.5528 0.5571 0.1536  0.0218  0.0643  362 ILE B O   
8003 C CB  . ILE B 362 ? 0.5872 1.5077 0.5736 0.1400  0.0189  0.0637  362 ILE B CB  
8004 C CG1 . ILE B 362 ? 0.5750 1.4709 0.5629 0.1150  0.0181  0.0533  362 ILE B CG1 
8005 C CG2 . ILE B 362 ? 0.5959 1.4723 0.5772 0.1636  0.0213  0.0734  362 ILE B CG2 
8006 C CD1 . ILE B 362 ? 0.5948 1.4445 0.5805 0.1219  0.0196  0.0550  362 ILE B CD1 
8007 N N   . LYS B 363 ? 0.5916 1.5675 0.5729 0.1956  0.0244  0.0817  363 LYS B N   
8008 C CA  . LYS B 363 ? 0.6176 1.5889 0.5951 0.2142  0.0274  0.0868  363 LYS B CA  
8009 C C   . LYS B 363 ? 0.6214 1.6560 0.6023 0.2166  0.0275  0.0859  363 LYS B C   
8010 O O   . LYS B 363 ? 0.6223 1.6572 0.6024 0.2215  0.0292  0.0858  363 LYS B O   
8011 C CB  . LYS B 363 ? 0.6595 1.6069 0.6284 0.2448  0.0308  0.0989  363 LYS B CB  
8012 C CG  . LYS B 363 ? 0.6962 1.5730 0.6603 0.2452  0.0319  0.1001  363 LYS B CG  
8013 C CD  . LYS B 363 ? 0.7501 1.6044 0.7038 0.2749  0.0361  0.1120  363 LYS B CD  
8014 C CE  . LYS B 363 ? 0.8058 1.5910 0.7545 0.2739  0.0374  0.1126  363 LYS B CE  
8015 N NZ  . LYS B 363 ? 0.8492 1.6107 0.7883 0.2953  0.0409  0.1228  363 LYS B NZ  
8016 N N   . GLY B 364 ? 0.6320 1.7213 0.6165 0.2131  0.0259  0.0852  364 GLY B N   
8017 C CA  . GLY B 364 ? 0.6041 1.7593 0.5929 0.2114  0.0256  0.0831  364 GLY B CA  
8018 C C   . GLY B 364 ? 0.5979 1.7628 0.5926 0.1791  0.0236  0.0704  364 GLY B C   
8019 O O   . GLY B 364 ? 0.6073 1.8091 0.6047 0.1765  0.0242  0.0680  364 GLY B O   
8020 N N   . VAL B 365 ? 0.5887 1.7195 0.5845 0.1549  0.0216  0.0625  365 VAL B N   
8021 C CA  . VAL B 365 ? 0.5754 1.7127 0.5747 0.1227  0.0201  0.0502  365 VAL B CA  
8022 C C   . VAL B 365 ? 0.5968 1.6877 0.5946 0.1152  0.0213  0.0464  365 VAL B C   
8023 O O   . VAL B 365 ? 0.6315 1.7420 0.6313 0.1013  0.0218  0.0402  365 VAL B O   
8024 C CB  . VAL B 365 ? 0.5521 1.6771 0.5516 0.0992  0.0179  0.0429  365 VAL B CB  
8025 C CG1 . VAL B 365 ? 0.5380 1.6633 0.5384 0.0663  0.0174  0.0302  365 VAL B CG1 
8026 C CG2 . VAL B 365 ? 0.5472 1.7231 0.5482 0.1040  0.0165  0.0454  365 VAL B CG2 
8027 N N   . TYR B 366 ? 0.6455 1.6758 0.6397 0.1240  0.0219  0.0501  366 TYR B N   
8028 C CA  . TYR B 366 ? 0.6476 1.6305 0.6401 0.1170  0.0228  0.0465  366 TYR B CA  
8029 C C   . TYR B 366 ? 0.6709 1.6247 0.6591 0.1441  0.0251  0.0557  366 TYR B C   
8030 O O   . TYR B 366 ? 0.6820 1.6388 0.6673 0.1678  0.0263  0.0649  366 TYR B O   
8031 C CB  . TYR B 366 ? 0.6250 1.5568 0.6162 0.0978  0.0214  0.0405  366 TYR B CB  
8032 C CG  . TYR B 366 ? 0.6231 1.5739 0.6159 0.0686  0.0198  0.0304  366 TYR B CG  
8033 C CD1 . TYR B 366 ? 0.6344 1.6053 0.6278 0.0480  0.0204  0.0219  366 TYR B CD1 
8034 C CD2 . TYR B 366 ? 0.6237 1.5692 0.6159 0.0612  0.0183  0.0291  366 TYR B CD2 
8035 C CE1 . TYR B 366 ? 0.6364 1.6212 0.6291 0.0205  0.0197  0.0122  366 TYR B CE1 
8036 C CE2 . TYR B 366 ? 0.6234 1.5832 0.6152 0.0343  0.0174  0.0195  366 TYR B CE2 
8037 C CZ  . TYR B 366 ? 0.6255 1.6043 0.6171 0.0139  0.0182  0.0110  366 TYR B CZ  
8038 O OH  . TYR B 366 ? 0.6442 1.6347 0.6332 -0.0135 0.0180  0.0011  366 TYR B OH  
8039 N N   . GLN B 367 ? 0.7179 1.6432 0.7048 0.1405  0.0262  0.0529  367 GLN B N   
8040 C CA  . GLN B 367 ? 0.7633 1.6467 0.7448 0.1617  0.0283  0.0598  367 GLN B CA  
8041 C C   . GLN B 367 ? 0.7711 1.5963 0.7502 0.1577  0.0274  0.0597  367 GLN B C   
8042 O O   . GLN B 367 ? 0.7734 1.5756 0.7545 0.1350  0.0255  0.0519  367 GLN B O   
8043 C CB  . GLN B 367 ? 0.8024 1.6755 0.7831 0.1582  0.0295  0.0564  367 GLN B CB  
8044 C CG  . GLN B 367 ? 0.8614 1.7128 0.8357 0.1849  0.0325  0.0646  367 GLN B CG  
8045 C CD  . GLN B 367 ? 0.9052 1.8053 0.8778 0.2088  0.0348  0.0726  367 GLN B CD  
8046 O OE1 . GLN B 367 ? 0.9445 1.8437 0.9126 0.2295  0.0362  0.0811  367 GLN B OE1 
8047 N NE2 . GLN B 367 ? 0.8607 1.8044 0.8364 0.2063  0.0355  0.0702  367 GLN B NE2 
8048 N N   . VAL B 368 ? 0.7803 1.5820 0.7543 0.1798  0.0290  0.0686  368 VAL B N   
8049 C CA  . VAL B 368 ? 0.7881 1.5356 0.7596 0.1778  0.0284  0.0694  368 VAL B CA  
8050 C C   . VAL B 368 ? 0.8258 1.5254 0.7908 0.1918  0.0308  0.0735  368 VAL B C   
8051 O O   . VAL B 368 ? 0.8791 1.5874 0.8394 0.2105  0.0335  0.0787  368 VAL B O   
8052 C CB  . VAL B 368 ? 0.7501 1.5041 0.7204 0.1879  0.0284  0.0755  368 VAL B CB  
8053 C CG1 . VAL B 368 ? 0.7409 1.5378 0.7172 0.1714  0.0259  0.0703  368 VAL B CG1 
8054 C CG2 . VAL B 368 ? 0.7575 1.5277 0.7215 0.2177  0.0318  0.0863  368 VAL B CG2 
8055 N N   . ASN B 369 ? 0.8289 1.4787 0.7931 0.1822  0.0297  0.0707  369 ASN B N   
8056 C CA  . ASN B 369 ? 0.8613 1.4632 0.8184 0.1955  0.0319  0.0752  369 ASN B CA  
8057 C C   . ASN B 369 ? 0.8561 1.4382 0.8084 0.2093  0.0334  0.0827  369 ASN B C   
8058 O O   . ASN B 369 ? 0.8401 1.3978 0.7946 0.1982  0.0316  0.0806  369 ASN B O   
8059 C CB  . ASN B 369 ? 0.9050 1.4648 0.8637 0.1776  0.0301  0.0680  369 ASN B CB  
8060 C CG  . ASN B 369 ? 0.9451 1.5126 0.9048 0.1705  0.0300  0.0627  369 ASN B CG  
8061 O OD1 . ASN B 369 ? 0.9956 1.5692 0.9509 0.1859  0.0325  0.0664  369 ASN B OD1 
8062 N ND2 . ASN B 369 ? 0.9199 1.4859 0.8845 0.1474  0.0276  0.0541  369 ASN B ND2 
8063 N N   . PRO B 370 ? 0.8774 1.4703 0.8224 0.2341  0.0370  0.0918  370 PRO B N   
8064 C CA  . PRO B 370 ? 0.8877 1.4679 0.8269 0.2488  0.0391  0.0998  370 PRO B CA  
8065 C C   . PRO B 370 ? 0.9110 1.4321 0.8455 0.2467  0.0399  0.1004  370 PRO B C   
8066 O O   . PRO B 370 ? 0.9226 1.4298 0.8555 0.2487  0.0403  0.1040  370 PRO B O   
8067 C CB  . PRO B 370 ? 0.8832 1.4801 0.8128 0.2767  0.0437  0.1089  370 PRO B CB  
8068 C CG  . PRO B 370 ? 0.8643 1.4986 0.7979 0.2746  0.0431  0.1052  370 PRO B CG  
8069 C CD  . PRO B 370 ? 0.8520 1.4650 0.7922 0.2508  0.0399  0.0953  370 PRO B CD  
8070 N N   . THR B 371 ? 0.9215 1.4099 0.8538 0.2424  0.0401  0.0969  371 THR B N   
8071 C CA  . THR B 371 ? 0.9136 1.3479 0.8424 0.2372  0.0404  0.0959  371 THR B CA  
8072 C C   . THR B 371 ? 0.8993 1.3234 0.8373 0.2139  0.0361  0.0891  371 THR B C   
8073 O O   . THR B 371 ? 0.8928 1.2809 0.8291 0.2104  0.0361  0.0898  371 THR B O   
8074 C CB  . THR B 371 ? 0.9663 1.3723 0.8904 0.2381  0.0415  0.0933  371 THR B CB  
8075 O OG1 . THR B 371 ? 0.9547 1.3296 0.8838 0.2182  0.0383  0.0860  371 THR B OG1 
8076 C CG2 . THR B 371 ? 0.9662 1.4085 0.8930 0.2393  0.0412  0.0907  371 THR B CG2 
8077 N N   . LYS B 372 ? 0.8590 1.3150 0.8058 0.1980  0.0328  0.0825  372 LYS B N   
8078 C CA  . LYS B 372 ? 0.8305 1.2792 0.7847 0.1760  0.0291  0.0756  372 LYS B CA  
8079 C C   . LYS B 372 ? 0.7989 1.2665 0.7558 0.1748  0.0284  0.0779  372 LYS B C   
8080 O O   . LYS B 372 ? 0.8175 1.2804 0.7794 0.1579  0.0257  0.0728  372 LYS B O   
8081 C CB  . LYS B 372 ? 0.8575 1.3277 0.8177 0.1584  0.0267  0.0670  372 LYS B CB  
8082 C CG  . LYS B 372 ? 0.8838 1.3226 0.8433 0.1496  0.0260  0.0618  372 LYS B CG  
8083 C CD  . LYS B 372 ? 0.8977 1.3078 0.8605 0.1314  0.0235  0.0561  372 LYS B CD  
8084 C CE  . LYS B 372 ? 0.9140 1.3079 0.8775 0.1183  0.0223  0.0491  372 LYS B CE  
8085 N NZ  . LYS B 372 ? 0.9138 1.2853 0.8799 0.1006  0.0200  0.0435  372 LYS B NZ  
8086 N N   . THR B 373 ? 0.7483 1.2370 0.7010 0.1934  0.0308  0.0858  373 THR B N   
8087 C CA  . THR B 373 ? 0.7176 1.2276 0.6721 0.1946  0.0303  0.0887  373 THR B CA  
8088 C C   . THR B 373 ? 0.7092 1.1800 0.6608 0.1960  0.0312  0.0922  373 THR B C   
8089 O O   . THR B 373 ? 0.7398 1.1789 0.6838 0.2094  0.0343  0.0979  373 THR B O   
8090 C CB  . THR B 373 ? 0.7131 1.2615 0.6634 0.2155  0.0329  0.0965  373 THR B CB  
8091 O OG1 . THR B 373 ? 0.6818 1.2755 0.6370 0.2102  0.0314  0.0922  373 THR B OG1 
8092 C CG2 . THR B 373 ? 0.6816 1.2450 0.6317 0.2204  0.0330  0.1012  373 THR B CG2 
8093 N N   . ARG B 374 ? 0.6538 1.1266 0.6109 0.1816  0.0286  0.0887  374 ARG B N   
8094 C CA  . ARG B 374 ? 0.6441 1.0865 0.5992 0.1826  0.0294  0.0922  374 ARG B CA  
8095 C C   . ARG B 374 ? 0.6221 1.0926 0.5784 0.1859  0.0292  0.0957  374 ARG B C   
8096 O O   . ARG B 374 ? 0.5865 1.0904 0.5483 0.1744  0.0265  0.0907  374 ARG B O   
8097 C CB  . ARG B 374 ? 0.6505 1.0624 0.6104 0.1627  0.0267  0.0850  374 ARG B CB  
8098 C CG  . ARG B 374 ? 0.6509 1.0375 0.6105 0.1568  0.0262  0.0804  374 ARG B CG  
8099 C CD  . ARG B 374 ? 0.6692 1.0190 0.6214 0.1701  0.0293  0.0860  374 ARG B CD  
8100 N NE  . ARG B 374 ? 0.7196 1.0481 0.6715 0.1646  0.0287  0.0813  374 ARG B NE  
8101 C CZ  . ARG B 374 ? 0.7274 1.0620 0.6752 0.1739  0.0303  0.0822  374 ARG B CZ  
8102 N NH1 . ARG B 374 ? 0.7503 1.1119 0.6941 0.1902  0.0327  0.0879  374 ARG B NH1 
8103 N NH2 . ARG B 374 ? 0.7755 1.0899 0.7232 0.1677  0.0295  0.0775  374 ARG B NH2 
8104 N N   . THR B 375 ? 0.6160 1.0715 0.5660 0.2008  0.0322  0.1040  375 THR B N   
8105 C CA  . THR B 375 ? 0.6260 1.1066 0.5755 0.2072  0.0327  0.1088  375 THR B CA  
8106 C C   . THR B 375 ? 0.6343 1.0828 0.5772 0.2180  0.0360  0.1165  375 THR B C   
8107 O O   . THR B 375 ? 0.6502 1.0637 0.5860 0.2270  0.0392  0.1204  375 THR B O   
8108 C CB  . THR B 375 ? 0.6328 1.1583 0.5795 0.2234  0.0341  0.1136  375 THR B CB  
8109 O OG1 . THR B 375 ? 0.6143 1.1690 0.5618 0.2266  0.0337  0.1167  375 THR B OG1 
8110 C CG2 . THR B 375 ? 0.6518 1.1605 0.5875 0.2473  0.0392  0.1226  375 THR B CG2 
8111 N N   . ASN B 376 ? 0.6312 1.0915 0.5756 0.2165  0.0354  0.1185  376 ASN B N   
8112 C CA  . ASN B 376 ? 0.6583 1.0934 0.5955 0.2283  0.0392  0.1268  376 ASN B CA  
8113 C C   . ASN B 376 ? 0.7040 1.1637 0.6329 0.2512  0.0429  0.1366  376 ASN B C   
8114 O O   . ASN B 376 ? 0.7333 1.1814 0.6561 0.2609  0.0459  0.1437  376 ASN B O   
8115 C CB  . ASN B 376 ? 0.6264 1.0526 0.5689 0.2141  0.0370  0.1240  376 ASN B CB  
8116 C CG  . ASN B 376 ? 0.6057 1.0756 0.5532 0.2092  0.0343  0.1220  376 ASN B CG  
8117 O OD1 . ASN B 376 ? 0.6240 1.1316 0.5744 0.2082  0.0324  0.1189  376 ASN B OD1 
8118 N ND2 . ASN B 376 ? 0.5938 1.0591 0.5422 0.2052  0.0341  0.1234  376 ASN B ND2 
8119 N N   . LEU B 377 ? 0.7384 1.2325 0.6666 0.2603  0.0428  0.1371  377 LEU B N   
8120 C CA  . LEU B 377 ? 0.7866 1.3090 0.7068 0.2835  0.0463  0.1465  377 LEU B CA  
8121 C C   . LEU B 377 ? 0.8476 1.3343 0.7531 0.3051  0.0529  0.1562  377 LEU B C   
8122 O O   . LEU B 377 ? 0.8329 1.2935 0.7343 0.3071  0.0546  0.1552  377 LEU B O   
8123 C CB  . LEU B 377 ? 0.7643 1.3364 0.6883 0.2866  0.0444  0.1441  377 LEU B CB  
8124 C CG  . LEU B 377 ? 0.7424 1.3609 0.6773 0.2701  0.0391  0.1368  377 LEU B CG  
8125 C CD1 . LEU B 377 ? 0.7201 1.3830 0.6586 0.2710  0.0376  0.1336  377 LEU B CD1 
8126 C CD2 . LEU B 377 ? 0.7407 1.3831 0.6739 0.2775  0.0395  0.1422  377 LEU B CD2 
8127 N N   . PRO B 378 ? 0.9369 1.4213 0.8333 0.3212  0.0570  0.1655  378 PRO B N   
8128 C CA  . PRO B 378 ? 1.0130 1.4608 0.8928 0.3420  0.0643  0.1754  378 PRO B CA  
8129 C C   . PRO B 378 ? 1.0796 1.5323 0.9502 0.3601  0.0678  0.1790  378 PRO B C   
8130 O O   . PRO B 378 ? 1.1301 1.5416 0.9879 0.3705  0.0732  0.1834  378 PRO B O   
8131 C CB  . PRO B 378 ? 1.0322 1.4965 0.9053 0.3570  0.0672  0.1845  378 PRO B CB  
8132 C CG  . PRO B 378 ? 0.9959 1.5162 0.8814 0.3486  0.0615  0.1799  378 PRO B CG  
8133 C CD  . PRO B 378 ? 0.9539 1.4718 0.8541 0.3209  0.0552  0.1674  378 PRO B CD  
8134 N N   . THR B 379 ? 1.1204 1.6235 0.9972 0.3631  0.0649  0.1770  379 THR B N   
8135 C CA  . THR B 379 ? 1.1619 1.6772 1.0322 0.3788  0.0675  0.1794  379 THR B CA  
8136 C C   . THR B 379 ? 1.2002 1.6724 1.0678 0.3722  0.0685  0.1750  379 THR B C   
8137 O O   . THR B 379 ? 1.2817 1.7270 1.1344 0.3903  0.0745  0.1813  379 THR B O   
8138 C CB  . THR B 379 ? 1.1370 1.7143 1.0191 0.3739  0.0625  0.1743  379 THR B CB  
8139 O OG1 . THR B 379 ? 1.1614 1.7813 1.0392 0.3924  0.0642  0.1821  379 THR B OG1 
8140 C CG2 . THR B 379 ? 1.1628 1.7458 1.0435 0.3788  0.0631  0.1721  379 THR B CG2 
8141 N N   . HIS B 380 ? 1.1662 1.6310 1.0472 0.3466  0.0629  0.1644  380 HIS B N   
8142 C CA  . HIS B 380 ? 1.1611 1.6005 1.0430 0.3384  0.0622  0.1584  380 HIS B CA  
8143 C C   . HIS B 380 ? 1.1710 1.5514 1.0407 0.3429  0.0670  0.1614  380 HIS B C   
8144 O O   . HIS B 380 ? 1.1659 1.5187 1.0298 0.3444  0.0697  0.1657  380 HIS B O   
8145 C CB  . HIS B 380 ? 1.1507 1.5984 1.0492 0.3103  0.0552  0.1465  380 HIS B CB  
8146 C CG  . HIS B 380 ? 1.1528 1.6560 1.0615 0.3044  0.0510  0.1416  380 HIS B CG  
8147 N ND1 . HIS B 380 ? 1.1320 1.6801 1.0437 0.3090  0.0499  0.1443  380 HIS B ND1 
8148 C CD2 . HIS B 380 ? 1.1305 1.6509 1.0468 0.2929  0.0478  0.1339  380 HIS B CD2 
8149 C CE1 . HIS B 380 ? 1.1009 1.6931 1.0216 0.3003  0.0462  0.1382  380 HIS B CE1 
8150 N NE2 . HIS B 380 ? 1.1127 1.6873 1.0361 0.2904  0.0451  0.1320  380 HIS B NE2 
8151 N N   . ARG B 381 ? 1.1946 1.5558 1.0598 0.3448  0.0684  0.1591  381 ARG B N   
8152 C CA  . ARG B 381 ? 1.2331 1.5377 1.0859 0.3474  0.0730  0.1607  381 ARG B CA  
8153 C C   . ARG B 381 ? 1.2075 1.4796 1.0673 0.3261  0.0702  0.1555  381 ARG B C   
8154 O O   . ARG B 381 ? 1.2228 1.4590 1.0726 0.3299  0.0745  0.1602  381 ARG B O   
8155 C CB  . ARG B 381 ? 1.2621 1.5567 1.1123 0.3481  0.0733  0.1566  381 ARG B CB  
8156 C CG  . ARG B 381 ? 1.3059 1.6142 1.1424 0.3743  0.0788  0.1641  381 ARG B CG  
8157 C CD  . ARG B 381 ? 1.3222 1.6686 1.1678 0.3719  0.0752  0.1589  381 ARG B CD  
8158 N NE  . ARG B 381 ? 1.3552 1.7341 1.1916 0.3972  0.0793  0.1666  381 ARG B NE  
8159 C CZ  . ARG B 381 ? 1.3318 1.7647 1.1778 0.3984  0.0761  0.1647  381 ARG B CZ  
8160 N NH1 . ARG B 381 ? 1.3009 1.7592 1.1648 0.3751  0.0690  0.1551  381 ARG B NH1 
8161 N NH2 . ARG B 381 ? 1.3489 1.8105 1.1855 0.4232  0.0803  0.1726  381 ARG B NH2 
8162 N N   . HIS B 382 ? 1.1528 1.4379 1.0287 0.3039  0.0634  0.1458  382 HIS B N   
8163 C CA  . HIS B 382 ? 1.1211 1.3787 1.0044 0.2834  0.0604  0.1404  382 HIS B CA  
8164 C C   . HIS B 382 ? 1.0294 1.3182 0.9275 0.2680  0.0547  0.1356  382 HIS B C   
8165 O O   . HIS B 382 ? 0.9847 1.2857 0.8944 0.2508  0.0496  0.1270  382 HIS B O   
8166 C CB  . HIS B 382 ? 1.1629 1.3930 1.0488 0.2705  0.0584  0.1329  382 HIS B CB  
8167 C CG  . HIS B 382 ? 1.2523 1.4529 1.1229 0.2849  0.0639  0.1365  382 HIS B CG  
8168 N ND1 . HIS B 382 ? 1.2648 1.4682 1.1356 0.2848  0.0630  0.1323  382 HIS B ND1 
8169 C CD2 . HIS B 382 ? 1.2803 1.4465 1.1335 0.3002  0.0710  0.1442  382 HIS B CD2 
8170 C CE1 . HIS B 382 ? 1.2739 1.4464 1.1284 0.2994  0.0689  0.1369  382 HIS B CE1 
8171 N NE2 . HIS B 382 ? 1.2891 1.4381 1.1323 0.3086  0.0740  0.1441  382 HIS B NE2 
8172 N N   . PRO B 383 ? 0.9824 1.2836 0.8792 0.2740  0.0560  0.1412  383 PRO B N   
8173 C CA  . PRO B 383 ? 0.9185 1.2473 0.8278 0.2594  0.0510  0.1368  383 PRO B CA  
8174 C C   . PRO B 383 ? 0.8788 1.1796 0.7958 0.2386  0.0479  0.1304  383 PRO B C   
8175 O O   . PRO B 383 ? 0.8939 1.1545 0.8049 0.2386  0.0507  0.1325  383 PRO B O   
8176 C CB  . PRO B 383 ? 0.9068 1.2483 0.8099 0.2739  0.0543  0.1456  383 PRO B CB  
8177 C CG  . PRO B 383 ? 0.9347 1.2382 0.8220 0.2907  0.0611  0.1539  383 PRO B CG  
8178 C CD  . PRO B 383 ? 0.9706 1.2608 0.8529 0.2953  0.0625  0.1520  383 PRO B CD  
8179 N N   . GLN B 384 ? 0.8089 1.1311 0.7380 0.2210  0.0426  0.1225  384 GLN B N   
8180 C CA  . GLN B 384 ? 0.7535 1.0533 0.6899 0.2013  0.0394  0.1158  384 GLN B CA  
8181 C C   . GLN B 384 ? 0.7100 1.0330 0.6542 0.1907  0.0363  0.1132  384 GLN B C   
8182 O O   . GLN B 384 ? 0.6837 1.0453 0.6314 0.1901  0.0344  0.1115  384 GLN B O   
8183 C CB  . GLN B 384 ? 0.7301 1.0275 0.6723 0.1884  0.0360  0.1073  384 GLN B CB  
8184 C CG  . GLN B 384 ? 0.7689 1.0414 0.7044 0.1957  0.0384  0.1082  384 GLN B CG  
8185 C CD  . GLN B 384 ? 0.7494 1.0283 0.6905 0.1846  0.0351  0.1001  384 GLN B CD  
8186 O OE1 . GLN B 384 ? 0.7455 1.0304 0.6826 0.1932  0.0365  0.1007  384 GLN B OE1 
8187 N NE2 . GLN B 384 ? 0.7255 1.0033 0.6751 0.1659  0.0311  0.0927  384 GLN B NE2 
8188 N N   . ASP B 385 ? 0.7003 1.0002 0.6470 0.1812  0.0357  0.1122  385 ASP B N   
8189 C CA  . ASP B 385 ? 0.6751 0.9922 0.6287 0.1692  0.0327  0.1086  385 ASP B CA  
8190 C C   . ASP B 385 ? 0.6345 0.9580 0.5959 0.1504  0.0284  0.0985  385 ASP B C   
8191 O O   . ASP B 385 ? 0.6081 0.9574 0.5740 0.1412  0.0259  0.0942  385 ASP B O   
8192 C CB  . ASP B 385 ? 0.7171 1.0076 0.6699 0.1669  0.0342  0.1118  385 ASP B CB  
8193 C CG  . ASP B 385 ? 0.7734 1.0666 0.7186 0.1834  0.0383  0.1215  385 ASP B CG  
8194 O OD1 . ASP B 385 ? 0.8121 1.1313 0.7532 0.1969  0.0398  0.1257  385 ASP B OD1 
8195 O OD2 . ASP B 385 ? 0.7801 1.0505 0.7233 0.1831  0.0403  0.1251  385 ASP B OD2 
8196 N N   . GLU B 386 ? 0.5961 0.8954 0.5580 0.1449  0.0278  0.0946  386 GLU B N   
8197 C CA  . GLU B 386 ? 0.5870 0.8854 0.5547 0.1277  0.0243  0.0855  386 GLU B CA  
8198 C C   . GLU B 386 ? 0.5789 0.8962 0.5467 0.1279  0.0234  0.0820  386 GLU B C   
8199 O O   . GLU B 386 ? 0.6304 0.9372 0.5944 0.1374  0.0251  0.0845  386 GLU B O   
8200 C CB  . GLU B 386 ? 0.6126 0.8721 0.5811 0.1206  0.0240  0.0834  386 GLU B CB  
8201 C CG  . GLU B 386 ? 0.6605 0.8994 0.6280 0.1224  0.0256  0.0881  386 GLU B CG  
8202 C CD  . GLU B 386 ? 0.7161 0.9246 0.6864 0.1113  0.0243  0.0844  386 GLU B CD  
8203 O OE1 . GLU B 386 ? 0.7193 0.9134 0.6898 0.1072  0.0233  0.0805  386 GLU B OE1 
8204 O OE2 . GLU B 386 ? 0.7318 0.9321 0.7041 0.1071  0.0244  0.0856  386 GLU B OE2 
8205 N N   . ILE B 387 ? 0.5402 0.8856 0.5117 0.1174  0.0211  0.0761  387 ILE B N   
8206 C CA  . ILE B 387 ? 0.5321 0.8979 0.5040 0.1157  0.0204  0.0722  387 ILE B CA  
8207 C C   . ILE B 387 ? 0.5174 0.8768 0.4924 0.0968  0.0179  0.0629  387 ILE B C   
8208 O O   . ILE B 387 ? 0.4974 0.8593 0.4743 0.0842  0.0166  0.0585  387 ILE B O   
8209 C CB  . ILE B 387 ? 0.5429 0.9542 0.5148 0.1215  0.0205  0.0739  387 ILE B CB  
8210 C CG1 . ILE B 387 ? 0.5345 0.9681 0.5097 0.1054  0.0183  0.0674  387 ILE B CG1 
8211 C CG2 . ILE B 387 ? 0.5157 0.9337 0.4836 0.1403  0.0232  0.0835  387 ILE B CG2 
8212 C CD1 . ILE B 387 ? 0.5643 0.9951 0.5396 0.1056  0.0184  0.0703  387 ILE B CD1 
8213 N N   . PRO B 388 ? 0.5152 0.8643 0.4896 0.0952  0.0178  0.0599  388 PRO B N   
8214 C CA  . PRO B 388 ? 0.5120 0.8533 0.4879 0.0785  0.0160  0.0516  388 PRO B CA  
8215 C C   . PRO B 388 ? 0.5156 0.8922 0.4921 0.0696  0.0153  0.0463  388 PRO B C   
8216 O O   . PRO B 388 ? 0.5520 0.9526 0.5280 0.0772  0.0160  0.0480  388 PRO B O   
8217 C CB  . PRO B 388 ? 0.5078 0.8247 0.4822 0.0824  0.0163  0.0514  388 PRO B CB  
8218 C CG  . PRO B 388 ? 0.5291 0.8572 0.5008 0.1000  0.0184  0.0580  388 PRO B CG  
8219 C CD  . PRO B 388 ? 0.5253 0.8657 0.4964 0.1094  0.0196  0.0644  388 PRO B CD  
8220 N N   . TYR B 389 ? 0.4976 0.8774 0.4742 0.0536  0.0143  0.0400  389 TYR B N   
8221 C CA  . TYR B 389 ? 0.4918 0.9023 0.4676 0.0419  0.0141  0.0339  389 TYR B CA  
8222 C C   . TYR B 389 ? 0.4855 0.8789 0.4586 0.0232  0.0137  0.0259  389 TYR B C   
8223 O O   . TYR B 389 ? 0.5112 0.8846 0.4835 0.0188  0.0134  0.0254  389 TYR B O   
8224 C CB  . TYR B 389 ? 0.4847 0.9305 0.4612 0.0440  0.0140  0.0359  389 TYR B CB  
8225 C CG  . TYR B 389 ? 0.4680 0.9483 0.4433 0.0304  0.0139  0.0292  389 TYR B CG  
8226 C CD1 . TYR B 389 ? 0.4740 0.9827 0.4500 0.0328  0.0142  0.0285  389 TYR B CD1 
8227 C CD2 . TYR B 389 ? 0.4763 0.9611 0.4490 0.0148  0.0136  0.0234  389 TYR B CD2 
8228 C CE1 . TYR B 389 ? 0.4777 1.0197 0.4524 0.0188  0.0143  0.0220  389 TYR B CE1 
8229 C CE2 . TYR B 389 ? 0.4889 1.0046 0.4592 0.0007  0.0139  0.0167  389 TYR B CE2 
8230 C CZ  . TYR B 389 ? 0.4899 1.0347 0.4615 0.0022  0.0141  0.0160  389 TYR B CZ  
8231 O OH  . TYR B 389 ? 0.4885 1.0649 0.4576 -0.0132 0.0145  0.0090  389 TYR B OH  
8232 N N   . CYS B 390 ? 0.4943 0.8947 0.4651 0.0129  0.0140  0.0199  390 CYS B N   
8233 C CA  . CYS B 390 ? 0.5288 0.9125 0.4948 -0.0048 0.0145  0.0121  390 CYS B CA  
8234 C C   . CYS B 390 ? 0.4998 0.8423 0.4646 -0.0055 0.0142  0.0123  390 CYS B C   
8235 O O   . CYS B 390 ? 0.4678 0.7986 0.4290 -0.0153 0.0146  0.0089  390 CYS B O   
8236 C CB  . CYS B 390 ? 0.5726 0.9782 0.5351 -0.0179 0.0151  0.0073  390 CYS B CB  
8237 S SG  . CYS B 390 ? 0.6679 1.1235 0.6304 -0.0230 0.0156  0.0043  390 CYS B SG  
8238 N N   . GLY B 391 ? 0.4978 0.8194 0.4654 0.0050  0.0136  0.0163  391 GLY B N   
8239 C CA  . GLY B 391 ? 0.4847 0.7692 0.4517 0.0047  0.0131  0.0166  391 GLY B CA  
8240 C C   . GLY B 391 ? 0.4958 0.7708 0.4649 0.0091  0.0127  0.0206  391 GLY B C   
8241 O O   . GLY B 391 ? 0.5151 0.7638 0.4834 0.0064  0.0125  0.0201  391 GLY B O   
8242 N N   . LYS B 392 ? 0.4900 0.7876 0.4615 0.0161  0.0128  0.0248  392 LYS B N   
8243 C CA  . LYS B 392 ? 0.4729 0.7640 0.4463 0.0212  0.0127  0.0293  392 LYS B CA  
8244 C C   . LYS B 392 ? 0.4727 0.7697 0.4492 0.0377  0.0130  0.0373  392 LYS B C   
8245 O O   . LYS B 392 ? 0.4617 0.7759 0.4384 0.0449  0.0134  0.0391  392 LYS B O   
8246 C CB  . LYS B 392 ? 0.4737 0.7860 0.4450 0.0131  0.0130  0.0266  392 LYS B CB  
8247 C CG  . LYS B 392 ? 0.5086 0.8027 0.4756 0.0006  0.0134  0.0215  392 LYS B CG  
8248 C CD  . LYS B 392 ? 0.5276 0.8127 0.4890 -0.0123 0.0141  0.0140  392 LYS B CD  
8249 C CE  . LYS B 392 ? 0.5606 0.8225 0.5166 -0.0215 0.0150  0.0103  392 LYS B CE  
8250 N NZ  . LYS B 392 ? 0.5866 0.8278 0.5364 -0.0306 0.0160  0.0047  392 LYS B NZ  
8251 N N   . ILE B 393 ? 0.4533 0.7348 0.4312 0.0441  0.0133  0.0423  393 ILE B N   
8252 C CA  . ILE B 393 ? 0.4527 0.7402 0.4315 0.0592  0.0144  0.0502  393 ILE B CA  
8253 C C   . ILE B 393 ? 0.4481 0.7515 0.4273 0.0603  0.0148  0.0529  393 ILE B C   
8254 O O   . ILE B 393 ? 0.4445 0.7345 0.4241 0.0545  0.0145  0.0521  393 ILE B O   
8255 C CB  . ILE B 393 ? 0.4589 0.7147 0.4380 0.0669  0.0151  0.0548  393 ILE B CB  
8256 C CG1 . ILE B 393 ? 0.4663 0.7075 0.4446 0.0666  0.0147  0.0522  393 ILE B CG1 
8257 C CG2 . ILE B 393 ? 0.4547 0.7145 0.4324 0.0823  0.0171  0.0632  393 ILE B CG2 
8258 C CD1 . ILE B 393 ? 0.4560 0.6633 0.4343 0.0680  0.0148  0.0537  393 ILE B CD1 
8259 N N   . PHE B 394 ? 0.4506 0.7838 0.4293 0.0683  0.0154  0.0562  394 PHE B N   
8260 C CA  . PHE B 394 ? 0.4385 0.7906 0.4171 0.0710  0.0158  0.0593  394 PHE B CA  
8261 C C   . PHE B 394 ? 0.4435 0.7897 0.4211 0.0881  0.0178  0.0688  394 PHE B C   
8262 O O   . PHE B 394 ? 0.4530 0.8069 0.4287 0.1005  0.0191  0.0732  394 PHE B O   
8263 C CB  . PHE B 394 ? 0.4184 0.8115 0.3965 0.0683  0.0152  0.0566  394 PHE B CB  
8264 C CG  . PHE B 394 ? 0.4038 0.8039 0.3809 0.0500  0.0140  0.0471  394 PHE B CG  
8265 C CD1 . PHE B 394 ? 0.4074 0.8010 0.3840 0.0437  0.0137  0.0422  394 PHE B CD1 
8266 C CD2 . PHE B 394 ? 0.3938 0.8056 0.3693 0.0390  0.0136  0.0429  394 PHE B CD2 
8267 C CE1 . PHE B 394 ? 0.3982 0.7958 0.3722 0.0266  0.0133  0.0336  394 PHE B CE1 
8268 C CE2 . PHE B 394 ? 0.3831 0.7980 0.3553 0.0216  0.0133  0.0340  394 PHE B CE2 
8269 C CZ  . PHE B 394 ? 0.3838 0.7912 0.3551 0.0154  0.0133  0.0294  394 PHE B CZ  
8270 N N   . ASN B 395 ? 0.4336 0.7651 0.4114 0.0891  0.0184  0.0721  395 ASN B N   
8271 C CA  . ASN B 395 ? 0.4519 0.7788 0.4274 0.1045  0.0209  0.0812  395 ASN B CA  
8272 C C   . ASN B 395 ? 0.4464 0.8066 0.4207 0.1102  0.0213  0.0844  395 ASN B C   
8273 O O   . ASN B 395 ? 0.4320 0.8012 0.4076 0.1019  0.0203  0.0818  395 ASN B O   
8274 C CB  . ASN B 395 ? 0.4488 0.7428 0.4247 0.1031  0.0219  0.0837  395 ASN B CB  
8275 C CG  . ASN B 395 ? 0.4760 0.7602 0.4478 0.1184  0.0253  0.0932  395 ASN B CG  
8276 O OD1 . ASN B 395 ? 0.5058 0.8111 0.4751 0.1278  0.0266  0.0982  395 ASN B OD1 
8277 N ND2 . ASN B 395 ? 0.4611 0.7127 0.4312 0.1207  0.0269  0.0957  395 ASN B ND2 
8278 N N   . LEU B 396 ? 0.4526 0.8317 0.4239 0.1248  0.0230  0.0900  396 LEU B N   
8279 C CA  . LEU B 396 ? 0.4660 0.8825 0.4362 0.1307  0.0230  0.0926  396 LEU B CA  
8280 C C   . LEU B 396 ? 0.4829 0.8945 0.4512 0.1368  0.0247  0.0988  396 LEU B C   
8281 O O   . LEU B 396 ? 0.4905 0.9293 0.4592 0.1354  0.0238  0.0985  396 LEU B O   
8282 C CB  . LEU B 396 ? 0.4814 0.9212 0.4484 0.1460  0.0245  0.0974  396 LEU B CB  
8283 C CG  . LEU B 396 ? 0.4802 0.9314 0.4492 0.1398  0.0229  0.0912  396 LEU B CG  
8284 C CD1 . LEU B 396 ? 0.4811 0.9538 0.4464 0.1572  0.0249  0.0969  396 LEU B CD1 
8285 C CD2 . LEU B 396 ? 0.4591 0.9368 0.4322 0.1219  0.0198  0.0820  396 LEU B CD2 
8286 N N   . THR B 397 ? 0.4907 0.8674 0.4569 0.1423  0.0270  0.1038  397 THR B N   
8287 C CA  . THR B 397 ? 0.4956 0.8640 0.4594 0.1485  0.0292  0.1102  397 THR B CA  
8288 C C   . THR B 397 ? 0.4914 0.8489 0.4595 0.1333  0.0273  0.1052  397 THR B C   
8289 O O   . THR B 397 ? 0.4920 0.8673 0.4604 0.1315  0.0268  0.1055  397 THR B O   
8290 C CB  . THR B 397 ? 0.5146 0.8504 0.4725 0.1612  0.0333  0.1182  397 THR B CB  
8291 O OG1 . THR B 397 ? 0.5346 0.8807 0.4867 0.1769  0.0356  0.1232  397 THR B OG1 
8292 C CG2 . THR B 397 ? 0.5094 0.8363 0.4640 0.1673  0.0361  0.1251  397 THR B CG2 
8293 N N   . THR B 398 ? 0.4987 0.8283 0.4698 0.1229  0.0263  0.1005  398 THR B N   
8294 C CA  . THR B 398 ? 0.4803 0.7961 0.4546 0.1100  0.0250  0.0963  398 THR B CA  
8295 C C   . THR B 398 ? 0.4660 0.7997 0.4428 0.0953  0.0219  0.0871  398 THR B C   
8296 O O   . THR B 398 ? 0.4563 0.7848 0.4341 0.0856  0.0212  0.0837  398 THR B O   
8297 C CB  . THR B 398 ? 0.4832 0.7623 0.4592 0.1055  0.0253  0.0954  398 THR B CB  
8298 O OG1 . THR B 398 ? 0.4781 0.7534 0.4556 0.0989  0.0234  0.0892  398 THR B OG1 
8299 C CG2 . THR B 398 ? 0.4676 0.7261 0.4395 0.1184  0.0289  0.1038  398 THR B CG2 
8300 N N   . ARG B 399 ? 0.4459 0.7993 0.4225 0.0935  0.0206  0.0831  399 ARG B N   
8301 C CA  . ARG B 399 ? 0.4394 0.8098 0.4166 0.0787  0.0183  0.0740  399 ARG B CA  
8302 C C   . ARG B 399 ? 0.4612 0.8054 0.4395 0.0656  0.0172  0.0673  399 ARG B C   
8303 O O   . ARG B 399 ? 0.4806 0.8322 0.4576 0.0524  0.0161  0.0596  399 ARG B O   
8304 C CB  . ARG B 399 ? 0.4379 0.8303 0.4137 0.0741  0.0179  0.0727  399 ARG B CB  
8305 C CG  . ARG B 399 ? 0.4494 0.8747 0.4238 0.0859  0.0186  0.0782  399 ARG B CG  
8306 C CD  . ARG B 399 ? 0.4679 0.8854 0.4411 0.0976  0.0206  0.0868  399 ARG B CD  
8307 N NE  . ARG B 399 ? 0.4686 0.9141 0.4394 0.1124  0.0218  0.0936  399 ARG B NE  
8308 C CZ  . ARG B 399 ? 0.4723 0.9533 0.4420 0.1117  0.0208  0.0925  399 ARG B CZ  
8309 N NH1 . ARG B 399 ? 0.4608 0.9515 0.4308 0.0961  0.0190  0.0847  399 ARG B NH1 
8310 N NH2 . ARG B 399 ? 0.5137 1.0204 0.4808 0.1268  0.0220  0.0993  399 ARG B NH2 
8311 N N   . GLN B 400 ? 0.4560 0.7695 0.4358 0.0691  0.0180  0.0702  400 GLN B N   
8312 C CA  . GLN B 400 ? 0.4490 0.7373 0.4298 0.0588  0.0170  0.0647  400 GLN B CA  
8313 C C   . GLN B 400 ? 0.4376 0.7287 0.4180 0.0542  0.0159  0.0595  400 GLN B C   
8314 O O   . GLN B 400 ? 0.4697 0.7706 0.4500 0.0626  0.0163  0.0623  400 GLN B O   
8315 C CB  . GLN B 400 ? 0.4504 0.7085 0.4331 0.0641  0.0180  0.0695  400 GLN B CB  
8316 C CG  . GLN B 400 ? 0.4452 0.6980 0.4283 0.0676  0.0194  0.0746  400 GLN B CG  
8317 C CD  . GLN B 400 ? 0.4601 0.7205 0.4425 0.0578  0.0187  0.0701  400 GLN B CD  
8318 O OE1 . GLN B 400 ? 0.4675 0.7500 0.4483 0.0591  0.0190  0.0710  400 GLN B OE1 
8319 N NE2 . GLN B 400 ? 0.4178 0.6603 0.4007 0.0483  0.0179  0.0652  400 GLN B NE2 
8320 N N   . VAL B 401 ? 0.4119 0.6940 0.3911 0.0414  0.0150  0.0522  401 VAL B N   
8321 C CA  . VAL B 401 ? 0.3964 0.6777 0.3745 0.0356  0.0142  0.0469  401 VAL B CA  
8322 C C   . VAL B 401 ? 0.4167 0.6664 0.3951 0.0309  0.0138  0.0444  401 VAL B C   
8323 O O   . VAL B 401 ? 0.3985 0.6339 0.3758 0.0243  0.0138  0.0421  401 VAL B O   
8324 C CB  . VAL B 401 ? 0.3934 0.6967 0.3676 0.0237  0.0139  0.0397  401 VAL B CB  
8325 C CG1 . VAL B 401 ? 0.3802 0.6827 0.3529 0.0176  0.0135  0.0344  401 VAL B CG1 
8326 C CG2 . VAL B 401 ? 0.4020 0.7399 0.3763 0.0285  0.0140  0.0421  401 VAL B CG2 
8327 N N   . ARG B 402 ? 0.4188 0.6590 0.3984 0.0353  0.0135  0.0452  402 ARG B N   
8328 C CA  . ARG B 402 ? 0.4210 0.6341 0.4011 0.0322  0.0129  0.0432  402 ARG B CA  
8329 C C   . ARG B 402 ? 0.4274 0.6438 0.4052 0.0265  0.0123  0.0376  402 ARG B C   
8330 O O   . ARG B 402 ? 0.4247 0.6631 0.4017 0.0279  0.0125  0.0370  402 ARG B O   
8331 C CB  . ARG B 402 ? 0.4267 0.6236 0.4094 0.0429  0.0133  0.0493  402 ARG B CB  
8332 C CG  . ARG B 402 ? 0.4444 0.6366 0.4287 0.0491  0.0144  0.0555  402 ARG B CG  
8333 C CD  . ARG B 402 ? 0.4540 0.6271 0.4399 0.0430  0.0140  0.0543  402 ARG B CD  
8334 N NE  . ARG B 402 ? 0.4477 0.5985 0.4345 0.0405  0.0131  0.0523  402 ARG B NE  
8335 C CZ  . ARG B 402 ? 0.4633 0.5968 0.4517 0.0454  0.0136  0.0563  402 ARG B CZ  
8336 N NH1 . ARG B 402 ? 0.4939 0.6276 0.4825 0.0531  0.0154  0.0626  402 ARG B NH1 
8337 N NH2 . ARG B 402 ? 0.4234 0.5391 0.4125 0.0422  0.0125  0.0538  402 ARG B NH2 
8338 N N   . THR B 403 ? 0.4491 0.6446 0.4256 0.0204  0.0118  0.0338  403 THR B N   
8339 C CA  . THR B 403 ? 0.4501 0.6450 0.4240 0.0154  0.0115  0.0289  403 THR B CA  
8340 C C   . THR B 403 ? 0.4570 0.6475 0.4334 0.0250  0.0111  0.0324  403 THR B C   
8341 O O   . THR B 403 ? 0.4692 0.6444 0.4480 0.0322  0.0110  0.0369  403 THR B O   
8342 C CB  . THR B 403 ? 0.4765 0.6489 0.4471 0.0071  0.0113  0.0243  403 THR B CB  
8343 O OG1 . THR B 403 ? 0.4906 0.6611 0.4584 0.0009  0.0121  0.0225  403 THR B OG1 
8344 C CG2 . THR B 403 ? 0.4716 0.6453 0.4376 -0.0002 0.0116  0.0185  403 THR B CG2 
8345 N N   . LEU B 404 ? 0.4737 0.6777 0.4487 0.0247  0.0112  0.0302  404 LEU B N   
8346 C CA  . LEU B 404 ? 0.4681 0.6684 0.4441 0.0339  0.0112  0.0330  404 LEU B CA  
8347 C C   . LEU B 404 ? 0.4899 0.6683 0.4645 0.0295  0.0104  0.0293  404 LEU B C   
8348 O O   . LEU B 404 ? 0.4489 0.6278 0.4205 0.0198  0.0104  0.0236  404 LEU B O   
8349 C CB  . LEU B 404 ? 0.4594 0.6878 0.4346 0.0370  0.0119  0.0329  404 LEU B CB  
8350 C CG  . LEU B 404 ? 0.4804 0.7084 0.4552 0.0468  0.0124  0.0353  404 LEU B CG  
8351 C CD1 . LEU B 404 ? 0.4691 0.6837 0.4443 0.0603  0.0132  0.0423  404 LEU B CD1 
8352 C CD2 . LEU B 404 ? 0.4641 0.7247 0.4382 0.0486  0.0131  0.0346  404 LEU B CD2 
8353 N N   . TYR B 405 ? 0.5236 0.6823 0.4994 0.0363  0.0101  0.0324  405 TYR B N   
8354 C CA  . TYR B 405 ? 0.5976 0.7375 0.5720 0.0330  0.0092  0.0291  405 TYR B CA  
8355 C C   . TYR B 405 ? 0.6582 0.7974 0.6314 0.0404  0.0095  0.0302  405 TYR B C   
8356 O O   . TYR B 405 ? 0.6781 0.8084 0.6515 0.0497  0.0101  0.0348  405 TYR B O   
8357 C CB  . TYR B 405 ? 0.5546 0.6706 0.5305 0.0312  0.0082  0.0296  405 TYR B CB  
8358 C CG  . TYR B 405 ? 0.5189 0.6336 0.4942 0.0225  0.0080  0.0268  405 TYR B CG  
8359 C CD1 . TYR B 405 ? 0.5131 0.6221 0.4844 0.0138  0.0079  0.0213  405 TYR B CD1 
8360 C CD2 . TYR B 405 ? 0.4927 0.6113 0.4701 0.0234  0.0085  0.0298  405 TYR B CD2 
8361 C CE1 . TYR B 405 ? 0.4579 0.5636 0.4266 0.0068  0.0084  0.0188  405 TYR B CE1 
8362 C CE2 . TYR B 405 ? 0.4736 0.5900 0.4493 0.0160  0.0087  0.0272  405 TYR B CE2 
8363 C CZ  . TYR B 405 ? 0.4628 0.5722 0.4338 0.0080  0.0087  0.0217  405 TYR B CZ  
8364 O OH  . TYR B 405 ? 0.4569 0.5621 0.4242 0.0015  0.0095  0.0192  405 TYR B OH  
8365 N N   . LYS B 406 ? 0.7470 0.8967 0.7180 0.0362  0.0096  0.0261  406 LYS B N   
8366 C CA  . LYS B 406 ? 0.8189 0.9632 0.7880 0.0401  0.0096  0.0252  406 LYS B CA  
8367 C C   . LYS B 406 ? 0.8532 0.9879 0.8219 0.0529  0.0104  0.0306  406 LYS B C   
8368 O O   . LYS B 406 ? 0.9533 1.1045 0.9216 0.0615  0.0119  0.0345  406 LYS B O   
8369 C CB  . LYS B 406 ? 0.8627 0.9889 0.8298 0.0316  0.0085  0.0201  406 LYS B CB  
8370 C CG  . LYS B 406 ? 0.8185 0.9333 0.7860 0.0238  0.0077  0.0184  406 LYS B CG  
8371 C CD  . LYS B 406 ? 0.7897 0.9149 0.7539 0.0131  0.0086  0.0138  406 LYS B CD  
8372 C CE  . LYS B 406 ? 0.8128 0.9211 0.7756 0.0072  0.0081  0.0121  406 LYS B CE  
8373 N NZ  . LYS B 406 ? 0.7910 0.8907 0.7475 -0.0017 0.0089  0.0067  406 LYS B NZ  
8374 N N   . LEU B 407 ? 0.8603 0.9696 0.8280 0.0547  0.0098  0.0310  407 LEU B N   
8375 C CA  . LEU B 407 ? 0.8706 0.9622 0.8370 0.0492  0.0083  0.0267  407 LEU B CA  
8376 C C   . LEU B 407 ? 0.8688 0.9473 0.8319 0.0586  0.0092  0.0290  407 LEU B C   
8377 O O   . LEU B 407 ? 0.8673 0.9293 0.8298 0.0624  0.0096  0.0320  407 LEU B O   
8378 C CB  . LEU B 407 ? 0.9207 0.9938 0.8891 0.0434  0.0068  0.0258  407 LEU B CB  
8379 C CG  . LEU B 407 ? 0.8952 0.9675 0.8643 0.0330  0.0057  0.0218  407 LEU B CG  
8380 C CD1 . LEU B 407 ? 0.8922 0.9515 0.8640 0.0312  0.0048  0.0233  407 LEU B CD1 
8381 C CD2 . LEU B 407 ? 0.9046 0.9687 0.8705 0.0280  0.0048  0.0169  407 LEU B CD2 
8382 N N   . PRO B 408 ? 0.8457 0.9309 0.8058 0.0618  0.0098  0.0275  408 PRO B N   
8383 C CA  . PRO B 408 ? 0.8186 0.8936 0.7740 0.0725  0.0114  0.0303  408 PRO B CA  
8384 C C   . PRO B 408 ? 0.8223 0.8682 0.7754 0.0714  0.0106  0.0295  408 PRO B C   
8385 O O   . PRO B 408 ? 0.7765 0.8128 0.7321 0.0624  0.0083  0.0259  408 PRO B O   
8386 C CB  . PRO B 408 ? 0.7814 0.8693 0.7346 0.0733  0.0118  0.0275  408 PRO B CB  
8387 C CG  . PRO B 408 ? 0.7796 0.8721 0.7355 0.0607  0.0099  0.0221  408 PRO B CG  
8388 C CD  . PRO B 408 ? 0.7970 0.8955 0.7568 0.0550  0.0093  0.0228  408 PRO B CD  
8389 N N   . PRO B 409 ? 0.8616 0.8938 0.8090 0.0808  0.0127  0.0327  409 PRO B N   
8390 C CA  . PRO B 409 ? 0.8400 0.8446 0.7839 0.0795  0.0124  0.0318  409 PRO B CA  
8391 C C   . PRO B 409 ? 0.7966 0.7924 0.7407 0.0720  0.0097  0.0260  409 PRO B C   
8392 O O   . PRO B 409 ? 0.7507 0.7551 0.6933 0.0729  0.0096  0.0236  409 PRO B O   
8393 C CB  . PRO B 409 ? 0.8735 0.8687 0.8085 0.0918  0.0160  0.0355  409 PRO B CB  
8394 C CG  . PRO B 409 ? 0.8813 0.9012 0.8158 0.0997  0.0176  0.0375  409 PRO B CG  
8395 C CD  . PRO B 409 ? 0.8788 0.9212 0.8215 0.0935  0.0159  0.0373  409 PRO B CD  
8396 N N   . ASN B 410 ? 0.7817 0.7615 0.7275 0.0649  0.0077  0.0240  410 ASN B N   
8397 C CA  . ASN B 410 ? 0.7505 0.7218 0.6964 0.0581  0.0051  0.0188  410 ASN B CA  
8398 C C   . ASN B 410 ? 0.7075 0.6942 0.6565 0.0528  0.0036  0.0155  410 ASN B C   
8399 O O   . ASN B 410 ? 0.7253 0.7083 0.6721 0.0503  0.0024  0.0117  410 ASN B O   
8400 C CB  . ASN B 410 ? 0.7984 0.7553 0.7369 0.0629  0.0060  0.0175  410 ASN B CB  
8401 C CG  . ASN B 410 ? 0.8784 0.8140 0.8120 0.0648  0.0074  0.0193  410 ASN B CG  
8402 O OD1 . ASN B 410 ? 0.8794 0.8062 0.8159 0.0581  0.0059  0.0187  410 ASN B OD1 
8403 N ND2 . ASN B 410 ? 0.8850 0.8122 0.8103 0.0739  0.0107  0.0217  410 ASN B ND2 
8404 N N   . TYR B 411 ? 0.6557 0.6586 0.6087 0.0507  0.0039  0.0168  411 TYR B N   
8405 C CA  . TYR B 411 ? 0.5940 0.6088 0.5485 0.0438  0.0031  0.0133  411 TYR B CA  
8406 C C   . TYR B 411 ? 0.5375 0.5407 0.4932 0.0362  0.0008  0.0103  411 TYR B C   
8407 O O   . TYR B 411 ? 0.5287 0.5238 0.4870 0.0348  0.0000  0.0118  411 TYR B O   
8408 C CB  . TYR B 411 ? 0.5748 0.6089 0.5321 0.0428  0.0042  0.0151  411 TYR B CB  
8409 C CG  . TYR B 411 ? 0.5488 0.5952 0.5057 0.0351  0.0042  0.0114  411 TYR B CG  
8410 C CD1 . TYR B 411 ? 0.5566 0.6169 0.5110 0.0354  0.0055  0.0097  411 TYR B CD1 
8411 C CD2 . TYR B 411 ? 0.5161 0.5601 0.4741 0.0274  0.0035  0.0097  411 TYR B CD2 
8412 C CE1 . TYR B 411 ? 0.5353 0.6059 0.4881 0.0270  0.0061  0.0061  411 TYR B CE1 
8413 C CE2 . TYR B 411 ? 0.4994 0.5516 0.4547 0.0199  0.0043  0.0061  411 TYR B CE2 
8414 C CZ  . TYR B 411 ? 0.4917 0.5568 0.4443 0.0191  0.0056  0.0042  411 TYR B CZ  
8415 O OH  . TYR B 411 ? 0.4872 0.5592 0.4358 0.0103  0.0070  0.0005  411 TYR B OH  
8416 N N   . GLU B 412 ? 0.4966 0.4992 0.4497 0.0318  0.0001  0.0063  412 GLU B N   
8417 C CA  . GLU B 412 ? 0.4795 0.4728 0.4324 0.0257  -0.0015 0.0038  412 GLU B CA  
8418 C C   . GLU B 412 ? 0.4670 0.4696 0.4205 0.0202  -0.0006 0.0033  412 GLU B C   
8419 O O   . GLU B 412 ? 0.4827 0.4948 0.4331 0.0170  0.0008  0.0013  412 GLU B O   
8420 C CB  . GLU B 412 ? 0.4914 0.4770 0.4397 0.0243  -0.0023 0.0001  412 GLU B CB  
8421 C CG  . GLU B 412 ? 0.5273 0.4989 0.4749 0.0275  -0.0040 -0.0001 412 GLU B CG  
8422 C CD  . GLU B 412 ? 0.5605 0.5254 0.5032 0.0267  -0.0048 -0.0038 412 GLU B CD  
8423 O OE1 . GLU B 412 ? 0.5524 0.5128 0.4935 0.0226  -0.0060 -0.0060 412 GLU B OE1 
8424 O OE2 . GLU B 412 ? 0.5972 0.5609 0.5370 0.0309  -0.0042 -0.0042 412 GLU B OE2 
8425 N N   . ILE B 413 ? 0.4503 0.4497 0.4071 0.0188  -0.0013 0.0050  413 ILE B N   
8426 C CA  . ILE B 413 ? 0.4571 0.4652 0.4143 0.0148  -0.0001 0.0053  413 ILE B CA  
8427 C C   . ILE B 413 ? 0.4544 0.4599 0.4057 0.0087  0.0006  0.0015  413 ILE B C   
8428 O O   . ILE B 413 ? 0.4410 0.4547 0.3895 0.0043  0.0025  0.0004  413 ILE B O   
8429 C CB  . ILE B 413 ? 0.4458 0.4513 0.4080 0.0156  -0.0009 0.0085  413 ILE B CB  
8430 C CG1 . ILE B 413 ? 0.4749 0.4911 0.4375 0.0126  0.0006  0.0093  413 ILE B CG1 
8431 C CG2 . ILE B 413 ? 0.4587 0.4514 0.4212 0.0141  -0.0027 0.0075  413 ILE B CG2 
8432 C CD1 . ILE B 413 ? 0.4690 0.5008 0.4328 0.0151  0.0021  0.0112  413 ILE B CD1 
8433 N N   . ARG B 414 ? 0.4628 0.4564 0.4107 0.0084  -0.0004 -0.0007 414 ARG B N   
8434 C CA  . ARG B 414 ? 0.4531 0.4414 0.3933 0.0036  0.0008  -0.0040 414 ARG B CA  
8435 C C   . ARG B 414 ? 0.4563 0.4541 0.3918 -0.0002 0.0034  -0.0062 414 ARG B C   
8436 O O   . ARG B 414 ? 0.4797 0.4752 0.4079 -0.0059 0.0057  -0.0087 414 ARG B O   
8437 C CB  . ARG B 414 ? 0.4490 0.4244 0.3863 0.0053  -0.0007 -0.0057 414 ARG B CB  
8438 C CG  . ARG B 414 ? 0.4380 0.4133 0.3744 0.0076  -0.0013 -0.0069 414 ARG B CG  
8439 C CD  . ARG B 414 ? 0.4356 0.3986 0.3696 0.0095  -0.0033 -0.0085 414 ARG B CD  
8440 N NE  . ARG B 414 ? 0.4154 0.3777 0.3500 0.0129  -0.0043 -0.0091 414 ARG B NE  
8441 C CZ  . ARG B 414 ? 0.4111 0.3764 0.3413 0.0126  -0.0028 -0.0109 414 ARG B CZ  
8442 N NH1 . ARG B 414 ? 0.4149 0.3841 0.3396 0.0080  -0.0002 -0.0126 414 ARG B NH1 
8443 N NH2 . ARG B 414 ? 0.3940 0.3583 0.3247 0.0167  -0.0036 -0.0111 414 ARG B NH2 
8444 N N   . HIS B 415 ? 0.4926 0.5012 0.4313 0.0027  0.0034  -0.0053 415 HIS B N   
8445 C CA  . HIS B 415 ? 0.4934 0.5157 0.4287 -0.0010 0.0058  -0.0073 415 HIS B CA  
8446 C C   . HIS B 415 ? 0.4886 0.5231 0.4229 -0.0067 0.0079  -0.0075 415 HIS B C   
8447 O O   . HIS B 415 ? 0.5388 0.5816 0.4678 -0.0132 0.0104  -0.0104 415 HIS B O   
8448 C CB  . HIS B 415 ? 0.4988 0.5321 0.4380 0.0050  0.0055  -0.0056 415 HIS B CB  
8449 C CG  . HIS B 415 ? 0.5453 0.5684 0.4827 0.0090  0.0043  -0.0065 415 HIS B CG  
8450 N ND1 . HIS B 415 ? 0.5483 0.5636 0.4794 0.0051  0.0050  -0.0099 415 HIS B ND1 
8451 C CD2 . HIS B 415 ? 0.5105 0.5295 0.4507 0.0168  0.0029  -0.0046 415 HIS B CD2 
8452 C CE1 . HIS B 415 ? 0.5643 0.5720 0.4952 0.0102  0.0036  -0.0101 415 HIS B CE1 
8453 N NE2 . HIS B 415 ? 0.5376 0.5471 0.4737 0.0171  0.0024  -0.0070 415 HIS B NE2 
8454 N N   . LYS B 416 ? 0.4893 0.5256 0.4285 -0.0048 0.0071  -0.0048 416 LYS B N   
8455 C CA  . LYS B 416 ? 0.4932 0.5404 0.4311 -0.0103 0.0089  -0.0052 416 LYS B CA  
8456 C C   . LYS B 416 ? 0.4811 0.5185 0.4093 -0.0188 0.0114  -0.0089 416 LYS B C   
8457 O O   . LYS B 416 ? 0.5105 0.5570 0.4347 -0.0256 0.0137  -0.0107 416 LYS B O   
8458 C CB  . LYS B 416 ? 0.5348 0.5835 0.4792 -0.0061 0.0076  -0.0013 416 LYS B CB  
8459 C CG  . LYS B 416 ? 0.5853 0.6504 0.5363 0.0000  0.0071  0.0022  416 LYS B CG  
8460 C CD  . LYS B 416 ? 0.5634 0.6503 0.5126 -0.0038 0.0090  0.0007  416 LYS B CD  
8461 C CE  . LYS B 416 ? 0.6324 0.7351 0.5870 0.0047  0.0086  0.0045  416 LYS B CE  
8462 N NZ  . LYS B 416 ? 0.7201 0.8488 0.6742 0.0016  0.0102  0.0038  416 LYS B NZ  
8463 N N   . PHE B 417 ? 0.4456 0.4644 0.3692 -0.0184 0.0111  -0.0101 417 PHE B N   
8464 C CA  . PHE B 417 ? 0.4574 0.4630 0.3711 -0.0239 0.0136  -0.0124 417 PHE B CA  
8465 C C   . PHE B 417 ? 0.4797 0.4760 0.3823 -0.0292 0.0164  -0.0162 417 PHE B C   
8466 O O   . PHE B 417 ? 0.5322 0.5271 0.4356 -0.0267 0.0153  -0.0166 417 PHE B O   
8467 C CB  . PHE B 417 ? 0.4605 0.4523 0.3763 -0.0184 0.0117  -0.0100 417 PHE B CB  
8468 C CG  . PHE B 417 ? 0.4605 0.4604 0.3868 -0.0137 0.0094  -0.0062 417 PHE B CG  
8469 C CD1 . PHE B 417 ? 0.4744 0.4851 0.4018 -0.0166 0.0107  -0.0055 417 PHE B CD1 
8470 C CD2 . PHE B 417 ? 0.4486 0.4458 0.3831 -0.0069 0.0061  -0.0034 417 PHE B CD2 
8471 C CE1 . PHE B 417 ? 0.4596 0.4773 0.3960 -0.0120 0.0088  -0.0016 417 PHE B CE1 
8472 C CE2 . PHE B 417 ? 0.4286 0.4319 0.3716 -0.0032 0.0045  0.0002  417 PHE B CE2 
8473 C CZ  . PHE B 417 ? 0.4474 0.4609 0.3915 -0.0053 0.0059  0.0012  417 PHE B CZ  
8474 N N   . LYS B 418 ? 0.4890 0.4780 0.3800 -0.0367 0.0203  -0.0190 418 LYS B N   
8475 C CA  . LYS B 418 ? 0.4976 0.4737 0.3754 -0.0423 0.0238  -0.0224 418 LYS B CA  
8476 C C   . LYS B 418 ? 0.5167 0.4701 0.3841 -0.0406 0.0258  -0.0224 418 LYS B C   
8477 O O   . LYS B 418 ? 0.5337 0.4800 0.3916 -0.0457 0.0293  -0.0238 418 LYS B O   
8478 C CB  . LYS B 418 ? 0.5311 0.5166 0.4009 -0.0538 0.0280  -0.0262 418 LYS B CB  
8479 C CG  . LYS B 418 ? 0.5570 0.5294 0.4121 -0.0610 0.0324  -0.0300 418 LYS B CG  
8480 C CD  . LYS B 418 ? 0.5728 0.5563 0.4200 -0.0741 0.0368  -0.0342 418 LYS B CD  
8481 C CE  . LYS B 418 ? 0.5867 0.5529 0.4168 -0.0822 0.0421  -0.0380 418 LYS B CE  
8482 N NZ  . LYS B 418 ? 0.6152 0.5970 0.4402 -0.0952 0.0456  -0.0421 418 LYS B NZ  
8483 N N   . LEU B 419 ? 0.5019 0.4441 0.3702 -0.0333 0.0236  -0.0209 419 LEU B N   
8484 C CA  . LEU B 419 ? 0.4892 0.4122 0.3485 -0.0295 0.0250  -0.0202 419 LEU B CA  
8485 C C   . LEU B 419 ? 0.5012 0.4062 0.3427 -0.0335 0.0300  -0.0230 419 LEU B C   
8486 O O   . LEU B 419 ? 0.5141 0.4018 0.3437 -0.0315 0.0330  -0.0228 419 LEU B O   
8487 C CB  . LEU B 419 ? 0.5050 0.4265 0.3736 -0.0196 0.0202  -0.0172 419 LEU B CB  
8488 C CG  . LEU B 419 ? 0.5201 0.4555 0.4051 -0.0150 0.0156  -0.0141 419 LEU B CG  
8489 C CD1 . LEU B 419 ? 0.5006 0.4318 0.3915 -0.0071 0.0116  -0.0120 419 LEU B CD1 
8490 C CD2 . LEU B 419 ? 0.5130 0.4511 0.3987 -0.0162 0.0167  -0.0128 419 LEU B CD2 
8491 N N   . TRP B 420 ? 0.4958 0.4047 0.3351 -0.0383 0.0311  -0.0253 420 TRP B N   
8492 C CA  . TRP B 420 ? 0.5164 0.4082 0.3392 -0.0418 0.0357  -0.0278 420 TRP B CA  
8493 C C   . TRP B 420 ? 0.5147 0.4096 0.3281 -0.0544 0.0407  -0.0316 420 TRP B C   
8494 O O   . TRP B 420 ? 0.4912 0.4064 0.3138 -0.0589 0.0392  -0.0326 420 TRP B O   
8495 C CB  . TRP B 420 ? 0.5103 0.4035 0.3375 -0.0372 0.0329  -0.0274 420 TRP B CB  
8496 C CG  . TRP B 420 ? 0.4919 0.3868 0.3308 -0.0261 0.0272  -0.0241 420 TRP B CG  
8497 C CD1 . TRP B 420 ? 0.4602 0.3714 0.3163 -0.0218 0.0219  -0.0221 420 TRP B CD1 
8498 C CD2 . TRP B 420 ? 0.4954 0.3755 0.3291 -0.0180 0.0265  -0.0224 420 TRP B CD2 
8499 N NE1 . TRP B 420 ? 0.4641 0.3710 0.3257 -0.0133 0.0180  -0.0198 420 TRP B NE1 
8500 C CE2 . TRP B 420 ? 0.4931 0.3834 0.3425 -0.0105 0.0203  -0.0199 420 TRP B CE2 
8501 C CE3 . TRP B 420 ? 0.5597 0.4199 0.3770 -0.0161 0.0305  -0.0226 420 TRP B CE3 
8502 C CZ2 . TRP B 420 ? 0.5251 0.4086 0.3746 -0.0023 0.0178  -0.0180 420 TRP B CZ2 
8503 C CZ3 . TRP B 420 ? 0.5691 0.4226 0.3865 -0.0061 0.0280  -0.0202 420 TRP B CZ3 
8504 C CH2 . TRP B 420 ? 0.5505 0.4168 0.3842 0.0001  0.0216  -0.0181 420 TRP B CH2 
8505 N N   . ASN B 421 ? 0.5538 0.4285 0.3478 -0.0600 0.0470  -0.0338 421 ASN B N   
8506 C CA  . ASN B 421 ? 0.5894 0.4640 0.3712 -0.0739 0.0527  -0.0382 421 ASN B CA  
8507 C C   . ASN B 421 ? 0.6242 0.4762 0.3872 -0.0767 0.0582  -0.0400 421 ASN B C   
8508 O O   . ASN B 421 ? 0.6429 0.4700 0.3907 -0.0729 0.0619  -0.0392 421 ASN B O   
8509 C CB  . ASN B 421 ? 0.6076 0.4783 0.3812 -0.0808 0.0564  -0.0398 421 ASN B CB  
8510 C CG  . ASN B 421 ? 0.6569 0.5256 0.4152 -0.0972 0.0630  -0.0451 421 ASN B CG  
8511 O OD1 . ASN B 421 ? 0.6675 0.5419 0.4236 -0.1038 0.0646  -0.0474 421 ASN B OD1 
8512 N ND2 . ASN B 421 ? 0.6861 0.5463 0.4329 -0.1043 0.0674  -0.0473 421 ASN B ND2 
8513 N N   . PHE B 422 ? 0.6231 0.4841 0.3867 -0.0827 0.0589  -0.0421 422 PHE B N   
8514 C CA  . PHE B 422 ? 0.6203 0.4617 0.3675 -0.0848 0.0637  -0.0435 422 PHE B CA  
8515 C C   . PHE B 422 ? 0.6707 0.4891 0.3930 -0.0962 0.0727  -0.0469 422 PHE B C   
8516 O O   . PHE B 422 ? 0.6962 0.4905 0.4005 -0.0962 0.0779  -0.0473 422 PHE B O   
8517 C CB  . PHE B 422 ? 0.5962 0.4549 0.3508 -0.0886 0.0622  -0.0448 422 PHE B CB  
8518 C CG  . PHE B 422 ? 0.6001 0.4408 0.3421 -0.0870 0.0653  -0.0450 422 PHE B CG  
8519 C CD1 . PHE B 422 ? 0.5702 0.4032 0.3168 -0.0733 0.0613  -0.0416 422 PHE B CD1 
8520 C CD2 . PHE B 422 ? 0.6308 0.4622 0.3555 -0.0998 0.0726  -0.0488 422 PHE B CD2 
8521 C CE1 . PHE B 422 ? 0.5921 0.4087 0.3265 -0.0712 0.0642  -0.0417 422 PHE B CE1 
8522 C CE2 . PHE B 422 ? 0.6314 0.4451 0.3434 -0.0980 0.0759  -0.0487 422 PHE B CE2 
8523 C CZ  . PHE B 422 ? 0.6197 0.4260 0.3366 -0.0831 0.0716  -0.0450 422 PHE B CZ  
8524 N N   . ASN B 423 ? 0.6943 0.5193 0.4147 -0.1057 0.0748  -0.0494 423 ASN B N   
8525 C CA  . ASN B 423 ? 0.7244 0.5273 0.4203 -0.1179 0.0836  -0.0532 423 ASN B CA  
8526 C C   . ASN B 423 ? 0.7143 0.4933 0.3987 -0.1108 0.0861  -0.0513 423 ASN B C   
8527 O O   . ASN B 423 ? 0.7334 0.4889 0.3948 -0.1191 0.0940  -0.0542 423 ASN B O   
8528 C CB  . ASN B 423 ? 0.7679 0.5921 0.4662 -0.1339 0.0852  -0.0577 423 ASN B CB  
8529 C CG  . ASN B 423 ? 0.8210 0.6707 0.5293 -0.1412 0.0835  -0.0597 423 ASN B CG  
8530 O OD1 . ASN B 423 ? 0.8561 0.6960 0.5554 -0.1437 0.0866  -0.0606 423 ASN B OD1 
8531 N ND2 . ASN B 423 ? 0.8265 0.7095 0.5530 -0.1439 0.0788  -0.0601 423 ASN B ND2 
8532 N N   . ASN B 424 ? 0.6791 0.4641 0.3787 -0.0958 0.0796  -0.0466 424 ASN B N   
8533 C CA  . ASN B 424 ? 0.6490 0.4149 0.3399 -0.0873 0.0812  -0.0442 424 ASN B CA  
8534 C C   . ASN B 424 ? 0.6153 0.3812 0.3175 -0.0696 0.0754  -0.0388 424 ASN B C   
8535 O O   . ASN B 424 ? 0.5824 0.3633 0.3016 -0.0618 0.0694  -0.0360 424 ASN B O   
8536 C CB  . ASN B 424 ? 0.6331 0.4124 0.3312 -0.0917 0.0799  -0.0451 424 ASN B CB  
8537 C CG  . ASN B 424 ? 0.6475 0.4037 0.3308 -0.0860 0.0839  -0.0437 424 ASN B CG  
8538 O OD1 . ASN B 424 ? 0.6728 0.4003 0.3364 -0.0808 0.0893  -0.0428 424 ASN B OD1 
8539 N ND2 . ASN B 424 ? 0.6273 0.3957 0.3193 -0.0864 0.0817  -0.0434 424 ASN B ND2 
8540 N N   . GLN B 425 ? 0.6382 0.3878 0.3304 -0.0638 0.0773  -0.0377 425 GLN B N   
8541 C CA  . GLN B 425 ? 0.6185 0.3720 0.3224 -0.0486 0.0713  -0.0333 425 GLN B CA  
8542 C C   . GLN B 425 ? 0.6308 0.3686 0.3270 -0.0358 0.0721  -0.0295 425 GLN B C   
8543 O O   . GLN B 425 ? 0.6344 0.3475 0.3082 -0.0367 0.0796  -0.0301 425 GLN B O   
8544 C CB  . GLN B 425 ? 0.6201 0.3654 0.3169 -0.0476 0.0726  -0.0336 425 GLN B CB  
8545 C CG  . GLN B 425 ? 0.6341 0.3886 0.3305 -0.0619 0.0748  -0.0378 425 GLN B CG  
8546 C CD  . GLN B 425 ? 0.6613 0.4158 0.3578 -0.0599 0.0739  -0.0377 425 GLN B CD  
8547 O OE1 . GLN B 425 ? 0.6505 0.3951 0.3446 -0.0481 0.0724  -0.0347 425 GLN B OE1 
8548 N NE2 . GLN B 425 ? 0.6623 0.4291 0.3611 -0.0715 0.0751  -0.0410 425 GLN B NE2 
8549 N N   . ILE B 426 ? 0.5860 0.3381 0.3001 -0.0239 0.0648  -0.0258 426 ILE B N   
8550 C CA  . ILE B 426 ? 0.5909 0.3363 0.3031 -0.0112 0.0640  -0.0219 426 ILE B CA  
8551 C C   . ILE B 426 ? 0.6050 0.3484 0.3185 0.0010  0.0610  -0.0189 426 ILE B C   
8552 O O   . ILE B 426 ? 0.5726 0.3340 0.3038 0.0025  0.0545  -0.0186 426 ILE B O   
8553 C CB  . ILE B 426 ? 0.5674 0.3359 0.3017 -0.0091 0.0575  -0.0202 426 ILE B CB  
8554 C CG1 . ILE B 426 ? 0.5561 0.3299 0.2903 -0.0215 0.0599  -0.0234 426 ILE B CG1 
8555 C CG2 . ILE B 426 ? 0.5727 0.3373 0.3063 0.0039  0.0565  -0.0161 426 ILE B CG2 
8556 C CD1 . ILE B 426 ? 0.5519 0.3454 0.3045 -0.0196 0.0548  -0.0216 426 ILE B CD1 
8557 N N   . SER B 427 ? 0.6419 0.3630 0.3357 0.0099  0.0661  -0.0167 427 SER B N   
8558 C CA  . SER B 427 ? 0.6638 0.3826 0.3563 0.0214  0.0639  -0.0140 427 SER B CA  
8559 C C   . SER B 427 ? 0.6457 0.3883 0.3609 0.0308  0.0550  -0.0110 427 SER B C   
8560 O O   . SER B 427 ? 0.6468 0.4016 0.3738 0.0312  0.0521  -0.0100 427 SER B O   
8561 C CB  . SER B 427 ? 0.6806 0.3707 0.3457 0.0304  0.0716  -0.0118 427 SER B CB  
8562 O OG  . SER B 427 ? 0.7168 0.4036 0.3782 0.0392  0.0727  -0.0089 427 SER B OG  
8563 N N   . ASP B 428 ? 0.6310 0.3801 0.3519 0.0377  0.0508  -0.0098 428 ASP B N   
8564 C CA  . ASP B 428 ? 0.6487 0.4212 0.3913 0.0442  0.0422  -0.0078 428 ASP B CA  
8565 C C   . ASP B 428 ? 0.6693 0.4448 0.4120 0.0556  0.0413  -0.0040 428 ASP B C   
8566 O O   . ASP B 428 ? 0.7049 0.5011 0.4661 0.0594  0.0346  -0.0025 428 ASP B O   
8567 C CB  . ASP B 428 ? 0.6550 0.4332 0.4020 0.0482  0.0383  -0.0079 428 ASP B CB  
8568 C CG  . ASP B 428 ? 0.6756 0.4349 0.4014 0.0578  0.0430  -0.0060 428 ASP B CG  
8569 O OD1 . ASP B 428 ? 0.7364 0.4806 0.4460 0.0646  0.0483  -0.0036 428 ASP B OD1 
8570 O OD2 . ASP B 428 ? 0.6704 0.4301 0.3954 0.0596  0.0414  -0.0066 428 ASP B OD2 
8571 N N   . ASP B 429 ? 0.6829 0.4378 0.4044 0.0609  0.0485  -0.0023 429 ASP B N   
8572 C CA  . ASP B 429 ? 0.6906 0.4476 0.4098 0.0729  0.0486  0.0015  429 ASP B CA  
8573 C C   . ASP B 429 ? 0.6767 0.4317 0.3953 0.0691  0.0513  0.0015  429 ASP B C   
8574 O O   . ASP B 429 ? 0.6889 0.4423 0.4021 0.0788  0.0530  0.0048  429 ASP B O   
8575 C CB  . ASP B 429 ? 0.7647 0.5012 0.4599 0.0856  0.0545  0.0045  429 ASP B CB  
8576 C CG  . ASP B 429 ? 0.8307 0.5348 0.4983 0.0813  0.0649  0.0030  429 ASP B CG  
8577 O OD1 . ASP B 429 ? 0.8374 0.5356 0.5033 0.0702  0.0679  0.0003  429 ASP B OD1 
8578 O OD2 . ASP B 429 ? 0.9301 0.6140 0.5765 0.0890  0.0704  0.0046  429 ASP B OD2 
8579 N N   . ASN B 430 ? 0.6486 0.4049 0.3726 0.0553  0.0518  -0.0020 430 ASN B N   
8580 C CA  . ASN B 430 ? 0.6298 0.3889 0.3571 0.0505  0.0530  -0.0024 430 ASN B CA  
8581 C C   . ASN B 430 ? 0.5903 0.3754 0.3439 0.0429  0.0458  -0.0035 430 ASN B C   
8582 O O   . ASN B 430 ? 0.5845 0.3711 0.3407 0.0316  0.0468  -0.0064 430 ASN B O   
8583 C CB  . ASN B 430 ? 0.6760 0.4116 0.3823 0.0410  0.0615  -0.0056 430 ASN B CB  
8584 C CG  . ASN B 430 ? 0.7329 0.4618 0.4319 0.0413  0.0654  -0.0050 430 ASN B CG  
8585 O OD1 . ASN B 430 ? 0.7402 0.4870 0.4549 0.0454  0.0608  -0.0028 430 ASN B OD1 
8586 N ND2 . ASN B 430 ? 0.7852 0.4876 0.4593 0.0363  0.0744  -0.0072 430 ASN B ND2 
8587 N N   . PRO B 431 ? 0.5706 0.3763 0.3429 0.0491  0.0386  -0.0011 431 PRO B N   
8588 C CA  . PRO B 431 ? 0.5472 0.3751 0.3426 0.0429  0.0324  -0.0017 431 PRO B CA  
8589 C C   . PRO B 431 ? 0.5467 0.3786 0.3455 0.0394  0.0337  -0.0012 431 PRO B C   
8590 O O   . PRO B 431 ? 0.5375 0.3793 0.3473 0.0304  0.0318  -0.0030 431 PRO B O   
8591 C CB  . PRO B 431 ? 0.5454 0.3905 0.3553 0.0512  0.0258  0.0009  431 PRO B CB  
8592 C CG  . PRO B 431 ? 0.5498 0.3845 0.3447 0.0632  0.0289  0.0036  431 PRO B CG  
8593 C CD  . PRO B 431 ? 0.5637 0.3733 0.3358 0.0616  0.0361  0.0019  431 PRO B CD  
8594 N N   . ALA B 432 ? 0.5508 0.3751 0.3396 0.0469  0.0371  0.0011  432 ALA B N   
8595 C CA  . ALA B 432 ? 0.5338 0.3604 0.3239 0.0443  0.0388  0.0016  432 ALA B CA  
8596 C C   . ALA B 432 ? 0.5400 0.3562 0.3212 0.0321  0.0434  -0.0023 432 ALA B C   
8597 O O   . ALA B 432 ? 0.5134 0.3412 0.3052 0.0252  0.0417  -0.0031 432 ALA B O   
8598 C CB  . ALA B 432 ? 0.5491 0.3657 0.3257 0.0555  0.0429  0.0048  432 ALA B CB  
8599 N N   . ARG B 433 ? 0.5733 0.3687 0.3349 0.0289  0.0492  -0.0047 433 ARG B N   
8600 C CA  . ARG B 433 ? 0.5977 0.3846 0.3503 0.0158  0.0536  -0.0091 433 ARG B CA  
8601 C C   . ARG B 433 ? 0.5765 0.3839 0.3481 0.0062  0.0483  -0.0113 433 ARG B C   
8602 O O   . ARG B 433 ? 0.5637 0.3790 0.3396 -0.0026 0.0486  -0.0133 433 ARG B O   
8603 C CB  . ARG B 433 ? 0.6279 0.3875 0.3548 0.0139  0.0612  -0.0113 433 ARG B CB  
8604 C CG  . ARG B 433 ? 0.6530 0.4089 0.3743 -0.0010 0.0641  -0.0162 433 ARG B CG  
8605 C CD  . ARG B 433 ? 0.6666 0.3943 0.3597 -0.0071 0.0739  -0.0191 433 ARG B CD  
8606 N NE  . ARG B 433 ? 0.7198 0.4323 0.3982 -0.0139 0.0784  -0.0220 433 ARG B NE  
8607 C CZ  . ARG B 433 ? 0.7092 0.4255 0.3868 -0.0289 0.0800  -0.0266 433 ARG B CZ  
8608 N NH1 . ARG B 433 ? 0.7273 0.4633 0.4182 -0.0384 0.0772  -0.0289 433 ARG B NH1 
8609 N NH2 . ARG B 433 ? 0.7042 0.4053 0.3670 -0.0342 0.0846  -0.0289 433 ARG B NH2 
8610 N N   . PHE B 434 ? 0.5662 0.3825 0.3484 0.0088  0.0436  -0.0107 434 PHE B N   
8611 C CA  . PHE B 434 ? 0.5321 0.3673 0.3319 0.0021  0.0386  -0.0121 434 PHE B CA  
8612 C C   . PHE B 434 ? 0.5065 0.3617 0.3251 0.0020  0.0339  -0.0104 434 PHE B C   
8613 O O   . PHE B 434 ? 0.4806 0.3469 0.3062 -0.0059 0.0332  -0.0120 434 PHE B O   
8614 C CB  . PHE B 434 ? 0.5181 0.3572 0.3246 0.0074  0.0344  -0.0113 434 PHE B CB  
8615 C CG  . PHE B 434 ? 0.4967 0.3517 0.3181 0.0017  0.0301  -0.0128 434 PHE B CG  
8616 C CD1 . PHE B 434 ? 0.4979 0.3492 0.3125 -0.0061 0.0327  -0.0161 434 PHE B CD1 
8617 C CD2 . PHE B 434 ? 0.4853 0.3581 0.3262 0.0050  0.0236  -0.0109 434 PHE B CD2 
8618 C CE1 . PHE B 434 ? 0.4954 0.3618 0.3230 -0.0098 0.0290  -0.0172 434 PHE B CE1 
8619 C CE2 . PHE B 434 ? 0.4726 0.3579 0.3252 0.0012  0.0202  -0.0120 434 PHE B CE2 
8620 C CZ  . PHE B 434 ? 0.4700 0.3528 0.3162 -0.0055 0.0228  -0.0150 434 PHE B CZ  
8621 N N   . LEU B 435 ? 0.5094 0.3700 0.3355 0.0109  0.0308  -0.0068 435 LEU B N   
8622 C CA  . LEU B 435 ? 0.5035 0.3815 0.3462 0.0111  0.0269  -0.0047 435 LEU B CA  
8623 C C   . LEU B 435 ? 0.5174 0.3937 0.3546 0.0058  0.0306  -0.0056 435 LEU B C   
8624 O O   . LEU B 435 ? 0.5148 0.4052 0.3632 0.0005  0.0286  -0.0059 435 LEU B O   
8625 C CB  . LEU B 435 ? 0.4954 0.3795 0.3458 0.0209  0.0236  -0.0009 435 LEU B CB  
8626 C CG  . LEU B 435 ? 0.4936 0.3949 0.3607 0.0210  0.0198  0.0014  435 LEU B CG  
8627 C CD1 . LEU B 435 ? 0.4631 0.3782 0.3458 0.0159  0.0153  0.0008  435 LEU B CD1 
8628 C CD2 . LEU B 435 ? 0.4908 0.3980 0.3634 0.0299  0.0173  0.0049  435 LEU B CD2 
8629 N N   . GLN B 436 ? 0.5248 0.3834 0.3436 0.0074  0.0364  -0.0061 436 GLN B N   
8630 C CA  . GLN B 436 ? 0.5377 0.3921 0.3483 0.0018  0.0406  -0.0076 436 GLN B CA  
8631 C C   . GLN B 436 ? 0.5422 0.4000 0.3511 -0.0106 0.0421  -0.0118 436 GLN B C   
8632 O O   . GLN B 436 ? 0.5479 0.4184 0.3642 -0.0161 0.0412  -0.0124 436 GLN B O   
8633 C CB  . GLN B 436 ? 0.5764 0.4073 0.3643 0.0059  0.0474  -0.0077 436 GLN B CB  
8634 C CG  . GLN B 436 ? 0.5776 0.4095 0.3675 0.0184  0.0464  -0.0032 436 GLN B CG  
8635 C CD  . GLN B 436 ? 0.6289 0.4359 0.3945 0.0250  0.0535  -0.0028 436 GLN B CD  
8636 O OE1 . GLN B 436 ? 0.6824 0.4706 0.4311 0.0236  0.0579  -0.0048 436 GLN B OE1 
8637 N NE2 . GLN B 436 ? 0.6619 0.4680 0.4245 0.0324  0.0550  0.0000  436 GLN B NE2 
8638 N N   . LYS B 437 ? 0.5594 0.4072 0.3585 -0.0150 0.0445  -0.0146 437 LYS B N   
8639 C CA  . LYS B 437 ? 0.5545 0.4077 0.3519 -0.0272 0.0461  -0.0187 437 LYS B CA  
8640 C C   . LYS B 437 ? 0.5116 0.3913 0.3314 -0.0289 0.0398  -0.0177 437 LYS B C   
8641 O O   . LYS B 437 ? 0.5407 0.4322 0.3633 -0.0371 0.0403  -0.0197 437 LYS B O   
8642 C CB  . LYS B 437 ? 0.5759 0.4160 0.3613 -0.0306 0.0490  -0.0213 437 LYS B CB  
8643 C CG  . LYS B 437 ? 0.6268 0.4687 0.4047 -0.0446 0.0526  -0.0261 437 LYS B CG  
8644 C CD  . LYS B 437 ? 0.7061 0.5421 0.4789 -0.0470 0.0536  -0.0278 437 LYS B CD  
8645 C CE  . LYS B 437 ? 0.7694 0.6159 0.5409 -0.0607 0.0555  -0.0322 437 LYS B CE  
8646 N NZ  . LYS B 437 ? 0.8322 0.6600 0.5803 -0.0719 0.0637  -0.0366 437 LYS B NZ  
8647 N N   . ALA B 438 ? 0.4591 0.3481 0.2938 -0.0210 0.0343  -0.0145 438 ALA B N   
8648 C CA  . ALA B 438 ? 0.4394 0.3501 0.2931 -0.0216 0.0290  -0.0132 438 ALA B CA  
8649 C C   . ALA B 438 ? 0.4569 0.3803 0.3205 -0.0207 0.0273  -0.0109 438 ALA B C   
8650 O O   . ALA B 438 ? 0.4552 0.3958 0.3314 -0.0224 0.0244  -0.0101 438 ALA B O   
8651 C CB  . ALA B 438 ? 0.4034 0.3178 0.2681 -0.0143 0.0242  -0.0109 438 ALA B CB  
8652 N N   . MET B 439 ? 0.4906 0.4055 0.3481 -0.0172 0.0293  -0.0095 439 MET B N   
8653 C CA  . MET B 439 ? 0.5166 0.4427 0.3824 -0.0163 0.0281  -0.0072 439 MET B CA  
8654 C C   . MET B 439 ? 0.5363 0.4616 0.3918 -0.0246 0.0325  -0.0102 439 MET B C   
8655 O O   . MET B 439 ? 0.5301 0.4675 0.3928 -0.0253 0.0315  -0.0089 439 MET B O   
8656 C CB  . MET B 439 ? 0.5085 0.4304 0.3766 -0.0071 0.0271  -0.0035 439 MET B CB  
8657 C CG  . MET B 439 ? 0.4898 0.4182 0.3712 -0.0003 0.0220  -0.0006 439 MET B CG  
8658 S SD  . MET B 439 ? 0.5227 0.4723 0.4247 -0.0013 0.0168  0.0017  439 MET B SD  
8659 C CE  . MET B 439 ? 0.4937 0.4458 0.3984 -0.0045 0.0150  -0.0006 439 MET B CE  
8660 N N   . ASP B 440 ? 0.5640 0.4750 0.4024 -0.0312 0.0375  -0.0143 440 ASP B N   
8661 C CA  . ASP B 440 ? 0.6319 0.5436 0.4597 -0.0422 0.0417  -0.0185 440 ASP B CA  
8662 C C   . ASP B 440 ? 0.6788 0.6162 0.5208 -0.0472 0.0385  -0.0186 440 ASP B C   
8663 O O   . ASP B 440 ? 0.6295 0.5812 0.4848 -0.0453 0.0343  -0.0172 440 ASP B O   
8664 C CB  . ASP B 440 ? 0.6406 0.5377 0.4513 -0.0507 0.0466  -0.0233 440 ASP B CB  
8665 C CG  . ASP B 440 ? 0.6536 0.5217 0.4427 -0.0486 0.0526  -0.0242 440 ASP B CG  
8666 O OD1 . ASP B 440 ? 0.6637 0.5244 0.4499 -0.0417 0.0535  -0.0218 440 ASP B OD1 
8667 O OD2 . ASP B 440 ? 0.6807 0.5331 0.4548 -0.0536 0.0569  -0.0273 440 ASP B OD2 
8668 N N   . PHE B 441 ? 0.7478 0.6899 0.5847 -0.0533 0.0409  -0.0204 441 PHE B N   
8669 C CA  . PHE B 441 ? 0.8205 0.7876 0.6693 -0.0567 0.0383  -0.0200 441 PHE B CA  
8670 C C   . PHE B 441 ? 0.8491 0.8345 0.7026 -0.0640 0.0372  -0.0225 441 PHE B C   
8671 O O   . PHE B 441 ? 0.8317 0.8377 0.7007 -0.0602 0.0330  -0.0196 441 PHE B O   
8672 C CB  . PHE B 441 ? 0.9053 0.8703 0.7439 -0.0623 0.0420  -0.0221 441 PHE B CB  
8673 C CG  . PHE B 441 ? 0.9685 0.9590 0.8177 -0.0652 0.0397  -0.0215 441 PHE B CG  
8674 C CD1 . PHE B 441 ? 0.9770 0.9820 0.8435 -0.0561 0.0349  -0.0160 441 PHE B CD1 
8675 C CD2 . PHE B 441 ? 1.0262 1.0254 0.8665 -0.0774 0.0427  -0.0265 441 PHE B CD2 
8676 C CE1 . PHE B 441 ? 0.9532 0.9807 0.8278 -0.0578 0.0333  -0.0150 441 PHE B CE1 
8677 C CE2 . PHE B 441 ? 1.0129 1.0372 0.8623 -0.0794 0.0406  -0.0258 441 PHE B CE2 
8678 C CZ  . PHE B 441 ? 0.9881 1.0261 0.8545 -0.0689 0.0359  -0.0198 441 PHE B CZ  
8679 N N   . PRO B 442 ? 0.8894 0.8673 0.7288 -0.0743 0.0414  -0.0277 442 PRO B N   
8680 C CA  . PRO B 442 ? 0.9302 0.9280 0.7725 -0.0828 0.0412  -0.0307 442 PRO B CA  
8681 C C   . PRO B 442 ? 0.8904 0.9098 0.7515 -0.0757 0.0357  -0.0270 442 PRO B C   
8682 O O   . PRO B 442 ? 0.9161 0.9602 0.7849 -0.0785 0.0342  -0.0270 442 PRO B O   
8683 C CB  . PRO B 442 ? 0.9393 0.9186 0.7655 -0.0902 0.0457  -0.0350 442 PRO B CB  
8684 C CG  . PRO B 442 ? 0.9745 0.9257 0.7835 -0.0906 0.0505  -0.0362 442 PRO B CG  
8685 C CD  . PRO B 442 ? 0.9374 0.8877 0.7556 -0.0790 0.0474  -0.0312 442 PRO B CD  
8686 N N   . PHE B 443 ? 0.8650 0.8751 0.7325 -0.0664 0.0330  -0.0238 443 PHE B N   
8687 C CA  . PHE B 443 ? 0.8844 0.9101 0.7666 -0.0600 0.0286  -0.0208 443 PHE B CA  
8688 C C   . PHE B 443 ? 0.8753 0.9212 0.7723 -0.0536 0.0249  -0.0165 443 PHE B C   
8689 O O   . PHE B 443 ? 0.9176 0.9812 0.8239 -0.0507 0.0226  -0.0149 443 PHE B O   
8690 C CB  . PHE B 443 ? 0.8443 0.8540 0.7291 -0.0517 0.0265  -0.0186 443 PHE B CB  
8691 C CG  . PHE B 443 ? 0.8065 0.8134 0.7018 -0.0413 0.0230  -0.0136 443 PHE B CG  
8692 C CD1 . PHE B 443 ? 0.7636 0.7830 0.6733 -0.0341 0.0188  -0.0098 443 PHE B CD1 
8693 C CD2 . PHE B 443 ? 0.7641 0.7566 0.6543 -0.0389 0.0242  -0.0126 443 PHE B CD2 
8694 C CE1 . PHE B 443 ? 0.7592 0.7760 0.6778 -0.0261 0.0160  -0.0055 443 PHE B CE1 
8695 C CE2 . PHE B 443 ? 0.7402 0.7325 0.6404 -0.0303 0.0210  -0.0081 443 PHE B CE2 
8696 C CZ  . PHE B 443 ? 0.7329 0.7373 0.6474 -0.0246 0.0170  -0.0047 443 PHE B CZ  
8697 N N   . ILE B 444 ? 0.8703 0.9126 0.7684 -0.0507 0.0247  -0.0143 444 ILE B N   
8698 C CA  . ILE B 444 ? 0.8474 0.9063 0.7583 -0.0442 0.0217  -0.0098 444 ILE B CA  
8699 C C   . ILE B 444 ? 0.8686 0.9399 0.7766 -0.0496 0.0234  -0.0108 444 ILE B C   
8700 O O   . ILE B 444 ? 0.8426 0.9235 0.7590 -0.0440 0.0215  -0.0069 444 ILE B O   
8701 C CB  . ILE B 444 ? 0.7963 0.8445 0.7156 -0.0339 0.0189  -0.0048 444 ILE B CB  
8702 C CG1 . ILE B 444 ? 0.7711 0.8357 0.7036 -0.0268 0.0159  0.0001  444 ILE B CG1 
8703 C CG2 . ILE B 444 ? 0.7427 0.7756 0.6552 -0.0339 0.0207  -0.0048 444 ILE B CG2 
8704 C CD1 . ILE B 444 ? 0.6908 0.7467 0.6321 -0.0179 0.0131  0.0045  444 ILE B CD1 
8705 N N   . CYS B 445 ? 0.9355 1.0067 0.8311 -0.0608 0.0271  -0.0163 445 CYS B N   
8706 C CA  . CYS B 445 ? 0.9775 1.0603 0.8683 -0.0677 0.0290  -0.0185 445 CYS B CA  
8707 C C   . CYS B 445 ? 0.9517 1.0652 0.8536 -0.0657 0.0265  -0.0162 445 CYS B C   
8708 O O   . CYS B 445 ? 0.9263 1.0513 0.8285 -0.0671 0.0267  -0.0158 445 CYS B O   
8709 C CB  . CYS B 445 ? 1.0489 1.1239 0.9222 -0.0818 0.0340  -0.0255 445 CYS B CB  
8710 S SG  . CYS B 445 ? 1.1693 1.2663 1.0405 -0.0929 0.0351  -0.0303 445 CYS B SG  
8711 N N   . ASN B 446 ? 0.9026 1.0291 0.8129 -0.0615 0.0242  -0.0144 446 ASN B N   
8712 C CA  . ASN B 446 ? 0.9157 1.0709 0.8363 -0.0568 0.0219  -0.0112 446 ASN B CA  
8713 C C   . ASN B 446 ? 0.8928 1.0490 0.8250 -0.0437 0.0190  -0.0041 446 ASN B C   
8714 O O   . ASN B 446 ? 0.8932 1.0708 0.8329 -0.0380 0.0175  -0.0006 446 ASN B O   
8715 C CB  . ASN B 446 ? 0.9193 1.0901 0.8426 -0.0575 0.0214  -0.0123 446 ASN B CB  
8716 C CG  . ASN B 446 ? 0.9628 1.1551 0.8793 -0.0700 0.0237  -0.0178 446 ASN B CG  
8717 O OD1 . ASN B 446 ? 0.9586 1.1705 0.8756 -0.0728 0.0239  -0.0180 446 ASN B OD1 
8718 N ND2 . ASN B 446 ? 0.9171 1.1065 0.8270 -0.0781 0.0256  -0.0223 446 ASN B ND2 
8719 N N   . SER B 447 ? 0.8551 0.9882 0.7878 -0.0390 0.0185  -0.0020 447 SER B N   
8720 C CA  . SER B 447 ? 0.8086 0.9402 0.7501 -0.0293 0.0165  0.0039  447 SER B CA  
8721 C C   . SER B 447 ? 0.7790 0.9052 0.7159 -0.0322 0.0180  0.0035  447 SER B C   
8722 O O   . SER B 447 ? 0.7509 0.8747 0.6939 -0.0254 0.0169  0.0082  447 SER B O   
8723 C CB  . SER B 447 ? 0.8152 0.9275 0.7612 -0.0221 0.0148  0.0067  447 SER B CB  
8724 O OG  . SER B 447 ? 0.8560 0.9744 0.8080 -0.0166 0.0131  0.0088  447 SER B OG  
8725 N N   . PHE B 448 ? 0.7316 0.8556 0.6572 -0.0426 0.0209  -0.0020 448 PHE B N   
8726 C CA  . PHE B 448 ? 0.6894 0.8050 0.6077 -0.0461 0.0230  -0.0034 448 PHE B CA  
8727 C C   . PHE B 448 ? 0.6638 0.7967 0.5754 -0.0554 0.0250  -0.0073 448 PHE B C   
8728 O O   . PHE B 448 ? 0.6976 0.8203 0.5962 -0.0642 0.0284  -0.0122 448 PHE B O   
8729 C CB  . PHE B 448 ? 0.7374 0.8260 0.6445 -0.0496 0.0256  -0.0066 448 PHE B CB  
8730 C CG  . PHE B 448 ? 0.7066 0.7790 0.6188 -0.0404 0.0241  -0.0023 448 PHE B CG  
8731 C CD1 . PHE B 448 ? 0.6956 0.7550 0.6017 -0.0395 0.0261  -0.0020 448 PHE B CD1 
8732 C CD2 . PHE B 448 ? 0.7063 0.7774 0.6291 -0.0326 0.0210  0.0015  448 PHE B CD2 
8733 C CE1 . PHE B 448 ? 0.6791 0.7269 0.5903 -0.0312 0.0247  0.0020  448 PHE B CE1 
8734 C CE2 . PHE B 448 ? 0.6994 0.7581 0.6270 -0.0253 0.0196  0.0052  448 PHE B CE2 
8735 C CZ  . PHE B 448 ? 0.7119 0.7601 0.6343 -0.0246 0.0214  0.0055  448 PHE B CZ  
8736 N N   . THR B 449 ? 0.6155 0.7747 0.5350 -0.0531 0.0232  -0.0053 449 THR B N   
8737 C CA  . THR B 449 ? 0.6158 0.7966 0.5302 -0.0619 0.0245  -0.0090 449 THR B CA  
8738 C C   . THR B 449 ? 0.5900 0.7815 0.5084 -0.0573 0.0238  -0.0054 449 THR B C   
8739 O O   . THR B 449 ? 0.5452 0.7271 0.4704 -0.0474 0.0224  0.0001  449 THR B O   
8740 C CB  . THR B 449 ? 0.6246 0.8322 0.5445 -0.0623 0.0231  -0.0092 449 THR B CB  
8741 O OG1 . THR B 449 ? 0.6235 0.8443 0.5562 -0.0490 0.0201  -0.0019 449 THR B OG1 
8742 C CG2 . THR B 449 ? 0.6179 0.8151 0.5353 -0.0653 0.0236  -0.0119 449 THR B CG2 
8743 N N   . LYS B 450 ? 0.5856 0.7977 0.4992 -0.0650 0.0249  -0.0087 450 LYS B N   
8744 C CA  . LYS B 450 ? 0.5711 0.7987 0.4886 -0.0607 0.0241  -0.0054 450 LYS B CA  
8745 C C   . LYS B 450 ? 0.5231 0.7660 0.4546 -0.0467 0.0209  0.0025  450 LYS B C   
8746 O O   . LYS B 450 ? 0.5067 0.7515 0.4433 -0.0388 0.0202  0.0077  450 LYS B O   
8747 C CB  . LYS B 450 ? 0.6001 0.8510 0.5098 -0.0725 0.0256  -0.0111 450 LYS B CB  
8748 C CG  . LYS B 450 ? 0.6351 0.9028 0.5418 -0.0818 0.0261  -0.0162 450 LYS B CG  
8749 C CD  . LYS B 450 ? 0.6866 0.9724 0.5826 -0.0967 0.0283  -0.0233 450 LYS B CD  
8750 C CE  . LYS B 450 ? 0.7306 1.0138 0.6159 -0.1118 0.0310  -0.0312 450 LYS B CE  
8751 N NZ  . LYS B 450 ? 0.7776 1.0829 0.6713 -0.1095 0.0291  -0.0301 450 LYS B NZ  
8752 N N   . PHE B 451 ? 0.4977 0.7501 0.4344 -0.0434 0.0196  0.0035  451 PHE B N   
8753 C CA  . PHE B 451 ? 0.4960 0.7599 0.4439 -0.0296 0.0173  0.0110  451 PHE B CA  
8754 C C   . PHE B 451 ? 0.4697 0.7101 0.4232 -0.0195 0.0165  0.0168  451 PHE B C   
8755 O O   . PHE B 451 ? 0.4523 0.6990 0.4126 -0.0089 0.0156  0.0234  451 PHE B O   
8756 C CB  . PHE B 451 ? 0.5238 0.7978 0.4744 -0.0281 0.0165  0.0105  451 PHE B CB  
8757 C CG  . PHE B 451 ? 0.5525 0.8620 0.5035 -0.0300 0.0163  0.0094  451 PHE B CG  
8758 C CD1 . PHE B 451 ? 0.5608 0.8925 0.5179 -0.0190 0.0152  0.0155  451 PHE B CD1 
8759 C CD2 . PHE B 451 ? 0.5718 0.8933 0.5164 -0.0428 0.0175  0.0023  451 PHE B CD2 
8760 C CE1 . PHE B 451 ? 0.5877 0.9553 0.5452 -0.0198 0.0150  0.0148  451 PHE B CE1 
8761 C CE2 . PHE B 451 ? 0.5814 0.9393 0.5269 -0.0451 0.0172  0.0011  451 PHE B CE2 
8762 C CZ  . PHE B 451 ? 0.5676 0.9496 0.5198 -0.0331 0.0158  0.0074  451 PHE B CZ  
8763 N N   . GLU B 452 ? 0.4497 0.6635 0.4000 -0.0229 0.0171  0.0145  452 GLU B N   
8764 C CA  . GLU B 452 ? 0.4487 0.6416 0.4043 -0.0148 0.0162  0.0193  452 GLU B CA  
8765 C C   . GLU B 452 ? 0.4444 0.6296 0.3985 -0.0145 0.0172  0.0209  452 GLU B C   
8766 O O   . GLU B 452 ? 0.4370 0.6181 0.3976 -0.0062 0.0164  0.0267  452 GLU B O   
8767 C CB  . GLU B 452 ? 0.4687 0.6389 0.4220 -0.0173 0.0162  0.0166  452 GLU B CB  
8768 C CG  . GLU B 452 ? 0.5066 0.6786 0.4646 -0.0127 0.0148  0.0178  452 GLU B CG  
8769 C CD  . GLU B 452 ? 0.5075 0.6937 0.4608 -0.0200 0.0154  0.0127  452 GLU B CD  
8770 O OE1 . GLU B 452 ? 0.5359 0.7314 0.4933 -0.0153 0.0144  0.0144  452 GLU B OE1 
8771 O OE2 . GLU B 452 ? 0.5261 0.7137 0.4707 -0.0307 0.0173  0.0070  452 GLU B OE2 
8772 N N   . PHE B 453 ? 0.4388 0.6219 0.3836 -0.0238 0.0191  0.0155  453 PHE B N   
8773 C CA  . PHE B 453 ? 0.4456 0.6162 0.3870 -0.0240 0.0205  0.0161  453 PHE B CA  
8774 C C   . PHE B 453 ? 0.4445 0.6319 0.3841 -0.0250 0.0213  0.0167  453 PHE B C   
8775 O O   . PHE B 453 ? 0.4548 0.6337 0.3923 -0.0239 0.0224  0.0180  453 PHE B O   
8776 C CB  . PHE B 453 ? 0.4629 0.6121 0.3930 -0.0318 0.0228  0.0102  453 PHE B CB  
8777 C CG  . PHE B 453 ? 0.4988 0.6292 0.4311 -0.0288 0.0220  0.0108  453 PHE B CG  
8778 C CD1 . PHE B 453 ? 0.4850 0.6043 0.4250 -0.0202 0.0206  0.0160  453 PHE B CD1 
8779 C CD2 . PHE B 453 ? 0.5149 0.6399 0.4414 -0.0348 0.0226  0.0060  453 PHE B CD2 
8780 C CE1 . PHE B 453 ? 0.4944 0.5985 0.4365 -0.0177 0.0196  0.0163  453 PHE B CE1 
8781 C CE2 . PHE B 453 ? 0.5099 0.6185 0.4383 -0.0316 0.0218  0.0066  453 PHE B CE2 
8782 C CZ  . PHE B 453 ? 0.5219 0.6206 0.4583 -0.0230 0.0201  0.0117  453 PHE B CZ  
8783 N N   . ASN B 454 ? 0.4312 0.6436 0.3715 -0.0269 0.0207  0.0159  454 ASN B N   
8784 C CA  . ASN B 454 ? 0.4288 0.6597 0.3672 -0.0279 0.0213  0.0164  454 ASN B CA  
8785 C C   . ASN B 454 ? 0.4151 0.6478 0.3620 -0.0163 0.0203  0.0244  454 ASN B C   
8786 O O   . ASN B 454 ? 0.4057 0.6329 0.3610 -0.0073 0.0190  0.0300  454 ASN B O   
8787 C CB  . ASN B 454 ? 0.4256 0.6866 0.3635 -0.0318 0.0206  0.0141  454 ASN B CB  
8788 C CG  . ASN B 454 ? 0.4142 0.6927 0.3626 -0.0198 0.0185  0.0211  454 ASN B CG  
8789 O OD1 . ASN B 454 ? 0.4182 0.7109 0.3703 -0.0126 0.0181  0.0261  454 ASN B OD1 
8790 N ND2 . ASN B 454 ? 0.4023 0.6778 0.3547 -0.0167 0.0175  0.0218  454 ASN B ND2 
8791 N N   . THR B 455 ? 0.4074 0.6469 0.3513 -0.0171 0.0214  0.0249  455 THR B N   
8792 C CA  . THR B 455 ? 0.4103 0.6558 0.3612 -0.0069 0.0209  0.0324  455 THR B CA  
8793 C C   . THR B 455 ? 0.4209 0.6946 0.3700 -0.0073 0.0209  0.0326  455 THR B C   
8794 O O   . THR B 455 ? 0.4197 0.6980 0.3692 -0.0033 0.0215  0.0361  455 THR B O   
8795 C CB  . THR B 455 ? 0.4237 0.6487 0.3739 -0.0050 0.0222  0.0344  455 THR B CB  
8796 O OG1 . THR B 455 ? 0.4333 0.6497 0.3725 -0.0147 0.0242  0.0276  455 THR B OG1 
8797 C CG2 . THR B 455 ? 0.4097 0.6128 0.3657 -0.0003 0.0215  0.0373  455 THR B CG2 
8798 N N   . VAL B 456 ? 0.4280 0.7216 0.3748 -0.0124 0.0202  0.0286  456 VAL B N   
8799 C CA  . VAL B 456 ? 0.4330 0.7589 0.3794 -0.0118 0.0197  0.0291  456 VAL B CA  
8800 C C   . VAL B 456 ? 0.4187 0.7575 0.3743 0.0026  0.0184  0.0377  456 VAL B C   
8801 O O   . VAL B 456 ? 0.4138 0.7564 0.3726 0.0118  0.0186  0.0442  456 VAL B O   
8802 C CB  . VAL B 456 ? 0.4489 0.7930 0.3888 -0.0242 0.0197  0.0209  456 VAL B CB  
8803 C CG1 . VAL B 456 ? 0.4385 0.8198 0.3785 -0.0234 0.0189  0.0214  456 VAL B CG1 
8804 C CG2 . VAL B 456 ? 0.4592 0.7863 0.3875 -0.0387 0.0219  0.0124  456 VAL B CG2 
8805 N N   . PHE B 457 ? 0.4167 0.7594 0.3756 0.0050  0.0174  0.0379  457 PHE B N   
8806 C CA  . PHE B 457 ? 0.4166 0.7653 0.3822 0.0195  0.0168  0.0460  457 PHE B CA  
8807 C C   . PHE B 457 ? 0.4045 0.7224 0.3748 0.0264  0.0171  0.0507  457 PHE B C   
8808 O O   . PHE B 457 ? 0.4011 0.7163 0.3753 0.0383  0.0176  0.0584  457 PHE B O   
8809 C CB  . PHE B 457 ? 0.4114 0.7842 0.3777 0.0204  0.0159  0.0446  457 PHE B CB  
8810 C CG  . PHE B 457 ? 0.4421 0.8059 0.4061 0.0097  0.0155  0.0374  457 PHE B CG  
8811 C CD1 . PHE B 457 ? 0.4254 0.7687 0.3928 0.0141  0.0152  0.0390  457 PHE B CD1 
8812 C CD2 . PHE B 457 ? 0.4510 0.8263 0.4083 -0.0050 0.0158  0.0287  457 PHE B CD2 
8813 C CE1 . PHE B 457 ? 0.4301 0.7652 0.3949 0.0047  0.0151  0.0326  457 PHE B CE1 
8814 C CE2 . PHE B 457 ? 0.4476 0.8135 0.4017 -0.0150 0.0161  0.0223  457 PHE B CE2 
8815 C CZ  . PHE B 457 ? 0.4332 0.7793 0.3913 -0.0096 0.0156  0.0245  457 PHE B CZ  
8816 N N   . ASN B 458 ? 0.4002 0.6950 0.3691 0.0187  0.0170  0.0460  458 ASN B N   
8817 C CA  . ASN B 458 ? 0.3914 0.6585 0.3645 0.0236  0.0170  0.0495  458 ASN B CA  
8818 C C   . ASN B 458 ? 0.3870 0.6390 0.3614 0.0259  0.0180  0.0531  458 ASN B C   
8819 O O   . ASN B 458 ? 0.3961 0.6467 0.3665 0.0193  0.0187  0.0497  458 ASN B O   
8820 C CB  . ASN B 458 ? 0.3813 0.6306 0.3522 0.0153  0.0166  0.0434  458 ASN B CB  
8821 C CG  . ASN B 458 ? 0.3851 0.6391 0.3578 0.0174  0.0157  0.0427  458 ASN B CG  
8822 O OD1 . ASN B 458 ? 0.3903 0.6345 0.3605 0.0104  0.0153  0.0374  458 ASN B OD1 
8823 N ND2 . ASN B 458 ? 0.3571 0.6255 0.3331 0.0276  0.0155  0.0483  458 ASN B ND2 
8824 N N   . ASP B 459 ? 0.4046 0.6444 0.3839 0.0349  0.0184  0.0598  459 ASP B N   
8825 C CA  . ASP B 459 ? 0.4096 0.6324 0.3908 0.0359  0.0194  0.0630  459 ASP B CA  
8826 C C   . ASP B 459 ? 0.3994 0.6012 0.3799 0.0286  0.0189  0.0581  459 ASP B C   
8827 O O   . ASP B 459 ? 0.3943 0.5907 0.3740 0.0249  0.0179  0.0540  459 ASP B O   
8828 C CB  . ASP B 459 ? 0.4279 0.6420 0.4134 0.0461  0.0204  0.0710  459 ASP B CB  
8829 C CG  . ASP B 459 ? 0.4697 0.7025 0.4544 0.0553  0.0216  0.0770  459 ASP B CG  
8830 O OD1 . ASP B 459 ? 0.5187 0.7660 0.5014 0.0546  0.0221  0.0772  459 ASP B OD1 
8831 O OD2 . ASP B 459 ? 0.4425 0.6746 0.4277 0.0639  0.0223  0.0817  459 ASP B OD2 
8832 N N   . GLN B 460 ? 0.3915 0.5827 0.3722 0.0271  0.0198  0.0588  460 GLN B N   
8833 C CA  . GLN B 460 ? 0.3863 0.5582 0.3665 0.0224  0.0196  0.0557  460 GLN B CA  
8834 C C   . GLN B 460 ? 0.3759 0.5335 0.3612 0.0254  0.0186  0.0576  460 GLN B C   
8835 O O   . GLN B 460 ? 0.3865 0.5331 0.3704 0.0213  0.0177  0.0534  460 GLN B O   
8836 C CB  . GLN B 460 ? 0.4026 0.5688 0.3831 0.0229  0.0209  0.0579  460 GLN B CB  
8837 C CG  . GLN B 460 ? 0.3941 0.5423 0.3741 0.0198  0.0210  0.0555  460 GLN B CG  
8838 C CD  . GLN B 460 ? 0.3862 0.5320 0.3649 0.0201  0.0226  0.0570  460 GLN B CD  
8839 O OE1 . GLN B 460 ? 0.3928 0.5459 0.3653 0.0176  0.0239  0.0547  460 GLN B OE1 
8840 N NE2 . GLN B 460 ? 0.3968 0.5328 0.3809 0.0229  0.0228  0.0607  460 GLN B NE2 
8841 N N   . ARG B 461 ? 0.3694 0.5266 0.3594 0.0325  0.0190  0.0640  461 ARG B N   
8842 C CA  . ARG B 461 ? 0.3780 0.5207 0.3716 0.0348  0.0184  0.0657  461 ARG B CA  
8843 C C   . ARG B 461 ? 0.3673 0.5118 0.3594 0.0344  0.0171  0.0625  461 ARG B C   
8844 O O   . ARG B 461 ? 0.3861 0.5175 0.3797 0.0336  0.0162  0.0612  461 ARG B O   
8845 C CB  . ARG B 461 ? 0.4063 0.5458 0.4028 0.0420  0.0200  0.0732  461 ARG B CB  
8846 C CG  . ARG B 461 ? 0.4434 0.5980 0.4379 0.0489  0.0211  0.0771  461 ARG B CG  
8847 C CD  . ARG B 461 ? 0.4797 0.6262 0.4752 0.0562  0.0234  0.0847  461 ARG B CD  
8848 N NE  . ARG B 461 ? 0.5350 0.6964 0.5276 0.0642  0.0251  0.0895  461 ARG B NE  
8849 C CZ  . ARG B 461 ? 0.5729 0.7347 0.5627 0.0725  0.0264  0.0934  461 ARG B CZ  
8850 N NH1 . ARG B 461 ? 0.5947 0.7416 0.5843 0.0731  0.0263  0.0928  461 ARG B NH1 
8851 N NH2 . ARG B 461 ? 0.6032 0.7803 0.5898 0.0807  0.0281  0.0981  461 ARG B NH2 
8852 N N   . THR B 462 ? 0.3521 0.5143 0.3413 0.0349  0.0171  0.0611  462 THR B N   
8853 C CA  . THR B 462 ? 0.3396 0.5074 0.3271 0.0341  0.0161  0.0578  462 THR B CA  
8854 C C   . THR B 462 ? 0.3451 0.5064 0.3292 0.0248  0.0151  0.0504  462 THR B C   
8855 O O   . THR B 462 ? 0.3385 0.4932 0.3224 0.0234  0.0142  0.0477  462 THR B O   
8856 C CB  . THR B 462 ? 0.3387 0.5310 0.3241 0.0368  0.0164  0.0585  462 THR B CB  
8857 O OG1 . THR B 462 ? 0.3438 0.5399 0.3309 0.0473  0.0177  0.0659  462 THR B OG1 
8858 C CG2 . THR B 462 ? 0.3373 0.5394 0.3205 0.0342  0.0154  0.0540  462 THR B CG2 
8859 N N   . VAL B 463 ? 0.3377 0.5001 0.3183 0.0190  0.0158  0.0473  463 VAL B N   
8860 C CA  . VAL B 463 ? 0.3489 0.5022 0.3239 0.0107  0.0158  0.0408  463 VAL B CA  
8861 C C   . VAL B 463 ? 0.3423 0.4746 0.3197 0.0113  0.0151  0.0410  463 VAL B C   
8862 O O   . VAL B 463 ? 0.3405 0.4642 0.3153 0.0079  0.0145  0.0370  463 VAL B O   
8863 C CB  . VAL B 463 ? 0.3671 0.5230 0.3361 0.0054  0.0174  0.0380  463 VAL B CB  
8864 C CG1 . VAL B 463 ? 0.3701 0.5116 0.3314 -0.0019 0.0182  0.0318  463 VAL B CG1 
8865 C CG2 . VAL B 463 ? 0.3406 0.5190 0.3063 0.0032  0.0179  0.0367  463 VAL B CG2 
8866 N N   . PHE B 464 ? 0.3418 0.4670 0.3241 0.0156  0.0153  0.0457  464 PHE B N   
8867 C CA  . PHE B 464 ? 0.3254 0.4339 0.3109 0.0164  0.0144  0.0463  464 PHE B CA  
8868 C C   . PHE B 464 ? 0.3326 0.4360 0.3209 0.0185  0.0130  0.0465  464 PHE B C   
8869 O O   . PHE B 464 ? 0.3162 0.4086 0.3036 0.0162  0.0120  0.0435  464 PHE B O   
8870 C CB  . PHE B 464 ? 0.3086 0.4137 0.2993 0.0199  0.0150  0.0516  464 PHE B CB  
8871 C CG  . PHE B 464 ? 0.3140 0.4200 0.3017 0.0179  0.0163  0.0509  464 PHE B CG  
8872 C CD1 . PHE B 464 ? 0.3071 0.4093 0.2873 0.0131  0.0170  0.0454  464 PHE B CD1 
8873 C CD2 . PHE B 464 ? 0.3110 0.4205 0.3024 0.0210  0.0175  0.0559  464 PHE B CD2 
8874 C CE1 . PHE B 464 ? 0.3076 0.4086 0.2837 0.0121  0.0187  0.0450  464 PHE B CE1 
8875 C CE2 . PHE B 464 ? 0.3082 0.4186 0.2965 0.0198  0.0189  0.0554  464 PHE B CE2 
8876 C CZ  . PHE B 464 ? 0.3041 0.4100 0.2847 0.0157  0.0195  0.0499  464 PHE B CZ  
8877 N N   . ALA B 465 ? 0.3300 0.4412 0.3204 0.0234  0.0131  0.0500  465 ALA B N   
8878 C CA  . ALA B 465 ? 0.3453 0.4517 0.3367 0.0260  0.0122  0.0499  465 ALA B CA  
8879 C C   . ALA B 465 ? 0.3614 0.4703 0.3486 0.0213  0.0114  0.0439  465 ALA B C   
8880 O O   . ALA B 465 ? 0.3575 0.4552 0.3444 0.0199  0.0103  0.0415  465 ALA B O   
8881 C CB  . ALA B 465 ? 0.3180 0.4331 0.3104 0.0334  0.0132  0.0549  465 ALA B CB  
8882 N N   . ASN B 466 ? 0.3562 0.4801 0.3396 0.0183  0.0120  0.0414  466 ASN B N   
8883 C CA  . ASN B 466 ? 0.3612 0.4881 0.3396 0.0123  0.0118  0.0356  466 ASN B CA  
8884 C C   . ASN B 466 ? 0.3469 0.4567 0.3219 0.0070  0.0117  0.0315  466 ASN B C   
8885 O O   . ASN B 466 ? 0.3436 0.4468 0.3166 0.0049  0.0111  0.0284  466 ASN B O   
8886 C CB  . ASN B 466 ? 0.3698 0.5154 0.3438 0.0078  0.0129  0.0330  466 ASN B CB  
8887 C CG  . ASN B 466 ? 0.3763 0.5420 0.3526 0.0132  0.0129  0.0360  466 ASN B CG  
8888 O OD1 . ASN B 466 ? 0.4080 0.5731 0.3871 0.0189  0.0123  0.0382  466 ASN B OD1 
8889 N ND2 . ASN B 466 ? 0.3622 0.5460 0.3370 0.0121  0.0136  0.0362  466 ASN B ND2 
8890 N N   . PHE B 467 ? 0.3448 0.4477 0.3188 0.0057  0.0124  0.0319  467 PHE B N   
8891 C CA  . PHE B 467 ? 0.3337 0.4211 0.3032 0.0020  0.0127  0.0285  467 PHE B CA  
8892 C C   . PHE B 467 ? 0.3254 0.3998 0.2995 0.0053  0.0110  0.0299  467 PHE B C   
8893 O O   . PHE B 467 ? 0.3369 0.4016 0.3073 0.0031  0.0106  0.0265  467 PHE B O   
8894 C CB  . PHE B 467 ? 0.3224 0.4073 0.2892 0.0011  0.0142  0.0290  467 PHE B CB  
8895 C CG  . PHE B 467 ? 0.3337 0.4029 0.2948 -0.0006 0.0149  0.0264  467 PHE B CG  
8896 C CD1 . PHE B 467 ? 0.3314 0.3936 0.2822 -0.0060 0.0165  0.0209  467 PHE B CD1 
8897 C CD2 . PHE B 467 ? 0.3285 0.3904 0.2938 0.0033  0.0145  0.0295  467 PHE B CD2 
8898 C CE1 . PHE B 467 ? 0.3283 0.3749 0.2723 -0.0063 0.0177  0.0189  467 PHE B CE1 
8899 C CE2 . PHE B 467 ? 0.3293 0.3786 0.2890 0.0031  0.0153  0.0275  467 PHE B CE2 
8900 C CZ  . PHE B 467 ? 0.3219 0.3628 0.2705 -0.0010 0.0170  0.0224  467 PHE B CZ  
8901 N N   . TYR B 468 ? 0.3209 0.3952 0.3024 0.0103  0.0101  0.0349  468 TYR B N   
8902 C CA  . TYR B 468 ? 0.3295 0.3927 0.3152 0.0125  0.0085  0.0360  468 TYR B CA  
8903 C C   . TYR B 468 ? 0.3389 0.4002 0.3229 0.0123  0.0075  0.0334  468 TYR B C   
8904 O O   . TYR B 468 ? 0.3477 0.3993 0.3297 0.0105  0.0066  0.0304  468 TYR B O   
8905 C CB  . TYR B 468 ? 0.3005 0.3643 0.2927 0.0169  0.0085  0.0416  468 TYR B CB  
8906 C CG  . TYR B 468 ? 0.2853 0.3377 0.2813 0.0178  0.0072  0.0427  468 TYR B CG  
8907 C CD1 . TYR B 468 ? 0.2819 0.3272 0.2791 0.0158  0.0063  0.0417  468 TYR B CD1 
8908 C CD2 . TYR B 468 ? 0.2827 0.3320 0.2804 0.0210  0.0071  0.0450  468 TYR B CD2 
8909 C CE1 . TYR B 468 ? 0.2821 0.3192 0.2829 0.0157  0.0050  0.0425  468 TYR B CE1 
8910 C CE2 . TYR B 468 ? 0.2752 0.3135 0.2753 0.0208  0.0062  0.0456  468 TYR B CE2 
8911 C CZ  . TYR B 468 ? 0.2854 0.3184 0.2874 0.0176  0.0050  0.0442  468 TYR B CZ  
8912 O OH  . TYR B 468 ? 0.3052 0.3292 0.3096 0.0165  0.0041  0.0446  468 TYR B OH  
8913 N N   . ASP B 469 ? 0.3482 0.4203 0.3325 0.0144  0.0080  0.0344  469 ASP B N   
8914 C CA  . ASP B 469 ? 0.3522 0.4250 0.3348 0.0147  0.0074  0.0322  469 ASP B CA  
8915 C C   . ASP B 469 ? 0.3743 0.4431 0.3507 0.0087  0.0074  0.0263  469 ASP B C   
8916 O O   . ASP B 469 ? 0.3840 0.4428 0.3594 0.0083  0.0064  0.0243  469 ASP B O   
8917 C CB  . ASP B 469 ? 0.3554 0.4445 0.3380 0.0180  0.0082  0.0340  469 ASP B CB  
8918 C CG  . ASP B 469 ? 0.3697 0.4590 0.3564 0.0257  0.0086  0.0400  469 ASP B CG  
8919 O OD1 . ASP B 469 ? 0.3647 0.4402 0.3540 0.0274  0.0082  0.0422  469 ASP B OD1 
8920 O OD2 . ASP B 469 ? 0.3722 0.4757 0.3586 0.0301  0.0096  0.0425  469 ASP B OD2 
8921 N N   . ALA B 470 ? 0.3593 0.4348 0.3303 0.0036  0.0089  0.0235  470 ALA B N   
8922 C CA  . ALA B 470 ? 0.3617 0.4310 0.3245 -0.0027 0.0099  0.0180  470 ALA B CA  
8923 C C   . ALA B 470 ? 0.3464 0.3976 0.3075 -0.0024 0.0094  0.0171  470 ALA B C   
8924 O O   . ALA B 470 ? 0.3636 0.4069 0.3202 -0.0045 0.0093  0.0139  470 ALA B O   
8925 C CB  . ALA B 470 ? 0.3605 0.4369 0.3165 -0.0087 0.0122  0.0153  470 ALA B CB  
8926 N N   . MET B 471 ? 0.3338 0.3800 0.2986 0.0005  0.0089  0.0201  471 MET B N   
8927 C CA  . MET B 471 ? 0.3270 0.3596 0.2908 0.0015  0.0082  0.0196  471 MET B CA  
8928 C C   . MET B 471 ? 0.3453 0.3720 0.3143 0.0045  0.0057  0.0205  471 MET B C   
8929 O O   . MET B 471 ? 0.3268 0.3434 0.2928 0.0045  0.0051  0.0185  471 MET B O   
8930 C CB  . MET B 471 ? 0.3274 0.3591 0.2935 0.0036  0.0086  0.0225  471 MET B CB  
8931 C CG  . MET B 471 ? 0.3277 0.3605 0.2859 0.0008  0.0114  0.0209  471 MET B CG  
8932 S SD  . MET B 471 ? 0.3483 0.3706 0.2916 -0.0047 0.0142  0.0148  471 MET B SD  
8933 C CE  . MET B 471 ? 0.3188 0.3256 0.2594 -0.0007 0.0137  0.0148  471 MET B CE  
8934 N N   . ILE B 472 ? 0.3329 0.3651 0.3084 0.0073  0.0046  0.0233  472 ILE B N   
8935 C CA  . ILE B 472 ? 0.3381 0.3643 0.3163 0.0094  0.0029  0.0233  472 ILE B CA  
8936 C C   . ILE B 472 ? 0.3643 0.3879 0.3366 0.0071  0.0029  0.0190  472 ILE B C   
8937 O O   . ILE B 472 ? 0.3513 0.3655 0.3222 0.0071  0.0017  0.0172  472 ILE B O   
8938 C CB  . ILE B 472 ? 0.3505 0.3818 0.3336 0.0132  0.0027  0.0270  472 ILE B CB  
8939 C CG1 . ILE B 472 ? 0.3492 0.3807 0.3377 0.0153  0.0030  0.0315  472 ILE B CG1 
8940 C CG2 . ILE B 472 ? 0.3438 0.3676 0.3272 0.0151  0.0015  0.0261  472 ILE B CG2 
8941 C CD1 . ILE B 472 ? 0.3541 0.3756 0.3459 0.0149  0.0015  0.0322  472 ILE B CD1 
8942 N N   . CYS B 473 ? 0.3558 0.3888 0.3245 0.0049  0.0045  0.0174  473 CYS B N   
8943 C CA  . CYS B 473 ? 0.3715 0.4032 0.3339 0.0016  0.0051  0.0132  473 CYS B CA  
8944 C C   . CYS B 473 ? 0.3704 0.3900 0.3254 -0.0017 0.0059  0.0099  473 CYS B C   
8945 O O   . CYS B 473 ? 0.4003 0.4124 0.3519 -0.0022 0.0055  0.0076  473 CYS B O   
8946 C CB  . CYS B 473 ? 0.3948 0.4408 0.3541 -0.0018 0.0069  0.0117  473 CYS B CB  
8947 S SG  . CYS B 473 ? 0.4887 0.5512 0.4545 0.0036  0.0064  0.0154  473 CYS B SG  
8948 N N   . VAL B 474 ? 0.3596 0.3769 0.3111 -0.0034 0.0074  0.0099  474 VAL B N   
8949 C CA  . VAL B 474 ? 0.3721 0.3762 0.3148 -0.0050 0.0089  0.0074  474 VAL B CA  
8950 C C   . VAL B 474 ? 0.3661 0.3614 0.3123 -0.0005 0.0065  0.0087  474 VAL B C   
8951 O O   . VAL B 474 ? 0.3713 0.3562 0.3107 -0.0005 0.0070  0.0064  474 VAL B O   
8952 C CB  . VAL B 474 ? 0.3776 0.3806 0.3159 -0.0061 0.0111  0.0080  474 VAL B CB  
8953 C CG1 . VAL B 474 ? 0.3539 0.3421 0.2834 -0.0048 0.0126  0.0067  474 VAL B CG1 
8954 C CG2 . VAL B 474 ? 0.3803 0.3906 0.3123 -0.0122 0.0139  0.0054  474 VAL B CG2 
8955 N N   . ALA B 475 ? 0.3441 0.3436 0.3001 0.0030  0.0042  0.0123  475 ALA B N   
8956 C CA  . ALA B 475 ? 0.3597 0.3534 0.3196 0.0061  0.0018  0.0133  475 ALA B CA  
8957 C C   . ALA B 475 ? 0.3648 0.3545 0.3249 0.0064  0.0002  0.0114  475 ALA B C   
8958 O O   . ALA B 475 ? 0.3974 0.3799 0.3547 0.0075  -0.0008 0.0099  475 ALA B O   
8959 C CB  . ALA B 475 ? 0.3280 0.3269 0.2974 0.0083  0.0004  0.0173  475 ALA B CB  
8960 N N   . TYR B 476 ? 0.3707 0.3658 0.3329 0.0059  0.0001  0.0114  476 TYR B N   
8961 C CA  . TYR B 476 ? 0.3627 0.3544 0.3239 0.0064  -0.0009 0.0094  476 TYR B CA  
8962 C C   . TYR B 476 ? 0.3747 0.3603 0.3264 0.0038  0.0005  0.0056  476 TYR B C   
8963 O O   . TYR B 476 ? 0.3534 0.3319 0.3029 0.0048  -0.0006 0.0038  476 TYR B O   
8964 C CB  . TYR B 476 ? 0.3450 0.3448 0.3091 0.0074  -0.0005 0.0105  476 TYR B CB  
8965 C CG  . TYR B 476 ? 0.3555 0.3550 0.3264 0.0111  -0.0019 0.0137  476 TYR B CG  
8966 C CD1 . TYR B 476 ? 0.3636 0.3541 0.3361 0.0123  -0.0039 0.0134  476 TYR B CD1 
8967 C CD2 . TYR B 476 ? 0.3522 0.3602 0.3267 0.0132  -0.0009 0.0171  476 TYR B CD2 
8968 C CE1 . TYR B 476 ? 0.3778 0.3657 0.3545 0.0147  -0.0045 0.0160  476 TYR B CE1 
8969 C CE2 . TYR B 476 ? 0.3685 0.3735 0.3470 0.0168  -0.0013 0.0203  476 TYR B CE2 
8970 C CZ  . TYR B 476 ? 0.3803 0.3743 0.3595 0.0170  -0.0029 0.0196  476 TYR B CZ  
8971 O OH  . TYR B 476 ? 0.3943 0.3830 0.3756 0.0194  -0.0027 0.0223  476 TYR B OH  
8972 N N   . LYS B 477 ? 0.3571 0.3447 0.3023 0.0002  0.0033  0.0041  477 LYS B N   
8973 C CA  . LYS B 477 ? 0.3845 0.3636 0.3187 -0.0029 0.0056  0.0005  477 LYS B CA  
8974 C C   . LYS B 477 ? 0.3913 0.3584 0.3210 -0.0001 0.0053  0.0005  477 LYS B C   
8975 O O   . LYS B 477 ? 0.4101 0.3685 0.3333 0.0002  0.0057  -0.0014 477 LYS B O   
8976 C CB  . LYS B 477 ? 0.4062 0.3885 0.3328 -0.0087 0.0092  -0.0013 477 LYS B CB  
8977 C CG  . LYS B 477 ? 0.4395 0.4121 0.3534 -0.0132 0.0122  -0.0053 477 LYS B CG  
8978 C CD  . LYS B 477 ? 0.4740 0.4506 0.3796 -0.0209 0.0160  -0.0080 477 LYS B CD  
8979 C CE  . LYS B 477 ? 0.4920 0.4545 0.3825 -0.0259 0.0199  -0.0119 477 LYS B CE  
8980 N NZ  . LYS B 477 ? 0.4977 0.4629 0.3783 -0.0355 0.0241  -0.0154 477 LYS B NZ  
8981 N N   . PHE B 478 ? 0.3780 0.3461 0.3114 0.0024  0.0048  0.0031  478 PHE B N   
8982 C CA  . PHE B 478 ? 0.3742 0.3348 0.3049 0.0065  0.0043  0.0039  478 PHE B CA  
8983 C C   . PHE B 478 ? 0.3766 0.3357 0.3117 0.0093  0.0010  0.0038  478 PHE B C   
8984 O O   . PHE B 478 ? 0.3560 0.3074 0.2846 0.0116  0.0011  0.0026  478 PHE B O   
8985 C CB  . PHE B 478 ? 0.3670 0.3331 0.3037 0.0090  0.0037  0.0072  478 PHE B CB  
8986 C CG  . PHE B 478 ? 0.3611 0.3232 0.2960 0.0139  0.0031  0.0083  478 PHE B CG  
8987 C CD1 . PHE B 478 ? 0.3618 0.3157 0.2853 0.0160  0.0064  0.0080  478 PHE B CD1 
8988 C CD2 . PHE B 478 ? 0.3600 0.3267 0.3035 0.0164  -0.0005 0.0097  478 PHE B CD2 
8989 C CE1 . PHE B 478 ? 0.3719 0.3237 0.2930 0.0220  0.0061  0.0095  478 PHE B CE1 
8990 C CE2 . PHE B 478 ? 0.3703 0.3367 0.3124 0.0211  -0.0012 0.0108  478 PHE B CE2 
8991 C CZ  . PHE B 478 ? 0.3740 0.3337 0.3052 0.0246  0.0019  0.0109  478 PHE B CZ  
8992 N N   . ASP B 479 ? 0.3853 0.3512 0.3305 0.0092  -0.0016 0.0050  479 ASP B N   
8993 C CA  . ASP B 479 ? 0.3716 0.3359 0.3208 0.0111  -0.0047 0.0046  479 ASP B CA  
8994 C C   . ASP B 479 ? 0.3861 0.3441 0.3285 0.0104  -0.0042 0.0015  479 ASP B C   
8995 O O   . ASP B 479 ? 0.3608 0.3138 0.3007 0.0125  -0.0058 0.0003  479 ASP B O   
8996 C CB  . ASP B 479 ? 0.3841 0.3541 0.3430 0.0107  -0.0066 0.0065  479 ASP B CB  
8997 C CG  . ASP B 479 ? 0.3896 0.3565 0.3513 0.0115  -0.0094 0.0055  479 ASP B CG  
8998 O OD1 . ASP B 479 ? 0.3946 0.3613 0.3580 0.0125  -0.0114 0.0056  479 ASP B OD1 
8999 O OD2 . ASP B 479 ? 0.4243 0.3897 0.3858 0.0112  -0.0096 0.0044  479 ASP B OD2 
9000 N N   . ALA B 480 ? 0.3856 0.3450 0.3245 0.0074  -0.0021 0.0001  480 ALA B N   
9001 C CA  . ALA B 480 ? 0.4038 0.3586 0.3358 0.0060  -0.0010 -0.0027 480 ALA B CA  
9002 C C   . ALA B 480 ? 0.4320 0.3761 0.3521 0.0059  0.0012  -0.0046 480 ALA B C   
9003 O O   . ALA B 480 ? 0.4514 0.3889 0.3664 0.0070  0.0009  -0.0064 480 ALA B O   
9004 C CB  . ALA B 480 ? 0.3947 0.3567 0.3261 0.0023  0.0009  -0.0036 480 ALA B CB  
9005 N N   . ALA B 481 ? 0.4281 0.3692 0.3426 0.0051  0.0039  -0.0040 481 ALA B N   
9006 C CA  . ALA B 481 ? 0.4611 0.3898 0.3629 0.0067  0.0067  -0.0050 481 ALA B CA  
9007 C C   . ALA B 481 ? 0.4679 0.3942 0.3716 0.0131  0.0038  -0.0036 481 ALA B C   
9008 O O   . ALA B 481 ? 0.5121 0.4292 0.4066 0.0157  0.0048  -0.0048 481 ALA B O   
9009 C CB  . ALA B 481 ? 0.4291 0.3546 0.3243 0.0054  0.0103  -0.0044 481 ALA B CB  
9010 N N   . MET B 482 ? 0.4484 0.3838 0.3637 0.0154  0.0004  -0.0013 482 MET B N   
9011 C CA  . MET B 482 ? 0.4823 0.4191 0.4004 0.0206  -0.0024 -0.0002 482 MET B CA  
9012 C C   . MET B 482 ? 0.4856 0.4200 0.4033 0.0211  -0.0047 -0.0022 482 MET B C   
9013 O O   . MET B 482 ? 0.5011 0.4322 0.4140 0.0253  -0.0054 -0.0024 482 MET B O   
9014 C CB  . MET B 482 ? 0.4705 0.4187 0.4017 0.0209  -0.0056 0.0022  482 MET B CB  
9015 C CG  . MET B 482 ? 0.4547 0.4066 0.3868 0.0221  -0.0040 0.0047  482 MET B CG  
9016 S SD  . MET B 482 ? 0.4786 0.4230 0.3978 0.0285  -0.0011 0.0054  482 MET B SD  
9017 C CE  . MET B 482 ? 0.5412 0.4742 0.4479 0.0247  0.0044  0.0038  482 MET B CE  
9018 N N   . MET B 483 ? 0.4932 0.4301 0.4160 0.0175  -0.0058 -0.0035 483 MET B N   
9019 C CA  . MET B 483 ? 0.4957 0.4304 0.4184 0.0180  -0.0079 -0.0055 483 MET B CA  
9020 C C   . MET B 483 ? 0.5065 0.4311 0.4163 0.0187  -0.0051 -0.0075 483 MET B C   
9021 O O   . MET B 483 ? 0.4923 0.4131 0.3982 0.0219  -0.0065 -0.0084 483 MET B O   
9022 C CB  . MET B 483 ? 0.5048 0.4435 0.4341 0.0150  -0.0089 -0.0061 483 MET B CB  
9023 C CG  . MET B 483 ? 0.5596 0.5052 0.4999 0.0146  -0.0114 -0.0041 483 MET B CG  
9024 S SD  . MET B 483 ? 0.5819 0.5299 0.5273 0.0164  -0.0153 -0.0038 483 MET B SD  
9025 C CE  . MET B 483 ? 0.6446 0.5992 0.5938 0.0170  -0.0145 -0.0005 483 MET B CE  
9026 N N   . ALA B 484 ? 0.5139 0.4342 0.4164 0.0155  -0.0010 -0.0081 484 ALA B N   
9027 C CA  . ALA B 484 ? 0.5252 0.4342 0.4137 0.0150  0.0026  -0.0099 484 ALA B CA  
9028 C C   . ALA B 484 ? 0.5363 0.4368 0.4156 0.0209  0.0038  -0.0088 484 ALA B C   
9029 O O   . ALA B 484 ? 0.5445 0.4353 0.4132 0.0231  0.0055  -0.0098 484 ALA B O   
9030 C CB  . ALA B 484 ? 0.5171 0.4239 0.3993 0.0089  0.0071  -0.0111 484 ALA B CB  
9031 N N   . LEU B 485 ? 0.5435 0.4476 0.4259 0.0238  0.0034  -0.0064 485 LEU B N   
9032 C CA  . LEU B 485 ? 0.5354 0.4332 0.4088 0.0308  0.0049  -0.0047 485 LEU B CA  
9033 C C   . LEU B 485 ? 0.5387 0.4409 0.4154 0.0360  0.0008  -0.0046 485 LEU B C   
9034 O O   . LEU B 485 ? 0.5244 0.4189 0.3902 0.0417  0.0023  -0.0043 485 LEU B O   
9035 C CB  . LEU B 485 ? 0.5103 0.4141 0.3880 0.0331  0.0049  -0.0020 485 LEU B CB  
9036 C CG  . LEU B 485 ? 0.5471 0.4404 0.4120 0.0347  0.0104  -0.0010 485 LEU B CG  
9037 C CD1 . LEU B 485 ? 0.5763 0.4560 0.4281 0.0284  0.0158  -0.0036 485 LEU B CD1 
9038 C CD2 . LEU B 485 ? 0.5140 0.4169 0.3877 0.0342  0.0097  0.0010  485 LEU B CD2 
9039 N N   . ARG B 486 ? 0.5360 0.4502 0.4271 0.0338  -0.0040 -0.0049 486 ARG B N   
9040 C CA  . ARG B 486 ? 0.5444 0.4645 0.4398 0.0369  -0.0083 -0.0054 486 ARG B CA  
9041 C C   . ARG B 486 ? 0.5292 0.4413 0.4174 0.0367  -0.0080 -0.0080 486 ARG B C   
9042 O O   . ARG B 486 ? 0.5435 0.4541 0.4259 0.0419  -0.0089 -0.0081 486 ARG B O   
9043 C CB  . ARG B 486 ? 0.5803 0.5124 0.4909 0.0331  -0.0127 -0.0055 486 ARG B CB  
9044 C CG  . ARG B 486 ? 0.6293 0.5681 0.5446 0.0346  -0.0173 -0.0066 486 ARG B CG  
9045 C CD  . ARG B 486 ? 0.7460 0.6922 0.6599 0.0407  -0.0185 -0.0048 486 ARG B CD  
9046 N NE  . ARG B 486 ? 0.8341 0.7892 0.7522 0.0413  -0.0229 -0.0063 486 ARG B NE  
9047 C CZ  . ARG B 486 ? 0.9561 0.9229 0.8757 0.0457  -0.0251 -0.0050 486 ARG B CZ  
9048 N NH1 . ARG B 486 ? 1.0059 0.9765 0.9231 0.0508  -0.0231 -0.0019 486 ARG B NH1 
9049 N NH2 . ARG B 486 ? 1.0211 0.9970 0.9444 0.0450  -0.0293 -0.0069 486 ARG B NH2 
9050 N N   . THR B 487 ? 0.4998 0.4083 0.3883 0.0312  -0.0066 -0.0098 487 THR B N   
9051 C CA  . THR B 487 ? 0.5001 0.4039 0.3845 0.0303  -0.0069 -0.0123 487 THR B CA  
9052 C C   . THR B 487 ? 0.5241 0.4145 0.3927 0.0310  -0.0020 -0.0131 487 THR B C   
9053 O O   . THR B 487 ? 0.5583 0.4438 0.4208 0.0330  -0.0022 -0.0145 487 THR B O   
9054 C CB  . THR B 487 ? 0.4873 0.3953 0.3796 0.0249  -0.0079 -0.0139 487 THR B CB  
9055 O OG1 . THR B 487 ? 0.4823 0.3894 0.3730 0.0205  -0.0043 -0.0136 487 THR B OG1 
9056 C CG2 . THR B 487 ? 0.4684 0.3863 0.3741 0.0242  -0.0124 -0.0133 487 THR B CG2 
9057 N N   . SER B 488 ? 0.5241 0.4078 0.3852 0.0288  0.0025  -0.0125 488 SER B N   
9058 C CA  . SER B 488 ? 0.5313 0.4001 0.3757 0.0278  0.0081  -0.0135 488 SER B CA  
9059 C C   . SER B 488 ? 0.5603 0.4172 0.3906 0.0338  0.0119  -0.0116 488 SER B C   
9060 O O   . SER B 488 ? 0.5780 0.4217 0.3936 0.0367  0.0154  -0.0118 488 SER B O   
9061 C CB  . SER B 488 ? 0.5254 0.3932 0.3682 0.0191  0.0117  -0.0152 488 SER B CB  
9062 O OG  . SER B 488 ? 0.5649 0.4172 0.3902 0.0168  0.0178  -0.0163 488 SER B OG  
9063 N N   . PHE B 489 ? 0.5257 0.3864 0.3593 0.0360  0.0119  -0.0094 489 PHE B N   
9064 C CA  . PHE B 489 ? 0.5563 0.4062 0.3762 0.0434  0.0156  -0.0071 489 PHE B CA  
9065 C C   . PHE B 489 ? 0.5754 0.4338 0.3993 0.0529  0.0114  -0.0050 489 PHE B C   
9066 O O   . PHE B 489 ? 0.5784 0.4296 0.3904 0.0616  0.0140  -0.0027 489 PHE B O   
9067 C CB  . PHE B 489 ? 0.5241 0.3750 0.3451 0.0422  0.0176  -0.0056 489 PHE B CB  
9068 C CG  . PHE B 489 ? 0.5097 0.3512 0.3232 0.0332  0.0227  -0.0077 489 PHE B CG  
9069 C CD1 . PHE B 489 ? 0.4899 0.3422 0.3153 0.0243  0.0207  -0.0097 489 PHE B CD1 
9070 C CD2 . PHE B 489 ? 0.5117 0.3349 0.3061 0.0338  0.0297  -0.0076 489 PHE B CD2 
9071 C CE1 . PHE B 489 ? 0.4818 0.3290 0.3009 0.0157  0.0251  -0.0118 489 PHE B CE1 
9072 C CE2 . PHE B 489 ? 0.5355 0.3511 0.3226 0.0241  0.0344  -0.0100 489 PHE B CE2 
9073 C CZ  . PHE B 489 ? 0.4976 0.3267 0.2976 0.0148  0.0319  -0.0122 489 PHE B CZ  
9074 N N   . LEU B 490 ? 0.5966 0.4709 0.4370 0.0513  0.0051  -0.0058 490 LEU B N   
9075 C CA  . LEU B 490 ? 0.6389 0.5253 0.4857 0.0579  0.0002  -0.0046 490 LEU B CA  
9076 C C   . LEU B 490 ? 0.6587 0.5528 0.5069 0.0646  0.0000  -0.0013 490 LEU B C   
9077 O O   . LEU B 490 ? 0.6738 0.5680 0.5139 0.0739  0.0004  0.0006  490 LEU B O   
9078 C CB  . LEU B 490 ? 0.6356 0.5146 0.4708 0.0636  0.0008  -0.0051 490 LEU B CB  
9079 C CG  . LEU B 490 ? 0.6546 0.5266 0.4874 0.0581  0.0012  -0.0082 490 LEU B CG  
9080 C CD1 . LEU B 490 ? 0.6254 0.4885 0.4443 0.0650  0.0027  -0.0081 490 LEU B CD1 
9081 C CD2 . LEU B 490 ? 0.6390 0.5245 0.4886 0.0524  -0.0045 -0.0104 490 LEU B CD2 
9082 N N   . VAL B 491 ? 0.6640 0.5664 0.5229 0.0606  -0.0010 -0.0004 491 VAL B N   
9083 C CA  . VAL B 491 ? 0.7061 0.6136 0.5642 0.0668  0.0001  0.0027  491 VAL B CA  
9084 C C   . VAL B 491 ? 0.7488 0.6745 0.6144 0.0737  -0.0043 0.0048  491 VAL B C   
9085 O O   . VAL B 491 ? 0.8064 0.7309 0.6616 0.0838  -0.0022 0.0074  491 VAL B O   
9086 C CB  . VAL B 491 ? 0.6763 0.5842 0.5397 0.0611  0.0019  0.0033  491 VAL B CB  
9087 C CG1 . VAL B 491 ? 0.6425 0.5621 0.5110 0.0664  0.0011  0.0066  491 VAL B CG1 
9088 C CG2 . VAL B 491 ? 0.6490 0.5371 0.4965 0.0590  0.0086  0.0025  491 VAL B CG2 
9089 N N   . ASN B 492 ? 0.7363 0.6785 0.6185 0.0686  -0.0099 0.0037  492 ASN B N   
9090 C CA  . ASN B 492 ? 0.8075 0.7701 0.6983 0.0728  -0.0143 0.0053  492 ASN B CA  
9091 C C   . ASN B 492 ? 0.8208 0.7937 0.7162 0.0757  -0.0135 0.0085  492 ASN B C   
9092 O O   . ASN B 492 ? 0.8642 0.8536 0.7740 0.0711  -0.0173 0.0087  492 ASN B O   
9093 C CB  . ASN B 492 ? 0.8234 0.7885 0.7046 0.0825  -0.0148 0.0060  492 ASN B CB  
9094 C CG  . ASN B 492 ? 0.9039 0.8604 0.7806 0.0802  -0.0158 0.0029  492 ASN B CG  
9095 O OD1 . ASN B 492 ? 0.9451 0.9011 0.8304 0.0712  -0.0183 -0.0001 492 ASN B OD1 
9096 N ND2 . ASN B 492 ? 0.9034 0.8527 0.7658 0.0892  -0.0136 0.0038  492 ASN B ND2 
9097 N N   . ASP B 493 ? 0.7951 0.7575 0.6775 0.0831  -0.0082 0.0111  493 ASP B N   
9098 C CA  . ASP B 493 ? 0.7627 0.7338 0.6473 0.0874  -0.0068 0.0145  493 ASP B CA  
9099 C C   . ASP B 493 ? 0.7247 0.6844 0.6085 0.0817  -0.0030 0.0146  493 ASP B C   
9100 O O   . ASP B 493 ? 0.7007 0.6416 0.5694 0.0843  0.0025  0.0148  493 ASP B O   
9101 C CB  . ASP B 493 ? 0.7834 0.7525 0.6532 0.1015  -0.0033 0.0179  493 ASP B CB  
9102 C CG  . ASP B 493 ? 0.8387 0.8190 0.7106 0.1075  -0.0019 0.0216  493 ASP B CG  
9103 O OD1 . ASP B 493 ? 0.7995 0.7910 0.6855 0.1003  -0.0041 0.0217  493 ASP B OD1 
9104 O OD2 . ASP B 493 ? 0.8997 0.8772 0.7582 0.1201  0.0016  0.0248  493 ASP B OD2 
9105 N N   . PHE B 494 ? 0.6655 0.6369 0.5648 0.0741  -0.0059 0.0144  494 PHE B N   
9106 C CA  . PHE B 494 ? 0.6719 0.6347 0.5723 0.0675  -0.0032 0.0140  494 PHE B CA  
9107 C C   . PHE B 494 ? 0.6692 0.6351 0.5680 0.0716  -0.0003 0.0171  494 PHE B C   
9108 O O   . PHE B 494 ? 0.6490 0.6120 0.5511 0.0660  0.0011  0.0170  494 PHE B O   
9109 C CB  . PHE B 494 ? 0.6589 0.6287 0.5745 0.0571  -0.0071 0.0120  494 PHE B CB  
9110 C CG  . PHE B 494 ? 0.6721 0.6334 0.5860 0.0525  -0.0083 0.0087  494 PHE B CG  
9111 C CD1 . PHE B 494 ? 0.6627 0.6100 0.5704 0.0479  -0.0052 0.0068  494 PHE B CD1 
9112 C CD2 . PHE B 494 ? 0.6652 0.6337 0.5835 0.0528  -0.0124 0.0073  494 PHE B CD2 
9113 C CE1 . PHE B 494 ? 0.7184 0.6593 0.6246 0.0442  -0.0060 0.0039  494 PHE B CE1 
9114 C CE2 . PHE B 494 ? 0.6941 0.6545 0.6101 0.0493  -0.0132 0.0042  494 PHE B CE2 
9115 C CZ  . PHE B 494 ? 0.7017 0.6484 0.6119 0.0452  -0.0100 0.0027  494 PHE B CZ  
9116 N N   . GLY B 495 ? 0.6526 0.6242 0.5454 0.0820  0.0007  0.0200  495 GLY B N   
9117 C CA  . GLY B 495 ? 0.6783 0.6541 0.5690 0.0875  0.0035  0.0232  495 GLY B CA  
9118 C C   . GLY B 495 ? 0.6740 0.6310 0.5536 0.0856  0.0092  0.0229  495 GLY B C   
9119 O O   . GLY B 495 ? 0.6656 0.6281 0.5516 0.0826  0.0097  0.0240  495 GLY B O   
9120 N N   . PHE B 496 ? 0.6226 0.5576 0.4850 0.0867  0.0136  0.0211  496 PHE B N   
9121 C CA  . PHE B 496 ? 0.5672 0.4821 0.4156 0.0840  0.0198  0.0200  496 PHE B CA  
9122 C C   . PHE B 496 ? 0.5350 0.4526 0.3944 0.0717  0.0184  0.0178  496 PHE B C   
9123 O O   . PHE B 496 ? 0.5371 0.4443 0.3887 0.0686  0.0226  0.0171  496 PHE B O   
9124 C CB  . PHE B 496 ? 0.5698 0.4609 0.3983 0.0851  0.0245  0.0178  496 PHE B CB  
9125 C CG  . PHE B 496 ? 0.5375 0.4259 0.3712 0.0753  0.0221  0.0141  496 PHE B CG  
9126 C CD1 . PHE B 496 ? 0.5223 0.4192 0.3629 0.0767  0.0175  0.0137  496 PHE B CD1 
9127 C CD2 . PHE B 496 ? 0.5268 0.4058 0.3585 0.0647  0.0243  0.0110  496 PHE B CD2 
9128 C CE1 . PHE B 496 ? 0.5319 0.4262 0.3768 0.0684  0.0155  0.0103  496 PHE B CE1 
9129 C CE2 . PHE B 496 ? 0.5396 0.4183 0.3763 0.0564  0.0221  0.0079  496 PHE B CE2 
9130 C CZ  . PHE B 496 ? 0.5319 0.4174 0.3749 0.0586  0.0178  0.0076  496 PHE B CZ  
9131 N N   . ILE B 497 ? 0.5118 0.4429 0.3881 0.0652  0.0128  0.0166  497 ILE B N   
9132 C CA  . ILE B 497 ? 0.4999 0.4349 0.3868 0.0549  0.0114  0.0151  497 ILE B CA  
9133 C C   . ILE B 497 ? 0.4744 0.4188 0.3685 0.0544  0.0117  0.0174  497 ILE B C   
9134 O O   . ILE B 497 ? 0.4508 0.3920 0.3451 0.0482  0.0135  0.0164  497 ILE B O   
9135 C CB  . ILE B 497 ? 0.5082 0.4539 0.4098 0.0495  0.0058  0.0137  497 ILE B CB  
9136 C CG1 . ILE B 497 ? 0.5055 0.4390 0.4001 0.0454  0.0066  0.0103  497 ILE B CG1 
9137 C CG2 . ILE B 497 ? 0.4900 0.4479 0.4071 0.0430  0.0031  0.0144  497 ILE B CG2 
9138 C CD1 . ILE B 497 ? 0.5280 0.4548 0.4129 0.0517  0.0069  0.0099  497 ILE B CD1 
9139 N N   . TRP B 498 ? 0.4513 0.4081 0.3505 0.0611  0.0103  0.0207  498 TRP B N   
9140 C CA  . TRP B 498 ? 0.4317 0.3991 0.3385 0.0611  0.0105  0.0233  498 TRP B CA  
9141 C C   . TRP B 498 ? 0.4452 0.3993 0.3393 0.0611  0.0160  0.0230  498 TRP B C   
9142 O O   . TRP B 498 ? 0.4046 0.3618 0.3044 0.0552  0.0162  0.0229  498 TRP B O   
9143 C CB  . TRP B 498 ? 0.4350 0.4174 0.3461 0.0695  0.0090  0.0268  498 TRP B CB  
9144 C CG  . TRP B 498 ? 0.4180 0.4117 0.3368 0.0693  0.0095  0.0296  498 TRP B CG  
9145 C CD1 . TRP B 498 ? 0.4227 0.4188 0.3350 0.0778  0.0127  0.0326  498 TRP B CD1 
9146 C CD2 . TRP B 498 ? 0.4000 0.4033 0.3334 0.0607  0.0071  0.0299  498 TRP B CD2 
9147 N NE1 . TRP B 498 ? 0.4242 0.4314 0.3467 0.0744  0.0122  0.0345  498 TRP B NE1 
9148 C CE2 . TRP B 498 ? 0.4073 0.4188 0.3425 0.0642  0.0090  0.0331  498 TRP B CE2 
9149 C CE3 . TRP B 498 ? 0.3864 0.3915 0.3302 0.0515  0.0040  0.0281  498 TRP B CE3 
9150 C CZ2 . TRP B 498 ? 0.4033 0.4246 0.3506 0.0582  0.0077  0.0345  498 TRP B CZ2 
9151 C CZ3 . TRP B 498 ? 0.3799 0.3939 0.3349 0.0462  0.0031  0.0297  498 TRP B CZ3 
9152 C CH2 . TRP B 498 ? 0.3766 0.3985 0.3335 0.0492  0.0048  0.0328  498 TRP B CH2 
9153 N N   . LEU B 499 ? 0.4815 0.4196 0.3569 0.0678  0.0209  0.0228  499 LEU B N   
9154 C CA  . LEU B 499 ? 0.4950 0.4188 0.3560 0.0679  0.0268  0.0223  499 LEU B CA  
9155 C C   . LEU B 499 ? 0.4718 0.3840 0.3280 0.0572  0.0287  0.0182  499 LEU B C   
9156 O O   . LEU B 499 ? 0.4797 0.3896 0.3334 0.0530  0.0312  0.0176  499 LEU B O   
9157 C CB  . LEU B 499 ? 0.5462 0.4540 0.3863 0.0789  0.0324  0.0235  499 LEU B CB  
9158 C CG  . LEU B 499 ? 0.5689 0.4894 0.4115 0.0902  0.0324  0.0281  499 LEU B CG  
9159 C CD1 . LEU B 499 ? 0.5863 0.4926 0.4085 0.1031  0.0373  0.0298  499 LEU B CD1 
9160 C CD2 . LEU B 499 ? 0.5555 0.4804 0.4006 0.0888  0.0342  0.0294  499 LEU B CD2 
9161 N N   . VAL B 500 ? 0.4498 0.3563 0.3049 0.0527  0.0275  0.0155  500 VAL B N   
9162 C CA  . VAL B 500 ? 0.4445 0.3446 0.2974 0.0419  0.0286  0.0116  500 VAL B CA  
9163 C C   . VAL B 500 ? 0.4452 0.3630 0.3165 0.0353  0.0246  0.0121  500 VAL B C   
9164 O O   . VAL B 500 ? 0.4538 0.3707 0.3229 0.0290  0.0267  0.0106  500 VAL B O   
9165 C CB  . VAL B 500 ? 0.4551 0.3491 0.3056 0.0388  0.0275  0.0090  500 VAL B CB  
9166 C CG1 . VAL B 500 ? 0.4250 0.3156 0.2738 0.0277  0.0287  0.0051  500 VAL B CG1 
9167 C CG2 . VAL B 500 ? 0.4589 0.3347 0.2905 0.0460  0.0317  0.0089  500 VAL B CG2 
9168 N N   . LEU B 501 ? 0.4103 0.3437 0.2985 0.0367  0.0191  0.0142  501 LEU B N   
9169 C CA  . LEU B 501 ? 0.4097 0.3585 0.3144 0.0321  0.0156  0.0155  501 LEU B CA  
9170 C C   . LEU B 501 ? 0.4151 0.3682 0.3201 0.0328  0.0177  0.0175  501 LEU B C   
9171 O O   . LEU B 501 ? 0.4226 0.3790 0.3304 0.0269  0.0182  0.0167  501 LEU B O   
9172 C CB  . LEU B 501 ? 0.3807 0.3433 0.3010 0.0341  0.0102  0.0176  501 LEU B CB  
9173 C CG  . LEU B 501 ? 0.3789 0.3548 0.3149 0.0291  0.0071  0.0191  501 LEU B CG  
9174 C CD1 . LEU B 501 ? 0.3765 0.3500 0.3125 0.0224  0.0076  0.0168  501 LEU B CD1 
9175 C CD2 . LEU B 501 ? 0.3572 0.3433 0.3061 0.0293  0.0025  0.0204  501 LEU B CD2 
9176 N N   . SER B 502 ? 0.4305 0.3845 0.3324 0.0404  0.0190  0.0202  502 SER B N   
9177 C CA  . SER B 502 ? 0.4571 0.4141 0.3575 0.0421  0.0215  0.0222  502 SER B CA  
9178 C C   . SER B 502 ? 0.4556 0.3994 0.3417 0.0377  0.0264  0.0193  502 SER B C   
9179 O O   . SER B 502 ? 0.4567 0.4069 0.3471 0.0337  0.0268  0.0197  502 SER B O   
9180 C CB  . SER B 502 ? 0.4821 0.4406 0.3781 0.0522  0.0229  0.0253  502 SER B CB  
9181 O OG  . SER B 502 ? 0.5536 0.5296 0.4652 0.0547  0.0182  0.0282  502 SER B OG  
9182 N N   . SER B 503 ? 0.4625 0.3878 0.3308 0.0383  0.0305  0.0166  503 SER B N   
9183 C CA  . SER B 503 ? 0.4788 0.3898 0.3316 0.0317  0.0356  0.0128  503 SER B CA  
9184 C C   . SER B 503 ? 0.4598 0.3793 0.3209 0.0212  0.0335  0.0102  503 SER B C   
9185 O O   . SER B 503 ? 0.4541 0.3729 0.3103 0.0155  0.0361  0.0084  503 SER B O   
9186 C CB  . SER B 503 ? 0.5248 0.4143 0.3581 0.0324  0.0400  0.0099  503 SER B CB  
9187 O OG  . SER B 503 ? 0.6795 0.5552 0.4969 0.0411  0.0448  0.0114  503 SER B OG  
9188 N N   . THR B 504 ? 0.4666 0.3941 0.3392 0.0188  0.0292  0.0100  504 THR B N   
9189 C CA  . THR B 504 ? 0.4597 0.3963 0.3400 0.0103  0.0273  0.0079  504 THR B CA  
9190 C C   . THR B 504 ? 0.4343 0.3869 0.3273 0.0093  0.0253  0.0105  504 THR B C   
9191 O O   . THR B 504 ? 0.4539 0.4099 0.3442 0.0034  0.0270  0.0088  504 THR B O   
9192 C CB  . THR B 504 ? 0.4643 0.4055 0.3538 0.0097  0.0233  0.0076  504 THR B CB  
9193 O OG1 . THR B 504 ? 0.4667 0.3927 0.3435 0.0112  0.0255  0.0055  504 THR B OG1 
9194 C CG2 . THR B 504 ? 0.4642 0.4142 0.3593 0.0020  0.0220  0.0056  504 THR B CG2 
9195 N N   . VAL B 505 ? 0.4308 0.3935 0.3367 0.0148  0.0219  0.0146  505 VAL B N   
9196 C CA  . VAL B 505 ? 0.4036 0.3803 0.3209 0.0146  0.0204  0.0177  505 VAL B CA  
9197 C C   . VAL B 505 ? 0.4097 0.3832 0.3173 0.0138  0.0245  0.0172  505 VAL B C   
9198 O O   . VAL B 505 ? 0.3820 0.3638 0.2925 0.0096  0.0247  0.0171  505 VAL B O   
9199 C CB  . VAL B 505 ? 0.3965 0.3821 0.3263 0.0203  0.0172  0.0220  505 VAL B CB  
9200 C CG1 . VAL B 505 ? 0.3939 0.3921 0.3335 0.0203  0.0165  0.0254  505 VAL B CG1 
9201 C CG2 . VAL B 505 ? 0.3694 0.3585 0.3087 0.0198  0.0132  0.0220  505 VAL B CG2 
9202 N N   . ARG B 506 ? 0.4140 0.3748 0.3085 0.0183  0.0280  0.0168  506 ARG B N   
9203 C CA  . ARG B 506 ? 0.4291 0.3836 0.3115 0.0177  0.0326  0.0158  506 ARG B CA  
9204 C C   . ARG B 506 ? 0.4167 0.3660 0.2891 0.0080  0.0352  0.0109  506 ARG B C   
9205 O O   . ARG B 506 ? 0.4249 0.3807 0.2971 0.0040  0.0363  0.0103  506 ARG B O   
9206 C CB  . ARG B 506 ? 0.4723 0.4116 0.3401 0.0253  0.0365  0.0163  506 ARG B CB  
9207 C CG  . ARG B 506 ? 0.5099 0.4405 0.3637 0.0263  0.0417  0.0156  506 ARG B CG  
9208 C CD  . ARG B 506 ? 0.5766 0.4846 0.4076 0.0219  0.0474  0.0106  506 ARG B CD  
9209 N NE  . ARG B 506 ? 0.6030 0.5109 0.4281 0.0117  0.0496  0.0067  506 ARG B NE  
9210 C CZ  . ARG B 506 ? 0.6311 0.5260 0.4416 0.0028  0.0531  0.0014  506 ARG B CZ  
9211 N NH1 . ARG B 506 ? 0.6052 0.4849 0.4055 0.0026  0.0550  -0.0005 506 ARG B NH1 
9212 N NH2 . ARG B 506 ? 0.6893 0.5882 0.4959 -0.0065 0.0548  -0.0019 506 ARG B NH2 
9213 N N   . ALA B 507 ? 0.4038 0.3439 0.2691 0.0038  0.0360  0.0074  507 ALA B N   
9214 C CA  . ALA B 507 ? 0.4011 0.3366 0.2555 -0.0063 0.0389  0.0022  507 ALA B CA  
9215 C C   . ALA B 507 ? 0.3888 0.3444 0.2564 -0.0122 0.0357  0.0022  507 ALA B C   
9216 O O   . ALA B 507 ? 0.3893 0.3489 0.2513 -0.0193 0.0378  -0.0004 507 ALA B O   
9217 C CB  . ALA B 507 ? 0.3968 0.3191 0.2418 -0.0092 0.0403  -0.0009 507 ALA B CB  
9218 N N   . TYR B 508 ? 0.3872 0.3553 0.2714 -0.0094 0.0307  0.0051  508 TYR B N   
9219 C CA  . TYR B 508 ? 0.3720 0.3584 0.2678 -0.0132 0.0279  0.0057  508 TYR B CA  
9220 C C   . TYR B 508 ? 0.3657 0.3637 0.2679 -0.0115 0.0275  0.0087  508 TYR B C   
9221 O O   . TYR B 508 ? 0.3731 0.3821 0.2755 -0.0165 0.0279  0.0074  508 TYR B O   
9222 C CB  . TYR B 508 ? 0.3740 0.3671 0.2832 -0.0101 0.0235  0.0079  508 TYR B CB  
9223 C CG  . TYR B 508 ? 0.3972 0.3853 0.3008 -0.0148 0.0239  0.0040  508 TYR B CG  
9224 C CD1 . TYR B 508 ? 0.4084 0.4083 0.3136 -0.0210 0.0236  0.0018  508 TYR B CD1 
9225 C CD2 . TYR B 508 ? 0.4019 0.3746 0.2979 -0.0129 0.0249  0.0026  508 TYR B CD2 
9226 C CE1 . TYR B 508 ? 0.4069 0.4036 0.3070 -0.0256 0.0242  -0.0016 508 TYR B CE1 
9227 C CE2 . TYR B 508 ? 0.4152 0.3831 0.3055 -0.0174 0.0256  -0.0008 508 TYR B CE2 
9228 C CZ  . TYR B 508 ? 0.4144 0.3942 0.3069 -0.0240 0.0253  -0.0030 508 TYR B CZ  
9229 O OH  . TYR B 508 ? 0.4167 0.3931 0.3038 -0.0287 0.0261  -0.0063 508 TYR B OH  
9230 N N   . ALA B 509 ? 0.3711 0.3671 0.2774 -0.0044 0.0270  0.0125  509 ALA B N   
9231 C CA  . ALA B 509 ? 0.3833 0.3891 0.2949 -0.0022 0.0270  0.0157  509 ALA B CA  
9232 C C   . ALA B 509 ? 0.4144 0.4167 0.3126 -0.0071 0.0312  0.0124  509 ALA B C   
9233 O O   . ALA B 509 ? 0.4325 0.4473 0.3344 -0.0091 0.0310  0.0133  509 ALA B O   
9234 C CB  . ALA B 509 ? 0.3693 0.3725 0.2853 0.0057  0.0265  0.0199  509 ALA B CB  
9235 N N   . SER B 510 ? 0.4320 0.4165 0.3135 -0.0090 0.0352  0.0086  510 SER B N   
9236 C CA  . SER B 510 ? 0.4673 0.4442 0.3328 -0.0146 0.0399  0.0046  510 SER B CA  
9237 C C   . SER B 510 ? 0.4863 0.4727 0.3495 -0.0251 0.0400  0.0003  510 SER B C   
9238 O O   . SER B 510 ? 0.5059 0.5000 0.3656 -0.0298 0.0415  -0.0012 510 SER B O   
9239 C CB  . SER B 510 ? 0.4938 0.4462 0.3400 -0.0137 0.0447  0.0017  510 SER B CB  
9240 O OG  . SER B 510 ? 0.5230 0.4654 0.3511 -0.0219 0.0498  -0.0034 510 SER B OG  
9241 N N   . ARG B 511 ? 0.4959 0.4830 0.3609 -0.0289 0.0386  -0.0017 511 ARG B N   
9242 C CA  . ARG B 511 ? 0.5180 0.5171 0.3816 -0.0388 0.0387  -0.0057 511 ARG B CA  
9243 C C   . ARG B 511 ? 0.4853 0.5092 0.3643 -0.0373 0.0351  -0.0023 511 ARG B C   
9244 O O   . ARG B 511 ? 0.4968 0.5328 0.3726 -0.0439 0.0361  -0.0048 511 ARG B O   
9245 C CB  . ARG B 511 ? 0.5517 0.5483 0.4152 -0.0423 0.0379  -0.0081 511 ARG B CB  
9246 C CG  . ARG B 511 ? 0.6799 0.6519 0.5245 -0.0461 0.0426  -0.0124 511 ARG B CG  
9247 C CD  . ARG B 511 ? 0.7427 0.7144 0.5870 -0.0507 0.0420  -0.0150 511 ARG B CD  
9248 N NE  . ARG B 511 ? 0.7642 0.7115 0.5952 -0.0494 0.0451  -0.0166 511 ARG B NE  
9249 C CZ  . ARG B 511 ? 0.7605 0.7030 0.5982 -0.0420 0.0425  -0.0139 511 ARG B CZ  
9250 N NH1 . ARG B 511 ? 0.7363 0.6949 0.5932 -0.0359 0.0369  -0.0097 511 ARG B NH1 
9251 N NH2 . ARG B 511 ? 0.7964 0.7171 0.6203 -0.0407 0.0458  -0.0154 511 ARG B NH2 
9252 N N   . ALA B 512 ? 0.4514 0.4825 0.3461 -0.0287 0.0311  0.0033  512 ALA B N   
9253 C CA  . ALA B 512 ? 0.4407 0.4923 0.3486 -0.0258 0.0283  0.0074  512 ALA B CA  
9254 C C   . ALA B 512 ? 0.4474 0.5025 0.3514 -0.0258 0.0302  0.0081  512 ALA B C   
9255 O O   . ALA B 512 ? 0.4345 0.5066 0.3414 -0.0282 0.0297  0.0084  512 ALA B O   
9256 C CB  . ALA B 512 ? 0.4135 0.4675 0.3362 -0.0171 0.0246  0.0132  512 ALA B CB  
9257 N N   . PHE B 513 ? 0.4355 0.4753 0.3326 -0.0224 0.0325  0.0086  513 PHE B N   
9258 C CA  . PHE B 513 ? 0.4476 0.4897 0.3407 -0.0215 0.0346  0.0095  513 PHE B CA  
9259 C C   . PHE B 513 ? 0.4838 0.5288 0.3636 -0.0315 0.0376  0.0037  513 PHE B C   
9260 O O   . PHE B 513 ? 0.4731 0.5331 0.3554 -0.0328 0.0374  0.0045  513 PHE B O   
9261 C CB  . PHE B 513 ? 0.4422 0.4670 0.3286 -0.0155 0.0370  0.0110  513 PHE B CB  
9262 C CG  . PHE B 513 ? 0.4473 0.4751 0.3308 -0.0132 0.0390  0.0126  513 PHE B CG  
9263 C CD1 . PHE B 513 ? 0.4557 0.4755 0.3220 -0.0191 0.0434  0.0078  513 PHE B CD1 
9264 C CD2 . PHE B 513 ? 0.4362 0.4742 0.3332 -0.0056 0.0367  0.0189  513 PHE B CD2 
9265 C CE1 . PHE B 513 ? 0.4608 0.4832 0.3239 -0.0168 0.0453  0.0092  513 PHE B CE1 
9266 C CE2 . PHE B 513 ? 0.4428 0.4842 0.3371 -0.0033 0.0386  0.0206  513 PHE B CE2 
9267 C CZ  . PHE B 513 ? 0.4437 0.4774 0.3211 -0.0086 0.0428  0.0158  513 PHE B CZ  
9268 N N   . LYS B 514 ? 0.5328 0.5638 0.3982 -0.0388 0.0407  -0.0021 514 LYS B N   
9269 C CA  . LYS B 514 ? 0.5789 0.6113 0.4299 -0.0505 0.0441  -0.0086 514 LYS B CA  
9270 C C   . LYS B 514 ? 0.5568 0.6159 0.4167 -0.0561 0.0412  -0.0094 514 LYS B C   
9271 O O   . LYS B 514 ? 0.5404 0.6121 0.3962 -0.0617 0.0423  -0.0117 514 LYS B O   
9272 C CB  . LYS B 514 ? 0.6417 0.6518 0.4749 -0.0576 0.0483  -0.0145 514 LYS B CB  
9273 C CG  . LYS B 514 ? 0.7429 0.7269 0.5579 -0.0559 0.0537  -0.0162 514 LYS B CG  
9274 C CD  . LYS B 514 ? 0.7988 0.7569 0.5980 -0.0582 0.0576  -0.0196 514 LYS B CD  
9275 C CE  . LYS B 514 ? 0.8822 0.8136 0.6592 -0.0572 0.0642  -0.0219 514 LYS B CE  
9276 N NZ  . LYS B 514 ? 0.8938 0.7971 0.6534 -0.0572 0.0688  -0.0244 514 LYS B NZ  
9277 N N   . LYS B 515 ? 0.5577 0.6262 0.4295 -0.0538 0.0378  -0.0075 515 LYS B N   
9278 C CA  . LYS B 515 ? 0.5532 0.6478 0.4333 -0.0572 0.0352  -0.0076 515 LYS B CA  
9279 C C   . LYS B 515 ? 0.5318 0.6462 0.4229 -0.0511 0.0328  -0.0026 515 LYS B C   
9280 O O   . LYS B 515 ? 0.5413 0.6766 0.4324 -0.0558 0.0326  -0.0041 515 LYS B O   
9281 C CB  . LYS B 515 ? 0.5767 0.6750 0.4671 -0.0537 0.0321  -0.0057 515 LYS B CB  
9282 C CG  . LYS B 515 ? 0.6069 0.7069 0.4894 -0.0639 0.0335  -0.0117 515 LYS B CG  
9283 C CD  . LYS B 515 ? 0.6694 0.7429 0.5342 -0.0709 0.0381  -0.0171 515 LYS B CD  
9284 C CE  . LYS B 515 ? 0.6922 0.7634 0.5514 -0.0786 0.0391  -0.0216 515 LYS B CE  
9285 N NZ  . LYS B 515 ? 0.7121 0.8049 0.5676 -0.0903 0.0400  -0.0265 515 LYS B NZ  
9286 N N   . ILE B 516 ? 0.5060 0.6138 0.4057 -0.0409 0.0314  0.0034  516 ILE B N   
9287 C CA  . ILE B 516 ? 0.4693 0.5926 0.3791 -0.0342 0.0296  0.0090  516 ILE B CA  
9288 C C   . ILE B 516 ? 0.4900 0.6175 0.3903 -0.0389 0.0322  0.0064  516 ILE B C   
9289 O O   . ILE B 516 ? 0.4497 0.5981 0.3543 -0.0385 0.0312  0.0081  516 ILE B O   
9290 C CB  . ILE B 516 ? 0.4501 0.5638 0.3701 -0.0237 0.0280  0.0155  516 ILE B CB  
9291 C CG1 . ILE B 516 ? 0.4292 0.5453 0.3606 -0.0189 0.0249  0.0187  516 ILE B CG1 
9292 C CG2 . ILE B 516 ? 0.4371 0.5610 0.3628 -0.0182 0.0278  0.0205  516 ILE B CG2 
9293 C CD1 . ILE B 516 ? 0.4103 0.5169 0.3511 -0.0105 0.0234  0.0243  516 ILE B CD1 
9294 N N   . VAL B 517 ? 0.4970 0.6043 0.3831 -0.0430 0.0359  0.0023  517 VAL B N   
9295 C CA  . VAL B 517 ? 0.5274 0.6350 0.4018 -0.0480 0.0390  -0.0008 517 VAL B CA  
9296 C C   . VAL B 517 ? 0.5387 0.6621 0.4055 -0.0599 0.0399  -0.0071 517 VAL B C   
9297 O O   . VAL B 517 ? 0.5365 0.6790 0.4045 -0.0616 0.0394  -0.0069 517 VAL B O   
9298 C CB  . VAL B 517 ? 0.5479 0.6275 0.4066 -0.0487 0.0435  -0.0037 517 VAL B CB  
9299 C CG1 . VAL B 517 ? 0.5482 0.6252 0.3898 -0.0576 0.0477  -0.0096 517 VAL B CG1 
9300 C CG2 . VAL B 517 ? 0.5032 0.5752 0.3701 -0.0367 0.0427  0.0029  517 VAL B CG2 
9301 N N   . THR B 518 ? 0.5681 0.6851 0.4277 -0.0680 0.0410  -0.0123 518 THR B N   
9302 C CA  . THR B 518 ? 0.5980 0.7306 0.4501 -0.0809 0.0420  -0.0188 518 THR B CA  
9303 C C   . THR B 518 ? 0.5893 0.7568 0.4550 -0.0790 0.0381  -0.0159 518 THR B C   
9304 O O   . THR B 518 ? 0.6235 0.8097 0.4839 -0.0872 0.0388  -0.0198 518 THR B O   
9305 C CB  . THR B 518 ? 0.5870 0.7082 0.4324 -0.0883 0.0434  -0.0235 518 THR B CB  
9306 O OG1 . THR B 518 ? 0.6146 0.7033 0.4441 -0.0904 0.0479  -0.0266 518 THR B OG1 
9307 C CG2 . THR B 518 ? 0.6178 0.7573 0.4556 -0.1028 0.0446  -0.0305 518 THR B CG2 
9308 N N   . TYR B 519 ? 0.5718 0.7478 0.4538 -0.0681 0.0342  -0.0091 519 TYR B N   
9309 C CA  . TYR B 519 ? 0.5270 0.7340 0.4207 -0.0646 0.0310  -0.0059 519 TYR B CA  
9310 C C   . TYR B 519 ? 0.4957 0.7108 0.4005 -0.0524 0.0289  0.0019  519 TYR B C   
9311 O O   . TYR B 519 ? 0.4934 0.7252 0.4103 -0.0440 0.0261  0.0076  519 TYR B O   
9312 C CB  . TYR B 519 ? 0.5683 0.7798 0.4699 -0.0624 0.0288  -0.0047 519 TYR B CB  
9313 C CG  . TYR B 519 ? 0.6168 0.8225 0.5071 -0.0753 0.0311  -0.0126 519 TYR B CG  
9314 C CD1 . TYR B 519 ? 0.6498 0.8761 0.5325 -0.0875 0.0323  -0.0187 519 TYR B CD1 
9315 C CD2 . TYR B 519 ? 0.6054 0.7854 0.4916 -0.0760 0.0323  -0.0141 519 TYR B CD2 
9316 C CE1 . TYR B 519 ? 0.6823 0.9028 0.5536 -0.1007 0.0349  -0.0262 519 TYR B CE1 
9317 C CE2 . TYR B 519 ? 0.6632 0.8364 0.5378 -0.0880 0.0349  -0.0212 519 TYR B CE2 
9318 C CZ  . TYR B 519 ? 0.6960 0.8889 0.5629 -0.1008 0.0364  -0.0273 519 TYR B CZ  
9319 O OH  . TYR B 519 ? 0.7316 0.9177 0.5862 -0.1141 0.0395  -0.0345 519 TYR B OH  
9320 N N   . LYS B 520 ? 0.4791 0.6815 0.3785 -0.0515 0.0309  0.0023  520 LYS B N   
9321 C CA  . LYS B 520 ? 0.4685 0.6769 0.3763 -0.0412 0.0297  0.0094  520 LYS B CA  
9322 C C   . LYS B 520 ? 0.4688 0.7077 0.3793 -0.0412 0.0285  0.0105  520 LYS B C   
9323 O O   . LYS B 520 ? 0.4681 0.7196 0.3693 -0.0515 0.0298  0.0042  520 LYS B O   
9324 C CB  . LYS B 520 ? 0.4742 0.6630 0.3733 -0.0417 0.0326  0.0084  520 LYS B CB  
9325 C CG  . LYS B 520 ? 0.4976 0.6905 0.4045 -0.0317 0.0320  0.0155  520 LYS B CG  
9326 C CD  . LYS B 520 ? 0.4949 0.6677 0.3928 -0.0316 0.0351  0.0145  520 LYS B CD  
9327 C CE  . LYS B 520 ? 0.5084 0.6573 0.4079 -0.0273 0.0354  0.0159  520 LYS B CE  
9328 N NZ  . LYS B 520 ? 0.5626 0.6920 0.4503 -0.0277 0.0391  0.0139  520 LYS B NZ  
9329 N N   . GLY B 521 ? 0.4674 0.7183 0.3900 -0.0298 0.0264  0.0184  521 GLY B N   
9330 C CA  . GLY B 521 ? 0.4622 0.7422 0.3878 -0.0270 0.0253  0.0209  521 GLY B CA  
9331 C C   . GLY B 521 ? 0.4666 0.7471 0.3991 -0.0158 0.0251  0.0290  521 GLY B C   
9332 O O   . GLY B 521 ? 0.4732 0.7322 0.4070 -0.0120 0.0260  0.0317  521 GLY B O   
9333 N N   . GLY B 522 ? 0.4730 0.7790 0.4096 -0.0101 0.0240  0.0332  522 GLY B N   
9334 C CA  . GLY B 522 ? 0.4437 0.7522 0.3850 0.0000  0.0243  0.0407  522 GLY B CA  
9335 C C   . GLY B 522 ? 0.4425 0.7339 0.3932 0.0105  0.0241  0.0485  522 GLY B C   
9336 O O   . GLY B 522 ? 0.4513 0.7386 0.4049 0.0172  0.0250  0.0543  522 GLY B O   
9337 N N   . LYS B 523 ? 0.4649 0.7461 0.4197 0.0114  0.0231  0.0485  523 LYS B N   
9338 C CA  . LYS B 523 ? 0.4508 0.7169 0.4138 0.0206  0.0228  0.0555  523 LYS B CA  
9339 C C   . LYS B 523 ? 0.4507 0.6900 0.4140 0.0177  0.0234  0.0539  523 LYS B C   
9340 O O   . LYS B 523 ? 0.4489 0.6743 0.4185 0.0234  0.0233  0.0588  523 LYS B O   
9341 C CB  . LYS B 523 ? 0.4505 0.7224 0.4177 0.0246  0.0214  0.0569  523 LYS B CB  
9342 C CG  . LYS B 523 ? 0.4477 0.7459 0.4162 0.0321  0.0211  0.0612  523 LYS B CG  
9343 C CD  . LYS B 523 ? 0.4470 0.7488 0.4191 0.0380  0.0202  0.0635  523 LYS B CD  
9344 C CE  . LYS B 523 ? 0.4698 0.7975 0.4423 0.0478  0.0203  0.0689  523 LYS B CE  
9345 N NZ  . LYS B 523 ? 0.4711 0.8091 0.4449 0.0520  0.0195  0.0691  523 LYS B NZ  
9346 N N   . TYR B 524 ? 0.4495 0.6814 0.4048 0.0087  0.0243  0.0471  524 TYR B N   
9347 C CA  . TYR B 524 ? 0.4737 0.6817 0.4275 0.0066  0.0252  0.0454  524 TYR B CA  
9348 C C   . TYR B 524 ? 0.4894 0.6913 0.4475 0.0131  0.0262  0.0516  524 TYR B C   
9349 O O   . TYR B 524 ? 0.4736 0.6871 0.4303 0.0149  0.0272  0.0537  524 TYR B O   
9350 C CB  . TYR B 524 ? 0.4776 0.6790 0.4192 -0.0032 0.0270  0.0373  524 TYR B CB  
9351 C CG  . TYR B 524 ? 0.4882 0.6656 0.4262 -0.0039 0.0284  0.0360  524 TYR B CG  
9352 C CD1 . TYR B 524 ? 0.4816 0.6437 0.4195 -0.0057 0.0279  0.0335  524 TYR B CD1 
9353 C CD2 . TYR B 524 ? 0.4926 0.6637 0.4272 -0.0021 0.0305  0.0373  524 TYR B CD2 
9354 C CE1 . TYR B 524 ? 0.4837 0.6254 0.4179 -0.0051 0.0293  0.0327  524 TYR B CE1 
9355 C CE2 . TYR B 524 ? 0.4936 0.6445 0.4246 -0.0014 0.0320  0.0364  524 TYR B CE2 
9356 C CZ  . TYR B 524 ? 0.5010 0.6378 0.4319 -0.0027 0.0314  0.0342  524 TYR B CZ  
9357 O OH  . TYR B 524 ? 0.4944 0.6130 0.4216 -0.0008 0.0329  0.0338  524 TYR B OH  
9358 N N   . ARG B 525 ? 0.5106 0.6962 0.4744 0.0164  0.0260  0.0546  525 ARG B N   
9359 C CA  . ARG B 525 ? 0.4932 0.6727 0.4604 0.0210  0.0274  0.0596  525 ARG B CA  
9360 C C   . ARG B 525 ? 0.4904 0.6542 0.4526 0.0178  0.0286  0.0561  525 ARG B C   
9361 O O   . ARG B 525 ? 0.4936 0.6579 0.4493 0.0165  0.0306  0.0546  525 ARG B O   
9362 C CB  . ARG B 525 ? 0.4940 0.6692 0.4713 0.0276  0.0268  0.0668  525 ARG B CB  
9363 C CG  . ARG B 525 ? 0.5557 0.7352 0.5371 0.0304  0.0253  0.0686  525 ARG B CG  
9364 C CD  . ARG B 525 ? 0.5764 0.7705 0.5597 0.0369  0.0259  0.0745  525 ARG B CD  
9365 N NE  . ARG B 525 ? 0.6152 0.8028 0.6036 0.0426  0.0273  0.0818  525 ARG B NE  
9366 C CZ  . ARG B 525 ? 0.6115 0.8027 0.6022 0.0496  0.0283  0.0882  525 ARG B CZ  
9367 N NH1 . ARG B 525 ? 0.6099 0.8124 0.5989 0.0530  0.0276  0.0884  525 ARG B NH1 
9368 N NH2 . ARG B 525 ? 0.6115 0.7946 0.6056 0.0533  0.0302  0.0945  525 ARG B NH2 
9369 N N   . LYS B 526 ? 0.4768 0.6269 0.4412 0.0172  0.0277  0.0548  526 LYS B N   
9370 C CA  . LYS B 526 ? 0.4503 0.5854 0.4099 0.0160  0.0290  0.0522  526 LYS B CA  
9371 C C   . LYS B 526 ? 0.4687 0.5920 0.4307 0.0152  0.0275  0.0504  526 LYS B C   
9372 O O   . LYS B 526 ? 0.4820 0.6032 0.4534 0.0186  0.0260  0.0546  526 LYS B O   
9373 C CB  . LYS B 526 ? 0.4510 0.5846 0.4152 0.0210  0.0303  0.0574  526 LYS B CB  
9374 C CG  . LYS B 526 ? 0.4519 0.5722 0.4105 0.0213  0.0318  0.0551  526 LYS B CG  
9375 C CD  . LYS B 526 ? 0.4764 0.5987 0.4377 0.0260  0.0336  0.0598  526 LYS B CD  
9376 C CE  . LYS B 526 ? 0.4952 0.6061 0.4541 0.0283  0.0346  0.0590  526 LYS B CE  
9377 N NZ  . LYS B 526 ? 0.5380 0.6530 0.4992 0.0330  0.0366  0.0634  526 LYS B NZ  
9378 N N   . VAL B 527 ? 0.4357 0.5502 0.3880 0.0103  0.0282  0.0442  527 VAL B N   
9379 C CA  . VAL B 527 ? 0.4164 0.5194 0.3689 0.0093  0.0271  0.0419  527 VAL B CA  
9380 C C   . VAL B 527 ? 0.4188 0.5066 0.3623 0.0094  0.0293  0.0391  527 VAL B C   
9381 O O   . VAL B 527 ? 0.4150 0.4974 0.3457 0.0057  0.0319  0.0346  527 VAL B O   
9382 C CB  . VAL B 527 ? 0.4187 0.5242 0.3667 0.0036  0.0263  0.0369  527 VAL B CB  
9383 C CG1 . VAL B 527 ? 0.4187 0.5100 0.3641 0.0020  0.0257  0.0338  527 VAL B CG1 
9384 C CG2 . VAL B 527 ? 0.3865 0.5067 0.3436 0.0055  0.0241  0.0403  527 VAL B CG2 
9385 N N   . THR B 528 ? 0.4138 0.4947 0.3630 0.0139  0.0284  0.0419  528 THR B N   
9386 C CA  . THR B 528 ? 0.4326 0.4997 0.3735 0.0157  0.0304  0.0399  528 THR B CA  
9387 C C   . THR B 528 ? 0.4288 0.4852 0.3670 0.0141  0.0293  0.0366  528 THR B C   
9388 O O   . THR B 528 ? 0.4108 0.4709 0.3571 0.0129  0.0265  0.0372  528 THR B O   
9389 C CB  . THR B 528 ? 0.4665 0.5352 0.4150 0.0221  0.0302  0.0450  528 THR B CB  
9390 O OG1 . THR B 528 ? 0.4516 0.5236 0.4126 0.0231  0.0270  0.0479  528 THR B OG1 
9391 C CG2 . THR B 528 ? 0.4754 0.5550 0.4274 0.0242  0.0314  0.0490  528 THR B CG2 
9392 N N   . PHE B 529 ? 0.4210 0.4632 0.3468 0.0148  0.0320  0.0334  529 PHE B N   
9393 C CA  . PHE B 529 ? 0.4118 0.4424 0.3338 0.0148  0.0315  0.0309  529 PHE B CA  
9394 C C   . PHE B 529 ? 0.4145 0.4496 0.3503 0.0194  0.0280  0.0350  529 PHE B C   
9395 O O   . PHE B 529 ? 0.4196 0.4530 0.3596 0.0177  0.0256  0.0340  529 PHE B O   
9396 C CB  . PHE B 529 ? 0.3970 0.4108 0.3023 0.0171  0.0356  0.0281  529 PHE B CB  
9397 C CG  . PHE B 529 ? 0.3953 0.3958 0.2943 0.0173  0.0358  0.0254  529 PHE B CG  
9398 C CD1 . PHE B 529 ? 0.3914 0.3848 0.2822 0.0101  0.0365  0.0204  529 PHE B CD1 
9399 C CD2 . PHE B 529 ? 0.4082 0.4047 0.3094 0.0246  0.0351  0.0279  529 PHE B CD2 
9400 C CE1 . PHE B 529 ? 0.3911 0.3714 0.2751 0.0104  0.0370  0.0180  529 PHE B CE1 
9401 C CE2 . PHE B 529 ? 0.3961 0.3805 0.2907 0.0254  0.0354  0.0256  529 PHE B CE2 
9402 C CZ  . PHE B 529 ? 0.3861 0.3617 0.2721 0.0184  0.0364  0.0207  529 PHE B CZ  
9403 N N   . GLN B 530 ? 0.4138 0.4545 0.3556 0.0246  0.0281  0.0394  530 GLN B N   
9404 C CA  . GLN B 530 ? 0.4206 0.4675 0.3753 0.0279  0.0252  0.0433  530 GLN B CA  
9405 C C   . GLN B 530 ? 0.4050 0.4590 0.3714 0.0244  0.0219  0.0447  530 GLN B C   
9406 O O   . GLN B 530 ? 0.3988 0.4517 0.3713 0.0244  0.0194  0.0450  530 GLN B O   
9407 C CB  . GLN B 530 ? 0.4288 0.4847 0.3890 0.0324  0.0261  0.0480  530 GLN B CB  
9408 C CG  . GLN B 530 ? 0.4794 0.5293 0.4296 0.0384  0.0291  0.0478  530 GLN B CG  
9409 C CD  . GLN B 530 ? 0.4933 0.5323 0.4268 0.0377  0.0332  0.0441  530 GLN B CD  
9410 O OE1 . GLN B 530 ? 0.4804 0.5235 0.4127 0.0343  0.0342  0.0438  530 GLN B OE1 
9411 N NE2 . GLN B 530 ? 0.5224 0.5470 0.4419 0.0406  0.0359  0.0411  530 GLN B NE2 
9412 N N   . CYS B 531 ? 0.3856 0.4469 0.3542 0.0219  0.0221  0.0457  531 CYS B N   
9413 C CA  . CYS B 531 ? 0.4015 0.4693 0.3801 0.0202  0.0197  0.0479  531 CYS B CA  
9414 C C   . CYS B 531 ? 0.3924 0.4545 0.3685 0.0173  0.0182  0.0441  531 CYS B C   
9415 O O   . CYS B 531 ? 0.3691 0.4305 0.3521 0.0172  0.0159  0.0451  531 CYS B O   
9416 C CB  . CYS B 531 ? 0.4204 0.4980 0.4006 0.0196  0.0206  0.0502  531 CYS B CB  
9417 S SG  . CYS B 531 ? 0.4867 0.5704 0.4768 0.0196  0.0185  0.0537  531 CYS B SG  
9418 N N   . LEU B 532 ? 0.3886 0.4462 0.3540 0.0143  0.0198  0.0395  532 LEU B N   
9419 C CA  . LEU B 532 ? 0.3776 0.4301 0.3388 0.0109  0.0190  0.0353  532 LEU B CA  
9420 C C   . LEU B 532 ? 0.3834 0.4259 0.3446 0.0125  0.0177  0.0342  532 LEU B C   
9421 O O   . LEU B 532 ? 0.3775 0.4186 0.3422 0.0113  0.0157  0.0333  532 LEU B O   
9422 C CB  . LEU B 532 ? 0.3863 0.4349 0.3342 0.0063  0.0217  0.0303  532 LEU B CB  
9423 C CG  . LEU B 532 ? 0.3778 0.4388 0.3250 0.0031  0.0225  0.0301  532 LEU B CG  
9424 C CD1 . LEU B 532 ? 0.3826 0.4390 0.3151 -0.0027 0.0257  0.0245  532 LEU B CD1 
9425 C CD2 . LEU B 532 ? 0.3511 0.4223 0.3060 0.0023  0.0201  0.0310  532 LEU B CD2 
9426 N N   . LYS B 533 ? 0.3810 0.4176 0.3382 0.0158  0.0190  0.0346  533 LYS B N   
9427 C CA  . LYS B 533 ? 0.3721 0.4007 0.3283 0.0182  0.0180  0.0337  533 LYS B CA  
9428 C C   . LYS B 533 ? 0.3645 0.3994 0.3341 0.0194  0.0146  0.0370  533 LYS B C   
9429 O O   . LYS B 533 ? 0.3606 0.3912 0.3316 0.0192  0.0126  0.0356  533 LYS B O   
9430 C CB  . LYS B 533 ? 0.3977 0.4203 0.3458 0.0229  0.0205  0.0340  533 LYS B CB  
9431 C CG  . LYS B 533 ? 0.4593 0.4710 0.4004 0.0256  0.0207  0.0318  533 LYS B CG  
9432 C CD  . LYS B 533 ? 0.4560 0.4580 0.3834 0.0305  0.0247  0.0312  533 LYS B CD  
9433 C CE  . LYS B 533 ? 0.4732 0.4846 0.4062 0.0365  0.0250  0.0356  533 LYS B CE  
9434 N NZ  . LYS B 533 ? 0.5266 0.5287 0.4470 0.0439  0.0282  0.0356  533 LYS B NZ  
9435 N N   . SER B 534 ? 0.3510 0.3954 0.3295 0.0200  0.0141  0.0411  534 SER B N   
9436 C CA  . SER B 534 ? 0.3611 0.4102 0.3511 0.0198  0.0116  0.0441  534 SER B CA  
9437 C C   . SER B 534 ? 0.3486 0.3961 0.3414 0.0171  0.0099  0.0432  534 SER B C   
9438 O O   . SER B 534 ? 0.3312 0.3763 0.3287 0.0165  0.0079  0.0433  534 SER B O   
9439 C CB  . SER B 534 ? 0.3589 0.4171 0.3562 0.0207  0.0122  0.0489  534 SER B CB  
9440 O OG  . SER B 534 ? 0.3789 0.4398 0.3745 0.0238  0.0136  0.0501  534 SER B OG  
9441 N N   . ILE B 535 ? 0.3591 0.4090 0.3487 0.0158  0.0110  0.0424  535 ILE B N   
9442 C CA  . ILE B 535 ? 0.3590 0.4087 0.3499 0.0144  0.0099  0.0415  535 ILE B CA  
9443 C C   . ILE B 535 ? 0.3592 0.4007 0.3454 0.0130  0.0087  0.0372  535 ILE B C   
9444 O O   . ILE B 535 ? 0.3757 0.4146 0.3655 0.0128  0.0070  0.0370  535 ILE B O   
9445 C CB  . ILE B 535 ? 0.3571 0.4146 0.3452 0.0136  0.0113  0.0416  535 ILE B CB  
9446 C CG1 . ILE B 535 ? 0.3566 0.4218 0.3505 0.0158  0.0121  0.0468  535 ILE B CG1 
9447 C CG2 . ILE B 535 ? 0.3628 0.4216 0.3500 0.0126  0.0104  0.0398  535 ILE B CG2 
9448 C CD1 . ILE B 535 ? 0.3643 0.4392 0.3548 0.0157  0.0137  0.0471  535 ILE B CD1 
9449 N N   . ALA B 536 ? 0.3428 0.3790 0.3203 0.0123  0.0101  0.0338  536 ALA B N   
9450 C CA  . ALA B 536 ? 0.3374 0.3647 0.3090 0.0112  0.0096  0.0299  536 ALA B CA  
9451 C C   . ALA B 536 ? 0.3530 0.3765 0.3295 0.0133  0.0073  0.0306  536 ALA B C   
9452 O O   . ALA B 536 ? 0.3471 0.3668 0.3243 0.0124  0.0056  0.0289  536 ALA B O   
9453 C CB  . ALA B 536 ? 0.3205 0.3404 0.2798 0.0104  0.0124  0.0266  536 ALA B CB  
9454 N N   . TRP B 537 ? 0.3575 0.3831 0.3371 0.0159  0.0072  0.0331  537 TRP B N   
9455 C CA  . TRP B 537 ? 0.3609 0.3861 0.3457 0.0172  0.0049  0.0337  537 TRP B CA  
9456 C C   . TRP B 537 ? 0.3749 0.4024 0.3684 0.0150  0.0027  0.0352  537 TRP B C   
9457 O O   . TRP B 537 ? 0.3829 0.4070 0.3783 0.0144  0.0006  0.0338  537 TRP B O   
9458 C CB  . TRP B 537 ? 0.3468 0.3776 0.3341 0.0203  0.0053  0.0364  537 TRP B CB  
9459 C CG  . TRP B 537 ? 0.3342 0.3600 0.3113 0.0243  0.0073  0.0349  537 TRP B CG  
9460 C CD1 . TRP B 537 ? 0.3271 0.3535 0.2985 0.0272  0.0103  0.0360  537 TRP B CD1 
9461 C CD2 . TRP B 537 ? 0.3235 0.3411 0.2931 0.0267  0.0071  0.0321  537 TRP B CD2 
9462 N NE1 . TRP B 537 ? 0.3332 0.3512 0.2934 0.0314  0.0122  0.0342  537 TRP B NE1 
9463 C CE2 . TRP B 537 ? 0.3305 0.3430 0.2889 0.0314  0.0105  0.0319  537 TRP B CE2 
9464 C CE3 . TRP B 537 ? 0.3189 0.3322 0.2887 0.0258  0.0049  0.0299  537 TRP B CE3 
9465 C CZ2 . TRP B 537 ? 0.3348 0.3377 0.2824 0.0355  0.0118  0.0300  537 TRP B CZ2 
9466 C CZ3 . TRP B 537 ? 0.3189 0.3241 0.2788 0.0296  0.0058  0.0278  537 TRP B CZ3 
9467 C CH2 . TRP B 537 ? 0.3312 0.3309 0.2799 0.0345  0.0093  0.0280  537 TRP B CH2 
9468 N N   . ARG B 538 ? 0.3672 0.3994 0.3648 0.0141  0.0035  0.0379  538 ARG B N   
9469 C CA  . ARG B 538 ? 0.3835 0.4151 0.3872 0.0127  0.0023  0.0398  538 ARG B CA  
9470 C C   . ARG B 538 ? 0.3675 0.3935 0.3681 0.0122  0.0015  0.0370  538 ARG B C   
9471 O O   . ARG B 538 ? 0.3733 0.3951 0.3767 0.0113  0.0001  0.0369  538 ARG B O   
9472 C CB  . ARG B 538 ? 0.3925 0.4294 0.3999 0.0131  0.0040  0.0438  538 ARG B CB  
9473 C CG  . ARG B 538 ? 0.4216 0.4642 0.4335 0.0131  0.0047  0.0471  538 ARG B CG  
9474 C CD  . ARG B 538 ? 0.4430 0.4859 0.4601 0.0120  0.0054  0.0512  538 ARG B CD  
9475 N NE  . ARG B 538 ? 0.4619 0.5117 0.4830 0.0118  0.0067  0.0547  538 ARG B NE  
9476 C CZ  . ARG B 538 ? 0.4734 0.5234 0.4994 0.0094  0.0074  0.0580  538 ARG B CZ  
9477 N NH1 . ARG B 538 ? 0.4665 0.5084 0.4929 0.0070  0.0071  0.0581  538 ARG B NH1 
9478 N NH2 . ARG B 538 ? 0.4537 0.5113 0.4831 0.0091  0.0088  0.0612  538 ARG B NH2 
9479 N N   . ALA B 539 ? 0.3471 0.3735 0.3417 0.0123  0.0026  0.0346  539 ALA B N   
9480 C CA  . ALA B 539 ? 0.3370 0.3600 0.3284 0.0117  0.0021  0.0320  539 ALA B CA  
9481 C C   . ALA B 539 ? 0.3378 0.3532 0.3271 0.0112  0.0003  0.0288  539 ALA B C   
9482 O O   . ALA B 539 ? 0.3579 0.3694 0.3481 0.0111  -0.0008 0.0279  539 ALA B O   
9483 C CB  . ALA B 539 ? 0.3065 0.3334 0.2916 0.0106  0.0038  0.0298  539 ALA B CB  
9484 N N   . PHE B 540 ? 0.3532 0.3663 0.3389 0.0116  0.0005  0.0275  540 PHE B N   
9485 C CA  . PHE B 540 ? 0.3619 0.3689 0.3453 0.0121  -0.0010 0.0250  540 PHE B CA  
9486 C C   . PHE B 540 ? 0.3947 0.4024 0.3856 0.0117  -0.0035 0.0264  540 PHE B C   
9487 O O   . PHE B 540 ? 0.3942 0.3972 0.3848 0.0111  -0.0053 0.0244  540 PHE B O   
9488 C CB  . PHE B 540 ? 0.3431 0.3476 0.3199 0.0141  0.0001  0.0240  540 PHE B CB  
9489 C CG  . PHE B 540 ? 0.3810 0.3788 0.3468 0.0133  0.0025  0.0207  540 PHE B CG  
9490 C CD1 . PHE B 540 ? 0.3777 0.3679 0.3379 0.0129  0.0020  0.0176  540 PHE B CD1 
9491 C CD2 . PHE B 540 ? 0.3897 0.3882 0.3499 0.0121  0.0054  0.0206  540 PHE B CD2 
9492 C CE1 . PHE B 540 ? 0.3886 0.3720 0.3379 0.0109  0.0047  0.0145  540 PHE B CE1 
9493 C CE2 . PHE B 540 ? 0.4054 0.3969 0.3542 0.0097  0.0080  0.0171  540 PHE B CE2 
9494 C CZ  . PHE B 540 ? 0.3986 0.3823 0.3419 0.0089  0.0078  0.0140  540 PHE B CZ  
9495 N N   . LEU B 541 ? 0.3883 0.4019 0.3853 0.0115  -0.0034 0.0297  541 LEU B N   
9496 C CA  . LEU B 541 ? 0.3811 0.3958 0.3846 0.0094  -0.0052 0.0309  541 LEU B CA  
9497 C C   . LEU B 541 ? 0.3950 0.4036 0.3995 0.0076  -0.0058 0.0305  541 LEU B C   
9498 O O   . LEU B 541 ? 0.3992 0.4042 0.4052 0.0055  -0.0075 0.0292  541 LEU B O   
9499 C CB  . LEU B 541 ? 0.3778 0.3997 0.3872 0.0085  -0.0043 0.0348  541 LEU B CB  
9500 C CG  . LEU B 541 ? 0.3757 0.4059 0.3885 0.0088  -0.0049 0.0360  541 LEU B CG  
9501 C CD1 . LEU B 541 ? 0.3612 0.3918 0.3718 0.0100  -0.0070 0.0331  541 LEU B CD1 
9502 C CD2 . LEU B 541 ? 0.3852 0.4201 0.3959 0.0119  -0.0026 0.0379  541 LEU B CD2 
9503 N N   . ALA B 542 ? 0.3888 0.3965 0.3919 0.0087  -0.0040 0.0318  542 ALA B N   
9504 C CA  . ALA B 542 ? 0.3849 0.3868 0.3882 0.0086  -0.0037 0.0325  542 ALA B CA  
9505 C C   . ALA B 542 ? 0.3870 0.3826 0.3861 0.0090  -0.0051 0.0287  542 ALA B C   
9506 O O   . ALA B 542 ? 0.3774 0.3659 0.3759 0.0085  -0.0055 0.0282  542 ALA B O   
9507 C CB  . ALA B 542 ? 0.3755 0.3808 0.3782 0.0111  -0.0014 0.0355  542 ALA B CB  
9508 N N   . VAL B 543 ? 0.3805 0.3776 0.3757 0.0097  -0.0054 0.0260  543 VAL B N   
9509 C CA  . VAL B 543 ? 0.3944 0.3861 0.3850 0.0100  -0.0064 0.0223  543 VAL B CA  
9510 C C   . VAL B 543 ? 0.4043 0.3928 0.3952 0.0088  -0.0088 0.0202  543 VAL B C   
9511 O O   . VAL B 543 ? 0.4163 0.3991 0.4061 0.0082  -0.0102 0.0182  543 VAL B O   
9512 C CB  . VAL B 543 ? 0.3867 0.3805 0.3715 0.0106  -0.0051 0.0203  543 VAL B CB  
9513 C CG1 . VAL B 543 ? 0.4040 0.3919 0.3836 0.0104  -0.0060 0.0165  543 VAL B CG1 
9514 C CG2 . VAL B 543 ? 0.3819 0.3807 0.3662 0.0114  -0.0033 0.0216  543 VAL B CG2 
9515 N N   . LEU B 544 ? 0.4045 0.3975 0.3965 0.0089  -0.0091 0.0207  544 LEU B N   
9516 C CA  . LEU B 544 ? 0.3984 0.3913 0.3902 0.0087  -0.0113 0.0189  544 LEU B CA  
9517 C C   . LEU B 544 ? 0.4530 0.4454 0.4499 0.0053  -0.0132 0.0190  544 LEU B C   
9518 O O   . LEU B 544 ? 0.4653 0.4557 0.4611 0.0043  -0.0154 0.0164  544 LEU B O   
9519 C CB  . LEU B 544 ? 0.3671 0.3665 0.3588 0.0107  -0.0109 0.0202  544 LEU B CB  
9520 C CG  . LEU B 544 ? 0.3675 0.3644 0.3512 0.0138  -0.0086 0.0193  544 LEU B CG  
9521 C CD1 . LEU B 544 ? 0.3321 0.3347 0.3154 0.0165  -0.0074 0.0214  544 LEU B CD1 
9522 C CD2 . LEU B 544 ? 0.3510 0.3407 0.3270 0.0154  -0.0091 0.0159  544 LEU B CD2 
9523 N N   . LYS B 545 ? 0.4655 0.4588 0.4668 0.0033  -0.0120 0.0219  545 LYS B N   
9524 C CA  . LYS B 545 ? 0.4770 0.4674 0.4815 -0.0011 -0.0128 0.0222  545 LYS B CA  
9525 C C   . LYS B 545 ? 0.4670 0.4467 0.4675 -0.0020 -0.0134 0.0196  545 LYS B C   
9526 O O   . LYS B 545 ? 0.4596 0.4354 0.4607 -0.0062 -0.0143 0.0183  545 LYS B O   
9527 C CB  . LYS B 545 ? 0.4755 0.4662 0.4833 -0.0025 -0.0104 0.0262  545 LYS B CB  
9528 C CG  . LYS B 545 ? 0.5190 0.5198 0.5324 -0.0049 -0.0104 0.0285  545 LYS B CG  
9529 C CD  . LYS B 545 ? 0.5713 0.5720 0.5866 -0.0049 -0.0075 0.0328  545 LYS B CD  
9530 C CE  . LYS B 545 ? 0.5918 0.5999 0.6125 -0.0094 -0.0072 0.0351  545 LYS B CE  
9531 N NZ  . LYS B 545 ? 0.6367 0.6397 0.6577 -0.0105 -0.0040 0.0390  545 LYS B NZ  
9532 N N   . ARG B 546 ? 0.4723 0.4476 0.4684 0.0017  -0.0125 0.0187  546 ARG B N   
9533 C CA  . ARG B 546 ? 0.4572 0.4230 0.4488 0.0020  -0.0129 0.0161  546 ARG B CA  
9534 C C   . ARG B 546 ? 0.4482 0.4129 0.4380 0.0006  -0.0157 0.0122  546 ARG B C   
9535 O O   . ARG B 546 ? 0.4390 0.3956 0.4253 0.0000  -0.0163 0.0098  546 ARG B O   
9536 C CB  . ARG B 546 ? 0.4293 0.3940 0.4170 0.0064  -0.0113 0.0162  546 ARG B CB  
9537 C CG  . ARG B 546 ? 0.4455 0.4119 0.4343 0.0085  -0.0086 0.0201  546 ARG B CG  
9538 C CD  . ARG B 546 ? 0.4481 0.4146 0.4327 0.0127  -0.0071 0.0198  546 ARG B CD  
9539 N NE  . ARG B 546 ? 0.4397 0.3967 0.4204 0.0139  -0.0072 0.0181  546 ARG B NE  
9540 C CZ  . ARG B 546 ? 0.4555 0.4121 0.4322 0.0181  -0.0059 0.0180  546 ARG B CZ  
9541 N NH1 . ARG B 546 ? 0.4173 0.3841 0.3941 0.0206  -0.0045 0.0193  546 ARG B NH1 
9542 N NH2 . ARG B 546 ? 0.4686 0.4154 0.4409 0.0195  -0.0058 0.0165  546 ARG B NH2 
9543 N N   . ARG B 547 ? 0.4514 0.4242 0.4427 0.0009  -0.0172 0.0116  547 ARG B N   
9544 C CA  . ARG B 547 ? 0.4612 0.4356 0.4511 0.0001  -0.0200 0.0084  547 ARG B CA  
9545 C C   . ARG B 547 ? 0.4840 0.4695 0.4789 -0.0018 -0.0214 0.0094  547 ARG B C   
9546 O O   . ARG B 547 ? 0.4844 0.4768 0.4781 0.0014  -0.0223 0.0091  547 ARG B O   
9547 C CB  . ARG B 547 ? 0.4619 0.4354 0.4460 0.0046  -0.0200 0.0066  547 ARG B CB  
9548 C CG  . ARG B 547 ? 0.4645 0.4305 0.4438 0.0066  -0.0183 0.0057  547 ARG B CG  
9549 C CD  . ARG B 547 ? 0.4804 0.4443 0.4531 0.0094  -0.0184 0.0032  547 ARG B CD  
9550 N NE  . ARG B 547 ? 0.5062 0.4671 0.4746 0.0108  -0.0160 0.0030  547 ARG B NE  
9551 C CZ  . ARG B 547 ? 0.5169 0.4727 0.4821 0.0112  -0.0157 0.0013  547 ARG B CZ  
9552 N NH1 . ARG B 547 ? 0.5544 0.5054 0.5194 0.0106  -0.0175 -0.0005 547 ARG B NH1 
9553 N NH2 . ARG B 547 ? 0.4651 0.4214 0.4270 0.0120  -0.0134 0.0012  547 ARG B NH2 
9554 N N   . THR B 548 ? 0.5102 0.4975 0.5098 -0.0068 -0.0212 0.0108  548 THR B N   
9555 C CA  . THR B 548 ? 0.5659 0.5663 0.5712 -0.0093 -0.0223 0.0121  548 THR B CA  
9556 C C   . THR B 548 ? 0.5775 0.5862 0.5824 -0.0095 -0.0255 0.0093  548 THR B C   
9557 O O   . THR B 548 ? 0.6457 0.6681 0.6540 -0.0083 -0.0264 0.0104  548 THR B O   
9558 C CB  . THR B 548 ? 0.5767 0.5767 0.5862 -0.0165 -0.0214 0.0135  548 THR B CB  
9559 O OG1 . THR B 548 ? 0.6831 0.6700 0.6886 -0.0206 -0.0213 0.0110  548 THR B OG1 
9560 C CG2 . THR B 548 ? 0.5505 0.5487 0.5618 -0.0151 -0.0182 0.0177  548 THR B CG2 
9561 N N   . GLU B 549 ? 0.5793 0.5806 0.5799 -0.0103 -0.0270 0.0057  549 GLU B N   
9562 C CA  . GLU B 549 ? 0.6294 0.6389 0.6290 -0.0102 -0.0302 0.0028  549 GLU B CA  
9563 C C   . GLU B 549 ? 0.5909 0.6050 0.5868 -0.0017 -0.0302 0.0035  549 GLU B C   
9564 O O   . GLU B 549 ? 0.6165 0.6440 0.6139 0.0007  -0.0315 0.0043  549 GLU B O   
9565 C CB  . GLU B 549 ? 0.6710 0.6698 0.6658 -0.0131 -0.0316 -0.0013 549 GLU B CB  
9566 C CG  . GLU B 549 ? 0.7356 0.7211 0.7239 -0.0079 -0.0302 -0.0021 549 GLU B CG  
9567 C CD  . GLU B 549 ? 0.7404 0.7142 0.7280 -0.0082 -0.0271 -0.0002 549 GLU B CD  
9568 O OE1 . GLU B 549 ? 0.7582 0.7315 0.7494 -0.0125 -0.0258 0.0016  549 GLU B OE1 
9569 O OE2 . GLU B 549 ? 0.7380 0.7039 0.7210 -0.0041 -0.0257 -0.0005 549 GLU B OE2 
9570 N N   . ILE B 550 ? 0.5394 0.5421 0.5295 0.0026  -0.0283 0.0035  550 ILE B N   
9571 C CA  . ILE B 550 ? 0.5284 0.5310 0.5125 0.0099  -0.0272 0.0041  550 ILE B CA  
9572 C C   . ILE B 550 ? 0.5324 0.5425 0.5185 0.0130  -0.0252 0.0078  550 ILE B C   
9573 O O   . ILE B 550 ? 0.4865 0.5037 0.4699 0.0183  -0.0252 0.0088  550 ILE B O   
9574 C CB  . ILE B 550 ? 0.4957 0.4843 0.4728 0.0119  -0.0252 0.0028  550 ILE B CB  
9575 C CG1 . ILE B 550 ? 0.5009 0.4846 0.4734 0.0120  -0.0272 -0.0007 550 ILE B CG1 
9576 C CG2 . ILE B 550 ? 0.4830 0.4688 0.4537 0.0172  -0.0224 0.0042  550 ILE B CG2 
9577 C CD1 . ILE B 550 ? 0.4820 0.4536 0.4506 0.0111  -0.0260 -0.0024 550 ILE B CD1 
9578 N N   . TYR B 551 ? 0.5268 0.5354 0.5172 0.0102  -0.0233 0.0100  551 TYR B N   
9579 C CA  . TYR B 551 ? 0.5061 0.5186 0.4966 0.0134  -0.0208 0.0132  551 TYR B CA  
9580 C C   . TYR B 551 ? 0.5222 0.5485 0.5206 0.0115  -0.0214 0.0159  551 TYR B C   
9581 O O   . TYR B 551 ? 0.5214 0.5517 0.5202 0.0144  -0.0192 0.0187  551 TYR B O   
9582 C CB  . TYR B 551 ? 0.4728 0.4765 0.4620 0.0124  -0.0181 0.0141  551 TYR B CB  
9583 C CG  . TYR B 551 ? 0.4539 0.4468 0.4348 0.0147  -0.0166 0.0121  551 TYR B CG  
9584 C CD1 . TYR B 551 ? 0.4589 0.4486 0.4312 0.0194  -0.0154 0.0113  551 TYR B CD1 
9585 C CD2 . TYR B 551 ? 0.4282 0.4142 0.4089 0.0122  -0.0159 0.0112  551 TYR B CD2 
9586 C CE1 . TYR B 551 ? 0.4502 0.4299 0.4143 0.0202  -0.0135 0.0093  551 TYR B CE1 
9587 C CE2 . TYR B 551 ? 0.4573 0.4359 0.4309 0.0135  -0.0144 0.0094  551 TYR B CE2 
9588 C CZ  . TYR B 551 ? 0.4771 0.4524 0.4425 0.0168  -0.0132 0.0083  551 TYR B CZ  
9589 O OH  . TYR B 551 ? 0.5039 0.4717 0.4617 0.0167  -0.0112 0.0063  551 TYR B OH  
9590 N N   . LYS B 552 ? 0.5114 0.5448 0.5156 0.0061  -0.0239 0.0148  552 LYS B N   
9591 C CA  . LYS B 552 ? 0.5307 0.5796 0.5423 0.0031  -0.0247 0.0168  552 LYS B CA  
9592 C C   . LYS B 552 ? 0.4714 0.5315 0.4828 0.0099  -0.0234 0.0199  552 LYS B C   
9593 O O   . LYS B 552 ? 0.4715 0.5363 0.4869 0.0093  -0.0216 0.0229  552 LYS B O   
9594 C CB  . LYS B 552 ? 0.5694 0.6279 0.5841 -0.0017 -0.0281 0.0141  552 LYS B CB  
9595 C CG  . LYS B 552 ? 0.6327 0.7109 0.6550 -0.0054 -0.0292 0.0157  552 LYS B CG  
9596 C CD  . LYS B 552 ? 0.6908 0.7672 0.7188 -0.0129 -0.0272 0.0177  552 LYS B CD  
9597 C CE  . LYS B 552 ? 0.7042 0.7997 0.7397 -0.0200 -0.0285 0.0181  552 LYS B CE  
9598 N NZ  . LYS B 552 ? 0.7149 0.8099 0.7551 -0.0256 -0.0259 0.0212  552 LYS B NZ  
9599 N N   . GLY B 553 ? 0.4499 0.5138 0.4557 0.0169  -0.0241 0.0192  553 GLY B N   
9600 C CA  . GLY B 553 ? 0.4239 0.4982 0.4276 0.0248  -0.0227 0.0221  553 GLY B CA  
9601 C C   . GLY B 553 ? 0.4210 0.4850 0.4195 0.0289  -0.0187 0.0243  553 GLY B C   
9602 O O   . GLY B 553 ? 0.4238 0.4960 0.4232 0.0328  -0.0169 0.0273  553 GLY B O   
9603 N N   . LEU B 554 ? 0.3981 0.4450 0.3909 0.0280  -0.0173 0.0226  554 LEU B N   
9604 C CA  . LEU B 554 ? 0.4065 0.4436 0.3935 0.0304  -0.0135 0.0238  554 LEU B CA  
9605 C C   . LEU B 554 ? 0.3956 0.4364 0.3908 0.0252  -0.0127 0.0261  554 LEU B C   
9606 O O   . LEU B 554 ? 0.4137 0.4568 0.4079 0.0279  -0.0103 0.0286  554 LEU B O   
9607 C CB  . LEU B 554 ? 0.3966 0.4172 0.3754 0.0298  -0.0124 0.0211  554 LEU B CB  
9608 C CG  . LEU B 554 ? 0.4159 0.4261 0.3878 0.0305  -0.0085 0.0213  554 LEU B CG  
9609 C CD1 . LEU B 554 ? 0.4209 0.4305 0.3842 0.0375  -0.0054 0.0230  554 LEU B CD1 
9610 C CD2 . LEU B 554 ? 0.3789 0.3758 0.3433 0.0290  -0.0078 0.0181  554 LEU B CD2 
9611 N N   . ILE B 555 ? 0.3808 0.4216 0.3831 0.0182  -0.0146 0.0253  555 ILE B N   
9612 C CA  . ILE B 555 ? 0.3780 0.4218 0.3875 0.0133  -0.0138 0.0277  555 ILE B CA  
9613 C C   . ILE B 555 ? 0.4135 0.4725 0.4290 0.0137  -0.0136 0.0308  555 ILE B C   
9614 O O   . ILE B 555 ? 0.4262 0.4873 0.4438 0.0138  -0.0114 0.0336  555 ILE B O   
9615 C CB  . ILE B 555 ? 0.3557 0.3957 0.3699 0.0061  -0.0156 0.0262  555 ILE B CB  
9616 C CG1 . ILE B 555 ? 0.3331 0.3586 0.3419 0.0060  -0.0152 0.0239  555 ILE B CG1 
9617 C CG2 . ILE B 555 ? 0.3291 0.3723 0.3499 0.0011  -0.0144 0.0291  555 ILE B CG2 
9618 C CD1 . ILE B 555 ? 0.3225 0.3421 0.3330 0.0007  -0.0168 0.0219  555 ILE B CD1 
9619 N N   . ASP B 556 ? 0.4193 0.4905 0.4376 0.0140  -0.0159 0.0302  556 ASP B N   
9620 C CA  . ASP B 556 ? 0.4237 0.5129 0.4480 0.0145  -0.0159 0.0330  556 ASP B CA  
9621 C C   . ASP B 556 ? 0.4115 0.5036 0.4305 0.0236  -0.0133 0.0355  556 ASP B C   
9622 O O   . ASP B 556 ? 0.4205 0.5221 0.4436 0.0242  -0.0117 0.0387  556 ASP B O   
9623 C CB  . ASP B 556 ? 0.4536 0.5575 0.4817 0.0129  -0.0192 0.0315  556 ASP B CB  
9624 C CG  . ASP B 556 ? 0.5187 0.6227 0.5529 0.0019  -0.0212 0.0294  556 ASP B CG  
9625 O OD1 . ASP B 556 ? 0.5360 0.6306 0.5724 -0.0037 -0.0196 0.0303  556 ASP B OD1 
9626 O OD2 . ASP B 556 ? 0.5686 0.6816 0.6045 -0.0008 -0.0241 0.0270  556 ASP B OD2 
9627 N N   . ARG B 557 ? 0.3944 0.4778 0.4034 0.0307  -0.0125 0.0341  557 ARG B N   
9628 C CA  . ARG B 557 ? 0.4114 0.4926 0.4123 0.0392  -0.0091 0.0361  557 ARG B CA  
9629 C C   . ARG B 557 ? 0.3758 0.4485 0.3759 0.0372  -0.0062 0.0375  557 ARG B C   
9630 O O   . ARG B 557 ? 0.3845 0.4634 0.3848 0.0405  -0.0040 0.0403  557 ARG B O   
9631 C CB  . ARG B 557 ? 0.4291 0.4982 0.4170 0.0464  -0.0080 0.0341  557 ARG B CB  
9632 C CG  . ARG B 557 ? 0.4445 0.5082 0.4214 0.0553  -0.0037 0.0360  557 ARG B CG  
9633 C CD  . ARG B 557 ? 0.4725 0.5236 0.4349 0.0628  -0.0019 0.0345  557 ARG B CD  
9634 N NE  . ARG B 557 ? 0.4859 0.5494 0.4488 0.0685  -0.0042 0.0350  557 ARG B NE  
9635 C CZ  . ARG B 557 ? 0.5169 0.5723 0.4670 0.0770  -0.0027 0.0345  557 ARG B CZ  
9636 N NH1 . ARG B 557 ? 0.5063 0.5397 0.4415 0.0798  0.0014  0.0333  557 ARG B NH1 
9637 N NH2 . ARG B 557 ? 0.5083 0.5779 0.4599 0.0823  -0.0052 0.0352  557 ARG B NH2 
9638 N N   . ILE B 558 ? 0.3648 0.4250 0.3643 0.0320  -0.0061 0.0355  558 ILE B N   
9639 C CA  . ILE B 558 ? 0.3511 0.4056 0.3498 0.0302  -0.0035 0.0368  558 ILE B CA  
9640 C C   . ILE B 558 ? 0.3614 0.4284 0.3699 0.0274  -0.0034 0.0403  558 ILE B C   
9641 O O   . ILE B 558 ? 0.3431 0.4125 0.3501 0.0300  -0.0008 0.0427  558 ILE B O   
9642 C CB  . ILE B 558 ? 0.3393 0.3820 0.3370 0.0252  -0.0038 0.0345  558 ILE B CB  
9643 C CG1 . ILE B 558 ? 0.3284 0.3589 0.3154 0.0278  -0.0033 0.0311  558 ILE B CG1 
9644 C CG2 . ILE B 558 ? 0.3310 0.3717 0.3294 0.0233  -0.0015 0.0362  558 ILE B CG2 
9645 C CD1 . ILE B 558 ? 0.3198 0.3412 0.3062 0.0233  -0.0040 0.0286  558 ILE B CD1 
9646 N N   . LYS B 559 ? 0.3732 0.4477 0.3908 0.0216  -0.0059 0.0406  559 LYS B N   
9647 C CA  . LYS B 559 ? 0.3805 0.4656 0.4071 0.0172  -0.0055 0.0438  559 LYS B CA  
9648 C C   . LYS B 559 ? 0.3766 0.4779 0.4057 0.0215  -0.0047 0.0467  559 LYS B C   
9649 O O   . LYS B 559 ? 0.3549 0.4631 0.3884 0.0204  -0.0029 0.0499  559 LYS B O   
9650 C CB  . LYS B 559 ? 0.3838 0.4712 0.4175 0.0091  -0.0078 0.0429  559 LYS B CB  
9651 C CG  . LYS B 559 ? 0.4056 0.4785 0.4383 0.0045  -0.0076 0.0418  559 LYS B CG  
9652 C CD  . LYS B 559 ? 0.4399 0.5138 0.4779 -0.0035 -0.0092 0.0410  559 LYS B CD  
9653 C CE  . LYS B 559 ? 0.4638 0.5224 0.4999 -0.0071 -0.0082 0.0406  559 LYS B CE  
9654 N NZ  . LYS B 559 ? 0.5078 0.5646 0.5462 -0.0148 -0.0097 0.0386  559 LYS B NZ  
9655 N N   . SER B 560 ? 0.3830 0.4909 0.4090 0.0271  -0.0057 0.0457  560 SER B N   
9656 C CA  . SER B 560 ? 0.4120 0.5371 0.4399 0.0325  -0.0049 0.0486  560 SER B CA  
9657 C C   . SER B 560 ? 0.4208 0.5403 0.4389 0.0418  -0.0013 0.0501  560 SER B C   
9658 O O   . SER B 560 ? 0.4497 0.5816 0.4691 0.0464  0.0003  0.0533  560 SER B O   
9659 C CB  . SER B 560 ? 0.4336 0.5724 0.4630 0.0349  -0.0076 0.0476  560 SER B CB  
9660 O OG  . SER B 560 ? 0.4931 0.6193 0.5132 0.0395  -0.0083 0.0446  560 SER B OG  
9661 N N   . ARG B 561 ? 0.3894 0.4902 0.3970 0.0444  0.0000  0.0477  561 ARG B N   
9662 C CA  . ARG B 561 ? 0.3926 0.4851 0.3877 0.0531  0.0038  0.0483  561 ARG B CA  
9663 C C   . ARG B 561 ? 0.3959 0.4769 0.3870 0.0506  0.0066  0.0483  561 ARG B C   
9664 O O   . ARG B 561 ? 0.3888 0.4665 0.3717 0.0563  0.0102  0.0495  561 ARG B O   
9665 C CB  . ARG B 561 ? 0.4261 0.5059 0.4088 0.0588  0.0043  0.0455  561 ARG B CB  
9666 C CG  . ARG B 561 ? 0.4276 0.5196 0.4108 0.0647  0.0024  0.0460  561 ARG B CG  
9667 C CD  . ARG B 561 ? 0.4518 0.5295 0.4192 0.0732  0.0045  0.0444  561 ARG B CD  
9668 N NE  . ARG B 561 ? 0.4710 0.5602 0.4394 0.0781  0.0019  0.0445  561 ARG B NE  
9669 C CZ  . ARG B 561 ? 0.4843 0.5655 0.4394 0.0874  0.0036  0.0441  561 ARG B CZ  
9670 N NH1 . ARG B 561 ? 0.4846 0.5435 0.4231 0.0922  0.0083  0.0432  561 ARG B NH1 
9671 N NH2 . ARG B 561 ? 0.4520 0.5471 0.4097 0.0915  0.0007  0.0443  561 ARG B NH2 
9672 N N   . GLU B 562 ? 0.3693 0.4445 0.3655 0.0426  0.0052  0.0469  562 GLU B N   
9673 C CA  . GLU B 562 ? 0.3679 0.4338 0.3603 0.0401  0.0075  0.0465  562 GLU B CA  
9674 C C   . GLU B 562 ? 0.3661 0.4401 0.3687 0.0351  0.0073  0.0495  562 GLU B C   
9675 O O   . GLU B 562 ? 0.3347 0.4162 0.3475 0.0302  0.0051  0.0507  562 GLU B O   
9676 C CB  . GLU B 562 ? 0.3549 0.4066 0.3422 0.0363  0.0069  0.0427  562 GLU B CB  
9677 C CG  . GLU B 562 ? 0.3756 0.4165 0.3518 0.0401  0.0074  0.0396  562 GLU B CG  
9678 C CD  . GLU B 562 ? 0.3816 0.4169 0.3450 0.0475  0.0113  0.0399  562 GLU B CD  
9679 O OE1 . GLU B 562 ? 0.3918 0.4246 0.3506 0.0479  0.0143  0.0406  562 GLU B OE1 
9680 O OE2 . GLU B 562 ? 0.3878 0.4206 0.3448 0.0532  0.0115  0.0394  562 GLU B OE2 
9681 N N   . LYS B 563 ? 0.3923 0.4631 0.3905 0.0359  0.0101  0.0503  563 LYS B N   
9682 C CA  . LYS B 563 ? 0.4071 0.4835 0.4124 0.0321  0.0106  0.0531  563 LYS B CA  
9683 C C   . LYS B 563 ? 0.3977 0.4671 0.4050 0.0266  0.0093  0.0517  563 LYS B C   
9684 O O   . LYS B 563 ? 0.4277 0.4885 0.4277 0.0263  0.0103  0.0492  563 LYS B O   
9685 C CB  . LYS B 563 ? 0.4266 0.5022 0.4249 0.0356  0.0141  0.0542  563 LYS B CB  
9686 C CG  . LYS B 563 ? 0.4587 0.5410 0.4631 0.0330  0.0151  0.0575  563 LYS B CG  
9687 C CD  . LYS B 563 ? 0.4581 0.5538 0.4734 0.0320  0.0143  0.0615  563 LYS B CD  
9688 C CE  . LYS B 563 ? 0.4862 0.5896 0.5026 0.0339  0.0170  0.0652  563 LYS B CE  
9689 N NZ  . LYS B 563 ? 0.4845 0.6015 0.5116 0.0317  0.0166  0.0692  563 LYS B NZ  
9690 N N   . LEU B 564 ? 0.3946 0.4678 0.4111 0.0222  0.0075  0.0533  564 LEU B N   
9691 C CA  . LEU B 564 ? 0.3885 0.4550 0.4066 0.0182  0.0066  0.0526  564 LEU B CA  
9692 C C   . LEU B 564 ? 0.3863 0.4557 0.4082 0.0165  0.0082  0.0562  564 LEU B C   
9693 O O   . LEU B 564 ? 0.4003 0.4646 0.4215 0.0151  0.0083  0.0562  564 LEU B O   
9694 C CB  . LEU B 564 ? 0.3860 0.4507 0.4089 0.0145  0.0040  0.0514  564 LEU B CB  
9695 C CG  . LEU B 564 ? 0.3924 0.4540 0.4115 0.0162  0.0021  0.0478  564 LEU B CG  
9696 C CD1 . LEU B 564 ? 0.3985 0.4585 0.4223 0.0117  -0.0004 0.0465  564 LEU B CD1 
9697 C CD2 . LEU B 564 ? 0.3916 0.4436 0.4016 0.0184  0.0028  0.0445  564 LEU B CD2 
9698 N N   . THR B 565 ? 0.3894 0.4676 0.4148 0.0173  0.0097  0.0597  565 THR B N   
9699 C CA  . THR B 565 ? 0.4015 0.4826 0.4299 0.0163  0.0117  0.0637  565 THR B CA  
9700 C C   . THR B 565 ? 0.4038 0.4859 0.4261 0.0197  0.0137  0.0637  565 THR B C   
9701 O O   . THR B 565 ? 0.4270 0.5095 0.4438 0.0227  0.0144  0.0618  565 THR B O   
9702 C CB  . THR B 565 ? 0.3669 0.4572 0.4025 0.0143  0.0126  0.0677  565 THR B CB  
9703 O OG1 . THR B 565 ? 0.3501 0.4492 0.3853 0.0178  0.0130  0.0678  565 THR B OG1 
9704 C CG2 . THR B 565 ? 0.3636 0.4524 0.4045 0.0089  0.0109  0.0674  565 THR B CG2 
9705 N N   . MET B 566 ? 0.4131 0.4951 0.4353 0.0194  0.0149  0.0658  566 MET B N   
9706 C CA  . MET B 566 ? 0.4298 0.5142 0.4462 0.0217  0.0166  0.0654  566 MET B CA  
9707 C C   . MET B 566 ? 0.4344 0.5242 0.4535 0.0223  0.0185  0.0701  566 MET B C   
9708 O O   . MET B 566 ? 0.4221 0.5101 0.4454 0.0210  0.0185  0.0731  566 MET B O   
9709 C CB  . MET B 566 ? 0.4575 0.5363 0.4674 0.0212  0.0158  0.0611  566 MET B CB  
9710 C CG  . MET B 566 ? 0.4868 0.5628 0.4991 0.0201  0.0148  0.0617  566 MET B CG  
9711 S SD  . MET B 566 ? 0.5749 0.6420 0.5893 0.0179  0.0122  0.0589  566 MET B SD  
9712 C CE  . MET B 566 ? 0.4983 0.5624 0.5104 0.0183  0.0118  0.0582  566 MET B CE  
9713 N N   . LYS B 567 ? 0.4400 0.5354 0.4554 0.0244  0.0203  0.0708  567 LYS B N   
9714 C CA  . LYS B 567 ? 0.4488 0.5504 0.4658 0.0257  0.0222  0.0752  567 LYS B CA  
9715 C C   . LYS B 567 ? 0.4394 0.5420 0.4518 0.0264  0.0222  0.0741  567 LYS B C   
9716 O O   . LYS B 567 ? 0.4292 0.5320 0.4351 0.0260  0.0220  0.0698  567 LYS B O   
9717 C CB  . LYS B 567 ? 0.4496 0.5579 0.4646 0.0278  0.0243  0.0766  567 LYS B CB  
9718 C CG  . LYS B 567 ? 0.4465 0.5620 0.4626 0.0294  0.0264  0.0813  567 LYS B CG  
9719 C CD  . LYS B 567 ? 0.4762 0.5979 0.4894 0.0317  0.0285  0.0821  567 LYS B CD  
9720 C CE  . LYS B 567 ? 0.4974 0.6266 0.5113 0.0335  0.0305  0.0868  567 LYS B CE  
9721 N NZ  . LYS B 567 ? 0.5221 0.6580 0.5370 0.0355  0.0328  0.0900  567 LYS B NZ  
9722 N N   . PHE B 568 ? 0.4380 0.5415 0.4532 0.0275  0.0228  0.0780  568 PHE B N   
9723 C CA  . PHE B 568 ? 0.4564 0.5644 0.4678 0.0296  0.0230  0.0781  568 PHE B CA  
9724 C C   . PHE B 568 ? 0.4574 0.5753 0.4672 0.0323  0.0252  0.0816  568 PHE B C   
9725 O O   . PHE B 568 ? 0.5075 0.6270 0.5202 0.0330  0.0268  0.0854  568 PHE B O   
9726 C CB  . PHE B 568 ? 0.4588 0.5613 0.4722 0.0309  0.0229  0.0806  568 PHE B CB  
9727 C CG  . PHE B 568 ? 0.4757 0.5694 0.4895 0.0285  0.0207  0.0766  568 PHE B CG  
9728 C CD1 . PHE B 568 ? 0.4610 0.5557 0.4706 0.0274  0.0190  0.0713  568 PHE B CD1 
9729 C CD2 . PHE B 568 ? 0.4815 0.5656 0.4991 0.0268  0.0204  0.0781  568 PHE B CD2 
9730 C CE1 . PHE B 568 ? 0.4533 0.5398 0.4630 0.0255  0.0171  0.0678  568 PHE B CE1 
9731 C CE2 . PHE B 568 ? 0.4748 0.5512 0.4925 0.0246  0.0183  0.0743  568 PHE B CE2 
9732 C CZ  . PHE B 568 ? 0.4572 0.5348 0.4710 0.0244  0.0166  0.0693  568 PHE B CZ  
9733 N N   . HIS B 569 ? 0.4663 0.5923 0.4716 0.0338  0.0252  0.0804  569 HIS B N   
9734 C CA  . HIS B 569 ? 0.4499 0.5870 0.4529 0.0364  0.0270  0.0832  569 HIS B CA  
9735 C C   . HIS B 569 ? 0.4593 0.6039 0.4614 0.0408  0.0276  0.0867  569 HIS B C   
9736 O O   . HIS B 569 ? 0.4608 0.6173 0.4601 0.0432  0.0287  0.0884  569 HIS B O   
9737 C CB  . HIS B 569 ? 0.4526 0.5954 0.4491 0.0337  0.0269  0.0779  569 HIS B CB  
9738 C CG  . HIS B 569 ? 0.4598 0.5956 0.4552 0.0314  0.0273  0.0754  569 HIS B CG  
9739 N ND1 . HIS B 569 ? 0.4699 0.5962 0.4642 0.0287  0.0260  0.0711  569 HIS B ND1 
9740 C CD2 . HIS B 569 ? 0.4869 0.6245 0.4817 0.0325  0.0291  0.0771  569 HIS B CD2 
9741 C CE1 . HIS B 569 ? 0.4735 0.5958 0.4660 0.0286  0.0270  0.0702  569 HIS B CE1 
9742 N NE2 . HIS B 569 ? 0.5103 0.6397 0.5032 0.0309  0.0289  0.0738  569 HIS B NE2 
9743 N N   . ASP B 570 ? 0.4798 0.6179 0.4837 0.0423  0.0270  0.0879  570 ASP B N   
9744 C CA  . ASP B 570 ? 0.4970 0.6406 0.4992 0.0483  0.0280  0.0922  570 ASP B CA  
9745 C C   . ASP B 570 ? 0.4857 0.6158 0.4902 0.0508  0.0297  0.0974  570 ASP B C   
9746 O O   . ASP B 570 ? 0.4729 0.5913 0.4790 0.0483  0.0286  0.0953  570 ASP B O   
9747 C CB  . ASP B 570 ? 0.5123 0.6625 0.5115 0.0484  0.0261  0.0879  570 ASP B CB  
9748 C CG  . ASP B 570 ? 0.5477 0.7077 0.5444 0.0561  0.0273  0.0924  570 ASP B CG  
9749 O OD1 . ASP B 570 ? 0.5225 0.6793 0.5192 0.0617  0.0299  0.0992  570 ASP B OD1 
9750 O OD2 . ASP B 570 ? 0.5749 0.7461 0.5691 0.0568  0.0260  0.0894  570 ASP B OD2 
9751 N N   . GLY B 571 ? 0.4814 0.6123 0.4850 0.0555  0.0327  0.1041  571 GLY B N   
9752 C CA  . GLY B 571 ? 0.4926 0.6089 0.4960 0.0577  0.0353  0.1094  571 GLY B CA  
9753 C C   . GLY B 571 ? 0.4901 0.5997 0.4900 0.0618  0.0353  0.1097  571 GLY B C   
9754 O O   . GLY B 571 ? 0.5048 0.5988 0.5030 0.0626  0.0374  0.1128  571 GLY B O   
9755 N N   . GLU B 572 ? 0.5283 0.6496 0.5264 0.0640  0.0331  0.1061  572 GLU B N   
9756 C CA  . GLU B 572 ? 0.5563 0.6746 0.5507 0.0693  0.0333  0.1067  572 GLU B CA  
9757 C C   . GLU B 572 ? 0.5221 0.6327 0.5185 0.0639  0.0304  0.1004  572 GLU B C   
9758 O O   . GLU B 572 ? 0.5453 0.6516 0.5388 0.0677  0.0305  0.1003  572 GLU B O   
9759 C CB  . GLU B 572 ? 0.6295 0.7683 0.6206 0.0757  0.0330  0.1072  572 GLU B CB  
9760 C CG  . GLU B 572 ? 0.7707 0.9083 0.7557 0.0867  0.0360  0.1135  572 GLU B CG  
9761 C CD  . GLU B 572 ? 0.8087 0.9509 0.7904 0.0934  0.0394  0.1208  572 GLU B CD  
9762 O OE1 . GLU B 572 ? 0.8370 0.9971 0.8201 0.0927  0.0385  0.1201  572 GLU B OE1 
9763 O OE2 . GLU B 572 ? 0.8987 1.0256 0.8754 0.0994  0.0434  0.1272  572 GLU B OE2 
9764 N N   . VAL B 573 ? 0.4738 0.5831 0.4745 0.0559  0.0281  0.0953  573 VAL B N   
9765 C CA  . VAL B 573 ? 0.4398 0.5409 0.4421 0.0508  0.0255  0.0897  573 VAL B CA  
9766 C C   . VAL B 573 ? 0.4407 0.5241 0.4422 0.0517  0.0267  0.0918  573 VAL B C   
9767 O O   . VAL B 573 ? 0.4184 0.4921 0.4196 0.0523  0.0294  0.0965  573 VAL B O   
9768 C CB  . VAL B 573 ? 0.4154 0.5146 0.4216 0.0433  0.0237  0.0854  573 VAL B CB  
9769 C CG1 . VAL B 573 ? 0.4123 0.5023 0.4217 0.0412  0.0253  0.0890  573 VAL B CG1 
9770 C CG2 . VAL B 573 ? 0.4108 0.5037 0.4175 0.0390  0.0210  0.0794  573 VAL B CG2 
9771 N N   . ASP B 574 ? 0.4411 0.5198 0.4414 0.0512  0.0250  0.0880  574 ASP B N   
9772 C CA  . ASP B 574 ? 0.4575 0.5182 0.4572 0.0496  0.0254  0.0880  574 ASP B CA  
9773 C C   . ASP B 574 ? 0.4335 0.4898 0.4381 0.0412  0.0226  0.0829  574 ASP B C   
9774 O O   . ASP B 574 ? 0.4313 0.4894 0.4363 0.0388  0.0199  0.0776  574 ASP B O   
9775 C CB  . ASP B 574 ? 0.4908 0.5484 0.4860 0.0545  0.0253  0.0871  574 ASP B CB  
9776 C CG  . ASP B 574 ? 0.5270 0.5642 0.5199 0.0529  0.0262  0.0870  574 ASP B CG  
9777 O OD1 . ASP B 574 ? 0.5546 0.5809 0.5493 0.0477  0.0271  0.0880  574 ASP B OD1 
9778 O OD2 . ASP B 574 ? 0.5986 0.6310 0.5874 0.0566  0.0262  0.0859  574 ASP B OD2 
9779 N N   . ALA B 575 ? 0.4291 0.4807 0.4369 0.0371  0.0235  0.0847  575 ALA B N   
9780 C CA  . ALA B 575 ? 0.4140 0.4636 0.4264 0.0302  0.0211  0.0806  575 ALA B CA  
9781 C C   . ALA B 575 ? 0.3923 0.4302 0.4040 0.0275  0.0195  0.0772  575 ALA B C   
9782 O O   . ALA B 575 ? 0.3515 0.3902 0.3655 0.0237  0.0168  0.0724  575 ALA B O   
9783 C CB  . ALA B 575 ? 0.4056 0.4536 0.4215 0.0267  0.0228  0.0840  575 ALA B CB  
9784 N N   . SER B 576 ? 0.3993 0.4260 0.4068 0.0302  0.0215  0.0796  576 SER B N   
9785 C CA  . SER B 576 ? 0.4212 0.4350 0.4271 0.0273  0.0205  0.0766  576 SER B CA  
9786 C C   . SER B 576 ? 0.4101 0.4273 0.4151 0.0285  0.0176  0.0715  576 SER B C   
9787 O O   . SER B 576 ? 0.4152 0.4251 0.4205 0.0249  0.0156  0.0676  576 SER B O   
9788 C CB  . SER B 576 ? 0.4316 0.4297 0.4310 0.0300  0.0242  0.0805  576 SER B CB  
9789 O OG  . SER B 576 ? 0.4975 0.4975 0.4914 0.0386  0.0255  0.0824  576 SER B OG  
9790 N N   . TYR B 577 ? 0.4007 0.4303 0.4046 0.0329  0.0173  0.0713  577 TYR B N   
9791 C CA  . TYR B 577 ? 0.4157 0.4504 0.4184 0.0333  0.0149  0.0665  577 TYR B CA  
9792 C C   . TYR B 577 ? 0.4176 0.4516 0.4231 0.0273  0.0120  0.0612  577 TYR B C   
9793 O O   . TYR B 577 ? 0.4099 0.4414 0.4139 0.0263  0.0102  0.0571  577 TYR B O   
9794 C CB  . TYR B 577 ? 0.4165 0.4673 0.4178 0.0370  0.0152  0.0668  577 TYR B CB  
9795 C CG  . TYR B 577 ? 0.4180 0.4742 0.4164 0.0384  0.0139  0.0630  577 TYR B CG  
9796 C CD1 . TYR B 577 ? 0.4166 0.4686 0.4115 0.0439  0.0149  0.0645  577 TYR B CD1 
9797 C CD2 . TYR B 577 ? 0.4078 0.4728 0.4062 0.0343  0.0121  0.0580  577 TYR B CD2 
9798 C CE1 . TYR B 577 ? 0.3956 0.4541 0.3882 0.0452  0.0138  0.0612  577 TYR B CE1 
9799 C CE2 . TYR B 577 ? 0.3695 0.4400 0.3651 0.0346  0.0112  0.0545  577 TYR B CE2 
9800 C CZ  . TYR B 577 ? 0.3808 0.4491 0.3742 0.0401  0.0119  0.0562  577 TYR B CZ  
9801 O OH  . TYR B 577 ? 0.3833 0.4586 0.3742 0.0406  0.0112  0.0529  577 TYR B OH  
9802 N N   . PHE B 578 ? 0.4018 0.4383 0.4110 0.0238  0.0118  0.0616  578 PHE B N   
9803 C CA  . PHE B 578 ? 0.4280 0.4658 0.4388 0.0198  0.0095  0.0572  578 PHE B CA  
9804 C C   . PHE B 578 ? 0.4433 0.4725 0.4568 0.0158  0.0081  0.0560  578 PHE B C   
9805 O O   . PHE B 578 ? 0.4359 0.4661 0.4503 0.0134  0.0062  0.0527  578 PHE B O   
9806 C CB  . PHE B 578 ? 0.4401 0.4873 0.4520 0.0193  0.0101  0.0579  578 PHE B CB  
9807 C CG  . PHE B 578 ? 0.4317 0.4885 0.4405 0.0221  0.0113  0.0585  578 PHE B CG  
9808 C CD1 . PHE B 578 ? 0.4413 0.5025 0.4459 0.0212  0.0105  0.0541  578 PHE B CD1 
9809 C CD2 . PHE B 578 ? 0.4299 0.4918 0.4393 0.0252  0.0134  0.0633  578 PHE B CD2 
9810 C CE1 . PHE B 578 ? 0.4301 0.5020 0.4316 0.0225  0.0116  0.0541  578 PHE B CE1 
9811 C CE2 . PHE B 578 ? 0.4652 0.5383 0.4717 0.0278  0.0143  0.0638  578 PHE B CE2 
9812 C CZ  . PHE B 578 ? 0.4369 0.5157 0.4396 0.0260  0.0133  0.0589  578 PHE B CZ  
9813 N N   . CYS B 579 ? 0.4650 0.4855 0.4785 0.0152  0.0094  0.0586  579 CYS B N   
9814 C CA  . CYS B 579 ? 0.4824 0.4951 0.4979 0.0102  0.0084  0.0574  579 CYS B CA  
9815 C C   . CYS B 579 ? 0.4677 0.4726 0.4805 0.0095  0.0064  0.0531  579 CYS B C   
9816 O O   . CYS B 579 ? 0.4380 0.4393 0.4524 0.0050  0.0047  0.0507  579 CYS B O   
9817 C CB  . CYS B 579 ? 0.5584 0.5623 0.5729 0.0089  0.0114  0.0616  579 CYS B CB  
9818 S SG  . CYS B 579 ? 0.7036 0.7143 0.7222 0.0069  0.0138  0.0665  579 CYS B SG  
9819 N N   . LYS B 580 ? 0.4397 0.4431 0.4482 0.0139  0.0067  0.0524  580 LYS B N   
9820 C CA  . LYS B 580 ? 0.4463 0.4401 0.4510 0.0143  0.0058  0.0494  580 LYS B CA  
9821 C C   . LYS B 580 ? 0.4140 0.4128 0.4158 0.0180  0.0049  0.0468  580 LYS B C   
9822 O O   . LYS B 580 ? 0.4088 0.4178 0.4105 0.0206  0.0056  0.0478  580 LYS B O   
9823 C CB  . LYS B 580 ? 0.4742 0.4558 0.4747 0.0162  0.0087  0.0527  580 LYS B CB  
9824 C CG  . LYS B 580 ? 0.4815 0.4671 0.4791 0.0231  0.0116  0.0572  580 LYS B CG  
9825 C CD  . LYS B 580 ? 0.5114 0.4835 0.5033 0.0258  0.0154  0.0616  580 LYS B CD  
9826 C CE  . LYS B 580 ? 0.5063 0.4855 0.4959 0.0334  0.0184  0.0669  580 LYS B CE  
9827 N NZ  . LYS B 580 ? 0.4922 0.4817 0.4797 0.0402  0.0177  0.0660  580 LYS B NZ  
9828 N N   . LEU B 581 ? 0.4030 0.3949 0.4020 0.0178  0.0036  0.0434  581 LEU B N   
9829 C CA  . LEU B 581 ? 0.4100 0.4054 0.4053 0.0217  0.0036  0.0417  581 LEU B CA  
9830 C C   . LEU B 581 ? 0.4276 0.4248 0.4203 0.0277  0.0064  0.0460  581 LEU B C   
9831 O O   . LEU B 581 ? 0.4738 0.4603 0.4638 0.0296  0.0083  0.0487  581 LEU B O   
9832 C CB  . LEU B 581 ? 0.4264 0.4121 0.4186 0.0212  0.0022  0.0382  581 LEU B CB  
9833 C CG  . LEU B 581 ? 0.4384 0.4261 0.4300 0.0187  -0.0002 0.0332  581 LEU B CG  
9834 C CD1 . LEU B 581 ? 0.4222 0.4177 0.4164 0.0159  -0.0011 0.0322  581 LEU B CD1 
9835 C CD2 . LEU B 581 ? 0.4440 0.4208 0.4345 0.0161  -0.0019 0.0304  581 LEU B CD2 
9836 N N   . PRO B 582 ? 0.4131 0.4238 0.4054 0.0306  0.0069  0.0466  582 PRO B N   
9837 C CA  . PRO B 582 ? 0.4273 0.4422 0.4164 0.0377  0.0094  0.0504  582 PRO B CA  
9838 C C   . PRO B 582 ? 0.4831 0.4909 0.4674 0.0416  0.0097  0.0492  582 PRO B C   
9839 O O   . PRO B 582 ? 0.4846 0.4924 0.4685 0.0391  0.0077  0.0446  582 PRO B O   
9840 C CB  . PRO B 582 ? 0.4216 0.4550 0.4114 0.0383  0.0092  0.0495  582 PRO B CB  
9841 C CG  . PRO B 582 ? 0.3993 0.4351 0.3920 0.0314  0.0073  0.0461  582 PRO B CG  
9842 C CD  . PRO B 582 ? 0.4109 0.4331 0.4044 0.0276  0.0056  0.0435  582 PRO B CD  
9843 N N   . GLU B 583 ? 0.5258 0.5272 0.5055 0.0485  0.0126  0.0534  583 GLU B N   
9844 C CA  . GLU B 583 ? 0.5744 0.5667 0.5480 0.0534  0.0136  0.0529  583 GLU B CA  
9845 C C   . GLU B 583 ? 0.5343 0.5389 0.5074 0.0551  0.0121  0.0493  583 GLU B C   
9846 O O   . GLU B 583 ? 0.4954 0.4917 0.4656 0.0552  0.0114  0.0464  583 GLU B O   
9847 C CB  . GLU B 583 ? 0.6685 0.6533 0.6354 0.0625  0.0178  0.0588  583 GLU B CB  
9848 C CG  . GLU B 583 ? 0.7854 0.7559 0.7514 0.0600  0.0200  0.0623  583 GLU B CG  
9849 C CD  . GLU B 583 ? 0.8774 0.8315 0.8443 0.0510  0.0185  0.0587  583 GLU B CD  
9850 O OE1 . GLU B 583 ? 0.8854 0.8244 0.8462 0.0518  0.0193  0.0570  583 GLU B OE1 
9851 O OE2 . GLU B 583 ? 0.8873 0.8445 0.8607 0.0432  0.0166  0.0574  583 GLU B OE2 
9852 N N   . LYS B 584 ? 0.4823 0.5069 0.4580 0.0556  0.0117  0.0492  584 LYS B N   
9853 C CA  . LYS B 584 ? 0.4778 0.5153 0.4528 0.0556  0.0106  0.0457  584 LYS B CA  
9854 C C   . LYS B 584 ? 0.4823 0.5151 0.4590 0.0472  0.0078  0.0397  584 LYS B C   
9855 O O   . LYS B 584 ? 0.5053 0.5435 0.4803 0.0467  0.0072  0.0364  584 LYS B O   
9856 C CB  . LYS B 584 ? 0.4681 0.5290 0.4448 0.0566  0.0110  0.0466  584 LYS B CB  
9857 C CG  . LYS B 584 ? 0.4727 0.5394 0.4533 0.0482  0.0095  0.0442  584 LYS B CG  
9858 C CD  . LYS B 584 ? 0.4662 0.5534 0.4477 0.0499  0.0106  0.0464  584 LYS B CD  
9859 C CE  . LYS B 584 ? 0.4511 0.5407 0.4352 0.0424  0.0097  0.0446  584 LYS B CE  
9860 N NZ  . LYS B 584 ? 0.4351 0.5366 0.4201 0.0461  0.0112  0.0490  584 LYS B NZ  
9861 N N   . PHE B 585 ? 0.4835 0.5064 0.4631 0.0412  0.0064  0.0385  585 PHE B N   
9862 C CA  . PHE B 585 ? 0.4697 0.4872 0.4501 0.0344  0.0041  0.0335  585 PHE B CA  
9863 C C   . PHE B 585 ? 0.4749 0.4745 0.4548 0.0330  0.0030  0.0326  585 PHE B C   
9864 O O   . PHE B 585 ? 0.4370 0.4314 0.4174 0.0283  0.0010  0.0289  585 PHE B O   
9865 C CB  . PHE B 585 ? 0.4589 0.4814 0.4424 0.0288  0.0033  0.0326  585 PHE B CB  
9866 C CG  . PHE B 585 ? 0.4312 0.4699 0.4139 0.0273  0.0040  0.0315  585 PHE B CG  
9867 C CD1 . PHE B 585 ? 0.4114 0.4564 0.3908 0.0250  0.0038  0.0276  585 PHE B CD1 
9868 C CD2 . PHE B 585 ? 0.4063 0.4535 0.3909 0.0270  0.0049  0.0340  585 PHE B CD2 
9869 C CE1 . PHE B 585 ? 0.4116 0.4711 0.3893 0.0218  0.0047  0.0260  585 PHE B CE1 
9870 C CE2 . PHE B 585 ? 0.3833 0.4452 0.3663 0.0244  0.0056  0.0324  585 PHE B CE2 
9871 C CZ  . PHE B 585 ? 0.3827 0.4507 0.3620 0.0213  0.0056  0.0283  585 PHE B CZ  
9872 N N   . ARG B 586 ? 0.5186 0.5088 0.4968 0.0369  0.0047  0.0361  586 ARG B N   
9873 C CA  . ARG B 586 ? 0.5635 0.5374 0.5412 0.0336  0.0041  0.0354  586 ARG B CA  
9874 C C   . ARG B 586 ? 0.5821 0.5456 0.5557 0.0337  0.0031  0.0318  586 ARG B C   
9875 O O   . ARG B 586 ? 0.6188 0.5728 0.5929 0.0286  0.0014  0.0293  586 ARG B O   
9876 C CB  . ARG B 586 ? 0.5949 0.5599 0.5709 0.0361  0.0069  0.0402  586 ARG B CB  
9877 C CG  . ARG B 586 ? 0.6555 0.6083 0.6329 0.0296  0.0063  0.0396  586 ARG B CG  
9878 C CD  . ARG B 586 ? 0.7468 0.6980 0.7254 0.0293  0.0087  0.0444  586 ARG B CD  
9879 N NE  . ARG B 586 ? 0.8255 0.7614 0.7966 0.0333  0.0125  0.0478  586 ARG B NE  
9880 C CZ  . ARG B 586 ? 0.9147 0.8330 0.8813 0.0290  0.0135  0.0467  586 ARG B CZ  
9881 N NH1 . ARG B 586 ? 0.8765 0.7931 0.8467 0.0208  0.0104  0.0422  586 ARG B NH1 
9882 N NH2 . ARG B 586 ? 0.8817 0.7838 0.8392 0.0331  0.0179  0.0500  586 ARG B NH2 
9883 N N   . PHE B 587 ? 0.5724 0.5393 0.5419 0.0393  0.0042  0.0316  587 PHE B N   
9884 C CA  . PHE B 587 ? 0.6073 0.5631 0.5716 0.0407  0.0039  0.0289  587 PHE B CA  
9885 C C   . PHE B 587 ? 0.5923 0.5569 0.5561 0.0406  0.0024  0.0250  587 PHE B C   
9886 O O   . PHE B 587 ? 0.5674 0.5257 0.5265 0.0434  0.0026  0.0232  587 PHE B O   
9887 C CB  . PHE B 587 ? 0.6404 0.5869 0.5976 0.0488  0.0074  0.0324  587 PHE B CB  
9888 C CG  . PHE B 587 ? 0.6986 0.6349 0.6543 0.0493  0.0099  0.0366  587 PHE B CG  
9889 C CD1 . PHE B 587 ? 0.6991 0.6199 0.6542 0.0427  0.0094  0.0353  587 PHE B CD1 
9890 C CD2 . PHE B 587 ? 0.6983 0.6415 0.6529 0.0561  0.0128  0.0419  587 PHE B CD2 
9891 C CE1 . PHE B 587 ? 0.7078 0.6188 0.6608 0.0420  0.0121  0.0391  587 PHE B CE1 
9892 C CE2 . PHE B 587 ? 0.7335 0.6660 0.6857 0.0565  0.0156  0.0461  587 PHE B CE2 
9893 C CZ  . PHE B 587 ? 0.7144 0.6301 0.6656 0.0492  0.0154  0.0446  587 PHE B CZ  
9894 N N   . VAL B 588 ? 0.5665 0.5447 0.5342 0.0371  0.0013  0.0237  588 VAL B N   
9895 C CA  . VAL B 588 ? 0.5297 0.5139 0.4961 0.0349  0.0001  0.0197  588 VAL B CA  
9896 C C   . VAL B 588 ? 0.5029 0.4744 0.4681 0.0311  -0.0020 0.0160  588 VAL B C   
9897 O O   . VAL B 588 ? 0.4943 0.4586 0.4619 0.0275  -0.0034 0.0160  588 VAL B O   
9898 C CB  . VAL B 588 ? 0.5259 0.5237 0.4948 0.0306  0.0000  0.0187  588 VAL B CB  
9899 C CG1 . VAL B 588 ? 0.5419 0.5538 0.5121 0.0340  0.0019  0.0222  588 VAL B CG1 
9900 C CG2 . VAL B 588 ? 0.4857 0.4787 0.4577 0.0253  -0.0015 0.0181  588 VAL B CG2 
9901 N N   . LYS B 589 ? 0.5230 0.4925 0.4843 0.0322  -0.0024 0.0131  589 LYS B N   
9902 C CA  . LYS B 589 ? 0.5328 0.4915 0.4924 0.0290  -0.0046 0.0095  589 LYS B CA  
9903 C C   . LYS B 589 ? 0.4952 0.4575 0.4563 0.0236  -0.0062 0.0071  589 LYS B C   
9904 O O   . LYS B 589 ? 0.4838 0.4556 0.4444 0.0224  -0.0053 0.0065  589 LYS B O   
9905 C CB  . LYS B 589 ? 0.5595 0.5152 0.5138 0.0321  -0.0042 0.0072  589 LYS B CB  
9906 C CG  . LYS B 589 ? 0.6382 0.5818 0.5885 0.0367  -0.0032 0.0082  589 LYS B CG  
9907 C CD  . LYS B 589 ? 0.6923 0.6247 0.6384 0.0353  -0.0048 0.0042  589 LYS B CD  
9908 C CE  . LYS B 589 ? 0.7287 0.6668 0.6710 0.0383  -0.0042 0.0022  589 LYS B CE  
9909 N NZ  . LYS B 589 ? 0.7237 0.6567 0.6640 0.0346  -0.0065 -0.0020 589 LYS B NZ  
9910 N N   . ILE B 590 ? 0.5023 0.4570 0.4645 0.0205  -0.0083 0.0056  590 ILE B N   
9911 C CA  . ILE B 590 ? 0.4932 0.4498 0.4553 0.0171  -0.0096 0.0036  590 ILE B CA  
9912 C C   . ILE B 590 ? 0.5078 0.4570 0.4665 0.0161  -0.0117 0.0002  590 ILE B C   
9913 O O   . ILE B 590 ? 0.5591 0.5084 0.5168 0.0144  -0.0128 -0.0011 590 ILE B O   
9914 C CB  . ILE B 590 ? 0.4842 0.4434 0.4511 0.0149  -0.0101 0.0058  590 ILE B CB  
9915 C CG1 . ILE B 590 ? 0.4888 0.4415 0.4583 0.0133  -0.0121 0.0059  590 ILE B CG1 
9916 C CG2 . ILE B 590 ? 0.4636 0.4300 0.4333 0.0162  -0.0080 0.0093  590 ILE B CG2 
9917 C CD1 . ILE B 590 ? 0.5093 0.4663 0.4838 0.0110  -0.0126 0.0078  590 ILE B CD1 
9918 N N   . ASN B 591 ? 0.5276 0.4702 0.4838 0.0179  -0.0121 -0.0010 591 ASN B N   
9919 C CA  . ASN B 591 ? 0.5442 0.4804 0.4967 0.0171  -0.0141 -0.0045 591 ASN B CA  
9920 C C   . ASN B 591 ? 0.5360 0.4717 0.4832 0.0195  -0.0130 -0.0065 591 ASN B C   
9921 O O   . ASN B 591 ? 0.5160 0.4512 0.4618 0.0227  -0.0114 -0.0056 591 ASN B O   
9922 C CB  . ASN B 591 ? 0.5748 0.5024 0.5277 0.0160  -0.0157 -0.0052 591 ASN B CB  
9923 C CG  . ASN B 591 ? 0.6201 0.5495 0.5781 0.0124  -0.0171 -0.0040 591 ASN B CG  
9924 O OD1 . ASN B 591 ? 0.6428 0.5779 0.6027 0.0109  -0.0185 -0.0043 591 ASN B OD1 
9925 N ND2 . ASN B 591 ? 0.6096 0.5338 0.5691 0.0110  -0.0165 -0.0025 591 ASN B ND2 
9926 N N   . ARG B 592 ? 0.5091 0.4450 0.4526 0.0184  -0.0135 -0.0088 592 ARG B N   
9927 C CA  . ARG B 592 ? 0.5281 0.4630 0.4659 0.0199  -0.0125 -0.0111 592 ARG B CA  
9928 C C   . ARG B 592 ? 0.5440 0.4704 0.4791 0.0216  -0.0142 -0.0132 592 ARG B C   
9929 O O   . ARG B 592 ? 0.5830 0.5046 0.5185 0.0200  -0.0167 -0.0145 592 ARG B O   
9930 C CB  . ARG B 592 ? 0.5322 0.4667 0.4653 0.0180  -0.0123 -0.0129 592 ARG B CB  
9931 C CG  . ARG B 592 ? 0.4923 0.4331 0.4228 0.0161  -0.0093 -0.0125 592 ARG B CG  
9932 C CD  . ARG B 592 ? 0.4557 0.3918 0.3786 0.0145  -0.0085 -0.0146 592 ARG B CD  
9933 N NE  . ARG B 592 ? 0.4481 0.3865 0.3654 0.0131  -0.0057 -0.0162 592 ARG B NE  
9934 C CZ  . ARG B 592 ? 0.4626 0.4019 0.3739 0.0092  -0.0026 -0.0169 592 ARG B CZ  
9935 N NH1 . ARG B 592 ? 0.4553 0.3923 0.3650 0.0074  -0.0017 -0.0160 592 ARG B NH1 
9936 N NH2 . ARG B 592 ? 0.4427 0.3849 0.3487 0.0070  -0.0001 -0.0186 592 ARG B NH2 
9937 N N   . LYS B 593 ? 0.5782 0.5038 0.5102 0.0246  -0.0127 -0.0137 593 LYS B N   
9938 C CA  . LYS B 593 ? 0.6701 0.5873 0.5971 0.0262  -0.0139 -0.0166 593 LYS B CA  
9939 C C   . LYS B 593 ? 0.6916 0.6115 0.6142 0.0298  -0.0117 -0.0172 593 LYS B C   
9940 O O   . LYS B 593 ? 0.6833 0.6105 0.6071 0.0322  -0.0093 -0.0150 593 LYS B O   
9941 C CB  . LYS B 593 ? 0.7161 0.6240 0.6435 0.0266  -0.0149 -0.0166 593 LYS B CB  
9942 C CG  . LYS B 593 ? 0.7852 0.6839 0.7079 0.0257  -0.0172 -0.0203 593 LYS B CG  
9943 C CD  . LYS B 593 ? 0.8168 0.7043 0.7351 0.0280  -0.0162 -0.0210 593 LYS B CD  
9944 C CE  . LYS B 593 ? 0.8529 0.7325 0.7645 0.0283  -0.0176 -0.0251 593 LYS B CE  
9945 N NZ  . LYS B 593 ? 0.8497 0.7179 0.7544 0.0322  -0.0155 -0.0257 593 LYS B NZ  
9946 N N   . ALA B 594 ? 0.7230 0.6384 0.6402 0.0303  -0.0124 -0.0202 594 ALA B N   
9947 C CA  . ALA B 594 ? 0.6860 0.6044 0.5987 0.0337  -0.0102 -0.0209 594 ALA B CA  
9948 C C   . ALA B 594 ? 0.7273 0.6406 0.6381 0.0392  -0.0091 -0.0202 594 ALA B C   
9949 O O   . ALA B 594 ? 0.6768 0.5784 0.5856 0.0395  -0.0106 -0.0214 594 ALA B O   
9950 C CB  . ALA B 594 ? 0.6379 0.5521 0.5450 0.0330  -0.0111 -0.0242 594 ALA B CB  
9951 N N   . SER B 595 ? 0.7176 0.6401 0.6282 0.0434  -0.0062 -0.0181 595 SER B N   
9952 C CA  . SER B 595 ? 0.7969 0.7145 0.7034 0.0505  -0.0044 -0.0171 595 SER B CA  
9953 C C   . SER B 595 ? 0.7646 0.6893 0.6665 0.0552  -0.0022 -0.0178 595 SER B C   
9954 O O   . SER B 595 ? 0.8071 0.7346 0.7064 0.0626  0.0002  -0.0157 595 SER B O   
9955 C CB  . SER B 595 ? 0.8116 0.7331 0.7214 0.0539  -0.0026 -0.0129 595 SER B CB  
9956 O OG  . SER B 595 ? 0.8692 0.8091 0.7832 0.0539  -0.0010 -0.0107 595 SER B OG  
9957 N N   . ILE B 596 ? 0.6775 0.6052 0.5777 0.0515  -0.0029 -0.0206 596 ILE B N   
9958 C CA  . ILE B 596 ? 0.6612 0.5947 0.5565 0.0550  -0.0010 -0.0218 596 ILE B CA  
9959 C C   . ILE B 596 ? 0.6760 0.6008 0.5665 0.0520  -0.0027 -0.0256 596 ILE B C   
9960 O O   . ILE B 596 ? 0.6453 0.5687 0.5302 0.0557  -0.0017 -0.0272 596 ILE B O   
9961 C CB  . ILE B 596 ? 0.6150 0.5690 0.5131 0.0537  0.0015  -0.0203 596 ILE B CB  
9962 C CG1 . ILE B 596 ? 0.5611 0.5191 0.4620 0.0447  0.0007  -0.0212 596 ILE B CG1 
9963 C CG2 . ILE B 596 ? 0.6188 0.5837 0.5204 0.0589  0.0034  -0.0164 596 ILE B CG2 
9964 C CD1 . ILE B 596 ? 0.5339 0.5060 0.4328 0.0407  0.0033  -0.0222 596 ILE B CD1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   1   MET MET A . n 
A 1 2   VAL 2   2   2   VAL VAL A . n 
A 1 3   HIS 3   3   3   HIS HIS A . n 
A 1 4   TYR 4   4   4   TYR TYR A . n 
A 1 5   TYR 5   5   5   TYR TYR A . n 
A 1 6   ARG 6   6   6   ARG ARG A . n 
A 1 7   LEU 7   7   7   LEU LEU A . n 
A 1 8   SER 8   8   8   SER SER A . n 
A 1 9   LEU 9   9   9   LEU LEU A . n 
A 1 10  LYS 10  10  10  LYS LYS A . n 
A 1 11  SER 11  11  11  SER SER A . n 
A 1 12  ARG 12  12  12  ARG ARG A . n 
A 1 13  GLN 13  13  13  GLN GLN A . n 
A 1 14  LYS 14  14  14  LYS LYS A . n 
A 1 15  ALA 15  15  15  ALA ALA A . n 
A 1 16  PRO 16  16  16  PRO PRO A . n 
A 1 17  LYS 17  17  17  LYS LYS A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  VAL 19  19  19  VAL VAL A . n 
A 1 20  ASN 20  20  20  ASN ASN A . n 
A 1 21  SER 21  21  21  SER SER A . n 
A 1 22  LYS 22  22  22  LYS LYS A . n 
A 1 23  TYR 23  23  23  TYR TYR A . n 
A 1 24  ASN 24  24  24  ASN ASN A . n 
A 1 25  SER 25  25  25  SER SER A . n 
A 1 26  ILE 26  26  26  ILE ILE A . n 
A 1 27  LEU 27  27  27  LEU LEU A . n 
A 1 28  ASN 28  28  28  ASN ASN A . n 
A 1 29  ILE 29  29  29  ILE ILE A . n 
A 1 30  ALA 30  30  30  ALA ALA A . n 
A 1 31  LEU 31  31  31  LEU LEU A . n 
A 1 32  LYS 32  32  32  LYS LYS A . n 
A 1 33  ASN 33  33  33  ASN ASN A . n 
A 1 34  PHE 34  34  34  PHE PHE A . n 
A 1 35  ARG 35  35  35  ARG ARG A . n 
A 1 36  LEU 36  36  36  LEU LEU A . n 
A 1 37  CYS 37  37  37  CYS CYS A . n 
A 1 38  LYS 38  38  38  LYS LYS A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  HIS 40  40  40  HIS HIS A . n 
A 1 41  LYS 41  41  41  LYS LYS A . n 
A 1 42  THR 42  42  42  THR THR A . n 
A 1 43  LYS 43  43  43  LYS LYS A . n 
A 1 44  LYS 44  44  44  LYS LYS A . n 
A 1 45  PRO 45  45  45  PRO PRO A . n 
A 1 46  VAL 46  46  46  VAL VAL A . n 
A 1 47  GLN 47  47  47  GLN GLN A . n 
A 1 48  ILE 48  48  48  ILE ILE A . n 
A 1 49  LEU 49  49  49  LEU LEU A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  LEU 51  51  51  LEU LEU A . n 
A 1 52  LEU 52  52  52  LEU LEU A . n 
A 1 53  GLN 53  53  53  GLN GLN A . n 
A 1 54  GLU 54  54  54  GLU GLU A . n 
A 1 55  ILE 55  55  55  ILE ILE A . n 
A 1 56  ILE 56  56  56  ILE ILE A . n 
A 1 57  PRO 57  57  57  PRO PRO A . n 
A 1 58  LYS 58  58  58  LYS LYS A . n 
A 1 59  SER 59  59  59  SER SER A . n 
A 1 60  TYR 60  60  60  TYR TYR A . n 
A 1 61  PHE 61  61  61  PHE PHE A . n 
A 1 62  GLY 62  62  62  GLY GLY A . n 
A 1 63  THR 63  63  63  THR THR A . n 
A 1 64  THR 64  64  64  THR THR A . n 
A 1 65  THR 65  65  65  THR THR A . n 
A 1 66  ASN 66  66  66  ASN ASN A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  LYS 68  68  68  LYS LYS A . n 
A 1 69  ARG 69  69  69  ARG ARG A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  TYR 71  71  71  TYR TYR A . n 
A 1 72  LYS 72  72  72  LYS LYS A . n 
A 1 73  VAL 73  73  73  VAL VAL A . n 
A 1 74  VAL 74  74  74  VAL VAL A . n 
A 1 75  GLU 75  75  75  GLU GLU A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  ILE 77  77  77  ILE ILE A . n 
A 1 78  LEU 78  78  78  LEU LEU A . n 
A 1 79  THR 79  79  79  THR THR A . n 
A 1 80  GLN 80  80  80  GLN GLN A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  SER 82  82  82  SER SER A . n 
A 1 83  PHE 83  83  83  PHE PHE A . n 
A 1 84  GLU 84  84  84  GLU GLU A . n 
A 1 85  CYS 85  85  85  CYS CYS A . n 
A 1 86  ILE 86  86  86  ILE ILE A . n 
A 1 87  HIS 87  87  87  HIS HIS A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  SER 89  89  89  SER SER A . n 
A 1 90  VAL 90  90  90  VAL VAL A . n 
A 1 91  LEU 91  91  91  LEU LEU A . n 
A 1 92  HIS 92  92  92  HIS HIS A . n 
A 1 93  LYS 93  93  93  LYS LYS A . n 
A 1 94  CYS 94  94  94  CYS CYS A . n 
A 1 95  TYR 95  95  95  TYR TYR A . n 
A 1 96  ASP 96  96  96  ASP ASP A . n 
A 1 97  TYR 97  97  97  TYR TYR A . n 
A 1 98  ASP 98  98  98  ASP ASP A . n 
A 1 99  ALA 99  99  99  ALA ALA A . n 
A 1 100 ILE 100 100 100 ILE ILE A . n 
A 1 101 PRO 101 101 101 PRO PRO A . n 
A 1 102 TRP 102 102 102 TRP TRP A . n 
A 1 103 LEU 103 103 103 LEU LEU A . n 
A 1 104 GLN 104 104 104 GLN GLN A . n 
A 1 105 ASN 105 105 105 ASN ASN A . n 
A 1 106 VAL 106 106 106 VAL VAL A . n 
A 1 107 GLU 107 107 107 GLU GLU A . n 
A 1 108 PRO 108 108 108 PRO PRO A . n 
A 1 109 ASN 109 109 109 ASN ASN A . n 
A 1 110 LEU 110 110 110 LEU LEU A . n 
A 1 111 ARG 111 111 111 ARG ARG A . n 
A 1 112 PRO 112 112 112 PRO PRO A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 LEU 114 114 114 LEU LEU A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 LEU 116 116 116 LEU LEU A . n 
A 1 117 LYS 117 117 117 LYS LYS A . n 
A 1 118 HIS 118 118 118 HIS HIS A . n 
A 1 119 ASN 119 119 119 ASN ASN A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 PHE 121 121 121 PHE PHE A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 ASP 124 124 124 ASP ASP A . n 
A 1 125 ASN 125 125 125 ASN ASN A . n 
A 1 126 ILE 126 126 126 ILE ILE A . n 
A 1 127 VAL 127 127 127 VAL VAL A . n 
A 1 128 LYS 128 128 128 LYS LYS A . n 
A 1 129 PRO 129 129 129 PRO PRO A . n 
A 1 130 ILE 130 130 130 ILE ILE A . n 
A 1 131 ILE 131 131 131 ILE ILE A . n 
A 1 132 ALA 132 132 132 ALA ALA A . n 
A 1 133 PHE 133 133 133 PHE PHE A . n 
A 1 134 TYR 134 134 134 TYR TYR A . n 
A 1 135 TYR 135 135 135 TYR TYR A . n 
A 1 136 LYS 136 136 136 LYS LYS A . n 
A 1 137 PRO 137 137 137 PRO PRO A . n 
A 1 138 ILE 138 138 138 ILE ILE A . n 
A 1 139 LYS 139 139 139 LYS LYS A . n 
A 1 140 THR 140 140 140 THR THR A . n 
A 1 141 LEU 141 141 141 LEU LEU A . n 
A 1 142 ASN 142 142 142 ASN ASN A . n 
A 1 143 GLY 143 143 143 GLY GLY A . n 
A 1 144 HIS 144 144 144 HIS HIS A . n 
A 1 145 GLU 145 145 145 GLU GLU A . n 
A 1 146 ILE 146 146 146 ILE ILE A . n 
A 1 147 LYS 147 147 147 LYS LYS A . n 
A 1 148 PHE 148 148 148 PHE PHE A . n 
A 1 149 ILE 149 149 149 ILE ILE A . n 
A 1 150 ARG 150 150 150 ARG ARG A . n 
A 1 151 LYS 151 151 151 LYS LYS A . n 
A 1 152 GLU 152 152 152 GLU GLU A . n 
A 1 153 GLU 153 153 153 GLU GLU A . n 
A 1 154 TYR 154 154 154 TYR TYR A . n 
A 1 155 ILE 155 155 155 ILE ILE A . n 
A 1 156 SER 156 156 156 SER SER A . n 
A 1 157 PHE 157 157 157 PHE PHE A . n 
A 1 158 GLU 158 158 158 GLU GLU A . n 
A 1 159 SER 159 159 159 SER SER A . n 
A 1 160 LYS 160 160 160 LYS LYS A . n 
A 1 161 VAL 161 161 161 VAL VAL A . n 
A 1 162 PHE 162 162 162 PHE PHE A . n 
A 1 163 HIS 163 163 163 HIS HIS A . n 
A 1 164 LYS 164 164 164 LYS LYS A . n 
A 1 165 LEU 165 165 165 LEU LEU A . n 
A 1 166 LYS 166 166 166 LYS LYS A . n 
A 1 167 LYS 167 167 167 LYS LYS A . n 
A 1 168 MET 168 168 168 MET MET A . n 
A 1 169 LYS 169 169 169 LYS LYS A . n 
A 1 170 TYR 170 170 170 TYR TYR A . n 
A 1 171 LEU 171 171 171 LEU LEU A . n 
A 1 172 VAL 172 172 172 VAL VAL A . n 
A 1 173 GLU 173 173 173 GLU GLU A . n 
A 1 174 VAL 174 174 174 VAL VAL A . n 
A 1 175 GLN 175 175 175 GLN GLN A . n 
A 1 176 ASP 176 176 176 ASP ASP A . n 
A 1 177 GLU 177 177 177 GLU GLU A . n 
A 1 178 VAL 178 178 178 VAL VAL A . n 
A 1 179 LYS 179 179 179 LYS LYS A . n 
A 1 180 PRO 180 180 180 PRO PRO A . n 
A 1 181 ARG 181 181 181 ARG ARG A . n 
A 1 182 GLY 182 182 182 GLY GLY A . n 
A 1 183 VAL 183 183 183 VAL VAL A . n 
A 1 184 LEU 184 184 184 LEU LEU A . n 
A 1 185 ASN 185 185 185 ASN ASN A . n 
A 1 186 ILE 186 186 186 ILE ILE A . n 
A 1 187 ILE 187 187 187 ILE ILE A . n 
A 1 188 PRO 188 188 188 PRO PRO A . n 
A 1 189 LYS 189 189 189 LYS LYS A . n 
A 1 190 GLN 190 190 190 GLN GLN A . n 
A 1 191 ASP 191 191 191 ASP ASP A . n 
A 1 192 ASN 192 192 192 ASN ASN A . n 
A 1 193 PHE 193 193 193 PHE PHE A . n 
A 1 194 ARG 194 194 194 ARG ARG A . n 
A 1 195 ALA 195 195 195 ALA ALA A . n 
A 1 196 ILE 196 196 196 ILE ILE A . n 
A 1 197 VAL 197 197 197 VAL VAL A . n 
A 1 198 SER 198 198 198 SER SER A . n 
A 1 199 ILE 199 199 199 ILE ILE A . n 
A 1 200 PHE 200 200 200 PHE PHE A . n 
A 1 201 PRO 201 201 201 PRO PRO A . n 
A 1 202 ASP 202 202 202 ASP ASP A . n 
A 1 203 SER 203 203 203 SER SER A . n 
A 1 204 ALA 204 204 204 ALA ALA A . n 
A 1 205 ARG 205 205 205 ARG ARG A . n 
A 1 206 LYS 206 206 206 LYS LYS A . n 
A 1 207 PRO 207 207 207 PRO PRO A . n 
A 1 208 PHE 208 208 208 PHE PHE A . n 
A 1 209 PHE 209 209 209 PHE PHE A . n 
A 1 210 LYS 210 210 210 LYS LYS A . n 
A 1 211 LEU 211 211 211 LEU LEU A . n 
A 1 212 LEU 212 212 212 LEU LEU A . n 
A 1 213 THR 213 213 213 THR THR A . n 
A 1 214 SER 214 214 214 SER SER A . n 
A 1 215 LYS 215 215 215 LYS LYS A . n 
A 1 216 ILE 216 216 216 ILE ILE A . n 
A 1 217 TYR 217 217 217 TYR TYR A . n 
A 1 218 LYS 218 218 218 LYS LYS A . n 
A 1 219 VAL 219 219 219 VAL VAL A . n 
A 1 220 LEU 220 220 220 LEU LEU A . n 
A 1 221 GLU 221 221 221 GLU GLU A . n 
A 1 222 GLU 222 222 222 GLU GLU A . n 
A 1 223 LYS 223 223 223 LYS LYS A . n 
A 1 224 TYR 224 224 224 TYR TYR A . n 
A 1 225 LYS 225 225 225 LYS LYS A . n 
A 1 226 THR 226 226 226 THR THR A . n 
A 1 227 SER 227 227 227 SER SER A . n 
A 1 228 GLY 228 228 228 GLY GLY A . n 
A 1 229 SER 229 229 229 SER SER A . n 
A 1 230 LEU 230 230 230 LEU LEU A . n 
A 1 231 TYR 231 231 231 TYR TYR A . n 
A 1 232 THR 232 232 232 THR THR A . n 
A 1 233 CYS 233 233 233 CYS CYS A . n 
A 1 234 TRP 234 234 234 TRP TRP A . n 
A 1 235 SER 235 235 235 SER SER A . n 
A 1 236 GLU 236 236 236 GLU GLU A . n 
A 1 237 PHE 237 237 237 PHE PHE A . n 
A 1 238 THR 238 238 238 THR THR A . n 
A 1 239 GLN 239 239 239 GLN GLN A . n 
A 1 240 LYS 240 240 240 LYS LYS A . n 
A 1 241 THR 241 241 241 THR THR A . n 
A 1 242 GLN 242 242 242 GLN GLN A . n 
A 1 243 GLY 243 243 243 GLY GLY A . n 
A 1 244 GLN 244 244 244 GLN GLN A . n 
A 1 245 ILE 245 245 245 ILE ILE A . n 
A 1 246 TYR 246 246 246 TYR TYR A . n 
A 1 247 GLY 247 247 247 GLY GLY A . n 
A 1 248 ILE 248 248 248 ILE ILE A . n 
A 1 249 LYS 249 249 249 LYS LYS A . n 
A 1 250 VAL 250 250 250 VAL VAL A . n 
A 1 251 ASP 251 251 251 ASP ASP A . n 
A 1 252 ILE 252 252 252 ILE ILE A . n 
A 1 253 ARG 253 253 253 ARG ARG A . n 
A 1 254 ASP 254 254 254 ASP ASP A . n 
A 1 255 ALA 255 255 255 ALA ALA A . n 
A 1 256 TYR 256 256 256 TYR TYR A . n 
A 1 257 GLY 257 257 257 GLY GLY A . n 
A 1 258 ASN 258 258 258 ASN ASN A . n 
A 1 259 VAL 259 259 259 VAL VAL A . n 
A 1 260 LYS 260 260 260 LYS LYS A . n 
A 1 261 ILE 261 261 261 ILE ILE A . n 
A 1 262 PRO 262 262 262 PRO PRO A . n 
A 1 263 VAL 263 263 263 VAL VAL A . n 
A 1 264 LEU 264 264 264 LEU LEU A . n 
A 1 265 CYS 265 265 265 CYS CYS A . n 
A 1 266 LYS 266 266 266 LYS LYS A . n 
A 1 267 LEU 267 267 267 LEU LEU A . n 
A 1 268 ILE 268 268 268 ILE ILE A . n 
A 1 269 GLN 269 269 269 GLN GLN A . n 
A 1 270 SER 270 270 270 SER SER A . n 
A 1 271 ILE 271 271 271 ILE ILE A . n 
A 1 272 PRO 272 272 272 PRO PRO A . n 
A 1 273 THR 273 273 273 THR THR A . n 
A 1 274 HIS 274 274 274 HIS HIS A . n 
A 1 275 LEU 275 275 275 LEU LEU A . n 
A 1 276 LEU 276 276 276 LEU LEU A . n 
A 1 277 ASP 277 277 277 ASP ASP A . n 
A 1 278 SER 278 278 278 SER SER A . n 
A 1 279 GLU 279 279 279 GLU GLU A . n 
A 1 280 LYS 280 280 280 LYS LYS A . n 
A 1 281 LYS 281 281 281 LYS LYS A . n 
A 1 282 ASN 282 282 282 ASN ASN A . n 
A 1 283 PHE 283 283 283 PHE PHE A . n 
A 1 284 ILE 284 284 284 ILE ILE A . n 
A 1 285 VAL 285 285 285 VAL VAL A . n 
A 1 286 ASP 286 286 286 ASP ASP A . n 
A 1 287 HIS 287 287 287 HIS HIS A . n 
A 1 288 ILE 288 288 288 ILE ILE A . n 
A 1 289 SER 289 289 289 SER SER A . n 
A 1 290 ASN 290 290 290 ASN ASN A . n 
A 1 291 GLN 291 291 291 GLN GLN A . n 
A 1 292 PHE 292 292 292 PHE PHE A . n 
A 1 293 VAL 293 293 293 VAL VAL A . n 
A 1 294 ALA 294 294 294 ALA ALA A . n 
A 1 295 PHE 295 295 295 PHE PHE A . n 
A 1 296 ARG 296 296 296 ARG ARG A . n 
A 1 297 ARG 297 297 297 ARG ARG A . n 
A 1 298 LYS 298 298 298 LYS LYS A . n 
A 1 299 ILE 299 299 299 ILE ILE A . n 
A 1 300 TYR 300 300 300 TYR TYR A . n 
A 1 301 LYS 301 301 301 LYS LYS A . n 
A 1 302 TRP 302 302 302 TRP TRP A . n 
A 1 303 ASN 303 303 303 ASN ASN A . n 
A 1 304 HIS 304 304 304 HIS HIS A . n 
A 1 305 GLY 305 305 305 GLY GLY A . n 
A 1 306 LEU 306 306 306 LEU LEU A . n 
A 1 307 LEU 307 307 307 LEU LEU A . n 
A 1 308 GLN 308 308 308 GLN GLN A . n 
A 1 309 GLY 309 309 309 GLY GLY A . n 
A 1 310 ASP 310 310 310 ASP ASP A . n 
A 1 311 PRO 311 311 311 PRO PRO A . n 
A 1 312 LEU 312 312 312 LEU LEU A . n 
A 1 313 SER 313 313 313 SER SER A . n 
A 1 314 GLY 314 314 314 GLY GLY A . n 
A 1 315 CYS 315 315 315 CYS CYS A . n 
A 1 316 LEU 316 316 316 LEU LEU A . n 
A 1 317 CYS 317 317 317 CYS CYS A . n 
A 1 318 GLU 318 318 318 GLU GLU A . n 
A 1 319 LEU 319 319 319 LEU LEU A . n 
A 1 320 TYR 320 320 320 TYR TYR A . n 
A 1 321 MET 321 321 321 MET MET A . n 
A 1 322 ALA 322 322 322 ALA ALA A . n 
A 1 323 PHE 323 323 323 PHE PHE A . n 
A 1 324 MET 324 324 324 MET MET A . n 
A 1 325 ASP 325 325 325 ASP ASP A . n 
A 1 326 ARG 326 326 326 ARG ARG A . n 
A 1 327 LEU 327 327 327 LEU LEU A . n 
A 1 328 TYR 328 328 328 TYR TYR A . n 
A 1 329 PHE 329 329 329 PHE PHE A . n 
A 1 330 SER 330 330 330 SER SER A . n 
A 1 331 ASN 331 331 331 ASN ASN A . n 
A 1 332 LEU 332 332 332 LEU LEU A . n 
A 1 333 ASP 333 333 333 ASP ASP A . n 
A 1 334 LYS 334 334 334 LYS LYS A . n 
A 1 335 ASP 335 335 335 ASP ASP A . n 
A 1 336 ALA 336 336 336 ALA ALA A . n 
A 1 337 PHE 337 337 337 PHE PHE A . n 
A 1 338 ILE 338 338 338 ILE ILE A . n 
A 1 339 HIS 339 339 339 HIS HIS A . n 
A 1 340 ARG 340 340 340 ARG ARG A . n 
A 1 341 THR 341 341 341 THR THR A . n 
A 1 342 VAL 342 342 342 VAL VAL A . n 
A 1 343 ASP 343 343 343 ASP ASP A . n 
A 1 344 ASP 344 344 344 ASP ASP A . n 
A 1 345 TYR 345 345 345 TYR TYR A . n 
A 1 346 PHE 346 346 346 PHE PHE A . n 
A 1 347 PHE 347 347 347 PHE PHE A . n 
A 1 348 CYS 348 348 348 CYS CYS A . n 
A 1 349 SER 349 349 349 SER SER A . n 
A 1 350 PRO 350 350 350 PRO PRO A . n 
A 1 351 HIS 351 351 351 HIS HIS A . n 
A 1 352 PRO 352 352 352 PRO PRO A . n 
A 1 353 HIS 353 353 353 HIS HIS A . n 
A 1 354 LYS 354 354 354 LYS LYS A . n 
A 1 355 VAL 355 355 355 VAL VAL A . n 
A 1 356 TYR 356 356 356 TYR TYR A . n 
A 1 357 ASP 357 357 357 ASP ASP A . n 
A 1 358 PHE 358 358 358 PHE PHE A . n 
A 1 359 GLU 359 359 359 GLU GLU A . n 
A 1 360 LEU 360 360 360 LEU LEU A . n 
A 1 361 LEU 361 361 361 LEU LEU A . n 
A 1 362 ILE 362 362 362 ILE ILE A . n 
A 1 363 LYS 363 363 363 LYS LYS A . n 
A 1 364 GLY 364 364 364 GLY GLY A . n 
A 1 365 VAL 365 365 365 VAL VAL A . n 
A 1 366 TYR 366 366 366 TYR TYR A . n 
A 1 367 GLN 367 367 367 GLN GLN A . n 
A 1 368 VAL 368 368 368 VAL VAL A . n 
A 1 369 ASN 369 369 369 ASN ASN A . n 
A 1 370 PRO 370 370 370 PRO PRO A . n 
A 1 371 THR 371 371 371 THR THR A . n 
A 1 372 LYS 372 372 372 LYS LYS A . n 
A 1 373 THR 373 373 373 THR THR A . n 
A 1 374 ARG 374 374 374 ARG ARG A . n 
A 1 375 THR 375 375 375 THR THR A . n 
A 1 376 ASN 376 376 376 ASN ASN A . n 
A 1 377 LEU 377 377 377 LEU LEU A . n 
A 1 378 PRO 378 378 378 PRO PRO A . n 
A 1 379 THR 379 379 379 THR THR A . n 
A 1 380 HIS 380 380 380 HIS HIS A . n 
A 1 381 ARG 381 381 381 ARG ARG A . n 
A 1 382 HIS 382 382 382 HIS HIS A . n 
A 1 383 PRO 383 383 383 PRO PRO A . n 
A 1 384 GLN 384 384 384 GLN GLN A . n 
A 1 385 ASP 385 385 385 ASP ASP A . n 
A 1 386 GLU 386 386 386 GLU GLU A . n 
A 1 387 ILE 387 387 387 ILE ILE A . n 
A 1 388 PRO 388 388 388 PRO PRO A . n 
A 1 389 TYR 389 389 389 TYR TYR A . n 
A 1 390 CYS 390 390 390 CYS CYS A . n 
A 1 391 GLY 391 391 391 GLY GLY A . n 
A 1 392 LYS 392 392 392 LYS LYS A . n 
A 1 393 ILE 393 393 393 ILE ILE A . n 
A 1 394 PHE 394 394 394 PHE PHE A . n 
A 1 395 ASN 395 395 395 ASN ASN A . n 
A 1 396 LEU 396 396 396 LEU LEU A . n 
A 1 397 THR 397 397 397 THR THR A . n 
A 1 398 THR 398 398 398 THR THR A . n 
A 1 399 ARG 399 399 399 ARG ARG A . n 
A 1 400 GLN 400 400 400 GLN GLN A . n 
A 1 401 VAL 401 401 401 VAL VAL A . n 
A 1 402 ARG 402 402 402 ARG ARG A . n 
A 1 403 THR 403 403 403 THR THR A . n 
A 1 404 LEU 404 404 404 LEU LEU A . n 
A 1 405 TYR 405 405 405 TYR TYR A . n 
A 1 406 LYS 406 406 406 LYS LYS A . n 
A 1 407 LEU 407 407 407 LEU LEU A . n 
A 1 408 PRO 408 408 408 PRO PRO A . n 
A 1 409 PRO 409 409 409 PRO PRO A . n 
A 1 410 ASN 410 410 410 ASN ASN A . n 
A 1 411 TYR 411 411 411 TYR TYR A . n 
A 1 412 GLU 412 412 412 GLU GLU A . n 
A 1 413 ILE 413 413 413 ILE ILE A . n 
A 1 414 ARG 414 414 414 ARG ARG A . n 
A 1 415 HIS 415 415 415 HIS HIS A . n 
A 1 416 LYS 416 416 416 LYS LYS A . n 
A 1 417 PHE 417 417 417 PHE PHE A . n 
A 1 418 LYS 418 418 418 LYS LYS A . n 
A 1 419 LEU 419 419 419 LEU LEU A . n 
A 1 420 TRP 420 420 420 TRP TRP A . n 
A 1 421 ASN 421 421 421 ASN ASN A . n 
A 1 422 PHE 422 422 422 PHE PHE A . n 
A 1 423 ASN 423 423 423 ASN ASN A . n 
A 1 424 ASN 424 424 424 ASN ASN A . n 
A 1 425 GLN 425 425 425 GLN GLN A . n 
A 1 426 ILE 426 426 426 ILE ILE A . n 
A 1 427 SER 427 427 427 SER SER A . n 
A 1 428 ASP 428 428 428 ASP ASP A . n 
A 1 429 ASP 429 429 429 ASP ASP A . n 
A 1 430 ASN 430 430 430 ASN ASN A . n 
A 1 431 PRO 431 431 431 PRO PRO A . n 
A 1 432 ALA 432 432 432 ALA ALA A . n 
A 1 433 ARG 433 433 433 ARG ARG A . n 
A 1 434 PHE 434 434 434 PHE PHE A . n 
A 1 435 LEU 435 435 435 LEU LEU A . n 
A 1 436 GLN 436 436 436 GLN GLN A . n 
A 1 437 LYS 437 437 437 LYS LYS A . n 
A 1 438 ALA 438 438 438 ALA ALA A . n 
A 1 439 MET 439 439 439 MET MET A . n 
A 1 440 ASP 440 440 440 ASP ASP A . n 
A 1 441 PHE 441 441 441 PHE PHE A . n 
A 1 442 PRO 442 442 442 PRO PRO A . n 
A 1 443 PHE 443 443 443 PHE PHE A . n 
A 1 444 ILE 444 444 444 ILE ILE A . n 
A 1 445 CYS 445 445 445 CYS CYS A . n 
A 1 446 ASN 446 446 446 ASN ASN A . n 
A 1 447 SER 447 447 447 SER SER A . n 
A 1 448 PHE 448 448 448 PHE PHE A . n 
A 1 449 THR 449 449 449 THR THR A . n 
A 1 450 LYS 450 450 450 LYS LYS A . n 
A 1 451 PHE 451 451 451 PHE PHE A . n 
A 1 452 GLU 452 452 452 GLU GLU A . n 
A 1 453 PHE 453 453 453 PHE PHE A . n 
A 1 454 ASN 454 454 454 ASN ASN A . n 
A 1 455 THR 455 455 455 THR THR A . n 
A 1 456 VAL 456 456 456 VAL VAL A . n 
A 1 457 PHE 457 457 457 PHE PHE A . n 
A 1 458 ASN 458 458 458 ASN ASN A . n 
A 1 459 ASP 459 459 459 ASP ASP A . n 
A 1 460 GLN 460 460 460 GLN GLN A . n 
A 1 461 ARG 461 461 461 ARG ARG A . n 
A 1 462 THR 462 462 462 THR THR A . n 
A 1 463 VAL 463 463 463 VAL VAL A . n 
A 1 464 PHE 464 464 464 PHE PHE A . n 
A 1 465 ALA 465 465 465 ALA ALA A . n 
A 1 466 ASN 466 466 466 ASN ASN A . n 
A 1 467 PHE 467 467 467 PHE PHE A . n 
A 1 468 TYR 468 468 468 TYR TYR A . n 
A 1 469 ASP 469 469 469 ASP ASP A . n 
A 1 470 ALA 470 470 470 ALA ALA A . n 
A 1 471 MET 471 471 471 MET MET A . n 
A 1 472 ILE 472 472 472 ILE ILE A . n 
A 1 473 CYS 473 473 473 CYS CYS A . n 
A 1 474 VAL 474 474 474 VAL VAL A . n 
A 1 475 ALA 475 475 475 ALA ALA A . n 
A 1 476 TYR 476 476 476 TYR TYR A . n 
A 1 477 LYS 477 477 477 LYS LYS A . n 
A 1 478 PHE 478 478 478 PHE PHE A . n 
A 1 479 ASP 479 479 479 ASP ASP A . n 
A 1 480 ALA 480 480 480 ALA ALA A . n 
A 1 481 ALA 481 481 481 ALA ALA A . n 
A 1 482 MET 482 482 482 MET MET A . n 
A 1 483 MET 483 483 483 MET MET A . n 
A 1 484 ALA 484 484 484 ALA ALA A . n 
A 1 485 LEU 485 485 485 LEU LEU A . n 
A 1 486 ARG 486 486 486 ARG ARG A . n 
A 1 487 THR 487 487 487 THR THR A . n 
A 1 488 SER 488 488 488 SER SER A . n 
A 1 489 PHE 489 489 489 PHE PHE A . n 
A 1 490 LEU 490 490 490 LEU LEU A . n 
A 1 491 VAL 491 491 491 VAL VAL A . n 
A 1 492 ASN 492 492 492 ASN ASN A . n 
A 1 493 ASP 493 493 493 ASP ASP A . n 
A 1 494 PHE 494 494 494 PHE PHE A . n 
A 1 495 GLY 495 495 495 GLY GLY A . n 
A 1 496 PHE 496 496 496 PHE PHE A . n 
A 1 497 ILE 497 497 497 ILE ILE A . n 
A 1 498 TRP 498 498 498 TRP TRP A . n 
A 1 499 LEU 499 499 499 LEU LEU A . n 
A 1 500 VAL 500 500 500 VAL VAL A . n 
A 1 501 LEU 501 501 501 LEU LEU A . n 
A 1 502 SER 502 502 502 SER SER A . n 
A 1 503 SER 503 503 503 SER SER A . n 
A 1 504 THR 504 504 504 THR THR A . n 
A 1 505 VAL 505 505 505 VAL VAL A . n 
A 1 506 ARG 506 506 506 ARG ARG A . n 
A 1 507 ALA 507 507 507 ALA ALA A . n 
A 1 508 TYR 508 508 508 TYR TYR A . n 
A 1 509 ALA 509 509 509 ALA ALA A . n 
A 1 510 SER 510 510 510 SER SER A . n 
A 1 511 ARG 511 511 511 ARG ARG A . n 
A 1 512 ALA 512 512 512 ALA ALA A . n 
A 1 513 PHE 513 513 513 PHE PHE A . n 
A 1 514 LYS 514 514 514 LYS LYS A . n 
A 1 515 LYS 515 515 515 LYS LYS A . n 
A 1 516 ILE 516 516 516 ILE ILE A . n 
A 1 517 VAL 517 517 517 VAL VAL A . n 
A 1 518 THR 518 518 518 THR THR A . n 
A 1 519 TYR 519 519 519 TYR TYR A . n 
A 1 520 LYS 520 520 520 LYS LYS A . n 
A 1 521 GLY 521 521 521 GLY GLY A . n 
A 1 522 GLY 522 522 522 GLY GLY A . n 
A 1 523 LYS 523 523 523 LYS LYS A . n 
A 1 524 TYR 524 524 524 TYR TYR A . n 
A 1 525 ARG 525 525 525 ARG ARG A . n 
A 1 526 LYS 526 526 526 LYS LYS A . n 
A 1 527 VAL 527 527 527 VAL VAL A . n 
A 1 528 THR 528 528 528 THR THR A . n 
A 1 529 PHE 529 529 529 PHE PHE A . n 
A 1 530 GLN 530 530 530 GLN GLN A . n 
A 1 531 CYS 531 531 531 CYS CYS A . n 
A 1 532 LEU 532 532 532 LEU LEU A . n 
A 1 533 LYS 533 533 533 LYS LYS A . n 
A 1 534 SER 534 534 534 SER SER A . n 
A 1 535 ILE 535 535 535 ILE ILE A . n 
A 1 536 ALA 536 536 536 ALA ALA A . n 
A 1 537 TRP 537 537 537 TRP TRP A . n 
A 1 538 ARG 538 538 538 ARG ARG A . n 
A 1 539 ALA 539 539 539 ALA ALA A . n 
A 1 540 PHE 540 540 540 PHE PHE A . n 
A 1 541 LEU 541 541 541 LEU LEU A . n 
A 1 542 ALA 542 542 542 ALA ALA A . n 
A 1 543 VAL 543 543 543 VAL VAL A . n 
A 1 544 LEU 544 544 544 LEU LEU A . n 
A 1 545 LYS 545 545 545 LYS LYS A . n 
A 1 546 ARG 546 546 546 ARG ARG A . n 
A 1 547 ARG 547 547 547 ARG ARG A . n 
A 1 548 THR 548 548 548 THR THR A . n 
A 1 549 GLU 549 549 549 GLU GLU A . n 
A 1 550 ILE 550 550 550 ILE ILE A . n 
A 1 551 TYR 551 551 551 TYR TYR A . n 
A 1 552 LYS 552 552 552 LYS LYS A . n 
A 1 553 GLY 553 553 553 GLY GLY A . n 
A 1 554 LEU 554 554 554 LEU LEU A . n 
A 1 555 ILE 555 555 555 ILE ILE A . n 
A 1 556 ASP 556 556 556 ASP ASP A . n 
A 1 557 ARG 557 557 557 ARG ARG A . n 
A 1 558 ILE 558 558 558 ILE ILE A . n 
A 1 559 LYS 559 559 559 LYS LYS A . n 
A 1 560 SER 560 560 560 SER SER A . n 
A 1 561 ARG 561 561 561 ARG ARG A . n 
A 1 562 GLU 562 562 562 GLU GLU A . n 
A 1 563 LYS 563 563 563 LYS LYS A . n 
A 1 564 LEU 564 564 564 LEU LEU A . n 
A 1 565 THR 565 565 565 THR THR A . n 
A 1 566 MET 566 566 566 MET MET A . n 
A 1 567 LYS 567 567 567 LYS LYS A . n 
A 1 568 PHE 568 568 568 PHE PHE A . n 
A 1 569 HIS 569 569 569 HIS HIS A . n 
A 1 570 ASP 570 570 570 ASP ASP A . n 
A 1 571 GLY 571 571 571 GLY GLY A . n 
A 1 572 GLU 572 572 572 GLU GLU A . n 
A 1 573 VAL 573 573 573 VAL VAL A . n 
A 1 574 ASP 574 574 574 ASP ASP A . n 
A 1 575 ALA 575 575 575 ALA ALA A . n 
A 1 576 SER 576 576 576 SER SER A . n 
A 1 577 TYR 577 577 577 TYR TYR A . n 
A 1 578 PHE 578 578 578 PHE PHE A . n 
A 1 579 CYS 579 579 579 CYS CYS A . n 
A 1 580 LYS 580 580 580 LYS LYS A . n 
A 1 581 LEU 581 581 581 LEU LEU A . n 
A 1 582 PRO 582 582 582 PRO PRO A . n 
A 1 583 GLU 583 583 583 GLU GLU A . n 
A 1 584 LYS 584 584 584 LYS LYS A . n 
A 1 585 PHE 585 585 585 PHE PHE A . n 
A 1 586 ARG 586 586 586 ARG ARG A . n 
A 1 587 PHE 587 587 587 PHE PHE A . n 
A 1 588 VAL 588 588 588 VAL VAL A . n 
A 1 589 LYS 589 589 589 LYS LYS A . n 
A 1 590 ILE 590 590 590 ILE ILE A . n 
A 1 591 ASN 591 591 591 ASN ASN A . n 
A 1 592 ARG 592 592 592 ARG ARG A . n 
A 1 593 LYS 593 593 593 LYS LYS A . n 
A 1 594 ALA 594 594 594 ALA ALA A . n 
A 1 595 SER 595 595 595 SER SER A . n 
A 1 596 ILE 596 596 596 ILE ILE A . n 
B 1 1   MET 1   1   1   MET MET B . n 
B 1 2   VAL 2   2   2   VAL VAL B . n 
B 1 3   HIS 3   3   3   HIS HIS B . n 
B 1 4   TYR 4   4   4   TYR TYR B . n 
B 1 5   TYR 5   5   5   TYR TYR B . n 
B 1 6   ARG 6   6   6   ARG ARG B . n 
B 1 7   LEU 7   7   7   LEU LEU B . n 
B 1 8   SER 8   8   8   SER SER B . n 
B 1 9   LEU 9   9   9   LEU LEU B . n 
B 1 10  LYS 10  10  10  LYS LYS B . n 
B 1 11  SER 11  11  11  SER SER B . n 
B 1 12  ARG 12  12  12  ARG ARG B . n 
B 1 13  GLN 13  13  13  GLN GLN B . n 
B 1 14  LYS 14  14  14  LYS LYS B . n 
B 1 15  ALA 15  15  15  ALA ALA B . n 
B 1 16  PRO 16  16  16  PRO PRO B . n 
B 1 17  LYS 17  17  17  LYS LYS B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  VAL 19  19  19  VAL VAL B . n 
B 1 20  ASN 20  20  20  ASN ASN B . n 
B 1 21  SER 21  21  21  SER SER B . n 
B 1 22  LYS 22  22  22  LYS LYS B . n 
B 1 23  TYR 23  23  23  TYR TYR B . n 
B 1 24  ASN 24  24  24  ASN ASN B . n 
B 1 25  SER 25  25  25  SER SER B . n 
B 1 26  ILE 26  26  26  ILE ILE B . n 
B 1 27  LEU 27  27  27  LEU LEU B . n 
B 1 28  ASN 28  28  28  ASN ASN B . n 
B 1 29  ILE 29  29  29  ILE ILE B . n 
B 1 30  ALA 30  30  30  ALA ALA B . n 
B 1 31  LEU 31  31  31  LEU LEU B . n 
B 1 32  LYS 32  32  32  LYS LYS B . n 
B 1 33  ASN 33  33  33  ASN ASN B . n 
B 1 34  PHE 34  34  34  PHE PHE B . n 
B 1 35  ARG 35  35  35  ARG ARG B . n 
B 1 36  LEU 36  36  36  LEU LEU B . n 
B 1 37  CYS 37  37  37  CYS CYS B . n 
B 1 38  LYS 38  38  38  LYS LYS B . n 
B 1 39  LYS 39  39  39  LYS LYS B . n 
B 1 40  HIS 40  40  40  HIS HIS B . n 
B 1 41  LYS 41  41  41  LYS LYS B . n 
B 1 42  THR 42  42  42  THR THR B . n 
B 1 43  LYS 43  43  43  LYS LYS B . n 
B 1 44  LYS 44  44  44  LYS LYS B . n 
B 1 45  PRO 45  45  45  PRO PRO B . n 
B 1 46  VAL 46  46  46  VAL VAL B . n 
B 1 47  GLN 47  47  47  GLN GLN B . n 
B 1 48  ILE 48  48  48  ILE ILE B . n 
B 1 49  LEU 49  49  49  LEU LEU B . n 
B 1 50  ALA 50  50  50  ALA ALA B . n 
B 1 51  LEU 51  51  51  LEU LEU B . n 
B 1 52  LEU 52  52  52  LEU LEU B . n 
B 1 53  GLN 53  53  53  GLN GLN B . n 
B 1 54  GLU 54  54  54  GLU GLU B . n 
B 1 55  ILE 55  55  55  ILE ILE B . n 
B 1 56  ILE 56  56  56  ILE ILE B . n 
B 1 57  PRO 57  57  57  PRO PRO B . n 
B 1 58  LYS 58  58  58  LYS LYS B . n 
B 1 59  SER 59  59  59  SER SER B . n 
B 1 60  TYR 60  60  60  TYR TYR B . n 
B 1 61  PHE 61  61  61  PHE PHE B . n 
B 1 62  GLY 62  62  62  GLY GLY B . n 
B 1 63  THR 63  63  63  THR THR B . n 
B 1 64  THR 64  64  64  THR THR B . n 
B 1 65  THR 65  65  65  THR THR B . n 
B 1 66  ASN 66  66  66  ASN ASN B . n 
B 1 67  LEU 67  67  67  LEU LEU B . n 
B 1 68  LYS 68  68  68  LYS LYS B . n 
B 1 69  ARG 69  69  69  ARG ARG B . n 
B 1 70  PHE 70  70  70  PHE PHE B . n 
B 1 71  TYR 71  71  71  TYR TYR B . n 
B 1 72  LYS 72  72  72  LYS LYS B . n 
B 1 73  VAL 73  73  73  VAL VAL B . n 
B 1 74  VAL 74  74  74  VAL VAL B . n 
B 1 75  GLU 75  75  75  GLU GLU B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  ILE 77  77  77  ILE ILE B . n 
B 1 78  LEU 78  78  78  LEU LEU B . n 
B 1 79  THR 79  79  79  THR THR B . n 
B 1 80  GLN 80  80  80  GLN GLN B . n 
B 1 81  SER 81  81  81  SER SER B . n 
B 1 82  SER 82  82  82  SER SER B . n 
B 1 83  PHE 83  83  83  PHE PHE B . n 
B 1 84  GLU 84  84  84  GLU GLU B . n 
B 1 85  CYS 85  85  85  CYS CYS B . n 
B 1 86  ILE 86  86  86  ILE ILE B . n 
B 1 87  HIS 87  87  87  HIS HIS B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  SER 89  89  89  SER SER B . n 
B 1 90  VAL 90  90  90  VAL VAL B . n 
B 1 91  LEU 91  91  91  LEU LEU B . n 
B 1 92  HIS 92  92  92  HIS HIS B . n 
B 1 93  LYS 93  93  93  LYS LYS B . n 
B 1 94  CYS 94  94  94  CYS CYS B . n 
B 1 95  TYR 95  95  95  TYR TYR B . n 
B 1 96  ASP 96  96  96  ASP ASP B . n 
B 1 97  TYR 97  97  97  TYR TYR B . n 
B 1 98  ASP 98  98  98  ASP ASP B . n 
B 1 99  ALA 99  99  99  ALA ALA B . n 
B 1 100 ILE 100 100 100 ILE ILE B . n 
B 1 101 PRO 101 101 101 PRO PRO B . n 
B 1 102 TRP 102 102 102 TRP TRP B . n 
B 1 103 LEU 103 103 103 LEU LEU B . n 
B 1 104 GLN 104 104 104 GLN GLN B . n 
B 1 105 ASN 105 105 105 ASN ASN B . n 
B 1 106 VAL 106 106 106 VAL VAL B . n 
B 1 107 GLU 107 107 107 GLU GLU B . n 
B 1 108 PRO 108 108 108 PRO PRO B . n 
B 1 109 ASN 109 109 109 ASN ASN B . n 
B 1 110 LEU 110 110 110 LEU LEU B . n 
B 1 111 ARG 111 111 111 ARG ARG B . n 
B 1 112 PRO 112 112 112 PRO PRO B . n 
B 1 113 LYS 113 113 113 LYS LYS B . n 
B 1 114 LEU 114 114 114 LEU LEU B . n 
B 1 115 LEU 115 115 115 LEU LEU B . n 
B 1 116 LEU 116 116 116 LEU LEU B . n 
B 1 117 LYS 117 117 117 LYS LYS B . n 
B 1 118 HIS 118 118 118 HIS HIS B . n 
B 1 119 ASN 119 119 119 ASN ASN B . n 
B 1 120 LEU 120 120 120 LEU LEU B . n 
B 1 121 PHE 121 121 121 PHE PHE B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 LEU 123 123 123 LEU LEU B . n 
B 1 124 ASP 124 124 124 ASP ASP B . n 
B 1 125 ASN 125 125 125 ASN ASN B . n 
B 1 126 ILE 126 126 126 ILE ILE B . n 
B 1 127 VAL 127 127 127 VAL VAL B . n 
B 1 128 LYS 128 128 128 LYS LYS B . n 
B 1 129 PRO 129 129 129 PRO PRO B . n 
B 1 130 ILE 130 130 130 ILE ILE B . n 
B 1 131 ILE 131 131 131 ILE ILE B . n 
B 1 132 ALA 132 132 132 ALA ALA B . n 
B 1 133 PHE 133 133 133 PHE PHE B . n 
B 1 134 TYR 134 134 134 TYR TYR B . n 
B 1 135 TYR 135 135 135 TYR TYR B . n 
B 1 136 LYS 136 136 136 LYS LYS B . n 
B 1 137 PRO 137 137 137 PRO PRO B . n 
B 1 138 ILE 138 138 138 ILE ILE B . n 
B 1 139 LYS 139 139 139 LYS LYS B . n 
B 1 140 THR 140 140 140 THR THR B . n 
B 1 141 LEU 141 141 141 LEU LEU B . n 
B 1 142 ASN 142 142 142 ASN ASN B . n 
B 1 143 GLY 143 143 143 GLY GLY B . n 
B 1 144 HIS 144 144 144 HIS HIS B . n 
B 1 145 GLU 145 145 145 GLU GLU B . n 
B 1 146 ILE 146 146 146 ILE ILE B . n 
B 1 147 LYS 147 147 147 LYS LYS B . n 
B 1 148 PHE 148 148 148 PHE PHE B . n 
B 1 149 ILE 149 149 149 ILE ILE B . n 
B 1 150 ARG 150 150 150 ARG ARG B . n 
B 1 151 LYS 151 151 151 LYS LYS B . n 
B 1 152 GLU 152 152 152 GLU GLU B . n 
B 1 153 GLU 153 153 153 GLU GLU B . n 
B 1 154 TYR 154 154 154 TYR TYR B . n 
B 1 155 ILE 155 155 155 ILE ILE B . n 
B 1 156 SER 156 156 156 SER SER B . n 
B 1 157 PHE 157 157 157 PHE PHE B . n 
B 1 158 GLU 158 158 158 GLU GLU B . n 
B 1 159 SER 159 159 159 SER SER B . n 
B 1 160 LYS 160 160 160 LYS LYS B . n 
B 1 161 VAL 161 161 161 VAL VAL B . n 
B 1 162 PHE 162 162 162 PHE PHE B . n 
B 1 163 HIS 163 163 163 HIS HIS B . n 
B 1 164 LYS 164 164 164 LYS LYS B . n 
B 1 165 LEU 165 165 165 LEU LEU B . n 
B 1 166 LYS 166 166 166 LYS LYS B . n 
B 1 167 LYS 167 167 167 LYS LYS B . n 
B 1 168 MET 168 168 168 MET MET B . n 
B 1 169 LYS 169 169 169 LYS LYS B . n 
B 1 170 TYR 170 170 170 TYR TYR B . n 
B 1 171 LEU 171 171 171 LEU LEU B . n 
B 1 172 VAL 172 172 172 VAL VAL B . n 
B 1 173 GLU 173 173 173 GLU GLU B . n 
B 1 174 VAL 174 174 174 VAL VAL B . n 
B 1 175 GLN 175 175 175 GLN GLN B . n 
B 1 176 ASP 176 176 176 ASP ASP B . n 
B 1 177 GLU 177 177 177 GLU GLU B . n 
B 1 178 VAL 178 178 178 VAL VAL B . n 
B 1 179 LYS 179 179 179 LYS LYS B . n 
B 1 180 PRO 180 180 180 PRO PRO B . n 
B 1 181 ARG 181 181 181 ARG ARG B . n 
B 1 182 GLY 182 182 182 GLY GLY B . n 
B 1 183 VAL 183 183 183 VAL VAL B . n 
B 1 184 LEU 184 184 184 LEU LEU B . n 
B 1 185 ASN 185 185 185 ASN ASN B . n 
B 1 186 ILE 186 186 186 ILE ILE B . n 
B 1 187 ILE 187 187 187 ILE ILE B . n 
B 1 188 PRO 188 188 188 PRO PRO B . n 
B 1 189 LYS 189 189 189 LYS LYS B . n 
B 1 190 GLN 190 190 190 GLN GLN B . n 
B 1 191 ASP 191 191 191 ASP ASP B . n 
B 1 192 ASN 192 192 192 ASN ASN B . n 
B 1 193 PHE 193 193 193 PHE PHE B . n 
B 1 194 ARG 194 194 194 ARG ARG B . n 
B 1 195 ALA 195 195 195 ALA ALA B . n 
B 1 196 ILE 196 196 196 ILE ILE B . n 
B 1 197 VAL 197 197 197 VAL VAL B . n 
B 1 198 SER 198 198 198 SER SER B . n 
B 1 199 ILE 199 199 199 ILE ILE B . n 
B 1 200 PHE 200 200 200 PHE PHE B . n 
B 1 201 PRO 201 201 201 PRO PRO B . n 
B 1 202 ASP 202 202 202 ASP ASP B . n 
B 1 203 SER 203 203 203 SER SER B . n 
B 1 204 ALA 204 204 204 ALA ALA B . n 
B 1 205 ARG 205 205 205 ARG ARG B . n 
B 1 206 LYS 206 206 206 LYS LYS B . n 
B 1 207 PRO 207 207 207 PRO PRO B . n 
B 1 208 PHE 208 208 208 PHE PHE B . n 
B 1 209 PHE 209 209 209 PHE PHE B . n 
B 1 210 LYS 210 210 210 LYS LYS B . n 
B 1 211 LEU 211 211 211 LEU LEU B . n 
B 1 212 LEU 212 212 212 LEU LEU B . n 
B 1 213 THR 213 213 213 THR THR B . n 
B 1 214 SER 214 214 214 SER SER B . n 
B 1 215 LYS 215 215 215 LYS LYS B . n 
B 1 216 ILE 216 216 216 ILE ILE B . n 
B 1 217 TYR 217 217 217 TYR TYR B . n 
B 1 218 LYS 218 218 218 LYS LYS B . n 
B 1 219 VAL 219 219 219 VAL VAL B . n 
B 1 220 LEU 220 220 220 LEU LEU B . n 
B 1 221 GLU 221 221 221 GLU GLU B . n 
B 1 222 GLU 222 222 222 GLU GLU B . n 
B 1 223 LYS 223 223 223 LYS LYS B . n 
B 1 224 TYR 224 224 224 TYR TYR B . n 
B 1 225 LYS 225 225 225 LYS LYS B . n 
B 1 226 THR 226 226 226 THR THR B . n 
B 1 227 SER 227 227 227 SER SER B . n 
B 1 228 GLY 228 228 228 GLY GLY B . n 
B 1 229 SER 229 229 229 SER SER B . n 
B 1 230 LEU 230 230 230 LEU LEU B . n 
B 1 231 TYR 231 231 231 TYR TYR B . n 
B 1 232 THR 232 232 232 THR THR B . n 
B 1 233 CYS 233 233 233 CYS CYS B . n 
B 1 234 TRP 234 234 234 TRP TRP B . n 
B 1 235 SER 235 235 235 SER SER B . n 
B 1 236 GLU 236 236 236 GLU GLU B . n 
B 1 237 PHE 237 237 237 PHE PHE B . n 
B 1 238 THR 238 238 238 THR THR B . n 
B 1 239 GLN 239 239 239 GLN GLN B . n 
B 1 240 LYS 240 240 240 LYS LYS B . n 
B 1 241 THR 241 241 241 THR THR B . n 
B 1 242 GLN 242 242 242 GLN GLN B . n 
B 1 243 GLY 243 243 243 GLY GLY B . n 
B 1 244 GLN 244 244 244 GLN GLN B . n 
B 1 245 ILE 245 245 245 ILE ILE B . n 
B 1 246 TYR 246 246 246 TYR TYR B . n 
B 1 247 GLY 247 247 247 GLY GLY B . n 
B 1 248 ILE 248 248 248 ILE ILE B . n 
B 1 249 LYS 249 249 249 LYS LYS B . n 
B 1 250 VAL 250 250 250 VAL VAL B . n 
B 1 251 ASP 251 251 251 ASP ASP B . n 
B 1 252 ILE 252 252 252 ILE ILE B . n 
B 1 253 ARG 253 253 253 ARG ARG B . n 
B 1 254 ASP 254 254 254 ASP ASP B . n 
B 1 255 ALA 255 255 255 ALA ALA B . n 
B 1 256 TYR 256 256 256 TYR TYR B . n 
B 1 257 GLY 257 257 257 GLY GLY B . n 
B 1 258 ASN 258 258 258 ASN ASN B . n 
B 1 259 VAL 259 259 259 VAL VAL B . n 
B 1 260 LYS 260 260 260 LYS LYS B . n 
B 1 261 ILE 261 261 261 ILE ILE B . n 
B 1 262 PRO 262 262 262 PRO PRO B . n 
B 1 263 VAL 263 263 263 VAL VAL B . n 
B 1 264 LEU 264 264 264 LEU LEU B . n 
B 1 265 CYS 265 265 265 CYS CYS B . n 
B 1 266 LYS 266 266 266 LYS LYS B . n 
B 1 267 LEU 267 267 267 LEU LEU B . n 
B 1 268 ILE 268 268 268 ILE ILE B . n 
B 1 269 GLN 269 269 269 GLN GLN B . n 
B 1 270 SER 270 270 270 SER SER B . n 
B 1 271 ILE 271 271 271 ILE ILE B . n 
B 1 272 PRO 272 272 272 PRO PRO B . n 
B 1 273 THR 273 273 273 THR THR B . n 
B 1 274 HIS 274 274 274 HIS HIS B . n 
B 1 275 LEU 275 275 275 LEU LEU B . n 
B 1 276 LEU 276 276 276 LEU LEU B . n 
B 1 277 ASP 277 277 277 ASP ASP B . n 
B 1 278 SER 278 278 278 SER SER B . n 
B 1 279 GLU 279 279 279 GLU GLU B . n 
B 1 280 LYS 280 280 280 LYS LYS B . n 
B 1 281 LYS 281 281 281 LYS LYS B . n 
B 1 282 ASN 282 282 282 ASN ASN B . n 
B 1 283 PHE 283 283 283 PHE PHE B . n 
B 1 284 ILE 284 284 284 ILE ILE B . n 
B 1 285 VAL 285 285 285 VAL VAL B . n 
B 1 286 ASP 286 286 286 ASP ASP B . n 
B 1 287 HIS 287 287 287 HIS HIS B . n 
B 1 288 ILE 288 288 288 ILE ILE B . n 
B 1 289 SER 289 289 289 SER SER B . n 
B 1 290 ASN 290 290 290 ASN ASN B . n 
B 1 291 GLN 291 291 291 GLN GLN B . n 
B 1 292 PHE 292 292 292 PHE PHE B . n 
B 1 293 VAL 293 293 293 VAL VAL B . n 
B 1 294 ALA 294 294 294 ALA ALA B . n 
B 1 295 PHE 295 295 295 PHE PHE B . n 
B 1 296 ARG 296 296 296 ARG ARG B . n 
B 1 297 ARG 297 297 297 ARG ARG B . n 
B 1 298 LYS 298 298 298 LYS LYS B . n 
B 1 299 ILE 299 299 299 ILE ILE B . n 
B 1 300 TYR 300 300 300 TYR TYR B . n 
B 1 301 LYS 301 301 301 LYS LYS B . n 
B 1 302 TRP 302 302 302 TRP TRP B . n 
B 1 303 ASN 303 303 303 ASN ASN B . n 
B 1 304 HIS 304 304 304 HIS HIS B . n 
B 1 305 GLY 305 305 305 GLY GLY B . n 
B 1 306 LEU 306 306 306 LEU LEU B . n 
B 1 307 LEU 307 307 307 LEU LEU B . n 
B 1 308 GLN 308 308 308 GLN GLN B . n 
B 1 309 GLY 309 309 309 GLY GLY B . n 
B 1 310 ASP 310 310 310 ASP ASP B . n 
B 1 311 PRO 311 311 311 PRO PRO B . n 
B 1 312 LEU 312 312 312 LEU LEU B . n 
B 1 313 SER 313 313 313 SER SER B . n 
B 1 314 GLY 314 314 314 GLY GLY B . n 
B 1 315 CYS 315 315 315 CYS CYS B . n 
B 1 316 LEU 316 316 316 LEU LEU B . n 
B 1 317 CYS 317 317 317 CYS CYS B . n 
B 1 318 GLU 318 318 318 GLU GLU B . n 
B 1 319 LEU 319 319 319 LEU LEU B . n 
B 1 320 TYR 320 320 320 TYR TYR B . n 
B 1 321 MET 321 321 321 MET MET B . n 
B 1 322 ALA 322 322 322 ALA ALA B . n 
B 1 323 PHE 323 323 323 PHE PHE B . n 
B 1 324 MET 324 324 324 MET MET B . n 
B 1 325 ASP 325 325 325 ASP ASP B . n 
B 1 326 ARG 326 326 326 ARG ARG B . n 
B 1 327 LEU 327 327 327 LEU LEU B . n 
B 1 328 TYR 328 328 328 TYR TYR B . n 
B 1 329 PHE 329 329 329 PHE PHE B . n 
B 1 330 SER 330 330 330 SER SER B . n 
B 1 331 ASN 331 331 331 ASN ASN B . n 
B 1 332 LEU 332 332 332 LEU LEU B . n 
B 1 333 ASP 333 333 333 ASP ASP B . n 
B 1 334 LYS 334 334 334 LYS LYS B . n 
B 1 335 ASP 335 335 335 ASP ASP B . n 
B 1 336 ALA 336 336 336 ALA ALA B . n 
B 1 337 PHE 337 337 337 PHE PHE B . n 
B 1 338 ILE 338 338 338 ILE ILE B . n 
B 1 339 HIS 339 339 339 HIS HIS B . n 
B 1 340 ARG 340 340 340 ARG ARG B . n 
B 1 341 THR 341 341 341 THR THR B . n 
B 1 342 VAL 342 342 342 VAL VAL B . n 
B 1 343 ASP 343 343 343 ASP ASP B . n 
B 1 344 ASP 344 344 344 ASP ASP B . n 
B 1 345 TYR 345 345 345 TYR TYR B . n 
B 1 346 PHE 346 346 346 PHE PHE B . n 
B 1 347 PHE 347 347 347 PHE PHE B . n 
B 1 348 CYS 348 348 348 CYS CYS B . n 
B 1 349 SER 349 349 349 SER SER B . n 
B 1 350 PRO 350 350 350 PRO PRO B . n 
B 1 351 HIS 351 351 351 HIS HIS B . n 
B 1 352 PRO 352 352 352 PRO PRO B . n 
B 1 353 HIS 353 353 353 HIS HIS B . n 
B 1 354 LYS 354 354 354 LYS LYS B . n 
B 1 355 VAL 355 355 355 VAL VAL B . n 
B 1 356 TYR 356 356 356 TYR TYR B . n 
B 1 357 ASP 357 357 357 ASP ASP B . n 
B 1 358 PHE 358 358 358 PHE PHE B . n 
B 1 359 GLU 359 359 359 GLU GLU B . n 
B 1 360 LEU 360 360 360 LEU LEU B . n 
B 1 361 LEU 361 361 361 LEU LEU B . n 
B 1 362 ILE 362 362 362 ILE ILE B . n 
B 1 363 LYS 363 363 363 LYS LYS B . n 
B 1 364 GLY 364 364 364 GLY GLY B . n 
B 1 365 VAL 365 365 365 VAL VAL B . n 
B 1 366 TYR 366 366 366 TYR TYR B . n 
B 1 367 GLN 367 367 367 GLN GLN B . n 
B 1 368 VAL 368 368 368 VAL VAL B . n 
B 1 369 ASN 369 369 369 ASN ASN B . n 
B 1 370 PRO 370 370 370 PRO PRO B . n 
B 1 371 THR 371 371 371 THR THR B . n 
B 1 372 LYS 372 372 372 LYS LYS B . n 
B 1 373 THR 373 373 373 THR THR B . n 
B 1 374 ARG 374 374 374 ARG ARG B . n 
B 1 375 THR 375 375 375 THR THR B . n 
B 1 376 ASN 376 376 376 ASN ASN B . n 
B 1 377 LEU 377 377 377 LEU LEU B . n 
B 1 378 PRO 378 378 378 PRO PRO B . n 
B 1 379 THR 379 379 379 THR THR B . n 
B 1 380 HIS 380 380 380 HIS HIS B . n 
B 1 381 ARG 381 381 381 ARG ARG B . n 
B 1 382 HIS 382 382 382 HIS HIS B . n 
B 1 383 PRO 383 383 383 PRO PRO B . n 
B 1 384 GLN 384 384 384 GLN GLN B . n 
B 1 385 ASP 385 385 385 ASP ASP B . n 
B 1 386 GLU 386 386 386 GLU GLU B . n 
B 1 387 ILE 387 387 387 ILE ILE B . n 
B 1 388 PRO 388 388 388 PRO PRO B . n 
B 1 389 TYR 389 389 389 TYR TYR B . n 
B 1 390 CYS 390 390 390 CYS CYS B . n 
B 1 391 GLY 391 391 391 GLY GLY B . n 
B 1 392 LYS 392 392 392 LYS LYS B . n 
B 1 393 ILE 393 393 393 ILE ILE B . n 
B 1 394 PHE 394 394 394 PHE PHE B . n 
B 1 395 ASN 395 395 395 ASN ASN B . n 
B 1 396 LEU 396 396 396 LEU LEU B . n 
B 1 397 THR 397 397 397 THR THR B . n 
B 1 398 THR 398 398 398 THR THR B . n 
B 1 399 ARG 399 399 399 ARG ARG B . n 
B 1 400 GLN 400 400 400 GLN GLN B . n 
B 1 401 VAL 401 401 401 VAL VAL B . n 
B 1 402 ARG 402 402 402 ARG ARG B . n 
B 1 403 THR 403 403 403 THR THR B . n 
B 1 404 LEU 404 404 404 LEU LEU B . n 
B 1 405 TYR 405 405 405 TYR TYR B . n 
B 1 406 LYS 406 406 406 LYS LYS B . n 
B 1 407 LEU 407 407 407 LEU LEU B . n 
B 1 408 PRO 408 408 408 PRO PRO B . n 
B 1 409 PRO 409 409 409 PRO PRO B . n 
B 1 410 ASN 410 410 410 ASN ASN B . n 
B 1 411 TYR 411 411 411 TYR TYR B . n 
B 1 412 GLU 412 412 412 GLU GLU B . n 
B 1 413 ILE 413 413 413 ILE ILE B . n 
B 1 414 ARG 414 414 414 ARG ARG B . n 
B 1 415 HIS 415 415 415 HIS HIS B . n 
B 1 416 LYS 416 416 416 LYS LYS B . n 
B 1 417 PHE 417 417 417 PHE PHE B . n 
B 1 418 LYS 418 418 418 LYS LYS B . n 
B 1 419 LEU 419 419 419 LEU LEU B . n 
B 1 420 TRP 420 420 420 TRP TRP B . n 
B 1 421 ASN 421 421 421 ASN ASN B . n 
B 1 422 PHE 422 422 422 PHE PHE B . n 
B 1 423 ASN 423 423 423 ASN ASN B . n 
B 1 424 ASN 424 424 424 ASN ASN B . n 
B 1 425 GLN 425 425 425 GLN GLN B . n 
B 1 426 ILE 426 426 426 ILE ILE B . n 
B 1 427 SER 427 427 427 SER SER B . n 
B 1 428 ASP 428 428 428 ASP ASP B . n 
B 1 429 ASP 429 429 429 ASP ASP B . n 
B 1 430 ASN 430 430 430 ASN ASN B . n 
B 1 431 PRO 431 431 431 PRO PRO B . n 
B 1 432 ALA 432 432 432 ALA ALA B . n 
B 1 433 ARG 433 433 433 ARG ARG B . n 
B 1 434 PHE 434 434 434 PHE PHE B . n 
B 1 435 LEU 435 435 435 LEU LEU B . n 
B 1 436 GLN 436 436 436 GLN GLN B . n 
B 1 437 LYS 437 437 437 LYS LYS B . n 
B 1 438 ALA 438 438 438 ALA ALA B . n 
B 1 439 MET 439 439 439 MET MET B . n 
B 1 440 ASP 440 440 440 ASP ASP B . n 
B 1 441 PHE 441 441 441 PHE PHE B . n 
B 1 442 PRO 442 442 442 PRO PRO B . n 
B 1 443 PHE 443 443 443 PHE PHE B . n 
B 1 444 ILE 444 444 444 ILE ILE B . n 
B 1 445 CYS 445 445 445 CYS CYS B . n 
B 1 446 ASN 446 446 446 ASN ASN B . n 
B 1 447 SER 447 447 447 SER SER B . n 
B 1 448 PHE 448 448 448 PHE PHE B . n 
B 1 449 THR 449 449 449 THR THR B . n 
B 1 450 LYS 450 450 450 LYS LYS B . n 
B 1 451 PHE 451 451 451 PHE PHE B . n 
B 1 452 GLU 452 452 452 GLU GLU B . n 
B 1 453 PHE 453 453 453 PHE PHE B . n 
B 1 454 ASN 454 454 454 ASN ASN B . n 
B 1 455 THR 455 455 455 THR THR B . n 
B 1 456 VAL 456 456 456 VAL VAL B . n 
B 1 457 PHE 457 457 457 PHE PHE B . n 
B 1 458 ASN 458 458 458 ASN ASN B . n 
B 1 459 ASP 459 459 459 ASP ASP B . n 
B 1 460 GLN 460 460 460 GLN GLN B . n 
B 1 461 ARG 461 461 461 ARG ARG B . n 
B 1 462 THR 462 462 462 THR THR B . n 
B 1 463 VAL 463 463 463 VAL VAL B . n 
B 1 464 PHE 464 464 464 PHE PHE B . n 
B 1 465 ALA 465 465 465 ALA ALA B . n 
B 1 466 ASN 466 466 466 ASN ASN B . n 
B 1 467 PHE 467 467 467 PHE PHE B . n 
B 1 468 TYR 468 468 468 TYR TYR B . n 
B 1 469 ASP 469 469 469 ASP ASP B . n 
B 1 470 ALA 470 470 470 ALA ALA B . n 
B 1 471 MET 471 471 471 MET MET B . n 
B 1 472 ILE 472 472 472 ILE ILE B . n 
B 1 473 CYS 473 473 473 CYS CYS B . n 
B 1 474 VAL 474 474 474 VAL VAL B . n 
B 1 475 ALA 475 475 475 ALA ALA B . n 
B 1 476 TYR 476 476 476 TYR TYR B . n 
B 1 477 LYS 477 477 477 LYS LYS B . n 
B 1 478 PHE 478 478 478 PHE PHE B . n 
B 1 479 ASP 479 479 479 ASP ASP B . n 
B 1 480 ALA 480 480 480 ALA ALA B . n 
B 1 481 ALA 481 481 481 ALA ALA B . n 
B 1 482 MET 482 482 482 MET MET B . n 
B 1 483 MET 483 483 483 MET MET B . n 
B 1 484 ALA 484 484 484 ALA ALA B . n 
B 1 485 LEU 485 485 485 LEU LEU B . n 
B 1 486 ARG 486 486 486 ARG ARG B . n 
B 1 487 THR 487 487 487 THR THR B . n 
B 1 488 SER 488 488 488 SER SER B . n 
B 1 489 PHE 489 489 489 PHE PHE B . n 
B 1 490 LEU 490 490 490 LEU LEU B . n 
B 1 491 VAL 491 491 491 VAL VAL B . n 
B 1 492 ASN 492 492 492 ASN ASN B . n 
B 1 493 ASP 493 493 493 ASP ASP B . n 
B 1 494 PHE 494 494 494 PHE PHE B . n 
B 1 495 GLY 495 495 495 GLY GLY B . n 
B 1 496 PHE 496 496 496 PHE PHE B . n 
B 1 497 ILE 497 497 497 ILE ILE B . n 
B 1 498 TRP 498 498 498 TRP TRP B . n 
B 1 499 LEU 499 499 499 LEU LEU B . n 
B 1 500 VAL 500 500 500 VAL VAL B . n 
B 1 501 LEU 501 501 501 LEU LEU B . n 
B 1 502 SER 502 502 502 SER SER B . n 
B 1 503 SER 503 503 503 SER SER B . n 
B 1 504 THR 504 504 504 THR THR B . n 
B 1 505 VAL 505 505 505 VAL VAL B . n 
B 1 506 ARG 506 506 506 ARG ARG B . n 
B 1 507 ALA 507 507 507 ALA ALA B . n 
B 1 508 TYR 508 508 508 TYR TYR B . n 
B 1 509 ALA 509 509 509 ALA ALA B . n 
B 1 510 SER 510 510 510 SER SER B . n 
B 1 511 ARG 511 511 511 ARG ARG B . n 
B 1 512 ALA 512 512 512 ALA ALA B . n 
B 1 513 PHE 513 513 513 PHE PHE B . n 
B 1 514 LYS 514 514 514 LYS LYS B . n 
B 1 515 LYS 515 515 515 LYS LYS B . n 
B 1 516 ILE 516 516 516 ILE ILE B . n 
B 1 517 VAL 517 517 517 VAL VAL B . n 
B 1 518 THR 518 518 518 THR THR B . n 
B 1 519 TYR 519 519 519 TYR TYR B . n 
B 1 520 LYS 520 520 520 LYS LYS B . n 
B 1 521 GLY 521 521 521 GLY GLY B . n 
B 1 522 GLY 522 522 522 GLY GLY B . n 
B 1 523 LYS 523 523 523 LYS LYS B . n 
B 1 524 TYR 524 524 524 TYR TYR B . n 
B 1 525 ARG 525 525 525 ARG ARG B . n 
B 1 526 LYS 526 526 526 LYS LYS B . n 
B 1 527 VAL 527 527 527 VAL VAL B . n 
B 1 528 THR 528 528 528 THR THR B . n 
B 1 529 PHE 529 529 529 PHE PHE B . n 
B 1 530 GLN 530 530 530 GLN GLN B . n 
B 1 531 CYS 531 531 531 CYS CYS B . n 
B 1 532 LEU 532 532 532 LEU LEU B . n 
B 1 533 LYS 533 533 533 LYS LYS B . n 
B 1 534 SER 534 534 534 SER SER B . n 
B 1 535 ILE 535 535 535 ILE ILE B . n 
B 1 536 ALA 536 536 536 ALA ALA B . n 
B 1 537 TRP 537 537 537 TRP TRP B . n 
B 1 538 ARG 538 538 538 ARG ARG B . n 
B 1 539 ALA 539 539 539 ALA ALA B . n 
B 1 540 PHE 540 540 540 PHE PHE B . n 
B 1 541 LEU 541 541 541 LEU LEU B . n 
B 1 542 ALA 542 542 542 ALA ALA B . n 
B 1 543 VAL 543 543 543 VAL VAL B . n 
B 1 544 LEU 544 544 544 LEU LEU B . n 
B 1 545 LYS 545 545 545 LYS LYS B . n 
B 1 546 ARG 546 546 546 ARG ARG B . n 
B 1 547 ARG 547 547 547 ARG ARG B . n 
B 1 548 THR 548 548 548 THR THR B . n 
B 1 549 GLU 549 549 549 GLU GLU B . n 
B 1 550 ILE 550 550 550 ILE ILE B . n 
B 1 551 TYR 551 551 551 TYR TYR B . n 
B 1 552 LYS 552 552 552 LYS LYS B . n 
B 1 553 GLY 553 553 553 GLY GLY B . n 
B 1 554 LEU 554 554 554 LEU LEU B . n 
B 1 555 ILE 555 555 555 ILE ILE B . n 
B 1 556 ASP 556 556 556 ASP ASP B . n 
B 1 557 ARG 557 557 557 ARG ARG B . n 
B 1 558 ILE 558 558 558 ILE ILE B . n 
B 1 559 LYS 559 559 559 LYS LYS B . n 
B 1 560 SER 560 560 560 SER SER B . n 
B 1 561 ARG 561 561 561 ARG ARG B . n 
B 1 562 GLU 562 562 562 GLU GLU B . n 
B 1 563 LYS 563 563 563 LYS LYS B . n 
B 1 564 LEU 564 564 564 LEU LEU B . n 
B 1 565 THR 565 565 565 THR THR B . n 
B 1 566 MET 566 566 566 MET MET B . n 
B 1 567 LYS 567 567 567 LYS LYS B . n 
B 1 568 PHE 568 568 568 PHE PHE B . n 
B 1 569 HIS 569 569 569 HIS HIS B . n 
B 1 570 ASP 570 570 570 ASP ASP B . n 
B 1 571 GLY 571 571 571 GLY GLY B . n 
B 1 572 GLU 572 572 572 GLU GLU B . n 
B 1 573 VAL 573 573 573 VAL VAL B . n 
B 1 574 ASP 574 574 574 ASP ASP B . n 
B 1 575 ALA 575 575 575 ALA ALA B . n 
B 1 576 SER 576 576 576 SER SER B . n 
B 1 577 TYR 577 577 577 TYR TYR B . n 
B 1 578 PHE 578 578 578 PHE PHE B . n 
B 1 579 CYS 579 579 579 CYS CYS B . n 
B 1 580 LYS 580 580 580 LYS LYS B . n 
B 1 581 LEU 581 581 581 LEU LEU B . n 
B 1 582 PRO 582 582 582 PRO PRO B . n 
B 1 583 GLU 583 583 583 GLU GLU B . n 
B 1 584 LYS 584 584 584 LYS LYS B . n 
B 1 585 PHE 585 585 585 PHE PHE B . n 
B 1 586 ARG 586 586 586 ARG ARG B . n 
B 1 587 PHE 587 587 587 PHE PHE B . n 
B 1 588 VAL 588 588 588 VAL VAL B . n 
B 1 589 LYS 589 589 589 LYS LYS B . n 
B 1 590 ILE 590 590 590 ILE ILE B . n 
B 1 591 ASN 591 591 591 ASN ASN B . n 
B 1 592 ARG 592 592 592 ARG ARG B . n 
B 1 593 LYS 593 593 593 LYS LYS B . n 
B 1 594 ALA 594 594 594 ALA ALA B . n 
B 1 595 SER 595 595 595 SER SER B . n 
B 1 596 ILE 596 596 596 ILE ILE B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 55C 1   601 601 55C BIB A . 
D 2 55C 1   601 601 55C BIB B . 
E 3 HOH 1   701 704 HOH HOH A . 
E 3 HOH 2   702 794 HOH HOH A . 
E 3 HOH 3   703 707 HOH HOH A . 
E 3 HOH 4   704 717 HOH HOH A . 
E 3 HOH 5   705 710 HOH HOH A . 
E 3 HOH 6   706 709 HOH HOH A . 
E 3 HOH 7   707 706 HOH HOH A . 
E 3 HOH 8   708 726 HOH HOH A . 
E 3 HOH 9   709 713 HOH HOH A . 
E 3 HOH 10  710 729 HOH HOH A . 
E 3 HOH 11  711 712 HOH HOH A . 
E 3 HOH 12  712 727 HOH HOH A . 
E 3 HOH 13  713 830 HOH HOH A . 
E 3 HOH 14  714 728 HOH HOH A . 
E 3 HOH 15  715 719 HOH HOH A . 
E 3 HOH 16  716 725 HOH HOH A . 
E 3 HOH 17  717 722 HOH HOH A . 
E 3 HOH 18  718 733 HOH HOH A . 
E 3 HOH 19  719 716 HOH HOH A . 
E 3 HOH 20  720 730 HOH HOH A . 
E 3 HOH 21  721 732 HOH HOH A . 
E 3 HOH 22  722 711 HOH HOH A . 
E 3 HOH 23  723 721 HOH HOH A . 
E 3 HOH 24  724 718 HOH HOH A . 
E 3 HOH 25  725 741 HOH HOH A . 
E 3 HOH 26  726 738 HOH HOH A . 
E 3 HOH 27  727 747 HOH HOH A . 
E 3 HOH 28  728 735 HOH HOH A . 
E 3 HOH 29  729 720 HOH HOH A . 
E 3 HOH 30  730 743 HOH HOH A . 
E 3 HOH 31  731 739 HOH HOH A . 
E 3 HOH 32  732 773 HOH HOH A . 
E 3 HOH 33  733 750 HOH HOH A . 
E 3 HOH 34  734 744 HOH HOH A . 
E 3 HOH 35  735 770 HOH HOH A . 
E 3 HOH 36  736 724 HOH HOH A . 
E 3 HOH 37  737 736 HOH HOH A . 
E 3 HOH 38  738 745 HOH HOH A . 
E 3 HOH 39  739 784 HOH HOH A . 
E 3 HOH 40  740 737 HOH HOH A . 
E 3 HOH 41  741 751 HOH HOH A . 
E 3 HOH 42  742 752 HOH HOH A . 
E 3 HOH 43  743 753 HOH HOH A . 
E 3 HOH 44  744 708 HOH HOH A . 
E 3 HOH 45  745 703 HOH HOH A . 
E 3 HOH 46  746 734 HOH HOH A . 
E 3 HOH 47  747 749 HOH HOH A . 
E 3 HOH 48  748 756 HOH HOH A . 
E 3 HOH 49  749 788 HOH HOH A . 
E 3 HOH 50  750 746 HOH HOH A . 
E 3 HOH 51  751 715 HOH HOH A . 
E 3 HOH 52  752 786 HOH HOH A . 
E 3 HOH 53  753 761 HOH HOH A . 
E 3 HOH 54  754 767 HOH HOH A . 
E 3 HOH 55  755 760 HOH HOH A . 
E 3 HOH 56  756 771 HOH HOH A . 
E 3 HOH 57  757 754 HOH HOH A . 
E 3 HOH 58  758 776 HOH HOH A . 
E 3 HOH 59  759 775 HOH HOH A . 
E 3 HOH 60  760 765 HOH HOH A . 
E 3 HOH 61  761 758 HOH HOH A . 
E 3 HOH 62  762 759 HOH HOH A . 
E 3 HOH 63  763 772 HOH HOH A . 
E 3 HOH 64  764 793 HOH HOH A . 
E 3 HOH 65  765 755 HOH HOH A . 
E 3 HOH 66  766 790 HOH HOH A . 
E 3 HOH 67  767 766 HOH HOH A . 
E 3 HOH 68  768 835 HOH HOH A . 
E 3 HOH 69  769 802 HOH HOH A . 
E 3 HOH 70  770 763 HOH HOH A . 
E 3 HOH 71  771 785 HOH HOH A . 
E 3 HOH 72  772 806 HOH HOH A . 
E 3 HOH 73  773 748 HOH HOH A . 
E 3 HOH 74  774 787 HOH HOH A . 
E 3 HOH 75  775 809 HOH HOH A . 
E 3 HOH 76  776 779 HOH HOH A . 
E 3 HOH 77  777 814 HOH HOH A . 
E 3 HOH 78  778 805 HOH HOH A . 
E 3 HOH 79  779 812 HOH HOH A . 
E 3 HOH 80  780 796 HOH HOH A . 
E 3 HOH 81  781 795 HOH HOH A . 
E 3 HOH 82  782 789 HOH HOH A . 
E 3 HOH 83  783 800 HOH HOH A . 
E 3 HOH 84  784 740 HOH HOH A . 
E 3 HOH 85  785 764 HOH HOH A . 
E 3 HOH 86  786 798 HOH HOH A . 
E 3 HOH 87  787 723 HOH HOH A . 
E 3 HOH 88  788 774 HOH HOH A . 
E 3 HOH 89  789 808 HOH HOH A . 
E 3 HOH 90  790 797 HOH HOH A . 
E 3 HOH 91  791 856 HOH HOH A . 
E 3 HOH 92  792 823 HOH HOH A . 
E 3 HOH 93  793 782 HOH HOH A . 
E 3 HOH 94  794 777 HOH HOH A . 
E 3 HOH 95  795 807 HOH HOH A . 
E 3 HOH 96  796 768 HOH HOH A . 
E 3 HOH 97  797 791 HOH HOH A . 
E 3 HOH 98  798 769 HOH HOH A . 
E 3 HOH 99  799 778 HOH HOH A . 
E 3 HOH 100 800 824 HOH HOH A . 
E 3 HOH 101 801 783 HOH HOH A . 
E 3 HOH 102 802 799 HOH HOH A . 
E 3 HOH 103 803 815 HOH HOH A . 
E 3 HOH 104 804 822 HOH HOH A . 
E 3 HOH 105 805 829 HOH HOH A . 
E 3 HOH 106 806 817 HOH HOH A . 
E 3 HOH 107 807 801 HOH HOH A . 
E 3 HOH 108 808 813 HOH HOH A . 
E 3 HOH 109 809 838 HOH HOH A . 
E 3 HOH 110 810 872 HOH HOH A . 
E 3 HOH 111 811 821 HOH HOH A . 
E 3 HOH 112 812 816 HOH HOH A . 
E 3 HOH 113 813 811 HOH HOH A . 
E 3 HOH 114 814 825 HOH HOH A . 
E 3 HOH 115 815 819 HOH HOH A . 
E 3 HOH 116 816 841 HOH HOH A . 
E 3 HOH 117 817 837 HOH HOH A . 
E 3 HOH 118 818 820 HOH HOH A . 
E 3 HOH 119 819 831 HOH HOH A . 
E 3 HOH 120 820 826 HOH HOH A . 
E 3 HOH 121 821 803 HOH HOH A . 
E 3 HOH 122 822 810 HOH HOH A . 
E 3 HOH 123 823 792 HOH HOH A . 
E 3 HOH 124 824 839 HOH HOH A . 
E 3 HOH 125 825 803 HOH HOH A . 
E 3 HOH 126 826 781 HOH HOH A . 
E 3 HOH 127 827 842 HOH HOH A . 
E 3 HOH 128 828 742 HOH HOH A . 
E 3 HOH 129 829 847 HOH HOH A . 
E 3 HOH 130 830 818 HOH HOH A . 
E 3 HOH 131 831 833 HOH HOH A . 
E 3 HOH 132 832 858 HOH HOH A . 
E 3 HOH 133 833 851 HOH HOH A . 
E 3 HOH 134 834 762 HOH HOH A . 
E 3 HOH 135 835 845 HOH HOH A . 
E 3 HOH 136 836 834 HOH HOH A . 
E 3 HOH 137 837 859 HOH HOH A . 
E 3 HOH 138 838 863 HOH HOH A . 
E 3 HOH 139 839 849 HOH HOH A . 
E 3 HOH 140 840 855 HOH HOH A . 
E 3 HOH 141 841 827 HOH HOH A . 
E 3 HOH 142 842 919 HOH HOH A . 
E 3 HOH 143 843 836 HOH HOH A . 
E 3 HOH 144 844 846 HOH HOH A . 
E 3 HOH 145 845 848 HOH HOH A . 
E 3 HOH 146 846 832 HOH HOH A . 
E 3 HOH 147 847 860 HOH HOH A . 
E 3 HOH 148 848 862 HOH HOH A . 
E 3 HOH 149 849 780 HOH HOH A . 
E 3 HOH 150 850 843 HOH HOH A . 
E 3 HOH 151 851 880 HOH HOH A . 
E 3 HOH 152 852 865 HOH HOH A . 
E 3 HOH 153 853 864 HOH HOH A . 
E 3 HOH 154 854 903 HOH HOH A . 
E 3 HOH 155 855 874 HOH HOH A . 
E 3 HOH 156 856 871 HOH HOH A . 
E 3 HOH 157 857 870 HOH HOH A . 
E 3 HOH 158 858 885 HOH HOH A . 
E 3 HOH 159 859 898 HOH HOH A . 
E 3 HOH 160 860 868 HOH HOH A . 
E 3 HOH 161 861 879 HOH HOH A . 
E 3 HOH 162 862 876 HOH HOH A . 
E 3 HOH 163 863 878 HOH HOH A . 
E 3 HOH 164 864 857 HOH HOH A . 
E 3 HOH 165 865 869 HOH HOH A . 
E 3 HOH 166 866 702 HOH HOH A . 
E 3 HOH 167 867 884 HOH HOH A . 
E 3 HOH 168 868 877 HOH HOH A . 
E 3 HOH 169 869 896 HOH HOH A . 
E 3 HOH 170 870 875 HOH HOH A . 
E 3 HOH 171 871 882 HOH HOH A . 
E 3 HOH 172 872 887 HOH HOH A . 
E 3 HOH 173 873 883 HOH HOH A . 
E 3 HOH 174 874 892 HOH HOH A . 
E 3 HOH 175 875 897 HOH HOH A . 
E 3 HOH 176 876 902 HOH HOH A . 
E 3 HOH 177 877 881 HOH HOH A . 
E 3 HOH 178 878 914 HOH HOH A . 
E 3 HOH 179 879 893 HOH HOH A . 
E 3 HOH 180 880 894 HOH HOH A . 
E 3 HOH 181 881 910 HOH HOH A . 
E 3 HOH 182 882 888 HOH HOH A . 
E 3 HOH 183 883 901 HOH HOH A . 
E 3 HOH 184 884 886 HOH HOH A . 
E 3 HOH 185 885 913 HOH HOH A . 
E 3 HOH 186 886 854 HOH HOH A . 
E 3 HOH 187 887 904 HOH HOH A . 
E 3 HOH 188 888 906 HOH HOH A . 
E 3 HOH 189 889 900 HOH HOH A . 
E 3 HOH 190 890 899 HOH HOH A . 
E 3 HOH 191 891 889 HOH HOH A . 
E 3 HOH 192 892 908 HOH HOH A . 
E 3 HOH 193 893 912 HOH HOH A . 
E 3 HOH 194 894 909 HOH HOH A . 
E 3 HOH 195 895 911 HOH HOH A . 
E 3 HOH 196 896 917 HOH HOH A . 
E 3 HOH 197 897 918 HOH HOH A . 
E 3 HOH 198 898 922 HOH HOH A . 
E 3 HOH 199 899 915 HOH HOH A . 
E 3 HOH 200 900 905 HOH HOH A . 
E 3 HOH 201 901 907 HOH HOH A . 
E 3 HOH 202 902 921 HOH HOH A . 
E 3 HOH 203 903 928 HOH HOH A . 
E 3 HOH 204 904 924 HOH HOH A . 
E 3 HOH 205 905 923 HOH HOH A . 
E 3 HOH 206 906 925 HOH HOH A . 
E 3 HOH 207 907 920 HOH HOH A . 
E 3 HOH 208 908 926 HOH HOH A . 
E 3 HOH 209 909 927 HOH HOH A . 
E 3 HOH 210 910 929 HOH HOH A . 
F 3 HOH 1   701 702 HOH HOH B . 
F 3 HOH 2   702 710 HOH HOH B . 
F 3 HOH 3   703 709 HOH HOH B . 
F 3 HOH 4   704 707 HOH HOH B . 
F 3 HOH 5   705 712 HOH HOH B . 
F 3 HOH 6   706 714 HOH HOH B . 
F 3 HOH 7   707 706 HOH HOH B . 
F 3 HOH 8   708 724 HOH HOH B . 
F 3 HOH 9   709 717 HOH HOH B . 
F 3 HOH 10  710 719 HOH HOH B . 
F 3 HOH 11  711 727 HOH HOH B . 
F 3 HOH 12  712 705 HOH HOH B . 
F 3 HOH 13  713 778 HOH HOH B . 
F 3 HOH 14  714 715 HOH HOH B . 
F 3 HOH 15  715 708 HOH HOH B . 
F 3 HOH 16  716 755 HOH HOH B . 
F 3 HOH 17  717 738 HOH HOH B . 
F 3 HOH 18  718 735 HOH HOH B . 
F 3 HOH 19  719 795 HOH HOH B . 
F 3 HOH 20  720 729 HOH HOH B . 
F 3 HOH 21  721 713 HOH HOH B . 
F 3 HOH 22  722 874 HOH HOH B . 
F 3 HOH 23  723 711 HOH HOH B . 
F 3 HOH 24  724 746 HOH HOH B . 
F 3 HOH 25  725 720 HOH HOH B . 
F 3 HOH 26  726 718 HOH HOH B . 
F 3 HOH 27  727 722 HOH HOH B . 
F 3 HOH 28  728 721 HOH HOH B . 
F 3 HOH 29  729 734 HOH HOH B . 
F 3 HOH 30  730 736 HOH HOH B . 
F 3 HOH 31  731 726 HOH HOH B . 
F 3 HOH 32  732 750 HOH HOH B . 
F 3 HOH 33  733 739 HOH HOH B . 
F 3 HOH 34  734 757 HOH HOH B . 
F 3 HOH 35  735 732 HOH HOH B . 
F 3 HOH 36  736 759 HOH HOH B . 
F 3 HOH 37  737 716 HOH HOH B . 
F 3 HOH 38  738 760 HOH HOH B . 
F 3 HOH 39  739 748 HOH HOH B . 
F 3 HOH 40  740 728 HOH HOH B . 
F 3 HOH 41  741 745 HOH HOH B . 
F 3 HOH 42  742 742 HOH HOH B . 
F 3 HOH 43  743 768 HOH HOH B . 
F 3 HOH 44  744 771 HOH HOH B . 
F 3 HOH 45  745 743 HOH HOH B . 
F 3 HOH 46  746 737 HOH HOH B . 
F 3 HOH 47  747 766 HOH HOH B . 
F 3 HOH 48  748 844 HOH HOH B . 
F 3 HOH 49  749 774 HOH HOH B . 
F 3 HOH 50  750 772 HOH HOH B . 
F 3 HOH 51  751 740 HOH HOH B . 
F 3 HOH 52  752 783 HOH HOH B . 
F 3 HOH 53  753 756 HOH HOH B . 
F 3 HOH 54  754 749 HOH HOH B . 
F 3 HOH 55  755 723 HOH HOH B . 
F 3 HOH 56  756 754 HOH HOH B . 
F 3 HOH 57  757 788 HOH HOH B . 
F 3 HOH 58  758 765 HOH HOH B . 
F 3 HOH 59  759 731 HOH HOH B . 
F 3 HOH 60  760 764 HOH HOH B . 
F 3 HOH 61  761 733 HOH HOH B . 
F 3 HOH 62  762 758 HOH HOH B . 
F 3 HOH 63  763 777 HOH HOH B . 
F 3 HOH 64  764 780 HOH HOH B . 
F 3 HOH 65  765 770 HOH HOH B . 
F 3 HOH 66  766 741 HOH HOH B . 
F 3 HOH 67  767 779 HOH HOH B . 
F 3 HOH 68  768 763 HOH HOH B . 
F 3 HOH 69  769 761 HOH HOH B . 
F 3 HOH 70  770 790 HOH HOH B . 
F 3 HOH 71  771 809 HOH HOH B . 
F 3 HOH 72  772 789 HOH HOH B . 
F 3 HOH 73  773 806 HOH HOH B . 
F 3 HOH 74  774 781 HOH HOH B . 
F 3 HOH 75  775 816 HOH HOH B . 
F 3 HOH 76  776 800 HOH HOH B . 
F 3 HOH 77  777 730 HOH HOH B . 
F 3 HOH 78  778 775 HOH HOH B . 
F 3 HOH 79  779 776 HOH HOH B . 
F 3 HOH 80  780 751 HOH HOH B . 
F 3 HOH 81  781 819 HOH HOH B . 
F 3 HOH 82  782 784 HOH HOH B . 
F 3 HOH 83  783 773 HOH HOH B . 
F 3 HOH 84  784 826 HOH HOH B . 
F 3 HOH 85  785 787 HOH HOH B . 
F 3 HOH 86  786 703 HOH HOH B . 
F 3 HOH 87  787 762 HOH HOH B . 
F 3 HOH 88  788 704 HOH HOH B . 
F 3 HOH 89  789 786 HOH HOH B . 
F 3 HOH 90  790 785 HOH HOH B . 
F 3 HOH 91  791 752 HOH HOH B . 
F 3 HOH 92  792 747 HOH HOH B . 
F 3 HOH 93  793 794 HOH HOH B . 
F 3 HOH 94  794 890 HOH HOH B . 
F 3 HOH 95  795 827 HOH HOH B . 
F 3 HOH 96  796 782 HOH HOH B . 
F 3 HOH 97  797 791 HOH HOH B . 
F 3 HOH 98  798 793 HOH HOH B . 
F 3 HOH 99  799 753 HOH HOH B . 
F 3 HOH 100 800 807 HOH HOH B . 
F 3 HOH 101 801 805 HOH HOH B . 
F 3 HOH 102 802 810 HOH HOH B . 
F 3 HOH 103 803 802 HOH HOH B . 
F 3 HOH 104 804 843 HOH HOH B . 
F 3 HOH 105 805 769 HOH HOH B . 
F 3 HOH 106 806 813 HOH HOH B . 
F 3 HOH 107 807 834 HOH HOH B . 
F 3 HOH 108 808 796 HOH HOH B . 
F 3 HOH 109 809 820 HOH HOH B . 
F 3 HOH 110 810 815 HOH HOH B . 
F 3 HOH 111 811 849 HOH HOH B . 
F 3 HOH 112 812 829 HOH HOH B . 
F 3 HOH 113 813 839 HOH HOH B . 
F 3 HOH 114 814 767 HOH HOH B . 
F 3 HOH 115 815 863 HOH HOH B . 
F 3 HOH 116 816 801 HOH HOH B . 
F 3 HOH 117 817 840 HOH HOH B . 
F 3 HOH 118 818 811 HOH HOH B . 
F 3 HOH 119 819 814 HOH HOH B . 
F 3 HOH 120 820 821 HOH HOH B . 
F 3 HOH 121 821 799 HOH HOH B . 
F 3 HOH 122 822 818 HOH HOH B . 
F 3 HOH 123 823 875 HOH HOH B . 
F 3 HOH 124 824 830 HOH HOH B . 
F 3 HOH 125 825 833 HOH HOH B . 
F 3 HOH 126 826 857 HOH HOH B . 
F 3 HOH 127 827 823 HOH HOH B . 
F 3 HOH 128 828 792 HOH HOH B . 
F 3 HOH 129 829 831 HOH HOH B . 
F 3 HOH 130 830 797 HOH HOH B . 
F 3 HOH 131 831 847 HOH HOH B . 
F 3 HOH 132 832 824 HOH HOH B . 
F 3 HOH 133 833 808 HOH HOH B . 
F 3 HOH 134 834 825 HOH HOH B . 
F 3 HOH 135 835 822 HOH HOH B . 
F 3 HOH 136 836 835 HOH HOH B . 
F 3 HOH 137 837 836 HOH HOH B . 
F 3 HOH 138 838 845 HOH HOH B . 
F 3 HOH 139 839 842 HOH HOH B . 
F 3 HOH 140 840 838 HOH HOH B . 
F 3 HOH 141 841 804 HOH HOH B . 
F 3 HOH 142 842 837 HOH HOH B . 
F 3 HOH 143 843 854 HOH HOH B . 
F 3 HOH 144 844 861 HOH HOH B . 
F 3 HOH 145 845 841 HOH HOH B . 
F 3 HOH 146 846 856 HOH HOH B . 
F 3 HOH 147 847 848 HOH HOH B . 
F 3 HOH 148 848 858 HOH HOH B . 
F 3 HOH 149 849 828 HOH HOH B . 
F 3 HOH 150 850 812 HOH HOH B . 
F 3 HOH 151 851 832 HOH HOH B . 
F 3 HOH 152 852 861 HOH HOH B . 
F 3 HOH 153 853 855 HOH HOH B . 
F 3 HOH 154 854 862 HOH HOH B . 
F 3 HOH 155 855 798 HOH HOH B . 
F 3 HOH 156 856 851 HOH HOH B . 
F 3 HOH 157 857 866 HOH HOH B . 
F 3 HOH 158 858 846 HOH HOH B . 
F 3 HOH 159 859 865 HOH HOH B . 
F 3 HOH 160 860 859 HOH HOH B . 
F 3 HOH 161 861 853 HOH HOH B . 
F 3 HOH 162 862 852 HOH HOH B . 
F 3 HOH 163 863 864 HOH HOH B . 
F 3 HOH 164 864 868 HOH HOH B . 
F 3 HOH 165 865 872 HOH HOH B . 
F 3 HOH 166 866 876 HOH HOH B . 
F 3 HOH 167 867 873 HOH HOH B . 
F 3 HOH 168 868 871 HOH HOH B . 
F 3 HOH 169 869 879 HOH HOH B . 
F 3 HOH 170 870 870 HOH HOH B . 
F 3 HOH 171 871 878 HOH HOH B . 
F 3 HOH 172 872 883 HOH HOH B . 
F 3 HOH 173 873 880 HOH HOH B . 
F 3 HOH 174 874 877 HOH HOH B . 
F 3 HOH 175 875 725 HOH HOH B . 
F 3 HOH 176 876 882 HOH HOH B . 
F 3 HOH 177 877 884 HOH HOH B . 
F 3 HOH 178 878 869 HOH HOH B . 
F 3 HOH 179 879 860 HOH HOH B . 
F 3 HOH 180 880 881 HOH HOH B . 
F 3 HOH 181 881 888 HOH HOH B . 
F 3 HOH 182 882 885 HOH HOH B . 
F 3 HOH 183 883 887 HOH HOH B . 
F 3 HOH 184 884 891 HOH HOH B . 
F 3 HOH 185 885 896 HOH HOH B . 
F 3 HOH 186 886 897 HOH HOH B . 
F 3 HOH 187 887 892 HOH HOH B . 
F 3 HOH 188 888 886 HOH HOH B . 
F 3 HOH 189 889 898 HOH HOH B . 
F 3 HOH 190 890 894 HOH HOH B . 
F 3 HOH 191 891 893 HOH HOH B . 
F 3 HOH 192 892 895 HOH HOH B . 
F 3 HOH 193 893 900 HOH HOH B . 
F 3 HOH 194 894 899 HOH HOH B . 
F 3 HOH 195 895 902 HOH HOH B . 
F 3 HOH 196 896 901 HOH HOH B . 
F 3 HOH 197 897 904 HOH HOH B . 
F 3 HOH 198 898 905 HOH HOH B . 
F 3 HOH 199 899 903 HOH HOH B . 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly              ?    monomeric 1 
2 author_defined_assembly              ?    monomeric 1 
3 author_and_software_defined_assembly PISA dimeric   2 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,E       
2 1 B,D,F       
3 1 A,B,C,D,E,F 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
3 'ABSA (A^2)' 1580  ? 
3 MORE         2     ? 
3 'SSA (A^2)'  58810 ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2015-09-09 
2 'Structure model' 1 1 2017-09-13 
3 'Structure model' 1 2 2018-10-10 
4 'Structure model' 1 3 2019-12-25 
5 'Structure model' 1 4 2023-09-27 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1  2 'Structure model' 'Author supporting evidence' 
2  2 'Structure model' 'Derived calculations'       
3  3 'Structure model' 'Data collection'            
4  3 'Structure model' 'Database references'        
5  3 'Structure model' 'Structure summary'          
6  4 'Structure model' 'Author supporting evidence' 
7  4 'Structure model' 'Structure summary'          
8  5 'Structure model' 'Data collection'            
9  5 'Structure model' 'Database references'        
10 5 'Structure model' 'Refinement description'     
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1  2 'Structure model' pdbx_audit_support            
2  2 'Structure model' pdbx_struct_oper_list         
3  3 'Structure model' citation                      
4  3 'Structure model' entity                        
5  4 'Structure model' entity                        
6  4 'Structure model' pdbx_audit_support            
7  5 'Structure model' chem_comp_atom                
8  5 'Structure model' chem_comp_bond                
9  5 'Structure model' database_2                    
10 5 'Structure model' pdbx_initial_refinement_model 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_pdbx_audit_support.funding_organization'  
2  2 'Structure model' '_pdbx_struct_oper_list.symmetry_operation' 
3  3 'Structure model' '_citation.journal_id_ISSN'                 
4  3 'Structure model' '_citation.page_first'                      
5  3 'Structure model' '_citation.page_last'                       
6  3 'Structure model' '_citation.pdbx_database_id_DOI'            
7  3 'Structure model' '_citation.pdbx_database_id_PubMed'         
8  3 'Structure model' '_citation.title'                           
9  3 'Structure model' '_entity.formula_weight'                    
10 4 'Structure model' '_entity.formula_weight'                    
11 4 'Structure model' '_pdbx_audit_support.funding_organization'  
12 5 'Structure model' '_database_2.pdbx_DOI'                      
13 5 'Structure model' '_database_2.pdbx_database_accession'       
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
'X-RAY DIFFRACTION' 1 ? refined 3.3100   5.6380  -50.5170 0.0957 0.2240 0.0165 0.0153  0.0044 -0.0053 0.7366 0.2405 1.0439 0.0701  
-0.6466 0.1246  0.0724  0.2986 -0.0057 -0.0183 -0.0141 -0.0267 -0.0191 -0.3968 -0.0583 
'X-RAY DIFFRACTION' 2 ? refined -10.7610 34.8410 -21.8880 0.1009 0.2408 0.0320 -0.0289 0.0170 -0.0135 0.3753 0.1821 1.6145 -0.0942 
-0.4253 -0.0243 -0.0508 0.1994 0.0559  0.0600  -0.0015 0.0022  0.1212  -0.5267 0.0523  
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1 1 A 1 ? ? A 596 ? ? ? ? 
'X-RAY DIFFRACTION' 2 2 B 1 ? ? B 596 ? ? ? ? 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC    ? ? ? 5.6.0117 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? MOSFLM    ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? SCALEPACK ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER    ? ? ? .        4 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 PRO A 45  ? ? -38.96  148.26  
2  1 PHE A 83  ? ? 80.31   -5.95   
3  1 TRP A 102 ? ? -67.63  0.84    
4  1 ILE A 126 ? ? -127.46 -50.45  
5  1 LEU A 141 ? ? 78.46   -9.30   
6  1 LYS A 167 ? ? -78.07  25.30   
7  1 MET A 168 ? ? -127.14 -160.32 
8  1 ASP A 176 ? ? 77.11   -12.67  
9  1 GLU A 177 ? ? -93.35  49.36   
10 1 VAL A 178 ? ? -135.48 -36.38  
11 1 LYS A 179 ? ? 71.39   105.04  
12 1 GLN A 190 ? ? 53.49   -84.43  
13 1 ASN A 192 ? ? -112.03 -134.74 
14 1 PRO A 201 ? ? -93.68  -79.78  
15 1 ASP A 202 ? ? 56.23   -93.04  
16 1 SER A 203 ? ? 46.21   92.20   
17 1 ALA A 204 ? ? 56.58   -89.10  
18 1 GLU A 222 ? ? -108.23 -71.53  
19 1 LYS A 225 ? ? -71.38  24.89   
20 1 SER A 227 ? ? -115.03 -83.53  
21 1 ASP A 254 ? ? 25.35   74.56   
22 1 PRO A 272 ? ? -117.63 78.60   
23 1 LEU A 276 ? ? -125.26 -53.31  
24 1 ASP A 277 ? ? 65.04   -139.02 
25 1 PHE A 295 ? ? -141.60 -135.61 
26 1 ARG A 297 ? ? 66.11   -18.09  
27 1 ASN A 303 ? ? -116.82 60.37   
28 1 PHE A 329 ? ? -116.89 65.80   
29 1 ASP A 333 ? ? 143.86  133.84  
30 1 ARG A 399 ? ? 73.25   -3.49   
31 1 LYS A 406 ? ? 119.32  10.43   
32 1 LYS A 526 ? ? -178.36 118.48  
33 1 SER B 25  ? ? -69.44  0.39    
34 1 PHE B 83  ? ? 78.71   -13.44  
35 1 HIS B 92  ? ? -143.71 -20.23  
36 1 LEU B 141 ? ? 73.87   -3.98   
37 1 LYS B 166 ? ? -68.34  -74.55  
38 1 LYS B 167 ? ? -79.54  31.55   
39 1 VAL B 174 ? ? -150.31 81.73   
40 1 GLN B 175 ? ? 56.07   -174.69 
41 1 GLU B 177 ? ? -159.21 18.23   
42 1 LYS B 179 ? ? -158.23 81.17   
43 1 ARG B 181 ? ? 96.57   -53.68  
44 1 GLN B 190 ? ? -56.39  94.03   
45 1 ASP B 191 ? ? 70.75   -0.41   
46 1 ASN B 192 ? ? -138.82 -159.00 
47 1 ASP B 202 ? ? 74.24   59.04   
48 1 ARG B 205 ? ? 74.62   141.82  
49 1 ASP B 254 ? ? 42.19   70.67   
50 1 ILE B 271 ? ? -39.42  116.66  
51 1 LEU B 275 ? ? -123.95 -69.21  
52 1 LEU B 276 ? ? -79.92  -98.22  
53 1 ASN B 290 ? ? -111.15 67.88   
54 1 PHE B 295 ? ? -115.28 -101.94 
55 1 ASN B 331 ? ? -100.58 43.31   
56 1 ASP B 333 ? ? 143.07  96.82   
57 1 THR B 341 ? ? -122.58 -168.13 
58 1 LYS B 406 ? ? 28.26   -104.11 
59 1 ASN B 430 ? ? -118.04 61.72   
60 1 VAL B 456 ? ? -83.21  -73.18  
61 1 ASN B 492 ? ? 74.94   -56.35  
62 1 ARG B 525 ? ? -107.94 -69.93  
63 1 LYS B 526 ? ? -171.13 113.10  
64 1 LYS B 552 ? ? -28.98  -61.81  
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   LYS 
_pdbx_validate_peptide_omega.auth_asym_id_1   B 
_pdbx_validate_peptide_omega.auth_seq_id_1    406 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   LEU 
_pdbx_validate_peptide_omega.auth_asym_id_2   B 
_pdbx_validate_peptide_omega.auth_seq_id_2    407 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            -41.10 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
55C C5   C Y N 1   
55C C3   C Y N 2   
55C C2   C Y N 3   
55C C4   C Y N 4   
55C N1   N N N 5   
55C O21  O N N 6   
55C C13  C N N 7   
55C C15  C Y N 8   
55C C17  C Y N 9   
55C C16  C Y N 10  
55C C20  C Y N 11  
55C C19  C Y N 12  
55C C18  C Y N 13  
55C C21  C N N 14  
55C O22  O N N 15  
55C O23  O N N 16  
55C C12  C N N 17  
55C C11  C N N 18  
55C C14  C N N 19  
55C C10  C Y N 20  
55C C9   C Y N 21  
55C C8   C Y N 22  
55C C6   C Y N 23  
55C C7   C Y N 24  
55C C1   C Y N 25  
55C H1   H N N 26  
55C H2   H N N 27  
55C H3   H N N 28  
55C H4   H N N 29  
55C H5   H N N 30  
55C H6   H N N 31  
55C H7   H N N 32  
55C H8   H N N 33  
55C H9   H N N 34  
55C H10  H N N 35  
55C H11  H N N 36  
55C H12  H N N 37  
55C H13  H N N 38  
55C H14  H N N 39  
55C H15  H N N 40  
55C H16  H N N 41  
55C H17  H N N 42  
ALA N    N N N 43  
ALA CA   C N S 44  
ALA C    C N N 45  
ALA O    O N N 46  
ALA CB   C N N 47  
ALA OXT  O N N 48  
ALA H    H N N 49  
ALA H2   H N N 50  
ALA HA   H N N 51  
ALA HB1  H N N 52  
ALA HB2  H N N 53  
ALA HB3  H N N 54  
ALA HXT  H N N 55  
ARG N    N N N 56  
ARG CA   C N S 57  
ARG C    C N N 58  
ARG O    O N N 59  
ARG CB   C N N 60  
ARG CG   C N N 61  
ARG CD   C N N 62  
ARG NE   N N N 63  
ARG CZ   C N N 64  
ARG NH1  N N N 65  
ARG NH2  N N N 66  
ARG OXT  O N N 67  
ARG H    H N N 68  
ARG H2   H N N 69  
ARG HA   H N N 70  
ARG HB2  H N N 71  
ARG HB3  H N N 72  
ARG HG2  H N N 73  
ARG HG3  H N N 74  
ARG HD2  H N N 75  
ARG HD3  H N N 76  
ARG HE   H N N 77  
ARG HH11 H N N 78  
ARG HH12 H N N 79  
ARG HH21 H N N 80  
ARG HH22 H N N 81  
ARG HXT  H N N 82  
ASN N    N N N 83  
ASN CA   C N S 84  
ASN C    C N N 85  
ASN O    O N N 86  
ASN CB   C N N 87  
ASN CG   C N N 88  
ASN OD1  O N N 89  
ASN ND2  N N N 90  
ASN OXT  O N N 91  
ASN H    H N N 92  
ASN H2   H N N 93  
ASN HA   H N N 94  
ASN HB2  H N N 95  
ASN HB3  H N N 96  
ASN HD21 H N N 97  
ASN HD22 H N N 98  
ASN HXT  H N N 99  
ASP N    N N N 100 
ASP CA   C N S 101 
ASP C    C N N 102 
ASP O    O N N 103 
ASP CB   C N N 104 
ASP CG   C N N 105 
ASP OD1  O N N 106 
ASP OD2  O N N 107 
ASP OXT  O N N 108 
ASP H    H N N 109 
ASP H2   H N N 110 
ASP HA   H N N 111 
ASP HB2  H N N 112 
ASP HB3  H N N 113 
ASP HD2  H N N 114 
ASP HXT  H N N 115 
CYS N    N N N 116 
CYS CA   C N R 117 
CYS C    C N N 118 
CYS O    O N N 119 
CYS CB   C N N 120 
CYS SG   S N N 121 
CYS OXT  O N N 122 
CYS H    H N N 123 
CYS H2   H N N 124 
CYS HA   H N N 125 
CYS HB2  H N N 126 
CYS HB3  H N N 127 
CYS HG   H N N 128 
CYS HXT  H N N 129 
GLN N    N N N 130 
GLN CA   C N S 131 
GLN C    C N N 132 
GLN O    O N N 133 
GLN CB   C N N 134 
GLN CG   C N N 135 
GLN CD   C N N 136 
GLN OE1  O N N 137 
GLN NE2  N N N 138 
GLN OXT  O N N 139 
GLN H    H N N 140 
GLN H2   H N N 141 
GLN HA   H N N 142 
GLN HB2  H N N 143 
GLN HB3  H N N 144 
GLN HG2  H N N 145 
GLN HG3  H N N 146 
GLN HE21 H N N 147 
GLN HE22 H N N 148 
GLN HXT  H N N 149 
GLU N    N N N 150 
GLU CA   C N S 151 
GLU C    C N N 152 
GLU O    O N N 153 
GLU CB   C N N 154 
GLU CG   C N N 155 
GLU CD   C N N 156 
GLU OE1  O N N 157 
GLU OE2  O N N 158 
GLU OXT  O N N 159 
GLU H    H N N 160 
GLU H2   H N N 161 
GLU HA   H N N 162 
GLU HB2  H N N 163 
GLU HB3  H N N 164 
GLU HG2  H N N 165 
GLU HG3  H N N 166 
GLU HE2  H N N 167 
GLU HXT  H N N 168 
GLY N    N N N 169 
GLY CA   C N N 170 
GLY C    C N N 171 
GLY O    O N N 172 
GLY OXT  O N N 173 
GLY H    H N N 174 
GLY H2   H N N 175 
GLY HA2  H N N 176 
GLY HA3  H N N 177 
GLY HXT  H N N 178 
HIS N    N N N 179 
HIS CA   C N S 180 
HIS C    C N N 181 
HIS O    O N N 182 
HIS CB   C N N 183 
HIS CG   C Y N 184 
HIS ND1  N Y N 185 
HIS CD2  C Y N 186 
HIS CE1  C Y N 187 
HIS NE2  N Y N 188 
HIS OXT  O N N 189 
HIS H    H N N 190 
HIS H2   H N N 191 
HIS HA   H N N 192 
HIS HB2  H N N 193 
HIS HB3  H N N 194 
HIS HD1  H N N 195 
HIS HD2  H N N 196 
HIS HE1  H N N 197 
HIS HE2  H N N 198 
HIS HXT  H N N 199 
HOH O    O N N 200 
HOH H1   H N N 201 
HOH H2   H N N 202 
ILE N    N N N 203 
ILE CA   C N S 204 
ILE C    C N N 205 
ILE O    O N N 206 
ILE CB   C N S 207 
ILE CG1  C N N 208 
ILE CG2  C N N 209 
ILE CD1  C N N 210 
ILE OXT  O N N 211 
ILE H    H N N 212 
ILE H2   H N N 213 
ILE HA   H N N 214 
ILE HB   H N N 215 
ILE HG12 H N N 216 
ILE HG13 H N N 217 
ILE HG21 H N N 218 
ILE HG22 H N N 219 
ILE HG23 H N N 220 
ILE HD11 H N N 221 
ILE HD12 H N N 222 
ILE HD13 H N N 223 
ILE HXT  H N N 224 
LEU N    N N N 225 
LEU CA   C N S 226 
LEU C    C N N 227 
LEU O    O N N 228 
LEU CB   C N N 229 
LEU CG   C N N 230 
LEU CD1  C N N 231 
LEU CD2  C N N 232 
LEU OXT  O N N 233 
LEU H    H N N 234 
LEU H2   H N N 235 
LEU HA   H N N 236 
LEU HB2  H N N 237 
LEU HB3  H N N 238 
LEU HG   H N N 239 
LEU HD11 H N N 240 
LEU HD12 H N N 241 
LEU HD13 H N N 242 
LEU HD21 H N N 243 
LEU HD22 H N N 244 
LEU HD23 H N N 245 
LEU HXT  H N N 246 
LYS N    N N N 247 
LYS CA   C N S 248 
LYS C    C N N 249 
LYS O    O N N 250 
LYS CB   C N N 251 
LYS CG   C N N 252 
LYS CD   C N N 253 
LYS CE   C N N 254 
LYS NZ   N N N 255 
LYS OXT  O N N 256 
LYS H    H N N 257 
LYS H2   H N N 258 
LYS HA   H N N 259 
LYS HB2  H N N 260 
LYS HB3  H N N 261 
LYS HG2  H N N 262 
LYS HG3  H N N 263 
LYS HD2  H N N 264 
LYS HD3  H N N 265 
LYS HE2  H N N 266 
LYS HE3  H N N 267 
LYS HZ1  H N N 268 
LYS HZ2  H N N 269 
LYS HZ3  H N N 270 
LYS HXT  H N N 271 
MET N    N N N 272 
MET CA   C N S 273 
MET C    C N N 274 
MET O    O N N 275 
MET CB   C N N 276 
MET CG   C N N 277 
MET SD   S N N 278 
MET CE   C N N 279 
MET OXT  O N N 280 
MET H    H N N 281 
MET H2   H N N 282 
MET HA   H N N 283 
MET HB2  H N N 284 
MET HB3  H N N 285 
MET HG2  H N N 286 
MET HG3  H N N 287 
MET HE1  H N N 288 
MET HE2  H N N 289 
MET HE3  H N N 290 
MET HXT  H N N 291 
PHE N    N N N 292 
PHE CA   C N S 293 
PHE C    C N N 294 
PHE O    O N N 295 
PHE CB   C N N 296 
PHE CG   C Y N 297 
PHE CD1  C Y N 298 
PHE CD2  C Y N 299 
PHE CE1  C Y N 300 
PHE CE2  C Y N 301 
PHE CZ   C Y N 302 
PHE OXT  O N N 303 
PHE H    H N N 304 
PHE H2   H N N 305 
PHE HA   H N N 306 
PHE HB2  H N N 307 
PHE HB3  H N N 308 
PHE HD1  H N N 309 
PHE HD2  H N N 310 
PHE HE1  H N N 311 
PHE HE2  H N N 312 
PHE HZ   H N N 313 
PHE HXT  H N N 314 
PRO N    N N N 315 
PRO CA   C N S 316 
PRO C    C N N 317 
PRO O    O N N 318 
PRO CB   C N N 319 
PRO CG   C N N 320 
PRO CD   C N N 321 
PRO OXT  O N N 322 
PRO H    H N N 323 
PRO HA   H N N 324 
PRO HB2  H N N 325 
PRO HB3  H N N 326 
PRO HG2  H N N 327 
PRO HG3  H N N 328 
PRO HD2  H N N 329 
PRO HD3  H N N 330 
PRO HXT  H N N 331 
SER N    N N N 332 
SER CA   C N S 333 
SER C    C N N 334 
SER O    O N N 335 
SER CB   C N N 336 
SER OG   O N N 337 
SER OXT  O N N 338 
SER H    H N N 339 
SER H2   H N N 340 
SER HA   H N N 341 
SER HB2  H N N 342 
SER HB3  H N N 343 
SER HG   H N N 344 
SER HXT  H N N 345 
THR N    N N N 346 
THR CA   C N S 347 
THR C    C N N 348 
THR O    O N N 349 
THR CB   C N R 350 
THR OG1  O N N 351 
THR CG2  C N N 352 
THR OXT  O N N 353 
THR H    H N N 354 
THR H2   H N N 355 
THR HA   H N N 356 
THR HB   H N N 357 
THR HG1  H N N 358 
THR HG21 H N N 359 
THR HG22 H N N 360 
THR HG23 H N N 361 
THR HXT  H N N 362 
TRP N    N N N 363 
TRP CA   C N S 364 
TRP C    C N N 365 
TRP O    O N N 366 
TRP CB   C N N 367 
TRP CG   C Y N 368 
TRP CD1  C Y N 369 
TRP CD2  C Y N 370 
TRP NE1  N Y N 371 
TRP CE2  C Y N 372 
TRP CE3  C Y N 373 
TRP CZ2  C Y N 374 
TRP CZ3  C Y N 375 
TRP CH2  C Y N 376 
TRP OXT  O N N 377 
TRP H    H N N 378 
TRP H2   H N N 379 
TRP HA   H N N 380 
TRP HB2  H N N 381 
TRP HB3  H N N 382 
TRP HD1  H N N 383 
TRP HE1  H N N 384 
TRP HE3  H N N 385 
TRP HZ2  H N N 386 
TRP HZ3  H N N 387 
TRP HH2  H N N 388 
TRP HXT  H N N 389 
TYR N    N N N 390 
TYR CA   C N S 391 
TYR C    C N N 392 
TYR O    O N N 393 
TYR CB   C N N 394 
TYR CG   C Y N 395 
TYR CD1  C Y N 396 
TYR CD2  C Y N 397 
TYR CE1  C Y N 398 
TYR CE2  C Y N 399 
TYR CZ   C Y N 400 
TYR OH   O N N 401 
TYR OXT  O N N 402 
TYR H    H N N 403 
TYR H2   H N N 404 
TYR HA   H N N 405 
TYR HB2  H N N 406 
TYR HB3  H N N 407 
TYR HD1  H N N 408 
TYR HD2  H N N 409 
TYR HE1  H N N 410 
TYR HE2  H N N 411 
TYR HH   H N N 412 
TYR HXT  H N N 413 
VAL N    N N N 414 
VAL CA   C N S 415 
VAL C    C N N 416 
VAL O    O N N 417 
VAL CB   C N N 418 
VAL CG1  C N N 419 
VAL CG2  C N N 420 
VAL OXT  O N N 421 
VAL H    H N N 422 
VAL H2   H N N 423 
VAL HA   H N N 424 
VAL HB   H N N 425 
VAL HG11 H N N 426 
VAL HG12 H N N 427 
VAL HG13 H N N 428 
VAL HG21 H N N 429 
VAL HG22 H N N 430 
VAL HG23 H N N 431 
VAL HXT  H N N 432 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
55C C20 C16  doub Y N 1   
55C C20 C19  sing Y N 2   
55C C16 C17  sing Y N 3   
55C C19 C18  doub Y N 4   
55C C17 C15  doub Y N 5   
55C C18 C15  sing Y N 6   
55C C18 C21  sing N N 7   
55C C15 N1   sing N N 8   
55C O22 C21  doub N N 9   
55C C21 O23  sing N N 10  
55C O21 C13  doub N N 11  
55C N1  C13  sing N N 12  
55C C13 C12  sing N N 13  
55C C12 C11  doub N E 14  
55C C14 C11  sing N N 15  
55C C11 C10  sing N N 16  
55C C10 C9   doub Y N 17  
55C C10 C7   sing Y N 18  
55C C9  C8   sing Y N 19  
55C C7  C6   doub Y N 20  
55C C8  C5   doub Y N 21  
55C C6  C5   sing Y N 22  
55C C6  C1   sing Y N 23  
55C C5  C4   sing Y N 24  
55C C1  C2   doub Y N 25  
55C C4  C3   doub Y N 26  
55C C2  C3   sing Y N 27  
55C C3  H1   sing N N 28  
55C C2  H2   sing N N 29  
55C C4  H3   sing N N 30  
55C N1  H4   sing N N 31  
55C C17 H5   sing N N 32  
55C C16 H6   sing N N 33  
55C C20 H7   sing N N 34  
55C C19 H8   sing N N 35  
55C O23 H9   sing N N 36  
55C C12 H10  sing N N 37  
55C C14 H11  sing N N 38  
55C C14 H12  sing N N 39  
55C C14 H13  sing N N 40  
55C C9  H14  sing N N 41  
55C C8  H15  sing N N 42  
55C C7  H16  sing N N 43  
55C C1  H17  sing N N 44  
ALA N   CA   sing N N 45  
ALA N   H    sing N N 46  
ALA N   H2   sing N N 47  
ALA CA  C    sing N N 48  
ALA CA  CB   sing N N 49  
ALA CA  HA   sing N N 50  
ALA C   O    doub N N 51  
ALA C   OXT  sing N N 52  
ALA CB  HB1  sing N N 53  
ALA CB  HB2  sing N N 54  
ALA CB  HB3  sing N N 55  
ALA OXT HXT  sing N N 56  
ARG N   CA   sing N N 57  
ARG N   H    sing N N 58  
ARG N   H2   sing N N 59  
ARG CA  C    sing N N 60  
ARG CA  CB   sing N N 61  
ARG CA  HA   sing N N 62  
ARG C   O    doub N N 63  
ARG C   OXT  sing N N 64  
ARG CB  CG   sing N N 65  
ARG CB  HB2  sing N N 66  
ARG CB  HB3  sing N N 67  
ARG CG  CD   sing N N 68  
ARG CG  HG2  sing N N 69  
ARG CG  HG3  sing N N 70  
ARG CD  NE   sing N N 71  
ARG CD  HD2  sing N N 72  
ARG CD  HD3  sing N N 73  
ARG NE  CZ   sing N N 74  
ARG NE  HE   sing N N 75  
ARG CZ  NH1  sing N N 76  
ARG CZ  NH2  doub N N 77  
ARG NH1 HH11 sing N N 78  
ARG NH1 HH12 sing N N 79  
ARG NH2 HH21 sing N N 80  
ARG NH2 HH22 sing N N 81  
ARG OXT HXT  sing N N 82  
ASN N   CA   sing N N 83  
ASN N   H    sing N N 84  
ASN N   H2   sing N N 85  
ASN CA  C    sing N N 86  
ASN CA  CB   sing N N 87  
ASN CA  HA   sing N N 88  
ASN C   O    doub N N 89  
ASN C   OXT  sing N N 90  
ASN CB  CG   sing N N 91  
ASN CB  HB2  sing N N 92  
ASN CB  HB3  sing N N 93  
ASN CG  OD1  doub N N 94  
ASN CG  ND2  sing N N 95  
ASN ND2 HD21 sing N N 96  
ASN ND2 HD22 sing N N 97  
ASN OXT HXT  sing N N 98  
ASP N   CA   sing N N 99  
ASP N   H    sing N N 100 
ASP N   H2   sing N N 101 
ASP CA  C    sing N N 102 
ASP CA  CB   sing N N 103 
ASP CA  HA   sing N N 104 
ASP C   O    doub N N 105 
ASP C   OXT  sing N N 106 
ASP CB  CG   sing N N 107 
ASP CB  HB2  sing N N 108 
ASP CB  HB3  sing N N 109 
ASP CG  OD1  doub N N 110 
ASP CG  OD2  sing N N 111 
ASP OD2 HD2  sing N N 112 
ASP OXT HXT  sing N N 113 
CYS N   CA   sing N N 114 
CYS N   H    sing N N 115 
CYS N   H2   sing N N 116 
CYS CA  C    sing N N 117 
CYS CA  CB   sing N N 118 
CYS CA  HA   sing N N 119 
CYS C   O    doub N N 120 
CYS C   OXT  sing N N 121 
CYS CB  SG   sing N N 122 
CYS CB  HB2  sing N N 123 
CYS CB  HB3  sing N N 124 
CYS SG  HG   sing N N 125 
CYS OXT HXT  sing N N 126 
GLN N   CA   sing N N 127 
GLN N   H    sing N N 128 
GLN N   H2   sing N N 129 
GLN CA  C    sing N N 130 
GLN CA  CB   sing N N 131 
GLN CA  HA   sing N N 132 
GLN C   O    doub N N 133 
GLN C   OXT  sing N N 134 
GLN CB  CG   sing N N 135 
GLN CB  HB2  sing N N 136 
GLN CB  HB3  sing N N 137 
GLN CG  CD   sing N N 138 
GLN CG  HG2  sing N N 139 
GLN CG  HG3  sing N N 140 
GLN CD  OE1  doub N N 141 
GLN CD  NE2  sing N N 142 
GLN NE2 HE21 sing N N 143 
GLN NE2 HE22 sing N N 144 
GLN OXT HXT  sing N N 145 
GLU N   CA   sing N N 146 
GLU N   H    sing N N 147 
GLU N   H2   sing N N 148 
GLU CA  C    sing N N 149 
GLU CA  CB   sing N N 150 
GLU CA  HA   sing N N 151 
GLU C   O    doub N N 152 
GLU C   OXT  sing N N 153 
GLU CB  CG   sing N N 154 
GLU CB  HB2  sing N N 155 
GLU CB  HB3  sing N N 156 
GLU CG  CD   sing N N 157 
GLU CG  HG2  sing N N 158 
GLU CG  HG3  sing N N 159 
GLU CD  OE1  doub N N 160 
GLU CD  OE2  sing N N 161 
GLU OE2 HE2  sing N N 162 
GLU OXT HXT  sing N N 163 
GLY N   CA   sing N N 164 
GLY N   H    sing N N 165 
GLY N   H2   sing N N 166 
GLY CA  C    sing N N 167 
GLY CA  HA2  sing N N 168 
GLY CA  HA3  sing N N 169 
GLY C   O    doub N N 170 
GLY C   OXT  sing N N 171 
GLY OXT HXT  sing N N 172 
HIS N   CA   sing N N 173 
HIS N   H    sing N N 174 
HIS N   H2   sing N N 175 
HIS CA  C    sing N N 176 
HIS CA  CB   sing N N 177 
HIS CA  HA   sing N N 178 
HIS C   O    doub N N 179 
HIS C   OXT  sing N N 180 
HIS CB  CG   sing N N 181 
HIS CB  HB2  sing N N 182 
HIS CB  HB3  sing N N 183 
HIS CG  ND1  sing Y N 184 
HIS CG  CD2  doub Y N 185 
HIS ND1 CE1  doub Y N 186 
HIS ND1 HD1  sing N N 187 
HIS CD2 NE2  sing Y N 188 
HIS CD2 HD2  sing N N 189 
HIS CE1 NE2  sing Y N 190 
HIS CE1 HE1  sing N N 191 
HIS NE2 HE2  sing N N 192 
HIS OXT HXT  sing N N 193 
HOH O   H1   sing N N 194 
HOH O   H2   sing N N 195 
ILE N   CA   sing N N 196 
ILE N   H    sing N N 197 
ILE N   H2   sing N N 198 
ILE CA  C    sing N N 199 
ILE CA  CB   sing N N 200 
ILE CA  HA   sing N N 201 
ILE C   O    doub N N 202 
ILE C   OXT  sing N N 203 
ILE CB  CG1  sing N N 204 
ILE CB  CG2  sing N N 205 
ILE CB  HB   sing N N 206 
ILE CG1 CD1  sing N N 207 
ILE CG1 HG12 sing N N 208 
ILE CG1 HG13 sing N N 209 
ILE CG2 HG21 sing N N 210 
ILE CG2 HG22 sing N N 211 
ILE CG2 HG23 sing N N 212 
ILE CD1 HD11 sing N N 213 
ILE CD1 HD12 sing N N 214 
ILE CD1 HD13 sing N N 215 
ILE OXT HXT  sing N N 216 
LEU N   CA   sing N N 217 
LEU N   H    sing N N 218 
LEU N   H2   sing N N 219 
LEU CA  C    sing N N 220 
LEU CA  CB   sing N N 221 
LEU CA  HA   sing N N 222 
LEU C   O    doub N N 223 
LEU C   OXT  sing N N 224 
LEU CB  CG   sing N N 225 
LEU CB  HB2  sing N N 226 
LEU CB  HB3  sing N N 227 
LEU CG  CD1  sing N N 228 
LEU CG  CD2  sing N N 229 
LEU CG  HG   sing N N 230 
LEU CD1 HD11 sing N N 231 
LEU CD1 HD12 sing N N 232 
LEU CD1 HD13 sing N N 233 
LEU CD2 HD21 sing N N 234 
LEU CD2 HD22 sing N N 235 
LEU CD2 HD23 sing N N 236 
LEU OXT HXT  sing N N 237 
LYS N   CA   sing N N 238 
LYS N   H    sing N N 239 
LYS N   H2   sing N N 240 
LYS CA  C    sing N N 241 
LYS CA  CB   sing N N 242 
LYS CA  HA   sing N N 243 
LYS C   O    doub N N 244 
LYS C   OXT  sing N N 245 
LYS CB  CG   sing N N 246 
LYS CB  HB2  sing N N 247 
LYS CB  HB3  sing N N 248 
LYS CG  CD   sing N N 249 
LYS CG  HG2  sing N N 250 
LYS CG  HG3  sing N N 251 
LYS CD  CE   sing N N 252 
LYS CD  HD2  sing N N 253 
LYS CD  HD3  sing N N 254 
LYS CE  NZ   sing N N 255 
LYS CE  HE2  sing N N 256 
LYS CE  HE3  sing N N 257 
LYS NZ  HZ1  sing N N 258 
LYS NZ  HZ2  sing N N 259 
LYS NZ  HZ3  sing N N 260 
LYS OXT HXT  sing N N 261 
MET N   CA   sing N N 262 
MET N   H    sing N N 263 
MET N   H2   sing N N 264 
MET CA  C    sing N N 265 
MET CA  CB   sing N N 266 
MET CA  HA   sing N N 267 
MET C   O    doub N N 268 
MET C   OXT  sing N N 269 
MET CB  CG   sing N N 270 
MET CB  HB2  sing N N 271 
MET CB  HB3  sing N N 272 
MET CG  SD   sing N N 273 
MET CG  HG2  sing N N 274 
MET CG  HG3  sing N N 275 
MET SD  CE   sing N N 276 
MET CE  HE1  sing N N 277 
MET CE  HE2  sing N N 278 
MET CE  HE3  sing N N 279 
MET OXT HXT  sing N N 280 
PHE N   CA   sing N N 281 
PHE N   H    sing N N 282 
PHE N   H2   sing N N 283 
PHE CA  C    sing N N 284 
PHE CA  CB   sing N N 285 
PHE CA  HA   sing N N 286 
PHE C   O    doub N N 287 
PHE C   OXT  sing N N 288 
PHE CB  CG   sing N N 289 
PHE CB  HB2  sing N N 290 
PHE CB  HB3  sing N N 291 
PHE CG  CD1  doub Y N 292 
PHE CG  CD2  sing Y N 293 
PHE CD1 CE1  sing Y N 294 
PHE CD1 HD1  sing N N 295 
PHE CD2 CE2  doub Y N 296 
PHE CD2 HD2  sing N N 297 
PHE CE1 CZ   doub Y N 298 
PHE CE1 HE1  sing N N 299 
PHE CE2 CZ   sing Y N 300 
PHE CE2 HE2  sing N N 301 
PHE CZ  HZ   sing N N 302 
PHE OXT HXT  sing N N 303 
PRO N   CA   sing N N 304 
PRO N   CD   sing N N 305 
PRO N   H    sing N N 306 
PRO CA  C    sing N N 307 
PRO CA  CB   sing N N 308 
PRO CA  HA   sing N N 309 
PRO C   O    doub N N 310 
PRO C   OXT  sing N N 311 
PRO CB  CG   sing N N 312 
PRO CB  HB2  sing N N 313 
PRO CB  HB3  sing N N 314 
PRO CG  CD   sing N N 315 
PRO CG  HG2  sing N N 316 
PRO CG  HG3  sing N N 317 
PRO CD  HD2  sing N N 318 
PRO CD  HD3  sing N N 319 
PRO OXT HXT  sing N N 320 
SER N   CA   sing N N 321 
SER N   H    sing N N 322 
SER N   H2   sing N N 323 
SER CA  C    sing N N 324 
SER CA  CB   sing N N 325 
SER CA  HA   sing N N 326 
SER C   O    doub N N 327 
SER C   OXT  sing N N 328 
SER CB  OG   sing N N 329 
SER CB  HB2  sing N N 330 
SER CB  HB3  sing N N 331 
SER OG  HG   sing N N 332 
SER OXT HXT  sing N N 333 
THR N   CA   sing N N 334 
THR N   H    sing N N 335 
THR N   H2   sing N N 336 
THR CA  C    sing N N 337 
THR CA  CB   sing N N 338 
THR CA  HA   sing N N 339 
THR C   O    doub N N 340 
THR C   OXT  sing N N 341 
THR CB  OG1  sing N N 342 
THR CB  CG2  sing N N 343 
THR CB  HB   sing N N 344 
THR OG1 HG1  sing N N 345 
THR CG2 HG21 sing N N 346 
THR CG2 HG22 sing N N 347 
THR CG2 HG23 sing N N 348 
THR OXT HXT  sing N N 349 
TRP N   CA   sing N N 350 
TRP N   H    sing N N 351 
TRP N   H2   sing N N 352 
TRP CA  C    sing N N 353 
TRP CA  CB   sing N N 354 
TRP CA  HA   sing N N 355 
TRP C   O    doub N N 356 
TRP C   OXT  sing N N 357 
TRP CB  CG   sing N N 358 
TRP CB  HB2  sing N N 359 
TRP CB  HB3  sing N N 360 
TRP CG  CD1  doub Y N 361 
TRP CG  CD2  sing Y N 362 
TRP CD1 NE1  sing Y N 363 
TRP CD1 HD1  sing N N 364 
TRP CD2 CE2  doub Y N 365 
TRP CD2 CE3  sing Y N 366 
TRP NE1 CE2  sing Y N 367 
TRP NE1 HE1  sing N N 368 
TRP CE2 CZ2  sing Y N 369 
TRP CE3 CZ3  doub Y N 370 
TRP CE3 HE3  sing N N 371 
TRP CZ2 CH2  doub Y N 372 
TRP CZ2 HZ2  sing N N 373 
TRP CZ3 CH2  sing Y N 374 
TRP CZ3 HZ3  sing N N 375 
TRP CH2 HH2  sing N N 376 
TRP OXT HXT  sing N N 377 
TYR N   CA   sing N N 378 
TYR N   H    sing N N 379 
TYR N   H2   sing N N 380 
TYR CA  C    sing N N 381 
TYR CA  CB   sing N N 382 
TYR CA  HA   sing N N 383 
TYR C   O    doub N N 384 
TYR C   OXT  sing N N 385 
TYR CB  CG   sing N N 386 
TYR CB  HB2  sing N N 387 
TYR CB  HB3  sing N N 388 
TYR CG  CD1  doub Y N 389 
TYR CG  CD2  sing Y N 390 
TYR CD1 CE1  sing Y N 391 
TYR CD1 HD1  sing N N 392 
TYR CD2 CE2  doub Y N 393 
TYR CD2 HD2  sing N N 394 
TYR CE1 CZ   doub Y N 395 
TYR CE1 HE1  sing N N 396 
TYR CE2 CZ   sing Y N 397 
TYR CE2 HE2  sing N N 398 
TYR CZ  OH   sing N N 399 
TYR OH  HH   sing N N 400 
TYR OXT HXT  sing N N 401 
VAL N   CA   sing N N 402 
VAL N   H    sing N N 403 
VAL N   H2   sing N N 404 
VAL CA  C    sing N N 405 
VAL CA  CB   sing N N 406 
VAL CA  HA   sing N N 407 
VAL C   O    doub N N 408 
VAL C   OXT  sing N N 409 
VAL CB  CG1  sing N N 410 
VAL CB  CG2  sing N N 411 
VAL CB  HB   sing N N 412 
VAL CG1 HG11 sing N N 413 
VAL CG1 HG12 sing N N 414 
VAL CG1 HG13 sing N N 415 
VAL CG2 HG21 sing N N 416 
VAL CG2 HG22 sing N N 417 
VAL CG2 HG23 sing N N 418 
VAL OXT HXT  sing N N 419 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           GM088332 
_pdbx_audit_support.ordinal                1 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '2-{[(2E)-3-(naphthalen-2-yl)but-2-enoyl]amino}benzoic acid' 55C 
3 water                                                        HOH 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   3DU6 
_pdbx_initial_refinement_model.details          ? 
# 
