data_7I58
# 
_entry.id   7I58 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   7I58         pdb_00007i58 10.2210/pdb7i58/pdb 
WWPDB D_1001408331 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-02 
_pdbx_audit_revision_history.part_number         ? 
# 
_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             ? 
# 
_pdbx_database_status.entry_id                        7I58 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2025-03-12 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frank.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lithgo, R.M.'        1  ? 
'Fairhead, M.'        2  ? 
'Koekemoer, L.'       3  ? 
'Balcomb, B.H.'       4  ? 
'Capkin, E.'          5  ? 
'Chandran, A.V.'      6  ? 
'Golding, M.'         7  ? 
'Godoy, A.S.'         8  ? 
'Aschenbrenner, J.C.' 9  ? 
'Marples, P.G.'       10 ? 
'Ni, X.'              11 ? 
'Thompson, W.'        12 ? 
'Tomlinson, C.W.E.'   13 ? 
'Wild, C.'            14 ? 
'Winokan, M.'         15 ? 
'Xavier, M.-A.E.'     16 ? 
'Kenton, N.'          17 ? 
'Tucker, J.'          18 ? 
'DiPoto, M.'          19 ? 
'Lee, A.'             20 ? 
'Fearon, D.'          21 ? 
'von Delft, F.'       22 ? 
# 
_citation.id                        primary 
_citation.title                     
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Lithgo, R.M.'        ? 1  
primary 'Fairhead, M.'        ? 2  
primary 'Koekemoer, L.'       ? 3  
primary 'Balcomb, B.H.'       ? 4  
primary 'Capkin, E.'          ? 5  
primary 'Chandran, A.V.'      ? 6  
primary 'Golding, M.'         ? 7  
primary 'Godoy, A.S.'         ? 8  
primary 'Aschenbrenner, J.C.' ? 9  
primary 'Marples, P.G.'       ? 10 
primary 'Ni, X.'              ? 11 
primary 'Thompson, W.'        ? 12 
primary 'Tomlinson, C.W.E.'   ? 13 
primary 'Wild, C.'            ? 14 
primary 'Winokan, M.'         ? 15 
primary 'Xavier, M.-A.E.'     ? 16 
primary 'Kenton, N.'          ? 17 
primary 'Tucker, J.'          ? 18 
primary 'DiPoto, M.'          ? 19 
primary 'Lee, A.'             ? 20 
primary 'Fearon, D.'          ? 21 
primary 'von Delft, F.'       ? 22 
# 
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 'Protease 2A'                                                                                         15892.732 
1   3.4.22.29 ? ? ? 
2 non-polymer syn '1-[(3R)-3-hydroxy-3-(1H-1,2,3-triazol-4-yl)pyrrolidin-1-yl]-2-[2-(methylsulfanyl)phenyl]ethan-1-one' 318.394   
1   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                                                            65.409    
1   ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                                                  78.133    
3   ?         ? ? ? 
5 water       nat water                                                                                                 18.015    
213 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'P2A,Picornain 2A,Protein 2A' 
# 
_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       
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '1-[(3R)-3-hydroxy-3-(1H-1,2,3-triazol-4-yl)pyrrolidin-1-yl]-2-[2-(methylsulfanyl)phenyl]ethan-1-one' A1B3P 
3 'ZINC ION'                                                                                            ZN    
4 'DIMETHYL SULFOXIDE'                                                                                  DMS   
5 water                                                                                                 HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   GLY n 
1 3   ALA n 
1 4   ILE n 
1 5   TYR n 
1 6   VAL n 
1 7   GLY n 
1 8   ASN n 
1 9   TYR n 
1 10  ARG n 
1 11  VAL n 
1 12  VAL n 
1 13  ASN n 
1 14  ARG n 
1 15  HIS n 
1 16  LEU n 
1 17  ALA n 
1 18  THR n 
1 19  HIS n 
1 20  ASN n 
1 21  ASP n 
1 22  TRP n 
1 23  ALA n 
1 24  ASN n 
1 25  LEU n 
1 26  VAL n 
1 27  TRP n 
1 28  GLU n 
1 29  ASP n 
1 30  SER n 
1 31  SER n 
1 32  ARG n 
1 33  ASP n 
1 34  LEU n 
1 35  LEU n 
1 36  VAL n 
1 37  SER n 
1 38  SER n 
1 39  THR n 
1 40  THR n 
1 41  ALA n 
1 42  GLN n 
1 43  GLY n 
1 44  CYS n 
1 45  ASP n 
1 46  THR n 
1 47  ILE n 
1 48  ALA n 
1 49  ARG n 
1 50  CYS n 
1 51  ASP n 
1 52  CYS n 
1 53  GLN n 
1 54  THR n 
1 55  GLY n 
1 56  VAL n 
1 57  TYR n 
1 58  TYR n 
1 59  CYS n 
1 60  SER n 
1 61  SER n 
1 62  ARG n 
1 63  ARG n 
1 64  LYS n 
1 65  HIS n 
1 66  TYR n 
1 67  PRO n 
1 68  VAL n 
1 69  SER n 
1 70  PHE n 
1 71  SER n 
1 72  LYS n 
1 73  PRO n 
1 74  SER n 
1 75  LEU n 
1 76  ILE n 
1 77  PHE n 
1 78  VAL n 
1 79  GLU n 
1 80  ALA n 
1 81  SER n 
1 82  GLU n 
1 83  TYR n 
1 84  TYR n 
1 85  PRO n 
1 86  ALA n 
1 87  ARG n 
1 88  TYR n 
1 89  GLN n 
1 90  SER n 
1 91  HIS n 
1 92  LEU n 
1 93  MET n 
1 94  LEU n 
1 95  ALA n 
1 96  VAL n 
1 97  GLY n 
1 98  HIS n 
1 99  SER n 
1 100 GLU n 
1 101 PRO n 
1 102 GLY n 
1 103 ASP n 
1 104 CYS n 
1 105 GLY n 
1 106 GLY n 
1 107 ILE n 
1 108 LEU n 
1 109 ARG n 
1 110 CYS n 
1 111 GLN n 
1 112 HIS n 
1 113 GLY n 
1 114 VAL n 
1 115 VAL n 
1 116 GLY n 
1 117 ILE n 
1 118 VAL n 
1 119 SER n 
1 120 THR n 
1 121 GLY n 
1 122 GLY n 
1 123 ASN n 
1 124 GLY n 
1 125 LEU n 
1 126 VAL n 
1 127 GLY n 
1 128 PHE n 
1 129 ALA n 
1 130 ASP n 
1 131 VAL n 
1 132 ARG n 
1 133 ASP n 
1 134 LEU n 
1 135 LEU n 
1 136 TRP n 
1 137 LEU n 
1 138 ASP n 
1 139 GLU n 
1 140 GLU n 
1 141 ALA n 
1 142 MET n 
1 143 GLU n 
1 144 GLN 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                   144 
_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      'Coxsackievirus A16' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     31704 
_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 
A1B3P non-polymer         . '1-[(3R)-3-hydroxy-3-(1H-1,2,3-triazol-4-yl)pyrrolidin-1-yl]-2-[2-(methylsulfanyl)phenyl]ethan-1-one' 
? 'C15 H18 N4 O2 S' 318.394 
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 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                                                  
? 'C2 H6 O S'       78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                                                             
? 'C5 H10 N2 O3'    146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                                       
? 'C5 H9 N O4'      147.129 
GLY   'peptide linking'   y GLYCINE                                                                                               
? 'C2 H5 N O2'      75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                                             
? 'C6 H10 N3 O2 1'  156.162 
HOH   non-polymer         . WATER                                                                                                 
? 'H2 O'            18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                                            
? 'C6 H13 N O2'     131.173 
LEU   'L-peptide linking' y LEUCINE                                                                                               
? 'C6 H13 N O2'     131.173 
LYS   'L-peptide linking' y LYSINE                                                                                                
? 'C6 H15 N2 O2 1'  147.195 
MET   'L-peptide linking' y METHIONINE                                                                                            
? 'C5 H11 N O2 S'   149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                                         
? 'C9 H11 N O2'     165.189 
PRO   'L-peptide linking' y PROLINE                                                                                               
? 'C5 H9 N O2'      115.130 
SER   'L-peptide linking' y SERINE                                                                                                
? 'C3 H7 N O3'      105.093 
THR   'L-peptide linking' y THREONINE                                                                                             
? 'C4 H9 N O3'      119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                                            
? 'C11 H12 N2 O2'   204.225 
TYR   'L-peptide linking' y TYROSINE                                                                                              
? 'C9 H11 N O3'     181.189 
VAL   'L-peptide linking' y VALINE                                                                                                
? 'C5 H11 N O2'     117.146 
ZN    non-polymer         . 'ZINC ION'                                                                                            
? 'Zn 2'            65.409  
# 
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   SER 1   7   7   SER SER A . n 
A 1 2   GLY 2   8   8   GLY GLY A . n 
A 1 3   ALA 3   9   9   ALA ALA A . n 
A 1 4   ILE 4   10  10  ILE ILE A . n 
A 1 5   TYR 5   11  11  TYR TYR A . n 
A 1 6   VAL 6   12  12  VAL VAL A . n 
A 1 7   GLY 7   13  13  GLY GLY A . n 
A 1 8   ASN 8   14  14  ASN ASN A . n 
A 1 9   TYR 9   15  15  TYR TYR A . n 
A 1 10  ARG 10  16  16  ARG ARG A . n 
A 1 11  VAL 11  17  17  VAL VAL A . n 
A 1 12  VAL 12  18  18  VAL VAL A . n 
A 1 13  ASN 13  19  19  ASN ASN A . n 
A 1 14  ARG 14  20  20  ARG ARG A . n 
A 1 15  HIS 15  21  21  HIS HIS A . n 
A 1 16  LEU 16  22  22  LEU LEU A . n 
A 1 17  ALA 17  23  23  ALA ALA A . n 
A 1 18  THR 18  24  24  THR THR A . n 
A 1 19  HIS 19  25  25  HIS HIS A . n 
A 1 20  ASN 20  26  26  ASN ASN A . n 
A 1 21  ASP 21  27  27  ASP ASP A . n 
A 1 22  TRP 22  28  28  TRP TRP A . n 
A 1 23  ALA 23  29  29  ALA ALA A . n 
A 1 24  ASN 24  30  30  ASN ASN A . n 
A 1 25  LEU 25  31  31  LEU LEU A . n 
A 1 26  VAL 26  32  32  VAL VAL A . n 
A 1 27  TRP 27  33  33  TRP TRP A . n 
A 1 28  GLU 28  34  34  GLU GLU A . n 
A 1 29  ASP 29  35  35  ASP ASP A . n 
A 1 30  SER 30  36  36  SER SER A . n 
A 1 31  SER 31  37  37  SER SER A . n 
A 1 32  ARG 32  38  38  ARG ARG A . n 
A 1 33  ASP 33  39  39  ASP ASP A . n 
A 1 34  LEU 34  40  40  LEU LEU A . n 
A 1 35  LEU 35  41  41  LEU LEU A . n 
A 1 36  VAL 36  42  42  VAL VAL A . n 
A 1 37  SER 37  43  43  SER SER A . n 
A 1 38  SER 38  44  44  SER SER A . n 
A 1 39  THR 39  45  45  THR THR A . n 
A 1 40  THR 40  46  46  THR THR A . n 
A 1 41  ALA 41  47  47  ALA ALA A . n 
A 1 42  GLN 42  48  48  GLN GLN A . n 
A 1 43  GLY 43  49  49  GLY GLY A . n 
A 1 44  CYS 44  50  50  CYS CYS A . n 
A 1 45  ASP 45  51  51  ASP ASP A . n 
A 1 46  THR 46  52  52  THR THR A . n 
A 1 47  ILE 47  53  53  ILE ILE A . n 
A 1 48  ALA 48  54  54  ALA ALA A . n 
A 1 49  ARG 49  55  55  ARG ARG A . n 
A 1 50  CYS 50  56  56  CYS CYS A . n 
A 1 51  ASP 51  57  57  ASP ASP A . n 
A 1 52  CYS 52  58  58  CYS CYS A . n 
A 1 53  GLN 53  59  59  GLN GLN A . n 
A 1 54  THR 54  60  60  THR THR A . n 
A 1 55  GLY 55  61  61  GLY GLY A . n 
A 1 56  VAL 56  62  62  VAL VAL A . n 
A 1 57  TYR 57  63  63  TYR TYR A . n 
A 1 58  TYR 58  64  64  TYR TYR A . n 
A 1 59  CYS 59  65  65  CYS CYS A . n 
A 1 60  SER 60  66  66  SER SER A . n 
A 1 61  SER 61  67  67  SER SER A . n 
A 1 62  ARG 62  68  68  ARG ARG A . n 
A 1 63  ARG 63  69  69  ARG ARG A . n 
A 1 64  LYS 64  70  70  LYS LYS A . n 
A 1 65  HIS 65  71  71  HIS HIS A . n 
A 1 66  TYR 66  72  72  TYR TYR A . n 
A 1 67  PRO 67  73  73  PRO PRO A . n 
A 1 68  VAL 68  74  74  VAL VAL A . n 
A 1 69  SER 69  75  75  SER SER A . n 
A 1 70  PHE 70  76  76  PHE PHE A . n 
A 1 71  SER 71  77  77  SER SER A . n 
A 1 72  LYS 72  78  78  LYS LYS A . n 
A 1 73  PRO 73  79  79  PRO PRO A . n 
A 1 74  SER 74  80  80  SER SER A . n 
A 1 75  LEU 75  81  81  LEU LEU A . n 
A 1 76  ILE 76  82  82  ILE ILE A . n 
A 1 77  PHE 77  83  83  PHE PHE A . n 
A 1 78  VAL 78  84  84  VAL VAL A . n 
A 1 79  GLU 79  85  85  GLU GLU A . n 
A 1 80  ALA 80  86  86  ALA ALA A . n 
A 1 81  SER 81  87  87  SER SER A . n 
A 1 82  GLU 82  88  88  GLU GLU A . n 
A 1 83  TYR 83  89  89  TYR TYR A . n 
A 1 84  TYR 84  90  90  TYR TYR A . n 
A 1 85  PRO 85  91  91  PRO PRO A . n 
A 1 86  ALA 86  92  92  ALA ALA A . n 
A 1 87  ARG 87  93  93  ARG ARG A . n 
A 1 88  TYR 88  94  94  TYR TYR A . n 
A 1 89  GLN 89  95  95  GLN GLN A . n 
A 1 90  SER 90  96  96  SER SER A . n 
A 1 91  HIS 91  97  97  HIS HIS A . n 
A 1 92  LEU 92  98  98  LEU LEU A . n 
A 1 93  MET 93  99  99  MET MET A . n 
A 1 94  LEU 94  100 100 LEU LEU A . n 
A 1 95  ALA 95  101 101 ALA ALA A . n 
A 1 96  VAL 96  102 102 VAL VAL A . n 
A 1 97  GLY 97  103 103 GLY GLY A . n 
A 1 98  HIS 98  104 104 HIS HIS A . n 
A 1 99  SER 99  105 105 SER SER A . n 
A 1 100 GLU 100 106 106 GLU GLU A . n 
A 1 101 PRO 101 107 107 PRO PRO A . n 
A 1 102 GLY 102 108 108 GLY GLY A . n 
A 1 103 ASP 103 109 109 ASP ASP A . n 
A 1 104 CYS 104 110 110 CYS CYS A . n 
A 1 105 GLY 105 111 111 GLY GLY A . n 
A 1 106 GLY 106 112 112 GLY GLY A . n 
A 1 107 ILE 107 113 113 ILE ILE A . n 
A 1 108 LEU 108 114 114 LEU LEU A . n 
A 1 109 ARG 109 115 115 ARG ARG A . n 
A 1 110 CYS 110 116 116 CYS CYS A . n 
A 1 111 GLN 111 117 117 GLN GLN A . n 
A 1 112 HIS 112 118 118 HIS HIS A . n 
A 1 113 GLY 113 119 119 GLY GLY A . n 
A 1 114 VAL 114 120 120 VAL VAL A . n 
A 1 115 VAL 115 121 121 VAL VAL A . n 
A 1 116 GLY 116 122 122 GLY GLY A . n 
A 1 117 ILE 117 123 123 ILE ILE A . n 
A 1 118 VAL 118 124 124 VAL VAL A . n 
A 1 119 SER 119 125 125 SER SER A . n 
A 1 120 THR 120 126 126 THR THR A . n 
A 1 121 GLY 121 127 127 GLY GLY A . n 
A 1 122 GLY 122 128 128 GLY GLY A . n 
A 1 123 ASN 123 129 129 ASN ASN A . n 
A 1 124 GLY 124 130 130 GLY GLY A . n 
A 1 125 LEU 125 131 131 LEU LEU A . n 
A 1 126 VAL 126 132 132 VAL VAL A . n 
A 1 127 GLY 127 133 133 GLY GLY A . n 
A 1 128 PHE 128 134 134 PHE PHE A . n 
A 1 129 ALA 129 135 135 ALA ALA A . n 
A 1 130 ASP 130 136 136 ASP ASP A . n 
A 1 131 VAL 131 137 137 VAL VAL A . n 
A 1 132 ARG 132 138 138 ARG ARG A . n 
A 1 133 ASP 133 139 139 ASP ASP A . n 
A 1 134 LEU 134 140 140 LEU LEU A . n 
A 1 135 LEU 135 141 141 LEU LEU A . n 
A 1 136 TRP 136 142 142 TRP TRP A . n 
A 1 137 LEU 137 143 143 LEU LEU A . n 
A 1 138 ASP 138 144 144 ASP ASP A . n 
A 1 139 GLU 139 145 145 GLU GLU A . n 
A 1 140 GLU 140 146 146 GLU GLU A . n 
A 1 141 ALA 141 147 ?   ?   ?   A . n 
A 1 142 MET 142 148 ?   ?   ?   A . n 
A 1 143 GLU 143 149 ?   ?   ?   A . n 
A 1 144 GLN 144 150 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1B3P 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1B3P 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
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 
B 2 A1B3P 1   201 201 A1B3P LIG A . 
C 3 ZN    1   202 1   ZN    ZN  A . 
D 4 DMS   1   203 0   DMS   DMS A . 
E 4 DMS   1   204 1   DMS   DMS A . 
F 4 DMS   1   205 3   DMS   DMS A . 
G 5 HOH   1   301 81  HOH   HOH A . 
G 5 HOH   2   302 179 HOH   HOH A . 
G 5 HOH   3   303 218 HOH   HOH A . 
G 5 HOH   4   304 88  HOH   HOH A . 
G 5 HOH   5   305 4   HOH   HOH A . 
G 5 HOH   6   306 114 HOH   HOH A . 
G 5 HOH   7   307 72  HOH   HOH A . 
G 5 HOH   8   308 191 HOH   HOH A . 
G 5 HOH   9   309 59  HOH   HOH A . 
G 5 HOH   10  310 68  HOH   HOH A . 
G 5 HOH   11  311 169 HOH   HOH A . 
G 5 HOH   12  312 79  HOH   HOH A . 
G 5 HOH   13  313 173 HOH   HOH A . 
G 5 HOH   14  314 25  HOH   HOH A . 
G 5 HOH   15  315 52  HOH   HOH A . 
G 5 HOH   16  316 2   HOH   HOH A . 
G 5 HOH   17  317 121 HOH   HOH A . 
G 5 HOH   18  318 28  HOH   HOH A . 
G 5 HOH   19  319 186 HOH   HOH A . 
G 5 HOH   20  320 138 HOH   HOH A . 
G 5 HOH   21  321 171 HOH   HOH A . 
G 5 HOH   22  322 9   HOH   HOH A . 
G 5 HOH   23  323 77  HOH   HOH A . 
G 5 HOH   24  324 78  HOH   HOH A . 
G 5 HOH   25  325 211 HOH   HOH A . 
G 5 HOH   26  326 227 HOH   HOH A . 
G 5 HOH   27  327 53  HOH   HOH A . 
G 5 HOH   28  328 50  HOH   HOH A . 
G 5 HOH   29  329 34  HOH   HOH A . 
G 5 HOH   30  330 251 HOH   HOH A . 
G 5 HOH   31  331 32  HOH   HOH A . 
G 5 HOH   32  332 161 HOH   HOH A . 
G 5 HOH   33  333 5   HOH   HOH A . 
G 5 HOH   34  334 229 HOH   HOH A . 
G 5 HOH   35  335 30  HOH   HOH A . 
G 5 HOH   36  336 205 HOH   HOH A . 
G 5 HOH   37  337 97  HOH   HOH A . 
G 5 HOH   38  338 178 HOH   HOH A . 
G 5 HOH   39  339 26  HOH   HOH A . 
G 5 HOH   40  340 117 HOH   HOH A . 
G 5 HOH   41  341 85  HOH   HOH A . 
G 5 HOH   42  342 60  HOH   HOH A . 
G 5 HOH   43  343 36  HOH   HOH A . 
G 5 HOH   44  344 174 HOH   HOH A . 
G 5 HOH   45  345 152 HOH   HOH A . 
G 5 HOH   46  346 21  HOH   HOH A . 
G 5 HOH   47  347 63  HOH   HOH A . 
G 5 HOH   48  348 15  HOH   HOH A . 
G 5 HOH   49  349 71  HOH   HOH A . 
G 5 HOH   50  350 105 HOH   HOH A . 
G 5 HOH   51  351 215 HOH   HOH A . 
G 5 HOH   52  352 147 HOH   HOH A . 
G 5 HOH   53  353 33  HOH   HOH A . 
G 5 HOH   54  354 108 HOH   HOH A . 
G 5 HOH   55  355 76  HOH   HOH A . 
G 5 HOH   56  356 182 HOH   HOH A . 
G 5 HOH   57  357 103 HOH   HOH A . 
G 5 HOH   58  358 100 HOH   HOH A . 
G 5 HOH   59  359 49  HOH   HOH A . 
G 5 HOH   60  360 62  HOH   HOH A . 
G 5 HOH   61  361 7   HOH   HOH A . 
G 5 HOH   62  362 29  HOH   HOH A . 
G 5 HOH   63  363 234 HOH   HOH A . 
G 5 HOH   64  364 219 HOH   HOH A . 
G 5 HOH   65  365 61  HOH   HOH A . 
G 5 HOH   66  366 116 HOH   HOH A . 
G 5 HOH   67  367 65  HOH   HOH A . 
G 5 HOH   68  368 37  HOH   HOH A . 
G 5 HOH   69  369 233 HOH   HOH A . 
G 5 HOH   70  370 16  HOH   HOH A . 
G 5 HOH   71  371 83  HOH   HOH A . 
G 5 HOH   72  372 12  HOH   HOH A . 
G 5 HOH   73  373 156 HOH   HOH A . 
G 5 HOH   74  374 10  HOH   HOH A . 
G 5 HOH   75  375 230 HOH   HOH A . 
G 5 HOH   76  376 104 HOH   HOH A . 
G 5 HOH   77  377 177 HOH   HOH A . 
G 5 HOH   78  378 24  HOH   HOH A . 
G 5 HOH   79  379 150 HOH   HOH A . 
G 5 HOH   80  380 107 HOH   HOH A . 
G 5 HOH   81  381 84  HOH   HOH A . 
G 5 HOH   82  382 106 HOH   HOH A . 
G 5 HOH   83  383 40  HOH   HOH A . 
G 5 HOH   84  384 148 HOH   HOH A . 
G 5 HOH   85  385 167 HOH   HOH A . 
G 5 HOH   86  386 20  HOH   HOH A . 
G 5 HOH   87  387 231 HOH   HOH A . 
G 5 HOH   88  388 14  HOH   HOH A . 
G 5 HOH   89  389 131 HOH   HOH A . 
G 5 HOH   90  390 57  HOH   HOH A . 
G 5 HOH   91  391 228 HOH   HOH A . 
G 5 HOH   92  392 253 HOH   HOH A . 
G 5 HOH   93  393 144 HOH   HOH A . 
G 5 HOH   94  394 213 HOH   HOH A . 
G 5 HOH   95  395 70  HOH   HOH A . 
G 5 HOH   96  396 51  HOH   HOH A . 
G 5 HOH   97  397 132 HOH   HOH A . 
G 5 HOH   98  398 93  HOH   HOH A . 
G 5 HOH   99  399 146 HOH   HOH A . 
G 5 HOH   100 400 201 HOH   HOH A . 
G 5 HOH   101 401 80  HOH   HOH A . 
G 5 HOH   102 402 18  HOH   HOH A . 
G 5 HOH   103 403 111 HOH   HOH A . 
G 5 HOH   104 404 11  HOH   HOH A . 
G 5 HOH   105 405 43  HOH   HOH A . 
G 5 HOH   106 406 137 HOH   HOH A . 
G 5 HOH   107 407 128 HOH   HOH A . 
G 5 HOH   108 408 38  HOH   HOH A . 
G 5 HOH   109 409 237 HOH   HOH A . 
G 5 HOH   110 410 181 HOH   HOH A . 
G 5 HOH   111 411 158 HOH   HOH A . 
G 5 HOH   112 412 89  HOH   HOH A . 
G 5 HOH   113 413 245 HOH   HOH A . 
G 5 HOH   114 414 216 HOH   HOH A . 
G 5 HOH   115 415 19  HOH   HOH A . 
G 5 HOH   116 416 23  HOH   HOH A . 
G 5 HOH   117 417 159 HOH   HOH A . 
G 5 HOH   118 418 8   HOH   HOH A . 
G 5 HOH   119 419 136 HOH   HOH A . 
G 5 HOH   120 420 48  HOH   HOH A . 
G 5 HOH   121 421 168 HOH   HOH A . 
G 5 HOH   122 422 142 HOH   HOH A . 
G 5 HOH   123 423 198 HOH   HOH A . 
G 5 HOH   124 424 154 HOH   HOH A . 
G 5 HOH   125 425 46  HOH   HOH A . 
G 5 HOH   126 426 119 HOH   HOH A . 
G 5 HOH   127 427 122 HOH   HOH A . 
G 5 HOH   128 428 123 HOH   HOH A . 
G 5 HOH   129 429 214 HOH   HOH A . 
G 5 HOH   130 430 250 HOH   HOH A . 
G 5 HOH   131 431 96  HOH   HOH A . 
G 5 HOH   132 432 112 HOH   HOH A . 
G 5 HOH   133 433 27  HOH   HOH A . 
G 5 HOH   134 434 203 HOH   HOH A . 
G 5 HOH   135 435 94  HOH   HOH A . 
G 5 HOH   136 436 175 HOH   HOH A . 
G 5 HOH   137 437 69  HOH   HOH A . 
G 5 HOH   138 438 212 HOH   HOH A . 
G 5 HOH   139 439 207 HOH   HOH A . 
G 5 HOH   140 440 199 HOH   HOH A . 
G 5 HOH   141 441 135 HOH   HOH A . 
G 5 HOH   142 442 249 HOH   HOH A . 
G 5 HOH   143 443 248 HOH   HOH A . 
G 5 HOH   144 444 133 HOH   HOH A . 
G 5 HOH   145 445 155 HOH   HOH A . 
G 5 HOH   146 446 13  HOH   HOH A . 
G 5 HOH   147 447 252 HOH   HOH A . 
G 5 HOH   148 448 35  HOH   HOH A . 
G 5 HOH   149 449 204 HOH   HOH A . 
G 5 HOH   150 450 98  HOH   HOH A . 
G 5 HOH   151 451 220 HOH   HOH A . 
G 5 HOH   152 452 238 HOH   HOH A . 
G 5 HOH   153 453 247 HOH   HOH A . 
G 5 HOH   154 454 206 HOH   HOH A . 
G 5 HOH   155 455 95  HOH   HOH A . 
G 5 HOH   156 456 110 HOH   HOH A . 
G 5 HOH   157 457 42  HOH   HOH A . 
G 5 HOH   158 458 126 HOH   HOH A . 
G 5 HOH   159 459 189 HOH   HOH A . 
G 5 HOH   160 460 224 HOH   HOH A . 
G 5 HOH   161 461 67  HOH   HOH A . 
G 5 HOH   162 462 190 HOH   HOH A . 
G 5 HOH   163 463 47  HOH   HOH A . 
G 5 HOH   164 464 239 HOH   HOH A . 
G 5 HOH   165 465 102 HOH   HOH A . 
G 5 HOH   166 466 82  HOH   HOH A . 
G 5 HOH   167 467 129 HOH   HOH A . 
G 5 HOH   168 468 202 HOH   HOH A . 
G 5 HOH   169 469 141 HOH   HOH A . 
G 5 HOH   170 470 39  HOH   HOH A . 
G 5 HOH   171 471 241 HOH   HOH A . 
G 5 HOH   172 472 170 HOH   HOH A . 
G 5 HOH   173 473 101 HOH   HOH A . 
G 5 HOH   174 474 41  HOH   HOH A . 
G 5 HOH   175 475 113 HOH   HOH A . 
G 5 HOH   176 476 157 HOH   HOH A . 
G 5 HOH   177 477 240 HOH   HOH A . 
G 5 HOH   178 478 134 HOH   HOH A . 
G 5 HOH   179 479 232 HOH   HOH A . 
G 5 HOH   180 480 192 HOH   HOH A . 
G 5 HOH   181 481 197 HOH   HOH A . 
G 5 HOH   182 482 90  HOH   HOH A . 
G 5 HOH   183 483 221 HOH   HOH A . 
G 5 HOH   184 484 236 HOH   HOH A . 
G 5 HOH   185 485 162 HOH   HOH A . 
G 5 HOH   186 486 91  HOH   HOH A . 
G 5 HOH   187 487 235 HOH   HOH A . 
G 5 HOH   188 488 223 HOH   HOH A . 
G 5 HOH   189 489 56  HOH   HOH A . 
G 5 HOH   190 490 127 HOH   HOH A . 
G 5 HOH   191 491 86  HOH   HOH A . 
G 5 HOH   192 492 165 HOH   HOH A . 
G 5 HOH   193 493 73  HOH   HOH A . 
G 5 HOH   194 494 99  HOH   HOH A . 
G 5 HOH   195 495 243 HOH   HOH A . 
G 5 HOH   196 496 200 HOH   HOH A . 
G 5 HOH   197 497 246 HOH   HOH A . 
G 5 HOH   198 498 87  HOH   HOH A . 
G 5 HOH   199 499 92  HOH   HOH A . 
G 5 HOH   200 500 151 HOH   HOH A . 
G 5 HOH   201 501 164 HOH   HOH A . 
G 5 HOH   202 502 185 HOH   HOH A . 
G 5 HOH   203 503 222 HOH   HOH A . 
G 5 HOH   204 504 160 HOH   HOH A . 
G 5 HOH   205 505 118 HOH   HOH A . 
G 5 HOH   206 506 209 HOH   HOH A . 
G 5 HOH   207 507 125 HOH   HOH A . 
G 5 HOH   208 508 226 HOH   HOH A . 
G 5 HOH   209 509 242 HOH   HOH A . 
G 5 HOH   210 510 208 HOH   HOH A . 
G 5 HOH   211 511 187 HOH   HOH A . 
G 5 HOH   212 512 225 HOH   HOH A . 
G 5 HOH   213 513 244 HOH   HOH A . 
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       BUSTER  '2.10.4 (23-JAN-2024)' ? 1 
'data scaling'   Aimless .                      ? 2 
phasing          PHASER  .                      ? 3 
'data reduction' XDS     .                      ? 4 
# 
_cell.entry_id           7I58 
_cell.length_a           87.938 
_cell.length_b           57.571 
_cell.length_c           32.769 
_cell.angle_alpha        90.00 
_cell.angle_beta         93.56 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I58 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
# 
_exptl.entry_id          7I58 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.60 
_exptl_crystal.density_percent_sol   52.78 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2025-01-17 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92201 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.92201 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7I58 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             48.17 
_reflns.d_resolution_high            1.45 
_reflns.number_obs                   28819 
_reflns.percent_possible_obs         99.4 
_reflns.pdbx_Rmerge_I_obs            0.271 
_reflns.pdbx_netI_over_sigmaI        1.8 
_reflns.pdbx_redundancy              6.0 
_reflns.pdbx_Rrim_I_all              0.296 
_reflns.pdbx_Rpim_I_all              0.118 
_reflns.pdbx_CC_half                 0.971 
_reflns.pdbx_number_measured_all     173585 
_reflns.pdbx_chi_squared             0.17 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.45 
_reflns_shell.d_res_low                   1.47 
_reflns_shell.number_measured_all         6330 
_reflns_shell.number_unique_obs           1375 
_reflns_shell.Rmerge_I_obs                2.286 
_reflns_shell.pdbx_chi_squared            0.04 
_reflns_shell.pdbx_redundancy             4.6 
_reflns_shell.percent_possible_obs        94.6 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.1 
_reflns_shell.pdbx_Rrim_I_all             2.585 
_reflns_shell.pdbx_Rpim_I_all             1.188 
_reflns_shell.pdbx_CC_half                0.534 
_reflns_shell.percent_possible_all        ? 
_reflns_shell.pdbx_Rsym_value             ? 
_reflns_shell.meanI_over_sigI_obs         ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 7I58 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     17233 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             18.77 
_refine.ls_d_res_high                            1.454 
_refine.ls_percent_reflns_obs                    59.9 
_refine.ls_R_factor_obs                          0.2924 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2887 
_refine.ls_R_factor_R_free                       0.3624 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.030 
_refine.ls_number_reflns_R_free                  866 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.919 
_refine.correlation_coeff_Fo_to_Fc_free          0.845 
_refine.B_iso_mean                               37.32 
_refine.aniso_B[1][1]                            9.08330 
_refine.aniso_B[2][2]                            -0.39260 
_refine.aniso_B[3][3]                            -8.69070 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -5.61000 
_refine.aniso_B[2][3]                            0.00000 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             0.167 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.174 
_refine.pdbx_overall_SU_R_Blow_DPI               0.186 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.186 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7I58 
_refine_analyze.Luzzati_coordinate_error_obs    0.46 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1083 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         35 
_refine_hist.number_atoms_solvent             213 
_refine_hist.number_atoms_total               1331 
_refine_hist.d_res_high                       1.454 
_refine_hist.d_res_low                        18.77 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
t_bond_d                  0.011 ? 2.00  1162 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.09  ? 2.00  1583 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  387  'X-RAY DIFFRACTION' SINUSOIDAL   
t_incorr_chiral_ct        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_pseud_angle             ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_trig_c_planes           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_gen_planes              ?     ? 5.00  215  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1162 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           3.59  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           17.88 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  141  'X-RAY DIFFRACTION' SEMIHARMONIC 
t_sum_occupancies         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_distance        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_angle           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_torsion         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_ideal_dist_contact      ?     ? 4.00  1085 'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   44 
_refine_ls_shell.d_res_high                       1.45 
_refine_ls_shell.d_res_low                        1.53 
_refine_ls_shell.number_reflns_R_work             382 
_refine_ls_shell.R_factor_R_work                  0.7103 
_refine_ls_shell.percent_reflns_obs               10.18 
_refine_ls_shell.R_factor_R_free                  0.7376 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            4.74 
_refine_ls_shell.number_reflns_R_free             19 
_refine_ls_shell.number_reflns_all                401 
_refine_ls_shell.R_factor_all                     0.7114 
# 
_struct.entry_id                  7I58 
_struct.title                     
;Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre -- Crystal structure of Coxsackievirus A16 (G-10) 2A protease in complex with ASAP-0036807-001 (A71EV2A-x4798)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I58 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN
;
# 
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 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 4 ? 
F N N 4 ? 
G N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    POLG_CX16G 
_struct_ref.pdbx_db_accession          Q65900 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_struct_ref.pdbx_align_begin           869 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              7I58 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 144 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q65900 
_struct_ref_seq.db_align_beg                  869 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1012 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       7 
_struct_ref_seq.pdbx_auth_seq_align_end       150 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_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 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2 AA2 THR A 18  ? ALA A 23  ? THR A 24  ALA A 29  1 ? 6 
HELX_P HELX_P3 AA3 GLU A 100 ? CYS A 104 ? GLU A 106 CYS A 110 5 ? 5 
HELX_P HELX_P4 AA4 LEU A 134 ? ASP A 138 ? LEU A 140 ASP A 144 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 
metalc1 metalc ? ? A CYS 50  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 56  A ZN 202 1_555 ? ? ? ? ? ? ? 2.408 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.153 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.508 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 C ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.365 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 52  ? A CYS 58  ? 1_555 105.2 ? 
2 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 100.2 ? 
3 SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 124.1 ? 
4 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 109.2 ? 
5 SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 97.2  ? 
6 SG ? A CYS 110 ? A CYS 116 ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 119.9 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 7 ? 
# 
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 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? 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 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA1 2 LEU A 34  ? CYS A 44  ? LEU A 40  CYS A 50  
AA1 3 ILE A 4   ? ASN A 13  ? ILE A 10  ASN A 19  
AA2 1 LYS A 64  ? SER A 69  ? LYS A 70  SER A 75  
AA2 2 THR A 54  ? CYS A 59  ? THR A 60  CYS A 65  
AA2 3 ILE A 107 ? ARG A 109 ? ILE A 113 ARG A 115 
AA2 4 VAL A 114 ? THR A 120 ? VAL A 120 THR A 126 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
# 
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 TRP A 27  ? N TRP A 33  O VAL A 36  ? O VAL A 42  
AA1 2 3 N LEU A 35  ? N LEU A 41  O VAL A 12  ? O VAL A 18  
AA2 1 2 O VAL A 68  ? O VAL A 74  N GLY A 55  ? N GLY A 61  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N LEU A 108 ? N LEU A 114 O GLY A 116 ? O GLY A 122 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O PHE A 128 ? O PHE A 134 N MET A 93  ? N MET A 99  
AA2 6 7 O ARG A 87  ? O ARG A 93  N VAL A 78  ? N VAL A 84  
# 
_pdbx_entry_details.entry_id                   7I58 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O A HOH 396 ? ? O A HOH 482 ? ? 1.57 
2 1 O A HOH 416 ? ? O A HOH 441 ? ? 1.93 
3 1 O A HOH 416 ? ? O A HOH 448 ? ? 1.94 
4 1 O A HOH 312 ? ? O A HOH 456 ? ? 1.97 
5 1 O A HOH 345 ? ? O A HOH 415 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 360 ? ? 1_555 O A HOH 399 ? ? 4_546 1.99 
2 1 O A HOH 440 ? ? 1_555 O A HOH 476 ? ? 4_556 2.18 
# 
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 ALA A 29  ? ? -66.41  2.39    
2 1 ASN A 30  ? ? -152.27 30.96   
3 1 CYS A 116 ? ? -116.23 -164.23 
4 1 SER A 125 ? ? -134.09 -47.41  
# 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         15.0667 
_pdbx_refine_tls.origin_y         7.5734 
_pdbx_refine_tls.origin_z         14.1738 
_pdbx_refine_tls.T[1][1]          0.2584 
_pdbx_refine_tls.T[2][2]          0.0234 
_pdbx_refine_tls.T[3][3]          -0.3362 
_pdbx_refine_tls.T[1][2]          -0.0330 
_pdbx_refine_tls.T[1][3]          -0.0477 
_pdbx_refine_tls.T[2][3]          -0.0255 
_pdbx_refine_tls.L[1][1]          0.8485 
_pdbx_refine_tls.L[2][2]          3.3992 
_pdbx_refine_tls.L[3][3]          1.2540 
_pdbx_refine_tls.L[1][2]          1.1982 
_pdbx_refine_tls.L[1][3]          -0.7226 
_pdbx_refine_tls.L[2][3]          0.2682 
_pdbx_refine_tls.S[1][1]          0.0436 
_pdbx_refine_tls.S[1][2]          -0.0732 
_pdbx_refine_tls.S[1][3]          0.4146 
_pdbx_refine_tls.S[2][1]          -0.0744 
_pdbx_refine_tls.S[2][2]          0.1287 
_pdbx_refine_tls.S[2][3]          -0.2075 
_pdbx_refine_tls.S[3][1]          -0.0444 
_pdbx_refine_tls.S[3][2]          0.0311 
_pdbx_refine_tls.S[3][3]          -0.1724 
# 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   '{ A|* }' 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 510 ? 5.82 . 
2 1 O ? A HOH 511 ? 6.27 . 
3 1 O ? A HOH 512 ? 6.34 . 
4 1 O ? A HOH 513 ? 6.83 . 
# 
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 147 ? A ALA 141 
2 1 Y 1 A MET 148 ? A MET 142 
3 1 Y 1 A GLU 149 ? A GLU 143 
4 1 Y 1 A GLN 150 ? A GLN 144 
# 
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 
A1B3P N1   N  Y N 1   
A1B3P N3   N  Y N 2   
A1B3P C4   C  Y N 3   
A1B3P C5   C  Y N 4   
A1B3P C6   C  Y N 5   
A1B3P C7   C  N N 6   
A1B3P C8   C  N N 7   
A1B3P C10  C  N N 8   
A1B3P C13  C  Y N 9   
A1B3P O    O  N N 10  
A1B3P C3   C  Y N 11  
A1B3P C2   C  Y N 12  
A1B3P C1   C  Y N 13  
A1B3P S    S  N N 14  
A1B3P C    C  N N 15  
A1B3P N    N  N N 16  
A1B3P C14  C  N N 17  
A1B3P C11  C  N R 18  
A1B3P O1   O  N N 19  
A1B3P C9   C  N N 20  
A1B3P C12  C  Y N 21  
A1B3P N2   N  Y N 22  
A1B3P H    H  N N 23  
A1B3P H6   H  N N 24  
A1B3P H7   H  N N 25  
A1B3P H9   H  N N 26  
A1B3P H8   H  N N 27  
A1B3P H12  H  N N 28  
A1B3P H13  H  N N 29  
A1B3P H15  H  N N 30  
A1B3P H5   H  N N 31  
A1B3P H4   H  N N 32  
A1B3P H2   H  N N 33  
A1B3P H1   H  N N 34  
A1B3P H3   H  N N 35  
A1B3P H16  H  N N 36  
A1B3P H17  H  N N 37  
A1B3P H14  H  N N 38  
A1B3P H10  H  N N 39  
A1B3P H11  H  N N 40  
ALA   N    N  N N 41  
ALA   CA   C  N S 42  
ALA   C    C  N N 43  
ALA   O    O  N N 44  
ALA   CB   C  N N 45  
ALA   OXT  O  N N 46  
ALA   H    H  N N 47  
ALA   H2   H  N N 48  
ALA   HA   H  N N 49  
ALA   HB1  H  N N 50  
ALA   HB2  H  N N 51  
ALA   HB3  H  N N 52  
ALA   HXT  H  N N 53  
ARG   N    N  N N 54  
ARG   CA   C  N S 55  
ARG   C    C  N N 56  
ARG   O    O  N N 57  
ARG   CB   C  N N 58  
ARG   CG   C  N N 59  
ARG   CD   C  N N 60  
ARG   NE   N  N N 61  
ARG   CZ   C  N N 62  
ARG   NH1  N  N N 63  
ARG   NH2  N  N N 64  
ARG   OXT  O  N N 65  
ARG   H    H  N N 66  
ARG   H2   H  N N 67  
ARG   HA   H  N N 68  
ARG   HB2  H  N N 69  
ARG   HB3  H  N N 70  
ARG   HG2  H  N N 71  
ARG   HG3  H  N N 72  
ARG   HD2  H  N N 73  
ARG   HD3  H  N N 74  
ARG   HE   H  N N 75  
ARG   HH11 H  N N 76  
ARG   HH12 H  N N 77  
ARG   HH21 H  N N 78  
ARG   HH22 H  N N 79  
ARG   HXT  H  N N 80  
ASN   N    N  N N 81  
ASN   CA   C  N S 82  
ASN   C    C  N N 83  
ASN   O    O  N N 84  
ASN   CB   C  N N 85  
ASN   CG   C  N N 86  
ASN   OD1  O  N N 87  
ASN   ND2  N  N N 88  
ASN   OXT  O  N N 89  
ASN   H    H  N N 90  
ASN   H2   H  N N 91  
ASN   HA   H  N N 92  
ASN   HB2  H  N N 93  
ASN   HB3  H  N N 94  
ASN   HD21 H  N N 95  
ASN   HD22 H  N N 96  
ASN   HXT  H  N N 97  
ASP   N    N  N N 98  
ASP   CA   C  N S 99  
ASP   C    C  N N 100 
ASP   O    O  N N 101 
ASP   CB   C  N N 102 
ASP   CG   C  N N 103 
ASP   OD1  O  N N 104 
ASP   OD2  O  N N 105 
ASP   OXT  O  N N 106 
ASP   H    H  N N 107 
ASP   H2   H  N N 108 
ASP   HA   H  N N 109 
ASP   HB2  H  N N 110 
ASP   HB3  H  N N 111 
ASP   HD2  H  N N 112 
ASP   HXT  H  N N 113 
CYS   N    N  N N 114 
CYS   CA   C  N R 115 
CYS   C    C  N N 116 
CYS   O    O  N N 117 
CYS   CB   C  N N 118 
CYS   SG   S  N N 119 
CYS   OXT  O  N N 120 
CYS   H    H  N N 121 
CYS   H2   H  N N 122 
CYS   HA   H  N N 123 
CYS   HB2  H  N N 124 
CYS   HB3  H  N N 125 
CYS   HG   H  N N 126 
CYS   HXT  H  N N 127 
DMS   S    S  N N 128 
DMS   O    O  N N 129 
DMS   C1   C  N N 130 
DMS   C2   C  N N 131 
DMS   H11  H  N N 132 
DMS   H12  H  N N 133 
DMS   H13  H  N N 134 
DMS   H21  H  N N 135 
DMS   H22  H  N N 136 
DMS   H23  H  N N 137 
GLN   N    N  N N 138 
GLN   CA   C  N S 139 
GLN   C    C  N N 140 
GLN   O    O  N N 141 
GLN   CB   C  N N 142 
GLN   CG   C  N N 143 
GLN   CD   C  N N 144 
GLN   OE1  O  N N 145 
GLN   NE2  N  N N 146 
GLN   OXT  O  N N 147 
GLN   H    H  N N 148 
GLN   H2   H  N N 149 
GLN   HA   H  N N 150 
GLN   HB2  H  N N 151 
GLN   HB3  H  N N 152 
GLN   HG2  H  N N 153 
GLN   HG3  H  N N 154 
GLN   HE21 H  N N 155 
GLN   HE22 H  N N 156 
GLN   HXT  H  N N 157 
GLU   N    N  N N 158 
GLU   CA   C  N S 159 
GLU   C    C  N N 160 
GLU   O    O  N N 161 
GLU   CB   C  N N 162 
GLU   CG   C  N N 163 
GLU   CD   C  N N 164 
GLU   OE1  O  N N 165 
GLU   OE2  O  N N 166 
GLU   OXT  O  N N 167 
GLU   H    H  N N 168 
GLU   H2   H  N N 169 
GLU   HA   H  N N 170 
GLU   HB2  H  N N 171 
GLU   HB3  H  N N 172 
GLU   HG2  H  N N 173 
GLU   HG3  H  N N 174 
GLU   HE2  H  N N 175 
GLU   HXT  H  N N 176 
GLY   N    N  N N 177 
GLY   CA   C  N N 178 
GLY   C    C  N N 179 
GLY   O    O  N N 180 
GLY   OXT  O  N N 181 
GLY   H    H  N N 182 
GLY   H2   H  N N 183 
GLY   HA2  H  N N 184 
GLY   HA3  H  N N 185 
GLY   HXT  H  N N 186 
HIS   N    N  N N 187 
HIS   CA   C  N S 188 
HIS   C    C  N N 189 
HIS   O    O  N N 190 
HIS   CB   C  N N 191 
HIS   CG   C  Y N 192 
HIS   ND1  N  Y N 193 
HIS   CD2  C  Y N 194 
HIS   CE1  C  Y N 195 
HIS   NE2  N  Y N 196 
HIS   OXT  O  N N 197 
HIS   H    H  N N 198 
HIS   H2   H  N N 199 
HIS   HA   H  N N 200 
HIS   HB2  H  N N 201 
HIS   HB3  H  N N 202 
HIS   HD1  H  N N 203 
HIS   HD2  H  N N 204 
HIS   HE1  H  N N 205 
HIS   HE2  H  N N 206 
HIS   HXT  H  N N 207 
HOH   O    O  N N 208 
HOH   H1   H  N N 209 
HOH   H2   H  N N 210 
ILE   N    N  N N 211 
ILE   CA   C  N S 212 
ILE   C    C  N N 213 
ILE   O    O  N N 214 
ILE   CB   C  N S 215 
ILE   CG1  C  N N 216 
ILE   CG2  C  N N 217 
ILE   CD1  C  N N 218 
ILE   OXT  O  N N 219 
ILE   H    H  N N 220 
ILE   H2   H  N N 221 
ILE   HA   H  N N 222 
ILE   HB   H  N N 223 
ILE   HG12 H  N N 224 
ILE   HG13 H  N N 225 
ILE   HG21 H  N N 226 
ILE   HG22 H  N N 227 
ILE   HG23 H  N N 228 
ILE   HD11 H  N N 229 
ILE   HD12 H  N N 230 
ILE   HD13 H  N N 231 
ILE   HXT  H  N N 232 
LEU   N    N  N N 233 
LEU   CA   C  N S 234 
LEU   C    C  N N 235 
LEU   O    O  N N 236 
LEU   CB   C  N N 237 
LEU   CG   C  N N 238 
LEU   CD1  C  N N 239 
LEU   CD2  C  N N 240 
LEU   OXT  O  N N 241 
LEU   H    H  N N 242 
LEU   H2   H  N N 243 
LEU   HA   H  N N 244 
LEU   HB2  H  N N 245 
LEU   HB3  H  N N 246 
LEU   HG   H  N N 247 
LEU   HD11 H  N N 248 
LEU   HD12 H  N N 249 
LEU   HD13 H  N N 250 
LEU   HD21 H  N N 251 
LEU   HD22 H  N N 252 
LEU   HD23 H  N N 253 
LEU   HXT  H  N N 254 
LYS   N    N  N N 255 
LYS   CA   C  N S 256 
LYS   C    C  N N 257 
LYS   O    O  N N 258 
LYS   CB   C  N N 259 
LYS   CG   C  N N 260 
LYS   CD   C  N N 261 
LYS   CE   C  N N 262 
LYS   NZ   N  N N 263 
LYS   OXT  O  N N 264 
LYS   H    H  N N 265 
LYS   H2   H  N N 266 
LYS   HA   H  N N 267 
LYS   HB2  H  N N 268 
LYS   HB3  H  N N 269 
LYS   HG2  H  N N 270 
LYS   HG3  H  N N 271 
LYS   HD2  H  N N 272 
LYS   HD3  H  N N 273 
LYS   HE2  H  N N 274 
LYS   HE3  H  N N 275 
LYS   HZ1  H  N N 276 
LYS   HZ2  H  N N 277 
LYS   HZ3  H  N N 278 
LYS   HXT  H  N N 279 
MET   N    N  N N 280 
MET   CA   C  N S 281 
MET   C    C  N N 282 
MET   O    O  N N 283 
MET   CB   C  N N 284 
MET   CG   C  N N 285 
MET   SD   S  N N 286 
MET   CE   C  N N 287 
MET   OXT  O  N N 288 
MET   H    H  N N 289 
MET   H2   H  N N 290 
MET   HA   H  N N 291 
MET   HB2  H  N N 292 
MET   HB3  H  N N 293 
MET   HG2  H  N N 294 
MET   HG3  H  N N 295 
MET   HE1  H  N N 296 
MET   HE2  H  N N 297 
MET   HE3  H  N N 298 
MET   HXT  H  N N 299 
PHE   N    N  N N 300 
PHE   CA   C  N S 301 
PHE   C    C  N N 302 
PHE   O    O  N N 303 
PHE   CB   C  N N 304 
PHE   CG   C  Y N 305 
PHE   CD1  C  Y N 306 
PHE   CD2  C  Y N 307 
PHE   CE1  C  Y N 308 
PHE   CE2  C  Y N 309 
PHE   CZ   C  Y N 310 
PHE   OXT  O  N N 311 
PHE   H    H  N N 312 
PHE   H2   H  N N 313 
PHE   HA   H  N N 314 
PHE   HB2  H  N N 315 
PHE   HB3  H  N N 316 
PHE   HD1  H  N N 317 
PHE   HD2  H  N N 318 
PHE   HE1  H  N N 319 
PHE   HE2  H  N N 320 
PHE   HZ   H  N N 321 
PHE   HXT  H  N N 322 
PRO   N    N  N N 323 
PRO   CA   C  N S 324 
PRO   C    C  N N 325 
PRO   O    O  N N 326 
PRO   CB   C  N N 327 
PRO   CG   C  N N 328 
PRO   CD   C  N N 329 
PRO   OXT  O  N N 330 
PRO   H    H  N N 331 
PRO   HA   H  N N 332 
PRO   HB2  H  N N 333 
PRO   HB3  H  N N 334 
PRO   HG2  H  N N 335 
PRO   HG3  H  N N 336 
PRO   HD2  H  N N 337 
PRO   HD3  H  N N 338 
PRO   HXT  H  N N 339 
SER   N    N  N N 340 
SER   CA   C  N S 341 
SER   C    C  N N 342 
SER   O    O  N N 343 
SER   CB   C  N N 344 
SER   OG   O  N N 345 
SER   OXT  O  N N 346 
SER   H    H  N N 347 
SER   H2   H  N N 348 
SER   HA   H  N N 349 
SER   HB2  H  N N 350 
SER   HB3  H  N N 351 
SER   HG   H  N N 352 
SER   HXT  H  N N 353 
THR   N    N  N N 354 
THR   CA   C  N S 355 
THR   C    C  N N 356 
THR   O    O  N N 357 
THR   CB   C  N R 358 
THR   OG1  O  N N 359 
THR   CG2  C  N N 360 
THR   OXT  O  N N 361 
THR   H    H  N N 362 
THR   H2   H  N N 363 
THR   HA   H  N N 364 
THR   HB   H  N N 365 
THR   HG1  H  N N 366 
THR   HG21 H  N N 367 
THR   HG22 H  N N 368 
THR   HG23 H  N N 369 
THR   HXT  H  N N 370 
TRP   N    N  N N 371 
TRP   CA   C  N S 372 
TRP   C    C  N N 373 
TRP   O    O  N N 374 
TRP   CB   C  N N 375 
TRP   CG   C  Y N 376 
TRP   CD1  C  Y N 377 
TRP   CD2  C  Y N 378 
TRP   NE1  N  Y N 379 
TRP   CE2  C  Y N 380 
TRP   CE3  C  Y N 381 
TRP   CZ2  C  Y N 382 
TRP   CZ3  C  Y N 383 
TRP   CH2  C  Y N 384 
TRP   OXT  O  N N 385 
TRP   H    H  N N 386 
TRP   H2   H  N N 387 
TRP   HA   H  N N 388 
TRP   HB2  H  N N 389 
TRP   HB3  H  N N 390 
TRP   HD1  H  N N 391 
TRP   HE1  H  N N 392 
TRP   HE3  H  N N 393 
TRP   HZ2  H  N N 394 
TRP   HZ3  H  N N 395 
TRP   HH2  H  N N 396 
TRP   HXT  H  N N 397 
TYR   N    N  N N 398 
TYR   CA   C  N S 399 
TYR   C    C  N N 400 
TYR   O    O  N N 401 
TYR   CB   C  N N 402 
TYR   CG   C  Y N 403 
TYR   CD1  C  Y N 404 
TYR   CD2  C  Y N 405 
TYR   CE1  C  Y N 406 
TYR   CE2  C  Y N 407 
TYR   CZ   C  Y N 408 
TYR   OH   O  N N 409 
TYR   OXT  O  N N 410 
TYR   H    H  N N 411 
TYR   H2   H  N N 412 
TYR   HA   H  N N 413 
TYR   HB2  H  N N 414 
TYR   HB3  H  N N 415 
TYR   HD1  H  N N 416 
TYR   HD2  H  N N 417 
TYR   HE1  H  N N 418 
TYR   HE2  H  N N 419 
TYR   HH   H  N N 420 
TYR   HXT  H  N N 421 
VAL   N    N  N N 422 
VAL   CA   C  N S 423 
VAL   C    C  N N 424 
VAL   O    O  N N 425 
VAL   CB   C  N N 426 
VAL   CG1  C  N N 427 
VAL   CG2  C  N N 428 
VAL   OXT  O  N N 429 
VAL   H    H  N N 430 
VAL   H2   H  N N 431 
VAL   HA   H  N N 432 
VAL   HB   H  N N 433 
VAL   HG11 H  N N 434 
VAL   HG12 H  N N 435 
VAL   HG13 H  N N 436 
VAL   HG21 H  N N 437 
VAL   HG22 H  N N 438 
VAL   HG23 H  N N 439 
VAL   HXT  H  N N 440 
ZN    ZN   ZN N N 441 
# 
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 
A1B3P C   S    sing N N 1   
A1B3P S   C1   sing N N 2   
A1B3P C1  C2   doub Y N 3   
A1B3P C2  C3   sing Y N 4   
A1B3P C3  C4   doub Y N 5   
A1B3P C4  C5   sing Y N 6   
A1B3P C5  C6   doub Y N 7   
A1B3P C1  C6   sing Y N 8   
A1B3P C6  C7   sing N N 9   
A1B3P C7  C8   sing N N 10  
A1B3P C8  O    doub N N 11  
A1B3P N   C8   sing N N 12  
A1B3P N   C9   sing N N 13  
A1B3P C9  C10  sing N N 14  
A1B3P C10 C11  sing N N 15  
A1B3P O1  C11  sing N N 16  
A1B3P C12 C11  sing N N 17  
A1B3P C12 C13  doub Y N 18  
A1B3P C13 N1   sing Y N 19  
A1B3P N1  N2   sing Y N 20  
A1B3P N2  N3   doub Y N 21  
A1B3P N3  C12  sing Y N 22  
A1B3P C11 C14  sing N N 23  
A1B3P C14 N    sing N N 24  
A1B3P N1  H    sing N N 25  
A1B3P C4  H6   sing N N 26  
A1B3P C5  H7   sing N N 27  
A1B3P C7  H9   sing N N 28  
A1B3P C7  H8   sing N N 29  
A1B3P C10 H12  sing N N 30  
A1B3P C10 H13  sing N N 31  
A1B3P C13 H15  sing N N 32  
A1B3P C3  H5   sing N N 33  
A1B3P C2  H4   sing N N 34  
A1B3P C   H2   sing N N 35  
A1B3P C   H1   sing N N 36  
A1B3P C   H3   sing N N 37  
A1B3P C14 H16  sing N N 38  
A1B3P C14 H17  sing N N 39  
A1B3P O1  H14  sing N N 40  
A1B3P C9  H10  sing N N 41  
A1B3P C9  H11  sing N N 42  
ALA   N   CA   sing N N 43  
ALA   N   H    sing N N 44  
ALA   N   H2   sing N N 45  
ALA   CA  C    sing N N 46  
ALA   CA  CB   sing N N 47  
ALA   CA  HA   sing N N 48  
ALA   C   O    doub N N 49  
ALA   C   OXT  sing N N 50  
ALA   CB  HB1  sing N N 51  
ALA   CB  HB2  sing N N 52  
ALA   CB  HB3  sing N N 53  
ALA   OXT HXT  sing N N 54  
ARG   N   CA   sing N N 55  
ARG   N   H    sing N N 56  
ARG   N   H2   sing N N 57  
ARG   CA  C    sing N N 58  
ARG   CA  CB   sing N N 59  
ARG   CA  HA   sing N N 60  
ARG   C   O    doub N N 61  
ARG   C   OXT  sing N N 62  
ARG   CB  CG   sing N N 63  
ARG   CB  HB2  sing N N 64  
ARG   CB  HB3  sing N N 65  
ARG   CG  CD   sing N N 66  
ARG   CG  HG2  sing N N 67  
ARG   CG  HG3  sing N N 68  
ARG   CD  NE   sing N N 69  
ARG   CD  HD2  sing N N 70  
ARG   CD  HD3  sing N N 71  
ARG   NE  CZ   sing N N 72  
ARG   NE  HE   sing N N 73  
ARG   CZ  NH1  sing N N 74  
ARG   CZ  NH2  doub N N 75  
ARG   NH1 HH11 sing N N 76  
ARG   NH1 HH12 sing N N 77  
ARG   NH2 HH21 sing N N 78  
ARG   NH2 HH22 sing N N 79  
ARG   OXT HXT  sing N N 80  
ASN   N   CA   sing N N 81  
ASN   N   H    sing N N 82  
ASN   N   H2   sing N N 83  
ASN   CA  C    sing N N 84  
ASN   CA  CB   sing N N 85  
ASN   CA  HA   sing N N 86  
ASN   C   O    doub N N 87  
ASN   C   OXT  sing N N 88  
ASN   CB  CG   sing N N 89  
ASN   CB  HB2  sing N N 90  
ASN   CB  HB3  sing N N 91  
ASN   CG  OD1  doub N N 92  
ASN   CG  ND2  sing N N 93  
ASN   ND2 HD21 sing N N 94  
ASN   ND2 HD22 sing N N 95  
ASN   OXT HXT  sing N N 96  
ASP   N   CA   sing N N 97  
ASP   N   H    sing N N 98  
ASP   N   H2   sing N N 99  
ASP   CA  C    sing N N 100 
ASP   CA  CB   sing N N 101 
ASP   CA  HA   sing N N 102 
ASP   C   O    doub N N 103 
ASP   C   OXT  sing N N 104 
ASP   CB  CG   sing N N 105 
ASP   CB  HB2  sing N N 106 
ASP   CB  HB3  sing N N 107 
ASP   CG  OD1  doub N N 108 
ASP   CG  OD2  sing N N 109 
ASP   OD2 HD2  sing N N 110 
ASP   OXT HXT  sing N N 111 
CYS   N   CA   sing N N 112 
CYS   N   H    sing N N 113 
CYS   N   H2   sing N N 114 
CYS   CA  C    sing N N 115 
CYS   CA  CB   sing N N 116 
CYS   CA  HA   sing N N 117 
CYS   C   O    doub N N 118 
CYS   C   OXT  sing N N 119 
CYS   CB  SG   sing N N 120 
CYS   CB  HB2  sing N N 121 
CYS   CB  HB3  sing N N 122 
CYS   SG  HG   sing N N 123 
CYS   OXT HXT  sing N N 124 
DMS   S   O    doub N N 125 
DMS   S   C1   sing N N 126 
DMS   S   C2   sing N N 127 
DMS   C1  H11  sing N N 128 
DMS   C1  H12  sing N N 129 
DMS   C1  H13  sing N N 130 
DMS   C2  H21  sing N N 131 
DMS   C2  H22  sing N N 132 
DMS   C2  H23  sing N N 133 
GLN   N   CA   sing N N 134 
GLN   N   H    sing N N 135 
GLN   N   H2   sing N N 136 
GLN   CA  C    sing N N 137 
GLN   CA  CB   sing N N 138 
GLN   CA  HA   sing N N 139 
GLN   C   O    doub N N 140 
GLN   C   OXT  sing N N 141 
GLN   CB  CG   sing N N 142 
GLN   CB  HB2  sing N N 143 
GLN   CB  HB3  sing N N 144 
GLN   CG  CD   sing N N 145 
GLN   CG  HG2  sing N N 146 
GLN   CG  HG3  sing N N 147 
GLN   CD  OE1  doub N N 148 
GLN   CD  NE2  sing N N 149 
GLN   NE2 HE21 sing N N 150 
GLN   NE2 HE22 sing N N 151 
GLN   OXT HXT  sing N N 152 
GLU   N   CA   sing N N 153 
GLU   N   H    sing N N 154 
GLU   N   H2   sing N N 155 
GLU   CA  C    sing N N 156 
GLU   CA  CB   sing N N 157 
GLU   CA  HA   sing N N 158 
GLU   C   O    doub N N 159 
GLU   C   OXT  sing N N 160 
GLU   CB  CG   sing N N 161 
GLU   CB  HB2  sing N N 162 
GLU   CB  HB3  sing N N 163 
GLU   CG  CD   sing N N 164 
GLU   CG  HG2  sing N N 165 
GLU   CG  HG3  sing N N 166 
GLU   CD  OE1  doub N N 167 
GLU   CD  OE2  sing N N 168 
GLU   OE2 HE2  sing N N 169 
GLU   OXT HXT  sing N N 170 
GLY   N   CA   sing N N 171 
GLY   N   H    sing N N 172 
GLY   N   H2   sing N N 173 
GLY   CA  C    sing N N 174 
GLY   CA  HA2  sing N N 175 
GLY   CA  HA3  sing N N 176 
GLY   C   O    doub N N 177 
GLY   C   OXT  sing N N 178 
GLY   OXT HXT  sing N N 179 
HIS   N   CA   sing N N 180 
HIS   N   H    sing N N 181 
HIS   N   H2   sing N N 182 
HIS   CA  C    sing N N 183 
HIS   CA  CB   sing N N 184 
HIS   CA  HA   sing N N 185 
HIS   C   O    doub N N 186 
HIS   C   OXT  sing N N 187 
HIS   CB  CG   sing N N 188 
HIS   CB  HB2  sing N N 189 
HIS   CB  HB3  sing N N 190 
HIS   CG  ND1  sing Y N 191 
HIS   CG  CD2  doub Y N 192 
HIS   ND1 CE1  doub Y N 193 
HIS   ND1 HD1  sing N N 194 
HIS   CD2 NE2  sing Y N 195 
HIS   CD2 HD2  sing N N 196 
HIS   CE1 NE2  sing Y N 197 
HIS   CE1 HE1  sing N N 198 
HIS   NE2 HE2  sing N N 199 
HIS   OXT HXT  sing N N 200 
HOH   O   H1   sing N N 201 
HOH   O   H2   sing N N 202 
ILE   N   CA   sing N N 203 
ILE   N   H    sing N N 204 
ILE   N   H2   sing N N 205 
ILE   CA  C    sing N N 206 
ILE   CA  CB   sing N N 207 
ILE   CA  HA   sing N N 208 
ILE   C   O    doub N N 209 
ILE   C   OXT  sing N N 210 
ILE   CB  CG1  sing N N 211 
ILE   CB  CG2  sing N N 212 
ILE   CB  HB   sing N N 213 
ILE   CG1 CD1  sing N N 214 
ILE   CG1 HG12 sing N N 215 
ILE   CG1 HG13 sing N N 216 
ILE   CG2 HG21 sing N N 217 
ILE   CG2 HG22 sing N N 218 
ILE   CG2 HG23 sing N N 219 
ILE   CD1 HD11 sing N N 220 
ILE   CD1 HD12 sing N N 221 
ILE   CD1 HD13 sing N N 222 
ILE   OXT HXT  sing N N 223 
LEU   N   CA   sing N N 224 
LEU   N   H    sing N N 225 
LEU   N   H2   sing N N 226 
LEU   CA  C    sing N N 227 
LEU   CA  CB   sing N N 228 
LEU   CA  HA   sing N N 229 
LEU   C   O    doub N N 230 
LEU   C   OXT  sing N N 231 
LEU   CB  CG   sing N N 232 
LEU   CB  HB2  sing N N 233 
LEU   CB  HB3  sing N N 234 
LEU   CG  CD1  sing N N 235 
LEU   CG  CD2  sing N N 236 
LEU   CG  HG   sing N N 237 
LEU   CD1 HD11 sing N N 238 
LEU   CD1 HD12 sing N N 239 
LEU   CD1 HD13 sing N N 240 
LEU   CD2 HD21 sing N N 241 
LEU   CD2 HD22 sing N N 242 
LEU   CD2 HD23 sing N N 243 
LEU   OXT HXT  sing N N 244 
LYS   N   CA   sing N N 245 
LYS   N   H    sing N N 246 
LYS   N   H2   sing N N 247 
LYS   CA  C    sing N N 248 
LYS   CA  CB   sing N N 249 
LYS   CA  HA   sing N N 250 
LYS   C   O    doub N N 251 
LYS   C   OXT  sing N N 252 
LYS   CB  CG   sing N N 253 
LYS   CB  HB2  sing N N 254 
LYS   CB  HB3  sing N N 255 
LYS   CG  CD   sing N N 256 
LYS   CG  HG2  sing N N 257 
LYS   CG  HG3  sing N N 258 
LYS   CD  CE   sing N N 259 
LYS   CD  HD2  sing N N 260 
LYS   CD  HD3  sing N N 261 
LYS   CE  NZ   sing N N 262 
LYS   CE  HE2  sing N N 263 
LYS   CE  HE3  sing N N 264 
LYS   NZ  HZ1  sing N N 265 
LYS   NZ  HZ2  sing N N 266 
LYS   NZ  HZ3  sing N N 267 
LYS   OXT HXT  sing N N 268 
MET   N   CA   sing N N 269 
MET   N   H    sing N N 270 
MET   N   H2   sing N N 271 
MET   CA  C    sing N N 272 
MET   CA  CB   sing N N 273 
MET   CA  HA   sing N N 274 
MET   C   O    doub N N 275 
MET   C   OXT  sing N N 276 
MET   CB  CG   sing N N 277 
MET   CB  HB2  sing N N 278 
MET   CB  HB3  sing N N 279 
MET   CG  SD   sing N N 280 
MET   CG  HG2  sing N N 281 
MET   CG  HG3  sing N N 282 
MET   SD  CE   sing N N 283 
MET   CE  HE1  sing N N 284 
MET   CE  HE2  sing N N 285 
MET   CE  HE3  sing N N 286 
MET   OXT HXT  sing N N 287 
PHE   N   CA   sing N N 288 
PHE   N   H    sing N N 289 
PHE   N   H2   sing N N 290 
PHE   CA  C    sing N N 291 
PHE   CA  CB   sing N N 292 
PHE   CA  HA   sing N N 293 
PHE   C   O    doub N N 294 
PHE   C   OXT  sing N N 295 
PHE   CB  CG   sing N N 296 
PHE   CB  HB2  sing N N 297 
PHE   CB  HB3  sing N N 298 
PHE   CG  CD1  doub Y N 299 
PHE   CG  CD2  sing Y N 300 
PHE   CD1 CE1  sing Y N 301 
PHE   CD1 HD1  sing N N 302 
PHE   CD2 CE2  doub Y N 303 
PHE   CD2 HD2  sing N N 304 
PHE   CE1 CZ   doub Y N 305 
PHE   CE1 HE1  sing N N 306 
PHE   CE2 CZ   sing Y N 307 
PHE   CE2 HE2  sing N N 308 
PHE   CZ  HZ   sing N N 309 
PHE   OXT HXT  sing N N 310 
PRO   N   CA   sing N N 311 
PRO   N   CD   sing N N 312 
PRO   N   H    sing N N 313 
PRO   CA  C    sing N N 314 
PRO   CA  CB   sing N N 315 
PRO   CA  HA   sing N N 316 
PRO   C   O    doub N N 317 
PRO   C   OXT  sing N N 318 
PRO   CB  CG   sing N N 319 
PRO   CB  HB2  sing N N 320 
PRO   CB  HB3  sing N N 321 
PRO   CG  CD   sing N N 322 
PRO   CG  HG2  sing N N 323 
PRO   CG  HG3  sing N N 324 
PRO   CD  HD2  sing N N 325 
PRO   CD  HD3  sing N N 326 
PRO   OXT HXT  sing N N 327 
SER   N   CA   sing N N 328 
SER   N   H    sing N N 329 
SER   N   H2   sing N N 330 
SER   CA  C    sing N N 331 
SER   CA  CB   sing N N 332 
SER   CA  HA   sing N N 333 
SER   C   O    doub N N 334 
SER   C   OXT  sing N N 335 
SER   CB  OG   sing N N 336 
SER   CB  HB2  sing N N 337 
SER   CB  HB3  sing N N 338 
SER   OG  HG   sing N N 339 
SER   OXT HXT  sing N N 340 
THR   N   CA   sing N N 341 
THR   N   H    sing N N 342 
THR   N   H2   sing N N 343 
THR   CA  C    sing N N 344 
THR   CA  CB   sing N N 345 
THR   CA  HA   sing N N 346 
THR   C   O    doub N N 347 
THR   C   OXT  sing N N 348 
THR   CB  OG1  sing N N 349 
THR   CB  CG2  sing N N 350 
THR   CB  HB   sing N N 351 
THR   OG1 HG1  sing N N 352 
THR   CG2 HG21 sing N N 353 
THR   CG2 HG22 sing N N 354 
THR   CG2 HG23 sing N N 355 
THR   OXT HXT  sing N N 356 
TRP   N   CA   sing N N 357 
TRP   N   H    sing N N 358 
TRP   N   H2   sing N N 359 
TRP   CA  C    sing N N 360 
TRP   CA  CB   sing N N 361 
TRP   CA  HA   sing N N 362 
TRP   C   O    doub N N 363 
TRP   C   OXT  sing N N 364 
TRP   CB  CG   sing N N 365 
TRP   CB  HB2  sing N N 366 
TRP   CB  HB3  sing N N 367 
TRP   CG  CD1  doub Y N 368 
TRP   CG  CD2  sing Y N 369 
TRP   CD1 NE1  sing Y N 370 
TRP   CD1 HD1  sing N N 371 
TRP   CD2 CE2  doub Y N 372 
TRP   CD2 CE3  sing Y N 373 
TRP   NE1 CE2  sing Y N 374 
TRP   NE1 HE1  sing N N 375 
TRP   CE2 CZ2  sing Y N 376 
TRP   CE3 CZ3  doub Y N 377 
TRP   CE3 HE3  sing N N 378 
TRP   CZ2 CH2  doub Y N 379 
TRP   CZ2 HZ2  sing N N 380 
TRP   CZ3 CH2  sing Y N 381 
TRP   CZ3 HZ3  sing N N 382 
TRP   CH2 HH2  sing N N 383 
TRP   OXT HXT  sing N N 384 
TYR   N   CA   sing N N 385 
TYR   N   H    sing N N 386 
TYR   N   H2   sing N N 387 
TYR   CA  C    sing N N 388 
TYR   CA  CB   sing N N 389 
TYR   CA  HA   sing N N 390 
TYR   C   O    doub N N 391 
TYR   C   OXT  sing N N 392 
TYR   CB  CG   sing N N 393 
TYR   CB  HB2  sing N N 394 
TYR   CB  HB3  sing N N 395 
TYR   CG  CD1  doub Y N 396 
TYR   CG  CD2  sing Y N 397 
TYR   CD1 CE1  sing Y N 398 
TYR   CD1 HD1  sing N N 399 
TYR   CD2 CE2  doub Y N 400 
TYR   CD2 HD2  sing N N 401 
TYR   CE1 CZ   doub Y N 402 
TYR   CE1 HE1  sing N N 403 
TYR   CE2 CZ   sing Y N 404 
TYR   CE2 HE2  sing N N 405 
TYR   CZ  OH   sing N N 406 
TYR   OH  HH   sing N N 407 
TYR   OXT HXT  sing N N 408 
VAL   N   CA   sing N N 409 
VAL   N   H    sing N N 410 
VAL   N   H2   sing N N 411 
VAL   CA  C    sing N N 412 
VAL   CA  CB   sing N N 413 
VAL   CA  HA   sing N N 414 
VAL   C   O    doub N N 415 
VAL   C   OXT  sing N N 416 
VAL   CB  CG1  sing N N 417 
VAL   CB  CG2  sing N N 418 
VAL   CB  HB   sing N N 419 
VAL   CG1 HG11 sing N N 420 
VAL   CG1 HG12 sing N N 421 
VAL   CG1 HG13 sing N N 422 
VAL   CG2 HG21 sing N N 423 
VAL   CG2 HG22 sing N N 424 
VAL   CG2 HG23 sing N N 425 
VAL   OXT HXT  sing N N 426 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171399 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002344 
_pdbx_deposit_group.group_description   
'Crystollographic structure of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitor' 
_pdbx_deposit_group.group_title         
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_atom_sites.entry_id                    7I58 
_atom_sites.fract_transf_matrix[1][1]   0.011372 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000707 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017370 
_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]   0.030576 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
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   . SER   A 1 1   ? 18.892 7.441   24.360 1.00 37.41  ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 20.184 7.232   23.711 1.00 38.37  ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 20.083 6.133   22.625 1.00 38.42  ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 19.190 5.295   22.705 1.00 39.20  ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 21.249 6.884   24.748 1.00 40.90  ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 20.918 5.664   25.398 1.00 44.11  ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 20.949 6.174   21.608 1.00 37.28  ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 20.920 5.182   20.527 1.00 36.69  ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 21.293 5.675   19.141 1.00 35.85  ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 20.837 6.731   18.716 1.00 35.48  ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 22.089 4.870   18.395 1.00 35.60  ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 22.544 5.199   17.044 1.00 35.17  ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 22.559 4.032   16.021 1.00 34.46  ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 22.692 2.851   16.378 1.00 34.62  ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.932 5.835   17.110 1.00 35.43  ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 22.489 4.391   14.737 1.00 33.30  ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.635 3.457   13.634 1.00 33.01  ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 24.065 3.628   13.062 1.00 32.92  ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.521 4.750   12.851 1.00 31.31  ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.560 3.670   12.545 1.00 33.06  ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 20.145 3.784   13.140 1.00 33.21  ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.643 2.569   11.458 1.00 34.16  ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.199 4.654   12.287 1.00 34.33  ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.782 2.518   12.849 1.00 34.58  ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 26.116 2.567   12.248 1.00 36.60  ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 26.066 1.813   10.938 1.00 37.40  ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 25.992 0.585   10.946 1.00 36.61  ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.200 2.010   13.184 1.00 37.18  ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.385 2.882   14.406 1.00 38.77  ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 28.252 3.965   14.387 1.00 39.84  ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 26.614 2.689   15.543 1.00 39.92  ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 28.377 4.806   15.481 1.00 41.09  ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 26.738 3.518   16.646 1.00 40.84  ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 27.632 4.568   16.619 1.00 42.08  ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 27.767 5.375   17.723 1.00 44.36  ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 26.003 2.573   9.822  1.00 38.21  ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 25.944 2.118   8.430  1.00 39.00  ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.160 2.680   7.650  1.00 40.74  ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.276 3.899   7.531  1.00 41.42  ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.576 2.470   7.755  1.00 39.39  ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.080 3.871   8.121  1.00 39.11  ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.630 2.284   6.239  1.00 40.67  ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.072 1.808   7.190  1.00 41.28  ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.281 2.199   6.455  1.00 42.16  ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.213 3.133   7.216  1.00 42.78  ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.669 2.788   8.300  1.00 42.71  ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.509 4.331   6.679  1.00 43.14  ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.326 5.309   7.427  1.00 43.38  ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.435 6.437   8.045  1.00 42.87  ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.922 7.540   8.272  1.00 42.96  ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.519 5.858   6.608  1.00 44.66  ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.773 4.986   6.612  1.00 48.74  ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.786 5.284   7.259  1.00 49.30  ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.758 3.893   5.859  1.00 50.33  ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.128 6.135   8.335  1.00 41.90  ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.146 7.077   8.940  1.00 41.04  ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.617 6.626   10.323 1.00 38.01  ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.588 5.435   10.628 1.00 37.00  ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.919 7.305   8.020  1.00 41.86  ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.241 7.802   6.625  1.00 44.29  ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 27.965 8.972   6.429  1.00 45.46  ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 26.801 7.112   5.499  1.00 45.71  ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.248 9.440   5.149  1.00 46.83  ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.088 7.565   4.213  1.00 46.87  ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 27.813 8.731   4.040  1.00 47.96  ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.122 9.174   2.770  1.00 49.52  ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.178 7.608   11.134 1.00 36.29  ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.528 7.423   12.427 1.00 35.15  ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.201 8.185   12.338 1.00 34.04  ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.223 9.373   12.059 1.00 34.03  ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.411 7.999   13.573 1.00 36.15  ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.678 8.295   14.900 1.00 37.55  ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.665 8.545   16.032 1.00 38.38  ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 27.153 9.431   17.072 1.00 39.03  ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 26.848 9.054   18.312 1.00 38.26  ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 26.950 7.778   18.671 1.00 37.75  ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 26.415 9.946   19.196 1.00 34.11  ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 24.060 7.522   12.540 1.00 33.32  ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.765 8.213   12.531 1.00 32.92  ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.247 8.292   13.957 1.00 31.92  ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 22.093 7.269   14.590 1.00 31.95  ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.709 7.575   11.594 1.00 33.72  ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.446 8.438   11.557 1.00 34.36  ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.275 7.393   10.185 1.00 34.06  ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 22.011 9.496   14.472 1.00 31.28  ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 21.477 9.744   15.823 1.00 31.06  ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 20.219 10.681  15.727 1.00 29.99  ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 19.872 11.147  14.630 1.00 29.79  ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 22.580 10.367  16.767 1.00 32.38  ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 23.619 9.340   17.168 1.00 32.51  ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 23.237 11.606  16.142 1.00 33.05  ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 19.561 10.964  16.870 1.00 29.35  ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 18.488 11.939  16.989 1.00 28.42  ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 19.204 13.269  17.034 1.00 29.16  ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 20.100 13.446  17.858 1.00 29.36  ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.688 11.740  18.298 1.00 26.95  ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 16.773 10.546  18.214 1.00 27.13  ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.163 9.449   18.584 1.00 27.92  ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 15.552 10.732  17.736 1.00 25.60  ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 18.863 14.180  16.104 1.00 29.52  ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 19.456 15.516  15.999 1.00 29.47  ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 19.566 16.247  17.366 1.00 29.69  ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 20.595 16.875  17.611 1.00 29.39  ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 18.678 16.376  14.977 1.00 29.17  ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.479 17.547  14.433 1.00 28.55  ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 18.582 18.672  13.988 1.00 31.40  ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.361 19.862  13.653 1.00 35.53  ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.318 21.015  14.326 1.00 39.32  ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 18.499 21.161  15.356 1.00 35.77  ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 20.079 22.038  13.953 1.00 42.38  ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 18.516 16.118  18.258 1.00 30.03  ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 18.412 16.755  19.612 1.00 30.76  ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 19.360 16.150  20.673 1.00 32.56  ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 19.689 16.839  21.634 1.00 33.24  ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 16.946 16.827  20.138 1.00 30.34  ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 16.349 15.545  20.652 1.00 32.28  ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 15.960 14.522  19.798 1.00 34.22  ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 16.071 15.174  21.924 1.00 33.29  ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 15.489 13.564  20.583 1.00 34.51  ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 15.525 13.921  21.871 1.00 34.28  ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 19.840 14.914  20.452 1.00 33.85  ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 20.803 14.174  21.290 1.00 35.30  ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 22.245 14.159  20.667 1.00 36.96  ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 23.141 13.496  21.209 1.00 36.96  ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 20.327 12.697  21.465 1.00 35.09  ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 18.970 12.455  22.163 1.00 36.60  ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 18.736 10.976  22.431 1.00 36.10  ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 18.854 13.238  23.477 1.00 37.23  ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 22.435 14.801  19.496 1.00 37.32  ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 23.716 14.820  18.803 1.00 38.24  ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 24.824 15.456  19.683 1.00 39.79  ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 24.625 16.551  20.213 1.00 40.06  ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 23.584 15.525  17.445 1.00 37.46  ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 25.951 14.711  19.892 1.00 40.26  ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 27.121 15.088  20.727 1.00 41.16  ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 28.005 16.180  20.063 1.00 42.87  ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 27.810 16.479  18.870 1.00 43.52  ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 27.963 13.814  21.103 1.00 41.47  ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 28.906 13.471  20.080 1.00 41.81  ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 27.114 12.600  21.451 1.00 41.94  ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 29.002 16.751  20.806 1.00 43.31  ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 29.912 17.748  20.244 1.00 44.21  ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 30.672 17.172  19.041 1.00 44.21  ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 30.778 17.833  18.014 1.00 43.77  ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 30.893 18.298  21.309 1.00 45.96  ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 32.032 19.097  20.729 1.00 49.38  ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 31.911 20.458  20.488 1.00 51.25  ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 33.251 18.685  20.291 1.00 50.88  ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 33.060 20.833  19.945 1.00 51.77  ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 33.901 19.807  19.810 1.00 51.99  ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 31.178 15.936  19.179 1.00 44.94  ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 31.901 15.181  18.148 1.00 46.06  ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 31.059 14.873  16.867 1.00 46.50  ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 31.637 14.622  15.804 1.00 46.99  ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 32.449 13.871  18.748 1.00 47.80  ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 33.592 13.269  17.968 1.00 52.42  ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.769 13.596  18.210 1.00 53.48  ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 33.268 12.374  17.005 1.00 52.88  ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 29.711 14.823  16.978 1.00 45.87  ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 28.867 14.591  15.807 1.00 45.02  ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 28.921 15.851  14.931 1.00 44.40  ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 29.044 15.740  13.713 1.00 44.52  ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 27.418 14.307  16.218 1.00 46.20  ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 27.189 12.934  16.804 1.00 48.79  ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 27.937 12.005  16.442 1.00 47.87  ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 26.245 12.786  17.614 1.00 50.69  ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 28.865 17.054  15.554 1.00 42.94  ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.920 18.331  14.838 1.00 41.99  ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 30.330 18.630  14.254 1.00 40.38  ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 30.438 19.119  13.131 1.00 38.82  ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 28.459 19.454  15.754 1.00 42.22  ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 27.012 19.375  16.118 1.00 42.27  ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 26.486 18.922  17.294 1.00 43.30  ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 25.903 19.855  15.337 1.00 41.68  ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 25.116 19.076  17.289 1.00 43.35  ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 24.738 19.680  16.113 1.00 42.47  ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 25.784 20.418  14.061 1.00 41.59  ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 23.474 20.054  15.652 1.00 42.63  ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.533 20.792  13.610 1.00 42.15  ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 23.395 20.605  14.397 1.00 42.40  ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 31.393 18.273  14.997 1.00 39.86  ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.766 18.398  14.510 1.00 40.41  ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 33.050 17.445  13.331 1.00 41.06  ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 34.169 17.443  12.819 1.00 42.11  ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 33.744 18.110  15.644 1.00 40.53  ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 32.045 16.674  12.862 1.00 40.03  ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 32.164 15.728  11.755 1.00 39.73  ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.811 15.540  11.036 1.00 39.17  ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.532 14.465  10.528 1.00 39.71  ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.686 14.398  12.297 1.00 41.54  ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 34.191 14.395  12.506 1.00 46.43  ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 34.979 14.496  11.547 1.00 48.27  ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 34.621 14.311  13.765 1.00 46.94  ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 29.973 16.586  11.015 1.00 38.31  ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.635 16.582  10.426 1.00 38.13  ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.642 16.181  8.959  1.00 38.63  ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.533 16.587  8.222  1.00 38.86  ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 28.002 17.986  10.600 1.00 37.64  ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.637 18.224  9.945  1.00 37.93  ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.565 17.289  10.523 1.00 38.79  ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.215 19.648  10.089 1.00 37.22  ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.653 15.377  8.531  1.00 38.85  ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.494 14.978  7.134  1.00 38.93  ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 26.152 15.589  6.644  1.00 38.17  ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 26.105 16.314  5.633  1.00 38.53  ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.538 13.429  6.980  1.00 39.97  ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 27.352 13.010  5.528  1.00 40.59  ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 28.831 12.860  7.541  1.00 40.45  ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 25.078 15.335  7.399  1.00 36.39  ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 23.760 15.859  7.073  1.00 35.19  ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 22.911 15.964  8.327  1.00 34.31  ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 23.015 15.130  9.206  1.00 34.82  ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 23.081 14.986  6.013  1.00 34.50  ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.612 15.241  5.798  1.00 34.89  ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 21.052 16.123  4.922  1.00 36.02  ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.516 14.541  6.418  1.00 34.83  ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.675 16.049  4.988  1.00 36.33  ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.323 15.073  5.885  1.00 35.62  ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.431 13.502  7.351  1.00 34.97  ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 18.067 14.609  6.263  1.00 35.87  ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.184 13.079  7.752  1.00 35.52  ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 18.019 13.617  7.195  1.00 35.38  ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 22.081 16.989  8.420  1.00 33.13  ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 21.173 17.154  9.551  1.00 32.56  ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 19.839 17.734  9.089  1.00 32.46  ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 19.780 18.395  8.053  1.00 31.82  ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 21.820 17.927  10.707 1.00 34.00  ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.354 19.311  10.369 1.00 37.13  ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.325 20.420  10.298 1.00 40.60  ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 21.289 21.135  9.272  1.00 43.99  ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 20.526 20.550  11.248 1.00 39.08  ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 18.760 17.428  9.793  1.00 32.97  ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.440 17.930  9.415  1.00 34.20  ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.643 18.135  10.648 1.00 35.11  ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 16.186 17.146  11.226 1.00 36.01  ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.721 16.975  8.450  1.00 35.22  ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.545 17.609  7.723  1.00 40.28  ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 14.833 18.412  8.342  1.00 39.38  ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 15.352 17.307  6.510  1.00 44.49  ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.454 19.398  11.075 1.00 34.66  ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 15.691 19.652  12.301 0.50 35.04  ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 15.689 19.657  12.299 0.50 35.03  ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 14.224 19.166  12.204 1.00 34.92  ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 13.718 18.576  13.166 1.00 35.20  ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 15.783 21.124  12.708 0.50 35.86  ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 15.755 21.135  12.685 0.50 35.80  ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 14.897 21.451  13.767 0.50 37.65  ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 14.942 21.931  11.837 0.50 37.62  ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 13.545 19.372  11.031 1.00 33.56  ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 12.152 18.902  10.911 1.00 32.93  ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 12.031 17.389  10.883 1.00 31.26  ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 10.934 16.897  11.083 1.00 31.54  ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 11.413 19.530  9.736  1.00 35.47  ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 11.538 18.793  8.527  1.00 39.68  ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 13.124 16.657  10.609 1.00 29.40  ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 13.111 15.213  10.656 1.00 28.38  ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 13.690 14.668  11.973 1.00 28.57  ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 13.531 13.465  12.217 1.00 29.96  ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 13.887 14.614  9.475  1.00 27.81  ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 13.226 14.802  8.102  1.00 25.08  ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 14.032 14.135  7.025  1.00 26.73  ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 14.034 12.688  7.190  1.00 28.47  ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 14.135 11.809  6.196  1.00 29.71  ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 14.287 12.228  4.940  1.00 28.58  ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 14.107 10.506  6.450  1.00 28.70  ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 14.375 15.504  12.801 1.00 27.24  ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 15.086 15.099  14.048 1.00 26.93  ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 16.207 14.110  13.688 1.00 26.68  ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 16.480 13.194  14.460 1.00 27.61  ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 14.149 14.597  15.235 1.00 27.98  ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 14.794 14.166  16.598 1.00 28.94  ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 15.556 14.970  17.185 1.00 28.07  ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 14.498 13.022  17.084 1.00 30.26  ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 16.874 14.286  12.519 1.00 25.84  ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 17.977 13.378  12.169 1.00 25.76  ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 19.330 14.065  11.995 1.00 25.61  ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 19.398 15.149  11.439 1.00 25.38  ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.659 12.520  10.936 1.00 26.10  ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 16.586 11.489  11.103 1.00 27.35  ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 16.343 10.797  9.748  1.00 28.09  ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 16.924 10.511  12.293 1.00 26.76  ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 20.405 13.423  12.467 1.00 25.71  ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 21.737 13.952  12.259 1.00 26.38  ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 22.635 12.815  11.908 1.00 27.61  ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 22.750 11.906  12.680 1.00 28.09  ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 22.295 14.701  13.473 1.00 25.19  ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 23.574 15.540  13.190 1.00 25.58  ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 23.549 16.882  13.900 1.00 24.97  ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 24.865 14.770  13.510 1.00 25.56  ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 23.299 12.882  10.764 1.00 29.74  ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 24.283 11.903  10.318 1.00 32.04  ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 25.681 12.522  10.527 1.00 33.40  ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 25.868 13.702  10.242 1.00 33.32  ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 24.041 11.522  8.841  1.00 33.48  ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 25.136 10.590  8.327  1.00 34.55  ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 22.654 10.891  8.640  1.00 34.24  ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 26.634 11.767  11.082 1.00 34.44  ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 28.005 12.246  11.231 1.00 36.76  ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 29.040 11.178  10.772 1.00 38.97  ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 28.654 10.046  10.477 1.00 38.72  ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 28.267 12.773  12.635 1.00 39.06  ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 28.431 11.744  13.596 1.00 42.74  ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 30.326 11.548  10.626 1.00 41.23  ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 31.338 10.616  10.107 1.00 44.16  ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 32.121 9.833   11.143 1.00 46.32  ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 32.651 10.418  12.085 1.00 46.83  ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 32.322 11.336  9.191  1.00 46.89  ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 32.887 12.478  9.817  1.00 50.92  ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 32.262 8.506   10.900 1.00 47.47  ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 33.000 7.546   11.732 1.00 48.49  ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 34.294 7.041   11.018 1.00 49.19  ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 34.451 7.166   9.798  1.00 49.16  ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 32.076 6.403   12.224 1.00 49.70  ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 31.715 5.561   11.139 1.00 51.18  ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 30.819 6.900   12.873 1.00 49.93  ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? 35.229 6.518   11.798 1.00 49.57  ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? 36.516 6.025   11.294 1.00 50.49  ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? 36.414 4.572   10.832 1.00 51.02  ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? 37.004 4.175   9.823  1.00 50.68  ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? 37.611 6.152   12.391 1.00 51.79  ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? 37.072 5.838   13.690 1.00 52.77  ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? 38.273 7.509   12.406 1.00 51.74  ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? 35.681 3.781   11.616 1.00 51.53  ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? 35.472 2.364   11.410 1.00 52.44  ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 34.195 2.109   10.605 1.00 52.68  ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 33.313 2.981   10.519 1.00 52.44  ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? 35.404 1.655   12.764 1.00 52.92  ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 34.119 0.913   9.978  1.00 52.44  ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 32.962 0.540   9.189  1.00 52.56  ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 31.850 0.053   10.106 1.00 51.81  ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 32.092 -0.588  11.127 1.00 52.33  ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 33.311 -0.519  8.122  1.00 54.93  ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 33.920 0.061   6.846  1.00 59.29  ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 33.006 -0.009  5.639  1.00 64.46  ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 32.547 -1.086  5.236  1.00 66.88  ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 32.752 1.139   5.009  1.00 64.51  ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 30.646 0.439   9.753  1.00 50.54  ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 29.426 0.069   10.439 1.00 49.88  ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 28.836 -1.137  9.750  1.00 48.60  ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 29.116 -1.387  8.567  1.00 48.56  ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 27.994 -1.882  10.478 1.00 47.37  ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 27.446 -3.102  9.924  1.00 46.37  ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 25.917 -3.200  9.948  1.00 43.45  ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 25.390 -4.248  9.567  1.00 43.16  ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 28.110 -4.298  10.590 1.00 48.60  ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 29.869 -4.466  10.177 1.00 55.80  ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 25.203 -2.112  10.299 1.00 41.24  ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 23.739 -2.142  10.262 1.00 40.64  ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 23.272 -2.016  8.842  1.00 40.35  ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 23.830 -1.228  8.078  1.00 40.34  ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 23.098 -1.037  11.124 1.00 41.97  ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 23.153 -1.336  12.613 1.00 43.65  ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 22.769 -2.459  13.007 1.00 43.64  ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 23.601 -0.459  13.375 1.00 44.70  ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 22.285 -2.843  8.461  1.00 40.00  ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 21.695 -2.832  7.114  1.00 39.18  ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 20.412 -1.970  7.165  1.00 38.33  ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 19.628 -2.146  8.088  1.00 38.69  ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 21.471 -4.290  6.597  1.00 39.57  ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 22.744 -4.928  6.472  1.00 39.62  ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 20.754 -4.332  5.243  1.00 40.23  ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 20.224 -1.009  6.238  1.00 37.19  ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 19.013 -0.172  6.246  1.00 36.88  ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 17.958 -0.891  5.429  1.00 35.80  ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 18.274 -1.356  4.361  1.00 36.91  ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 19.237 1.276   5.708  1.00 37.14  ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 20.336 2.056   6.466  1.00 38.02  ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 17.941 2.068   5.660  1.00 37.58  ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 20.400 1.912   7.993  1.00 39.31  ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 16.723 -0.984  5.907  1.00 34.28  ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 15.636 -1.609  5.170  1.00 33.65  ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 15.293 -0.717  3.964  1.00 35.61  ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 15.229 0.506   4.114  1.00 35.95  ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 14.412 -1.732  6.070  1.00 31.98  ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 15.115 -1.310  2.767  1.00 36.60  ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 14.671 -0.590  1.567  1.00 37.99  ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 13.339 -1.236  1.175  1.00 39.38  ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 13.290 -2.128  0.317  1.00 41.74  ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 15.725 -0.652  0.450  1.00 39.48  ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 17.092 -0.143  0.900  1.00 37.78  ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 17.044 1.278   1.420  1.00 36.47  ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 18.364 1.810   1.745  1.00 35.79  ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 18.571 3.015   2.265  1.00 37.78  ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 17.550 3.815   2.532  1.00 37.86  ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 19.799 3.414   2.564  1.00 37.41  ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 12.257 -0.789  1.847  1.00 38.41  ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 10.956 -1.424  1.787  1.00 38.82  ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 9.773  -0.474  2.187  1.00 38.67  ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 9.987  0.679   2.553  1.00 37.34  ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 11.022 -2.626  2.733  1.00 37.40  ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 11.078 -2.161  4.497  1.00 36.50  ? 56  CYS   A SG  1 
ATOM   392  N  N   A ASP   A 1 51  ? 8.531  -0.993  2.135  0.50 39.56  ? 57  ASP   A N   1 
ATOM   393  N  N   B ASP   A 1 51  ? 8.545  -1.010  2.134  0.50 39.60  ? 57  ASP   A N   1 
ATOM   394  C  CA  A ASP   A 1 51  ? 7.333  -0.289  2.591  0.50 39.79  ? 57  ASP   A CA  1 
ATOM   395  C  CA  B ASP   A 1 51  ? 7.314  -0.354  2.547  0.50 39.98  ? 57  ASP   A CA  1 
ATOM   396  C  C   A ASP   A 1 51  ? 6.660  -1.062  3.752  0.50 38.99  ? 57  ASP   A C   1 
ATOM   397  C  C   B ASP   A 1 51  ? 6.653  -1.191  3.672  0.50 39.03  ? 57  ASP   A C   1 
ATOM   398  O  O   A ASP   A 1 51  ? 5.434  -1.031  3.883  0.50 39.84  ? 57  ASP   A O   1 
ATOM   399  O  O   B ASP   A 1 51  ? 5.430  -1.337  3.695  0.50 39.83  ? 57  ASP   A O   1 
ATOM   400  C  CB  A ASP   A 1 51  ? 6.338  0.009   1.448  0.50 43.18  ? 57  ASP   A CB  1 
ATOM   401  C  CB  B ASP   A 1 51  ? 6.353  -0.211  1.358  0.50 43.73  ? 57  ASP   A CB  1 
ATOM   402  C  CG  A ASP   A 1 51  ? 5.630  -1.176  0.808  0.50 46.07  ? 57  ASP   A CG  1 
ATOM   403  C  CG  B ASP   A 1 51  ? 5.410  0.969   1.461  0.50 47.67  ? 57  ASP   A CG  1 
ATOM   404  O  OD1 A ASP   A 1 51  ? 5.844  -2.324  1.267  0.50 45.80  ? 57  ASP   A OD1 1 
ATOM   405  O  OD1 B ASP   A 1 51  ? 5.703  1.899   2.242  0.50 49.33  ? 57  ASP   A OD1 1 
ATOM   406  O  OD2 A ASP   A 1 51  ? 4.872  -0.959  -0.161 0.50 48.08  ? 57  ASP   A OD2 1 
ATOM   407  O  OD2 B ASP   A 1 51  ? 4.382  0.962   0.765  0.50 49.51  ? 57  ASP   A OD2 1 
ATOM   408  N  N   . CYS   A 1 52  ? 7.466  -1.753  4.588  1.00 36.97  ? 58  CYS   A N   1 
ATOM   409  C  CA  . CYS   A 1 52  ? 6.984  -2.549  5.715  1.00 33.88  ? 58  CYS   A CA  1 
ATOM   410  C  C   . CYS   A 1 52  ? 6.254  -1.671  6.685  1.00 31.53  ? 58  CYS   A C   1 
ATOM   411  O  O   . CYS   A 1 52  ? 6.702  -0.561  6.932  1.00 31.33  ? 58  CYS   A O   1 
ATOM   412  C  CB  . CYS   A 1 52  ? 8.139  -3.244  6.419  1.00 32.65  ? 58  CYS   A CB  1 
ATOM   413  S  SG  . CYS   A 1 52  ? 8.749  -4.720  5.585  1.00 32.47  ? 58  CYS   A SG  1 
ATOM   414  N  N   . GLN   A 1 53  ? 5.130  -2.157  7.213  1.00 30.30  ? 59  GLN   A N   1 
ATOM   415  C  CA  . GLN   A 1 53  ? 4.356  -1.465  8.238  1.00 29.48  ? 59  GLN   A CA  1 
ATOM   416  C  C   . GLN   A 1 53  ? 4.237  -2.284  9.560  1.00 27.29  ? 59  GLN   A C   1 
ATOM   417  O  O   . GLN   A 1 53  ? 3.349  -2.000  10.356 1.00 26.53  ? 59  GLN   A O   1 
ATOM   418  C  CB  . GLN   A 1 53  ? 2.968  -1.072  7.734  1.00 32.00  ? 59  GLN   A CB  1 
ATOM   419  C  CG  . GLN   A 1 53  ? 2.965  0.089   6.755  1.00 36.06  ? 59  GLN   A CG  1 
ATOM   420  C  CD  . GLN   A 1 53  ? 1.551  0.573   6.596  1.00 41.30  ? 59  GLN   A CD  1 
ATOM   421  O  OE1 . GLN   A 1 53  ? 0.942  0.431   5.526  1.00 44.63  ? 59  GLN   A OE1 1 
ATOM   422  N  NE2 . GLN   A 1 53  ? 0.982  1.127   7.689  1.00 40.55  ? 59  GLN   A NE2 1 
ATOM   423  N  N   . THR   A 1 54  ? 5.050  -3.332  9.725  1.00 26.49  ? 60  THR   A N   1 
ATOM   424  C  CA  . THR   A 1 54  ? 5.152  -4.133  10.932 1.00 26.28  ? 60  THR   A CA  1 
ATOM   425  C  C   . THR   A 1 54  ? 6.639  -4.365  11.213 1.00 25.44  ? 60  THR   A C   1 
ATOM   426  O  O   . THR   A 1 54  ? 7.439  -4.529  10.283 1.00 25.22  ? 60  THR   A O   1 
ATOM   427  C  CB  . THR   A 1 54  ? 4.320  -5.426  10.922 1.00 28.06  ? 60  THR   A CB  1 
ATOM   428  O  OG1 . THR   A 1 54  ? 4.928  -6.366  10.060 1.00 31.25  ? 60  THR   A OG1 1 
ATOM   429  C  CG2 . THR   A 1 54  ? 2.858  -5.224  10.542 1.00 28.31  ? 60  THR   A CG2 1 
ATOM   430  N  N   . GLY   A 1 55  ? 7.007  -4.335  12.505 1.00 24.14  ? 61  GLY   A N   1 
ATOM   431  C  CA  . GLY   A 1 55  ? 8.394  -4.494  12.929 1.00 23.79  ? 61  GLY   A CA  1 
ATOM   432  C  C   . GLY   A 1 55  ? 8.590  -4.681  14.419 1.00 24.14  ? 61  GLY   A C   1 
ATOM   433  O  O   . GLY   A 1 55  ? 7.642  -4.994  15.123 1.00 24.11  ? 61  GLY   A O   1 
ATOM   434  N  N   . VAL   A 1 56  ? 9.836  -4.523  14.907 1.00 24.54  ? 62  VAL   A N   1 
ATOM   435  C  CA  . VAL   A 1 56  ? 10.210 -4.673  16.331 1.00 24.88  ? 62  VAL   A CA  1 
ATOM   436  C  C   . VAL   A 1 56  ? 11.075 -3.474  16.763 1.00 24.15  ? 62  VAL   A C   1 
ATOM   437  O  O   . VAL   A 1 56  ? 11.948 -3.056  15.999 1.00 24.48  ? 62  VAL   A O   1 
ATOM   438  C  CB  . VAL   A 1 56  ? 10.936 -6.032  16.540 1.00 25.52  ? 62  VAL   A CB  1 
ATOM   439  C  CG1 . VAL   A 1 56  ? 11.671 -6.085  17.884 1.00 26.36  ? 62  VAL   A CG1 1 
ATOM   440  C  CG2 . VAL   A 1 56  ? 9.949  -7.194  16.399 1.00 25.81  ? 62  VAL   A CG2 1 
ATOM   441  N  N   . TYR   A 1 57  ? 10.798 -2.862  17.933 1.00 24.43  ? 63  TYR   A N   1 
ATOM   442  C  CA  . TYR   A 1 57  ? 11.596 -1.712  18.382 1.00 24.77  ? 63  TYR   A CA  1 
ATOM   443  C  C   . TYR   A 1 57  ? 12.115 -1.900  19.799 1.00 26.71  ? 63  TYR   A C   1 
ATOM   444  O  O   . TYR   A 1 57  ? 11.412 -2.496  20.643 1.00 26.86  ? 63  TYR   A O   1 
ATOM   445  C  CB  . TYR   A 1 57  ? 10.867 -0.346  18.210 1.00 24.02  ? 63  TYR   A CB  1 
ATOM   446  C  CG  . TYR   A 1 57  ? 9.910  0.018   19.340 1.00 24.31  ? 63  TYR   A CG  1 
ATOM   447  C  CD1 . TYR   A 1 57  ? 8.703  -0.646  19.497 1.00 24.85  ? 63  TYR   A CD1 1 
ATOM   448  C  CD2 . TYR   A 1 57  ? 10.233 1.004   20.265 1.00 25.53  ? 63  TYR   A CD2 1 
ATOM   449  C  CE1 . TYR   A 1 57  ? 7.815  -0.309  20.509 1.00 25.92  ? 63  TYR   A CE1 1 
ATOM   450  C  CE2 . TYR   A 1 57  ? 9.365  1.329   21.307 1.00 26.63  ? 63  TYR   A CE2 1 
ATOM   451  C  CZ  . TYR   A 1 57  ? 8.167  0.649   21.439 1.00 27.26  ? 63  TYR   A CZ  1 
ATOM   452  O  OH  . TYR   A 1 57  ? 7.286  0.957   22.440 1.00 28.69  ? 63  TYR   A OH  1 
ATOM   453  N  N   . TYR   A 1 58  ? 13.329 -1.368  20.078 1.00 27.18  ? 64  TYR   A N   1 
ATOM   454  C  CA  . TYR   A 1 58  ? 13.858 -1.434  21.423 1.00 29.42  ? 64  TYR   A CA  1 
ATOM   455  C  C   . TYR   A 1 58  ? 13.332 -0.237  22.235 1.00 30.68  ? 64  TYR   A C   1 
ATOM   456  O  O   . TYR   A 1 58  ? 13.269 0.883   21.724 1.00 29.88  ? 64  TYR   A O   1 
ATOM   457  C  CB  . TYR   A 1 58  ? 15.391 -1.471  21.423 1.00 30.71  ? 64  TYR   A CB  1 
ATOM   458  C  CG  . TYR   A 1 58  ? 15.939 -1.646  22.817 1.00 34.55  ? 64  TYR   A CG  1 
ATOM   459  C  CD1 . TYR   A 1 58  ? 15.592 -2.751  23.590 1.00 36.61  ? 64  TYR   A CD1 1 
ATOM   460  C  CD2 . TYR   A 1 58  ? 16.753 -0.679  23.393 1.00 36.50  ? 64  TYR   A CD2 1 
ATOM   461  C  CE1 . TYR   A 1 58  ? 16.068 -2.906  24.880 1.00 39.06  ? 64  TYR   A CE1 1 
ATOM   462  C  CE2 . TYR   A 1 58  ? 17.254 -0.834  24.683 1.00 38.32  ? 64  TYR   A CE2 1 
ATOM   463  C  CZ  . TYR   A 1 58  ? 16.887 -1.934  25.435 1.00 40.29  ? 64  TYR   A CZ  1 
ATOM   464  O  OH  . TYR   A 1 58  ? 17.416 -2.104  26.702 1.00 42.52  ? 64  TYR   A OH  1 
ATOM   465  N  N   . CYS   A 1 59  ? 12.918 -0.494  23.500 1.00 32.56  ? 65  CYS   A N   1 
ATOM   466  C  CA  . CYS   A 1 59  ? 12.417 0.460   24.476 1.00 34.08  ? 65  CYS   A CA  1 
ATOM   467  C  C   . CYS   A 1 59  ? 13.343 0.284   25.691 1.00 37.95  ? 65  CYS   A C   1 
ATOM   468  O  O   . CYS   A 1 59  ? 13.216 -0.716  26.398 1.00 40.03  ? 65  CYS   A O   1 
ATOM   469  C  CB  . CYS   A 1 59  ? 10.968 0.120   24.822 1.00 34.26  ? 65  CYS   A CB  1 
ATOM   470  S  SG  . CYS   A 1 59  ? 10.204 1.194   26.071 1.00 36.78  ? 65  CYS   A SG  1 
ATOM   471  N  N   . SER   A 1 60  ? 14.302 1.208   25.905 1.00 38.95  ? 66  SER   A N   1 
ATOM   472  C  CA  . SER   A 1 60  ? 15.224 1.149   27.049 1.00 41.24  ? 66  SER   A CA  1 
ATOM   473  C  C   . SER   A 1 60  ? 14.533 1.383   28.424 1.00 43.12  ? 66  SER   A C   1 
ATOM   474  O  O   . SER   A 1 60  ? 15.037 0.942   29.463 1.00 44.71  ? 66  SER   A O   1 
ATOM   475  C  CB  . SER   A 1 60  ? 16.376 2.132   26.868 1.00 41.05  ? 66  SER   A CB  1 
ATOM   476  O  OG  . SER   A 1 60  ? 15.956 3.486   26.912 1.00 41.40  ? 66  SER   A OG  1 
ATOM   477  N  N   . SER   A 1 61  ? 13.384 2.056   28.425 1.00 42.68  ? 67  SER   A N   1 
ATOM   478  C  CA  . SER   A 1 61  ? 12.612 2.297   29.639 1.00 43.98  ? 67  SER   A CA  1 
ATOM   479  C  C   . SER   A 1 61  ? 11.954 0.992   30.182 1.00 45.78  ? 67  SER   A C   1 
ATOM   480  O  O   . SER   A 1 61  ? 11.397 0.988   31.279 1.00 46.93  ? 67  SER   A O   1 
ATOM   481  C  CB  . SER   A 1 61  ? 11.559 3.376   29.398 1.00 42.75  ? 67  SER   A CB  1 
ATOM   482  O  OG  . SER   A 1 61  ? 10.464 2.886   28.640 1.00 41.94  ? 67  SER   A OG  1 
ATOM   483  N  N   . ARG   A 1 62  ? 11.973 -0.088  29.394 1.00 45.67  ? 68  ARG   A N   1 
ATOM   484  C  CA  . ARG   A 1 62  ? 11.412 -1.379  29.763 1.00 46.75  ? 68  ARG   A CA  1 
ATOM   485  C  C   . ARG   A 1 62  ? 12.395 -2.523  29.571 1.00 47.33  ? 68  ARG   A C   1 
ATOM   486  O  O   . ARG   A 1 62  ? 11.992 -3.654  29.785 1.00 48.43  ? 68  ARG   A O   1 
ATOM   487  C  CB  . ARG   A 1 62  ? 10.175 -1.668  28.897 1.00 45.75  ? 68  ARG   A CB  1 
ATOM   488  C  CG  . ARG   A 1 62  ? 9.003  -0.741  29.160 1.00 45.63  ? 68  ARG   A CG  1 
ATOM   489  C  CD  . ARG   A 1 62  ? 8.287  -1.136  30.444 1.00 47.11  ? 68  ARG   A CD  1 
ATOM   490  N  NE  . ARG   A 1 62  ? 7.140  -0.283  30.756 1.00 46.53  ? 68  ARG   A NE  1 
ATOM   491  C  CZ  . ARG   A 1 62  ? 7.214  0.879   31.389 1.00 46.31  ? 68  ARG   A CZ  1 
ATOM   492  N  NH1 . ARG   A 1 62  ? 8.386  1.357   31.777 1.00 46.69  ? 68  ARG   A NH1 1 
ATOM   493  N  NH2 . ARG   A 1 62  ? 6.119  1.587   31.615 1.00 45.67  ? 68  ARG   A NH2 1 
ATOM   494  N  N   . ARG   A 1 63  ? 13.649 -2.256  29.117 1.00 46.47  ? 69  ARG   A N   1 
ATOM   495  C  CA  . ARG   A 1 63  ? 14.688 -3.223  28.713 1.00 46.43  ? 69  ARG   A CA  1 
ATOM   496  C  C   . ARG   A 1 63  ? 14.064 -4.305  27.802 1.00 45.90  ? 69  ARG   A C   1 
ATOM   497  O  O   . ARG   A 1 63  ? 14.339 -5.501  27.948 1.00 46.85  ? 69  ARG   A O   1 
ATOM   498  C  CB  . ARG   A 1 63  ? 15.407 -3.842  29.918 1.00 48.21  ? 69  ARG   A CB  1 
ATOM   499  C  CG  . ARG   A 1 63  ? 16.181 -2.848  30.779 1.00 50.39  ? 69  ARG   A CG  1 
ATOM   500  C  CD  . ARG   A 1 63  ? 17.068 -3.607  31.749 1.00 53.33  ? 69  ARG   A CD  1 
ATOM   501  N  NE  . ARG   A 1 63  ? 17.684 -2.742  32.758 1.00 56.83  ? 69  ARG   A NE  1 
ATOM   502  C  CZ  . ARG   A 1 63  ? 17.348 -2.729  34.047 1.00 56.87  ? 69  ARG   A CZ  1 
ATOM   503  N  NH1 . ARG   A 1 63  ? 16.378 -3.519  34.494 1.00 56.48  ? 69  ARG   A NH1 1 
ATOM   504  N  NH2 . ARG   A 1 63  ? 17.960 -1.904  34.892 1.00 55.82  ? 69  ARG   A NH2 1 
ATOM   505  N  N   . LYS   A 1 64  ? 13.184 -3.864  26.875 1.00 43.53  ? 70  LYS   A N   1 
ATOM   506  C  CA  . LYS   A 1 64  ? 12.372 -4.760  26.077 1.00 41.50  ? 70  LYS   A CA  1 
ATOM   507  C  C   . LYS   A 1 64  ? 12.188 -4.359  24.612 1.00 38.35  ? 70  LYS   A C   1 
ATOM   508  O  O   . LYS   A 1 64  ? 12.058 -3.167  24.328 1.00 38.04  ? 70  LYS   A O   1 
ATOM   509  C  CB  . LYS   A 1 64  ? 10.984 -4.843  26.726 1.00 43.43  ? 70  LYS   A CB  1 
ATOM   510  C  CG  . LYS   A 1 64  ? 10.531 -6.252  27.026 1.00 50.17  ? 70  LYS   A CG  1 
ATOM   511  C  CD  . LYS   A 1 64  ? 9.175  -6.257  27.718 1.00 56.57  ? 70  LYS   A CD  1 
ATOM   512  C  CE  . LYS   A 1 64  ? 9.173  -7.062  28.996 1.00 61.55  ? 70  LYS   A CE  1 
ATOM   513  N  NZ  . LYS   A 1 64  ? 10.006 -6.427  30.060 1.00 64.79  ? 70  LYS   A NZ  1 
ATOM   514  N  N   . HIS   A 1 65  ? 12.083 -5.383  23.699 1.00 35.96  ? 71  HIS   A N   1 
ATOM   515  C  CA  . HIS   A 1 65  ? 11.827 -5.269  22.247 1.00 34.63  ? 71  HIS   A CA  1 
ATOM   516  C  C   . HIS   A 1 65  ? 10.338 -5.610  22.030 1.00 33.78  ? 71  HIS   A C   1 
ATOM   517  O  O   . HIS   A 1 65  ? 9.840  -6.620  22.588 1.00 34.53  ? 71  HIS   A O   1 
ATOM   518  C  CB  . HIS   A 1 65  ? 12.723 -6.214  21.410 1.00 34.17  ? 71  HIS   A CB  1 
ATOM   519  C  CG  . HIS   A 1 65  ? 14.193 -5.914  21.492 1.00 36.03  ? 71  HIS   A CG  1 
ATOM   520  N  ND1 . HIS   A 1 65  ? 14.840 -5.196  20.505 1.00 37.33  ? 71  HIS   A ND1 1 
ATOM   521  C  CD2 . HIS   A 1 65  ? 15.089 -6.218  22.466 1.00 37.50  ? 71  HIS   A CD2 1 
ATOM   522  C  CE1 . HIS   A 1 65  ? 16.110 -5.124  20.878 1.00 37.65  ? 71  HIS   A CE1 1 
ATOM   523  N  NE2 . HIS   A 1 65  ? 16.304 -5.702  22.065 1.00 38.19  ? 71  HIS   A NE2 1 
ATOM   524  N  N   . TYR   A 1 66  ? 9.601  -4.692  21.382 1.00 31.23  ? 72  TYR   A N   1 
ATOM   525  C  CA  . TYR   A 1 66  ? 8.170  -4.855  21.211 1.00 30.42  ? 72  TYR   A CA  1 
ATOM   526  C  C   . TYR   A 1 66  ? 7.764  -4.924  19.729 1.00 29.47  ? 72  TYR   A C   1 
ATOM   527  O  O   . TYR   A 1 66  ? 8.066  -4.006  18.976 1.00 28.73  ? 72  TYR   A O   1 
ATOM   528  C  CB  . TYR   A 1 66  ? 7.411  -3.674  21.856 1.00 31.17  ? 72  TYR   A CB  1 
ATOM   529  C  CG  . TYR   A 1 66  ? 7.477  -3.560  23.371 1.00 33.21  ? 72  TYR   A CG  1 
ATOM   530  C  CD1 . TYR   A 1 66  ? 6.690  -4.368  24.184 1.00 35.59  ? 72  TYR   A CD1 1 
ATOM   531  C  CD2 . TYR   A 1 66  ? 8.211  -2.555  23.981 1.00 34.61  ? 72  TYR   A CD2 1 
ATOM   532  C  CE1 . TYR   A 1 66  ? 6.721  -4.248  25.574 1.00 37.54  ? 72  TYR   A CE1 1 
ATOM   533  C  CE2 . TYR   A 1 66  ? 8.215  -2.395  25.364 1.00 36.51  ? 72  TYR   A CE2 1 
ATOM   534  C  CZ  . TYR   A 1 66  ? 7.490  -3.260  26.163 1.00 38.64  ? 72  TYR   A CZ  1 
ATOM   535  O  OH  . TYR   A 1 66  ? 7.504  -3.114  27.543 1.00 42.55  ? 72  TYR   A OH  1 
ATOM   536  N  N   . PRO   A 1 67  ? 6.977  -5.948  19.323 1.00 29.33  ? 73  PRO   A N   1 
ATOM   537  C  CA  . PRO   A 1 67  ? 6.458  -5.960  17.946 1.00 29.57  ? 73  PRO   A CA  1 
ATOM   538  C  C   . PRO   A 1 67  ? 5.355  -4.888  17.754 1.00 29.23  ? 73  PRO   A C   1 
ATOM   539  O  O   . PRO   A 1 67  ? 4.442  -4.781  18.560 1.00 29.87  ? 73  PRO   A O   1 
ATOM   540  C  CB  . PRO   A 1 67  ? 5.920  -7.388  17.759 1.00 29.87  ? 73  PRO   A CB  1 
ATOM   541  C  CG  . PRO   A 1 67  ? 6.260  -8.139  19.025 1.00 30.58  ? 73  PRO   A CG  1 
ATOM   542  C  CD  . PRO   A 1 67  ? 6.504  -7.110  20.101 1.00 29.40  ? 73  PRO   A CD  1 
ATOM   543  N  N   . VAL   A 1 68  ? 5.424  -4.111  16.679 1.00 27.67  ? 74  VAL   A N   1 
ATOM   544  C  CA  . VAL   A 1 68  ? 4.454  -3.039  16.409 1.00 26.89  ? 74  VAL   A CA  1 
ATOM   545  C  C   . VAL   A 1 68  ? 4.038  -2.968  14.951 1.00 26.50  ? 74  VAL   A C   1 
ATOM   546  O  O   . VAL   A 1 68  ? 4.744  -3.457  14.064 1.00 25.17  ? 74  VAL   A O   1 
ATOM   547  C  CB  . VAL   A 1 68  ? 5.001  -1.651  16.840 1.00 26.76  ? 74  VAL   A CB  1 
ATOM   548  C  CG1 . VAL   A 1 68  ? 4.866  -1.402  18.346 1.00 26.43  ? 74  VAL   A CG1 1 
ATOM   549  C  CG2 . VAL   A 1 68  ? 6.426  -1.421  16.319 1.00 26.86  ? 74  VAL   A CG2 1 
ATOM   550  N  N   . SER   A 1 69  ? 2.846  -2.379  14.724 1.00 27.13  ? 75  SER   A N   1 
ATOM   551  C  CA  . SER   A 1 69  ? 2.236  -1.958  13.462 1.00 27.33  ? 75  SER   A CA  1 
ATOM   552  C  C   . SER   A 1 69  ? 2.456  -0.457  13.450 1.00 26.63  ? 75  SER   A C   1 
ATOM   553  O  O   . SER   A 1 69  ? 2.073  0.197   14.424 1.00 26.02  ? 75  SER   A O   1 
ATOM   554  C  CB  . SER   A 1 69  ? 0.733  -2.159  13.522 1.00 29.32  ? 75  SER   A CB  1 
ATOM   555  O  OG  . SER   A 1 69  ? 0.447  -3.511  13.260 1.00 34.37  ? 75  SER   A OG  1 
ATOM   556  N  N   . PHE   A 1 70  ? 3.076  0.108   12.408 1.00 26.32  ? 76  PHE   A N   1 
ATOM   557  C  CA  . PHE   A 1 70  ? 3.322  1.551   12.392 1.00 26.21  ? 76  PHE   A CA  1 
ATOM   558  C  C   . PHE   A 1 70  ? 2.799  2.145   11.075 1.00 27.63  ? 76  PHE   A C   1 
ATOM   559  O  O   . PHE   A 1 70  ? 2.709  1.429   10.072 1.00 27.53  ? 76  PHE   A O   1 
ATOM   560  C  CB  . PHE   A 1 70  ? 4.823  1.871   12.648 1.00 25.15  ? 76  PHE   A CB  1 
ATOM   561  C  CG  . PHE   A 1 70  ? 5.783  1.120   11.744 1.00 24.66  ? 76  PHE   A CG  1 
ATOM   562  C  CD1 . PHE   A 1 70  ? 6.247  -0.140  12.090 1.00 24.78  ? 76  PHE   A CD1 1 
ATOM   563  C  CD2 . PHE   A 1 70  ? 6.158  1.646   10.508 1.00 25.31  ? 76  PHE   A CD2 1 
ATOM   564  C  CE1 . PHE   A 1 70  ? 7.090  -0.849  11.241 1.00 25.22  ? 76  PHE   A CE1 1 
ATOM   565  C  CE2 . PHE   A 1 70  ? 7.040  0.960   9.684  1.00 25.53  ? 76  PHE   A CE2 1 
ATOM   566  C  CZ  . PHE   A 1 70  ? 7.500  -0.288  10.054 1.00 25.02  ? 76  PHE   A CZ  1 
ATOM   567  N  N   . SER   A 1 71  ? 2.415  3.434   11.083 1.00 27.88  ? 77  SER   A N   1 
ATOM   568  C  CA  . SER   A 1 71  ? 1.907  4.073   9.865  1.00 28.93  ? 77  SER   A CA  1 
ATOM   569  C  C   . SER   A 1 71  ? 3.074  4.474   8.991  1.00 29.84  ? 77  SER   A C   1 
ATOM   570  O  O   . SER   A 1 71  ? 4.171  4.597   9.512  1.00 28.98  ? 77  SER   A O   1 
ATOM   571  C  CB  . SER   A 1 71  ? 1.078  5.312   10.201 1.00 29.54  ? 77  SER   A CB  1 
ATOM   572  O  OG  . SER   A 1 71  ? 1.529  6.019   11.345 1.00 29.49  ? 77  SER   A OG  1 
ATOM   573  N  N   . LYS   A 1 72  ? 2.835  4.728   7.674  1.00 31.76  ? 78  LYS   A N   1 
ATOM   574  C  CA  . LYS   A 1 72  ? 3.845  5.189   6.721  1.00 33.18  ? 78  LYS   A CA  1 
ATOM   575  C  C   . LYS   A 1 72  ? 4.418  6.574   7.103  1.00 32.48  ? 78  LYS   A C   1 
ATOM   576  O  O   . LYS   A 1 72  ? 3.724  7.329   7.777  1.00 32.22  ? 78  LYS   A O   1 
ATOM   577  C  CB  . LYS   A 1 72  ? 3.235  5.185   5.302  1.00 35.80  ? 78  LYS   A CB  1 
ATOM   578  C  CG  . LYS   A 1 72  ? 3.067  3.756   4.839  1.00 40.53  ? 78  LYS   A CG  1 
ATOM   579  C  CD  . LYS   A 1 72  ? 2.028  3.513   3.792  1.00 45.82  ? 78  LYS   A CD  1 
ATOM   580  C  CE  . LYS   A 1 72  ? 2.352  2.190   3.164  1.00 49.65  ? 78  LYS   A CE  1 
ATOM   581  N  NZ  . LYS   A 1 72  ? 1.427  1.835   2.064  1.00 52.92  ? 78  LYS   A NZ  1 
ATOM   582  N  N   . PRO   A 1 73  ? 5.674  6.932   6.732  1.00 32.37  ? 79  PRO   A N   1 
ATOM   583  C  CA  . PRO   A 1 73  ? 6.214  8.242   7.141  1.00 32.22  ? 79  PRO   A CA  1 
ATOM   584  C  C   . PRO   A 1 73  ? 5.328  9.381   6.667  1.00 32.42  ? 79  PRO   A C   1 
ATOM   585  O  O   . PRO   A 1 73  ? 4.906  9.411   5.507  1.00 32.64  ? 79  PRO   A O   1 
ATOM   586  C  CB  . PRO   A 1 73  ? 7.641  8.248   6.594  1.00 33.61  ? 79  PRO   A CB  1 
ATOM   587  C  CG  . PRO   A 1 73  ? 7.954  6.820   6.319  1.00 34.41  ? 79  PRO   A CG  1 
ATOM   588  C  CD  . PRO   A 1 73  ? 6.664  6.173   5.947  1.00 33.07  ? 79  PRO   A CD  1 
ATOM   589  N  N   A SER   A 1 74  ? 4.959  10.267  7.596  0.50 31.64  ? 80  SER   A N   1 
ATOM   590  N  N   B SER   A 1 74  ? 4.958  10.267  7.596  0.50 31.62  ? 80  SER   A N   1 
ATOM   591  C  CA  A SER   A 1 74  ? 4.011  11.336  7.312  0.50 31.41  ? 80  SER   A CA  1 
ATOM   592  C  CA  B SER   A 1 74  ? 4.011  11.335  7.311  0.50 31.40  ? 80  SER   A CA  1 
ATOM   593  C  C   A SER   A 1 74  ? 4.384  12.621  8.049  0.50 30.71  ? 80  SER   A C   1 
ATOM   594  C  C   B SER   A 1 74  ? 4.384  12.621  8.050  0.50 30.69  ? 80  SER   A C   1 
ATOM   595  O  O   A SER   A 1 74  ? 5.238  12.605  8.939  0.50 31.12  ? 80  SER   A O   1 
ATOM   596  O  O   B SER   A 1 74  ? 5.238  12.605  8.940  0.50 31.08  ? 80  SER   A O   1 
ATOM   597  C  CB  A SER   A 1 74  ? 2.604  10.898  7.736  0.50 33.08  ? 80  SER   A CB  1 
ATOM   598  C  CB  B SER   A 1 74  ? 2.604  10.898  7.736  0.50 33.05  ? 80  SER   A CB  1 
ATOM   599  O  OG  A SER   A 1 74  ? 2.269  9.567   7.358  0.50 36.06  ? 80  SER   A OG  1 
ATOM   600  O  OG  B SER   A 1 74  ? 2.269  9.567   7.358  0.50 36.09  ? 80  SER   A OG  1 
ATOM   601  N  N   . LEU   A 1 75  ? 3.716  13.731  7.713  1.00 29.88  ? 81  LEU   A N   1 
ATOM   602  C  CA  . LEU   A 1 75  ? 3.939  14.991  8.402  1.00 29.56  ? 81  LEU   A CA  1 
ATOM   603  C  C   . LEU   A 1 75  ? 2.983  14.995  9.616  1.00 30.04  ? 81  LEU   A C   1 
ATOM   604  O  O   . LEU   A 1 75  ? 1.769  15.152  9.466  1.00 30.40  ? 81  LEU   A O   1 
ATOM   605  C  CB  . LEU   A 1 75  ? 3.655  16.172  7.477  1.00 29.39  ? 81  LEU   A CB  1 
ATOM   606  C  CG  . LEU   A 1 75  ? 4.237  17.487  7.937  1.00 29.84  ? 81  LEU   A CG  1 
ATOM   607  C  CD1 . LEU   A 1 75  ? 5.739  17.443  7.919  1.00 29.90  ? 81  LEU   A CD1 1 
ATOM   608  C  CD2 . LEU   A 1 75  ? 3.726  18.619  7.069  1.00 30.20  ? 81  LEU   A CD2 1 
ATOM   609  N  N   . ILE   A 1 76  ? 3.530  14.767  10.807 1.00 30.00  ? 82  ILE   A N   1 
ATOM   610  C  CA  . ILE   A 1 76  ? 2.732  14.675  12.027 1.00 30.68  ? 82  ILE   A CA  1 
ATOM   611  C  C   . ILE   A 1 76  ? 3.059  15.825  12.985 1.00 31.27  ? 82  ILE   A C   1 
ATOM   612  O  O   . ILE   A 1 76  ? 4.220  16.189  13.154 1.00 30.95  ? 82  ILE   A O   1 
ATOM   613  C  CB  . ILE   A 1 76  ? 2.974  13.304  12.762 1.00 30.86  ? 82  ILE   A CB  1 
ATOM   614  C  CG1 . ILE   A 1 76  ? 3.061  12.092  11.792 1.00 30.85  ? 82  ILE   A CG1 1 
ATOM   615  C  CG2 . ILE   A 1 76  ? 1.953  13.063  13.896 1.00 31.41  ? 82  ILE   A CG2 1 
ATOM   616  C  CD1 . ILE   A 1 76  ? 1.878  11.656  11.242 1.00 32.59  ? 82  ILE   A CD1 1 
ATOM   617  N  N   . PHE   A 1 77  ? 2.037  16.370  13.630 1.00 31.98  ? 83  PHE   A N   1 
ATOM   618  C  CA  . PHE   A 1 77  ? 2.205  17.402  14.625 1.00 33.29  ? 83  PHE   A CA  1 
ATOM   619  C  C   . PHE   A 1 77  ? 2.755  16.753  15.913 1.00 33.86  ? 83  PHE   A C   1 
ATOM   620  O  O   . PHE   A 1 77  ? 2.251  15.717  16.350 1.00 34.72  ? 83  PHE   A O   1 
ATOM   621  C  CB  . PHE   A 1 77  ? 0.876  18.114  14.893 1.00 33.99  ? 83  PHE   A CB  1 
ATOM   622  C  CG  . PHE   A 1 77  ? 1.101  19.330  15.755 1.00 35.50  ? 83  PHE   A CG  1 
ATOM   623  C  CD1 . PHE   A 1 77  ? 1.788  20.431  15.262 1.00 37.16  ? 83  PHE   A CD1 1 
ATOM   624  C  CD2 . PHE   A 1 77  ? 0.728  19.333  17.087 1.00 36.16  ? 83  PHE   A CD2 1 
ATOM   625  C  CE1 . PHE   A 1 77  ? 2.041  21.536  16.079 1.00 38.06  ? 83  PHE   A CE1 1 
ATOM   626  C  CE2 . PHE   A 1 77  ? 0.990  20.431  17.898 1.00 37.12  ? 83  PHE   A CE2 1 
ATOM   627  C  CZ  . PHE   A 1 77  ? 1.626  21.530  17.388 1.00 37.11  ? 83  PHE   A CZ  1 
ATOM   628  N  N   . VAL   A 1 78  ? 3.809  17.352  16.493 1.00 33.53  ? 84  VAL   A N   1 
ATOM   629  C  CA  . VAL   A 1 78  ? 4.507  16.872  17.691 1.00 33.44  ? 84  VAL   A CA  1 
ATOM   630  C  C   . VAL   A 1 78  ? 4.416  17.952  18.775 1.00 33.65  ? 84  VAL   A C   1 
ATOM   631  O  O   . VAL   A 1 78  ? 4.644  19.126  18.476 1.00 34.16  ? 84  VAL   A O   1 
ATOM   632  C  CB  . VAL   A 1 78  ? 6.005  16.598  17.335 1.00 33.68  ? 84  VAL   A CB  1 
ATOM   633  C  CG1 . VAL   A 1 78  ? 6.832  16.251  18.564 1.00 33.74  ? 84  VAL   A CG1 1 
ATOM   634  C  CG2 . VAL   A 1 78  ? 6.156  15.555  16.237 1.00 33.68  ? 84  VAL   A CG2 1 
ATOM   635  N  N   . GLU   A 1 79  ? 4.134  17.572  20.027 1.00 33.60  ? 85  GLU   A N   1 
ATOM   636  C  CA  . GLU   A 1 79  ? 4.072  18.537  21.121 1.00 34.51  ? 85  GLU   A CA  1 
ATOM   637  C  C   . GLU   A 1 79  ? 5.384  19.270  21.345 1.00 34.41  ? 85  GLU   A C   1 
ATOM   638  O  O   . GLU   A 1 79  ? 6.449  18.713  21.120 1.00 33.71  ? 85  GLU   A O   1 
ATOM   639  C  CB  . GLU   A 1 79  ? 3.694  17.835  22.453 1.00 38.51  ? 85  GLU   A CB  1 
ATOM   640  C  CG  . GLU   A 1 79  ? 2.210  17.581  22.625 1.00 45.22  ? 85  GLU   A CG  1 
ATOM   641  C  CD  . GLU   A 1 79  ? 1.349  18.809  22.432 1.00 52.35  ? 85  GLU   A CD  1 
ATOM   642  O  OE1 . GLU   A 1 79  ? 1.516  19.783  23.201 1.00 55.54  ? 85  GLU   A OE1 1 
ATOM   643  O  OE2 . GLU   A 1 79  ? 0.527  18.806  21.490 1.00 54.29  ? 85  GLU   A OE2 1 
ATOM   644  N  N   . ALA   A 1 80  ? 5.299  20.494  21.870 1.00 35.48  ? 86  ALA   A N   1 
ATOM   645  C  CA  . ALA   A 1 80  ? 6.456  21.277  22.282 1.00 36.97  ? 86  ALA   A CA  1 
ATOM   646  C  C   . ALA   A 1 80  ? 7.139  20.590  23.481 1.00 38.43  ? 86  ALA   A C   1 
ATOM   647  O  O   . ALA   A 1 80  ? 6.479  20.039  24.362 1.00 38.59  ? 86  ALA   A O   1 
ATOM   648  C  CB  . ALA   A 1 80  ? 6.016  22.667  22.693 1.00 37.33  ? 86  ALA   A CB  1 
ATOM   649  N  N   . SER   A 1 81  ? 8.462  20.599  23.488 1.00 39.36  ? 87  SER   A N   1 
ATOM   650  C  CA  . SER   A 1 81  ? 9.278  20.024  24.558 1.00 40.19  ? 87  SER   A CA  1 
ATOM   651  C  C   . SER   A 1 81  ? 10.486 20.995  24.792 1.00 42.25  ? 87  SER   A C   1 
ATOM   652  O  O   . SER   A 1 81  ? 10.374 22.171  24.403 1.00 43.03  ? 87  SER   A O   1 
ATOM   653  C  CB  . SER   A 1 81  ? 9.693  18.595  24.198 1.00 39.68  ? 87  SER   A CB  1 
ATOM   654  O  OG  . SER   A 1 81  ? 10.778 18.574  23.291 1.00 39.44  ? 87  SER   A OG  1 
ATOM   655  N  N   . GLU   A 1 82  ? 11.577 20.574  25.483 1.00 42.99  ? 88  GLU   A N   1 
ATOM   656  C  CA  . GLU   A 1 82  ? 12.716 21.488  25.695 1.00 44.39  ? 88  GLU   A CA  1 
ATOM   657  C  C   . GLU   A 1 82  ? 13.732 21.512  24.501 1.00 43.87  ? 88  GLU   A C   1 
ATOM   658  O  O   . GLU   A 1 82  ? 14.618 22.384  24.451 1.00 44.38  ? 88  GLU   A O   1 
ATOM   659  C  CB  . GLU   A 1 82  ? 13.431 21.232  27.042 1.00 49.17  ? 88  GLU   A CB  1 
ATOM   660  C  CG  . GLU   A 1 82  ? 13.492 19.784  27.525 1.00 58.76  ? 88  GLU   A CG  1 
ATOM   661  C  CD  . GLU   A 1 82  ? 13.273 19.629  29.028 1.00 71.37  ? 88  GLU   A CD  1 
ATOM   662  O  OE1 . GLU   A 1 82  ? 12.178 19.167  29.427 1.00 74.06  ? 88  GLU   A OE1 1 
ATOM   663  O  OE2 . GLU   A 1 82  ? 14.191 19.982  29.809 1.00 74.72  ? 88  GLU   A OE2 1 
ATOM   664  N  N   . TYR   A 1 83  ? 13.578 20.571  23.542 1.00 42.26  ? 89  TYR   A N   1 
ATOM   665  C  CA  . TYR   A 1 83  ? 14.454 20.406  22.385 1.00 41.35  ? 89  TYR   A CA  1 
ATOM   666  C  C   . TYR   A 1 83  ? 13.922 21.064  21.109 1.00 40.62  ? 89  TYR   A C   1 
ATOM   667  O  O   . TYR   A 1 83  ? 14.695 21.547  20.267 1.00 39.77  ? 89  TYR   A O   1 
ATOM   668  C  CB  . TYR   A 1 83  ? 14.664 18.926  22.130 1.00 40.96  ? 89  TYR   A CB  1 
ATOM   669  C  CG  . TYR   A 1 83  ? 15.277 18.202  23.301 1.00 41.48  ? 89  TYR   A CG  1 
ATOM   670  C  CD1 . TYR   A 1 83  ? 14.487 17.519  24.211 1.00 42.73  ? 89  TYR   A CD1 1 
ATOM   671  C  CD2 . TYR   A 1 83  ? 16.650 18.163  23.473 1.00 42.30  ? 89  TYR   A CD2 1 
ATOM   672  C  CE1 . TYR   A 1 83  ? 15.048 16.801  25.254 1.00 43.69  ? 89  TYR   A CE1 1 
ATOM   673  C  CE2 . TYR   A 1 83  ? 17.226 17.425  24.495 1.00 43.52  ? 89  TYR   A CE2 1 
ATOM   674  C  CZ  . TYR   A 1 83  ? 16.422 16.754  25.393 1.00 44.65  ? 89  TYR   A CZ  1 
ATOM   675  O  OH  . TYR   A 1 83  ? 16.989 16.103  26.465 1.00 46.47  ? 89  TYR   A OH  1 
ATOM   676  N  N   . TYR   A 1 84  ? 12.600 21.067  20.968 1.00 40.46  ? 90  TYR   A N   1 
ATOM   677  C  CA  . TYR   A 1 84  ? 11.930 21.661  19.819 1.00 40.81  ? 90  TYR   A CA  1 
ATOM   678  C  C   . TYR   A 1 84  ? 10.641 22.335  20.263 1.00 41.91  ? 90  TYR   A C   1 
ATOM   679  O  O   . TYR   A 1 84  ? 9.954  21.813  21.163 1.00 42.67  ? 90  TYR   A O   1 
ATOM   680  C  CB  . TYR   A 1 84  ? 11.514 20.549  18.813 1.00 40.04  ? 90  TYR   A CB  1 
ATOM   681  C  CG  . TYR   A 1 84  ? 12.646 19.746  18.221 1.00 39.26  ? 90  TYR   A CG  1 
ATOM   682  C  CD1 . TYR   A 1 84  ? 13.359 20.216  17.123 1.00 39.38  ? 90  TYR   A CD1 1 
ATOM   683  C  CD2 . TYR   A 1 84  ? 12.982 18.501  18.733 1.00 39.18  ? 90  TYR   A CD2 1 
ATOM   684  C  CE1 . TYR   A 1 84  ? 14.381 19.467  16.555 1.00 39.62  ? 90  TYR   A CE1 1 
ATOM   685  C  CE2 . TYR   A 1 84  ? 14.009 17.749  18.181 1.00 39.20  ? 90  TYR   A CE2 1 
ATOM   686  C  CZ  . TYR   A 1 84  ? 14.686 18.220  17.072 1.00 39.58  ? 90  TYR   A CZ  1 
ATOM   687  O  OH  . TYR   A 1 84  ? 15.756 17.519  16.566 1.00 39.42  ? 90  TYR   A OH  1 
ATOM   688  N  N   . PRO   A 1 85  ? 10.185 23.385  19.544 1.00 41.79  ? 91  PRO   A N   1 
ATOM   689  C  CA  . PRO   A 1 85  ? 8.836  23.909  19.831 1.00 42.02  ? 91  PRO   A CA  1 
ATOM   690  C  C   . PRO   A 1 85  ? 7.727  22.992  19.216 1.00 41.46  ? 91  PRO   A C   1 
ATOM   691  O  O   . PRO   A 1 85  ? 8.025  21.954  18.589 1.00 40.55  ? 91  PRO   A O   1 
ATOM   692  C  CB  . PRO   A 1 85  ? 8.866  25.335  19.242 1.00 42.84  ? 91  PRO   A CB  1 
ATOM   693  C  CG  . PRO   A 1 85  ? 9.985  25.346  18.248 1.00 43.29  ? 91  PRO   A CG  1 
ATOM   694  C  CD  . PRO   A 1 85  ? 10.825 24.089  18.414 1.00 41.52  ? 91  PRO   A CD  1 
ATOM   695  N  N   . ALA   A 1 86  ? 6.439  23.358  19.408 1.00 41.12  ? 92  ALA   A N   1 
ATOM   696  C  CA  . ALA   A 1 86  ? 5.334  22.558  18.863 1.00 40.82  ? 92  ALA   A CA  1 
ATOM   697  C  C   . ALA   A 1 86  ? 5.344  22.804  17.375 1.00 40.98  ? 92  ALA   A C   1 
ATOM   698  O  O   . ALA   A 1 86  ? 5.294  23.958  16.954 1.00 41.09  ? 92  ALA   A O   1 
ATOM   699  C  CB  . ALA   A 1 86  ? 4.007  22.989  19.466 1.00 40.50  ? 92  ALA   A CB  1 
ATOM   700  N  N   . ARG   A 1 87  ? 5.541  21.742  16.586 1.00 40.19  ? 93  ARG   A N   1 
ATOM   701  C  CA  . ARG   A 1 87  ? 5.687  21.865  15.134 1.00 39.77  ? 93  ARG   A CA  1 
ATOM   702  C  C   . ARG   A 1 87  ? 5.319  20.519  14.422 1.00 38.59  ? 93  ARG   A C   1 
ATOM   703  O  O   . ARG   A 1 87  ? 5.075  19.524  15.107 1.00 38.82  ? 93  ARG   A O   1 
ATOM   704  C  CB  . ARG   A 1 87  ? 7.173  22.248  14.828 1.00 41.34  ? 93  ARG   A CB  1 
ATOM   705  C  CG  . ARG   A 1 87  ? 8.143  21.025  14.707 1.00 44.69  ? 93  ARG   A CG  1 
ATOM   706  C  CD  . ARG   A 1 87  ? 9.373  21.050  15.605 1.00 47.29  ? 93  ARG   A CD  1 
ATOM   707  N  NE  . ARG   A 1 87  ? 10.441 20.194  15.070 1.00 47.12  ? 93  ARG   A NE  1 
ATOM   708  C  CZ  . ARG   A 1 87  ? 10.559 18.892  15.311 1.00 45.73  ? 93  ARG   A CZ  1 
ATOM   709  N  NH1 . ARG   A 1 87  ? 9.674  18.269  16.085 1.00 43.65  ? 93  ARG   A NH1 1 
ATOM   710  N  NH2 . ARG   A 1 87  ? 11.564 18.204  14.786 1.00 44.23  ? 93  ARG   A NH2 1 
ATOM   711  N  N   . TYR   A 1 88  ? 5.358  20.481  13.057 1.00 36.94  ? 94  TYR   A N   1 
ATOM   712  C  CA  . TYR   A 1 88  ? 5.166  19.244  12.297 1.00 35.82  ? 94  TYR   A CA  1 
ATOM   713  C  C   . TYR   A 1 88  ? 6.538  18.638  11.962 1.00 33.30  ? 94  TYR   A C   1 
ATOM   714  O  O   . TYR   A 1 88  ? 7.402  19.285  11.355 1.00 33.46  ? 94  TYR   A O   1 
ATOM   715  C  CB  . TYR   A 1 88  ? 4.383  19.452  10.975 1.00 36.38  ? 94  TYR   A CB  1 
ATOM   716  C  CG  . TYR   A 1 88  ? 2.931  19.828  11.169 1.00 37.88  ? 94  TYR   A CG  1 
ATOM   717  C  CD1 . TYR   A 1 88  ? 1.939  18.861  11.197 1.00 38.45  ? 94  TYR   A CD1 1 
ATOM   718  C  CD2 . TYR   A 1 88  ? 2.548  21.155  11.292 1.00 38.88  ? 94  TYR   A CD2 1 
ATOM   719  C  CE1 . TYR   A 1 88  ? 0.608  19.202  11.381 1.00 39.44  ? 94  TYR   A CE1 1 
ATOM   720  C  CE2 . TYR   A 1 88  ? 1.219  21.508  11.483 1.00 39.81  ? 94  TYR   A CE2 1 
ATOM   721  C  CZ  . TYR   A 1 88  ? 0.250  20.531  11.522 1.00 40.43  ? 94  TYR   A CZ  1 
ATOM   722  O  OH  . TYR   A 1 88  ? -1.061 20.908  11.718 1.00 42.37  ? 94  TYR   A OH  1 
ATOM   723  N  N   . GLN   A 1 89  ? 6.734  17.398  12.395 1.00 30.80  ? 95  GLN   A N   1 
ATOM   724  C  CA  . GLN   A 1 89  ? 7.939  16.668  12.091 1.00 27.77  ? 95  GLN   A CA  1 
ATOM   725  C  C   . GLN   A 1 89  ? 7.612  15.797  10.895 1.00 26.61  ? 95  GLN   A C   1 
ATOM   726  O  O   . GLN   A 1 89  ? 6.550  15.163  10.856 1.00 25.68  ? 95  GLN   A O   1 
ATOM   727  C  CB  . GLN   A 1 89  ? 8.393  15.807  13.282 1.00 25.97  ? 95  GLN   A CB  1 
ATOM   728  C  CG  . GLN   A 1 89  ? 9.607  14.934  12.969 1.00 23.58  ? 95  GLN   A CG  1 
ATOM   729  C  CD  . GLN   A 1 89  ? 10.332 14.491  14.205 1.00 24.84  ? 95  GLN   A CD  1 
ATOM   730  O  OE1 . GLN   A 1 89  ? 10.762 15.289  15.020 1.00 25.11  ? 95  GLN   A OE1 1 
ATOM   731  N  NE2 . GLN   A 1 89  ? 10.479 13.204  14.392 1.00 26.35  ? 95  GLN   A NE2 1 
ATOM   732  N  N   . SER   A 1 90  ? 8.504  15.799  9.893  1.00 26.39  ? 96  SER   A N   1 
ATOM   733  C  CA  . SER   A 1 90  ? 8.338  14.994  8.678  1.00 26.34  ? 96  SER   A CA  1 
ATOM   734  C  C   . SER   A 1 90  ? 8.968  13.601  8.824  1.00 25.95  ? 96  SER   A C   1 
ATOM   735  O  O   . SER   A 1 90  ? 9.725  13.355  9.782  1.00 25.28  ? 96  SER   A O   1 
ATOM   736  C  CB  . SER   A 1 90  ? 8.934  15.725  7.472  1.00 28.85  ? 96  SER   A CB  1 
ATOM   737  O  OG  . SER   A 1 90  ? 10.279 16.107  7.709  1.00 31.83  ? 96  SER   A OG  1 
ATOM   738  N  N   . HIS   A 1 91  ? 8.571  12.669  7.923  1.00 26.94  ? 97  HIS   A N   1 
ATOM   739  C  CA  . HIS   A 1 91  ? 9.038  11.275  7.849  1.00 27.74  ? 97  HIS   A CA  1 
ATOM   740  C  C   . HIS   A 1 91  ? 8.827  10.510  9.182  1.00 26.62  ? 97  HIS   A C   1 
ATOM   741  O  O   . HIS   A 1 91  ? 9.600  9.614   9.542  1.00 24.92  ? 97  HIS   A O   1 
ATOM   742  C  CB  . HIS   A 1 91  ? 10.495 11.218  7.349  1.00 28.11  ? 97  HIS   A CB  1 
ATOM   743  C  CG  . HIS   A 1 91  ? 10.648 11.839  6.003  1.00 30.66  ? 97  HIS   A CG  1 
ATOM   744  N  ND1 . HIS   A 1 91  ? 10.884 11.080  4.890  1.00 31.69  ? 97  HIS   A ND1 1 
ATOM   745  C  CD2 . HIS   A 1 91  ? 10.538 13.135  5.630  1.00 32.54  ? 97  HIS   A CD2 1 
ATOM   746  C  CE1 . HIS   A 1 91  ? 10.937 11.933  3.886  1.00 33.26  ? 97  HIS   A CE1 1 
ATOM   747  N  NE2 . HIS   A 1 91  ? 10.720 13.179  4.288  1.00 33.27  ? 97  HIS   A NE2 1 
ATOM   748  N  N   . LEU   A 1 92  ? 7.737  10.851  9.880  1.00 26.08  ? 98  LEU   A N   1 
ATOM   749  C  CA  . LEU   A 1 92  ? 7.434  10.243  11.170 1.00 25.18  ? 98  LEU   A CA  1 
ATOM   750  C  C   . LEU   A 1 92  ? 6.419  9.123   11.027 1.00 25.02  ? 98  LEU   A C   1 
ATOM   751  O  O   . LEU   A 1 92  ? 5.503  9.208   10.221 1.00 25.72  ? 98  LEU   A O   1 
ATOM   752  C  CB  . LEU   A 1 92  ? 6.933  11.334  12.123 1.00 24.28  ? 98  LEU   A CB  1 
ATOM   753  C  CG  . LEU   A 1 92  ? 6.901  11.011  13.614 1.00 22.57  ? 98  LEU   A CG  1 
ATOM   754  C  CD1 . LEU   A 1 92  ? 8.231  10.485  14.099 1.00 21.66  ? 98  LEU   A CD1 1 
ATOM   755  C  CD2 . LEU   A 1 92  ? 6.498  12.206  14.380 1.00 22.81  ? 98  LEU   A CD2 1 
ATOM   756  N  N   . MET   A 1 93  ? 6.611  8.061   11.789 1.00 23.89  ? 99  MET   A N   1 
ATOM   757  C  CA  . MET   A 1 93  ? 5.759  6.884   11.778 1.00 23.44  ? 99  MET   A CA  1 
ATOM   758  C  C   . MET   A 1 93  ? 5.323  6.647   13.211 1.00 23.16  ? 99  MET   A C   1 
ATOM   759  O  O   . MET   A 1 93  ? 6.180  6.601   14.098 1.00 22.42  ? 99  MET   A O   1 
ATOM   760  C  CB  . MET   A 1 93  ? 6.570  5.705   11.267 1.00 23.70  ? 99  MET   A CB  1 
ATOM   761  C  CG  . MET   A 1 93  ? 7.082  5.927   9.831  1.00 25.64  ? 99  MET   A CG  1 
ATOM   762  S  SD  . MET   A 1 93  ? 8.084  4.562   9.298  1.00 28.06  ? 99  MET   A SD  1 
ATOM   763  C  CE  . MET   A 1 93  ? 9.519  4.788   10.339 1.00 22.61  ? 99  MET   A CE  1 
ATOM   764  N  N   . LEU   A 1 94  ? 4.000  6.563   13.459 1.00 23.68  ? 100 LEU   A N   1 
ATOM   765  C  CA  . LEU   A 1 94  ? 3.490  6.286   14.803 1.00 24.74  ? 100 LEU   A CA  1 
ATOM   766  C  C   . LEU   A 1 94  ? 2.976  4.873   14.979 1.00 24.46  ? 100 LEU   A C   1 
ATOM   767  O  O   . LEU   A 1 94  ? 2.339  4.311   14.073 1.00 22.84  ? 100 LEU   A O   1 
ATOM   768  C  CB  . LEU   A 1 94  ? 2.383  7.267   15.213 1.00 25.78  ? 100 LEU   A CB  1 
ATOM   769  C  CG  . LEU   A 1 94  ? 2.763  8.720   15.060 1.00 28.03  ? 100 LEU   A CG  1 
ATOM   770  C  CD1 . LEU   A 1 94  ? 1.527  9.573   14.964 1.00 29.62  ? 100 LEU   A CD1 1 
ATOM   771  C  CD2 . LEU   A 1 94  ? 3.701  9.131   16.180 1.00 27.10  ? 100 LEU   A CD2 1 
ATOM   772  N  N   . ALA   A 1 95  ? 3.203  4.350   16.198 1.00 24.85  ? 101 ALA   A N   1 
ATOM   773  C  CA  . ALA   A 1 95  ? 2.748  3.047   16.706 1.00 25.80  ? 101 ALA   A CA  1 
ATOM   774  C  C   . ALA   A 1 95  ? 2.158  3.188   18.131 1.00 26.10  ? 101 ALA   A C   1 
ATOM   775  O  O   . ALA   A 1 95  ? 2.489  4.107   18.872 1.00 25.59  ? 101 ALA   A O   1 
ATOM   776  C  CB  . ALA   A 1 95  ? 3.887  2.046   16.724 1.00 25.75  ? 101 ALA   A CB  1 
ATOM   777  N  N   . VAL   A 1 96  ? 1.258  2.276   18.499 1.00 27.27  ? 102 VAL   A N   1 
ATOM   778  C  CA  . VAL   A 1 96  ? 0.684  2.219   19.837 1.00 28.24  ? 102 VAL   A CA  1 
ATOM   779  C  C   . VAL   A 1 96  ? 1.732  1.461   20.656 1.00 29.38  ? 102 VAL   A C   1 
ATOM   780  O  O   . VAL   A 1 96  ? 2.022  0.281   20.383 1.00 29.56  ? 102 VAL   A O   1 
ATOM   781  C  CB  . VAL   A 1 96  ? -0.717 1.521   19.874 1.00 28.66  ? 102 VAL   A CB  1 
ATOM   782  C  CG1 . VAL   A 1 96  ? -1.213 1.334   21.303 1.00 29.59  ? 102 VAL   A CG1 1 
ATOM   783  C  CG2 . VAL   A 1 96  ? -1.740 2.295   19.067 1.00 29.39  ? 102 VAL   A CG2 1 
ATOM   784  N  N   . GLY   A 1 97  ? 2.345  2.159   21.605 1.00 29.78  ? 103 GLY   A N   1 
ATOM   785  C  CA  . GLY   A 1 97  ? 3.366  1.538   22.430 1.00 31.05  ? 103 GLY   A CA  1 
ATOM   786  C  C   . GLY   A 1 97  ? 3.983  2.456   23.446 1.00 32.86  ? 103 GLY   A C   1 
ATOM   787  O  O   . GLY   A 1 97  ? 3.883  3.674   23.304 1.00 33.15  ? 103 GLY   A O   1 
ATOM   788  N  N   . HIS   A 1 98  ? 4.640  1.874   24.472 1.00 33.36  ? 104 HIS   A N   1 
ATOM   789  C  CA  . HIS   A 1 98  ? 5.291  2.672   25.486 1.00 34.75  ? 104 HIS   A CA  1 
ATOM   790  C  C   . HIS   A 1 98  ? 6.547  3.341   24.966 1.00 34.63  ? 104 HIS   A C   1 
ATOM   791  O  O   . HIS   A 1 98  ? 7.383  2.716   24.315 1.00 34.00  ? 104 HIS   A O   1 
ATOM   792  C  CB  . HIS   A 1 98  ? 5.583  1.842   26.752 1.00 37.45  ? 104 HIS   A CB  1 
ATOM   793  C  CG  . HIS   A 1 98  ? 6.113  2.666   27.878 1.00 39.76  ? 104 HIS   A CG  1 
ATOM   794  N  ND1 . HIS   A 1 98  ? 5.328  3.612   28.498 1.00 41.10  ? 104 HIS   A ND1 1 
ATOM   795  C  CD2 . HIS   A 1 98  ? 7.364  2.729   28.385 1.00 40.90  ? 104 HIS   A CD2 1 
ATOM   796  C  CE1 . HIS   A 1 98  ? 6.113  4.191   29.395 1.00 42.58  ? 104 HIS   A CE1 1 
ATOM   797  N  NE2 . HIS   A 1 98  ? 7.348  3.697   29.352 1.00 42.63  ? 104 HIS   A NE2 1 
ATOM   798  N  N   . SER   A 1 99  ? 6.699  4.609   25.311 1.00 35.42  ? 105 SER   A N   1 
ATOM   799  C  CA  . SER   A 1 99  ? 7.834  5.421   24.922 1.00 35.98  ? 105 SER   A CA  1 
ATOM   800  C  C   . SER   A 1 99  ? 8.104  6.476   26.023 1.00 36.41  ? 105 SER   A C   1 
ATOM   801  O  O   . SER   A 1 99  ? 7.161  7.051   26.549 1.00 37.23  ? 105 SER   A O   1 
ATOM   802  C  CB  . SER   A 1 99  ? 7.498  6.123   23.616 1.00 37.23  ? 105 SER   A CB  1 
ATOM   803  O  OG  . SER   A 1 99  ? 8.587  6.903   23.166 1.00 40.13  ? 105 SER   A OG  1 
ATOM   804  N  N   . GLU   A 1 100 ? 9.369  6.700   26.385 1.00 35.99  ? 106 GLU   A N   1 
ATOM   805  C  CA  . GLU   A 1 100 ? 9.837  7.722   27.349 1.00 36.40  ? 106 GLU   A CA  1 
ATOM   806  C  C   . GLU   A 1 100 ? 10.964 8.538   26.710 1.00 36.09  ? 106 GLU   A C   1 
ATOM   807  O  O   . GLU   A 1 100 ? 11.601 8.008   25.805 1.00 36.59  ? 106 GLU   A O   1 
ATOM   808  C  CB  . GLU   A 1 100 ? 10.306 7.088   28.668 1.00 38.65  ? 106 GLU   A CB  1 
ATOM   809  C  CG  . GLU   A 1 100 ? 9.131  6.793   29.558 1.00 40.56  ? 106 GLU   A CG  1 
ATOM   810  C  CD  . GLU   A 1 100 ? 9.487  5.972   30.771 1.00 43.24  ? 106 GLU   A CD  1 
ATOM   811  O  OE1 . GLU   A 1 100 ? 10.461 6.337   31.467 1.00 43.47  ? 106 GLU   A OE1 1 
ATOM   812  O  OE2 . GLU   A 1 100 ? 8.798  4.958   31.016 1.00 43.22  ? 106 GLU   A OE2 1 
ATOM   813  N  N   . PRO   A 1 101 ? 11.210 9.823   27.076 1.00 35.53  ? 107 PRO   A N   1 
ATOM   814  C  CA  . PRO   A 1 101 ? 12.263 10.600  26.381 1.00 35.19  ? 107 PRO   A CA  1 
ATOM   815  C  C   . PRO   A 1 101 ? 13.639 9.935   26.198 1.00 36.13  ? 107 PRO   A C   1 
ATOM   816  O  O   . PRO   A 1 101 ? 14.233 10.046  25.108 1.00 36.93  ? 107 PRO   A O   1 
ATOM   817  C  CB  . PRO   A 1 101 ? 12.369 11.881  27.208 1.00 35.15  ? 107 PRO   A CB  1 
ATOM   818  C  CG  . PRO   A 1 101 ? 11.002 12.052  27.773 1.00 36.11  ? 107 PRO   A CG  1 
ATOM   819  C  CD  . PRO   A 1 101 ? 10.542 10.651  28.113 1.00 35.43  ? 107 PRO   A CD  1 
ATOM   820  N  N   . GLY   A 1 102 ? 14.123 9.235   27.214 1.00 36.28  ? 108 GLY   A N   1 
ATOM   821  C  CA  . GLY   A 1 102 ? 15.399 8.533   27.131 1.00 36.79  ? 108 GLY   A CA  1 
ATOM   822  C  C   . GLY   A 1 102 ? 15.406 7.317   26.220 1.00 36.57  ? 108 GLY   A C   1 
ATOM   823  O  O   . GLY   A 1 102 ? 16.437 6.655   26.073 1.00 37.13  ? 108 GLY   A O   1 
ATOM   824  N  N   . ASP   A 1 103 ? 14.249 7.005   25.605 1.00 35.68  ? 109 ASP   A N   1 
ATOM   825  C  CA  . ASP   A 1 103 ? 14.080 5.916   24.659 1.00 34.48  ? 109 ASP   A CA  1 
ATOM   826  C  C   . ASP   A 1 103 ? 14.517 6.307   23.239 1.00 32.60  ? 109 ASP   A C   1 
ATOM   827  O  O   . ASP   A 1 103 ? 14.862 5.405   22.500 1.00 32.44  ? 109 ASP   A O   1 
ATOM   828  C  CB  . ASP   A 1 103 ? 12.637 5.390   24.630 1.00 34.46  ? 109 ASP   A CB  1 
ATOM   829  C  CG  . ASP   A 1 103 ? 12.310 4.506   25.791 1.00 37.86  ? 109 ASP   A CG  1 
ATOM   830  O  OD1 . ASP   A 1 103 ? 13.206 3.796   26.256 1.00 38.28  ? 109 ASP   A OD1 1 
ATOM   831  O  OD2 . ASP   A 1 103 ? 11.177 4.567   26.269 1.00 40.02  ? 109 ASP   A OD2 1 
ATOM   832  N  N   . CYS   A 1 104 ? 14.550 7.621   22.879 1.00 30.62  ? 110 CYS   A N   1 
ATOM   833  C  CA  . CYS   A 1 104 ? 15.007 8.177   21.583 1.00 29.21  ? 110 CYS   A CA  1 
ATOM   834  C  C   . CYS   A 1 104 ? 16.325 7.523   21.198 1.00 29.21  ? 110 CYS   A C   1 
ATOM   835  O  O   . CYS   A 1 104 ? 17.292 7.633   21.947 1.00 30.25  ? 110 CYS   A O   1 
ATOM   836  C  CB  . CYS   A 1 104 ? 15.189 9.693   21.658 1.00 28.98  ? 110 CYS   A CB  1 
ATOM   837  S  SG  . CYS   A 1 104 ? 13.656 10.667  21.672 1.00 29.43  ? 110 CYS   A SG  1 
ATOM   838  N  N   . GLY   A 1 105 ? 16.360 6.856   20.056 1.00 28.62  ? 111 GLY   A N   1 
ATOM   839  C  CA  . GLY   A 1 105 ? 17.573 6.180   19.617 1.00 28.74  ? 111 GLY   A CA  1 
ATOM   840  C  C   . GLY   A 1 105 ? 17.375 4.689   19.427 1.00 29.72  ? 111 GLY   A C   1 
ATOM   841  O  O   . GLY   A 1 105 ? 18.086 4.089   18.623 1.00 31.53  ? 111 GLY   A O   1 
ATOM   842  N  N   . GLY   A 1 106 ? 16.391 4.100   20.118 1.00 27.94  ? 112 GLY   A N   1 
ATOM   843  C  CA  . GLY   A 1 106 ? 16.021 2.702   19.956 1.00 27.35  ? 112 GLY   A CA  1 
ATOM   844  C  C   . GLY   A 1 106 ? 15.578 2.420   18.536 1.00 26.63  ? 112 GLY   A C   1 
ATOM   845  O  O   . GLY   A 1 106 ? 14.747 3.139   17.958 1.00 26.45  ? 112 GLY   A O   1 
ATOM   846  N  N   . ILE   A 1 107 ? 16.196 1.406   17.940 1.00 25.66  ? 113 ILE   A N   1 
ATOM   847  C  CA  . ILE   A 1 107 ? 16.003 1.034   16.551 1.00 24.57  ? 113 ILE   A CA  1 
ATOM   848  C  C   . ILE   A 1 107 ? 14.646 0.335   16.304 1.00 23.01  ? 113 ILE   A C   1 
ATOM   849  O  O   . ILE   A 1 107 ? 14.169 -0.447  17.119 1.00 22.95  ? 113 ILE   A O   1 
ATOM   850  C  CB  . ILE   A 1 107 ? 17.264 0.199   16.041 1.00 24.97  ? 113 ILE   A CB  1 
ATOM   851  C  CG1 . ILE   A 1 107 ? 18.526 1.079   15.941 1.00 25.12  ? 113 ILE   A CG1 1 
ATOM   852  C  CG2 . ILE   A 1 107 ? 17.037 -0.505  14.689 1.00 25.61  ? 113 ILE   A CG2 1 
ATOM   853  C  CD1 . ILE   A 1 107 ? 19.818 0.297   15.738 1.00 26.74  ? 113 ILE   A CD1 1 
ATOM   854  N  N   . LEU   A 1 108 ? 13.994 0.701   15.203 1.00 21.08  ? 114 LEU   A N   1 
ATOM   855  C  CA  . LEU   A 1 108 ? 12.799 0.045   14.709 1.00 21.16  ? 114 LEU   A CA  1 
ATOM   856  C  C   . LEU   A 1 108 ? 13.322 -0.830  13.514 1.00 21.56  ? 114 LEU   A C   1 
ATOM   857  O  O   . LEU   A 1 108 ? 14.107 -0.348  12.705 1.00 21.13  ? 114 LEU   A O   1 
ATOM   858  C  CB  . LEU   A 1 108 ? 11.734 1.038   14.232 1.00 20.77  ? 114 LEU   A CB  1 
ATOM   859  C  CG  . LEU   A 1 108 ? 10.578 0.431   13.439 1.00 21.95  ? 114 LEU   A CG  1 
ATOM   860  C  CD1 . LEU   A 1 108 ? 9.811  -0.632  14.221 1.00 21.63  ? 114 LEU   A CD1 1 
ATOM   861  C  CD2 . LEU   A 1 108 ? 9.667  1.519   12.894 1.00 23.25  ? 114 LEU   A CD2 1 
ATOM   862  N  N   . ARG   A 1 109 ? 12.983 -2.129  13.489 1.00 21.84  ? 115 ARG   A N   1 
ATOM   863  C  CA  . ARG   A 1 109 ? 13.485 -3.010  12.467 1.00 22.84  ? 115 ARG   A CA  1 
ATOM   864  C  C   . ARG   A 1 109 ? 12.437 -3.946  11.962 1.00 23.42  ? 115 ARG   A C   1 
ATOM   865  O  O   . ARG   A 1 109 ? 11.561 -4.344  12.697 1.00 22.99  ? 115 ARG   A O   1 
ATOM   866  C  CB  . ARG   A 1 109 ? 14.743 -3.754  12.919 1.00 25.79  ? 115 ARG   A CB  1 
ATOM   867  C  CG  . ARG   A 1 109 ? 14.473 -4.901  13.888 1.00 35.09  ? 115 ARG   A CG  1 
ATOM   868  C  CD  . ARG   A 1 109 ? 15.692 -5.782  14.090 1.00 43.45  ? 115 ARG   A CD  1 
ATOM   869  N  NE  . ARG   A 1 109 ? 16.378 -5.442  15.337 1.00 50.72  ? 115 ARG   A NE  1 
ATOM   870  C  CZ  . ARG   A 1 109 ? 17.347 -4.532  15.434 1.00 55.15  ? 115 ARG   A CZ  1 
ATOM   871  N  NH1 . ARG   A 1 109 ? 17.771 -3.878  14.349 1.00 56.14  ? 115 ARG   A NH1 1 
ATOM   872  N  NH2 . ARG   A 1 109 ? 17.911 -4.277  16.612 1.00 52.68  ? 115 ARG   A NH2 1 
ATOM   873  N  N   . CYS   A 1 110 ? 12.521 -4.289  10.675 1.00 24.31  ? 116 CYS   A N   1 
ATOM   874  C  CA  . CYS   A 1 110 ? 11.610 -5.214  10.045 1.00 26.11  ? 116 CYS   A CA  1 
ATOM   875  C  C   . CYS   A 1 110 ? 12.464 -6.451  9.600  1.00 28.09  ? 116 CYS   A C   1 
ATOM   876  O  O   . CYS   A 1 110 ? 13.623 -6.595  10.015 1.00 28.04  ? 116 CYS   A O   1 
ATOM   877  C  CB  . CYS   A 1 110 ? 10.986 -4.509  8.841  1.00 27.12  ? 116 CYS   A CB  1 
ATOM   878  S  SG  . CYS   A 1 110 ? 12.210 -3.880  7.659  1.00 28.93  ? 116 CYS   A SG  1 
ATOM   879  N  N   . GLN   A 1 111 ? 11.923 -7.307  8.709  1.00 29.95  ? 117 GLN   A N   1 
ATOM   880  C  CA  . GLN   A 1 111 ? 12.705 -8.410  8.131  1.00 32.17  ? 117 GLN   A CA  1 
ATOM   881  C  C   . GLN   A 1 111 ? 13.796 -7.900  7.145  1.00 32.59  ? 117 GLN   A C   1 
ATOM   882  O  O   . GLN   A 1 111 ? 14.739 -8.626  6.866  1.00 33.32  ? 117 GLN   A O   1 
ATOM   883  C  CB  . GLN   A 1 111 ? 11.782 -9.362  7.367  1.00 35.85  ? 117 GLN   A CB  1 
ATOM   884  C  CG  . GLN   A 1 111 ? 11.161 -8.681  6.170  1.00 42.62  ? 117 GLN   A CG  1 
ATOM   885  C  CD  . GLN   A 1 111 ? 10.332 -9.598  5.357  1.00 52.37  ? 117 GLN   A CD  1 
ATOM   886  O  OE1 . GLN   A 1 111 ? 9.206  -9.250  4.992  1.00 55.89  ? 117 GLN   A OE1 1 
ATOM   887  N  NE2 . GLN   A 1 111 ? 10.867 -10.785 5.051  1.00 53.99  ? 117 GLN   A NE2 1 
ATOM   888  N  N   . HIS   A 1 112 ? 13.640 -6.688  6.596  1.00 32.50  ? 118 HIS   A N   1 
ATOM   889  C  CA  . HIS   A 1 112 ? 14.559 -6.099  5.612  1.00 33.06  ? 118 HIS   A CA  1 
ATOM   890  C  C   . HIS   A 1 112 ? 15.756 -5.380  6.206  1.00 32.46  ? 118 HIS   A C   1 
ATOM   891  O  O   . HIS   A 1 112 ? 16.788 -5.248  5.547  1.00 32.65  ? 118 HIS   A O   1 
ATOM   892  C  CB  . HIS   A 1 112 ? 13.805 -5.176  4.661  1.00 34.58  ? 118 HIS   A CB  1 
ATOM   893  C  CG  . HIS   A 1 112 ? 12.853 -5.931  3.786  1.00 39.02  ? 118 HIS   A CG  1 
ATOM   894  N  ND1 . HIS   A 1 112 ? 11.507 -6.005  4.084  1.00 41.58  ? 118 HIS   A ND1 1 
ATOM   895  C  CD2 . HIS   A 1 112 ? 13.096 -6.691  2.696  1.00 40.80  ? 118 HIS   A CD2 1 
ATOM   896  C  CE1 . HIS   A 1 112 ? 10.968 -6.766  3.147  1.00 42.16  ? 118 HIS   A CE1 1 
ATOM   897  N  NE2 . HIS   A 1 112 ? 11.884 -7.205  2.294  1.00 42.69  ? 118 HIS   A NE2 1 
ATOM   898  N  N   . GLY   A 1 113 ? 15.619 -4.955  7.450  1.00 31.65  ? 119 GLY   A N   1 
ATOM   899  C  CA  . GLY   A 1 113 ? 16.678 -4.308  8.200  1.00 29.61  ? 119 GLY   A CA  1 
ATOM   900  C  C   . GLY   A 1 113 ? 16.190 -3.209  9.105  1.00 26.81  ? 119 GLY   A C   1 
ATOM   901  O  O   . GLY   A 1 113 ? 15.089 -3.252  9.662  1.00 25.55  ? 119 GLY   A O   1 
ATOM   902  N  N   . VAL   A 1 114 ? 17.004 -2.192  9.199  1.00 25.65  ? 120 VAL   A N   1 
ATOM   903  C  CA  . VAL   A 1 114 ? 16.724 -1.042  10.020 1.00 24.60  ? 120 VAL   A CA  1 
ATOM   904  C  C   . VAL   A 1 114 ? 15.814 -0.045  9.305  1.00 23.93  ? 120 VAL   A C   1 
ATOM   905  O  O   . VAL   A 1 114 ? 16.201 0.498   8.261  1.00 23.67  ? 120 VAL   A O   1 
ATOM   906  C  CB  . VAL   A 1 114 ? 18.083 -0.462  10.464 1.00 25.30  ? 120 VAL   A CB  1 
ATOM   907  C  CG1 . VAL   A 1 114 ? 17.913 0.891   11.144 1.00 27.59  ? 120 VAL   A CG1 1 
ATOM   908  C  CG2 . VAL   A 1 114 ? 18.809 -1.461  11.397 1.00 25.57  ? 120 VAL   A CG2 1 
ATOM   909  N  N   . VAL   A 1 115 ? 14.593 0.188   9.861  1.00 22.85  ? 121 VAL   A N   1 
ATOM   910  C  CA  . VAL   A 1 115 ? 13.560 1.127   9.384  1.00 22.12  ? 121 VAL   A CA  1 
ATOM   911  C  C   . VAL   A 1 115 ? 13.833 2.593   9.926  1.00 22.24  ? 121 VAL   A C   1 
ATOM   912  O  O   . VAL   A 1 115 ? 13.701 3.570   9.195  1.00 22.42  ? 121 VAL   A O   1 
ATOM   913  C  CB  . VAL   A 1 115 ? 12.163 0.625   9.832  1.00 22.09  ? 121 VAL   A CB  1 
ATOM   914  C  CG1 . VAL   A 1 115 ? 11.074 1.614   9.468  1.00 22.77  ? 121 VAL   A CG1 1 
ATOM   915  C  CG2 . VAL   A 1 115 ? 11.861 -0.761  9.301  1.00 23.09  ? 121 VAL   A CG2 1 
ATOM   916  N  N   . GLY   A 1 116 ? 14.158 2.724   11.227 1.00 21.09  ? 122 GLY   A N   1 
ATOM   917  C  CA  . GLY   A 1 116 ? 14.445 4.019   11.815 1.00 20.84  ? 122 GLY   A CA  1 
ATOM   918  C  C   . GLY   A 1 116 ? 14.820 3.981   13.287 1.00 21.75  ? 122 GLY   A C   1 
ATOM   919  O  O   . GLY   A 1 116 ? 15.317 2.957   13.790 1.00 22.23  ? 122 GLY   A O   1 
ATOM   920  N  N   . ILE   A 1 117 ? 14.616 5.109   13.987 1.00 21.29  ? 123 ILE   A N   1 
ATOM   921  C  CA  . ILE   A 1 117 ? 14.908 5.221   15.428 1.00 21.86  ? 123 ILE   A CA  1 
ATOM   922  C  C   . ILE   A 1 117 ? 13.789 6.030   16.169 1.00 23.63  ? 123 ILE   A C   1 
ATOM   923  O  O   . ILE   A 1 117 ? 13.134 6.878   15.531 1.00 23.76  ? 123 ILE   A O   1 
ATOM   924  C  CB  . ILE   A 1 117 ? 16.300 5.858   15.687 1.00 21.90  ? 123 ILE   A CB  1 
ATOM   925  C  CG1 . ILE   A 1 117 ? 16.514 7.123   14.847 1.00 22.70  ? 123 ILE   A CG1 1 
ATOM   926  C  CG2 . ILE   A 1 117 ? 17.438 4.892   15.536 1.00 22.55  ? 123 ILE   A CG2 1 
ATOM   927  C  CD1 . ILE   A 1 117 ? 17.657 7.929   15.357 1.00 24.86  ? 123 ILE   A CD1 1 
ATOM   928  N  N   . VAL   A 1 118 ? 13.564 5.764   17.512 1.00 23.92  ? 124 VAL   A N   1 
ATOM   929  C  CA  . VAL   A 1 118 ? 12.560 6.491   18.321 1.00 24.26  ? 124 VAL   A CA  1 
ATOM   930  C  C   . VAL   A 1 118 ? 12.877 8.014   18.307 1.00 25.09  ? 124 VAL   A C   1 
ATOM   931  O  O   . VAL   A 1 118 ? 14.019 8.399   18.413 1.00 25.09  ? 124 VAL   A O   1 
ATOM   932  C  CB  . VAL   A 1 118 ? 12.398 5.948   19.780 1.00 24.82  ? 124 VAL   A CB  1 
ATOM   933  C  CG1 . VAL   A 1 118 ? 11.478 6.847   20.615 1.00 25.14  ? 124 VAL   A CG1 1 
ATOM   934  C  CG2 . VAL   A 1 118 ? 11.909 4.494   19.802 1.00 24.46  ? 124 VAL   A CG2 1 
ATOM   935  N  N   . SER   A 1 119 ? 11.855 8.850   18.092 1.00 25.76  ? 125 SER   A N   1 
ATOM   936  C  CA  . SER   A 1 119 ? 11.953 10.284  18.005 1.00 26.92  ? 125 SER   A CA  1 
ATOM   937  C  C   . SER   A 1 119 ? 10.860 10.985  18.827 1.00 27.58  ? 125 SER   A C   1 
ATOM   938  O  O   . SER   A 1 119 ? 11.172 11.880  19.576 1.00 27.91  ? 125 SER   A O   1 
ATOM   939  C  CB  . SER   A 1 119 ? 11.946 10.736  16.547 1.00 28.81  ? 125 SER   A CB  1 
ATOM   940  O  OG  . SER   A 1 119 ? 12.112 12.144  16.513 1.00 30.73  ? 125 SER   A OG  1 
ATOM   941  N  N   . THR   A 1 120 ? 9.596  10.585  18.722 1.00 28.16  ? 126 THR   A N   1 
ATOM   942  C  CA  . THR   A 1 120 ? 8.507  11.208  19.491 1.00 27.74  ? 126 THR   A CA  1 
ATOM   943  C  C   . THR   A 1 120 ? 7.828  10.151  20.452 1.00 29.26  ? 126 THR   A C   1 
ATOM   944  O  O   . THR   A 1 120 ? 8.145  8.960   20.386 1.00 28.87  ? 126 THR   A O   1 
ATOM   945  C  CB  . THR   A 1 120 ? 7.542  11.981  18.544 1.00 27.27  ? 126 THR   A CB  1 
ATOM   946  O  OG1 . THR   A 1 120 ? 6.833  11.092  17.657 1.00 27.73  ? 126 THR   A OG1 1 
ATOM   947  C  CG2 . THR   A 1 120 ? 8.256  13.065  17.730 1.00 26.65  ? 126 THR   A CG2 1 
ATOM   948  N  N   . GLY   A 1 121 ? 6.950  10.613  21.357 1.00 30.86  ? 127 GLY   A N   1 
ATOM   949  C  CA  . GLY   A 1 121 ? 6.284  9.743   22.327 1.00 32.70  ? 127 GLY   A CA  1 
ATOM   950  C  C   . GLY   A 1 121 ? 5.183  10.390  23.141 1.00 34.91  ? 127 GLY   A C   1 
ATOM   951  O  O   . GLY   A 1 121 ? 4.647  11.420  22.759 1.00 35.44  ? 127 GLY   A O   1 
ATOM   952  N  N   . GLY   A 1 122 ? 4.797  9.754   24.245 1.00 36.76  ? 128 GLY   A N   1 
ATOM   953  C  CA  . GLY   A 1 122 ? 3.723  10.225  25.132 1.00 37.50  ? 128 GLY   A CA  1 
ATOM   954  C  C   . GLY   A 1 122 ? 2.343  9.729   24.716 1.00 37.84  ? 128 GLY   A C   1 
ATOM   955  O  O   . GLY   A 1 122 ? 2.129  9.363   23.552 1.00 38.39  ? 128 GLY   A O   1 
ATOM   956  N  N   . ASN   A 1 123 ? 1.399  9.704   25.653 1.00 37.51  ? 129 ASN   A N   1 
ATOM   957  C  CA  . ASN   A 1 123 ? 0.022  9.285   25.380 1.00 37.87  ? 129 ASN   A CA  1 
ATOM   958  C  C   . ASN   A 1 123 ? -0.113 7.838   24.938 1.00 36.36  ? 129 ASN   A C   1 
ATOM   959  O  O   . ASN   A 1 123 ? -1.140 7.489   24.350 1.00 36.72  ? 129 ASN   A O   1 
ATOM   960  C  CB  . ASN   A 1 123 ? -0.649 10.192  24.329 1.00 40.46  ? 129 ASN   A CB  1 
ATOM   961  C  CG  . ASN   A 1 123 ? -1.033 11.558  24.827 1.00 46.64  ? 129 ASN   A CG  1 
ATOM   962  O  OD1 . ASN   A 1 123 ? -0.992 11.846  26.035 1.00 48.78  ? 129 ASN   A OD1 1 
ATOM   963  N  ND2 . ASN   A 1 123 ? -1.425 12.426  23.897 1.00 47.75  ? 129 ASN   A ND2 1 
ATOM   964  N  N   . GLY   A 1 124 ? 0.856  6.993   25.271 1.00 34.45  ? 130 GLY   A N   1 
ATOM   965  C  CA  . GLY   A 1 124 ? 0.809  5.590   24.865 1.00 33.36  ? 130 GLY   A CA  1 
ATOM   966  C  C   . GLY   A 1 124 ? 1.081  5.356   23.377 1.00 32.11  ? 130 GLY   A C   1 
ATOM   967  O  O   . GLY   A 1 124 ? 0.704  4.322   22.822 1.00 32.42  ? 130 GLY   A O   1 
ATOM   968  N  N   . LEU   A 1 125 ? 1.732  6.323   22.733 1.00 30.55  ? 131 LEU   A N   1 
ATOM   969  C  CA  . LEU   A 1 125 ? 2.148  6.280   21.348 1.00 30.44  ? 131 LEU   A CA  1 
ATOM   970  C  C   . LEU   A 1 125 ? 3.693  6.437   21.295 1.00 29.67  ? 131 LEU   A C   1 
ATOM   971  O  O   . LEU   A 1 125 ? 4.284  7.023   22.213 1.00 31.49  ? 131 LEU   A O   1 
ATOM   972  C  CB  . LEU   A 1 125 ? 1.495  7.441   20.565 1.00 30.89  ? 131 LEU   A CB  1 
ATOM   973  C  CG  . LEU   A 1 125 ? -0.023 7.531   20.487 1.00 31.25  ? 131 LEU   A CG  1 
ATOM   974  C  CD1 . LEU   A 1 125 ? -0.398 8.611   19.465 1.00 30.99  ? 131 LEU   A CD1 1 
ATOM   975  C  CD2 . LEU   A 1 125 ? -0.628 6.184   20.059 1.00 31.81  ? 131 LEU   A CD2 1 
ATOM   976  N  N   . VAL   A 1 126 ? 4.340  5.852   20.297 1.00 27.47  ? 132 VAL   A N   1 
ATOM   977  C  CA  . VAL   A 1 126 ? 5.790  5.963   20.093 1.00 26.22  ? 132 VAL   A CA  1 
ATOM   978  C  C   . VAL   A 1 126 ? 6.006  6.343   18.628 1.00 25.44  ? 132 VAL   A C   1 
ATOM   979  O  O   . VAL   A 1 126 ? 5.435  5.725   17.716 1.00 25.11  ? 132 VAL   A O   1 
ATOM   980  C  CB  . VAL   A 1 126 ? 6.587  4.689   20.546 1.00 25.96  ? 132 VAL   A CB  1 
ATOM   981  C  CG1 . VAL   A 1 126 ? 5.875  3.399   20.161 1.00 25.40  ? 132 VAL   A CG1 1 
ATOM   982  C  CG2 . VAL   A 1 126 ? 8.053  4.705   20.099 1.00 25.87  ? 132 VAL   A CG2 1 
ATOM   983  N  N   . GLY   A 1 127 ? 6.768  7.392   18.408 1.00 24.46  ? 133 GLY   A N   1 
ATOM   984  C  CA  . GLY   A 1 127 ? 7.066  7.856   17.061 1.00 24.63  ? 133 GLY   A CA  1 
ATOM   985  C  C   . GLY   A 1 127 ? 8.494  7.577   16.625 1.00 23.73  ? 133 GLY   A C   1 
ATOM   986  O  O   . GLY   A 1 127 ? 9.439  7.757   17.406 1.00 23.27  ? 133 GLY   A O   1 
ATOM   987  N  N   . PHE   A 1 128 ? 8.647  7.136   15.371 1.00 22.00  ? 134 PHE   A N   1 
ATOM   988  C  CA  . PHE   A 1 128 ? 9.932  6.785   14.759 1.00 21.75  ? 134 PHE   A CA  1 
ATOM   989  C  C   . PHE   A 1 128 ? 10.276 7.627   13.542 1.00 21.39  ? 134 PHE   A C   1 
ATOM   990  O  O   . PHE   A 1 128 ? 9.451  7.808   12.630 1.00 21.72  ? 134 PHE   A O   1 
ATOM   991  C  CB  . PHE   A 1 128 ? 9.943  5.335   14.302 1.00 20.74  ? 134 PHE   A CB  1 
ATOM   992  C  CG  . PHE   A 1 128 ? 9.449  4.343   15.312 1.00 20.94  ? 134 PHE   A CG  1 
ATOM   993  C  CD1 . PHE   A 1 128 ? 10.295 3.845   16.286 1.00 21.47  ? 134 PHE   A CD1 1 
ATOM   994  C  CD2 . PHE   A 1 128 ? 8.146  3.870   15.266 1.00 21.34  ? 134 PHE   A CD2 1 
ATOM   995  C  CE1 . PHE   A 1 128 ? 9.826  2.946   17.235 1.00 21.59  ? 134 PHE   A CE1 1 
ATOM   996  C  CE2 . PHE   A 1 128 ? 7.685  2.970   16.224 1.00 21.76  ? 134 PHE   A CE2 1 
ATOM   997  C  CZ  . PHE   A 1 128 ? 8.519  2.532   17.212 1.00 21.23  ? 134 PHE   A CZ  1 
ATOM   998  N  N   . ALA   A 1 129 ? 11.518 8.091   13.508 1.00 20.78  ? 135 ALA   A N   1 
ATOM   999  C  CA  . ALA   A 1 129 ? 12.129 8.820   12.417 1.00 21.26  ? 135 ALA   A CA  1 
ATOM   1000 C  C   . ALA   A 1 129 ? 12.559 7.794   11.338 1.00 21.46  ? 135 ALA   A C   1 
ATOM   1001 O  O   . ALA   A 1 129 ? 13.490 7.016   11.531 1.00 20.43  ? 135 ALA   A O   1 
ATOM   1002 C  CB  . ALA   A 1 129 ? 13.366 9.566   12.933 1.00 21.18  ? 135 ALA   A CB  1 
ATOM   1003 N  N   . ASP   A 1 130 ? 11.844 7.771   10.219 1.00 23.11  ? 136 ASP   A N   1 
ATOM   1004 C  CA  . ASP   A 1 130 ? 12.199 6.910   9.078  1.00 25.26  ? 136 ASP   A CA  1 
ATOM   1005 C  C   . ASP   A 1 130 ? 13.575 7.269   8.445  1.00 26.37  ? 136 ASP   A C   1 
ATOM   1006 O  O   . ASP   A 1 130 ? 13.897 8.446   8.280  1.00 27.60  ? 136 ASP   A O   1 
ATOM   1007 C  CB  . ASP   A 1 130 ? 11.113 7.003   7.996  1.00 26.36  ? 136 ASP   A CB  1 
ATOM   1008 C  CG  . ASP   A 1 130 ? 11.332 6.027   6.860  1.00 29.24  ? 136 ASP   A CG  1 
ATOM   1009 O  OD1 . ASP   A 1 130 ? 11.524 4.843   7.134  1.00 27.63  ? 136 ASP   A OD1 1 
ATOM   1010 O  OD2 . ASP   A 1 130 ? 11.392 6.470   5.715  1.00 33.16  ? 136 ASP   A OD2 1 
ATOM   1011 N  N   . VAL   A 1 131 ? 14.371 6.257   8.101  1.00 26.36  ? 137 VAL   A N   1 
ATOM   1012 C  CA  . VAL   A 1 131 ? 15.675 6.399   7.437  1.00 27.07  ? 137 VAL   A CA  1 
ATOM   1013 C  C   . VAL   A 1 131 ? 15.755 5.558   6.101  1.00 29.34  ? 137 VAL   A C   1 
ATOM   1014 O  O   . VAL   A 1 131 ? 16.788 5.577   5.437  1.00 29.87  ? 137 VAL   A O   1 
ATOM   1015 C  CB  . VAL   A 1 131 ? 16.856 6.061   8.393  1.00 26.55  ? 137 VAL   A CB  1 
ATOM   1016 C  CG1 . VAL   A 1 131 ? 16.829 6.935   9.648  1.00 26.30  ? 137 VAL   A CG1 1 
ATOM   1017 C  CG2 . VAL   A 1 131 ? 16.881 4.572   8.767  1.00 26.02  ? 137 VAL   A CG2 1 
ATOM   1018 N  N   . ARG   A 1 132 ? 14.655 4.849   5.717  1.00 29.80  ? 138 ARG   A N   1 
ATOM   1019 C  CA  . ARG   A 1 132 ? 14.572 3.977   4.545  1.00 31.40  ? 138 ARG   A CA  1 
ATOM   1020 C  C   . ARG   A 1 132 ? 14.671 4.684   3.161  1.00 34.07  ? 138 ARG   A C   1 
ATOM   1021 O  O   . ARG   A 1 132 ? 14.831 4.007   2.131  1.00 35.71  ? 138 ARG   A O   1 
ATOM   1022 C  CB  . ARG   A 1 132 ? 13.297 3.136   4.609  1.00 30.70  ? 138 ARG   A CB  1 
ATOM   1023 C  CG  . ARG   A 1 132 ? 13.221 2.191   5.772  1.00 30.38  ? 138 ARG   A CG  1 
ATOM   1024 C  CD  . ARG   A 1 132 ? 11.950 1.410   5.658  1.00 30.05  ? 138 ARG   A CD  1 
ATOM   1025 N  NE  . ARG   A 1 132 ? 10.791 2.200   6.076  1.00 29.38  ? 138 ARG   A NE  1 
ATOM   1026 C  CZ  . ARG   A 1 132 ? 9.551  1.733   6.128  1.00 29.24  ? 138 ARG   A CZ  1 
ATOM   1027 N  NH1 . ARG   A 1 132 ? 9.284  0.497   5.731  1.00 30.05  ? 138 ARG   A NH1 1 
ATOM   1028 N  NH2 . ARG   A 1 132 ? 8.565  2.504   6.552  1.00 28.90  ? 138 ARG   A NH2 1 
ATOM   1029 N  N   . ASP   A 1 133 ? 14.556 6.026   3.142  1.00 33.93  ? 139 ASP   A N   1 
ATOM   1030 C  CA  . ASP   A 1 133 ? 14.628 6.883   1.952  1.00 34.74  ? 139 ASP   A CA  1 
ATOM   1031 C  C   . ASP   A 1 133 ? 16.006 7.539   1.799  1.00 33.56  ? 139 ASP   A C   1 
ATOM   1032 O  O   . ASP   A 1 133 ? 16.265 8.119   0.755  1.00 34.22  ? 139 ASP   A O   1 
ATOM   1033 C  CB  . ASP   A 1 133 ? 13.555 7.987   2.005  1.00 35.61  ? 139 ASP   A CB  1 
ATOM   1034 C  CG  . ASP   A 1 133 ? 13.811 8.953   3.141  1.00 39.53  ? 139 ASP   A CG  1 
ATOM   1035 O  OD1 . ASP   A 1 133 ? 13.733 8.524   4.324  1.00 41.57  ? 139 ASP   A OD1 1 
ATOM   1036 O  OD2 . ASP   A 1 133 ? 14.158 10.097  2.861  1.00 40.50  ? 139 ASP   A OD2 1 
ATOM   1037 N  N   . LEU   A 1 134 ? 16.875 7.475   2.832  1.00 31.92  ? 140 LEU   A N   1 
ATOM   1038 C  CA  . LEU   A 1 134 ? 18.213 8.033   2.717  1.00 31.16  ? 140 LEU   A CA  1 
ATOM   1039 C  C   . LEU   A 1 134 ? 19.096 6.969   2.054  1.00 32.60  ? 140 LEU   A C   1 
ATOM   1040 O  O   . LEU   A 1 134 ? 19.940 6.368   2.716  1.00 32.28  ? 140 LEU   A O   1 
ATOM   1041 C  CB  . LEU   A 1 134 ? 18.791 8.488   4.079  1.00 29.78  ? 140 LEU   A CB  1 
ATOM   1042 C  CG  . LEU   A 1 134 ? 18.004 9.531   4.881  1.00 28.20  ? 140 LEU   A CG  1 
ATOM   1043 C  CD1 . LEU   A 1 134 ? 18.618 9.757   6.237  1.00 27.72  ? 140 LEU   A CD1 1 
ATOM   1044 C  CD2 . LEU   A 1 134 ? 17.870 10.807  4.139  1.00 28.14  ? 140 LEU   A CD2 1 
ATOM   1045 N  N   . LEU   A 1 135 ? 18.880 6.730   0.717  1.00 33.62  ? 141 LEU   A N   1 
ATOM   1046 C  CA  . LEU   A 1 135 ? 19.597 5.738   -0.106 1.00 35.11  ? 141 LEU   A CA  1 
ATOM   1047 C  C   . LEU   A 1 135 ? 21.117 5.928   -0.144 1.00 36.17  ? 141 LEU   A C   1 
ATOM   1048 O  O   . LEU   A 1 135 ? 21.859 4.974   -0.416 1.00 35.79  ? 141 LEU   A O   1 
ATOM   1049 C  CB  . LEU   A 1 135 ? 19.061 5.706   -1.560 1.00 35.84  ? 141 LEU   A CB  1 
ATOM   1050 C  CG  . LEU   A 1 135 ? 17.549 5.736   -1.784 1.00 38.07  ? 141 LEU   A CG  1 
ATOM   1051 C  CD1 . LEU   A 1 135 ? 17.222 5.687   -3.297 1.00 39.80  ? 141 LEU   A CD1 1 
ATOM   1052 C  CD2 . LEU   A 1 135 ? 16.854 4.620   -1.033 1.00 38.45  ? 141 LEU   A CD2 1 
ATOM   1053 N  N   . TRP   A 1 136 ? 21.578 7.178   0.040  1.00 37.32  ? 142 TRP   A N   1 
ATOM   1054 C  CA  . TRP   A 1 136 ? 22.999 7.476   -0.002 1.00 38.51  ? 142 TRP   A CA  1 
ATOM   1055 C  C   . TRP   A 1 136 ? 23.793 6.859   1.130  1.00 41.47  ? 142 TRP   A C   1 
ATOM   1056 O  O   . TRP   A 1 136 ? 24.979 6.630   0.932  1.00 42.32  ? 142 TRP   A O   1 
ATOM   1057 C  CB  . TRP   A 1 136 ? 23.263 8.969   -0.067 1.00 37.48  ? 142 TRP   A CB  1 
ATOM   1058 C  CG  . TRP   A 1 136 ? 22.472 9.801   0.892  1.00 37.68  ? 142 TRP   A CG  1 
ATOM   1059 C  CD1 . TRP   A 1 136 ? 21.328 10.485  0.620  1.00 38.65  ? 142 TRP   A CD1 1 
ATOM   1060 C  CD2 . TRP   A 1 136 ? 22.813 10.110  2.257  1.00 37.60  ? 142 TRP   A CD2 1 
ATOM   1061 N  NE1 . TRP   A 1 136 ? 20.942 11.219  1.719  1.00 39.08  ? 142 TRP   A NE1 1 
ATOM   1062 C  CE2 . TRP   A 1 136 ? 21.832 11.001  2.741  1.00 38.57  ? 142 TRP   A CE2 1 
ATOM   1063 C  CE3 . TRP   A 1 136 ? 23.882 9.766   3.102  1.00 37.61  ? 142 TRP   A CE3 1 
ATOM   1064 C  CZ2 . TRP   A 1 136 ? 21.880 11.539  4.034  1.00 38.50  ? 142 TRP   A CZ2 1 
ATOM   1065 C  CZ3 . TRP   A 1 136 ? 23.930 10.312  4.374  1.00 37.96  ? 142 TRP   A CZ3 1 
ATOM   1066 C  CH2 . TRP   A 1 136 ? 22.941 11.188  4.826  1.00 37.94  ? 142 TRP   A CH2 1 
ATOM   1067 N  N   . LEU   A 1 137 ? 23.156 6.588   2.313  1.00 42.36  ? 143 LEU   A N   1 
ATOM   1068 C  CA  . LEU   A 1 137 ? 23.799 5.998   3.483  1.00 43.97  ? 143 LEU   A CA  1 
ATOM   1069 C  C   . LEU   A 1 137 ? 24.619 4.747   3.149  1.00 47.32  ? 143 LEU   A C   1 
ATOM   1070 O  O   . LEU   A 1 137 ? 25.651 4.493   3.766  1.00 46.51  ? 143 LEU   A O   1 
ATOM   1071 C  CB  . LEU   A 1 137 ? 22.721 5.646   4.510  1.00 43.35  ? 143 LEU   A CB  1 
ATOM   1072 C  CG  . LEU   A 1 137 ? 22.196 6.810   5.340  1.00 44.05  ? 143 LEU   A CG  1 
ATOM   1073 C  CD1 . LEU   A 1 137 ? 20.943 6.417   6.077  1.00 45.08  ? 143 LEU   A CD1 1 
ATOM   1074 C  CD2 . LEU   A 1 137 ? 23.232 7.269   6.355  1.00 44.05  ? 143 LEU   A CD2 1 
ATOM   1075 N  N   . ASP   A 1 138 ? 24.154 3.977   2.148  1.00 50.85  ? 144 ASP   A N   1 
ATOM   1076 C  CA  . ASP   A 1 138 ? 24.762 2.728   1.693  1.00 54.84  ? 144 ASP   A CA  1 
ATOM   1077 C  C   . ASP   A 1 138 ? 26.027 2.915   0.865  1.00 58.61  ? 144 ASP   A C   1 
ATOM   1078 O  O   . ASP   A 1 138 ? 27.041 2.265   1.135  1.00 58.77  ? 144 ASP   A O   1 
ATOM   1079 C  CB  . ASP   A 1 138 ? 23.728 1.879   0.924  1.00 56.90  ? 144 ASP   A CB  1 
ATOM   1080 C  CG  . ASP   A 1 138 ? 22.502 1.519   1.744  1.00 61.42  ? 144 ASP   A CG  1 
ATOM   1081 O  OD1 . ASP   A 1 138 ? 22.557 1.653   2.995  1.00 62.48  ? 144 ASP   A OD1 1 
ATOM   1082 O  OD2 . ASP   A 1 138 ? 21.484 1.107   1.142  1.00 63.33  ? 144 ASP   A OD2 1 
ATOM   1083 N  N   . GLU   A 1 139 ? 25.978 3.834   -0.107 1.00 61.36  ? 145 GLU   A N   1 
ATOM   1084 C  CA  . GLU   A 1 139 ? 27.063 4.146   -1.039 1.00 64.34  ? 145 GLU   A CA  1 
ATOM   1085 C  C   . GLU   A 1 139 ? 28.044 5.249   -0.509 1.00 67.08  ? 145 GLU   A C   1 
ATOM   1086 O  O   . GLU   A 1 139 ? 27.839 5.748   0.605  1.00 67.86  ? 145 GLU   A O   1 
ATOM   1087 C  CB  . GLU   A 1 139 ? 26.457 4.487   -2.420 1.00 67.51  ? 145 GLU   A CB  1 
ATOM   1088 C  CG  . GLU   A 1 139 ? 25.179 5.318   -2.372 1.00 73.83  ? 145 GLU   A CG  1 
ATOM   1089 C  CD  . GLU   A 1 139 ? 24.182 5.109   -3.502 1.00 81.76  ? 145 GLU   A CD  1 
ATOM   1090 O  OE1 . GLU   A 1 139 ? 23.770 6.119   -4.122 1.00 82.19  ? 145 GLU   A OE1 1 
ATOM   1091 O  OE2 . GLU   A 1 139 ? 23.798 3.942   -3.754 1.00 84.79  ? 145 GLU   A OE2 1 
ATOM   1092 N  N   . GLU   A 1 140 ? 29.129 5.587   -1.284 1.00 68.09  ? 146 GLU   A N   1 
ATOM   1093 C  CA  . GLU   A 1 140 ? 30.199 6.559   -0.939 1.00 69.39  ? 146 GLU   A CA  1 
ATOM   1094 C  C   . GLU   A 1 140 ? 31.178 5.984   0.101  1.00 70.32  ? 146 GLU   A C   1 
ATOM   1095 O  O   . GLU   A 1 140 ? 32.387 6.208   0.012  1.00 70.78  ? 146 GLU   A O   1 
ATOM   1096 C  CB  . GLU   A 1 140 ? 29.651 7.954   -0.524 1.00 71.68  ? 146 GLU   A CB  1 
ATOM   1097 C  CG  . GLU   A 1 140 ? 30.575 8.828   0.315  1.00 76.79  ? 146 GLU   A CG  1 
ATOM   1098 C  CD  . GLU   A 1 140 ? 30.475 10.328  0.095  1.00 83.47  ? 146 GLU   A CD  1 
ATOM   1099 O  OE1 . GLU   A 1 140 ? 29.522 10.771  -0.586 1.00 84.35  ? 146 GLU   A OE1 1 
ATOM   1100 O  OE2 . GLU   A 1 140 ? 31.354 11.063  0.601  1.00 85.57  ? 146 GLU   A OE2 1 
HETATM 1101 N  N1  . A1B3P B 2 .   ? 10.394 16.061  17.913 1.00 35.03  ? 201 A1B3P A N1  1 
HETATM 1102 N  N3  . A1B3P B 2 .   ? 11.946 14.743  18.553 1.00 35.32  ? 201 A1B3P A N3  1 
HETATM 1103 C  C4  . A1B3P B 2 .   ? 6.806  11.500  26.504 1.00 35.02  ? 201 A1B3P A C4  1 
HETATM 1104 C  C5  . A1B3P B 2 .   ? 7.119  12.583  25.704 1.00 35.21  ? 201 A1B3P A C5  1 
HETATM 1105 C  C6  . A1B3P B 2 .   ? 8.039  12.473  24.662 1.00 35.56  ? 201 A1B3P A C6  1 
HETATM 1106 C  C7  . A1B3P B 2 .   ? 8.386  13.702  23.851 1.00 36.51  ? 201 A1B3P A C7  1 
HETATM 1107 C  C8  . A1B3P B 2 .   ? 9.727  14.299  24.249 1.00 36.90  ? 201 A1B3P A C8  1 
HETATM 1108 C  C10 . A1B3P B 2 .   ? 12.360 15.536  21.995 1.00 36.33  ? 201 A1B3P A C10 1 
HETATM 1109 C  C13 . A1B3P B 2 .   ? 10.277 16.013  19.244 1.00 35.16  ? 201 A1B3P A C13 1 
HETATM 1110 O  O   . A1B3P B 2 .   ? 10.021 14.460  25.431 1.00 36.45  ? 201 A1B3P A O   1 
HETATM 1111 C  C3  . A1B3P B 2 .   ? 7.386  10.279  26.266 1.00 35.05  ? 201 A1B3P A C3  1 
HETATM 1112 C  C2  . A1B3P B 2 .   ? 8.283  10.126  25.221 1.00 34.75  ? 201 A1B3P A C2  1 
HETATM 1113 C  C1  . A1B3P B 2 .   ? 8.627  11.221  24.428 1.00 34.88  ? 201 A1B3P A C1  1 
HETATM 1114 S  S   . A1B3P B 2 .   ? 9.842  11.120  23.147 1.00 33.97  ? 201 A1B3P A S   1 
HETATM 1115 C  C   . A1B3P B 2 .   ? 10.203 9.373   23.015 1.00 33.77  ? 201 A1B3P A C   1 
HETATM 1116 N  N   . A1B3P B 2 .   ? 10.565 14.636  23.239 1.00 36.67  ? 201 A1B3P A N   1 
HETATM 1117 C  C14 . A1B3P B 2 .   ? 10.194 14.599  21.823 1.00 36.21  ? 201 A1B3P A C14 1 
HETATM 1118 C  C11 . A1B3P B 2 .   ? 11.508 14.650  21.080 1.00 35.97  ? 201 A1B3P A C11 1 
HETATM 1119 O  O1  . A1B3P B 2 .   ? 12.093 13.347  21.004 1.00 35.41  ? 201 A1B3P A O1  1 
HETATM 1120 C  C9  . A1B3P B 2 .   ? 11.950 15.110  23.406 1.00 36.57  ? 201 A1B3P A C9  1 
HETATM 1121 C  C12 . A1B3P B 2 .   ? 11.261 15.161  19.661 1.00 35.65  ? 201 A1B3P A C12 1 
HETATM 1122 N  N2  . A1B3P B 2 .   ? 11.405 15.292  17.483 1.00 35.07  ? 201 A1B3P A N2  1 
HETATM 1123 ZN ZN  . ZN    C 3 .   ? 10.860 -4.297  5.587  1.00 30.28  2 202 ZN    A ZN  1 
HETATM 1124 S  S   . DMS   D 4 .   ? 14.334 21.263  8.416  1.00 106.68 ? 203 DMS   A S   1 
HETATM 1125 O  O   . DMS   D 4 .   ? 14.278 22.281  9.517  1.00 106.55 ? 203 DMS   A O   1 
HETATM 1126 C  C1  . DMS   D 4 .   ? 13.045 21.651  7.195  1.00 106.71 ? 203 DMS   A C1  1 
HETATM 1127 C  C2  . DMS   D 4 .   ? 15.723 21.675  7.318  1.00 106.76 ? 203 DMS   A C2  1 
HETATM 1128 S  S   . DMS   E 4 .   ? 20.438 -3.107  22.600 1.00 83.91  ? 204 DMS   A S   1 
HETATM 1129 O  O   . DMS   E 4 .   ? 20.584 -2.332  23.887 1.00 83.78  ? 204 DMS   A O   1 
HETATM 1130 C  C1  . DMS   E 4 .   ? 21.818 -4.296  22.484 1.00 83.90  ? 204 DMS   A C1  1 
HETATM 1131 C  C2  . DMS   E 4 .   ? 19.133 -4.355  22.820 1.00 83.72  ? 204 DMS   A C2  1 
HETATM 1132 S  S   . DMS   F 4 .   ? 0.342  -1.644  24.106 1.00 119.76 ? 205 DMS   A S   1 
HETATM 1133 O  O   . DMS   F 4 .   ? -0.940 -1.831  23.344 1.00 119.63 ? 205 DMS   A O   1 
HETATM 1134 C  C1  . DMS   F 4 .   ? -0.056 -0.833  25.680 1.00 119.76 ? 205 DMS   A C1  1 
HETATM 1135 C  C2  . DMS   F 4 .   ? 0.788  -3.244  24.847 1.00 119.71 ? 205 DMS   A C2  1 
HETATM 1136 O  O   . HOH   G 5 .   ? 31.099 19.536  11.016 1.00 74.29  ? 301 HOH   A O   1 
HETATM 1137 O  O   . HOH   G 5 .   ? 9.160  15.002  27.474 1.00 38.09  ? 302 HOH   A O   1 
HETATM 1138 O  O   . HOH   G 5 .   ? -0.035 15.980  8.277  1.00 24.75  ? 303 HOH   A O   1 
HETATM 1139 O  O   . HOH   G 5 .   ? 25.263 18.761  20.617 1.00 41.86  ? 304 HOH   A O   1 
HETATM 1140 O  O   . HOH   G 5 .   ? 19.376 9.050   19.347 1.00 23.37  ? 305 HOH   A O   1 
HETATM 1141 O  O   . HOH   G 5 .   ? 36.895 15.159  10.253 1.00 52.19  ? 306 HOH   A O   1 
HETATM 1142 O  O   . HOH   G 5 .   ? 2.991  -1.088  3.724  1.00 39.84  ? 307 HOH   A O   1 
HETATM 1143 O  O   . HOH   G 5 .   ? 23.645 12.589  23.489 1.00 28.31  ? 308 HOH   A O   1 
HETATM 1144 O  O   . HOH   G 5 .   ? 10.539 8.466   4.463  1.00 30.94  ? 309 HOH   A O   1 
HETATM 1145 O  O   . HOH   G 5 .   ? 5.549  -3.959  28.930 1.00 29.80  ? 310 HOH   A O   1 
HETATM 1146 O  O   . HOH   G 5 .   ? 8.058  -3.327  0.519  1.00 19.39  ? 311 HOH   A O   1 
HETATM 1147 O  O   . HOH   G 5 .   ? 9.256  -4.712  31.783 1.00 19.94  ? 312 HOH   A O   1 
HETATM 1148 O  O   . HOH   G 5 .   ? 4.111  19.737  25.364 1.00 40.39  ? 313 HOH   A O   1 
HETATM 1149 O  O   . HOH   G 5 .   ? -0.512 2.588   24.326 1.00 35.73  ? 314 HOH   A O   1 
HETATM 1150 O  O   . HOH   G 5 .   ? 27.925 16.657  3.800  1.00 34.46  ? 315 HOH   A O   1 
HETATM 1151 O  O   . HOH   G 5 .   ? 14.742 2.892   23.180 1.00 28.65  ? 316 HOH   A O   1 
HETATM 1152 O  O   . HOH   G 5 .   ? 28.446 3.750   2.773  1.00 66.94  ? 317 HOH   A O   1 
HETATM 1153 O  O   . HOH   G 5 .   ? 11.302 12.003  11.409 1.00 21.97  ? 318 HOH   A O   1 
HETATM 1154 O  O   . HOH   G 5 .   ? 14.897 23.984  14.529 1.00 43.25  ? 319 HOH   A O   1 
HETATM 1155 O  O   . HOH   G 5 .   ? 2.155  -5.898  17.806 1.00 20.46  ? 320 HOH   A O   1 
HETATM 1156 O  O   . HOH   G 5 .   ? 3.010  13.330  23.633 1.00 33.39  ? 321 HOH   A O   1 
HETATM 1157 O  O   . HOH   G 5 .   ? 13.105 2.367   0.887  1.00 19.48  ? 322 HOH   A O   1 
HETATM 1158 O  O   . HOH   G 5 .   ? 23.576 0.256   15.966 1.00 38.19  ? 323 HOH   A O   1 
HETATM 1159 O  O   . HOH   G 5 .   ? 14.418 -8.643  11.568 1.00 32.12  ? 324 HOH   A O   1 
HETATM 1160 O  O   . HOH   G 5 .   ? 17.662 0.578   29.932 1.00 55.78  ? 325 HOH   A O   1 
HETATM 1161 O  O   . HOH   G 5 .   ? -2.108 23.161  12.761 1.00 59.87  ? 326 HOH   A O   1 
HETATM 1162 O  O   . HOH   G 5 .   ? 2.686  10.656  21.075 1.00 17.42  ? 327 HOH   A O   1 
HETATM 1163 O  O   . HOH   G 5 .   ? 17.865 19.025  17.316 1.00 29.71  ? 328 HOH   A O   1 
HETATM 1164 O  O   . HOH   G 5 .   ? 19.050 -0.129  27.553 1.00 46.63  ? 329 HOH   A O   1 
HETATM 1165 O  O   . HOH   G 5 .   ? 9.659  18.761  20.831 1.00 49.31  ? 330 HOH   A O   1 
HETATM 1166 O  O   . HOH   G 5 .   ? -0.178 12.222  21.497 1.00 23.33  ? 331 HOH   A O   1 
HETATM 1167 O  O   . HOH   G 5 .   ? 5.620  0.674   -2.194 1.00 34.66  ? 332 HOH   A O   1 
HETATM 1168 O  O   . HOH   G 5 .   ? 34.580 4.830   14.092 1.00 47.40  ? 333 HOH   A O   1 
HETATM 1169 O  O   . HOH   G 5 .   ? 26.744 8.539   0.129  1.00 47.21  ? 334 HOH   A O   1 
HETATM 1170 O  O   . HOH   G 5 .   ? 2.961  8.272   10.487 1.00 26.44  ? 335 HOH   A O   1 
HETATM 1171 O  O   . HOH   G 5 .   ? 19.182 -1.075  31.198 1.00 46.65  ? 336 HOH   A O   1 
HETATM 1172 O  O   . HOH   G 5 .   ? 29.671 21.215  19.119 1.00 48.17  ? 337 HOH   A O   1 
HETATM 1173 O  O   . HOH   G 5 .   ? 30.734 11.820  21.271 1.00 30.57  ? 338 HOH   A O   1 
HETATM 1174 O  O   . HOH   G 5 .   ? 29.367 3.403   11.090 1.00 37.08  ? 339 HOH   A O   1 
HETATM 1175 O  O   . HOH   G 5 .   ? 11.861 21.708  13.263 1.00 40.17  ? 340 HOH   A O   1 
HETATM 1176 O  O   . HOH   G 5 .   ? 17.171 20.370  20.024 1.00 44.36  ? 341 HOH   A O   1 
HETATM 1177 O  O   . HOH   G 5 .   ? 23.636 -6.371  9.472  1.00 36.47  ? 342 HOH   A O   1 
HETATM 1178 O  O   . HOH   G 5 .   ? 22.463 -0.643  4.518  1.00 33.87  ? 343 HOH   A O   1 
HETATM 1179 O  O   . HOH   G 5 .   ? 6.828  3.973   32.822 1.00 31.99  ? 344 HOH   A O   1 
HETATM 1180 O  O   . HOH   G 5 .   ? 6.274  2.189   5.031  1.00 45.09  ? 345 HOH   A O   1 
HETATM 1181 O  O   . HOH   G 5 .   ? 14.961 12.592  24.261 1.00 25.97  ? 346 HOH   A O   1 
HETATM 1182 O  O   . HOH   G 5 .   ? -2.792 8.671   22.446 1.00 25.78  ? 347 HOH   A O   1 
HETATM 1183 O  O   . HOH   G 5 .   ? 15.164 -2.988  17.684 1.00 31.08  ? 348 HOH   A O   1 
HETATM 1184 O  O   . HOH   G 5 .   ? 33.701 18.845  10.441 1.00 35.62  ? 349 HOH   A O   1 
HETATM 1185 O  O   . HOH   G 5 .   ? 14.925 14.648  3.666  1.00 32.23  ? 350 HOH   A O   1 
HETATM 1186 O  O   . HOH   G 5 .   ? 18.429 -4.637  27.382 1.00 44.15  ? 351 HOH   A O   1 
HETATM 1187 O  O   . HOH   G 5 .   ? 10.347 18.325  5.973  1.00 34.07  ? 352 HOH   A O   1 
HETATM 1188 O  O   . HOH   G 5 .   ? 0.210  0.434   16.531 1.00 16.49  ? 353 HOH   A O   1 
HETATM 1189 O  O   . HOH   G 5 .   ? -2.631 7.362   26.746 1.00 28.11  ? 354 HOH   A O   1 
HETATM 1190 O  O   . HOH   G 5 .   ? 6.587  -2.327  -1.974 1.00 28.98  ? 355 HOH   A O   1 
HETATM 1191 O  O   . HOH   G 5 .   ? 29.570 5.223   4.142  1.00 42.45  ? 356 HOH   A O   1 
HETATM 1192 O  O   . HOH   G 5 .   ? 15.462 24.114  26.555 1.00 34.18  ? 357 HOH   A O   1 
HETATM 1193 O  O   . HOH   G 5 .   ? 19.099 13.380  1.997  1.00 52.35  ? 358 HOH   A O   1 
HETATM 1194 O  O   . HOH   G 5 .   ? 19.568 -4.868  18.877 1.00 56.93  ? 359 HOH   A O   1 
HETATM 1195 O  O   . HOH   G 5 .   ? 12.927 -7.865  24.877 1.00 23.11  ? 360 HOH   A O   1 
HETATM 1196 O  O   . HOH   G 5 .   ? 8.045  3.284   3.175  1.00 26.98  ? 361 HOH   A O   1 
HETATM 1197 O  O   . HOH   G 5 .   ? 17.503 3.001   23.129 1.00 18.45  ? 362 HOH   A O   1 
HETATM 1198 O  O   . HOH   G 5 .   ? 24.031 8.917   -3.487 1.00 42.72  ? 363 HOH   A O   1 
HETATM 1199 O  O   . HOH   G 5 .   ? 5.766  9.204   2.762  1.00 86.01  ? 364 HOH   A O   1 
HETATM 1200 O  O   . HOH   G 5 .   ? 18.289 -2.187  18.565 1.00 34.73  ? 365 HOH   A O   1 
HETATM 1201 O  O   . HOH   G 5 .   ? 22.886 17.721  22.208 1.00 56.65  ? 366 HOH   A O   1 
HETATM 1202 O  O   . HOH   G 5 .   ? 2.604  3.883   27.549 1.00 27.16  ? 367 HOH   A O   1 
HETATM 1203 O  O   . HOH   G 5 .   ? 0.585  -2.231  20.221 1.00 24.08  ? 368 HOH   A O   1 
HETATM 1204 O  O   . HOH   G 5 .   ? 21.397 7.766   -4.450 1.00 35.45  ? 369 HOH   A O   1 
HETATM 1205 O  O   . HOH   G 5 .   ? 18.094 21.431  9.794  1.00 44.05  ? 370 HOH   A O   1 
HETATM 1206 O  O   . HOH   G 5 .   ? 30.809 -0.139  13.700 1.00 49.00  ? 371 HOH   A O   1 
HETATM 1207 O  O   . HOH   G 5 .   ? 13.021 10.951  9.490  1.00 23.38  ? 372 HOH   A O   1 
HETATM 1208 O  O   . HOH   G 5 .   ? 28.293 -2.129  13.374 1.00 32.19  ? 373 HOH   A O   1 
HETATM 1209 O  O   . HOH   G 5 .   ? 22.165 8.809   21.234 1.00 28.08  ? 374 HOH   A O   1 
HETATM 1210 O  O   . HOH   G 5 .   ? 36.258 20.680  18.311 1.00 34.59  ? 375 HOH   A O   1 
HETATM 1211 O  O   . HOH   G 5 .   ? 4.009  -4.777  21.457 1.00 17.57  ? 376 HOH   A O   1 
HETATM 1212 O  O   . HOH   G 5 .   ? 0.100  4.662   6.625  1.00 20.00  ? 377 HOH   A O   1 
HETATM 1213 O  O   . HOH   G 5 .   ? 9.799  5.413   3.462  1.00 22.55  ? 378 HOH   A O   1 
HETATM 1214 O  O   . HOH   G 5 .   ? 9.122  24.843  24.227 1.00 40.05  ? 379 HOH   A O   1 
HETATM 1215 O  O   . HOH   G 5 .   ? 25.864 4.636   19.863 1.00 47.79  ? 380 HOH   A O   1 
HETATM 1216 O  O   . HOH   G 5 .   ? 19.040 9.648   26.328 1.00 36.39  ? 381 HOH   A O   1 
HETATM 1217 O  O   . HOH   G 5 .   ? 4.865  -5.039  6.529  1.00 15.93  ? 382 HOH   A O   1 
HETATM 1218 O  O   . HOH   G 5 .   ? 15.080 -4.360  1.142  1.00 18.67  ? 383 HOH   A O   1 
HETATM 1219 O  O   . HOH   G 5 .   ? 12.829 -7.037  30.799 1.00 36.22  ? 384 HOH   A O   1 
HETATM 1220 O  O   . HOH   G 5 .   ? 6.908  15.955  22.165 1.00 36.64  ? 385 HOH   A O   1 
HETATM 1221 O  O   . HOH   G 5 .   ? 9.537  4.168   33.801 1.00 35.49  ? 386 HOH   A O   1 
HETATM 1222 O  O   . HOH   G 5 .   ? 7.651  20.802  8.789  1.00 57.85  ? 387 HOH   A O   1 
HETATM 1223 O  O   . HOH   G 5 .   ? 2.205  13.184  17.954 1.00 28.74  ? 388 HOH   A O   1 
HETATM 1224 O  O   . HOH   G 5 .   ? 30.334 -3.437  6.740  1.00 42.51  ? 389 HOH   A O   1 
HETATM 1225 O  O   . HOH   G 5 .   ? 17.499 -6.291  2.810  1.00 39.61  ? 390 HOH   A O   1 
HETATM 1226 O  O   . HOH   G 5 .   ? 29.189 7.466   20.667 1.00 60.68  ? 391 HOH   A O   1 
HETATM 1227 O  O   . HOH   G 5 .   ? 10.990 17.573  27.155 1.00 37.68  ? 392 HOH   A O   1 
HETATM 1228 O  O   . HOH   G 5 .   ? 4.694  8.252   27.821 1.00 39.35  ? 393 HOH   A O   1 
HETATM 1229 O  O   . HOH   G 5 .   ? 1.173  -5.710  15.210 1.00 32.64  ? 394 HOH   A O   1 
HETATM 1230 O  O   . HOH   G 5 .   ? 31.662 9.626   6.201  1.00 36.30  ? 395 HOH   A O   1 
HETATM 1231 O  O   . HOH   G 5 .   ? 18.008 -0.209  19.769 1.00 19.64  ? 396 HOH   A O   1 
HETATM 1232 O  O   . HOH   G 5 .   ? 21.895 2.359   -1.989 1.00 63.92  ? 397 HOH   A O   1 
HETATM 1233 O  O   . HOH   G 5 .   ? 2.978  25.910  17.288 1.00 48.41  ? 398 HOH   A O   1 
HETATM 1234 O  O   . HOH   G 5 .   ? 30.279 19.535  8.488  1.00 15.33  ? 399 HOH   A O   1 
HETATM 1235 O  O   . HOH   G 5 .   ? 4.759  -4.321  3.483  1.00 35.59  ? 400 HOH   A O   1 
HETATM 1236 O  O   . HOH   G 5 .   ? 1.085  -1.710  17.156 1.00 27.93  ? 401 HOH   A O   1 
HETATM 1237 O  O   . HOH   G 5 .   ? 4.025  11.037  18.918 1.00 26.69  ? 402 HOH   A O   1 
HETATM 1238 O  O   . HOH   G 5 .   ? 14.656 12.314  0.783  1.00 49.09  ? 403 HOH   A O   1 
HETATM 1239 O  O   . HOH   G 5 .   ? 4.347  -1.181  24.137 1.00 19.46  ? 404 HOH   A O   1 
HETATM 1240 O  O   . HOH   G 5 .   ? 3.929  6.858   25.557 1.00 21.42  ? 405 HOH   A O   1 
HETATM 1241 O  O   . HOH   G 5 .   ? 11.781 9.144   31.203 1.00 43.40  ? 406 HOH   A O   1 
HETATM 1242 O  O   . HOH   G 5 .   ? 6.683  11.441  3.936  1.00 42.80  ? 407 HOH   A O   1 
HETATM 1243 O  O   . HOH   G 5 .   ? 3.398  -2.275  21.551 1.00 15.94  ? 408 HOH   A O   1 
HETATM 1244 O  O   . HOH   G 5 .   ? 36.834 0.591   8.453  1.00 45.72  ? 409 HOH   A O   1 
HETATM 1245 O  O   . HOH   G 5 .   ? 23.914 21.928  7.741  1.00 32.21  ? 410 HOH   A O   1 
HETATM 1246 O  O   . HOH   G 5 .   ? 17.099 11.123  0.251  1.00 45.90  ? 411 HOH   A O   1 
HETATM 1247 O  O   . HOH   G 5 .   ? 23.704 2.461   19.671 1.00 23.31  ? 412 HOH   A O   1 
HETATM 1248 O  O   . HOH   G 5 .   ? 32.674 7.669   2.813  1.00 49.96  ? 413 HOH   A O   1 
HETATM 1249 O  O   . HOH   G 5 .   ? 11.738 14.272  1.488  1.00 43.57  ? 414 HOH   A O   1 
HETATM 1250 O  O   . HOH   G 5 .   ? 5.375  2.347   7.017  1.00 43.25  ? 415 HOH   A O   1 
HETATM 1251 O  O   . HOH   G 5 .   ? 22.017 19.014  5.845  1.00 3.00   ? 416 HOH   A O   1 
HETATM 1252 O  O   . HOH   G 5 .   ? 18.199 9.171   -1.577 1.00 26.95  ? 417 HOH   A O   1 
HETATM 1253 O  O   . HOH   G 5 .   ? 7.065  13.529  5.224  1.00 29.57  ? 418 HOH   A O   1 
HETATM 1254 O  O   . HOH   G 5 .   ? 15.781 17.177  29.541 1.00 36.61  ? 419 HOH   A O   1 
HETATM 1255 O  O   . HOH   G 5 .   ? 1.964  10.367  28.785 1.00 20.69  ? 420 HOH   A O   1 
HETATM 1256 O  O   . HOH   G 5 .   ? -0.688 15.665  11.534 1.00 52.13  ? 421 HOH   A O   1 
HETATM 1257 O  O   . HOH   G 5 .   ? 14.048 -11.232 4.397  1.00 26.92  ? 422 HOH   A O   1 
HETATM 1258 O  O   . HOH   G 5 .   ? 9.333  -7.918  0.305  1.00 30.80  ? 423 HOH   A O   1 
HETATM 1259 O  O   . HOH   G 5 .   ? 15.373 -7.617  25.617 1.00 37.71  ? 424 HOH   A O   1 
HETATM 1260 O  O   . HOH   G 5 .   ? 30.825 10.549  15.672 1.00 53.12  ? 425 HOH   A O   1 
HETATM 1261 O  O   . HOH   G 5 .   ? 22.017 -5.147  11.148 1.00 69.43  ? 426 HOH   A O   1 
HETATM 1262 O  O   . HOH   G 5 .   ? 30.592 7.116   17.195 1.00 41.13  ? 427 HOH   A O   1 
HETATM 1263 O  O   . HOH   G 5 .   ? 8.565  -7.262  8.505  1.00 39.14  ? 428 HOH   A O   1 
HETATM 1264 O  O   . HOH   G 5 .   ? 19.282 2.795   26.084 1.00 32.45  ? 429 HOH   A O   1 
HETATM 1265 O  O   . HOH   G 5 .   ? 29.838 -0.022  3.518  1.00 40.45  ? 430 HOH   A O   1 
HETATM 1266 O  O   . HOH   G 5 .   ? 1.943  14.011  4.847  1.00 51.42  ? 431 HOH   A O   1 
HETATM 1267 O  O   . HOH   G 5 .   ? 37.536 17.765  12.749 1.00 33.03  ? 432 HOH   A O   1 
HETATM 1268 O  O   . HOH   G 5 .   ? 21.916 19.565  19.191 1.00 53.26  ? 433 HOH   A O   1 
HETATM 1269 O  O   . HOH   G 5 .   ? 3.142  14.323  20.091 1.00 26.01  ? 434 HOH   A O   1 
HETATM 1270 O  O   . HOH   G 5 .   ? 28.633 12.528  2.511  1.00 53.31  ? 435 HOH   A O   1 
HETATM 1271 O  O   . HOH   G 5 .   ? 7.195  -5.168  2.559  1.00 22.92  ? 436 HOH   A O   1 
HETATM 1272 O  O   . HOH   G 5 .   ? 24.262 6.960   21.362 1.00 27.93  ? 437 HOH   A O   1 
HETATM 1273 O  O   . HOH   G 5 .   ? 16.907 -7.473  10.471 1.00 36.33  ? 438 HOH   A O   1 
HETATM 1274 O  O   . HOH   G 5 .   ? 20.695 9.159   -2.619 1.00 49.54  ? 439 HOH   A O   1 
HETATM 1275 O  O   . HOH   G 5 .   ? 24.329 15.066  24.028 1.00 23.31  ? 440 HOH   A O   1 
HETATM 1276 O  O   . HOH   G 5 .   ? 23.939 18.987  5.661  1.00 30.87  ? 441 HOH   A O   1 
HETATM 1277 O  O   . HOH   G 5 .   ? 24.461 10.385  22.013 1.00 28.41  ? 442 HOH   A O   1 
HETATM 1278 O  O   . HOH   G 5 .   ? 26.397 -1.924  14.792 1.00 28.96  ? 443 HOH   A O   1 
HETATM 1279 O  O   . HOH   G 5 .   ? 30.413 10.654  18.743 1.00 43.82  ? 444 HOH   A O   1 
HETATM 1280 O  O   . HOH   G 5 .   ? 4.227  -0.873  28.912 1.00 22.36  ? 445 HOH   A O   1 
HETATM 1281 O  O   . HOH   G 5 .   ? -0.124 16.393  18.848 1.00 38.33  ? 446 HOH   A O   1 
HETATM 1282 O  O   . HOH   G 5 .   ? 19.442 -7.439  6.376  1.00 63.53  ? 447 HOH   A O   1 
HETATM 1283 O  O   . HOH   G 5 .   ? 21.025 20.663  5.626  1.00 10.97  ? 448 HOH   A O   1 
HETATM 1284 O  O   . HOH   G 5 .   ? 0.838  14.511  22.131 1.00 27.69  ? 449 HOH   A O   1 
HETATM 1285 O  O   . HOH   G 5 .   ? 11.922 11.353  0.386  1.00 55.00  ? 450 HOH   A O   1 
HETATM 1286 O  O   . HOH   G 5 .   ? 31.749 3.741   2.785  1.00 39.03  ? 451 HOH   A O   1 
HETATM 1287 O  O   . HOH   G 5 .   ? 38.916 5.570   7.115  1.00 46.43  ? 452 HOH   A O   1 
HETATM 1288 O  O   . HOH   G 5 .   ? 21.596 -2.305  34.560 1.00 35.81  ? 453 HOH   A O   1 
HETATM 1289 O  O   . HOH   G 5 .   ? 36.817 16.730  15.459 1.00 52.21  ? 454 HOH   A O   1 
HETATM 1290 O  O   . HOH   G 5 .   ? 19.597 -5.283  10.022 1.00 35.78  ? 455 HOH   A O   1 
HETATM 1291 O  O   . HOH   G 5 .   ? 7.477  -5.215  32.457 1.00 40.78  ? 456 HOH   A O   1 
HETATM 1292 O  O   . HOH   G 5 .   ? 6.870  -8.535  23.663 1.00 33.55  ? 457 HOH   A O   1 
HETATM 1293 O  O   . HOH   G 5 .   ? 3.411  -6.872  15.263 1.00 54.69  ? 458 HOH   A O   1 
HETATM 1294 O  O   . HOH   G 5 .   ? 7.478  -7.527  2.200  1.00 49.42  ? 459 HOH   A O   1 
HETATM 1295 O  O   . HOH   G 5 .   ? 21.353 -3.349  32.598 1.00 31.83  ? 460 HOH   A O   1 
HETATM 1296 O  O   . HOH   G 5 .   ? 13.341 -12.995 6.803  1.00 41.73  ? 461 HOH   A O   1 
HETATM 1297 O  O   . HOH   G 5 .   ? 8.205  25.462  15.125 1.00 48.35  ? 462 HOH   A O   1 
HETATM 1298 O  O   . HOH   G 5 .   ? 31.482 2.017   13.853 1.00 46.35  ? 463 HOH   A O   1 
HETATM 1299 O  O   . HOH   G 5 .   ? -0.326 5.565   28.616 1.00 55.71  ? 464 HOH   A O   1 
HETATM 1300 O  O   . HOH   G 5 .   ? 11.232 -13.062 8.121  1.00 33.82  ? 465 HOH   A O   1 
HETATM 1301 O  O   . HOH   G 5 .   ? 15.578 10.905  -1.818 1.00 30.80  ? 466 HOH   A O   1 
HETATM 1302 O  O   . HOH   G 5 .   ? 14.241 -6.344  32.930 1.00 52.33  ? 467 HOH   A O   1 
HETATM 1303 O  O   . HOH   G 5 .   ? -0.696 13.613  17.757 1.00 41.55  ? 468 HOH   A O   1 
HETATM 1304 O  O   . HOH   G 5 .   ? 22.094 2.493   22.109 1.00 42.29  ? 469 HOH   A O   1 
HETATM 1305 O  O   . HOH   G 5 .   ? 36.426 -1.571  11.915 1.00 49.20  ? 470 HOH   A O   1 
HETATM 1306 O  O   . HOH   G 5 .   ? 25.701 11.777  -0.590 1.00 40.75  ? 471 HOH   A O   1 
HETATM 1307 O  O   . HOH   G 5 .   ? 6.218  16.270  25.751 1.00 39.22  ? 472 HOH   A O   1 
HETATM 1308 O  O   . HOH   G 5 .   ? 36.436 10.024  13.410 1.00 39.12  ? 473 HOH   A O   1 
HETATM 1309 O  O   . HOH   G 5 .   ? -2.233 2.939   5.788  1.00 104.91 ? 474 HOH   A O   1 
HETATM 1310 O  O   . HOH   G 5 .   ? 12.254 24.401  14.905 1.00 54.48  ? 475 HOH   A O   1 
HETATM 1311 O  O   . HOH   G 5 .   ? 15.984 -12.284 8.387  1.00 33.04  ? 476 HOH   A O   1 
HETATM 1312 O  O   . HOH   G 5 .   ? 24.626 13.151  1.805  1.00 30.10  ? 477 HOH   A O   1 
HETATM 1313 O  O   . HOH   G 5 .   ? 17.414 11.868  27.091 1.00 54.53  ? 478 HOH   A O   1 
HETATM 1314 O  O   . HOH   G 5 .   ? 8.105  20.230  6.557  1.00 38.96  ? 479 HOH   A O   1 
HETATM 1315 O  O   . HOH   G 5 .   ? 35.499 7.517   17.219 1.00 45.58  ? 480 HOH   A O   1 
HETATM 1316 O  O   . HOH   G 5 .   ? 22.283 -9.119  6.923  1.00 22.28  ? 481 HOH   A O   1 
HETATM 1317 O  O   . HOH   G 5 .   ? 19.568 -0.237  19.930 1.00 20.18  ? 482 HOH   A O   1 
HETATM 1318 O  O   . HOH   G 5 .   ? 5.782  6.165   2.521  1.00 26.45  ? 483 HOH   A O   1 
HETATM 1319 O  O   . HOH   G 5 .   ? 1.802  17.754  26.961 1.00 39.05  ? 484 HOH   A O   1 
HETATM 1320 O  O   . HOH   G 5 .   ? 22.698 -5.841  2.246  1.00 41.57  ? 485 HOH   A O   1 
HETATM 1321 O  O   . HOH   G 5 .   ? 21.937 -2.033  17.250 1.00 33.56  ? 486 HOH   A O   1 
HETATM 1322 O  O   . HOH   G 5 .   ? 1.045  15.880  25.071 1.00 33.97  ? 487 HOH   A O   1 
HETATM 1323 O  O   . HOH   G 5 .   ? 19.593 13.679  -1.623 1.00 54.66  ? 488 HOH   A O   1 
HETATM 1324 O  O   . HOH   G 5 .   ? 22.129 10.402  24.642 1.00 31.99  ? 489 HOH   A O   1 
HETATM 1325 O  O   . HOH   G 5 .   ? 17.011 14.469  1.841  1.00 46.45  ? 490 HOH   A O   1 
HETATM 1326 O  O   . HOH   G 5 .   ? 8.837  7.633   2.292  1.00 57.87  ? 491 HOH   A O   1 
HETATM 1327 O  O   . HOH   G 5 .   ? 16.431 -7.052  31.573 1.00 32.70  ? 492 HOH   A O   1 
HETATM 1328 O  O   . HOH   G 5 .   ? 31.732 4.415   15.838 1.00 44.17  ? 493 HOH   A O   1 
HETATM 1329 O  O   . HOH   G 5 .   ? 3.203  -1.622  26.925 1.00 46.66  ? 494 HOH   A O   1 
HETATM 1330 O  O   . HOH   G 5 .   ? -2.336 19.490  25.650 1.00 28.55  ? 495 HOH   A O   1 
HETATM 1331 O  O   . HOH   G 5 .   ? 33.704 17.312  23.665 1.00 30.42  ? 496 HOH   A O   1 
HETATM 1332 O  O   . HOH   G 5 .   ? 20.184 11.558  -2.812 1.00 39.99  ? 497 HOH   A O   1 
HETATM 1333 O  O   . HOH   G 5 .   ? 37.473 -2.010  8.773  1.00 128.01 ? 498 HOH   A O   1 
HETATM 1334 O  O   . HOH   G 5 .   ? 4.164  -7.205  22.772 1.00 47.13  ? 499 HOH   A O   1 
HETATM 1335 O  O   . HOH   G 5 .   ? 18.344 -7.505  35.775 1.00 38.76  ? 500 HOH   A O   1 
HETATM 1336 O  O   . HOH   G 5 .   ? 20.379 12.857  26.909 1.00 55.11  ? 501 HOH   A O   1 
HETATM 1337 O  O   . HOH   G 5 .   ? 3.807  15.175  25.584 1.00 61.79  ? 502 HOH   A O   1 
HETATM 1338 O  O   . HOH   G 5 .   ? 22.708 12.493  -2.693 1.00 37.20  ? 503 HOH   A O   1 
HETATM 1339 O  O   . HOH   G 5 .   ? 35.992 -3.833  7.593  1.00 41.69  ? 504 HOH   A O   1 
HETATM 1340 O  O   . HOH   G 5 .   ? 11.986 14.153  30.821 1.00 34.87  ? 505 HOH   A O   1 
HETATM 1341 O  O   . HOH   G 5 .   ? 3.320  -3.766  -4.315 1.00 37.35  ? 506 HOH   A O   1 
HETATM 1342 O  O   . HOH   G 5 .   ? 4.823  -6.958  25.084 1.00 43.94  ? 507 HOH   A O   1 
HETATM 1343 O  O   . HOH   G 5 .   ? 2.490  26.398  21.371 1.00 49.58  ? 508 HOH   A O   1 
HETATM 1344 O  O   . HOH   G 5 .   ? 5.356  23.393  8.039  1.00 48.89  ? 509 HOH   A O   1 
HETATM 1345 O  O   . HOH   G 5 .   ? 2.399  -5.914  27.463 1.00 64.97  ? 510 HOH   A O   1 
HETATM 1346 O  O   . HOH   G 5 .   ? 4.147  14.719  28.233 1.00 56.68  ? 511 HOH   A O   1 
HETATM 1347 O  O   . HOH   G 5 .   ? 2.724  29.396  14.947 1.00 33.50  ? 512 HOH   A O   1 
HETATM 1348 O  O   . HOH   G 5 .   ? 4.669  22.387  5.922  1.00 59.81  ? 513 HOH   A 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   . SER   A 1   ? 0.7657 0.5283 0.1275 -0.0546 -0.1222 -0.1052 7   SER   A N   
2    C CA  . SER   A 1   ? 0.7610 0.5408 0.1561 -0.0503 -0.1280 -0.1037 7   SER   A CA  
3    C C   . SER   A 1   ? 0.7580 0.5441 0.1579 -0.0406 -0.1255 -0.0928 7   SER   A C   
4    O O   . SER   A 1   ? 0.7795 0.5569 0.1529 -0.0377 -0.1250 -0.0870 7   SER   A O   
5    C CB  . SER   A 1   ? 0.7911 0.5744 0.1886 -0.0542 -0.1495 -0.1104 7   SER   A CB  
6    O OG  . SER   A 1   ? 0.8460 0.6187 0.2114 -0.0525 -0.1644 -0.1072 7   SER   A OG  
7    N N   . GLY   A 2   ? 0.7285 0.5275 0.1605 -0.0369 -0.1215 -0.0908 8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.7192 0.5207 0.1542 -0.0298 -0.1164 -0.0815 8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.6982 0.5050 0.1589 -0.0293 -0.1005 -0.0787 8   GLY   A C   
10   O O   . GLY   A 2   ? 0.6933 0.4968 0.1580 -0.0331 -0.0889 -0.0791 8   GLY   A O   
11   N N   . ALA   A 3   ? 0.6883 0.5001 0.1642 -0.0250 -0.0985 -0.0755 9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.6758 0.4882 0.1722 -0.0263 -0.0818 -0.0734 9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.6710 0.4779 0.1607 -0.0228 -0.0739 -0.0656 9   ALA   A C   
14   O O   . ALA   A 3   ? 0.6755 0.4828 0.1570 -0.0175 -0.0827 -0.0634 9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.6615 0.4863 0.1982 -0.0287 -0.0822 -0.0831 9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.6581 0.4572 0.1498 -0.0266 -0.0565 -0.0617 10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.6594 0.4498 0.1449 -0.0265 -0.0450 -0.0559 10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.6439 0.4392 0.1677 -0.0282 -0.0343 -0.0632 10  ILE   A C   
19   O O   . ILE   A 4   ? 0.6161 0.4137 0.1598 -0.0330 -0.0273 -0.0689 10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.6753 0.4494 0.1316 -0.0319 -0.0333 -0.0461 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.6869 0.4594 0.1155 -0.0308 -0.0429 -0.0404 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.6981 0.4594 0.1405 -0.0341 -0.0214 -0.0404 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.7096 0.4712 0.1238 -0.0360 -0.0352 -0.0324 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.6604 0.4570 0.1965 -0.0242 -0.0318 -0.0637 11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.6711 0.4721 0.2475 -0.0258 -0.0187 -0.0711 11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.6928 0.4745 0.2538 -0.0298 0.0023  -0.0660 11  TYR   A C   
27   O O   . TYR   A 5   ? 0.6873 0.4652 0.2385 -0.0249 0.0009  -0.0621 11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.6588 0.4795 0.2744 -0.0176 -0.0338 -0.0778 11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.6688 0.5059 0.2983 -0.0171 -0.0538 -0.0840 11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.6662 0.5146 0.3327 -0.0222 -0.0499 -0.0940 11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.6924 0.5305 0.2938 -0.0134 -0.0746 -0.0805 11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.6750 0.5360 0.3501 -0.0239 -0.0673 -0.1002 11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.6985 0.5469 0.3065 -0.0154 -0.0913 -0.0868 11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.6979 0.5581 0.3427 -0.0207 -0.0882 -0.0965 11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.7225 0.5914 0.3714 -0.0244 -0.1046 -0.1032 11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.7112 0.4771 0.2635 -0.0399 0.0216  -0.0656 12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.7365 0.4777 0.2675 -0.0484 0.0444  -0.0614 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.7489 0.4850 0.3140 -0.0557 0.0668  -0.0714 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.7550 0.4908 0.3281 -0.0611 0.0702  -0.0751 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.7653 0.4863 0.2449 -0.0558 0.0455  -0.0498 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.7602 0.4862 0.2397 -0.0570 0.0371  -0.0493 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.7996 0.4909 0.2545 -0.0684 0.0693  -0.0463 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.7496 0.4818 0.3371 -0.0558 0.0827  -0.0765 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.7502 0.4772 0.3745 -0.0632 0.1072  -0.0877 13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.7313 0.4848 0.4092 -0.0599 0.0993  -0.0992 13  GLY   A C   
46   O O   . GLY   A 7   ? 0.7098 0.4904 0.4225 -0.0487 0.0795  -0.1027 13  GLY   A O   
47   N N   . ASN   A 8   ? 0.7369 0.4816 0.4205 -0.0703 0.1139  -0.1051 14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.7156 0.4852 0.4474 -0.0689 0.1061  -0.1166 14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.7168 0.4894 0.4228 -0.0693 0.0886  -0.1120 14  ASN   A C   
50   O O   . ASN   A 8   ? 0.7067 0.4880 0.4377 -0.0736 0.0899  -0.1208 14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.7215 0.4843 0.4913 -0.0796 0.1350  -0.1300 14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.7477 0.5266 0.5774 -0.0752 0.1446  -0.1405 14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.7261 0.5317 0.6155 -0.0729 0.1401  -0.1524 14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.7773 0.5399 0.5951 -0.0745 0.1590  -0.1366 14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.7226 0.4883 0.3810 -0.0650 0.0732  -0.0990 15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.7194 0.4866 0.3532 -0.0643 0.0577  -0.0938 15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.6755 0.4631 0.3058 -0.0535 0.0295  -0.0910 15  TYR   A C   
58   O O   . TYR   A 9   ? 0.6622 0.4551 0.2887 -0.0465 0.0208  -0.0874 15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.7571 0.4958 0.3377 -0.0702 0.0649  -0.0807 15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.8008 0.5114 0.3704 -0.0828 0.0912  -0.0811 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.8091 0.5167 0.4015 -0.0898 0.1038  -0.0904 15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.8405 0.5241 0.3723 -0.0894 0.1040  -0.0723 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.8415 0.5186 0.4191 -0.1027 0.1291  -0.0910 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.8714 0.5236 0.3859 -0.1032 0.1283  -0.0724 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.8791 0.5273 0.4160 -0.1097 0.1412  -0.0817 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.9173 0.5305 0.4338 -0.1245 0.1667  -0.0825 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.6519 0.4471 0.2800 -0.0534 0.0172  -0.0928 16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.6370 0.4449 0.2536 -0.0465 -0.0064 -0.0907 16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.6397 0.4335 0.2200 -0.0487 -0.0063 -0.0826 16  ARG   A C   
70   O O   . ARG   A 10  ? 0.6404 0.4274 0.2251 -0.0545 0.0029  -0.0852 16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.6303 0.4597 0.2834 -0.0464 -0.0198 -0.1030 16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.6522 0.4875 0.2871 -0.0442 -0.0403 -0.1029 16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.6451 0.5005 0.3126 -0.0450 -0.0568 -0.1143 16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.6584 0.5134 0.3110 -0.0491 -0.0673 -0.1182 16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.6536 0.5117 0.2882 -0.0470 -0.0880 -0.1181 16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.6481 0.5100 0.2761 -0.0396 -0.1020 -0.1131 16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.6074 0.4613 0.2275 -0.0530 -0.0933 -0.1231 16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.6433 0.4322 0.1905 -0.0443 -0.0153 -0.0728 17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.6506 0.4293 0.1707 -0.0454 -0.0163 -0.0652 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.6359 0.4253 0.1517 -0.0414 -0.0328 -0.0685 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.6380 0.4329 0.1432 -0.0367 -0.0445 -0.0673 17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.6773 0.4407 0.1631 -0.0457 -0.0123 -0.0517 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.6942 0.4486 0.1626 -0.0467 -0.0130 -0.0439 17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.6873 0.4358 0.1710 -0.0517 0.0046  -0.0491 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.6259 0.4150 0.1475 -0.0441 -0.0325 -0.0730 18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.6240 0.4181 0.1382 -0.0430 -0.0445 -0.0775 18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.6190 0.4016 0.1191 -0.0438 -0.0379 -0.0718 18  VAL   A C   
88   O O   . VAL   A 12  ? 0.6208 0.3927 0.1184 -0.0448 -0.0269 -0.0639 18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.6286 0.4338 0.1678 -0.0470 -0.0508 -0.0914 18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.6208 0.4397 0.1749 -0.0444 -0.0634 -0.0958 18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.6304 0.4327 0.1927 -0.0531 -0.0365 -0.0969 18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.6136 0.3966 0.1048 -0.0438 -0.0442 -0.0758 19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.6065 0.3802 0.0930 -0.0443 -0.0371 -0.0732 19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.6100 0.3809 0.1170 -0.0495 -0.0283 -0.0814 19  ASN   A C   
95   O O   . ASN   A 13  ? 0.6070 0.3847 0.1240 -0.0540 -0.0335 -0.0933 19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.5929 0.3661 0.0648 -0.0444 -0.0438 -0.0778 19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.5984 0.3721 0.0602 -0.0397 -0.0484 -0.0671 19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.6101 0.3885 0.0621 -0.0385 -0.0582 -0.0683 19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.5745 0.3436 0.0545 -0.0367 -0.0406 -0.0540 19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.6164 0.3762 0.1290 -0.0497 -0.0160 -0.0748 20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.6121 0.3653 0.1422 -0.0550 -0.0048 -0.0817 20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.6126 0.3674 0.1479 -0.0598 -0.0058 -0.0952 20  ARG   A C   
103  O O   . ARG   A 14  ? 0.6028 0.3606 0.1535 -0.0665 -0.0032 -0.1063 20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.6144 0.3509 0.1431 -0.0530 0.0066  -0.0702 20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.6052 0.3310 0.1483 -0.0587 0.0200  -0.0749 20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.6477 0.3550 0.1903 -0.0566 0.0299  -0.0660 20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.7000 0.3949 0.2549 -0.0629 0.0438  -0.0726 20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.7469 0.4346 0.3123 -0.0656 0.0527  -0.0804 20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.7012 0.3914 0.2665 -0.0624 0.0501  -0.0825 20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.7865 0.4621 0.3616 -0.0723 0.0662  -0.0868 20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.6225 0.3745 0.1441 -0.0579 -0.0091 -0.0951 21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.6341 0.3819 0.1527 -0.0643 -0.0081 -0.1078 21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.6555 0.4132 0.1683 -0.0705 -0.0229 -0.1195 21  HIS   A C   
114  O O   . HIS   A 15  ? 0.6660 0.4191 0.1780 -0.0793 -0.0222 -0.1317 21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.6360 0.3745 0.1423 -0.0614 -0.0034 -0.1045 21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.6658 0.4093 0.1514 -0.0585 -0.0147 -0.1019 21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.6900 0.4403 0.1699 -0.0511 -0.0209 -0.0893 21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.6865 0.4256 0.1528 -0.0634 -0.0193 -0.1105 21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.7000 0.4513 0.1598 -0.0511 -0.0288 -0.0911 21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.7028 0.4466 0.1529 -0.0584 -0.0281 -0.1035 21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.6692 0.4387 0.1783 -0.0665 -0.0362 -0.1155 22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.6847 0.4647 0.1918 -0.0701 -0.0536 -0.1235 22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.6913 0.4852 0.2277 -0.0714 -0.0562 -0.1271 22  LEU   A C   
124  O O   . LEU   A 16  ? 0.6853 0.4910 0.2281 -0.0729 -0.0722 -0.1324 22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.6883 0.4711 0.1739 -0.0636 -0.0662 -0.1161 22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.7212 0.4916 0.1778 -0.0635 -0.0651 -0.1144 22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.7215 0.4938 0.1565 -0.0586 -0.0780 -0.1088 22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.7371 0.4963 0.1812 -0.0739 -0.0653 -0.1270 22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.6908 0.4823 0.2448 -0.0706 -0.0408 -0.1236 23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.6894 0.4914 0.2721 -0.0727 -0.0383 -0.1277 23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.6989 0.5105 0.3023 -0.0823 -0.0448 -0.1431 23  ALA   A C   
132  O O   . ALA   A 17  ? 0.7063 0.5089 0.3070 -0.0897 -0.0377 -0.1502 23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.6809 0.4716 0.2708 -0.0723 -0.0183 -0.1215 23  ALA   A CB  
134  N N   . THR   A 18  ? 0.6919 0.5216 0.3160 -0.0824 -0.0594 -0.1480 24  THR   A N   
135  C CA  . THR   A 18  ? 0.6908 0.5344 0.3388 -0.0915 -0.0715 -0.1617 24  THR   A CA  
136  C C   . THR   A 18  ? 0.7003 0.5470 0.3816 -0.0992 -0.0549 -0.1708 24  THR   A C   
137  O O   . THR   A 18  ? 0.7107 0.5476 0.3952 -0.0966 -0.0346 -0.1653 24  THR   A O   
138  C CB  . THR   A 18  ? 0.6831 0.5459 0.3467 -0.0867 -0.0942 -0.1614 24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.6705 0.5462 0.3718 -0.0831 -0.0864 -0.1614 24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.7019 0.5590 0.3328 -0.0776 -0.1064 -0.1506 24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.6939 0.5529 0.3986 -0.1098 -0.0637 -0.1847 25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.6930 0.5557 0.4310 -0.1185 -0.0478 -0.1950 25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.6791 0.5517 0.4490 -0.1130 -0.0379 -0.1923 25  HIS   A C   
144  O O   . HIS   A 19  ? 0.6742 0.5360 0.4528 -0.1159 -0.0142 -0.1930 25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.7031 0.5804 0.4626 -0.1316 -0.0625 -0.2106 25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.7284 0.6161 0.5316 -0.1404 -0.0488 -0.2225 25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.7582 0.6302 0.5588 -0.1507 -0.0272 -0.2301 25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.7241 0.6343 0.5746 -0.1401 -0.0513 -0.2276 25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.7462 0.6312 0.5896 -0.1572 -0.0177 -0.2401 25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.7299 0.6388 0.6065 -0.1514 -0.0311 -0.2395 25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.6771 0.5675 0.4627 -0.1057 -0.0550 -0.1892 26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.6778 0.5776 0.4945 -0.1000 -0.0463 -0.1870 26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.6994 0.5776 0.4900 -0.0934 -0.0249 -0.1742 26  ASN   A C   
154  O O   . ASN   A 20  ? 0.6987 0.5760 0.5108 -0.0933 -0.0082 -0.1746 26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.6870 0.6077 0.5213 -0.0922 -0.0717 -0.1848 26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.7232 0.6606 0.6081 -0.0892 -0.0650 -0.1885 26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.7137 0.6715 0.6466 -0.0957 -0.0695 -0.2008 26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.7348 0.6632 0.6112 -0.0802 -0.0530 -0.1784 26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.7124 0.5731 0.4575 -0.0886 -0.0260 -0.1630 27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.7168 0.5574 0.4361 -0.0837 -0.0092 -0.1502 27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.7142 0.5371 0.4357 -0.0917 0.0151  -0.1529 27  ASP   A C   
162  O O   . ASP   A 21  ? 0.7205 0.5305 0.4408 -0.0923 0.0327  -0.1483 27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.7500 0.5789 0.4264 -0.0775 -0.0174 -0.1388 27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.7834 0.6222 0.4484 -0.0693 -0.0368 -0.1332 27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.7622 0.6108 0.4459 -0.0654 -0.0389 -0.1326 27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.8182 0.6527 0.4552 -0.0670 -0.0481 -0.1296 27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.6965 0.5160 0.4189 -0.0988 0.0170  -0.1609 28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.6905 0.4911 0.4138 -0.1066 0.0396  -0.1639 28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.6545 0.4625 0.4174 -0.1154 0.0535  -0.1766 28  TRP   A C   
170  O O   . TRP   A 22  ? 0.6422 0.4305 0.4021 -0.1195 0.0758  -0.1747 28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.6992 0.4931 0.4120 -0.1116 0.0382  -0.1693 28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.7157 0.4977 0.3928 -0.1042 0.0318  -0.1576 28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.7302 0.5209 0.3939 -0.1014 0.0135  -0.1581 28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.7245 0.4824 0.3768 -0.0997 0.0445  -0.1445 28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.7458 0.5205 0.3806 -0.0954 0.0162  -0.1472 28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.7425 0.4985 0.3726 -0.0938 0.0340  -0.1385 28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.7327 0.4688 0.3788 -0.1006 0.0631  -0.1370 28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.7577 0.4949 0.3670 -0.0879 0.0410  -0.1255 28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.7549 0.4706 0.3761 -0.0948 0.0675  -0.1228 28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.7621 0.4804 0.3686 -0.0879 0.0562  -0.1171 28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.6264 0.4619 0.4263 -0.1181 0.0397  -0.1887 29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.6140 0.4615 0.4598 -0.1256 0.0516  -0.2014 29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.6216 0.4640 0.4743 -0.1211 0.0650  -0.1954 29  ALA   A C   
184  O O   . ALA   A 23  ? 0.6195 0.4692 0.5113 -0.1272 0.0792  -0.2059 29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.5912 0.4719 0.4770 -0.1279 0.0287  -0.2135 29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.6259 0.4543 0.4410 -0.1117 0.0628  -0.1795 30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.6260 0.4452 0.4383 -0.1085 0.0754  -0.1728 30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.6468 0.4374 0.4042 -0.1041 0.0803  -0.1551 30  ASN   A C   
189  O O   . ASN   A 24  ? 0.6598 0.4462 0.4029 -0.0986 0.0798  -0.1462 30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.6321 0.4773 0.4688 -0.0996 0.0564  -0.1730 30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.6640 0.5386 0.5616 -0.1031 0.0506  -0.1889 30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.6753 0.5503 0.6084 -0.1101 0.0715  -0.1988 30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.6579 0.5566 0.5690 -0.0995 0.0221  -0.1921 30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.6516 0.4236 0.3806 -0.1066 0.0841  -0.1501 31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.6732 0.4204 0.3551 -0.1024 0.0854  -0.1330 31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.6945 0.4166 0.3564 -0.1062 0.1037  -0.1249 31  LEU   A C   
197  O O   . LEU   A 25  ? 0.6966 0.4070 0.3728 -0.1157 0.1244  -0.1329 31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.6774 0.4085 0.3443 -0.1055 0.0900  -0.1316 31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.7040 0.4084 0.3289 -0.1017 0.0921  -0.1137 31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.7177 0.4328 0.3235 -0.0910 0.0718  -0.1029 31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.7030 0.3899 0.3214 -0.1049 0.1002  -0.1135 31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.7122 0.4242 0.3395 -0.1003 0.0969  -0.1097 32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.7322 0.4159 0.3311 -0.1057 0.1125  -0.1005 32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.7457 0.4034 0.3011 -0.1052 0.1099  -0.0839 32  VAL   A C   
205  O O   . VAL   A 26  ? 0.7678 0.3942 0.3021 -0.1138 0.1257  -0.0790 32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.7438 0.4361 0.3390 -0.1011 0.1072  -0.0968 32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.7743 0.4335 0.3345 -0.1092 0.1244  -0.0877 32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.7246 0.4439 0.3683 -0.0996 0.1074  -0.1119 32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.7229 0.3929 0.2669 -0.0954 0.0897  -0.0754 33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.7244 0.3760 0.2367 -0.0928 0.0840  -0.0597 33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.7042 0.3764 0.2231 -0.0828 0.0657  -0.0586 33  TRP   A C   
212  O O   . TRP   A 27  ? 0.6988 0.3947 0.2293 -0.0775 0.0537  -0.0640 33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.7344 0.3671 0.2095 -0.0945 0.0830  -0.0444 33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.7524 0.3738 0.1995 -0.0899 0.0705  -0.0269 33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.7843 0.3763 0.2080 -0.0940 0.0745  -0.0146 33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.7482 0.3866 0.1885 -0.0806 0.0517  -0.0190 33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.7931 0.3860 0.2014 -0.0869 0.0578  0.0005  33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.7712 0.3926 0.1895 -0.0792 0.0449  -0.0026 33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.7378 0.4027 0.1883 -0.0738 0.0400  -0.0242 33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.7730 0.4058 0.1840 -0.0716 0.0282  0.0074  33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.7461 0.4192 0.1844 -0.0669 0.0248  -0.0146 33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.7551 0.4134 0.1757 -0.0660 0.0197  0.0005  33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.6952 0.3564 0.2070 -0.0807 0.0646  -0.0522 34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.6814 0.3574 0.1982 -0.0725 0.0511  -0.0513 34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.6921 0.3505 0.1906 -0.0684 0.0483  -0.0350 34  GLU   A C   
226  O O   . GLU   A 28  ? 0.6966 0.3297 0.1826 -0.0726 0.0573  -0.0268 34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.6861 0.3758 0.2300 -0.0740 0.0529  -0.0676 34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.7281 0.4008 0.2818 -0.0809 0.0692  -0.0732 34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.7816 0.4348 0.3261 -0.0778 0.0728  -0.0636 34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.8368 0.4639 0.3707 -0.0818 0.0846  -0.0566 34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.7585 0.4205 0.3060 -0.0715 0.0645  -0.0628 34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.6954 0.3656 0.1918 -0.0605 0.0354  -0.0296 35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.7184 0.3759 0.2053 -0.0554 0.0310  -0.0140 35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.7199 0.3923 0.2216 -0.0484 0.0250  -0.0182 35  ASP   A C   
235  O O   . ASP   A 29  ? 0.7269 0.4161 0.2252 -0.0449 0.0148  -0.0192 35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.7418 0.3932 0.2033 -0.0548 0.0216  0.0021  35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.8152 0.4485 0.2669 -0.0518 0.0165  0.0205  35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.7966 0.4335 0.2660 -0.0448 0.0146  0.0220  35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.8836 0.4974 0.3094 -0.0569 0.0145  0.0336  35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.7121 0.3760 0.2287 -0.0472 0.0331  -0.0212 36  SER   A N   
241  C CA  A SER   A 30  ? 0.7089 0.3833 0.2394 -0.0422 0.0313  -0.0269 36  SER   A CA  
242  C CA  B SER   A 30  ? 0.7087 0.3830 0.2393 -0.0422 0.0313  -0.0268 36  SER   A CA  
243  C C   . SER   A 30  ? 0.7069 0.3858 0.2340 -0.0342 0.0207  -0.0132 36  SER   A C   
244  O O   . SER   A 30  ? 0.7048 0.3989 0.2339 -0.0319 0.0153  -0.0189 36  SER   A O   
245  C CB  A SER   A 30  ? 0.7183 0.3792 0.2651 -0.0432 0.0448  -0.0327 36  SER   A CB  
246  C CB  B SER   A 30  ? 0.7177 0.3782 0.2645 -0.0430 0.0448  -0.0321 36  SER   A CB  
247  O OG  A SER   A 30  ? 0.7353 0.4006 0.2946 -0.0386 0.0461  -0.0362 36  SER   A OG  
248  O OG  B SER   A 30  ? 0.7468 0.3881 0.2943 -0.0379 0.0469  -0.0157 36  SER   A OG  
249  N N   . SER   A 31  ? 0.6964 0.3613 0.2173 -0.0311 0.0170  0.0050  37  SER   A N   
250  C CA  . SER   A 31  ? 0.6858 0.3574 0.2082 -0.0241 0.0054  0.0183  37  SER   A CA  
251  C C   . SER   A 31  ? 0.6653 0.3523 0.1701 -0.0255 -0.0059 0.0193  37  SER   A C   
252  O O   . SER   A 31  ? 0.6642 0.3612 0.1729 -0.0208 -0.0142 0.0255  37  SER   A O   
253  C CB  . SER   A 31  ? 0.7245 0.3777 0.2453 -0.0208 0.0006  0.0384  37  SER   A CB  
254  O OG  . SER   A 31  ? 0.7898 0.4350 0.2828 -0.0257 -0.0087 0.0506  37  SER   A OG  
255  N N   . ARG   A 32  ? 0.6470 0.3351 0.1348 -0.0319 -0.0052 0.0133  38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.6353 0.3363 0.1068 -0.0331 -0.0139 0.0129  38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.6304 0.3479 0.1074 -0.0333 -0.0133 -0.0042 38  ARG   A C   
258  O O   . ARG   A 32  ? 0.6484 0.3765 0.1132 -0.0329 -0.0208 -0.0047 38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.6393 0.3293 0.0881 -0.0400 -0.0132 0.0180  38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.6158 0.2870 0.0503 -0.0423 -0.0181 0.0365  38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.6515 0.3086 0.0556 -0.0515 -0.0143 0.0393  38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.6737 0.3436 0.0645 -0.0527 -0.0197 0.0369  38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.7028 0.3608 0.0652 -0.0602 -0.0203 0.0439  38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.7022 0.3334 0.0501 -0.0685 -0.0160 0.0524  38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.6873 0.3569 0.0464 -0.0606 -0.0240 0.0401  38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.6082 0.3263 0.1006 -0.0350 -0.0052 -0.0178 39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.5991 0.3300 0.0942 -0.0372 -0.0067 -0.0341 39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.5967 0.3336 0.0833 -0.0404 -0.0105 -0.0374 39  ASP   A C   
269  O O   . ASP   A 33  ? 0.6065 0.3548 0.0878 -0.0401 -0.0181 -0.0442 39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.6104 0.3503 0.1023 -0.0342 -0.0122 -0.0384 39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.6213 0.3695 0.1088 -0.0378 -0.0161 -0.0542 39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.6077 0.3538 0.1051 -0.0425 -0.0113 -0.0656 39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.6409 0.3960 0.1129 -0.0368 -0.0248 -0.0547 39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.5899 0.3167 0.0751 -0.0439 -0.0041 -0.0328 40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.5883 0.3197 0.0707 -0.0472 -0.0041 -0.0371 40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.5812 0.3100 0.0818 -0.0530 0.0063  -0.0476 40  LEU   A C   
277  O O   . LEU   A 34  ? 0.5815 0.2961 0.0866 -0.0562 0.0165  -0.0460 40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.6032 0.3249 0.0637 -0.0484 -0.0045 -0.0240 40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.6227 0.3507 0.0659 -0.0444 -0.0155 -0.0160 40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.6444 0.3592 0.0637 -0.0484 -0.0146 -0.0034 40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.6087 0.3539 0.0544 -0.0413 -0.0233 -0.0264 40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.5739 0.3164 0.0867 -0.0544 0.0035  -0.0584 41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.5747 0.3179 0.1098 -0.0604 0.0133  -0.0691 41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.5854 0.3367 0.1270 -0.0608 0.0128  -0.0720 41  LEU   A C   
285  O O   . LEU   A 35  ? 0.5854 0.3520 0.1300 -0.0566 0.0004  -0.0754 41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.5484 0.3035 0.1051 -0.0626 0.0100  -0.0834 41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.5450 0.2993 0.1276 -0.0705 0.0224  -0.0949 41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.5354 0.2864 0.1271 -0.0747 0.0265  -0.1031 41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.5298 0.3038 0.1375 -0.0719 0.0165  -0.1058 41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.6159 0.3546 0.1597 -0.0665 0.0275  -0.0712 42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.6393 0.3829 0.1952 -0.0680 0.0326  -0.0757 42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.6403 0.3935 0.2351 -0.0733 0.0410  -0.0912 42  VAL   A C   
293  O O   . VAL   A 36  ? 0.6413 0.3835 0.2412 -0.0795 0.0525  -0.0947 42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.6743 0.3934 0.2042 -0.0732 0.0464  -0.0654 42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.6822 0.4027 0.2280 -0.0764 0.0575  -0.0720 42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.6985 0.4105 0.1922 -0.0691 0.0360  -0.0503 42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.6369 0.4111 0.2607 -0.0708 0.0342  -0.1004 43  SER   A N   
298  C CA  . SER   A 37  ? 0.6479 0.4344 0.3145 -0.0761 0.0411  -0.1153 43  SER   A CA  
299  C C   . SER   A 37  ? 0.6645 0.4589 0.3574 -0.0753 0.0478  -0.1198 43  SER   A C   
300  O O   . SER   A 37  ? 0.6690 0.4587 0.3433 -0.0703 0.0457  -0.1112 43  SER   A O   
301  C CB  . SER   A 37  ? 0.6633 0.4709 0.3500 -0.0750 0.0237  -0.1248 43  SER   A CB  
302  O OG  . SER   A 37  ? 0.6992 0.5276 0.3971 -0.0680 0.0029  -0.1263 43  SER   A OG  
303  N N   . SER   A 38  ? 0.6752 0.4795 0.4119 -0.0810 0.0585  -0.1332 44  SER   A N   
304  C CA  . SER   A 38  ? 0.6995 0.5102 0.4680 -0.0805 0.0688  -0.1385 44  SER   A CA  
305  C C   . SER   A 38  ? 0.7021 0.5448 0.5130 -0.0724 0.0484  -0.1451 44  SER   A C   
306  O O   . SER   A 38  ? 0.6922 0.5554 0.5318 -0.0734 0.0344  -0.1542 44  SER   A O   
307  C CB  . SER   A 38  ? 0.7290 0.5290 0.5235 -0.0921 0.0968  -0.1494 44  SER   A CB  
308  O OG  . SER   A 38  ? 0.7675 0.5791 0.5881 -0.0979 0.0951  -0.1607 44  SER   A OG  
309  N N   . THR   A 39  ? 0.7144 0.5593 0.5301 -0.0653 0.0476  -0.1406 45  THR   A N   
310  C CA  . THR   A 39  ? 0.7050 0.5766 0.5609 -0.0559 0.0286  -0.1442 45  THR   A CA  
311  C C   . THR   A 39  ? 0.6940 0.5716 0.6032 -0.0573 0.0486  -0.1535 45  THR   A C   
312  O O   . THR   A 39  ? 0.7027 0.5587 0.6066 -0.0657 0.0789  -0.1556 45  THR   A O   
313  C CB  . THR   A 39  ? 0.7329 0.6025 0.5530 -0.0451 0.0089  -0.1315 45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.7716 0.6166 0.5565 -0.0457 0.0272  -0.1223 45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.7492 0.6181 0.5299 -0.0438 -0.0118 -0.1258 45  THR   A CG2 
316  N N   . THR   A 40  ? 0.6718 0.5779 0.6337 -0.0498 0.0316  -0.1593 46  THR   A N   
317  C CA  . THR   A 40  ? 0.6585 0.5762 0.6837 -0.0495 0.0480  -0.1693 46  THR   A CA  
318  C C   . THR   A 40  ? 0.6698 0.5777 0.6910 -0.0407 0.0555  -0.1617 46  THR   A C   
319  O O   . THR   A 40  ? 0.6617 0.5583 0.7057 -0.0445 0.0851  -0.1669 46  THR   A O   
320  C CB  . THR   A 40  ? 0.6401 0.5960 0.7316 -0.0453 0.0230  -0.1791 46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.6558 0.6239 0.7252 -0.0367 -0.0151 -0.1709 46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.6259 0.5915 0.7483 -0.0579 0.0318  -0.1933 46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.6851 0.5958 0.6769 -0.0297 0.0296  -0.1502 47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.7027 0.6044 0.6855 -0.0202 0.0318  -0.1418 47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.7417 0.6097 0.6502 -0.0247 0.0458  -0.1306 47  ALA   A C   
326  O O   . ALA   A 41  ? 0.7574 0.6138 0.6213 -0.0319 0.0445  -0.1269 47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.6990 0.6211 0.6908 -0.0064 -0.0058 -0.1356 47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.7476 0.5996 0.6455 -0.0211 0.0602  -0.1253 48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.7821 0.6028 0.6123 -0.0263 0.0729  -0.1148 48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.7864 0.6091 0.5731 -0.0178 0.0445  -0.1030 48  GLN   A C   
331  O O   . GLN   A 42  ? 0.7805 0.6206 0.5873 -0.0059 0.0216  -0.1013 48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.8186 0.6176 0.6509 -0.0289 0.1027  -0.1152 48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.8770 0.6566 0.7192 -0.0440 0.1391  -0.1245 48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.9789 0.7188 0.7516 -0.0573 0.1602  -0.1169 48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 1.0271 0.7489 0.7652 -0.0564 0.1653  -0.1090 48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.9923 0.7161 0.7425 -0.0708 0.1728  -0.1189 48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.7958 0.6003 0.5242 -0.0245 0.0457  -0.0952 49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.8040 0.6059 0.4852 -0.0194 0.0245  -0.0846 49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.8078 0.5872 0.4517 -0.0199 0.0368  -0.0763 49  GLY   A C   
340  O O   . GLY   A 43  ? 0.8150 0.5749 0.4553 -0.0281 0.0639  -0.0777 49  GLY   A O   
341  N N   . CYS   A 44  ? 0.8029 0.5821 0.4151 -0.0129 0.0184  -0.0681 50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.8084 0.5672 0.3861 -0.0132 0.0287  -0.0608 50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.7960 0.5421 0.3130 -0.0173 0.0211  -0.0507 50  CYS   A C   
344  O O   . CYS   A 44  ? 0.8081 0.5378 0.2939 -0.0183 0.0279  -0.0448 50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.8251 0.5921 0.4293 -0.0005 0.0198  -0.0610 50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.8885 0.6650 0.5665 0.0030  0.0376  -0.0718 50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.7712 0.5231 0.2727 -0.0206 0.0099  -0.0493 51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.7839 0.5253 0.2351 -0.0247 0.0041  -0.0402 51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.7973 0.5163 0.2197 -0.0371 0.0239  -0.0352 51  ASP   A C   
350  O O   . ASP   A 45  ? 0.7945 0.5074 0.2309 -0.0442 0.0383  -0.0390 51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.7979 0.5517 0.2450 -0.0238 -0.0130 -0.0404 51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.8117 0.5805 0.2663 -0.0142 -0.0354 -0.0429 51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.8200 0.5837 0.2544 -0.0095 -0.0416 -0.0388 51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.8125 0.5954 0.2904 -0.0125 -0.0461 -0.0490 51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.8118 0.5162 0.1919 -0.0409 0.0251  -0.0270 52  THR   A N   
356  C CA  . THR   A 46  ? 0.8216 0.5019 0.1651 -0.0545 0.0404  -0.0204 52  THR   A CA  
357  C C   . THR   A 46  ? 0.8187 0.5007 0.1368 -0.0584 0.0276  -0.0127 52  THR   A C   
358  O O   . THR   A 46  ? 0.8220 0.5160 0.1320 -0.0521 0.0110  -0.0103 52  THR   A O   
359  C CB  . THR   A 46  ? 0.8419 0.5048 0.1569 -0.0577 0.0501  -0.0167 52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.8339 0.4928 0.1786 -0.0548 0.0661  -0.0241 52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.8745 0.5113 0.1426 -0.0737 0.0614  -0.0087 52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.8120 0.4812 0.1197 -0.0683 0.0351  -0.0092 53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.8138 0.4847 0.1027 -0.0708 0.0224  -0.0008 53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.8207 0.4743 0.0652 -0.0805 0.0227  0.0098  53  ILE   A C   
365  O O   . ILE   A 47  ? 0.8493 0.4803 0.0730 -0.0911 0.0381  0.0114  53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.8157 0.4807 0.1148 -0.0759 0.0270  -0.0005 53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.8062 0.4882 0.1502 -0.0684 0.0277  -0.0121 53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.8268 0.4922 0.1088 -0.0773 0.0137  0.0097  53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.8056 0.5140 0.1738 -0.0556 0.0111  -0.0183 53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.7981 0.4610 0.0435 -0.0781 0.0068  0.0156  54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.7924 0.4423 0.0440 -0.0880 0.0038  0.0227  54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.8368 0.4683 0.0481 -0.0998 0.0057  0.0324  54  ALA   A C   
373  O O   . ALA   A 48  ? 0.8383 0.4762 0.0514 -0.0963 0.0005  0.0349  54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.7520 0.4200 0.0431 -0.0820 -0.0118 0.0234  54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.8692 0.4750 0.0466 -0.1146 0.0134  0.0378  55  ARG   A N   
376  C CA  . ARG   A 49  ? 0.9060 0.4892 0.0483 -0.1282 0.0124  0.0486  55  ARG   A CA  
377  C C   . ARG   A 49  ? 0.9334 0.5129 0.0500 -0.1368 -0.0003 0.0582  55  ARG   A C   
378  O O   . ARG   A 49  ? 0.9892 0.5455 0.0512 -0.1509 0.0082  0.0629  55  ARG   A O   
379  C CB  . ARG   A 49  ? 0.9495 0.5004 0.0502 -0.1413 0.0357  0.0481  55  ARG   A CB  
380  C CG  . ARG   A 49  ? 0.9130 0.4717 0.0507 -0.1325 0.0497  0.0357  55  ARG   A CG  
381  C CD  . ARG   A 49  ? 0.8814 0.4560 0.0482 -0.1237 0.0393  0.0361  55  ARG   A CD  
382  N NE  . ARG   A 49  ? 0.8616 0.4406 0.0576 -0.1188 0.0538  0.0243  55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.8726 0.4647 0.0982 -0.1116 0.0487  0.0213  55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.8711 0.4720 0.0955 -0.1074 0.0312  0.0299  55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.8547 0.4523 0.1145 -0.1084 0.0615  0.0090  55  ARG   A NH2 
386  N N   . CYS   A 50  ? 0.9025 0.5054 0.0517 -0.1289 -0.0192 0.0612  56  CYS   A N   
387  C CA  . CYS   A 50  ? 0.9070 0.5161 0.0518 -0.1340 -0.0322 0.0669  56  CYS   A CA  
388  C C   . CYS   A 50  ? 0.8922 0.5217 0.0554 -0.1276 -0.0515 0.0750  56  CYS   A C   
389  O O   . CYS   A 50  ? 0.8625 0.5008 0.0554 -0.1183 -0.0537 0.0738  56  CYS   A O   
390  C CB  . CYS   A 50  ? 0.8735 0.4965 0.0510 -0.1270 -0.0275 0.0554  56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.8367 0.4927 0.0575 -0.1059 -0.0329 0.0475  56  CYS   A SG  
392  N N   A ASP   A 51  ? 0.9039 0.5413 0.0578 -0.1326 -0.0642 0.0818  57  ASP   A N   
393  N N   B ASP   A 51  ? 0.9049 0.5421 0.0577 -0.1328 -0.0638 0.0817  57  ASP   A N   
394  C CA  A ASP   A 51  ? 0.8950 0.5543 0.0626 -0.1257 -0.0818 0.0899  57  ASP   A CA  
395  C CA  B ASP   A 51  ? 0.8993 0.5574 0.0625 -0.1273 -0.0820 0.0905  57  ASP   A CA  
396  C C   A ASP   A 51  ? 0.8678 0.5518 0.0618 -0.1180 -0.0831 0.0816  57  ASP   A C   
397  C C   B ASP   A 51  ? 0.8699 0.5517 0.0613 -0.1202 -0.0825 0.0815  57  ASP   A C   
398  O O   A ASP   A 51  ? 0.8749 0.5739 0.0648 -0.1181 -0.0972 0.0894  57  ASP   A O   
399  O O   B ASP   A 51  ? 0.8776 0.5716 0.0640 -0.1231 -0.0953 0.0885  57  ASP   A O   
400  C CB  A ASP   A 51  ? 0.9606 0.6090 0.0711 -0.1379 -0.1013 0.1123  57  ASP   A CB  
401  C CB  B ASP   A 51  ? 0.9734 0.6177 0.0706 -0.1417 -0.1000 0.1125  57  ASP   A CB  
402  C CG  A ASP   A 51  ? 1.0177 0.6576 0.0751 -0.1533 -0.1079 0.1204  57  ASP   A CG  
403  C CG  B ASP   A 51  ? 1.0173 0.6752 0.1187 -0.1352 -0.1212 0.1281  57  ASP   A CG  
404  O OD1 A ASP   A 51  ? 1.0147 0.6577 0.0677 -0.1540 -0.0966 0.1096  57  ASP   A OD1 
405  O OD1 B ASP   A 51  ? 1.0234 0.6912 0.1596 -0.1218 -0.1187 0.1242  57  ASP   A OD1 
406  O OD2 A ASP   A 51  ? 1.0573 0.6861 0.0836 -0.1654 -0.1244 0.1367  57  ASP   A OD2 
407  O OD2 B ASP   A 51  ? 1.0438 0.7025 0.1347 -0.1439 -0.1388 0.1407  57  ASP   A OD2 
408  N N   . CYS   A 52  ? 0.8303 0.5170 0.0574 -0.1118 -0.0686 0.0660  58  CYS   A N   
409  C CA  . CYS   A 52  ? 0.7649 0.4683 0.0542 -0.1058 -0.0642 0.0534  58  CYS   A CA  
410  C C   . CYS   A 52  ? 0.7092 0.4346 0.0544 -0.0954 -0.0686 0.0497  58  CYS   A C   
411  O O   . CYS   A 52  ? 0.7027 0.4314 0.0563 -0.0876 -0.0691 0.0496  58  CYS   A O   
412  C CB  . CYS   A 52  ? 0.7447 0.4436 0.0524 -0.0990 -0.0514 0.0421  58  CYS   A CB  
413  S SG  . CYS   A 52  ? 0.7559 0.4313 0.0466 -0.1103 -0.0403 0.0394  58  CYS   A SG  
414  N N   . GLN   A 53  ? 0.6799 0.4187 0.0525 -0.0962 -0.0707 0.0473  59  GLN   A N   
415  C CA  . GLN   A 53  ? 0.6540 0.4122 0.0539 -0.0871 -0.0736 0.0451  59  GLN   A CA  
416  C C   . GLN   A 53  ? 0.6116 0.3758 0.0496 -0.0823 -0.0636 0.0333  59  GLN   A C   
417  O O   . GLN   A 53  ? 0.5905 0.3681 0.0494 -0.0786 -0.0639 0.0308  59  GLN   A O   
418  C CB  . GLN   A 53  ? 0.6936 0.4636 0.0588 -0.0916 -0.0901 0.0585  59  GLN   A CB  
419  C CG  . GLN   A 53  ? 0.7667 0.5320 0.0714 -0.0918 -0.1079 0.0779  59  GLN   A CG  
420  C CD  . GLN   A 53  ? 0.8424 0.6247 0.1022 -0.0906 -0.1324 0.0972  59  GLN   A CD  
421  O OE1 . GLN   A 53  ? 0.8900 0.6691 0.1368 -0.1008 -0.1461 0.1103  59  GLN   A OE1 
422  N NE2 . GLN   A 53  ? 0.8135 0.6138 0.1133 -0.0800 -0.1294 0.0900  59  GLN   A NE2 
423  N N   . THR   A 54  ? 0.6037 0.3558 0.0472 -0.0832 -0.0553 0.0276  60  THR   A N   
424  C CA  . THR   A 54  ? 0.6004 0.3523 0.0459 -0.0785 -0.0499 0.0207  60  THR   A CA  
425  C C   . THR   A 54  ? 0.5905 0.3311 0.0450 -0.0725 -0.0442 0.0164  60  THR   A C   
426  O O   . THR   A 54  ? 0.5922 0.3221 0.0441 -0.0760 -0.0419 0.0181  60  THR   A O   
427  C CB  . THR   A 54  ? 0.6358 0.3847 0.0456 -0.0868 -0.0501 0.0214  60  THR   A CB  
428  O OG1 . THR   A 54  ? 0.7027 0.4358 0.0488 -0.0936 -0.0502 0.0253  60  THR   A OG1 
429  C CG2 . THR   A 54  ? 0.6332 0.3957 0.0469 -0.0940 -0.0561 0.0259  60  THR   A CG2 
430  N N   . GLY   A 55  ? 0.5658 0.3080 0.0436 -0.0642 -0.0412 0.0107  61  GLY   A N   
431  C CA  . GLY   A 55  ? 0.5630 0.2977 0.0432 -0.0574 -0.0390 0.0076  61  GLY   A CA  
432  C C   . GLY   A 55  ? 0.5700 0.3039 0.0433 -0.0507 -0.0399 0.0029  61  GLY   A C   
433  O O   . GLY   A 55  ? 0.5693 0.3037 0.0432 -0.0527 -0.0391 0.0014  61  GLY   A O   
434  N N   . VAL   A 56  ? 0.5788 0.3100 0.0437 -0.0437 -0.0418 0.0003  62  VAL   A N   
435  C CA  . VAL   A 56  ? 0.5867 0.3139 0.0447 -0.0381 -0.0447 -0.0042 62  VAL   A CA  
436  C C   . VAL   A 56  ? 0.5693 0.3034 0.0449 -0.0329 -0.0475 -0.0064 62  VAL   A C   
437  O O   . VAL   A 56  ? 0.5736 0.3114 0.0451 -0.0313 -0.0483 -0.0057 62  VAL   A O   
438  C CB  . VAL   A 56  ? 0.6056 0.3196 0.0443 -0.0355 -0.0453 -0.0046 62  VAL   A CB  
439  C CG1 . VAL   A 56  ? 0.6238 0.3321 0.0457 -0.0290 -0.0522 -0.0087 62  VAL   A CG1 
440  C CG2 . VAL   A 56  ? 0.6161 0.3209 0.0436 -0.0416 -0.0413 -0.0032 62  VAL   A CG2 
441  N N   . TYR   A 57  ? 0.5738 0.3088 0.0457 -0.0319 -0.0500 -0.0103 63  TYR   A N   
442  C CA  . TYR   A 57  ? 0.5768 0.3175 0.0469 -0.0287 -0.0542 -0.0140 63  TYR   A CA  
443  C C   . TYR   A 57  ? 0.6167 0.3490 0.0493 -0.0271 -0.0628 -0.0206 63  TYR   A C   
444  O O   . TYR   A 57  ? 0.6251 0.3465 0.0491 -0.0298 -0.0616 -0.0216 63  TYR   A O   
445  C CB  . TYR   A 57  ? 0.5584 0.3078 0.0463 -0.0308 -0.0506 -0.0138 63  TYR   A CB  
446  C CG  . TYR   A 57  ? 0.5655 0.3118 0.0465 -0.0336 -0.0489 -0.0178 63  TYR   A CG  
447  C CD1 . TYR   A 57  ? 0.5775 0.3207 0.0459 -0.0375 -0.0459 -0.0176 63  TYR   A CD1 
448  C CD2 . TYR   A 57  ? 0.5884 0.3336 0.0481 -0.0339 -0.0517 -0.0248 63  TYR   A CD2 
449  C CE1 . TYR   A 57  ? 0.5998 0.3387 0.0463 -0.0412 -0.0432 -0.0234 63  TYR   A CE1 
450  C CE2 . TYR   A 57  ? 0.6122 0.3509 0.0487 -0.0383 -0.0490 -0.0312 63  TYR   A CE2 
451  C CZ  . TYR   A 57  ? 0.6263 0.3614 0.0480 -0.0419 -0.0448 -0.0315 63  TYR   A CZ  
452  O OH  . TYR   A 57  ? 0.6571 0.3842 0.0490 -0.0474 -0.0397 -0.0401 63  TYR   A OH  
453  N N   . TYR   A 58  ? 0.6225 0.3586 0.0515 -0.0237 -0.0699 -0.0242 64  TYR   A N   
454  C CA  . TYR   A 58  ? 0.6674 0.3952 0.0553 -0.0237 -0.0822 -0.0318 64  TYR   A CA  
455  C C   . TYR   A 58  ? 0.6907 0.4176 0.0576 -0.0293 -0.0830 -0.0396 64  TYR   A C   
456  O O   . TYR   A 58  ? 0.6695 0.4070 0.0587 -0.0299 -0.0775 -0.0397 64  TYR   A O   
457  C CB  . TYR   A 58  ? 0.6869 0.4202 0.0597 -0.0188 -0.0953 -0.0355 64  TYR   A CB  
458  C CG  . TYR   A 58  ? 0.7605 0.4841 0.0681 -0.0202 -0.1167 -0.0458 64  TYR   A CG  
459  C CD1 . TYR   A 58  ? 0.8076 0.5132 0.0701 -0.0209 -0.1242 -0.0465 64  TYR   A CD1 
460  C CD2 . TYR   A 58  ? 0.7909 0.5208 0.0751 -0.0227 -0.1317 -0.0564 64  TYR   A CD2 
461  C CE1 . TYR   A 58  ? 0.8589 0.5511 0.0740 -0.0234 -0.1436 -0.0536 64  TYR   A CE1 
462  C CE2 . TYR   A 58  ? 0.8287 0.5473 0.0800 -0.0256 -0.1504 -0.0631 64  TYR   A CE2 
463  C CZ  . TYR   A 58  ? 0.8755 0.5744 0.0811 -0.0264 -0.1586 -0.0625 64  TYR   A CZ  
464  O OH  . TYR   A 58  ? 0.9210 0.6052 0.0892 -0.0303 -0.1799 -0.0681 64  TYR   A OH  
465  N N   . CYS   A 59  ? 0.7335 0.4446 0.0590 -0.0342 -0.0878 -0.0462 65  CYS   A N   
466  C CA  . CYS   A 59  ? 0.7653 0.4688 0.0610 -0.0416 -0.0871 -0.0565 65  CYS   A CA  
467  C C   . CYS   A 59  ? 0.8422 0.5314 0.0683 -0.0454 -0.1079 -0.0692 65  CYS   A C   
468  O O   . CYS   A 59  ? 0.8900 0.5612 0.0699 -0.0476 -0.1156 -0.0714 65  CYS   A O   
469  C CB  . CYS   A 59  ? 0.7752 0.4681 0.0585 -0.0470 -0.0756 -0.0573 65  CYS   A CB  
470  S SG  . CYS   A 59  ? 0.8287 0.5067 0.0620 -0.0582 -0.0700 -0.0746 65  CYS   A SG  
471  N N   . SER   A 60  ? 0.8550 0.5512 0.0737 -0.0469 -0.1189 -0.0775 66  SER   A N   
472  C CA  . SER   A 60  ? 0.9004 0.5847 0.0817 -0.0517 -0.1395 -0.0864 66  SER   A CA  
473  C C   . SER   A 60  ? 0.9485 0.6060 0.0838 -0.0643 -0.1377 -0.0969 66  SER   A C   
474  O O   . SER   A 60  ? 0.9853 0.6243 0.0891 -0.0695 -0.1536 -0.0998 66  SER   A O   
475  C CB  . SER   A 60  ? 0.8856 0.5859 0.0883 -0.0519 -0.1488 -0.0921 66  SER   A CB  
476  O OG  . SER   A 60  ? 0.8846 0.5869 0.1016 -0.0579 -0.1345 -0.0986 66  SER   A OG  
477  N N   . SER   A 61  ? 0.9439 0.5976 0.0802 -0.0695 -0.1177 -0.1016 67  SER   A N   
478  C CA  . SER   A 61  ? 0.9815 0.6078 0.0817 -0.0822 -0.1092 -0.1119 67  SER   A CA  
479  C C   . SER   A 61  ? 1.0276 0.6311 0.0808 -0.0852 -0.1093 -0.1113 67  SER   A C   
480  O O   . SER   A 61  ? 1.0633 0.6384 0.0815 -0.0971 -0.1025 -0.1194 67  SER   A O   
481  C CB  . SER   A 61  ? 0.9571 0.5877 0.0796 -0.0856 -0.0856 -0.1172 67  SER   A CB  
482  O OG  . SER   A 61  ? 0.9401 0.5792 0.0744 -0.0802 -0.0723 -0.1111 67  SER   A OG  
483  N N   . ARG   A 62  ? 1.0218 0.6354 0.0779 -0.0754 -0.1137 -0.1014 68  ARG   A N   
484  C CA  . ARG   A 62  ? 1.0542 0.6474 0.0748 -0.0770 -0.1127 -0.0986 68  ARG   A CA  
485  C C   . ARG   A 62  ? 1.0645 0.6578 0.0761 -0.0683 -0.1326 -0.0894 68  ARG   A C   
486  O O   . ARG   A 62  ? 1.0948 0.6710 0.0743 -0.0685 -0.1321 -0.0866 68  ARG   A O   
487  C CB  . ARG   A 62  ? 1.0323 0.6365 0.0695 -0.0744 -0.0932 -0.0950 68  ARG   A CB  
488  C CG  . ARG   A 62  ? 1.0294 0.6313 0.0728 -0.0824 -0.0723 -0.1044 68  ARG   A CG  
489  C CD  . ARG   A 62  ? 1.0756 0.6428 0.0713 -0.0954 -0.0631 -0.1143 68  ARG   A CD  
490  N NE  . ARG   A 62  ? 1.0661 0.6287 0.0731 -0.1038 -0.0398 -0.1244 68  ARG   A NE  
491  C CZ  . ARG   A 62  ? 1.0639 0.6186 0.0771 -0.1111 -0.0332 -0.1333 68  ARG   A CZ  
492  N NH1 . ARG   A 62  ? 1.0715 0.6232 0.0792 -0.1120 -0.0497 -0.1338 68  ARG   A NH1 
493  N NH2 . ARG   A 62  ? 1.0524 0.6027 0.0802 -0.1179 -0.0094 -0.1421 68  ARG   A NH2 
494  N N   . ARG   A 63  ? 1.0368 0.6494 0.0796 -0.0603 -0.1480 -0.0848 69  ARG   A N   
495  C CA  . ARG   A 63  ? 1.0314 0.6506 0.0820 -0.0496 -0.1648 -0.0755 69  ARG   A CA  
496  C C   . ARG   A 63  ? 1.0229 0.6450 0.0760 -0.0430 -0.1530 -0.0673 69  ARG   A C   
497  O O   . ARG   A 63  ? 1.0472 0.6562 0.0768 -0.0386 -0.1618 -0.0620 69  ARG   A O   
498  C CB  . ARG   A 63  ? 1.0740 0.6689 0.0887 -0.0522 -0.1877 -0.0755 69  ARG   A CB  
499  C CG  . ARG   A 63  ? 1.1044 0.6986 0.1115 -0.0592 -0.2058 -0.0837 69  ARG   A CG  
500  C CD  . ARG   A 63  ? 1.1600 0.7322 0.1341 -0.0603 -0.2337 -0.0805 69  ARG   A CD  
501  N NE  . ARG   A 63  ? 1.2106 0.7740 0.1749 -0.0713 -0.2495 -0.0879 69  ARG   A NE  
502  C CZ  . ARG   A 63  ? 1.2420 0.7692 0.1498 -0.0860 -0.2559 -0.0939 69  ARG   A CZ  
503  N NH1 . ARG   A 63  ? 1.2643 0.7604 0.1214 -0.0911 -0.2458 -0.0941 69  ARG   A NH1 
504  N NH2 . ARG   A 63  ? 1.2338 0.7536 0.1334 -0.0974 -0.2704 -0.1007 69  ARG   A NH2 
505  N N   . LYS   A 64  ? 0.9732 0.6108 0.0699 -0.0429 -0.1310 -0.0641 70  LYS   A N   
506  C CA  . LYS   A 64  ? 0.9369 0.5758 0.0640 -0.0400 -0.1147 -0.0546 70  LYS   A CA  
507  C C   . LYS   A 64  ? 0.8662 0.5306 0.0603 -0.0351 -0.1012 -0.0465 70  LYS   A C   
508  O O   . LYS   A 64  ? 0.8528 0.5314 0.0612 -0.0368 -0.0978 -0.0499 70  LYS   A O   
509  C CB  . LYS   A 64  ? 0.9817 0.6042 0.0643 -0.0501 -0.1035 -0.0621 70  LYS   A CB  
510  C CG  . LYS   A 64  ? 1.1114 0.7080 0.0870 -0.0532 -0.1117 -0.0686 70  LYS   A CG  
511  C CD  . LYS   A 64  ? 1.2067 0.7867 0.1562 -0.0644 -0.0948 -0.0768 70  LYS   A CD  
512  C CE  . LYS   A 64  ? 1.3010 0.8435 0.1942 -0.0717 -0.0991 -0.0814 70  LYS   A CE  
513  N NZ  . LYS   A 64  ? 1.3518 0.8796 0.2304 -0.0749 -0.1151 -0.0856 70  LYS   A NZ  
514  N N   . HIS   A 65  ? 0.8218 0.4880 0.0566 -0.0308 -0.0922 -0.0364 71  HIS   A N   
515  C CA  . HIS   A 65  ? 0.7881 0.4721 0.0557 -0.0290 -0.0828 -0.0307 71  HIS   A CA  
516  C C   . HIS   A 65  ? 0.7746 0.4559 0.0531 -0.0356 -0.0698 -0.0286 71  HIS   A C   
517  O O   . HIS   A 65  ? 0.7986 0.4629 0.0504 -0.0387 -0.0682 -0.0294 71  HIS   A O   
518  C CB  . HIS   A 65  ? 0.7799 0.4647 0.0538 -0.0225 -0.0848 -0.0253 71  HIS   A CB  
519  C CG  . HIS   A 65  ? 0.8095 0.5010 0.0583 -0.0159 -0.1003 -0.0287 71  HIS   A CG  
520  N ND1 . HIS   A 65  ? 0.8239 0.5329 0.0613 -0.0138 -0.1031 -0.0300 71  HIS   A ND1 
521  C CD2 . HIS   A 65  ? 0.8402 0.5231 0.0617 -0.0120 -0.1169 -0.0320 71  HIS   A CD2 
522  C CE1 . HIS   A 65  ? 0.8264 0.5388 0.0651 -0.0083 -0.1161 -0.0327 71  HIS   A CE1 
523  N NE2 . HIS   A 65  ? 0.8436 0.5420 0.0652 -0.0069 -0.1278 -0.0343 71  HIS   A NE2 
524  N N   . TYR   A 66  ? 0.7196 0.4162 0.0507 -0.0382 -0.0603 -0.0256 72  TYR   A N   
525  C CA  . TYR   A 66  ? 0.7048 0.4029 0.0481 -0.0445 -0.0509 -0.0244 72  TYR   A CA  
526  C C   . TYR   A 66  ? 0.6805 0.3926 0.0467 -0.0452 -0.0475 -0.0181 72  TYR   A C   
527  O O   . TYR   A 66  ? 0.6599 0.3848 0.0469 -0.0429 -0.0485 -0.0156 72  TYR   A O   
528  C CB  . TYR   A 66  ? 0.7159 0.4187 0.0496 -0.0483 -0.0478 -0.0307 72  TYR   A CB  
529  C CG  . TYR   A 66  ? 0.7636 0.4482 0.0498 -0.0522 -0.0499 -0.0407 72  TYR   A CG  
530  C CD1 . TYR   A 66  ? 0.8177 0.4835 0.0508 -0.0591 -0.0464 -0.0475 72  TYR   A CD1 
531  C CD2 . TYR   A 66  ? 0.7885 0.4725 0.0540 -0.0514 -0.0561 -0.0478 72  TYR   A CD2 
532  C CE1 . TYR   A 66  ? 0.8649 0.5086 0.0529 -0.0650 -0.0470 -0.0577 72  TYR   A CE1 
533  C CE2 . TYR   A 66  ? 0.8341 0.4981 0.0548 -0.0577 -0.0577 -0.0585 72  TYR   A CE2 
534  C CZ  . TYR   A 66  ? 0.8854 0.5275 0.0555 -0.0648 -0.0540 -0.0648 72  TYR   A CZ  
535  O OH  . TYR   A 66  ? 0.9705 0.5864 0.0599 -0.0735 -0.0570 -0.0813 72  TYR   A OH  
536  N N   . PRO   A 67  ? 0.6807 0.3887 0.0450 -0.0501 -0.0430 -0.0156 73  PRO   A N   
537  C CA  . PRO   A 67  ? 0.6794 0.3993 0.0448 -0.0536 -0.0421 -0.0107 73  PRO   A CA  
538  C C   . PRO   A 67  ? 0.6649 0.4004 0.0455 -0.0565 -0.0408 -0.0106 73  PRO   A C   
539  O O   . PRO   A 67  ? 0.6777 0.4128 0.0444 -0.0596 -0.0376 -0.0157 73  PRO   A O   
540  C CB  . PRO   A 67  ? 0.6909 0.4002 0.0439 -0.0595 -0.0381 -0.0096 73  PRO   A CB  
541  C CG  . PRO   A 67  ? 0.7136 0.4040 0.0441 -0.0578 -0.0378 -0.0140 73  PRO   A CG  
542  C CD  . PRO   A 67  ? 0.6909 0.3816 0.0446 -0.0542 -0.0391 -0.0173 73  PRO   A CD  
543  N N   . VAL   A 68  ? 0.6292 0.3766 0.0457 -0.0558 -0.0420 -0.0050 74  VAL   A N   
544  C CA  . VAL   A 68  ? 0.6075 0.3694 0.0447 -0.0568 -0.0420 -0.0035 74  VAL   A CA  
545  C C   . VAL   A 68  ? 0.5957 0.3659 0.0454 -0.0610 -0.0454 0.0042  74  VAL   A C   
546  O O   . VAL   A 68  ? 0.5745 0.3378 0.0442 -0.0629 -0.0446 0.0076  74  VAL   A O   
547  C CB  . VAL   A 68  ? 0.6030 0.3689 0.0449 -0.0506 -0.0434 -0.0059 74  VAL   A CB  
548  C CG1 . VAL   A 68  ? 0.6003 0.3597 0.0443 -0.0497 -0.0386 -0.0136 74  VAL   A CG1 
549  C CG2 . VAL   A 68  ? 0.6068 0.3690 0.0450 -0.0464 -0.0469 -0.0041 74  VAL   A CG2 
550  N N   . SER   A 69  ? 0.6007 0.3842 0.0459 -0.0633 -0.0486 0.0067  75  SER   A N   
551  C CA  . SER   A 69  ? 0.5990 0.3924 0.0470 -0.0670 -0.0560 0.0155  75  SER   A CA  
552  C C   . SER   A 69  ? 0.5828 0.3818 0.0473 -0.0599 -0.0583 0.0171  75  SER   A C   
553  O O   . SER   A 69  ? 0.5690 0.3728 0.0470 -0.0553 -0.0541 0.0116  75  SER   A O   
554  C CB  . SER   A 69  ? 0.6294 0.4364 0.0482 -0.0720 -0.0611 0.0175  75  SER   A CB  
555  O OG  . SER   A 69  ? 0.7259 0.5285 0.0517 -0.0805 -0.0672 0.0194  75  SER   A OG  
556  N N   . PHE   A 70  ? 0.5781 0.3734 0.0487 -0.0597 -0.0626 0.0235  76  PHE   A N   
557  C CA  . PHE   A 70  ? 0.5728 0.3709 0.0522 -0.0532 -0.0647 0.0255  76  PHE   A CA  
558  C C   . PHE   A 70  ? 0.5961 0.3972 0.0564 -0.0563 -0.0774 0.0393  76  PHE   A C   
559  O O   . PHE   A 70  ? 0.5972 0.3930 0.0558 -0.0648 -0.0805 0.0442  76  PHE   A O   
560  C CB  . PHE   A 70  ? 0.5587 0.3460 0.0509 -0.0489 -0.0585 0.0199  76  PHE   A CB  
561  C CG  . PHE   A 70  ? 0.5568 0.3325 0.0477 -0.0536 -0.0571 0.0216  76  PHE   A CG  
562  C CD1 . PHE   A 70  ? 0.5610 0.3302 0.0504 -0.0555 -0.0525 0.0172  76  PHE   A CD1 
563  C CD2 . PHE   A 70  ? 0.5718 0.3408 0.0492 -0.0569 -0.0612 0.0288  76  PHE   A CD2 
564  C CE1 . PHE   A 70  ? 0.5764 0.3341 0.0478 -0.0597 -0.0515 0.0192  76  PHE   A CE1 
565  C CE2 . PHE   A 70  ? 0.5828 0.3385 0.0486 -0.0626 -0.0585 0.0296  76  PHE   A CE2 
566  C CZ  . PHE   A 70  ? 0.5765 0.3274 0.0467 -0.0636 -0.0527 0.0241  76  PHE   A CZ  
567  N N   . SER   A 71  ? 0.5971 0.4044 0.0579 -0.0502 -0.0833 0.0452  77  SER   A N   
568  C CA  . SER   A 71  ? 0.6133 0.4211 0.0649 -0.0522 -0.0976 0.0616  77  SER   A CA  
569  C C   . SER   A 71  ? 0.6384 0.4285 0.0668 -0.0541 -0.0987 0.0668  77  SER   A C   
570  O O   . SER   A 71  ? 0.6287 0.4117 0.0606 -0.0509 -0.0879 0.0565  77  SER   A O   
571  C CB  . SER   A 71  ? 0.6164 0.4354 0.0704 -0.0431 -0.1061 0.0705  77  SER   A CB  
572  O OG  . SER   A 71  ? 0.6174 0.4358 0.0673 -0.0350 -0.0962 0.0609  77  SER   A OG  
573  N N   . LYS   A 72  ? 0.6751 0.4569 0.0747 -0.0597 -0.1133 0.0845  78  LYS   A N   
574  C CA  . LYS   A 72  ? 0.7115 0.4723 0.0769 -0.0630 -0.1150 0.0928  78  LYS   A CA  
575  C C   . LYS   A 72  ? 0.6997 0.4569 0.0775 -0.0533 -0.1105 0.0923  78  LYS   A C   
576  O O   . LYS   A 72  ? 0.6849 0.4547 0.0846 -0.0444 -0.1132 0.0938  78  LYS   A O   
577  C CB  . LYS   A 72  ? 0.7606 0.5106 0.0889 -0.0723 -0.1342 0.1149  78  LYS   A CB  
578  C CG  . LYS   A 72  ? 0.8381 0.5871 0.1146 -0.0833 -0.1408 0.1199  78  LYS   A CG  
579  C CD  . LYS   A 72  ? 0.9139 0.6555 0.1714 -0.0950 -0.1591 0.1372  78  LYS   A CD  
580  C CE  . LYS   A 72  ? 0.9814 0.7120 0.1932 -0.1088 -0.1553 0.1347  78  LYS   A CE  
581  N NZ  . LYS   A 72  ? 1.0326 0.7570 0.2212 -0.1232 -0.1740 0.1502  78  LYS   A NZ  
582  N N   . PRO   A 73  ? 0.7084 0.4483 0.0732 -0.0551 -0.1020 0.0892  79  PRO   A N   
583  C CA  . PRO   A 73  ? 0.7054 0.4417 0.0770 -0.0468 -0.0970 0.0886  79  PRO   A CA  
584  C C   . PRO   A 73  ? 0.7030 0.4371 0.0916 -0.0425 -0.1078 0.1041  79  PRO   A C   
585  O O   . PRO   A 73  ? 0.7126 0.4350 0.0928 -0.0490 -0.1190 0.1180  79  PRO   A O   
586  C CB  . PRO   A 73  ? 0.7395 0.4568 0.0807 -0.0521 -0.0878 0.0859  79  PRO   A CB  
587  C CG  . PRO   A 73  ? 0.7607 0.4753 0.0716 -0.0602 -0.0863 0.0829  79  PRO   A CG  
588  C CD  . PRO   A 73  ? 0.7324 0.4545 0.0696 -0.0650 -0.0957 0.0870  79  PRO   A CD  
589  N N   A SER   A 74  ? 0.6767 0.4219 0.1037 -0.0324 -0.1030 0.0984  80  SER   A N   
590  N N   B SER   A 74  ? 0.6765 0.4216 0.1034 -0.0324 -0.1030 0.0984  80  SER   A N   
591  C CA  A SER   A 74  ? 0.6630 0.4090 0.1217 -0.0260 -0.1113 0.1109  80  SER   A CA  
592  C CA  B SER   A 74  ? 0.6628 0.4088 0.1215 -0.0260 -0.1113 0.1109  80  SER   A CA  
593  C C   A SER   A 74  ? 0.6455 0.3881 0.1333 -0.0175 -0.0981 0.1028  80  SER   A C   
594  C C   B SER   A 74  ? 0.6452 0.3878 0.1330 -0.0175 -0.0981 0.1028  80  SER   A C   
595  O O   A SER   A 74  ? 0.6510 0.3947 0.1366 -0.0170 -0.0839 0.0862  80  SER   A O   
596  O O   B SER   A 74  ? 0.6505 0.3942 0.1361 -0.0170 -0.0839 0.0862  80  SER   A O   
597  C CB  A SER   A 74  ? 0.6677 0.4361 0.1532 -0.0225 -0.1195 0.1131  80  SER   A CB  
598  C CB  B SER   A 74  ? 0.6673 0.4357 0.1528 -0.0225 -0.1195 0.1131  80  SER   A CB  
599  O OG  A SER   A 74  ? 0.7119 0.4866 0.1714 -0.0311 -0.1286 0.1160  80  SER   A OG  
600  O OG  B SER   A 74  ? 0.7124 0.4870 0.1718 -0.0311 -0.1286 0.1160  80  SER   A OG  
601  N N   . LEU   A 75  ? 0.6271 0.3650 0.1430 -0.0109 -0.1035 0.1148  81  LEU   A N   
602  C CA  . LEU   A 75  ? 0.6149 0.3480 0.1603 -0.0030 -0.0899 0.1077  81  LEU   A CA  
603  C C   . LEU   A 75  ? 0.6010 0.3550 0.1852 0.0041  -0.0833 0.0979  81  LEU   A C   
604  O O   . LEU   A 75  ? 0.5920 0.3568 0.2062 0.0093  -0.0928 0.1083  81  LEU   A O   
605  C CB  . LEU   A 75  ? 0.6146 0.3300 0.1721 0.0012  -0.0977 0.1257  81  LEU   A CB  
606  C CG  . LEU   A 75  ? 0.6183 0.3207 0.1949 0.0068  -0.0816 0.1188  81  LEU   A CG  
607  C CD1 . LEU   A 75  ? 0.6344 0.3225 0.1790 -0.0009 -0.0689 0.1069  81  LEU   A CD1 
608  C CD2 . LEU   A 75  ? 0.6234 0.3085 0.2155 0.0126  -0.0909 0.1385  81  LEU   A CD2 
609  N N   . ILE   A 76  ? 0.5996 0.3587 0.1817 0.0031  -0.0675 0.0779  82  ILE   A N   
610  C CA  . ILE   A 76  ? 0.5940 0.3678 0.2037 0.0068  -0.0581 0.0660  82  ILE   A CA  
611  C C   . ILE   A 76  ? 0.5970 0.3627 0.2284 0.0106  -0.0392 0.0531  82  ILE   A C   
612  O O   . ILE   A 76  ? 0.6030 0.3571 0.2160 0.0072  -0.0314 0.0445  82  ILE   A O   
613  C CB  . ILE   A 76  ? 0.6023 0.3858 0.1843 0.0000  -0.0557 0.0525  82  ILE   A CB  
614  C CG1 . ILE   A 76  ? 0.6123 0.3984 0.1612 -0.0063 -0.0712 0.0625  82  ILE   A CG1 
615  C CG2 . ILE   A 76  ? 0.5971 0.3931 0.2033 0.0018  -0.0465 0.0416  82  ILE   A CG2 
616  C CD1 . ILE   A 76  ? 0.6265 0.4247 0.1873 -0.0063 -0.0835 0.0738  82  ILE   A CD1 
617  N N   . PHE   A 77  ? 0.5906 0.3624 0.2620 0.0167  -0.0308 0.0506  83  PHE   A N   
618  C CA  . PHE   A 77  ? 0.6035 0.3659 0.2954 0.0189  -0.0103 0.0370  83  PHE   A CA  
619  C C   . PHE   A 77  ? 0.6189 0.3816 0.2859 0.0108  0.0020  0.0151  83  PHE   A C   
620  O O   . PHE   A 77  ? 0.6293 0.4030 0.2868 0.0074  -0.0003 0.0102  83  PHE   A O   
621  C CB  . PHE   A 77  ? 0.5931 0.3607 0.3377 0.0277  -0.0032 0.0409  83  PHE   A CB  
622  C CG  . PHE   A 77  ? 0.6103 0.3630 0.3755 0.0297  0.0196  0.0286  83  PHE   A CG  
623  C CD1 . PHE   A 77  ? 0.6368 0.3722 0.4031 0.0325  0.0221  0.0343  83  PHE   A CD1 
624  C CD2 . PHE   A 77  ? 0.6149 0.3672 0.3917 0.0264  0.0401  0.0099  83  PHE   A CD2 
625  C CE1 . PHE   A 77  ? 0.6480 0.3679 0.4300 0.0328  0.0446  0.0218  83  PHE   A CE1 
626  C CE2 . PHE   A 77  ? 0.6283 0.3636 0.4184 0.0259  0.0625  -0.0027 83  PHE   A CE2 
627  C CZ  . PHE   A 77  ? 0.6319 0.3520 0.4261 0.0293  0.0646  0.0034  83  PHE   A CZ  
628  N N   . VAL   A 78  ? 0.6235 0.3728 0.2778 0.0068  0.0139  0.0025  84  VAL   A N   
629  C CA  . VAL   A 78  ? 0.6325 0.3783 0.2596 -0.0019 0.0226  -0.0172 84  VAL   A CA  
630  C C   . VAL   A 78  ? 0.6337 0.3664 0.2785 -0.0036 0.0440  -0.0315 84  VAL   A C   
631  O O   . VAL   A 78  ? 0.6377 0.3597 0.3006 -0.0003 0.0512  -0.0286 84  VAL   A O   
632  C CB  . VAL   A 78  ? 0.6481 0.3896 0.2420 -0.0072 0.0148  -0.0191 84  VAL   A CB  
633  C CG1 . VAL   A 78  ? 0.6587 0.3959 0.2275 -0.0159 0.0208  -0.0382 84  VAL   A CG1 
634  C CG2 . VAL   A 78  ? 0.6517 0.4020 0.2259 -0.0069 -0.0030 -0.0058 84  VAL   A CG2 
635  N N   . GLU   A 79  ? 0.6372 0.3670 0.2726 -0.0102 0.0553  -0.0475 85  GLU   A N   
636  C CA  . GLU   A 79  ? 0.6509 0.3641 0.2962 -0.0149 0.0777  -0.0633 85  GLU   A CA  
637  C C   . GLU   A 79  ? 0.6600 0.3599 0.2876 -0.0210 0.0811  -0.0714 85  GLU   A C   
638  O O   . GLU   A 79  ? 0.6595 0.3634 0.2579 -0.0251 0.0676  -0.0718 85  GLU   A O   
639  C CB  . GLU   A 79  ? 0.7106 0.4182 0.3345 -0.0247 0.0879  -0.0803 85  GLU   A CB  
640  C CG  . GLU   A 79  ? 0.7837 0.4968 0.4375 -0.0211 0.0983  -0.0797 85  GLU   A CG  
641  C CD  . GLU   A 79  ? 0.8578 0.5672 0.5640 -0.0128 0.1144  -0.0758 85  GLU   A CD  
642  O OE1 . GLU   A 79  ? 0.9032 0.5934 0.6137 -0.0173 0.1339  -0.0876 85  GLU   A OE1 
643  O OE2 . GLU   A 79  ? 0.8648 0.5900 0.6080 -0.0021 0.1066  -0.0605 85  GLU   A OE2 
644  N N   . ALA   A 80  ? 0.6727 0.3565 0.3190 -0.0225 0.1008  -0.0796 86  ALA   A N   
645  C CA  . ALA   A 80  ? 0.7017 0.3707 0.3323 -0.0309 0.1079  -0.0908 86  ALA   A CA  
646  C C   . ALA   A 80  ? 0.7357 0.3994 0.3252 -0.0450 0.1064  -0.1084 86  ALA   A C   
647  O O   . ALA   A 80  ? 0.7426 0.4028 0.3210 -0.0499 0.1124  -0.1167 86  ALA   A O   
648  C CB  . ALA   A 80  ? 0.7030 0.3535 0.3618 -0.0306 0.1324  -0.0972 86  ALA   A CB  
649  N N   . SER   A 81  ? 0.7552 0.4181 0.3220 -0.0516 0.0971  -0.1132 87  SER   A N   
650  C CA  . SER   A 81  ? 0.7802 0.4381 0.3089 -0.0649 0.0911  -0.1281 87  SER   A CA  
651  C C   . SER   A 81  ? 0.8110 0.4591 0.3351 -0.0737 0.0947  -0.1378 87  SER   A C   
652  O O   . SER   A 81  ? 0.8152 0.4552 0.3646 -0.0704 0.1086  -0.1356 87  SER   A O   
653  C CB  . SER   A 81  ? 0.7751 0.4503 0.2823 -0.0624 0.0679  -0.1209 87  SER   A CB  
654  O OG  . SER   A 81  ? 0.7681 0.4540 0.2764 -0.0599 0.0544  -0.1144 87  SER   A OG  
655  N N   . GLU   A 82  ? 0.8307 0.4778 0.3247 -0.0854 0.0833  -0.1488 88  GLU   A N   
656  C CA  . GLU   A 82  ? 0.8512 0.4912 0.3444 -0.0948 0.0861  -0.1585 88  GLU   A CA  
657  C C   . GLU   A 82  ? 0.8343 0.4910 0.3417 -0.0887 0.0733  -0.1491 88  GLU   A C   
658  O O   . GLU   A 82  ? 0.8400 0.4922 0.3538 -0.0952 0.0777  -0.1558 88  GLU   A O   
659  C CB  . GLU   A 82  ? 0.9270 0.5560 0.3851 -0.1122 0.0806  -0.1757 88  GLU   A CB  
660  C CG  . GLU   A 82  ? 1.0559 0.6927 0.4839 -0.1141 0.0599  -0.1753 88  GLU   A CG  
661  C CD  . GLU   A 82  ? 1.2361 0.8498 0.6260 -0.1308 0.0634  -0.1911 88  GLU   A CD  
662  O OE1 . GLU   A 82  ? 1.2778 0.8768 0.6596 -0.1319 0.0785  -0.1938 88  GLU   A OE1 
663  O OE2 . GLU   A 82  ? 1.2873 0.8960 0.6555 -0.1440 0.0517  -0.2012 88  GLU   A OE2 
664  N N   . TYR   A 83  ? 0.8069 0.4806 0.3183 -0.0776 0.0595  -0.1345 89  TYR   A N   
665  C CA  . TYR   A 83  ? 0.7877 0.4747 0.3089 -0.0725 0.0490  -0.1255 89  TYR   A CA  
666  C C   . TYR   A 83  ? 0.7715 0.4557 0.3163 -0.0620 0.0574  -0.1107 89  TYR   A C   
667  O O   . TYR   A 83  ? 0.7576 0.4417 0.3119 -0.0617 0.0582  -0.1071 89  TYR   A O   
668  C CB  . TYR   A 83  ? 0.7822 0.4853 0.2887 -0.0685 0.0298  -0.1190 89  TYR   A CB  
669  C CG  . TYR   A 83  ? 0.7964 0.5012 0.2783 -0.0778 0.0178  -0.1310 89  TYR   A CG  
670  C CD1 . TYR   A 83  ? 0.8216 0.5203 0.2817 -0.0800 0.0162  -0.1344 89  TYR   A CD1 
671  C CD2 . TYR   A 83  ? 0.8049 0.5165 0.2856 -0.0847 0.0073  -0.1388 89  TYR   A CD2 
672  C CE1 . TYR   A 83  ? 0.8437 0.5402 0.2760 -0.0888 0.0031  -0.1438 89  TYR   A CE1 
673  C CE2 . TYR   A 83  ? 0.8273 0.5406 0.2857 -0.0924 -0.0080 -0.1475 89  TYR   A CE2 
674  C CZ  . TYR   A 83  ? 0.8536 0.5577 0.2852 -0.0946 -0.0106 -0.1496 89  TYR   A CZ  
675  O OH  . TYR   A 83  ? 0.8867 0.5875 0.2914 -0.1034 -0.0265 -0.1578 89  TYR   A OH  
676  N N   . TYR   A 84  ? 0.7673 0.4484 0.3217 -0.0540 0.0632  -0.1020 90  TYR   A N   
677  C CA  . TYR   A 84  ? 0.7654 0.4427 0.3424 -0.0436 0.0682  -0.0861 90  TYR   A CA  
678  C C   . TYR   A 84  ? 0.7762 0.4431 0.3731 -0.0393 0.0835  -0.0858 90  TYR   A C   
679  O O   . TYR   A 84  ? 0.7873 0.4558 0.3783 -0.0414 0.0860  -0.0925 90  TYR   A O   
680  C CB  . TYR   A 84  ? 0.7524 0.4437 0.3253 -0.0352 0.0521  -0.0695 90  TYR   A CB  
681  C CG  . TYR   A 84  ? 0.7449 0.4459 0.3010 -0.0380 0.0387  -0.0679 90  TYR   A CG  
682  C CD1 . TYR   A 84  ? 0.7467 0.4426 0.3070 -0.0375 0.0392  -0.0607 90  TYR   A CD1 
683  C CD2 . TYR   A 84  ? 0.7464 0.4595 0.2828 -0.0411 0.0267  -0.0732 90  TYR   A CD2 
684  C CE1 . TYR   A 84  ? 0.7512 0.4549 0.2993 -0.0405 0.0300  -0.0601 90  TYR   A CE1 
685  C CE2 . TYR   A 84  ? 0.7472 0.4691 0.2732 -0.0428 0.0160  -0.0718 90  TYR   A CE2 
686  C CZ  . TYR   A 84  ? 0.7510 0.4688 0.2843 -0.0424 0.0184  -0.0653 90  TYR   A CZ  
687  O OH  . TYR   A 84  ? 0.7488 0.4740 0.2751 -0.0451 0.0113  -0.0661 90  TYR   A OH  
688  N N   . PRO   A 85  ? 0.7699 0.4260 0.3919 -0.0320 0.0933  -0.0760 91  PRO   A N   
689  C CA  . PRO   A 85  ? 0.7661 0.4153 0.4152 -0.0250 0.1064  -0.0728 91  PRO   A CA  
690  C C   . PRO   A 85  ? 0.7501 0.4151 0.4101 -0.0146 0.0930  -0.0567 91  PRO   A C   
691  O O   . PRO   A 85  ? 0.7401 0.4190 0.3817 -0.0139 0.0745  -0.0489 91  PRO   A O   
692  C CB  . PRO   A 85  ? 0.7748 0.4064 0.4464 -0.0205 0.1190  -0.0667 91  PRO   A CB  
693  C CG  . PRO   A 85  ? 0.7849 0.4178 0.4422 -0.0212 0.1069  -0.0585 91  PRO   A CG  
694  C CD  . PRO   A 85  ? 0.7671 0.4157 0.3947 -0.0296 0.0927  -0.0667 91  PRO   A CD  
695  N N   . ALA   A 86  ? 0.7360 0.3991 0.4275 -0.0071 0.1029  -0.0525 92  ALA   A N   
696  C CA  . ALA   A 86  ? 0.7217 0.4013 0.4280 0.0018  0.0900  -0.0381 92  ALA   A CA  
697  C C   . ALA   A 86  ? 0.7208 0.4017 0.4346 0.0104  0.0744  -0.0163 92  ALA   A C   
698  O O   . ALA   A 86  ? 0.7208 0.3870 0.4535 0.0152  0.0818  -0.0099 92  ALA   A O   
699  C CB  . ALA   A 86  ? 0.7055 0.3832 0.4502 0.0074  0.1057  -0.0401 92  ALA   A CB  
700  N N   . ARG   A 87  ? 0.7132 0.4075 0.4061 0.0103  0.0539  -0.0060 93  ARG   A N   
701  C CA  . ARG   A 87  ? 0.7104 0.4015 0.3991 0.0149  0.0385  0.0139  93  ARG   A CA  
702  C C   . ARG   A 87  ? 0.6954 0.4030 0.3678 0.0151  0.0175  0.0256  93  ARG   A C   
703  O O   . ARG   A 87  ? 0.6969 0.4183 0.3599 0.0116  0.0162  0.0167  93  ARG   A O   
704  C CB  . ARG   A 87  ? 0.7436 0.4220 0.4051 0.0073  0.0412  0.0081  93  ARG   A CB  
705  C CG  . ARG   A 87  ? 0.7944 0.4837 0.4197 -0.0008 0.0302  0.0026  93  ARG   A CG  
706  C CD  . ARG   A 87  ? 0.8336 0.5207 0.4425 -0.0104 0.0391  -0.0172 93  ARG   A CD  
707  N NE  . ARG   A 87  ? 0.8385 0.5310 0.4208 -0.0159 0.0288  -0.0173 93  ARG   A NE  
708  C CZ  . ARG   A 87  ? 0.8223 0.5290 0.3863 -0.0184 0.0185  -0.0204 93  ARG   A CZ  
709  N NH1 . ARG   A 87  ? 0.7922 0.5086 0.3578 -0.0167 0.0168  -0.0239 93  ARG   A NH1 
710  N NH2 . ARG   A 87  ? 0.8088 0.5185 0.3533 -0.0228 0.0116  -0.0205 93  ARG   A NH2 
711  N N   . TYR   A 88  ? 0.6790 0.3819 0.3425 0.0173  0.0020  0.0447  94  TYR   A N   
712  C CA  . TYR   A 88  ? 0.6686 0.3827 0.3097 0.0147  -0.0168 0.0552  94  TYR   A CA  
713  C C   . TYR   A 88  ? 0.6518 0.3607 0.2526 0.0055  -0.0184 0.0492  94  TYR   A C   
714  O O   . TYR   A 88  ? 0.6631 0.3552 0.2531 0.0029  -0.0148 0.0514  94  TYR   A O   
715  C CB  . TYR   A 88  ? 0.6748 0.3838 0.3237 0.0198  -0.0340 0.0796  94  TYR   A CB  
716  C CG  . TYR   A 88  ? 0.6753 0.3945 0.3693 0.0297  -0.0371 0.0881  94  TYR   A CG  
717  C CD1 . TYR   A 88  ? 0.6726 0.4126 0.3759 0.0303  -0.0482 0.0917  94  TYR   A CD1 
718  C CD2 . TYR   A 88  ? 0.6798 0.3876 0.4098 0.0384  -0.0282 0.0924  94  TYR   A CD2 
719  C CE1 . TYR   A 88  ? 0.6652 0.4169 0.4164 0.0393  -0.0502 0.0986  94  TYR   A CE1 
720  C CE2 . TYR   A 88  ? 0.6719 0.3901 0.4504 0.0484  -0.0299 0.0999  94  TYR   A CE2 
721  C CZ  . TYR   A 88  ? 0.6681 0.4093 0.4588 0.0488  -0.0412 0.1028  94  TYR   A CZ  
722  O OH  . TYR   A 88  ? 0.6704 0.4237 0.5157 0.0587  -0.0418 0.1093  94  TYR   A OH  
723  N N   . GLN   A 89  ? 0.6224 0.3449 0.2030 0.0006  -0.0224 0.0409  95  GLN   A N   
724  C CA  . GLN   A 89  ? 0.5957 0.3159 0.1435 -0.0070 -0.0245 0.0358  95  GLN   A CA  
725  C C   . GLN   A 89  ? 0.5880 0.3083 0.1150 -0.0092 -0.0397 0.0516  95  GLN   A C   
726  O O   . GLN   A 89  ? 0.5707 0.3027 0.1023 -0.0072 -0.0492 0.0586  95  GLN   A O   
727  C CB  . GLN   A 89  ? 0.5726 0.3049 0.1094 -0.0108 -0.0206 0.0180  95  GLN   A CB  
728  C CG  . GLN   A 89  ? 0.5517 0.2843 0.0598 -0.0172 -0.0243 0.0138  95  GLN   A CG  
729  C CD  . GLN   A 89  ? 0.5675 0.3069 0.0692 -0.0206 -0.0199 -0.0043 95  GLN   A CD  
730  O OE1 . GLN   A 89  ? 0.5685 0.3042 0.0812 -0.0218 -0.0107 -0.0158 95  GLN   A OE1 
731  N NE2 . GLN   A 89  ? 0.5903 0.3382 0.0725 -0.0227 -0.0269 -0.0069 95  GLN   A NE2 
732  N N   . SER   A 90  ? 0.5978 0.3034 0.1015 -0.0148 -0.0409 0.0569  96  SER   A N   
733  C CA  . SER   A 90  ? 0.6081 0.3080 0.0849 -0.0199 -0.0534 0.0712  96  SER   A CA  
734  C C   . SER   A 90  ? 0.6089 0.3172 0.0600 -0.0262 -0.0539 0.0628  96  SER   A C   
735  O O   . SER   A 90  ? 0.5960 0.3126 0.0519 -0.0264 -0.0453 0.0461  96  SER   A O   
736  C CB  . SER   A 90  ? 0.6537 0.3278 0.1145 -0.0245 -0.0526 0.0820  96  SER   A CB  
737  O OG  . SER   A 90  ? 0.6960 0.3614 0.1521 -0.0286 -0.0378 0.0687  96  SER   A OG  
738  N N   . HIS   A 91  ? 0.6267 0.3333 0.0636 -0.0314 -0.0639 0.0720  97  HIS   A N   
739  C CA  . HIS   A 91  ? 0.6415 0.3526 0.0597 -0.0377 -0.0638 0.0656  97  HIS   A CA  
740  C C   . HIS   A 91  ? 0.6125 0.3444 0.0544 -0.0338 -0.0607 0.0507  97  HIS   A C   
741  O O   . HIS   A 91  ? 0.5803 0.3156 0.0511 -0.0369 -0.0531 0.0366  97  HIS   A O   
742  C CB  . HIS   A 91  ? 0.6582 0.3542 0.0557 -0.0443 -0.0539 0.0603  97  HIS   A CB  
743  C CG  . HIS   A 91  ? 0.7102 0.3805 0.0744 -0.0505 -0.0556 0.0764  97  HIS   A CG  
744  N ND1 . HIS   A 91  ? 0.7403 0.3943 0.0695 -0.0609 -0.0566 0.0833  97  HIS   A ND1 
745  C CD2 . HIS   A 91  ? 0.7352 0.3912 0.1098 -0.0485 -0.0551 0.0840  97  HIS   A CD2 
746  C CE1 . HIS   A 91  ? 0.7727 0.4018 0.0892 -0.0659 -0.0570 0.0947  97  HIS   A CE1 
747  N NE2 . HIS   A 91  ? 0.7636 0.3934 0.1072 -0.0580 -0.0568 0.0961  97  HIS   A NE2 
748  N N   . LEU   A 92  ? 0.5958 0.3395 0.0558 -0.0277 -0.0638 0.0518  98  LEU   A N   
749  C CA  . LEU   A 92  ? 0.5733 0.3317 0.0518 -0.0253 -0.0594 0.0385  98  LEU   A CA  
750  C C   . LEU   A 92  ? 0.5641 0.3323 0.0542 -0.0279 -0.0652 0.0411  98  LEU   A C   
751  O O   . LEU   A 92  ? 0.5742 0.3437 0.0595 -0.0286 -0.0753 0.0545  98  LEU   A O   
752  C CB  . LEU   A 92  ? 0.5551 0.3178 0.0498 -0.0188 -0.0540 0.0342  98  LEU   A CB  
753  C CG  . LEU   A 92  ? 0.5210 0.2913 0.0451 -0.0182 -0.0443 0.0170  98  LEU   A CG  
754  C CD1 . LEU   A 92  ? 0.5063 0.2732 0.0433 -0.0218 -0.0390 0.0065  98  LEU   A CD1 
755  C CD2 . LEU   A 92  ? 0.5244 0.2934 0.0488 -0.0139 -0.0372 0.0131  98  LEU   A CD2 
756  N N   . MET   A 93  ? 0.5413 0.3153 0.0509 -0.0298 -0.0592 0.0294  99  MET   A N   
757  C CA  . MET   A 93  ? 0.5293 0.3109 0.0503 -0.0333 -0.0614 0.0297  99  MET   A CA  
758  C C   . MET   A 93  ? 0.5213 0.3108 0.0477 -0.0303 -0.0558 0.0202  99  MET   A C   
759  O O   . MET   A 93  ? 0.5104 0.2958 0.0454 -0.0292 -0.0489 0.0109  99  MET   A O   
760  C CB  . MET   A 93  ? 0.5383 0.3127 0.0496 -0.0394 -0.0603 0.0283  99  MET   A CB  
761  C CG  . MET   A 93  ? 0.5792 0.3407 0.0545 -0.0445 -0.0661 0.0388  99  MET   A CG  
762  S SD  . MET   A 93  ? 0.6317 0.3829 0.0517 -0.0513 -0.0658 0.0396  99  MET   A SD  
763  C CE  . MET   A 93  ? 0.5308 0.2821 0.0461 -0.0459 -0.0489 0.0209  99  MET   A CE  
764  N N   . LEU   A 94  ? 0.5256 0.3254 0.0487 -0.0297 -0.0589 0.0229  100 LEU   A N   
765  C CA  . LEU   A 94  ? 0.5426 0.3465 0.0511 -0.0289 -0.0532 0.0132  100 LEU   A CA  
766  C C   . LEU   A 94  ? 0.5368 0.3440 0.0486 -0.0343 -0.0524 0.0111  100 LEU   A C   
767  O O   . LEU   A 94  ? 0.5038 0.3167 0.0474 -0.0381 -0.0557 0.0178  100 LEU   A O   
768  C CB  . LEU   A 94  ? 0.5568 0.3684 0.0544 -0.0244 -0.0529 0.0145  100 LEU   A CB  
769  C CG  . LEU   A 94  ? 0.5866 0.3929 0.0855 -0.0188 -0.0516 0.0175  100 LEU   A CG  
770  C CD1 . LEU   A 94  ? 0.5893 0.4038 0.1323 -0.0135 -0.0507 0.0245  100 LEU   A CD1 
771  C CD2 . LEU   A 94  ? 0.5808 0.3772 0.0716 -0.0194 -0.0396 0.0013  100 LEU   A CD2 
772  N N   . ALA   A 95  ? 0.5470 0.3488 0.0483 -0.0356 -0.0451 0.0004  101 ALA   A N   
773  C CA  . ALA   A 95  ? 0.5660 0.3666 0.0479 -0.0407 -0.0432 -0.0038 101 ALA   A CA  
774  C C   . ALA   A 95  ? 0.5744 0.3713 0.0461 -0.0420 -0.0334 -0.0155 101 ALA   A C   
775  O O   . ALA   A 95  ? 0.5676 0.3589 0.0457 -0.0398 -0.0274 -0.0218 101 ALA   A O   
776  C CB  . ALA   A 95  ? 0.5694 0.3591 0.0498 -0.0424 -0.0433 -0.0048 101 ALA   A CB  
777  N N   . VAL   A 96  ? 0.5967 0.3949 0.0446 -0.0472 -0.0305 -0.0198 102 VAL   A N   
778  C CA  . VAL   A 96  ? 0.6186 0.4084 0.0460 -0.0513 -0.0184 -0.0337 102 VAL   A CA  
779  C C   . VAL   A 96  ? 0.6489 0.4198 0.0475 -0.0541 -0.0182 -0.0395 102 VAL   A C   
780  O O   . VAL   A 96  ? 0.6553 0.4221 0.0457 -0.0562 -0.0229 -0.0350 102 VAL   A O   
781  C CB  . VAL   A 96  ? 0.6225 0.4203 0.0462 -0.0569 -0.0134 -0.0363 102 VAL   A CB  
782  C CG1 . VAL   A 96  ? 0.6465 0.4297 0.0483 -0.0633 0.0032  -0.0530 102 VAL   A CG1 
783  C CG2 . VAL   A 96  ? 0.6230 0.4416 0.0522 -0.0535 -0.0181 -0.0311 102 VAL   A CG2 
784  N N   . GLY   A 97  ? 0.6611 0.4199 0.0505 -0.0541 -0.0134 -0.0481 103 GLY   A N   
785  C CA  . GLY   A 97  ? 0.6936 0.4342 0.0520 -0.0567 -0.0163 -0.0531 103 GLY   A CA  
786  C C   . GLY   A 97  ? 0.7323 0.4596 0.0569 -0.0585 -0.0135 -0.0665 103 GLY   A C   
787  O O   . GLY   A 97  ? 0.7333 0.4664 0.0600 -0.0561 -0.0096 -0.0714 103 GLY   A O   
788  N N   . HIS   A 98  ? 0.7521 0.4599 0.0557 -0.0632 -0.0156 -0.0707 104 HIS   A N   
789  C CA  . HIS   A 98  ? 0.7845 0.4771 0.0586 -0.0672 -0.0149 -0.0832 104 HIS   A CA  
790  C C   . HIS   A 98  ? 0.7772 0.4794 0.0592 -0.0611 -0.0266 -0.0798 104 HIS   A C   
791  O O   . HIS   A 98  ? 0.7631 0.4722 0.0565 -0.0558 -0.0382 -0.0698 104 HIS   A O   
792  C CB  . HIS   A 98  ? 0.8479 0.5130 0.0621 -0.0757 -0.0170 -0.0940 104 HIS   A CB  
793  C CG  . HIS   A 98  ? 0.8986 0.5438 0.0683 -0.0830 -0.0169 -0.1110 104 HIS   A CG  
794  N ND1 . HIS   A 98  ? 0.9206 0.5549 0.0861 -0.0903 0.0012  -0.1251 104 HIS   A ND1 
795  C CD2 . HIS   A 98  ? 0.9238 0.5600 0.0701 -0.0841 -0.0324 -0.1131 104 HIS   A CD2 
796  C CE1 . HIS   A 98  ? 0.9518 0.5689 0.0972 -0.0971 -0.0029 -0.1332 104 HIS   A CE1 
797  N NE2 . HIS   A 98  ? 0.9579 0.5766 0.0852 -0.0936 -0.0249 -0.1277 104 HIS   A NE2 
798  N N   . SER   A 99  ? 0.7917 0.4916 0.0623 -0.0629 -0.0216 -0.0912 105 SER   A N   
799  C CA  . SER   A 99  ? 0.7959 0.5029 0.0683 -0.0593 -0.0303 -0.0921 105 SER   A CA  
800  C C   . SER   A 99  ? 0.8078 0.4990 0.0766 -0.0672 -0.0225 -0.1053 105 SER   A C   
801  O O   . SER   A 99  ? 0.8193 0.5012 0.0941 -0.0721 -0.0058 -0.1126 105 SER   A O   
802  C CB  . SER   A 99  ? 0.7917 0.5180 0.1049 -0.0516 -0.0272 -0.0814 105 SER   A CB  
803  O OG  . SER   A 99  ? 0.8211 0.5531 0.1503 -0.0487 -0.0327 -0.0796 105 SER   A OG  
804  N N   . GLU   A 100 ? 0.8041 0.4919 0.0716 -0.0693 -0.0333 -0.1068 106 GLU   A N   
805  C CA  . GLU   A 100 ? 0.8166 0.4898 0.0767 -0.0783 -0.0290 -0.1193 106 GLU   A CA  
806  C C   . GLU   A 100 ? 0.8014 0.4883 0.0817 -0.0744 -0.0371 -0.1183 106 GLU   A C   
807  O O   . GLU   A 100 ? 0.7989 0.5019 0.0894 -0.0665 -0.0491 -0.1087 106 GLU   A O   
808  C CB  . GLU   A 100 ? 0.8688 0.5184 0.0813 -0.0890 -0.0381 -0.1285 106 GLU   A CB  
809  C CG  . GLU   A 100 ? 0.9119 0.5381 0.0911 -0.0981 -0.0229 -0.1387 106 GLU   A CG  
810  C CD  . GLU   A 100 ? 0.9735 0.5723 0.0971 -0.1088 -0.0333 -0.1457 106 GLU   A CD  
811  O OE1 . GLU   A 100 ? 0.9859 0.5736 0.0920 -0.1162 -0.0450 -0.1514 106 GLU   A OE1 
812  O OE2 . GLU   A 100 ? 0.9843 0.5723 0.0855 -0.1102 -0.0305 -0.1438 106 GLU   A OE2 
813  N N   . PRO   A 101 ? 0.7917 0.4727 0.0856 -0.0799 -0.0282 -0.1263 107 PRO   A N   
814  C CA  . PRO   A 101 ? 0.7739 0.4686 0.0946 -0.0764 -0.0338 -0.1238 107 PRO   A CA  
815  C C   . PRO   A 101 ? 0.7842 0.4891 0.0995 -0.0745 -0.0550 -0.1211 107 PRO   A C   
816  O O   . PRO   A 101 ? 0.7799 0.5017 0.1215 -0.0671 -0.0584 -0.1134 107 PRO   A O   
817  C CB  . PRO   A 101 ? 0.7780 0.4577 0.1000 -0.0867 -0.0222 -0.1366 107 PRO   A CB  
818  C CG  . PRO   A 101 ? 0.7976 0.4616 0.1127 -0.0907 -0.0030 -0.1417 107 PRO   A CG  
819  C CD  . PRO   A 101 ? 0.7987 0.4588 0.0887 -0.0905 -0.0100 -0.1374 107 PRO   A CD  
820  N N   . GLY   A 102 ? 0.7985 0.4927 0.0871 -0.0807 -0.0680 -0.1249 108 GLY   A N   
821  C CA  . GLY   A 102 ? 0.8020 0.5062 0.0898 -0.0779 -0.0892 -0.1220 108 GLY   A CA  
822  C C   . GLY   A 102 ? 0.7939 0.5107 0.0849 -0.0668 -0.0962 -0.1102 108 GLY   A C   
823  O O   . GLY   A 102 ? 0.7988 0.5240 0.0879 -0.0632 -0.1131 -0.1086 108 GLY   A O   
824  N N   . ASP   A 103 ? 0.7800 0.4980 0.0775 -0.0617 -0.0833 -0.1021 109 ASP   A N   
825  C CA  . ASP   A 103 ? 0.7554 0.4833 0.0715 -0.0525 -0.0842 -0.0873 109 ASP   A CA  
826  C C   . ASP   A 103 ? 0.7122 0.4578 0.0687 -0.0454 -0.0800 -0.0781 109 ASP   A C   
827  O O   . ASP   A 103 ? 0.7059 0.4583 0.0686 -0.0397 -0.0846 -0.0702 109 ASP   A O   
828  C CB  . ASP   A 103 ? 0.7600 0.4812 0.0682 -0.0524 -0.0733 -0.0829 109 ASP   A CB  
829  C CG  . ASP   A 103 ? 0.8317 0.5332 0.0737 -0.0589 -0.0808 -0.0938 109 ASP   A CG  
830  O OD1 . ASP   A 103 ? 0.8420 0.5388 0.0736 -0.0586 -0.0953 -0.0924 109 ASP   A OD1 
831  O OD2 . ASP   A 103 ? 0.8709 0.5605 0.0893 -0.0642 -0.0696 -0.1006 109 ASP   A OD2 
832  N N   . CYS   A 104 ? 0.6734 0.4236 0.0665 -0.0463 -0.0690 -0.0770 110 CYS   A N   
833  C CA  . CYS   A 104 ? 0.6420 0.4034 0.0645 -0.0419 -0.0644 -0.0707 110 CYS   A CA  
834  C C   . CYS   A 104 ? 0.6371 0.4070 0.0658 -0.0393 -0.0745 -0.0699 110 CYS   A C   
835  O O   . CYS   A 104 ? 0.6531 0.4240 0.0723 -0.0428 -0.0850 -0.0798 110 CYS   A O   
836  C CB  . CYS   A 104 ? 0.6377 0.3972 0.0662 -0.0461 -0.0572 -0.0791 110 CYS   A CB  
837  S SG  . CYS   A 104 ? 0.6514 0.4019 0.0649 -0.0469 -0.0431 -0.0828 110 CYS   A SG  
838  N N   . GLY   A 105 ? 0.6252 0.4001 0.0620 -0.0343 -0.0727 -0.0607 111 GLY   A N   
839  C CA  . GLY   A 105 ? 0.6227 0.4046 0.0648 -0.0315 -0.0797 -0.0608 111 GLY   A CA  
840  C C   . GLY   A 105 ? 0.6428 0.4223 0.0641 -0.0275 -0.0849 -0.0555 111 GLY   A C   
841  O O   . GLY   A 105 ? 0.6739 0.4574 0.0667 -0.0253 -0.0899 -0.0576 111 GLY   A O   
842  N N   . GLY   A 106 ? 0.6154 0.3866 0.0597 -0.0271 -0.0799 -0.0475 112 GLY   A N   
843  C CA  . GLY   A 106 ? 0.6080 0.3739 0.0573 -0.0239 -0.0788 -0.0396 112 GLY   A CA  
844  C C   . GLY   A 106 ? 0.5954 0.3631 0.0534 -0.0230 -0.0700 -0.0318 112 GLY   A C   
845  O O   . GLY   A 106 ? 0.5925 0.3611 0.0514 -0.0253 -0.0638 -0.0292 112 GLY   A O   
846  N N   . ILE   A 107 ? 0.5778 0.3449 0.0523 -0.0200 -0.0686 -0.0271 113 ILE   A N   
847  C CA  . ILE   A 107 ? 0.5584 0.3235 0.0518 -0.0211 -0.0589 -0.0197 113 ILE   A CA  
848  C C   . ILE   A 107 ? 0.5339 0.2925 0.0478 -0.0235 -0.0524 -0.0130 113 ILE   A C   
849  O O   . ILE   A 107 ? 0.5357 0.2892 0.0471 -0.0227 -0.0544 -0.0133 113 ILE   A O   
850  C CB  . ILE   A 107 ? 0.5655 0.3308 0.0523 -0.0180 -0.0602 -0.0208 113 ILE   A CB  
851  C CG1 . ILE   A 107 ? 0.5620 0.3361 0.0563 -0.0174 -0.0617 -0.0265 113 ILE   A CG1 
852  C CG2 . ILE   A 107 ? 0.5825 0.3400 0.0503 -0.0212 -0.0528 -0.0159 113 ILE   A CG2 
853  C CD1 . ILE   A 107 ? 0.5896 0.3668 0.0595 -0.0137 -0.0673 -0.0323 113 ILE   A CD1 
854  N N   . LEU   A 108 ? 0.4993 0.2571 0.0447 -0.0274 -0.0445 -0.0073 114 LEU   A N   
855  C CA  . LEU   A 108 ? 0.5031 0.2568 0.0440 -0.0314 -0.0425 -0.0035 114 LEU   A CA  
856  C C   . LEU   A 108 ? 0.5142 0.2603 0.0446 -0.0346 -0.0393 -0.0008 114 LEU   A C   
857  O O   . LEU   A 108 ? 0.5080 0.2523 0.0427 -0.0361 -0.0361 -0.0001 114 LEU   A O   
858  C CB  . LEU   A 108 ? 0.4941 0.2515 0.0437 -0.0345 -0.0413 -0.0008 114 LEU   A CB  
859  C CG  . LEU   A 108 ? 0.5173 0.2728 0.0438 -0.0399 -0.0425 0.0036  114 LEU   A CG  
860  C CD1 . LEU   A 108 ? 0.5117 0.2665 0.0437 -0.0405 -0.0419 0.0022  114 LEU   A CD1 
861  C CD2 . LEU   A 108 ? 0.5393 0.2995 0.0446 -0.0419 -0.0462 0.0076  114 LEU   A CD2 
862  N N   . ARG   A 109 ? 0.5236 0.2630 0.0431 -0.0360 -0.0387 0.0002  115 ARG   A N   
863  C CA  . ARG   A 109 ? 0.5477 0.2773 0.0426 -0.0396 -0.0352 0.0020  115 ARG   A CA  
864  C C   . ARG   A 109 ? 0.5625 0.2849 0.0424 -0.0466 -0.0337 0.0050  115 ARG   A C   
865  O O   . ARG   A 109 ? 0.5531 0.2777 0.0426 -0.0464 -0.0354 0.0045  115 ARG   A O   
866  C CB  . ARG   A 109 ? 0.6047 0.3316 0.0437 -0.0332 -0.0389 -0.0017 115 ARG   A CB  
867  C CG  . ARG   A 109 ? 0.7791 0.5021 0.0519 -0.0298 -0.0543 -0.0058 115 ARG   A CG  
868  C CD  . ARG   A 109 ? 0.9044 0.6221 0.1244 -0.0234 -0.0582 -0.0095 115 ARG   A CD  
869  N NE  . ARG   A 109 ? 0.9877 0.7132 0.2262 -0.0157 -0.0706 -0.0160 115 ARG   A NE  
870  C CZ  . ARG   A 109 ? 1.0293 0.7652 0.3011 -0.0128 -0.0730 -0.0202 115 ARG   A CZ  
871  N NH1 . ARG   A 109 ? 1.0351 0.7731 0.3248 -0.0164 -0.0619 -0.0190 115 ARG   A NH1 
872  N NH2 . ARG   A 109 ? 0.9915 0.7337 0.2764 -0.0075 -0.0865 -0.0260 115 ARG   A NH2 
873  N N   . CYS   A 110 ? 0.5849 0.2967 0.0421 -0.0545 -0.0295 0.0082  116 CYS   A N   
874  C CA  . CYS   A 110 ? 0.6232 0.3264 0.0423 -0.0635 -0.0291 0.0118  116 CYS   A CA  
875  C C   . CYS   A 110 ? 0.6691 0.3563 0.0420 -0.0652 -0.0225 0.0115  116 CYS   A C   
876  O O   . CYS   A 110 ? 0.6684 0.3553 0.0417 -0.0571 -0.0203 0.0082  116 CYS   A O   
877  C CB  . CYS   A 110 ? 0.6436 0.3440 0.0430 -0.0734 -0.0308 0.0175  116 CYS   A CB  
878  S SG  . CYS   A 110 ? 0.6848 0.3715 0.0429 -0.0775 -0.0249 0.0202  116 CYS   A SG  
879  N N   . GLN   A 111 ? 0.7111 0.3846 0.0422 -0.0762 -0.0185 0.0152  117 GLN   A N   
880  C CA  . GLN   A 111 ? 0.7621 0.4167 0.0437 -0.0794 -0.0081 0.0152  117 GLN   A CA  
881  C C   . GLN   A 111 ? 0.7748 0.4189 0.0445 -0.0828 0.0014  0.0154  117 GLN   A C   
882  O O   . GLN   A 111 ? 0.7952 0.4260 0.0449 -0.0822 0.0130  0.0132  117 GLN   A O   
883  C CB  . GLN   A 111 ? 0.8392 0.4793 0.0437 -0.0931 -0.0046 0.0207  117 GLN   A CB  
884  C CG  . GLN   A 111 ? 0.9699 0.6043 0.0453 -0.1069 -0.0062 0.0340  117 GLN   A CG  
885  C CD  . GLN   A 111 ? 1.1236 0.7443 0.1218 -0.1223 -0.0039 0.0416  117 GLN   A CD  
886  O OE1 . GLN   A 111 ? 1.1680 0.7965 0.1588 -0.1298 -0.0160 0.0483  117 GLN   A OE1 
887  N NE2 . GLN   A 111 ? 1.1591 0.7591 0.1333 -0.1275 0.0115  0.0388  117 GLN   A NE2 
888  N N   . HIS   A 112 ? 0.7713 0.4190 0.0444 -0.0870 -0.0018 0.0184  118 HIS   A N   
889  C CA  . HIS   A 112 ? 0.7895 0.4239 0.0428 -0.0926 0.0087  0.0190  118 HIS   A CA  
890  C C   . HIS   A 112 ? 0.7714 0.4175 0.0444 -0.0811 0.0107  0.0137  118 HIS   A C   
891  O O   . HIS   A 112 ? 0.7817 0.4160 0.0429 -0.0840 0.0243  0.0112  118 HIS   A O   
892  C CB  . HIS   A 112 ? 0.8211 0.4489 0.0438 -0.1041 0.0044  0.0272  118 HIS   A CB  
893  C CG  . HIS   A 112 ? 0.9115 0.5235 0.0476 -0.1190 0.0047  0.0374  118 HIS   A CG  
894  N ND1 . HIS   A 112 ? 0.9522 0.5770 0.0507 -0.1202 -0.0099 0.0453  118 HIS   A ND1 
895  C CD2 . HIS   A 112 ? 0.9595 0.5440 0.0468 -0.1338 0.0184  0.0403  118 HIS   A CD2 
896  C CE1 . HIS   A 112 ? 0.9736 0.5804 0.0479 -0.1357 -0.0071 0.0495  118 HIS   A CE1 
897  N NE2 . HIS   A 112 ? 0.9948 0.5756 0.0514 -0.1448 0.0099  0.0473  118 HIS   A NE2 
898  N N   . GLY   A 113 ? 0.7442 0.4118 0.0467 -0.0693 -0.0014 0.0111  119 GLY   A N   
899  C CA  . GLY   A 113 ? 0.6998 0.3809 0.0443 -0.0588 -0.0030 0.0049  119 GLY   A CA  
900  C C   . GLY   A 113 ? 0.6386 0.3378 0.0422 -0.0528 -0.0143 0.0039  119 GLY   A C   
901  O O   . GLY   A 113 ? 0.6119 0.3176 0.0414 -0.0519 -0.0212 0.0055  119 GLY   A O   
902  N N   . VAL   A 114 ? 0.6139 0.3198 0.0409 -0.0499 -0.0132 0.0009  120 VAL   A N   
903  C CA  . VAL   A 114 ? 0.5861 0.3067 0.0418 -0.0450 -0.0210 -0.0005 120 VAL   A CA  
904  C C   . VAL   A 114 ? 0.5751 0.2916 0.0426 -0.0516 -0.0211 0.0042  120 VAL   A C   
905  O O   . VAL   A 114 ? 0.5768 0.2819 0.0407 -0.0582 -0.0145 0.0056  120 VAL   A O   
906  C CB  . VAL   A 114 ? 0.5948 0.3243 0.0421 -0.0397 -0.0209 -0.0074 120 VAL   A CB  
907  C CG1 . VAL   A 114 ? 0.6304 0.3714 0.0465 -0.0373 -0.0296 -0.0117 120 VAL   A CG1 
908  C CG2 . VAL   A 114 ? 0.5962 0.3327 0.0425 -0.0312 -0.0260 -0.0122 120 VAL   A CG2 
909  N N   . VAL   A 115 ? 0.5510 0.2750 0.0421 -0.0502 -0.0274 0.0062  121 VAL   A N   
910  C CA  . VAL   A 115 ? 0.5374 0.2610 0.0420 -0.0542 -0.0297 0.0102  121 VAL   A CA  
911  C C   . VAL   A 115 ? 0.5351 0.2667 0.0432 -0.0491 -0.0316 0.0083  121 VAL   A C   
912  O O   . VAL   A 115 ? 0.5422 0.2673 0.0423 -0.0526 -0.0309 0.0115  121 VAL   A O   
913  C CB  . VAL   A 115 ? 0.5332 0.2633 0.0428 -0.0543 -0.0349 0.0121  121 VAL   A CB  
914  C CG1 . VAL   A 115 ? 0.5439 0.2771 0.0440 -0.0564 -0.0403 0.0172  121 VAL   A CG1 
915  C CG2 . VAL   A 115 ? 0.5565 0.2779 0.0428 -0.0605 -0.0339 0.0143  121 VAL   A CG2 
916  N N   . GLY   A 116 ? 0.5078 0.2511 0.0423 -0.0418 -0.0331 0.0031  122 GLY   A N   
917  C CA  . GLY   A 116 ? 0.5000 0.2495 0.0424 -0.0385 -0.0338 0.0001  122 GLY   A CA  
918  C C   . GLY   A 116 ? 0.5109 0.2706 0.0449 -0.0329 -0.0389 -0.0065 122 GLY   A C   
919  O O   . GLY   A 116 ? 0.5195 0.2808 0.0444 -0.0305 -0.0418 -0.0091 122 GLY   A O   
920  N N   . ILE   A 117 ? 0.5003 0.2644 0.0440 -0.0313 -0.0395 -0.0093 123 ILE   A N   
921  C CA  . ILE   A 117 ? 0.5072 0.2776 0.0458 -0.0284 -0.0443 -0.0164 123 ILE   A CA  
922  C C   . ILE   A 117 ? 0.5397 0.3107 0.0476 -0.0288 -0.0471 -0.0203 123 ILE   A C   
923  O O   . ILE   A 117 ? 0.5440 0.3130 0.0458 -0.0295 -0.0445 -0.0169 123 ILE   A O   
924  C CB  . ILE   A 117 ? 0.5050 0.2799 0.0472 -0.0284 -0.0451 -0.0229 123 ILE   A CB  
925  C CG1 . ILE   A 117 ? 0.5220 0.2939 0.0467 -0.0315 -0.0409 -0.0248 123 ILE   A CG1 
926  C CG2 . ILE   A 117 ? 0.5155 0.2929 0.0483 -0.0269 -0.0483 -0.0256 123 ILE   A CG2 
927  C CD1 . ILE   A 117 ? 0.5576 0.3347 0.0524 -0.0332 -0.0449 -0.0394 123 ILE   A CD1 
928  N N   . VAL   A 118 ? 0.5446 0.3157 0.0484 -0.0285 -0.0502 -0.0260 124 VAL   A N   
929  C CA  . VAL   A 118 ? 0.5516 0.3207 0.0495 -0.0299 -0.0476 -0.0296 124 VAL   A CA  
930  C C   . VAL   A 118 ? 0.5674 0.3362 0.0498 -0.0312 -0.0455 -0.0365 124 VAL   A C   
931  O O   . VAL   A 118 ? 0.5658 0.3361 0.0515 -0.0324 -0.0471 -0.0414 124 VAL   A O   
932  C CB  . VAL   A 118 ? 0.5644 0.3282 0.0505 -0.0321 -0.0502 -0.0358 124 VAL   A CB  
933  C CG1 . VAL   A 118 ? 0.5727 0.3316 0.0511 -0.0354 -0.0442 -0.0418 124 VAL   A CG1 
934  C CG2 . VAL   A 118 ? 0.5595 0.3204 0.0494 -0.0313 -0.0510 -0.0304 124 VAL   A CG2 
935  N N   . SER   A 119 ? 0.5814 0.3484 0.0489 -0.0309 -0.0413 -0.0367 125 SER   A N   
936  C CA  . SER   A 119 ? 0.6047 0.3681 0.0500 -0.0316 -0.0373 -0.0442 125 SER   A CA  
937  C C   . SER   A 119 ? 0.6170 0.3756 0.0554 -0.0322 -0.0298 -0.0511 125 SER   A C   
938  O O   . SER   A 119 ? 0.6208 0.3733 0.0665 -0.0354 -0.0233 -0.0610 125 SER   A O   
939  C CB  . SER   A 119 ? 0.6303 0.3928 0.0714 -0.0293 -0.0367 -0.0339 125 SER   A CB  
940  O OG  . SER   A 119 ? 0.6499 0.4065 0.1112 -0.0295 -0.0283 -0.0362 125 SER   A OG  
941  N N   . THR   A 120 ? 0.6233 0.3843 0.0625 -0.0299 -0.0286 -0.0450 126 THR   A N   
942  C CA  . THR   A 120 ? 0.6147 0.3716 0.0675 -0.0303 -0.0177 -0.0502 126 THR   A CA  
943  C C   . THR   A 120 ? 0.6417 0.3968 0.0733 -0.0339 -0.0173 -0.0570 126 THR   A C   
944  O O   . THR   A 120 ? 0.6441 0.4016 0.0514 -0.0349 -0.0267 -0.0554 126 THR   A O   
945  C CB  . THR   A 120 ? 0.5975 0.3581 0.0805 -0.0243 -0.0141 -0.0376 126 THR   A CB  
946  O OG1 . THR   A 120 ? 0.6015 0.3712 0.0809 -0.0218 -0.0233 -0.0248 126 THR   A OG1 
947  C CG2 . THR   A 120 ? 0.5860 0.3422 0.0843 -0.0220 -0.0127 -0.0321 126 THR   A CG2 
948  N N   . GLY   A 121 ? 0.6615 0.4096 0.1016 -0.0365 -0.0045 -0.0654 127 GLY   A N   
949  C CA  . GLY   A 121 ? 0.6939 0.4357 0.1128 -0.0418 -0.0004 -0.0736 127 GLY   A CA  
950  C C   . GLY   A 121 ? 0.7193 0.4524 0.1546 -0.0449 0.0181  -0.0826 127 GLY   A C   
951  O O   . GLY   A 121 ? 0.7131 0.4493 0.1841 -0.0405 0.0271  -0.0793 127 GLY   A O   
952  N N   . GLY   A 122 ? 0.7556 0.4761 0.1651 -0.0528 0.0249  -0.0940 128 GLY   A N   
953  C CA  . GLY   A 122 ? 0.7652 0.4736 0.1861 -0.0581 0.0461  -0.1052 128 GLY   A CA  
954  C C   . GLY   A 122 ? 0.7575 0.4781 0.2019 -0.0546 0.0517  -0.0997 128 GLY   A C   
955  O O   . GLY   A 122 ? 0.7522 0.4925 0.2137 -0.0467 0.0390  -0.0848 128 GLY   A O   
956  N N   . ASN   A 123 ? 0.7575 0.4655 0.2022 -0.0618 0.0709  -0.1120 129 ASN   A N   
957  C CA  . ASN   A 123 ? 0.7487 0.4689 0.2213 -0.0598 0.0787  -0.1092 129 ASN   A CA  
958  C C   . ASN   A 123 ? 0.7346 0.4645 0.1826 -0.0602 0.0644  -0.1023 129 ASN   A C   
959  O O   . ASN   A 123 ? 0.7241 0.4708 0.2001 -0.0571 0.0647  -0.0958 129 ASN   A O   
960  C CB  . ASN   A 123 ? 0.7542 0.4957 0.2875 -0.0482 0.0783  -0.0963 129 ASN   A CB  
961  C CG  . ASN   A 123 ? 0.8235 0.5556 0.3931 -0.0473 0.0992  -0.1040 129 ASN   A CG  
962  O OD1 . ASN   A 123 ? 0.8648 0.5729 0.4155 -0.0573 0.1183  -0.1211 129 ASN   A OD1 
963  N ND2 . ASN   A 123 ? 0.8152 0.5633 0.4358 -0.0361 0.0963  -0.0911 129 ASN   A ND2 
964  N N   . GLY   A 124 ? 0.7308 0.4495 0.1287 -0.0646 0.0527  -0.1043 130 GLY   A N   
965  C CA  . GLY   A 124 ? 0.7238 0.4485 0.0953 -0.0651 0.0403  -0.0981 130 GLY   A CA  
966  C C   . GLY   A 124 ? 0.6947 0.4428 0.0825 -0.0559 0.0215  -0.0799 130 GLY   A C   
967  O O   . GLY   A 124 ? 0.6985 0.4556 0.0777 -0.0561 0.0143  -0.0732 130 GLY   A O   
968  N N   . LEU   A 125 ? 0.6656 0.4207 0.0744 -0.0492 0.0149  -0.0726 131 LEU   A N   
969  C CA  . LEU   A 125 ? 0.6555 0.4264 0.0748 -0.0422 -0.0014 -0.0563 131 LEU   A CA  
970  C C   . LEU   A 125 ? 0.6553 0.4191 0.0528 -0.0411 -0.0106 -0.0564 131 LEU   A C   
971  O O   . LEU   A 125 ? 0.6850 0.4362 0.0752 -0.0441 -0.0045 -0.0672 131 LEU   A O   
972  C CB  . LEU   A 125 ? 0.6403 0.4242 0.1093 -0.0353 0.0003  -0.0468 131 LEU   A CB  
973  C CG  . LEU   A 125 ? 0.6286 0.4238 0.1348 -0.0343 0.0082  -0.0452 131 LEU   A CG  
974  C CD1 . LEU   A 125 ? 0.6058 0.4137 0.1577 -0.0256 0.0026  -0.0311 131 LEU   A CD1 
975  C CD2 . LEU   A 125 ? 0.6375 0.4422 0.1288 -0.0380 0.0006  -0.0406 131 LEU   A CD2 
976  N N   . VAL   A 126 ? 0.6128 0.3841 0.0468 -0.0381 -0.0220 -0.0399 132 VAL   A N   
977  C CA  . VAL   A 126 ? 0.5910 0.3588 0.0465 -0.0364 -0.0275 -0.0355 132 VAL   A CA  
978  C C   . VAL   A 126 ? 0.5721 0.3491 0.0455 -0.0317 -0.0337 -0.0238 132 VAL   A C   
979  O O   . VAL   A 126 ? 0.5627 0.3464 0.0448 -0.0316 -0.0380 -0.0149 132 VAL   A O   
980  C CB  . VAL   A 126 ? 0.5896 0.3498 0.0469 -0.0389 -0.0316 -0.0346 132 VAL   A CB  
981  C CG1 . VAL   A 126 ? 0.5784 0.3410 0.0456 -0.0403 -0.0322 -0.0284 132 VAL   A CG1 
982  C CG2 . VAL   A 126 ? 0.5875 0.3481 0.0473 -0.0361 -0.0387 -0.0321 132 VAL   A CG2 
983  N N   . GLY   A 127 ? 0.5548 0.3300 0.0447 -0.0294 -0.0325 -0.0234 133 GLY   A N   
984  C CA  . GLY   A 127 ? 0.5563 0.3348 0.0447 -0.0266 -0.0381 -0.0141 133 GLY   A CA  
985  C C   . GLY   A 127 ? 0.5409 0.3157 0.0452 -0.0273 -0.0400 -0.0125 133 GLY   A C   
986  O O   . GLY   A 127 ? 0.5339 0.3052 0.0450 -0.0282 -0.0379 -0.0194 133 GLY   A O   
987  N N   . PHE   A 128 ? 0.5085 0.2834 0.0439 -0.0278 -0.0414 -0.0032 134 PHE   A N   
988  C CA  . PHE   A 128 ? 0.5059 0.2765 0.0439 -0.0292 -0.0419 -0.0024 134 PHE   A CA  
989  C C   . PHE   A 128 ? 0.5019 0.2670 0.0437 -0.0300 -0.0413 0.0031  134 PHE   A C   
990  O O   . PHE   A 128 ? 0.5087 0.2721 0.0445 -0.0310 -0.0445 0.0108  134 PHE   A O   
991  C CB  . PHE   A 128 ? 0.4874 0.2570 0.0438 -0.0318 -0.0418 0.0006  134 PHE   A CB  
992  C CG  . PHE   A 128 ? 0.4901 0.2617 0.0440 -0.0318 -0.0420 -0.0026 134 PHE   A CG  
993  C CD1 . PHE   A 128 ? 0.5006 0.2698 0.0452 -0.0306 -0.0428 -0.0080 134 PHE   A CD1 
994  C CD2 . PHE   A 128 ? 0.4959 0.2710 0.0441 -0.0336 -0.0429 -0.0004 134 PHE   A CD2 
995  C CE1 . PHE   A 128 ? 0.5045 0.2711 0.0447 -0.0314 -0.0428 -0.0105 134 PHE   A CE1 
996  C CE2 . PHE   A 128 ? 0.5042 0.2784 0.0440 -0.0347 -0.0419 -0.0041 134 PHE   A CE2 
997  C CZ  . PHE   A 128 ? 0.4972 0.2653 0.0441 -0.0337 -0.0405 -0.0084 134 PHE   A CZ  
998  N N   . ALA   A 129 ? 0.4927 0.2539 0.0431 -0.0305 -0.0377 -0.0004 135 ALA   A N   
999  C CA  . ALA   A 129 ? 0.5063 0.2587 0.0428 -0.0328 -0.0362 0.0031  135 ALA   A CA  
1000 C C   . ALA   A 129 ? 0.5133 0.2591 0.0431 -0.0375 -0.0363 0.0071  135 ALA   A C   
1001 O O   . ALA   A 129 ? 0.4933 0.2406 0.0422 -0.0382 -0.0332 0.0030  135 ALA   A O   
1002 C CB  . ALA   A 129 ? 0.5051 0.2574 0.0424 -0.0328 -0.0320 -0.0046 135 ALA   A CB  
1003 N N   . ASP   A 130 ? 0.5479 0.2859 0.0442 -0.0412 -0.0407 0.0167  136 ASP   A N   
1004 C CA  . ASP   A 130 ? 0.5938 0.3204 0.0456 -0.0482 -0.0416 0.0229  136 ASP   A CA  
1005 C C   . ASP   A 130 ? 0.6221 0.3360 0.0441 -0.0522 -0.0341 0.0216  136 ASP   A C   
1006 O O   . ASP   A 130 ? 0.6485 0.3556 0.0445 -0.0522 -0.0318 0.0239  136 ASP   A O   
1007 C CB  . ASP   A 130 ? 0.6177 0.3358 0.0481 -0.0531 -0.0488 0.0358  136 ASP   A CB  
1008 C CG  . ASP   A 130 ? 0.6782 0.3817 0.0509 -0.0626 -0.0500 0.0445  136 ASP   A CG  
1009 O OD1 . ASP   A 130 ? 0.6473 0.3551 0.0476 -0.0638 -0.0460 0.0364  136 ASP   A OD1 
1010 O OD2 . ASP   A 130 ? 0.7596 0.4436 0.0569 -0.0693 -0.0534 0.0610  136 ASP   A OD2 
1011 N N   . VAL   A 131 ? 0.6246 0.3339 0.0430 -0.0561 -0.0288 0.0182  137 VAL   A N   
1012 C CA  . VAL   A 131 ? 0.6449 0.3416 0.0422 -0.0613 -0.0180 0.0152  137 VAL   A CA  
1013 C C   . VAL   A 131 ? 0.6981 0.3738 0.0428 -0.0717 -0.0124 0.0231  137 VAL   A C   
1014 O O   . VAL   A 131 ? 0.7157 0.3769 0.0425 -0.0779 0.0007  0.0203  137 VAL   A O   
1015 C CB  . VAL   A 131 ? 0.6282 0.3388 0.0419 -0.0561 -0.0145 0.0029  137 VAL   A CB  
1016 C CG1 . VAL   A 131 ? 0.6147 0.3413 0.0433 -0.0491 -0.0203 -0.0039 137 VAL   A CG1 
1017 C CG2 . VAL   A 131 ? 0.6145 0.3315 0.0428 -0.0538 -0.0169 0.0013  137 VAL   A CG2 
1018 N N   . ARG   A 132 ? 0.7076 0.3803 0.0443 -0.0752 -0.0203 0.0310  138 ARG   A N   
1019 C CA  . ARG   A 132 ? 0.7478 0.3996 0.0456 -0.0868 -0.0159 0.0377  138 ARG   A CA  
1020 C C   . ARG   A 132 ? 0.8120 0.4345 0.0481 -0.0988 -0.0106 0.0505  138 ARG   A C   
1021 O O   . ARG   A 132 ? 0.8541 0.4534 0.0495 -0.1112 -0.0030 0.0555  138 ARG   A O   
1022 C CB  . ARG   A 132 ? 0.7307 0.3892 0.0464 -0.0882 -0.0267 0.0410  138 ARG   A CB  
1023 C CG  . ARG   A 132 ? 0.7142 0.3925 0.0475 -0.0797 -0.0289 0.0339  138 ARG   A CG  
1024 C CD  . ARG   A 132 ? 0.7068 0.3886 0.0465 -0.0835 -0.0368 0.0380  138 ARG   A CD  
1025 N NE  . ARG   A 132 ? 0.6863 0.3816 0.0484 -0.0793 -0.0474 0.0420  138 ARG   A NE  
1026 C CZ  . ARG   A 132 ? 0.6788 0.3822 0.0501 -0.0815 -0.0551 0.0453  138 ARG   A CZ  
1027 N NH1 . ARG   A 132 ? 0.6972 0.3947 0.0500 -0.0890 -0.0543 0.0463  138 ARG   A NH1 
1028 N NH2 . ARG   A 132 ? 0.6646 0.3812 0.0524 -0.0766 -0.0634 0.0490  138 ARG   A NH2 
1029 N N   . ASP   A 133 ? 0.8099 0.4300 0.0494 -0.0961 -0.0132 0.0549  139 ASP   A N   
1030 C CA  . ASP   A 133 ? 0.8386 0.4290 0.0525 -0.1064 -0.0090 0.0648  139 ASP   A CA  
1031 C C   . ASP   A 133 ? 0.8229 0.4018 0.0503 -0.1089 0.0102  0.0538  139 ASP   A C   
1032 O O   . ASP   A 133 ? 0.8492 0.3980 0.0531 -0.1197 0.0186  0.0594  139 ASP   A O   
1033 C CB  . ASP   A 133 ? 0.8478 0.4408 0.0643 -0.1014 -0.0250 0.0780  139 ASP   A CB  
1034 C CG  . ASP   A 133 ? 0.8766 0.4897 0.1357 -0.0886 -0.0238 0.0687  139 ASP   A CG  
1035 O OD1 . ASP   A 133 ? 0.8855 0.5255 0.1686 -0.0790 -0.0267 0.0588  139 ASP   A OD1 
1036 O OD2 . ASP   A 133 ? 0.8913 0.4907 0.1569 -0.0893 -0.0188 0.0703  139 ASP   A OD2 
1037 N N   . LEU   A 134 ? 0.7823 0.3839 0.0466 -0.0998 0.0167  0.0384  140 LEU   A N   
1038 C CA  . LEU   A 134 ? 0.7706 0.3646 0.0487 -0.1028 0.0351  0.0272  140 LEU   A CA  
1039 C C   . LEU   A 134 ? 0.7987 0.3781 0.0619 -0.1120 0.0523  0.0213  140 LEU   A C   
1040 O O   . LEU   A 134 ? 0.7797 0.3767 0.0702 -0.1065 0.0585  0.0087  140 LEU   A O   
1041 C CB  . LEU   A 134 ? 0.7283 0.3518 0.0515 -0.0908 0.0333  0.0134  140 LEU   A CB  
1042 C CG  . LEU   A 134 ? 0.6957 0.3333 0.0425 -0.0818 0.0198  0.0159  140 LEU   A CG  
1043 C CD1 . LEU   A 134 ? 0.6704 0.3342 0.0488 -0.0730 0.0186  0.0015  140 LEU   A CD1 
1044 C CD2 . LEU   A 134 ? 0.7049 0.3202 0.0441 -0.0868 0.0238  0.0232  140 LEU   A CD2 
1045 N N   . LEU   A 135 ? 0.8379 0.3828 0.0569 -0.1269 0.0598  0.0309  141 LEU   A N   
1046 C CA  . LEU   A 135 ? 0.8711 0.3941 0.0686 -0.1390 0.0794  0.0263  141 LEU   A CA  
1047 C C   . LEU   A 135 ? 0.8759 0.3954 0.1030 -0.1414 0.1038  0.0100  141 LEU   A C   
1048 O O   . LEU   A 135 ? 0.8728 0.3858 0.1012 -0.1460 0.1207  0.0020  141 LEU   A O   
1049 C CB  . LEU   A 135 ? 0.9117 0.3924 0.0579 -0.1573 0.0823  0.0386  141 LEU   A CB  
1050 C CG  . LEU   A 135 ? 0.9529 0.4319 0.0616 -0.1584 0.0584  0.0578  141 LEU   A CG  
1051 C CD1 . LEU   A 135 ? 1.0085 0.4407 0.0632 -0.1797 0.0621  0.0688  141 LEU   A CD1 
1052 C CD2 . LEU   A 135 ? 0.9466 0.4531 0.0611 -0.1500 0.0452  0.0580  141 LEU   A CD2 
1053 N N   . TRP   A 136 ? 0.8823 0.4032 0.1327 -0.1395 0.1075  0.0053  142 TRP   A N   
1054 C CA  . TRP   A 136 ? 0.8873 0.4063 0.1697 -0.1427 0.1304  -0.0107 142 TRP   A CA  
1055 C C   . TRP   A 136 ? 0.8954 0.4515 0.2290 -0.1299 0.1290  -0.0247 142 TRP   A C   
1056 O O   . TRP   A 136 ? 0.8988 0.4522 0.2568 -0.1340 0.1496  -0.0373 142 TRP   A O   
1057 C CB  . TRP   A 136 ? 0.8733 0.3841 0.1669 -0.1449 0.1349  -0.0128 142 TRP   A CB  
1058 C CG  . TRP   A 136 ? 0.8623 0.3971 0.1724 -0.1319 0.1121  -0.0076 142 TRP   A CG  
1059 C CD1 . TRP   A 136 ? 0.8877 0.4102 0.1707 -0.1318 0.0975  0.0079  142 TRP   A CD1 
1060 C CD2 . TRP   A 136 ? 0.8326 0.4049 0.1911 -0.1184 0.1030  -0.0184 142 TRP   A CD2 
1061 N NE1 . TRP   A 136 ? 0.8739 0.4234 0.1874 -0.1188 0.0828  0.0065  142 TRP   A NE1 
1062 C CE2 . TRP   A 136 ? 0.8432 0.4223 0.1998 -0.1113 0.0858  -0.0098 142 TRP   A CE2 
1063 C CE3 . TRP   A 136 ? 0.8086 0.4081 0.2124 -0.1123 0.1073  -0.0346 142 TRP   A CE3 
1064 C CZ2 . TRP   A 136 ? 0.8202 0.4291 0.2136 -0.1001 0.0755  -0.0177 142 TRP   A CZ2 
1065 C CZ3 . TRP   A 136 ? 0.7913 0.4210 0.2298 -0.1015 0.0936  -0.0413 142 TRP   A CZ3 
1066 C CH2 . TRP   A 136 ? 0.7927 0.4254 0.2237 -0.0963 0.0792  -0.0335 142 TRP   A CH2 
1067 N N   . LEU   A 137 ? 0.8900 0.4792 0.2404 -0.1150 0.1051  -0.0225 143 LEU   A N   
1068 C CA  . LEU   A 137 ? 0.8846 0.5076 0.2786 -0.1025 0.0985  -0.0337 143 LEU   A CA  
1069 C C   . LEU   A 137 ? 0.9254 0.5449 0.3277 -0.1045 0.1135  -0.0403 143 LEU   A C   
1070 O O   . LEU   A 137 ? 0.8935 0.5329 0.3408 -0.0982 0.1173  -0.0524 143 LEU   A O   
1071 C CB  . LEU   A 137 ? 0.8705 0.5166 0.2600 -0.0906 0.0727  -0.0269 143 LEU   A CB  
1072 C CG  . LEU   A 137 ? 0.8690 0.5311 0.2737 -0.0837 0.0579  -0.0268 143 LEU   A CG  
1073 C CD1 . LEU   A 137 ? 0.8825 0.5580 0.2723 -0.0756 0.0370  -0.0184 143 LEU   A CD1 
1074 C CD2 . LEU   A 137 ? 0.8450 0.5313 0.2972 -0.0773 0.0568  -0.0415 143 LEU   A CD2 
1075 N N   . ASP   A 138 ? 0.9935 0.5860 0.3526 -0.1143 0.1224  -0.0321 144 ASP   A N   
1076 C CA  . ASP   A 138 ? 1.0478 0.6299 0.4059 -0.1181 0.1395  -0.0368 144 ASP   A CA  
1077 C C   . ASP   A 138 ? 1.0961 0.6587 0.4721 -0.1288 0.1702  -0.0484 144 ASP   A C   
1078 O O   . ASP   A 138 ? 1.0833 0.6551 0.4945 -0.1248 0.1825  -0.0587 144 ASP   A O   
1079 C CB  . ASP   A 138 ? 1.1018 0.6584 0.4017 -0.1275 0.1389  -0.0242 144 ASP   A CB  
1080 C CG  . ASP   A 138 ? 1.1565 0.7338 0.4434 -0.1171 0.1117  -0.0147 144 ASP   A CG  
1081 O OD1 . ASP   A 138 ? 1.1473 0.7570 0.4697 -0.1019 0.0962  -0.0195 144 ASP   A OD1 
1082 O OD2 . ASP   A 138 ? 1.2019 0.7619 0.4423 -0.1251 0.1058  -0.0029 144 ASP   A OD2 
1083 N N   . GLU   A 139 ? 1.1469 0.6826 0.5017 -0.1420 0.1827  -0.0471 145 GLU   A N   
1084 C CA  . GLU   A 139 ? 1.1913 0.7000 0.5531 -0.1562 0.2154  -0.0578 145 GLU   A CA  
1085 C C   . GLU   A 139 ? 1.2054 0.7286 0.6149 -0.1541 0.2215  -0.0699 145 GLU   A C   
1086 O O   . GLU   A 139 ? 1.2011 0.7494 0.6277 -0.1438 0.1996  -0.0678 145 GLU   A O   
1087 C CB  . GLU   A 139 ? 1.2714 0.7295 0.5643 -0.1767 0.2285  -0.0474 145 GLU   A CB  
1088 C CG  . GLU   A 139 ? 1.3665 0.8185 0.6201 -0.1770 0.2041  -0.0310 145 GLU   A CG  
1089 C CD  . GLU   A 139 ? 1.5039 0.9166 0.6859 -0.1924 0.2023  -0.0155 145 GLU   A CD  
1090 O OE1 . GLU   A 139 ? 1.5313 0.9146 0.6769 -0.2034 0.2012  -0.0064 145 GLU   A OE1 
1091 O OE2 . GLU   A 139 ? 1.5499 0.9605 0.7112 -0.1938 0.2005  -0.0118 145 GLU   A OE2 
1092 N N   . GLU   A 140 ? 1.2166 0.7225 0.6479 -0.1652 0.2536  -0.0837 146 GLU   A N   
1093 C CA  . GLU   A 140 ? 1.2135 0.7295 0.6936 -0.1668 0.2669  -0.0985 146 GLU   A CA  
1094 C C   . GLU   A 140 ? 1.1840 0.7483 0.7395 -0.1505 0.2574  -0.1110 146 GLU   A C   
1095 O O   . GLU   A 140 ? 1.1702 0.7426 0.7766 -0.1533 0.2765  -0.1268 146 GLU   A O   
1096 C CB  . GLU   A 140 ? 1.2507 0.7601 0.7127 -0.1694 0.2564  -0.0930 146 GLU   A CB  
1097 C CG  . GLU   A 140 ? 1.2836 0.8328 0.8011 -0.1575 0.2416  -0.1020 146 GLU   A CG  
1098 C CD  . GLU   A 140 ? 1.3743 0.9072 0.8899 -0.1666 0.2520  -0.1061 146 GLU   A CD  
1099 O OE1 . GLU   A 140 ? 1.4096 0.9185 0.8768 -0.1707 0.2441  -0.0925 146 GLU   A OE1 
1100 O OE2 . GLU   A 140 ? 1.3806 0.9253 0.9454 -0.1695 0.2676  -0.1228 146 GLU   A OE2 
1101 N N1  . A1B3P B .   ? 0.6911 0.4246 0.2155 -0.0267 0.0069  -0.0463 201 A1B3P A N1  
1102 N N3  . A1B3P B .   ? 0.7028 0.4441 0.1951 -0.0343 -0.0055 -0.0587 201 A1B3P A N3  
1103 C C4  . A1B3P B .   ? 0.7603 0.4391 0.1312 -0.0724 0.0350  -0.1243 201 A1B3P A C4  
1104 C C5  . A1B3P B .   ? 0.7481 0.4365 0.1532 -0.0660 0.0369  -0.1183 201 A1B3P A C5  
1105 C C6  . A1B3P B .   ? 0.7447 0.4489 0.1575 -0.0589 0.0208  -0.1073 201 A1B3P A C6  
1106 C C7  . A1B3P B .   ? 0.7440 0.4535 0.1897 -0.0535 0.0250  -0.1017 201 A1B3P A C7  
1107 C C8  . A1B3P B .   ? 0.7542 0.4570 0.1907 -0.0601 0.0218  -0.1104 201 A1B3P A C8  
1108 C C10 . A1B3P B .   ? 0.7289 0.4508 0.2006 -0.0530 0.0074  -0.0976 201 A1B3P A C10 
1109 C C13 . A1B3P B .   ? 0.6958 0.4265 0.2136 -0.0316 0.0126  -0.0606 201 A1B3P A C13 
1110 O O   . A1B3P B .   ? 0.7606 0.4482 0.1762 -0.0707 0.0261  -0.1244 201 A1B3P A O   
1111 C C3  . A1B3P B .   ? 0.7666 0.4526 0.1124 -0.0704 0.0163  -0.1182 201 A1B3P A C3  
1112 C C2  . A1B3P B .   ? 0.7536 0.4567 0.1099 -0.0626 0.0007  -0.1071 201 A1B3P A C2  
1113 C C1  . A1B3P B .   ? 0.7417 0.4534 0.1302 -0.0576 0.0032  -0.1022 201 A1B3P A C1  
1114 S S   . A1B3P B .   ? 0.7215 0.4492 0.1201 -0.0507 -0.0125 -0.0910 201 A1B3P A S   
1115 C C   . A1B3P B .   ? 0.7269 0.4604 0.0958 -0.0491 -0.0292 -0.0858 201 A1B3P A C   
1116 N N   . A1B3P B .   ? 0.7428 0.4561 0.1943 -0.0550 0.0143  -0.1024 201 A1B3P A N   
1117 C C14 . A1B3P B .   ? 0.7259 0.4515 0.1983 -0.0447 0.0107  -0.0859 201 A1B3P A C14 
1118 C C11 . A1B3P B .   ? 0.7206 0.4523 0.1937 -0.0443 0.0015  -0.0828 201 A1B3P A C11 
1119 O O1  . A1B3P B .   ? 0.7178 0.4577 0.1698 -0.0445 -0.0133 -0.0813 201 A1B3P A O1  
1120 C C9  . A1B3P B .   ? 0.7432 0.4551 0.1914 -0.0607 0.0093  -0.1096 201 A1B3P A C9  
1121 C C12 . A1B3P B .   ? 0.7082 0.4433 0.2030 -0.0368 0.0032  -0.0680 201 A1B3P A C12 
1122 N N2  . A1B3P B .   ? 0.6955 0.4343 0.2028 -0.0291 -0.0027 -0.0457 201 A1B3P A N2  
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