data_7XL0
# 
_entry.id   7XL0 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_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   7XL0         pdb_00007xl0 10.2210/pdb7xl0/pdb 
WWPDB D_1300029082 ?            ?                   
# 
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 2022-11-09 
2 'Structure model' 1 1 2023-11-29 
3 'Structure model' 1 2 2024-11-13 
# 
_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' 'Data collection'        
2 2 'Structure model' 'Refinement description' 
3 3 'Structure model' 'Structure summary'      
# 
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' chem_comp_atom                
2 2 'Structure model' chem_comp_bond                
3 2 'Structure model' pdbx_initial_refinement_model 
4 2 'Structure model' struct_ncs_dom_lim            
5 3 'Structure model' pdbx_entry_details            
6 3 'Structure model' pdbx_modification_feature     
# 
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' '_struct_ncs_dom_lim.beg_auth_comp_id'         
2 2 'Structure model' '_struct_ncs_dom_lim.beg_label_asym_id'        
3 2 'Structure model' '_struct_ncs_dom_lim.beg_label_comp_id'        
4 2 'Structure model' '_struct_ncs_dom_lim.beg_label_seq_id'         
5 2 'Structure model' '_struct_ncs_dom_lim.end_auth_comp_id'         
6 2 'Structure model' '_struct_ncs_dom_lim.end_label_asym_id'        
7 2 'Structure model' '_struct_ncs_dom_lim.end_label_comp_id'        
8 2 'Structure model' '_struct_ncs_dom_lim.end_label_seq_id'         
9 3 'Structure model' '_pdbx_entry_details.has_protein_modification' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        7XL0 
_pdbx_database_status.recvd_initial_deposition_date   2022-04-20 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              tsumoto@bioeng.t.u-tokyo.ac.jp 
_pdbx_contact_author.name_first         Kouhei 
_pdbx_contact_author.name_last          Tsumoto 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7643-5164 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Caaveiro, J.M.M.' 1 ? 
'Mori, C.'         2 ? 
'Kinoshita, S.'    3 ? 
'Nakakido, M.'     4 ? 
'Tsumoto, K.'      5 ? 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Protein Sci.' 
_citation.journal_id_ASTM           PRCIEI 
_citation.journal_id_CSD            0795 
_citation.journal_id_ISSN           1469-896X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            31 
_citation.language                  ? 
_citation.page_first                e4450 
_citation.page_last                 e4450 
_citation.title                     
;Molecular basis for thermal stability and affinity in a VHH: Contribution of the framework region and its influence in the conformation of the CDR3.
;
_citation.year                      2022 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/pro.4450 
_citation.pdbx_database_id_PubMed   36153698 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Kinoshita, S.'    1 0000-0001-7176-9421 
primary 'Nakakido, M.'     2 0000-0003-0328-9914 
primary 'Mori, C.'         3 ?                   
primary 'Kuroda, D.'       4 ?                   
primary 'Caaveiro, J.M.M.' 5 0000-0001-5568-2369 
primary 'Tsumoto, K.'      6 ?                   
# 
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 'Nanobody Vobarilizumab' 14080.711 2   ? ? ? ? 
2 non-polymer syn 'SULFATE ION'            96.063    2   ? ? ? ? 
3 non-polymer syn GLYCEROL                 92.094    1   ? ? ? ? 
4 water       nat water                    18.015    188 ? ? ? ? 
# 
_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       
;EVQLVESGGGLVQPGGSLRLSCAASGSVFKINVMAWYRQAPGKGRELVAGIISGGSTSYADSVKGRFTISRDNAKNTLYL
QMNSLRPEDTAVYYCAFITTESDYDLGRRYWGQGTLVTVSSAAAHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;EVQLVESGGGLVQPGGSLRLSCAASGSVFKINVMAWYRQAPGKGRELVAGIISGGSTSYADSVKGRFTISRDNAKNTLYL
QMNSLRPEDTAVYYCAFITTESDYDLGRRYWGQGTLVTVSSAAAHHHHHH
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SULFATE ION' SO4 
3 GLYCEROL      GOL 
4 water         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLU n 
1 2   VAL n 
1 3   GLN n 
1 4   LEU n 
1 5   VAL n 
1 6   GLU n 
1 7   SER n 
1 8   GLY n 
1 9   GLY n 
1 10  GLY n 
1 11  LEU n 
1 12  VAL n 
1 13  GLN n 
1 14  PRO n 
1 15  GLY n 
1 16  GLY n 
1 17  SER n 
1 18  LEU n 
1 19  ARG n 
1 20  LEU n 
1 21  SER n 
1 22  CYS n 
1 23  ALA n 
1 24  ALA n 
1 25  SER n 
1 26  GLY n 
1 27  SER n 
1 28  VAL n 
1 29  PHE n 
1 30  LYS n 
1 31  ILE n 
1 32  ASN n 
1 33  VAL n 
1 34  MET n 
1 35  ALA n 
1 36  TRP n 
1 37  TYR n 
1 38  ARG n 
1 39  GLN n 
1 40  ALA n 
1 41  PRO n 
1 42  GLY n 
1 43  LYS n 
1 44  GLY n 
1 45  ARG n 
1 46  GLU n 
1 47  LEU n 
1 48  VAL n 
1 49  ALA n 
1 50  GLY n 
1 51  ILE n 
1 52  ILE n 
1 53  SER n 
1 54  GLY n 
1 55  GLY n 
1 56  SER n 
1 57  THR n 
1 58  SER n 
1 59  TYR n 
1 60  ALA n 
1 61  ASP n 
1 62  SER n 
1 63  VAL n 
1 64  LYS n 
1 65  GLY n 
1 66  ARG n 
1 67  PHE n 
1 68  THR n 
1 69  ILE n 
1 70  SER n 
1 71  ARG n 
1 72  ASP n 
1 73  ASN n 
1 74  ALA n 
1 75  LYS n 
1 76  ASN n 
1 77  THR n 
1 78  LEU n 
1 79  TYR n 
1 80  LEU n 
1 81  GLN n 
1 82  MET n 
1 83  ASN n 
1 84  SER n 
1 85  LEU n 
1 86  ARG n 
1 87  PRO n 
1 88  GLU n 
1 89  ASP n 
1 90  THR n 
1 91  ALA n 
1 92  VAL n 
1 93  TYR n 
1 94  TYR n 
1 95  CYS n 
1 96  ALA n 
1 97  PHE n 
1 98  ILE n 
1 99  THR n 
1 100 THR n 
1 101 GLU n 
1 102 SER n 
1 103 ASP n 
1 104 TYR n 
1 105 ASP n 
1 106 LEU n 
1 107 GLY n 
1 108 ARG n 
1 109 ARG n 
1 110 TYR n 
1 111 TRP n 
1 112 GLY n 
1 113 GLN n 
1 114 GLY n 
1 115 THR n 
1 116 LEU n 
1 117 VAL n 
1 118 THR n 
1 119 VAL n 
1 120 SER n 
1 121 SER n 
1 122 ALA n 
1 123 ALA n 
1 124 ALA n 
1 125 HIS n 
1 126 HIS n 
1 127 HIS n 
1 128 HIS n 
1 129 HIS n 
1 130 HIS 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                   130 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_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      'Lama glama' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9844 
_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                   ? 
# 
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 
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  
GOL non-polymer         . GLYCEROL        'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
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 
SO4 non-polymer         . 'SULFATE ION'   ?                               'O4 S -2'        96.063  
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 
# 
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   GLU 1   1   1   GLU GLU A . n 
A 1 2   VAL 2   2   2   VAL VAL A . n 
A 1 3   GLN 3   3   3   GLN GLN A . n 
A 1 4   LEU 4   4   4   LEU LEU A . n 
A 1 5   VAL 5   5   5   VAL VAL A . n 
A 1 6   GLU 6   6   6   GLU GLU A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   GLY 9   9   9   GLY GLY A . n 
A 1 10  GLY 10  10  10  GLY GLY A . n 
A 1 11  LEU 11  11  11  LEU LEU A . n 
A 1 12  VAL 12  12  12  VAL VAL A . n 
A 1 13  GLN 13  13  13  GLN GLN A . n 
A 1 14  PRO 14  14  14  PRO PRO A . n 
A 1 15  GLY 15  15  15  GLY GLY A . n 
A 1 16  GLY 16  16  16  GLY GLY A . n 
A 1 17  SER 17  17  17  SER SER A . n 
A 1 18  LEU 18  18  18  LEU LEU A . n 
A 1 19  ARG 19  19  19  ARG ARG A . n 
A 1 20  LEU 20  20  20  LEU LEU A . n 
A 1 21  SER 21  21  21  SER SER A . n 
A 1 22  CYS 22  22  22  CYS CYS A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  ALA 24  24  24  ALA ALA A . n 
A 1 25  SER 25  25  25  SER SER A . n 
A 1 26  GLY 26  26  26  GLY GLY A . n 
A 1 27  SER 27  27  27  SER SER A . n 
A 1 28  VAL 28  28  28  VAL VAL A . n 
A 1 29  PHE 29  29  29  PHE PHE A . n 
A 1 30  LYS 30  30  30  LYS LYS A . n 
A 1 31  ILE 31  31  31  ILE ILE A . n 
A 1 32  ASN 32  32  32  ASN ASN A . n 
A 1 33  VAL 33  33  33  VAL VAL A . n 
A 1 34  MET 34  34  34  MET MET A . n 
A 1 35  ALA 35  35  35  ALA ALA A . n 
A 1 36  TRP 36  36  36  TRP TRP A . n 
A 1 37  TYR 37  37  37  TYR TYR A . n 
A 1 38  ARG 38  38  38  ARG ARG A . n 
A 1 39  GLN 39  39  39  GLN GLN A . n 
A 1 40  ALA 40  40  40  ALA ALA A . n 
A 1 41  PRO 41  41  41  PRO PRO A . n 
A 1 42  GLY 42  42  42  GLY GLY A . n 
A 1 43  LYS 43  43  43  LYS LYS A . n 
A 1 44  GLY 44  44  44  GLY GLY A . n 
A 1 45  ARG 45  45  45  ARG ARG A . n 
A 1 46  GLU 46  46  46  GLU GLU A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  VAL 48  48  48  VAL VAL A . n 
A 1 49  ALA 49  49  49  ALA ALA A . n 
A 1 50  GLY 50  50  50  GLY GLY A . n 
A 1 51  ILE 51  51  51  ILE ILE A . n 
A 1 52  ILE 52  52  52  ILE ILE A . n 
A 1 53  SER 53  53  53  SER SER A . n 
A 1 54  GLY 54  54  54  GLY GLY A . n 
A 1 55  GLY 55  55  55  GLY GLY A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  SER 58  58  58  SER SER A . n 
A 1 59  TYR 59  59  59  TYR TYR A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  ASP 61  61  61  ASP ASP A . n 
A 1 62  SER 62  62  62  SER SER A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  LYS 64  64  64  LYS LYS A . n 
A 1 65  GLY 65  65  65  GLY GLY A . n 
A 1 66  ARG 66  66  66  ARG ARG A . n 
A 1 67  PHE 67  67  67  PHE PHE A . n 
A 1 68  THR 68  68  68  THR THR A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  SER 70  70  70  SER SER A . n 
A 1 71  ARG 71  71  71  ARG ARG A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  ASN 73  73  73  ASN ASN A . n 
A 1 74  ALA 74  74  74  ALA ALA A . n 
A 1 75  LYS 75  75  75  LYS LYS A . n 
A 1 76  ASN 76  76  76  ASN ASN A . n 
A 1 77  THR 77  77  77  THR THR A . n 
A 1 78  LEU 78  78  78  LEU LEU A . n 
A 1 79  TYR 79  79  79  TYR TYR A . n 
A 1 80  LEU 80  80  80  LEU LEU A . n 
A 1 81  GLN 81  81  81  GLN GLN A . n 
A 1 82  MET 82  82  82  MET MET A . n 
A 1 83  ASN 83  83  83  ASN ASN A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  LEU 85  85  85  LEU LEU A . n 
A 1 86  ARG 86  86  86  ARG ARG A . n 
A 1 87  PRO 87  87  87  PRO PRO A . n 
A 1 88  GLU 88  88  88  GLU GLU A . n 
A 1 89  ASP 89  89  89  ASP ASP A . n 
A 1 90  THR 90  90  90  THR THR A . n 
A 1 91  ALA 91  91  91  ALA ALA A . n 
A 1 92  VAL 92  92  92  VAL VAL A . n 
A 1 93  TYR 93  93  93  TYR TYR A . n 
A 1 94  TYR 94  94  94  TYR TYR A . n 
A 1 95  CYS 95  95  95  CYS CYS A . n 
A 1 96  ALA 96  96  96  ALA ALA A . n 
A 1 97  PHE 97  97  97  PHE PHE A . n 
A 1 98  ILE 98  98  98  ILE ILE A . n 
A 1 99  THR 99  99  99  THR THR A . n 
A 1 100 THR 100 100 100 THR THR A . n 
A 1 101 GLU 101 101 101 GLU GLU A . n 
A 1 102 SER 102 102 102 SER SER A . n 
A 1 103 ASP 103 103 103 ASP ASP A . n 
A 1 104 TYR 104 104 104 TYR TYR A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 GLY 107 107 107 GLY GLY A . n 
A 1 108 ARG 108 108 108 ARG ARG A . n 
A 1 109 ARG 109 109 109 ARG ARG A . n 
A 1 110 TYR 110 110 110 TYR TYR A . n 
A 1 111 TRP 111 111 111 TRP TRP A . n 
A 1 112 GLY 112 112 112 GLY GLY A . n 
A 1 113 GLN 113 113 113 GLN GLN A . n 
A 1 114 GLY 114 114 114 GLY GLY A . n 
A 1 115 THR 115 115 115 THR THR A . n 
A 1 116 LEU 116 116 116 LEU LEU A . n 
A 1 117 VAL 117 117 117 VAL VAL A . n 
A 1 118 THR 118 118 118 THR THR A . n 
A 1 119 VAL 119 119 119 VAL VAL A . n 
A 1 120 SER 120 120 120 SER SER A . n 
A 1 121 SER 121 121 121 SER SER A . n 
A 1 122 ALA 122 122 ?   ?   ?   A . n 
A 1 123 ALA 123 123 ?   ?   ?   A . n 
A 1 124 ALA 124 124 ?   ?   ?   A . n 
A 1 125 HIS 125 125 ?   ?   ?   A . n 
A 1 126 HIS 126 126 ?   ?   ?   A . n 
A 1 127 HIS 127 127 ?   ?   ?   A . n 
A 1 128 HIS 128 128 ?   ?   ?   A . n 
A 1 129 HIS 129 129 ?   ?   ?   A . n 
A 1 130 HIS 130 130 ?   ?   ?   A . n 
B 1 1   GLU 1   1   ?   ?   ?   B . n 
B 1 2   VAL 2   2   ?   ?   ?   B . n 
B 1 3   GLN 3   3   3   GLN GLN B . n 
B 1 4   LEU 4   4   4   LEU LEU B . n 
B 1 5   VAL 5   5   5   VAL VAL B . n 
B 1 6   GLU 6   6   6   GLU GLU B . n 
B 1 7   SER 7   7   7   SER SER B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   GLY 9   9   9   GLY GLY B . n 
B 1 10  GLY 10  10  10  GLY GLY B . n 
B 1 11  LEU 11  11  11  LEU LEU B . n 
B 1 12  VAL 12  12  12  VAL VAL B . n 
B 1 13  GLN 13  13  13  GLN GLN B . n 
B 1 14  PRO 14  14  14  PRO PRO B . n 
B 1 15  GLY 15  15  15  GLY GLY B . n 
B 1 16  GLY 16  16  16  GLY GLY B . n 
B 1 17  SER 17  17  17  SER SER B . n 
B 1 18  LEU 18  18  18  LEU LEU B . n 
B 1 19  ARG 19  19  19  ARG ARG B . n 
B 1 20  LEU 20  20  20  LEU LEU B . n 
B 1 21  SER 21  21  21  SER SER B . n 
B 1 22  CYS 22  22  22  CYS CYS B . n 
B 1 23  ALA 23  23  23  ALA ALA B . n 
B 1 24  ALA 24  24  24  ALA ALA B . n 
B 1 25  SER 25  25  25  SER SER B . n 
B 1 26  GLY 26  26  26  GLY GLY B . n 
B 1 27  SER 27  27  27  SER SER B . n 
B 1 28  VAL 28  28  28  VAL VAL B . n 
B 1 29  PHE 29  29  29  PHE PHE B . n 
B 1 30  LYS 30  30  30  LYS LYS B . n 
B 1 31  ILE 31  31  31  ILE ILE B . n 
B 1 32  ASN 32  32  32  ASN ASN B . n 
B 1 33  VAL 33  33  33  VAL VAL B . n 
B 1 34  MET 34  34  34  MET MET B . n 
B 1 35  ALA 35  35  35  ALA ALA B . n 
B 1 36  TRP 36  36  36  TRP TRP B . n 
B 1 37  TYR 37  37  37  TYR TYR B . n 
B 1 38  ARG 38  38  38  ARG ARG B . n 
B 1 39  GLN 39  39  39  GLN GLN B . n 
B 1 40  ALA 40  40  40  ALA ALA B . n 
B 1 41  PRO 41  41  41  PRO PRO B . n 
B 1 42  GLY 42  42  42  GLY GLY B . n 
B 1 43  LYS 43  43  43  LYS LYS B . n 
B 1 44  GLY 44  44  44  GLY GLY B . n 
B 1 45  ARG 45  45  45  ARG ARG B . n 
B 1 46  GLU 46  46  46  GLU GLU B . n 
B 1 47  LEU 47  47  47  LEU LEU B . n 
B 1 48  VAL 48  48  48  VAL VAL B . n 
B 1 49  ALA 49  49  49  ALA ALA B . n 
B 1 50  GLY 50  50  50  GLY GLY B . n 
B 1 51  ILE 51  51  51  ILE ILE B . n 
B 1 52  ILE 52  52  52  ILE ILE B . n 
B 1 53  SER 53  53  53  SER SER B . n 
B 1 54  GLY 54  54  54  GLY GLY B . n 
B 1 55  GLY 55  55  55  GLY GLY B . n 
B 1 56  SER 56  56  56  SER SER B . n 
B 1 57  THR 57  57  57  THR THR B . n 
B 1 58  SER 58  58  58  SER SER B . n 
B 1 59  TYR 59  59  59  TYR TYR B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  ASP 61  61  61  ASP ASP B . n 
B 1 62  SER 62  62  62  SER SER B . n 
B 1 63  VAL 63  63  63  VAL VAL B . n 
B 1 64  LYS 64  64  64  LYS LYS B . n 
B 1 65  GLY 65  65  65  GLY GLY B . n 
B 1 66  ARG 66  66  66  ARG ARG B . n 
B 1 67  PHE 67  67  67  PHE PHE B . n 
B 1 68  THR 68  68  68  THR THR B . n 
B 1 69  ILE 69  69  69  ILE ILE B . n 
B 1 70  SER 70  70  70  SER SER B . n 
B 1 71  ARG 71  71  71  ARG ARG B . n 
B 1 72  ASP 72  72  72  ASP ASP B . n 
B 1 73  ASN 73  73  73  ASN ASN B . n 
B 1 74  ALA 74  74  74  ALA ALA B . n 
B 1 75  LYS 75  75  75  LYS LYS B . n 
B 1 76  ASN 76  76  76  ASN ASN B . n 
B 1 77  THR 77  77  77  THR THR B . n 
B 1 78  LEU 78  78  78  LEU LEU B . n 
B 1 79  TYR 79  79  79  TYR TYR B . n 
B 1 80  LEU 80  80  80  LEU LEU B . n 
B 1 81  GLN 81  81  81  GLN GLN B . n 
B 1 82  MET 82  82  82  MET MET B . n 
B 1 83  ASN 83  83  83  ASN ASN B . n 
B 1 84  SER 84  84  84  SER SER B . n 
B 1 85  LEU 85  85  85  LEU LEU B . n 
B 1 86  ARG 86  86  86  ARG ARG B . n 
B 1 87  PRO 87  87  87  PRO PRO B . n 
B 1 88  GLU 88  88  88  GLU GLU B . n 
B 1 89  ASP 89  89  89  ASP ASP B . n 
B 1 90  THR 90  90  90  THR THR B . n 
B 1 91  ALA 91  91  91  ALA ALA B . n 
B 1 92  VAL 92  92  92  VAL VAL B . n 
B 1 93  TYR 93  93  93  TYR TYR B . n 
B 1 94  TYR 94  94  94  TYR TYR B . n 
B 1 95  CYS 95  95  95  CYS CYS B . n 
B 1 96  ALA 96  96  96  ALA ALA B . n 
B 1 97  PHE 97  97  97  PHE PHE B . n 
B 1 98  ILE 98  98  98  ILE ILE B . n 
B 1 99  THR 99  99  99  THR THR B . n 
B 1 100 THR 100 100 100 THR THR B . n 
B 1 101 GLU 101 101 101 GLU GLU B . n 
B 1 102 SER 102 102 102 SER SER B . n 
B 1 103 ASP 103 103 103 ASP ASP B . n 
B 1 104 TYR 104 104 104 TYR TYR B . n 
B 1 105 ASP 105 105 105 ASP ASP B . n 
B 1 106 LEU 106 106 106 LEU LEU B . n 
B 1 107 GLY 107 107 107 GLY GLY B . n 
B 1 108 ARG 108 108 108 ARG ARG B . n 
B 1 109 ARG 109 109 109 ARG ARG B . n 
B 1 110 TYR 110 110 110 TYR TYR B . n 
B 1 111 TRP 111 111 111 TRP TRP B . n 
B 1 112 GLY 112 112 112 GLY GLY B . n 
B 1 113 GLN 113 113 113 GLN GLN B . n 
B 1 114 GLY 114 114 114 GLY GLY B . n 
B 1 115 THR 115 115 115 THR THR B . n 
B 1 116 LEU 116 116 116 LEU LEU B . n 
B 1 117 VAL 117 117 117 VAL VAL B . n 
B 1 118 THR 118 118 118 THR THR B . n 
B 1 119 VAL 119 119 119 VAL VAL B . n 
B 1 120 SER 120 120 120 SER SER B . n 
B 1 121 SER 121 121 121 SER SER B . n 
B 1 122 ALA 122 122 ?   ?   ?   B . n 
B 1 123 ALA 123 123 ?   ?   ?   B . n 
B 1 124 ALA 124 124 ?   ?   ?   B . n 
B 1 125 HIS 125 125 ?   ?   ?   B . n 
B 1 126 HIS 126 126 ?   ?   ?   B . n 
B 1 127 HIS 127 127 ?   ?   ?   B . n 
B 1 128 HIS 128 128 ?   ?   ?   B . n 
B 1 129 HIS 129 129 ?   ?   ?   B . n 
B 1 130 HIS 130 130 ?   ?   ?   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 SO4 1  201 1   SO4 SO4 A . 
D 2 SO4 1  202 2   SO4 SO4 A . 
E 3 GOL 1  203 11  GOL GOL A . 
F 4 HOH 1  301 176 HOH HOH A . 
F 4 HOH 2  302 152 HOH HOH A . 
F 4 HOH 3  303 160 HOH HOH A . 
F 4 HOH 4  304 157 HOH HOH A . 
F 4 HOH 5  305 22  HOH HOH A . 
F 4 HOH 6  306 139 HOH HOH A . 
F 4 HOH 7  307 101 HOH HOH A . 
F 4 HOH 8  308 60  HOH HOH A . 
F 4 HOH 9  309 70  HOH HOH A . 
F 4 HOH 10 310 183 HOH HOH A . 
F 4 HOH 11 311 26  HOH HOH A . 
F 4 HOH 12 312 7   HOH HOH A . 
F 4 HOH 13 313 68  HOH HOH A . 
F 4 HOH 14 314 14  HOH HOH A . 
F 4 HOH 15 315 130 HOH HOH A . 
F 4 HOH 16 316 116 HOH HOH A . 
F 4 HOH 17 317 76  HOH HOH A . 
F 4 HOH 18 318 91  HOH HOH A . 
F 4 HOH 19 319 94  HOH HOH A . 
F 4 HOH 20 320 184 HOH HOH A . 
F 4 HOH 21 321 167 HOH HOH A . 
F 4 HOH 22 322 129 HOH HOH A . 
F 4 HOH 23 323 33  HOH HOH A . 
F 4 HOH 24 324 48  HOH HOH A . 
F 4 HOH 25 325 62  HOH HOH A . 
F 4 HOH 26 326 117 HOH HOH A . 
F 4 HOH 27 327 166 HOH HOH A . 
F 4 HOH 28 328 4   HOH HOH A . 
F 4 HOH 29 329 181 HOH HOH A . 
F 4 HOH 30 330 25  HOH HOH A . 
F 4 HOH 31 331 137 HOH HOH A . 
F 4 HOH 32 332 104 HOH HOH A . 
F 4 HOH 33 333 81  HOH HOH A . 
F 4 HOH 34 334 165 HOH HOH A . 
F 4 HOH 35 335 138 HOH HOH A . 
F 4 HOH 36 336 1   HOH HOH A . 
F 4 HOH 37 337 46  HOH HOH A . 
F 4 HOH 38 338 56  HOH HOH A . 
F 4 HOH 39 339 50  HOH HOH A . 
F 4 HOH 40 340 180 HOH HOH A . 
F 4 HOH 41 341 86  HOH HOH A . 
F 4 HOH 42 342 115 HOH HOH A . 
F 4 HOH 43 343 97  HOH HOH A . 
F 4 HOH 44 344 42  HOH HOH A . 
F 4 HOH 45 345 105 HOH HOH A . 
F 4 HOH 46 346 61  HOH HOH A . 
F 4 HOH 47 347 12  HOH HOH A . 
F 4 HOH 48 348 90  HOH HOH A . 
F 4 HOH 49 349 6   HOH HOH A . 
F 4 HOH 50 350 20  HOH HOH A . 
F 4 HOH 51 351 106 HOH HOH A . 
F 4 HOH 52 352 132 HOH HOH A . 
F 4 HOH 53 353 95  HOH HOH A . 
F 4 HOH 54 354 11  HOH HOH A . 
F 4 HOH 55 355 162 HOH HOH A . 
F 4 HOH 56 356 31  HOH HOH A . 
F 4 HOH 57 357 54  HOH HOH A . 
F 4 HOH 58 358 49  HOH HOH A . 
F 4 HOH 59 359 135 HOH HOH A . 
F 4 HOH 60 360 44  HOH HOH A . 
F 4 HOH 61 361 122 HOH HOH A . 
F 4 HOH 62 362 178 HOH HOH A . 
F 4 HOH 63 363 153 HOH HOH A . 
F 4 HOH 64 364 92  HOH HOH A . 
F 4 HOH 65 365 43  HOH HOH A . 
F 4 HOH 66 366 52  HOH HOH A . 
F 4 HOH 67 367 158 HOH HOH A . 
F 4 HOH 68 368 15  HOH HOH A . 
F 4 HOH 69 369 175 HOH HOH A . 
F 4 HOH 70 370 87  HOH HOH A . 
F 4 HOH 71 371 51  HOH HOH A . 
F 4 HOH 72 372 55  HOH HOH A . 
F 4 HOH 73 373 99  HOH HOH A . 
F 4 HOH 74 374 177 HOH HOH A . 
F 4 HOH 75 375 41  HOH HOH A . 
F 4 HOH 76 376 164 HOH HOH A . 
F 4 HOH 77 377 2   HOH HOH A . 
F 4 HOH 78 378 133 HOH HOH A . 
F 4 HOH 79 379 16  HOH HOH A . 
F 4 HOH 80 380 123 HOH HOH A . 
F 4 HOH 81 381 131 HOH HOH A . 
F 4 HOH 82 382 10  HOH HOH A . 
F 4 HOH 83 383 38  HOH HOH A . 
F 4 HOH 84 384 190 HOH HOH A . 
F 4 HOH 85 385 179 HOH HOH A . 
F 4 HOH 86 386 58  HOH HOH A . 
F 4 HOH 87 387 163 HOH HOH A . 
F 4 HOH 88 388 75  HOH HOH A . 
F 4 HOH 89 389 89  HOH HOH A . 
F 4 HOH 90 390 141 HOH HOH A . 
F 4 HOH 91 391 161 HOH HOH A . 
G 4 HOH 1  201 85  HOH HOH B . 
G 4 HOH 2  202 186 HOH HOH B . 
G 4 HOH 3  203 67  HOH HOH B . 
G 4 HOH 4  204 93  HOH HOH B . 
G 4 HOH 5  205 169 HOH HOH B . 
G 4 HOH 6  206 172 HOH HOH B . 
G 4 HOH 7  207 65  HOH HOH B . 
G 4 HOH 8  208 125 HOH HOH B . 
G 4 HOH 9  209 188 HOH HOH B . 
G 4 HOH 10 210 100 HOH HOH B . 
G 4 HOH 11 211 83  HOH HOH B . 
G 4 HOH 12 212 47  HOH HOH B . 
G 4 HOH 13 213 148 HOH HOH B . 
G 4 HOH 14 214 155 HOH HOH B . 
G 4 HOH 15 215 79  HOH HOH B . 
G 4 HOH 16 216 28  HOH HOH B . 
G 4 HOH 17 217 37  HOH HOH B . 
G 4 HOH 18 218 19  HOH HOH B . 
G 4 HOH 19 219 21  HOH HOH B . 
G 4 HOH 20 220 18  HOH HOH B . 
G 4 HOH 21 221 57  HOH HOH B . 
G 4 HOH 22 222 63  HOH HOH B . 
G 4 HOH 23 223 73  HOH HOH B . 
G 4 HOH 24 224 151 HOH HOH B . 
G 4 HOH 25 225 17  HOH HOH B . 
G 4 HOH 26 226 149 HOH HOH B . 
G 4 HOH 27 227 171 HOH HOH B . 
G 4 HOH 28 228 78  HOH HOH B . 
G 4 HOH 29 229 107 HOH HOH B . 
G 4 HOH 30 230 23  HOH HOH B . 
G 4 HOH 31 231 45  HOH HOH B . 
G 4 HOH 32 232 77  HOH HOH B . 
G 4 HOH 33 233 53  HOH HOH B . 
G 4 HOH 34 234 39  HOH HOH B . 
G 4 HOH 35 235 159 HOH HOH B . 
G 4 HOH 36 236 102 HOH HOH B . 
G 4 HOH 37 237 69  HOH HOH B . 
G 4 HOH 38 238 142 HOH HOH B . 
G 4 HOH 39 239 120 HOH HOH B . 
G 4 HOH 40 240 64  HOH HOH B . 
G 4 HOH 41 241 168 HOH HOH B . 
G 4 HOH 42 242 9   HOH HOH B . 
G 4 HOH 43 243 32  HOH HOH B . 
G 4 HOH 44 244 72  HOH HOH B . 
G 4 HOH 45 245 103 HOH HOH B . 
G 4 HOH 46 246 82  HOH HOH B . 
G 4 HOH 47 247 8   HOH HOH B . 
G 4 HOH 48 248 27  HOH HOH B . 
G 4 HOH 49 249 35  HOH HOH B . 
G 4 HOH 50 250 74  HOH HOH B . 
G 4 HOH 51 251 59  HOH HOH B . 
G 4 HOH 52 252 29  HOH HOH B . 
G 4 HOH 53 253 144 HOH HOH B . 
G 4 HOH 54 254 30  HOH HOH B . 
G 4 HOH 55 255 5   HOH HOH B . 
G 4 HOH 56 256 189 HOH HOH B . 
G 4 HOH 57 257 150 HOH HOH B . 
G 4 HOH 58 258 66  HOH HOH B . 
G 4 HOH 59 259 193 HOH HOH B . 
G 4 HOH 60 260 146 HOH HOH B . 
G 4 HOH 61 261 192 HOH HOH B . 
G 4 HOH 62 262 36  HOH HOH B . 
G 4 HOH 63 263 3   HOH HOH B . 
G 4 HOH 64 264 136 HOH HOH B . 
G 4 HOH 65 265 143 HOH HOH B . 
G 4 HOH 66 266 170 HOH HOH B . 
G 4 HOH 67 267 113 HOH HOH B . 
G 4 HOH 68 268 134 HOH HOH B . 
G 4 HOH 69 269 112 HOH HOH B . 
G 4 HOH 70 270 173 HOH HOH B . 
G 4 HOH 71 271 191 HOH HOH B . 
G 4 HOH 72 272 185 HOH HOH B . 
G 4 HOH 73 273 84  HOH HOH B . 
G 4 HOH 74 274 124 HOH HOH B . 
G 4 HOH 75 275 145 HOH HOH B . 
G 4 HOH 76 276 182 HOH HOH B . 
G 4 HOH 77 277 194 HOH HOH B . 
G 4 HOH 78 278 174 HOH HOH B . 
G 4 HOH 79 279 88  HOH HOH B . 
G 4 HOH 80 280 13  HOH HOH B . 
G 4 HOH 81 281 127 HOH HOH B . 
G 4 HOH 82 282 98  HOH HOH B . 
G 4 HOH 83 283 110 HOH HOH B . 
G 4 HOH 84 284 154 HOH HOH B . 
G 4 HOH 85 285 126 HOH HOH B . 
G 4 HOH 86 286 147 HOH HOH B . 
G 4 HOH 87 287 118 HOH HOH B . 
G 4 HOH 88 288 111 HOH HOH B . 
G 4 HOH 89 289 187 HOH HOH B . 
G 4 HOH 90 290 195 HOH HOH B . 
G 4 HOH 91 291 71  HOH HOH B . 
G 4 HOH 92 292 121 HOH HOH B . 
G 4 HOH 93 293 119 HOH HOH B . 
G 4 HOH 94 294 24  HOH HOH B . 
G 4 HOH 95 295 109 HOH HOH B . 
G 4 HOH 96 296 40  HOH HOH B . 
G 4 HOH 97 297 156 HOH HOH B . 
# 
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      ? ? ? 5.8.0238 1 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.27     2 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? MOSFLM      ? ? ? 7.2.2    3 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALA       ? ? ? 3.3.22   4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER      ? ? ? 2.8.2    5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   101.920 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     7XL0 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     124.591 
_cell.length_a_esd                 ? 
_cell.length_b                     56.420 
_cell.length_b_esd                 ? 
_cell.length_c                     42.240 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
# 
_symmetry.entry_id                         7XL0 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_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                   7XL0 
_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            2.58 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         52.31 
_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            293 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;0.2 M lithium sulfate
20% PEG 3,350
;
_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.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER R 4M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2019-03-16 
_diffrn_detector.pdbx_frequency               ? 
# 
_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   1.000 
_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                        'PHOTON FACTORY BEAMLINE BL-1A' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL-1A 
_diffrn_source.pdbx_synchrotron_site       'Photon Factory' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       7XL0 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.70 
_reflns.d_resolution_low                               52 
_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                                     31315 
_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                           98.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.0 
_reflns.pdbx_Rmerge_I_obs                              0.092 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.5 
_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                                0.04 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.995 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.70 
_reflns_shell.d_res_low                                     1.79 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           4.4 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4232 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.336 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               0.160 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.890 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            0.0200 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.2900 
_refine.aniso_B[2][2]                            0.0100 
_refine.aniso_B[2][3]                            0.0000 
_refine.aniso_B[3][3]                            -0.1400 
_refine.B_iso_max                                91.970 
_refine.B_iso_mean                               25.8950 
_refine.B_iso_min                                12.200 
_refine.correlation_coeff_Fo_to_Fc               0.9670 
_refine.correlation_coeff_Fo_to_Fc_free          0.9500 
_refine.details                                  
'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES      : REFINED INDIVIDUALLY' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 7XL0 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.7000 
_refine.ls_d_res_low                             51.2500 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     30038 
_refine.ls_number_reflns_R_free                  1275 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.8900 
_refine.ls_percent_reflns_R_free                 4.1000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1539 
_refine.ls_R_factor_R_free                       0.1963 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1521 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      5HVG 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.1120 
_refine.pdbx_overall_ESU_R_Free                  0.0890 
_refine.pdbx_solvent_vdw_probe_radii             1.2000 
_refine.pdbx_solvent_ion_probe_radii             0.8000 
_refine.pdbx_solvent_shrinkage_radii             0.8000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             3.8760 
_refine.overall_SU_ML                            0.0570 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         final 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.7000 
_refine_hist.d_res_low                        51.2500 
_refine_hist.number_atoms_solvent             188 
_refine_hist.number_atoms_total               2018 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       240 
_refine_hist.pdbx_B_iso_mean_ligand           33.71 
_refine_hist.pdbx_B_iso_mean_solvent          34.58 
_refine_hist.pdbx_number_atoms_protein        1814 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         16 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.006  0.013  1918 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.018  1759 ? r_bond_other_d         ? ? 
'X-RAY DIFFRACTION' ? 1.353  1.639  2611 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 1.295  1.574  4077 ? r_angle_other_deg      ? ? 
'X-RAY DIFFRACTION' ? 7.363  5.000  258  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 32.849 20.833 96   ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 12.259 15.000 316  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 13.479 15.000 16   ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.058  0.200  248  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.006  0.020  2192 ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  432  ? r_gen_planes_other     ? ? 
'X-RAY DIFFRACTION' ? 1.113  3.000  3677 ? r_rigid_bond_restr     ? ? 
# 
loop_
_refine_ls_restr_ncs.pdbx_refine_id 
_refine_ls_restr_ncs.dom_id 
_refine_ls_restr_ncs.ncs_model_details 
_refine_ls_restr_ncs.rms_dev_B_iso 
_refine_ls_restr_ncs.rms_dev_position 
_refine_ls_restr_ncs.weight_B_iso 
_refine_ls_restr_ncs.weight_position 
_refine_ls_restr_ncs.pdbx_ordinal 
_refine_ls_restr_ncs.pdbx_type 
_refine_ls_restr_ncs.pdbx_asym_id 
_refine_ls_restr_ncs.pdbx_auth_asym_id 
_refine_ls_restr_ncs.pdbx_number 
_refine_ls_restr_ncs.pdbx_rms 
_refine_ls_restr_ncs.pdbx_weight 
_refine_ls_restr_ncs.pdbx_ens_id 
'X-RAY DIFFRACTION' 1 ? ? 0.160 ? 0.050 1 'interatomic distance' ? A 3227 ? ? 1 
'X-RAY DIFFRACTION' 2 ? ? 0.160 ? 0.050 2 'interatomic distance' ? B 3227 ? ? 1 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.7000 
_refine_ls_shell.d_res_low                        1.7440 
_refine_ls_shell.number_reflns_all                1973 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             76 
_refine_ls_shell.number_reflns_R_work             1897 
_refine_ls_shell.percent_reflns_obs               85.6700 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free                  0.2450 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.R_factor_R_work                  0.2100 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
# 
loop_
_struct_ncs_dom.pdbx_ens_id 
_struct_ncs_dom.id 
_struct_ncs_dom.details 
1 1 A 
1 2 B 
# 
loop_
_struct_ncs_dom_lim.pdbx_ens_id 
_struct_ncs_dom_lim.dom_id 
_struct_ncs_dom_lim.pdbx_component_id 
_struct_ncs_dom_lim.beg_label_asym_id 
_struct_ncs_dom_lim.beg_label_comp_id 
_struct_ncs_dom_lim.beg_label_seq_id 
_struct_ncs_dom_lim.beg_label_alt_id 
_struct_ncs_dom_lim.end_label_asym_id 
_struct_ncs_dom_lim.end_label_comp_id 
_struct_ncs_dom_lim.end_label_seq_id 
_struct_ncs_dom_lim.end_label_alt_id 
_struct_ncs_dom_lim.beg_auth_asym_id 
_struct_ncs_dom_lim.beg_auth_comp_id 
_struct_ncs_dom_lim.beg_auth_seq_id 
_struct_ncs_dom_lim.end_auth_asym_id 
_struct_ncs_dom_lim.end_auth_comp_id 
_struct_ncs_dom_lim.end_auth_seq_id 
_struct_ncs_dom_lim.pdbx_refine_code 
_struct_ncs_dom_lim.selection_details 
1 1 0 A GLN 3 . A SER 120 . A GLN 3 A SER 120 0 ? 
1 2 0 B GLN 3 . B SER 120 . B GLN 3 B SER 120 0 ? 
# 
_struct_ncs_ens.id        1 
_struct_ncs_ens.details   ? 
# 
_struct.entry_id                     7XL0 
_struct.title                        'Crystal structure of Vobarilizumab at 1.70 Angstrom' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        7XL0 
_struct_keywords.text            
'nanobody VHH protein engineering protein stability surface plasmon resonance differential scanning calorimetry, IMMUNE SYSTEM' 
_struct_keywords.pdbx_keywords   'IMMUNE SYSTEM' 
# 
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 4 ? 
G N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    PDB 
_struct_ref.db_code                    7XL0 
_struct_ref.pdbx_db_accession          7XL0 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_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 7XL0 A 1 ? 130 ? 7XL0 1 ? 130 ? 1 130 
2 1 7XL0 B 1 ? 130 ? 7XL0 1 ? 130 ? 1 130 
# 
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_and_software_defined_assembly PISA monomeric 1 
2 author_and_software_defined_assembly PISA monomeric 1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 170  ? 
1 MORE         -12  ? 
1 'SSA (A^2)'  6640 ? 
2 'ABSA (A^2)' 160  ? 
2 MORE         -11  ? 
2 'SSA (A^2)'  6650 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F 
2 1 B,G       
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_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_
_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 ASP A 61 ? LYS A 64 ? ASP A 61 LYS A 64 5 ? 4 
HELX_P HELX_P2 AA2 ASN A 73 ? LYS A 75 ? ASN A 73 LYS A 75 5 ? 3 
HELX_P HELX_P3 AA3 ARG A 86 ? THR A 90 ? ARG A 86 THR A 90 5 ? 5 
HELX_P HELX_P4 AA4 ASN B 73 ? LYS B 75 ? ASN B 73 LYS B 75 5 ? 3 
HELX_P HELX_P5 AA5 ARG B 86 ? THR B 90 ? ARG B 86 THR B 90 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ? ? A CYS 22 SG ? ? ? 1_555 A CYS 95 SG ? ? A CYS 22 A CYS 95 1_555 ? ? ? ? ? ? ? 2.089 ? ? 
disulf2 disulf ? ? B CYS 22 SG ? ? ? 1_555 B CYS 95 SG ? ? B CYS 22 B CYS 95 1_555 ? ? ? ? ? ? ? 2.094 ? ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 22 ? CYS A 95 ? CYS A 22 ? 1_555 CYS A 95 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS B 22 ? CYS B 95 ? CYS B 22 ? 1_555 CYS B 95 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 6 ? 
AA3 ? 4 ? 
AA4 ? 4 ? 
AA5 ? 6 ? 
AA6 ? 4 ? 
# 
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 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? anti-parallel 
AA6 3 4 ? 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 VAL A 2   ? SER A 7   ? VAL A 2   SER A 7   
AA1 2 LEU A 18  ? GLY A 26  ? LEU A 18  GLY A 26  
AA1 3 THR A 77  ? MET A 82  ? THR A 77  MET A 82  
AA1 4 PHE A 67  ? ASP A 72  ? PHE A 67  ASP A 72  
AA2 1 GLY A 10  ? VAL A 12  ? GLY A 10  VAL A 12  
AA2 2 THR A 115 ? VAL A 119 ? THR A 115 VAL A 119 
AA2 3 ALA A 91  ? THR A 100 ? ALA A 91  THR A 100 
AA2 4 LYS A 30  ? GLN A 39  ? LYS A 30  GLN A 39  
AA2 5 ARG A 45  ? ILE A 52  ? ARG A 45  ILE A 52  
AA2 6 THR A 57  ? TYR A 59  ? THR A 57  TYR A 59  
AA3 1 GLY A 10  ? VAL A 12  ? GLY A 10  VAL A 12  
AA3 2 THR A 115 ? VAL A 119 ? THR A 115 VAL A 119 
AA3 3 ALA A 91  ? THR A 100 ? ALA A 91  THR A 100 
AA3 4 ARG A 108 ? TRP A 111 ? ARG A 108 TRP A 111 
AA4 1 LEU B 4   ? SER B 7   ? LEU B 4   SER B 7   
AA4 2 LEU B 18  ? ALA B 24  ? LEU B 18  ALA B 24  
AA4 3 THR B 77  ? MET B 82  ? THR B 77  MET B 82  
AA4 4 PHE B 67  ? ASP B 72  ? PHE B 67  ASP B 72  
AA5 1 GLY B 10  ? VAL B 12  ? GLY B 10  VAL B 12  
AA5 2 THR B 115 ? VAL B 119 ? THR B 115 VAL B 119 
AA5 3 ALA B 91  ? THR B 100 ? ALA B 91  THR B 100 
AA5 4 LYS B 30  ? GLN B 39  ? LYS B 30  GLN B 39  
AA5 5 GLU B 46  ? ILE B 52  ? GLU B 46  ILE B 52  
AA5 6 THR B 57  ? TYR B 59  ? THR B 57  TYR B 59  
AA6 1 GLY B 10  ? VAL B 12  ? GLY B 10  VAL B 12  
AA6 2 THR B 115 ? VAL B 119 ? THR B 115 VAL B 119 
AA6 3 ALA B 91  ? THR B 100 ? ALA B 91  THR B 100 
AA6 4 ARG B 108 ? TRP B 111 ? ARG B 108 TRP B 111 
# 
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 VAL A 5   ? N VAL A 5   O ALA A 23  ? O ALA A 23  
AA1 2 3 N LEU A 18  ? N LEU A 18  O MET A 82  ? O MET A 82  
AA1 3 4 O GLN A 81  ? O GLN A 81  N THR A 68  ? N THR A 68  
AA2 1 2 N VAL A 12  ? N VAL A 12  O THR A 118 ? O THR A 118 
AA2 2 3 O THR A 115 ? O THR A 115 N TYR A 93  ? N TYR A 93  
AA2 3 4 O TYR A 94  ? O TYR A 94  N TYR A 37  ? N TYR A 37  
AA2 4 5 N TRP A 36  ? N TRP A 36  O ALA A 49  ? O ALA A 49  
AA2 5 6 N GLY A 50  ? N GLY A 50  O SER A 58  ? O SER A 58  
AA3 1 2 N VAL A 12  ? N VAL A 12  O THR A 118 ? O THR A 118 
AA3 2 3 O THR A 115 ? O THR A 115 N TYR A 93  ? N TYR A 93  
AA3 3 4 N PHE A 97  ? N PHE A 97  O TYR A 110 ? O TYR A 110 
AA4 1 2 N VAL B 5   ? N VAL B 5   O ALA B 23  ? O ALA B 23  
AA4 2 3 N LEU B 18  ? N LEU B 18  O MET B 82  ? O MET B 82  
AA4 3 4 O TYR B 79  ? O TYR B 79  N SER B 70  ? N SER B 70  
AA5 1 2 N GLY B 10  ? N GLY B 10  O THR B 118 ? O THR B 118 
AA5 2 3 O THR B 115 ? O THR B 115 N TYR B 93  ? N TYR B 93  
AA5 3 4 O TYR B 94  ? O TYR B 94  N TYR B 37  ? N TYR B 37  
AA5 4 5 N TRP B 36  ? N TRP B 36  O ALA B 49  ? O ALA B 49  
AA5 5 6 N GLY B 50  ? N GLY B 50  O SER B 58  ? O SER B 58  
AA6 1 2 N GLY B 10  ? N GLY B 10  O THR B 118 ? O THR B 118 
AA6 2 3 O THR B 115 ? O THR B 115 N TYR B 93  ? N TYR B 93  
AA6 3 4 N PHE B 97  ? N PHE B 97  O TYR B 110 ? O TYR B 110 
# 
_pdbx_entry_details.entry_id                   7XL0 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
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 PHE A 29 ? ? -96.60 -122.65 
2 1 SER B 27 ? ? -53.50 79.99   
3 1 PHE B 29 ? ? -95.10 -159.30 
4 1 SER B 56 ? ? -54.42 101.02  
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A ALA 122 ? A ALA 122 
2  1 Y 1 A ALA 123 ? A ALA 123 
3  1 Y 1 A ALA 124 ? A ALA 124 
4  1 Y 1 A HIS 125 ? A HIS 125 
5  1 Y 1 A HIS 126 ? A HIS 126 
6  1 Y 1 A HIS 127 ? A HIS 127 
7  1 Y 1 A HIS 128 ? A HIS 128 
8  1 Y 1 A HIS 129 ? A HIS 129 
9  1 Y 1 A HIS 130 ? A HIS 130 
10 1 Y 1 B GLU 1   ? B GLU 1   
11 1 Y 1 B VAL 2   ? B VAL 2   
12 1 Y 1 B ALA 122 ? B ALA 122 
13 1 Y 1 B ALA 123 ? B ALA 123 
14 1 Y 1 B ALA 124 ? B ALA 124 
15 1 Y 1 B HIS 125 ? B HIS 125 
16 1 Y 1 B HIS 126 ? B HIS 126 
17 1 Y 1 B HIS 127 ? B HIS 127 
18 1 Y 1 B HIS 128 ? B HIS 128 
19 1 Y 1 B HIS 129 ? B HIS 129 
20 1 Y 1 B HIS 130 ? B HIS 130 
# 
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 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
GOL C1   C N N 137 
GOL O1   O N N 138 
GOL C2   C N N 139 
GOL O2   O N N 140 
GOL C3   C N N 141 
GOL O3   O N N 142 
GOL H11  H N N 143 
GOL H12  H N N 144 
GOL HO1  H N N 145 
GOL H2   H N N 146 
GOL HO2  H N N 147 
GOL H31  H N N 148 
GOL H32  H N N 149 
GOL HO3  H N N 150 
HIS N    N N N 151 
HIS CA   C N S 152 
HIS C    C N N 153 
HIS O    O N N 154 
HIS CB   C N N 155 
HIS CG   C Y N 156 
HIS ND1  N Y N 157 
HIS CD2  C Y N 158 
HIS CE1  C Y N 159 
HIS NE2  N Y N 160 
HIS OXT  O N N 161 
HIS H    H N N 162 
HIS H2   H N N 163 
HIS HA   H N N 164 
HIS HB2  H N N 165 
HIS HB3  H N N 166 
HIS HD1  H N N 167 
HIS HD2  H N N 168 
HIS HE1  H N N 169 
HIS HE2  H N N 170 
HIS HXT  H N N 171 
HOH O    O N N 172 
HOH H1   H N N 173 
HOH H2   H N N 174 
ILE N    N N N 175 
ILE CA   C N S 176 
ILE C    C N N 177 
ILE O    O N N 178 
ILE CB   C N S 179 
ILE CG1  C N N 180 
ILE CG2  C N N 181 
ILE CD1  C N N 182 
ILE OXT  O N N 183 
ILE H    H N N 184 
ILE H2   H N N 185 
ILE HA   H N N 186 
ILE HB   H N N 187 
ILE HG12 H N N 188 
ILE HG13 H N N 189 
ILE HG21 H N N 190 
ILE HG22 H N N 191 
ILE HG23 H N N 192 
ILE HD11 H N N 193 
ILE HD12 H N N 194 
ILE HD13 H N N 195 
ILE HXT  H N N 196 
LEU N    N N N 197 
LEU CA   C N S 198 
LEU C    C N N 199 
LEU O    O N N 200 
LEU CB   C N N 201 
LEU CG   C N N 202 
LEU CD1  C N N 203 
LEU CD2  C N N 204 
LEU OXT  O N N 205 
LEU H    H N N 206 
LEU H2   H N N 207 
LEU HA   H N N 208 
LEU HB2  H N N 209 
LEU HB3  H N N 210 
LEU HG   H N N 211 
LEU HD11 H N N 212 
LEU HD12 H N N 213 
LEU HD13 H N N 214 
LEU HD21 H N N 215 
LEU HD22 H N N 216 
LEU HD23 H N N 217 
LEU HXT  H N N 218 
LYS N    N N N 219 
LYS CA   C N S 220 
LYS C    C N N 221 
LYS O    O N N 222 
LYS CB   C N N 223 
LYS CG   C N N 224 
LYS CD   C N N 225 
LYS CE   C N N 226 
LYS NZ   N N N 227 
LYS OXT  O N N 228 
LYS H    H N N 229 
LYS H2   H N N 230 
LYS HA   H N N 231 
LYS HB2  H N N 232 
LYS HB3  H N N 233 
LYS HG2  H N N 234 
LYS HG3  H N N 235 
LYS HD2  H N N 236 
LYS HD3  H N N 237 
LYS HE2  H N N 238 
LYS HE3  H N N 239 
LYS HZ1  H N N 240 
LYS HZ2  H N N 241 
LYS HZ3  H N N 242 
LYS HXT  H N N 243 
MET N    N N N 244 
MET CA   C N S 245 
MET C    C N N 246 
MET O    O N N 247 
MET CB   C N N 248 
MET CG   C N N 249 
MET SD   S N N 250 
MET CE   C N N 251 
MET OXT  O N N 252 
MET H    H N N 253 
MET H2   H N N 254 
MET HA   H N N 255 
MET HB2  H N N 256 
MET HB3  H N N 257 
MET HG2  H N N 258 
MET HG3  H N N 259 
MET HE1  H N N 260 
MET HE2  H N N 261 
MET HE3  H N N 262 
MET HXT  H N N 263 
PHE N    N N N 264 
PHE CA   C N S 265 
PHE C    C N N 266 
PHE O    O N N 267 
PHE CB   C N N 268 
PHE CG   C Y N 269 
PHE CD1  C Y N 270 
PHE CD2  C Y N 271 
PHE CE1  C Y N 272 
PHE CE2  C Y N 273 
PHE CZ   C Y N 274 
PHE OXT  O N N 275 
PHE H    H N N 276 
PHE H2   H N N 277 
PHE HA   H N N 278 
PHE HB2  H N N 279 
PHE HB3  H N N 280 
PHE HD1  H N N 281 
PHE HD2  H N N 282 
PHE HE1  H N N 283 
PHE HE2  H N N 284 
PHE HZ   H N N 285 
PHE HXT  H N N 286 
PRO N    N N N 287 
PRO CA   C N S 288 
PRO C    C N N 289 
PRO O    O N N 290 
PRO CB   C N N 291 
PRO CG   C N N 292 
PRO CD   C N N 293 
PRO OXT  O N N 294 
PRO H    H N N 295 
PRO HA   H N N 296 
PRO HB2  H N N 297 
PRO HB3  H N N 298 
PRO HG2  H N N 299 
PRO HG3  H N N 300 
PRO HD2  H N N 301 
PRO HD3  H N N 302 
PRO HXT  H N N 303 
SER N    N N N 304 
SER CA   C N S 305 
SER C    C N N 306 
SER O    O N N 307 
SER CB   C N N 308 
SER OG   O N N 309 
SER OXT  O N N 310 
SER H    H N N 311 
SER H2   H N N 312 
SER HA   H N N 313 
SER HB2  H N N 314 
SER HB3  H N N 315 
SER HG   H N N 316 
SER HXT  H N N 317 
SO4 S    S N N 318 
SO4 O1   O N N 319 
SO4 O2   O N N 320 
SO4 O3   O N N 321 
SO4 O4   O N N 322 
THR N    N N N 323 
THR CA   C N S 324 
THR C    C N N 325 
THR O    O N N 326 
THR CB   C N R 327 
THR OG1  O N N 328 
THR CG2  C N N 329 
THR OXT  O N N 330 
THR H    H N N 331 
THR H2   H N N 332 
THR HA   H N N 333 
THR HB   H N N 334 
THR HG1  H N N 335 
THR HG21 H N N 336 
THR HG22 H N N 337 
THR HG23 H N N 338 
THR HXT  H N N 339 
TRP N    N N N 340 
TRP CA   C N S 341 
TRP C    C N N 342 
TRP O    O N N 343 
TRP CB   C N N 344 
TRP CG   C Y N 345 
TRP CD1  C Y N 346 
TRP CD2  C Y N 347 
TRP NE1  N Y N 348 
TRP CE2  C Y N 349 
TRP CE3  C Y N 350 
TRP CZ2  C Y N 351 
TRP CZ3  C Y N 352 
TRP CH2  C Y N 353 
TRP OXT  O N N 354 
TRP H    H N N 355 
TRP H2   H N N 356 
TRP HA   H N N 357 
TRP HB2  H N N 358 
TRP HB3  H N N 359 
TRP HD1  H N N 360 
TRP HE1  H N N 361 
TRP HE3  H N N 362 
TRP HZ2  H N N 363 
TRP HZ3  H N N 364 
TRP HH2  H N N 365 
TRP HXT  H N N 366 
TYR N    N N N 367 
TYR CA   C N S 368 
TYR C    C N N 369 
TYR O    O N N 370 
TYR CB   C N N 371 
TYR CG   C Y N 372 
TYR CD1  C Y N 373 
TYR CD2  C Y N 374 
TYR CE1  C Y N 375 
TYR CE2  C Y N 376 
TYR CZ   C Y N 377 
TYR OH   O N N 378 
TYR OXT  O N N 379 
TYR H    H N N 380 
TYR H2   H N N 381 
TYR HA   H N N 382 
TYR HB2  H N N 383 
TYR HB3  H N N 384 
TYR HD1  H N N 385 
TYR HD2  H N N 386 
TYR HE1  H N N 387 
TYR HE2  H N N 388 
TYR HH   H N N 389 
TYR HXT  H N N 390 
VAL N    N N N 391 
VAL CA   C N S 392 
VAL C    C N N 393 
VAL O    O N N 394 
VAL CB   C N N 395 
VAL CG1  C N N 396 
VAL CG2  C N N 397 
VAL OXT  O N N 398 
VAL H    H N N 399 
VAL H2   H N N 400 
VAL HA   H N N 401 
VAL HB   H N N 402 
VAL HG11 H N N 403 
VAL HG12 H N N 404 
VAL HG13 H N N 405 
VAL HG21 H N N 406 
VAL HG22 H N N 407 
VAL HG23 H N N 408 
VAL HXT  H N N 409 
# 
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 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
GOL C1  O1   sing N N 129 
GOL C1  C2   sing N N 130 
GOL C1  H11  sing N N 131 
GOL C1  H12  sing N N 132 
GOL O1  HO1  sing N N 133 
GOL C2  O2   sing N N 134 
GOL C2  C3   sing N N 135 
GOL C2  H2   sing N N 136 
GOL O2  HO2  sing N N 137 
GOL C3  O3   sing N N 138 
GOL C3  H31  sing N N 139 
GOL C3  H32  sing N N 140 
GOL O3  HO3  sing N N 141 
HIS N   CA   sing N N 142 
HIS N   H    sing N N 143 
HIS N   H2   sing N N 144 
HIS CA  C    sing N N 145 
HIS CA  CB   sing N N 146 
HIS CA  HA   sing N N 147 
HIS C   O    doub N N 148 
HIS C   OXT  sing N N 149 
HIS CB  CG   sing N N 150 
HIS CB  HB2  sing N N 151 
HIS CB  HB3  sing N N 152 
HIS CG  ND1  sing Y N 153 
HIS CG  CD2  doub Y N 154 
HIS ND1 CE1  doub Y N 155 
HIS ND1 HD1  sing N N 156 
HIS CD2 NE2  sing Y N 157 
HIS CD2 HD2  sing N N 158 
HIS CE1 NE2  sing Y N 159 
HIS CE1 HE1  sing N N 160 
HIS NE2 HE2  sing N N 161 
HIS OXT HXT  sing N N 162 
HOH O   H1   sing N N 163 
HOH O   H2   sing N N 164 
ILE N   CA   sing N N 165 
ILE N   H    sing N N 166 
ILE N   H2   sing N N 167 
ILE CA  C    sing N N 168 
ILE CA  CB   sing N N 169 
ILE CA  HA   sing N N 170 
ILE C   O    doub N N 171 
ILE C   OXT  sing N N 172 
ILE CB  CG1  sing N N 173 
ILE CB  CG2  sing N N 174 
ILE CB  HB   sing N N 175 
ILE CG1 CD1  sing N N 176 
ILE CG1 HG12 sing N N 177 
ILE CG1 HG13 sing N N 178 
ILE CG2 HG21 sing N N 179 
ILE CG2 HG22 sing N N 180 
ILE CG2 HG23 sing N N 181 
ILE CD1 HD11 sing N N 182 
ILE CD1 HD12 sing N N 183 
ILE CD1 HD13 sing N N 184 
ILE OXT HXT  sing N N 185 
LEU N   CA   sing N N 186 
LEU N   H    sing N N 187 
LEU N   H2   sing N N 188 
LEU CA  C    sing N N 189 
LEU CA  CB   sing N N 190 
LEU CA  HA   sing N N 191 
LEU C   O    doub N N 192 
LEU C   OXT  sing N N 193 
LEU CB  CG   sing N N 194 
LEU CB  HB2  sing N N 195 
LEU CB  HB3  sing N N 196 
LEU CG  CD1  sing N N 197 
LEU CG  CD2  sing N N 198 
LEU CG  HG   sing N N 199 
LEU CD1 HD11 sing N N 200 
LEU CD1 HD12 sing N N 201 
LEU CD1 HD13 sing N N 202 
LEU CD2 HD21 sing N N 203 
LEU CD2 HD22 sing N N 204 
LEU CD2 HD23 sing N N 205 
LEU OXT HXT  sing N N 206 
LYS N   CA   sing N N 207 
LYS N   H    sing N N 208 
LYS N   H2   sing N N 209 
LYS CA  C    sing N N 210 
LYS CA  CB   sing N N 211 
LYS CA  HA   sing N N 212 
LYS C   O    doub N N 213 
LYS C   OXT  sing N N 214 
LYS CB  CG   sing N N 215 
LYS CB  HB2  sing N N 216 
LYS CB  HB3  sing N N 217 
LYS CG  CD   sing N N 218 
LYS CG  HG2  sing N N 219 
LYS CG  HG3  sing N N 220 
LYS CD  CE   sing N N 221 
LYS CD  HD2  sing N N 222 
LYS CD  HD3  sing N N 223 
LYS CE  NZ   sing N N 224 
LYS CE  HE2  sing N N 225 
LYS CE  HE3  sing N N 226 
LYS NZ  HZ1  sing N N 227 
LYS NZ  HZ2  sing N N 228 
LYS NZ  HZ3  sing N N 229 
LYS OXT HXT  sing N N 230 
MET N   CA   sing N N 231 
MET N   H    sing N N 232 
MET N   H2   sing N N 233 
MET CA  C    sing N N 234 
MET CA  CB   sing N N 235 
MET CA  HA   sing N N 236 
MET C   O    doub N N 237 
MET C   OXT  sing N N 238 
MET CB  CG   sing N N 239 
MET CB  HB2  sing N N 240 
MET CB  HB3  sing N N 241 
MET CG  SD   sing N N 242 
MET CG  HG2  sing N N 243 
MET CG  HG3  sing N N 244 
MET SD  CE   sing N N 245 
MET CE  HE1  sing N N 246 
MET CE  HE2  sing N N 247 
MET CE  HE3  sing N N 248 
MET OXT HXT  sing N N 249 
PHE N   CA   sing N N 250 
PHE N   H    sing N N 251 
PHE N   H2   sing N N 252 
PHE CA  C    sing N N 253 
PHE CA  CB   sing N N 254 
PHE CA  HA   sing N N 255 
PHE C   O    doub N N 256 
PHE C   OXT  sing N N 257 
PHE CB  CG   sing N N 258 
PHE CB  HB2  sing N N 259 
PHE CB  HB3  sing N N 260 
PHE CG  CD1  doub Y N 261 
PHE CG  CD2  sing Y N 262 
PHE CD1 CE1  sing Y N 263 
PHE CD1 HD1  sing N N 264 
PHE CD2 CE2  doub Y N 265 
PHE CD2 HD2  sing N N 266 
PHE CE1 CZ   doub Y N 267 
PHE CE1 HE1  sing N N 268 
PHE CE2 CZ   sing Y N 269 
PHE CE2 HE2  sing N N 270 
PHE CZ  HZ   sing N N 271 
PHE OXT HXT  sing N N 272 
PRO N   CA   sing N N 273 
PRO N   CD   sing N N 274 
PRO N   H    sing N N 275 
PRO CA  C    sing N N 276 
PRO CA  CB   sing N N 277 
PRO CA  HA   sing N N 278 
PRO C   O    doub N N 279 
PRO C   OXT  sing N N 280 
PRO CB  CG   sing N N 281 
PRO CB  HB2  sing N N 282 
PRO CB  HB3  sing N N 283 
PRO CG  CD   sing N N 284 
PRO CG  HG2  sing N N 285 
PRO CG  HG3  sing N N 286 
PRO CD  HD2  sing N N 287 
PRO CD  HD3  sing N N 288 
PRO OXT HXT  sing N N 289 
SER N   CA   sing N N 290 
SER N   H    sing N N 291 
SER N   H2   sing N N 292 
SER CA  C    sing N N 293 
SER CA  CB   sing N N 294 
SER CA  HA   sing N N 295 
SER C   O    doub N N 296 
SER C   OXT  sing N N 297 
SER CB  OG   sing N N 298 
SER CB  HB2  sing N N 299 
SER CB  HB3  sing N N 300 
SER OG  HG   sing N N 301 
SER OXT HXT  sing N N 302 
SO4 S   O1   doub N N 303 
SO4 S   O2   doub N N 304 
SO4 S   O3   sing N N 305 
SO4 S   O4   sing N N 306 
THR N   CA   sing N N 307 
THR N   H    sing N N 308 
THR N   H2   sing N N 309 
THR CA  C    sing N N 310 
THR CA  CB   sing N N 311 
THR CA  HA   sing N N 312 
THR C   O    doub N N 313 
THR C   OXT  sing N N 314 
THR CB  OG1  sing N N 315 
THR CB  CG2  sing N N 316 
THR CB  HB   sing N N 317 
THR OG1 HG1  sing N N 318 
THR CG2 HG21 sing N N 319 
THR CG2 HG22 sing N N 320 
THR CG2 HG23 sing N N 321 
THR OXT HXT  sing N N 322 
TRP N   CA   sing N N 323 
TRP N   H    sing N N 324 
TRP N   H2   sing N N 325 
TRP CA  C    sing N N 326 
TRP CA  CB   sing N N 327 
TRP CA  HA   sing N N 328 
TRP C   O    doub N N 329 
TRP C   OXT  sing N N 330 
TRP CB  CG   sing N N 331 
TRP CB  HB2  sing N N 332 
TRP CB  HB3  sing N N 333 
TRP CG  CD1  doub Y N 334 
TRP CG  CD2  sing Y N 335 
TRP CD1 NE1  sing Y N 336 
TRP CD1 HD1  sing N N 337 
TRP CD2 CE2  doub Y N 338 
TRP CD2 CE3  sing Y N 339 
TRP NE1 CE2  sing Y N 340 
TRP NE1 HE1  sing N N 341 
TRP CE2 CZ2  sing Y N 342 
TRP CE3 CZ3  doub Y N 343 
TRP CE3 HE3  sing N N 344 
TRP CZ2 CH2  doub Y N 345 
TRP CZ2 HZ2  sing N N 346 
TRP CZ3 CH2  sing Y N 347 
TRP CZ3 HZ3  sing N N 348 
TRP CH2 HH2  sing N N 349 
TRP OXT HXT  sing N N 350 
TYR N   CA   sing N N 351 
TYR N   H    sing N N 352 
TYR N   H2   sing N N 353 
TYR CA  C    sing N N 354 
TYR CA  CB   sing N N 355 
TYR CA  HA   sing N N 356 
TYR C   O    doub N N 357 
TYR C   OXT  sing N N 358 
TYR CB  CG   sing N N 359 
TYR CB  HB2  sing N N 360 
TYR CB  HB3  sing N N 361 
TYR CG  CD1  doub Y N 362 
TYR CG  CD2  sing Y N 363 
TYR CD1 CE1  sing Y N 364 
TYR CD1 HD1  sing N N 365 
TYR CD2 CE2  doub Y N 366 
TYR CD2 HD2  sing N N 367 
TYR CE1 CZ   doub Y N 368 
TYR CE1 HE1  sing N N 369 
TYR CE2 CZ   sing Y N 370 
TYR CE2 HE2  sing N N 371 
TYR CZ  OH   sing N N 372 
TYR OH  HH   sing N N 373 
TYR OXT HXT  sing N N 374 
VAL N   CA   sing N N 375 
VAL N   H    sing N N 376 
VAL N   H2   sing N N 377 
VAL CA  C    sing N N 378 
VAL CA  CB   sing N N 379 
VAL CA  HA   sing N N 380 
VAL C   O    doub N N 381 
VAL C   OXT  sing N N 382 
VAL CB  CG1  sing N N 383 
VAL CB  CG2  sing N N 384 
VAL CB  HB   sing N N 385 
VAL CG1 HG11 sing N N 386 
VAL CG1 HG12 sing N N 387 
VAL CG1 HG13 sing N N 388 
VAL CG2 HG21 sing N N 389 
VAL CG2 HG22 sing N N 390 
VAL CG2 HG23 sing N N 391 
VAL OXT HXT  sing N N 392 
# 
_pdbx_audit_support.funding_organization   'Japan Society for the Promotion of Science (JSPS)' 
_pdbx_audit_support.country                Japan 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_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   5HVG 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    7XL0 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.fract_transf_matrix[1][1]   0.008026 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001694 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017724 
_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]   0.024196 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
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   . GLU A 1 1   ? 17.266 -18.781 20.355  1.00 49.69 ? 1   GLU A N   1 
ATOM   2    C CA  . GLU A 1 1   ? 17.654 -18.660 18.920  1.00 46.03 ? 1   GLU A CA  1 
ATOM   3    C C   . GLU A 1 1   ? 16.452 -19.033 18.042  1.00 39.95 ? 1   GLU A C   1 
ATOM   4    O O   . GLU A 1 1   ? 15.576 -19.810 18.490  1.00 36.49 ? 1   GLU A O   1 
ATOM   5    C CB  . GLU A 1 1   ? 18.892 -19.516 18.626  1.00 54.41 ? 1   GLU A CB  1 
ATOM   6    C CG  . GLU A 1 1   ? 19.243 -19.647 17.149  1.00 55.27 ? 1   GLU A CG  1 
ATOM   7    C CD  . GLU A 1 1   ? 19.857 -20.984 16.768  1.00 62.32 ? 1   GLU A CD  1 
ATOM   8    O OE1 . GLU A 1 1   ? 20.939 -21.310 17.299  1.00 67.41 ? 1   GLU A OE1 1 
ATOM   9    O OE2 . GLU A 1 1   ? 19.243 -21.704 15.950  1.00 62.80 ? 1   GLU A OE2 1 
ATOM   10   N N   . VAL A 1 2   ? 16.423 -18.470 16.835  1.00 31.03 ? 2   VAL A N   1 
ATOM   11   C CA  . VAL A 1 2   ? 15.333 -18.609 15.834  1.00 24.73 ? 2   VAL A CA  1 
ATOM   12   C C   . VAL A 1 2   ? 15.947 -19.162 14.544  1.00 22.08 ? 2   VAL A C   1 
ATOM   13   O O   . VAL A 1 2   ? 17.086 -18.774 14.228  1.00 23.40 ? 2   VAL A O   1 
ATOM   14   C CB  . VAL A 1 2   ? 14.667 -17.241 15.617  1.00 25.58 ? 2   VAL A CB  1 
ATOM   15   C CG1 . VAL A 1 2   ? 13.702 -17.253 14.444  1.00 25.43 ? 2   VAL A CG1 1 
ATOM   16   C CG2 . VAL A 1 2   ? 13.986 -16.753 16.889  1.00 28.34 ? 2   VAL A CG2 1 
ATOM   17   N N   . GLN A 1 3   ? 15.229 -20.058 13.864  1.00 19.74 ? 3   GLN A N   1 
ATOM   18   C CA  A GLN A 1 3   ? 15.633 -20.634 12.549  0.50 19.52 ? 3   GLN A CA  1 
ATOM   19   C CA  B GLN A 1 3   ? 15.630 -20.637 12.556  0.50 20.33 ? 3   GLN A CA  1 
ATOM   20   C C   . GLN A 1 3   ? 14.591 -20.209 11.511  1.00 18.94 ? 3   GLN A C   1 
ATOM   21   O O   . GLN A 1 3   ? 13.381 -20.252 11.824  1.00 18.83 ? 3   GLN A O   1 
ATOM   22   C CB  A GLN A 1 3   ? 15.759 -22.162 12.620  0.50 22.77 ? 3   GLN A CB  1 
ATOM   23   C CB  B GLN A 1 3   ? 15.757 -22.158 12.688  0.50 23.35 ? 3   GLN A CB  1 
ATOM   24   C CG  A GLN A 1 3   ? 16.354 -22.796 11.365  0.50 24.91 ? 3   GLN A CG  1 
ATOM   25   C CG  B GLN A 1 3   ? 16.622 -22.608 13.866  0.50 27.70 ? 3   GLN A CG  1 
ATOM   26   C CD  A GLN A 1 3   ? 15.990 -24.253 11.210  0.50 27.13 ? 3   GLN A CD  1 
ATOM   27   C CD  B GLN A 1 3   ? 15.861 -22.758 15.166  0.50 30.87 ? 3   GLN A CD  1 
ATOM   28   O OE1 A GLN A 1 3   ? 16.317 -24.890 10.212  0.50 26.87 ? 3   GLN A OE1 1 
ATOM   29   O OE1 B GLN A 1 3   ? 16.306 -22.320 16.228  0.50 34.55 ? 3   GLN A OE1 1 
ATOM   30   N NE2 A GLN A 1 3   ? 15.291 -24.791 12.198  0.50 29.45 ? 3   GLN A NE2 1 
ATOM   31   N NE2 B GLN A 1 3   ? 14.699 -23.390 15.101  0.50 34.07 ? 3   GLN A NE2 1 
ATOM   32   N N   . LEU A 1 4   ? 15.049 -19.772 10.344  1.00 16.99 ? 4   LEU A N   1 
ATOM   33   C CA  . LEU A 1 4   ? 14.157 -19.372 9.235   1.00 16.07 ? 4   LEU A CA  1 
ATOM   34   C C   . LEU A 1 4   ? 14.356 -20.372 8.103   1.00 18.79 ? 4   LEU A C   1 
ATOM   35   O O   . LEU A 1 4   ? 15.509 -20.616 7.718   1.00 20.94 ? 4   LEU A O   1 
ATOM   36   C CB  . LEU A 1 4   ? 14.490 -17.946 8.783   1.00 17.03 ? 4   LEU A CB  1 
ATOM   37   C CG  . LEU A 1 4   ? 14.282 -16.854 9.831   1.00 18.29 ? 4   LEU A CG  1 
ATOM   38   C CD1 . LEU A 1 4   ? 14.576 -15.494 9.239   1.00 17.55 ? 4   LEU A CD1 1 
ATOM   39   C CD2 . LEU A 1 4   ? 12.875 -16.880 10.418  1.00 19.78 ? 4   LEU A CD2 1 
ATOM   40   N N   . VAL A 1 5   ? 13.262 -20.942 7.610   1.00 19.06 ? 5   VAL A N   1 
ATOM   41   C CA  . VAL A 1 5   ? 13.283 -21.930 6.500   1.00 20.40 ? 5   VAL A CA  1 
ATOM   42   C C   . VAL A 1 5   ? 12.556 -21.318 5.301   1.00 18.00 ? 5   VAL A C   1 
ATOM   43   O O   . VAL A 1 5   ? 11.361 -21.021 5.424   1.00 18.61 ? 5   VAL A O   1 
ATOM   44   C CB  . VAL A 1 5   ? 12.643 -23.252 6.954   1.00 24.23 ? 5   VAL A CB  1 
ATOM   45   C CG1 . VAL A 1 5   ? 12.532 -24.247 5.807   1.00 26.67 ? 5   VAL A CG1 1 
ATOM   46   C CG2 . VAL A 1 5   ? 13.393 -23.849 8.133   1.00 27.31 ? 5   VAL A CG2 1 
ATOM   47   N N   . GLU A 1 6   ? 13.272 -21.148 4.192   1.00 18.59 ? 6   GLU A N   1 
ATOM   48   C CA  . GLU A 1 6   ? 12.725 -20.571 2.941   1.00 19.02 ? 6   GLU A CA  1 
ATOM   49   C C   . GLU A 1 6   ? 12.306 -21.707 2.015   1.00 20.38 ? 6   GLU A C   1 
ATOM   50   O O   . GLU A 1 6   ? 12.969 -22.757 2.018   1.00 24.39 ? 6   GLU A O   1 
ATOM   51   C CB  . GLU A 1 6   ? 13.754 -19.735 2.186   1.00 19.22 ? 6   GLU A CB  1 
ATOM   52   C CG  . GLU A 1 6   ? 14.139 -18.485 2.907   1.00 20.11 ? 6   GLU A CG  1 
ATOM   53   C CD  . GLU A 1 6   ? 15.087 -17.604 2.119   1.00 20.74 ? 6   GLU A CD  1 
ATOM   54   O OE1 . GLU A 1 6   ? 14.762 -17.282 0.946   1.00 20.66 ? 6   GLU A OE1 1 
ATOM   55   O OE2 . GLU A 1 6   ? 16.113 -17.228 2.690   1.00 18.74 ? 6   GLU A OE2 1 
ATOM   56   N N   . SER A 1 7   ? 11.275 -21.465 1.219   1.00 20.55 ? 7   SER A N   1 
ATOM   57   C CA  . SER A 1 7   ? 10.834 -22.377 0.139   1.00 23.93 ? 7   SER A CA  1 
ATOM   58   C C   . SER A 1 7   ? 10.217 -21.558 -0.995  1.00 23.39 ? 7   SER A C   1 
ATOM   59   O O   . SER A 1 7   ? 9.868  -20.400 -0.753  1.00 22.20 ? 7   SER A O   1 
ATOM   60   C CB  . SER A 1 7   ? 9.886  -23.420 0.665   1.00 26.90 ? 7   SER A CB  1 
ATOM   61   O OG  . SER A 1 7   ? 8.800  -22.823 1.346   1.00 29.19 ? 7   SER A OG  1 
ATOM   62   N N   . GLY A 1 8   ? 10.116 -22.160 -2.179  1.00 24.53 ? 8   GLY A N   1 
ATOM   63   C CA  . GLY A 1 8   ? 9.311  -21.632 -3.298  1.00 26.74 ? 8   GLY A CA  1 
ATOM   64   C C   . GLY A 1 8   ? 10.138 -21.085 -4.449  1.00 28.27 ? 8   GLY A C   1 
ATOM   65   O O   . GLY A 1 8   ? 9.515  -20.542 -5.394  1.00 35.54 ? 8   GLY A O   1 
ATOM   66   N N   . GLY A 1 9   ? 11.466 -21.215 -4.408  1.00 27.94 ? 9   GLY A N   1 
ATOM   67   C CA  . GLY A 1 9   ? 12.367 -20.697 -5.459  1.00 28.60 ? 9   GLY A CA  1 
ATOM   68   C C   . GLY A 1 9   ? 12.359 -21.540 -6.724  1.00 28.15 ? 9   GLY A C   1 
ATOM   69   O O   . GLY A 1 9   ? 11.564 -22.483 -6.813  1.00 33.57 ? 9   GLY A O   1 
ATOM   70   N N   . GLY A 1 10  ? 13.215 -21.191 -7.688  1.00 26.22 ? 10  GLY A N   1 
ATOM   71   C CA  . GLY A 1 10  ? 13.486 -21.992 -8.895  1.00 26.15 ? 10  GLY A CA  1 
ATOM   72   C C   . GLY A 1 10  ? 13.441 -21.170 -10.171 1.00 26.91 ? 10  GLY A C   1 
ATOM   73   O O   . GLY A 1 10  ? 13.624 -19.936 -10.119 1.00 24.69 ? 10  GLY A O   1 
ATOM   74   N N   . LEU A 1 11  ? 13.205 -21.855 -11.289 1.00 27.30 ? 11  LEU A N   1 
ATOM   75   C CA  . LEU A 1 11  ? 13.295 -21.311 -12.664 1.00 26.25 ? 11  LEU A CA  1 
ATOM   76   C C   . LEU A 1 11  ? 11.892 -20.908 -13.119 1.00 25.95 ? 11  LEU A C   1 
ATOM   77   O O   . LEU A 1 11  ? 10.966 -21.721 -12.956 1.00 28.82 ? 11  LEU A O   1 
ATOM   78   C CB  . LEU A 1 11  ? 13.886 -22.407 -13.554 1.00 31.97 ? 11  LEU A CB  1 
ATOM   79   C CG  . LEU A 1 11  ? 14.036 -22.069 -15.032 1.00 34.79 ? 11  LEU A CG  1 
ATOM   80   C CD1 . LEU A 1 11  ? 14.953 -20.875 -15.239 1.00 37.72 ? 11  LEU A CD1 1 
ATOM   81   C CD2 . LEU A 1 11  ? 14.581 -23.271 -15.786 1.00 38.74 ? 11  LEU A CD2 1 
ATOM   82   N N   . VAL A 1 12  ? 11.735 -19.694 -13.639 1.00 23.96 ? 12  VAL A N   1 
ATOM   83   C CA  . VAL A 1 12  ? 10.428 -19.180 -14.142 1.00 27.84 ? 12  VAL A CA  1 
ATOM   84   C C   . VAL A 1 12  ? 10.679 -18.424 -15.451 1.00 25.23 ? 12  VAL A C   1 
ATOM   85   O O   . VAL A 1 12  ? 11.783 -17.872 -15.625 1.00 23.47 ? 12  VAL A O   1 
ATOM   86   C CB  . VAL A 1 12  ? 9.734  -18.323 -13.062 1.00 32.27 ? 12  VAL A CB  1 
ATOM   87   C CG1 . VAL A 1 12  ? 10.613 -17.185 -12.591 1.00 33.62 ? 12  VAL A CG1 1 
ATOM   88   C CG2 . VAL A 1 12  ? 8.384  -17.772 -13.497 1.00 33.51 ? 12  VAL A CG2 1 
ATOM   89   N N   . GLN A 1 13  ? 9.696  -18.441 -16.351 1.00 28.99 ? 13  GLN A N   1 
ATOM   90   C CA  . GLN A 1 13  ? 9.747  -17.720 -17.644 1.00 31.89 ? 13  GLN A CA  1 
ATOM   91   C C   . GLN A 1 13  ? 9.544  -16.235 -17.369 1.00 26.03 ? 13  GLN A C   1 
ATOM   92   O O   . GLN A 1 13  ? 8.828  -15.869 -16.438 1.00 24.26 ? 13  GLN A O   1 
ATOM   93   C CB  . GLN A 1 13  ? 8.673  -18.255 -18.595 1.00 37.18 ? 13  GLN A CB  1 
ATOM   94   C CG  . GLN A 1 13  ? 8.826  -19.734 -18.915 1.00 43.69 ? 13  GLN A CG  1 
ATOM   95   C CD  . GLN A 1 13  ? 10.203 -20.031 -19.453 1.00 50.61 ? 13  GLN A CD  1 
ATOM   96   O OE1 . GLN A 1 13  ? 10.554 -19.635 -20.562 1.00 62.25 ? 13  GLN A OE1 1 
ATOM   97   N NE2 . GLN A 1 13  ? 11.010 -20.705 -18.651 1.00 56.09 ? 13  GLN A NE2 1 
ATOM   98   N N   . PRO A 1 14  ? 10.173 -15.329 -18.151 1.00 24.62 ? 14  PRO A N   1 
ATOM   99   C CA  . PRO A 1 14  ? 9.839  -13.908 -18.079 1.00 24.86 ? 14  PRO A CA  1 
ATOM   100  C C   . PRO A 1 14  ? 8.322  -13.713 -18.197 1.00 26.14 ? 14  PRO A C   1 
ATOM   101  O O   . PRO A 1 14  ? 7.703  -14.401 -19.001 1.00 24.44 ? 14  PRO A O   1 
ATOM   102  C CB  . PRO A 1 14  ? 10.612 -13.321 -19.260 1.00 29.36 ? 14  PRO A CB  1 
ATOM   103  C CG  . PRO A 1 14  ? 11.816 -14.225 -19.352 1.00 29.50 ? 14  PRO A CG  1 
ATOM   104  C CD  . PRO A 1 14  ? 11.247 -15.610 -19.116 1.00 27.16 ? 14  PRO A CD  1 
ATOM   105  N N   . GLY A 1 15  ? 7.770  -12.814 -17.379 1.00 25.66 ? 15  GLY A N   1 
ATOM   106  C CA  . GLY A 1 15  ? 6.322  -12.548 -17.265 1.00 26.67 ? 15  GLY A CA  1 
ATOM   107  C C   . GLY A 1 15  ? 5.652  -13.446 -16.241 1.00 26.01 ? 15  GLY A C   1 
ATOM   108  O O   . GLY A 1 15  ? 4.468  -13.221 -15.960 1.00 27.71 ? 15  GLY A O   1 
ATOM   109  N N   . GLY A 1 16  ? 6.380  -14.426 -15.700 1.00 22.65 ? 16  GLY A N   1 
ATOM   110  C CA  . GLY A 1 16  ? 5.832  -15.475 -14.826 1.00 24.30 ? 16  GLY A CA  1 
ATOM   111  C C   . GLY A 1 16  ? 5.663  -15.004 -13.392 1.00 20.08 ? 16  GLY A C   1 
ATOM   112  O O   . GLY A 1 16  ? 5.962  -13.824 -13.086 1.00 19.61 ? 16  GLY A O   1 
ATOM   113  N N   . SER A 1 17  ? 5.192  -15.912 -12.546 1.00 19.90 ? 17  SER A N   1 
ATOM   114  C CA  . SER A 1 17  ? 4.875  -15.683 -11.111 1.00 20.78 ? 17  SER A CA  1 
ATOM   115  C C   . SER A 1 17  ? 5.572  -16.736 -10.249 1.00 20.85 ? 17  SER A C   1 
ATOM   116  O O   . SER A 1 17  ? 5.711  -17.897 -10.709 1.00 23.53 ? 17  SER A O   1 
ATOM   117  C CB  . SER A 1 17  ? 3.382  -15.714 -10.877 1.00 20.90 ? 17  SER A CB  1 
ATOM   118  O OG  . SER A 1 17  ? 2.729  -14.654 -11.562 1.00 21.31 ? 17  SER A OG  1 
ATOM   119  N N   . LEU A 1 18  ? 5.955  -16.348 -9.030  1.00 20.59 ? 18  LEU A N   1 
ATOM   120  C CA  A LEU A 1 18  ? 6.510  -17.253 -7.985  0.50 20.26 ? 18  LEU A CA  1 
ATOM   121  C CA  B LEU A 1 18  ? 6.494  -17.262 -7.987  0.50 20.03 ? 18  LEU A CA  1 
ATOM   122  C C   . LEU A 1 18  ? 6.048  -16.750 -6.616  1.00 18.22 ? 18  LEU A C   1 
ATOM   123  O O   . LEU A 1 18  ? 5.910  -15.531 -6.482  1.00 19.24 ? 18  LEU A O   1 
ATOM   124  C CB  A LEU A 1 18  ? 8.041  -17.259 -8.058  0.50 22.94 ? 18  LEU A CB  1 
ATOM   125  C CB  B LEU A 1 18  ? 8.021  -17.289 -8.074  0.50 21.99 ? 18  LEU A CB  1 
ATOM   126  C CG  A LEU A 1 18  ? 8.649  -18.240 -9.057  0.50 24.59 ? 18  LEU A CG  1 
ATOM   127  C CG  B LEU A 1 18  ? 8.695  -18.604 -7.699  0.50 24.33 ? 18  LEU A CG  1 
ATOM   128  C CD1 A LEU A 1 18  ? 10.170 -18.145 -9.070  0.50 23.71 ? 18  LEU A CD1 1 
ATOM   129  C CD1 B LEU A 1 18  ? 8.425  -19.671 -8.750  0.50 27.71 ? 18  LEU A CD1 1 
ATOM   130  C CD2 A LEU A 1 18  ? 8.206  -19.656 -8.730  0.50 29.06 ? 18  LEU A CD2 1 
ATOM   131  C CD2 B LEU A 1 18  ? 10.194 -18.396 -7.534  0.50 24.33 ? 18  LEU A CD2 1 
ATOM   132  N N   . ARG A 1 19  ? 5.825  -17.656 -5.671  1.00 19.22 ? 19  ARG A N   1 
ATOM   133  C CA  . ARG A 1 19  ? 5.594  -17.271 -4.253  1.00 19.12 ? 19  ARG A CA  1 
ATOM   134  C C   . ARG A 1 19  ? 6.706  -17.861 -3.380  1.00 19.52 ? 19  ARG A C   1 
ATOM   135  O O   . ARG A 1 19  ? 6.881  -19.098 -3.381  1.00 22.13 ? 19  ARG A O   1 
ATOM   136  C CB  . ARG A 1 19  ? 4.227  -17.688 -3.701  1.00 23.00 ? 19  ARG A CB  1 
ATOM   137  C CG  . ARG A 1 19  ? 3.966  -17.072 -2.328  1.00 28.34 ? 19  ARG A CG  1 
ATOM   138  C CD  . ARG A 1 19  ? 2.794  -17.606 -1.529  1.00 36.39 ? 19  ARG A CD  1 
ATOM   139  N NE  . ARG A 1 19  ? 3.004  -18.972 -1.059  1.00 42.65 ? 19  ARG A NE  1 
ATOM   140  C CZ  . ARG A 1 19  ? 2.330  -19.550 -0.063  1.00 45.95 ? 19  ARG A CZ  1 
ATOM   141  N NH1 . ARG A 1 19  ? 1.382  -18.895 0.587   1.00 46.36 ? 19  ARG A NH1 1 
ATOM   142  N NH2 . ARG A 1 19  ? 2.598  -20.801 0.273   1.00 52.16 ? 19  ARG A NH2 1 
ATOM   143  N N   . LEU A 1 20  ? 7.448  -17.001 -2.678  1.00 17.53 ? 20  LEU A N   1 
ATOM   144  C CA  . LEU A 1 20  ? 8.426  -17.449 -1.660  1.00 16.89 ? 20  LEU A CA  1 
ATOM   145  C C   . LEU A 1 20  ? 7.739  -17.466 -0.293  1.00 15.54 ? 20  LEU A C   1 
ATOM   146  O O   . LEU A 1 20  ? 6.862  -16.623 -0.033  1.00 17.17 ? 20  LEU A O   1 
ATOM   147  C CB  . LEU A 1 20  ? 9.649  -16.534 -1.627  1.00 17.13 ? 20  LEU A CB  1 
ATOM   148  C CG  . LEU A 1 20  ? 10.390 -16.379 -2.951  1.00 18.19 ? 20  LEU A CG  1 
ATOM   149  C CD1 . LEU A 1 20  ? 11.653 -15.562 -2.752  1.00 20.48 ? 20  LEU A CD1 1 
ATOM   150  C CD2 . LEU A 1 20  ? 10.709 -17.731 -3.569  1.00 19.45 ? 20  LEU A CD2 1 
ATOM   151  N N   . SER A 1 21  ? 8.153  -18.396 0.558   1.00 15.86 ? 21  SER A N   1 
ATOM   152  C CA  . SER A 1 21  ? 7.744  -18.404 1.977   1.00 17.29 ? 21  SER A CA  1 
ATOM   153  C C   . SER A 1 21  ? 8.970  -18.530 2.885   1.00 15.52 ? 21  SER A C   1 
ATOM   154  O O   . SER A 1 21  ? 10.001 -19.068 2.470   1.00 16.82 ? 21  SER A O   1 
ATOM   155  C CB  . SER A 1 21  ? 6.707  -19.452 2.230   1.00 22.30 ? 21  SER A CB  1 
ATOM   156  O OG  . SER A 1 21  ? 7.288  -20.726 2.196   1.00 28.05 ? 21  SER A OG  1 
ATOM   157  N N   . CYS A 1 22  ? 8.837  -18.020 4.097   1.00 14.78 ? 22  CYS A N   1 
ATOM   158  C CA  . CYS A 1 22  ? 9.904  -17.976 5.126   1.00 15.51 ? 22  CYS A CA  1 
ATOM   159  C C   . CYS A 1 22  ? 9.249  -18.263 6.484   1.00 16.33 ? 22  CYS A C   1 
ATOM   160  O O   . CYS A 1 22  ? 8.562  -17.377 6.984   1.00 18.68 ? 22  CYS A O   1 
ATOM   161  C CB  . CYS A 1 22  ? 10.599 -16.622 5.086   1.00 18.24 ? 22  CYS A CB  1 
ATOM   162  S SG  . CYS A 1 22  ? 11.833 -16.443 6.393   1.00 22.94 ? 22  CYS A SG  1 
ATOM   163  N N   . ALA A 1 23  ? 9.394  -19.487 6.990   1.00 17.93 ? 23  ALA A N   1 
ATOM   164  C CA  . ALA A 1 23  ? 8.760  -19.984 8.230   1.00 19.71 ? 23  ALA A CA  1 
ATOM   165  C C   . ALA A 1 23  ? 9.772  -19.878 9.370   1.00 19.36 ? 23  ALA A C   1 
ATOM   166  O O   . ALA A 1 23  ? 10.897 -20.394 9.204   1.00 19.60 ? 23  ALA A O   1 
ATOM   167  C CB  . ALA A 1 23  ? 8.289  -21.409 8.037   1.00 23.92 ? 23  ALA A CB  1 
ATOM   168  N N   . ALA A 1 24  ? 9.389  -19.255 10.483  1.00 20.70 ? 24  ALA A N   1 
ATOM   169  C CA  . ALA A 1 24  ? 10.238 -19.141 11.696  1.00 20.74 ? 24  ALA A CA  1 
ATOM   170  C C   . ALA A 1 24  ? 9.878  -20.233 12.705  1.00 23.85 ? 24  ALA A C   1 
ATOM   171  O O   . ALA A 1 24  ? 8.676  -20.500 12.904  1.00 26.03 ? 24  ALA A O   1 
ATOM   172  C CB  . ALA A 1 24  ? 10.129 -17.769 12.314  1.00 20.82 ? 24  ALA A CB  1 
ATOM   173  N N   . SER A 1 25  ? 10.903 -20.844 13.301  1.00 25.14 ? 25  SER A N   1 
ATOM   174  C CA  . SER A 1 25  ? 10.787 -21.810 14.425  1.00 26.31 ? 25  SER A CA  1 
ATOM   175  C C   . SER A 1 25  ? 11.769 -21.412 15.530  1.00 25.94 ? 25  SER A C   1 
ATOM   176  O O   . SER A 1 25  ? 12.633 -20.555 15.273  1.00 22.50 ? 25  SER A O   1 
ATOM   177  C CB  . SER A 1 25  ? 11.031 -23.212 13.948  1.00 29.45 ? 25  SER A CB  1 
ATOM   178  O OG  . SER A 1 25  ? 12.336 -23.329 13.405  1.00 29.76 ? 25  SER A OG  1 
ATOM   179  N N   . GLY A 1 26  ? 11.629 -22.008 16.714  1.00 27.99 ? 26  GLY A N   1 
ATOM   180  C CA  . GLY A 1 26  ? 12.485 -21.731 17.881  1.00 30.36 ? 26  GLY A CA  1 
ATOM   181  C C   . GLY A 1 26  ? 11.850 -20.713 18.814  1.00 29.96 ? 26  GLY A C   1 
ATOM   182  O O   . GLY A 1 26  ? 10.623 -20.523 18.732  1.00 35.64 ? 26  GLY A O   1 
ATOM   183  N N   . SER A 1 27  ? 12.673 -20.082 19.654  1.00 32.22 ? 27  SER A N   1 
ATOM   184  C CA  . SER A 1 27  ? 12.253 -19.144 20.727  1.00 35.21 ? 27  SER A CA  1 
ATOM   185  C C   . SER A 1 27  ? 11.893 -17.787 20.114  1.00 27.27 ? 27  SER A C   1 
ATOM   186  O O   . SER A 1 27  ? 12.725 -16.859 20.207  1.00 28.62 ? 27  SER A O   1 
ATOM   187  C CB  . SER A 1 27  ? 13.336 -19.022 21.775  1.00 40.76 ? 27  SER A CB  1 
ATOM   188  O OG  . SER A 1 27  ? 13.721 -20.302 22.253  1.00 47.53 ? 27  SER A OG  1 
ATOM   189  N N   . VAL A 1 28  ? 10.718 -17.689 19.480  1.00 25.46 ? 28  VAL A N   1 
ATOM   190  C CA  . VAL A 1 28  ? 10.204 -16.425 18.872  1.00 26.81 ? 28  VAL A CA  1 
ATOM   191  C C   . VAL A 1 28  ? 9.463  -15.617 19.945  1.00 25.32 ? 28  VAL A C   1 
ATOM   192  O O   . VAL A 1 28  ? 8.414  -16.084 20.442  1.00 29.00 ? 28  VAL A O   1 
ATOM   193  C CB  . VAL A 1 28  ? 9.300  -16.678 17.650  1.00 28.06 ? 28  VAL A CB  1 
ATOM   194  C CG1 . VAL A 1 28  ? 8.751  -15.363 17.117  1.00 28.57 ? 28  VAL A CG1 1 
ATOM   195  C CG2 . VAL A 1 28  ? 10.020 -17.449 16.554  1.00 29.10 ? 28  VAL A CG2 1 
ATOM   196  N N   . PHE A 1 29  ? 9.995  -14.445 20.296  1.00 22.82 ? 29  PHE A N   1 
ATOM   197  C CA  . PHE A 1 29  ? 9.343  -13.442 21.182  1.00 21.48 ? 29  PHE A CA  1 
ATOM   198  C C   . PHE A 1 29  ? 8.661  -12.404 20.294  1.00 20.08 ? 29  PHE A C   1 
ATOM   199  O O   . PHE A 1 29  ? 7.813  -12.816 19.495  1.00 25.04 ? 29  PHE A O   1 
ATOM   200  C CB  . PHE A 1 29  ? 10.358 -12.913 22.192  1.00 20.36 ? 29  PHE A CB  1 
ATOM   201  C CG  . PHE A 1 29  ? 10.721 -13.980 23.184  1.00 20.96 ? 29  PHE A CG  1 
ATOM   202  C CD1 . PHE A 1 29  ? 9.948  -14.180 24.315  1.00 21.05 ? 29  PHE A CD1 1 
ATOM   203  C CD2 . PHE A 1 29  ? 11.780 -14.841 22.948  1.00 23.92 ? 29  PHE A CD2 1 
ATOM   204  C CE1 . PHE A 1 29  ? 10.256 -15.192 25.215  1.00 22.31 ? 29  PHE A CE1 1 
ATOM   205  C CE2 . PHE A 1 29  ? 12.090 -15.848 23.850  1.00 25.15 ? 29  PHE A CE2 1 
ATOM   206  C CZ  . PHE A 1 29  ? 11.320 -16.027 24.977  1.00 23.80 ? 29  PHE A CZ  1 
ATOM   207  N N   . LYS A 1 30  ? 8.999  -11.124 20.431  1.00 19.97 ? 30  LYS A N   1 
ATOM   208  C CA  . LYS A 1 30  ? 8.373  -10.046 19.630  1.00 19.75 ? 30  LYS A CA  1 
ATOM   209  C C   . LYS A 1 30  ? 9.130  -9.969  18.302  1.00 19.51 ? 30  LYS A C   1 
ATOM   210  O O   . LYS A 1 30  ? 10.378 -9.882  18.339  1.00 20.49 ? 30  LYS A O   1 
ATOM   211  C CB  . LYS A 1 30  ? 8.409  -8.690  20.345  1.00 24.48 ? 30  LYS A CB  1 
ATOM   212  C CG  . LYS A 1 30  ? 7.771  -7.572  19.529  1.00 29.59 ? 30  LYS A CG  1 
ATOM   213  C CD  . LYS A 1 30  ? 7.532  -6.276  20.251  1.00 36.16 ? 30  LYS A CD  1 
ATOM   214  C CE  . LYS A 1 30  ? 7.224  -5.111  19.323  1.00 43.83 ? 30  LYS A CE  1 
ATOM   215  N NZ  . LYS A 1 30  ? 6.773  -5.524  17.968  1.00 47.19 ? 30  LYS A NZ  1 
ATOM   216  N N   . ILE A 1 31  ? 8.409  -10.031 17.179  1.00 22.53 ? 31  ILE A N   1 
ATOM   217  C CA  . ILE A 1 31  ? 9.003  -9.792  15.831  1.00 20.14 ? 31  ILE A CA  1 
ATOM   218  C C   . ILE A 1 31  ? 8.814  -8.313  15.475  1.00 22.10 ? 31  ILE A C   1 
ATOM   219  O O   . ILE A 1 31  ? 7.653  -7.886  15.325  1.00 25.57 ? 31  ILE A O   1 
ATOM   220  C CB  . ILE A 1 31  ? 8.413  -10.738 14.771  1.00 22.56 ? 31  ILE A CB  1 
ATOM   221  C CG1 . ILE A 1 31  ? 8.569  -12.205 15.177  1.00 23.12 ? 31  ILE A CG1 1 
ATOM   222  C CG2 . ILE A 1 31  ? 9.046  -10.463 13.419  1.00 22.55 ? 31  ILE A CG2 1 
ATOM   223  C CD1 . ILE A 1 31  ? 7.766  -13.173 14.337  1.00 26.39 ? 31  ILE A CD1 1 
ATOM   224  N N   . ASN A 1 32  ? 9.920  -7.571  15.370  1.00 21.56 ? 32  ASN A N   1 
ATOM   225  C CA  . ASN A 1 32  ? 9.949  -6.128  15.023  1.00 24.44 ? 32  ASN A CA  1 
ATOM   226  C C   . ASN A 1 32  ? 9.886  -5.939  13.509  1.00 21.83 ? 32  ASN A C   1 
ATOM   227  O O   . ASN A 1 32  ? 9.242  -4.976  13.064  1.00 22.92 ? 32  ASN A O   1 
ATOM   228  C CB  . ASN A 1 32  ? 11.196 -5.449  15.585  1.00 26.23 ? 32  ASN A CB  1 
ATOM   229  C CG  . ASN A 1 32  ? 11.130 -5.343  17.092  1.00 31.96 ? 32  ASN A CG  1 
ATOM   230  O OD1 . ASN A 1 32  ? 10.130 -4.884  17.639  1.00 38.93 ? 32  ASN A OD1 1 
ATOM   231  N ND2 . ASN A 1 32  ? 12.172 -5.803  17.764  1.00 43.39 ? 32  ASN A ND2 1 
ATOM   232  N N   . VAL A 1 33  ? 10.564 -6.801  12.757  1.00 20.22 ? 33  VAL A N   1 
ATOM   233  C CA  . VAL A 1 33  ? 10.759 -6.650  11.288  1.00 20.61 ? 33  VAL A CA  1 
ATOM   234  C C   . VAL A 1 33  ? 10.704 -8.029  10.636  1.00 17.27 ? 33  VAL A C   1 
ATOM   235  O O   . VAL A 1 33  ? 11.326 -8.961  11.175  1.00 15.57 ? 33  VAL A O   1 
ATOM   236  C CB  . VAL A 1 33  ? 12.125 -6.001  10.992  1.00 25.69 ? 33  VAL A CB  1 
ATOM   237  C CG1 . VAL A 1 33  ? 12.377 -5.874  9.502   1.00 29.15 ? 33  VAL A CG1 1 
ATOM   238  C CG2 . VAL A 1 33  ? 12.293 -4.671  11.700  1.00 29.19 ? 33  VAL A CG2 1 
ATOM   239  N N   . MET A 1 34  ? 10.069 -8.118  9.477   1.00 17.23 ? 34  MET A N   1 
ATOM   240  C CA  . MET A 1 34  ? 10.211 -9.262  8.546   1.00 16.80 ? 34  MET A CA  1 
ATOM   241  C C   . MET A 1 34  ? 10.524 -8.666  7.174   1.00 15.20 ? 34  MET A C   1 
ATOM   242  O O   . MET A 1 34  ? 9.771  -7.781  6.730   1.00 17.77 ? 34  MET A O   1 
ATOM   243  C CB  . MET A 1 34  ? 8.927  -10.087 8.455   1.00 17.60 ? 34  MET A CB  1 
ATOM   244  C CG  . MET A 1 34  ? 8.510  -10.758 9.733   1.00 20.11 ? 34  MET A CG  1 
ATOM   245  S SD  . MET A 1 34  ? 6.889  -11.511 9.422   1.00 27.89 ? 34  MET A SD  1 
ATOM   246  C CE  . MET A 1 34  ? 6.469  -12.126 11.048  1.00 29.97 ? 34  MET A CE  1 
ATOM   247  N N   . ALA A 1 35  ? 11.594 -9.107  6.522   1.00 13.73 ? 35  ALA A N   1 
ATOM   248  C CA  . ALA A 1 35  ? 11.991 -8.489  5.238   1.00 14.20 ? 35  ALA A CA  1 
ATOM   249  C C   . ALA A 1 35  ? 12.603 -9.507  4.288   1.00 13.72 ? 35  ALA A C   1 
ATOM   250  O O   . ALA A 1 35  ? 13.133 -10.534 4.738   1.00 14.52 ? 35  ALA A O   1 
ATOM   251  C CB  . ALA A 1 35  ? 12.921 -7.327  5.466   1.00 14.97 ? 35  ALA A CB  1 
ATOM   252  N N   . TRP A 1 36  ? 12.483 -9.194  3.001   1.00 14.03 ? 36  TRP A N   1 
ATOM   253  C CA  . TRP A 1 36  ? 13.103 -9.932  1.878   1.00 13.75 ? 36  TRP A CA  1 
ATOM   254  C C   . TRP A 1 36  ? 14.241 -9.099  1.316   1.00 13.23 ? 36  TRP A C   1 
ATOM   255  O O   . TRP A 1 36  ? 14.040 -7.895  1.120   1.00 14.24 ? 36  TRP A O   1 
ATOM   256  C CB  . TRP A 1 36  ? 12.093 -10.253 0.778   1.00 13.23 ? 36  TRP A CB  1 
ATOM   257  C CG  . TRP A 1 36  ? 11.033 -11.212 1.207   1.00 13.61 ? 36  TRP A CG  1 
ATOM   258  C CD1 . TRP A 1 36  ? 9.766  -10.902 1.614   1.00 14.44 ? 36  TRP A CD1 1 
ATOM   259  C CD2 . TRP A 1 36  ? 11.150 -12.641 1.291   1.00 12.52 ? 36  TRP A CD2 1 
ATOM   260  N NE1 . TRP A 1 36  ? 9.089  -12.046 1.931   1.00 14.19 ? 36  TRP A NE1 1 
ATOM   261  C CE2 . TRP A 1 36  ? 9.908  -13.129 1.746   1.00 13.60 ? 36  TRP A CE2 1 
ATOM   262  C CE3 . TRP A 1 36  ? 12.171 -13.558 1.016   1.00 12.20 ? 36  TRP A CE3 1 
ATOM   263  C CZ2 . TRP A 1 36  ? 9.672  -14.492 1.920   1.00 15.89 ? 36  TRP A CZ2 1 
ATOM   264  C CZ3 . TRP A 1 36  ? 11.934 -14.902 1.184   1.00 13.69 ? 36  TRP A CZ3 1 
ATOM   265  C CH2 . TRP A 1 36  ? 10.705 -15.357 1.647   1.00 14.97 ? 36  TRP A CH2 1 
ATOM   266  N N   . TYR A 1 37  ? 15.371 -9.754  1.082   1.00 13.37 ? 37  TYR A N   1 
ATOM   267  C CA  . TYR A 1 37  ? 16.581 -9.195  0.454   1.00 13.42 ? 37  TYR A CA  1 
ATOM   268  C C   . TYR A 1 37  ? 16.904 -10.045 -0.766  1.00 12.96 ? 37  TYR A C   1 
ATOM   269  O O   . TYR A 1 37  ? 16.487 -11.220 -0.838  1.00 13.96 ? 37  TYR A O   1 
ATOM   270  C CB  . TYR A 1 37  ? 17.762 -9.207  1.430   1.00 15.02 ? 37  TYR A CB  1 
ATOM   271  C CG  . TYR A 1 37  ? 17.547 -8.374  2.669   1.00 15.07 ? 37  TYR A CG  1 
ATOM   272  C CD1 . TYR A 1 37  ? 16.770 -8.845  3.718   1.00 15.37 ? 37  TYR A CD1 1 
ATOM   273  C CD2 . TYR A 1 37  ? 18.123 -7.127  2.807   1.00 17.13 ? 37  TYR A CD2 1 
ATOM   274  C CE1 . TYR A 1 37  ? 16.536 -8.077  4.846   1.00 16.47 ? 37  TYR A CE1 1 
ATOM   275  C CE2 . TYR A 1 37  ? 17.929 -6.362  3.947   1.00 18.13 ? 37  TYR A CE2 1 
ATOM   276  C CZ  . TYR A 1 37  ? 17.118 -6.829  4.964   1.00 18.00 ? 37  TYR A CZ  1 
ATOM   277  O OH  . TYR A 1 37  ? 16.935 -6.082  6.094   1.00 19.83 ? 37  TYR A OH  1 
ATOM   278  N N   . ARG A 1 38  ? 17.681 -9.496  -1.692  1.00 13.69 ? 38  ARG A N   1 
ATOM   279  C CA  . ARG A 1 38  ? 18.156 -10.327 -2.815  1.00 15.02 ? 38  ARG A CA  1 
ATOM   280  C C   . ARG A 1 38  ? 19.567 -9.895  -3.189  1.00 15.70 ? 38  ARG A C   1 
ATOM   281  O O   . ARG A 1 38  ? 19.886 -8.686  -3.074  1.00 16.20 ? 38  ARG A O   1 
ATOM   282  C CB  . ARG A 1 38  ? 17.209 -10.273 -4.020  1.00 15.55 ? 38  ARG A CB  1 
ATOM   283  C CG  . ARG A 1 38  ? 17.229 -8.944  -4.753  1.00 16.80 ? 38  ARG A CG  1 
ATOM   284  C CD  . ARG A 1 38  ? 16.188 -8.944  -5.840  1.00 19.42 ? 38  ARG A CD  1 
ATOM   285  N NE  . ARG A 1 38  ? 16.123 -7.654  -6.488  1.00 20.36 ? 38  ARG A NE  1 
ATOM   286  C CZ  . ARG A 1 38  ? 15.254 -7.333  -7.439  1.00 22.10 ? 38  ARG A CZ  1 
ATOM   287  N NH1 . ARG A 1 38  ? 14.374 -8.221  -7.869  1.00 20.74 ? 38  ARG A NH1 1 
ATOM   288  N NH2 . ARG A 1 38  ? 15.299 -6.126  -7.974  1.00 26.79 ? 38  ARG A NH2 1 
ATOM   289  N N   . GLN A 1 39  ? 20.352 -10.882 -3.604  1.00 15.80 ? 39  GLN A N   1 
ATOM   290  C CA  A GLN A 1 39  ? 21.730 -10.658 -4.099  0.60 16.39 ? 39  GLN A CA  1 
ATOM   291  C CA  B GLN A 1 39  ? 21.747 -10.722 -4.077  0.40 16.42 ? 39  GLN A CA  1 
ATOM   292  C C   . GLN A 1 39  ? 21.808 -11.145 -5.547  1.00 17.45 ? 39  GLN A C   1 
ATOM   293  O O   . GLN A 1 39  ? 21.366 -12.239 -5.825  1.00 20.79 ? 39  GLN A O   1 
ATOM   294  C CB  A GLN A 1 39  ? 22.754 -11.336 -3.186  0.60 16.84 ? 39  GLN A CB  1 
ATOM   295  C CB  B GLN A 1 39  ? 22.661 -11.599 -3.218  0.40 16.52 ? 39  GLN A CB  1 
ATOM   296  C CG  A GLN A 1 39  ? 24.189 -11.244 -3.698  0.60 16.83 ? 39  GLN A CG  1 
ATOM   297  C CG  B GLN A 1 39  ? 24.122 -11.596 -3.652  0.40 16.64 ? 39  GLN A CG  1 
ATOM   298  C CD  A GLN A 1 39  ? 24.464 -12.227 -4.809  0.60 17.17 ? 39  GLN A CD  1 
ATOM   299  C CD  B GLN A 1 39  ? 24.708 -10.211 -3.553  0.40 17.40 ? 39  GLN A CD  1 
ATOM   300  O OE1 A GLN A 1 39  ? 23.712 -13.179 -5.009  0.60 17.19 ? 39  GLN A OE1 1 
ATOM   301  O OE1 B GLN A 1 39  ? 25.019 -9.723  -2.467  0.40 17.53 ? 39  GLN A OE1 1 
ATOM   302  N NE2 A GLN A 1 39  ? 25.534 -11.995 -5.557  0.60 19.10 ? 39  GLN A NE2 1 
ATOM   303  N NE2 B GLN A 1 39  ? 24.845 -9.559  -4.695  0.40 18.00 ? 39  GLN A NE2 1 
ATOM   304  N N   . ALA A 1 40  ? 22.399 -10.330 -6.407  1.00 20.24 ? 40  ALA A N   1 
ATOM   305  C CA  . ALA A 1 40  ? 22.681 -10.702 -7.805  1.00 20.83 ? 40  ALA A CA  1 
ATOM   306  C C   . ALA A 1 40  ? 24.077 -10.213 -8.157  1.00 24.22 ? 40  ALA A C   1 
ATOM   307  O O   . ALA A 1 40  ? 24.539 -9.220  -7.608  1.00 24.50 ? 40  ALA A O   1 
ATOM   308  C CB  . ALA A 1 40  ? 21.627 -10.123 -8.711  1.00 22.30 ? 40  ALA A CB  1 
ATOM   309  N N   . PRO A 1 41  ? 24.770 -10.869 -9.112  1.00 27.63 ? 41  PRO A N   1 
ATOM   310  C CA  . PRO A 1 41  ? 26.096 -10.406 -9.522  1.00 30.86 ? 41  PRO A CA  1 
ATOM   311  C C   . PRO A 1 41  ? 26.049 -8.937  -9.984  1.00 28.90 ? 41  PRO A C   1 
ATOM   312  O O   . PRO A 1 41  ? 25.183 -8.597  -10.772 1.00 28.08 ? 41  PRO A O   1 
ATOM   313  C CB  . PRO A 1 41  ? 26.516 -11.388 -10.628 1.00 36.60 ? 41  PRO A CB  1 
ATOM   314  C CG  . PRO A 1 41  ? 25.247 -12.143 -11.025 1.00 36.41 ? 41  PRO A CG  1 
ATOM   315  C CD  . PRO A 1 41  ? 24.304 -12.057 -9.842  1.00 31.13 ? 41  PRO A CD  1 
ATOM   316  N N   . GLY A 1 42  ? 26.931 -8.102  -9.427  1.00 30.10 ? 42  GLY A N   1 
ATOM   317  C CA  . GLY A 1 42  ? 27.090 -6.673  -9.764  1.00 28.76 ? 42  GLY A CA  1 
ATOM   318  C C   . GLY A 1 42  ? 26.047 -5.772  -9.123  1.00 28.14 ? 42  GLY A C   1 
ATOM   319  O O   . GLY A 1 42  ? 26.059 -4.563  -9.434  1.00 32.97 ? 42  GLY A O   1 
ATOM   320  N N   . LYS A 1 43  ? 25.175 -6.303  -8.259  1.00 23.86 ? 43  LYS A N   1 
ATOM   321  C CA  . LYS A 1 43  ? 24.034 -5.540  -7.679  1.00 25.60 ? 43  LYS A CA  1 
ATOM   322  C C   . LYS A 1 43  ? 24.114 -5.511  -6.150  1.00 27.18 ? 43  LYS A C   1 
ATOM   323  O O   . LYS A 1 43  ? 23.133 -5.031  -5.508  1.00 32.41 ? 43  LYS A O   1 
ATOM   324  C CB  . LYS A 1 43  ? 22.712 -6.180  -8.104  1.00 26.25 ? 43  LYS A CB  1 
ATOM   325  C CG  . LYS A 1 43  ? 22.419 -6.120  -9.599  1.00 27.47 ? 43  LYS A CG  1 
ATOM   326  C CD  . LYS A 1 43  ? 22.289 -4.716  -10.152 1.00 29.42 ? 43  LYS A CD  1 
ATOM   327  C CE  . LYS A 1 43  ? 21.270 -3.868  -9.418  1.00 31.81 ? 43  LYS A CE  1 
ATOM   328  N NZ  . LYS A 1 43  ? 19.956 -4.545  -9.316  1.00 33.42 ? 43  LYS A NZ  1 
ATOM   329  N N   . GLY A 1 44  ? 25.193 -6.034  -5.574  1.00 24.63 ? 44  GLY A N   1 
ATOM   330  C CA  . GLY A 1 44  ? 25.288 -6.201  -4.113  1.00 27.26 ? 44  GLY A CA  1 
ATOM   331  C C   . GLY A 1 44  ? 24.044 -6.871  -3.549  1.00 25.66 ? 44  GLY A C   1 
ATOM   332  O O   . GLY A 1 44  ? 23.360 -7.645  -4.279  1.00 28.16 ? 44  GLY A O   1 
ATOM   333  N N   . ARG A 1 45  ? 23.743 -6.617  -2.286  1.00 19.15 ? 45  ARG A N   1 
ATOM   334  C CA  . ARG A 1 45  ? 22.499 -7.122  -1.657  1.00 17.74 ? 45  ARG A CA  1 
ATOM   335  C C   . ARG A 1 45  ? 21.552 -5.939  -1.473  1.00 18.26 ? 45  ARG A C   1 
ATOM   336  O O   . ARG A 1 45  ? 22.011 -4.886  -1.009  1.00 18.46 ? 45  ARG A O   1 
ATOM   337  C CB  . ARG A 1 45  ? 22.821 -7.829  -0.344  1.00 18.94 ? 45  ARG A CB  1 
ATOM   338  C CG  . ARG A 1 45  ? 21.667 -8.644  0.213   1.00 18.06 ? 45  ARG A CG  1 
ATOM   339  C CD  . ARG A 1 45  ? 22.064 -9.289  1.517   1.00 20.12 ? 45  ARG A CD  1 
ATOM   340  N NE  . ARG A 1 45  ? 22.202 -8.283  2.557   1.00 21.20 ? 45  ARG A NE  1 
ATOM   341  C CZ  . ARG A 1 45  ? 22.703 -8.505  3.769   1.00 22.38 ? 45  ARG A CZ  1 
ATOM   342  N NH1 . ARG A 1 45  ? 22.750 -7.517  4.645   1.00 22.92 ? 45  ARG A NH1 1 
ATOM   343  N NH2 . ARG A 1 45  ? 23.146 -9.706  4.106   1.00 25.29 ? 45  ARG A NH2 1 
ATOM   344  N N   . GLU A 1 46  ? 20.282 -6.129  -1.829  1.00 17.11 ? 46  GLU A N   1 
ATOM   345  C CA  A GLU A 1 46  ? 19.228 -5.085  -1.872  0.50 16.56 ? 46  GLU A CA  1 
ATOM   346  C CA  B GLU A 1 46  ? 19.267 -5.049  -1.780  0.50 16.73 ? 46  GLU A CA  1 
ATOM   347  C C   . GLU A 1 46  ? 18.058 -5.520  -0.977  1.00 16.03 ? 46  GLU A C   1 
ATOM   348  O O   . GLU A 1 46  ? 17.691 -6.706  -1.054  1.00 15.62 ? 46  GLU A O   1 
ATOM   349  C CB  A GLU A 1 46  ? 18.805 -4.934  -3.336  0.50 18.39 ? 46  GLU A CB  1 
ATOM   350  C CB  B GLU A 1 46  ? 18.886 -4.607  -3.188  0.50 18.73 ? 46  GLU A CB  1 
ATOM   351  C CG  A GLU A 1 46  ? 17.688 -3.941  -3.594  0.50 19.58 ? 46  GLU A CG  1 
ATOM   352  C CG  B GLU A 1 46  ? 20.113 -4.282  -4.006  0.50 21.18 ? 46  GLU A CG  1 
ATOM   353  C CD  A GLU A 1 46  ? 17.268 -3.819  -5.051  0.50 21.16 ? 46  GLU A CD  1 
ATOM   354  C CD  B GLU A 1 46  ? 19.838 -3.709  -5.373  0.50 21.80 ? 46  GLU A CD  1 
ATOM   355  O OE1 A GLU A 1 46  ? 16.910 -2.693  -5.458  0.50 22.99 ? 46  GLU A OE1 1 
ATOM   356  O OE1 B GLU A 1 46  ? 18.651 -3.464  -5.683  0.50 23.29 ? 46  GLU A OE1 1 
ATOM   357  O OE2 A GLU A 1 46  ? 17.260 -4.858  -5.766  0.50 20.53 ? 46  GLU A OE2 1 
ATOM   358  O OE2 B GLU A 1 46  ? 20.814 -3.528  -6.109  0.50 26.17 ? 46  GLU A OE2 1 
ATOM   359  N N   . LEU A 1 47  ? 17.487 -4.603  -0.199  1.00 16.61 ? 47  LEU A N   1 
ATOM   360  C CA  . LEU A 1 47  ? 16.189 -4.845  0.481   1.00 17.18 ? 47  LEU A CA  1 
ATOM   361  C C   . LEU A 1 47  ? 15.119 -4.815  -0.621  1.00 17.51 ? 47  LEU A C   1 
ATOM   362  O O   . LEU A 1 47  ? 15.024 -3.808  -1.323  1.00 21.72 ? 47  LEU A O   1 
ATOM   363  C CB  . LEU A 1 47  ? 15.952 -3.770  1.543   1.00 21.76 ? 47  LEU A CB  1 
ATOM   364  C CG  . LEU A 1 47  ? 14.553 -3.742  2.160   1.00 24.91 ? 47  LEU A CG  1 
ATOM   365  C CD1 . LEU A 1 47  ? 14.292 -4.986  2.980   1.00 25.85 ? 47  LEU A CD1 1 
ATOM   366  C CD2 . LEU A 1 47  ? 14.378 -2.499  3.016   1.00 29.01 ? 47  LEU A CD2 1 
ATOM   367  N N   . VAL A 1 48  ? 14.344 -5.886  -0.762  1.00 15.63 ? 48  VAL A N   1 
ATOM   368  C CA  . VAL A 1 48  ? 13.285 -6.057  -1.801  1.00 16.43 ? 48  VAL A CA  1 
ATOM   369  C C   . VAL A 1 48  ? 11.954 -5.529  -1.254  1.00 15.47 ? 48  VAL A C   1 
ATOM   370  O O   . VAL A 1 48  ? 11.265 -4.763  -1.955  1.00 17.14 ? 48  VAL A O   1 
ATOM   371  C CB  . VAL A 1 48  ? 13.187 -7.541  -2.208  1.00 18.21 ? 48  VAL A CB  1 
ATOM   372  C CG1 . VAL A 1 48  ? 11.985 -7.827  -3.083  1.00 21.33 ? 48  VAL A CG1 1 
ATOM   373  C CG2 . VAL A 1 48  ? 14.466 -8.006  -2.869  1.00 20.19 ? 48  VAL A CG2 1 
ATOM   374  N N   . ALA A 1 49  ? 11.600 -5.940  -0.044  1.00 16.30 ? 49  ALA A N   1 
ATOM   375  C CA  . ALA A 1 49  ? 10.296 -5.643  0.578   1.00 16.35 ? 49  ALA A CA  1 
ATOM   376  C C   . ALA A 1 49  ? 10.410 -5.916  2.074   1.00 15.01 ? 49  ALA A C   1 
ATOM   377  O O   . ALA A 1 49  ? 11.099 -6.871  2.457   1.00 15.83 ? 49  ALA A O   1 
ATOM   378  C CB  . ALA A 1 49  ? 9.212  -6.482  -0.062  1.00 17.15 ? 49  ALA A CB  1 
ATOM   379  N N   . GLY A 1 50  ? 9.742  -5.105  2.886   1.00 17.38 ? 50  GLY A N   1 
ATOM   380  C CA  . GLY A 1 50  ? 9.721  -5.315  4.339   1.00 17.00 ? 50  GLY A CA  1 
ATOM   381  C C   . GLY A 1 50  ? 8.394  -4.940  4.951   1.00 18.29 ? 50  GLY A C   1 
ATOM   382  O O   . GLY A 1 50  ? 7.675  -4.112  4.345   1.00 20.46 ? 50  GLY A O   1 
ATOM   383  N N   . ILE A 1 51  ? 8.093  -5.561  6.090   1.00 20.66 ? 51  ILE A N   1 
ATOM   384  C CA  . ILE A 1 51  ? 6.931  -5.247  6.972   1.00 24.47 ? 51  ILE A CA  1 
ATOM   385  C C   . ILE A 1 51  ? 7.481  -4.984  8.373   1.00 24.84 ? 51  ILE A C   1 
ATOM   386  O O   . ILE A 1 51  ? 8.144  -5.891  8.910   1.00 22.88 ? 51  ILE A O   1 
ATOM   387  C CB  . ILE A 1 51  ? 5.910  -6.395  7.054   1.00 29.63 ? 51  ILE A CB  1 
ATOM   388  C CG1 . ILE A 1 51  ? 5.324  -6.808  5.705   1.00 34.36 ? 51  ILE A CG1 1 
ATOM   389  C CG2 . ILE A 1 51  ? 4.810  -6.026  8.048   1.00 32.64 ? 51  ILE A CG2 1 
ATOM   390  C CD1 . ILE A 1 51  ? 4.626  -8.153  5.761   1.00 35.28 ? 51  ILE A CD1 1 
ATOM   391  N N   . ILE A 1 52  ? 7.216  -3.810  8.940   1.00 26.51 ? 52  ILE A N   1 
ATOM   392  C CA  . ILE A 1 52  ? 7.576  -3.490  10.353  1.00 30.72 ? 52  ILE A CA  1 
ATOM   393  C C   . ILE A 1 52  ? 6.349  -3.780  11.223  1.00 32.91 ? 52  ILE A C   1 
ATOM   394  O O   . ILE A 1 52  ? 5.225  -3.568  10.739  1.00 38.30 ? 52  ILE A O   1 
ATOM   395  C CB  . ILE A 1 52  ? 8.088  -2.041  10.465  1.00 35.86 ? 52  ILE A CB  1 
ATOM   396  C CG1 . ILE A 1 52  ? 7.008  -0.994  10.184  1.00 42.93 ? 52  ILE A CG1 1 
ATOM   397  C CG2 . ILE A 1 52  ? 9.294  -1.845  9.557   1.00 36.09 ? 52  ILE A CG2 1 
ATOM   398  C CD1 . ILE A 1 52  ? 7.117  0.240   11.057  1.00 50.38 ? 52  ILE A CD1 1 
ATOM   399  N N   . SER A 1 53  ? 6.549  -4.249  12.455  1.00 33.51 ? 53  SER A N   1 
ATOM   400  C CA  . SER A 1 53  ? 5.452  -4.527  13.421  1.00 37.92 ? 53  SER A CA  1 
ATOM   401  C C   . SER A 1 53  ? 4.622  -3.253  13.574  1.00 39.59 ? 53  SER A C   1 
ATOM   402  O O   . SER A 1 53  ? 5.171  -2.240  14.050  1.00 47.70 ? 53  SER A O   1 
ATOM   403  C CB  . SER A 1 53  ? 5.961  -5.031  14.751  1.00 43.43 ? 53  SER A CB  1 
ATOM   404  O OG  . SER A 1 53  ? 7.032  -4.233  15.234  1.00 52.06 ? 53  SER A OG  1 
ATOM   405  N N   . GLY A 1 54  ? 3.357  -3.319  13.154  1.00 43.91 ? 54  GLY A N   1 
ATOM   406  C CA  . GLY A 1 54  ? 2.489  -2.156  12.892  1.00 49.35 ? 54  GLY A CA  1 
ATOM   407  C C   . GLY A 1 54  ? 1.842  -2.258  11.519  1.00 50.10 ? 54  GLY A C   1 
ATOM   408  O O   . GLY A 1 54  ? 0.743  -1.706  11.347  1.00 57.76 ? 54  GLY A O   1 
ATOM   409  N N   . GLY A 1 55  ? 2.503  -2.935  10.571  1.00 51.65 ? 55  GLY A N   1 
ATOM   410  C CA  . GLY A 1 55  ? 1.969  -3.235  9.224   1.00 51.93 ? 55  GLY A CA  1 
ATOM   411  C C   . GLY A 1 55  ? 2.562  -2.347  8.137   1.00 46.88 ? 55  GLY A C   1 
ATOM   412  O O   . GLY A 1 55  ? 2.257  -2.596  6.954   1.00 52.23 ? 55  GLY A O   1 
ATOM   413  N N   . SER A 1 56  ? 3.362  -1.341  8.509   1.00 45.00 ? 56  SER A N   1 
ATOM   414  C CA  . SER A 1 56  ? 4.015  -0.385  7.573   1.00 41.14 ? 56  SER A CA  1 
ATOM   415  C C   . SER A 1 56  ? 4.973  -1.142  6.642   1.00 36.27 ? 56  SER A C   1 
ATOM   416  O O   . SER A 1 56  ? 6.013  -1.621  7.132   1.00 33.04 ? 56  SER A O   1 
ATOM   417  C CB  . SER A 1 56  ? 4.719  0.714   8.324   1.00 44.67 ? 56  SER A CB  1 
ATOM   418  O OG  . SER A 1 56  ? 5.628  1.402   7.479   1.00 49.32 ? 56  SER A OG  1 
ATOM   419  N N   . THR A 1 57  ? 4.647  -1.209  5.346   1.00 35.87 ? 57  THR A N   1 
ATOM   420  C CA  . THR A 1 57  ? 5.440  -1.926  4.317   1.00 33.37 ? 57  THR A CA  1 
ATOM   421  C C   . THR A 1 57  ? 6.297  -0.962  3.495   1.00 31.63 ? 57  THR A C   1 
ATOM   422  O O   . THR A 1 57  ? 5.933  0.215   3.336   1.00 33.64 ? 57  THR A O   1 
ATOM   423  C CB  . THR A 1 57  ? 4.569  -2.706  3.329   1.00 36.10 ? 57  THR A CB  1 
ATOM   424  O OG1 . THR A 1 57  ? 3.802  -1.739  2.617   1.00 41.14 ? 57  THR A OG1 1 
ATOM   425  C CG2 . THR A 1 57  ? 3.674  -3.726  3.991   1.00 38.76 ? 57  THR A CG2 1 
ATOM   426  N N   . SER A 1 58  ? 7.373  -1.501  2.934   1.00 26.00 ? 58  SER A N   1 
ATOM   427  C CA  . SER A 1 58  ? 8.343  -0.788  2.068   1.00 27.86 ? 58  SER A CA  1 
ATOM   428  C C   . SER A 1 58  ? 8.786  -1.730  0.940   1.00 25.19 ? 58  SER A C   1 
ATOM   429  O O   . SER A 1 58  ? 8.842  -2.950  1.175   1.00 23.96 ? 58  SER A O   1 
ATOM   430  C CB  . SER A 1 58  ? 9.496  -0.289  2.900   1.00 30.82 ? 58  SER A CB  1 
ATOM   431  O OG  . SER A 1 58  ? 10.607 0.074   2.102   1.00 39.22 ? 58  SER A OG  1 
ATOM   432  N N   . TYR A 1 59  ? 9.051  -1.181  -0.244  1.00 25.85 ? 59  TYR A N   1 
ATOM   433  C CA  . TYR A 1 59  ? 9.478  -1.923  -1.459  1.00 23.16 ? 59  TYR A CA  1 
ATOM   434  C C   . TYR A 1 59  ? 10.612 -1.172  -2.157  1.00 26.04 ? 59  TYR A C   1 
ATOM   435  O O   . TYR A 1 59  ? 10.570 0.072   -2.220  1.00 27.27 ? 59  TYR A O   1 
ATOM   436  C CB  . TYR A 1 59  ? 8.324  -2.071  -2.451  1.00 25.37 ? 59  TYR A CB  1 
ATOM   437  C CG  . TYR A 1 59  ? 7.178  -2.926  -1.978  1.00 23.85 ? 59  TYR A CG  1 
ATOM   438  C CD1 . TYR A 1 59  ? 6.077  -2.362  -1.356  1.00 27.57 ? 59  TYR A CD1 1 
ATOM   439  C CD2 . TYR A 1 59  ? 7.177  -4.297  -2.170  1.00 23.97 ? 59  TYR A CD2 1 
ATOM   440  C CE1 . TYR A 1 59  ? 5.015  -3.140  -0.922  1.00 25.99 ? 59  TYR A CE1 1 
ATOM   441  C CE2 . TYR A 1 59  ? 6.119  -5.090  -1.754  1.00 23.97 ? 59  TYR A CE2 1 
ATOM   442  C CZ  . TYR A 1 59  ? 5.034  -4.510  -1.119  1.00 24.41 ? 59  TYR A CZ  1 
ATOM   443  O OH  . TYR A 1 59  ? 3.983  -5.280  -0.711  1.00 22.72 ? 59  TYR A OH  1 
ATOM   444  N N   . ALA A 1 60  ? 11.569 -1.920  -2.707  1.00 24.71 ? 60  ALA A N   1 
ATOM   445  C CA  . ALA A 1 60  ? 12.556 -1.415  -3.680  1.00 25.77 ? 60  ALA A CA  1 
ATOM   446  C C   . ALA A 1 60  ? 11.779 -0.819  -4.855  1.00 26.08 ? 60  ALA A C   1 
ATOM   447  O O   . ALA A 1 60  ? 10.757 -1.431  -5.268  1.00 25.11 ? 60  ALA A O   1 
ATOM   448  C CB  . ALA A 1 60  ? 13.478 -2.517  -4.134  1.00 26.76 ? 60  ALA A CB  1 
ATOM   449  N N   . ASP A 1 61  ? 12.227 0.336   -5.351  1.00 26.91 ? 61  ASP A N   1 
ATOM   450  C CA  . ASP A 1 61  ? 11.677 0.984   -6.573  1.00 31.22 ? 61  ASP A CA  1 
ATOM   451  C C   . ASP A 1 61  ? 11.514 -0.048  -7.695  1.00 29.89 ? 61  ASP A C   1 
ATOM   452  O O   . ASP A 1 61  ? 10.483 -0.016  -8.400  1.00 29.47 ? 61  ASP A O   1 
ATOM   453  C CB  . ASP A 1 61  ? 12.592 2.102   -7.079  1.00 34.17 ? 61  ASP A CB  1 
ATOM   454  C CG  . ASP A 1 61  ? 12.465 3.415   -6.328  1.00 38.60 ? 61  ASP A CG  1 
ATOM   455  O OD1 . ASP A 1 61  ? 11.665 3.477   -5.370  1.00 42.69 ? 61  ASP A OD1 1 
ATOM   456  O OD2 . ASP A 1 61  ? 13.161 4.374   -6.719  1.00 47.43 ? 61  ASP A OD2 1 
ATOM   457  N N   . SER A 1 62  ? 12.514 -0.916  -7.867  1.00 28.18 ? 62  SER A N   1 
ATOM   458  C CA  . SER A 1 62  ? 12.603 -1.858  -9.015  1.00 31.65 ? 62  SER A CA  1 
ATOM   459  C C   . SER A 1 62  ? 11.455 -2.882  -8.999  1.00 28.68 ? 62  SER A C   1 
ATOM   460  O O   . SER A 1 62  ? 11.215 -3.468  -10.056 1.00 28.25 ? 62  SER A O   1 
ATOM   461  C CB  . SER A 1 62  ? 13.938 -2.549  -9.036  1.00 35.59 ? 62  SER A CB  1 
ATOM   462  O OG  . SER A 1 62  ? 14.155 -3.231  -7.814  1.00 42.68 ? 62  SER A OG  1 
ATOM   463  N N   . VAL A 1 63  ? 10.779 -3.112  -7.864  1.00 25.30 ? 63  VAL A N   1 
ATOM   464  C CA  . VAL A 1 63  ? 9.749  -4.193  -7.736  1.00 23.78 ? 63  VAL A CA  1 
ATOM   465  C C   . VAL A 1 63  ? 8.374  -3.626  -7.368  1.00 25.05 ? 63  VAL A C   1 
ATOM   466  O O   . VAL A 1 63  ? 7.410  -4.435  -7.330  1.00 23.91 ? 63  VAL A O   1 
ATOM   467  C CB  . VAL A 1 63  ? 10.181 -5.289  -6.737  1.00 22.95 ? 63  VAL A CB  1 
ATOM   468  C CG1 . VAL A 1 63  ? 11.577 -5.792  -7.047  1.00 21.85 ? 63  VAL A CG1 1 
ATOM   469  C CG2 . VAL A 1 63  ? 10.076 -4.839  -5.282  1.00 22.49 ? 63  VAL A CG2 1 
ATOM   470  N N   . LYS A 1 64  ? 8.270  -2.315  -7.123  1.00 27.91 ? 64  LYS A N   1 
ATOM   471  C CA  . LYS A 1 64  ? 6.986  -1.669  -6.749  1.00 32.02 ? 64  LYS A CA  1 
ATOM   472  C C   . LYS A 1 64  ? 5.949  -2.006  -7.827  1.00 30.86 ? 64  LYS A C   1 
ATOM   473  O O   . LYS A 1 64  ? 6.279  -1.888  -9.027  1.00 31.50 ? 64  LYS A O   1 
ATOM   474  C CB  . LYS A 1 64  ? 7.164  -0.161  -6.540  1.00 38.54 ? 64  LYS A CB  1 
ATOM   475  C CG  . LYS A 1 64  ? 7.151  0.275   -5.080  1.00 46.26 ? 64  LYS A CG  1 
ATOM   476  C CD  . LYS A 1 64  ? 7.096  1.776   -4.869  1.00 53.90 ? 64  LYS A CD  1 
ATOM   477  C CE  . LYS A 1 64  ? 8.449  2.445   -4.990  1.00 55.45 ? 64  LYS A CE  1 
ATOM   478  N NZ  . LYS A 1 64  ? 9.320  2.126   -3.834  1.00 55.92 ? 64  LYS A NZ  1 
ATOM   479  N N   . GLY A 1 65  ? 4.770  -2.475  -7.412  1.00 29.39 ? 65  GLY A N   1 
ATOM   480  C CA  . GLY A 1 65  ? 3.648  -2.808  -8.308  1.00 34.70 ? 65  GLY A CA  1 
ATOM   481  C C   . GLY A 1 65  ? 3.673  -4.244  -8.815  1.00 33.46 ? 65  GLY A C   1 
ATOM   482  O O   . GLY A 1 65  ? 2.651  -4.666  -9.367  1.00 36.74 ? 65  GLY A O   1 
ATOM   483  N N   . ARG A 1 66  ? 4.795  -4.966  -8.678  1.00 27.94 ? 66  ARG A N   1 
ATOM   484  C CA  . ARG A 1 66  ? 4.953  -6.354  -9.195  1.00 26.00 ? 66  ARG A CA  1 
ATOM   485  C C   . ARG A 1 66  ? 5.034  -7.371  -8.049  1.00 25.40 ? 66  ARG A C   1 
ATOM   486  O O   . ARG A 1 66  ? 4.554  -8.516  -8.227  1.00 22.87 ? 66  ARG A O   1 
ATOM   487  C CB  . ARG A 1 66  ? 6.206  -6.441  -10.066 1.00 26.96 ? 66  ARG A CB  1 
ATOM   488  C CG  . ARG A 1 66  ? 6.179  -5.498  -11.259 1.00 27.44 ? 66  ARG A CG  1 
ATOM   489  C CD  . ARG A 1 66  ? 7.313  -5.750  -12.224 1.00 24.75 ? 66  ARG A CD  1 
ATOM   490  N NE  . ARG A 1 66  ? 8.610  -5.549  -11.612 1.00 23.57 ? 66  ARG A NE  1 
ATOM   491  C CZ  . ARG A 1 66  ? 9.535  -6.492  -11.424 1.00 22.32 ? 66  ARG A CZ  1 
ATOM   492  N NH1 . ARG A 1 66  ? 10.695 -6.166  -10.877 1.00 23.02 ? 66  ARG A NH1 1 
ATOM   493  N NH2 . ARG A 1 66  ? 9.311  -7.745  -11.788 1.00 21.77 ? 66  ARG A NH2 1 
ATOM   494  N N   . PHE A 1 67  ? 5.661  -6.999  -6.931  1.00 25.31 ? 67  PHE A N   1 
ATOM   495  C CA  . PHE A 1 67  ? 5.865  -7.892  -5.760  1.00 22.77 ? 67  PHE A CA  1 
ATOM   496  C C   . PHE A 1 67  ? 4.936  -7.449  -4.625  1.00 22.37 ? 67  PHE A C   1 
ATOM   497  O O   . PHE A 1 67  ? 4.752  -6.223  -4.450  1.00 23.89 ? 67  PHE A O   1 
ATOM   498  C CB  . PHE A 1 67  ? 7.327  -7.860  -5.303  1.00 21.91 ? 67  PHE A CB  1 
ATOM   499  C CG  . PHE A 1 67  ? 8.340  -8.489  -6.231  1.00 21.26 ? 67  PHE A CG  1 
ATOM   500  C CD1 . PHE A 1 67  ? 8.032  -8.821  -7.547  1.00 22.98 ? 67  PHE A CD1 1 
ATOM   501  C CD2 . PHE A 1 67  ? 9.637  -8.710  -5.795  1.00 20.16 ? 67  PHE A CD2 1 
ATOM   502  C CE1 . PHE A 1 67  ? 8.984  -9.382  -8.385  1.00 21.88 ? 67  PHE A CE1 1 
ATOM   503  C CE2 . PHE A 1 67  ? 10.590 -9.266  -6.637  1.00 19.70 ? 67  PHE A CE2 1 
ATOM   504  C CZ  . PHE A 1 67  ? 10.265 -9.606  -7.929  1.00 21.21 ? 67  PHE A CZ  1 
ATOM   505  N N   . THR A 1 68  ? 4.393  -8.400  -3.866  1.00 20.97 ? 68  THR A N   1 
ATOM   506  C CA  . THR A 1 68  ? 3.576  -8.135  -2.649  1.00 21.55 ? 68  THR A CA  1 
ATOM   507  C C   . THR A 1 68  ? 4.126  -8.934  -1.464  1.00 19.64 ? 68  THR A C   1 
ATOM   508  O O   . THR A 1 68  ? 4.218  -10.174 -1.556  1.00 17.69 ? 68  THR A O   1 
ATOM   509  C CB  . THR A 1 68  ? 2.099  -8.491  -2.852  1.00 24.26 ? 68  THR A CB  1 
ATOM   510  O OG1 . THR A 1 68  ? 1.615  -7.721  -3.951  1.00 26.88 ? 68  THR A OG1 1 
ATOM   511  C CG2 . THR A 1 68  ? 1.260  -8.206  -1.624  1.00 27.11 ? 68  THR A CG2 1 
ATOM   512  N N   . ILE A 1 69  ? 4.420  -8.239  -0.367  1.00 19.36 ? 69  ILE A N   1 
ATOM   513  C CA  . ILE A 1 69  ? 4.850  -8.889  0.901   1.00 19.18 ? 69  ILE A CA  1 
ATOM   514  C C   . ILE A 1 69  ? 3.609  -9.098  1.766   1.00 18.32 ? 69  ILE A C   1 
ATOM   515  O O   . ILE A 1 69  ? 2.725  -8.226  1.757   1.00 21.86 ? 69  ILE A O   1 
ATOM   516  C CB  . ILE A 1 69  ? 5.957  -8.074  1.597   1.00 18.26 ? 69  ILE A CB  1 
ATOM   517  C CG1 . ILE A 1 69  ? 6.653  -8.911  2.667   1.00 16.19 ? 69  ILE A CG1 1 
ATOM   518  C CG2 . ILE A 1 69  ? 5.444  -6.751  2.145   1.00 19.90 ? 69  ILE A CG2 1 
ATOM   519  C CD1 . ILE A 1 69  ? 7.861  -8.246  3.262   1.00 17.57 ? 69  ILE A CD1 1 
ATOM   520  N N   . SER A 1 70  ? 3.530  -10.240 2.434   1.00 18.37 ? 70  SER A N   1 
ATOM   521  C CA  . SER A 1 70  ? 2.473  -10.530 3.434   1.00 18.81 ? 70  SER A CA  1 
ATOM   522  C C   . SER A 1 70  ? 3.037  -11.450 4.510   1.00 18.81 ? 70  SER A C   1 
ATOM   523  O O   . SER A 1 70  ? 4.136  -11.987 4.333   1.00 20.20 ? 70  SER A O   1 
ATOM   524  C CB  . SER A 1 70  ? 1.251  -11.122 2.782   1.00 19.79 ? 70  SER A CB  1 
ATOM   525  O OG  . SER A 1 70  ? 1.554  -12.362 2.171   1.00 19.88 ? 70  SER A OG  1 
ATOM   526  N N   . ARG A 1 71  ? 2.289  -11.616 5.594   1.00 19.52 ? 71  ARG A N   1 
ATOM   527  C CA  . ARG A 1 71  ? 2.706  -12.480 6.715   1.00 23.19 ? 71  ARG A CA  1 
ATOM   528  C C   . ARG A 1 71  ? 1.461  -13.159 7.267   1.00 24.19 ? 71  ARG A C   1 
ATOM   529  O O   . ARG A 1 71  ? 0.385  -12.557 7.201   1.00 24.35 ? 71  ARG A O   1 
ATOM   530  C CB  . ARG A 1 71  ? 3.426  -11.654 7.786   1.00 27.25 ? 71  ARG A CB  1 
ATOM   531  C CG  . ARG A 1 71  ? 2.596  -10.498 8.325   1.00 32.30 ? 71  ARG A CG  1 
ATOM   532  C CD  . ARG A 1 71  ? 3.340  -9.694  9.375   1.00 39.64 ? 71  ARG A CD  1 
ATOM   533  N NE  . ARG A 1 71  ? 2.503  -8.632  9.922   1.00 46.46 ? 71  ARG A NE  1 
ATOM   534  C CZ  . ARG A 1 71  ? 2.831  -7.857  10.952  1.00 50.98 ? 71  ARG A CZ  1 
ATOM   535  N NH1 . ARG A 1 71  ? 3.983  -8.029  11.580  1.00 56.32 ? 71  ARG A NH1 1 
ATOM   536  N NH2 . ARG A 1 71  ? 1.998  -6.917  11.359  1.00 53.74 ? 71  ARG A NH2 1 
ATOM   537  N N   . ASP A 1 72  ? 1.633  -14.383 7.756   1.00 23.70 ? 72  ASP A N   1 
ATOM   538  C CA  . ASP A 1 72  ? 0.697  -15.066 8.680   1.00 23.74 ? 72  ASP A CA  1 
ATOM   539  C C   . ASP A 1 72  ? 1.263  -14.883 10.091  1.00 24.91 ? 72  ASP A C   1 
ATOM   540  O O   . ASP A 1 72  ? 2.189  -15.639 10.438  1.00 26.43 ? 72  ASP A O   1 
ATOM   541  C CB  . ASP A 1 72  ? 0.536  -16.528 8.271   1.00 25.35 ? 72  ASP A CB  1 
ATOM   542  C CG  . ASP A 1 72  ? -0.454 -17.310 9.123   1.00 30.36 ? 72  ASP A CG  1 
ATOM   543  O OD1 . ASP A 1 72  ? -0.579 -16.992 10.316  1.00 27.81 ? 72  ASP A OD1 1 
ATOM   544  O OD2 . ASP A 1 72  ? -1.089 -18.227 8.574   1.00 42.19 ? 72  ASP A OD2 1 
ATOM   545  N N   . ASN A 1 73  ? 0.733  -13.897 10.835  1.00 24.88 ? 73  ASN A N   1 
ATOM   546  C CA  . ASN A 1 73  ? 1.217  -13.497 12.186  1.00 28.02 ? 73  ASN A CA  1 
ATOM   547  C C   . ASN A 1 73  ? 1.133  -14.698 13.129  1.00 27.71 ? 73  ASN A C   1 
ATOM   548  O O   . ASN A 1 73  ? 2.070  -14.886 13.936  1.00 30.14 ? 73  ASN A O   1 
ATOM   549  C CB  . ASN A 1 73  ? 0.401  -12.361 12.813  1.00 31.02 ? 73  ASN A CB  1 
ATOM   550  C CG  . ASN A 1 73  ? 0.702  -10.989 12.250  1.00 38.76 ? 73  ASN A CG  1 
ATOM   551  O OD1 . ASN A 1 73  ? 1.733  -10.787 11.616  1.00 46.44 ? 73  ASN A OD1 1 
ATOM   552  N ND2 . ASN A 1 73  ? -0.188 -10.037 12.486  1.00 43.14 ? 73  ASN A ND2 1 
ATOM   553  N N   . ALA A 1 74  ? 0.045  -15.466 13.029  1.00 26.45 ? 74  ALA A N   1 
ATOM   554  C CA  . ALA A 1 74  ? -0.241 -16.618 13.916  1.00 28.81 ? 74  ALA A CA  1 
ATOM   555  C C   . ALA A 1 74  ? 0.837  -17.689 13.724  1.00 30.55 ? 74  ALA A C   1 
ATOM   556  O O   . ALA A 1 74  ? 1.173  -18.359 14.718  1.00 32.43 ? 74  ALA A O   1 
ATOM   557  C CB  . ALA A 1 74  ? -1.617 -17.178 13.653  1.00 29.28 ? 74  ALA A CB  1 
ATOM   558  N N   . LYS A 1 75  ? 1.359  -17.846 12.504  1.00 28.79 ? 75  LYS A N   1 
ATOM   559  C CA  . LYS A 1 75  ? 2.315  -18.933 12.161  1.00 31.04 ? 75  LYS A CA  1 
ATOM   560  C C   . LYS A 1 75  ? 3.725  -18.369 11.958  1.00 25.82 ? 75  LYS A C   1 
ATOM   561  O O   . LYS A 1 75  ? 4.604  -19.149 11.510  1.00 29.72 ? 75  LYS A O   1 
ATOM   562  C CB  . LYS A 1 75  ? 1.813  -19.681 10.926  1.00 39.00 ? 75  LYS A CB  1 
ATOM   563  C CG  . LYS A 1 75  ? 0.725  -20.710 11.196  1.00 44.60 ? 75  LYS A CG  1 
ATOM   564  C CD  . LYS A 1 75  ? 0.067  -21.213 9.933   1.00 53.94 ? 75  LYS A CD  1 
ATOM   565  C CE  . LYS A 1 75  ? -0.548 -22.586 10.107  1.00 59.86 ? 75  LYS A CE  1 
ATOM   566  N NZ  . LYS A 1 75  ? -0.994 -23.148 8.811   1.00 64.97 ? 75  LYS A NZ  1 
ATOM   567  N N   . ASN A 1 76  ? 3.941  -17.086 12.272  1.00 21.88 ? 76  ASN A N   1 
ATOM   568  C CA  . ASN A 1 76  ? 5.263  -16.413 12.156  1.00 22.07 ? 76  ASN A CA  1 
ATOM   569  C C   . ASN A 1 76  ? 5.857  -16.731 10.779  1.00 20.78 ? 76  ASN A C   1 
ATOM   570  O O   . ASN A 1 76  ? 7.054  -17.085 10.694  1.00 21.04 ? 76  ASN A O   1 
ATOM   571  C CB  . ASN A 1 76  ? 6.215  -16.840 13.272  1.00 25.28 ? 76  ASN A CB  1 
ATOM   572  C CG  . ASN A 1 76  ? 5.702  -16.489 14.654  1.00 26.47 ? 76  ASN A CG  1 
ATOM   573  O OD1 . ASN A 1 76  ? 5.218  -15.385 14.890  1.00 29.65 ? 76  ASN A OD1 1 
ATOM   574  N ND2 . ASN A 1 76  ? 5.843  -17.413 15.587  1.00 31.57 ? 76  ASN A ND2 1 
ATOM   575  N N   . THR A 1 77  ? 5.034  -16.656 9.730   1.00 19.92 ? 77  THR A N   1 
ATOM   576  C CA  . THR A 1 77  ? 5.487  -16.978 8.353   1.00 19.93 ? 77  THR A CA  1 
ATOM   577  C C   . THR A 1 77  ? 5.393  -15.720 7.496   1.00 19.34 ? 77  THR A C   1 
ATOM   578  O O   . THR A 1 77  ? 4.412  -14.971 7.621   1.00 19.40 ? 77  THR A O   1 
ATOM   579  C CB  . THR A 1 77  ? 4.748  -18.179 7.757   1.00 23.52 ? 77  THR A CB  1 
ATOM   580  O OG1 . THR A 1 77  ? 4.965  -19.280 8.641   1.00 25.80 ? 77  THR A OG1 1 
ATOM   581  C CG2 . THR A 1 77  ? 5.237  -18.523 6.367   1.00 24.63 ? 77  THR A CG2 1 
ATOM   582  N N   . LEU A 1 78  ? 6.418  -15.520 6.676   1.00 17.34 ? 78  LEU A N   1 
ATOM   583  C CA  . LEU A 1 78  ? 6.563  -14.353 5.789   1.00 16.95 ? 78  LEU A CA  1 
ATOM   584  C C   . LEU A 1 78  ? 6.466  -14.869 4.353   1.00 15.14 ? 78  LEU A C   1 
ATOM   585  O O   . LEU A 1 78  ? 7.002  -15.951 4.072   1.00 15.45 ? 78  LEU A O   1 
ATOM   586  C CB  . LEU A 1 78  ? 7.915  -13.692 6.072   1.00 17.94 ? 78  LEU A CB  1 
ATOM   587  C CG  . LEU A 1 78  ? 8.303  -12.561 5.132   1.00 18.48 ? 78  LEU A CG  1 
ATOM   588  C CD1 . LEU A 1 78  ? 7.436  -11.338 5.343   1.00 20.88 ? 78  LEU A CD1 1 
ATOM   589  C CD2 . LEU A 1 78  ? 9.771  -12.240 5.266   1.00 20.30 ? 78  LEU A CD2 1 
ATOM   590  N N   . TYR A 1 79  ? 5.763  -14.129 3.505   1.00 15.75 ? 79  TYR A N   1 
ATOM   591  C CA  . TYR A 1 79  ? 5.561  -14.483 2.081   1.00 15.54 ? 79  TYR A CA  1 
ATOM   592  C C   . TYR A 1 79  ? 6.037  -13.351 1.178   1.00 14.65 ? 79  TYR A C   1 
ATOM   593  O O   . TYR A 1 79  ? 5.954  -12.157 1.532   1.00 15.38 ? 79  TYR A O   1 
ATOM   594  C CB  . TYR A 1 79  ? 4.091  -14.795 1.797   1.00 16.94 ? 79  TYR A CB  1 
ATOM   595  C CG  . TYR A 1 79  ? 3.500  -15.862 2.686   1.00 17.38 ? 79  TYR A CG  1 
ATOM   596  C CD1 . TYR A 1 79  ? 3.783  -17.206 2.493   1.00 18.58 ? 79  TYR A CD1 1 
ATOM   597  C CD2 . TYR A 1 79  ? 2.678  -15.521 3.747   1.00 19.43 ? 79  TYR A CD2 1 
ATOM   598  C CE1 . TYR A 1 79  ? 3.251  -18.184 3.325   1.00 20.58 ? 79  TYR A CE1 1 
ATOM   599  C CE2 . TYR A 1 79  ? 2.135  -16.483 4.579   1.00 21.47 ? 79  TYR A CE2 1 
ATOM   600  C CZ  . TYR A 1 79  ? 2.418  -17.818 4.366   1.00 20.34 ? 79  TYR A CZ  1 
ATOM   601  O OH  . TYR A 1 79  ? 1.850  -18.735 5.198   1.00 26.02 ? 79  TYR A OH  1 
ATOM   602  N N   . LEU A 1 80  ? 6.462  -13.725 -0.026  1.00 16.61 ? 80  LEU A N   1 
ATOM   603  C CA  . LEU A 1 80  ? 6.682  -12.760 -1.126  1.00 16.85 ? 80  LEU A CA  1 
ATOM   604  C C   . LEU A 1 80  ? 5.981  -13.295 -2.375  1.00 17.11 ? 80  LEU A C   1 
ATOM   605  O O   . LEU A 1 80  ? 6.399  -14.363 -2.868  1.00 17.94 ? 80  LEU A O   1 
ATOM   606  C CB  . LEU A 1 80  ? 8.183  -12.566 -1.367  1.00 17.20 ? 80  LEU A CB  1 
ATOM   607  C CG  . LEU A 1 80  ? 8.509  -11.460 -2.366  1.00 17.29 ? 80  LEU A CG  1 
ATOM   608  C CD1 . LEU A 1 80  ? 8.028  -10.109 -1.846  1.00 18.49 ? 80  LEU A CD1 1 
ATOM   609  C CD2 . LEU A 1 80  ? 9.993  -11.425 -2.681  1.00 17.72 ? 80  LEU A CD2 1 
ATOM   610  N N   . GLN A 1 81  ? 4.952  -12.584 -2.835  1.00 16.77 ? 81  GLN A N   1 
ATOM   611  C CA  . GLN A 1 81  ? 4.273  -12.882 -4.119  1.00 18.08 ? 81  GLN A CA  1 
ATOM   612  C C   . GLN A 1 81  ? 4.999  -12.086 -5.200  1.00 16.08 ? 81  GLN A C   1 
ATOM   613  O O   . GLN A 1 81  ? 5.025  -10.850 -5.120  1.00 16.80 ? 81  GLN A O   1 
ATOM   614  C CB  . GLN A 1 81  ? 2.788  -12.527 -4.088  1.00 18.78 ? 81  GLN A CB  1 
ATOM   615  C CG  . GLN A 1 81  ? 2.083  -12.797 -5.415  1.00 19.69 ? 81  GLN A CG  1 
ATOM   616  C CD  . GLN A 1 81  ? 2.042  -14.269 -5.742  1.00 22.13 ? 81  GLN A CD  1 
ATOM   617  O OE1 . GLN A 1 81  ? 1.516  -15.059 -4.958  1.00 26.44 ? 81  GLN A OE1 1 
ATOM   618  N NE2 . GLN A 1 81  ? 2.567  -14.645 -6.906  1.00 21.55 ? 81  GLN A NE2 1 
ATOM   619  N N   . MET A 1 82  ? 5.575  -12.779 -6.174  1.00 17.09 ? 82  MET A N   1 
ATOM   620  C CA  . MET A 1 82  ? 6.258  -12.151 -7.333  1.00 17.81 ? 82  MET A CA  1 
ATOM   621  C C   . MET A 1 82  ? 5.407  -12.368 -8.592  1.00 18.40 ? 82  MET A C   1 
ATOM   622  O O   . MET A 1 82  ? 4.989  -13.519 -8.848  1.00 20.06 ? 82  MET A O   1 
ATOM   623  C CB  . MET A 1 82  ? 7.652  -12.762 -7.485  1.00 19.44 ? 82  MET A CB  1 
ATOM   624  C CG  . MET A 1 82  ? 8.499  -12.606 -6.234  1.00 23.35 ? 82  MET A CG  1 
ATOM   625  S SD  . MET A 1 82  ? 10.210 -13.132 -6.529  1.00 34.29 ? 82  MET A SD  1 
ATOM   626  C CE  . MET A 1 82  ? 9.997  -14.891 -6.331  1.00 31.20 ? 82  MET A CE  1 
ATOM   627  N N   . ASN A 1 83  ? 5.087  -11.273 -9.283  1.00 18.48 ? 83  ASN A N   1 
ATOM   628  C CA  . ASN A 1 83  ? 4.377  -11.283 -10.587 1.00 20.38 ? 83  ASN A CA  1 
ATOM   629  C C   . ASN A 1 83  ? 5.210  -10.530 -11.627 1.00 20.17 ? 83  ASN A C   1 
ATOM   630  O O   . ASN A 1 83  ? 6.110  -9.765  -11.240 1.00 21.04 ? 83  ASN A O   1 
ATOM   631  C CB  . ASN A 1 83  ? 2.985  -10.661 -10.476 1.00 21.44 ? 83  ASN A CB  1 
ATOM   632  C CG  . ASN A 1 83  ? 2.065  -11.511 -9.632  1.00 21.98 ? 83  ASN A CG  1 
ATOM   633  O OD1 . ASN A 1 83  ? 1.923  -12.707 -9.889  1.00 23.82 ? 83  ASN A OD1 1 
ATOM   634  N ND2 . ASN A 1 83  ? 1.461  -10.907 -8.620  1.00 21.13 ? 83  ASN A ND2 1 
ATOM   635  N N   . SER A 1 84  ? 4.891  -10.729 -12.904 1.00 19.53 ? 84  SER A N   1 
ATOM   636  C CA  . SER A 1 84  ? 5.531  -10.020 -14.039 1.00 22.01 ? 84  SER A CA  1 
ATOM   637  C C   . SER A 1 84  ? 7.052  -10.079 -13.888 1.00 19.06 ? 84  SER A C   1 
ATOM   638  O O   . SER A 1 84  ? 7.710  -9.022  -13.979 1.00 20.78 ? 84  SER A O   1 
ATOM   639  C CB  . SER A 1 84  ? 5.054  -8.596  -14.089 1.00 23.85 ? 84  SER A CB  1 
ATOM   640  O OG  . SER A 1 84  ? 3.648  -8.546  -14.181 1.00 27.93 ? 84  SER A OG  1 
ATOM   641  N N   . LEU A 1 85  ? 7.593  -11.263 -13.629 1.00 18.82 ? 85  LEU A N   1 
ATOM   642  C CA  . LEU A 1 85  ? 9.038  -11.428 -13.345 1.00 18.35 ? 85  LEU A CA  1 
ATOM   643  C C   . LEU A 1 85  ? 9.868  -11.071 -14.586 1.00 18.96 ? 85  LEU A C   1 
ATOM   644  O O   . LEU A 1 85  ? 9.427  -11.325 -15.730 1.00 20.37 ? 85  LEU A O   1 
ATOM   645  C CB  . LEU A 1 85  ? 9.293  -12.847 -12.836 1.00 17.65 ? 85  LEU A CB  1 
ATOM   646  C CG  . LEU A 1 85  ? 9.052  -13.001 -11.335 1.00 17.72 ? 85  LEU A CG  1 
ATOM   647  C CD1 . LEU A 1 85  ? 8.941  -14.459 -10.945 1.00 20.20 ? 85  LEU A CD1 1 
ATOM   648  C CD2 . LEU A 1 85  ? 10.152 -12.319 -10.534 1.00 19.67 ? 85  LEU A CD2 1 
ATOM   649  N N   . ARG A 1 86  ? 11.000 -10.422 -14.354 1.00 18.57 ? 86  ARG A N   1 
ATOM   650  C CA  . ARG A 1 86  ? 11.938 -9.962  -15.410 1.00 19.82 ? 86  ARG A CA  1 
ATOM   651  C C   . ARG A 1 86  ? 13.275 -10.657 -15.217 1.00 19.61 ? 86  ARG A C   1 
ATOM   652  O O   . ARG A 1 86  ? 13.612 -11.057 -14.104 1.00 16.94 ? 86  ARG A O   1 
ATOM   653  C CB  . ARG A 1 86  ? 12.149 -8.453  -15.315 1.00 22.35 ? 86  ARG A CB  1 
ATOM   654  C CG  . ARG A 1 86  ? 10.876 -7.628  -15.373 1.00 25.12 ? 86  ARG A CG  1 
ATOM   655  C CD  . ARG A 1 86  ? 11.180 -6.227  -14.886 1.00 28.76 ? 86  ARG A CD  1 
ATOM   656  N NE  . ARG A 1 86  ? 10.053 -5.325  -15.013 1.00 32.48 ? 86  ARG A NE  1 
ATOM   657  C CZ  . ARG A 1 86  ? 10.036 -4.065  -14.584 1.00 35.01 ? 86  ARG A CZ  1 
ATOM   658  N NH1 . ARG A 1 86  ? 11.095 -3.532  -13.994 1.00 39.43 ? 86  ARG A NH1 1 
ATOM   659  N NH2 . ARG A 1 86  ? 8.957  -3.328  -14.768 1.00 38.19 ? 86  ARG A NH2 1 
ATOM   660  N N   . PRO A 1 87  ? 14.071 -10.838 -16.292 1.00 20.11 ? 87  PRO A N   1 
ATOM   661  C CA  . PRO A 1 87  ? 15.407 -11.418 -16.155 1.00 20.56 ? 87  PRO A CA  1 
ATOM   662  C C   . PRO A 1 87  ? 16.235 -10.768 -15.032 1.00 20.01 ? 87  PRO A C   1 
ATOM   663  O O   . PRO A 1 87  ? 16.944 -11.486 -14.354 1.00 20.50 ? 87  PRO A O   1 
ATOM   664  C CB  . PRO A 1 87  ? 16.011 -11.161 -17.541 1.00 21.74 ? 87  PRO A CB  1 
ATOM   665  C CG  . PRO A 1 87  ? 14.816 -11.253 -18.462 1.00 22.52 ? 87  PRO A CG  1 
ATOM   666  C CD  . PRO A 1 87  ? 13.721 -10.548 -17.694 1.00 22.77 ? 87  PRO A CD  1 
ATOM   667  N N   . GLU A 1 88  ? 16.114 -9.451  -14.854 1.00 20.53 ? 88  GLU A N   1 
ATOM   668  C CA  . GLU A 1 88  ? 16.905 -8.668  -13.869 1.00 23.01 ? 88  GLU A CA  1 
ATOM   669  C C   . GLU A 1 88  ? 16.454 -8.981  -12.437 1.00 20.19 ? 88  GLU A C   1 
ATOM   670  O O   . GLU A 1 88  ? 17.158 -8.542  -11.514 1.00 21.78 ? 88  GLU A O   1 
ATOM   671  C CB  . GLU A 1 88  ? 16.840 -7.164  -14.132 1.00 26.43 ? 88  GLU A CB  1 
ATOM   672  C CG  . GLU A 1 88  ? 15.444 -6.581  -14.120 1.00 32.18 ? 88  GLU A CG  1 
ATOM   673  C CD  . GLU A 1 88  ? 14.838 -6.386  -15.503 1.00 39.71 ? 88  GLU A CD  1 
ATOM   674  O OE1 . GLU A 1 88  ? 14.075 -5.404  -15.666 1.00 45.72 ? 88  GLU A OE1 1 
ATOM   675  O OE2 . GLU A 1 88  ? 15.132 -7.216  -16.423 1.00 38.65 ? 88  GLU A OE2 1 
ATOM   676  N N   . ASP A 1 89  ? 15.366 -9.732  -12.254 1.00 18.91 ? 89  ASP A N   1 
ATOM   677  C CA  . ASP A 1 89  ? 14.916 -10.217 -10.922 1.00 17.65 ? 89  ASP A CA  1 
ATOM   678  C C   . ASP A 1 89  ? 15.693 -11.479 -10.523 1.00 16.40 ? 89  ASP A C   1 
ATOM   679  O O   . ASP A 1 89  ? 15.513 -11.947 -9.383  1.00 17.58 ? 89  ASP A O   1 
ATOM   680  C CB  . ASP A 1 89  ? 13.412 -10.501 -10.908 1.00 17.15 ? 89  ASP A CB  1 
ATOM   681  C CG  . ASP A 1 89  ? 12.560 -9.255  -11.066 1.00 18.08 ? 89  ASP A CG  1 
ATOM   682  O OD1 . ASP A 1 89  ? 12.899 -8.224  -10.449 1.00 19.06 ? 89  ASP A OD1 1 
ATOM   683  O OD2 . ASP A 1 89  ? 11.562 -9.325  -11.807 1.00 21.77 ? 89  ASP A OD2 1 
ATOM   684  N N   . THR A 1 90  ? 16.493 -12.045 -11.425 1.00 17.15 ? 90  THR A N   1 
ATOM   685  C CA  . THR A 1 90  ? 17.315 -13.248 -11.141 1.00 16.21 ? 90  THR A CA  1 
ATOM   686  C C   . THR A 1 90  ? 18.257 -12.926 -9.985  1.00 16.92 ? 90  THR A C   1 
ATOM   687  O O   . THR A 1 90  ? 18.986 -11.912 -10.065 1.00 17.89 ? 90  THR A O   1 
ATOM   688  C CB  . THR A 1 90  ? 18.125 -13.696 -12.359 1.00 18.56 ? 90  THR A CB  1 
ATOM   689  O OG1 . THR A 1 90  ? 17.189 -14.085 -13.359 1.00 17.62 ? 90  THR A OG1 1 
ATOM   690  C CG2 . THR A 1 90  ? 19.053 -14.848 -12.064 1.00 19.38 ? 90  THR A CG2 1 
ATOM   691  N N   . ALA A 1 91  ? 18.209 -13.724 -8.925  1.00 16.26 ? 91  ALA A N   1 
ATOM   692  C CA  . ALA A 1 91  ? 18.938 -13.418 -7.679  1.00 16.75 ? 91  ALA A CA  1 
ATOM   693  C C   . ALA A 1 91  ? 18.740 -14.540 -6.676  1.00 16.13 ? 91  ALA A C   1 
ATOM   694  O O   . ALA A 1 91  ? 17.818 -15.359 -6.838  1.00 15.12 ? 91  ALA A O   1 
ATOM   695  C CB  . ALA A 1 91  ? 18.465 -12.096 -7.103  1.00 18.75 ? 91  ALA A CB  1 
ATOM   696  N N   . VAL A 1 92  ? 19.591 -14.550 -5.653  1.00 15.05 ? 92  VAL A N   1 
ATOM   697  C CA  . VAL A 1 92  ? 19.313 -15.334 -4.427  1.00 14.72 ? 92  VAL A CA  1 
ATOM   698  C C   . VAL A 1 92  ? 18.478 -14.438 -3.518  1.00 13.74 ? 92  VAL A C   1 
ATOM   699  O O   . VAL A 1 92  ? 18.905 -13.309 -3.233  1.00 13.10 ? 92  VAL A O   1 
ATOM   700  C CB  . VAL A 1 92  ? 20.595 -15.846 -3.755  1.00 17.48 ? 92  VAL A CB  1 
ATOM   701  C CG1 . VAL A 1 92  ? 20.294 -16.532 -2.438  1.00 17.21 ? 92  VAL A CG1 1 
ATOM   702  C CG2 . VAL A 1 92  ? 21.355 -16.779 -4.676  1.00 17.76 ? 92  VAL A CG2 1 
ATOM   703  N N   . TYR A 1 93  ? 17.317 -14.940 -3.105  1.00 14.79 ? 93  TYR A N   1 
ATOM   704  C CA  . TYR A 1 93  ? 16.374 -14.221 -2.225  1.00 13.62 ? 93  TYR A CA  1 
ATOM   705  C C   . TYR A 1 93  ? 16.542 -14.740 -0.801  1.00 13.52 ? 93  TYR A C   1 
ATOM   706  O O   . TYR A 1 93  ? 16.540 -15.961 -0.602  1.00 13.22 ? 93  TYR A O   1 
ATOM   707  C CB  . TYR A 1 93  ? 14.946 -14.373 -2.742  1.00 14.04 ? 93  TYR A CB  1 
ATOM   708  C CG  . TYR A 1 93  ? 14.688 -13.538 -3.970  1.00 14.38 ? 93  TYR A CG  1 
ATOM   709  C CD1 . TYR A 1 93  ? 15.185 -13.919 -5.208  1.00 15.28 ? 93  TYR A CD1 1 
ATOM   710  C CD2 . TYR A 1 93  ? 13.992 -12.343 -3.886  1.00 14.74 ? 93  TYR A CD2 1 
ATOM   711  C CE1 . TYR A 1 93  ? 14.974 -13.138 -6.333  1.00 16.21 ? 93  TYR A CE1 1 
ATOM   712  C CE2 . TYR A 1 93  ? 13.776 -11.551 -5.001  1.00 15.73 ? 93  TYR A CE2 1 
ATOM   713  C CZ  . TYR A 1 93  ? 14.281 -11.943 -6.230  1.00 16.26 ? 93  TYR A CZ  1 
ATOM   714  O OH  . TYR A 1 93  ? 14.073 -11.139 -7.321  1.00 16.74 ? 93  TYR A OH  1 
ATOM   715  N N   . TYR A 1 94  ? 16.648 -13.817 0.153   1.00 13.79 ? 94  TYR A N   1 
ATOM   716  C CA  . TYR A 1 94  ? 16.815 -14.117 1.598   1.00 13.84 ? 94  TYR A CA  1 
ATOM   717  C C   . TYR A 1 94  ? 15.655 -13.498 2.360   1.00 13.57 ? 94  TYR A C   1 
ATOM   718  O O   . TYR A 1 94  ? 15.227 -12.373 2.016   1.00 16.40 ? 94  TYR A O   1 
ATOM   719  C CB  . TYR A 1 94  ? 18.093 -13.487 2.160   1.00 15.58 ? 94  TYR A CB  1 
ATOM   720  C CG  . TYR A 1 94  ? 19.351 -13.820 1.404   1.00 17.91 ? 94  TYR A CG  1 
ATOM   721  C CD1 . TYR A 1 94  ? 19.771 -12.994 0.380   1.00 17.53 ? 94  TYR A CD1 1 
ATOM   722  C CD2 . TYR A 1 94  ? 20.120 -14.932 1.709   1.00 17.11 ? 94  TYR A CD2 1 
ATOM   723  C CE1 . TYR A 1 94  ? 20.933 -13.247 -0.319  1.00 19.96 ? 94  TYR A CE1 1 
ATOM   724  C CE2 . TYR A 1 94  ? 21.293 -15.198 1.019   1.00 20.41 ? 94  TYR A CE2 1 
ATOM   725  C CZ  . TYR A 1 94  ? 21.693 -14.357 -0.006  1.00 19.89 ? 94  TYR A CZ  1 
ATOM   726  O OH  . TYR A 1 94  ? 22.838 -14.568 -0.716  1.00 23.40 ? 94  TYR A OH  1 
ATOM   727  N N   . CYS A 1 95  ? 15.205 -14.160 3.410   1.00 12.63 ? 95  CYS A N   1 
ATOM   728  C CA  . CYS A 1 95  ? 14.353 -13.503 4.422   1.00 13.21 ? 95  CYS A CA  1 
ATOM   729  C C   . CYS A 1 95  ? 15.187 -13.198 5.664   1.00 13.51 ? 95  CYS A C   1 
ATOM   730  O O   . CYS A 1 95  ? 16.185 -13.898 5.925   1.00 13.70 ? 95  CYS A O   1 
ATOM   731  C CB  . CYS A 1 95  ? 13.144 -14.350 4.756   1.00 16.84 ? 95  CYS A CB  1 
ATOM   732  S SG  . CYS A 1 95  ? 13.580 -16.000 5.336   1.00 21.22 ? 95  CYS A SG  1 
ATOM   733  N N   . ALA A 1 96  ? 14.820 -12.141 6.378   1.00 14.32 ? 96  ALA A N   1 
ATOM   734  C CA  . ALA A 1 96  ? 15.397 -11.834 7.704   1.00 13.39 ? 96  ALA A CA  1 
ATOM   735  C C   . ALA A 1 96  ? 14.278 -11.398 8.644   1.00 12.87 ? 96  ALA A C   1 
ATOM   736  O O   . ALA A 1 96  ? 13.350 -10.711 8.188   1.00 15.06 ? 96  ALA A O   1 
ATOM   737  C CB  . ALA A 1 96  ? 16.478 -10.801 7.586   1.00 14.53 ? 96  ALA A CB  1 
ATOM   738  N N   . PHE A 1 97  ? 14.369 -11.812 9.906   1.00 13.54 ? 97  PHE A N   1 
ATOM   739  C CA  . PHE A 1 97  ? 13.486 -11.351 11.002  1.00 14.44 ? 97  PHE A CA  1 
ATOM   740  C C   . PHE A 1 97  ? 14.365 -10.650 12.030  1.00 14.60 ? 97  PHE A C   1 
ATOM   741  O O   . PHE A 1 97  ? 15.459 -11.177 12.333  1.00 15.64 ? 97  PHE A O   1 
ATOM   742  C CB  . PHE A 1 97  ? 12.764 -12.503 11.710  1.00 14.52 ? 97  PHE A CB  1 
ATOM   743  C CG  . PHE A 1 97  ? 11.621 -13.176 10.996  1.00 16.81 ? 97  PHE A CG  1 
ATOM   744  C CD1 . PHE A 1 97  ? 11.529 -13.214 9.613   1.00 17.15 ? 97  PHE A CD1 1 
ATOM   745  C CD2 . PHE A 1 97  ? 10.659 -13.843 11.739  1.00 17.67 ? 97  PHE A CD2 1 
ATOM   746  C CE1 . PHE A 1 97  ? 10.499 -13.913 8.998   1.00 19.13 ? 97  PHE A CE1 1 
ATOM   747  C CE2 . PHE A 1 97  ? 9.620  -14.519 11.121  1.00 18.61 ? 97  PHE A CE2 1 
ATOM   748  C CZ  . PHE A 1 97  ? 9.544  -14.558 9.752   1.00 18.79 ? 97  PHE A CZ  1 
ATOM   749  N N   . ILE A 1 98  ? 13.900 -9.525  12.570  1.00 15.19 ? 98  ILE A N   1 
ATOM   750  C CA  . ILE A 1 98  ? 14.460 -8.962  13.827  1.00 15.18 ? 98  ILE A CA  1 
ATOM   751  C C   . ILE A 1 98  ? 13.488 -9.314  14.953  1.00 15.23 ? 98  ILE A C   1 
ATOM   752  O O   . ILE A 1 98  ? 12.287 -9.008  14.813  1.00 16.02 ? 98  ILE A O   1 
ATOM   753  C CB  . ILE A 1 98  ? 14.744 -7.451  13.736  1.00 16.33 ? 98  ILE A CB  1 
ATOM   754  C CG1 . ILE A 1 98  ? 15.833 -7.156  12.701  1.00 17.49 ? 98  ILE A CG1 1 
ATOM   755  C CG2 . ILE A 1 98  ? 15.124 -6.910  15.101  1.00 17.19 ? 98  ILE A CG2 1 
ATOM   756  C CD1 . ILE A 1 98  ? 16.074 -5.696  12.463  1.00 19.48 ? 98  ILE A CD1 1 
ATOM   757  N N   . THR A 1 99  ? 14.000 -9.954  16.004  1.00 16.78 ? 99  THR A N   1 
ATOM   758  C CA  . THR A 1 99  ? 13.198 -10.280 17.207  1.00 18.59 ? 99  THR A CA  1 
ATOM   759  C C   . THR A 1 99  ? 13.812 -9.601  18.427  1.00 20.86 ? 99  THR A C   1 
ATOM   760  O O   . THR A 1 99  ? 15.037 -9.341  18.423  1.00 19.93 ? 99  THR A O   1 
ATOM   761  C CB  . THR A 1 99  ? 13.054 -11.794 17.403  1.00 21.37 ? 99  THR A CB  1 
ATOM   762  O OG1 . THR A 1 99  ? 14.312 -12.329 17.811  1.00 20.70 ? 99  THR A OG1 1 
ATOM   763  C CG2 . THR A 1 99  ? 12.573 -12.504 16.156  1.00 22.31 ? 99  THR A CG2 1 
ATOM   764  N N   . THR A 1 100 ? 12.952 -9.346  19.413  1.00 21.85 ? 100 THR A N   1 
ATOM   765  C CA  A THR A 1 100 ? 13.297 -8.706  20.705  0.50 23.39 ? 100 THR A CA  1 
ATOM   766  C CA  B THR A 1 100 ? 13.323 -8.740  20.715  0.50 23.03 ? 100 THR A CA  1 
ATOM   767  C C   . THR A 1 100 ? 12.485 -9.395  21.811  1.00 24.11 ? 100 THR A C   1 
ATOM   768  O O   . THR A 1 100 ? 11.347 -9.818  21.528  1.00 22.88 ? 100 THR A O   1 
ATOM   769  C CB  A THR A 1 100 ? 13.056 -7.190  20.615  0.50 25.06 ? 100 THR A CB  1 
ATOM   770  C CB  B THR A 1 100 ? 13.112 -7.220  20.747  0.50 25.91 ? 100 THR A CB  1 
ATOM   771  O OG1 A THR A 1 100 ? 13.746 -6.561  21.690  0.50 27.46 ? 100 THR A OG1 1 
ATOM   772  O OG1 B THR A 1 100 ? 11.785 -6.942  20.299  0.50 28.61 ? 100 THR A OG1 1 
ATOM   773  C CG2 A THR A 1 100 ? 11.593 -6.805  20.640  0.50 26.21 ? 100 THR A CG2 1 
ATOM   774  C CG2 B THR A 1 100 ? 14.113 -6.457  19.908  0.50 26.31 ? 100 THR A CG2 1 
ATOM   775  N N   . GLU A 1 101 ? 13.038 -9.472  23.019  1.00 27.44 ? 101 GLU A N   1 
ATOM   776  C CA  . GLU A 1 101 ? 12.305 -9.971  24.213  1.00 30.50 ? 101 GLU A CA  1 
ATOM   777  C C   . GLU A 1 101 ? 11.846 -8.770  25.049  1.00 34.12 ? 101 GLU A C   1 
ATOM   778  O O   . GLU A 1 101 ? 10.958 -8.978  25.879  1.00 40.47 ? 101 GLU A O   1 
ATOM   779  C CB  . GLU A 1 101 ? 13.160 -10.966 25.004  1.00 34.89 ? 101 GLU A CB  1 
ATOM   780  C CG  . GLU A 1 101 ? 12.373 -11.746 26.039  1.00 37.08 ? 101 GLU A CG  1 
ATOM   781  C CD  . GLU A 1 101 ? 13.125 -12.897 26.683  1.00 40.52 ? 101 GLU A CD  1 
ATOM   782  O OE1 . GLU A 1 101 ? 13.937 -13.537 25.988  1.00 43.16 ? 101 GLU A OE1 1 
ATOM   783  O OE2 . GLU A 1 101 ? 12.898 -13.154 27.886  1.00 49.05 ? 101 GLU A OE2 1 
ATOM   784  N N   . SER A 1 102 ? 12.402 -7.566  24.827  1.00 35.18 ? 102 SER A N   1 
ATOM   785  C CA  . SER A 1 102 ? 11.948 -6.292  25.452  1.00 37.62 ? 102 SER A CA  1 
ATOM   786  C C   . SER A 1 102 ? 12.555 -5.072  24.745  1.00 34.16 ? 102 SER A C   1 
ATOM   787  O O   . SER A 1 102 ? 13.551 -5.231  24.010  1.00 33.21 ? 102 SER A O   1 
ATOM   788  C CB  . SER A 1 102 ? 12.273 -6.264  26.927  1.00 42.39 ? 102 SER A CB  1 
ATOM   789  O OG  . SER A 1 102 ? 13.682 -6.258  27.140  1.00 37.00 ? 102 SER A OG  1 
ATOM   790  N N   . ASP A 1 103 ? 11.991 -3.888  25.005  1.00 33.26 ? 103 ASP A N   1 
ATOM   791  C CA  . ASP A 1 103 ? 12.468 -2.590  24.462  1.00 33.53 ? 103 ASP A CA  1 
ATOM   792  C C   . ASP A 1 103 ? 13.849 -2.256  25.036  1.00 27.18 ? 103 ASP A C   1 
ATOM   793  O O   . ASP A 1 103 ? 14.525 -1.392  24.446  1.00 30.21 ? 103 ASP A O   1 
ATOM   794  C CB  . ASP A 1 103 ? 11.471 -1.463  24.734  1.00 41.36 ? 103 ASP A CB  1 
ATOM   795  C CG  . ASP A 1 103 ? 10.273 -1.450  23.801  1.00 49.22 ? 103 ASP A CG  1 
ATOM   796  O OD1 . ASP A 1 103 ? 10.296 -2.178  22.786  1.00 56.45 ? 103 ASP A OD1 1 
ATOM   797  O OD2 . ASP A 1 103 ? 9.328  -0.707  24.100  1.00 61.93 ? 103 ASP A OD2 1 
ATOM   798  N N   . TYR A 1 104 ? 14.280 -2.938  26.102  1.00 24.22 ? 104 TYR A N   1 
ATOM   799  C CA  . TYR A 1 104 ? 15.591 -2.711  26.753  1.00 23.14 ? 104 TYR A CA  1 
ATOM   800  C C   . TYR A 1 104 ? 16.702 -3.530  26.084  1.00 24.08 ? 104 TYR A C   1 
ATOM   801  O O   . TYR A 1 104 ? 17.874 -3.315  26.447  1.00 24.26 ? 104 TYR A O   1 
ATOM   802  C CB  . TYR A 1 104 ? 15.474 -2.996  28.249  1.00 22.08 ? 104 TYR A CB  1 
ATOM   803  C CG  . TYR A 1 104 ? 14.653 -1.959  28.964  1.00 22.03 ? 104 TYR A CG  1 
ATOM   804  C CD1 . TYR A 1 104 ? 15.265 -0.896  29.600  1.00 24.43 ? 104 TYR A CD1 1 
ATOM   805  C CD2 . TYR A 1 104 ? 13.268 -2.003  28.968  1.00 24.22 ? 104 TYR A CD2 1 
ATOM   806  C CE1 . TYR A 1 104 ? 14.527 0.065   30.273  1.00 26.78 ? 104 TYR A CE1 1 
ATOM   807  C CE2 . TYR A 1 104 ? 12.515 -1.039  29.618  1.00 24.10 ? 104 TYR A CE2 1 
ATOM   808  C CZ  . TYR A 1 104 ? 13.144 0.002   30.272  1.00 24.65 ? 104 TYR A CZ  1 
ATOM   809  O OH  . TYR A 1 104 ? 12.400 0.949   30.921  1.00 26.67 ? 104 TYR A OH  1 
ATOM   810  N N   . ASP A 1 105 ? 16.366 -4.425  25.149  1.00 25.00 ? 105 ASP A N   1 
ATOM   811  C CA  . ASP A 1 105 ? 17.391 -5.152  24.359  1.00 24.27 ? 105 ASP A CA  1 
ATOM   812  C C   . ASP A 1 105 ? 17.459 -4.569  22.945  1.00 23.25 ? 105 ASP A C   1 
ATOM   813  O O   . ASP A 1 105 ? 16.498 -3.928  22.484  1.00 23.43 ? 105 ASP A O   1 
ATOM   814  C CB  . ASP A 1 105 ? 17.182 -6.667  24.397  1.00 27.55 ? 105 ASP A CB  1 
ATOM   815  C CG  . ASP A 1 105 ? 15.973 -7.163  23.636  1.00 31.64 ? 105 ASP A CG  1 
ATOM   816  O OD1 . ASP A 1 105 ? 15.005 -7.595  24.301  1.00 36.98 ? 105 ASP A OD1 1 
ATOM   817  O OD2 . ASP A 1 105 ? 16.018 -7.141  22.389  1.00 36.52 ? 105 ASP A OD2 1 
ATOM   818  N N   . LEU A 1 106 ? 18.597 -4.777  22.291  1.00 22.21 ? 106 LEU A N   1 
ATOM   819  C CA  . LEU A 1 106 ? 18.900 -4.220  20.948  1.00 23.12 ? 106 LEU A CA  1 
ATOM   820  C C   . LEU A 1 106 ? 18.277 -5.075  19.843  1.00 23.06 ? 106 LEU A C   1 
ATOM   821  O O   . LEU A 1 106 ? 18.324 -4.646  18.683  1.00 22.63 ? 106 LEU A O   1 
ATOM   822  C CB  . LEU A 1 106 ? 20.419 -4.139  20.788  1.00 23.79 ? 106 LEU A CB  1 
ATOM   823  C CG  . LEU A 1 106 ? 21.129 -3.232  21.795  1.00 25.47 ? 106 LEU A CG  1 
ATOM   824  C CD1 . LEU A 1 106 ? 22.540 -2.921  21.332  1.00 26.94 ? 106 LEU A CD1 1 
ATOM   825  C CD2 . LEU A 1 106 ? 20.342 -1.947  22.038  1.00 28.22 ? 106 LEU A CD2 1 
ATOM   826  N N   . GLY A 1 107 ? 17.752 -6.244  20.177  1.00 25.97 ? 107 GLY A N   1 
ATOM   827  C CA  . GLY A 1 107 ? 17.178 -7.162  19.183  1.00 23.78 ? 107 GLY A CA  1 
ATOM   828  C C   . GLY A 1 107 ? 18.249 -8.000  18.525  1.00 23.27 ? 107 GLY A C   1 
ATOM   829  O O   . GLY A 1 107 ? 19.452 -7.718  18.707  1.00 22.76 ? 107 GLY A O   1 
ATOM   830  N N   . ARG A 1 108 ? 17.825 -9.059  17.845  1.00 20.95 ? 108 ARG A N   1 
ATOM   831  C CA  . ARG A 1 108 ? 18.723 -9.960  17.090  1.00 22.44 ? 108 ARG A CA  1 
ATOM   832  C C   . ARG A 1 108 ? 18.127 -10.103 15.693  1.00 18.86 ? 108 ARG A C   1 
ATOM   833  O O   . ARG A 1 108 ? 16.898 -10.130 15.582  1.00 20.61 ? 108 ARG A O   1 
ATOM   834  C CB  . ARG A 1 108 ? 18.853 -11.320 17.781  1.00 25.15 ? 108 ARG A CB  1 
ATOM   835  C CG  . ARG A 1 108 ? 19.478 -11.267 19.165  1.00 28.07 ? 108 ARG A CG  1 
ATOM   836  C CD  . ARG A 1 108 ? 20.944 -10.888 19.120  1.00 30.77 ? 108 ARG A CD  1 
ATOM   837  N NE  . ARG A 1 108 ? 21.537 -10.893 20.453  1.00 34.28 ? 108 ARG A NE  1 
ATOM   838  C CZ  . ARG A 1 108 ? 21.426 -9.911  21.351  1.00 36.10 ? 108 ARG A CZ  1 
ATOM   839  N NH1 . ARG A 1 108 ? 20.729 -8.818  21.088  1.00 33.47 ? 108 ARG A NH1 1 
ATOM   840  N NH2 . ARG A 1 108 ? 22.019 -10.028 22.524  1.00 37.15 ? 108 ARG A NH2 1 
ATOM   841  N N   . ARG A 1 109 ? 18.980 -10.176 14.672  1.00 17.34 ? 109 ARG A N   1 
ATOM   842  C CA  . ARG A 1 109 ? 18.541 -10.469 13.292  1.00 17.25 ? 109 ARG A CA  1 
ATOM   843  C C   . ARG A 1 109 ? 18.877 -11.925 12.970  1.00 17.57 ? 109 ARG A C   1 
ATOM   844  O O   . ARG A 1 109 ? 20.020 -12.347 13.217  1.00 18.45 ? 109 ARG A O   1 
ATOM   845  C CB  . ARG A 1 109 ? 19.177 -9.520  12.278  1.00 17.01 ? 109 ARG A CB  1 
ATOM   846  C CG  . ARG A 1 109 ? 18.549 -9.650  10.897  1.00 17.45 ? 109 ARG A CG  1 
ATOM   847  C CD  . ARG A 1 109 ? 19.159 -8.753  9.859   1.00 18.04 ? 109 ARG A CD  1 
ATOM   848  N NE  . ARG A 1 109 ? 18.934 -7.339  10.096  1.00 17.08 ? 109 ARG A NE  1 
ATOM   849  C CZ  . ARG A 1 109 ? 19.822 -6.477  10.594  1.00 17.32 ? 109 ARG A CZ  1 
ATOM   850  N NH1 . ARG A 1 109 ? 21.036 -6.863  10.969  1.00 17.29 ? 109 ARG A NH1 1 
ATOM   851  N NH2 . ARG A 1 109 ? 19.480 -5.210  10.720  1.00 18.05 ? 109 ARG A NH2 1 
ATOM   852  N N   . TYR A 1 110 ? 17.898 -12.649 12.433  1.00 15.81 ? 110 TYR A N   1 
ATOM   853  C CA  . TYR A 1 110 ? 18.027 -14.040 11.944  1.00 16.65 ? 110 TYR A CA  1 
ATOM   854  C C   . TYR A 1 110 ? 17.785 -14.050 10.437  1.00 15.20 ? 110 TYR A C   1 
ATOM   855  O O   . TYR A 1 110 ? 16.942 -13.266 9.960   1.00 12.96 ? 110 TYR A O   1 
ATOM   856  C CB  . TYR A 1 110 ? 17.055 -14.943 12.693  1.00 17.04 ? 110 TYR A CB  1 
ATOM   857  C CG  . TYR A 1 110 ? 17.352 -14.956 14.167  1.00 20.00 ? 110 TYR A CG  1 
ATOM   858  C CD1 . TYR A 1 110 ? 18.423 -15.688 14.663  1.00 21.18 ? 110 TYR A CD1 1 
ATOM   859  C CD2 . TYR A 1 110 ? 16.633 -14.165 15.044  1.00 21.51 ? 110 TYR A CD2 1 
ATOM   860  C CE1 . TYR A 1 110 ? 18.737 -15.674 16.010  1.00 24.71 ? 110 TYR A CE1 1 
ATOM   861  C CE2 . TYR A 1 110 ? 16.941 -14.134 16.395  1.00 22.92 ? 110 TYR A CE2 1 
ATOM   862  C CZ  . TYR A 1 110 ? 17.989 -14.899 16.876  1.00 24.15 ? 110 TYR A CZ  1 
ATOM   863  O OH  . TYR A 1 110 ? 18.300 -14.879 18.203  1.00 30.42 ? 110 TYR A OH  1 
ATOM   864  N N   . TRP A 1 111 ? 18.534 -14.891 9.725   1.00 15.32 ? 111 TRP A N   1 
ATOM   865  C CA  . TRP A 1 111 ? 18.520 -14.980 8.245   1.00 15.08 ? 111 TRP A CA  1 
ATOM   866  C C   . TRP A 1 111 ? 18.096 -16.369 7.787   1.00 15.00 ? 111 TRP A C   1 
ATOM   867  O O   . TRP A 1 111 ? 18.576 -17.367 8.355   1.00 14.30 ? 111 TRP A O   1 
ATOM   868  C CB  . TRP A 1 111 ? 19.902 -14.665 7.682   1.00 14.98 ? 111 TRP A CB  1 
ATOM   869  C CG  . TRP A 1 111 ? 20.290 -13.233 7.812   1.00 15.17 ? 111 TRP A CG  1 
ATOM   870  C CD1 . TRP A 1 111 ? 20.977 -12.643 8.833   1.00 16.16 ? 111 TRP A CD1 1 
ATOM   871  C CD2 . TRP A 1 111 ? 20.024 -12.205 6.850   1.00 14.78 ? 111 TRP A CD2 1 
ATOM   872  N NE1 . TRP A 1 111 ? 21.145 -11.315 8.576   1.00 17.67 ? 111 TRP A NE1 1 
ATOM   873  C CE2 . TRP A 1 111 ? 20.576 -11.013 7.364   1.00 16.36 ? 111 TRP A CE2 1 
ATOM   874  C CE3 . TRP A 1 111 ? 19.381 -12.184 5.609   1.00 15.18 ? 111 TRP A CE3 1 
ATOM   875  C CZ2 . TRP A 1 111 ? 20.489 -9.804  6.678   1.00 16.74 ? 111 TRP A CZ2 1 
ATOM   876  C CZ3 . TRP A 1 111 ? 19.305 -10.991 4.931   1.00 15.97 ? 111 TRP A CZ3 1 
ATOM   877  C CH2 . TRP A 1 111 ? 19.863 -9.824  5.453   1.00 16.13 ? 111 TRP A CH2 1 
ATOM   878  N N   . GLY A 1 112 ? 17.306 -16.414 6.717   1.00 14.07 ? 112 GLY A N   1 
ATOM   879  C CA  . GLY A 1 112 ? 17.157 -17.618 5.900   1.00 14.70 ? 112 GLY A CA  1 
ATOM   880  C C   . GLY A 1 112 ? 18.443 -17.859 5.117   1.00 15.57 ? 112 GLY A C   1 
ATOM   881  O O   . GLY A 1 112 ? 19.286 -16.939 5.007   1.00 17.02 ? 112 GLY A O   1 
ATOM   882  N N   . GLN A 1 113 ? 18.599 -19.063 4.587   1.00 17.13 ? 113 GLN A N   1 
ATOM   883  C CA  . GLN A 1 113 ? 19.853 -19.497 3.923   1.00 16.95 ? 113 GLN A CA  1 
ATOM   884  C C   . GLN A 1 113 ? 19.918 -18.924 2.508   1.00 16.67 ? 113 GLN A C   1 
ATOM   885  O O   . GLN A 1 113 ? 21.033 -18.886 1.951   1.00 17.43 ? 113 GLN A O   1 
ATOM   886  C CB  . GLN A 1 113 ? 19.952 -21.022 3.918   1.00 18.82 ? 113 GLN A CB  1 
ATOM   887  C CG  . GLN A 1 113 ? 19.978 -21.609 5.323   1.00 19.30 ? 113 GLN A CG  1 
ATOM   888  C CD  . GLN A 1 113 ? 20.267 -23.087 5.335   1.00 21.20 ? 113 GLN A CD  1 
ATOM   889  O OE1 . GLN A 1 113 ? 19.893 -23.814 4.414   1.00 21.72 ? 113 GLN A OE1 1 
ATOM   890  N NE2 . GLN A 1 113 ? 20.940 -23.536 6.389   1.00 20.38 ? 113 GLN A NE2 1 
ATOM   891  N N   . GLY A 1 114 ? 18.783 -18.486 1.960   1.00 18.29 ? 114 GLY A N   1 
ATOM   892  C CA  . GLY A 1 114 ? 18.718 -18.005 0.572   1.00 17.65 ? 114 GLY A CA  1 
ATOM   893  C C   . GLY A 1 114 ? 18.165 -19.045 -0.377  1.00 18.56 ? 114 GLY A C   1 
ATOM   894  O O   . GLY A 1 114 ? 18.426 -20.232 -0.183  1.00 19.53 ? 114 GLY A O   1 
ATOM   895  N N   . THR A 1 115 ? 17.405 -18.600 -1.381  1.00 18.19 ? 115 THR A N   1 
ATOM   896  C CA  . THR A 1 115 ? 16.882 -19.479 -2.454  1.00 20.54 ? 115 THR A CA  1 
ATOM   897  C C   . THR A 1 115 ? 17.064 -18.779 -3.799  1.00 19.67 ? 115 THR A C   1 
ATOM   898  O O   . THR A 1 115 ? 16.772 -17.577 -3.901  1.00 16.56 ? 115 THR A O   1 
ATOM   899  C CB  . THR A 1 115 ? 15.437 -19.914 -2.198  1.00 24.03 ? 115 THR A CB  1 
ATOM   900  O OG1 . THR A 1 115 ? 15.186 -21.002 -3.094  1.00 29.37 ? 115 THR A OG1 1 
ATOM   901  C CG2 . THR A 1 115 ? 14.419 -18.817 -2.426  1.00 26.42 ? 115 THR A CG2 1 
ATOM   902  N N   . LEU A 1 116 ? 17.565 -19.520 -4.787  1.00 18.66 ? 116 LEU A N   1 
ATOM   903  C CA  . LEU A 1 116 ? 17.783 -18.968 -6.144  1.00 18.75 ? 116 LEU A CA  1 
ATOM   904  C C   . LEU A 1 116 ? 16.435 -18.866 -6.861  1.00 17.66 ? 116 LEU A C   1 
ATOM   905  O O   . LEU A 1 116 ? 15.668 -19.838 -6.852  1.00 19.13 ? 116 LEU A O   1 
ATOM   906  C CB  . LEU A 1 116 ? 18.754 -19.863 -6.913  1.00 21.00 ? 116 LEU A CB  1 
ATOM   907  C CG  . LEU A 1 116 ? 19.051 -19.440 -8.349  1.00 22.26 ? 116 LEU A CG  1 
ATOM   908  C CD1 . LEU A 1 116 ? 19.700 -18.065 -8.404  1.00 23.46 ? 116 LEU A CD1 1 
ATOM   909  C CD2 . LEU A 1 116 ? 19.935 -20.480 -9.016  1.00 24.68 ? 116 LEU A CD2 1 
ATOM   910  N N   . VAL A 1 117 ? 16.206 -17.716 -7.479  1.00 16.64 ? 117 VAL A N   1 
ATOM   911  C CA  . VAL A 1 117 ? 15.121 -17.462 -8.459  1.00 16.37 ? 117 VAL A CA  1 
ATOM   912  C C   . VAL A 1 117 ? 15.812 -17.078 -9.761  1.00 15.60 ? 117 VAL A C   1 
ATOM   913  O O   . VAL A 1 117 ? 16.557 -16.095 -9.768  1.00 17.09 ? 117 VAL A O   1 
ATOM   914  C CB  . VAL A 1 117 ? 14.157 -16.367 -7.979  1.00 16.73 ? 117 VAL A CB  1 
ATOM   915  C CG1 . VAL A 1 117 ? 13.153 -16.004 -9.067  1.00 18.73 ? 117 VAL A CG1 1 
ATOM   916  C CG2 . VAL A 1 117 ? 13.458 -16.782 -6.686  1.00 16.14 ? 117 VAL A CG2 1 
ATOM   917  N N   . THR A 1 118 ? 15.566 -17.842 -10.820 1.00 19.13 ? 118 THR A N   1 
ATOM   918  C CA  . THR A 1 118 ? 16.169 -17.601 -12.152 1.00 20.72 ? 118 THR A CA  1 
ATOM   919  C C   . THR A 1 118 ? 15.031 -17.287 -13.116 1.00 17.97 ? 118 THR A C   1 
ATOM   920  O O   . THR A 1 118 ? 14.130 -18.101 -13.207 1.00 20.83 ? 118 THR A O   1 
ATOM   921  C CB  . THR A 1 118 ? 16.990 -18.802 -12.632 1.00 22.58 ? 118 THR A CB  1 
ATOM   922  O OG1 . THR A 1 118 ? 18.011 -19.071 -11.671 1.00 23.74 ? 118 THR A OG1 1 
ATOM   923  C CG2 . THR A 1 118 ? 17.624 -18.565 -13.985 1.00 24.69 ? 118 THR A CG2 1 
ATOM   924  N N   . VAL A 1 119 ? 15.080 -16.125 -13.748 1.00 17.89 ? 119 VAL A N   1 
ATOM   925  C CA  . VAL A 1 119 ? 14.060 -15.687 -14.738 1.00 17.92 ? 119 VAL A CA  1 
ATOM   926  C C   . VAL A 1 119 ? 14.740 -15.671 -16.111 1.00 18.02 ? 119 VAL A C   1 
ATOM   927  O O   . VAL A 1 119 ? 15.455 -14.698 -16.425 1.00 19.88 ? 119 VAL A O   1 
ATOM   928  C CB  . VAL A 1 119 ? 13.454 -14.322 -14.393 1.00 18.56 ? 119 VAL A CB  1 
ATOM   929  C CG1 . VAL A 1 119 ? 12.276 -14.028 -15.314 1.00 19.36 ? 119 VAL A CG1 1 
ATOM   930  C CG2 . VAL A 1 119 ? 13.043 -14.223 -12.927 1.00 19.41 ? 119 VAL A CG2 1 
ATOM   931  N N   . SER A 1 120 ? 14.517 -16.713 -16.896 1.00 21.10 ? 120 SER A N   1 
ATOM   932  C CA  . SER A 1 120 ? 15.169 -16.882 -18.220 1.00 22.06 ? 120 SER A CA  1 
ATOM   933  C C   . SER A 1 120 ? 14.334 -17.831 -19.078 1.00 23.63 ? 120 SER A C   1 
ATOM   934  O O   . SER A 1 120 ? 13.409 -18.446 -18.537 1.00 25.41 ? 120 SER A O   1 
ATOM   935  C CB  . SER A 1 120 ? 16.590 -17.364 -18.053 1.00 26.14 ? 120 SER A CB  1 
ATOM   936  O OG  . SER A 1 120 ? 16.625 -18.682 -17.539 1.00 31.78 ? 120 SER A OG  1 
ATOM   937  N N   . SER A 1 121 ? 14.655 -17.943 -20.369 1.00 30.06 ? 121 SER A N   1 
ATOM   938  C CA  . SER A 1 121 ? 13.978 -18.870 -21.317 1.00 39.71 ? 121 SER A CA  1 
ATOM   939  C C   . SER A 1 121 ? 14.945 -19.983 -21.734 1.00 47.04 ? 121 SER A C   1 
ATOM   940  O O   . SER A 1 121 ? 14.984 -21.009 -21.054 1.00 55.32 ? 121 SER A O   1 
ATOM   941  C CB  . SER A 1 121 ? 13.419 -18.137 -22.513 1.00 44.21 ? 121 SER A CB  1 
ATOM   942  O OG  . SER A 1 121 ? 14.327 -17.156 -22.982 1.00 45.73 ? 121 SER A OG  1 
ATOM   943  N N   . GLN B 1 3   ? 26.047 -16.128 18.969  1.00 42.75 ? 3   GLN B N   1 
ATOM   944  C CA  . GLN B 1 3   ? 25.522 -16.179 17.592  1.00 36.47 ? 3   GLN B CA  1 
ATOM   945  C C   . GLN B 1 3   ? 26.715 -16.155 16.622  1.00 30.12 ? 3   GLN B C   1 
ATOM   946  O O   . GLN B 1 3   ? 27.650 -15.370 16.825  1.00 29.96 ? 3   GLN B O   1 
ATOM   947  C CB  . GLN B 1 3   ? 24.536 -15.032 17.310  1.00 40.56 ? 3   GLN B CB  1 
ATOM   948  C CG  . GLN B 1 3   ? 23.769 -15.176 15.988  1.00 38.88 ? 3   GLN B CG  1 
ATOM   949  C CD  . GLN B 1 3   ? 22.729 -14.100 15.739  1.00 39.04 ? 3   GLN B CD  1 
ATOM   950  O OE1 . GLN B 1 3   ? 22.689 -13.076 16.422  1.00 36.54 ? 3   GLN B OE1 1 
ATOM   951  N NE2 . GLN B 1 3   ? 21.870 -14.312 14.745  1.00 30.42 ? 3   GLN B NE2 1 
ATOM   952  N N   . LEU B 1 4   ? 26.681 -16.996 15.597  1.00 22.85 ? 4   LEU B N   1 
ATOM   953  C CA  . LEU B 1 4   ? 27.493 -16.800 14.372  1.00 21.31 ? 4   LEU B CA  1 
ATOM   954  C C   . LEU B 1 4   ? 26.531 -16.383 13.253  1.00 23.04 ? 4   LEU B C   1 
ATOM   955  O O   . LEU B 1 4   ? 25.528 -17.100 13.042  1.00 23.69 ? 4   LEU B O   1 
ATOM   956  C CB  . LEU B 1 4   ? 28.213 -18.099 14.018  1.00 22.63 ? 4   LEU B CB  1 
ATOM   957  C CG  . LEU B 1 4   ? 29.186 -18.673 15.046  1.00 26.09 ? 4   LEU B CG  1 
ATOM   958  C CD1 . LEU B 1 4   ? 29.808 -19.977 14.529  1.00 26.50 ? 4   LEU B CD1 1 
ATOM   959  C CD2 . LEU B 1 4   ? 30.268 -17.672 15.391  1.00 26.69 ? 4   LEU B CD2 1 
ATOM   960  N N   . VAL B 1 5   ? 26.807 -15.262 12.587  1.00 23.66 ? 5   VAL B N   1 
ATOM   961  C CA  . VAL B 1 5   ? 25.941 -14.764 11.480  1.00 24.12 ? 5   VAL B CA  1 
ATOM   962  C C   . VAL B 1 5   ? 26.790 -14.719 10.211  1.00 20.81 ? 5   VAL B C   1 
ATOM   963  O O   . VAL B 1 5   ? 27.850 -14.060 10.199  1.00 22.26 ? 5   VAL B O   1 
ATOM   964  C CB  . VAL B 1 5   ? 25.221 -13.430 11.779  1.00 30.25 ? 5   VAL B CB  1 
ATOM   965  C CG1 . VAL B 1 5   ? 26.117 -12.367 12.382  1.00 35.22 ? 5   VAL B CG1 1 
ATOM   966  C CG2 . VAL B 1 5   ? 24.516 -12.902 10.539  1.00 30.01 ? 5   VAL B CG2 1 
ATOM   967  N N   . GLU B 1 6   ? 26.341 -15.437 9.185   1.00 20.98 ? 6   GLU B N   1 
ATOM   968  C CA  . GLU B 1 6   ? 27.046 -15.507 7.883   1.00 21.39 ? 6   GLU B CA  1 
ATOM   969  C C   . GLU B 1 6   ? 26.457 -14.500 6.909   1.00 21.02 ? 6   GLU B C   1 
ATOM   970  O O   . GLU B 1 6   ? 25.241 -14.286 6.937   1.00 23.47 ? 6   GLU B O   1 
ATOM   971  C CB  . GLU B 1 6   ? 26.936 -16.888 7.253   1.00 20.55 ? 6   GLU B CB  1 
ATOM   972  C CG  . GLU B 1 6   ? 27.647 -17.940 8.061   1.00 19.91 ? 6   GLU B CG  1 
ATOM   973  C CD  . GLU B 1 6   ? 27.386 -19.300 7.491   1.00 21.19 ? 6   GLU B CD  1 
ATOM   974  O OE1 . GLU B 1 6   ? 27.627 -19.459 6.263   1.00 21.56 ? 6   GLU B OE1 1 
ATOM   975  O OE2 . GLU B 1 6   ? 26.910 -20.163 8.245   1.00 20.01 ? 6   GLU B OE2 1 
ATOM   976  N N   . SER B 1 7   ? 27.323 -13.973 6.049   1.00 20.34 ? 7   SER B N   1 
ATOM   977  C CA  A SER B 1 7   ? 26.996 -12.968 5.007   0.50 22.05 ? 7   SER B CA  1 
ATOM   978  C CA  B SER B 1 7   ? 26.951 -13.019 4.976   0.50 21.22 ? 7   SER B CA  1 
ATOM   979  C C   . SER B 1 7   ? 27.926 -13.198 3.810   1.00 20.88 ? 7   SER B C   1 
ATOM   980  O O   . SER B 1 7   ? 28.922 -13.936 3.981   1.00 19.13 ? 7   SER B O   1 
ATOM   981  C CB  A SER B 1 7   ? 27.160 -11.568 5.544   0.50 24.03 ? 7   SER B CB  1 
ATOM   982  C CB  B SER B 1 7   ? 26.939 -11.599 5.487   0.50 20.61 ? 7   SER B CB  1 
ATOM   983  O OG  A SER B 1 7   ? 26.412 -11.373 6.730   0.50 25.94 ? 7   SER B OG  1 
ATOM   984  O OG  B SER B 1 7   ? 28.220 -11.225 5.967   0.50 19.44 ? 7   SER B OG  1 
ATOM   985  N N   . GLY B 1 8   ? 27.623 -12.584 2.669   1.00 22.06 ? 8   GLY B N   1 
ATOM   986  C CA  . GLY B 1 8   ? 28.544 -12.539 1.513   1.00 24.63 ? 8   GLY B CA  1 
ATOM   987  C C   . GLY B 1 8   ? 28.291 -13.637 0.490   1.00 25.45 ? 8   GLY B C   1 
ATOM   988  O O   . GLY B 1 8   ? 29.076 -13.732 -0.487  1.00 29.29 ? 8   GLY B O   1 
ATOM   989  N N   . GLY B 1 9   ? 27.247 -14.442 0.675   1.00 24.49 ? 9   GLY B N   1 
ATOM   990  C CA  . GLY B 1 9   ? 26.928 -15.538 -0.260  1.00 26.95 ? 9   GLY B CA  1 
ATOM   991  C C   . GLY B 1 9   ? 26.187 -15.014 -1.476  1.00 25.28 ? 9   GLY B C   1 
ATOM   992  O O   . GLY B 1 9   ? 26.081 -13.770 -1.629  1.00 29.05 ? 9   GLY B O   1 
ATOM   993  N N   . GLY B 1 10  ? 25.692 -15.921 -2.313  1.00 20.39 ? 10  GLY B N   1 
ATOM   994  C CA  . GLY B 1 10  ? 24.727 -15.589 -3.370  1.00 20.71 ? 10  GLY B CA  1 
ATOM   995  C C   . GLY B 1 10  ? 25.054 -16.266 -4.686  1.00 21.03 ? 10  GLY B C   1 
ATOM   996  O O   . GLY B 1 10  ? 25.653 -17.336 -4.676  1.00 21.21 ? 10  GLY B O   1 
ATOM   997  N N   . LEU B 1 11  ? 24.652 -15.625 -5.775  1.00 20.97 ? 11  LEU B N   1 
ATOM   998  C CA  . LEU B 1 11  ? 24.709 -16.144 -7.159  1.00 20.12 ? 11  LEU B CA  1 
ATOM   999  C C   . LEU B 1 11  ? 25.956 -15.563 -7.825  1.00 24.78 ? 11  LEU B C   1 
ATOM   1000 O O   . LEU B 1 11  ? 26.203 -14.338 -7.698  1.00 27.93 ? 11  LEU B O   1 
ATOM   1001 C CB  . LEU B 1 11  ? 23.427 -15.720 -7.883  1.00 21.86 ? 11  LEU B CB  1 
ATOM   1002 C CG  . LEU B 1 11  ? 23.381 -15.961 -9.391  1.00 22.58 ? 11  LEU B CG  1 
ATOM   1003 C CD1 . LEU B 1 11  ? 23.424 -17.444 -9.725  1.00 23.65 ? 11  LEU B CD1 1 
ATOM   1004 C CD2 . LEU B 1 11  ? 22.142 -15.315 -9.982  1.00 24.83 ? 11  LEU B CD2 1 
ATOM   1005 N N   . VAL B 1 12  ? 26.725 -16.410 -8.499  1.00 23.23 ? 12  VAL B N   1 
ATOM   1006 C CA  A VAL B 1 12  ? 27.941 -15.967 -9.234  0.50 26.51 ? 12  VAL B CA  1 
ATOM   1007 C CA  B VAL B 1 12  ? 27.934 -15.958 -9.250  0.50 26.53 ? 12  VAL B CA  1 
ATOM   1008 C C   . VAL B 1 12  ? 28.051 -16.769 -10.538 1.00 28.32 ? 12  VAL B C   1 
ATOM   1009 O O   . VAL B 1 12  ? 27.548 -17.900 -10.577 1.00 27.94 ? 12  VAL B O   1 
ATOM   1010 C CB  A VAL B 1 12  ? 29.164 -16.095 -8.305  0.50 29.10 ? 12  VAL B CB  1 
ATOM   1011 C CB  B VAL B 1 12  ? 29.211 -16.090 -8.403  0.50 30.05 ? 12  VAL B CB  1 
ATOM   1012 C CG1 A VAL B 1 12  ? 29.396 -17.526 -7.855  0.50 30.12 ? 12  VAL B CG1 1 
ATOM   1013 C CG1 B VAL B 1 12  ? 29.327 -14.969 -7.387  0.50 31.37 ? 12  VAL B CG1 1 
ATOM   1014 C CG2 A VAL B 1 12  ? 30.408 -15.486 -8.912  0.50 29.73 ? 12  VAL B CG2 1 
ATOM   1015 C CG2 B VAL B 1 12  ? 29.292 -17.447 -7.731  0.50 29.83 ? 12  VAL B CG2 1 
ATOM   1016 N N   . GLN B 1 13  ? 28.667 -16.181 -11.559 1.00 32.36 ? 13  GLN B N   1 
ATOM   1017 C CA  . GLN B 1 13  ? 28.993 -16.884 -12.823 1.00 34.15 ? 13  GLN B CA  1 
ATOM   1018 C C   . GLN B 1 13  ? 30.206 -17.768 -12.560 1.00 30.72 ? 13  GLN B C   1 
ATOM   1019 O O   . GLN B 1 13  ? 31.038 -17.437 -11.716 1.00 29.36 ? 13  GLN B O   1 
ATOM   1020 C CB  . GLN B 1 13  ? 29.241 -15.878 -13.947 1.00 41.32 ? 13  GLN B CB  1 
ATOM   1021 C CG  . GLN B 1 13  ? 28.029 -15.009 -14.264 1.00 45.86 ? 13  GLN B CG  1 
ATOM   1022 C CD  . GLN B 1 13  ? 27.074 -15.631 -15.256 1.00 55.91 ? 13  GLN B CD  1 
ATOM   1023 O OE1 . GLN B 1 13  ? 26.213 -16.433 -14.901 1.00 60.76 ? 13  GLN B OE1 1 
ATOM   1024 N NE2 . GLN B 1 13  ? 27.193 -15.231 -16.514 1.00 62.33 ? 13  GLN B NE2 1 
ATOM   1025 N N   . PRO B 1 14  ? 30.352 -18.910 -13.265 1.00 30.03 ? 14  PRO B N   1 
ATOM   1026 C CA  . PRO B 1 14  ? 31.586 -19.687 -13.197 1.00 29.23 ? 14  PRO B CA  1 
ATOM   1027 C C   . PRO B 1 14  ? 32.803 -18.781 -13.445 1.00 27.71 ? 14  PRO B C   1 
ATOM   1028 O O   . PRO B 1 14  ? 32.729 -17.910 -14.307 1.00 28.87 ? 14  PRO B O   1 
ATOM   1029 C CB  . PRO B 1 14  ? 31.418 -20.732 -14.311 1.00 31.86 ? 14  PRO B CB  1 
ATOM   1030 C CG  . PRO B 1 14  ? 29.925 -20.905 -14.421 1.00 34.89 ? 14  PRO B CG  1 
ATOM   1031 C CD  . PRO B 1 14  ? 29.359 -19.524 -14.161 1.00 34.35 ? 14  PRO B CD  1 
ATOM   1032 N N   . GLY B 1 15  ? 33.865 -18.990 -12.661 1.00 25.98 ? 15  GLY B N   1 
ATOM   1033 C CA  . GLY B 1 15  ? 35.091 -18.175 -12.678 1.00 29.10 ? 15  GLY B CA  1 
ATOM   1034 C C   . GLY B 1 15  ? 35.006 -16.982 -11.742 1.00 29.33 ? 15  GLY B C   1 
ATOM   1035 O O   . GLY B 1 15  ? 36.039 -16.321 -11.546 1.00 31.29 ? 15  GLY B O   1 
ATOM   1036 N N   . GLY B 1 16  ? 33.828 -16.725 -11.161 1.00 29.52 ? 16  GLY B N   1 
ATOM   1037 C CA  . GLY B 1 16  ? 33.584 -15.553 -10.303 1.00 29.39 ? 16  GLY B CA  1 
ATOM   1038 C C   . GLY B 1 16  ? 34.138 -15.747 -8.901  1.00 28.59 ? 16  GLY B C   1 
ATOM   1039 O O   . GLY B 1 16  ? 34.645 -16.858 -8.588  1.00 26.70 ? 16  GLY B O   1 
ATOM   1040 N N   . SER B 1 17  ? 34.039 -14.703 -8.082  1.00 28.35 ? 17  SER B N   1 
ATOM   1041 C CA  . SER B 1 17  ? 34.528 -14.671 -6.682  1.00 26.40 ? 17  SER B CA  1 
ATOM   1042 C C   . SER B 1 17  ? 33.400 -14.242 -5.743  1.00 25.72 ? 17  SER B C   1 
ATOM   1043 O O   . SER B 1 17  ? 32.512 -13.477 -6.157  1.00 27.13 ? 17  SER B O   1 
ATOM   1044 C CB  . SER B 1 17  ? 35.719 -13.761 -6.527  1.00 32.20 ? 17  SER B CB  1 
ATOM   1045 O OG  . SER B 1 17  ? 36.819 -14.226 -7.291  1.00 40.24 ? 17  SER B OG  1 
ATOM   1046 N N   . LEU B 1 18  ? 33.483 -14.717 -4.503  1.00 25.73 ? 18  LEU B N   1 
ATOM   1047 C CA  . LEU B 1 18  ? 32.647 -14.289 -3.355  1.00 26.72 ? 18  LEU B CA  1 
ATOM   1048 C C   . LEU B 1 18  ? 33.557 -14.311 -2.130  1.00 26.27 ? 18  LEU B C   1 
ATOM   1049 O O   . LEU B 1 18  ? 34.488 -15.138 -2.110  1.00 26.65 ? 18  LEU B O   1 
ATOM   1050 C CB  . LEU B 1 18  ? 31.505 -15.289 -3.165  1.00 29.40 ? 18  LEU B CB  1 
ATOM   1051 C CG  . LEU B 1 18  ? 30.353 -15.254 -4.157  1.00 32.96 ? 18  LEU B CG  1 
ATOM   1052 C CD1 . LEU B 1 18  ? 29.408 -16.406 -3.869  1.00 35.74 ? 18  LEU B CD1 1 
ATOM   1053 C CD2 . LEU B 1 18  ? 29.611 -13.928 -4.117  1.00 35.19 ? 18  LEU B CD2 1 
ATOM   1054 N N   . ARG B 1 19  ? 33.299 -13.466 -1.131  1.00 24.92 ? 19  ARG B N   1 
ATOM   1055 C CA  . ARG B 1 19  ? 33.932 -13.625 0.200   1.00 24.81 ? 19  ARG B CA  1 
ATOM   1056 C C   . ARG B 1 19  ? 32.821 -13.826 1.226   1.00 23.11 ? 19  ARG B C   1 
ATOM   1057 O O   . ARG B 1 19  ? 32.007 -12.903 1.402   1.00 25.24 ? 19  ARG B O   1 
ATOM   1058 C CB  . ARG B 1 19  ? 34.824 -12.442 0.584   1.00 27.13 ? 19  ARG B CB  1 
ATOM   1059 C CG  . ARG B 1 19  ? 35.632 -12.690 1.849   1.00 32.18 ? 19  ARG B CG  1 
ATOM   1060 C CD  . ARG B 1 19  ? 36.405 -11.457 2.290   1.00 35.34 ? 19  ARG B CD  1 
ATOM   1061 N NE  . ARG B 1 19  ? 35.529 -10.552 3.019   1.00 38.70 ? 19  ARG B NE  1 
ATOM   1062 C CZ  . ARG B 1 19  ? 35.928 -9.582  3.836   1.00 38.93 ? 19  ARG B CZ  1 
ATOM   1063 N NH1 . ARG B 1 19  ? 37.215 -9.371  4.061   1.00 42.96 ? 19  ARG B NH1 1 
ATOM   1064 N NH2 . ARG B 1 19  ? 35.024 -8.835  4.444   1.00 42.55 ? 19  ARG B NH2 1 
ATOM   1065 N N   . LEU B 1 20  ? 32.789 -14.993 1.856   1.00 20.30 ? 20  LEU B N   1 
ATOM   1066 C CA  . LEU B 1 20  ? 31.872 -15.255 2.990   1.00 18.82 ? 20  LEU B CA  1 
ATOM   1067 C C   . LEU B 1 20  ? 32.493 -14.669 4.250   1.00 19.07 ? 20  LEU B C   1 
ATOM   1068 O O   . LEU B 1 20  ? 33.724 -14.690 4.394   1.00 19.78 ? 20  LEU B O   1 
ATOM   1069 C CB  . LEU B 1 20  ? 31.621 -16.751 3.168   1.00 20.25 ? 20  LEU B CB  1 
ATOM   1070 C CG  . LEU B 1 20  ? 31.103 -17.487 1.935   1.00 22.45 ? 20  LEU B CG  1 
ATOM   1071 C CD1 . LEU B 1 20  ? 30.712 -18.909 2.298   1.00 21.62 ? 20  LEU B CD1 1 
ATOM   1072 C CD2 . LEU B 1 20  ? 29.934 -16.751 1.299   1.00 24.73 ? 20  LEU B CD2 1 
ATOM   1073 N N   . SER B 1 21  ? 31.633 -14.162 5.112   1.00 19.22 ? 21  SER B N   1 
ATOM   1074 C CA  A SER B 1 21  ? 31.987 -13.618 6.446   0.50 21.49 ? 21  SER B CA  1 
ATOM   1075 C CA  B SER B 1 21  ? 32.028 -13.667 6.449   0.50 21.92 ? 21  SER B CA  1 
ATOM   1076 C C   . SER B 1 21  ? 31.148 -14.358 7.488   1.00 21.65 ? 21  SER B C   1 
ATOM   1077 O O   . SER B 1 21  ? 29.981 -14.661 7.194   1.00 21.40 ? 21  SER B O   1 
ATOM   1078 C CB  A SER B 1 21  ? 31.723 -12.132 6.527   0.50 23.07 ? 21  SER B CB  1 
ATOM   1079 C CB  B SER B 1 21  ? 31.969 -12.159 6.537   0.50 24.71 ? 21  SER B CB  1 
ATOM   1080 O OG  A SER B 1 21  ? 32.553 -11.387 5.648   0.50 24.23 ? 21  SER B OG  1 
ATOM   1081 O OG  B SER B 1 21  ? 30.671 -11.673 6.242   0.50 27.43 ? 21  SER B OG  1 
ATOM   1082 N N   . CYS B 1 22  ? 31.728 -14.626 8.632   1.00 22.07 ? 22  CYS B N   1 
ATOM   1083 C CA  . CYS B 1 22  ? 31.050 -15.268 9.773   1.00 22.84 ? 22  CYS B CA  1 
ATOM   1084 C C   . CYS B 1 22  ? 31.410 -14.443 11.002  1.00 23.16 ? 22  CYS B C   1 
ATOM   1085 O O   . CYS B 1 22  ? 32.569 -14.523 11.431  1.00 25.33 ? 22  CYS B O   1 
ATOM   1086 C CB  . CYS B 1 22  ? 31.505 -16.716 9.868   1.00 25.22 ? 22  CYS B CB  1 
ATOM   1087 S SG  . CYS B 1 22  ? 30.963 -17.584 11.358  1.00 27.07 ? 22  CYS B SG  1 
ATOM   1088 N N   . ALA B 1 23  ? 30.471 -13.615 11.464  1.00 24.37 ? 23  ALA B N   1 
ATOM   1089 C CA  . ALA B 1 23  ? 30.668 -12.679 12.595  1.00 26.39 ? 23  ALA B CA  1 
ATOM   1090 C C   . ALA B 1 23  ? 30.138 -13.343 13.869  1.00 26.05 ? 23  ALA B C   1 
ATOM   1091 O O   . ALA B 1 23  ? 28.973 -13.786 13.872  1.00 24.15 ? 23  ALA B O   1 
ATOM   1092 C CB  . ALA B 1 23  ? 29.991 -11.364 12.317  1.00 27.00 ? 23  ALA B CB  1 
ATOM   1093 N N   . ALA B 1 24  ? 30.992 -13.447 14.889  1.00 25.56 ? 24  ALA B N   1 
ATOM   1094 C CA  . ALA B 1 24  ? 30.691 -14.087 16.186  1.00 27.33 ? 24  ALA B CA  1 
ATOM   1095 C C   . ALA B 1 24  ? 30.364 -13.012 17.220  1.00 30.08 ? 24  ALA B C   1 
ATOM   1096 O O   . ALA B 1 24  ? 31.030 -11.950 17.224  1.00 33.13 ? 24  ALA B O   1 
ATOM   1097 C CB  . ALA B 1 24  ? 31.865 -14.923 16.630  1.00 29.25 ? 24  ALA B CB  1 
ATOM   1098 N N   . SER B 1 25  ? 29.363 -13.291 18.054  1.00 33.04 ? 25  SER B N   1 
ATOM   1099 C CA  . SER B 1 25  ? 29.083 -12.583 19.330  1.00 39.39 ? 25  SER B CA  1 
ATOM   1100 C C   . SER B 1 25  ? 28.896 -13.618 20.446  1.00 41.73 ? 25  SER B C   1 
ATOM   1101 O O   . SER B 1 25  ? 28.757 -14.817 20.132  1.00 39.15 ? 25  SER B O   1 
ATOM   1102 C CB  . SER B 1 25  ? 27.876 -11.705 19.193  1.00 42.71 ? 25  SER B CB  1 
ATOM   1103 O OG  . SER B 1 25  ? 26.743 -12.481 18.827  1.00 45.84 ? 25  SER B OG  1 
ATOM   1104 N N   . GLY B 1 26  ? 28.908 -13.172 21.705  1.00 48.33 ? 26  GLY B N   1 
ATOM   1105 C CA  . GLY B 1 26  ? 28.545 -14.005 22.867  1.00 56.86 ? 26  GLY B CA  1 
ATOM   1106 C C   . GLY B 1 26  ? 29.754 -14.425 23.680  1.00 66.12 ? 26  GLY B C   1 
ATOM   1107 O O   . GLY B 1 26  ? 30.898 -14.229 23.216  1.00 58.92 ? 26  GLY B O   1 
ATOM   1108 N N   . SER B 1 27  ? 29.497 -14.992 24.863  1.00 78.00 ? 27  SER B N   1 
ATOM   1109 C CA  . SER B 1 27  ? 30.481 -15.354 25.919  1.00 79.42 ? 27  SER B CA  1 
ATOM   1110 C C   . SER B 1 27  ? 31.595 -16.233 25.338  1.00 75.80 ? 27  SER B C   1 
ATOM   1111 O O   . SER B 1 27  ? 31.563 -17.466 25.549  1.00 62.39 ? 27  SER B O   1 
ATOM   1112 C CB  . SER B 1 27  ? 29.789 -16.027 27.086  1.00 88.15 ? 27  SER B CB  1 
ATOM   1113 O OG  . SER B 1 27  ? 28.848 -16.995 26.640  1.00 91.97 ? 27  SER B OG  1 
ATOM   1114 N N   . VAL B 1 28  ? 32.565 -15.603 24.671  1.00 78.30 ? 28  VAL B N   1 
ATOM   1115 C CA  . VAL B 1 28  ? 33.633 -16.282 23.875  1.00 81.13 ? 28  VAL B CA  1 
ATOM   1116 C C   . VAL B 1 28  ? 34.693 -16.822 24.846  1.00 82.60 ? 28  VAL B C   1 
ATOM   1117 O O   . VAL B 1 28  ? 35.435 -16.012 25.436  1.00 87.15 ? 28  VAL B O   1 
ATOM   1118 C CB  . VAL B 1 28  ? 34.213 -15.365 22.771  1.00 81.28 ? 28  VAL B CB  1 
ATOM   1119 C CG1 . VAL B 1 28  ? 34.167 -13.885 23.132  1.00 79.79 ? 28  VAL B CG1 1 
ATOM   1120 C CG2 . VAL B 1 28  ? 35.624 -15.750 22.336  1.00 80.33 ? 28  VAL B CG2 1 
ATOM   1121 N N   . PHE B 1 29  ? 34.745 -18.148 24.989  1.00 78.98 ? 29  PHE B N   1 
ATOM   1122 C CA  . PHE B 1 29  ? 35.752 -18.890 25.789  1.00 73.92 ? 29  PHE B CA  1 
ATOM   1123 C C   . PHE B 1 29  ? 36.869 -19.325 24.836  1.00 63.63 ? 29  PHE B C   1 
ATOM   1124 O O   . PHE B 1 29  ? 36.997 -18.709 23.748  1.00 64.59 ? 29  PHE B O   1 
ATOM   1125 C CB  . PHE B 1 29  ? 35.110 -20.078 26.511  1.00 77.90 ? 29  PHE B CB  1 
ATOM   1126 C CG  . PHE B 1 29  ? 33.840 -19.776 27.266  1.00 84.37 ? 29  PHE B CG  1 
ATOM   1127 C CD1 . PHE B 1 29  ? 33.798 -18.785 28.236  1.00 87.93 ? 29  PHE B CD1 1 
ATOM   1128 C CD2 . PHE B 1 29  ? 32.691 -20.515 27.029  1.00 82.74 ? 29  PHE B CD2 1 
ATOM   1129 C CE1 . PHE B 1 29  ? 32.627 -18.521 28.929  1.00 83.04 ? 29  PHE B CE1 1 
ATOM   1130 C CE2 . PHE B 1 29  ? 31.524 -20.253 27.726  1.00 81.06 ? 29  PHE B CE2 1 
ATOM   1131 C CZ  . PHE B 1 29  ? 31.492 -19.255 28.672  1.00 78.81 ? 29  PHE B CZ  1 
ATOM   1132 N N   . LYS B 1 30  ? 37.661 -20.338 25.200  1.00 48.95 ? 30  LYS B N   1 
ATOM   1133 C CA  . LYS B 1 30  ? 38.798 -20.765 24.346  1.00 43.24 ? 30  LYS B CA  1 
ATOM   1134 C C   . LYS B 1 30  ? 38.232 -21.288 23.020  1.00 37.80 ? 30  LYS B C   1 
ATOM   1135 O O   . LYS B 1 30  ? 37.397 -22.187 23.067  1.00 35.70 ? 30  LYS B O   1 
ATOM   1136 C CB  . LYS B 1 30  ? 39.671 -21.812 25.038  1.00 47.80 ? 30  LYS B CB  1 
ATOM   1137 C CG  . LYS B 1 30  ? 40.839 -22.318 24.204  1.00 54.79 ? 30  LYS B CG  1 
ATOM   1138 C CD  . LYS B 1 30  ? 41.621 -21.229 23.498  1.00 60.42 ? 30  LYS B CD  1 
ATOM   1139 C CE  . LYS B 1 30  ? 42.611 -21.762 22.485  1.00 64.94 ? 30  LYS B CE  1 
ATOM   1140 N NZ  . LYS B 1 30  ? 43.103 -20.679 21.601  1.00 67.62 ? 30  LYS B NZ  1 
ATOM   1141 N N   . ILE B 1 31  ? 38.618 -20.690 21.893  1.00 37.79 ? 31  ILE B N   1 
ATOM   1142 C CA  . ILE B 1 31  ? 38.242 -21.176 20.532  1.00 35.30 ? 31  ILE B CA  1 
ATOM   1143 C C   . ILE B 1 31  ? 39.393 -22.047 20.030  1.00 37.31 ? 31  ILE B C   1 
ATOM   1144 O O   . ILE B 1 31  ? 40.503 -21.507 19.835  1.00 39.31 ? 31  ILE B O   1 
ATOM   1145 C CB  . ILE B 1 31  ? 37.936 -20.018 19.561  1.00 38.13 ? 31  ILE B CB  1 
ATOM   1146 C CG1 . ILE B 1 31  ? 36.854 -19.084 20.111  1.00 38.21 ? 31  ILE B CG1 1 
ATOM   1147 C CG2 . ILE B 1 31  ? 37.573 -20.557 18.178  1.00 36.52 ? 31  ILE B CG2 1 
ATOM   1148 C CD1 . ILE B 1 31  ? 36.822 -17.729 19.441  1.00 42.17 ? 31  ILE B CD1 1 
ATOM   1149 N N   . ASN B 1 32  ? 39.130 -23.343 19.851  1.00 34.92 ? 32  ASN B N   1 
ATOM   1150 C CA  . ASN B 1 32  ? 40.114 -24.355 19.382  1.00 37.84 ? 32  ASN B CA  1 
ATOM   1151 C C   . ASN B 1 32  ? 40.214 -24.278 17.855  1.00 33.33 ? 32  ASN B C   1 
ATOM   1152 O O   . ASN B 1 32  ? 41.344 -24.236 17.329  1.00 36.34 ? 32  ASN B O   1 
ATOM   1153 C CB  . ASN B 1 32  ? 39.734 -25.768 19.826  1.00 41.62 ? 32  ASN B CB  1 
ATOM   1154 C CG  . ASN B 1 32  ? 39.692 -25.922 21.330  1.00 46.21 ? 32  ASN B CG  1 
ATOM   1155 O OD1 . ASN B 1 32  ? 40.659 -25.619 22.020  1.00 51.77 ? 32  ASN B OD1 1 
ATOM   1156 N ND2 . ASN B 1 32  ? 38.575 -26.401 21.845  1.00 54.97 ? 32  ASN B ND2 1 
ATOM   1157 N N   . VAL B 1 33  ? 39.062 -24.195 17.180  1.00 28.87 ? 33  VAL B N   1 
ATOM   1158 C CA  . VAL B 1 33  ? 38.975 -24.300 15.700  1.00 25.87 ? 33  VAL B CA  1 
ATOM   1159 C C   . VAL B 1 33  ? 37.909 -23.335 15.172  1.00 22.30 ? 33  VAL B C   1 
ATOM   1160 O O   . VAL B 1 33  ? 36.862 -23.160 15.814  1.00 22.76 ? 33  VAL B O   1 
ATOM   1161 C CB  . VAL B 1 33  ? 38.675 -25.742 15.247  1.00 29.80 ? 33  VAL B CB  1 
ATOM   1162 C CG1 . VAL B 1 33  ? 38.697 -25.858 13.734  1.00 31.25 ? 33  VAL B CG1 1 
ATOM   1163 C CG2 . VAL B 1 33  ? 39.633 -26.749 15.854  1.00 30.67 ? 33  VAL B CG2 1 
ATOM   1164 N N   . MET B 1 34  ? 38.206 -22.732 14.024  1.00 22.38 ? 34  MET B N   1 
ATOM   1165 C CA  A MET B 1 34  ? 37.211 -22.014 13.193  0.50 22.01 ? 34  MET B CA  1 
ATOM   1166 C CA  B MET B 1 34  ? 37.230 -21.988 13.184  0.50 21.91 ? 34  MET B CA  1 
ATOM   1167 C C   . MET B 1 34  ? 37.229 -22.636 11.798  1.00 21.08 ? 34  MET B C   1 
ATOM   1168 O O   . MET B 1 34  ? 38.325 -22.798 11.238  1.00 24.75 ? 34  MET B O   1 
ATOM   1169 C CB  A MET B 1 34  ? 37.540 -20.526 13.111  0.50 23.01 ? 34  MET B CB  1 
ATOM   1170 C CB  B MET B 1 34  ? 37.619 -20.514 13.042  0.50 23.43 ? 34  MET B CB  1 
ATOM   1171 C CG  A MET B 1 34  ? 37.398 -19.826 14.444  0.50 24.85 ? 34  MET B CG  1 
ATOM   1172 C CG  B MET B 1 34  ? 37.694 -19.762 14.350  0.50 24.76 ? 34  MET B CG  1 
ATOM   1173 S SD  A MET B 1 34  ? 37.844 -18.098 14.293  0.50 30.84 ? 34  MET B SD  1 
ATOM   1174 S SD  B MET B 1 34  ? 38.630 -18.227 14.148  0.50 30.16 ? 34  MET B SD  1 
ATOM   1175 C CE  A MET B 1 34  ? 39.579 -18.306 13.911  0.50 30.43 ? 34  MET B CE  1 
ATOM   1176 C CE  B MET B 1 34  ? 38.689 -17.662 15.848  0.50 28.89 ? 34  MET B CE  1 
ATOM   1177 N N   . ALA B 1 35  ? 36.065 -23.023 11.294  1.00 18.61 ? 35  ALA B N   1 
ATOM   1178 C CA  . ALA B 1 35  ? 36.004 -23.828 10.061  1.00 18.33 ? 35  ALA B CA  1 
ATOM   1179 C C   . ALA B 1 35  ? 34.802 -23.443 9.205   1.00 17.94 ? 35  ALA B C   1 
ATOM   1180 O O   . ALA B 1 35  ? 33.796 -22.915 9.725   1.00 19.38 ? 35  ALA B O   1 
ATOM   1181 C CB  . ALA B 1 35  ? 35.978 -25.297 10.398  1.00 18.82 ? 35  ALA B CB  1 
ATOM   1182 N N   . TRP B 1 36  ? 34.931 -23.734 7.916   1.00 16.68 ? 36  TRP B N   1 
ATOM   1183 C CA  . TRP B 1 36  ? 33.835 -23.678 6.922   1.00 16.64 ? 36  TRP B CA  1 
ATOM   1184 C C   . TRP B 1 36  ? 33.495 -25.102 6.489   1.00 15.86 ? 36  TRP B C   1 
ATOM   1185 O O   . TRP B 1 36  ? 34.421 -25.884 6.222   1.00 17.13 ? 36  TRP B O   1 
ATOM   1186 C CB  . TRP B 1 36  ? 34.227 -22.816 5.724   1.00 16.85 ? 36  TRP B CB  1 
ATOM   1187 C CG  . TRP B 1 36  ? 34.406 -21.374 6.076   1.00 17.97 ? 36  TRP B CG  1 
ATOM   1188 C CD1 . TRP B 1 36  ? 35.568 -20.733 6.389   1.00 19.20 ? 36  TRP B CD1 1 
ATOM   1189 C CD2 . TRP B 1 36  ? 33.364 -20.389 6.188   1.00 17.58 ? 36  TRP B CD2 1 
ATOM   1190 N NE1 . TRP B 1 36  ? 35.329 -19.413 6.650   1.00 19.95 ? 36  TRP B NE1 1 
ATOM   1191 C CE2 . TRP B 1 36  ? 33.985 -19.176 6.555   1.00 18.21 ? 36  TRP B CE2 1 
ATOM   1192 C CE3 . TRP B 1 36  ? 31.983 -20.403 5.971   1.00 18.62 ? 36  TRP B CE3 1 
ATOM   1193 C CZ2 . TRP B 1 36  ? 33.271 -17.990 6.712   1.00 19.41 ? 36  TRP B CZ2 1 
ATOM   1194 C CZ3 . TRP B 1 36  ? 31.277 -19.232 6.149   1.00 18.68 ? 36  TRP B CZ3 1 
ATOM   1195 C CH2 . TRP B 1 36  ? 31.913 -18.043 6.510   1.00 17.10 ? 36  TRP B CH2 1 
ATOM   1196 N N   . TYR B 1 37  ? 32.197 -25.383 6.424   1.00 15.22 ? 37  TYR B N   1 
ATOM   1197 C CA  . TYR B 1 37  ? 31.601 -26.636 5.917   1.00 16.40 ? 37  TYR B CA  1 
ATOM   1198 C C   . TYR B 1 37  ? 30.652 -26.273 4.785   1.00 16.56 ? 37  TYR B C   1 
ATOM   1199 O O   . TYR B 1 37  ? 30.172 -25.129 4.735   1.00 17.19 ? 37  TYR B O   1 
ATOM   1200 C CB  . TYR B 1 37  ? 30.833 -27.364 7.019   1.00 17.66 ? 37  TYR B CB  1 
ATOM   1201 C CG  . TYR B 1 37  ? 31.688 -27.873 8.142   1.00 18.87 ? 37  TYR B CG  1 
ATOM   1202 C CD1 . TYR B 1 37  ? 32.115 -27.031 9.150   1.00 18.83 ? 37  TYR B CD1 1 
ATOM   1203 C CD2 . TYR B 1 37  ? 32.036 -29.215 8.215   1.00 19.65 ? 37  TYR B CD2 1 
ATOM   1204 C CE1 . TYR B 1 37  ? 32.888 -27.505 10.198  1.00 21.95 ? 37  TYR B CE1 1 
ATOM   1205 C CE2 . TYR B 1 37  ? 32.825 -29.699 9.245   1.00 23.20 ? 37  TYR B CE2 1 
ATOM   1206 C CZ  . TYR B 1 37  ? 33.255 -28.839 10.238  1.00 22.88 ? 37  TYR B CZ  1 
ATOM   1207 O OH  . TYR B 1 37  ? 34.024 -29.327 11.256  1.00 27.95 ? 37  TYR B OH  1 
ATOM   1208 N N   . ARG B 1 38  ? 30.330 -27.234 3.935   1.00 16.73 ? 38  ARG B N   1 
ATOM   1209 C CA  . ARG B 1 38  ? 29.289 -27.006 2.909   1.00 18.26 ? 38  ARG B CA  1 
ATOM   1210 C C   . ARG B 1 38  ? 28.449 -28.263 2.772   1.00 18.63 ? 38  ARG B C   1 
ATOM   1211 O O   . ARG B 1 38  ? 28.990 -29.363 2.964   1.00 20.61 ? 38  ARG B O   1 
ATOM   1212 C CB  . ARG B 1 38  ? 29.920 -26.583 1.586   1.00 18.46 ? 38  ARG B CB  1 
ATOM   1213 C CG  . ARG B 1 38  ? 30.710 -27.663 0.867   1.00 19.89 ? 38  ARG B CG  1 
ATOM   1214 C CD  . ARG B 1 38  ? 31.385 -27.054 -0.350  1.00 19.87 ? 38  ARG B CD  1 
ATOM   1215 N NE  . ARG B 1 38  ? 32.238 -27.996 -1.065  1.00 22.29 ? 38  ARG B NE  1 
ATOM   1216 C CZ  . ARG B 1 38  ? 32.974 -27.684 -2.140  1.00 23.13 ? 38  ARG B CZ  1 
ATOM   1217 N NH1 . ARG B 1 38  ? 32.986 -26.453 -2.626  1.00 20.81 ? 38  ARG B NH1 1 
ATOM   1218 N NH2 . ARG B 1 38  ? 33.710 -28.606 -2.731  1.00 25.68 ? 38  ARG B NH2 1 
ATOM   1219 N N   . GLN B 1 39  ? 27.176 -28.077 2.461   1.00 20.23 ? 39  GLN B N   1 
ATOM   1220 C CA  . GLN B 1 39  ? 26.218 -29.176 2.203   1.00 22.24 ? 39  GLN B CA  1 
ATOM   1221 C C   . GLN B 1 39  ? 25.632 -28.946 0.819   1.00 24.69 ? 39  GLN B C   1 
ATOM   1222 O O   . GLN B 1 39  ? 24.895 -27.941 0.624   1.00 21.34 ? 39  GLN B O   1 
ATOM   1223 C CB  . GLN B 1 39  ? 25.107 -29.217 3.244   1.00 24.36 ? 39  GLN B CB  1 
ATOM   1224 C CG  . GLN B 1 39  ? 24.227 -30.444 3.085   1.00 26.57 ? 39  GLN B CG  1 
ATOM   1225 C CD  . GLN B 1 39  ? 23.488 -30.760 4.358   1.00 31.32 ? 39  GLN B CD  1 
ATOM   1226 O OE1 . GLN B 1 39  ? 23.095 -29.859 5.097   1.00 38.72 ? 39  GLN B OE1 1 
ATOM   1227 N NE2 . GLN B 1 39  ? 23.298 -32.045 4.623   1.00 36.13 ? 39  GLN B NE2 1 
ATOM   1228 N N   . ALA B 1 40  ? 26.055 -29.771 -0.131  1.00 27.78 ? 40  ALA B N   1 
ATOM   1229 C CA  . ALA B 1 40  ? 25.575 -29.746 -1.529  1.00 31.69 ? 40  ALA B CA  1 
ATOM   1230 C C   . ALA B 1 40  ? 24.378 -30.681 -1.627  1.00 35.46 ? 40  ALA B C   1 
ATOM   1231 O O   . ALA B 1 40  ? 24.206 -31.540 -0.766  1.00 34.80 ? 40  ALA B O   1 
ATOM   1232 C CB  . ALA B 1 40  ? 26.696 -30.148 -2.455  1.00 34.13 ? 40  ALA B CB  1 
ATOM   1233 N N   . PRO B 1 41  ? 23.504 -30.511 -2.645  1.00 42.16 ? 41  PRO B N   1 
ATOM   1234 C CA  . PRO B 1 41  ? 22.377 -31.415 -2.870  1.00 45.28 ? 41  PRO B CA  1 
ATOM   1235 C C   . PRO B 1 41  ? 22.764 -32.898 -2.762  1.00 43.67 ? 41  PRO B C   1 
ATOM   1236 O O   . PRO B 1 41  ? 23.702 -33.316 -3.431  1.00 45.80 ? 41  PRO B O   1 
ATOM   1237 C CB  . PRO B 1 41  ? 21.929 -31.068 -4.301  1.00 46.90 ? 41  PRO B CB  1 
ATOM   1238 C CG  . PRO B 1 41  ? 22.292 -29.611 -4.456  1.00 47.84 ? 41  PRO B CG  1 
ATOM   1239 C CD  . PRO B 1 41  ? 23.541 -29.415 -3.623  1.00 44.47 ? 41  PRO B CD  1 
ATOM   1240 N N   . GLY B 1 42  ? 22.062 -33.633 -1.890  1.00 41.97 ? 42  GLY B N   1 
ATOM   1241 C CA  . GLY B 1 42  ? 22.190 -35.093 -1.705  1.00 44.20 ? 42  GLY B CA  1 
ATOM   1242 C C   . GLY B 1 42  ? 23.405 -35.500 -0.882  1.00 40.94 ? 42  GLY B C   1 
ATOM   1243 O O   . GLY B 1 42  ? 23.653 -36.709 -0.795  1.00 43.34 ? 42  GLY B O   1 
ATOM   1244 N N   . LYS B 1 43  ? 24.134 -34.550 -0.287  1.00 39.39 ? 43  LYS B N   1 
ATOM   1245 C CA  . LYS B 1 43  ? 25.380 -34.834 0.479   1.00 36.84 ? 43  LYS B CA  1 
ATOM   1246 C C   . LYS B 1 43  ? 25.232 -34.361 1.927   1.00 34.15 ? 43  LYS B C   1 
ATOM   1247 O O   . LYS B 1 43  ? 24.328 -33.561 2.204   1.00 31.73 ? 43  LYS B O   1 
ATOM   1248 C CB  . LYS B 1 43  ? 26.588 -34.148 -0.163  1.00 39.95 ? 43  LYS B CB  1 
ATOM   1249 C CG  . LYS B 1 43  ? 26.898 -34.566 -1.592  1.00 44.01 ? 43  LYS B CG  1 
ATOM   1250 C CD  . LYS B 1 43  ? 28.320 -34.245 -1.996  1.00 45.03 ? 43  LYS B CD  1 
ATOM   1251 C CE  . LYS B 1 43  ? 28.448 -33.855 -3.450  1.00 49.26 ? 43  LYS B CE  1 
ATOM   1252 N NZ  . LYS B 1 43  ? 29.854 -33.939 -3.908  1.00 54.88 ? 43  LYS B NZ  1 
ATOM   1253 N N   . GLY B 1 44  ? 26.085 -34.871 2.815   1.00 32.68 ? 44  GLY B N   1 
ATOM   1254 C CA  . GLY B 1 44  ? 26.203 -34.379 4.198   1.00 32.10 ? 44  GLY B CA  1 
ATOM   1255 C C   . GLY B 1 44  ? 27.033 -33.112 4.245   1.00 30.35 ? 44  GLY B C   1 
ATOM   1256 O O   . GLY B 1 44  ? 27.585 -32.723 3.200   1.00 30.30 ? 44  GLY B O   1 
ATOM   1257 N N   . ARG B 1 45  ? 27.132 -32.484 5.416   1.00 30.01 ? 45  ARG B N   1 
ATOM   1258 C CA  . ARG B 1 45  ? 28.051 -31.338 5.636   1.00 27.09 ? 45  ARG B CA  1 
ATOM   1259 C C   . ARG B 1 45  ? 29.488 -31.850 5.546   1.00 26.87 ? 45  ARG B C   1 
ATOM   1260 O O   . ARG B 1 45  ? 29.811 -32.826 6.241   1.00 35.25 ? 45  ARG B O   1 
ATOM   1261 C CB  . ARG B 1 45  ? 27.813 -30.683 6.996   1.00 31.19 ? 45  ARG B CB  1 
ATOM   1262 C CG  . ARG B 1 45  ? 26.526 -29.885 7.066   1.00 34.25 ? 45  ARG B CG  1 
ATOM   1263 C CD  . ARG B 1 45  ? 26.404 -29.093 8.345   1.00 34.75 ? 45  ARG B CD  1 
ATOM   1264 N NE  . ARG B 1 45  ? 25.007 -28.753 8.577   1.00 38.80 ? 45  ARG B NE  1 
ATOM   1265 C CZ  . ARG B 1 45  ? 24.557 -28.002 9.573   1.00 37.43 ? 45  ARG B CZ  1 
ATOM   1266 N NH1 . ARG B 1 45  ? 25.400 -27.481 10.449  1.00 37.59 ? 45  ARG B NH1 1 
ATOM   1267 N NH2 . ARG B 1 45  ? 23.257 -27.774 9.681   1.00 38.95 ? 45  ARG B NH2 1 
ATOM   1268 N N   . GLU B 1 46  ? 30.306 -31.208 4.719   1.00 20.86 ? 46  GLU B N   1 
ATOM   1269 C CA  . GLU B 1 46  ? 31.717 -31.589 4.467   1.00 21.70 ? 46  GLU B CA  1 
ATOM   1270 C C   . GLU B 1 46  ? 32.624 -30.405 4.790   1.00 18.65 ? 46  GLU B C   1 
ATOM   1271 O O   . GLU B 1 46  ? 32.266 -29.288 4.424   1.00 17.97 ? 46  GLU B O   1 
ATOM   1272 C CB  . GLU B 1 46  ? 31.848 -32.032 3.014   1.00 26.26 ? 46  GLU B CB  1 
ATOM   1273 C CG  . GLU B 1 46  ? 30.810 -33.071 2.652   1.00 33.72 ? 46  GLU B CG  1 
ATOM   1274 C CD  . GLU B 1 46  ? 31.005 -33.765 1.315   1.00 37.79 ? 46  GLU B CD  1 
ATOM   1275 O OE1 . GLU B 1 46  ? 31.357 -33.076 0.327   1.00 42.18 ? 46  GLU B OE1 1 
ATOM   1276 O OE2 . GLU B 1 46  ? 30.793 -34.992 1.263   1.00 46.81 ? 46  GLU B OE2 1 
ATOM   1277 N N   . LEU B 1 47  ? 33.749 -30.672 5.456   1.00 18.08 ? 47  LEU B N   1 
ATOM   1278 C CA  . LEU B 1 47  ? 34.764 -29.654 5.800   1.00 19.13 ? 47  LEU B CA  1 
ATOM   1279 C C   . LEU B 1 47  ? 35.383 -29.088 4.522   1.00 20.99 ? 47  LEU B C   1 
ATOM   1280 O O   . LEU B 1 47  ? 35.875 -29.880 3.698   1.00 25.64 ? 47  LEU B O   1 
ATOM   1281 C CB  . LEU B 1 47  ? 35.844 -30.288 6.680   1.00 22.99 ? 47  LEU B CB  1 
ATOM   1282 C CG  . LEU B 1 47  ? 36.955 -29.325 7.090   1.00 24.00 ? 47  LEU B CG  1 
ATOM   1283 C CD1 . LEU B 1 47  ? 36.412 -28.266 8.040   1.00 23.26 ? 47  LEU B CD1 1 
ATOM   1284 C CD2 . LEU B 1 47  ? 38.121 -30.070 7.714   1.00 28.19 ? 47  LEU B CD2 1 
ATOM   1285 N N   . VAL B 1 48  ? 35.341 -27.768 4.364   1.00 19.45 ? 48  VAL B N   1 
ATOM   1286 C CA  . VAL B 1 48  ? 35.931 -27.032 3.209   1.00 20.97 ? 48  VAL B CA  1 
ATOM   1287 C C   . VAL B 1 48  ? 37.316 -26.513 3.628   1.00 19.75 ? 48  VAL B C   1 
ATOM   1288 O O   . VAL B 1 48  ? 38.300 -26.645 2.862   1.00 20.08 ? 48  VAL B O   1 
ATOM   1289 C CB  . VAL B 1 48  ? 34.983 -25.887 2.794   1.00 23.93 ? 48  VAL B CB  1 
ATOM   1290 C CG1 . VAL B 1 48  ? 35.598 -25.008 1.727   1.00 26.84 ? 48  VAL B CG1 1 
ATOM   1291 C CG2 . VAL B 1 48  ? 33.613 -26.395 2.346   1.00 25.58 ? 48  VAL B CG2 1 
ATOM   1292 N N   . ALA B 1 49  ? 37.400 -25.898 4.807   1.00 18.82 ? 49  ALA B N   1 
ATOM   1293 C CA  . ALA B 1 49  ? 38.615 -25.198 5.274   1.00 19.23 ? 49  ALA B CA  1 
ATOM   1294 C C   . ALA B 1 49  ? 38.528 -25.002 6.780   1.00 19.29 ? 49  ALA B C   1 
ATOM   1295 O O   . ALA B 1 49  ? 37.424 -24.770 7.283   1.00 19.82 ? 49  ALA B O   1 
ATOM   1296 C CB  . ALA B 1 49  ? 38.759 -23.882 4.559   1.00 19.82 ? 49  ALA B CB  1 
ATOM   1297 N N   . GLY B 1 50  ? 39.658 -25.088 7.464   1.00 20.97 ? 50  GLY B N   1 
ATOM   1298 C CA  . GLY B 1 50  ? 39.707 -24.873 8.914   1.00 20.79 ? 50  GLY B CA  1 
ATOM   1299 C C   . GLY B 1 50  ? 41.016 -24.240 9.329   1.00 22.76 ? 50  GLY B C   1 
ATOM   1300 O O   . GLY B 1 50  ? 42.028 -24.411 8.621   1.00 23.55 ? 50  GLY B O   1 
ATOM   1301 N N   . ILE B 1 51  ? 40.964 -23.501 10.432  1.00 24.08 ? 51  ILE B N   1 
ATOM   1302 C CA  A ILE B 1 51  ? 42.132 -22.873 11.127  0.50 26.88 ? 51  ILE B CA  1 
ATOM   1303 C CA  B ILE B 1 51  ? 42.168 -22.947 11.099  0.50 26.27 ? 51  ILE B CA  1 
ATOM   1304 C C   . ILE B 1 51  ? 42.088 -23.325 12.584  1.00 27.39 ? 51  ILE B C   1 
ATOM   1305 O O   . ILE B 1 51  ? 41.057 -23.055 13.217  1.00 27.13 ? 51  ILE B O   1 
ATOM   1306 C CB  A ILE B 1 51  ? 42.092 -21.331 11.075  0.50 29.02 ? 51  ILE B CB  1 
ATOM   1307 C CB  B ILE B 1 51  ? 42.287 -21.441 10.794  0.50 27.49 ? 51  ILE B CB  1 
ATOM   1308 C CG1 A ILE B 1 51  ? 42.201 -20.779 9.655   0.50 30.64 ? 51  ILE B CG1 1 
ATOM   1309 C CG1 B ILE B 1 51  ? 43.559 -20.832 11.386  0.50 31.40 ? 51  ILE B CG1 1 
ATOM   1310 C CG2 A ILE B 1 51  ? 43.156 -20.726 11.984  0.50 31.77 ? 51  ILE B CG2 1 
ATOM   1311 C CG2 B ILE B 1 51  ? 41.035 -20.677 11.202  0.50 27.22 ? 51  ILE B CG2 1 
ATOM   1312 C CD1 A ILE B 1 51  ? 42.716 -19.355 9.592   0.50 31.92 ? 51  ILE B CD1 1 
ATOM   1313 C CD1 B ILE B 1 51  ? 43.953 -19.525 10.737  0.50 34.22 ? 51  ILE B CD1 1 
ATOM   1314 N N   . ILE B 1 52  ? 43.145 -23.980 13.068  1.00 29.90 ? 52  ILE B N   1 
ATOM   1315 C CA  . ILE B 1 52  ? 43.313 -24.367 14.499  1.00 33.74 ? 52  ILE B CA  1 
ATOM   1316 C C   . ILE B 1 52  ? 44.082 -23.228 15.176  1.00 37.55 ? 52  ILE B C   1 
ATOM   1317 O O   . ILE B 1 52  ? 44.974 -22.654 14.526  1.00 42.58 ? 52  ILE B O   1 
ATOM   1318 C CB  . ILE B 1 52  ? 44.025 -25.726 14.638  1.00 37.01 ? 52  ILE B CB  1 
ATOM   1319 C CG1 . ILE B 1 52  ? 43.151 -26.878 14.130  1.00 39.50 ? 52  ILE B CG1 1 
ATOM   1320 C CG2 . ILE B 1 52  ? 44.492 -25.964 16.069  1.00 39.38 ? 52  ILE B CG2 1 
ATOM   1321 C CD1 . ILE B 1 52  ? 43.934 -28.115 13.747  1.00 42.96 ? 52  ILE B CD1 1 
ATOM   1322 N N   . SER B 1 53  ? 43.699 -22.862 16.400  1.00 39.03 ? 53  SER B N   1 
ATOM   1323 C CA  . SER B 1 53  ? 44.257 -21.674 17.095  1.00 44.79 ? 53  SER B CA  1 
ATOM   1324 C C   . SER B 1 53  ? 45.773 -21.848 17.208  1.00 48.16 ? 53  SER B C   1 
ATOM   1325 O O   . SER B 1 53  ? 46.197 -22.801 17.884  1.00 53.08 ? 53  SER B O   1 
ATOM   1326 C CB  . SER B 1 53  ? 43.584 -21.454 18.412  1.00 48.67 ? 53  SER B CB  1 
ATOM   1327 O OG  . SER B 1 53  ? 42.194 -21.245 18.205  1.00 51.34 ? 53  SER B OG  1 
ATOM   1328 N N   . GLY B 1 54  ? 46.534 -20.983 16.525  1.00 55.46 ? 54  GLY B N   1 
ATOM   1329 C CA  . GLY B 1 54  ? 47.961 -21.183 16.202  1.00 55.67 ? 54  GLY B CA  1 
ATOM   1330 C C   . GLY B 1 54  ? 48.238 -20.959 14.721  1.00 58.31 ? 54  GLY B C   1 
ATOM   1331 O O   . GLY B 1 54  ? 49.399 -20.669 14.383  1.00 58.75 ? 54  GLY B O   1 
ATOM   1332 N N   . GLY B 1 55  ? 47.216 -21.103 13.866  1.00 57.41 ? 55  GLY B N   1 
ATOM   1333 C CA  . GLY B 1 55  ? 47.270 -20.737 12.434  1.00 56.02 ? 55  GLY B CA  1 
ATOM   1334 C C   . GLY B 1 55  ? 47.367 -21.940 11.509  1.00 51.81 ? 55  GLY B C   1 
ATOM   1335 O O   . GLY B 1 55  ? 47.295 -21.730 10.286  1.00 51.63 ? 55  GLY B O   1 
ATOM   1336 N N   . SER B 1 56  ? 47.545 -23.144 12.068  1.00 53.39 ? 56  SER B N   1 
ATOM   1337 C CA  . SER B 1 56  ? 47.596 -24.456 11.363  1.00 45.45 ? 56  SER B CA  1 
ATOM   1338 C C   . SER B 1 56  ? 46.339 -24.651 10.504  1.00 40.23 ? 56  SER B C   1 
ATOM   1339 O O   . SER B 1 56  ? 45.273 -24.965 11.061  1.00 39.76 ? 56  SER B O   1 
ATOM   1340 C CB  . SER B 1 56  ? 47.756 -25.556 12.375  1.00 48.46 ? 56  SER B CB  1 
ATOM   1341 O OG  . SER B 1 56  ? 48.340 -25.034 13.564  1.00 54.12 ? 56  SER B OG  1 
ATOM   1342 N N   . THR B 1 57  ? 46.457 -24.425 9.195   1.00 37.10 ? 57  THR B N   1 
ATOM   1343 C CA  . THR B 1 57  ? 45.311 -24.266 8.257   1.00 37.07 ? 57  THR B CA  1 
ATOM   1344 C C   . THR B 1 57  ? 45.204 -25.526 7.397   1.00 32.15 ? 57  THR B C   1 
ATOM   1345 O O   . THR B 1 57  ? 46.261 -26.078 7.037   1.00 37.49 ? 57  THR B O   1 
ATOM   1346 C CB  . THR B 1 57  ? 45.486 -22.984 7.434   1.00 41.47 ? 57  THR B CB  1 
ATOM   1347 O OG1 . THR B 1 57  ? 45.368 -21.891 8.347   1.00 46.39 ? 57  THR B OG1 1 
ATOM   1348 C CG2 . THR B 1 57  ? 44.485 -22.844 6.311   1.00 42.71 ? 57  THR B CG2 1 
ATOM   1349 N N   . SER B 1 58  ? 43.984 -25.969 7.090   1.00 28.34 ? 58  SER B N   1 
ATOM   1350 C CA  . SER B 1 58  ? 43.739 -27.179 6.269   1.00 28.67 ? 58  SER B CA  1 
ATOM   1351 C C   . SER B 1 58  ? 42.564 -26.934 5.317   1.00 25.23 ? 58  SER B C   1 
ATOM   1352 O O   . SER B 1 58  ? 41.670 -26.121 5.636   1.00 24.12 ? 58  SER B O   1 
ATOM   1353 C CB  . SER B 1 58  ? 43.552 -28.393 7.134   1.00 30.14 ? 58  SER B CB  1 
ATOM   1354 O OG  . SER B 1 58  ? 42.348 -28.316 7.844   1.00 37.17 ? 58  SER B OG  1 
ATOM   1355 N N   . TYR B 1 59  ? 42.629 -27.569 4.146   1.00 20.59 ? 59  TYR B N   1 
ATOM   1356 C CA  . TYR B 1 59  ? 41.664 -27.392 3.032   1.00 19.94 ? 59  TYR B CA  1 
ATOM   1357 C C   . TYR B 1 59  ? 41.291 -28.751 2.455   1.00 20.78 ? 59  TYR B C   1 
ATOM   1358 O O   . TYR B 1 59  ? 42.187 -29.629 2.319   1.00 21.33 ? 59  TYR B O   1 
ATOM   1359 C CB  . TYR B 1 59  ? 42.265 -26.547 1.907   1.00 20.44 ? 59  TYR B CB  1 
ATOM   1360 C CG  . TYR B 1 59  ? 42.543 -25.119 2.283   1.00 20.82 ? 59  TYR B CG  1 
ATOM   1361 C CD1 . TYR B 1 59  ? 43.799 -24.732 2.722   1.00 21.29 ? 59  TYR B CD1 1 
ATOM   1362 C CD2 . TYR B 1 59  ? 41.548 -24.158 2.205   1.00 20.39 ? 59  TYR B CD2 1 
ATOM   1363 C CE1 . TYR B 1 59  ? 44.068 -23.416 3.063   1.00 22.89 ? 59  TYR B CE1 1 
ATOM   1364 C CE2 . TYR B 1 59  ? 41.798 -22.842 2.554   1.00 22.50 ? 59  TYR B CE2 1 
ATOM   1365 C CZ  . TYR B 1 59  ? 43.062 -22.468 2.977   1.00 23.05 ? 59  TYR B CZ  1 
ATOM   1366 O OH  . TYR B 1 59  ? 43.299 -21.175 3.333   1.00 23.32 ? 59  TYR B OH  1 
ATOM   1367 N N   . ALA B 1 60  ? 40.024 -28.904 2.069   1.00 20.11 ? 60  ALA B N   1 
ATOM   1368 C CA  . ALA B 1 60  ? 39.597 -29.987 1.162   1.00 20.49 ? 60  ALA B CA  1 
ATOM   1369 C C   . ALA B 1 60  ? 40.391 -29.814 -0.139  1.00 20.52 ? 60  ALA B C   1 
ATOM   1370 O O   . ALA B 1 60  ? 40.550 -28.668 -0.591  1.00 19.42 ? 60  ALA B O   1 
ATOM   1371 C CB  . ALA B 1 60  ? 38.112 -29.937 0.930   1.00 22.32 ? 60  ALA B CB  1 
ATOM   1372 N N   . ASP B 1 61  ? 40.899 -30.898 -0.712  1.00 18.32 ? 61  ASP B N   1 
ATOM   1373 C CA  . ASP B 1 61  ? 41.694 -30.805 -1.965  1.00 19.14 ? 61  ASP B CA  1 
ATOM   1374 C C   . ASP B 1 61  ? 40.807 -30.218 -3.073  1.00 19.19 ? 61  ASP B C   1 
ATOM   1375 O O   . ASP B 1 61  ? 41.372 -29.581 -3.969  1.00 21.01 ? 61  ASP B O   1 
ATOM   1376 C CB  . ASP B 1 61  ? 42.325 -32.143 -2.326  1.00 19.15 ? 61  ASP B CB  1 
ATOM   1377 C CG  . ASP B 1 61  ? 41.300 -33.202 -2.655  1.00 20.58 ? 61  ASP B CG  1 
ATOM   1378 O OD1 . ASP B 1 61  ? 40.913 -33.923 -1.727  1.00 22.20 ? 61  ASP B OD1 1 
ATOM   1379 O OD2 . ASP B 1 61  ? 40.890 -33.271 -3.820  1.00 22.03 ? 61  ASP B OD2 1 
ATOM   1380 N N   . SER B 1 62  ? 39.481 -30.382 -3.020  1.00 20.30 ? 62  SER B N   1 
ATOM   1381 C CA  . SER B 1 62  ? 38.537 -29.851 -4.047  1.00 21.41 ? 62  SER B CA  1 
ATOM   1382 C C   . SER B 1 62  ? 38.594 -28.314 -4.133  1.00 21.12 ? 62  SER B C   1 
ATOM   1383 O O   . SER B 1 62  ? 38.175 -27.781 -5.175  1.00 23.49 ? 62  SER B O   1 
ATOM   1384 C CB  . SER B 1 62  ? 37.136 -30.328 -3.787  1.00 23.06 ? 62  SER B CB  1 
ATOM   1385 O OG  . SER B 1 62  ? 36.705 -29.911 -2.506  1.00 24.44 ? 62  SER B OG  1 
ATOM   1386 N N   . VAL B 1 63  ? 39.070 -27.614 -3.090  1.00 18.80 ? 63  VAL B N   1 
ATOM   1387 C CA  . VAL B 1 63  ? 39.070 -26.121 -3.044  1.00 20.80 ? 63  VAL B CA  1 
ATOM   1388 C C   . VAL B 1 63  ? 40.491 -25.571 -2.853  1.00 21.96 ? 63  VAL B C   1 
ATOM   1389 O O   . VAL B 1 63  ? 40.651 -24.346 -2.909  1.00 21.48 ? 63  VAL B O   1 
ATOM   1390 C CB  . VAL B 1 63  ? 38.100 -25.594 -1.964  1.00 19.12 ? 63  VAL B CB  1 
ATOM   1391 C CG1 . VAL B 1 63  ? 36.712 -26.205 -2.108  1.00 18.91 ? 63  VAL B CG1 1 
ATOM   1392 C CG2 . VAL B 1 63  ? 38.628 -25.792 -0.553  1.00 20.47 ? 63  VAL B CG2 1 
ATOM   1393 N N   . LYS B 1 64  ? 41.490 -26.426 -2.638  1.00 25.02 ? 64  LYS B N   1 
ATOM   1394 C CA  . LYS B 1 64  ? 42.899 -26.006 -2.416  1.00 28.16 ? 64  LYS B CA  1 
ATOM   1395 C C   . LYS B 1 64  ? 43.329 -25.139 -3.605  1.00 26.60 ? 64  LYS B C   1 
ATOM   1396 O O   . LYS B 1 64  ? 43.056 -25.535 -4.747  1.00 28.15 ? 64  LYS B O   1 
ATOM   1397 C CB  . LYS B 1 64  ? 43.804 -27.231 -2.231  1.00 31.61 ? 64  LYS B CB  1 
ATOM   1398 C CG  . LYS B 1 64  ? 45.278 -26.932 -1.994  1.00 37.35 ? 64  LYS B CG  1 
ATOM   1399 C CD  . LYS B 1 64  ? 45.533 -26.027 -0.803  1.00 40.46 ? 64  LYS B CD  1 
ATOM   1400 C CE  . LYS B 1 64  ? 47.001 -25.861 -0.469  1.00 44.82 ? 64  LYS B CE  1 
ATOM   1401 N NZ  . LYS B 1 64  ? 47.604 -27.123 0.023   1.00 44.46 ? 64  LYS B NZ  1 
ATOM   1402 N N   . GLY B 1 65  ? 43.912 -23.970 -3.325  1.00 29.98 ? 65  GLY B N   1 
ATOM   1403 C CA  . GLY B 1 65  ? 44.419 -23.024 -4.338  1.00 31.10 ? 65  GLY B CA  1 
ATOM   1404 C C   . GLY B 1 65  ? 43.373 -22.011 -4.792  1.00 31.95 ? 65  GLY B C   1 
ATOM   1405 O O   . GLY B 1 65  ? 43.777 -20.972 -5.339  1.00 35.51 ? 65  GLY B O   1 
ATOM   1406 N N   . ARG B 1 66  ? 42.082 -22.278 -4.570  1.00 26.77 ? 66  ARG B N   1 
ATOM   1407 C CA  . ARG B 1 66  ? 40.959 -21.407 -5.010  1.00 25.69 ? 66  ARG B CA  1 
ATOM   1408 C C   . ARG B 1 66  ? 40.329 -20.686 -3.814  1.00 26.27 ? 66  ARG B C   1 
ATOM   1409 O O   . ARG B 1 66  ? 39.931 -19.522 -3.982  1.00 27.08 ? 66  ARG B O   1 
ATOM   1410 C CB  . ARG B 1 66  ? 39.907 -22.241 -5.741  1.00 25.67 ? 66  ARG B CB  1 
ATOM   1411 C CG  . ARG B 1 66  ? 40.446 -22.953 -6.969  1.00 27.43 ? 66  ARG B CG  1 
ATOM   1412 C CD  . ARG B 1 66  ? 39.367 -23.640 -7.780  1.00 25.36 ? 66  ARG B CD  1 
ATOM   1413 N NE  . ARG B 1 66  ? 38.600 -24.622 -7.020  1.00 24.98 ? 66  ARG B NE  1 
ATOM   1414 C CZ  . ARG B 1 66  ? 37.305 -24.534 -6.730  1.00 23.43 ? 66  ARG B CZ  1 
ATOM   1415 N NH1 . ARG B 1 66  ? 36.729 -25.485 -6.012  1.00 21.76 ? 66  ARG B NH1 1 
ATOM   1416 N NH2 . ARG B 1 66  ? 36.582 -23.512 -7.138  1.00 23.64 ? 66  ARG B NH2 1 
ATOM   1417 N N   . PHE B 1 67  ? 40.196 -21.366 -2.674  1.00 24.12 ? 67  PHE B N   1 
ATOM   1418 C CA  . PHE B 1 67  ? 39.569 -20.812 -1.453  1.00 23.59 ? 67  PHE B CA  1 
ATOM   1419 C C   . PHE B 1 67  ? 40.645 -20.529 -0.408  1.00 24.28 ? 67  PHE B C   1 
ATOM   1420 O O   . PHE B 1 67  ? 41.597 -21.323 -0.281  1.00 28.22 ? 67  PHE B O   1 
ATOM   1421 C CB  . PHE B 1 67  ? 38.543 -21.775 -0.867  1.00 22.32 ? 67  PHE B CB  1 
ATOM   1422 C CG  . PHE B 1 67  ? 37.298 -22.024 -1.679  1.00 21.62 ? 67  PHE B CG  1 
ATOM   1423 C CD1 . PHE B 1 67  ? 37.182 -21.636 -3.009  1.00 22.89 ? 67  PHE B CD1 1 
ATOM   1424 C CD2 . PHE B 1 67  ? 36.237 -22.695 -1.091  1.00 20.76 ? 67  PHE B CD2 1 
ATOM   1425 C CE1 . PHE B 1 67  ? 36.022 -21.902 -3.720  1.00 21.58 ? 67  PHE B CE1 1 
ATOM   1426 C CE2 . PHE B 1 67  ? 35.092 -22.979 -1.811  1.00 20.09 ? 67  PHE B CE2 1 
ATOM   1427 C CZ  . PHE B 1 67  ? 34.982 -22.569 -3.116  1.00 22.18 ? 67  PHE B CZ  1 
ATOM   1428 N N   . THR B 1 68  ? 40.484 -19.424 0.322   1.00 23.54 ? 68  THR B N   1 
ATOM   1429 C CA  . THR B 1 68  ? 41.390 -19.019 1.426   1.00 25.07 ? 68  THR B CA  1 
ATOM   1430 C C   . THR B 1 68  ? 40.571 -18.720 2.679   1.00 24.17 ? 68  THR B C   1 
ATOM   1431 O O   . THR B 1 68  ? 39.691 -17.859 2.611   1.00 25.56 ? 68  THR B O   1 
ATOM   1432 C CB  . THR B 1 68  ? 42.250 -17.806 1.070   1.00 26.84 ? 68  THR B CB  1 
ATOM   1433 O OG1 . THR B 1 68  ? 42.985 -18.124 -0.108  1.00 29.75 ? 68  THR B OG1 1 
ATOM   1434 C CG2 . THR B 1 68  ? 43.208 -17.440 2.182   1.00 29.88 ? 68  THR B CG2 1 
ATOM   1435 N N   . ILE B 1 69  ? 40.891 -19.391 3.778   1.00 23.23 ? 69  ILE B N   1 
ATOM   1436 C CA  . ILE B 1 69  ? 40.298 -19.117 5.118   1.00 23.78 ? 69  ILE B CA  1 
ATOM   1437 C C   . ILE B 1 69  ? 41.218 -18.115 5.817   1.00 26.24 ? 69  ILE B C   1 
ATOM   1438 O O   . ILE B 1 69  ? 42.456 -18.224 5.683   1.00 28.41 ? 69  ILE B O   1 
ATOM   1439 C CB  . ILE B 1 69  ? 40.075 -20.409 5.929   1.00 23.14 ? 69  ILE B CB  1 
ATOM   1440 C CG1 . ILE B 1 69  ? 39.222 -20.174 7.179   1.00 21.48 ? 69  ILE B CG1 1 
ATOM   1441 C CG2 . ILE B 1 69  ? 41.391 -21.080 6.280   1.00 24.15 ? 69  ILE B CG2 1 
ATOM   1442 C CD1 . ILE B 1 69  ? 38.835 -21.466 7.883   1.00 22.57 ? 69  ILE B CD1 1 
ATOM   1443 N N   . SER B 1 70  ? 40.622 -17.126 6.474   1.00 25.92 ? 70  SER B N   1 
ATOM   1444 C CA  . SER B 1 70  ? 41.341 -16.090 7.252   1.00 28.17 ? 70  SER B CA  1 
ATOM   1445 C C   . SER B 1 70  ? 40.419 -15.604 8.364   1.00 28.12 ? 70  SER B C   1 
ATOM   1446 O O   . SER B 1 70  ? 39.222 -15.915 8.334   1.00 27.51 ? 70  SER B O   1 
ATOM   1447 C CB  . SER B 1 70  ? 41.808 -14.957 6.375   1.00 27.80 ? 70  SER B CB  1 
ATOM   1448 O OG  . SER B 1 70  ? 40.708 -14.274 5.790   1.00 27.97 ? 70  SER B OG  1 
ATOM   1449 N N   . ARG B 1 71  ? 40.963 -14.866 9.314   1.00 31.39 ? 71  ARG B N   1 
ATOM   1450 C CA  . ARG B 1 71  ? 40.197 -14.387 10.487  1.00 32.68 ? 71  ARG B CA  1 
ATOM   1451 C C   . ARG B 1 71  ? 40.676 -12.978 10.814  1.00 34.48 ? 71  ARG B C   1 
ATOM   1452 O O   . ARG B 1 71  ? 41.861 -12.678 10.541  1.00 34.68 ? 71  ARG B O   1 
ATOM   1453 C CB  . ARG B 1 71  ? 40.414 -15.341 11.663  1.00 37.08 ? 71  ARG B CB  1 
ATOM   1454 C CG  . ARG B 1 71  ? 41.878 -15.505 12.050  1.00 40.61 ? 71  ARG B CG  1 
ATOM   1455 C CD  . ARG B 1 71  ? 42.108 -16.598 13.066  1.00 43.32 ? 71  ARG B CD  1 
ATOM   1456 N NE  . ARG B 1 71  ? 43.512 -16.960 13.204  1.00 46.73 ? 71  ARG B NE  1 
ATOM   1457 C CZ  . ARG B 1 71  ? 43.963 -17.986 13.922  1.00 51.91 ? 71  ARG B CZ  1 
ATOM   1458 N NH1 . ARG B 1 71  ? 43.121 -18.767 14.580  1.00 55.14 ? 71  ARG B NH1 1 
ATOM   1459 N NH2 . ARG B 1 71  ? 45.261 -18.230 13.978  1.00 56.35 ? 71  ARG B NH2 1 
ATOM   1460 N N   . ASP B 1 72  ? 39.772 -12.145 11.308  1.00 36.88 ? 72  ASP B N   1 
ATOM   1461 C CA  . ASP B 1 72  ? 40.126 -10.892 12.013  1.00 41.59 ? 72  ASP B CA  1 
ATOM   1462 C C   . ASP B 1 72  ? 39.709 -11.086 13.469  1.00 45.18 ? 72  ASP B C   1 
ATOM   1463 O O   . ASP B 1 72  ? 38.517 -10.901 13.748  1.00 39.53 ? 72  ASP B O   1 
ATOM   1464 C CB  . ASP B 1 72  ? 39.458 -9.686  11.349  1.00 43.76 ? 72  ASP B CB  1 
ATOM   1465 C CG  . ASP B 1 72  ? 39.915 -8.363  11.921  1.00 49.34 ? 72  ASP B CG  1 
ATOM   1466 O OD1 . ASP B 1 72  ? 40.248 -8.333  13.112  1.00 55.58 ? 72  ASP B OD1 1 
ATOM   1467 O OD2 . ASP B 1 72  ? 39.925 -7.376  11.167  1.00 51.82 ? 72  ASP B OD2 1 
ATOM   1468 N N   . ASN B 1 73  ? 40.628 -11.495 14.348  1.00 49.83 ? 73  ASN B N   1 
ATOM   1469 C CA  . ASN B 1 73  ? 40.316 -11.790 15.776  1.00 53.16 ? 73  ASN B CA  1 
ATOM   1470 C C   . ASN B 1 73  ? 39.925 -10.489 16.486  1.00 57.61 ? 73  ASN B C   1 
ATOM   1471 O O   . ASN B 1 73  ? 39.123 -10.570 17.421  1.00 60.10 ? 73  ASN B O   1 
ATOM   1472 C CB  . ASN B 1 73  ? 41.444 -12.551 16.485  1.00 55.04 ? 73  ASN B CB  1 
ATOM   1473 C CG  . ASN B 1 73  ? 41.398 -14.043 16.223  1.00 54.77 ? 73  ASN B CG  1 
ATOM   1474 O OD1 . ASN B 1 73  ? 42.425 -14.718 16.266  1.00 62.00 ? 73  ASN B OD1 1 
ATOM   1475 N ND2 . ASN B 1 73  ? 40.216 -14.574 15.955  1.00 51.27 ? 73  ASN B ND2 1 
ATOM   1476 N N   . ALA B 1 74  ? 40.437 -9.336  16.049  1.00 58.01 ? 74  ALA B N   1 
ATOM   1477 C CA  . ALA B 1 74  ? 40.052 -7.994  16.551  1.00 60.15 ? 74  ALA B CA  1 
ATOM   1478 C C   . ALA B 1 74  ? 38.551 -7.745  16.327  1.00 57.70 ? 74  ALA B C   1 
ATOM   1479 O O   . ALA B 1 74  ? 37.930 -7.098  17.179  1.00 59.16 ? 74  ALA B O   1 
ATOM   1480 C CB  . ALA B 1 74  ? 40.894 -6.933  15.883  1.00 61.75 ? 74  ALA B CB  1 
ATOM   1481 N N   . LYS B 1 75  ? 37.992 -8.245  15.222  1.00 54.68 ? 75  LYS B N   1 
ATOM   1482 C CA  . LYS B 1 75  ? 36.574 -8.034  14.817  1.00 54.22 ? 75  LYS B CA  1 
ATOM   1483 C C   . LYS B 1 75  ? 35.756 -9.322  15.014  1.00 50.11 ? 75  LYS B C   1 
ATOM   1484 O O   . LYS B 1 75  ? 34.584 -9.348  14.592  1.00 50.38 ? 75  LYS B O   1 
ATOM   1485 C CB  . LYS B 1 75  ? 36.537 -7.524  13.372  1.00 60.00 ? 75  LYS B CB  1 
ATOM   1486 C CG  . LYS B 1 75  ? 36.712 -6.014  13.257  1.00 62.86 ? 75  LYS B CG  1 
ATOM   1487 C CD  . LYS B 1 75  ? 37.139 -5.503  11.897  1.00 64.72 ? 75  LYS B CD  1 
ATOM   1488 C CE  . LYS B 1 75  ? 36.212 -5.893  10.767  1.00 63.40 ? 75  LYS B CE  1 
ATOM   1489 N NZ  . LYS B 1 75  ? 36.509 -5.109  9.545   1.00 63.39 ? 75  LYS B NZ  1 
ATOM   1490 N N   . ASN B 1 76  ? 36.339 -10.342 15.648  1.00 44.72 ? 76  ASN B N   1 
ATOM   1491 C CA  . ASN B 1 76  ? 35.680 -11.639 15.961  1.00 39.12 ? 76  ASN B CA  1 
ATOM   1492 C C   . ASN B 1 76  ? 35.013 -12.185 14.695  1.00 32.21 ? 76  ASN B C   1 
ATOM   1493 O O   . ASN B 1 76  ? 33.870 -12.648 14.789  1.00 29.94 ? 76  ASN B O   1 
ATOM   1494 C CB  . ASN B 1 76  ? 34.659 -11.492 17.095  1.00 40.98 ? 76  ASN B CB  1 
ATOM   1495 C CG  . ASN B 1 76  ? 35.267 -11.001 18.391  1.00 47.11 ? 76  ASN B CG  1 
ATOM   1496 O OD1 . ASN B 1 76  ? 34.665 -10.198 19.103  1.00 53.85 ? 76  ASN B OD1 1 
ATOM   1497 N ND2 . ASN B 1 76  ? 36.465 -11.467 18.698  1.00 53.67 ? 76  ASN B ND2 1 
ATOM   1498 N N   . THR B 1 77  ? 35.680 -12.102 13.544  1.00 29.38 ? 77  THR B N   1 
ATOM   1499 C CA  . THR B 1 77  ? 35.095 -12.490 12.237  1.00 28.92 ? 77  THR B CA  1 
ATOM   1500 C C   . THR B 1 77  ? 35.994 -13.523 11.551  1.00 26.42 ? 77  THR B C   1 
ATOM   1501 O O   . THR B 1 77  ? 37.234 -13.407 11.627  1.00 28.19 ? 77  THR B O   1 
ATOM   1502 C CB  . THR B 1 77  ? 34.823 -11.272 11.345  1.00 32.58 ? 77  THR B CB  1 
ATOM   1503 O OG1 . THR B 1 77  ? 33.941 -10.375 12.024  1.00 37.42 ? 77  THR B OG1 1 
ATOM   1504 C CG2 . THR B 1 77  ? 34.176 -11.641 10.031  1.00 31.80 ? 77  THR B CG2 1 
ATOM   1505 N N   . LEU B 1 78  ? 35.360 -14.504 10.909  1.00 23.76 ? 78  LEU B N   1 
ATOM   1506 C CA  . LEU B 1 78  ? 36.008 -15.548 10.080  1.00 23.38 ? 78  LEU B CA  1 
ATOM   1507 C C   . LEU B 1 78  ? 35.623 -15.284 8.625   1.00 20.32 ? 78  LEU B C   1 
ATOM   1508 O O   . LEU B 1 78  ? 34.450 -14.922 8.377   1.00 22.62 ? 78  LEU B O   1 
ATOM   1509 C CB  . LEU B 1 78  ? 35.524 -16.926 10.542  1.00 22.70 ? 78  LEU B CB  1 
ATOM   1510 C CG  . LEU B 1 78  ? 36.020 -18.116 9.719   1.00 22.13 ? 78  LEU B CG  1 
ATOM   1511 C CD1 . LEU B 1 78  ? 37.506 -18.338 9.964   1.00 23.21 ? 78  LEU B CD1 1 
ATOM   1512 C CD2 . LEU B 1 78  ? 35.244 -19.393 10.044  1.00 23.49 ? 78  LEU B CD2 1 
ATOM   1513 N N   . TYR B 1 79  ? 36.560 -15.460 7.699   1.00 19.61 ? 79  TYR B N   1 
ATOM   1514 C CA  . TYR B 1 79  ? 36.326 -15.230 6.254   1.00 20.58 ? 79  TYR B CA  1 
ATOM   1515 C C   . TYR B 1 79  ? 36.624 -16.488 5.439   1.00 20.41 ? 79  TYR B C   1 
ATOM   1516 O O   . TYR B 1 79  ? 37.499 -17.273 5.800   1.00 20.88 ? 79  TYR B O   1 
ATOM   1517 C CB  . TYR B 1 79  ? 37.188 -14.083 5.731   1.00 22.43 ? 79  TYR B CB  1 
ATOM   1518 C CG  . TYR B 1 79  ? 37.007 -12.795 6.487   1.00 24.45 ? 79  TYR B CG  1 
ATOM   1519 C CD1 . TYR B 1 79  ? 35.874 -12.011 6.323   1.00 26.81 ? 79  TYR B CD1 1 
ATOM   1520 C CD2 . TYR B 1 79  ? 37.964 -12.370 7.390   1.00 27.76 ? 79  TYR B CD2 1 
ATOM   1521 C CE1 . TYR B 1 79  ? 35.710 -10.824 7.017   1.00 28.04 ? 79  TYR B CE1 1 
ATOM   1522 C CE2 . TYR B 1 79  ? 37.814 -11.188 8.093   1.00 29.27 ? 79  TYR B CE2 1 
ATOM   1523 C CZ  . TYR B 1 79  ? 36.685 -10.413 7.907   1.00 27.96 ? 79  TYR B CZ  1 
ATOM   1524 O OH  . TYR B 1 79  ? 36.532 -9.260  8.614   1.00 34.39 ? 79  TYR B OH  1 
ATOM   1525 N N   . LEU B 1 80  ? 35.913 -16.626 4.327   1.00 20.59 ? 80  LEU B N   1 
ATOM   1526 C CA  . LEU B 1 80  ? 36.274 -17.573 3.255   1.00 20.85 ? 80  LEU B CA  1 
ATOM   1527 C C   . LEU B 1 80  ? 36.280 -16.805 1.939   1.00 20.29 ? 80  LEU B C   1 
ATOM   1528 O O   . LEU B 1 80  ? 35.203 -16.430 1.449   1.00 20.57 ? 80  LEU B O   1 
ATOM   1529 C CB  . LEU B 1 80  ? 35.306 -18.749 3.216   1.00 20.29 ? 80  LEU B CB  1 
ATOM   1530 C CG  . LEU B 1 80  ? 35.726 -19.878 2.276   1.00 20.65 ? 80  LEU B CG  1 
ATOM   1531 C CD1 . LEU B 1 80  ? 36.984 -20.563 2.782   1.00 20.66 ? 80  LEU B CD1 1 
ATOM   1532 C CD2 . LEU B 1 80  ? 34.599 -20.888 2.098   1.00 20.22 ? 80  LEU B CD2 1 
ATOM   1533 N N   . GLN B 1 81  ? 37.473 -16.567 1.402   1.00 23.30 ? 81  GLN B N   1 
ATOM   1534 C CA  . GLN B 1 81  ? 37.659 -15.985 0.053   1.00 24.06 ? 81  GLN B CA  1 
ATOM   1535 C C   . GLN B 1 81  ? 37.510 -17.111 -0.963  1.00 24.29 ? 81  GLN B C   1 
ATOM   1536 O O   . GLN B 1 81  ? 38.290 -18.069 -0.876  1.00 25.48 ? 81  GLN B O   1 
ATOM   1537 C CB  . GLN B 1 81  ? 39.034 -15.339 -0.102  1.00 25.32 ? 81  GLN B CB  1 
ATOM   1538 C CG  . GLN B 1 81  ? 39.208 -14.667 -1.457  1.00 27.47 ? 81  GLN B CG  1 
ATOM   1539 C CD  . GLN B 1 81  ? 38.222 -13.539 -1.644  1.00 27.60 ? 81  GLN B CD  1 
ATOM   1540 O OE1 . GLN B 1 81  ? 38.048 -12.680 -0.778  1.00 29.30 ? 81  GLN B OE1 1 
ATOM   1541 N NE2 . GLN B 1 81  ? 37.529 -13.558 -2.770  1.00 28.87 ? 81  GLN B NE2 1 
ATOM   1542 N N   . MET B 1 82  ? 36.518 -17.013 -1.847  1.00 23.03 ? 82  MET B N   1 
ATOM   1543 C CA  . MET B 1 82  ? 36.169 -18.089 -2.803  1.00 22.90 ? 82  MET B CA  1 
ATOM   1544 C C   . MET B 1 82  ? 36.417 -17.566 -4.215  1.00 23.95 ? 82  MET B C   1 
ATOM   1545 O O   . MET B 1 82  ? 35.591 -16.789 -4.703  1.00 24.48 ? 82  MET B O   1 
ATOM   1546 C CB  . MET B 1 82  ? 34.708 -18.524 -2.657  1.00 24.65 ? 82  MET B CB  1 
ATOM   1547 C CG  . MET B 1 82  ? 34.377 -19.005 -1.263  1.00 25.30 ? 82  MET B CG  1 
ATOM   1548 S SD  . MET B 1 82  ? 32.602 -19.159 -0.951  1.00 28.73 ? 82  MET B SD  1 
ATOM   1549 C CE  . MET B 1 82  ? 32.236 -20.698 -1.780  1.00 26.96 ? 82  MET B CE  1 
ATOM   1550 N N   . ASN B 1 83  ? 37.514 -17.980 -4.842  1.00 24.16 ? 83  ASN B N   1 
ATOM   1551 C CA  . ASN B 1 83  ? 37.889 -17.524 -6.205  1.00 26.20 ? 83  ASN B CA  1 
ATOM   1552 C C   . ASN B 1 83  ? 37.657 -18.668 -7.189  1.00 24.18 ? 83  ASN B C   1 
ATOM   1553 O O   . ASN B 1 83  ? 37.561 -19.823 -6.753  1.00 24.26 ? 83  ASN B O   1 
ATOM   1554 C CB  . ASN B 1 83  ? 39.327 -17.015 -6.252  1.00 29.82 ? 83  ASN B CB  1 
ATOM   1555 C CG  . ASN B 1 83  ? 39.566 -15.811 -5.364  1.00 29.96 ? 83  ASN B CG  1 
ATOM   1556 O OD1 . ASN B 1 83  ? 38.694 -14.962 -5.190  1.00 32.78 ? 83  ASN B OD1 1 
ATOM   1557 N ND2 . ASN B 1 83  ? 40.752 -15.722 -4.798  1.00 31.85 ? 83  ASN B ND2 1 
ATOM   1558 N N   . SER B 1 84  ? 37.586 -18.350 -8.479  1.00 25.63 ? 84  SER B N   1 
ATOM   1559 C CA  . SER B 1 84  ? 37.510 -19.349 -9.572  1.00 27.65 ? 84  SER B CA  1 
ATOM   1560 C C   . SER B 1 84  ? 36.376 -20.335 -9.281  1.00 26.00 ? 84  SER B C   1 
ATOM   1561 O O   . SER B 1 84  ? 36.603 -21.550 -9.366  1.00 25.38 ? 84  SER B O   1 
ATOM   1562 C CB  . SER B 1 84  ? 38.827 -20.047 -9.729  1.00 31.67 ? 84  SER B CB  1 
ATOM   1563 O OG  . SER B 1 84  ? 39.865 -19.097 -9.924  1.00 38.16 ? 84  SER B OG  1 
ATOM   1564 N N   . LEU B 1 85  ? 35.193 -19.818 -8.938  1.00 25.53 ? 85  LEU B N   1 
ATOM   1565 C CA  . LEU B 1 85  ? 34.061 -20.665 -8.492  1.00 24.22 ? 85  LEU B CA  1 
ATOM   1566 C C   . LEU B 1 85  ? 33.562 -21.534 -9.655  1.00 24.91 ? 85  LEU B C   1 
ATOM   1567 O O   . LEU B 1 85  ? 33.617 -21.093 -10.830 1.00 25.18 ? 85  LEU B O   1 
ATOM   1568 C CB  . LEU B 1 85  ? 32.964 -19.785 -7.886  1.00 23.97 ? 85  LEU B CB  1 
ATOM   1569 C CG  . LEU B 1 85  ? 33.212 -19.423 -6.422  1.00 23.97 ? 85  LEU B CG  1 
ATOM   1570 C CD1 . LEU B 1 85  ? 32.387 -18.233 -5.967  1.00 25.39 ? 85  LEU B CD1 1 
ATOM   1571 C CD2 . LEU B 1 85  ? 32.932 -20.626 -5.538  1.00 24.78 ? 85  LEU B CD2 1 
ATOM   1572 N N   . ARG B 1 86  ? 33.176 -22.769 -9.328  1.00 23.85 ? 86  ARG B N   1 
ATOM   1573 C CA  . ARG B 1 86  ? 32.697 -23.799 -10.289 1.00 24.98 ? 86  ARG B CA  1 
ATOM   1574 C C   . ARG B 1 86  ? 31.286 -24.228 -9.918  1.00 24.36 ? 86  ARG B C   1 
ATOM   1575 O O   . ARG B 1 86  ? 30.905 -24.129 -8.756  1.00 22.68 ? 86  ARG B O   1 
ATOM   1576 C CB  . ARG B 1 86  ? 33.592 -25.037 -10.246 1.00 27.21 ? 86  ARG B CB  1 
ATOM   1577 C CG  . ARG B 1 86  ? 35.058 -24.764 -10.514 1.00 31.13 ? 86  ARG B CG  1 
ATOM   1578 C CD  . ARG B 1 86  ? 35.867 -25.985 -10.138 1.00 34.74 ? 86  ARG B CD  1 
ATOM   1579 N NE  . ARG B 1 86  ? 37.288 -25.760 -10.349 1.00 37.90 ? 86  ARG B NE  1 
ATOM   1580 C CZ  . ARG B 1 86  ? 38.246 -26.621 -10.031 1.00 39.50 ? 86  ARG B CZ  1 
ATOM   1581 N NH1 . ARG B 1 86  ? 37.945 -27.780 -9.469  1.00 41.54 ? 86  ARG B NH1 1 
ATOM   1582 N NH2 . ARG B 1 86  ? 39.508 -26.307 -10.267 1.00 40.04 ? 86  ARG B NH2 1 
ATOM   1583 N N   . PRO B 1 87  ? 30.480 -24.741 -10.878 1.00 25.67 ? 87  PRO B N   1 
ATOM   1584 C CA  . PRO B 1 87  ? 29.156 -25.281 -10.560 1.00 28.35 ? 87  PRO B CA  1 
ATOM   1585 C C   . PRO B 1 87  ? 29.162 -26.248 -9.367  1.00 27.14 ? 87  PRO B C   1 
ATOM   1586 O O   . PRO B 1 87  ? 28.233 -26.192 -8.575  1.00 28.34 ? 87  PRO B O   1 
ATOM   1587 C CB  . PRO B 1 87  ? 28.752 -25.983 -11.862 1.00 30.26 ? 87  PRO B CB  1 
ATOM   1588 C CG  . PRO B 1 87  ? 29.423 -25.149 -12.927 1.00 30.72 ? 87  PRO B CG  1 
ATOM   1589 C CD  . PRO B 1 87  ? 30.757 -24.755 -12.325 1.00 29.29 ? 87  PRO B CD  1 
ATOM   1590 N N   . GLU B 1 88  ? 30.208 -27.077 -9.250  1.00 25.03 ? 88  GLU B N   1 
ATOM   1591 C CA  . GLU B 1 88  ? 30.322 -28.129 -8.203  1.00 27.47 ? 88  GLU B CA  1 
ATOM   1592 C C   . GLU B 1 88  ? 30.534 -27.492 -6.819  1.00 24.45 ? 88  GLU B C   1 
ATOM   1593 O O   . GLU B 1 88  ? 30.476 -28.232 -5.822  1.00 25.03 ? 88  GLU B O   1 
ATOM   1594 C CB  . GLU B 1 88  ? 31.429 -29.131 -8.542  1.00 31.66 ? 88  GLU B CB  1 
ATOM   1595 C CG  . GLU B 1 88  ? 32.833 -28.555 -8.589  1.00 35.75 ? 88  GLU B CG  1 
ATOM   1596 C CD  . GLU B 1 88  ? 33.857 -29.457 -9.261  1.00 40.40 ? 88  GLU B CD  1 
ATOM   1597 O OE1 . GLU B 1 88  ? 34.835 -28.924 -9.807  1.00 51.06 ? 88  GLU B OE1 1 
ATOM   1598 O OE2 . GLU B 1 88  ? 33.671 -30.688 -9.243  1.00 47.30 ? 88  GLU B OE2 1 
ATOM   1599 N N   . ASP B 1 89  ? 30.798 -26.185 -6.754  1.00 22.63 ? 89  ASP B N   1 
ATOM   1600 C CA  . ASP B 1 89  ? 30.927 -25.441 -5.474  1.00 20.77 ? 89  ASP B CA  1 
ATOM   1601 C C   . ASP B 1 89  ? 29.542 -25.049 -4.955  1.00 19.62 ? 89  ASP B C   1 
ATOM   1602 O O   . ASP B 1 89  ? 29.473 -24.574 -3.805  1.00 19.64 ? 89  ASP B O   1 
ATOM   1603 C CB  . ASP B 1 89  ? 31.823 -24.209 -5.613  1.00 19.44 ? 89  ASP B CB  1 
ATOM   1604 C CG  . ASP B 1 89  ? 33.268 -24.537 -5.937  1.00 21.13 ? 89  ASP B CG  1 
ATOM   1605 O OD1 . ASP B 1 89  ? 33.807 -25.499 -5.334  1.00 21.39 ? 89  ASP B OD1 1 
ATOM   1606 O OD2 . ASP B 1 89  ? 33.847 -23.829 -6.786  1.00 22.37 ? 89  ASP B OD2 1 
ATOM   1607 N N   . THR B 1 90  ? 28.482 -25.216 -5.752  1.00 19.50 ? 90  THR B N   1 
ATOM   1608 C CA  . THR B 1 90  ? 27.105 -24.844 -5.331  1.00 18.44 ? 90  THR B CA  1 
ATOM   1609 C C   . THR B 1 90  ? 26.741 -25.647 -4.083  1.00 18.65 ? 90  THR B C   1 
ATOM   1610 O O   . THR B 1 90  ? 26.833 -26.881 -4.118  1.00 20.41 ? 90  THR B O   1 
ATOM   1611 C CB  . THR B 1 90  ? 26.062 -25.088 -6.426  1.00 19.93 ? 90  THR B CB  1 
ATOM   1612 O OG1 . THR B 1 90  ? 26.404 -24.244 -7.526  1.00 21.40 ? 90  THR B OG1 1 
ATOM   1613 C CG2 . THR B 1 90  ? 24.654 -24.802 -5.947  1.00 18.56 ? 90  THR B CG2 1 
ATOM   1614 N N   . ALA B 1 91  ? 26.341 -24.962 -3.015  1.00 16.62 ? 91  ALA B N   1 
ATOM   1615 C CA  . ALA B 1 91  ? 26.061 -25.600 -1.713  1.00 16.42 ? 91  ALA B CA  1 
ATOM   1616 C C   . ALA B 1 91  ? 25.598 -24.541 -0.724  1.00 16.11 ? 91  ALA B C   1 
ATOM   1617 O O   . ALA B 1 91  ? 25.816 -23.332 -0.971  1.00 16.63 ? 91  ALA B O   1 
ATOM   1618 C CB  . ALA B 1 91  ? 27.293 -26.309 -1.195  1.00 17.15 ? 91  ALA B CB  1 
ATOM   1619 N N   . VAL B 1 92  ? 25.015 -24.992 0.382   1.00 16.41 ? 92  VAL B N   1 
ATOM   1620 C CA  . VAL B 1 92  ? 24.842 -24.130 1.584   1.00 17.43 ? 92  VAL B CA  1 
ATOM   1621 C C   . VAL B 1 92  ? 26.139 -24.208 2.392   1.00 15.24 ? 92  VAL B C   1 
ATOM   1622 O O   . VAL B 1 92  ? 26.566 -25.325 2.732   1.00 16.44 ? 92  VAL B O   1 
ATOM   1623 C CB  . VAL B 1 92  ? 23.610 -24.552 2.396   1.00 17.82 ? 92  VAL B CB  1 
ATOM   1624 C CG1 . VAL B 1 92  ? 23.515 -23.755 3.693   1.00 18.24 ? 92  VAL B CG1 1 
ATOM   1625 C CG2 . VAL B 1 92  ? 22.337 -24.429 1.571   1.00 20.05 ? 92  VAL B CG2 1 
ATOM   1626 N N   . TYR B 1 93  ? 26.761 -23.062 2.650   1.00 15.59 ? 93  TYR B N   1 
ATOM   1627 C CA  . TYR B 1 93  ? 28.046 -22.959 3.384   1.00 14.78 ? 93  TYR B CA  1 
ATOM   1628 C C   . TYR B 1 93  ? 27.749 -22.550 4.823   1.00 15.48 ? 93  TYR B C   1 
ATOM   1629 O O   . TYR B 1 93  ? 26.976 -21.588 5.033   1.00 15.09 ? 93  TYR B O   1 
ATOM   1630 C CB  . TYR B 1 93  ? 28.986 -21.961 2.714   1.00 15.16 ? 93  TYR B CB  1 
ATOM   1631 C CG  . TYR B 1 93  ? 29.610 -22.509 1.458   1.00 16.01 ? 93  TYR B CG  1 
ATOM   1632 C CD1 . TYR B 1 93  ? 28.856 -22.701 0.314   1.00 16.62 ? 93  TYR B CD1 1 
ATOM   1633 C CD2 . TYR B 1 93  ? 30.939 -22.895 1.432   1.00 17.42 ? 93  TYR B CD2 1 
ATOM   1634 C CE1 . TYR B 1 93  ? 29.417 -23.223 -0.837  1.00 16.99 ? 93  TYR B CE1 1 
ATOM   1635 C CE2 . TYR B 1 93  ? 31.520 -23.411 0.285   1.00 17.69 ? 93  TYR B CE2 1 
ATOM   1636 C CZ  . TYR B 1 93  ? 30.753 -23.581 -0.850  1.00 17.13 ? 93  TYR B CZ  1 
ATOM   1637 O OH  . TYR B 1 93  ? 31.318 -24.101 -1.974  1.00 18.18 ? 93  TYR B OH  1 
ATOM   1638 N N   . TYR B 1 94  ? 28.365 -23.260 5.759   1.00 14.90 ? 94  TYR B N   1 
ATOM   1639 C CA  . TYR B 1 94  ? 28.241 -23.036 7.217   1.00 16.06 ? 94  TYR B CA  1 
ATOM   1640 C C   . TYR B 1 94  ? 29.616 -22.701 7.783   1.00 17.82 ? 94  TYR B C   1 
ATOM   1641 O O   . TYR B 1 94  ? 30.608 -23.347 7.421   1.00 19.15 ? 94  TYR B O   1 
ATOM   1642 C CB  . TYR B 1 94  ? 27.720 -24.286 7.913   1.00 17.05 ? 94  TYR B CB  1 
ATOM   1643 C CG  . TYR B 1 94  ? 26.328 -24.709 7.539   1.00 17.05 ? 94  TYR B CG  1 
ATOM   1644 C CD1 . TYR B 1 94  ? 26.099 -25.537 6.455   1.00 17.28 ? 94  TYR B CD1 1 
ATOM   1645 C CD2 . TYR B 1 94  ? 25.244 -24.352 8.326   1.00 16.52 ? 94  TYR B CD2 1 
ATOM   1646 C CE1 . TYR B 1 94  ? 24.827 -25.971 6.132   1.00 18.59 ? 94  TYR B CE1 1 
ATOM   1647 C CE2 . TYR B 1 94  ? 23.957 -24.776 8.015   1.00 19.69 ? 94  TYR B CE2 1 
ATOM   1648 C CZ  . TYR B 1 94  ? 23.750 -25.585 6.911   1.00 19.24 ? 94  TYR B CZ  1 
ATOM   1649 O OH  . TYR B 1 94  ? 22.500 -26.022 6.578   1.00 21.11 ? 94  TYR B OH  1 
ATOM   1650 N N   . CYS B 1 95  ? 29.664 -21.765 8.724   1.00 17.58 ? 95  CYS B N   1 
ATOM   1651 C CA  . CYS B 1 95  ? 30.846 -21.601 9.596   1.00 17.73 ? 95  CYS B CA  1 
ATOM   1652 C C   . CYS B 1 95  ? 30.564 -22.293 10.924  1.00 17.32 ? 95  CYS B C   1 
ATOM   1653 O O   . CYS B 1 95  ? 29.388 -22.410 11.315  1.00 17.47 ? 95  CYS B O   1 
ATOM   1654 C CB  . CYS B 1 95  ? 31.213 -20.145 9.797   1.00 21.57 ? 95  CYS B CB  1 
ATOM   1655 S SG  . CYS B 1 95  ? 29.880 -19.172 10.528  1.00 25.19 ? 95  CYS B SG  1 
ATOM   1656 N N   . ALA B 1 96  ? 31.619 -22.783 11.555  1.00 17.70 ? 96  ALA B N   1 
ATOM   1657 C CA  . ALA B 1 96  ? 31.534 -23.405 12.883  1.00 18.75 ? 96  ALA B CA  1 
ATOM   1658 C C   . ALA B 1 96  ? 32.733 -22.957 13.706  1.00 19.31 ? 96  ALA B C   1 
ATOM   1659 O O   . ALA B 1 96  ? 33.843 -22.813 13.150  1.00 19.05 ? 96  ALA B O   1 
ATOM   1660 C CB  . ALA B 1 96  ? 31.466 -24.903 12.752  1.00 19.81 ? 96  ALA B CB  1 
ATOM   1661 N N   . PHE B 1 97  ? 32.480 -22.690 14.984  1.00 18.83 ? 97  PHE B N   1 
ATOM   1662 C CA  . PHE B 1 97  ? 33.523 -22.488 16.018  1.00 21.32 ? 97  PHE B CA  1 
ATOM   1663 C C   . PHE B 1 97  ? 33.446 -23.696 16.949  1.00 22.26 ? 97  PHE B C   1 
ATOM   1664 O O   . PHE B 1 97  ? 32.326 -24.091 17.342  1.00 20.16 ? 97  PHE B O   1 
ATOM   1665 C CB  . PHE B 1 97  ? 33.300 -21.179 16.781  1.00 22.73 ? 97  PHE B CB  1 
ATOM   1666 C CG  . PHE B 1 97  ? 33.654 -19.894 16.063  1.00 24.21 ? 97  PHE B CG  1 
ATOM   1667 C CD1 . PHE B 1 97  ? 33.630 -19.790 14.676  1.00 24.68 ? 97  PHE B CD1 1 
ATOM   1668 C CD2 . PHE B 1 97  ? 33.973 -18.754 16.789  1.00 27.09 ? 97  PHE B CD2 1 
ATOM   1669 C CE1 . PHE B 1 97  ? 33.968 -18.605 14.039  1.00 25.32 ? 97  PHE B CE1 1 
ATOM   1670 C CE2 . PHE B 1 97  ? 34.298 -17.566 16.151  1.00 30.23 ? 97  PHE B CE2 1 
ATOM   1671 C CZ  . PHE B 1 97  ? 34.298 -17.494 14.776  1.00 28.82 ? 97  PHE B CZ  1 
ATOM   1672 N N   . ILE B 1 98  ? 34.591 -24.307 17.235  1.00 24.22 ? 98  ILE B N   1 
ATOM   1673 C CA  . ILE B 1 98  ? 34.711 -25.307 18.330  1.00 27.63 ? 98  ILE B CA  1 
ATOM   1674 C C   . ILE B 1 98  ? 35.379 -24.585 19.495  1.00 26.24 ? 98  ILE B C   1 
ATOM   1675 O O   . ILE B 1 98  ? 36.440 -23.981 19.301  1.00 28.56 ? 98  ILE B O   1 
ATOM   1676 C CB  . ILE B 1 98  ? 35.476 -26.572 17.912  1.00 32.88 ? 98  ILE B CB  1 
ATOM   1677 C CG1 . ILE B 1 98  ? 34.759 -27.323 16.788  1.00 36.46 ? 98  ILE B CG1 1 
ATOM   1678 C CG2 . ILE B 1 98  ? 35.713 -27.452 19.132  1.00 35.28 ? 98  ILE B CG2 1 
ATOM   1679 C CD1 . ILE B 1 98  ? 35.450 -28.606 16.378  1.00 39.70 ? 98  ILE B CD1 1 
ATOM   1680 N N   . THR B 1 99  ? 34.726 -24.597 20.649  1.00 27.91 ? 99  THR B N   1 
ATOM   1681 C CA  . THR B 1 99  ? 35.154 -23.873 21.867  1.00 31.34 ? 99  THR B CA  1 
ATOM   1682 C C   . THR B 1 99  ? 35.310 -24.895 22.991  1.00 36.03 ? 99  THR B C   1 
ATOM   1683 O O   . THR B 1 99  ? 34.669 -25.958 22.946  1.00 36.12 ? 99  THR B O   1 
ATOM   1684 C CB  . THR B 1 99  ? 34.170 -22.748 22.214  1.00 34.00 ? 99  THR B CB  1 
ATOM   1685 O OG1 . THR B 1 99  ? 32.953 -23.347 22.651  1.00 39.02 ? 99  THR B OG1 1 
ATOM   1686 C CG2 . THR B 1 99  ? 33.900 -21.823 21.047  1.00 36.48 ? 99  THR B CG2 1 
ATOM   1687 N N   . THR B 1 100 ? 36.158 -24.570 23.952  1.00 38.67 ? 100 THR B N   1 
ATOM   1688 C CA  . THR B 1 100 ? 36.462 -25.376 25.154  1.00 42.68 ? 100 THR B CA  1 
ATOM   1689 C C   . THR B 1 100 ? 36.407 -24.381 26.305  1.00 47.25 ? 100 THR B C   1 
ATOM   1690 O O   . THR B 1 100 ? 37.146 -23.375 26.212  1.00 49.61 ? 100 THR B O   1 
ATOM   1691 C CB  . THR B 1 100 ? 37.802 -26.085 24.951  1.00 45.58 ? 100 THR B CB  1 
ATOM   1692 O OG1 . THR B 1 100 ? 37.636 -26.988 23.859  1.00 49.39 ? 100 THR B OG1 1 
ATOM   1693 C CG2 . THR B 1 100 ? 38.291 -26.825 26.174  1.00 51.03 ? 100 THR B CG2 1 
ATOM   1694 N N   . GLU B 1 101 ? 35.434 -24.532 27.201  1.00 46.34 ? 101 GLU B N   1 
ATOM   1695 C CA  . GLU B 1 101 ? 35.269 -23.608 28.348  1.00 48.87 ? 101 GLU B CA  1 
ATOM   1696 C C   . GLU B 1 101 ? 36.487 -23.770 29.261  1.00 51.28 ? 101 GLU B C   1 
ATOM   1697 O O   . GLU B 1 101 ? 37.280 -22.810 29.392  1.00 54.88 ? 101 GLU B O   1 
ATOM   1698 C CB  . GLU B 1 101 ? 33.960 -23.880 29.083  1.00 52.30 ? 101 GLU B CB  1 
ATOM   1699 C CG  . GLU B 1 101 ? 33.924 -23.266 30.474  1.00 57.35 ? 101 GLU B CG  1 
ATOM   1700 C CD  . GLU B 1 101 ? 32.704 -22.416 30.773  1.00 60.88 ? 101 GLU B CD  1 
ATOM   1701 O OE1 . GLU B 1 101 ? 31.634 -22.689 30.193  1.00 68.39 ? 101 GLU B OE1 1 
ATOM   1702 O OE2 . GLU B 1 101 ? 32.843 -21.466 31.565  1.00 67.54 ? 101 GLU B OE2 1 
ATOM   1703 N N   . SER B 1 102 ? 36.623 -24.955 29.851  1.00 45.60 ? 102 SER B N   1 
ATOM   1704 C CA  . SER B 1 102 ? 37.792 -25.353 30.680  1.00 44.82 ? 102 SER B CA  1 
ATOM   1705 C C   . SER B 1 102 ? 38.492 -26.551 30.037  1.00 42.47 ? 102 SER B C   1 
ATOM   1706 O O   . SER B 1 102 ? 37.883 -27.234 29.181  1.00 39.09 ? 102 SER B O   1 
ATOM   1707 C CB  . SER B 1 102 ? 37.402 -25.655 32.100  1.00 46.35 ? 102 SER B CB  1 
ATOM   1708 O OG  . SER B 1 102 ? 36.509 -26.750 32.156  1.00 48.40 ? 102 SER B OG  1 
ATOM   1709 N N   . ASP B 1 103 ? 39.718 -26.817 30.484  1.00 40.99 ? 103 ASP B N   1 
ATOM   1710 C CA  . ASP B 1 103 ? 40.574 -27.916 29.967  1.00 43.96 ? 103 ASP B CA  1 
ATOM   1711 C C   . ASP B 1 103 ? 39.963 -29.263 30.379  1.00 32.02 ? 103 ASP B C   1 
ATOM   1712 O O   . ASP B 1 103 ? 40.344 -30.277 29.785  1.00 34.73 ? 103 ASP B O   1 
ATOM   1713 C CB  . ASP B 1 103 ? 42.013 -27.730 30.457  1.00 49.72 ? 103 ASP B CB  1 
ATOM   1714 C CG  . ASP B 1 103 ? 42.548 -26.339 30.153  1.00 55.05 ? 103 ASP B CG  1 
ATOM   1715 O OD1 . ASP B 1 103 ? 42.468 -25.939 28.977  1.00 57.76 ? 103 ASP B OD1 1 
ATOM   1716 O OD2 . ASP B 1 103 ? 43.003 -25.651 31.096  1.00 55.79 ? 103 ASP B OD2 1 
ATOM   1717 N N   . TYR B 1 104 ? 39.037 -29.276 31.346  1.00 27.70 ? 104 TYR B N   1 
ATOM   1718 C CA  . TYR B 1 104 ? 38.402 -30.525 31.855  1.00 23.48 ? 104 TYR B CA  1 
ATOM   1719 C C   . TYR B 1 104 ? 37.085 -30.815 31.133  1.00 21.20 ? 104 TYR B C   1 
ATOM   1720 O O   . TYR B 1 104 ? 36.478 -31.866 31.409  1.00 17.40 ? 104 TYR B O   1 
ATOM   1721 C CB  . TYR B 1 104 ? 38.220 -30.451 33.375  1.00 23.45 ? 104 TYR B CB  1 
ATOM   1722 C CG  . TYR B 1 104 ? 39.540 -30.510 34.093  1.00 24.30 ? 104 TYR B CG  1 
ATOM   1723 C CD1 . TYR B 1 104 ? 40.091 -31.720 34.467  1.00 25.66 ? 104 TYR B CD1 1 
ATOM   1724 C CD2 . TYR B 1 104 ? 40.286 -29.363 34.302  1.00 29.96 ? 104 TYR B CD2 1 
ATOM   1725 C CE1 . TYR B 1 104 ? 41.327 -31.781 35.087  1.00 27.69 ? 104 TYR B CE1 1 
ATOM   1726 C CE2 . TYR B 1 104 ? 41.529 -29.410 34.912  1.00 28.86 ? 104 TYR B CE2 1 
ATOM   1727 C CZ  . TYR B 1 104 ? 42.058 -30.628 35.296  1.00 27.73 ? 104 TYR B CZ  1 
ATOM   1728 O OH  . TYR B 1 104 ? 43.281 -30.696 35.903  1.00 30.98 ? 104 TYR B OH  1 
ATOM   1729 N N   . ASP B 1 105 ? 36.650 -29.942 30.228  1.00 23.18 ? 105 ASP B N   1 
ATOM   1730 C CA  . ASP B 1 105 ? 35.328 -30.076 29.563  1.00 23.58 ? 105 ASP B CA  1 
ATOM   1731 C C   . ASP B 1 105 ? 35.515 -30.627 28.148  1.00 21.39 ? 105 ASP B C   1 
ATOM   1732 O O   . ASP B 1 105 ? 36.610 -30.438 27.565  1.00 21.84 ? 105 ASP B O   1 
ATOM   1733 C CB  . ASP B 1 105 ? 34.594 -28.739 29.467  1.00 26.90 ? 105 ASP B CB  1 
ATOM   1734 C CG  . ASP B 1 105 ? 34.224 -28.087 30.783  1.00 32.86 ? 105 ASP B CG  1 
ATOM   1735 O OD1 . ASP B 1 105 ? 33.903 -28.823 31.754  1.00 38.00 ? 105 ASP B OD1 1 
ATOM   1736 O OD2 . ASP B 1 105 ? 34.264 -26.847 30.820  1.00 38.52 ? 105 ASP B OD2 1 
ATOM   1737 N N   . LEU B 1 106 ? 34.462 -31.249 27.616  1.00 20.97 ? 106 LEU B N   1 
ATOM   1738 C CA  . LEU B 1 106 ? 34.365 -31.602 26.182  1.00 21.16 ? 106 LEU B CA  1 
ATOM   1739 C C   . LEU B 1 106 ? 34.126 -30.318 25.392  1.00 22.29 ? 106 LEU B C   1 
ATOM   1740 O O   . LEU B 1 106 ? 33.683 -29.323 25.997  1.00 22.21 ? 106 LEU B O   1 
ATOM   1741 C CB  . LEU B 1 106 ? 33.236 -32.614 25.992  1.00 22.48 ? 106 LEU B CB  1 
ATOM   1742 C CG  . LEU B 1 106 ? 33.495 -33.963 26.653  1.00 22.68 ? 106 LEU B CG  1 
ATOM   1743 C CD1 . LEU B 1 106 ? 32.304 -34.896 26.484  1.00 22.94 ? 106 LEU B CD1 1 
ATOM   1744 C CD2 . LEU B 1 106 ? 34.756 -34.595 26.084  1.00 23.57 ? 106 LEU B CD2 1 
ATOM   1745 N N   . GLY B 1 107 ? 34.454 -30.327 24.099  1.00 22.92 ? 107 GLY B N   1 
ATOM   1746 C CA  . GLY B 1 107 ? 34.236 -29.164 23.226  1.00 24.94 ? 107 GLY B CA  1 
ATOM   1747 C C   . GLY B 1 107 ? 32.754 -28.891 23.025  1.00 24.53 ? 107 GLY B C   1 
ATOM   1748 O O   . GLY B 1 107 ? 31.920 -29.766 23.310  1.00 26.12 ? 107 GLY B O   1 
ATOM   1749 N N   . ARG B 1 108 ? 32.447 -27.697 22.548  1.00 26.79 ? 108 ARG B N   1 
ATOM   1750 C CA  . ARG B 1 108 ? 31.108 -27.335 22.032  1.00 26.47 ? 108 ARG B CA  1 
ATOM   1751 C C   . ARG B 1 108 ? 31.308 -26.809 20.621  1.00 25.92 ? 108 ARG B C   1 
ATOM   1752 O O   . ARG B 1 108 ? 32.335 -26.142 20.379  1.00 26.06 ? 108 ARG B O   1 
ATOM   1753 C CB  . ARG B 1 108 ? 30.442 -26.286 22.918  1.00 32.52 ? 108 ARG B CB  1 
ATOM   1754 C CG  . ARG B 1 108 ? 30.129 -26.793 24.315  1.00 32.97 ? 108 ARG B CG  1 
ATOM   1755 C CD  . ARG B 1 108 ? 29.079 -27.889 24.313  1.00 35.57 ? 108 ARG B CD  1 
ATOM   1756 N NE  . ARG B 1 108 ? 28.654 -28.198 25.669  1.00 38.64 ? 108 ARG B NE  1 
ATOM   1757 C CZ  . ARG B 1 108 ? 29.327 -28.959 26.531  1.00 38.69 ? 108 ARG B CZ  1 
ATOM   1758 N NH1 . ARG B 1 108 ? 30.483 -29.513 26.192  1.00 35.82 ? 108 ARG B NH1 1 
ATOM   1759 N NH2 . ARG B 1 108 ? 28.836 -29.153 27.742  1.00 39.88 ? 108 ARG B NH2 1 
ATOM   1760 N N   . ARG B 1 109 ? 30.405 -27.167 19.721  1.00 22.70 ? 109 ARG B N   1 
ATOM   1761 C CA  . ARG B 1 109 ? 30.438 -26.639 18.346  1.00 22.01 ? 109 ARG B CA  1 
ATOM   1762 C C   . ARG B 1 109 ? 29.259 -25.689 18.195  1.00 22.15 ? 109 ARG B C   1 
ATOM   1763 O O   . ARG B 1 109 ? 28.128 -26.088 18.552  1.00 27.42 ? 109 ARG B O   1 
ATOM   1764 C CB  . ARG B 1 109 ? 30.385 -27.765 17.321  1.00 22.85 ? 109 ARG B CB  1 
ATOM   1765 C CG  . ARG B 1 109 ? 30.722 -27.297 15.921  1.00 23.76 ? 109 ARG B CG  1 
ATOM   1766 C CD  . ARG B 1 109 ? 30.638 -28.466 14.963  1.00 27.51 ? 109 ARG B CD  1 
ATOM   1767 N NE  . ARG B 1 109 ? 31.735 -29.409 15.103  1.00 28.90 ? 109 ARG B NE  1 
ATOM   1768 C CZ  . ARG B 1 109 ? 31.668 -30.620 15.648  1.00 27.24 ? 109 ARG B CZ  1 
ATOM   1769 N NH1 . ARG B 1 109 ? 30.541 -31.088 16.155  1.00 27.84 ? 109 ARG B NH1 1 
ATOM   1770 N NH2 . ARG B 1 109 ? 32.754 -31.369 15.683  1.00 27.66 ? 109 ARG B NH2 1 
ATOM   1771 N N   . TYR B 1 110 ? 29.529 -24.485 17.701  1.00 21.45 ? 110 TYR B N   1 
ATOM   1772 C CA  . TYR B 1 110 ? 28.511 -23.462 17.362  1.00 20.62 ? 110 TYR B CA  1 
ATOM   1773 C C   . TYR B 1 110 ? 28.524 -23.249 15.856  1.00 18.71 ? 110 TYR B C   1 
ATOM   1774 O O   . TYR B 1 110 ? 29.610 -23.267 15.261  1.00 18.97 ? 110 TYR B O   1 
ATOM   1775 C CB  . TYR B 1 110 ? 28.780 -22.178 18.138  1.00 22.01 ? 110 TYR B CB  1 
ATOM   1776 C CG  . TYR B 1 110 ? 28.672 -22.415 19.617  1.00 25.70 ? 110 TYR B CG  1 
ATOM   1777 C CD1 . TYR B 1 110 ? 27.433 -22.530 20.224  1.00 28.26 ? 110 TYR B CD1 1 
ATOM   1778 C CD2 . TYR B 1 110 ? 29.799 -22.622 20.387  1.00 26.63 ? 110 TYR B CD2 1 
ATOM   1779 C CE1 . TYR B 1 110 ? 27.316 -22.781 21.582  1.00 33.55 ? 110 TYR B CE1 1 
ATOM   1780 C CE2 . TYR B 1 110 ? 29.699 -22.868 21.747  1.00 31.31 ? 110 TYR B CE2 1 
ATOM   1781 C CZ  . TYR B 1 110 ? 28.455 -22.959 22.343  1.00 32.41 ? 110 TYR B CZ  1 
ATOM   1782 O OH  . TYR B 1 110 ? 28.350 -23.213 23.675  1.00 39.14 ? 110 TYR B OH  1 
ATOM   1783 N N   . TRP B 1 111 ? 27.337 -23.079 15.283  1.00 20.37 ? 111 TRP B N   1 
ATOM   1784 C CA  . TRP B 1 111 ? 27.128 -23.027 13.820  1.00 17.94 ? 111 TRP B CA  1 
ATOM   1785 C C   . TRP B 1 111 ? 26.508 -21.700 13.410  1.00 17.35 ? 111 TRP B C   1 
ATOM   1786 O O   . TRP B 1 111 ? 25.577 -21.241 14.083  1.00 19.32 ? 111 TRP B O   1 
ATOM   1787 C CB  . TRP B 1 111 ? 26.213 -24.154 13.368  1.00 18.79 ? 111 TRP B CB  1 
ATOM   1788 C CG  . TRP B 1 111 ? 26.788 -25.521 13.493  1.00 20.27 ? 111 TRP B CG  1 
ATOM   1789 C CD1 . TRP B 1 111 ? 26.626 -26.391 14.529  1.00 22.01 ? 111 TRP B CD1 1 
ATOM   1790 C CD2 . TRP B 1 111 ? 27.589 -26.190 12.514  1.00 18.74 ? 111 TRP B CD2 1 
ATOM   1791 N NE1 . TRP B 1 111 ? 27.263 -27.570 14.252  1.00 22.18 ? 111 TRP B NE1 1 
ATOM   1792 C CE2 . TRP B 1 111 ? 27.855 -27.476 13.017  1.00 20.32 ? 111 TRP B CE2 1 
ATOM   1793 C CE3 . TRP B 1 111 ? 28.106 -25.829 11.265  1.00 20.19 ? 111 TRP B CE3 1 
ATOM   1794 C CZ2 . TRP B 1 111 ? 28.626 -28.397 12.313  1.00 21.88 ? 111 TRP B CZ2 1 
ATOM   1795 C CZ3 . TRP B 1 111 ? 28.863 -26.748 10.572  1.00 20.34 ? 111 TRP B CZ3 1 
ATOM   1796 C CH2 . TRP B 1 111 ? 29.118 -28.011 11.090  1.00 20.96 ? 111 TRP B CH2 1 
ATOM   1797 N N   . GLY B 1 112 ? 26.962 -21.168 12.279  1.00 16.06 ? 112 GLY B N   1 
ATOM   1798 C CA  . GLY B 1 112 ? 26.239 -20.106 11.565  1.00 16.14 ? 112 GLY B CA  1 
ATOM   1799 C C   . GLY B 1 112 ? 24.953 -20.657 10.985  1.00 16.45 ? 112 GLY B C   1 
ATOM   1800 O O   . GLY B 1 112 ? 24.764 -21.889 11.021  1.00 17.76 ? 112 GLY B O   1 
ATOM   1801 N N   . GLN B 1 113 ? 24.091 -19.783 10.470  1.00 16.89 ? 113 GLN B N   1 
ATOM   1802 C CA  . GLN B 1 113 ? 22.735 -20.165 9.997   1.00 17.96 ? 113 GLN B CA  1 
ATOM   1803 C C   . GLN B 1 113 ? 22.820 -20.913 8.666   1.00 15.74 ? 113 GLN B C   1 
ATOM   1804 O O   . GLN B 1 113 ? 21.837 -21.585 8.315   1.00 16.73 ? 113 GLN B O   1 
ATOM   1805 C CB  . GLN B 1 113 ? 21.825 -18.939 9.898   1.00 18.41 ? 113 GLN B CB  1 
ATOM   1806 C CG  . GLN B 1 113 ? 21.969 -18.106 8.627   1.00 18.66 ? 113 GLN B CG  1 
ATOM   1807 C CD  . GLN B 1 113 ? 23.140 -17.153 8.609   1.00 20.25 ? 113 GLN B CD  1 
ATOM   1808 O OE1 . GLN B 1 113 ? 23.904 -17.049 9.567   1.00 20.31 ? 113 GLN B OE1 1 
ATOM   1809 N NE2 . GLN B 1 113 ? 23.273 -16.422 7.507   1.00 19.09 ? 113 GLN B NE2 1 
ATOM   1810 N N   . GLY B 1 114 ? 23.957 -20.818 7.968   1.00 15.86 ? 114 GLY B N   1 
ATOM   1811 C CA  . GLY B 1 114 ? 24.129 -21.385 6.621   1.00 15.84 ? 114 GLY B CA  1 
ATOM   1812 C C   . GLY B 1 114 ? 23.737 -20.371 5.567   1.00 16.82 ? 114 GLY B C   1 
ATOM   1813 O O   . GLY B 1 114 ? 22.735 -19.686 5.760   1.00 18.31 ? 114 GLY B O   1 
ATOM   1814 N N   . THR B 1 115 ? 24.475 -20.277 4.461   1.00 16.77 ? 115 THR B N   1 
ATOM   1815 C CA  . THR B 1 115 ? 24.125 -19.331 3.380   1.00 16.55 ? 115 THR B CA  1 
ATOM   1816 C C   . THR B 1 115 ? 24.437 -19.997 2.041   1.00 16.62 ? 115 THR B C   1 
ATOM   1817 O O   . THR B 1 115 ? 25.456 -20.699 1.934   1.00 15.44 ? 115 THR B O   1 
ATOM   1818 C CB  . THR B 1 115 ? 24.796 -17.972 3.606   1.00 17.66 ? 115 THR B CB  1 
ATOM   1819 O OG1 . THR B 1 115 ? 23.951 -17.006 2.970   1.00 19.05 ? 115 THR B OG1 1 
ATOM   1820 C CG2 . THR B 1 115 ? 26.233 -17.937 3.128   1.00 19.68 ? 115 THR B CG2 1 
ATOM   1821 N N   . LEU B 1 116 ? 23.545 -19.809 1.079   1.00 15.16 ? 116 LEU B N   1 
ATOM   1822 C CA  . LEU B 1 116 ? 23.669 -20.407 -0.261  1.00 15.66 ? 116 LEU B CA  1 
ATOM   1823 C C   . LEU B 1 116 ? 24.764 -19.693 -1.048  1.00 15.97 ? 116 LEU B C   1 
ATOM   1824 O O   . LEU B 1 116 ? 24.773 -18.444 -1.098  1.00 17.65 ? 116 LEU B O   1 
ATOM   1825 C CB  . LEU B 1 116 ? 22.324 -20.290 -0.981  1.00 17.48 ? 116 LEU B CB  1 
ATOM   1826 C CG  . LEU B 1 116 ? 22.278 -20.866 -2.394  1.00 17.82 ? 116 LEU B CG  1 
ATOM   1827 C CD1 . LEU B 1 116 ? 22.558 -22.361 -2.383  1.00 17.70 ? 116 LEU B CD1 1 
ATOM   1828 C CD2 . LEU B 1 116 ? 20.932 -20.580 -3.025  1.00 19.67 ? 116 LEU B CD2 1 
ATOM   1829 N N   . VAL B 1 117 ? 25.603 -20.495 -1.690  1.00 15.06 ? 117 VAL B N   1 
ATOM   1830 C CA  . VAL B 1 117 ? 26.486 -20.068 -2.811  1.00 17.32 ? 117 VAL B CA  1 
ATOM   1831 C C   . VAL B 1 117 ? 26.051 -20.882 -4.021  1.00 16.82 ? 117 VAL B C   1 
ATOM   1832 O O   . VAL B 1 117 ? 26.069 -22.123 -3.936  1.00 17.88 ? 117 VAL B O   1 
ATOM   1833 C CB  . VAL B 1 117 ? 27.967 -20.289 -2.486  1.00 18.44 ? 117 VAL B CB  1 
ATOM   1834 C CG1 . VAL B 1 117 ? 28.850 -20.037 -3.705  1.00 20.79 ? 117 VAL B CG1 1 
ATOM   1835 C CG2 . VAL B 1 117 ? 28.413 -19.440 -1.305  1.00 19.13 ? 117 VAL B CG2 1 
ATOM   1836 N N   . THR B 1 118 ? 25.628 -20.219 -5.088  1.00 17.82 ? 118 THR B N   1 
ATOM   1837 C CA  . THR B 1 118 ? 25.069 -20.906 -6.270  1.00 18.51 ? 118 THR B CA  1 
ATOM   1838 C C   . THR B 1 118 ? 25.822 -20.378 -7.485  1.00 19.11 ? 118 THR B C   1 
ATOM   1839 O O   . THR B 1 118 ? 25.918 -19.155 -7.660  1.00 18.43 ? 118 THR B O   1 
ATOM   1840 C CB  . THR B 1 118 ? 23.547 -20.764 -6.316  1.00 19.80 ? 118 THR B CB  1 
ATOM   1841 O OG1 . THR B 1 118 ? 23.075 -21.618 -7.355  1.00 22.79 ? 118 THR B OG1 1 
ATOM   1842 C CG2 . THR B 1 118 ? 23.106 -19.334 -6.507  1.00 20.77 ? 118 THR B CG2 1 
ATOM   1843 N N   . VAL B 1 119 ? 26.420 -21.295 -8.234  1.00 21.45 ? 119 VAL B N   1 
ATOM   1844 C CA  . VAL B 1 119 ? 27.256 -20.982 -9.422  1.00 22.78 ? 119 VAL B CA  1 
ATOM   1845 C C   . VAL B 1 119 ? 26.466 -21.468 -10.640 1.00 27.00 ? 119 VAL B C   1 
ATOM   1846 O O   . VAL B 1 119 ? 26.113 -22.653 -10.686 1.00 27.78 ? 119 VAL B O   1 
ATOM   1847 C CB  . VAL B 1 119 ? 28.651 -21.624 -9.294  1.00 23.53 ? 119 VAL B CB  1 
ATOM   1848 C CG1 . VAL B 1 119 ? 29.578 -21.185 -10.412 1.00 25.91 ? 119 VAL B CG1 1 
ATOM   1849 C CG2 . VAL B 1 119 ? 29.295 -21.337 -7.948  1.00 25.04 ? 119 VAL B CG2 1 
ATOM   1850 N N   . SER B 1 120 ? 26.100 -20.552 -11.537 1.00 30.25 ? 120 SER B N   1 
ATOM   1851 C CA  . SER B 1 120 ? 25.271 -20.833 -12.737 1.00 37.44 ? 120 SER B CA  1 
ATOM   1852 C C   . SER B 1 120 ? 26.003 -21.816 -13.661 1.00 42.32 ? 120 SER B C   1 
ATOM   1853 O O   . SER B 1 120 ? 27.204 -22.068 -13.434 1.00 38.88 ? 120 SER B O   1 
ATOM   1854 C CB  . SER B 1 120 ? 24.922 -19.557 -13.457 1.00 40.06 ? 120 SER B CB  1 
ATOM   1855 O OG  . SER B 1 120 ? 26.091 -18.924 -13.953 1.00 41.38 ? 120 SER B OG  1 
ATOM   1856 N N   . SER B 1 121 ? 25.293 -22.357 -14.656 1.00 49.43 ? 121 SER B N   1 
ATOM   1857 C CA  . SER B 1 121 ? 25.821 -23.298 -15.681 1.00 55.25 ? 121 SER B CA  1 
ATOM   1858 C C   . SER B 1 121 ? 26.201 -24.627 -15.016 1.00 59.42 ? 121 SER B C   1 
ATOM   1859 O O   . SER B 1 121 ? 25.345 -25.484 -14.787 1.00 75.70 ? 121 SER B O   1 
ATOM   1860 C CB  . SER B 1 121 ? 26.990 -22.699 -16.436 1.00 53.47 ? 121 SER B CB  1 
ATOM   1861 O OG  . SER B 1 121 ? 28.029 -23.653 -16.589 1.00 56.22 ? 121 SER B OG  1 
HETATM 1862 S S   . SO4 C 2 .   ? 21.176 -6.507  24.294  1.00 34.27 ? 201 SO4 A S   1 
HETATM 1863 O O1  . SO4 C 2 .   ? 22.459 -5.904  24.045  1.00 35.78 ? 201 SO4 A O1  1 
HETATM 1864 O O2  . SO4 C 2 .   ? 20.419 -6.583  23.060  1.00 33.23 ? 201 SO4 A O2  1 
HETATM 1865 O O3  . SO4 C 2 .   ? 21.373 -7.834  24.810  1.00 40.30 ? 201 SO4 A O3  1 
HETATM 1866 O O4  . SO4 C 2 .   ? 20.441 -5.733  25.250  1.00 35.75 ? 201 SO4 A O4  1 
HETATM 1867 S S   . SO4 D 2 .   ? 22.629 -3.484  11.939  1.00 33.31 ? 202 SO4 A S   1 
HETATM 1868 O O1  . SO4 D 2 .   ? 23.497 -2.585  11.237  1.00 35.48 ? 202 SO4 A O1  1 
HETATM 1869 O O2  . SO4 D 2 .   ? 21.270 -3.205  11.578  1.00 30.82 ? 202 SO4 A O2  1 
HETATM 1870 O O3  . SO4 D 2 .   ? 22.957 -4.845  11.597  1.00 33.04 ? 202 SO4 A O3  1 
HETATM 1871 O O4  . SO4 D 2 .   ? 22.808 -3.304  13.358  1.00 42.33 ? 202 SO4 A O4  1 
HETATM 1872 C C1  . GOL E 3 .   ? 20.708 -5.834  7.111   1.00 32.27 ? 203 GOL A C1  1 
HETATM 1873 O O1  . GOL E 3 .   ? 22.019 -6.371  7.272   1.00 33.77 ? 203 GOL A O1  1 
HETATM 1874 C C2  . GOL E 3 .   ? 20.697 -4.329  7.280   1.00 30.87 ? 203 GOL A C2  1 
HETATM 1875 O O2  . GOL E 3 .   ? 21.378 -3.725  6.183   1.00 29.75 ? 203 GOL A O2  1 
HETATM 1876 C C3  . GOL E 3 .   ? 19.302 -3.747  7.405   1.00 29.84 ? 203 GOL A C3  1 
HETATM 1877 O O3  . GOL E 3 .   ? 18.527 -3.945  6.222   1.00 28.52 ? 203 GOL A O3  1 
HETATM 1878 O O   . HOH F 4 .   ? 0.427  -16.760 1.276   0.60 33.89 ? 301 HOH A O   1 
HETATM 1879 O O   . HOH F 4 .   ? 2.070  -4.048  0.283   0.60 30.81 ? 302 HOH A O   1 
HETATM 1880 O O   . HOH F 4 .   ? 17.013 -14.059 20.184  0.60 22.31 ? 303 HOH A O   1 
HETATM 1881 O O   . HOH F 4 .   ? 23.761 -5.672  8.979   0.60 29.17 ? 304 HOH A O   1 
HETATM 1882 O O   . HOH F 4 .   ? 2.390  -12.159 -0.244  1.00 25.57 ? 305 HOH A O   1 
HETATM 1883 O O   . HOH F 4 .   ? 2.561  -21.161 4.732   1.00 40.76 ? 306 HOH A O   1 
HETATM 1884 O O   . HOH F 4 .   ? 1.339  -6.451  3.040   1.00 36.37 ? 307 HOH A O   1 
HETATM 1885 O O   . HOH F 4 .   ? 18.022 -9.084  -9.093  1.00 29.34 ? 308 HOH A O   1 
HETATM 1886 O O   . HOH F 4 .   ? 14.031 -3.879  21.574  1.00 34.01 ? 309 HOH A O   1 
HETATM 1887 O O   . HOH F 4 .   ? 15.202 -16.395 20.962  0.60 34.82 ? 310 HOH A O   1 
HETATM 1888 O O   . HOH F 4 .   ? 18.401 -1.644  4.941   1.00 24.80 ? 311 HOH A O   1 
HETATM 1889 O O   . HOH F 4 .   ? 18.999 -18.778 12.413  1.00 20.78 ? 312 HOH A O   1 
HETATM 1890 O O   . HOH F 4 .   ? 18.584 -24.082 2.126   1.00 27.44 ? 313 HOH A O   1 
HETATM 1891 O O   . HOH F 4 .   ? 2.885  -12.990 -13.840 1.00 27.42 ? 314 HOH A O   1 
HETATM 1892 O O   . HOH F 4 .   ? 7.329  -19.929 15.122  1.00 38.19 ? 315 HOH A O   1 
HETATM 1893 O O   . HOH F 4 .   ? 11.563 -3.679  20.988  1.00 42.57 ? 316 HOH A O   1 
HETATM 1894 O O   . HOH F 4 .   ? 15.798 -1.256  -1.259  1.00 32.49 ? 317 HOH A O   1 
HETATM 1895 O O   . HOH F 4 .   ? 16.179 -22.400 -6.239  1.00 30.21 ? 318 HOH A O   1 
HETATM 1896 O O   . HOH F 4 .   ? 18.904 -5.330  27.917  1.00 38.40 ? 319 HOH A O   1 
HETATM 1897 O O   . HOH F 4 .   ? 15.009 -14.062 23.567  0.60 29.99 ? 320 HOH A O   1 
HETATM 1898 O O   . HOH F 4 .   ? 14.474 -0.886  21.788  0.60 29.96 ? 321 HOH A O   1 
HETATM 1899 O O   . HOH F 4 .   ? 13.502 -23.014 -2.425  0.60 42.85 ? 322 HOH A O   1 
HETATM 1900 O O   . HOH F 4 .   ? 17.165 -22.723 8.162   1.00 26.18 ? 323 HOH A O   1 
HETATM 1901 O O   . HOH F 4 .   ? 12.950 -14.246 19.493  1.00 24.58 ? 324 HOH A O   1 
HETATM 1902 O O   . HOH F 4 .   ? 19.560 -22.682 0.140   1.00 33.82 ? 325 HOH A O   1 
HETATM 1903 O O   . HOH F 4 .   ? 13.008 -25.474 2.216   1.00 45.99 ? 326 HOH A O   1 
HETATM 1904 O O   . HOH F 4 .   ? 22.993 -9.577  -12.080 0.60 25.47 ? 327 HOH A O   1 
HETATM 1905 O O   . HOH F 4 .   ? 21.961 -16.406 4.771   1.00 17.77 ? 328 HOH A O   1 
HETATM 1906 O O   . HOH F 4 .   ? 26.981 -7.832  -2.184  0.60 34.55 ? 329 HOH A O   1 
HETATM 1907 O O   . HOH F 4 .   ? 9.211  -22.074 4.092   1.00 27.79 ? 330 HOH A O   1 
HETATM 1908 O O   . HOH F 4 .   ? 8.434  -0.826  6.120   1.00 37.42 ? 331 HOH A O   1 
HETATM 1909 O O   . HOH F 4 .   ? 20.338 -10.637 -12.083 1.00 40.27 ? 332 HOH A O   1 
HETATM 1910 O O   . HOH F 4 .   ? 20.996 -14.411 18.423  1.00 47.72 ? 333 HOH A O   1 
HETATM 1911 O O   . HOH F 4 .   ? 18.906 -4.849  -11.849 0.60 40.76 ? 334 HOH A O   1 
HETATM 1912 O O   . HOH F 4 .   ? 20.678 -18.810 -12.380 1.00 40.21 ? 335 HOH A O   1 
HETATM 1913 O O   . HOH F 4 .   ? 17.941 -19.484 10.031  1.00 17.83 ? 336 HOH A O   1 
HETATM 1914 O O   . HOH F 4 .   ? 6.048  -20.596 -1.200  1.00 36.50 ? 337 HOH A O   1 
HETATM 1915 O O   . HOH F 4 .   ? 14.472 -14.804 -21.518 1.00 34.66 ? 338 HOH A O   1 
HETATM 1916 O O   . HOH F 4 .   ? 14.127 -5.714  -10.686 1.00 27.67 ? 339 HOH A O   1 
HETATM 1917 O O   . HOH F 4 .   ? 4.959  -14.981 -19.092 0.60 41.86 ? 340 HOH A O   1 
HETATM 1918 O O   . HOH F 4 .   ? 5.627  -10.403 17.311  1.00 39.25 ? 341 HOH A O   1 
HETATM 1919 O O   . HOH F 4 .   ? 11.444 -22.747 10.642  1.00 37.74 ? 342 HOH A O   1 
HETATM 1920 O O   . HOH F 4 .   ? -0.257 -14.488 2.542   1.00 31.12 ? 343 HOH A O   1 
HETATM 1921 O O   . HOH F 4 .   ? 21.975 -6.442  18.680  1.00 27.28 ? 344 HOH A O   1 
HETATM 1922 O O   . HOH F 4 .   ? 17.389 -9.440  21.476  1.00 33.85 ? 345 HOH A O   1 
HETATM 1923 O O   . HOH F 4 .   ? 8.318  -2.621  -10.868 1.00 39.46 ? 346 HOH A O   1 
HETATM 1924 O O   . HOH F 4 .   ? 20.778 -7.292  -5.429  1.00 23.50 ? 347 HOH A O   1 
HETATM 1925 O O   . HOH F 4 .   ? 16.732 -21.417 -10.665 1.00 42.13 ? 348 HOH A O   1 
HETATM 1926 O O   . HOH F 4 .   ? 20.379 -16.338 11.397  1.00 20.51 ? 349 HOH A O   1 
HETATM 1927 O O   . HOH F 4 .   ? 16.452 -20.993 4.709   1.00 29.02 ? 350 HOH A O   1 
HETATM 1928 O O   . HOH F 4 .   ? 6.776  -7.588  10.984  1.00 45.71 ? 351 HOH A O   1 
HETATM 1929 O O   . HOH F 4 .   ? 23.142 -6.462  21.293  1.00 41.22 ? 352 HOH A O   1 
HETATM 1930 O O   . HOH F 4 .   ? 17.183 -3.192  -8.298  1.00 40.39 ? 353 HOH A O   1 
HETATM 1931 O O   . HOH F 4 .   ? 21.759 -10.237 15.492  1.00 25.22 ? 354 HOH A O   1 
HETATM 1932 O O   . HOH F 4 .   ? 15.292 -0.660  -6.744  0.60 25.48 ? 355 HOH A O   1 
HETATM 1933 O O   . HOH F 4 .   ? 4.789  -18.375 -14.030 1.00 26.09 ? 356 HOH A O   1 
HETATM 1934 O O   . HOH F 4 .   ? 16.972 -0.421  -3.638  1.00 30.63 ? 357 HOH A O   1 
HETATM 1935 O O   . HOH F 4 .   ? 7.842  1.458   -0.483  1.00 37.40 ? 358 HOH A O   1 
HETATM 1936 O O   . HOH F 4 .   ? 25.113 -6.477  -12.778 1.00 32.71 ? 359 HOH A O   1 
HETATM 1937 O O   . HOH F 4 .   ? 4.300  -3.341  -4.601  1.00 38.45 ? 360 HOH A O   1 
HETATM 1938 O O   . HOH F 4 .   ? 4.840  -22.203 2.815   1.00 41.88 ? 361 HOH A O   1 
HETATM 1939 O O   . HOH F 4 .   ? 6.636  -20.941 -5.742  0.60 34.03 ? 362 HOH A O   1 
HETATM 1940 O O   . HOH F 4 .   ? 2.907  0.990   4.501   0.60 35.38 ? 363 HOH A O   1 
HETATM 1941 O O   . HOH F 4 .   ? 7.678  -6.824  -15.924 1.00 40.29 ? 364 HOH A O   1 
HETATM 1942 O O   . HOH F 4 .   ? 18.530 -22.292 -4.572  1.00 25.22 ? 365 HOH A O   1 
HETATM 1943 O O   . HOH F 4 .   ? 16.117 -11.687 20.062  1.00 32.54 ? 366 HOH A O   1 
HETATM 1944 O O   . HOH F 4 .   ? 13.712 -4.214  -12.785 0.60 27.20 ? 367 HOH A O   1 
HETATM 1945 O O   . HOH F 4 .   ? 22.487 -9.400  10.483  1.00 23.14 ? 368 HOH A O   1 
HETATM 1946 O O   . HOH F 4 .   ? 24.341 -4.023  6.310   0.60 40.88 ? 369 HOH A O   1 
HETATM 1947 O O   . HOH F 4 .   ? 3.129  -10.929 -17.341 1.00 44.28 ? 370 HOH A O   1 
HETATM 1948 O O   . HOH F 4 .   ? 13.178 -24.791 -10.660 1.00 40.15 ? 371 HOH A O   1 
HETATM 1949 O O   . HOH F 4 .   ? 23.908 -12.116 2.481   1.00 37.69 ? 372 HOH A O   1 
HETATM 1950 O O   . HOH F 4 .   ? 9.650  -24.259 17.112  1.00 43.01 ? 373 HOH A O   1 
HETATM 1951 O O   . HOH F 4 .   ? 10.821 -25.138 -2.125  0.60 41.45 ? 374 HOH A O   1 
HETATM 1952 O O   . HOH F 4 .   ? 19.236 -6.860  -7.431  1.00 31.87 ? 375 HOH A O   1 
HETATM 1953 O O   . HOH F 4 .   ? 20.026 -7.428  -11.607 0.60 34.36 ? 376 HOH A O   1 
HETATM 1954 O O   . HOH F 4 .   ? -0.155 -9.686  5.604   1.00 22.59 ? 377 HOH A O   1 
HETATM 1955 O O   . HOH F 4 .   ? 0.275  -19.480 -2.516  1.00 49.18 ? 378 HOH A O   1 
HETATM 1956 O O   . HOH F 4 .   ? 1.085  -18.188 -4.644  1.00 37.33 ? 379 HOH A O   1 
HETATM 1957 O O   . HOH F 4 .   ? 4.558  -20.233 -7.052  1.00 40.65 ? 380 HOH A O   1 
HETATM 1958 O O   . HOH F 4 .   ? 20.780 -20.287 13.478  1.00 51.49 ? 381 HOH A O   1 
HETATM 1959 O O   . HOH F 4 .   ? 28.332 -5.417  -6.310  1.00 23.74 ? 382 HOH A O   1 
HETATM 1960 O O   . HOH F 4 .   ? 22.867 -10.364 13.108  1.00 34.15 ? 383 HOH A O   1 
HETATM 1961 O O   . HOH F 4 .   ? 22.130 -18.515 15.379  0.60 29.16 ? 384 HOH A O   1 
HETATM 1962 O O   . HOH F 4 .   ? 14.416 -24.073 -5.303  0.60 38.56 ? 385 HOH A O   1 
HETATM 1963 O O   . HOH F 4 .   ? 14.077 -12.761 21.561  1.00 33.54 ? 386 HOH A O   1 
HETATM 1964 O O   . HOH F 4 .   ? 2.084  -14.484 -0.960  0.60 25.95 ? 387 HOH A O   1 
HETATM 1965 O O   . HOH F 4 .   ? 24.505 -8.546  9.222   1.00 36.58 ? 388 HOH A O   1 
HETATM 1966 O O   . HOH F 4 .   ? 16.968 -23.172 -8.590  1.00 37.23 ? 389 HOH A O   1 
HETATM 1967 O O   . HOH F 4 .   ? 23.075 -8.540  17.273  0.60 21.88 ? 390 HOH A O   1 
HETATM 1968 O O   . HOH F 4 .   ? 9.770  -24.698 9.393   0.60 52.54 ? 391 HOH A O   1 
HETATM 1969 O O   . HOH G 4 .   ? 23.157 -22.103 -9.744  1.00 35.87 ? 201 HOH B O   1 
HETATM 1970 O O   . HOH G 4 .   ? 29.920 -23.388 25.562  1.00 42.71 ? 202 HOH B O   1 
HETATM 1971 O O   . HOH G 4 .   ? 24.078 -16.512 0.315   1.00 23.63 ? 203 HOH B O   1 
HETATM 1972 O O   . HOH G 4 .   ? 34.141 -29.213 13.769  1.00 34.60 ? 204 HOH B O   1 
HETATM 1973 O O   . HOH G 4 .   ? 31.777 -11.047 3.112   0.60 32.63 ? 205 HOH B O   1 
HETATM 1974 O O   . HOH G 4 .   ? 32.364 -30.913 -0.554  0.60 36.46 ? 206 HOH B O   1 
HETATM 1975 O O   . HOH G 4 .   ? 45.698 -20.441 3.860   1.00 35.08 ? 207 HOH B O   1 
HETATM 1976 O O   . HOH G 4 .   ? 45.029 -18.189 5.572   0.60 35.01 ? 208 HOH B O   1 
HETATM 1977 O O   . HOH G 4 .   ? 25.574 -25.705 18.476  0.60 38.29 ? 209 HOH B O   1 
HETATM 1978 O O   . HOH G 4 .   ? 34.512 -31.867 11.214  1.00 35.57 ? 210 HOH B O   1 
HETATM 1979 O O   . HOH G 4 .   ? 34.606 -31.225 -1.697  1.00 38.56 ? 211 HOH B O   1 
HETATM 1980 O O   . HOH G 4 .   ? 29.611 -28.142 -3.353  1.00 29.26 ? 212 HOH B O   1 
HETATM 1981 O O   . HOH G 4 .   ? 32.490 -24.518 24.952  0.60 29.17 ? 213 HOH B O   1 
HETATM 1982 O O   . HOH G 4 .   ? 39.402 -10.820 3.923   0.60 46.21 ? 214 HOH B O   1 
HETATM 1983 O O   . HOH G 4 .   ? 34.353 -7.849  8.185   1.00 38.81 ? 215 HOH B O   1 
HETATM 1984 O O   . HOH G 4 .   ? 22.287 -27.410 4.344   1.00 26.54 ? 216 HOH B O   1 
HETATM 1985 O O   . HOH G 4 .   ? 44.004 -30.095 0.442   1.00 21.88 ? 217 HOH B O   1 
HETATM 1986 O O   . HOH G 4 .   ? 22.923 -23.747 11.571  1.00 29.89 ? 218 HOH B O   1 
HETATM 1987 O O   . HOH G 4 .   ? 30.733 -32.163 23.500  1.00 26.14 ? 219 HOH B O   1 
HETATM 1988 O O   . HOH G 4 .   ? 40.120 -15.304 3.329   1.00 34.18 ? 220 HOH B O   1 
HETATM 1989 O O   . HOH G 4 .   ? 43.826 -22.816 -0.595  1.00 33.37 ? 221 HOH B O   1 
HETATM 1990 O O   . HOH G 4 .   ? 27.006 -28.771 -6.042  1.00 35.80 ? 222 HOH B O   1 
HETATM 1991 O O   . HOH G 4 .   ? 37.642 -15.671 -9.423  1.00 36.01 ? 223 HOH B O   1 
HETATM 1992 O O   . HOH G 4 .   ? 45.227 -19.498 -0.742  0.60 34.40 ? 224 HOH B O   1 
HETATM 1993 O O   . HOH G 4 .   ? 19.358 -21.779 9.391   1.00 20.95 ? 225 HOH B O   1 
HETATM 1994 O O   B HOH G 4 .   ? 41.142 -21.151 15.151  0.50 21.60 ? 226 HOH B O   1 
HETATM 1995 O O   . HOH G 4 .   ? 39.960 -22.476 29.806  0.60 41.27 ? 227 HOH B O   1 
HETATM 1996 O O   . HOH G 4 .   ? 41.245 -11.591 5.640   1.00 42.09 ? 228 HOH B O   1 
HETATM 1997 O O   . HOH G 4 .   ? 23.637 -26.138 12.065  1.00 41.89 ? 229 HOH B O   1 
HETATM 1998 O O   . HOH G 4 .   ? 28.475 -11.796 8.735   1.00 28.99 ? 230 HOH B O   1 
HETATM 1999 O O   . HOH G 4 .   ? 43.832 -27.205 10.297  1.00 25.57 ? 231 HOH B O   1 
HETATM 2000 O O   . HOH G 4 .   ? 24.780 -38.281 1.201   1.00 39.52 ? 232 HOH B O   1 
HETATM 2001 O O   . HOH G 4 .   ? 34.483 -28.196 -5.461  1.00 27.67 ? 233 HOH B O   1 
HETATM 2002 O O   . HOH G 4 .   ? 24.882 -19.126 15.790  1.00 24.80 ? 234 HOH B O   1 
HETATM 2003 O O   . HOH G 4 .   ? 22.504 -22.536 -14.488 0.60 39.64 ? 235 HOH B O   1 
HETATM 2004 O O   . HOH G 4 .   ? 35.750 -27.723 34.672  1.00 41.30 ? 236 HOH B O   1 
HETATM 2005 O O   . HOH G 4 .   ? 40.883 -26.318 -6.364  1.00 29.02 ? 237 HOH B O   1 
HETATM 2006 O O   . HOH G 4 .   ? 34.954 -31.667 1.707   0.60 30.38 ? 238 HOH B O   1 
HETATM 2007 O O   . HOH G 4 .   ? 35.309 -6.724  6.319   1.00 54.28 ? 239 HOH B O   1 
HETATM 2008 O O   . HOH G 4 .   ? 41.247 -17.630 -2.325  1.00 35.91 ? 240 HOH B O   1 
HETATM 2009 O O   . HOH G 4 .   ? 23.548 -12.108 6.266   1.00 36.71 ? 241 HOH B O   1 
HETATM 2010 O O   . HOH G 4 .   ? 37.028 -34.447 32.488  1.00 18.87 ? 242 HOH B O   1 
HETATM 2011 O O   . HOH G 4 .   ? 25.079 -23.213 17.026  1.00 25.34 ? 243 HOH B O   1 
HETATM 2012 O O   . HOH G 4 .   ? 31.083 -11.680 -1.394  1.00 29.36 ? 244 HOH B O   1 
HETATM 2013 O O   . HOH G 4 .   ? 33.292 -26.513 26.430  1.00 40.28 ? 245 HOH B O   1 
HETATM 2014 O O   . HOH G 4 .   ? 29.548 -13.456 -11.335 1.00 39.24 ? 246 HOH B O   1 
HETATM 2015 O O   . HOH G 4 .   ? 38.243 -32.868 -1.530  1.00 23.54 ? 247 HOH B O   1 
HETATM 2016 O O   . HOH G 4 .   ? 25.070 -14.366 2.686   1.00 25.59 ? 248 HOH B O   1 
HETATM 2017 O O   . HOH G 4 .   ? 47.390 -26.590 4.410   1.00 32.67 ? 249 HOH B O   1 
HETATM 2018 O O   . HOH G 4 .   ? 24.278 -9.403  6.825   1.00 28.90 ? 250 HOH B O   1 
HETATM 2019 O O   . HOH G 4 .   ? 28.321 -28.990 20.621  1.00 29.25 ? 251 HOH B O   1 
HETATM 2020 O O   . HOH G 4 .   ? 22.650 -16.643 13.148  1.00 30.17 ? 252 HOH B O   1 
HETATM 2021 O O   . HOH G 4 .   ? 27.727 -13.506 -18.815 0.60 42.09 ? 253 HOH B O   1 
HETATM 2022 O O   . HOH G 4 .   ? 28.399 -31.427 0.511   1.00 29.49 ? 254 HOH B O   1 
HETATM 2023 O O   . HOH G 4 .   ? 20.886 -23.105 -6.066  1.00 23.46 ? 255 HOH B O   1 
HETATM 2024 O O   . HOH G 4 .   ? 36.387 -28.984 -7.228  0.60 33.20 ? 256 HOH B O   1 
HETATM 2025 O O   . HOH G 4 .   ? 24.449 -11.749 -0.139  0.60 23.67 ? 257 HOH B O   1 
HETATM 2026 O O   . HOH G 4 .   ? 32.059 -27.788 -11.504 1.00 33.96 ? 258 HOH B O   1 
HETATM 2027 O O   . HOH G 4 .   ? 38.089 -6.994  5.691   0.60 35.79 ? 259 HOH B O   1 
HETATM 2028 O O   A HOH G 4 .   ? 28.323 -12.187 -7.549  0.50 30.99 ? 260 HOH B O   1 
HETATM 2029 O O   . HOH G 4 .   ? 25.945 -33.873 7.836   0.60 37.90 ? 261 HOH B O   1 
HETATM 2030 O O   . HOH G 4 .   ? 43.981 -15.205 9.154   1.00 35.05 ? 262 HOH B O   1 
HETATM 2031 O O   . HOH G 4 .   ? 27.619 -30.223 15.843  1.00 30.54 ? 263 HOH B O   1 
HETATM 2032 O O   . HOH G 4 .   ? 28.016 -11.343 -2.101  1.00 39.19 ? 264 HOH B O   1 
HETATM 2033 O O   . HOH G 4 .   ? 30.052 -37.586 -0.281  0.60 39.57 ? 265 HOH B O   1 
HETATM 2034 O O   . HOH G 4 .   ? 32.876 -12.120 -9.368  0.60 29.42 ? 266 HOH B O   1 
HETATM 2035 O O   . HOH G 4 .   ? 38.618 -31.427 25.373  1.00 60.10 ? 267 HOH B O   1 
HETATM 2036 O O   . HOH G 4 .   ? 39.943 -17.843 21.775  0.60 44.56 ? 268 HOH B O   1 
HETATM 2037 O O   . HOH G 4 .   ? 33.247 -19.059 33.547  1.00 42.58 ? 269 HOH B O   1 
HETATM 2038 O O   . HOH G 4 .   ? 23.648 -32.479 7.768   0.60 44.57 ? 270 HOH B O   1 
HETATM 2039 O O   . HOH G 4 .   ? 26.704 -26.924 21.287  0.60 34.69 ? 271 HOH B O   1 
HETATM 2040 O O   . HOH G 4 .   ? 28.197 -18.239 20.076  1.00 53.70 ? 272 HOH B O   1 
HETATM 2041 O O   . HOH G 4 .   ? 33.213 -30.652 -5.164  1.00 52.37 ? 273 HOH B O   1 
HETATM 2042 O O   . HOH G 4 .   ? 29.234 -32.514 25.778  1.00 36.55 ? 274 HOH B O   1 
HETATM 2043 O O   . HOH G 4 .   ? 27.506 -37.456 1.311   0.60 39.51 ? 275 HOH B O   1 
HETATM 2044 O O   . HOH G 4 .   ? 25.595 -16.222 22.456  1.00 43.60 ? 276 HOH B O   1 
HETATM 2045 O O   . HOH G 4 .   ? 47.835 -24.698 2.568   0.60 33.49 ? 277 HOH B O   1 
HETATM 2046 O O   . HOH G 4 .   ? 42.424 -25.429 -8.428  0.60 28.53 ? 278 HOH B O   1 
HETATM 2047 O O   . HOH G 4 .   ? 28.665 -20.394 27.753  0.60 37.49 ? 279 HOH B O   1 
HETATM 2048 O O   . HOH G 4 .   ? 22.464 -13.546 4.685   1.00 32.12 ? 280 HOH B O   1 
HETATM 2049 O O   . HOH G 4 .   ? 26.451 -9.030  2.358   0.60 31.52 ? 281 HOH B O   1 
HETATM 2050 O O   . HOH G 4 .   ? 24.535 -30.846 11.927  1.00 51.27 ? 282 HOH B O   1 
HETATM 2051 O O   . HOH G 4 .   ? 22.438 -25.798 -2.350  1.00 37.59 ? 283 HOH B O   1 
HETATM 2052 O O   . HOH G 4 .   ? 30.356 -31.792 12.339  0.60 40.35 ? 284 HOH B O   1 
HETATM 2053 O O   . HOH G 4 .   ? 28.519 -31.261 22.102  1.00 38.94 ? 285 HOH B O   1 
HETATM 2054 O O   . HOH G 4 .   ? 25.001 -20.690 18.120  1.00 37.37 ? 286 HOH B O   1 
HETATM 2055 O O   . HOH G 4 .   ? 36.699 -34.055 -3.437  1.00 37.31 ? 287 HOH B O   1 
HETATM 2056 O O   . HOH G 4 .   ? 38.384 -26.357 36.002  1.00 42.83 ? 288 HOH B O   1 
HETATM 2057 O O   . HOH G 4 .   ? 41.941 -14.090 1.616   0.60 27.14 ? 289 HOH B O   1 
HETATM 2058 O O   . HOH G 4 .   ? 46.768 -18.489 2.092   0.60 39.00 ? 290 HOH B O   1 
HETATM 2059 O O   . HOH G 4 .   ? 34.611 -26.860 -13.787 1.00 42.55 ? 291 HOH B O   1 
HETATM 2060 O O   . HOH G 4 .   ? 28.607 -31.630 10.418  1.00 51.09 ? 292 HOH B O   1 
HETATM 2061 O O   . HOH G 4 .   ? 30.131 -11.759 -9.586  1.00 44.63 ? 293 HOH B O   1 
HETATM 2062 O O   . HOH G 4 .   ? 36.722 -33.308 0.640   1.00 26.14 ? 294 HOH B O   1 
HETATM 2063 O O   . HOH G 4 .   ? 26.869 -39.752 3.932   0.60 39.99 ? 295 HOH B O   1 
HETATM 2064 O O   . HOH G 4 .   ? 21.508 -25.822 -4.929  1.00 34.23 ? 296 HOH B O   1 
HETATM 2065 O O   . HOH G 4 .   ? 22.192 -27.384 -6.933  0.60 37.93 ? 297 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   . GLU A 1   ? 0.7036 0.7662 0.4181 0.0594  -0.0832 0.0216  1   GLU A N   
2    C CA  . GLU A 1   ? 0.5710 0.7562 0.4215 0.0433  -0.0723 -0.0268 1   GLU A CA  
3    C C   . GLU A 1   ? 0.5247 0.6325 0.3606 0.0147  0.0028  0.0006  1   GLU A C   
4    O O   . GLU A 1   ? 0.4931 0.5678 0.3256 0.0095  -0.0499 -0.0172 1   GLU A O   
5    C CB  . GLU A 1   ? 0.6604 0.8299 0.5769 0.1405  -0.0943 -0.0281 1   GLU A CB  
6    C CG  . GLU A 1   ? 0.6087 0.8636 0.6275 0.1840  -0.0650 -0.0827 1   GLU A CG  
7    C CD  . GLU A 1   ? 0.7169 0.8370 0.8138 0.1748  -0.0947 -0.1025 1   GLU A CD  
8    O OE1 . GLU A 1   ? 0.6598 0.9102 0.9912 0.1909  -0.0388 0.0465  1   GLU A OE1 
9    O OE2 . GLU A 1   ? 0.8103 0.7555 0.8203 0.1533  -0.0088 -0.1694 1   GLU A OE2 
10   N N   . VAL A 2   ? 0.3468 0.5200 0.3121 -0.0050 -0.0229 -0.0672 2   VAL A N   
11   C CA  . VAL A 2   ? 0.3258 0.3886 0.2250 0.0218  0.0258  -0.0566 2   VAL A CA  
12   C C   . VAL A 2   ? 0.2935 0.3303 0.2148 -0.0044 0.0186  -0.0456 2   VAL A C   
13   O O   . VAL A 2   ? 0.2790 0.3569 0.2529 0.0024  0.0215  -0.0627 2   VAL A O   
14   C CB  . VAL A 2   ? 0.3117 0.3763 0.2837 0.0170  0.0668  -0.0768 2   VAL A CB  
15   C CG1 . VAL A 2   ? 0.3360 0.3426 0.2874 0.0632  0.0471  -0.0335 2   VAL A CG1 
16   C CG2 . VAL A 2   ? 0.3622 0.4131 0.3015 0.0023  0.0886  -0.0994 2   VAL A CG2 
17   N N   . GLN A 3   ? 0.2780 0.2632 0.2088 0.0297  -0.0212 -0.0052 3   GLN A N   
18   C CA  A GLN A 3   ? 0.2640 0.2634 0.2142 0.0343  -0.0204 -0.0026 3   GLN A CA  
19   C CA  B GLN A 3   ? 0.2686 0.2938 0.2098 0.0320  -0.0298 -0.0131 3   GLN A CA  
20   C C   . GLN A 3   ? 0.2371 0.2711 0.2112 0.0367  0.0005  0.0207  3   GLN A C   
21   O O   . GLN A 3   ? 0.2293 0.2704 0.2157 0.0259  -0.0165 0.0059  3   GLN A O   
22   C CB  A GLN A 3   ? 0.3307 0.2642 0.2699 0.0396  -0.0097 0.0101  3   GLN A CB  
23   C CB  B GLN A 3   ? 0.3442 0.2966 0.2461 0.0436  -0.0293 -0.0231 3   GLN A CB  
24   C CG  A GLN A 3   ? 0.3779 0.2581 0.3104 0.0533  0.0056  -0.0066 3   GLN A CG  
25   C CG  B GLN A 3   ? 0.3941 0.3584 0.2998 0.0533  -0.0839 -0.0274 3   GLN A CG  
26   C CD  A GLN A 3   ? 0.4047 0.2695 0.3564 0.0225  0.0462  -0.0084 3   GLN A CD  
27   C CD  B GLN A 3   ? 0.4536 0.4213 0.2979 0.0406  -0.0725 -0.0274 3   GLN A CD  
28   O OE1 A GLN A 3   ? 0.3658 0.2575 0.3976 0.0503  0.0281  -0.0377 3   GLN A OE1 
29   O OE1 B GLN A 3   ? 0.5296 0.4551 0.3278 0.0520  -0.1527 -0.0060 3   GLN A OE1 
30   N NE2 A GLN A 3   ? 0.5184 0.2143 0.3862 0.0428  0.0557  0.0668  3   GLN A NE2 
31   N NE2 B GLN A 3   ? 0.4581 0.4917 0.3444 0.0198  -0.0472 -0.0494 3   GLN A NE2 
32   N N   . LEU A 4   ? 0.1943 0.2437 0.2076 0.0473  -0.0081 0.0055  4   LEU A N   
33   C CA  . LEU A 4   ? 0.1664 0.2368 0.2071 0.0187  -0.0185 -0.0185 4   LEU A CA  
34   C C   . LEU A 4   ? 0.2179 0.2618 0.2343 0.0206  -0.0295 -0.0438 4   LEU A C   
35   O O   . LEU A 4   ? 0.2171 0.3347 0.2435 0.0110  -0.0157 -0.0327 4   LEU A O   
36   C CB  . LEU A 4   ? 0.1844 0.2417 0.2208 -0.0002 -0.0081 -0.0168 4   LEU A CB  
37   C CG  . LEU A 4   ? 0.1772 0.2576 0.2598 -0.0089 -0.0039 -0.0411 4   LEU A CG  
38   C CD1 . LEU A 4   ? 0.1555 0.2752 0.2360 -0.0114 -0.0081 -0.0257 4   LEU A CD1 
39   C CD2 . LEU A 4   ? 0.2195 0.2670 0.2650 -0.0273 0.0435  -0.0504 4   LEU A CD2 
40   N N   . VAL A 5   ? 0.2350 0.2294 0.2595 0.0004  -0.0379 -0.0164 5   VAL A N   
41   C CA  . VAL A 5   ? 0.2824 0.2379 0.2546 0.0074  -0.0319 -0.0255 5   VAL A CA  
42   C C   . VAL A 5   ? 0.2478 0.2059 0.2302 -0.0113 0.0082  -0.0141 5   VAL A C   
43   O O   . VAL A 5   ? 0.2584 0.2489 0.1995 0.0220  0.0061  -0.0216 5   VAL A O   
44   C CB  . VAL A 5   ? 0.3913 0.2277 0.3016 -0.0127 -0.0371 -0.0266 5   VAL A CB  
45   C CG1 . VAL A 5   ? 0.4173 0.2646 0.3311 -0.0163 -0.0663 -0.0569 5   VAL A CG1 
46   C CG2 . VAL A 5   ? 0.4256 0.2727 0.3392 0.0122  -0.0584 -0.0231 5   VAL A CG2 
47   N N   . GLU A 6   ? 0.2180 0.2348 0.2533 -0.0083 0.0264  -0.0239 6   GLU A N   
48   C CA  . GLU A 6   ? 0.2078 0.2627 0.2519 -0.0073 0.0148  -0.0258 6   GLU A CA  
49   C C   . GLU A 6   ? 0.2550 0.2658 0.2532 -0.0019 0.0143  -0.0324 6   GLU A C   
50   O O   . GLU A 6   ? 0.3496 0.2796 0.2975 0.0374  0.0303  -0.0447 6   GLU A O   
51   C CB  . GLU A 6   ? 0.2024 0.2584 0.2693 -0.0029 0.0102  -0.0122 6   GLU A CB  
52   C CG  . GLU A 6   ? 0.2359 0.2890 0.2390 -0.0199 -0.0029 -0.0142 6   GLU A CG  
53   C CD  . GLU A 6   ? 0.2558 0.2883 0.2438 -0.0083 0.0003  0.0223  6   GLU A CD  
54   O OE1 . GLU A 6   ? 0.2726 0.3132 0.1990 0.0066  0.0240  -0.0266 6   GLU A OE1 
55   O OE2 . GLU A 6   ? 0.2047 0.2797 0.2276 0.0708  -0.0101 0.0299  6   GLU A OE2 
56   N N   . SER A 7   ? 0.2534 0.2579 0.2692 -0.0014 0.0065  -0.0146 7   SER A N   
57   C CA  . SER A 7   ? 0.3083 0.3134 0.2875 -0.0186 -0.0273 -0.0329 7   SER A CA  
58   C C   . SER A 7   ? 0.3217 0.3023 0.2648 -0.0208 -0.0192 -0.0360 7   SER A C   
59   O O   . SER A 7   ? 0.3297 0.2873 0.2262 -0.0528 -0.0135 -0.0515 7   SER A O   
60   C CB  . SER A 7   ? 0.3531 0.3584 0.3105 -0.0426 -0.0082 -0.0155 7   SER A CB  
61   O OG  . SER A 7   ? 0.3273 0.3763 0.4053 -0.0614 0.0061  -0.0511 7   SER A OG  
62   N N   . GLY A 8   ? 0.3317 0.3063 0.2938 -0.0489 0.0233  -0.0757 8   GLY A N   
63   C CA  . GLY A 8   ? 0.3832 0.3278 0.3050 -0.0347 -0.0032 -0.0464 8   GLY A CA  
64   C C   . GLY A 8   ? 0.3788 0.3545 0.3405 -0.0444 0.0136  -0.0507 8   GLY A C   
65   O O   . GLY A 8   ? 0.6124 0.5083 0.2297 -0.0685 0.0246  0.0192  8   GLY A O   
66   N N   . GLY A 9   ? 0.3674 0.3116 0.3826 -0.0400 0.0960  -0.0358 9   GLY A N   
67   C CA  . GLY A 9   ? 0.3741 0.3702 0.3421 -0.0525 0.0704  -0.0389 9   GLY A CA  
68   C C   . GLY A 9   ? 0.3533 0.3517 0.3645 -0.0567 0.0581  -0.0447 9   GLY A C   
69   O O   . GLY A 9   ? 0.4126 0.4200 0.4429 -0.1175 0.0999  -0.1302 9   GLY A O   
70   N N   . GLY A 10  ? 0.4102 0.3678 0.2179 -0.0333 0.0146  -0.0636 10  GLY A N   
71   C CA  . GLY A 10  ? 0.3792 0.3618 0.2524 0.0142  0.0751  -0.0539 10  GLY A CA  
72   C C   . GLY A 10  ? 0.4161 0.3526 0.2538 0.0000  0.0540  -0.0625 10  GLY A C   
73   O O   . GLY A 10  ? 0.3432 0.3720 0.2226 -0.0347 0.0397  -0.0767 10  GLY A O   
74   N N   . LEU A 11  ? 0.4140 0.3424 0.2810 -0.0315 0.0265  -0.0613 11  LEU A N   
75   C CA  . LEU A 11  ? 0.3673 0.3631 0.2669 -0.0313 0.0027  -0.0779 11  LEU A CA  
76   C C   . LEU A 11  ? 0.3704 0.3778 0.2377 -0.0421 0.0019  -0.0279 11  LEU A C   
77   O O   . LEU A 11  ? 0.3282 0.4185 0.3483 -0.0580 -0.0319 -0.0347 11  LEU A O   
78   C CB  . LEU A 11  ? 0.4647 0.3922 0.3577 0.0044  0.0320  -0.1049 11  LEU A CB  
79   C CG  . LEU A 11  ? 0.5022 0.4515 0.3679 -0.0378 0.0379  -0.1149 11  LEU A CG  
80   C CD1 . LEU A 11  ? 0.4858 0.5104 0.4370 -0.0754 0.0397  -0.1435 11  LEU A CD1 
81   C CD2 . LEU A 11  ? 0.5394 0.4832 0.4492 0.0098  0.0548  -0.1339 11  LEU A CD2 
82   N N   . VAL A 12  ? 0.3282 0.3861 0.1958 -0.0454 0.0246  -0.0245 12  VAL A N   
83   C CA  . VAL A 12  ? 0.3273 0.4251 0.3051 -0.0057 0.0292  -0.0170 12  VAL A CA  
84   C C   . VAL A 12  ? 0.2763 0.4422 0.2399 -0.0319 -0.0208 -0.0580 12  VAL A C   
85   O O   . VAL A 12  ? 0.2476 0.4825 0.1615 -0.0006 -0.0179 -0.0180 12  VAL A O   
86   C CB  . VAL A 12  ? 0.3712 0.4830 0.3718 0.0476  0.0394  -0.0421 12  VAL A CB  
87   C CG1 . VAL A 12  ? 0.3883 0.4724 0.4167 0.0632  0.0914  -0.1040 12  VAL A CG1 
88   C CG2 . VAL A 12  ? 0.3815 0.5118 0.3798 0.0413  0.0125  0.0178  12  VAL A CG2 
89   N N   . GLN A 13  ? 0.3059 0.4908 0.3045 -0.0394 -0.0631 -0.0476 13  GLN A N   
90   C CA  . GLN A 13  ? 0.3875 0.5248 0.2990 0.0009  -0.0317 -0.0624 13  GLN A CA  
91   C C   . GLN A 13  ? 0.2781 0.5165 0.1944 -0.0065 -0.0336 -0.0631 13  GLN A C   
92   O O   . GLN A 13  ? 0.2506 0.4700 0.2010 0.0165  -0.0254 -0.0316 13  GLN A O   
93   C CB  . GLN A 13  ? 0.4930 0.6183 0.3013 0.0042  -0.0745 -0.1256 13  GLN A CB  
94   C CG  . GLN A 13  ? 0.5908 0.5999 0.4690 0.0063  -0.0230 -0.0612 13  GLN A CG  
95   C CD  . GLN A 13  ? 0.6761 0.7401 0.5067 0.0851  0.0522  -0.0430 13  GLN A CD  
96   O OE1 . GLN A 13  ? 0.9352 0.8343 0.5956 0.0390  0.0809  0.0838  13  GLN A OE1 
97   N NE2 . GLN A 13  ? 0.8358 0.8709 0.4245 0.1070  0.0395  0.0223  13  GLN A NE2 
98   N N   . PRO A 14  ? 0.2073 0.5229 0.2052 0.0015  0.0096  -0.0716 14  PRO A N   
99   C CA  . PRO A 14  ? 0.2277 0.5255 0.1912 0.0123  -0.0158 -0.0456 14  PRO A CA  
100  C C   . PRO A 14  ? 0.2234 0.5100 0.2596 0.0016  -0.0287 -0.0684 14  PRO A C   
101  O O   . PRO A 14  ? 0.2512 0.4866 0.1908 -0.0040 0.0123  -0.0651 14  PRO A O   
102  C CB  . PRO A 14  ? 0.2840 0.5540 0.2775 0.0113  0.0409  -0.0067 14  PRO A CB  
103  C CG  . PRO A 14  ? 0.2999 0.5493 0.2717 0.0140  0.0735  -0.0018 14  PRO A CG  
104  C CD  . PRO A 14  ? 0.2572 0.5505 0.2240 -0.0045 0.0517  -0.0369 14  PRO A CD  
105  N N   . GLY A 15  ? 0.2651 0.5001 0.2095 0.0428  -0.0406 -0.0273 15  GLY A N   
106  C CA  . GLY A 15  ? 0.2510 0.5086 0.2536 0.0163  -0.0110 -0.0255 15  GLY A CA  
107  C C   . GLY A 15  ? 0.2401 0.4954 0.2526 0.0227  -0.0266 -0.0258 15  GLY A C   
108  O O   . GLY A 15  ? 0.2357 0.5545 0.2626 0.0433  -0.0410 -0.0296 15  GLY A O   
109  N N   . GLY A 16  ? 0.1967 0.4609 0.2028 -0.0053 -0.0034 -0.0341 16  GLY A N   
110  C CA  . GLY A 16  ? 0.2597 0.4440 0.2193 -0.0217 -0.0050 -0.0499 16  GLY A CA  
111  C C   . GLY A 16  ? 0.1857 0.3692 0.2079 -0.0076 -0.0062 -0.0282 16  GLY A C   
112  O O   . GLY A 16  ? 0.1670 0.3695 0.2083 -0.0008 0.0021  -0.0146 16  GLY A O   
113  N N   . SER A 17  ? 0.1988 0.3880 0.1692 -0.0097 0.0036  -0.0380 17  SER A N   
114  C CA  . SER A 17  ? 0.2266 0.3888 0.1739 -0.0074 0.0087  -0.0538 17  SER A CA  
115  C C   . SER A 17  ? 0.2224 0.3745 0.1951 -0.0079 -0.0070 -0.0610 17  SER A C   
116  O O   . SER A 17  ? 0.2678 0.4095 0.2165 0.0257  -0.0125 -0.0930 17  SER A O   
117  C CB  . SER A 17  ? 0.2300 0.3763 0.1878 -0.0211 0.0221  -0.0093 17  SER A CB  
118  O OG  . SER A 17  ? 0.2268 0.3772 0.2055 -0.0144 0.0348  -0.0069 17  SER A OG  
119  N N   . LEU A 18  ? 0.2108 0.3790 0.1923 -0.0109 0.0028  -0.0610 18  LEU A N   
120  C CA  A LEU A 18  ? 0.2260 0.3768 0.1670 -0.0148 0.0079  -0.0624 18  LEU A CA  
121  C CA  B LEU A 18  ? 0.2175 0.3734 0.1699 -0.0121 0.0104  -0.0627 18  LEU A CA  
122  C C   . LEU A 18  ? 0.2075 0.3283 0.1564 -0.0100 -0.0147 -0.0588 18  LEU A C   
123  O O   . LEU A 18  ? 0.2644 0.3155 0.1511 -0.0138 -0.0177 -0.0181 18  LEU A O   
124  C CB  A LEU A 18  ? 0.2255 0.4182 0.2277 -0.0125 -0.0098 -0.0566 18  LEU A CB  
125  C CB  B LEU A 18  ? 0.2171 0.4000 0.2183 0.0020  0.0004  -0.0645 18  LEU A CB  
126  C CG  A LEU A 18  ? 0.2727 0.3881 0.2734 -0.0086 -0.0233 -0.0737 18  LEU A CG  
127  C CG  B LEU A 18  ? 0.2550 0.3879 0.2816 -0.0031 -0.0208 -0.0547 18  LEU A CG  
128  C CD1 A LEU A 18  ? 0.2727 0.3722 0.2556 -0.0145 -0.0394 -0.0726 18  LEU A CD1 
129  C CD1 B LEU A 18  ? 0.3338 0.3835 0.3355 0.0011  -0.0335 -0.0737 18  LEU A CD1 
130  C CD2 A LEU A 18  ? 0.3483 0.3976 0.3581 -0.0085 -0.0358 -0.0406 18  LEU A CD2 
131  C CD2 B LEU A 18  ? 0.2487 0.3867 0.2887 0.0011  -0.0081 -0.0615 18  LEU A CD2 
132  N N   . ARG A 19  ? 0.2282 0.3143 0.1876 -0.0004 -0.0035 -0.0380 19  ARG A N   
133  C CA  . ARG A 19  ? 0.2085 0.3227 0.1951 -0.0410 -0.0035 -0.0631 19  ARG A CA  
134  C C   . ARG A 19  ? 0.2143 0.2927 0.2346 -0.0353 0.0075  -0.0316 19  ARG A C   
135  O O   . ARG A 19  ? 0.2609 0.2965 0.2834 -0.0537 -0.0439 -0.0738 19  ARG A O   
136  C CB  . ARG A 19  ? 0.2098 0.3969 0.2670 -0.0302 0.0216  -0.0005 19  ARG A CB  
137  C CG  . ARG A 19  ? 0.3088 0.4516 0.3160 -0.0298 0.0201  -0.0353 19  ARG A CG  
138  C CD  . ARG A 19  ? 0.4271 0.5507 0.4047 -0.0271 0.1121  0.0443  19  ARG A CD  
139  N NE  . ARG A 19  ? 0.5733 0.5120 0.5350 -0.0432 0.0981  0.0020  19  ARG A NE  
140  C CZ  . ARG A 19  ? 0.6506 0.6098 0.4854 -0.0481 0.0289  0.0755  19  ARG A CZ  
141  N NH1 . ARG A 19  ? 0.5657 0.7495 0.4461 -0.0370 -0.0307 0.0505  19  ARG A NH1 
142  N NH2 . ARG A 19  ? 0.7269 0.6272 0.6276 -0.0289 -0.0402 0.0769  19  ARG A NH2 
143  N N   . LEU A 20  ? 0.2037 0.2850 0.1773 -0.0297 0.0075  -0.0074 20  LEU A N   
144  C CA  . LEU A 20  ? 0.2209 0.2779 0.1427 -0.0155 0.0294  0.0126  20  LEU A CA  
145  C C   . LEU A 20  ? 0.1851 0.2724 0.1326 -0.0179 0.0100  -0.0171 20  LEU A C   
146  O O   . LEU A 20  ? 0.2316 0.2688 0.1517 -0.0133 0.0389  -0.0227 20  LEU A O   
147  C CB  . LEU A 20  ? 0.2012 0.2903 0.1592 -0.0092 0.0185  0.0125  20  LEU A CB  
148  C CG  . LEU A 20  ? 0.2272 0.3036 0.1602 0.0044  0.0294  0.0012  20  LEU A CG  
149  C CD1 . LEU A 20  ? 0.2319 0.3556 0.1905 -0.0101 0.0308  -0.0246 20  LEU A CD1 
150  C CD2 . LEU A 20  ? 0.2409 0.3331 0.1649 -0.0123 0.0415  -0.0322 20  LEU A CD2 
151  N N   . SER A 21  ? 0.1882 0.2616 0.1525 -0.0451 -0.0007 -0.0061 21  SER A N   
152  C CA  . SER A 21  ? 0.2167 0.2867 0.1535 -0.0119 0.0037  -0.0083 21  SER A CA  
153  C C   . SER A 21  ? 0.1922 0.2408 0.1567 -0.0048 0.0152  -0.0162 21  SER A C   
154  O O   . SER A 21  ? 0.1818 0.2800 0.1771 -0.0034 -0.0004 -0.0409 21  SER A O   
155  C CB  . SER A 21  ? 0.2580 0.3428 0.2465 -0.0452 0.0497  0.0081  21  SER A CB  
156  O OG  . SER A 21  ? 0.3784 0.3290 0.3581 -0.0472 0.0230  0.0347  21  SER A OG  
157  N N   . CYS A 22  ? 0.1618 0.2563 0.1434 -0.0088 -0.0156 -0.0177 22  CYS A N   
158  C CA  . CYS A 22  ? 0.1572 0.2933 0.1387 0.0153  -0.0125 0.0029  22  CYS A CA  
159  C C   . CYS A 22  ? 0.1740 0.2939 0.1523 -0.0059 0.0067  -0.0212 22  CYS A C   
160  O O   . CYS A 22  ? 0.1856 0.3438 0.1801 0.0445  0.0281  0.0017  22  CYS A O   
161  C CB  . CYS A 22  ? 0.2022 0.3009 0.1900 0.0110  0.0020  0.0183  22  CYS A CB  
162  S SG  . CYS A 22  ? 0.2260 0.4117 0.2340 -0.0117 -0.0163 -0.0018 22  CYS A SG  
163  N N   . ALA A 23  ? 0.1884 0.3260 0.1668 0.0050  0.0069  0.0204  23  ALA A N   
164  C CA  . ALA A 23  ? 0.2354 0.3365 0.1769 -0.0019 0.0059  0.0336  23  ALA A CA  
165  C C   . ALA A 23  ? 0.2215 0.3133 0.2004 -0.0085 -0.0055 0.0332  23  ALA A C   
166  O O   . ALA A 23  ? 0.2066 0.3118 0.2263 -0.0113 -0.0421 0.0269  23  ALA A O   
167  C CB  . ALA A 23  ? 0.3024 0.3673 0.2391 -0.0443 0.0069  0.0267  23  ALA A CB  
168  N N   . ALA A 24  ? 0.1942 0.3684 0.2236 0.0081  -0.0153 0.0033  24  ALA A N   
169  C CA  . ALA A 24  ? 0.2057 0.3559 0.2263 -0.0383 -0.0257 0.0485  24  ALA A CA  
170  C C   . ALA A 24  ? 0.2487 0.4083 0.2490 -0.0652 -0.0402 0.0800  24  ALA A C   
171  O O   . ALA A 24  ? 0.2697 0.4716 0.2476 -0.1064 0.0078  0.0924  24  ALA A O   
172  C CB  . ALA A 24  ? 0.2319 0.3608 0.1980 -0.0264 -0.0026 0.0513  24  ALA A CB  
173  N N   . SER A 25  ? 0.3000 0.3562 0.2988 -0.0239 -0.0193 0.1176  25  SER A N   
174  C CA  . SER A 25  ? 0.3884 0.3695 0.2416 -0.0372 -0.0139 0.0892  25  SER A CA  
175  C C   . SER A 25  ? 0.3667 0.3456 0.2731 -0.0090 -0.0324 0.1039  25  SER A C   
176  O O   . SER A 25  ? 0.3002 0.3558 0.1988 0.0041  -0.0376 0.0468  25  SER A O   
177  C CB  . SER A 25  ? 0.4630 0.3550 0.3008 -0.0284 -0.0268 0.0954  25  SER A CB  
178  O OG  . SER A 25  ? 0.4985 0.3258 0.3063 -0.0193 -0.0057 0.0336  25  SER A OG  
179  N N   . GLY A 26  ? 0.4045 0.4136 0.2452 -0.0158 0.0153  0.0859  26  GLY A N   
180  C CA  . GLY A 26  ? 0.4397 0.4016 0.3121 -0.0080 -0.0272 0.0483  26  GLY A CA  
181  C C   . GLY A 26  ? 0.4333 0.4192 0.2859 0.0558  -0.0258 0.0870  26  GLY A C   
182  O O   . GLY A 26  ? 0.4222 0.5224 0.4093 0.0425  0.0726  -0.0278 26  GLY A O   
183  N N   . SER A 27  ? 0.4923 0.4027 0.3290 0.0427  -0.0250 0.0539  27  SER A N   
184  C CA  . SER A 27  ? 0.5498 0.4083 0.3794 0.0719  -0.0157 0.0411  27  SER A CA  
185  C C   . SER A 27  ? 0.4335 0.3970 0.2056 0.0322  0.0237  0.0180  27  SER A C   
186  O O   . SER A 27  ? 0.4544 0.3886 0.2443 0.0293  0.0002  0.0233  27  SER A O   
187  C CB  . SER A 27  ? 0.6355 0.4544 0.4585 0.0663  -0.1008 0.0997  27  SER A CB  
188  O OG  . SER A 27  ? 0.7466 0.4864 0.5728 0.1192  -0.0960 0.1411  27  SER A OG  
189  N N   . VAL A 28  ? 0.3839 0.3905 0.1930 0.0017  0.0539  -0.0555 28  VAL A N   
190  C CA  . VAL A 28  ? 0.3429 0.4167 0.2590 -0.0089 0.0374  -0.0191 28  VAL A CA  
191  C C   . VAL A 28  ? 0.3332 0.3457 0.2829 -0.0191 0.0067  -0.0296 28  VAL A C   
192  O O   . VAL A 28  ? 0.3208 0.4043 0.3768 -0.0342 0.0203  -0.0195 28  VAL A O   
193  C CB  . VAL A 28  ? 0.3254 0.4610 0.2795 -0.0223 0.0424  -0.0518 28  VAL A CB  
194  C CG1 . VAL A 28  ? 0.3563 0.4940 0.2350 -0.0267 0.0269  -0.0002 28  VAL A CG1 
195  C CG2 . VAL A 28  ? 0.3338 0.4998 0.2720 -0.0619 0.0523  -0.0802 28  VAL A CG2 
196  N N   . PHE A 29  ? 0.2631 0.3423 0.2616 -0.0072 0.0160  -0.0335 29  PHE A N   
197  C CA  . PHE A 29  ? 0.2525 0.3303 0.2332 0.0026  0.0022  -0.0129 29  PHE A CA  
198  C C   . PHE A 29  ? 0.2687 0.3126 0.1814 0.0332  0.0474  -0.0268 29  PHE A C   
199  O O   . PHE A 29  ? 0.2733 0.3728 0.3050 0.0250  -0.0418 0.0345  29  PHE A O   
200  C CB  . PHE A 29  ? 0.2117 0.3136 0.2483 -0.0354 0.0289  -0.0118 29  PHE A CB  
201  C CG  . PHE A 29  ? 0.2124 0.3455 0.2383 -0.0082 0.0160  -0.0100 29  PHE A CG  
202  C CD1 . PHE A 29  ? 0.2187 0.3597 0.2211 -0.0053 0.0231  -0.0459 29  PHE A CD1 
203  C CD2 . PHE A 29  ? 0.2805 0.3952 0.2332 0.0394  0.0614  -0.0222 29  PHE A CD2 
204  C CE1 . PHE A 29  ? 0.2522 0.3845 0.2110 0.0098  0.0244  -0.0417 29  PHE A CE1 
205  C CE2 . PHE A 29  ? 0.2856 0.4271 0.2427 0.0469  0.0499  0.0002  29  PHE A CE2 
206  C CZ  . PHE A 29  ? 0.2671 0.4321 0.2049 0.0434  0.0108  -0.0010 29  PHE A CZ  
207  N N   . LYS A 30  ? 0.2717 0.3278 0.1592 0.0242  0.0282  -0.0137 30  LYS A N   
208  C CA  . LYS A 30  ? 0.2951 0.3246 0.1305 0.0342  0.0766  0.0135  30  LYS A CA  
209  C C   . LYS A 30  ? 0.2823 0.3293 0.1294 0.0146  0.0720  -0.0001 30  LYS A C   
210  O O   . LYS A 30  ? 0.2862 0.3476 0.1444 -0.0331 0.0617  -0.0268 30  LYS A O   
211  C CB  . LYS A 30  ? 0.3653 0.3539 0.2107 0.0392  0.0526  -0.0198 30  LYS A CB  
212  C CG  . LYS A 30  ? 0.4417 0.3898 0.2928 0.0799  0.0063  -0.0031 30  LYS A CG  
213  C CD  . LYS A 30  ? 0.5486 0.4149 0.4104 0.0772  -0.0103 -0.0491 30  LYS A CD  
214  C CE  . LYS A 30  ? 0.6162 0.5714 0.4777 0.1145  -0.0708 0.0420  30  LYS A CE  
215  N NZ  . LYS A 30  ? 0.6722 0.5766 0.5441 0.1339  -0.0836 -0.0351 30  LYS A NZ  
216  N N   . ILE A 31  ? 0.2795 0.3923 0.1840 0.0023  0.0387  0.0035  31  ILE A N   
217  C CA  . ILE A 31  ? 0.2638 0.3480 0.1532 -0.0022 0.0112  -0.0071 31  ILE A CA  
218  C C   . ILE A 31  ? 0.2777 0.3641 0.1978 0.0317  0.0016  -0.0074 31  ILE A C   
219  O O   . ILE A 31  ? 0.3230 0.3773 0.2712 0.0739  -0.0650 0.0445  31  ILE A O   
220  C CB  . ILE A 31  ? 0.3118 0.3348 0.2105 -0.0186 0.0212  -0.0305 31  ILE A CB  
221  C CG1 . ILE A 31  ? 0.3132 0.3428 0.2222 -0.0158 0.0182  -0.0090 31  ILE A CG1 
222  C CG2 . ILE A 31  ? 0.2815 0.3438 0.2312 -0.0259 0.0205  0.0060  31  ILE A CG2 
223  C CD1 . ILE A 31  ? 0.3250 0.4034 0.2740 -0.0550 0.0028  -0.0158 31  ILE A CD1 
224  N N   . ASN A 32  ? 0.2960 0.3432 0.1798 0.0248  0.0480  -0.0399 32  ASN A N   
225  C CA  . ASN A 32  ? 0.3657 0.3529 0.2100 0.0514  0.0355  -0.0189 32  ASN A CA  
226  C C   . ASN A 32  ? 0.2974 0.3189 0.2130 0.0399  0.0177  -0.0174 32  ASN A C   
227  O O   . ASN A 32  ? 0.3543 0.2974 0.2190 0.0492  0.0159  -0.0249 32  ASN A O   
228  C CB  . ASN A 32  ? 0.3866 0.3888 0.2210 0.0411  0.0227  -0.0304 32  ASN A CB  
229  C CG  . ASN A 32  ? 0.5035 0.4899 0.2210 0.0586  0.0317  -0.0119 32  ASN A CG  
230  O OD1 . ASN A 32  ? 0.6226 0.5218 0.3347 0.1347  0.0939  -0.0459 32  ASN A OD1 
231  N ND2 . ASN A 32  ? 0.4584 0.7513 0.4388 -0.0318 -0.1049 -0.0579 32  ASN A ND2 
232  N N   . VAL A 33  ? 0.2699 0.2850 0.2131 -0.0066 0.0230  -0.0271 33  VAL A N   
233  C CA  . VAL A 33  ? 0.3041 0.2589 0.2199 -0.0188 0.0264  0.0049  33  VAL A CA  
234  C C   . VAL A 33  ? 0.2434 0.2495 0.1633 -0.0127 0.0193  0.0233  33  VAL A C   
235  O O   . VAL A 33  ? 0.2069 0.2483 0.1362 0.0188  0.0192  -0.0228 33  VAL A O   
236  C CB  . VAL A 33  ? 0.3599 0.3165 0.2996 -0.0861 0.0410  0.0169  33  VAL A CB  
237  C CG1 . VAL A 33  ? 0.4423 0.3504 0.3147 -0.1472 0.0784  0.0205  33  VAL A CG1 
238  C CG2 . VAL A 33  ? 0.4129 0.3193 0.3768 -0.0470 0.0431  0.0044  33  VAL A CG2 
239  N N   . MET A 34  ? 0.2126 0.2401 0.2018 0.0352  -0.0107 0.0155  34  MET A N   
240  C CA  . MET A 34  ? 0.2194 0.2571 0.1618 0.0415  0.0161  0.0224  34  MET A CA  
241  C C   . MET A 34  ? 0.1859 0.2473 0.1442 0.0454  0.0053  0.0057  34  MET A C   
242  O O   . MET A 34  ? 0.2505 0.2578 0.1666 0.0815  0.0220  0.0260  34  MET A O   
243  C CB  . MET A 34  ? 0.2348 0.2527 0.1811 0.0327  0.0109  0.0078  34  MET A CB  
244  C CG  . MET A 34  ? 0.2701 0.2778 0.2159 0.0229  0.0213  0.0327  34  MET A CG  
245  S SD  . MET A 34  ? 0.2666 0.4489 0.3441 -0.0074 0.0221  0.0449  34  MET A SD  
246  C CE  . MET A 34  ? 0.3193 0.5324 0.2870 0.0503  -0.0030 0.0261  34  MET A CE  
247  N N   . ALA A 35  ? 0.1737 0.2024 0.1454 0.0403  -0.0096 -0.0101 35  ALA A N   
248  C CA  . ALA A 35  ? 0.1896 0.2029 0.1469 0.0197  -0.0089 -0.0074 35  ALA A CA  
249  C C   . ALA A 35  ? 0.1721 0.2041 0.1451 0.0196  -0.0025 0.0033  35  ALA A C   
250  O O   . ALA A 35  ? 0.2130 0.2301 0.1087 0.0443  0.0031  0.0128  35  ALA A O   
251  C CB  . ALA A 35  ? 0.2022 0.2112 0.1552 0.0124  0.0017  -0.0337 35  ALA A CB  
252  N N   . TRP A 36  ? 0.1775 0.2066 0.1489 0.0278  -0.0103 0.0156  36  TRP A N   
253  C CA  . TRP A 36  ? 0.1573 0.1933 0.1715 0.0130  0.0041  0.0068  36  TRP A CA  
254  C C   . TRP A 36  ? 0.1738 0.1754 0.1532 -0.0028 -0.0131 -0.0023 36  TRP A C   
255  O O   . TRP A 36  ? 0.1692 0.1904 0.1812 0.0179  -0.0034 0.0192  36  TRP A O   
256  C CB  . TRP A 36  ? 0.1480 0.2066 0.1480 0.0075  0.0169  0.0064  36  TRP A CB  
257  C CG  . TRP A 36  ? 0.1470 0.2147 0.1555 -0.0077 0.0081  -0.0135 36  TRP A CG  
258  C CD1 . TRP A 36  ? 0.1515 0.2272 0.1697 0.0114  0.0026  -0.0189 36  TRP A CD1 
259  C CD2 . TRP A 36  ? 0.1269 0.2125 0.1363 -0.0132 -0.0120 -0.0116 36  TRP A CD2 
260  N NE1 . TRP A 36  ? 0.1301 0.2573 0.1517 -0.0066 0.0249  -0.0287 36  TRP A NE1 
261  C CE2 . TRP A 36  ? 0.1369 0.2358 0.1437 -0.0098 0.0066  -0.0066 36  TRP A CE2 
262  C CE3 . TRP A 36  ? 0.1107 0.2118 0.1410 -0.0188 -0.0072 -0.0045 36  TRP A CE3 
263  C CZ2 . TRP A 36  ? 0.1632 0.2476 0.1927 -0.0295 0.0111  -0.0079 36  TRP A CZ2 
264  C CZ3 . TRP A 36  ? 0.1380 0.2245 0.1575 -0.0261 -0.0156 -0.0037 36  TRP A CZ3 
265  C CH2 . TRP A 36  ? 0.1533 0.2445 0.1709 -0.0350 -0.0015 -0.0027 36  TRP A CH2 
266  N N   . TYR A 37  ? 0.1685 0.1798 0.1597 -0.0025 -0.0130 0.0136  37  TYR A N   
267  C CA  . TYR A 37  ? 0.1799 0.1713 0.1587 -0.0024 0.0030  0.0152  37  TYR A CA  
268  C C   . TYR A 37  ? 0.1703 0.1797 0.1421 -0.0196 -0.0192 0.0141  37  TYR A C   
269  O O   . TYR A 37  ? 0.1950 0.1766 0.1586 -0.0160 0.0030  -0.0171 37  TYR A O   
270  C CB  . TYR A 37  ? 0.1868 0.2202 0.1636 -0.0254 0.0000  0.0163  37  TYR A CB  
271  C CG  . TYR A 37  ? 0.1961 0.2124 0.1641 -0.0238 -0.0009 0.0167  37  TYR A CG  
272  C CD1 . TYR A 37  ? 0.1655 0.2203 0.1981 -0.0491 0.0040  0.0113  37  TYR A CD1 
273  C CD2 . TYR A 37  ? 0.2302 0.2199 0.2005 -0.0373 0.0055  0.0066  37  TYR A CD2 
274  C CE1 . TYR A 37  ? 0.1996 0.2486 0.1774 -0.0326 0.0072  0.0185  37  TYR A CE1 
275  C CE2 . TYR A 37  ? 0.2524 0.2396 0.1966 -0.0408 0.0225  0.0101  37  TYR A CE2 
276  C CZ  . TYR A 37  ? 0.2480 0.2458 0.1899 -0.0370 0.0158  0.0107  37  TYR A CZ  
277  O OH  . TYR A 37  ? 0.2479 0.2604 0.2449 -0.0254 0.0609  -0.0238 37  TYR A OH  
278  N N   . ARG A 38  ? 0.1641 0.2039 0.1518 -0.0134 -0.0092 0.0116  38  ARG A N   
279  C CA  . ARG A 38  ? 0.1624 0.2275 0.1807 -0.0054 0.0048  -0.0106 38  ARG A CA  
280  C C   . ARG A 38  ? 0.1899 0.2349 0.1717 -0.0336 0.0174  0.0110  38  ARG A C   
281  O O   . ARG A 38  ? 0.2048 0.2401 0.1706 -0.0293 0.0252  -0.0189 38  ARG A O   
282  C CB  . ARG A 38  ? 0.1331 0.2465 0.2111 -0.0018 -0.0030 -0.0157 38  ARG A CB  
283  C CG  . ARG A 38  ? 0.1695 0.2574 0.2111 0.0280  -0.0079 -0.0086 38  ARG A CG  
284  C CD  . ARG A 38  ? 0.2212 0.2956 0.2207 0.0018  -0.0360 -0.0034 38  ARG A CD  
285  N NE  . ARG A 38  ? 0.2638 0.2877 0.2220 0.0120  -0.0356 -0.0103 38  ARG A NE  
286  C CZ  . ARG A 38  ? 0.2665 0.3132 0.2600 0.0256  -0.0462 0.0170  38  ARG A CZ  
287  N NH1 . ARG A 38  ? 0.2493 0.2781 0.2607 0.0245  -0.0036 0.0252  38  ARG A NH1 
288  N NH2 . ARG A 38  ? 0.3479 0.3228 0.3470 0.0037  -0.1437 0.0387  38  ARG A NH2 
289  N N   . GLN A 39  ? 0.1963 0.2427 0.1611 -0.0259 0.0200  0.0111  39  GLN A N   
290  C CA  A GLN A 39  ? 0.1983 0.2492 0.1749 0.0050  0.0349  0.0034  39  GLN A CA  
291  C CA  B GLN A 39  ? 0.2054 0.2427 0.1758 -0.0083 0.0363  0.0014  39  GLN A CA  
292  C C   . GLN A 39  ? 0.2442 0.2481 0.1704 0.0146  0.0280  0.0085  39  GLN A C   
293  O O   . GLN A 39  ? 0.3014 0.3299 0.1585 -0.0694 0.0620  -0.0295 39  GLN A O   
294  C CB  A GLN A 39  ? 0.2053 0.2737 0.1608 0.0115  0.0286  0.0024  39  GLN A CB  
295  C CB  B GLN A 39  ? 0.2159 0.2398 0.1718 -0.0154 0.0232  0.0025  39  GLN A CB  
296  C CG  A GLN A 39  ? 0.1976 0.2810 0.1608 0.0031  0.0137  0.0225  39  GLN A CG  
297  C CG  B GLN A 39  ? 0.2106 0.2391 0.1824 -0.0257 0.0130  0.0073  39  GLN A CG  
298  C CD  A GLN A 39  ? 0.2083 0.2476 0.1964 0.0365  0.0249  0.0286  39  GLN A CD  
299  C CD  B GLN A 39  ? 0.2299 0.2346 0.1965 -0.0272 0.0152  0.0147  39  GLN A CD  
300  O OE1 A GLN A 39  ? 0.2295 0.2382 0.1854 0.0447  0.0290  0.0088  39  GLN A OE1 
301  O OE1 B GLN A 39  ? 0.2484 0.2155 0.2020 -0.0124 -0.0002 0.0188  39  GLN A OE1 
302  N NE2 A GLN A 39  ? 0.2341 0.2686 0.2228 0.0317  0.0370  0.0777  39  GLN A NE2 
303  N NE2 B GLN A 39  ? 0.2282 0.2468 0.2086 -0.0351 0.0215  0.0226  39  GLN A NE2 
304  N N   . ALA A 40  ? 0.3312 0.2513 0.1864 0.0273  0.0415  0.0275  40  ALA A N   
305  C CA  . ALA A 40  ? 0.3518 0.2437 0.1959 0.0401  0.0435  -0.0005 40  ALA A CA  
306  C C   . ALA A 40  ? 0.3588 0.3263 0.2349 0.0389  0.0417  0.0263  40  ALA A C   
307  O O   . ALA A 40  ? 0.3364 0.4235 0.1710 0.0190  0.0711  -0.0162 40  ALA A O   
308  C CB  . ALA A 40  ? 0.3810 0.2410 0.2250 -0.0107 -0.0048 0.0215  40  ALA A CB  
309  N N   . PRO A 41  ? 0.4218 0.3774 0.2506 0.0865  0.0782  0.0466  41  PRO A N   
310  C CA  . PRO A 41  ? 0.4163 0.4637 0.2925 0.0760  0.0561  0.0351  41  PRO A CA  
311  C C   . PRO A 41  ? 0.4174 0.4475 0.2331 0.0107  0.0429  0.0149  41  PRO A C   
312  O O   . PRO A 41  ? 0.4380 0.4401 0.1884 0.0226  0.0634  0.0392  41  PRO A O   
313  C CB  . PRO A 41  ? 0.4756 0.5584 0.3566 0.0698  0.0770  -0.0388 41  PRO A CB  
314  C CG  . PRO A 41  ? 0.5297 0.5163 0.3371 0.0189  0.1115  -0.0363 41  PRO A CG  
315  C CD  . PRO A 41  ? 0.4781 0.4049 0.2998 0.0333  0.0768  0.0461  41  PRO A CD  
316  N N   . GLY A 42  ? 0.4037 0.4948 0.2449 -0.0327 0.0098  0.0999  42  GLY A N   
317  C CA  . GLY A 42  ? 0.3193 0.5080 0.2652 -0.1222 0.0883  0.0904  42  GLY A CA  
318  C C   . GLY A 42  ? 0.3829 0.4761 0.2099 -0.1380 0.0738  0.0786  42  GLY A C   
319  O O   . GLY A 42  ? 0.4640 0.4988 0.2897 -0.1550 0.0362  0.0903  42  GLY A O   
320  N N   . LYS A 43  ? 0.2902 0.3956 0.2207 -0.1161 0.0342  0.0801  43  LYS A N   
321  C CA  . LYS A 43  ? 0.3617 0.3941 0.2169 -0.0773 0.0351  0.0594  43  LYS A CA  
322  C C   . LYS A 43  ? 0.3737 0.4322 0.2267 -0.0337 0.0079  0.0524  43  LYS A C   
323  O O   . LYS A 43  ? 0.4058 0.3685 0.4569 -0.0010 -0.0136 -0.1155 43  LYS A O   
324  C CB  . LYS A 43  ? 0.3593 0.3493 0.2888 -0.0736 0.0394  0.0286  43  LYS A CB  
325  C CG  . LYS A 43  ? 0.3794 0.3892 0.2748 -0.0341 0.0560  0.0138  43  LYS A CG  
326  C CD  . LYS A 43  ? 0.3999 0.3926 0.3253 -0.0533 0.0663  0.0291  43  LYS A CD  
327  C CE  . LYS A 43  ? 0.3869 0.4263 0.3952 -0.0207 0.0382  0.0298  43  LYS A CE  
328  N NZ  . LYS A 43  ? 0.3608 0.5026 0.4062 -0.0151 0.0348  0.0631  43  LYS A NZ  
329  N N   . GLY A 44  ? 0.2252 0.5143 0.1964 -0.1258 0.0189  0.0449  44  GLY A N   
330  C CA  . GLY A 44  ? 0.3039 0.5255 0.2061 -0.0925 0.0030  0.0394  44  GLY A CA  
331  C C   . GLY A 44  ? 0.3156 0.4665 0.1927 -0.0689 0.0450  -0.0070 44  GLY A C   
332  O O   . GLY A 44  ? 0.3486 0.4582 0.2631 -0.0712 0.0164  -0.0107 44  GLY A O   
333  N N   . ARG A 45  ? 0.2031 0.3157 0.2086 -0.0356 0.0551  -0.0011 45  ARG A N   
334  C CA  . ARG A 45  ? 0.1914 0.2779 0.2047 -0.0294 0.0458  -0.0061 45  ARG A CA  
335  C C   . ARG A 45  ? 0.2091 0.2495 0.2350 -0.0383 0.0328  -0.0058 45  ARG A C   
336  O O   . ARG A 45  ? 0.1881 0.2586 0.2546 -0.0463 0.0402  -0.0147 45  ARG A O   
337  C CB  . ARG A 45  ? 0.2106 0.3078 0.2010 -0.0021 0.0391  -0.0121 45  ARG A CB  
338  C CG  . ARG A 45  ? 0.2104 0.2861 0.1896 -0.0107 0.0276  -0.0229 45  ARG A CG  
339  C CD  . ARG A 45  ? 0.2229 0.3344 0.2068 -0.0013 0.0068  -0.0155 45  ARG A CD  
340  N NE  . ARG A 45  ? 0.2622 0.2977 0.2455 -0.0063 0.0131  -0.0223 45  ARG A NE  
341  C CZ  . ARG A 45  ? 0.2657 0.3178 0.2667 -0.0445 -0.0110 0.0085  45  ARG A CZ  
342  N NH1 . ARG A 45  ? 0.3115 0.3171 0.2422 -0.0780 0.0277  0.0272  45  ARG A NH1 
343  N NH2 . ARG A 45  ? 0.3474 0.3511 0.2622 -0.0017 -0.0266 -0.0007 45  ARG A NH2 
344  N N   . GLU A 46  ? 0.2109 0.2270 0.2121 -0.0227 0.0248  -0.0013 46  GLU A N   
345  C CA  A GLU A 46  ? 0.1911 0.2316 0.2062 -0.0277 0.0328  0.0138  46  GLU A CA  
346  C CA  B GLU A 46  ? 0.1891 0.2300 0.2163 -0.0330 0.0380  -0.0022 46  GLU A CA  
347  C C   . GLU A 46  ? 0.1961 0.2146 0.1983 -0.0218 0.0328  0.0189  46  GLU A C   
348  O O   . GLU A 46  ? 0.1834 0.2072 0.2028 -0.0102 0.0387  0.0039  46  GLU A O   
349  C CB  A GLU A 46  ? 0.2237 0.2533 0.2215 -0.0015 0.0261  0.0515  46  GLU A CB  
350  C CB  B GLU A 46  ? 0.2227 0.2600 0.2289 -0.0308 0.0490  0.0222  46  GLU A CB  
351  C CG  A GLU A 46  ? 0.2377 0.2652 0.2409 0.0087  0.0133  0.0533  46  GLU A CG  
352  C CG  B GLU A 46  ? 0.2390 0.3049 0.2605 -0.0607 0.0624  0.0193  46  GLU A CG  
353  C CD  A GLU A 46  ? 0.2821 0.2673 0.2547 0.0294  -0.0020 0.0834  46  GLU A CD  
354  C CD  B GLU A 46  ? 0.2653 0.3029 0.2601 -0.0633 0.0788  0.0291  46  GLU A CD  
355  O OE1 A GLU A 46  ? 0.2673 0.3031 0.3031 0.0310  -0.0237 0.1348  46  GLU A OE1 
356  O OE1 B GLU A 46  ? 0.2851 0.2969 0.3028 -0.0488 0.0321  -0.0228 46  GLU A OE1 
357  O OE2 A GLU A 46  ? 0.2716 0.2907 0.2177 0.0652  -0.0008 0.0792  46  GLU A OE2 
358  O OE2 B GLU A 46  ? 0.2923 0.3617 0.3404 -0.0957 0.1220  0.0483  46  GLU A OE2 
359  N N   . LEU A 47  ? 0.2003 0.2084 0.2223 -0.0111 0.0350  0.0218  47  LEU A N   
360  C CA  . LEU A 47  ? 0.2115 0.2323 0.2088 -0.0189 0.0462  0.0298  47  LEU A CA  
361  C C   . LEU A 47  ? 0.1870 0.2325 0.2456 -0.0102 0.0449  0.0445  47  LEU A C   
362  O O   . LEU A 47  ? 0.2495 0.2611 0.3146 -0.0026 0.0629  0.0865  47  LEU A O   
363  C CB  . LEU A 47  ? 0.2835 0.2788 0.2643 -0.0105 0.0530  -0.0083 47  LEU A CB  
364  C CG  . LEU A 47  ? 0.3172 0.3305 0.2985 -0.0153 0.0936  -0.0151 47  LEU A CG  
365  C CD1 . LEU A 47  ? 0.3558 0.3371 0.2893 0.0199  0.0487  0.0067  47  LEU A CD1 
366  C CD2 . LEU A 47  ? 0.4061 0.3671 0.3290 0.0098  0.1039  -0.0329 47  LEU A CD2 
367  N N   . VAL A 48  ? 0.1811 0.2232 0.1893 0.0020  0.0096  0.0385  48  VAL A N   
368  C CA  . VAL A 48  ? 0.2218 0.2232 0.1792 -0.0007 -0.0105 0.0402  48  VAL A CA  
369  C C   . VAL A 48  ? 0.2187 0.1987 0.1701 -0.0038 -0.0207 0.0376  48  VAL A C   
370  O O   . VAL A 48  ? 0.2162 0.2202 0.2146 0.0283  -0.0403 0.0183  48  VAL A O   
371  C CB  . VAL A 48  ? 0.2503 0.2481 0.1935 0.0061  -0.0300 0.0006  48  VAL A CB  
372  C CG1 . VAL A 48  ? 0.2822 0.2850 0.2430 -0.0217 -0.0544 -0.0185 48  VAL A CG1 
373  C CG2 . VAL A 48  ? 0.2687 0.2751 0.2232 0.0351  -0.0386 -0.0251 48  VAL A CG2 
374  N N   . ALA A 49  ? 0.2239 0.2168 0.1784 0.0114  -0.0184 0.0562  49  ALA A N   
375  C CA  . ALA A 49  ? 0.2342 0.2072 0.1797 0.0151  -0.0165 0.0328  49  ALA A CA  
376  C C   . ALA A 49  ? 0.2061 0.1953 0.1687 0.0107  -0.0040 0.0139  49  ALA A C   
377  O O   . ALA A 49  ? 0.1892 0.2204 0.1918 0.0323  0.0119  0.0202  49  ALA A O   
378  C CB  . ALA A 49  ? 0.2008 0.2478 0.2029 -0.0013 -0.0019 0.0331  49  ALA A CB  
379  N N   . GLY A 50  ? 0.2264 0.2321 0.2019 0.0485  -0.0126 0.0029  50  GLY A N   
380  C CA  . GLY A 50  ? 0.2306 0.2263 0.1890 0.0390  -0.0237 -0.0178 50  GLY A CA  
381  C C   . GLY A 50  ? 0.2275 0.2330 0.2342 0.0223  -0.0118 -0.0245 50  GLY A C   
382  O O   . GLY A 50  ? 0.2519 0.2534 0.2718 0.0414  -0.0166 -0.0147 50  GLY A O   
383  N N   . ILE A 51  ? 0.2764 0.2427 0.2655 0.0578  0.0212  0.0125  51  ILE A N   
384  C CA  . ILE A 51  ? 0.3303 0.3187 0.2806 0.0877  0.0453  -0.0103 51  ILE A CA  
385  C C   . ILE A 51  ? 0.3870 0.3089 0.2478 0.0931  0.0586  0.0033  51  ILE A C   
386  O O   . ILE A 51  ? 0.3651 0.3052 0.1989 0.1058  0.0634  -0.0216 51  ILE A O   
387  C CB  . ILE A 51  ? 0.3171 0.4251 0.3836 0.0404  0.0972  -0.0251 51  ILE A CB  
388  C CG1 . ILE A 51  ? 0.4122 0.4700 0.4231 0.0337  0.0623  -0.0495 51  ILE A CG1 
389  C CG2 . ILE A 51  ? 0.3715 0.4227 0.4458 0.1011  0.1125  -0.0954 51  ILE A CG2 
390  C CD1 . ILE A 51  ? 0.4282 0.4817 0.4305 0.0235  0.1127  -0.0147 51  ILE A CD1 
391  N N   . ILE A 52  ? 0.4488 0.3029 0.2555 0.1164  0.0281  0.0019  52  ILE A N   
392  C CA  . ILE A 52  ? 0.4680 0.4424 0.2567 0.1011  0.0358  -0.0337 52  ILE A CA  
393  C C   . ILE A 52  ? 0.4633 0.4723 0.3147 0.1177  0.0507  0.0049  52  ILE A C   
394  O O   . ILE A 52  ? 0.4677 0.6605 0.3269 0.1485  0.0425  0.0277  52  ILE A O   
395  C CB  . ILE A 52  ? 0.5478 0.4787 0.3360 0.0422  0.0609  -0.0775 52  ILE A CB  
396  C CG1 . ILE A 52  ? 0.6131 0.5818 0.4359 0.0906  -0.0068 -0.0822 52  ILE A CG1 
397  C CG2 . ILE A 52  ? 0.5362 0.4996 0.3352 -0.0368 0.0336  -0.1007 52  ILE A CG2 
398  C CD1 . ILE A 52  ? 0.7554 0.6680 0.4907 0.0157  -0.0395 -0.1544 52  ILE A CD1 
399  N N   . SER A 53  ? 0.5397 0.4586 0.2749 0.1402  0.0577  -0.0471 53  SER A N   
400  C CA  . SER A 53  ? 0.5719 0.5362 0.3326 0.1085  0.0971  -0.0661 53  SER A CA  
401  C C   . SER A 53  ? 0.6080 0.5923 0.3038 0.1664  0.0569  -0.0566 53  SER A C   
402  O O   . SER A 53  ? 0.7632 0.5296 0.5196 0.1586  0.0948  -0.1036 53  SER A O   
403  C CB  . SER A 53  ? 0.6249 0.5846 0.4403 0.0873  -0.0037 -0.0072 53  SER A CB  
404  O OG  . SER A 53  ? 0.7018 0.6821 0.5940 0.0249  -0.0463 -0.0278 53  SER A OG  
405  N N   . GLY A 54  ? 0.6211 0.7302 0.3169 0.2056  0.0253  -0.0890 54  GLY A N   
406  C CA  . GLY A 54  ? 0.6635 0.7214 0.4901 0.2149  0.0320  -0.0392 54  GLY A CA  
407  C C   . GLY A 54  ? 0.6177 0.7972 0.4886 0.2658  0.0381  -0.0594 54  GLY A C   
408  O O   . GLY A 54  ? 0.6130 0.8584 0.7230 0.3083  0.0996  -0.0334 54  GLY A O   
409  N N   . GLY A 55  ? 0.5692 0.9152 0.4781 0.2240  0.1269  -0.0130 55  GLY A N   
410  C CA  . GLY A 55  ? 0.5920 0.8727 0.5081 0.1869  0.1133  -0.0627 55  GLY A CA  
411  C C   . GLY A 55  ? 0.4297 0.8033 0.5481 0.2180  0.1329  -0.0843 55  GLY A C   
412  O O   . GLY A 55  ? 0.5157 0.9483 0.5202 0.1898  0.1640  -0.0256 55  GLY A O   
413  N N   . SER A 56  ? 0.4518 0.7187 0.5392 0.2286  0.1081  0.0186  56  SER A N   
414  C CA  . SER A 56  ? 0.4873 0.5637 0.5121 0.2338  0.0762  -0.0426 56  SER A CA  
415  C C   . SER A 56  ? 0.4705 0.5175 0.3901 0.2499  0.0054  -0.0161 56  SER A C   
416  O O   . SER A 56  ? 0.4843 0.5172 0.2538 0.2338  0.0176  -0.0053 56  SER A O   
417  C CB  . SER A 56  ? 0.5988 0.4714 0.6270 0.2330  0.0783  -0.0691 56  SER A CB  
418  O OG  . SER A 56  ? 0.6906 0.4742 0.7091 0.1325  0.0832  -0.0861 56  SER A OG  
419  N N   . THR A 57  ? 0.4583 0.4952 0.4092 0.2841  -0.0376 0.0132  57  THR A N   
420  C CA  . THR A 57  ? 0.4504 0.4218 0.3956 0.2315  -0.0264 0.0376  57  THR A CA  
421  C C   . THR A 57  ? 0.5157 0.3309 0.3552 0.2270  -0.0187 0.0091  57  THR A C   
422  O O   . THR A 57  ? 0.5781 0.3395 0.3603 0.2415  0.0180  0.0408  57  THR A O   
423  C CB  . THR A 57  ? 0.4522 0.4830 0.4363 0.1998  -0.0721 0.0733  57  THR A CB  
424  O OG1 . THR A 57  ? 0.5434 0.5322 0.4874 0.2658  -0.1044 0.0631  57  THR A OG1 
425  C CG2 . THR A 57  ? 0.4357 0.4945 0.5425 0.1984  -0.1021 0.1423  57  THR A CG2 
426  N N   . SER A 58  ? 0.4335 0.2750 0.2790 0.1246  -0.0292 0.0129  58  SER A N   
427  C CA  . SER A 58  ? 0.5223 0.3275 0.2088 0.1003  -0.0118 0.0181  58  SER A CA  
428  C C   . SER A 58  ? 0.4534 0.2679 0.2357 0.1011  -0.0085 0.0273  58  SER A C   
429  O O   . SER A 58  ? 0.4650 0.2678 0.1772 0.0647  -0.0094 0.0171  58  SER A O   
430  C CB  . SER A 58  ? 0.6140 0.3848 0.1720 -0.0021 -0.0074 0.0237  58  SER A CB  
431  O OG  . SER A 58  ? 0.6179 0.4929 0.3790 -0.0253 0.0465  -0.0223 58  SER A OG  
432  N N   . TYR A 59  ? 0.4655 0.2448 0.2718 0.1096  0.0108  0.0448  59  TYR A N   
433  C CA  . TYR A 59  ? 0.3933 0.2147 0.2717 0.0868  -0.0161 0.0242  59  TYR A CA  
434  C C   . TYR A 59  ? 0.4340 0.2520 0.3031 0.0468  -0.0301 0.0310  59  TYR A C   
435  O O   . TYR A 59  ? 0.4719 0.2507 0.3133 0.0179  -0.0404 0.0233  59  TYR A O   
436  C CB  . TYR A 59  ? 0.4031 0.2947 0.2660 0.1017  -0.0154 0.0128  59  TYR A CB  
437  C CG  . TYR A 59  ? 0.3777 0.2965 0.2317 0.1054  -0.0108 0.0054  59  TYR A CG  
438  C CD1 . TYR A 59  ? 0.3925 0.3648 0.2903 0.1152  0.0176  0.0047  59  TYR A CD1 
439  C CD2 . TYR A 59  ? 0.3784 0.3011 0.2311 0.1140  -0.0143 0.0115  59  TYR A CD2 
440  C CE1 . TYR A 59  ? 0.3695 0.3332 0.2848 0.1030  -0.0620 0.0136  59  TYR A CE1 
441  C CE2 . TYR A 59  ? 0.3459 0.3149 0.2500 0.1049  -0.0175 -0.0242 59  TYR A CE2 
442  C CZ  . TYR A 59  ? 0.3289 0.3416 0.2568 0.1100  -0.0312 -0.0086 59  TYR A CZ  
443  O OH  . TYR A 59  ? 0.2630 0.3878 0.2125 0.0922  -0.0645 -0.0224 59  TYR A OH  
444  N N   . ALA A 60  ? 0.4112 0.2285 0.2989 0.0241  -0.0156 0.0612  60  ALA A N   
445  C CA  . ALA A 60  ? 0.4283 0.2714 0.2793 0.0063  -0.0289 0.0705  60  ALA A CA  
446  C C   . ALA A 60  ? 0.3711 0.3202 0.2993 0.0232  -0.0458 0.0503  60  ALA A C   
447  O O   . ALA A 60  ? 0.3487 0.3006 0.3047 0.0379  -0.0650 0.0652  60  ALA A O   
448  C CB  . ALA A 60  ? 0.4483 0.2733 0.2951 0.0001  -0.0054 0.0800  60  ALA A CB  
449  N N   . ASP A 61  ? 0.4197 0.3079 0.2947 0.0315  -0.0442 0.0468  61  ASP A N   
450  C CA  . ASP A 61  ? 0.4689 0.3716 0.3454 0.0411  -0.0864 0.0788  61  ASP A CA  
451  C C   . ASP A 61  ? 0.4347 0.3661 0.3345 0.0545  -0.0436 0.0726  61  ASP A C   
452  O O   . ASP A 61  ? 0.4565 0.3366 0.3267 0.1008  -0.0749 0.0606  61  ASP A O   
453  C CB  . ASP A 61  ? 0.4865 0.3999 0.4117 0.0279  -0.0860 0.0996  61  ASP A CB  
454  C CG  . ASP A 61  ? 0.5787 0.4385 0.4494 -0.0051 -0.0580 0.0614  61  ASP A CG  
455  O OD1 . ASP A 61  ? 0.5988 0.5178 0.5052 0.1032  -0.0301 -0.0087 61  ASP A OD1 
456  O OD2 . ASP A 61  ? 0.6918 0.4444 0.6657 -0.0650 -0.0674 0.0726  61  ASP A OD2 
457  N N   . SER A 62  ? 0.4092 0.3327 0.3288 0.0152  0.0231  0.0941  62  SER A N   
458  C CA  . SER A 62  ? 0.4292 0.3742 0.3989 0.0159  0.0286  0.0429  62  SER A CA  
459  C C   . SER A 62  ? 0.4167 0.3641 0.3087 0.0103  0.0025  0.0396  62  SER A C   
460  O O   . SER A 62  ? 0.4637 0.3355 0.2740 0.0025  0.0147  0.0693  62  SER A O   
461  C CB  . SER A 62  ? 0.4248 0.4844 0.4430 0.0410  0.0714  -0.0010 62  SER A CB  
462  O OG  . SER A 62  ? 0.5143 0.5264 0.5807 0.0517  0.0067  0.0950  62  SER A OG  
463  N N   . VAL A 63  ? 0.4126 0.2663 0.2822 0.0604  -0.0127 0.0592  63  VAL A N   
464  C CA  . VAL A 63  ? 0.3680 0.2861 0.2493 0.0584  -0.0367 0.0352  63  VAL A CA  
465  C C   . VAL A 63  ? 0.3563 0.3147 0.2806 0.0417  -0.0474 0.0336  63  VAL A C   
466  O O   . VAL A 63  ? 0.3252 0.3433 0.2399 0.0421  -0.0411 0.0282  63  VAL A O   
467  C CB  . VAL A 63  ? 0.3502 0.2810 0.2404 0.0457  -0.0204 0.0422  63  VAL A CB  
468  C CG1 . VAL A 63  ? 0.3362 0.3058 0.1879 0.0282  -0.0062 0.0599  63  VAL A CG1 
469  C CG2 . VAL A 63  ? 0.3366 0.2778 0.2399 0.0437  -0.0080 0.0582  63  VAL A CG2 
470  N N   . LYS A 64  ? 0.3772 0.3261 0.3569 0.0667  -0.0455 0.0150  64  LYS A N   
471  C CA  . LYS A 64  ? 0.4178 0.3952 0.4035 0.0933  -0.0036 0.0091  64  LYS A CA  
472  C C   . LYS A 64  ? 0.3616 0.3958 0.4150 0.0701  0.0145  0.0484  64  LYS A C   
473  O O   . LYS A 64  ? 0.3748 0.4306 0.3913 0.1098  -0.0131 0.0834  64  LYS A O   
474  C CB  . LYS A 64  ? 0.5254 0.3971 0.5417 0.0760  -0.0198 0.0197  64  LYS A CB  
475  C CG  . LYS A 64  ? 0.6751 0.5193 0.5630 0.0892  -0.0846 -0.0129 64  LYS A CG  
476  C CD  . LYS A 64  ? 0.7702 0.5429 0.7346 0.0651  -0.0948 -0.0709 64  LYS A CD  
477  C CE  . LYS A 64  ? 0.7185 0.6639 0.7243 0.0815  -0.1363 -0.0940 64  LYS A CE  
478  N NZ  . LYS A 64  ? 0.7807 0.6632 0.6807 0.0771  -0.1357 -0.0927 64  LYS A NZ  
479  N N   . GLY A 65  ? 0.3958 0.3216 0.3989 0.0492  0.0410  0.0445  65  GLY A N   
480  C CA  . GLY A 65  ? 0.4489 0.4061 0.4633 0.0847  -0.0404 0.0244  65  GLY A CA  
481  C C   . GLY A 65  ? 0.3694 0.3980 0.5036 0.1023  -0.0997 0.0242  65  GLY A C   
482  O O   . GLY A 65  ? 0.3474 0.4791 0.5693 0.1116  -0.1298 0.0054  65  GLY A O   
483  N N   . ARG A 66  ? 0.3215 0.4073 0.3325 0.0707  -0.0540 0.0356  66  ARG A N   
484  C CA  . ARG A 66  ? 0.3182 0.4141 0.2555 0.0765  -0.0650 0.0291  66  ARG A CA  
485  C C   . ARG A 66  ? 0.3142 0.3869 0.2639 0.0395  -0.0456 0.0179  66  ARG A C   
486  O O   . ARG A 66  ? 0.2654 0.3769 0.2266 0.0521  -0.0340 0.0374  66  ARG A O   
487  C CB  . ARG A 66  ? 0.3431 0.4016 0.2795 0.0713  -0.0339 -0.0022 66  ARG A CB  
488  C CG  . ARG A 66  ? 0.3230 0.4539 0.2656 0.0409  -0.0216 0.0017  66  ARG A CG  
489  C CD  . ARG A 66  ? 0.3047 0.4199 0.2158 0.0212  -0.0453 -0.0195 66  ARG A CD  
490  N NE  . ARG A 66  ? 0.2699 0.3748 0.2508 0.0447  -0.0236 0.0388  66  ARG A NE  
491  C CZ  . ARG A 66  ? 0.2694 0.3473 0.2311 0.0307  -0.0213 0.0307  66  ARG A CZ  
492  N NH1 . ARG A 66  ? 0.2542 0.3656 0.2548 0.0387  -0.0256 0.0378  66  ARG A NH1 
493  N NH2 . ARG A 66  ? 0.2680 0.3459 0.2130 0.0310  -0.0267 0.0375  66  ARG A NH2 
494  N N   . PHE A 67  ? 0.3258 0.3924 0.2432 0.0461  -0.0402 0.0258  67  PHE A N   
495  C CA  . PHE A 67  ? 0.2852 0.3734 0.2065 0.0495  0.0054  0.0059  67  PHE A CA  
496  C C   . PHE A 67  ? 0.2660 0.3702 0.2137 0.0582  -0.0048 -0.0098 67  PHE A C   
497  O O   . PHE A 67  ? 0.3331 0.3865 0.1879 0.0818  -0.0190 -0.0075 67  PHE A O   
498  C CB  . PHE A 67  ? 0.2768 0.3604 0.1952 0.0242  0.0135  0.0272  67  PHE A CB  
499  C CG  . PHE A 67  ? 0.2586 0.3509 0.1982 0.0265  -0.0022 0.0173  67  PHE A CG  
500  C CD1 . PHE A 67  ? 0.2837 0.3963 0.1931 0.0405  0.0040  0.0197  67  PHE A CD1 
501  C CD2 . PHE A 67  ? 0.2556 0.3423 0.1681 0.0051  -0.0075 0.0221  67  PHE A CD2 
502  C CE1 . PHE A 67  ? 0.2467 0.4116 0.1728 0.0524  -0.0089 0.0420  67  PHE A CE1 
503  C CE2 . PHE A 67  ? 0.1851 0.3395 0.2236 0.0150  -0.0373 0.0077  67  PHE A CE2 
504  C CZ  . PHE A 67  ? 0.2266 0.4229 0.1560 0.0272  0.0182  0.0586  67  PHE A CZ  
505  N N   . THR A 68  ? 0.2087 0.3974 0.1904 0.0591  0.0029  -0.0264 68  THR A N   
506  C CA  . THR A 68  ? 0.2298 0.3763 0.2128 0.0713  0.0212  -0.0319 68  THR A CA  
507  C C   . THR A 68  ? 0.1996 0.3016 0.2449 0.0382  0.0064  -0.0303 68  THR A C   
508  O O   . THR A 68  ? 0.2076 0.2911 0.1733 -0.0008 -0.0029 -0.0489 68  THR A O   
509  C CB  . THR A 68  ? 0.2399 0.4126 0.2691 0.0484  0.0093  -0.0217 68  THR A CB  
510  O OG1 . THR A 68  ? 0.2732 0.4601 0.2878 0.0849  -0.0255 -0.0243 68  THR A OG1 
511  C CG2 . THR A 68  ? 0.2382 0.4827 0.3091 0.0212  0.0284  -0.0549 68  THR A CG2 
512  N N   . ILE A 69  ? 0.1642 0.3199 0.2512 0.0160  0.0042  -0.0280 69  ILE A N   
513  C CA  . ILE A 69  ? 0.1678 0.3297 0.2309 -0.0004 0.0289  -0.0227 69  ILE A CA  
514  C C   . ILE A 69  ? 0.1904 0.3091 0.1967 -0.0230 0.0256  -0.0400 69  ILE A C   
515  O O   . ILE A 69  ? 0.2061 0.3722 0.2520 0.0122  0.0373  -0.0137 69  ILE A O   
516  C CB  . ILE A 69  ? 0.1687 0.2967 0.2283 -0.0058 0.0370  -0.0167 69  ILE A CB  
517  C CG1 . ILE A 69  ? 0.1357 0.2547 0.2246 -0.0001 0.0604  -0.0195 69  ILE A CG1 
518  C CG2 . ILE A 69  ? 0.2163 0.3003 0.2394 0.0309  0.0155  -0.0016 69  ILE A CG2 
519  C CD1 . ILE A 69  ? 0.1474 0.2831 0.2370 0.0052  0.0322  -0.0190 69  ILE A CD1 
520  N N   . SER A 70  ? 0.1554 0.3408 0.2017 -0.0324 0.0341  -0.0128 70  SER A N   
521  C CA  . SER A 70  ? 0.1562 0.3471 0.2114 0.0010  0.0496  -0.0098 70  SER A CA  
522  C C   . SER A 70  ? 0.1495 0.3851 0.1799 0.0072  0.0388  -0.0234 70  SER A C   
523  O O   . SER A 70  ? 0.1578 0.3941 0.2156 0.0314  0.0158  -0.0119 70  SER A O   
524  C CB  . SER A 70  ? 0.1701 0.3550 0.2269 0.0064  0.0174  0.0006  70  SER A CB  
525  O OG  . SER A 70  ? 0.1956 0.3501 0.2096 0.0098  -0.0029 0.0062  70  SER A OG  
526  N N   . ARG A 71  ? 0.1177 0.4291 0.1949 0.0199  0.0435  -0.0283 71  ARG A N   
527  C CA  . ARG A 71  ? 0.1978 0.4460 0.2372 0.0111  0.0404  0.0077  71  ARG A CA  
528  C C   . ARG A 71  ? 0.2083 0.4981 0.2126 0.0256  0.0514  0.0514  71  ARG A C   
529  O O   . ARG A 71  ? 0.2151 0.5544 0.1557 0.0467  0.0557  0.0570  71  ARG A O   
530  C CB  . ARG A 71  ? 0.2238 0.5243 0.2872 -0.0002 -0.0196 -0.0095 71  ARG A CB  
531  C CG  . ARG A 71  ? 0.3206 0.5618 0.3447 0.0312  0.0015  -0.0330 71  ARG A CG  
532  C CD  . ARG A 71  ? 0.4869 0.6334 0.3856 -0.0019 -0.0083 -0.0819 71  ARG A CD  
533  N NE  . ARG A 71  ? 0.5724 0.6869 0.5059 0.0475  0.0116  -0.0709 71  ARG A NE  
534  C CZ  . ARG A 71  ? 0.6222 0.8106 0.5039 0.0379  -0.0076 -0.1177 71  ARG A CZ  
535  N NH1 . ARG A 71  ? 0.7070 0.8881 0.5449 0.0433  -0.0918 -0.0866 71  ARG A NH1 
536  N NH2 . ARG A 71  ? 0.6283 0.7686 0.6450 0.0533  -0.0672 -0.1004 71  ARG A NH2 
537  N N   . ASP A 72  ? 0.1889 0.4920 0.2196 -0.0065 0.0392  0.0629  72  ASP A N   
538  C CA  . ASP A 72  ? 0.1471 0.5542 0.2006 -0.0158 0.0267  0.0547  72  ASP A CA  
539  C C   . ASP A 72  ? 0.2198 0.5103 0.2161 -0.0055 0.0013  0.0190  72  ASP A C   
540  O O   . ASP A 72  ? 0.1954 0.6185 0.1902 0.0167  0.0188  0.0577  72  ASP A O   
541  C CB  . ASP A 72  ? 0.1618 0.5764 0.2248 -0.0215 0.0066  0.0074  72  ASP A CB  
542  C CG  . ASP A 72  ? 0.2365 0.6462 0.2705 -0.0620 0.0637  -0.0130 72  ASP A CG  
543  O OD1 . ASP A 72  ? 0.2113 0.5916 0.2536 -0.0094 0.0560  0.0300  72  ASP A OD1 
544  O OD2 . ASP A 72  ? 0.3484 0.8133 0.4412 -0.2521 0.1831  -0.0950 72  ASP A OD2 
545  N N   . ASN A 73  ? 0.1975 0.4819 0.2659 -0.0161 0.0090  0.0295  73  ASN A N   
546  C CA  . ASN A 73  ? 0.2571 0.5212 0.2860 -0.0327 -0.0051 -0.0043 73  ASN A CA  
547  C C   . ASN A 73  ? 0.2178 0.5857 0.2491 -0.0465 -0.0172 0.0309  73  ASN A C   
548  O O   . ASN A 73  ? 0.2063 0.7087 0.2301 -0.0540 -0.0104 0.0275  73  ASN A O   
549  C CB  . ASN A 73  ? 0.2459 0.5663 0.3663 -0.0204 0.0168  -0.0305 73  ASN A CB  
550  C CG  . ASN A 73  ? 0.4425 0.5374 0.4927 -0.0057 0.0216  -0.0554 73  ASN A CG  
551  O OD1 . ASN A 73  ? 0.5515 0.6754 0.5374 -0.0169 0.1010  -0.0684 73  ASN A OD1 
552  N ND2 . ASN A 73  ? 0.4671 0.6794 0.4925 0.0965  -0.1052 -0.0661 73  ASN A ND2 
553  N N   . ALA A 74  ? 0.2571 0.5115 0.2363 -0.0505 -0.0464 0.0313  74  ALA A N   
554  C CA  . ALA A 74  ? 0.2647 0.5458 0.2840 -0.0361 -0.0496 0.0735  74  ALA A CA  
555  C C   . ALA A 74  ? 0.3241 0.5489 0.2876 -0.0062 0.0082  0.1014  74  ALA A C   
556  O O   . ALA A 74  ? 0.3067 0.6094 0.3161 0.0024  0.0844  0.1793  74  ALA A O   
557  C CB  . ALA A 74  ? 0.2703 0.5377 0.3044 -0.0726 -0.0044 0.0785  74  ALA A CB  
558  N N   . LYS A 75  ? 0.2716 0.5006 0.3215 -0.0167 0.0501  0.1178  75  LYS A N   
559  C CA  . LYS A 75  ? 0.3335 0.4670 0.3788 -0.0181 0.0502  0.1000  75  LYS A CA  
560  C C   . LYS A 75  ? 0.3204 0.3604 0.3000 0.0146  0.0429  0.0901  75  LYS A C   
561  O O   . LYS A 75  ? 0.2463 0.4525 0.4303 0.0143  0.0497  0.0772  75  LYS A O   
562  C CB  . LYS A 75  ? 0.4354 0.5178 0.5284 -0.0291 0.0568  -0.0378 75  LYS A CB  
563  C CG  . LYS A 75  ? 0.4055 0.6655 0.6234 -0.0750 0.0809  -0.0104 75  LYS A CG  
564  C CD  . LYS A 75  ? 0.5606 0.7223 0.7665 -0.0760 0.0209  -0.1438 75  LYS A CD  
565  C CE  . LYS A 75  ? 0.6502 0.7355 0.8885 -0.1109 0.0184  -0.1452 75  LYS A CE  
566  N NZ  . LYS A 75  ? 0.7492 0.8011 0.9182 -0.0632 0.0165  -0.2097 75  LYS A NZ  
567  N N   . ASN A 76  ? 0.2210 0.4207 0.1896 -0.0071 0.0076  0.0108  76  ASN A N   
568  C CA  . ASN A 76  ? 0.2277 0.4201 0.1904 -0.0086 0.0355  0.0300  76  ASN A CA  
569  C C   . ASN A 76  ? 0.2097 0.4182 0.1614 0.0115  -0.0297 -0.0111 76  ASN A C   
570  O O   . ASN A 76  ? 0.1971 0.4215 0.1805 -0.0074 -0.0253 0.0145  76  ASN A O   
571  C CB  . ASN A 76  ? 0.2093 0.5167 0.2342 -0.0163 -0.0027 -0.0029 76  ASN A CB  
572  C CG  . ASN A 76  ? 0.2360 0.5081 0.2615 -0.0367 0.0353  -0.0125 76  ASN A CG  
573  O OD1 . ASN A 76  ? 0.2652 0.5481 0.3131 -0.0262 0.0390  -0.0790 76  ASN A OD1 
574  N ND2 . ASN A 76  ? 0.2967 0.5389 0.3638 -0.0689 0.0234  0.0462  76  ASN A ND2 
575  N N   . THR A 77  ? 0.1843 0.4042 0.1682 0.0145  -0.0236 0.0018  77  THR A N   
576  C CA  . THR A 77  ? 0.1379 0.4050 0.2143 0.0099  0.0303  -0.0147 77  THR A CA  
577  C C   . THR A 77  ? 0.1524 0.4136 0.1687 0.0308  0.0378  -0.0293 77  THR A C   
578  O O   . THR A 77  ? 0.1256 0.4243 0.1869 0.0246  0.0322  -0.0033 77  THR A O   
579  C CB  . THR A 77  ? 0.2533 0.3898 0.2505 0.0160  -0.0137 -0.0286 77  THR A CB  
580  O OG1 . THR A 77  ? 0.3058 0.4279 0.2463 -0.0200 -0.0169 0.0015  77  THR A OG1 
581  C CG2 . THR A 77  ? 0.2453 0.4278 0.2624 0.0049  0.0194  0.0065  77  THR A CG2 
582  N N   . LEU A 78  ? 0.1275 0.3401 0.1910 -0.0294 0.0189  -0.0350 78  LEU A N   
583  C CA  . LEU A 78  ? 0.1499 0.3279 0.1662 -0.0090 0.0036  -0.0499 78  LEU A CA  
584  C C   . LEU A 78  ? 0.1395 0.2718 0.1638 -0.0119 -0.0025 -0.0377 78  LEU A C   
585  O O   . LEU A 78  ? 0.1572 0.2587 0.1709 -0.0218 0.0134  -0.0237 78  LEU A O   
586  C CB  . LEU A 78  ? 0.1548 0.3359 0.1906 -0.0094 -0.0222 -0.0433 78  LEU A CB  
587  C CG  . LEU A 78  ? 0.1788 0.3267 0.1967 -0.0291 -0.0179 -0.0493 78  LEU A CG  
588  C CD1 . LEU A 78  ? 0.2239 0.3215 0.2478 -0.0255 0.0028  -0.0418 78  LEU A CD1 
589  C CD2 . LEU A 78  ? 0.1839 0.3558 0.2314 -0.0454 -0.0104 -0.0087 78  LEU A CD2 
590  N N   . TYR A 79  ? 0.1534 0.2972 0.1474 -0.0143 0.0057  -0.0185 79  TYR A N   
591  C CA  . TYR A 79  ? 0.1428 0.2912 0.1563 -0.0097 -0.0091 -0.0379 79  TYR A CA  
592  C C   . TYR A 79  ? 0.1006 0.2793 0.1767 -0.0181 0.0012  -0.0516 79  TYR A C   
593  O O   . TYR A 79  ? 0.1627 0.2800 0.1416 0.0023  0.0044  -0.0311 79  TYR A O   
594  C CB  . TYR A 79  ? 0.1302 0.3202 0.1930 -0.0034 -0.0028 -0.0040 79  TYR A CB  
595  C CG  . TYR A 79  ? 0.1362 0.3149 0.2090 -0.0141 -0.0315 0.0132  79  TYR A CG  
596  C CD1 . TYR A 79  ? 0.1584 0.3056 0.2419 -0.0176 -0.0159 0.0345  79  TYR A CD1 
597  C CD2 . TYR A 79  ? 0.1694 0.3460 0.2226 0.0080  -0.0191 0.0248  79  TYR A CD2 
598  C CE1 . TYR A 79  ? 0.2216 0.3169 0.2433 -0.0479 -0.0252 0.0237  79  TYR A CE1 
599  C CE2 . TYR A 79  ? 0.2022 0.3405 0.2730 -0.0174 0.0016  0.0299  79  TYR A CE2 
600  C CZ  . TYR A 79  ? 0.1972 0.3309 0.2444 -0.0310 -0.0338 0.0326  79  TYR A CZ  
601  O OH  . TYR A 79  ? 0.2881 0.3776 0.3229 -0.0554 -0.0181 0.0826  79  TYR A OH  
602  N N   . LEU A 80  ? 0.1647 0.3165 0.1499 -0.0239 0.0090  -0.0207 80  LEU A N   
603  C CA  . LEU A 80  ? 0.1681 0.2876 0.1843 -0.0131 -0.0022 -0.0107 80  LEU A CA  
604  C C   . LEU A 80  ? 0.1822 0.2899 0.1779 -0.0076 -0.0033 -0.0156 80  LEU A C   
605  O O   . LEU A 80  ? 0.2296 0.2678 0.1842 -0.0151 -0.0320 -0.0220 80  LEU A O   
606  C CB  . LEU A 80  ? 0.1698 0.2979 0.1857 -0.0294 -0.0090 -0.0003 80  LEU A CB  
607  C CG  . LEU A 80  ? 0.1728 0.3073 0.1768 -0.0295 -0.0231 0.0157  80  LEU A CG  
608  C CD1 . LEU A 80  ? 0.1925 0.3017 0.2082 -0.0297 -0.0146 0.0269  80  LEU A CD1 
609  C CD2 . LEU A 80  ? 0.1761 0.3149 0.1819 -0.0066 -0.0100 0.0307  80  LEU A CD2 
610  N N   . GLN A 81  ? 0.1604 0.2853 0.1912 -0.0080 0.0039  -0.0400 81  GLN A N   
611  C CA  . GLN A 81  ? 0.1845 0.3111 0.1911 -0.0090 -0.0129 -0.0351 81  GLN A CA  
612  C C   . GLN A 81  ? 0.1548 0.2698 0.1863 0.0021  -0.0303 -0.0297 81  GLN A C   
613  O O   . GLN A 81  ? 0.1843 0.2748 0.1789 -0.0100 0.0156  -0.0319 81  GLN A O   
614  C CB  . GLN A 81  ? 0.1872 0.3377 0.1884 0.0011  0.0048  -0.0553 81  GLN A CB  
615  C CG  . GLN A 81  ? 0.1890 0.3758 0.1830 0.0078  0.0032  -0.0485 81  GLN A CG  
616  C CD  . GLN A 81  ? 0.2595 0.3910 0.1902 -0.0162 -0.0261 -0.0665 81  GLN A CD  
617  O OE1 . GLN A 81  ? 0.2841 0.4511 0.2693 -0.0476 0.0484  -0.0712 81  GLN A OE1 
618  N NE2 . GLN A 81  ? 0.1706 0.4097 0.2384 -0.0044 -0.0105 -0.0933 81  GLN A NE2 
619  N N   . MET A 82  ? 0.1376 0.3127 0.1990 0.0002  -0.0208 -0.0370 82  MET A N   
620  C CA  . MET A 82  ? 0.1470 0.3241 0.2055 -0.0063 -0.0160 -0.0236 82  MET A CA  
621  C C   . MET A 82  ? 0.1926 0.3228 0.1834 0.0106  -0.0063 -0.0402 82  MET A C   
622  O O   . MET A 82  ? 0.2318 0.3689 0.1612 -0.0273 -0.0549 -0.0641 82  MET A O   
623  C CB  . MET A 82  ? 0.1683 0.3781 0.1921 0.0237  0.0120  -0.0226 82  MET A CB  
624  C CG  . MET A 82  ? 0.2257 0.4418 0.2196 -0.0110 -0.0199 -0.0465 82  MET A CG  
625  S SD  . MET A 82  ? 0.2824 0.6190 0.4013 0.0926  0.0026  0.0010  82  MET A SD  
626  C CE  . MET A 82  ? 0.2244 0.5914 0.3694 0.0219  -0.0125 -0.0515 82  MET A CE  
627  N N   . ASN A 83  ? 0.1683 0.3552 0.1784 0.0279  -0.0034 -0.0264 83  ASN A N   
628  C CA  . ASN A 83  ? 0.1979 0.3795 0.1966 0.0016  -0.0228 -0.0254 83  ASN A CA  
629  C C   . ASN A 83  ? 0.1917 0.3599 0.2146 0.0212  0.0032  -0.0234 83  ASN A C   
630  O O   . ASN A 83  ? 0.1712 0.4146 0.2136 0.0090  -0.0032 0.0057  83  ASN A O   
631  C CB  . ASN A 83  ? 0.1980 0.3975 0.2189 0.0157  -0.0242 -0.0142 83  ASN A CB  
632  C CG  . ASN A 83  ? 0.1826 0.3956 0.2569 0.0150  0.0108  -0.0497 83  ASN A CG  
633  O OD1 . ASN A 83  ? 0.1854 0.4122 0.3073 -0.0144 0.0277  -0.0671 83  ASN A OD1 
634  N ND2 . ASN A 83  ? 0.1243 0.4573 0.2210 -0.0099 -0.0308 -0.0967 83  ASN A ND2 
635  N N   . SER A 84  ? 0.1475 0.3649 0.2295 0.0042  -0.0092 -0.0185 84  SER A N   
636  C CA  . SER A 84  ? 0.2034 0.4133 0.2193 0.0149  -0.0125 0.0159  84  SER A CA  
637  C C   . SER A 84  ? 0.1956 0.3687 0.1599 0.0366  0.0103  -0.0127 84  SER A C   
638  O O   . SER A 84  ? 0.1764 0.3915 0.2214 0.0534  0.0093  0.0159  84  SER A O   
639  C CB  . SER A 84  ? 0.2031 0.4178 0.2853 0.0244  0.0064  -0.0118 84  SER A CB  
640  O OG  . SER A 84  ? 0.1995 0.5144 0.3469 0.0227  0.0132  0.0419  84  SER A OG  
641  N N   . LEU A 85  ? 0.1718 0.3601 0.1828 0.0018  0.0036  -0.0074 85  LEU A N   
642  C CA  . LEU A 85  ? 0.1689 0.3672 0.1608 0.0168  0.0185  0.0080  85  LEU A CA  
643  C C   . LEU A 85  ? 0.1821 0.3643 0.1740 -0.0029 0.0234  0.0161  85  LEU A C   
644  O O   . LEU A 85  ? 0.1616 0.4378 0.1746 0.0153  0.0243  0.0045  85  LEU A O   
645  C CB  . LEU A 85  ? 0.1542 0.3425 0.1737 0.0106  0.0299  -0.0002 85  LEU A CB  
646  C CG  . LEU A 85  ? 0.1583 0.3486 0.1661 -0.0062 0.0066  -0.0095 85  LEU A CG  
647  C CD1 . LEU A 85  ? 0.2028 0.3515 0.2129 -0.0076 0.0222  0.0015  85  LEU A CD1 
648  C CD2 . LEU A 85  ? 0.1645 0.3753 0.2073 -0.0533 0.0129  0.0027  85  LEU A CD2 
649  N N   . ARG A 86  ? 0.1698 0.3670 0.1685 0.0111  0.0085  0.0300  86  ARG A N   
650  C CA  . ARG A 86  ? 0.1947 0.3828 0.1756 0.0120  0.0145  0.0565  86  ARG A CA  
651  C C   . ARG A 86  ? 0.1973 0.3884 0.1593 0.0257  0.0264  0.0269  86  ARG A C   
652  O O   . ARG A 86  ? 0.1793 0.3131 0.1511 -0.0135 0.0231  0.0193  86  ARG A O   
653  C CB  . ARG A 86  ? 0.2466 0.3844 0.2180 0.0098  0.0223  0.0424  86  ARG A CB  
654  C CG  . ARG A 86  ? 0.2713 0.4192 0.2636 0.0351  0.0293  0.0337  86  ARG A CG  
655  C CD  . ARG A 86  ? 0.3369 0.4275 0.3284 0.0519  0.0098  0.0080  86  ARG A CD  
656  N NE  . ARG A 86  ? 0.3965 0.4533 0.3842 0.0898  0.0010  0.0631  86  ARG A NE  
657  C CZ  . ARG A 86  ? 0.3518 0.4736 0.5046 0.0619  -0.0185 0.0243  86  ARG A CZ  
658  N NH1 . ARG A 86  ? 0.3739 0.5066 0.6174 0.0287  -0.0656 0.0798  86  ARG A NH1 
659  N NH2 . ARG A 86  ? 0.3640 0.5042 0.5828 0.0744  -0.0409 0.0469  86  ARG A NH2 
660  N N   . PRO A 87  ? 0.1652 0.4106 0.1882 0.0010  0.0454  0.0478  87  PRO A N   
661  C CA  . PRO A 87  ? 0.1880 0.4091 0.1839 0.0249  0.0250  0.0689  87  PRO A CA  
662  C C   . PRO A 87  ? 0.2076 0.3793 0.1731 0.0284  0.0369  0.0659  87  PRO A C   
663  O O   . PRO A 87  ? 0.1931 0.3831 0.2027 0.0465  0.0127  0.0393  87  PRO A O   
664  C CB  . PRO A 87  ? 0.2041 0.4310 0.1906 0.0348  0.0418  0.0554  87  PRO A CB  
665  C CG  . PRO A 87  ? 0.2091 0.4632 0.1834 0.0109  0.0482  0.0507  87  PRO A CG  
666  C CD  . PRO A 87  ? 0.2090 0.4451 0.2108 0.0432  0.0222  0.0507  87  PRO A CD  
667  N N   . GLU A 88  ? 0.2041 0.3805 0.1952 0.0017  0.0428  0.0468  88  GLU A N   
668  C CA  . GLU A 88  ? 0.2560 0.4157 0.2024 -0.0022 0.0006  0.0594  88  GLU A CA  
669  C C   . GLU A 88  ? 0.2368 0.3331 0.1972 -0.0263 0.0067  0.0296  88  GLU A C   
670  O O   . GLU A 88  ? 0.2710 0.3771 0.1792 -0.0535 0.0154  0.0077  88  GLU A O   
671  C CB  . GLU A 88  ? 0.2893 0.4120 0.3028 -0.0347 -0.0228 0.0707  88  GLU A CB  
672  C CG  . GLU A 88  ? 0.3542 0.4312 0.4373 0.0427  -0.0061 0.0573  88  GLU A CG  
673  C CD  . GLU A 88  ? 0.4560 0.5344 0.5184 0.0965  -0.0729 0.1588  88  GLU A CD  
674  O OE1 . GLU A 88  ? 0.4394 0.5959 0.7018 0.1694  0.0306  0.1036  88  GLU A OE1 
675  O OE2 . GLU A 88  ? 0.3486 0.4981 0.6216 0.0195  -0.0706 0.1199  88  GLU A OE2 
676  N N   . ASP A 89  ? 0.1964 0.3373 0.1847 0.0110  -0.0010 0.0587  89  ASP A N   
677  C CA  . ASP A 89  ? 0.1922 0.3076 0.1709 0.0181  0.0040  0.0351  89  ASP A CA  
678  C C   . ASP A 89  ? 0.1701 0.3062 0.1468 0.0212  0.0066  0.0222  89  ASP A C   
679  O O   . ASP A 89  ? 0.1693 0.3550 0.1435 -0.0064 0.0122  0.0248  89  ASP A O   
680  C CB  . ASP A 89  ? 0.1858 0.3290 0.1369 0.0221  -0.0115 0.0385  89  ASP A CB  
681  C CG  . ASP A 89  ? 0.2070 0.2923 0.1877 0.0061  0.0011  0.0470  89  ASP A CG  
682  O OD1 . ASP A 89  ? 0.1839 0.3183 0.2220 0.0029  0.0057  0.0265  89  ASP A OD1 
683  O OD2 . ASP A 89  ? 0.2180 0.3892 0.2199 0.0151  -0.0190 0.0108  89  ASP A OD2 
684  N N   . THR A 90  ? 0.2140 0.2876 0.1498 0.0216  0.0107  0.0079  90  THR A N   
685  C CA  . THR A 90  ? 0.1855 0.2935 0.1369 0.0291  0.0187  0.0072  90  THR A CA  
686  C C   . THR A 90  ? 0.1910 0.2755 0.1761 0.0162  0.0001  0.0097  90  THR A C   
687  O O   . THR A 90  ? 0.2216 0.2982 0.1599 -0.0051 -0.0168 0.0317  90  THR A O   
688  C CB  . THR A 90  ? 0.2174 0.3362 0.1513 0.0308  0.0294  -0.0156 90  THR A CB  
689  O OG1 . THR A 90  ? 0.2174 0.3195 0.1323 0.0138  0.0363  -0.0081 90  THR A OG1 
690  C CG2 . THR A 90  ? 0.2122 0.3589 0.1652 0.0453  0.0107  -0.0048 90  THR A CG2 
691  N N   . ALA A 91  ? 0.1734 0.2677 0.1767 0.0154  0.0051  0.0042  91  ALA A N   
692  C CA  . ALA A 91  ? 0.1750 0.2866 0.1746 0.0135  -0.0007 0.0107  91  ALA A CA  
693  C C   . ALA A 91  ? 0.1657 0.2945 0.1527 0.0234  -0.0096 0.0037  91  ALA A C   
694  O O   . ALA A 91  ? 0.1857 0.2794 0.1092 0.0238  -0.0062 0.0115  91  ALA A O   
695  C CB  . ALA A 91  ? 0.2449 0.2647 0.2027 0.0160  -0.0041 0.0352  91  ALA A CB  
696  N N   . VAL A 92  ? 0.1422 0.2794 0.1499 0.0278  -0.0006 0.0261  92  VAL A N   
697  C CA  . VAL A 92  ? 0.1587 0.2728 0.1275 0.0302  0.0153  0.0046  92  VAL A CA  
698  C C   . VAL A 92  ? 0.1571 0.2019 0.1630 0.0264  -0.0054 0.0040  92  VAL A C   
699  O O   . VAL A 92  ? 0.1514 0.2127 0.1337 0.0027  0.0255  0.0142  92  VAL A O   
700  C CB  . VAL A 92  ? 0.1847 0.2966 0.1826 0.0621  -0.0019 0.0056  92  VAL A CB  
701  C CG1 . VAL A 92  ? 0.1810 0.3015 0.1714 0.0763  0.0070  -0.0004 92  VAL A CG1 
702  C CG2 . VAL A 92  ? 0.1812 0.3221 0.1713 0.0746  0.0043  0.0103  92  VAL A CG2 
703  N N   . TYR A 93  ? 0.1684 0.2292 0.1641 0.0215  0.0131  -0.0063 93  TYR A N   
704  C CA  . TYR A 93  ? 0.1544 0.2197 0.1434 0.0217  0.0063  0.0072  93  TYR A CA  
705  C C   . TYR A 93  ? 0.1507 0.2129 0.1500 0.0135  -0.0035 0.0150  93  TYR A C   
706  O O   . TYR A 93  ? 0.1753 0.2118 0.1150 0.0234  0.0070  -0.0054 93  TYR A O   
707  C CB  . TYR A 93  ? 0.1543 0.2197 0.1594 0.0124  0.0008  0.0108  93  TYR A CB  
708  C CG  . TYR A 93  ? 0.1661 0.2369 0.1431 0.0011  -0.0028 0.0102  93  TYR A CG  
709  C CD1 . TYR A 93  ? 0.1432 0.2737 0.1635 0.0065  0.0054  0.0001  93  TYR A CD1 
710  C CD2 . TYR A 93  ? 0.1787 0.2438 0.1375 0.0103  0.0067  0.0087  93  TYR A CD2 
711  C CE1 . TYR A 93  ? 0.2065 0.2544 0.1548 0.0035  -0.0005 -0.0048 93  TYR A CE1 
712  C CE2 . TYR A 93  ? 0.1900 0.2495 0.1580 0.0248  0.0024  0.0201  93  TYR A CE2 
713  C CZ  . TYR A 93  ? 0.1983 0.2671 0.1523 0.0154  -0.0080 0.0100  93  TYR A CZ  
714  O OH  . TYR A 93  ? 0.2190 0.2526 0.1642 0.0126  0.0058  0.0251  93  TYR A OH  
715  N N   . TYR A 94  ? 0.1664 0.2194 0.1382 -0.0119 -0.0025 0.0277  94  TYR A N   
716  C CA  . TYR A 94  ? 0.1808 0.2130 0.1321 -0.0082 -0.0057 0.0041  94  TYR A CA  
717  C C   . TYR A 94  ? 0.1865 0.1804 0.1486 -0.0130 0.0113  0.0205  94  TYR A C   
718  O O   . TYR A 94  ? 0.2475 0.1957 0.1797 0.0306  0.0380  0.0135  94  TYR A O   
719  C CB  . TYR A 94  ? 0.1837 0.2620 0.1461 -0.0098 -0.0164 -0.0067 94  TYR A CB  
720  C CG  . TYR A 94  ? 0.1897 0.3089 0.1817 0.0038  -0.0052 0.0020  94  TYR A CG  
721  C CD1 . TYR A 94  ? 0.1893 0.3187 0.1579 0.0146  -0.0371 0.0070  94  TYR A CD1 
722  C CD2 . TYR A 94  ? 0.2041 0.3191 0.1268 0.0236  0.0146  0.0143  94  TYR A CD2 
723  C CE1 . TYR A 94  ? 0.2311 0.3391 0.1882 0.0462  -0.0061 -0.0042 94  TYR A CE1 
724  C CE2 . TYR A 94  ? 0.2081 0.3767 0.1905 0.0354  0.0239  -0.0122 94  TYR A CE2 
725  C CZ  . TYR A 94  ? 0.2319 0.3196 0.2042 0.0441  0.0047  -0.0057 94  TYR A CZ  
726  O OH  . TYR A 94  ? 0.2492 0.4305 0.2092 0.0077  0.0334  -0.0138 94  TYR A OH  
727  N N   . CYS A 95  ? 0.1698 0.1807 0.1293 0.0033  -0.0013 0.0159  95  CYS A N   
728  C CA  . CYS A 95  ? 0.1666 0.1980 0.1373 0.0098  -0.0080 -0.0009 95  CYS A CA  
729  C C   . CYS A 95  ? 0.1752 0.2107 0.1273 0.0210  -0.0057 0.0046  95  CYS A C   
730  O O   . CYS A 95  ? 0.1538 0.2471 0.1197 0.0212  0.0081  0.0156  95  CYS A O   
731  C CB  . CYS A 95  ? 0.1985 0.2688 0.1724 -0.0435 -0.0202 -0.0118 95  CYS A CB  
732  S SG  . CYS A 95  ? 0.2359 0.3092 0.2609 -0.0205 -0.0064 0.0251  95  CYS A SG  
733  N N   . ALA A 96  ? 0.1761 0.2487 0.1192 0.0421  -0.0111 -0.0083 96  ALA A N   
734  C CA  . ALA A 96  ? 0.1822 0.1975 0.1288 0.0138  -0.0043 -0.0336 96  ALA A CA  
735  C C   . ALA A 96  ? 0.1718 0.1867 0.1305 0.0026  0.0047  -0.0002 96  ALA A C   
736  O O   . ALA A 96  ? 0.1906 0.2402 0.1412 0.0380  -0.0046 -0.0070 96  ALA A O   
737  C CB  . ALA A 96  ? 0.2161 0.2002 0.1357 0.0019  0.0104  -0.0220 96  ALA A CB  
738  N N   . PHE A 97  ? 0.1739 0.2129 0.1274 0.0090  -0.0200 0.0000  97  PHE A N   
739  C CA  . PHE A 97  ? 0.1857 0.2033 0.1593 0.0176  -0.0070 -0.0158 97  PHE A CA  
740  C C   . PHE A 97  ? 0.1918 0.2208 0.1421 0.0087  -0.0096 0.0004  97  PHE A C   
741  O O   . PHE A 97  ? 0.2021 0.2414 0.1506 0.0264  -0.0013 -0.0079 97  PHE A O   
742  C CB  . PHE A 97  ? 0.1874 0.2372 0.1269 0.0020  0.0010  -0.0153 97  PHE A CB  
743  C CG  . PHE A 97  ? 0.1958 0.2671 0.1757 -0.0182 -0.0004 -0.0253 97  PHE A CG  
744  C CD1 . PHE A 97  ? 0.1912 0.2809 0.1796 -0.0043 -0.0230 -0.0333 97  PHE A CD1 
745  C CD2 . PHE A 97  ? 0.2142 0.2599 0.1972 -0.0375 -0.0069 -0.0158 97  PHE A CD2 
746  C CE1 . PHE A 97  ? 0.1958 0.3032 0.2279 -0.0331 -0.0278 -0.0087 97  PHE A CE1 
747  C CE2 . PHE A 97  ? 0.1948 0.2923 0.2196 -0.0570 0.0035  -0.0014 97  PHE A CE2 
748  C CZ  . PHE A 97  ? 0.2092 0.2802 0.2246 -0.0330 -0.0298 -0.0114 97  PHE A CZ  
749  N N   . ILE A 98  ? 0.2124 0.2035 0.1611 0.0031  -0.0231 0.0072  98  ILE A N   
750  C CA  . ILE A 98  ? 0.1969 0.2221 0.1575 -0.0130 0.0105  -0.0251 98  ILE A CA  
751  C C   . ILE A 98  ? 0.2096 0.2162 0.1527 -0.0127 0.0086  -0.0237 98  ILE A C   
752  O O   . ILE A 98  ? 0.2090 0.2411 0.1584 -0.0117 0.0235  0.0012  98  ILE A O   
753  C CB  . ILE A 98  ? 0.2307 0.2276 0.1619 -0.0003 -0.0059 0.0022  98  ILE A CB  
754  C CG1 . ILE A 98  ? 0.2267 0.2628 0.1748 0.0050  0.0053  -0.0221 98  ILE A CG1 
755  C CG2 . ILE A 98  ? 0.2255 0.2431 0.1844 0.0104  -0.0081 -0.0306 98  ILE A CG2 
756  C CD1 . ILE A 98  ? 0.2874 0.2676 0.1850 -0.0154 -0.0092 -0.0221 98  ILE A CD1 
757  N N   . THR A 99  ? 0.2266 0.2466 0.1644 -0.0099 0.0134  -0.0008 99  THR A N   
758  C CA  . THR A 99  ? 0.2238 0.3173 0.1650 -0.0424 0.0108  -0.0167 99  THR A CA  
759  C C   . THR A 99  ? 0.2525 0.3639 0.1760 -0.0373 0.0234  -0.0504 99  THR A C   
760  O O   . THR A 99  ? 0.2720 0.3028 0.1822 -0.0837 0.0329  -0.0509 99  THR A O   
761  C CB  . THR A 99  ? 0.2735 0.3186 0.2197 -0.0305 -0.0022 -0.0010 99  THR A CB  
762  O OG1 . THR A 99  ? 0.2617 0.3267 0.1978 -0.0363 -0.0058 0.0113  99  THR A OG1 
763  C CG2 . THR A 99  ? 0.2863 0.3235 0.2378 -0.0460 -0.0106 -0.0141 99  THR A CG2 
764  N N   . THR A 100 ? 0.3212 0.3493 0.1594 -0.0264 0.0373  -0.0596 100 THR A N   
765  C CA  A THR A 100 ? 0.3395 0.3932 0.1558 -0.0703 0.0179  -0.0463 100 THR A CA  
766  C CA  B THR A 100 ? 0.3363 0.3853 0.1534 -0.0556 0.0149  -0.0396 100 THR A CA  
767  C C   . THR A 100 ? 0.3233 0.4073 0.1854 -0.0890 0.0149  -0.0360 100 THR A C   
768  O O   . THR A 100 ? 0.3157 0.4398 0.1137 -0.0811 0.0128  -0.0648 100 THR A O   
769  C CB  A THR A 100 ? 0.3917 0.3911 0.1693 -0.0792 0.0242  -0.0471 100 THR A CB  
770  C CB  B THR A 100 ? 0.3954 0.3922 0.1967 -0.0288 0.0170  -0.0275 100 THR A CB  
771  O OG1 A THR A 100 ? 0.4184 0.4293 0.1954 -0.0992 0.0306  -0.0876 100 THR A OG1 
772  O OG1 B THR A 100 ? 0.4210 0.4073 0.2585 -0.0193 -0.0252 -0.0416 100 THR A OG1 
773  C CG2 A THR A 100 ? 0.4069 0.3932 0.1956 -0.0635 0.0198  -0.0651 100 THR A CG2 
774  C CG2 B THR A 100 ? 0.3926 0.3826 0.2243 -0.0115 0.0329  -0.0295 100 THR A CG2 
775  N N   . GLU A 101 ? 0.3468 0.4977 0.1980 -0.0888 -0.0081 -0.0474 101 GLU A N   
776  C CA  . GLU A 101 ? 0.3794 0.4875 0.2919 -0.1203 0.0561  -0.0453 101 GLU A CA  
777  C C   . GLU A 101 ? 0.4505 0.5326 0.3129 -0.1209 0.0560  -0.1077 101 GLU A C   
778  O O   . GLU A 101 ? 0.5581 0.5123 0.4673 -0.2427 0.1486  -0.1469 101 GLU A O   
779  C CB  . GLU A 101 ? 0.4381 0.5515 0.3359 -0.0752 0.0396  -0.0203 101 GLU A CB  
780  C CG  . GLU A 101 ? 0.4508 0.5216 0.4362 -0.1147 0.0618  -0.0120 101 GLU A CG  
781  C CD  . GLU A 101 ? 0.4583 0.6343 0.4470 -0.0492 0.0611  -0.0169 101 GLU A CD  
782  O OE1 . GLU A 101 ? 0.4934 0.6656 0.4807 0.0008  0.0864  -0.0101 101 GLU A OE1 
783  O OE2 . GLU A 101 ? 0.6104 0.7502 0.5031 -0.0833 0.1074  0.0931  101 GLU A OE2 
784  N N   . SER A 102 ? 0.4344 0.6078 0.2943 -0.1514 0.1175  -0.0563 102 SER A N   
785  C CA  . SER A 102 ? 0.4058 0.6150 0.4085 -0.1166 0.0553  -0.0767 102 SER A CA  
786  C C   . SER A 102 ? 0.3741 0.5793 0.3443 -0.0958 0.0409  -0.1186 102 SER A C   
787  O O   . SER A 102 ? 0.3168 0.5269 0.4180 -0.1900 0.0395  -0.1590 102 SER A O   
788  C CB  . SER A 102 ? 0.4288 0.7766 0.4052 -0.1388 0.0628  -0.0439 102 SER A CB  
789  O OG  . SER A 102 ? 0.4184 0.6995 0.2880 -0.2822 0.0508  0.0854  102 SER A OG  
790  N N   . ASP A 103 ? 0.3237 0.5589 0.3811 -0.1029 -0.0417 -0.1056 103 ASP A N   
791  C CA  . ASP A 103 ? 0.3568 0.5607 0.3563 -0.0512 -0.0531 -0.0794 103 ASP A CA  
792  C C   . ASP A 103 ? 0.3625 0.4262 0.2439 -0.0183 -0.0544 -0.0649 103 ASP A C   
793  O O   . ASP A 103 ? 0.4269 0.4495 0.2714 0.0093  -0.0164 -0.0142 103 ASP A O   
794  C CB  . ASP A 103 ? 0.4018 0.6670 0.5025 0.0049  -0.0492 -0.1355 103 ASP A CB  
795  C CG  . ASP A 103 ? 0.4727 0.8145 0.5829 0.0572  -0.1260 -0.1357 103 ASP A CG  
796  O OD1 . ASP A 103 ? 0.6156 0.9143 0.6147 -0.0014 -0.1877 -0.1869 103 ASP A OD1 
797  O OD2 . ASP A 103 ? 0.5616 0.9735 0.8179 0.1842  -0.0798 -0.0773 103 ASP A OD2 
798  N N   . TYR A 104 ? 0.3171 0.3611 0.2419 -0.0572 0.0257  -0.0292 104 TYR A N   
799  C CA  . TYR A 104 ? 0.3484 0.3257 0.2051 -0.0504 -0.0125 -0.0065 104 TYR A CA  
800  C C   . TYR A 104 ? 0.3161 0.3590 0.2398 -0.0802 0.0135  -0.0108 104 TYR A C   
801  O O   . TYR A 104 ? 0.3118 0.3864 0.2236 -0.0497 -0.0028 -0.0406 104 TYR A O   
802  C CB  . TYR A 104 ? 0.3427 0.2944 0.2016 -0.0587 -0.0193 -0.0135 104 TYR A CB  
803  C CG  . TYR A 104 ? 0.3254 0.2814 0.2301 -0.0379 -0.0465 -0.0152 104 TYR A CG  
804  C CD1 . TYR A 104 ? 0.2910 0.2988 0.3383 -0.0389 -0.0403 -0.0574 104 TYR A CD1 
805  C CD2 . TYR A 104 ? 0.3277 0.2991 0.2932 -0.0622 -0.0010 -0.0498 104 TYR A CD2 
806  C CE1 . TYR A 104 ? 0.3216 0.2881 0.4076 -0.0378 -0.0306 -0.0768 104 TYR A CE1 
807  C CE2 . TYR A 104 ? 0.3092 0.3013 0.3049 -0.0515 0.0084  -0.0257 104 TYR A CE2 
808  C CZ  . TYR A 104 ? 0.3196 0.2928 0.3239 -0.0466 0.0148  -0.0364 104 TYR A CZ  
809  O OH  . TYR A 104 ? 0.3651 0.2693 0.3788 -0.0139 -0.0362 -0.0532 104 TYR A OH  
810  N N   . ASP A 105 ? 0.3342 0.3762 0.2391 -0.0527 -0.0016 -0.0198 105 ASP A N   
811  C CA  . ASP A 105 ? 0.3614 0.3603 0.2005 -0.0402 -0.0227 -0.0274 105 ASP A CA  
812  C C   . ASP A 105 ? 0.3558 0.3196 0.2078 -0.0372 -0.0158 -0.0361 105 ASP A C   
813  O O   . ASP A 105 ? 0.3502 0.3591 0.1807 -0.0345 0.0217  0.0021  105 ASP A O   
814  C CB  . ASP A 105 ? 0.4292 0.3791 0.2384 -0.0787 -0.0516 -0.0146 105 ASP A CB  
815  C CG  . ASP A 105 ? 0.4229 0.4652 0.3138 -0.0830 -0.0720 -0.0252 105 ASP A CG  
816  O OD1 . ASP A 105 ? 0.4919 0.6494 0.2636 -0.1194 -0.0770 0.0313  105 ASP A OD1 
817  O OD2 . ASP A 105 ? 0.5247 0.5409 0.3221 -0.0808 -0.0353 -0.0216 105 ASP A OD2 
818  N N   . LEU A 106 ? 0.3330 0.2823 0.2287 -0.0609 -0.0284 -0.0359 106 LEU A N   
819  C CA  . LEU A 106 ? 0.3500 0.3124 0.2158 -0.0841 -0.0259 -0.0476 106 LEU A CA  
820  C C   . LEU A 106 ? 0.3471 0.3126 0.2164 -0.0662 -0.0260 -0.0559 106 LEU A C   
821  O O   . LEU A 106 ? 0.3335 0.3167 0.2094 -0.0860 -0.0251 -0.0621 106 LEU A O   
822  C CB  . LEU A 106 ? 0.3343 0.3179 0.2518 -0.0639 -0.0397 -0.0361 106 LEU A CB  
823  C CG  . LEU A 106 ? 0.3761 0.3362 0.2552 -0.0774 -0.0594 -0.0325 106 LEU A CG  
824  C CD1 . LEU A 106 ? 0.3707 0.3493 0.3035 -0.0632 -0.0421 -0.0076 106 LEU A CD1 
825  C CD2 . LEU A 106 ? 0.3725 0.3796 0.3199 -0.0666 -0.0163 -0.0445 106 LEU A CD2 
826  N N   . GLY A 107 ? 0.4156 0.3338 0.2372 -0.1037 0.0002  -0.0768 107 GLY A N   
827  C CA  . GLY A 107 ? 0.3741 0.3369 0.1924 -0.0751 -0.0155 -0.0509 107 GLY A CA  
828  C C   . GLY A 107 ? 0.3529 0.3118 0.2194 -0.0917 -0.0129 -0.0384 107 GLY A C   
829  O O   . GLY A 107 ? 0.3254 0.3482 0.1912 -0.0393 -0.0240 -0.0619 107 GLY A O   
830  N N   . ARG A 108 ? 0.3398 0.3164 0.1395 -0.0615 -0.0402 -0.0232 108 ARG A N   
831  C CA  . ARG A 108 ? 0.3489 0.3331 0.1707 -0.0247 -0.0635 -0.0302 108 ARG A CA  
832  C C   . ARG A 108 ? 0.2767 0.2763 0.1634 -0.0299 -0.0393 -0.0389 108 ARG A C   
833  O O   . ARG A 108 ? 0.2770 0.3239 0.1821 -0.0333 -0.0375 -0.0176 108 ARG A O   
834  C CB  . ARG A 108 ? 0.3906 0.3562 0.2085 -0.0027 -0.0828 -0.0133 108 ARG A CB  
835  C CG  . ARG A 108 ? 0.4349 0.3987 0.2329 -0.0031 -0.1183 -0.0088 108 ARG A CG  
836  C CD  . ARG A 108 ? 0.4299 0.4779 0.2614 0.0202  -0.1156 -0.0060 108 ARG A CD  
837  N NE  . ARG A 108 ? 0.5052 0.4771 0.3202 0.0529  -0.1993 -0.0237 108 ARG A NE  
838  C CZ  . ARG A 108 ? 0.5718 0.4940 0.3055 0.0291  -0.1623 -0.0272 108 ARG A CZ  
839  N NH1 . ARG A 108 ? 0.5372 0.4482 0.2863 -0.0041 -0.1829 -0.0741 108 ARG A NH1 
840  N NH2 . ARG A 108 ? 0.5917 0.4941 0.3257 -0.0033 -0.1805 0.0093  108 ARG A NH2 
841  N N   . ARG A 109 ? 0.2410 0.2258 0.1919 -0.0109 -0.0413 -0.0194 109 ARG A N   
842  C CA  . ARG A 109 ? 0.2241 0.2483 0.1828 -0.0055 -0.0344 -0.0126 109 ARG A CA  
843  C C   . ARG A 109 ? 0.2005 0.2555 0.2113 0.0064  -0.0448 -0.0080 109 ARG A C   
844  O O   . ARG A 109 ? 0.1946 0.2850 0.2211 0.0094  -0.0678 -0.0233 109 ARG A O   
845  C CB  . ARG A 109 ? 0.2195 0.2383 0.1885 -0.0198 -0.0255 -0.0245 109 ARG A CB  
846  C CG  . ARG A 109 ? 0.2323 0.2533 0.1772 -0.0180 -0.0106 -0.0340 109 ARG A CG  
847  C CD  . ARG A 109 ? 0.2429 0.2544 0.1881 -0.0093 -0.0059 -0.0238 109 ARG A CD  
848  N NE  . ARG A 109 ? 0.2158 0.2597 0.1734 -0.0035 -0.0073 -0.0408 109 ARG A NE  
849  C CZ  . ARG A 109 ? 0.2143 0.2533 0.1904 -0.0139 -0.0055 -0.0243 109 ARG A CZ  
850  N NH1 . ARG A 109 ? 0.2211 0.2267 0.2091 -0.0140 -0.0126 -0.0281 109 ARG A NH1 
851  N NH2 . ARG A 109 ? 0.2253 0.2408 0.2195 -0.0268 -0.0299 -0.0230 109 ARG A NH2 
852  N N   . TYR A 110 ? 0.1828 0.2442 0.1735 -0.0037 -0.0254 0.0165  110 TYR A N   
853  C CA  . TYR A 110 ? 0.2050 0.2517 0.1759 0.0212  -0.0186 0.0153  110 TYR A CA  
854  C C   . TYR A 110 ? 0.1819 0.2236 0.1720 0.0310  -0.0137 0.0095  110 TYR A C   
855  O O   . TYR A 110 ? 0.1595 0.2083 0.1246 0.0128  -0.0120 0.0040  110 TYR A O   
856  C CB  . TYR A 110 ? 0.2477 0.2414 0.1582 0.0048  0.0009  0.0050  110 TYR A CB  
857  C CG  . TYR A 110 ? 0.3043 0.2895 0.1658 0.0020  -0.0272 -0.0038 110 TYR A CG  
858  C CD1 . TYR A 110 ? 0.3104 0.3328 0.1615 0.0197  -0.0200 -0.0071 110 TYR A CD1 
859  C CD2 . TYR A 110 ? 0.3363 0.3231 0.1577 0.0100  -0.0357 -0.0182 110 TYR A CD2 
860  C CE1 . TYR A 110 ? 0.3875 0.3831 0.1683 0.0248  -0.0346 -0.0172 110 TYR A CE1 
861  C CE2 . TYR A 110 ? 0.3961 0.3371 0.1374 -0.0024 -0.0096 -0.0149 110 TYR A CE2 
862  C CZ  . TYR A 110 ? 0.4050 0.3643 0.1481 0.0104  -0.0167 -0.0109 110 TYR A CZ  
863  O OH  . TYR A 110 ? 0.5388 0.4418 0.1751 0.0207  -0.0880 0.0105  110 TYR A OH  
864  N N   . TRP A 111 ? 0.1701 0.2162 0.1955 0.0307  -0.0225 0.0010  111 TRP A N   
865  C CA  . TRP A 111 ? 0.1567 0.2262 0.1900 0.0295  -0.0234 0.0191  111 TRP A CA  
866  C C   . TRP A 111 ? 0.1604 0.2296 0.1796 0.0265  -0.0119 0.0252  111 TRP A C   
867  O O   . TRP A 111 ? 0.1654 0.2357 0.1422 0.0385  0.0012  0.0217  111 TRP A O   
868  C CB  . TRP A 111 ? 0.1770 0.2187 0.1732 0.0331  -0.0031 0.0222  111 TRP A CB  
869  C CG  . TRP A 111 ? 0.1654 0.2273 0.1836 0.0190  -0.0063 0.0131  111 TRP A CG  
870  C CD1 . TRP A 111 ? 0.1512 0.2499 0.2127 0.0172  -0.0208 0.0063  111 TRP A CD1 
871  C CD2 . TRP A 111 ? 0.1581 0.2169 0.1863 0.0281  -0.0193 0.0025  111 TRP A CD2 
872  N NE1 . TRP A 111 ? 0.1933 0.2549 0.2229 -0.0039 -0.0396 0.0098  111 TRP A NE1 
873  C CE2 . TRP A 111 ? 0.1817 0.2284 0.2115 0.0105  -0.0242 0.0024  111 TRP A CE2 
874  C CE3 . TRP A 111 ? 0.1749 0.2252 0.1766 0.0252  -0.0161 -0.0011 111 TRP A CE3 
875  C CZ2 . TRP A 111 ? 0.1940 0.2254 0.2166 -0.0216 -0.0248 0.0052  111 TRP A CZ2 
876  C CZ3 . TRP A 111 ? 0.2046 0.2339 0.1681 0.0102  -0.0480 0.0056  111 TRP A CZ3 
877  C CH2 . TRP A 111 ? 0.2153 0.1983 0.1989 0.0129  -0.0097 0.0187  111 TRP A CH2 
878  N N   . GLY A 112 ? 0.1205 0.2324 0.1817 0.0238  -0.0056 0.0241  112 GLY A N   
879  C CA  . GLY A 112 ? 0.1518 0.2359 0.1705 0.0525  -0.0036 0.0070  112 GLY A CA  
880  C C   . GLY A 112 ? 0.1579 0.2526 0.1809 0.0464  0.0023  0.0054  112 GLY A C   
881  O O   . GLY A 112 ? 0.2141 0.2466 0.1857 0.0345  0.0276  0.0025  112 GLY A O   
882  N N   . GLN A 113 ? 0.2095 0.2609 0.1804 0.0696  -0.0184 -0.0007 113 GLN A N   
883  C CA  . GLN A 113 ? 0.2159 0.2700 0.1580 0.0642  -0.0002 0.0089  113 GLN A CA  
884  C C   . GLN A 113 ? 0.1994 0.2675 0.1662 0.0625  -0.0164 0.0177  113 GLN A C   
885  O O   . GLN A 113 ? 0.2294 0.2891 0.1437 0.0461  0.0159  0.0075  113 GLN A O   
886  C CB  . GLN A 113 ? 0.2331 0.2683 0.2134 0.0498  -0.0127 0.0170  113 GLN A CB  
887  C CG  . GLN A 113 ? 0.2451 0.2813 0.2069 0.0645  -0.0269 0.0124  113 GLN A CG  
888  C CD  . GLN A 113 ? 0.2766 0.2800 0.2486 0.0506  -0.0314 0.0062  113 GLN A CD  
889  O OE1 . GLN A 113 ? 0.2718 0.2623 0.2909 0.0516  -0.0488 -0.0100 113 GLN A OE1 
890  N NE2 . GLN A 113 ? 0.2063 0.3138 0.2543 0.0665  -0.0166 0.0126  113 GLN A NE2 
891  N N   . GLY A 114 ? 0.1868 0.3180 0.1902 0.0649  -0.0116 0.0185  114 GLY A N   
892  C CA  . GLY A 114 ? 0.2283 0.2677 0.1742 0.0454  -0.0162 -0.0042 114 GLY A CA  
893  C C   . GLY A 114 ? 0.2539 0.2421 0.2090 0.0436  -0.0192 -0.0015 114 GLY A C   
894  O O   . GLY A 114 ? 0.3707 0.2352 0.1361 0.0363  -0.0112 -0.0244 114 GLY A O   
895  N N   . THR A 115 ? 0.2540 0.2505 0.1866 0.0417  -0.0229 -0.0194 115 THR A N   
896  C CA  . THR A 115 ? 0.3299 0.2595 0.1909 0.0335  -0.0081 -0.0340 115 THR A CA  
897  C C   . THR A 115 ? 0.2908 0.2543 0.2021 0.0477  0.0200  -0.0249 115 THR A C   
898  O O   . THR A 115 ? 0.2258 0.2486 0.1545 0.0228  -0.0049 -0.0248 115 THR A O   
899  C CB  . THR A 115 ? 0.3634 0.2759 0.2738 -0.0335 -0.0176 -0.0228 115 THR A CB  
900  O OG1 . THR A 115 ? 0.4875 0.3243 0.3041 -0.0355 0.0488  -0.0831 115 THR A OG1 
901  C CG2 . THR A 115 ? 0.3715 0.3342 0.2979 -0.0044 -0.0033 -0.0239 115 THR A CG2 
902  N N   . LEU A 116 ? 0.2768 0.2495 0.1825 0.0454  -0.0009 -0.0241 116 LEU A N   
903  C CA  . LEU A 116 ? 0.2412 0.3007 0.1705 0.0511  -0.0084 -0.0303 116 LEU A CA  
904  C C   . LEU A 116 ? 0.2343 0.2503 0.1861 0.0328  -0.0077 -0.0252 116 LEU A C   
905  O O   . LEU A 116 ? 0.2992 0.2634 0.1642 0.0027  0.0048  -0.0250 116 LEU A O   
906  C CB  . LEU A 116 ? 0.2746 0.3337 0.1893 0.0886  -0.0039 -0.0317 116 LEU A CB  
907  C CG  . LEU A 116 ? 0.2673 0.3774 0.2010 0.0891  -0.0106 -0.0073 116 LEU A CG  
908  C CD1 . LEU A 116 ? 0.2973 0.3871 0.2069 0.1017  -0.0009 -0.0042 116 LEU A CD1 
909  C CD2 . LEU A 116 ? 0.2864 0.4230 0.2280 0.1314  -0.0482 -0.0338 116 LEU A CD2 
910  N N   . VAL A 117 ? 0.2129 0.2688 0.1505 0.0347  -0.0246 -0.0229 117 VAL A N   
911  C CA  . VAL A 117 ? 0.2200 0.2672 0.1346 0.0205  -0.0197 -0.0054 117 VAL A CA  
912  C C   . VAL A 117 ? 0.1740 0.2602 0.1586 0.0308  -0.0089 -0.0028 117 VAL A C   
913  O O   . VAL A 117 ? 0.2041 0.2914 0.1536 -0.0020 -0.0280 -0.0151 117 VAL A O   
914  C CB  . VAL A 117 ? 0.1992 0.2916 0.1448 0.0290  -0.0109 -0.0001 117 VAL A CB  
915  C CG1 . VAL A 117 ? 0.2226 0.3272 0.1617 0.0547  -0.0248 -0.0140 117 VAL A CG1 
916  C CG2 . VAL A 117 ? 0.2041 0.2880 0.1211 0.0091  -0.0307 -0.0145 117 VAL A CG2 
917  N N   . THR A 118 ? 0.2547 0.3064 0.1656 0.0221  -0.0028 -0.0197 118 THR A N   
918  C CA  . THR A 118 ? 0.2422 0.3765 0.1684 0.0416  -0.0098 0.0050  118 THR A CA  
919  C C   . THR A 118 ? 0.2140 0.3133 0.1551 0.0422  0.0080  -0.0112 118 THR A C   
920  O O   . THR A 118 ? 0.2268 0.3778 0.1870 0.0049  -0.0212 -0.0330 118 THR A O   
921  C CB  . THR A 118 ? 0.2677 0.4033 0.1868 0.0681  0.0013  0.0098  118 THR A CB  
922  O OG1 . THR A 118 ? 0.2871 0.4327 0.1820 0.0784  -0.0112 0.0046  118 THR A OG1 
923  C CG2 . THR A 118 ? 0.2630 0.4529 0.2220 0.0481  0.0345  0.0200  118 THR A CG2 
924  N N   . VAL A 119 ? 0.2248 0.3250 0.1296 0.0500  0.0250  -0.0117 119 VAL A N   
925  C CA  . VAL A 119 ? 0.2141 0.3512 0.1153 0.0203  0.0236  0.0027  119 VAL A CA  
926  C C   . VAL A 119 ? 0.2283 0.3429 0.1133 0.0358  0.0257  -0.0160 119 VAL A C   
927  O O   . VAL A 119 ? 0.2267 0.3700 0.1585 0.0113  0.0157  -0.0018 119 VAL A O   
928  C CB  . VAL A 119 ? 0.2130 0.3574 0.1345 0.0302  0.0210  0.0126  119 VAL A CB  
929  C CG1 . VAL A 119 ? 0.1871 0.3856 0.1627 0.0131  0.0139  -0.0001 119 VAL A CG1 
930  C CG2 . VAL A 119 ? 0.2293 0.3713 0.1366 0.0179  0.0241  0.0108  119 VAL A CG2 
931  N N   . SER A 120 ? 0.2777 0.3664 0.1573 0.0427  0.0227  -0.0542 120 SER A N   
932  C CA  . SER A 120 ? 0.2911 0.3772 0.1698 0.0062  0.0483  -0.0621 120 SER A CA  
933  C C   . SER A 120 ? 0.3140 0.4128 0.1709 -0.0316 0.0445  -0.0550 120 SER A C   
934  O O   . SER A 120 ? 0.3070 0.4628 0.1957 -0.0403 0.0469  -0.0372 120 SER A O   
935  C CB  . SER A 120 ? 0.2966 0.4387 0.2576 -0.0044 -0.0029 -0.0377 120 SER A CB  
936  O OG  . SER A 120 ? 0.3651 0.4601 0.3821 0.0421  -0.0399 -0.0156 120 SER A OG  
937  N N   . SER A 121 ? 0.4517 0.5234 0.1669 -0.0595 0.0740  -0.0328 121 SER A N   
938  C CA  . SER A 121 ? 0.5892 0.5837 0.3359 -0.0913 -0.0202 -0.0883 121 SER A CA  
939  C C   . SER A 121 ? 0.6731 0.6413 0.4727 0.0106  -0.0088 -0.0520 121 SER A C   
940  O O   . SER A 121 ? 0.7441 0.6728 0.6850 -0.0350 0.1533  0.0564  121 SER A O   
941  C CB  . SER A 121 ? 0.6939 0.6608 0.3249 -0.0999 0.0112  -0.0307 121 SER A CB  
942  O OG  . SER A 121 ? 0.7082 0.7830 0.2462 -0.1821 0.0586  -0.0890 121 SER A OG  
943  N N   . GLN B 3   ? 0.6453 0.6205 0.3581 -0.0189 -0.0680 -0.1740 3   GLN B N   
944  C CA  . GLN B 3   ? 0.5209 0.5581 0.3065 0.0194  0.0330  -0.1129 3   GLN B CA  
945  C C   . GLN B 3   ? 0.4673 0.4137 0.2634 -0.0050 0.0020  -0.0721 3   GLN B C   
946  O O   . GLN B 3   ? 0.4579 0.4736 0.2067 -0.0463 0.0643  -0.0671 3   GLN B O   
947  C CB  . GLN B 3   ? 0.5521 0.5811 0.4078 0.0381  -0.0329 -0.1450 3   GLN B CB  
948  C CG  . GLN B 3   ? 0.5313 0.5083 0.4375 0.0550  -0.0694 -0.1087 3   GLN B CG  
949  C CD  . GLN B 3   ? 0.5188 0.5054 0.4591 0.0256  -0.0933 -0.1011 3   GLN B CD  
950  O OE1 . GLN B 3   ? 0.4926 0.4978 0.3980 0.0388  -0.1431 -0.0788 3   GLN B OE1 
951  N NE2 . GLN B 3   ? 0.3489 0.3556 0.4512 0.0611  -0.0380 -0.0367 3   GLN B NE2 
952  N N   . LEU B 4   ? 0.3157 0.3285 0.2240 0.0569  0.0007  -0.0196 4   LEU B N   
953  C CA  . LEU B 4   ? 0.3217 0.2919 0.1960 0.0391  -0.0233 0.0068  4   LEU B CA  
954  C C   . LEU B 4   ? 0.2988 0.3126 0.2638 0.0882  -0.0341 0.0040  4   LEU B C   
955  O O   . LEU B 4   ? 0.3499 0.3083 0.2417 0.0588  -0.0335 -0.0277 4   LEU B O   
956  C CB  . LEU B 4   ? 0.3110 0.3272 0.2217 0.0713  -0.0010 0.0000  4   LEU B CB  
957  C CG  . LEU B 4   ? 0.3446 0.3270 0.3194 0.0849  -0.0408 0.0202  4   LEU B CG  
958  C CD1 . LEU B 4   ? 0.3617 0.2995 0.3455 0.0892  -0.0392 0.0432  4   LEU B CD1 
959  C CD2 . LEU B 4   ? 0.3746 0.3005 0.3390 0.1019  -0.0739 0.0063  4   LEU B CD2 
960  N N   . VAL B 5   ? 0.3484 0.3065 0.2440 0.0969  -0.0553 -0.0031 5   VAL B N   
961  C CA  . VAL B 5   ? 0.3312 0.3407 0.2444 0.1066  -0.0257 0.0387  5   VAL B CA  
962  C C   . VAL B 5   ? 0.2714 0.2657 0.2534 0.0951  -0.0344 0.0246  5   VAL B C   
963  O O   . VAL B 5   ? 0.2970 0.3082 0.2402 0.0633  0.0002  -0.0076 5   VAL B O   
964  C CB  . VAL B 5   ? 0.4077 0.3567 0.3849 0.1414  -0.0816 0.0147  5   VAL B CB  
965  C CG1 . VAL B 5   ? 0.4674 0.3696 0.5009 0.1212  -0.0786 -0.0251 5   VAL B CG1 
966  C CG2 . VAL B 5   ? 0.3990 0.3992 0.3421 0.1880  -0.0327 0.0065  5   VAL B CG2 
967  N N   . GLU B 6   ? 0.2757 0.2575 0.2638 0.0843  -0.0224 0.0275  6   GLU B N   
968  C CA  . GLU B 6   ? 0.2819 0.2493 0.2813 0.0571  0.0013  0.0114  6   GLU B CA  
969  C C   . GLU B 6   ? 0.2787 0.2410 0.2789 0.0630  0.0085  0.0106  6   GLU B C   
970  O O   . GLU B 6   ? 0.2868 0.3258 0.2791 0.1021  0.0345  -0.0001 6   GLU B O   
971  C CB  . GLU B 6   ? 0.2626 0.2426 0.2753 0.0427  -0.0207 0.0260  6   GLU B CB  
972  C CG  . GLU B 6   ? 0.2399 0.2637 0.2528 0.0644  -0.0154 0.0050  6   GLU B CG  
973  C CD  . GLU B 6   ? 0.2595 0.2830 0.2625 0.0400  -0.0071 -0.0057 6   GLU B CD  
974  O OE1 . GLU B 6   ? 0.2851 0.2900 0.2439 0.0384  -0.0362 -0.0072 6   GLU B OE1 
975  O OE2 . GLU B 6   ? 0.2237 0.3144 0.2220 0.0285  0.0148  -0.0342 6   GLU B OE2 
976  N N   . SER B 7   ? 0.2926 0.1999 0.2803 0.0648  0.0257  -0.0053 7   SER B N   
977  C CA  A SER B 7   ? 0.3379 0.2431 0.2565 0.0641  0.0248  0.0003  7   SER B CA  
978  C CA  B SER B 7   ? 0.3214 0.2312 0.2536 0.0449  0.0206  -0.0021 7   SER B CA  
979  C C   . SER B 7   ? 0.3306 0.2226 0.2399 0.0662  0.0153  0.0021  7   SER B C   
980  O O   . SER B 7   ? 0.2739 0.2250 0.2278 0.0418  0.0216  -0.0019 7   SER B O   
981  C CB  A SER B 7   ? 0.3853 0.2513 0.2765 0.0520  0.0208  -0.0099 7   SER B CB  
982  C CB  B SER B 7   ? 0.3224 0.2297 0.2306 0.0219  0.0316  0.0022  7   SER B CB  
983  O OG  A SER B 7   ? 0.4097 0.2757 0.3001 0.0802  0.0303  -0.0378 7   SER B OG  
984  O OG  B SER B 7   ? 0.3317 0.1810 0.2256 0.0142  0.0217  0.0044  7   SER B OG  
985  N N   . GLY B 8   ? 0.3439 0.2251 0.2689 0.0999  -0.0272 0.0124  8   GLY B N   
986  C CA  . GLY B 8   ? 0.3876 0.2573 0.2908 0.1251  0.0085  0.0181  8   GLY B CA  
987  C C   . GLY B 8   ? 0.4058 0.2213 0.3399 0.1002  -0.0198 0.0278  8   GLY B C   
988  O O   . GLY B 8   ? 0.5382 0.2955 0.2791 0.1039  -0.0024 0.0308  8   GLY B O   
989  N N   . GLY B 9   ? 0.4108 0.2165 0.3031 0.0829  -0.0668 0.0147  9   GLY B N   
990  C CA  . GLY B 9   ? 0.4585 0.2580 0.3072 0.0797  -0.0507 -0.0159 9   GLY B CA  
991  C C   . GLY B 9   ? 0.4029 0.2430 0.3147 0.0731  -0.0421 -0.0241 9   GLY B C   
992  O O   . GLY B 9   ? 0.4980 0.2660 0.3397 0.0729  -0.0314 0.0525  9   GLY B O   
993  N N   . GLY B 10  ? 0.2927 0.2323 0.2495 0.0652  0.0291  -0.0219 10  GLY B N   
994  C CA  . GLY B 10  ? 0.2787 0.2747 0.2333 0.0907  0.0546  -0.0080 10  GLY B CA  
995  C C   . GLY B 10  ? 0.2998 0.2899 0.2093 0.0945  0.0191  -0.0044 10  GLY B C   
996  O O   . GLY B 10  ? 0.4000 0.2303 0.1754 0.0676  0.0003  0.0260  10  GLY B O   
997  N N   . LEU B 11  ? 0.2848 0.2681 0.2436 0.1098  0.0218  0.0212  11  LEU B N   
998  C CA  . LEU B 11  ? 0.2493 0.2993 0.2158 0.1000  0.0451  0.0499  11  LEU B CA  
999  C C   . LEU B 11  ? 0.3123 0.3137 0.3154 0.0643  0.0756  0.0799  11  LEU B C   
1000 O O   . LEU B 11  ? 0.3450 0.3233 0.3928 0.0566  0.1963  0.0773  11  LEU B O   
1001 C CB  . LEU B 11  ? 0.2898 0.3467 0.1938 0.1064  0.0184  0.0665  11  LEU B CB  
1002 C CG  . LEU B 11  ? 0.3037 0.3699 0.1842 0.0931  -0.0027 0.0856  11  LEU B CG  
1003 C CD1 . LEU B 11  ? 0.3350 0.3962 0.1673 0.1013  -0.0156 0.0687  11  LEU B CD1 
1004 C CD2 . LEU B 11  ? 0.3172 0.3816 0.2444 0.1280  -0.0060 0.0682  11  LEU B CD2 
1005 N N   . VAL B 12  ? 0.3270 0.3046 0.2509 0.0798  0.0621  0.1142  12  VAL B N   
1006 C CA  A VAL B 12  ? 0.3310 0.3404 0.3356 0.0932  0.0865  0.1306  12  VAL B CA  
1007 C CA  B VAL B 12  ? 0.3268 0.3407 0.3404 0.0991  0.0891  0.1280  12  VAL B CA  
1008 C C   . VAL B 12  ? 0.3943 0.3355 0.3461 0.1352  0.0812  0.1276  12  VAL B C   
1009 O O   . VAL B 12  ? 0.4205 0.4037 0.2372 0.0824  0.1549  0.1018  12  VAL B O   
1010 C CB  A VAL B 12  ? 0.3439 0.3802 0.3815 0.0542  0.0548  0.1057  12  VAL B CB  
1011 C CB  B VAL B 12  ? 0.3421 0.3879 0.4114 0.0739  0.0495  0.0974  12  VAL B CB  
1012 C CG1 A VAL B 12  ? 0.3553 0.3931 0.3958 0.0737  0.0160  0.1119  12  VAL B CG1 
1013 C CG1 B VAL B 12  ? 0.3645 0.3835 0.4438 0.0766  0.0615  0.0848  12  VAL B CG1 
1014 C CG2 A VAL B 12  ? 0.3608 0.3723 0.3963 0.0535  0.0738  0.1147  12  VAL B CG2 
1015 C CG2 B VAL B 12  ? 0.3164 0.3961 0.4209 0.1005  0.0260  0.1041  12  VAL B CG2 
1016 N N   . GLN B 13  ? 0.4235 0.4314 0.3743 0.1087  0.1014  0.1369  13  GLN B N   
1017 C CA  . GLN B 13  ? 0.4493 0.4784 0.3696 0.1239  0.0712  0.1265  13  GLN B CA  
1018 C C   . GLN B 13  ? 0.4173 0.4635 0.2863 0.0870  0.0402  0.1477  13  GLN B C   
1019 O O   . GLN B 13  ? 0.3748 0.4462 0.2944 0.0754  0.0850  0.1031  13  GLN B O   
1020 C CB  . GLN B 13  ? 0.5828 0.5913 0.3958 0.0601  0.0480  0.1948  13  GLN B CB  
1021 C CG  . GLN B 13  ? 0.5748 0.6856 0.4820 0.0537  0.0314  0.2461  13  GLN B CG  
1022 C CD  . GLN B 13  ? 0.7548 0.8304 0.5390 0.0110  -0.0513 0.2080  13  GLN B CD  
1023 O OE1 . GLN B 13  ? 0.7168 0.9353 0.6562 -0.0265 -0.1394 0.2494  13  GLN B OE1 
1024 N NE2 . GLN B 13  ? 0.9271 0.8965 0.5445 0.0663  -0.0814 0.2460  13  GLN B NE2 
1025 N N   . PRO B 14  ? 0.3387 0.4535 0.3486 0.0964  0.0585  0.1307  14  PRO B N   
1026 C CA  . PRO B 14  ? 0.3429 0.4489 0.3186 0.1026  0.0591  0.0909  14  PRO B CA  
1027 C C   . PRO B 14  ? 0.3508 0.4192 0.2826 0.0892  0.0175  0.0626  14  PRO B C   
1028 O O   . PRO B 14  ? 0.3581 0.4163 0.3225 0.0751  0.0708  0.0831  14  PRO B O   
1029 C CB  . PRO B 14  ? 0.3821 0.4623 0.3661 0.0759  0.0290  0.0734  14  PRO B CB  
1030 C CG  . PRO B 14  ? 0.3873 0.5280 0.4101 0.0939  0.0208  0.0948  14  PRO B CG  
1031 C CD  . PRO B 14  ? 0.3752 0.5305 0.3992 0.0969  0.0408  0.0816  14  PRO B CD  
1032 N N   . GLY B 15  ? 0.3440 0.4216 0.2212 0.0637  0.0393  0.0876  15  GLY B N   
1033 C CA  . GLY B 15  ? 0.3913 0.4276 0.2867 0.0355  0.0654  0.1094  15  GLY B CA  
1034 C C   . GLY B 15  ? 0.4045 0.4376 0.2720 0.0438  0.0744  0.1036  15  GLY B C   
1035 O O   . GLY B 15  ? 0.4439 0.4078 0.3369 0.0070  0.1465  0.1164  15  GLY B O   
1036 N N   . GLY B 16  ? 0.4699 0.3989 0.2528 0.0746  0.1014  0.0806  16  GLY B N   
1037 C CA  . GLY B 16  ? 0.4546 0.3621 0.2997 0.0720  0.1043  0.0913  16  GLY B CA  
1038 C C   . GLY B 16  ? 0.4525 0.3152 0.3185 0.0816  0.0800  0.0633  16  GLY B C   
1039 O O   . GLY B 16  ? 0.4451 0.2753 0.2940 0.0656  0.1225  0.0303  16  GLY B O   
1040 N N   . SER B 17  ? 0.4418 0.3301 0.3051 0.0883  0.0977  0.0644  17  SER B N   
1041 C CA  . SER B 17  ? 0.4131 0.2783 0.3116 0.1268  0.0922  0.0391  17  SER B CA  
1042 C C   . SER B 17  ? 0.3573 0.2945 0.3253 0.1118  0.0788  0.0638  17  SER B C   
1043 O O   . SER B 17  ? 0.4244 0.2962 0.3100 0.1002  0.0352  0.1290  17  SER B O   
1044 C CB  . SER B 17  ? 0.4349 0.4113 0.3773 0.0741  0.1006  -0.0093 17  SER B CB  
1045 O OG  . SER B 17  ? 0.4214 0.5573 0.5501 0.1021  0.1561  0.0767  17  SER B OG  
1046 N N   . LEU B 18  ? 0.4257 0.2212 0.3304 0.0862  0.1077  0.0632  18  LEU B N   
1047 C CA  . LEU B 18  ? 0.4059 0.2504 0.3589 0.1037  0.1015  0.0395  18  LEU B CA  
1048 C C   . LEU B 18  ? 0.4243 0.2209 0.3526 0.0781  0.0991  0.0697  18  LEU B C   
1049 O O   . LEU B 18  ? 0.4234 0.2743 0.3146 0.1060  0.1119  0.0451  18  LEU B O   
1050 C CB  . LEU B 18  ? 0.4375 0.2893 0.3899 0.0804  0.0907  0.0432  18  LEU B CB  
1051 C CG  . LEU B 18  ? 0.4335 0.3833 0.4354 0.0548  0.0857  0.0148  18  LEU B CG  
1052 C CD1 . LEU B 18  ? 0.4773 0.4435 0.4368 0.0266  0.1083  0.0701  18  LEU B CD1 
1053 C CD2 . LEU B 18  ? 0.4902 0.3974 0.4494 0.0818  0.0729  0.0091  18  LEU B CD2 
1054 N N   . ARG B 19  ? 0.3911 0.2254 0.3301 0.0370  0.0680  0.0693  19  ARG B N   
1055 C CA  . ARG B 19  ? 0.3489 0.2646 0.3289 0.0101  0.0681  0.0547  19  ARG B CA  
1056 C C   . ARG B 19  ? 0.3318 0.2316 0.3146 0.0441  0.0597  0.0464  19  ARG B C   
1057 O O   . ARG B 19  ? 0.3580 0.2688 0.3319 0.0819  0.0877  0.0882  19  ARG B O   
1058 C CB  . ARG B 19  ? 0.3846 0.2549 0.3912 -0.0115 0.0738  0.0704  19  ARG B CB  
1059 C CG  . ARG B 19  ? 0.4385 0.3338 0.4502 -0.0183 0.0208  0.0593  19  ARG B CG  
1060 C CD  . ARG B 19  ? 0.5452 0.3579 0.4394 -0.0282 0.0163  0.0013  19  ARG B CD  
1061 N NE  . ARG B 19  ? 0.6366 0.3694 0.4641 -0.0142 0.0300  -0.0123 19  ARG B NE  
1062 C CZ  . ARG B 19  ? 0.6619 0.4054 0.4117 -0.0283 0.0054  0.0043  19  ARG B CZ  
1063 N NH1 . ARG B 19  ? 0.6608 0.5203 0.4510 -0.0568 0.0205  0.0055  19  ARG B NH1 
1064 N NH2 . ARG B 19  ? 0.7617 0.3352 0.5197 0.0495  -0.0125 0.0219  19  ARG B NH2 
1065 N N   . LEU B 20  ? 0.2735 0.2124 0.2854 0.0396  0.0408  0.0239  20  LEU B N   
1066 C CA  . LEU B 20  ? 0.2363 0.1940 0.2845 0.0341  0.0256  0.0059  20  LEU B CA  
1067 C C   . LEU B 20  ? 0.2410 0.1864 0.2971 0.0289  0.0244  0.0007  20  LEU B C   
1068 O O   . LEU B 20  ? 0.2404 0.2116 0.2994 0.0519  0.0058  -0.0047 20  LEU B O   
1069 C CB  . LEU B 20  ? 0.2675 0.1961 0.3058 0.0213  0.0148  0.0097  20  LEU B CB  
1070 C CG  . LEU B 20  ? 0.3232 0.2222 0.3076 -0.0033 0.0006  0.0085  20  LEU B CG  
1071 C CD1 . LEU B 20  ? 0.3086 0.2367 0.2759 0.0083  -0.0050 0.0474  20  LEU B CD1 
1072 C CD2 . LEU B 20  ? 0.3336 0.2923 0.3137 0.0064  -0.0194 0.0099  20  LEU B CD2 
1073 N N   . SER B 21  ? 0.2534 0.2013 0.2753 0.0342  0.0142  -0.0190 21  SER B N   
1074 C CA  A SER B 21  ? 0.2849 0.2575 0.2738 0.0119  -0.0092 -0.0048 21  SER B CA  
1075 C CA  B SER B 21  ? 0.2989 0.2623 0.2715 0.0161  -0.0060 0.0009  21  SER B CA  
1076 C C   . SER B 21  ? 0.3233 0.2597 0.2395 0.0104  -0.0020 -0.0106 21  SER B C   
1077 O O   . SER B 21  ? 0.3067 0.2506 0.2557 0.0447  0.0215  0.0086  21  SER B O   
1078 C CB  A SER B 21  ? 0.2971 0.2602 0.3190 0.0191  -0.0287 0.0063  21  SER B CB  
1079 C CB  B SER B 21  ? 0.3549 0.2615 0.3225 0.0147  -0.0092 0.0296  21  SER B CB  
1080 O OG  A SER B 21  ? 0.3517 0.2450 0.3239 0.0134  -0.0031 -0.0055 21  SER B OG  
1081 O OG  B SER B 21  ? 0.3979 0.2609 0.3834 0.0719  -0.0023 0.0375  21  SER B OG  
1082 N N   . CYS B 22  ? 0.2826 0.2730 0.2828 0.0180  -0.0298 -0.0026 22  CYS B N   
1083 C CA  . CYS B 22  ? 0.2955 0.2983 0.2739 0.0141  -0.0096 -0.0038 22  CYS B CA  
1084 C C   . CYS B 22  ? 0.2957 0.2829 0.3011 0.0185  -0.0049 -0.0206 22  CYS B C   
1085 O O   . CYS B 22  ? 0.3002 0.3530 0.3092 0.0609  -0.0202 -0.0234 22  CYS B O   
1086 C CB  . CYS B 22  ? 0.3444 0.3046 0.3088 0.0233  0.0060  -0.0044 22  CYS B CB  
1087 S SG  . CYS B 22  ? 0.3919 0.3282 0.3082 0.0061  -0.0135 0.0155  22  CYS B SG  
1088 N N   . ALA B 23  ? 0.3409 0.2725 0.3125 0.0550  -0.0350 -0.0275 23  ALA B N   
1089 C CA  . ALA B 23  ? 0.3846 0.3108 0.3072 0.0223  -0.0217 -0.0380 23  ALA B CA  
1090 C C   . ALA B 23  ? 0.3647 0.3049 0.3201 0.0227  -0.0102 -0.0314 23  ALA B C   
1091 O O   . ALA B 23  ? 0.3455 0.3310 0.2408 0.0432  -0.0209 -0.0179 23  ALA B O   
1092 C CB  . ALA B 23  ? 0.3975 0.3042 0.3240 0.0136  0.0255  -0.0089 23  ALA B CB  
1093 N N   . ALA B 24  ? 0.3682 0.2714 0.3313 0.0526  -0.0138 -0.0209 24  ALA B N   
1094 C CA  . ALA B 24  ? 0.3982 0.3076 0.3325 0.0390  -0.0002 -0.0098 24  ALA B CA  
1095 C C   . ALA B 24  ? 0.4649 0.3495 0.3284 0.0049  0.0510  -0.0222 24  ALA B C   
1096 O O   . ALA B 24  ? 0.5409 0.3876 0.3302 -0.0548 0.0835  -0.0638 24  ALA B O   
1097 C CB  . ALA B 24  ? 0.4042 0.3929 0.3140 0.0393  -0.0462 0.0126  24  ALA B CB  
1098 N N   . SER B 25  ? 0.5600 0.3781 0.3170 0.0380  0.1245  -0.0087 25  SER B N   
1099 C CA  . SER B 25  ? 0.6498 0.4651 0.3816 0.0571  0.0985  -0.1043 25  SER B CA  
1100 C C   . SER B 25  ? 0.7299 0.4837 0.3718 0.0679  0.1166  -0.1021 25  SER B C   
1101 O O   . SER B 25  ? 0.7231 0.5293 0.2350 0.0319  0.0366  -0.1512 25  SER B O   
1102 C CB  . SER B 25  ? 0.6411 0.4437 0.5379 0.0495  0.0872  -0.1321 25  SER B CB  
1103 O OG  . SER B 25  ? 0.6633 0.4687 0.6095 0.0211  0.1119  -0.1973 25  SER B OG  
1104 N N   . GLY B 26  ? 0.8706 0.5724 0.3932 0.0681  0.0941  -0.1599 26  GLY B N   
1105 C CA  . GLY B 26  ? 0.9707 0.6884 0.5011 0.0852  0.0628  -0.0199 26  GLY B CA  
1106 C C   . GLY B 26  ? 0.9749 0.7818 0.7553 0.1173  0.0083  -0.0167 26  GLY B C   
1107 O O   . GLY B 26  ? 0.9025 0.5537 0.7822 0.2181  -0.0474 0.0235  26  GLY B O   
1108 N N   . SER B 27  ? 1.1788 0.8425 0.9423 0.0596  0.0558  0.1330  27  SER B N   
1109 C CA  . SER B 27  ? 1.1447 0.8704 1.0023 0.0901  0.0622  0.0925  27  SER B CA  
1110 C C   . SER B 27  ? 1.1627 0.7740 0.9432 0.0346  0.1159  0.0840  27  SER B C   
1111 O O   . SER B 27  ? 0.9943 0.7825 0.5937 0.3308  -0.0129 0.1886  27  SER B O   
1112 C CB  . SER B 27  ? 1.1983 1.0156 1.1351 -0.0355 0.2137  0.0275  27  SER B CB  
1113 O OG  . SER B 27  ? 0.9775 1.1954 1.3215 -0.1872 0.4688  0.0849  27  SER B OG  
1114 N N   . VAL B 28  ? 1.1895 0.8607 0.9246 -0.0314 0.1057  0.0620  28  VAL B N   
1115 C CA  . VAL B 28  ? 1.2486 0.8994 0.9342 -0.0026 0.0603  -0.0367 28  VAL B CA  
1116 C C   . VAL B 28  ? 1.2517 0.9010 0.9854 0.0161  0.0385  -0.0607 28  VAL B C   
1117 O O   . VAL B 28  ? 1.4135 1.1008 0.7970 -0.0211 0.0573  -0.2083 28  VAL B O   
1118 C CB  . VAL B 28  ? 1.3126 0.8741 0.9013 -0.0731 0.0189  -0.0734 28  VAL B CB  
1119 C CG1 . VAL B 28  ? 1.3355 0.8145 0.8813 -0.0507 -0.0068 0.0397  28  VAL B CG1 
1120 C CG2 . VAL B 28  ? 1.3234 0.9263 0.8023 -0.0950 0.0355  -0.1670 28  VAL B CG2 
1121 N N   . PHE B 29  ? 1.1531 0.9110 0.9366 0.0768  0.0719  0.0072  29  PHE B N   
1122 C CA  . PHE B 29  ? 1.0823 0.9997 0.7263 0.0329  0.0737  -0.0358 29  PHE B CA  
1123 C C   . PHE B 29  ? 1.0073 0.7436 0.6667 0.1292  -0.0844 -0.0973 29  PHE B C   
1124 O O   . PHE B 29  ? 1.0200 0.9259 0.5080 0.1589  -0.0317 -0.1945 29  PHE B O   
1125 C CB  . PHE B 29  ? 1.1797 1.0000 0.7801 0.0557  0.0988  0.0272  29  PHE B CB  
1126 C CG  . PHE B 29  ? 1.2333 1.1328 0.8394 0.0070  0.1695  0.0249  29  PHE B CG  
1127 C CD1 . PHE B 29  ? 1.2858 1.2711 0.7838 -0.0273 0.1922  -0.0092 29  PHE B CD1 
1128 C CD2 . PHE B 29  ? 1.2711 1.0614 0.8113 -0.0245 0.1865  0.0556  29  PHE B CD2 
1129 C CE1 . PHE B 29  ? 1.3644 1.3093 0.4811 -0.1690 0.2603  0.0883  29  PHE B CE1 
1130 C CE2 . PHE B 29  ? 1.3431 1.1024 0.6341 -0.1546 0.2836  0.1595  29  PHE B CE2 
1131 C CZ  . PHE B 29  ? 1.3805 1.2192 0.3946 -0.2251 0.3613  0.2270  29  PHE B CZ  
1132 N N   . LYS B 30  ? 0.8091 0.6730 0.3776 0.0294  -0.1901 -0.2251 30  LYS B N   
1133 C CA  . LYS B 30  ? 0.6806 0.5603 0.4021 -0.0060 -0.2360 -0.1580 30  LYS B CA  
1134 C C   . LYS B 30  ? 0.5732 0.4752 0.3878 -0.0367 -0.2225 -0.0985 30  LYS B C   
1135 O O   . LYS B 30  ? 0.6547 0.3658 0.3357 -0.0140 -0.2842 -0.0351 30  LYS B O   
1136 C CB  . LYS B 30  ? 0.7357 0.6217 0.4586 0.0287  -0.1805 -0.0936 30  LYS B CB  
1137 C CG  . LYS B 30  ? 0.7854 0.7103 0.5858 -0.0066 -0.0732 -0.0781 30  LYS B CG  
1138 C CD  . LYS B 30  ? 0.8607 0.7698 0.6650 -0.0630 -0.0604 -0.0480 30  LYS B CD  
1139 C CE  . LYS B 30  ? 0.9445 0.8400 0.6829 -0.0714 -0.0137 -0.0721 30  LYS B CE  
1140 N NZ  . LYS B 30  ? 0.9804 0.8802 0.7083 -0.1108 0.0138  -0.0775 30  LYS B NZ  
1141 N N   . ILE B 31  ? 0.5149 0.5195 0.4014 -0.0558 -0.2255 -0.0851 31  ILE B N   
1142 C CA  . ILE B 31  ? 0.5019 0.4527 0.3865 -0.0089 -0.1743 -0.0950 31  ILE B CA  
1143 C C   . ILE B 31  ? 0.4621 0.5044 0.4512 0.0068  -0.1477 -0.0342 31  ILE B C   
1144 O O   . ILE B 31  ? 0.4957 0.4757 0.5220 0.0100  -0.0920 -0.0463 31  ILE B O   
1145 C CB  . ILE B 31  ? 0.5566 0.4699 0.4222 -0.0066 -0.1266 -0.0616 31  ILE B CB  
1146 C CG1 . ILE B 31  ? 0.5895 0.4471 0.4149 -0.0119 -0.1222 -0.0857 31  ILE B CG1 
1147 C CG2 . ILE B 31  ? 0.5185 0.4587 0.4103 0.0065  -0.1405 -0.0382 31  ILE B CG2 
1148 C CD1 . ILE B 31  ? 0.6237 0.4957 0.4826 0.0007  -0.1515 -0.0379 31  ILE B CD1 
1149 N N   . ASN B 32  ? 0.3772 0.5105 0.4391 0.0253  -0.1816 -0.0268 32  ASN B N   
1150 C CA  . ASN B 32  ? 0.4328 0.4840 0.5209 0.0253  -0.1291 -0.0072 32  ASN B CA  
1151 C C   . ASN B 32  ? 0.3158 0.4355 0.5151 0.0457  -0.1331 0.0010  32  ASN B C   
1152 O O   . ASN B 32  ? 0.2937 0.5138 0.5733 0.1221  -0.1257 -0.0059 32  ASN B O   
1153 C CB  . ASN B 32  ? 0.4703 0.5342 0.5768 0.0206  -0.1321 0.0737  32  ASN B CB  
1154 C CG  . ASN B 32  ? 0.5100 0.6708 0.5749 -0.0217 -0.1411 0.0143  32  ASN B CG  
1155 O OD1 . ASN B 32  ? 0.4887 0.8703 0.6077 0.1004  -0.2419 0.1065  32  ASN B OD1 
1156 N ND2 . ASN B 32  ? 0.5915 0.7641 0.7328 -0.0381 -0.0405 0.0561  32  ASN B ND2 
1157 N N   . VAL B 33  ? 0.3480 0.3506 0.3984 0.0726  -0.1154 -0.0110 33  VAL B N   
1158 C CA  . VAL B 33  ? 0.3031 0.2902 0.3894 0.0757  -0.0996 -0.0060 33  VAL B CA  
1159 C C   . VAL B 33  ? 0.2697 0.2606 0.3170 0.0571  -0.0628 -0.0143 33  VAL B C   
1160 O O   . VAL B 33  ? 0.2685 0.2605 0.3355 0.0663  -0.0510 -0.0236 33  VAL B O   
1161 C CB  . VAL B 33  ? 0.4087 0.2793 0.4442 0.0782  -0.0996 -0.0045 33  VAL B CB  
1162 C CG1 . VAL B 33  ? 0.4579 0.2764 0.4531 0.0781  -0.0745 -0.0323 33  VAL B CG1 
1163 C CG2 . VAL B 33  ? 0.3951 0.2945 0.4758 0.0876  -0.0887 -0.0058 33  VAL B CG2 
1164 N N   . MET B 34  ? 0.2924 0.2653 0.2925 0.0431  -0.0452 -0.0348 34  MET B N   
1165 C CA  A MET B 34  ? 0.2667 0.2952 0.2741 0.0360  -0.0384 -0.0385 34  MET B CA  
1166 C CA  B MET B 34  ? 0.2758 0.2767 0.2799 0.0419  -0.0372 -0.0410 34  MET B CA  
1167 C C   . MET B 34  ? 0.2397 0.2913 0.2697 0.0060  -0.0456 -0.0330 34  MET B C   
1168 O O   . MET B 34  ? 0.2520 0.3346 0.3537 0.0319  -0.0171 -0.0582 34  MET B O   
1169 C CB  A MET B 34  ? 0.2807 0.3068 0.2864 0.0092  -0.0420 -0.0452 34  MET B CB  
1170 C CB  B MET B 34  ? 0.3064 0.2811 0.3027 0.0219  -0.0401 -0.0568 34  MET B CB  
1171 C CG  A MET B 34  ? 0.3032 0.3416 0.2994 0.0169  -0.0157 -0.0587 34  MET B CG  
1172 C CG  B MET B 34  ? 0.3451 0.2728 0.3228 0.0367  -0.0040 -0.0745 34  MET B CG  
1173 S SD  A MET B 34  ? 0.3682 0.3761 0.4274 -0.0412 -0.0138 -0.0629 34  MET B SD  
1174 S SD  B MET B 34  ? 0.4125 0.2911 0.4419 -0.0073 -0.0297 -0.1038 34  MET B SD  
1175 C CE  A MET B 34  ? 0.3609 0.3817 0.4133 -0.0593 -0.0205 -0.0945 34  MET B CE  
1176 C CE  B MET B 34  ? 0.4556 0.2098 0.4323 -0.0420 -0.0412 -0.0882 34  MET B CE  
1177 N N   . ALA B 35  ? 0.2025 0.2456 0.2587 0.0438  -0.0398 -0.0066 35  ALA B N   
1178 C CA  . ALA B 35  ? 0.2160 0.2565 0.2238 0.0446  -0.0305 0.0063  35  ALA B CA  
1179 C C   . ALA B 35  ? 0.2345 0.2319 0.2150 0.0737  -0.0241 -0.0002 35  ALA B C   
1180 O O   . ALA B 35  ? 0.2505 0.2603 0.2252 0.0901  -0.0120 0.0041  35  ALA B O   
1181 C CB  . ALA B 35  ? 0.2134 0.2658 0.2357 0.0468  -0.0415 0.0184  35  ALA B CB  
1182 N N   . TRP B 36  ? 0.2248 0.2100 0.1988 0.0755  -0.0010 0.0220  36  TRP B N   
1183 C CA  . TRP B 36  ? 0.2190 0.2048 0.2083 0.0376  -0.0051 0.0172  36  TRP B CA  
1184 C C   . TRP B 36  ? 0.2175 0.1908 0.1941 0.0381  -0.0028 0.0406  36  TRP B C   
1185 O O   . TRP B 36  ? 0.2340 0.2264 0.1901 0.0533  0.0073  0.0281  36  TRP B O   
1186 C CB  . TRP B 36  ? 0.2322 0.1945 0.2134 0.0553  0.0002  0.0262  36  TRP B CB  
1187 C CG  . TRP B 36  ? 0.2440 0.1942 0.2443 0.0411  -0.0167 0.0336  36  TRP B CG  
1188 C CD1 . TRP B 36  ? 0.2345 0.2040 0.2907 0.0406  -0.0128 0.0351  36  TRP B CD1 
1189 C CD2 . TRP B 36  ? 0.2254 0.2039 0.2385 0.0348  0.0006  0.0189  36  TRP B CD2 
1190 N NE1 . TRP B 36  ? 0.2430 0.2175 0.2974 0.0264  -0.0254 -0.0088 36  TRP B NE1 
1191 C CE2 . TRP B 36  ? 0.2483 0.2062 0.2372 0.0328  -0.0156 0.0174  36  TRP B CE2 
1192 C CE3 . TRP B 36  ? 0.2306 0.2291 0.2476 0.0458  0.0012  0.0215  36  TRP B CE3 
1193 C CZ2 . TRP B 36  ? 0.2436 0.2252 0.2684 0.0329  0.0110  0.0074  36  TRP B CZ2 
1194 C CZ3 . TRP B 36  ? 0.2563 0.2220 0.2312 0.0448  -0.0076 -0.0047 36  TRP B CZ3 
1195 C CH2 . TRP B 36  ? 0.2431 0.1979 0.2084 0.0605  -0.0106 0.0331  36  TRP B CH2 
1196 N N   . TYR B 37  ? 0.1999 0.1788 0.1995 0.0568  0.0171  0.0366  37  TYR B N   
1197 C CA  . TYR B 37  ? 0.1741 0.2143 0.2348 0.0487  0.0008  0.0144  37  TYR B CA  
1198 C C   . TYR B 37  ? 0.2082 0.2052 0.2157 0.0436  0.0007  0.0264  37  TYR B C   
1199 O O   . TYR B 37  ? 0.2025 0.2126 0.2380 0.0611  -0.0314 0.0108  37  TYR B O   
1200 C CB  . TYR B 37  ? 0.2151 0.2405 0.2154 0.0232  -0.0008 0.0094  37  TYR B CB  
1201 C CG  . TYR B 37  ? 0.2272 0.2454 0.2443 0.0333  -0.0100 0.0233  37  TYR B CG  
1202 C CD1 . TYR B 37  ? 0.2288 0.2516 0.2347 0.0320  0.0125  0.0132  37  TYR B CD1 
1203 C CD2 . TYR B 37  ? 0.2700 0.2635 0.2127 0.0705  -0.0214 0.0128  37  TYR B CD2 
1204 C CE1 . TYR B 37  ? 0.2487 0.3162 0.2690 0.0375  -0.0262 0.0047  37  TYR B CE1 
1205 C CE2 . TYR B 37  ? 0.3007 0.3031 0.2778 0.1001  -0.0656 0.0155  37  TYR B CE2 
1206 C CZ  . TYR B 37  ? 0.2678 0.3250 0.2764 0.0563  -0.0379 0.0099  37  TYR B CZ  
1207 O OH  . TYR B 37  ? 0.2887 0.4561 0.3171 0.1103  -0.0518 0.0318  37  TYR B OH  
1208 N N   . ARG B 38  ? 0.2117 0.1782 0.2456 0.0471  0.0281  0.0199  38  ARG B N   
1209 C CA  . ARG B 38  ? 0.2420 0.2149 0.2366 0.0345  0.0029  0.0023  38  ARG B CA  
1210 C C   . ARG B 38  ? 0.2648 0.2077 0.2354 0.0384  0.0173  -0.0019 38  ARG B C   
1211 O O   . ARG B 38  ? 0.2909 0.1993 0.2926 0.0270  -0.0532 0.0285  38  ARG B O   
1212 C CB  . ARG B 38  ? 0.2231 0.2344 0.2437 0.0292  0.0042  0.0092  38  ARG B CB  
1213 C CG  . ARG B 38  ? 0.2435 0.2749 0.2371 0.0357  0.0277  -0.0043 38  ARG B CG  
1214 C CD  . ARG B 38  ? 0.2508 0.2661 0.2380 0.0426  0.0264  0.0004  38  ARG B CD  
1215 N NE  . ARG B 38  ? 0.2810 0.2901 0.2757 0.0655  0.0365  -0.0122 38  ARG B NE  
1216 C CZ  . ARG B 38  ? 0.2746 0.2840 0.3202 0.0585  0.0708  -0.0258 38  ARG B CZ  
1217 N NH1 . ARG B 38  ? 0.2405 0.2653 0.2846 0.0849  0.0701  -0.0611 38  ARG B NH1 
1218 N NH2 . ARG B 38  ? 0.3253 0.2620 0.3882 0.0747  0.0868  -0.0187 38  ARG B NH2 
1219 N N   . GLN B 39  ? 0.2677 0.2396 0.2611 0.0613  0.0133  0.0130  39  GLN B N   
1220 C CA  . GLN B 39  ? 0.3367 0.2239 0.2843 0.0287  0.0028  0.0103  39  GLN B CA  
1221 C C   . GLN B 39  ? 0.3842 0.2529 0.3007 0.0248  -0.0205 0.0186  39  GLN B C   
1222 O O   . GLN B 39  ? 0.2952 0.1995 0.3158 -0.0398 -0.0314 0.0247  39  GLN B O   
1223 C CB  . GLN B 39  ? 0.3505 0.2632 0.3115 0.0226  0.0253  -0.0077 39  GLN B CB  
1224 C CG  . GLN B 39  ? 0.3648 0.2718 0.3729 0.0004  0.0058  0.0243  39  GLN B CG  
1225 C CD  . GLN B 39  ? 0.4390 0.3212 0.4298 -0.0454 0.0575  0.0426  39  GLN B CD  
1226 O OE1 . GLN B 39  ? 0.4865 0.4168 0.5679 0.0240  0.1191  -0.0023 39  GLN B OE1 
1227 N NE2 . GLN B 39  ? 0.5091 0.3175 0.5459 -0.0020 0.0527  0.0880  39  GLN B NE2 
1228 N N   . ALA B 40  ? 0.4787 0.2377 0.3389 0.0497  -0.0260 0.0020  40  ALA B N   
1229 C CA  . ALA B 40  ? 0.5499 0.3038 0.3504 0.0199  -0.0586 0.0049  40  ALA B CA  
1230 C C   . ALA B 40  ? 0.5808 0.3724 0.3938 -0.0081 -0.1016 -0.0130 40  ALA B C   
1231 O O   . ALA B 40  ? 0.5637 0.3805 0.3779 -0.0742 -0.1013 -0.0223 40  ALA B O   
1232 C CB  . ALA B 40  ? 0.5474 0.3681 0.3810 -0.0024 -0.0425 -0.0065 40  ALA B CB  
1233 N N   . PRO B 41  ? 0.7073 0.4147 0.4797 0.0268  -0.1949 0.0169  41  PRO B N   
1234 C CA  . PRO B 41  ? 0.7086 0.4468 0.5650 0.0106  -0.1700 -0.0045 41  PRO B CA  
1235 C C   . PRO B 41  ? 0.7023 0.4283 0.5287 -0.0238 -0.1620 -0.0395 41  PRO B C   
1236 O O   . PRO B 41  ? 0.6699 0.4191 0.6509 -0.0647 -0.1557 -0.1265 41  PRO B O   
1237 C CB  . PRO B 41  ? 0.7543 0.4489 0.5786 -0.0067 -0.1979 0.0085  41  PRO B CB  
1238 C CG  . PRO B 41  ? 0.7485 0.4388 0.6302 0.0357  -0.1866 0.0380  41  PRO B CG  
1239 C CD  . PRO B 41  ? 0.7850 0.4005 0.5041 0.0151  -0.1625 0.0212  41  PRO B CD  
1240 N N   . GLY B 42  ? 0.6306 0.3793 0.5846 -0.0693 -0.1865 -0.0660 42  GLY B N   
1241 C CA  . GLY B 42  ? 0.6613 0.3948 0.6232 -0.0303 -0.1396 -0.0406 42  GLY B CA  
1242 C C   . GLY B 42  ? 0.6406 0.3115 0.6033 -0.0131 -0.1060 -0.0454 42  GLY B C   
1243 O O   . GLY B 42  ? 0.6643 0.2663 0.7159 -0.1472 -0.1018 0.0462  42  GLY B O   
1244 N N   . LYS B 43  ? 0.5672 0.3157 0.6135 -0.0616 -0.1026 0.0428  43  LYS B N   
1245 C CA  . LYS B 43  ? 0.5366 0.3123 0.5508 -0.0181 -0.0488 0.0121  43  LYS B CA  
1246 C C   . LYS B 43  ? 0.4553 0.3167 0.5253 -0.0167 -0.0598 0.0228  43  LYS B C   
1247 O O   . LYS B 43  ? 0.3976 0.3315 0.4761 -0.0316 -0.1086 -0.0224 43  LYS B O   
1248 C CB  . LYS B 43  ? 0.5611 0.3380 0.6185 -0.0316 -0.0212 0.0059  43  LYS B CB  
1249 C CG  . LYS B 43  ? 0.5998 0.4403 0.6318 -0.0327 0.0013  -0.0055 43  LYS B CG  
1250 C CD  . LYS B 43  ? 0.6033 0.4396 0.6678 -0.0371 0.0159  -0.0054 43  LYS B CD  
1251 C CE  . LYS B 43  ? 0.6747 0.5319 0.6651 -0.0357 0.0128  -0.0232 43  LYS B CE  
1252 N NZ  . LYS B 43  ? 0.7103 0.6300 0.7448 -0.0081 0.0518  0.0030  43  LYS B NZ  
1253 N N   . GLY B 44  ? 0.4308 0.3224 0.4884 -0.0037 -0.0204 0.0165  44  GLY B N   
1254 C CA  . GLY B 44  ? 0.4081 0.3784 0.4329 -0.0053 -0.0372 0.0614  44  GLY B CA  
1255 C C   . GLY B 44  ? 0.3694 0.4014 0.3821 -0.0068 -0.0327 0.0557  44  GLY B C   
1256 O O   . GLY B 44  ? 0.3423 0.4175 0.3915 -0.0478 -0.0657 0.0875  44  GLY B O   
1257 N N   . ARG B 45  ? 0.3762 0.3868 0.3770 0.0150  -0.0071 0.0556  45  ARG B N   
1258 C CA  . ARG B 45  ? 0.3358 0.3701 0.3231 0.0297  -0.0215 0.0818  45  ARG B CA  
1259 C C   . ARG B 45  ? 0.3336 0.3260 0.3612 0.0170  0.0043  0.0823  45  ARG B C   
1260 O O   . ARG B 45  ? 0.4384 0.4657 0.4351 0.0407  0.0076  0.1946  45  ARG B O   
1261 C CB  . ARG B 45  ? 0.3646 0.4964 0.3237 0.0579  -0.0183 0.0608  45  ARG B CB  
1262 C CG  . ARG B 45  ? 0.4230 0.4834 0.3949 0.0857  -0.0141 0.0746  45  ARG B CG  
1263 C CD  . ARG B 45  ? 0.4454 0.4563 0.4183 0.0348  -0.0419 0.0359  45  ARG B CD  
1264 N NE  . ARG B 45  ? 0.4631 0.4956 0.5155 0.0369  -0.0096 0.0298  45  ARG B NE  
1265 C CZ  . ARG B 45  ? 0.5012 0.4141 0.5067 0.0439  -0.0428 0.0426  45  ARG B CZ  
1266 N NH1 . ARG B 45  ? 0.4890 0.3965 0.5426 0.0267  -0.0481 0.0245  45  ARG B NH1 
1267 N NH2 . ARG B 45  ? 0.4894 0.4329 0.5576 -0.0100 -0.0306 0.0660  45  ARG B NH2 
1268 N N   . GLU B 46  ? 0.2933 0.2103 0.2891 0.0329  -0.0199 0.0145  46  GLU B N   
1269 C CA  . GLU B 46  ? 0.2901 0.2366 0.2975 0.0462  -0.0269 -0.0015 46  GLU B CA  
1270 C C   . GLU B 46  ? 0.2585 0.2003 0.2498 0.0748  -0.0125 -0.0041 46  GLU B C   
1271 O O   . GLU B 46  ? 0.2339 0.1889 0.2598 0.0597  -0.0021 -0.0061 46  GLU B O   
1272 C CB  . GLU B 46  ? 0.3743 0.3161 0.3070 0.0484  -0.0040 -0.0410 46  GLU B CB  
1273 C CG  . GLU B 46  ? 0.4707 0.4026 0.4076 -0.0226 -0.0027 -0.0602 46  GLU B CG  
1274 C CD  . GLU B 46  ? 0.6120 0.4059 0.4177 -0.0327 0.0214  -0.0812 46  GLU B CD  
1275 O OE1 . GLU B 46  ? 0.5952 0.5945 0.4126 -0.0894 0.1540  -0.1030 46  GLU B OE1 
1276 O OE2 . GLU B 46  ? 0.7551 0.4260 0.5975 -0.1238 -0.0134 -0.0515 46  GLU B OE2 
1277 N N   . LEU B 47  ? 0.2444 0.1927 0.2497 0.0630  -0.0095 -0.0121 47  LEU B N   
1278 C CA  . LEU B 47  ? 0.2384 0.1959 0.2924 0.0520  -0.0019 -0.0037 47  LEU B CA  
1279 C C   . LEU B 47  ? 0.2714 0.2221 0.3038 0.0696  0.0429  -0.0213 47  LEU B C   
1280 O O   . LEU B 47  ? 0.3859 0.2181 0.3698 0.0379  0.1399  -0.0340 47  LEU B O   
1281 C CB  . LEU B 47  ? 0.2979 0.2463 0.3290 0.0653  -0.0463 0.0052  47  LEU B CB  
1282 C CG  . LEU B 47  ? 0.2948 0.2671 0.3498 0.0615  -0.0535 0.0039  47  LEU B CG  
1283 C CD1 . LEU B 47  ? 0.2900 0.2432 0.3503 0.0952  -0.0747 0.0210  47  LEU B CD1 
1284 C CD2 . LEU B 47  ? 0.3423 0.3096 0.4189 0.0833  -0.0911 0.0241  47  LEU B CD2 
1285 N N   . VAL B 48  ? 0.2386 0.2169 0.2834 0.0302  0.0368  -0.0104 48  VAL B N   
1286 C CA  . VAL B 48  ? 0.2638 0.2459 0.2867 0.0123  0.0406  -0.0088 48  VAL B CA  
1287 C C   . VAL B 48  ? 0.2525 0.2368 0.2610 0.0396  0.0416  -0.0237 48  VAL B C   
1288 O O   . VAL B 48  ? 0.2494 0.2469 0.2665 0.0343  0.0452  0.0135  48  VAL B O   
1289 C CB  . VAL B 48  ? 0.2920 0.2993 0.3180 0.0242  0.0002  0.0307  48  VAL B CB  
1290 C CG1 . VAL B 48  ? 0.3046 0.3478 0.3671 0.0456  0.0394  0.0635  48  VAL B CG1 
1291 C CG2 . VAL B 48  ? 0.2807 0.3246 0.3663 0.0366  0.0007  0.0640  48  VAL B CG2 
1292 N N   . ALA B 49  ? 0.2249 0.2466 0.2436 0.0261  0.0422  -0.0076 49  ALA B N   
1293 C CA  . ALA B 49  ? 0.2397 0.2409 0.2498 0.0337  0.0354  -0.0325 49  ALA B CA  
1294 C C   . ALA B 49  ? 0.2342 0.2371 0.2616 0.0293  0.0183  -0.0496 49  ALA B C   
1295 O O   . ALA B 49  ? 0.2127 0.2625 0.2778 0.0194  0.0208  -0.0201 49  ALA B O   
1296 C CB  . ALA B 49  ? 0.2205 0.2768 0.2555 0.0147  0.0365  -0.0064 49  ALA B CB  
1297 N N   . GLY B 50  ? 0.2413 0.2560 0.2994 0.0618  0.0091  0.0053  50  GLY B N   
1298 C CA  . GLY B 50  ? 0.2510 0.2319 0.3068 0.0422  0.0018  -0.0303 50  GLY B CA  
1299 C C   . GLY B 50  ? 0.2515 0.2587 0.3545 0.0359  -0.0114 -0.0135 50  GLY B C   
1300 O O   . GLY B 50  ? 0.2597 0.2570 0.3778 0.0348  0.0068  -0.0166 50  GLY B O   
1301 N N   . ILE B 51  ? 0.2711 0.2835 0.3603 0.0359  -0.0322 -0.0360 51  ILE B N   
1302 C CA  A ILE B 51  ? 0.2734 0.3396 0.4082 0.0069  -0.0291 -0.0551 51  ILE B CA  
1303 C CA  B ILE B 51  ? 0.2611 0.3288 0.4080 0.0136  -0.0200 -0.0527 51  ILE B CA  
1304 C C   . ILE B 51  ? 0.2800 0.3610 0.3995 0.0164  -0.0211 -0.0731 51  ILE B C   
1305 O O   . ILE B 51  ? 0.2405 0.3600 0.4302 0.0080  -0.0308 -0.0554 51  ILE B O   
1306 C CB  A ILE B 51  ? 0.3181 0.3395 0.4450 -0.0229 -0.0490 -0.0763 51  ILE B CB  
1307 C CB  B ILE B 51  ? 0.2910 0.3220 0.4313 0.0162  -0.0188 -0.0682 51  ILE B CB  
1308 C CG1 A ILE B 51  ? 0.3724 0.3358 0.4559 -0.0314 -0.0491 -0.0675 51  ILE B CG1 
1309 C CG1 B ILE B 51  ? 0.3014 0.3684 0.5231 -0.0138 -0.0288 -0.0685 51  ILE B CG1 
1310 C CG2 A ILE B 51  ? 0.3292 0.3886 0.4892 -0.0527 -0.0608 -0.0824 51  ILE B CG2 
1311 C CG2 B ILE B 51  ? 0.2849 0.2958 0.4535 0.0050  -0.0054 -0.0523 51  ILE B CG2 
1312 C CD1 A ILE B 51  ? 0.4288 0.3254 0.4582 -0.0322 -0.0798 -0.0944 51  ILE B CD1 
1313 C CD1 B ILE B 51  ? 0.3537 0.3928 0.5534 -0.0207 -0.0117 -0.0459 51  ILE B CD1 
1314 N N   . ILE B 52  ? 0.2665 0.4360 0.4332 0.0470  -0.0124 -0.0611 52  ILE B N   
1315 C CA  . ILE B 52  ? 0.3590 0.5233 0.3996 0.0032  0.0307  -0.0937 52  ILE B CA  
1316 C C   . ILE B 52  ? 0.4061 0.5517 0.4688 -0.0013 0.0206  -0.1290 52  ILE B C   
1317 O O   . ILE B 52  ? 0.5216 0.6757 0.4204 -0.0880 0.0616  -0.1668 52  ILE B O   
1318 C CB  . ILE B 52  ? 0.4519 0.5145 0.4395 0.0103  0.0155  -0.1010 52  ILE B CB  
1319 C CG1 . ILE B 52  ? 0.5141 0.5721 0.4144 -0.0174 -0.0002 -0.1266 52  ILE B CG1 
1320 C CG2 . ILE B 52  ? 0.4941 0.5701 0.4320 0.0297  0.0220  -0.1223 52  ILE B CG2 
1321 C CD1 . ILE B 52  ? 0.5468 0.5594 0.5258 0.0001  0.0011  -0.0871 52  ILE B CD1 
1322 N N   . SER B 53  ? 0.4150 0.6011 0.4666 0.1352  -0.0199 -0.1309 53  SER B N   
1323 C CA  . SER B 53  ? 0.5050 0.6389 0.5579 0.0982  -0.0533 -0.1553 53  SER B CA  
1324 C C   . SER B 53  ? 0.5130 0.7171 0.5997 0.0590  -0.1206 -0.1521 53  SER B C   
1325 O O   . SER B 53  ? 0.7121 0.7644 0.5400 0.1987  -0.2283 -0.2252 53  SER B O   
1326 C CB  . SER B 53  ? 0.5636 0.7029 0.5825 0.1419  -0.0173 -0.1638 53  SER B CB  
1327 O OG  . SER B 53  ? 0.5614 0.6953 0.6939 0.0955  -0.0156 -0.2631 53  SER B OG  
1328 N N   . GLY B 54  ? 0.6321 0.8041 0.6708 -0.0794 -0.0842 -0.1816 54  GLY B N   
1329 C CA  . GLY B 54  ? 0.6105 0.7495 0.7553 -0.1163 -0.1160 -0.1826 54  GLY B CA  
1330 C C   . GLY B 54  ? 0.6552 0.7997 0.7604 -0.1249 -0.1189 -0.1663 54  GLY B C   
1331 O O   . GLY B 54  ? 0.5384 0.8320 0.8619 -0.1455 -0.2915 -0.2609 54  GLY B O   
1332 N N   . GLY B 55  ? 0.6385 0.7349 0.8078 -0.1773 -0.1130 -0.1573 55  GLY B N   
1333 C CA  . GLY B 55  ? 0.5747 0.7301 0.8236 -0.1247 -0.0601 -0.1259 55  GLY B CA  
1334 C C   . GLY B 55  ? 0.4972 0.7044 0.7669 -0.0945 -0.0140 -0.0815 55  GLY B C   
1335 O O   . GLY B 55  ? 0.5282 0.6803 0.7530 -0.0738 0.0724  -0.0845 55  GLY B O   
1336 N N   . SER B 56  ? 0.4783 0.6460 0.9040 -0.0593 0.0159  -0.1067 56  SER B N   
1337 C CA  . SER B 56  ? 0.3065 0.6436 0.7768 0.0203  -0.0729 -0.0434 56  SER B CA  
1338 C C   . SER B 56  ? 0.3899 0.5246 0.6139 -0.0485 -0.0437 -0.1102 56  SER B C   
1339 O O   . SER B 56  ? 0.2913 0.6294 0.5897 -0.0198 -0.0993 -0.1571 56  SER B O   
1340 C CB  . SER B 56  ? 0.2859 0.6165 0.9389 0.1079  -0.1013 0.0207  56  SER B CB  
1341 O OG  . SER B 56  ? 0.4419 0.8116 0.8026 0.1208  -0.0497 0.0660  56  SER B OG  
1342 N N   . THR B 57  ? 0.3581 0.4428 0.6087 -0.0564 -0.0038 -0.0942 57  THR B N   
1343 C CA  . THR B 57  ? 0.3644 0.4651 0.5788 0.0137  0.0319  -0.0492 57  THR B CA  
1344 C C   . THR B 57  ? 0.2998 0.4861 0.4356 0.0256  0.0362  -0.0147 57  THR B C   
1345 O O   . THR B 57  ? 0.3842 0.5073 0.5328 0.1325  0.0475  -0.0052 57  THR B O   
1346 C CB  . THR B 57  ? 0.4258 0.4917 0.6582 -0.0173 0.0834  -0.0348 57  THR B CB  
1347 O OG1 . THR B 57  ? 0.4976 0.4306 0.8344 -0.0830 0.1452  -0.0769 57  THR B OG1 
1348 C CG2 . THR B 57  ? 0.4057 0.5749 0.6420 -0.0242 0.0848  -0.0358 57  THR B CG2 
1349 N N   . SER B 58  ? 0.2820 0.4071 0.3874 0.0856  0.0206  -0.0457 58  SER B N   
1350 C CA  . SER B 58  ? 0.3138 0.3852 0.3900 0.0776  -0.0168 -0.0313 58  SER B CA  
1351 C C   . SER B 58  ? 0.3025 0.3287 0.3272 0.0936  0.0192  -0.0526 58  SER B C   
1352 O O   . SER B 58  ? 0.3167 0.3049 0.2949 0.1074  0.0176  -0.0077 58  SER B O   
1353 C CB  . SER B 58  ? 0.4097 0.3256 0.4095 0.0208  0.0086  -0.0885 58  SER B CB  
1354 O OG  . SER B 58  ? 0.4606 0.4863 0.4654 0.0157  0.0602  -0.0078 58  SER B OG  
1355 N N   . TYR B 59  ? 0.2200 0.2752 0.2868 0.0587  0.0369  -0.0174 59  TYR B N   
1356 C CA  . TYR B 59  ? 0.2048 0.2798 0.2729 0.0385  0.0533  0.0151  59  TYR B CA  
1357 C C   . TYR B 59  ? 0.2353 0.2833 0.2710 0.0493  0.0401  0.0069  59  TYR B C   
1358 O O   . TYR B 59  ? 0.2373 0.2459 0.3272 0.0396  0.0280  0.0310  59  TYR B O   
1359 C CB  . TYR B 59  ? 0.1898 0.2890 0.2979 0.0132  0.0342  0.0223  59  TYR B CB  
1360 C CG  . TYR B 59  ? 0.1989 0.2760 0.3160 0.0225  0.0381  0.0285  59  TYR B CG  
1361 C CD1 . TYR B 59  ? 0.1950 0.3105 0.3033 0.0456  0.0226  0.0250  59  TYR B CD1 
1362 C CD2 . TYR B 59  ? 0.1597 0.2835 0.3314 0.0101  0.0193  0.0362  59  TYR B CD2 
1363 C CE1 . TYR B 59  ? 0.1835 0.3220 0.3638 0.0194  0.0170  0.0021  59  TYR B CE1 
1364 C CE2 . TYR B 59  ? 0.2107 0.2944 0.3497 0.0351  -0.0085 0.0141  59  TYR B CE2 
1365 C CZ  . TYR B 59  ? 0.2078 0.2936 0.3743 0.0152  0.0214  0.0077  59  TYR B CZ  
1366 O OH  . TYR B 59  ? 0.1862 0.2816 0.4182 0.0007  0.0378  0.0238  59  TYR B OH  
1367 N N   . ALA B 60  ? 0.2234 0.2610 0.2795 0.0680  0.0518  0.0076  60  ALA B N   
1368 C CA  . ALA B 60  ? 0.2849 0.2622 0.2313 0.0616  0.0435  0.0127  60  ALA B CA  
1369 C C   . ALA B 60  ? 0.2930 0.2483 0.2383 0.0456  0.0476  0.0054  60  ALA B C   
1370 O O   . ALA B 60  ? 0.2618 0.2465 0.2292 0.0456  0.0351  -0.0071 60  ALA B O   
1371 C CB  . ALA B 60  ? 0.2877 0.2823 0.2777 0.0369  0.0453  -0.0062 60  ALA B CB  
1372 N N   . ASP B 61  ? 0.2824 0.2176 0.1959 0.0661  0.0353  0.0514  61  ASP B N   
1373 C CA  . ASP B 61  ? 0.2875 0.2303 0.2094 0.0458  0.0429  0.0430  61  ASP B CA  
1374 C C   . ASP B 61  ? 0.2844 0.2108 0.2337 0.0702  0.0354  0.0375  61  ASP B C   
1375 O O   . ASP B 61  ? 0.3054 0.2257 0.2672 0.0834  0.0645  0.0558  61  ASP B O   
1376 C CB  . ASP B 61  ? 0.2753 0.2288 0.2233 0.0399  0.0464  0.0400  61  ASP B CB  
1377 C CG  . ASP B 61  ? 0.3029 0.2156 0.2632 0.0385  0.0285  0.0236  61  ASP B CG  
1378 O OD1 . ASP B 61  ? 0.3264 0.2270 0.2898 0.0370  0.0385  0.0412  61  ASP B OD1 
1379 O OD2 . ASP B 61  ? 0.2897 0.2793 0.2681 0.0548  0.0210  0.0159  61  ASP B OD2 
1380 N N   . SER B 62  ? 0.2906 0.2400 0.2407 0.0667  0.0074  0.0409  62  SER B N   
1381 C CA  . SER B 62  ? 0.2703 0.2713 0.2717 0.0861  -0.0063 0.0244  62  SER B CA  
1382 C C   . SER B 62  ? 0.2521 0.2783 0.2721 0.0643  0.0184  0.0148  62  SER B C   
1383 O O   . SER B 62  ? 0.3408 0.2554 0.2963 0.0848  0.0051  0.0240  62  SER B O   
1384 C CB  . SER B 62  ? 0.2973 0.2754 0.3031 0.0692  -0.0137 0.0413  62  SER B CB  
1385 O OG  . SER B 62  ? 0.2897 0.3115 0.3274 0.0882  0.0252  0.0352  62  SER B OG  
1386 N N   . VAL B 63  ? 0.2282 0.2217 0.2642 0.0718  0.0377  0.0185  63  VAL B N   
1387 C CA  . VAL B 63  ? 0.2673 0.2290 0.2938 0.0681  0.0463  0.0174  63  VAL B CA  
1388 C C   . VAL B 63  ? 0.2687 0.2523 0.3132 0.0693  0.0435  0.0337  63  VAL B C   
1389 O O   . VAL B 63  ? 0.2546 0.2458 0.3156 0.0793  0.0336  0.0247  63  VAL B O   
1390 C CB  . VAL B 63  ? 0.2758 0.1830 0.2675 0.0494  0.0494  0.0284  63  VAL B CB  
1391 C CG1 . VAL B 63  ? 0.2423 0.2114 0.2645 0.0847  0.0342  0.0526  63  VAL B CG1 
1392 C CG2 . VAL B 63  ? 0.2869 0.2066 0.2843 0.0469  0.0270  -0.0015 63  VAL B CG2 
1393 N N   . LYS B 64  ? 0.2936 0.2809 0.3761 0.0894  0.0366  0.0761  64  LYS B N   
1394 C CA  . LYS B 64  ? 0.3237 0.3351 0.4108 0.0236  0.0576  0.0747  64  LYS B CA  
1395 C C   . LYS B 64  ? 0.2961 0.3109 0.4034 0.0760  0.0629  0.0761  64  LYS B C   
1396 O O   . LYS B 64  ? 0.2837 0.4132 0.3726 0.0680  0.0920  0.0726  64  LYS B O   
1397 C CB  . LYS B 64  ? 0.3721 0.3603 0.4686 0.0532  0.0185  0.0927  64  LYS B CB  
1398 C CG  . LYS B 64  ? 0.4109 0.4441 0.5640 -0.0202 0.0106  0.0794  64  LYS B CG  
1399 C CD  . LYS B 64  ? 0.4417 0.5422 0.5532 -0.0313 0.0145  0.0554  64  LYS B CD  
1400 C CE  . LYS B 64  ? 0.4471 0.6083 0.6473 -0.0149 -0.0123 0.0589  64  LYS B CE  
1401 N NZ  . LYS B 64  ? 0.4655 0.5699 0.6537 -0.0937 0.0084  0.1085  64  LYS B NZ  
1402 N N   . GLY B 65  ? 0.3271 0.3368 0.4749 0.0374  0.0833  0.0821  65  GLY B N   
1403 C CA  . GLY B 65  ? 0.3749 0.3418 0.4647 0.0504  0.0738  0.1019  65  GLY B CA  
1404 C C   . GLY B 65  ? 0.3619 0.3531 0.4989 0.0360  0.0732  0.1376  65  GLY B C   
1405 O O   . GLY B 65  ? 0.3806 0.3976 0.5707 -0.0454 0.0513  0.1467  65  GLY B O   
1406 N N   . ARG B 66  ? 0.3461 0.3152 0.3556 0.0796  0.0817  0.0737  66  ARG B N   
1407 C CA  . ARG B 66  ? 0.3413 0.2956 0.3390 0.0625  0.0812  0.0745  66  ARG B CA  
1408 C C   . ARG B 66  ? 0.3326 0.3108 0.3546 0.0752  0.0828  0.0701  66  ARG B C   
1409 O O   . ARG B 66  ? 0.3411 0.2953 0.3924 0.0326  0.0959  0.1103  66  ARG B O   
1410 C CB  . ARG B 66  ? 0.3278 0.3323 0.3151 0.0716  0.0731  0.0648  66  ARG B CB  
1411 C CG  . ARG B 66  ? 0.3320 0.3727 0.3375 0.0978  0.0569  0.0270  66  ARG B CG  
1412 C CD  . ARG B 66  ? 0.3120 0.3561 0.2954 0.0931  0.0465  0.0652  66  ARG B CD  
1413 N NE  . ARG B 66  ? 0.2876 0.3676 0.2938 0.0748  0.0466  0.0462  66  ARG B NE  
1414 C CZ  . ARG B 66  ? 0.2943 0.3118 0.2840 0.0879  0.0569  0.0645  66  ARG B CZ  
1415 N NH1 . ARG B 66  ? 0.2461 0.2973 0.2831 0.0990  0.0704  0.0475  66  ARG B NH1 
1416 N NH2 . ARG B 66  ? 0.3154 0.2864 0.2961 0.0877  0.1096  0.0916  66  ARG B NH2 
1417 N N   . PHE B 67  ? 0.2946 0.2585 0.3631 0.0661  0.0802  0.0582  67  PHE B N   
1418 C CA  . PHE B 67  ? 0.2943 0.2472 0.3545 0.0679  0.0610  0.0420  67  PHE B CA  
1419 C C   . PHE B 67  ? 0.2496 0.2620 0.4107 0.0440  0.0716  0.0458  67  PHE B C   
1420 O O   . PHE B 67  ? 0.3272 0.3075 0.4373 0.1078  0.0647  0.0639  67  PHE B O   
1421 C CB  . PHE B 67  ? 0.2856 0.2467 0.3157 0.0485  0.0426  0.0148  67  PHE B CB  
1422 C CG  . PHE B 67  ? 0.2844 0.2485 0.2886 0.0486  0.0412  0.0350  67  PHE B CG  
1423 C CD1 . PHE B 67  ? 0.2812 0.3278 0.2605 0.0333  0.0447  -0.0073 67  PHE B CD1 
1424 C CD2 . PHE B 67  ? 0.2661 0.2297 0.2928 0.0461  0.0333  0.0102  67  PHE B CD2 
1425 C CE1 . PHE B 67  ? 0.2607 0.3008 0.2581 0.0588  0.0443  0.0196  67  PHE B CE1 
1426 C CE2 . PHE B 67  ? 0.2474 0.2357 0.2801 0.0477  0.0479  0.0221  67  PHE B CE2 
1427 C CZ  . PHE B 67  ? 0.2672 0.3066 0.2689 0.0378  0.0364  0.0096  67  PHE B CZ  
1428 N N   . THR B 68  ? 0.2503 0.2434 0.4004 0.0202  0.0362  0.0439  68  THR B N   
1429 C CA  . THR B 68  ? 0.2629 0.2630 0.4265 0.0361  0.0182  0.0385  68  THR B CA  
1430 C C   . THR B 68  ? 0.2820 0.2447 0.3915 0.0011  0.0142  0.0492  68  THR B C   
1431 O O   . THR B 68  ? 0.2586 0.2816 0.4309 0.0118  0.0207  0.0508  68  THR B O   
1432 C CB  . THR B 68  ? 0.3041 0.2804 0.4351 0.0073  0.0144  0.0507  68  THR B CB  
1433 O OG1 . THR B 68  ? 0.3408 0.3286 0.4606 -0.0068 0.0657  0.0751  68  THR B OG1 
1434 C CG2 . THR B 68  ? 0.3788 0.2904 0.4661 -0.0305 -0.0140 0.0419  68  THR B CG2 
1435 N N   . ILE B 69  ? 0.2653 0.2008 0.4164 -0.0083 -0.0009 0.0480  69  ILE B N   
1436 C CA  . ILE B 69  ? 0.2332 0.2662 0.4041 0.0013  -0.0320 0.0214  69  ILE B CA  
1437 C C   . ILE B 69  ? 0.2563 0.3058 0.4347 -0.0295 -0.0098 0.0022  69  ILE B C   
1438 O O   . ILE B 69  ? 0.2420 0.3405 0.4967 0.0346  -0.0459 0.0037  69  ILE B O   
1439 C CB  . ILE B 69  ? 0.2404 0.2689 0.3698 -0.0050 -0.0367 0.0144  69  ILE B CB  
1440 C CG1 . ILE B 69  ? 0.1997 0.2639 0.3526 0.0092  -0.0635 0.0273  69  ILE B CG1 
1441 C CG2 . ILE B 69  ? 0.2625 0.2776 0.3773 0.0092  -0.0488 0.0303  69  ILE B CG2 
1442 C CD1 . ILE B 69  ? 0.2123 0.2513 0.3939 0.0008  -0.0184 0.0107  69  ILE B CD1 
1443 N N   . SER B 70  ? 0.2982 0.2640 0.4223 -0.0474 0.0008  0.0143  70  SER B N   
1444 C CA  . SER B 70  ? 0.3308 0.2856 0.4539 -0.0391 -0.0322 -0.0046 70  SER B CA  
1445 C C   . SER B 70  ? 0.3475 0.2735 0.4474 -0.0624 -0.0451 -0.0423 70  SER B C   
1446 O O   . SER B 70  ? 0.3486 0.2514 0.4453 -0.0668 -0.0516 0.0211  70  SER B O   
1447 C CB  . SER B 70  ? 0.3182 0.2871 0.4509 -0.0057 -0.0306 0.0112  70  SER B CB  
1448 O OG  . SER B 70  ? 0.3325 0.3088 0.4211 -0.0104 -0.0460 0.0334  70  SER B OG  
1449 N N   . ARG B 71  ? 0.3273 0.3688 0.4964 -0.0765 -0.1048 -0.0531 71  ARG B N   
1450 C CA  . ARG B 71  ? 0.3598 0.3742 0.5076 -0.0809 -0.0868 -0.0667 71  ARG B CA  
1451 C C   . ARG B 71  ? 0.3781 0.3894 0.5424 -0.0946 -0.1087 -0.1022 71  ARG B C   
1452 O O   . ARG B 71  ? 0.4011 0.3318 0.5848 -0.1169 -0.0927 -0.1051 71  ARG B O   
1453 C CB  . ARG B 71  ? 0.4164 0.4535 0.5387 -0.0724 -0.0583 -0.0112 71  ARG B CB  
1454 C CG  . ARG B 71  ? 0.4311 0.5251 0.5866 -0.0392 -0.0925 -0.0506 71  ARG B CG  
1455 C CD  . ARG B 71  ? 0.4834 0.5128 0.6497 -0.0377 -0.0641 -0.0200 71  ARG B CD  
1456 N NE  . ARG B 71  ? 0.4749 0.5969 0.7037 -0.0536 -0.1181 -0.0347 71  ARG B NE  
1457 C CZ  . ARG B 71  ? 0.5838 0.6379 0.7505 0.0101  -0.0575 0.0071  71  ARG B CZ  
1458 N NH1 . ARG B 71  ? 0.7455 0.5801 0.7694 -0.0283 -0.0270 0.0002  71  ARG B NH1 
1459 N NH2 . ARG B 71  ? 0.6248 0.6941 0.8219 0.1043  -0.0662 0.0079  71  ARG B NH2 
1460 N N   . ASP B 72  ? 0.4125 0.4305 0.5581 -0.0938 -0.0867 -0.1260 72  ASP B N   
1461 C CA  . ASP B 72  ? 0.5767 0.4293 0.5741 -0.1130 -0.0664 -0.1401 72  ASP B CA  
1462 C C   . ASP B 72  ? 0.6294 0.5080 0.5792 -0.0670 -0.0810 -0.0514 72  ASP B C   
1463 O O   . ASP B 72  ? 0.6019 0.4539 0.4461 -0.1112 -0.1060 -0.1336 72  ASP B O   
1464 C CB  . ASP B 72  ? 0.6507 0.4454 0.5664 -0.1642 -0.1073 -0.0933 72  ASP B CB  
1465 C CG  . ASP B 72  ? 0.7694 0.4604 0.6448 -0.1678 -0.0589 -0.1570 72  ASP B CG  
1466 O OD1 . ASP B 72  ? 0.7609 0.6637 0.6868 -0.1299 -0.1131 -0.0659 72  ASP B OD1 
1467 O OD2 . ASP B 72  ? 0.8736 0.4585 0.6367 -0.1758 -0.0511 -0.1596 72  ASP B OD2 
1468 N N   . ASN B 73  ? 0.6536 0.6038 0.6357 -0.0667 -0.1390 -0.0444 73  ASN B N   
1469 C CA  . ASN B 73  ? 0.7305 0.6494 0.6397 -0.0142 -0.0456 -0.0979 73  ASN B CA  
1470 C C   . ASN B 73  ? 0.8187 0.6893 0.6808 -0.0598 0.0337  -0.1496 73  ASN B C   
1471 O O   . ASN B 73  ? 0.8888 0.7889 0.6057 -0.1132 0.0384  -0.2347 73  ASN B O   
1472 C CB  . ASN B 73  ? 0.7938 0.6907 0.6066 -0.0194 -0.0679 -0.0173 73  ASN B CB  
1473 C CG  . ASN B 73  ? 0.7132 0.7034 0.6644 -0.0233 -0.1133 -0.0399 73  ASN B CG  
1474 O OD1 . ASN B 73  ? 0.7719 0.8188 0.7650 0.0467  -0.2658 -0.0205 73  ASN B OD1 
1475 N ND2 . ASN B 73  ? 0.6853 0.5878 0.6748 0.0122  -0.1253 -0.0225 73  ASN B ND2 
1476 N N   . ALA B 74  ? 0.7818 0.7007 0.7216 -0.1099 0.0281  -0.1891 74  ALA B N   
1477 C CA  . ALA B 74  ? 0.8330 0.7150 0.7374 -0.1067 0.0255  -0.2232 74  ALA B CA  
1478 C C   . ALA B 74  ? 0.8401 0.6556 0.6965 -0.1083 0.0146  -0.2812 74  ALA B C   
1479 O O   . ALA B 74  ? 0.9228 0.6393 0.6854 -0.1715 0.0703  -0.2849 74  ALA B O   
1480 C CB  . ALA B 74  ? 0.8319 0.7678 0.7462 -0.1048 0.0931  -0.2415 74  ALA B CB  
1481 N N   . LYS B 75  ? 0.7575 0.6179 0.7020 -0.0418 -0.0099 -0.2608 75  LYS B N   
1482 C CA  . LYS B 75  ? 0.7932 0.5520 0.7149 -0.0220 -0.0362 -0.1745 75  LYS B CA  
1483 C C   . LYS B 75  ? 0.6680 0.5880 0.6476 -0.0116 -0.0566 -0.1466 75  LYS B C   
1484 O O   . LYS B 75  ? 0.6482 0.5658 0.7001 0.0469  -0.0260 -0.1149 75  LYS B O   
1485 C CB  . LYS B 75  ? 0.8925 0.6338 0.7532 0.0095  -0.0197 -0.1334 75  LYS B CB  
1486 C CG  . LYS B 75  ? 0.9276 0.6677 0.7929 -0.0656 -0.0271 -0.0756 75  LYS B CG  
1487 C CD  . LYS B 75  ? 0.9590 0.7800 0.7201 -0.0226 -0.0726 -0.0893 75  LYS B CD  
1488 C CE  . LYS B 75  ? 0.9713 0.7785 0.6590 -0.0064 -0.0481 -0.1000 75  LYS B CE  
1489 N NZ  . LYS B 75  ? 0.9615 0.7537 0.6934 -0.0212 -0.0609 -0.0730 75  LYS B NZ  
1490 N N   . ASN B 76  ? 0.5877 0.6078 0.5034 -0.1245 -0.0741 -0.0849 76  ASN B N   
1491 C CA  . ASN B 76  ? 0.5102 0.5586 0.4173 -0.0800 -0.0868 -0.1019 76  ASN B CA  
1492 C C   . ASN B 76  ? 0.4200 0.4470 0.3567 -0.0741 -0.0375 -0.0410 76  ASN B C   
1493 O O   . ASN B 76  ? 0.3633 0.4266 0.3477 -0.0016 -0.0268 -0.0028 76  ASN B O   
1494 C CB  . ASN B 76  ? 0.5063 0.5972 0.4534 -0.0735 -0.0631 -0.1096 76  ASN B CB  
1495 C CG  . ASN B 76  ? 0.5705 0.7243 0.4949 -0.0548 -0.1565 -0.0866 76  ASN B CG  
1496 O OD1 . ASN B 76  ? 0.6018 0.7147 0.7294 -0.0213 -0.1065 -0.1239 76  ASN B OD1 
1497 N ND2 . ASN B 76  ? 0.5493 0.7917 0.6981 0.0102  -0.0299 -0.0531 76  ASN B ND2 
1498 N N   . THR B 77  ? 0.3550 0.4066 0.3545 -0.0254 -0.0414 -0.0659 77  THR B N   
1499 C CA  . THR B 77  ? 0.3783 0.3583 0.3620 0.0107  -0.0586 -0.0646 77  THR B CA  
1500 C C   . THR B 77  ? 0.3700 0.2853 0.3484 -0.0017 -0.0632 -0.0186 77  THR B C   
1501 O O   . THR B 77  ? 0.3628 0.3166 0.3917 0.0138  -0.0158 -0.0449 77  THR B O   
1502 C CB  . THR B 77  ? 0.4828 0.3504 0.4046 0.0290  -0.0131 -0.0435 77  THR B CB  
1503 O OG1 . THR B 77  ? 0.5663 0.3722 0.4831 0.0983  -0.0090 -0.0409 77  THR B OG1 
1504 C CG2 . THR B 77  ? 0.4407 0.3524 0.4150 0.0582  -0.0416 -0.0189 77  THR B CG2 
1505 N N   . LEU B 78  ? 0.3549 0.2386 0.3090 0.0207  -0.0540 -0.0066 78  LEU B N   
1506 C CA  . LEU B 78  ? 0.3105 0.2678 0.3100 0.0283  -0.0369 0.0057  78  LEU B CA  
1507 C C   . LEU B 78  ? 0.2966 0.1787 0.2966 0.0357  -0.0109 -0.0014 78  LEU B C   
1508 O O   . LEU B 78  ? 0.2952 0.2294 0.3348 0.0407  -0.0393 -0.0462 78  LEU B O   
1509 C CB  . LEU B 78  ? 0.2851 0.2772 0.2999 0.0115  -0.0494 0.0147  78  LEU B CB  
1510 C CG  . LEU B 78  ? 0.3073 0.2543 0.2791 -0.0027 -0.0322 0.0309  78  LEU B CG  
1511 C CD1 . LEU B 78  ? 0.2954 0.2501 0.3361 -0.0087 0.0274  0.0410  78  LEU B CD1 
1512 C CD2 . LEU B 78  ? 0.3078 0.2825 0.3020 -0.0119 0.0010  0.0419  78  LEU B CD2 
1513 N N   . TYR B 79  ? 0.2447 0.1762 0.3239 0.0141  -0.0194 0.0008  79  TYR B N   
1514 C CA  . TYR B 79  ? 0.2636 0.1987 0.3197 0.0175  -0.0352 0.0021  79  TYR B CA  
1515 C C   . TYR B 79  ? 0.2547 0.1865 0.3342 0.0036  -0.0203 0.0107  79  TYR B C   
1516 O O   . TYR B 79  ? 0.2719 0.2004 0.3211 0.0169  -0.0287 0.0161  79  TYR B O   
1517 C CB  . TYR B 79  ? 0.3096 0.2065 0.3359 0.0010  -0.0479 0.0165  79  TYR B CB  
1518 C CG  . TYR B 79  ? 0.3726 0.2247 0.3314 -0.0040 -0.0363 -0.0040 79  TYR B CG  
1519 C CD1 . TYR B 79  ? 0.4052 0.2282 0.3850 0.0077  -0.0582 -0.0052 79  TYR B CD1 
1520 C CD2 . TYR B 79  ? 0.3944 0.2808 0.3793 -0.0033 -0.0677 -0.0102 79  TYR B CD2 
1521 C CE1 . TYR B 79  ? 0.4272 0.2379 0.4002 0.0450  -0.0466 -0.0081 79  TYR B CE1 
1522 C CE2 . TYR B 79  ? 0.4189 0.2760 0.4172 0.0190  -0.0492 -0.0115 79  TYR B CE2 
1523 C CZ  . TYR B 79  ? 0.4302 0.2170 0.4152 0.0006  -0.0404 0.0114  79  TYR B CZ  
1524 O OH  . TYR B 79  ? 0.5400 0.3183 0.4481 -0.0250 -0.0349 -0.0958 79  TYR B OH  
1525 N N   . LEU B 80  ? 0.2436 0.2351 0.3035 0.0233  0.0058  0.0037  80  LEU B N   
1526 C CA  . LEU B 80  ? 0.2586 0.2544 0.2792 0.0209  -0.0095 -0.0065 80  LEU B CA  
1527 C C   . LEU B 80  ? 0.2652 0.1871 0.3185 0.0418  0.0130  0.0041  80  LEU B C   
1528 O O   . LEU B 80  ? 0.2773 0.2070 0.2971 0.0552  0.0179  0.0163  80  LEU B O   
1529 C CB  . LEU B 80  ? 0.2467 0.2423 0.2817 0.0370  -0.0018 -0.0006 80  LEU B CB  
1530 C CG  . LEU B 80  ? 0.2711 0.2447 0.2687 0.0301  -0.0066 -0.0077 80  LEU B CG  
1531 C CD1 . LEU B 80  ? 0.2673 0.2445 0.2731 0.0266  -0.0148 -0.0237 80  LEU B CD1 
1532 C CD2 . LEU B 80  ? 0.2853 0.2169 0.2660 0.0384  -0.0184 -0.0166 80  LEU B CD2 
1533 N N   . GLN B 81  ? 0.2793 0.2534 0.3524 0.0222  0.0264  0.0067  81  GLN B N   
1534 C CA  . GLN B 81  ? 0.2907 0.2762 0.3473 0.0390  0.0224  0.0242  81  GLN B CA  
1535 C C   . GLN B 81  ? 0.3022 0.2747 0.3458 0.0264  0.0191  0.0325  81  GLN B C   
1536 O O   . GLN B 81  ? 0.3146 0.2947 0.3587 0.0449  -0.0215 0.0195  81  GLN B O   
1537 C CB  . GLN B 81  ? 0.2883 0.2946 0.3789 0.0449  0.0099  0.0417  81  GLN B CB  
1538 C CG  . GLN B 81  ? 0.3409 0.3326 0.3702 0.0195  0.0187  0.0424  81  GLN B CG  
1539 C CD  . GLN B 81  ? 0.3338 0.3164 0.3984 0.0047  -0.0042 0.0286  81  GLN B CD  
1540 O OE1 . GLN B 81  ? 0.4483 0.2740 0.3908 0.0128  0.0201  0.0613  81  GLN B OE1 
1541 N NE2 . GLN B 81  ? 0.4155 0.2756 0.4057 -0.0028 -0.0475 0.0712  81  GLN B NE2 
1542 N N   . MET B 82  ? 0.3177 0.2564 0.3006 0.0400  0.0344  0.0547  82  MET B N   
1543 C CA  . MET B 82  ? 0.3273 0.2616 0.2812 0.0577  0.0697  0.0267  82  MET B CA  
1544 C C   . MET B 82  ? 0.3544 0.2645 0.2911 0.0605  0.0416  0.0545  82  MET B C   
1545 O O   . MET B 82  ? 0.3216 0.3158 0.2926 0.0740  0.0591  0.0609  82  MET B O   
1546 C CB  . MET B 82  ? 0.3448 0.2952 0.2964 0.0307  0.0407  0.0362  82  MET B CB  
1547 C CG  . MET B 82  ? 0.3524 0.3211 0.2878 0.0020  0.0497  0.0055  82  MET B CG  
1548 S SD  . MET B 82  ? 0.3620 0.3610 0.3685 -0.0396 0.0624  0.0161  82  MET B SD  
1549 C CE  . MET B 82  ? 0.3546 0.3266 0.3428 0.0686  0.0944  -0.0009 82  MET B CE  
1550 N N   . ASN B 83  ? 0.3285 0.2635 0.3259 0.0484  0.0349  0.0545  83  ASN B N   
1551 C CA  . ASN B 83  ? 0.3468 0.3144 0.3342 0.0624  0.0551  0.0642  83  ASN B CA  
1552 C C   . ASN B 83  ? 0.2950 0.3082 0.3156 0.0467  0.0442  0.0789  83  ASN B C   
1553 O O   . ASN B 83  ? 0.3143 0.3191 0.2881 0.0223  0.0672  0.0795  83  ASN B O   
1554 C CB  . ASN B 83  ? 0.3873 0.3084 0.4374 0.0146  0.0665  0.0726  83  ASN B CB  
1555 C CG  . ASN B 83  ? 0.4293 0.3238 0.3853 0.0179  0.0371  0.0925  83  ASN B CG  
1556 O OD1 . ASN B 83  ? 0.4372 0.3141 0.4942 0.0070  0.0993  0.1304  83  ASN B OD1 
1557 N ND2 . ASN B 83  ? 0.3854 0.3386 0.4860 0.0183  0.0667  0.0372  83  ASN B ND2 
1558 N N   . SER B 84  ? 0.3341 0.3152 0.3245 0.0483  0.0535  0.1135  84  SER B N   
1559 C CA  . SER B 84  ? 0.3801 0.3116 0.3586 0.0624  0.0507  0.0809  84  SER B CA  
1560 C C   . SER B 84  ? 0.3441 0.3250 0.3186 0.0910  0.0681  0.0464  84  SER B C   
1561 O O   . SER B 84  ? 0.3263 0.3396 0.2983 0.1142  0.0955  0.0316  84  SER B O   
1562 C CB  . SER B 84  ? 0.3957 0.3574 0.4500 0.0733  0.0757  0.0744  84  SER B CB  
1563 O OG  . SER B 84  ? 0.4890 0.4310 0.5299 -0.0061 0.0597  0.0706  84  SER B OG  
1564 N N   . LEU B 85  ? 0.3470 0.3180 0.3049 0.0874  0.0621  0.0325  85  LEU B N   
1565 C CA  . LEU B 85  ? 0.3319 0.2847 0.3036 0.1002  0.0434  0.0406  85  LEU B CA  
1566 C C   . LEU B 85  ? 0.3768 0.2966 0.2727 0.0817  0.0617  0.0488  85  LEU B C   
1567 O O   . LEU B 85  ? 0.3696 0.3202 0.2667 0.0447  0.0562  0.0518  85  LEU B O   
1568 C CB  . LEU B 85  ? 0.3506 0.2786 0.2814 0.0845  0.0664  0.0307  85  LEU B CB  
1569 C CG  . LEU B 85  ? 0.3540 0.2883 0.2683 0.0782  0.0312  0.0738  85  LEU B CG  
1570 C CD1 . LEU B 85  ? 0.3198 0.3276 0.3172 0.0757  0.0542  0.0619  85  LEU B CD1 
1571 C CD2 . LEU B 85  ? 0.3958 0.2960 0.2495 0.0564  0.0801  0.0534  85  LEU B CD2 
1572 N N   . ARG B 86  ? 0.3716 0.2996 0.2350 0.0941  0.0975  0.0528  86  ARG B N   
1573 C CA  . ARG B 86  ? 0.3572 0.3126 0.2792 0.0896  0.0356  0.0455  86  ARG B CA  
1574 C C   . ARG B 86  ? 0.3675 0.3039 0.2539 0.0731  0.0372  0.0098  86  ARG B C   
1575 O O   . ARG B 86  ? 0.3221 0.2998 0.2396 0.0625  0.0270  0.0303  86  ARG B O   
1576 C CB  . ARG B 86  ? 0.3966 0.2933 0.3438 0.0917  0.0374  0.0289  86  ARG B CB  
1577 C CG  . ARG B 86  ? 0.3906 0.3631 0.4290 0.0869  0.0118  0.0249  86  ARG B CG  
1578 C CD  . ARG B 86  ? 0.4175 0.4183 0.4840 0.1169  -0.0302 0.0517  86  ARG B CD  
1579 N NE  . ARG B 86  ? 0.4343 0.4586 0.5471 0.0669  -0.0235 0.0627  86  ARG B NE  
1580 C CZ  . ARG B 86  ? 0.4530 0.4523 0.5954 0.0729  -0.0258 0.0875  86  ARG B CZ  
1581 N NH1 . ARG B 86  ? 0.4903 0.4870 0.6008 0.0800  -0.0592 0.1508  86  ARG B NH1 
1582 N NH2 . ARG B 86  ? 0.4476 0.4831 0.5904 0.0825  -0.0002 0.0744  86  ARG B NH2 
1583 N N   . PRO B 87  ? 0.3960 0.3750 0.2042 0.0749  0.0288  0.0048  87  PRO B N   
1584 C CA  . PRO B 87  ? 0.4189 0.4070 0.2512 0.0548  0.0574  -0.0356 87  PRO B CA  
1585 C C   . PRO B 87  ? 0.3893 0.3843 0.2575 0.0560  0.0220  -0.0417 87  PRO B C   
1586 O O   . PRO B 87  ? 0.3512 0.4453 0.2802 0.0714  0.0066  -0.0504 87  PRO B O   
1587 C CB  . PRO B 87  ? 0.4340 0.4450 0.2705 0.0409  0.0083  -0.0286 87  PRO B CB  
1588 C CG  . PRO B 87  ? 0.4759 0.4752 0.2160 0.0540  0.0104  -0.0375 87  PRO B CG  
1589 C CD  . PRO B 87  ? 0.4413 0.4575 0.2138 0.0577  0.0413  -0.0242 87  PRO B CD  
1590 N N   . GLU B 88  ? 0.3858 0.3407 0.2243 0.0473  0.0769  -0.0526 88  GLU B N   
1591 C CA  . GLU B 88  ? 0.4123 0.3591 0.2721 0.0564  0.0427  -0.0278 88  GLU B CA  
1592 C C   . GLU B 88  ? 0.3528 0.3099 0.2661 0.0499  0.0695  -0.0197 88  GLU B C   
1593 O O   . GLU B 88  ? 0.3870 0.2617 0.3022 0.0390  0.0598  -0.0089 88  GLU B O   
1594 C CB  . GLU B 88  ? 0.4446 0.3648 0.3934 0.0702  0.0849  -0.0091 88  GLU B CB  
1595 C CG  . GLU B 88  ? 0.4447 0.4168 0.4966 0.0750  0.0730  0.0300  88  GLU B CG  
1596 C CD  . GLU B 88  ? 0.5381 0.4432 0.5537 0.0801  0.1476  0.0074  88  GLU B CD  
1597 O OE1 . GLU B 88  ? 0.5062 0.6555 0.7783 0.0729  0.2269  0.0045  88  GLU B OE1 
1598 O OE2 . GLU B 88  ? 0.6459 0.4469 0.7043 0.0564  0.1506  -0.0174 88  GLU B OE2 
1599 N N   . ASP B 89  ? 0.3299 0.3103 0.2195 0.0469  0.0322  -0.0053 89  ASP B N   
1600 C CA  . ASP B 89  ? 0.3014 0.2614 0.2262 0.0541  0.0374  0.0010  89  ASP B CA  
1601 C C   . ASP B 89  ? 0.2701 0.2663 0.2089 0.0311  0.0136  -0.0018 89  ASP B C   
1602 O O   . ASP B 89  ? 0.2701 0.2802 0.1956 0.0429  -0.0017 -0.0029 89  ASP B O   
1603 C CB  . ASP B 89  ? 0.2894 0.2284 0.2208 0.0806  0.0328  0.0222  89  ASP B CB  
1604 C CG  . ASP B 89  ? 0.2944 0.2671 0.2414 0.0759  0.0495  0.0438  89  ASP B CG  
1605 O OD1 . ASP B 89  ? 0.2942 0.2735 0.2448 0.1015  0.0216  0.0112  89  ASP B OD1 
1606 O OD2 . ASP B 89  ? 0.2631 0.3238 0.2630 0.0673  0.0933  0.0339  89  ASP B OD2 
1607 N N   . THR B 90  ? 0.2510 0.2837 0.2059 0.0347  0.0301  -0.0048 90  THR B N   
1608 C CA  . THR B 90  ? 0.2518 0.2408 0.2079 0.0550  0.0130  -0.0072 90  THR B CA  
1609 C C   . THR B 90  ? 0.2734 0.2563 0.1787 0.0495  -0.0044 -0.0157 90  THR B C   
1610 O O   . THR B 90  ? 0.3213 0.2545 0.1995 0.0146  0.0616  -0.0055 90  THR B O   
1611 C CB  . THR B 90  ? 0.2686 0.2591 0.2292 0.0397  -0.0097 -0.0050 90  THR B CB  
1612 O OG1 . THR B 90  ? 0.3053 0.2928 0.2150 0.0728  0.0172  0.0050  90  THR B OG1 
1613 C CG2 . THR B 90  ? 0.2674 0.2329 0.2047 0.0340  -0.0214 -0.0205 90  THR B CG2 
1614 N N   . ALA B 91  ? 0.2229 0.2141 0.1942 0.0394  0.0212  0.0064  91  ALA B N   
1615 C CA  . ALA B 91  ? 0.2158 0.2236 0.1844 0.0132  0.0031  0.0062  91  ALA B CA  
1616 C C   . ALA B 91  ? 0.1976 0.2194 0.1948 0.0417  -0.0019 0.0169  91  ALA B C   
1617 O O   . ALA B 91  ? 0.2120 0.2144 0.2054 0.0517  -0.0104 0.0098  91  ALA B O   
1618 C CB  . ALA B 91  ? 0.2185 0.2102 0.2226 0.0265  0.0212  0.0036  91  ALA B CB  
1619 N N   . VAL B 92  ? 0.2145 0.2193 0.1896 0.0109  -0.0037 0.0096  92  VAL B N   
1620 C CA  . VAL B 92  ? 0.2346 0.2398 0.1876 0.0370  -0.0028 0.0036  92  VAL B CA  
1621 C C   . VAL B 92  ? 0.2043 0.1943 0.1801 0.0315  0.0212  -0.0076 92  VAL B C   
1622 O O   . VAL B 92  ? 0.2383 0.1938 0.1922 0.0174  -0.0018 0.0020  92  VAL B O   
1623 C CB  . VAL B 92  ? 0.2313 0.2451 0.2004 0.0456  -0.0049 0.0267  92  VAL B CB  
1624 C CG1 . VAL B 92  ? 0.2256 0.2534 0.2138 0.0819  0.0120  0.0100  92  VAL B CG1 
1625 C CG2 . VAL B 92  ? 0.2476 0.3041 0.2097 0.0411  -0.0144 0.0133  92  VAL B CG2 
1626 N N   . TYR B 93  ? 0.2117 0.1945 0.1861 0.0341  -0.0053 -0.0092 93  TYR B N   
1627 C CA  . TYR B 93  ? 0.1973 0.2042 0.1601 0.0467  0.0152  -0.0100 93  TYR B CA  
1628 C C   . TYR B 93  ? 0.2338 0.1922 0.1620 0.0389  0.0167  -0.0119 93  TYR B C   
1629 O O   . TYR B 93  ? 0.2142 0.1997 0.1591 0.0413  0.0087  0.0026  93  TYR B O   
1630 C CB  . TYR B 93  ? 0.2109 0.1947 0.1703 0.0471  0.0146  -0.0001 93  TYR B CB  
1631 C CG  . TYR B 93  ? 0.2211 0.2164 0.1705 0.0526  0.0284  0.0041  93  TYR B CG  
1632 C CD1 . TYR B 93  ? 0.2152 0.2043 0.2119 0.0403  0.0158  -0.0078 93  TYR B CD1 
1633 C CD2 . TYR B 93  ? 0.2239 0.2624 0.1755 0.0558  0.0168  -0.0130 93  TYR B CD2 
1634 C CE1 . TYR B 93  ? 0.2329 0.2209 0.1915 0.0340  0.0134  0.0035  93  TYR B CE1 
1635 C CE2 . TYR B 93  ? 0.2361 0.2602 0.1756 0.0608  0.0283  0.0011  93  TYR B CE2 
1636 C CZ  . TYR B 93  ? 0.2291 0.2307 0.1907 0.0339  0.0264  0.0050  93  TYR B CZ  
1637 O OH  . TYR B 93  ? 0.2503 0.2553 0.1850 0.0665  0.0258  0.0137  93  TYR B OH  
1638 N N   . TYR B 94  ? 0.2052 0.1664 0.1943 0.0498  0.0084  -0.0136 94  TYR B N   
1639 C CA  . TYR B 94  ? 0.2201 0.1927 0.1972 0.0533  0.0270  -0.0152 94  TYR B CA  
1640 C C   . TYR B 94  ? 0.2351 0.2584 0.1833 0.0503  0.0066  -0.0170 94  TYR B C   
1641 O O   . TYR B 94  ? 0.2609 0.2382 0.2283 0.0557  0.0235  -0.0241 94  TYR B O   
1642 C CB  . TYR B 94  ? 0.2219 0.2260 0.1996 0.0302  0.0245  0.0000  94  TYR B CB  
1643 C CG  . TYR B 94  ? 0.2090 0.2219 0.2169 0.0436  0.0243  0.0244  94  TYR B CG  
1644 C CD1 . TYR B 94  ? 0.2165 0.2365 0.2036 0.0253  0.0115  0.0356  94  TYR B CD1 
1645 C CD2 . TYR B 94  ? 0.2212 0.2240 0.1821 0.0194  0.0282  0.0070  94  TYR B CD2 
1646 C CE1 . TYR B 94  ? 0.2051 0.2671 0.2342 0.0321  0.0070  0.0442  94  TYR B CE1 
1647 C CE2 . TYR B 94  ? 0.2204 0.2952 0.2323 0.0160  0.0231  0.0165  94  TYR B CE2 
1648 C CZ  . TYR B 94  ? 0.2169 0.2567 0.2572 0.0166  0.0165  0.0091  94  TYR B CZ  
1649 O OH  . TYR B 94  ? 0.2165 0.2836 0.3020 0.0374  -0.0146 0.0065  94  TYR B OH  
1650 N N   . CYS B 95  ? 0.2212 0.2277 0.2188 0.0673  0.0232  -0.0148 95  CYS B N   
1651 C CA  . CYS B 95  ? 0.2228 0.2460 0.2046 0.0583  0.0235  -0.0108 95  CYS B CA  
1652 C C   . CYS B 95  ? 0.2191 0.2346 0.2044 0.0773  -0.0099 0.0031  95  CYS B C   
1653 O O   . CYS B 95  ? 0.2002 0.2490 0.2146 0.0623  -0.0448 0.0009  95  CYS B O   
1654 C CB  . CYS B 95  ? 0.3140 0.2456 0.2599 0.0336  0.0138  0.0068  95  CYS B CB  
1655 S SG  . CYS B 95  ? 0.3637 0.2798 0.3136 0.0396  0.0403  -0.0206 95  CYS B SG  
1656 N N   . ALA B 96  ? 0.2175 0.2547 0.2001 0.0807  -0.0025 0.0256  96  ALA B N   
1657 C CA  . ALA B 96  ? 0.2594 0.2608 0.1920 0.0388  -0.0035 0.0197  96  ALA B CA  
1658 C C   . ALA B 96  ? 0.2493 0.2541 0.2302 0.0436  -0.0124 0.0170  96  ALA B C   
1659 O O   . ALA B 96  ? 0.2405 0.2612 0.2218 0.0791  -0.0196 0.0414  96  ALA B O   
1660 C CB  . ALA B 96  ? 0.2740 0.2589 0.2197 0.0524  -0.0027 0.0048  96  ALA B CB  
1661 N N   . PHE B 97  ? 0.2356 0.2721 0.2076 0.0472  -0.0424 0.0182  97  PHE B N   
1662 C CA  . PHE B 97  ? 0.2385 0.3007 0.2707 0.0411  -0.0686 0.0028  97  PHE B CA  
1663 C C   . PHE B 97  ? 0.2481 0.3104 0.2871 0.0208  -0.0654 0.0094  97  PHE B C   
1664 O O   . PHE B 97  ? 0.2369 0.2847 0.2443 0.0494  -0.0609 0.0334  97  PHE B O   
1665 C CB  . PHE B 97  ? 0.2632 0.3412 0.2592 0.0450  -0.0562 -0.0302 97  PHE B CB  
1666 C CG  . PHE B 97  ? 0.2693 0.3500 0.3002 0.0129  -0.0254 -0.0387 97  PHE B CG  
1667 C CD1 . PHE B 97  ? 0.2924 0.3470 0.2981 0.0410  -0.0166 -0.0263 97  PHE B CD1 
1668 C CD2 . PHE B 97  ? 0.3429 0.3717 0.3146 -0.0034 -0.0618 -0.0433 97  PHE B CD2 
1669 C CE1 . PHE B 97  ? 0.2761 0.3539 0.3320 0.0266  0.0064  -0.0407 97  PHE B CE1 
1670 C CE2 . PHE B 97  ? 0.4106 0.3789 0.3589 -0.0246 -0.0321 -0.0336 97  PHE B CE2 
1671 C CZ  . PHE B 97  ? 0.3784 0.3571 0.3592 -0.0063 -0.0192 -0.0363 97  PHE B CZ  
1672 N N   . ILE B 98  ? 0.2738 0.3356 0.3108 0.0663  -0.0630 -0.0271 98  ILE B N   
1673 C CA  . ILE B 98  ? 0.3442 0.3690 0.3366 0.0280  -0.0946 -0.0010 98  ILE B CA  
1674 C C   . ILE B 98  ? 0.3323 0.3263 0.3383 0.0386  -0.1235 0.0250  98  ILE B C   
1675 O O   . ILE B 98  ? 0.3436 0.4118 0.3295 0.0146  -0.0978 0.0598  98  ILE B O   
1676 C CB  . ILE B 98  ? 0.3841 0.4085 0.4566 0.0449  -0.1140 -0.0502 98  ILE B CB  
1677 C CG1 . ILE B 98  ? 0.4075 0.4018 0.5757 0.0220  -0.1366 -0.1060 98  ILE B CG1 
1678 C CG2 . ILE B 98  ? 0.3929 0.4193 0.5284 0.0380  -0.1625 -0.0013 98  ILE B CG2 
1679 C CD1 . ILE B 98  ? 0.4279 0.4528 0.6274 0.0705  -0.1153 -0.1009 98  ILE B CD1 
1680 N N   . THR B 99  ? 0.4203 0.3303 0.3096 0.0595  -0.1287 0.0310  99  THR B N   
1681 C CA  . THR B 99  ? 0.5183 0.3442 0.3281 0.0419  -0.1481 0.0141  99  THR B CA  
1682 C C   . THR B 99  ? 0.6400 0.3527 0.3760 0.0185  -0.1654 0.0449  99  THR B C   
1683 O O   . THR B 99  ? 0.6488 0.3563 0.3670 0.0168  -0.2316 0.0872  99  THR B O   
1684 C CB  . THR B 99  ? 0.5278 0.3943 0.3695 0.0722  -0.1219 0.0439  99  THR B CB  
1685 O OG1 . THR B 99  ? 0.5607 0.5410 0.3805 0.0795  -0.0751 0.0885  99  THR B OG1 
1686 C CG2 . THR B 99  ? 0.5639 0.4333 0.3887 0.1159  -0.1077 0.0556  99  THR B CG2 
1687 N N   . THR B 100 ? 0.6695 0.3640 0.4358 -0.0143 -0.1907 0.0209  100 THR B N   
1688 C CA  . THR B 100 ? 0.8174 0.4186 0.3857 0.0034  -0.1064 0.0301  100 THR B CA  
1689 C C   . THR B 100 ? 0.9163 0.4889 0.3898 -0.0625 -0.1449 -0.0042 100 THR B C   
1690 O O   . THR B 100 ? 0.9548 0.5675 0.3624 -0.1179 -0.0197 0.0469  100 THR B O   
1691 C CB  . THR B 100 ? 0.8435 0.4521 0.4361 0.0464  -0.1126 -0.0501 100 THR B CB  
1692 O OG1 . THR B 100 ? 0.8088 0.5265 0.5410 0.0395  -0.1304 -0.1433 100 THR B OG1 
1693 C CG2 . THR B 100 ? 0.9335 0.5251 0.4803 0.0746  -0.1096 -0.0068 100 THR B CG2 
1694 N N   . GLU B 101 ? 0.8306 0.4323 0.4977 0.0275  -0.1526 0.0935  101 GLU B N   
1695 C CA  . GLU B 101 ? 0.8736 0.5035 0.4795 0.0534  -0.2134 0.0857  101 GLU B CA  
1696 C C   . GLU B 101 ? 0.8963 0.4882 0.5637 0.0221  -0.2735 0.1275  101 GLU B C   
1697 O O   . GLU B 101 ? 0.9500 0.6161 0.5189 -0.0389 -0.2922 -0.0199 101 GLU B O   
1698 C CB  . GLU B 101 ? 0.8770 0.5208 0.5890 0.0333  -0.1718 0.1044  101 GLU B CB  
1699 C CG  . GLU B 101 ? 0.9585 0.5506 0.6696 0.0771  -0.0615 0.0152  101 GLU B CG  
1700 C CD  . GLU B 101 ? 0.8303 0.6720 0.8108 0.0393  -0.0754 -0.0265 101 GLU B CD  
1701 O OE1 . GLU B 101 ? 0.9199 0.7992 0.8791 -0.1002 -0.1334 -0.0302 101 GLU B OE1 
1702 O OE2 . GLU B 101 ? 0.8789 0.8216 0.8657 0.0587  -0.0490 -0.1605 101 GLU B OE2 
1703 N N   . SER B 102 ? 0.8060 0.4596 0.4667 -0.0476 -0.2682 0.0946  102 SER B N   
1704 C CA  . SER B 102 ? 0.6769 0.5033 0.5227 -0.0725 -0.2247 0.0698  102 SER B CA  
1705 C C   . SER B 102 ? 0.5489 0.4967 0.5679 -0.0473 -0.1922 0.1483  102 SER B C   
1706 O O   . SER B 102 ? 0.5520 0.4940 0.4390 -0.0859 -0.1110 0.1848  102 SER B O   
1707 C CB  . SER B 102 ? 0.7639 0.5175 0.4795 -0.1705 -0.2247 -0.0231 102 SER B CB  
1708 O OG  . SER B 102 ? 0.7518 0.5299 0.5569 -0.1578 -0.1356 -0.0025 102 SER B OG  
1709 N N   . ASP B 103 ? 0.4747 0.4142 0.6683 -0.1139 -0.1745 0.1155  103 ASP B N   
1710 C CA  . ASP B 103 ? 0.5224 0.4996 0.6481 -0.1113 -0.0783 0.1116  103 ASP B CA  
1711 C C   . ASP B 103 ? 0.3447 0.4569 0.4148 -0.0366 -0.0565 0.0776  103 ASP B C   
1712 O O   . ASP B 103 ? 0.3883 0.5106 0.4205 0.0181  0.0357  0.1138  103 ASP B O   
1713 C CB  . ASP B 103 ? 0.5166 0.6124 0.7601 -0.1324 -0.0679 0.1267  103 ASP B CB  
1714 C CG  . ASP B 103 ? 0.6591 0.6193 0.8131 -0.1914 -0.0821 0.0975  103 ASP B CG  
1715 O OD1 . ASP B 103 ? 0.7667 0.5999 0.8278 -0.2237 0.0538  0.1229  103 ASP B OD1 
1716 O OD2 . ASP B 103 ? 0.7491 0.5801 0.7904 -0.1190 -0.0782 0.0826  103 ASP B OD2 
1717 N N   . TYR B 104 ? 0.3840 0.3605 0.3079 -0.0217 -0.0833 0.0603  104 TYR B N   
1718 C CA  . TYR B 104 ? 0.3125 0.3473 0.2323 0.0132  -0.0469 0.0394  104 TYR B CA  
1719 C C   . TYR B 104 ? 0.3017 0.2623 0.2414 -0.0102 -0.0223 0.0302  104 TYR B C   
1720 O O   . TYR B 104 ? 0.2001 0.2687 0.1921 0.0116  -0.0154 0.0160  104 TYR B O   
1721 C CB  . TYR B 104 ? 0.2958 0.3587 0.2362 0.0584  -0.0378 -0.0031 104 TYR B CB  
1722 C CG  . TYR B 104 ? 0.2989 0.3133 0.3110 0.0502  -0.0638 0.0145  104 TYR B CG  
1723 C CD1 . TYR B 104 ? 0.3351 0.2754 0.3644 0.0383  -0.0723 -0.0058 104 TYR B CD1 
1724 C CD2 . TYR B 104 ? 0.3563 0.3570 0.4248 0.0127  -0.0918 0.0309  104 TYR B CD2 
1725 C CE1 . TYR B 104 ? 0.3420 0.2744 0.4354 0.0582  -0.0950 -0.0114 104 TYR B CE1 
1726 C CE2 . TYR B 104 ? 0.3562 0.3243 0.4160 0.0254  -0.0954 0.0524  104 TYR B CE2 
1727 C CZ  . TYR B 104 ? 0.3692 0.2772 0.4072 0.0276  -0.0579 0.0071  104 TYR B CZ  
1728 O OH  . TYR B 104 ? 0.3792 0.3723 0.4256 -0.0131 -0.0585 0.0102  104 TYR B OH  
1729 N N   . ASP B 105 ? 0.3416 0.2717 0.2673 0.0066  -0.0282 0.0371  105 ASP B N   
1730 C CA  . ASP B 105 ? 0.3407 0.2606 0.2946 0.0065  -0.0308 0.0030  105 ASP B CA  
1731 C C   . ASP B 105 ? 0.2815 0.2501 0.2809 0.0097  -0.0310 0.0205  105 ASP B C   
1732 O O   . ASP B 105 ? 0.2672 0.3073 0.2551 0.0152  -0.0549 0.0334  105 ASP B O   
1733 C CB  . ASP B 105 ? 0.3883 0.2972 0.3362 0.0532  -0.0374 -0.0151 105 ASP B CB  
1734 C CG  . ASP B 105 ? 0.5046 0.3337 0.4102 0.0411  0.0252  -0.0692 105 ASP B CG  
1735 O OD1 . ASP B 105 ? 0.6420 0.3878 0.4138 0.0004  0.0304  -0.0576 105 ASP B OD1 
1736 O OD2 . ASP B 105 ? 0.6178 0.3276 0.5180 0.0658  0.0008  -0.0529 105 ASP B OD2 
1737 N N   . LEU B 106 ? 0.2343 0.2808 0.2817 0.0387  -0.0336 0.0177  106 LEU B N   
1738 C CA  . LEU B 106 ? 0.2586 0.2721 0.2730 0.0380  -0.0206 0.0266  106 LEU B CA  
1739 C C   . LEU B 106 ? 0.2834 0.3042 0.2591 0.0778  -0.0295 0.0327  106 LEU B C   
1740 O O   . LEU B 106 ? 0.3291 0.2867 0.2279 0.0796  -0.0703 0.0367  106 LEU B O   
1741 C CB  . LEU B 106 ? 0.2474 0.3032 0.3035 0.0315  -0.0490 0.0516  106 LEU B CB  
1742 C CG  . LEU B 106 ? 0.2750 0.2971 0.2893 0.0198  -0.0213 0.0559  106 LEU B CG  
1743 C CD1 . LEU B 106 ? 0.3099 0.2898 0.2718 0.0009  -0.0354 0.0574  106 LEU B CD1 
1744 C CD2 . LEU B 106 ? 0.2971 0.3337 0.2646 0.0416  -0.0164 0.0606  106 LEU B CD2 
1745 N N   . GLY B 107 ? 0.2737 0.3285 0.2685 0.0998  -0.0060 0.0485  107 GLY B N   
1746 C CA  . GLY B 107 ? 0.3186 0.3709 0.2578 0.0929  -0.0219 0.0654  107 GLY B CA  
1747 C C   . GLY B 107 ? 0.3069 0.3632 0.2617 0.0760  -0.0205 0.0490  107 GLY B C   
1748 O O   . GLY B 107 ? 0.3270 0.3665 0.2989 0.0725  -0.0438 0.1034  107 GLY B O   
1749 N N   . ARG B 108 ? 0.3531 0.3955 0.2690 0.1001  -0.0472 0.0653  108 ARG B N   
1750 C CA  . ARG B 108 ? 0.3349 0.4056 0.2651 0.0816  -0.0328 0.0898  108 ARG B CA  
1751 C C   . ARG B 108 ? 0.3321 0.4084 0.2441 0.0447  -0.0361 0.0552  108 ARG B C   
1752 O O   . ARG B 108 ? 0.3286 0.3740 0.2875 0.0480  -0.0937 0.0736  108 ARG B O   
1753 C CB  . ARG B 108 ? 0.4580 0.4366 0.3411 0.1081  -0.0102 0.0445  108 ARG B CB  
1754 C CG  . ARG B 108 ? 0.4530 0.4259 0.3738 0.1359  0.0151  0.0821  108 ARG B CG  
1755 C CD  . ARG B 108 ? 0.4495 0.4844 0.4176 0.1169  -0.0020 0.0733  108 ARG B CD  
1756 N NE  . ARG B 108 ? 0.4547 0.5588 0.4544 0.1631  0.0391  0.1330  108 ARG B NE  
1757 C CZ  . ARG B 108 ? 0.5114 0.5101 0.4483 0.1661  0.0833  0.1633  108 ARG B CZ  
1758 N NH1 . ARG B 108 ? 0.4714 0.4630 0.4263 0.1176  0.0767  0.1461  108 ARG B NH1 
1759 N NH2 . ARG B 108 ? 0.5093 0.5287 0.4773 0.1783  0.1380  0.1471  108 ARG B NH2 
1760 N N   . ARG B 109 ? 0.3130 0.3166 0.2326 0.0799  -0.0328 0.0510  109 ARG B N   
1761 C CA  . ARG B 109 ? 0.2902 0.3122 0.2338 0.0804  -0.0407 0.0520  109 ARG B CA  
1762 C C   . ARG B 109 ? 0.2837 0.3322 0.2257 0.0946  -0.0277 0.0250  109 ARG B C   
1763 O O   . ARG B 109 ? 0.2978 0.3910 0.3530 0.0835  -0.0288 0.0721  109 ARG B O   
1764 C CB  . ARG B 109 ? 0.2964 0.3145 0.2570 0.0982  -0.0324 0.0377  109 ARG B CB  
1765 C CG  . ARG B 109 ? 0.3138 0.3281 0.2608 0.0818  -0.0546 0.0633  109 ARG B CG  
1766 C CD  . ARG B 109 ? 0.3626 0.4121 0.2706 0.0612  -0.0452 0.0128  109 ARG B CD  
1767 N NE  . ARG B 109 ? 0.3681 0.4171 0.3125 0.0480  -0.0665 0.0318  109 ARG B NE  
1768 C CZ  . ARG B 109 ? 0.3267 0.4388 0.2695 0.0305  -0.0616 0.0467  109 ARG B CZ  
1769 N NH1 . ARG B 109 ? 0.3265 0.4032 0.3281 0.0230  -0.0455 0.0460  109 ARG B NH1 
1770 N NH2 . ARG B 109 ? 0.3523 0.4281 0.2705 0.0459  -0.0334 0.0520  109 ARG B NH2 
1771 N N   . TYR B 110 ? 0.2693 0.3340 0.2116 0.1079  -0.0031 0.0074  110 TYR B N   
1772 C CA  . TYR B 110 ? 0.2756 0.3207 0.1871 0.0902  -0.0452 0.0192  110 TYR B CA  
1773 C C   . TYR B 110 ? 0.2266 0.2943 0.1901 0.0737  -0.0248 0.0184  110 TYR B C   
1774 O O   . TYR B 110 ? 0.2309 0.2903 0.1995 0.0617  -0.0120 0.0291  110 TYR B O   
1775 C CB  . TYR B 110 ? 0.3298 0.3298 0.1766 0.1023  -0.0488 0.0141  110 TYR B CB  
1776 C CG  . TYR B 110 ? 0.4034 0.3949 0.1781 0.1000  -0.0373 0.0294  110 TYR B CG  
1777 C CD1 . TYR B 110 ? 0.3992 0.4471 0.2275 0.1150  -0.0300 0.0432  110 TYR B CD1 
1778 C CD2 . TYR B 110 ? 0.3691 0.4174 0.2253 0.1137  -0.0244 0.0314  110 TYR B CD2 
1779 C CE1 . TYR B 110 ? 0.4716 0.5726 0.2306 0.1271  -0.0312 0.0445  110 TYR B CE1 
1780 C CE2 . TYR B 110 ? 0.4674 0.4915 0.2304 0.0944  -0.0468 0.0619  110 TYR B CE2 
1781 C CZ  . TYR B 110 ? 0.4776 0.5219 0.2318 0.1461  -0.0320 0.0535  110 TYR B CZ  
1782 O OH  . TYR B 110 ? 0.6521 0.6195 0.2152 0.1112  -0.1013 0.0493  110 TYR B OH  
1783 N N   . TRP B 111 ? 0.2198 0.3401 0.2141 0.1048  -0.0155 0.0186  111 TRP B N   
1784 C CA  . TRP B 111 ? 0.2118 0.2661 0.2035 0.0932  0.0077  0.0301  111 TRP B CA  
1785 C C   . TRP B 111 ? 0.2133 0.2597 0.1861 0.0827  0.0091  0.0346  111 TRP B C   
1786 O O   . TRP B 111 ? 0.2347 0.3080 0.1914 0.0978  0.0057  -0.0003 111 TRP B O   
1787 C CB  . TRP B 111 ? 0.2476 0.2830 0.1833 0.0606  0.0167  0.0285  111 TRP B CB  
1788 C CG  . TRP B 111 ? 0.2670 0.2823 0.2205 0.0585  0.0188  0.0139  111 TRP B CG  
1789 C CD1 . TRP B 111 ? 0.2975 0.2848 0.2540 0.0389  0.0011  0.0301  111 TRP B CD1 
1790 C CD2 . TRP B 111 ? 0.2260 0.2758 0.2103 0.0661  0.0181  0.0359  111 TRP B CD2 
1791 N NE1 . TRP B 111 ? 0.2923 0.2979 0.2526 0.0502  0.0331  0.0524  111 TRP B NE1 
1792 C CE2 . TRP B 111 ? 0.2602 0.2784 0.2334 0.0480  0.0133  0.0428  111 TRP B CE2 
1793 C CE3 . TRP B 111 ? 0.2719 0.2716 0.2235 0.0731  0.0300  0.0549  111 TRP B CE3 
1794 C CZ2 . TRP B 111 ? 0.3011 0.2794 0.2508 0.0735  0.0246  0.0546  111 TRP B CZ2 
1795 C CZ3 . TRP B 111 ? 0.2584 0.2956 0.2188 0.0745  0.0558  0.0664  111 TRP B CZ3 
1796 C CH2 . TRP B 111 ? 0.2720 0.2747 0.2496 0.0830  0.0418  0.0397  111 TRP B CH2 
1797 N N   . GLY B 112 ? 0.1884 0.2380 0.1836 0.0932  0.0190  0.0253  112 GLY B N   
1798 C CA  . GLY B 112 ? 0.2131 0.2235 0.1766 0.0929  0.0230  0.0214  112 GLY B CA  
1799 C C   . GLY B 112 ? 0.2033 0.2352 0.1863 0.0775  0.0383  0.0172  112 GLY B C   
1800 O O   . GLY B 112 ? 0.2036 0.2382 0.2327 0.0677  0.0074  0.0285  112 GLY B O   
1801 N N   . GLN B 113 ? 0.2116 0.2543 0.1756 0.0755  0.0236  0.0299  113 GLN B N   
1802 C CA  . GLN B 113 ? 0.2250 0.2451 0.2121 0.0604  0.0163  -0.0077 113 GLN B CA  
1803 C C   . GLN B 113 ? 0.1802 0.2371 0.1806 0.0543  0.0169  0.0177  113 GLN B C   
1804 O O   . GLN B 113 ? 0.2056 0.2538 0.1763 0.0405  0.0205  -0.0208 113 GLN B O   
1805 C CB  . GLN B 113 ? 0.2039 0.2601 0.2352 0.0705  -0.0029 -0.0204 113 GLN B CB  
1806 C CG  . GLN B 113 ? 0.2264 0.2735 0.2089 0.0703  -0.0141 -0.0338 113 GLN B CG  
1807 C CD  . GLN B 113 ? 0.2368 0.2978 0.2345 0.0567  -0.0203 0.0132  113 GLN B CD  
1808 O OE1 . GLN B 113 ? 0.2832 0.2794 0.2089 0.0767  -0.0253 0.0038  113 GLN B OE1 
1809 N NE2 . GLN B 113 ? 0.2032 0.3216 0.2006 0.0672  0.0039  -0.0081 113 GLN B NE2 
1810 N N   . GLY B 114 ? 0.1694 0.2675 0.1654 0.0646  0.0026  0.0144  114 GLY B N   
1811 C CA  . GLY B 114 ? 0.1642 0.2512 0.1862 0.0777  0.0153  -0.0040 114 GLY B CA  
1812 C C   . GLY B 114 ? 0.2004 0.2620 0.1767 0.0598  0.0195  0.0029  114 GLY B C   
1813 O O   . GLY B 114 ? 0.2300 0.3038 0.1617 0.0884  0.0388  -0.0005 114 GLY B O   
1814 N N   . THR B 115 ? 0.2188 0.2309 0.1872 0.0386  0.0289  0.0129  115 THR B N   
1815 C CA  . THR B 115 ? 0.2090 0.2536 0.1662 0.0527  -0.0094 -0.0112 115 THR B CA  
1816 C C   . THR B 115 ? 0.1967 0.2609 0.1735 0.0756  -0.0039 -0.0132 115 THR B C   
1817 O O   . THR B 115 ? 0.1845 0.2178 0.1841 0.0580  -0.0086 0.0117  115 THR B O   
1818 C CB  . THR B 115 ? 0.2410 0.2368 0.1931 0.0540  -0.0039 0.0069  115 THR B CB  
1819 O OG1 . THR B 115 ? 0.2679 0.2364 0.2196 0.0590  -0.0168 0.0124  115 THR B OG1 
1820 C CG2 . THR B 115 ? 0.2442 0.2697 0.2336 0.0476  -0.0028 0.0175  115 THR B CG2 
1821 N N   . LEU B 116 ? 0.2008 0.2013 0.1739 0.0607  -0.0138 -0.0093 116 LEU B N   
1822 C CA  . LEU B 116 ? 0.2129 0.2108 0.1711 0.0594  -0.0059 -0.0098 116 LEU B CA  
1823 C C   . LEU B 116 ? 0.2164 0.2070 0.1834 0.0352  -0.0215 -0.0199 116 LEU B C   
1824 O O   . LEU B 116 ? 0.2926 0.2149 0.1630 0.0186  0.0191  0.0159  116 LEU B O   
1825 C CB  . LEU B 116 ? 0.2225 0.2270 0.2144 0.0607  -0.0276 -0.0172 116 LEU B CB  
1826 C CG  . LEU B 116 ? 0.2470 0.2385 0.1912 0.0662  -0.0104 0.0020  116 LEU B CG  
1827 C CD1 . LEU B 116 ? 0.2238 0.2281 0.2206 0.0411  -0.0155 0.0094  116 LEU B CD1 
1828 C CD2 . LEU B 116 ? 0.2492 0.2803 0.2178 0.0830  -0.0117 0.0002  116 LEU B CD2 
1829 N N   . VAL B 117 ? 0.2066 0.1988 0.1666 0.0525  -0.0110 0.0217  117 VAL B N   
1830 C CA  . VAL B 117 ? 0.2476 0.2197 0.1905 0.0381  0.0145  0.0198  117 VAL B CA  
1831 C C   . VAL B 117 ? 0.2214 0.2134 0.2041 0.0526  0.0062  0.0118  117 VAL B C   
1832 O O   . VAL B 117 ? 0.2871 0.2180 0.1740 0.0482  0.0029  0.0258  117 VAL B O   
1833 C CB  . VAL B 117 ? 0.2380 0.2547 0.2080 0.0302  0.0231  0.0111  117 VAL B CB  
1834 C CG1 . VAL B 117 ? 0.2489 0.2913 0.2494 0.0237  0.0538  0.0256  117 VAL B CG1 
1835 C CG2 . VAL B 117 ? 0.2673 0.2442 0.2154 0.0254  0.0015  0.0215  117 VAL B CG2 
1836 N N   . THR B 118 ? 0.2557 0.2121 0.2091 0.0804  0.0084  0.0105  118 THR B N   
1837 C CA  . THR B 118 ? 0.2525 0.2536 0.1971 0.0494  0.0273  0.0124  118 THR B CA  
1838 C C   . THR B 118 ? 0.2478 0.2757 0.2025 0.0478  0.0329  0.0173  118 THR B C   
1839 O O   . THR B 118 ? 0.2319 0.2749 0.1934 0.0702  0.0348  0.0074  118 THR B O   
1840 C CB  . THR B 118 ? 0.2539 0.2864 0.2118 0.0542  0.0054  0.0040  118 THR B CB  
1841 O OG1 . THR B 118 ? 0.2677 0.3313 0.2667 0.0526  0.0042  -0.0459 118 THR B OG1 
1842 C CG2 . THR B 118 ? 0.2853 0.2845 0.2191 0.0594  0.0049  -0.0012 118 THR B CG2 
1843 N N   . VAL B 119 ? 0.2885 0.3246 0.2017 0.0666  0.0622  0.0139  119 VAL B N   
1844 C CA  . VAL B 119 ? 0.3032 0.3325 0.2297 0.0701  0.0769  0.0513  119 VAL B CA  
1845 C C   . VAL B 119 ? 0.3782 0.3910 0.2565 0.0894  0.0497  0.0201  119 VAL B C   
1846 O O   . VAL B 119 ? 0.3859 0.4441 0.2253 0.0141  0.0346  -0.0107 119 VAL B O   
1847 C CB  . VAL B 119 ? 0.2834 0.3286 0.2819 0.0605  0.1093  -0.0051 119 VAL B CB  
1848 C CG1 . VAL B 119 ? 0.3228 0.3502 0.3115 0.0481  0.1336  0.0122  119 VAL B CG1 
1849 C CG2 . VAL B 119 ? 0.3041 0.3287 0.3183 0.0466  0.0847  0.0118  119 VAL B CG2 
1850 N N   . SER B 120 ? 0.3734 0.5247 0.2511 0.1708  0.0492  0.0526  120 SER B N   
1851 C CA  . SER B 120 ? 0.4617 0.6348 0.3259 0.1079  0.0014  0.0275  120 SER B CA  
1852 C C   . SER B 120 ? 0.5634 0.6666 0.3777 0.1395  0.0185  -0.0030 120 SER B C   
1853 O O   . SER B 120 ? 0.5265 0.6676 0.2830 0.0702  0.0523  -0.0566 120 SER B O   
1854 C CB  . SER B 120 ? 0.4633 0.6290 0.4297 0.1502  0.0214  0.0394  120 SER B CB  
1855 O OG  . SER B 120 ? 0.4796 0.6495 0.4429 0.1333  -0.0296 0.1115  120 SER B OG  
1856 N N   . SER B 121 ? 0.6940 0.7323 0.4518 0.0371  0.0151  -0.0626 121 SER B N   
1857 C CA  . SER B 121 ? 0.6999 0.8131 0.5861 0.0369  0.1528  -0.0873 121 SER B CA  
1858 C C   . SER B 121 ? 0.7478 0.8585 0.6514 0.0102  0.0832  -0.0322 121 SER B C   
1859 O O   . SER B 121 ? 0.9647 0.9088 1.0027 -0.1297 0.1837  -0.1296 121 SER B O   
1860 C CB  . SER B 121 ? 0.7286 0.8442 0.4587 0.0232  0.1473  -0.1037 121 SER B CB  
1861 O OG  . SER B 121 ? 0.6664 0.9808 0.4886 0.0497  0.1581  -0.0471 121 SER B OG  
1862 S S   . SO4 C .   ? 0.4496 0.5190 0.3333 -0.0675 -0.0971 -0.0053 201 SO4 A S   
1863 O O1  . SO4 C .   ? 0.4131 0.4499 0.4963 -0.0179 -0.0745 0.0187  201 SO4 A O1  
1864 O O2  . SO4 C .   ? 0.4688 0.4554 0.3381 -0.0741 -0.1069 0.0008  201 SO4 A O2  
1865 O O3  . SO4 C .   ? 0.5716 0.4852 0.4745 -0.0309 -0.0982 -0.0213 201 SO4 A O3  
1866 O O4  . SO4 C .   ? 0.4612 0.4285 0.4684 -0.0605 -0.1024 -0.0438 201 SO4 A O4  
1867 S S   . SO4 D .   ? 0.4226 0.4542 0.3886 -0.0955 -0.0012 -0.0547 202 SO4 A S   
1868 O O1  . SO4 D .   ? 0.4384 0.4512 0.4585 -0.0618 0.0399  0.0302  202 SO4 A O1  
1869 O O2  . SO4 D .   ? 0.4046 0.3146 0.4518 -0.0381 0.0477  -0.0115 202 SO4 A O2  
1870 O O3  . SO4 D .   ? 0.3300 0.4863 0.4389 -0.0292 -0.0299 -0.0562 202 SO4 A O3  
1871 O O4  . SO4 D .   ? 0.6486 0.5391 0.4207 0.0039  -0.0496 -0.0852 202 SO4 A O4  
1872 C C1  . GOL E .   ? 0.4519 0.4098 0.3645 0.0125  0.0752  -0.0437 203 GOL A C1  
1873 O O1  . GOL E .   ? 0.5152 0.4090 0.3588 0.0946  0.0639  -0.0709 203 GOL A O1  
1874 C C2  . GOL E .   ? 0.4767 0.4011 0.2951 -0.0318 0.0739  -0.0185 203 GOL A C2  
1875 O O2  . GOL E .   ? 0.4515 0.4028 0.2759 -0.0763 0.0520  -0.0324 203 GOL A O2  
1876 C C3  . GOL E .   ? 0.4742 0.3851 0.2743 -0.0278 0.0493  -0.0348 203 GOL A C3  
1877 O O3  . GOL E .   ? 0.4709 0.3641 0.2486 -0.0983 0.0792  -0.0158 203 GOL A O3  
1878 O O   . HOH F .   ? 0.2114 0.5646 0.5115 0.0734  0.0024  -0.0918 301 HOH A O   
1879 O O   . HOH F .   ? 0.3061 0.3313 0.5331 0.1297  0.0257  -0.1242 302 HOH A O   
1880 O O   . HOH F .   ? 0.3403 0.3386 0.1684 0.0524  0.0156  0.0566  303 HOH A O   
1881 O O   . HOH F .   ? 0.3132 0.4195 0.3754 -0.1397 0.0807  -0.0691 304 HOH A O   
1882 O O   . HOH F .   ? 0.2914 0.4253 0.2549 -0.0005 0.0814  0.0412  305 HOH A O   
1883 O O   . HOH F .   ? 0.3773 0.6287 0.5424 -0.1725 0.0314  0.1483  306 HOH A O   
1884 O O   . HOH F .   ? 0.3123 0.6451 0.4243 0.2601  -0.0505 -0.1660 307 HOH A O   
1885 O O   . HOH F .   ? 0.3403 0.3996 0.3747 -0.0072 -0.0504 0.1186  308 HOH A O   
1886 O O   . HOH F .   ? 0.3515 0.5465 0.3941 -0.0728 0.0011  0.0224  309 HOH A O   
1887 O O   . HOH F .   ? 0.4239 0.5152 0.3839 0.0685  -0.1506 0.0420  310 HOH A O   
1888 O O   . HOH F .   ? 0.3629 0.2715 0.3076 -0.0246 0.1168  0.0169  311 HOH A O   
1889 O O   . HOH F .   ? 0.2362 0.3613 0.1919 0.0627  -0.0274 0.0266  312 HOH A O   
1890 O O   . HOH F .   ? 0.4426 0.2951 0.3047 0.0028  -0.0749 0.0179  313 HOH A O   
1891 O O   . HOH F .   ? 0.2061 0.5099 0.3257 0.0429  0.0139  -0.0147 314 HOH A O   
1892 O O   . HOH F .   ? 0.5776 0.5739 0.2995 -0.0132 0.1085  0.0510  315 HOH A O   
1893 O O   . HOH F .   ? 0.5301 0.5215 0.5657 0.0154  0.0510  -0.0099 316 HOH A O   
1894 O O   . HOH F .   ? 0.4589 0.3149 0.4606 0.0473  0.0685  0.0714  317 HOH A O   
1895 O O   . HOH F .   ? 0.5009 0.2762 0.3705 0.0188  -0.0805 -0.0228 318 HOH A O   
1896 O O   . HOH F .   ? 0.5769 0.5112 0.3709 -0.0943 -0.0094 -0.0259 319 HOH A O   
1897 O O   . HOH F .   ? 0.2225 0.4509 0.4659 0.0818  -0.0559 -0.0063 320 HOH A O   
1898 O O   . HOH F .   ? 0.2985 0.5897 0.2499 -0.0348 -0.0311 -0.0996 321 HOH A O   
1899 O O   . HOH F .   ? 0.6178 0.3383 0.6720 -0.1232 0.2264  -0.1172 322 HOH A O   
1900 O O   . HOH F .   ? 0.3204 0.3060 0.3683 0.0544  0.0079  -0.0273 323 HOH A O   
1901 O O   . HOH F .   ? 0.2940 0.4040 0.2359 0.0214  0.0803  0.0345  324 HOH A O   
1902 O O   . HOH F .   ? 0.3705 0.3474 0.5670 0.1067  -0.0068 -0.0572 325 HOH A O   
1903 O O   . HOH F .   ? 0.8391 0.4016 0.5065 -0.0486 0.0975  -0.0364 326 HOH A O   
1904 O O   . HOH F .   ? 0.3506 0.4323 0.1847 -0.0877 0.0246  0.0643  327 HOH A O   
1905 O O   . HOH F .   ? 0.1649 0.2999 0.2103 0.0733  0.0039  -0.0156 328 HOH A O   
1906 O O   . HOH F .   ? 0.2682 0.5466 0.4979 0.0739  0.0819  0.1546  329 HOH A O   
1907 O O   . HOH F .   ? 0.3141 0.4003 0.3413 -0.1093 -0.0563 -0.0579 330 HOH A O   
1908 O O   . HOH F .   ? 0.5013 0.5159 0.4043 0.1609  -0.1044 -0.1049 331 HOH A O   
1909 O O   . HOH F .   ? 0.5796 0.7249 0.2253 -0.0394 0.0269  0.0424  332 HOH A O   
1910 O O   . HOH F .   ? 0.5238 0.6733 0.6161 -0.0838 -0.2545 -0.0950 333 HOH A O   
1911 O O   . HOH F .   ? 0.1862 0.8164 0.5457 -0.0266 0.0453  -0.1236 334 HOH A O   
1912 O O   . HOH F .   ? 0.4007 0.7847 0.3421 0.1578  0.0711  0.1107  335 HOH A O   
1913 O O   . HOH F .   ? 0.1861 0.2692 0.2220 0.0627  -0.0009 0.0203  336 HOH A O   
1914 O O   . HOH F .   ? 0.5334 0.4838 0.3696 -0.0650 -0.0876 -0.0693 337 HOH A O   
1915 O O   . HOH F .   ? 0.3072 0.5450 0.4645 -0.0412 0.0685  -0.0818 338 HOH A O   
1916 O O   . HOH F .   ? 0.3025 0.4523 0.2965 0.0230  -0.0266 0.0661  339 HOH A O   
1917 O O   . HOH F .   ? 0.4124 0.6292 0.5489 -0.1760 -0.0572 -0.1255 340 HOH A O   
1918 O O   . HOH F .   ? 0.3105 0.7916 0.3890 0.0452  -0.0107 0.1278  341 HOH A O   
1919 O O   . HOH F .   ? 0.6239 0.3462 0.4635 0.0564  0.0930  0.0981  342 HOH A O   
1920 O O   . HOH F .   ? 0.2796 0.5492 0.3534 -0.0262 0.0807  -0.0334 343 HOH A O   
1921 O O   . HOH F .   ? 0.3252 0.3940 0.3171 -0.0258 -0.0571 -0.0626 344 HOH A O   
1922 O O   . HOH F .   ? 0.5659 0.3695 0.3505 -0.0474 -0.0473 -0.0587 345 HOH A O   
1923 O O   . HOH F .   ? 0.4642 0.4976 0.5372 0.0107  -0.0685 0.0133  346 HOH A O   
1924 O O   . HOH F .   ? 0.3285 0.3816 0.1826 -0.1177 0.0148  0.0477  347 HOH A O   
1925 O O   . HOH F .   ? 0.3693 0.7150 0.5162 0.0669  -0.1503 -0.0117 348 HOH A O   
1926 O O   . HOH F .   ? 0.2632 0.3145 0.2013 0.0538  -0.0249 0.0200  349 HOH A O   
1927 O O   . HOH F .   ? 0.2556 0.3496 0.4972 0.0812  0.0585  0.0660  350 HOH A O   
1928 O O   . HOH F .   ? 0.7284 0.5773 0.4308 0.2182  0.2535  0.0939  351 HOH A O   
1929 O O   . HOH F .   ? 0.5549 0.4487 0.5623 0.0763  -0.2864 -0.1156 352 HOH A O   
1930 O O   . HOH F .   ? 0.7226 0.4366 0.3751 -0.1727 -0.0042 -0.0578 353 HOH A O   
1931 O O   . HOH F .   ? 0.2617 0.4050 0.2915 0.0038  -0.1251 -0.0157 354 HOH A O   
1932 O O   . HOH F .   ? 0.3045 0.3496 0.3139 -0.0861 0.0254  -0.0336 355 HOH A O   
1933 O O   . HOH F .   ? 0.3634 0.3915 0.2364 -0.0248 -0.0346 -0.1103 356 HOH A O   
1934 O O   . HOH F .   ? 0.1966 0.4372 0.5300 -0.1249 -0.0414 0.2178  357 HOH A O   
1935 O O   . HOH F .   ? 0.6800 0.3176 0.4234 0.2356  0.0870  0.0927  358 HOH A O   
1936 O O   . HOH F .   ? 0.4872 0.4995 0.2562 -0.0305 -0.1323 -0.0108 359 HOH A O   
1937 O O   . HOH F .   ? 0.4677 0.4906 0.5025 0.1518  -0.1065 0.0514  360 HOH A O   
1938 O O   . HOH F .   ? 0.4696 0.5741 0.5475 -0.1910 -0.0245 0.0579  361 HOH A O   
1939 O O   . HOH F .   ? 0.4745 0.4373 0.3808 -0.0646 -0.0398 -0.1625 362 HOH A O   
1940 O O   . HOH F .   ? 0.5029 0.4561 0.3851 0.1278  0.0231  -0.0476 363 HOH A O   
1941 O O   . HOH F .   ? 0.4456 0.5690 0.5160 0.0769  -0.0635 0.0157  364 HOH A O   
1942 O O   . HOH F .   ? 0.4196 0.3200 0.2185 0.0586  -0.0452 -0.0340 365 HOH A O   
1943 O O   . HOH F .   ? 0.3412 0.6048 0.2900 0.0555  -0.0705 0.0550  366 HOH A O   
1944 O O   . HOH F .   ? 0.4868 0.2431 0.3035 -0.0399 -0.2003 0.1577  367 HOH A O   
1945 O O   . HOH F .   ? 0.2864 0.3270 0.2657 -0.0257 -0.0890 -0.0248 368 HOH A O   
1946 O O   . HOH F .   ? 0.5396 0.4829 0.5307 -0.1945 -0.0449 0.2935  369 HOH A O   
1947 O O   . HOH F .   ? 0.5292 0.7698 0.3832 0.1385  -0.0534 0.0334  370 HOH A O   
1948 O O   . HOH F .   ? 0.7477 0.3511 0.4266 -0.0461 0.0830  -0.1584 371 HOH A O   
1949 O O   . HOH F .   ? 0.7038 0.3961 0.3320 0.1997  -0.0863 0.0409  372 HOH A O   
1950 O O   . HOH F .   ? 0.7067 0.4417 0.4855 -0.2013 0.1007  0.0475  373 HOH A O   
1951 O O   . HOH F .   ? 0.6495 0.3914 0.5338 0.2225  -0.0685 -0.0766 374 HOH A O   
1952 O O   . HOH F .   ? 0.2431 0.5300 0.4377 -0.0419 -0.0361 0.1664  375 HOH A O   
1953 O O   . HOH F .   ? 0.2843 0.5055 0.5154 -0.2359 -0.1745 0.0765  376 HOH A O   
1954 O O   . HOH F .   ? 0.2177 0.4666 0.1740 0.1781  0.0539  -0.0024 377 HOH A O   
1955 O O   . HOH F .   ? 0.4961 0.7651 0.6073 -0.2093 -0.0213 0.1034  378 HOH A O   
1956 O O   . HOH F .   ? 0.3039 0.5147 0.5998 -0.0430 0.0437  -0.0957 379 HOH A O   
1957 O O   . HOH F .   ? 0.5846 0.3939 0.5659 0.1087  -0.0938 0.0062  380 HOH A O   
1958 O O   . HOH F .   ? 0.5682 0.6592 0.7289 0.2012  0.0087  0.1841  381 HOH A O   
1959 O O   . HOH F .   ? 0.1803 0.3130 0.4087 -0.0235 -0.0223 -0.0976 382 HOH A O   
1960 O O   . HOH F .   ? 0.3698 0.6249 0.3026 0.1876  0.0044  0.0056  383 HOH A O   
1961 O O   . HOH F .   ? 0.3000 0.4720 0.3357 0.1007  0.1071  0.0242  384 HOH A O   
1962 O O   . HOH F .   ? 0.4814 0.4807 0.5027 -0.1024 0.1101  -0.0410 385 HOH A O   
1963 O O   . HOH F .   ? 0.3675 0.5494 0.3574 0.0337  -0.0430 -0.0879 386 HOH A O   
1964 O O   . HOH F .   ? 0.3992 0.3345 0.2523 0.0881  -0.0951 0.0092  387 HOH A O   
1965 O O   . HOH F .   ? 0.4065 0.5437 0.4395 -0.0626 0.0460  0.0579  388 HOH A O   
1966 O O   . HOH F .   ? 0.5614 0.5190 0.3339 0.1050  -0.0130 -0.0280 389 HOH A O   
1967 O O   . HOH F .   ? 0.2568 0.3096 0.2647 -0.0526 -0.1281 -0.0688 390 HOH A O   
1968 O O   . HOH F .   ? 0.5718 0.5570 0.8674 0.0875  -0.0060 0.2294  391 HOH A O   
1969 O O   . HOH G .   ? 0.4077 0.6076 0.3475 0.1431  0.0976  -0.0166 201 HOH B O   
1970 O O   . HOH G .   ? 0.7064 0.6222 0.2941 0.2279  -0.0034 -0.0001 202 HOH B O   
1971 O O   . HOH G .   ? 0.3261 0.2672 0.3044 0.0372  0.0829  0.0453  203 HOH B O   
1972 O O   . HOH G .   ? 0.4575 0.5477 0.3091 -0.0369 0.0656  0.1056  204 HOH B O   
1973 O O   . HOH G .   ? 0.6614 0.2422 0.3358 0.0811  0.0744  -0.0475 205 HOH B O   
1974 O O   . HOH G .   ? 0.8431 0.2142 0.3279 0.1273  0.2070  0.0125  206 HOH B O   
1975 O O   . HOH G .   ? 0.3059 0.4107 0.6162 -0.0353 -0.0432 0.0378  207 HOH B O   
1976 O O   . HOH G .   ? 0.2283 0.5067 0.5949 -0.1002 -0.0034 -0.0105 208 HOH B O   
1977 O O   . HOH G .   ? 0.6032 0.4836 0.3680 0.0743  0.0433  0.1866  209 HOH B O   
1978 O O   . HOH G .   ? 0.5385 0.4590 0.3538 0.3097  -0.0060 -0.0367 210 HOH B O   
1979 O O   . HOH G .   ? 0.5133 0.4381 0.5134 0.0211  0.1817  0.0255  211 HOH B O   
1980 O O   . HOH G .   ? 0.4600 0.3062 0.3455 0.0445  0.0556  -0.0345 212 HOH B O   
1981 O O   . HOH G .   ? 0.4922 0.3097 0.3063 0.1380  -0.0654 -0.0667 213 HOH B O   
1982 O O   . HOH G .   ? 0.7053 0.4659 0.5844 0.0035  -0.0073 -0.0837 214 HOH B O   
1983 O O   . HOH G .   ? 0.4971 0.4458 0.5315 0.0271  0.1058  -0.1363 215 HOH B O   
1984 O O   . HOH G .   ? 0.2632 0.3720 0.3729 -0.0185 0.0068  -0.0564 216 HOH B O   
1985 O O   . HOH G .   ? 0.2928 0.2687 0.2696 0.0463  0.0369  0.0014  217 HOH B O   
1986 O O   . HOH G .   ? 0.3227 0.3926 0.4202 0.0168  0.0270  0.0542  218 HOH B O   
1987 O O   . HOH G .   ? 0.3629 0.3875 0.2425 0.0366  0.0121  0.0690  219 HOH B O   
1988 O O   . HOH G .   ? 0.3206 0.3130 0.6649 0.0283  -0.0603 -0.0131 220 HOH B O   
1989 O O   . HOH G .   ? 0.3274 0.4135 0.5269 0.1187  0.1882  0.1144  221 HOH B O   
1990 O O   . HOH G .   ? 0.6631 0.2708 0.4263 0.1112  -0.0145 -0.0453 222 HOH B O   
1991 O O   . HOH G .   ? 0.4781 0.3894 0.5003 0.1495  0.1551  0.1736  223 HOH B O   
1992 O O   . HOH G .   ? 0.4375 0.4206 0.4486 0.0356  0.0599  0.0711  224 HOH B O   
1993 O O   . HOH G .   ? 0.2986 0.2784 0.2187 0.0834  0.0137  0.0371  225 HOH B O   
1994 O O   B HOH G .   ? 0.2956 0.2440 0.2811 0.0270  -0.1396 -0.0773 226 HOH B O   
1995 O O   . HOH G .   ? 0.4639 0.5461 0.5579 -0.1014 0.1007  0.1615  227 HOH B O   
1996 O O   . HOH G .   ? 0.5836 0.3790 0.6364 -0.1021 0.1061  -0.0047 228 HOH B O   
1997 O O   . HOH G .   ? 0.4299 0.4704 0.6911 0.0140  -0.0504 -0.0437 229 HOH B O   
1998 O O   . HOH G .   ? 0.5179 0.2571 0.3264 0.0508  -0.0031 -0.0188 230 HOH B O   
1999 O O   . HOH G .   ? 0.2283 0.3903 0.3527 0.0706  -0.0620 -0.0842 231 HOH B O   
2000 O O   . HOH G .   ? 0.4887 0.4385 0.5742 -0.0423 0.0169  -0.0033 232 HOH B O   
2001 O O   . HOH G .   ? 0.4458 0.2551 0.3503 0.0977  0.0937  0.0268  233 HOH B O   
2002 O O   . HOH G .   ? 0.3443 0.3378 0.2599 0.0882  0.0568  -0.0291 234 HOH B O   
2003 O O   . HOH G .   ? 0.3941 0.6405 0.4714 0.1144  0.1401  -0.0914 235 HOH B O   
2004 O O   . HOH G .   ? 0.5047 0.5115 0.5530 0.1056  0.2252  0.0872  236 HOH B O   
2005 O O   . HOH G .   ? 0.3282 0.3946 0.3799 0.0668  0.0673  0.0356  237 HOH B O   
2006 O O   . HOH G .   ? 0.3104 0.3399 0.5040 0.0034  -0.0066 -0.1868 238 HOH B O   
2007 O O   . HOH G .   ? 0.9026 0.5334 0.6261 -0.2726 0.0290  -0.0200 239 HOH B O   
2008 O O   . HOH G .   ? 0.5654 0.2819 0.5168 -0.0791 0.0968  0.0598  240 HOH B O   
2009 O O   . HOH G .   ? 0.3850 0.5311 0.4786 0.0502  -0.0473 0.0900  241 HOH B O   
2010 O O   . HOH G .   ? 0.2233 0.3009 0.1926 0.0337  -0.0330 0.0277  242 HOH B O   
2011 O O   . HOH G .   ? 0.2608 0.4509 0.2508 0.1015  0.0316  0.0936  243 HOH B O   
2012 O O   . HOH G .   ? 0.3199 0.3472 0.4483 0.0652  -0.0179 0.0600  244 HOH B O   
2013 O O   . HOH G .   ? 0.7511 0.5289 0.2503 0.2920  -0.0474 -0.0655 245 HOH B O   
2014 O O   . HOH G .   ? 0.3923 0.4048 0.6937 -0.0556 0.0605  0.2206  246 HOH B O   
2015 O O   . HOH G .   ? 0.2866 0.2824 0.3254 0.0355  -0.0437 0.0378  247 HOH B O   
2016 O O   . HOH G .   ? 0.4328 0.2221 0.3174 0.0927  -0.0363 -0.0193 248 HOH B O   
2017 O O   . HOH G .   ? 0.3575 0.4700 0.4136 -0.0224 -0.0115 -0.0868 249 HOH B O   
2018 O O   . HOH G .   ? 0.3398 0.4590 0.2989 0.0431  -0.0327 -0.0498 250 HOH B O   
2019 O O   . HOH G .   ? 0.3119 0.4826 0.3168 0.0526  -0.0323 0.0914  251 HOH B O   
2020 O O   . HOH G .   ? 0.3741 0.3605 0.4117 0.0561  -0.0972 -0.1045 252 HOH B O   
2021 O O   . HOH G .   ? 0.5824 0.5011 0.5157 -0.1129 -0.1096 0.2283  253 HOH B O   
2022 O O   . HOH G .   ? 0.5543 0.2952 0.2708 0.0859  0.0388  -0.0142 254 HOH B O   
2023 O O   . HOH G .   ? 0.3163 0.3487 0.2262 0.0356  0.0377  -0.0245 255 HOH B O   
2024 O O   . HOH G .   ? 0.4389 0.4860 0.3364 0.0909  0.1456  -0.0539 256 HOH B O   
2025 O O   . HOH G .   ? 0.5768 0.1840 0.1386 0.0611  -0.0340 0.0096  257 HOH B O   
2026 O O   . HOH G .   ? 0.4798 0.3707 0.4397 0.0382  0.0707  -0.0910 258 HOH B O   
2027 O O   . HOH G .   ? 0.6028 0.3704 0.3866 -0.0186 -0.0669 0.0571  259 HOH B O   
2028 O O   A HOH G .   ? 0.3433 0.2682 0.5656 0.0849  0.1352  0.0136  260 HOH B O   
2029 O O   . HOH G .   ? 0.5552 0.3540 0.5307 -0.1224 0.0034  0.1490  261 HOH B O   
2030 O O   . HOH G .   ? 0.2534 0.4685 0.6095 0.0117  -0.0262 -0.0569 262 HOH B O   
2031 O O   . HOH G .   ? 0.3662 0.3445 0.4494 0.0455  -0.1024 0.0465  263 HOH B O   
2032 O O   . HOH G .   ? 0.4376 0.4152 0.6360 -0.0801 0.1517  0.1027  264 HOH B O   
2033 O O   . HOH G .   ? 0.7997 0.3010 0.4028 -0.1994 -0.0180 0.0166  265 HOH B O   
2034 O O   . HOH G .   ? 0.5415 0.3123 0.2638 0.1795  0.0363  0.1552  266 HOH B O   
2035 O O   . HOH G .   ? 0.8959 0.3496 1.0379 -0.0028 0.1628  0.2562  267 HOH B O   
2036 O O   . HOH G .   ? 0.3004 0.7402 0.6522 -0.1731 -0.1174 -0.3847 268 HOH B O   
2037 O O   . HOH G .   ? 0.4792 0.5511 0.5874 0.0579  -0.0248 0.0986  269 HOH B O   
2038 O O   . HOH G .   ? 0.6093 0.5959 0.4881 -0.0067 -0.0834 0.0830  270 HOH B O   
2039 O O   . HOH G .   ? 0.3529 0.6534 0.3116 0.1918  -0.1133 -0.0203 271 HOH B O   
2040 O O   . HOH G .   ? 0.7733 0.6119 0.6549 0.0883  0.2362  -0.1278 272 HOH B O   
2041 O O   . HOH G .   ? 0.5929 0.6465 0.7502 -0.0110 0.0587  0.0147  273 HOH B O   
2042 O O   . HOH G .   ? 0.3965 0.5260 0.4659 0.0018  -0.0116 0.0279  274 HOH B O   
2043 O O   . HOH G .   ? 0.4135 0.3194 0.7680 -0.0718 0.0414  -0.1709 275 HOH B O   
2044 O O   . HOH G .   ? 0.4176 0.7804 0.4586 0.0546  -0.0976 0.0732  276 HOH B O   
2045 O O   . HOH G .   ? 0.4153 0.4303 0.4266 0.0600  0.0846  -0.0136 277 HOH B O   
2046 O O   . HOH G .   ? 0.3480 0.3864 0.3496 0.1090  -0.0174 0.0829  278 HOH B O   
2047 O O   . HOH G .   ? 0.4337 0.6422 0.3485 0.0276  0.1210  0.0568  279 HOH B O   
2048 O O   . HOH G .   ? 0.2648 0.4767 0.4789 -0.1180 0.0796  -0.2168 280 HOH B O   
2049 O O   . HOH G .   ? 0.3220 0.3672 0.5082 0.1023  0.0014  0.1063  281 HOH B O   
2050 O O   . HOH G .   ? 0.9174 0.3678 0.6628 0.0050  0.0475  0.2478  282 HOH B O   
2051 O O   . HOH G .   ? 0.5067 0.3416 0.5798 0.0425  0.0161  -0.0077 283 HOH B O   
2052 O O   . HOH G .   ? 0.6832 0.3225 0.5271 -0.0130 -0.1731 -0.0295 284 HOH B O   
2053 O O   . HOH G .   ? 0.4527 0.5696 0.4572 0.0267  -0.1406 0.1618  285 HOH B O   
2054 O O   . HOH G .   ? 0.5000 0.5286 0.3910 0.1315  -0.1284 0.0409  286 HOH B O   
2055 O O   . HOH G .   ? 0.4831 0.5089 0.4257 0.1179  -0.0388 -0.1478 287 HOH B O   
2056 O O   . HOH G .   ? 0.6379 0.4811 0.5081 -0.0657 0.1214  -0.0292 288 HOH B O   
2057 O O   . HOH G .   ? 0.2632 0.2380 0.5296 -0.0498 0.0866  -0.0275 289 HOH B O   
2058 O O   . HOH G .   ? 0.3178 0.4926 0.6711 0.0128  0.1147  0.1433  290 HOH B O   
2059 O O   . HOH G .   ? 0.5483 0.5971 0.4711 0.0529  0.0508  -0.0533 291 HOH B O   
2060 O O   . HOH G .   ? 0.9536 0.4412 0.5462 0.0226  0.0359  -0.0555 292 HOH B O   
2061 O O   . HOH G .   ? 0.4356 0.5059 0.7541 -0.0362 -0.0083 0.1639  293 HOH B O   
2062 O O   . HOH G .   ? 0.3242 0.3876 0.2813 0.0627  0.0180  0.0696  294 HOH B O   
2063 O O   . HOH G .   ? 0.6060 0.3896 0.5238 -0.0262 0.1457  -0.1389 295 HOH B O   
2064 O O   . HOH G .   ? 0.3386 0.4935 0.4683 0.0088  0.0051  0.0738  296 HOH B O   
2065 O O   . HOH G .   ? 0.3688 0.3773 0.6948 0.0082  -0.0269 -0.1366 297 HOH B O   
# 
