data_7HZM
# 
_entry.id   7HZM 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   7HZM         pdb_00007hzm 10.2210/pdb7hzm/pdb 
WWPDB D_1001408130 ?            ?                   
# 
_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       2025-02-12 
# 
_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                        7HZM 
_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   2025-01-14 
_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 'ZINC ION'                                  65.409    1   ?         ? ? ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE'                        78.133    4   ?         ? ? ? 
4 non-polymer syn 'SULFATE ION'                               96.063    1   ?         ? ? ? 
5 non-polymer syn 5-fluoro-1-methyl-1H-indazole-3-carboxamide 193.178   1   ?         ? ? ? 
6 water       nat water                                       18.015    228 ?         ? ? ? 
# 
_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 'ZINC ION'                                  ZN    
3 'DIMETHYL SULFOXIDE'                        DMS   
4 'SULFATE ION'                               SO4   
5 5-fluoro-1-methyl-1H-indazole-3-carboxamide A1BQ3 
6 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 
A1BQ3 non-polymer         . 5-fluoro-1-methyl-1H-indazole-3-carboxamide ? 'C9 H8 F N3 O'   193.178 
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 
SO4   non-polymer         . 'SULFATE ION'                               ? 'O4 S -2'        96.063  
THR   'L-peptide linking' y THREONINE                                   ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                  ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                    ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                      ? 'C5 H11 N O2'    117.146 
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        A1BQ3 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BQ3 
_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 ZN    1   201 1   ZN    ZN  A . 
C 3 DMS   1   202 -1  DMS   DMS A . 
D 3 DMS   1   203 0   DMS   DMS A . 
E 3 DMS   1   204 1   DMS   DMS A . 
F 3 DMS   1   205 3   DMS   DMS A . 
G 4 SO4   1   206 1   SO4   SO4 A . 
H 5 A1BQ3 1   207 246 A1BQ3 LIG A . 
I 6 HOH   1   301 135 HOH   HOH A . 
I 6 HOH   2   302 94  HOH   HOH A . 
I 6 HOH   3   303 43  HOH   HOH A . 
I 6 HOH   4   304 238 HOH   HOH A . 
I 6 HOH   5   305 141 HOH   HOH A . 
I 6 HOH   6   306 147 HOH   HOH A . 
I 6 HOH   7   307 85  HOH   HOH A . 
I 6 HOH   8   308 77  HOH   HOH A . 
I 6 HOH   9   309 103 HOH   HOH A . 
I 6 HOH   10  310 234 HOH   HOH A . 
I 6 HOH   11  311 207 HOH   HOH A . 
I 6 HOH   12  312 219 HOH   HOH A . 
I 6 HOH   13  313 31  HOH   HOH A . 
I 6 HOH   14  314 33  HOH   HOH A . 
I 6 HOH   15  315 105 HOH   HOH A . 
I 6 HOH   16  316 35  HOH   HOH A . 
I 6 HOH   17  317 224 HOH   HOH A . 
I 6 HOH   18  318 34  HOH   HOH A . 
I 6 HOH   19  319 182 HOH   HOH A . 
I 6 HOH   20  320 5   HOH   HOH A . 
I 6 HOH   21  321 107 HOH   HOH A . 
I 6 HOH   22  322 60  HOH   HOH A . 
I 6 HOH   23  323 229 HOH   HOH A . 
I 6 HOH   24  324 70  HOH   HOH A . 
I 6 HOH   25  325 131 HOH   HOH A . 
I 6 HOH   26  326 59  HOH   HOH A . 
I 6 HOH   27  327 205 HOH   HOH A . 
I 6 HOH   28  328 63  HOH   HOH A . 
I 6 HOH   29  329 30  HOH   HOH A . 
I 6 HOH   30  330 152 HOH   HOH A . 
I 6 HOH   31  331 249 HOH   HOH A . 
I 6 HOH   32  332 45  HOH   HOH A . 
I 6 HOH   33  333 36  HOH   HOH A . 
I 6 HOH   34  334 184 HOH   HOH A . 
I 6 HOH   35  335 237 HOH   HOH A . 
I 6 HOH   36  336 211 HOH   HOH A . 
I 6 HOH   37  337 4   HOH   HOH A . 
I 6 HOH   38  338 110 HOH   HOH A . 
I 6 HOH   39  339 49  HOH   HOH A . 
I 6 HOH   40  340 97  HOH   HOH A . 
I 6 HOH   41  341 220 HOH   HOH A . 
I 6 HOH   42  342 231 HOH   HOH A . 
I 6 HOH   43  343 144 HOH   HOH A . 
I 6 HOH   44  344 236 HOH   HOH A . 
I 6 HOH   45  345 2   HOH   HOH A . 
I 6 HOH   46  346 197 HOH   HOH A . 
I 6 HOH   47  347 204 HOH   HOH A . 
I 6 HOH   48  348 74  HOH   HOH A . 
I 6 HOH   49  349 233 HOH   HOH A . 
I 6 HOH   50  350 247 HOH   HOH A . 
I 6 HOH   51  351 13  HOH   HOH A . 
I 6 HOH   52  352 66  HOH   HOH A . 
I 6 HOH   53  353 28  HOH   HOH A . 
I 6 HOH   54  354 137 HOH   HOH A . 
I 6 HOH   55  355 195 HOH   HOH A . 
I 6 HOH   56  356 112 HOH   HOH A . 
I 6 HOH   57  357 104 HOH   HOH A . 
I 6 HOH   58  358 37  HOH   HOH A . 
I 6 HOH   59  359 75  HOH   HOH A . 
I 6 HOH   60  360 50  HOH   HOH A . 
I 6 HOH   61  361 24  HOH   HOH A . 
I 6 HOH   62  362 164 HOH   HOH A . 
I 6 HOH   63  363 68  HOH   HOH A . 
I 6 HOH   64  364 88  HOH   HOH A . 
I 6 HOH   65  365 248 HOH   HOH A . 
I 6 HOH   66  366 138 HOH   HOH A . 
I 6 HOH   67  367 181 HOH   HOH A . 
I 6 HOH   68  368 109 HOH   HOH A . 
I 6 HOH   69  369 58  HOH   HOH A . 
I 6 HOH   70  370 29  HOH   HOH A . 
I 6 HOH   71  371 25  HOH   HOH A . 
I 6 HOH   72  372 78  HOH   HOH A . 
I 6 HOH   73  373 161 HOH   HOH A . 
I 6 HOH   74  374 116 HOH   HOH A . 
I 6 HOH   75  375 82  HOH   HOH A . 
I 6 HOH   76  376 113 HOH   HOH A . 
I 6 HOH   77  377 8   HOH   HOH A . 
I 6 HOH   78  378 15  HOH   HOH A . 
I 6 HOH   79  379 16  HOH   HOH A . 
I 6 HOH   80  380 96  HOH   HOH A . 
I 6 HOH   81  381 46  HOH   HOH A . 
I 6 HOH   82  382 42  HOH   HOH A . 
I 6 HOH   83  383 21  HOH   HOH A . 
I 6 HOH   84  384 108 HOH   HOH A . 
I 6 HOH   85  385 133 HOH   HOH A . 
I 6 HOH   86  386 203 HOH   HOH A . 
I 6 HOH   87  387 90  HOH   HOH A . 
I 6 HOH   88  388 84  HOH   HOH A . 
I 6 HOH   89  389 132 HOH   HOH A . 
I 6 HOH   90  390 174 HOH   HOH A . 
I 6 HOH   91  391 169 HOH   HOH A . 
I 6 HOH   92  392 12  HOH   HOH A . 
I 6 HOH   93  393 178 HOH   HOH A . 
I 6 HOH   94  394 69  HOH   HOH A . 
I 6 HOH   95  395 173 HOH   HOH A . 
I 6 HOH   96  396 72  HOH   HOH A . 
I 6 HOH   97  397 62  HOH   HOH A . 
I 6 HOH   98  398 213 HOH   HOH A . 
I 6 HOH   99  399 198 HOH   HOH A . 
I 6 HOH   100 400 186 HOH   HOH A . 
I 6 HOH   101 401 67  HOH   HOH A . 
I 6 HOH   102 402 19  HOH   HOH A . 
I 6 HOH   103 403 124 HOH   HOH A . 
I 6 HOH   104 404 7   HOH   HOH A . 
I 6 HOH   105 405 226 HOH   HOH A . 
I 6 HOH   106 406 150 HOH   HOH A . 
I 6 HOH   107 407 148 HOH   HOH A . 
I 6 HOH   108 408 20  HOH   HOH A . 
I 6 HOH   109 409 91  HOH   HOH A . 
I 6 HOH   110 410 71  HOH   HOH A . 
I 6 HOH   111 411 40  HOH   HOH A . 
I 6 HOH   112 412 41  HOH   HOH A . 
I 6 HOH   113 413 217 HOH   HOH A . 
I 6 HOH   114 414 111 HOH   HOH A . 
I 6 HOH   115 415 26  HOH   HOH A . 
I 6 HOH   116 416 128 HOH   HOH A . 
I 6 HOH   117 417 123 HOH   HOH A . 
I 6 HOH   118 418 57  HOH   HOH A . 
I 6 HOH   119 419 168 HOH   HOH A . 
I 6 HOH   120 420 114 HOH   HOH A . 
I 6 HOH   121 421 51  HOH   HOH A . 
I 6 HOH   122 422 81  HOH   HOH A . 
I 6 HOH   123 423 9   HOH   HOH A . 
I 6 HOH   124 424 199 HOH   HOH A . 
I 6 HOH   125 425 155 HOH   HOH A . 
I 6 HOH   126 426 126 HOH   HOH A . 
I 6 HOH   127 427 167 HOH   HOH A . 
I 6 HOH   128 428 218 HOH   HOH A . 
I 6 HOH   129 429 214 HOH   HOH A . 
I 6 HOH   130 430 157 HOH   HOH A . 
I 6 HOH   131 431 235 HOH   HOH A . 
I 6 HOH   132 432 101 HOH   HOH A . 
I 6 HOH   133 433 79  HOH   HOH A . 
I 6 HOH   134 434 159 HOH   HOH A . 
I 6 HOH   135 435 47  HOH   HOH A . 
I 6 HOH   136 436 119 HOH   HOH A . 
I 6 HOH   137 437 100 HOH   HOH A . 
I 6 HOH   138 438 61  HOH   HOH A . 
I 6 HOH   139 439 230 HOH   HOH A . 
I 6 HOH   140 440 17  HOH   HOH A . 
I 6 HOH   141 441 53  HOH   HOH A . 
I 6 HOH   142 442 215 HOH   HOH A . 
I 6 HOH   143 443 210 HOH   HOH A . 
I 6 HOH   144 444 89  HOH   HOH A . 
I 6 HOH   145 445 11  HOH   HOH A . 
I 6 HOH   146 446 64  HOH   HOH A . 
I 6 HOH   147 447 80  HOH   HOH A . 
I 6 HOH   148 448 38  HOH   HOH A . 
I 6 HOH   149 449 39  HOH   HOH A . 
I 6 HOH   150 450 48  HOH   HOH A . 
I 6 HOH   151 451 202 HOH   HOH A . 
I 6 HOH   152 452 117 HOH   HOH A . 
I 6 HOH   153 453 27  HOH   HOH A . 
I 6 HOH   154 454 177 HOH   HOH A . 
I 6 HOH   155 455 250 HOH   HOH A . 
I 6 HOH   156 456 10  HOH   HOH A . 
I 6 HOH   157 457 212 HOH   HOH A . 
I 6 HOH   158 458 65  HOH   HOH A . 
I 6 HOH   159 459 106 HOH   HOH A . 
I 6 HOH   160 460 171 HOH   HOH A . 
I 6 HOH   161 461 201 HOH   HOH A . 
I 6 HOH   162 462 14  HOH   HOH A . 
I 6 HOH   163 463 192 HOH   HOH A . 
I 6 HOH   164 464 136 HOH   HOH A . 
I 6 HOH   165 465 127 HOH   HOH A . 
I 6 HOH   166 466 121 HOH   HOH A . 
I 6 HOH   167 467 134 HOH   HOH A . 
I 6 HOH   168 468 176 HOH   HOH A . 
I 6 HOH   169 469 146 HOH   HOH A . 
I 6 HOH   170 470 23  HOH   HOH A . 
I 6 HOH   171 471 93  HOH   HOH A . 
I 6 HOH   172 472 95  HOH   HOH A . 
I 6 HOH   173 473 245 HOH   HOH A . 
I 6 HOH   174 474 52  HOH   HOH A . 
I 6 HOH   175 475 187 HOH   HOH A . 
I 6 HOH   176 476 158 HOH   HOH A . 
I 6 HOH   177 477 151 HOH   HOH A . 
I 6 HOH   178 478 32  HOH   HOH A . 
I 6 HOH   179 479 102 HOH   HOH A . 
I 6 HOH   180 480 225 HOH   HOH A . 
I 6 HOH   181 481 227 HOH   HOH A . 
I 6 HOH   182 482 189 HOH   HOH A . 
I 6 HOH   183 483 193 HOH   HOH A . 
I 6 HOH   184 484 216 HOH   HOH A . 
I 6 HOH   185 485 232 HOH   HOH A . 
I 6 HOH   186 486 228 HOH   HOH A . 
I 6 HOH   187 487 175 HOH   HOH A . 
I 6 HOH   188 488 179 HOH   HOH A . 
I 6 HOH   189 489 122 HOH   HOH A . 
I 6 HOH   190 490 76  HOH   HOH A . 
I 6 HOH   191 491 154 HOH   HOH A . 
I 6 HOH   192 492 56  HOH   HOH A . 
I 6 HOH   193 493 183 HOH   HOH A . 
I 6 HOH   194 494 223 HOH   HOH A . 
I 6 HOH   195 495 99  HOH   HOH A . 
I 6 HOH   196 496 240 HOH   HOH A . 
I 6 HOH   197 497 98  HOH   HOH A . 
I 6 HOH   198 498 156 HOH   HOH A . 
I 6 HOH   199 499 120 HOH   HOH A . 
I 6 HOH   200 500 162 HOH   HOH A . 
I 6 HOH   201 501 222 HOH   HOH A . 
I 6 HOH   202 502 153 HOH   HOH A . 
I 6 HOH   203 503 180 HOH   HOH A . 
I 6 HOH   204 504 140 HOH   HOH A . 
I 6 HOH   205 505 86  HOH   HOH A . 
I 6 HOH   206 506 83  HOH   HOH A . 
I 6 HOH   207 507 191 HOH   HOH A . 
I 6 HOH   208 508 87  HOH   HOH A . 
I 6 HOH   209 509 129 HOH   HOH A . 
I 6 HOH   210 510 209 HOH   HOH A . 
I 6 HOH   211 511 206 HOH   HOH A . 
I 6 HOH   212 512 73  HOH   HOH A . 
I 6 HOH   213 513 246 HOH   HOH A . 
I 6 HOH   214 514 190 HOH   HOH A . 
I 6 HOH   215 515 208 HOH   HOH A . 
I 6 HOH   216 516 221 HOH   HOH A . 
I 6 HOH   217 517 165 HOH   HOH A . 
I 6 HOH   218 518 241 HOH   HOH A . 
I 6 HOH   219 519 239 HOH   HOH A . 
I 6 HOH   220 520 200 HOH   HOH A . 
I 6 HOH   221 521 118 HOH   HOH A . 
I 6 HOH   222 522 92  HOH   HOH A . 
I 6 HOH   223 523 243 HOH   HOH A . 
I 6 HOH   224 524 242 HOH   HOH A . 
I 6 HOH   225 525 125 HOH   HOH A . 
I 6 HOH   226 526 142 HOH   HOH A . 
I 6 HOH   227 527 244 HOH   HOH A . 
I 6 HOH   228 528 160 HOH   HOH A . 
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       REFMAC  5.8.0267 ? 1 
refinement       REFMAC5 .        ? 2 
'data scaling'   Aimless .        ? 3 
phasing          PHASER  .        ? 4 
'data reduction' XDS     .        ? 5 
# 
_cell.entry_id           7HZM 
_cell.length_a           86.468 
_cell.length_b           57.055 
_cell.length_c           32.376 
_cell.angle_alpha        90.00 
_cell.angle_beta         94.82 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HZM 
_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          7HZM 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.50 
_exptl_crystal.density_percent_sol   50.87 
_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   2024-09-04 
_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   0.92134 
_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        0.92134 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HZM 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             47.57 
_reflns.d_resolution_high            1.19 
_reflns.number_obs                   41117 
_reflns.percent_possible_obs         81.2 
_reflns.pdbx_Rmerge_I_obs            0.042 
_reflns.pdbx_netI_over_sigmaI        19.5 
_reflns.pdbx_redundancy              5.5 
_reflns.pdbx_Rrim_I_all              0.046 
_reflns.pdbx_Rpim_I_all              0.018 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     224762 
_reflns.pdbx_chi_squared             0.96 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_CC_star                 ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.19 
_reflns_shell.d_res_low                   1.25 
_reflns_shell.number_measured_all         3602 
_reflns_shell.number_unique_obs           2198 
_reflns_shell.Rmerge_I_obs                0.436 
_reflns_shell.pdbx_chi_squared            0.65 
_reflns_shell.pdbx_redundancy             1.6 
_reflns_shell.percent_possible_obs        29.9 
_reflns_shell.pdbx_netI_over_sigmaI_obs   1.3 
_reflns_shell.pdbx_Rrim_I_all             0.596 
_reflns_shell.pdbx_Rpim_I_all             0.403 
_reflns_shell.pdbx_CC_half                0.668 
_reflns_shell.percent_possible_all        ? 
_reflns_shell.pdbx_Rsym_value             ? 
_reflns_shell.meanI_over_sigI_obs         ? 
_reflns_shell.number_measured_obs         ? 
_reflns_shell.number_unique_all           ? 
_reflns_shell.pdbx_CC_star                ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 7HZM 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     39083 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             47.57 
_refine.ls_d_res_high                            1.19 
_refine.ls_percent_reflns_obs                    81.11 
_refine.ls_R_factor_obs                          0.33233 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.32973 
_refine.ls_R_factor_R_free                       0.38082 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.9 
_refine.ls_number_reflns_R_free                  2034 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.898 
_refine.correlation_coeff_Fo_to_Fc_free          0.866 
_refine.B_iso_mean                               18.582 
_refine.aniso_B[1][1]                            -0.03 
_refine.aniso_B[2][2]                            0.02 
_refine.aniso_B[3][3]                            -0.06 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            0.42 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.117 
_refine.pdbx_overall_ESU_R_Free                  0.118 
_refine.overall_SU_ML                            0.124 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             2.738 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.pdbx_number_atoms_protein        1083 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         36 
_refine_hist.number_atoms_solvent             228 
_refine_hist.number_atoms_total               1347 
_refine_hist.d_res_high                       1.19 
_refine_hist.d_res_low                        47.57 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.008  0.014  ? 2646 'X-RAY DIFFRACTION' ? 
r_bond_other_d               0.001  0.015  ? 1772 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.568  1.623  ? 2806 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            1.291  1.580  ? 4080 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       7.170  5.000  ? 268  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       31.606 21.963 ? 107  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       13.455 15.000 ? 277  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       17.192 15.000 ? 12   'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.063  0.200  ? 242  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.007  0.020  ? 2593 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           0.002  0.020  ? 503  'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  1.212  1.733  ? 1358 'X-RAY DIFFRACTION' ? 
r_mcbond_other               1.221  1.719  ? 1339 'X-RAY DIFFRACTION' ? 
r_mcangle_it                 2.258  2.592  ? 1312 'X-RAY DIFFRACTION' ? 
r_mcangle_other              2.257  2.592  ? 1313 'X-RAY DIFFRACTION' ? 
r_scbond_it                  0.990  1.950  ? 1288 'X-RAY DIFFRACTION' ? 
r_scbond_other               0.986  1.926  ? 1285 'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              1.665  2.852  ? 1489 'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       9.866  24.007 ? 2672 'X-RAY DIFFRACTION' ? 
r_long_range_B_other         9.864  24.023 ? 2673 'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       1.187 
_refine_ls_shell.d_res_low                        1.217 
_refine_ls_shell.number_reflns_R_work             829 
_refine_ls_shell.R_factor_R_work                  0.391 
_refine_ls_shell.percent_reflns_obs               23.19 
_refine_ls_shell.R_factor_R_free                  0.347 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             37 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.number_reflns_obs                ? 
# 
_struct.entry_id                  7HZM 
_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-0030611-001 (A71EV2A-x2351)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HZM 
_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 3 ? 
E N N 3 ? 
F N N 3 ? 
G N N 4 ? 
H N N 5 ? 
I N N 6 ? 
# 
_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              7HZM 
_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,H,I 
# 
_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  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
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 ? GLU A 139 ? LEU A 140 GLU A 145 5 ? 6 
# 
_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 B ZN . ZN ? ? A CYS 56  A ZN 201 1_555 ? ? ? ? ? ? ? 2.384 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 B ZN . ZN ? ? A CYS 58  A ZN 201 1_555 ? ? ? ? ? ? ? 2.395 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 B ZN . ZN ? ? A CYS 116 A ZN 201 1_555 ? ? ? ? ? ? ? 2.331 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 B ZN . ZN ? ? A HIS 118 A ZN 201 1_555 ? ? ? ? ? ? ? 2.068 ? ? 
# 
_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 ? B ZN . ? A ZN 201 ? 1_555 SG  ? A CYS 52  ? A CYS 58  ? 1_555 108.0 ? 
2 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? B ZN . ? A ZN 201 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 108.4 ? 
3 SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? B ZN . ? A ZN 201 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 118.4 ? 
4 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? B ZN . ? A ZN 201 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 100.7 ? 
5 SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? B ZN . ? A ZN 201 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 101.9 ? 
6 SG ? A CYS 110 ? A CYS 116 ? 1_555 ZN ? B ZN . ? A ZN 201 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 117.6 ? 
# 
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 TYR A 9   ? ASN A 13  ? TYR A 15  ASN A 19  
AA1 2 LEU A 34  ? SER A 38  ? LEU A 40  SER A 44  
AA1 3 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
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 ? CYS A 110 ? ILE A 113 CYS A 116 
AA2 4 GLY A 113 ? GLY A 122 ? GLY A 119 GLY A 128 
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 VAL A 12  ? N VAL A 18  O LEU A 35  ? O LEU A 41  
AA1 2 3 O LEU A 34  ? O LEU A 40  N ASP A 29  ? N ASP A 35  
AA2 1 2 O LYS A 64  ? O LYS A 70  N CYS A 59  ? N CYS A 65  
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 VAL A 115 ? O VAL A 121 
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                   7HZM 
_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 383 ? ? O A HOH 443 ? ? 1.46 
2 1 O  A HOH 515 ? ? O A HOH 522 ? ? 1.95 
3 1 O  A HOH 330 ? ? O A HOH 402 ? ? 1.98 
4 1 O  A HOH 451 ? ? O A HOH 478 ? ? 2.04 
5 1 O  A VAL 32  ? ? O A HOH 301 ? ? 2.11 
6 1 O  A HOH 386 ? ? O A HOH 460 ? ? 2.11 
7 1 OH A TYR 15  ? ? O A HOH 302 ? ? 2.13 
8 1 N  A SER 105 ? ? O A HOH 303 ? ? 2.14 
9 1 O  A HOH 385 ? ? O A HOH 393 ? ? 2.14 
# 
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 338 ? ? 1_555 O A HOH 433 ? ? 1_556 2.03 
2 1 O A HOH 328 ? ? 1_555 O A HOH 329 ? ? 2_556 2.16 
# 
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 VAL A 32  ? ? -130.02 -53.09 
2 1 SER A 125 ? ? -133.42 -39.45 
# 
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 527 ? 7.73  . 
2 1 O ? A HOH 528 ? 11.05 . 
# 
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 
A1BQ3 N1   N  Y N 1   
A1BQ3 C4   C  Y N 2   
A1BQ3 C5   C  Y N 3   
A1BQ3 C6   C  Y N 4   
A1BQ3 C7   C  Y N 5   
A1BQ3 C8   C  Y N 6   
A1BQ3 N    N  Y N 7   
A1BQ3 C    C  N N 8   
A1BQ3 O    O  N N 9   
A1BQ3 C1   C  Y N 10  
A1BQ3 C2   C  N N 11  
A1BQ3 C3   C  Y N 12  
A1BQ3 F    F  N N 13  
A1BQ3 N2   N  N N 14  
A1BQ3 H5   H  N N 15  
A1BQ3 H6   H  N N 16  
A1BQ3 H7   H  N N 17  
A1BQ3 H1   H  N N 18  
A1BQ3 H    H  N N 19  
A1BQ3 H2   H  N N 20  
A1BQ3 H3   H  N N 21  
A1BQ3 H4   H  N N 22  
ALA   N    N  N N 23  
ALA   CA   C  N S 24  
ALA   C    C  N N 25  
ALA   O    O  N N 26  
ALA   CB   C  N N 27  
ALA   OXT  O  N N 28  
ALA   H    H  N N 29  
ALA   H2   H  N N 30  
ALA   HA   H  N N 31  
ALA   HB1  H  N N 32  
ALA   HB2  H  N N 33  
ALA   HB3  H  N N 34  
ALA   HXT  H  N N 35  
ARG   N    N  N N 36  
ARG   CA   C  N S 37  
ARG   C    C  N N 38  
ARG   O    O  N N 39  
ARG   CB   C  N N 40  
ARG   CG   C  N N 41  
ARG   CD   C  N N 42  
ARG   NE   N  N N 43  
ARG   CZ   C  N N 44  
ARG   NH1  N  N N 45  
ARG   NH2  N  N N 46  
ARG   OXT  O  N N 47  
ARG   H    H  N N 48  
ARG   H2   H  N N 49  
ARG   HA   H  N N 50  
ARG   HB2  H  N N 51  
ARG   HB3  H  N N 52  
ARG   HG2  H  N N 53  
ARG   HG3  H  N N 54  
ARG   HD2  H  N N 55  
ARG   HD3  H  N N 56  
ARG   HE   H  N N 57  
ARG   HH11 H  N N 58  
ARG   HH12 H  N N 59  
ARG   HH21 H  N N 60  
ARG   HH22 H  N N 61  
ARG   HXT  H  N N 62  
ASN   N    N  N N 63  
ASN   CA   C  N S 64  
ASN   C    C  N N 65  
ASN   O    O  N N 66  
ASN   CB   C  N N 67  
ASN   CG   C  N N 68  
ASN   OD1  O  N N 69  
ASN   ND2  N  N N 70  
ASN   OXT  O  N N 71  
ASN   H    H  N N 72  
ASN   H2   H  N N 73  
ASN   HA   H  N N 74  
ASN   HB2  H  N N 75  
ASN   HB3  H  N N 76  
ASN   HD21 H  N N 77  
ASN   HD22 H  N N 78  
ASN   HXT  H  N N 79  
ASP   N    N  N N 80  
ASP   CA   C  N S 81  
ASP   C    C  N N 82  
ASP   O    O  N N 83  
ASP   CB   C  N N 84  
ASP   CG   C  N N 85  
ASP   OD1  O  N N 86  
ASP   OD2  O  N N 87  
ASP   OXT  O  N N 88  
ASP   H    H  N N 89  
ASP   H2   H  N N 90  
ASP   HA   H  N N 91  
ASP   HB2  H  N N 92  
ASP   HB3  H  N N 93  
ASP   HD2  H  N N 94  
ASP   HXT  H  N N 95  
CYS   N    N  N N 96  
CYS   CA   C  N R 97  
CYS   C    C  N N 98  
CYS   O    O  N N 99  
CYS   CB   C  N N 100 
CYS   SG   S  N N 101 
CYS   OXT  O  N N 102 
CYS   H    H  N N 103 
CYS   H2   H  N N 104 
CYS   HA   H  N N 105 
CYS   HB2  H  N N 106 
CYS   HB3  H  N N 107 
CYS   HG   H  N N 108 
CYS   HXT  H  N N 109 
DMS   S    S  N N 110 
DMS   O    O  N N 111 
DMS   C1   C  N N 112 
DMS   C2   C  N N 113 
DMS   H11  H  N N 114 
DMS   H12  H  N N 115 
DMS   H13  H  N N 116 
DMS   H21  H  N N 117 
DMS   H22  H  N N 118 
DMS   H23  H  N N 119 
GLN   N    N  N N 120 
GLN   CA   C  N S 121 
GLN   C    C  N N 122 
GLN   O    O  N N 123 
GLN   CB   C  N N 124 
GLN   CG   C  N N 125 
GLN   CD   C  N N 126 
GLN   OE1  O  N N 127 
GLN   NE2  N  N N 128 
GLN   OXT  O  N N 129 
GLN   H    H  N N 130 
GLN   H2   H  N N 131 
GLN   HA   H  N N 132 
GLN   HB2  H  N N 133 
GLN   HB3  H  N N 134 
GLN   HG2  H  N N 135 
GLN   HG3  H  N N 136 
GLN   HE21 H  N N 137 
GLN   HE22 H  N N 138 
GLN   HXT  H  N N 139 
GLU   N    N  N N 140 
GLU   CA   C  N S 141 
GLU   C    C  N N 142 
GLU   O    O  N N 143 
GLU   CB   C  N N 144 
GLU   CG   C  N N 145 
GLU   CD   C  N N 146 
GLU   OE1  O  N N 147 
GLU   OE2  O  N N 148 
GLU   OXT  O  N N 149 
GLU   H    H  N N 150 
GLU   H2   H  N N 151 
GLU   HA   H  N N 152 
GLU   HB2  H  N N 153 
GLU   HB3  H  N N 154 
GLU   HG2  H  N N 155 
GLU   HG3  H  N N 156 
GLU   HE2  H  N N 157 
GLU   HXT  H  N N 158 
GLY   N    N  N N 159 
GLY   CA   C  N N 160 
GLY   C    C  N N 161 
GLY   O    O  N N 162 
GLY   OXT  O  N N 163 
GLY   H    H  N N 164 
GLY   H2   H  N N 165 
GLY   HA2  H  N N 166 
GLY   HA3  H  N N 167 
GLY   HXT  H  N N 168 
HIS   N    N  N N 169 
HIS   CA   C  N S 170 
HIS   C    C  N N 171 
HIS   O    O  N N 172 
HIS   CB   C  N N 173 
HIS   CG   C  Y N 174 
HIS   ND1  N  Y N 175 
HIS   CD2  C  Y N 176 
HIS   CE1  C  Y N 177 
HIS   NE2  N  Y N 178 
HIS   OXT  O  N N 179 
HIS   H    H  N N 180 
HIS   H2   H  N N 181 
HIS   HA   H  N N 182 
HIS   HB2  H  N N 183 
HIS   HB3  H  N N 184 
HIS   HD1  H  N N 185 
HIS   HD2  H  N N 186 
HIS   HE1  H  N N 187 
HIS   HE2  H  N N 188 
HIS   HXT  H  N N 189 
HOH   O    O  N N 190 
HOH   H1   H  N N 191 
HOH   H2   H  N N 192 
ILE   N    N  N N 193 
ILE   CA   C  N S 194 
ILE   C    C  N N 195 
ILE   O    O  N N 196 
ILE   CB   C  N S 197 
ILE   CG1  C  N N 198 
ILE   CG2  C  N N 199 
ILE   CD1  C  N N 200 
ILE   OXT  O  N N 201 
ILE   H    H  N N 202 
ILE   H2   H  N N 203 
ILE   HA   H  N N 204 
ILE   HB   H  N N 205 
ILE   HG12 H  N N 206 
ILE   HG13 H  N N 207 
ILE   HG21 H  N N 208 
ILE   HG22 H  N N 209 
ILE   HG23 H  N N 210 
ILE   HD11 H  N N 211 
ILE   HD12 H  N N 212 
ILE   HD13 H  N N 213 
ILE   HXT  H  N N 214 
LEU   N    N  N N 215 
LEU   CA   C  N S 216 
LEU   C    C  N N 217 
LEU   O    O  N N 218 
LEU   CB   C  N N 219 
LEU   CG   C  N N 220 
LEU   CD1  C  N N 221 
LEU   CD2  C  N N 222 
LEU   OXT  O  N N 223 
LEU   H    H  N N 224 
LEU   H2   H  N N 225 
LEU   HA   H  N N 226 
LEU   HB2  H  N N 227 
LEU   HB3  H  N N 228 
LEU   HG   H  N N 229 
LEU   HD11 H  N N 230 
LEU   HD12 H  N N 231 
LEU   HD13 H  N N 232 
LEU   HD21 H  N N 233 
LEU   HD22 H  N N 234 
LEU   HD23 H  N N 235 
LEU   HXT  H  N N 236 
LYS   N    N  N N 237 
LYS   CA   C  N S 238 
LYS   C    C  N N 239 
LYS   O    O  N N 240 
LYS   CB   C  N N 241 
LYS   CG   C  N N 242 
LYS   CD   C  N N 243 
LYS   CE   C  N N 244 
LYS   NZ   N  N N 245 
LYS   OXT  O  N N 246 
LYS   H    H  N N 247 
LYS   H2   H  N N 248 
LYS   HA   H  N N 249 
LYS   HB2  H  N N 250 
LYS   HB3  H  N N 251 
LYS   HG2  H  N N 252 
LYS   HG3  H  N N 253 
LYS   HD2  H  N N 254 
LYS   HD3  H  N N 255 
LYS   HE2  H  N N 256 
LYS   HE3  H  N N 257 
LYS   HZ1  H  N N 258 
LYS   HZ2  H  N N 259 
LYS   HZ3  H  N N 260 
LYS   HXT  H  N N 261 
MET   N    N  N N 262 
MET   CA   C  N S 263 
MET   C    C  N N 264 
MET   O    O  N N 265 
MET   CB   C  N N 266 
MET   CG   C  N N 267 
MET   SD   S  N N 268 
MET   CE   C  N N 269 
MET   OXT  O  N N 270 
MET   H    H  N N 271 
MET   H2   H  N N 272 
MET   HA   H  N N 273 
MET   HB2  H  N N 274 
MET   HB3  H  N N 275 
MET   HG2  H  N N 276 
MET   HG3  H  N N 277 
MET   HE1  H  N N 278 
MET   HE2  H  N N 279 
MET   HE3  H  N N 280 
MET   HXT  H  N N 281 
PHE   N    N  N N 282 
PHE   CA   C  N S 283 
PHE   C    C  N N 284 
PHE   O    O  N N 285 
PHE   CB   C  N N 286 
PHE   CG   C  Y N 287 
PHE   CD1  C  Y N 288 
PHE   CD2  C  Y N 289 
PHE   CE1  C  Y N 290 
PHE   CE2  C  Y N 291 
PHE   CZ   C  Y N 292 
PHE   OXT  O  N N 293 
PHE   H    H  N N 294 
PHE   H2   H  N N 295 
PHE   HA   H  N N 296 
PHE   HB2  H  N N 297 
PHE   HB3  H  N N 298 
PHE   HD1  H  N N 299 
PHE   HD2  H  N N 300 
PHE   HE1  H  N N 301 
PHE   HE2  H  N N 302 
PHE   HZ   H  N N 303 
PHE   HXT  H  N N 304 
PRO   N    N  N N 305 
PRO   CA   C  N S 306 
PRO   C    C  N N 307 
PRO   O    O  N N 308 
PRO   CB   C  N N 309 
PRO   CG   C  N N 310 
PRO   CD   C  N N 311 
PRO   OXT  O  N N 312 
PRO   H    H  N N 313 
PRO   HA   H  N N 314 
PRO   HB2  H  N N 315 
PRO   HB3  H  N N 316 
PRO   HG2  H  N N 317 
PRO   HG3  H  N N 318 
PRO   HD2  H  N N 319 
PRO   HD3  H  N N 320 
PRO   HXT  H  N N 321 
SER   N    N  N N 322 
SER   CA   C  N S 323 
SER   C    C  N N 324 
SER   O    O  N N 325 
SER   CB   C  N N 326 
SER   OG   O  N N 327 
SER   OXT  O  N N 328 
SER   H    H  N N 329 
SER   H2   H  N N 330 
SER   HA   H  N N 331 
SER   HB2  H  N N 332 
SER   HB3  H  N N 333 
SER   HG   H  N N 334 
SER   HXT  H  N N 335 
SO4   S    S  N N 336 
SO4   O1   O  N N 337 
SO4   O2   O  N N 338 
SO4   O3   O  N N 339 
SO4   O4   O  N N 340 
THR   N    N  N N 341 
THR   CA   C  N S 342 
THR   C    C  N N 343 
THR   O    O  N N 344 
THR   CB   C  N R 345 
THR   OG1  O  N N 346 
THR   CG2  C  N N 347 
THR   OXT  O  N N 348 
THR   H    H  N N 349 
THR   H2   H  N N 350 
THR   HA   H  N N 351 
THR   HB   H  N N 352 
THR   HG1  H  N N 353 
THR   HG21 H  N N 354 
THR   HG22 H  N N 355 
THR   HG23 H  N N 356 
THR   HXT  H  N N 357 
TRP   N    N  N N 358 
TRP   CA   C  N S 359 
TRP   C    C  N N 360 
TRP   O    O  N N 361 
TRP   CB   C  N N 362 
TRP   CG   C  Y N 363 
TRP   CD1  C  Y N 364 
TRP   CD2  C  Y N 365 
TRP   NE1  N  Y N 366 
TRP   CE2  C  Y N 367 
TRP   CE3  C  Y N 368 
TRP   CZ2  C  Y N 369 
TRP   CZ3  C  Y N 370 
TRP   CH2  C  Y N 371 
TRP   OXT  O  N N 372 
TRP   H    H  N N 373 
TRP   H2   H  N N 374 
TRP   HA   H  N N 375 
TRP   HB2  H  N N 376 
TRP   HB3  H  N N 377 
TRP   HD1  H  N N 378 
TRP   HE1  H  N N 379 
TRP   HE3  H  N N 380 
TRP   HZ2  H  N N 381 
TRP   HZ3  H  N N 382 
TRP   HH2  H  N N 383 
TRP   HXT  H  N N 384 
TYR   N    N  N N 385 
TYR   CA   C  N S 386 
TYR   C    C  N N 387 
TYR   O    O  N N 388 
TYR   CB   C  N N 389 
TYR   CG   C  Y N 390 
TYR   CD1  C  Y N 391 
TYR   CD2  C  Y N 392 
TYR   CE1  C  Y N 393 
TYR   CE2  C  Y N 394 
TYR   CZ   C  Y N 395 
TYR   OH   O  N N 396 
TYR   OXT  O  N N 397 
TYR   H    H  N N 398 
TYR   H2   H  N N 399 
TYR   HA   H  N N 400 
TYR   HB2  H  N N 401 
TYR   HB3  H  N N 402 
TYR   HD1  H  N N 403 
TYR   HD2  H  N N 404 
TYR   HE1  H  N N 405 
TYR   HE2  H  N N 406 
TYR   HH   H  N N 407 
TYR   HXT  H  N N 408 
VAL   N    N  N N 409 
VAL   CA   C  N S 410 
VAL   C    C  N N 411 
VAL   O    O  N N 412 
VAL   CB   C  N N 413 
VAL   CG1  C  N N 414 
VAL   CG2  C  N N 415 
VAL   OXT  O  N N 416 
VAL   H    H  N N 417 
VAL   H2   H  N N 418 
VAL   HA   H  N N 419 
VAL   HB   H  N N 420 
VAL   HG11 H  N N 421 
VAL   HG12 H  N N 422 
VAL   HG13 H  N N 423 
VAL   HG21 H  N N 424 
VAL   HG22 H  N N 425 
VAL   HG23 H  N N 426 
VAL   HXT  H  N N 427 
ZN    ZN   ZN N N 428 
# 
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 
A1BQ3 C   N    sing N N 1   
A1BQ3 N   N1   sing Y N 2   
A1BQ3 N1  C1   doub Y N 3   
A1BQ3 C2  C1   sing N N 4   
A1BQ3 N2  C2   sing N N 5   
A1BQ3 O   C2   doub N N 6   
A1BQ3 C1  C3   sing Y N 7   
A1BQ3 C3  C4   doub Y N 8   
A1BQ3 C4  C5   sing Y N 9   
A1BQ3 C5  F    sing N N 10  
A1BQ3 C6  C5   doub Y N 11  
A1BQ3 C7  C6   sing Y N 12  
A1BQ3 C8  C7   doub Y N 13  
A1BQ3 C3  C8   sing Y N 14  
A1BQ3 N   C8   sing Y N 15  
A1BQ3 C4  H5   sing N N 16  
A1BQ3 C6  H6   sing N N 17  
A1BQ3 C7  H7   sing N N 18  
A1BQ3 C   H1   sing N N 19  
A1BQ3 C   H    sing N N 20  
A1BQ3 C   H2   sing N N 21  
A1BQ3 N2  H3   sing N N 22  
A1BQ3 N2  H4   sing N N 23  
ALA   N   CA   sing N N 24  
ALA   N   H    sing N N 25  
ALA   N   H2   sing N N 26  
ALA   CA  C    sing N N 27  
ALA   CA  CB   sing N N 28  
ALA   CA  HA   sing N N 29  
ALA   C   O    doub N N 30  
ALA   C   OXT  sing N N 31  
ALA   CB  HB1  sing N N 32  
ALA   CB  HB2  sing N N 33  
ALA   CB  HB3  sing N N 34  
ALA   OXT HXT  sing N N 35  
ARG   N   CA   sing N N 36  
ARG   N   H    sing N N 37  
ARG   N   H2   sing N N 38  
ARG   CA  C    sing N N 39  
ARG   CA  CB   sing N N 40  
ARG   CA  HA   sing N N 41  
ARG   C   O    doub N N 42  
ARG   C   OXT  sing N N 43  
ARG   CB  CG   sing N N 44  
ARG   CB  HB2  sing N N 45  
ARG   CB  HB3  sing N N 46  
ARG   CG  CD   sing N N 47  
ARG   CG  HG2  sing N N 48  
ARG   CG  HG3  sing N N 49  
ARG   CD  NE   sing N N 50  
ARG   CD  HD2  sing N N 51  
ARG   CD  HD3  sing N N 52  
ARG   NE  CZ   sing N N 53  
ARG   NE  HE   sing N N 54  
ARG   CZ  NH1  sing N N 55  
ARG   CZ  NH2  doub N N 56  
ARG   NH1 HH11 sing N N 57  
ARG   NH1 HH12 sing N N 58  
ARG   NH2 HH21 sing N N 59  
ARG   NH2 HH22 sing N N 60  
ARG   OXT HXT  sing N N 61  
ASN   N   CA   sing N N 62  
ASN   N   H    sing N N 63  
ASN   N   H2   sing N N 64  
ASN   CA  C    sing N N 65  
ASN   CA  CB   sing N N 66  
ASN   CA  HA   sing N N 67  
ASN   C   O    doub N N 68  
ASN   C   OXT  sing N N 69  
ASN   CB  CG   sing N N 70  
ASN   CB  HB2  sing N N 71  
ASN   CB  HB3  sing N N 72  
ASN   CG  OD1  doub N N 73  
ASN   CG  ND2  sing N N 74  
ASN   ND2 HD21 sing N N 75  
ASN   ND2 HD22 sing N N 76  
ASN   OXT HXT  sing N N 77  
ASP   N   CA   sing N N 78  
ASP   N   H    sing N N 79  
ASP   N   H2   sing N N 80  
ASP   CA  C    sing N N 81  
ASP   CA  CB   sing N N 82  
ASP   CA  HA   sing N N 83  
ASP   C   O    doub N N 84  
ASP   C   OXT  sing N N 85  
ASP   CB  CG   sing N N 86  
ASP   CB  HB2  sing N N 87  
ASP   CB  HB3  sing N N 88  
ASP   CG  OD1  doub N N 89  
ASP   CG  OD2  sing N N 90  
ASP   OD2 HD2  sing N N 91  
ASP   OXT HXT  sing N N 92  
CYS   N   CA   sing N N 93  
CYS   N   H    sing N N 94  
CYS   N   H2   sing N N 95  
CYS   CA  C    sing N N 96  
CYS   CA  CB   sing N N 97  
CYS   CA  HA   sing N N 98  
CYS   C   O    doub N N 99  
CYS   C   OXT  sing N N 100 
CYS   CB  SG   sing N N 101 
CYS   CB  HB2  sing N N 102 
CYS   CB  HB3  sing N N 103 
CYS   SG  HG   sing N N 104 
CYS   OXT HXT  sing N N 105 
DMS   S   O    doub N N 106 
DMS   S   C1   sing N N 107 
DMS   S   C2   sing N N 108 
DMS   C1  H11  sing N N 109 
DMS   C1  H12  sing N N 110 
DMS   C1  H13  sing N N 111 
DMS   C2  H21  sing N N 112 
DMS   C2  H22  sing N N 113 
DMS   C2  H23  sing N N 114 
GLN   N   CA   sing N N 115 
GLN   N   H    sing N N 116 
GLN   N   H2   sing N N 117 
GLN   CA  C    sing N N 118 
GLN   CA  CB   sing N N 119 
GLN   CA  HA   sing N N 120 
GLN   C   O    doub N N 121 
GLN   C   OXT  sing N N 122 
GLN   CB  CG   sing N N 123 
GLN   CB  HB2  sing N N 124 
GLN   CB  HB3  sing N N 125 
GLN   CG  CD   sing N N 126 
GLN   CG  HG2  sing N N 127 
GLN   CG  HG3  sing N N 128 
GLN   CD  OE1  doub N N 129 
GLN   CD  NE2  sing N N 130 
GLN   NE2 HE21 sing N N 131 
GLN   NE2 HE22 sing N N 132 
GLN   OXT HXT  sing N N 133 
GLU   N   CA   sing N N 134 
GLU   N   H    sing N N 135 
GLU   N   H2   sing N N 136 
GLU   CA  C    sing N N 137 
GLU   CA  CB   sing N N 138 
GLU   CA  HA   sing N N 139 
GLU   C   O    doub N N 140 
GLU   C   OXT  sing N N 141 
GLU   CB  CG   sing N N 142 
GLU   CB  HB2  sing N N 143 
GLU   CB  HB3  sing N N 144 
GLU   CG  CD   sing N N 145 
GLU   CG  HG2  sing N N 146 
GLU   CG  HG3  sing N N 147 
GLU   CD  OE1  doub N N 148 
GLU   CD  OE2  sing N N 149 
GLU   OE2 HE2  sing N N 150 
GLU   OXT HXT  sing N N 151 
GLY   N   CA   sing N N 152 
GLY   N   H    sing N N 153 
GLY   N   H2   sing N N 154 
GLY   CA  C    sing N N 155 
GLY   CA  HA2  sing N N 156 
GLY   CA  HA3  sing N N 157 
GLY   C   O    doub N N 158 
GLY   C   OXT  sing N N 159 
GLY   OXT HXT  sing N N 160 
HIS   N   CA   sing N N 161 
HIS   N   H    sing N N 162 
HIS   N   H2   sing N N 163 
HIS   CA  C    sing N N 164 
HIS   CA  CB   sing N N 165 
HIS   CA  HA   sing N N 166 
HIS   C   O    doub N N 167 
HIS   C   OXT  sing N N 168 
HIS   CB  CG   sing N N 169 
HIS   CB  HB2  sing N N 170 
HIS   CB  HB3  sing N N 171 
HIS   CG  ND1  sing Y N 172 
HIS   CG  CD2  doub Y N 173 
HIS   ND1 CE1  doub Y N 174 
HIS   ND1 HD1  sing N N 175 
HIS   CD2 NE2  sing Y N 176 
HIS   CD2 HD2  sing N N 177 
HIS   CE1 NE2  sing Y N 178 
HIS   CE1 HE1  sing N N 179 
HIS   NE2 HE2  sing N N 180 
HIS   OXT HXT  sing N N 181 
HOH   O   H1   sing N N 182 
HOH   O   H2   sing N N 183 
ILE   N   CA   sing N N 184 
ILE   N   H    sing N N 185 
ILE   N   H2   sing N N 186 
ILE   CA  C    sing N N 187 
ILE   CA  CB   sing N N 188 
ILE   CA  HA   sing N N 189 
ILE   C   O    doub N N 190 
ILE   C   OXT  sing N N 191 
ILE   CB  CG1  sing N N 192 
ILE   CB  CG2  sing N N 193 
ILE   CB  HB   sing N N 194 
ILE   CG1 CD1  sing N N 195 
ILE   CG1 HG12 sing N N 196 
ILE   CG1 HG13 sing N N 197 
ILE   CG2 HG21 sing N N 198 
ILE   CG2 HG22 sing N N 199 
ILE   CG2 HG23 sing N N 200 
ILE   CD1 HD11 sing N N 201 
ILE   CD1 HD12 sing N N 202 
ILE   CD1 HD13 sing N N 203 
ILE   OXT HXT  sing N N 204 
LEU   N   CA   sing N N 205 
LEU   N   H    sing N N 206 
LEU   N   H2   sing N N 207 
LEU   CA  C    sing N N 208 
LEU   CA  CB   sing N N 209 
LEU   CA  HA   sing N N 210 
LEU   C   O    doub N N 211 
LEU   C   OXT  sing N N 212 
LEU   CB  CG   sing N N 213 
LEU   CB  HB2  sing N N 214 
LEU   CB  HB3  sing N N 215 
LEU   CG  CD1  sing N N 216 
LEU   CG  CD2  sing N N 217 
LEU   CG  HG   sing N N 218 
LEU   CD1 HD11 sing N N 219 
LEU   CD1 HD12 sing N N 220 
LEU   CD1 HD13 sing N N 221 
LEU   CD2 HD21 sing N N 222 
LEU   CD2 HD22 sing N N 223 
LEU   CD2 HD23 sing N N 224 
LEU   OXT HXT  sing N N 225 
LYS   N   CA   sing N N 226 
LYS   N   H    sing N N 227 
LYS   N   H2   sing N N 228 
LYS   CA  C    sing N N 229 
LYS   CA  CB   sing N N 230 
LYS   CA  HA   sing N N 231 
LYS   C   O    doub N N 232 
LYS   C   OXT  sing N N 233 
LYS   CB  CG   sing N N 234 
LYS   CB  HB2  sing N N 235 
LYS   CB  HB3  sing N N 236 
LYS   CG  CD   sing N N 237 
LYS   CG  HG2  sing N N 238 
LYS   CG  HG3  sing N N 239 
LYS   CD  CE   sing N N 240 
LYS   CD  HD2  sing N N 241 
LYS   CD  HD3  sing N N 242 
LYS   CE  NZ   sing N N 243 
LYS   CE  HE2  sing N N 244 
LYS   CE  HE3  sing N N 245 
LYS   NZ  HZ1  sing N N 246 
LYS   NZ  HZ2  sing N N 247 
LYS   NZ  HZ3  sing N N 248 
LYS   OXT HXT  sing N N 249 
MET   N   CA   sing N N 250 
MET   N   H    sing N N 251 
MET   N   H2   sing N N 252 
MET   CA  C    sing N N 253 
MET   CA  CB   sing N N 254 
MET   CA  HA   sing N N 255 
MET   C   O    doub N N 256 
MET   C   OXT  sing N N 257 
MET   CB  CG   sing N N 258 
MET   CB  HB2  sing N N 259 
MET   CB  HB3  sing N N 260 
MET   CG  SD   sing N N 261 
MET   CG  HG2  sing N N 262 
MET   CG  HG3  sing N N 263 
MET   SD  CE   sing N N 264 
MET   CE  HE1  sing N N 265 
MET   CE  HE2  sing N N 266 
MET   CE  HE3  sing N N 267 
MET   OXT HXT  sing N N 268 
PHE   N   CA   sing N N 269 
PHE   N   H    sing N N 270 
PHE   N   H2   sing N N 271 
PHE   CA  C    sing N N 272 
PHE   CA  CB   sing N N 273 
PHE   CA  HA   sing N N 274 
PHE   C   O    doub N N 275 
PHE   C   OXT  sing N N 276 
PHE   CB  CG   sing N N 277 
PHE   CB  HB2  sing N N 278 
PHE   CB  HB3  sing N N 279 
PHE   CG  CD1  doub Y N 280 
PHE   CG  CD2  sing Y N 281 
PHE   CD1 CE1  sing Y N 282 
PHE   CD1 HD1  sing N N 283 
PHE   CD2 CE2  doub Y N 284 
PHE   CD2 HD2  sing N N 285 
PHE   CE1 CZ   doub Y N 286 
PHE   CE1 HE1  sing N N 287 
PHE   CE2 CZ   sing Y N 288 
PHE   CE2 HE2  sing N N 289 
PHE   CZ  HZ   sing N N 290 
PHE   OXT HXT  sing N N 291 
PRO   N   CA   sing N N 292 
PRO   N   CD   sing N N 293 
PRO   N   H    sing N N 294 
PRO   CA  C    sing N N 295 
PRO   CA  CB   sing N N 296 
PRO   CA  HA   sing N N 297 
PRO   C   O    doub N N 298 
PRO   C   OXT  sing N N 299 
PRO   CB  CG   sing N N 300 
PRO   CB  HB2  sing N N 301 
PRO   CB  HB3  sing N N 302 
PRO   CG  CD   sing N N 303 
PRO   CG  HG2  sing N N 304 
PRO   CG  HG3  sing N N 305 
PRO   CD  HD2  sing N N 306 
PRO   CD  HD3  sing N N 307 
PRO   OXT HXT  sing N N 308 
SER   N   CA   sing N N 309 
SER   N   H    sing N N 310 
SER   N   H2   sing N N 311 
SER   CA  C    sing N N 312 
SER   CA  CB   sing N N 313 
SER   CA  HA   sing N N 314 
SER   C   O    doub N N 315 
SER   C   OXT  sing N N 316 
SER   CB  OG   sing N N 317 
SER   CB  HB2  sing N N 318 
SER   CB  HB3  sing N N 319 
SER   OG  HG   sing N N 320 
SER   OXT HXT  sing N N 321 
SO4   S   O1   doub N N 322 
SO4   S   O2   doub N N 323 
SO4   S   O3   sing N N 324 
SO4   S   O4   sing N N 325 
THR   N   CA   sing N N 326 
THR   N   H    sing N N 327 
THR   N   H2   sing N N 328 
THR   CA  C    sing N N 329 
THR   CA  CB   sing N N 330 
THR   CA  HA   sing N N 331 
THR   C   O    doub N N 332 
THR   C   OXT  sing N N 333 
THR   CB  OG1  sing N N 334 
THR   CB  CG2  sing N N 335 
THR   CB  HB   sing N N 336 
THR   OG1 HG1  sing N N 337 
THR   CG2 HG21 sing N N 338 
THR   CG2 HG22 sing N N 339 
THR   CG2 HG23 sing N N 340 
THR   OXT HXT  sing N N 341 
TRP   N   CA   sing N N 342 
TRP   N   H    sing N N 343 
TRP   N   H2   sing N N 344 
TRP   CA  C    sing N N 345 
TRP   CA  CB   sing N N 346 
TRP   CA  HA   sing N N 347 
TRP   C   O    doub N N 348 
TRP   C   OXT  sing N N 349 
TRP   CB  CG   sing N N 350 
TRP   CB  HB2  sing N N 351 
TRP   CB  HB3  sing N N 352 
TRP   CG  CD1  doub Y N 353 
TRP   CG  CD2  sing Y N 354 
TRP   CD1 NE1  sing Y N 355 
TRP   CD1 HD1  sing N N 356 
TRP   CD2 CE2  doub Y N 357 
TRP   CD2 CE3  sing Y N 358 
TRP   NE1 CE2  sing Y N 359 
TRP   NE1 HE1  sing N N 360 
TRP   CE2 CZ2  sing Y N 361 
TRP   CE3 CZ3  doub Y N 362 
TRP   CE3 HE3  sing N N 363 
TRP   CZ2 CH2  doub Y N 364 
TRP   CZ2 HZ2  sing N N 365 
TRP   CZ3 CH2  sing Y N 366 
TRP   CZ3 HZ3  sing N N 367 
TRP   CH2 HH2  sing N N 368 
TRP   OXT HXT  sing N N 369 
TYR   N   CA   sing N N 370 
TYR   N   H    sing N N 371 
TYR   N   H2   sing N N 372 
TYR   CA  C    sing N N 373 
TYR   CA  CB   sing N N 374 
TYR   CA  HA   sing N N 375 
TYR   C   O    doub N N 376 
TYR   C   OXT  sing N N 377 
TYR   CB  CG   sing N N 378 
TYR   CB  HB2  sing N N 379 
TYR   CB  HB3  sing N N 380 
TYR   CG  CD1  doub Y N 381 
TYR   CG  CD2  sing Y N 382 
TYR   CD1 CE1  sing Y N 383 
TYR   CD1 HD1  sing N N 384 
TYR   CD2 CE2  doub Y N 385 
TYR   CD2 HD2  sing N N 386 
TYR   CE1 CZ   doub Y N 387 
TYR   CE1 HE1  sing N N 388 
TYR   CE2 CZ   sing Y N 389 
TYR   CE2 HE2  sing N N 390 
TYR   CZ  OH   sing N N 391 
TYR   OH  HH   sing N N 392 
TYR   OXT HXT  sing N N 393 
VAL   N   CA   sing N N 394 
VAL   N   H    sing N N 395 
VAL   N   H2   sing N N 396 
VAL   CA  C    sing N N 397 
VAL   CA  CB   sing N N 398 
VAL   CA  HA   sing N N 399 
VAL   C   O    doub N N 400 
VAL   C   OXT  sing N N 401 
VAL   CB  CG1  sing N N 402 
VAL   CB  CG2  sing N N 403 
VAL   CB  HB   sing N N 404 
VAL   CG1 HG11 sing N N 405 
VAL   CG1 HG12 sing N N 406 
VAL   CG1 HG13 sing N N 407 
VAL   CG2 HG21 sing N N 408 
VAL   CG2 HG22 sing N N 409 
VAL   CG2 HG23 sing N N 410 
VAL   OXT HXT  sing N N 411 
# 
_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_1002330 
_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' 
# 
_pdbx_initial_refinement_model.accession_code   8POA 
_pdbx_initial_refinement_model.details          ? 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.type             'experimental model' 
# 
_atom_sites.entry_id                    7HZM 
_atom_sites.fract_transf_matrix[1][1]   0.011565 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000975 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017527 
_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]   0.030997 
_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  
F  
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   ? 18.248 6.697   24.888 1.00 20.87  ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 19.354 6.915   23.919 1.00 20.30  ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 19.363 5.756   22.932 1.00 19.58  ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 18.633 4.754   23.191 1.00 18.66  ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 20.679 7.004   24.603 1.00 22.25  ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 20.936 5.808   25.326 1.00 24.71  ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 20.233 5.841   21.927 1.00 16.79  ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 20.382 4.787   20.917 1.00 14.64  ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 20.786 5.349   19.576 1.00 12.96  ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 20.409 6.511   19.256 1.00 12.57  ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 21.521 4.564   18.817 1.00 12.27  ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 21.992 4.926   17.466 1.00 11.66  ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 21.872 3.739   16.494 1.00 12.49  ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 21.747 2.574   16.982 1.00 15.03  ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.433 5.405   17.560 1.00 12.46  ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 21.876 4.036   15.194 1.00 13.08  ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.043 3.072   14.058 1.00 14.36  ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 23.499 3.227   13.612 1.00 15.80  ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.073 4.272   13.891 1.00 15.63  ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.061 3.381   12.895 1.00 13.72  ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 19.620 3.584   13.385 1.00 14.14  ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.111 2.372   11.754 1.00 14.37  ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 18.722 4.041   12.274 1.00 14.91  ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.063 2.254   12.887 1.00 17.84  ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 25.488 2.229   12.478 1.00 22.15  ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 25.538 1.604   11.083 1.00 21.42  ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 25.766 0.389   10.942 1.00 27.70  ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 26.291 1.508   13.564 1.00 21.81  ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 26.543 2.311   14.817 1.00 22.01  ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 27.352 3.439   14.814 1.00 22.04  ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 26.013 1.908   16.026 1.00 22.39  ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 27.583 4.159   15.977 1.00 22.35  ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 26.201 2.631   17.187 1.00 24.37  ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 26.995 3.765   17.159 1.00 22.54  ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 27.169 4.449   18.312 1.00 26.39  ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 25.153 2.376   10.071 1.00 25.21  ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 25.176 1.881   8.665  1.00 23.75  ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 26.541 2.269   8.096  1.00 24.49  ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 26.688 3.424   7.593  1.00 22.31  ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 23.957 2.339   7.835  1.00 24.43  ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 23.794 3.848   7.777  1.00 24.02  ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 23.976 1.733   6.438  1.00 24.27  ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 27.513 1.359   8.328  1.00 27.56  ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 28.910 1.410   7.855  1.00 26.38  ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 29.811 2.149   8.826  1.00 24.15  ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 29.998 1.672   9.980  1.00 22.06  ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.372 3.270   8.387  1.00 21.93  ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.155 4.173   9.275  1.00 23.21  ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.291 5.384   9.626  1.00 23.13  ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.878 6.450   9.881  1.00 18.88  ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.484 4.615   8.661  1.00 22.78  ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.475 3.481   8.582  1.00 26.24  ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.285 3.309   9.486  1.00 25.74  ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.393 2.706   7.514  1.00 27.02  ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 28.960 5.217   9.615  1.00 25.04  ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 27.988 6.291   9.952  1.00 26.32  ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.321 5.925   11.275 1.00 25.25  ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.164 4.739   11.644 1.00 26.86  ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.924 6.530   8.872  1.00 28.26  ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.397 6.986   7.513  1.00 32.94  ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 28.087 8.177   7.347  1.00 36.02  ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.096 6.253   6.373  1.00 36.14  ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.499 8.607   6.093  1.00 37.12  ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.497 6.669   5.114  1.00 38.04  ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 28.205 7.848   4.974  1.00 39.26  ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.605 8.251   3.735  1.00 41.16  ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 26.950 6.961   12.008 1.00 21.42  ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.222 6.833   13.280 1.00 18.50  ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 24.964 7.674   13.130 1.00 15.82  ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.112 8.861   12.883 1.00 15.78  ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.114 7.329   14.409 1.00 18.62  ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.363 7.697   15.667 1.00 20.39  ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.373 7.838   16.770 1.00 20.28  ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 26.942 8.881   17.669 1.00 20.60  ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 26.230 8.704   18.762 1.00 19.84  ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 25.818 7.496   19.134 1.00 21.23  ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 25.903 9.754   19.487 1.00 20.34  ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 23.779 7.077   13.261 1.00 12.22  ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.503 7.821   13.054 1.00 10.27  ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 21.812 7.988   14.389 1.00 9.14   ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 21.599 7.000   15.070 1.00 8.85   ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.540 7.102   12.115 1.00 9.87   ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.368 8.027   11.820 1.00 9.12   ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.250 6.639   10.848 1.00 10.65  ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 21.563 9.238   14.757 1.00 7.54   ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 21.073 9.570   16.115 1.00 7.14   ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 19.913 10.556  16.035 1.00 6.92   ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 19.761 11.244  15.006 1.00 6.98   ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 22.174 10.163  17.009 1.00 8.11   ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 23.126 9.069   17.443 1.00 8.83   ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 22.925 11.352  16.410 1.00 8.69   ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 19.153 10.635  17.113 1.00 7.03   ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 18.179 11.741  17.250 1.00 7.85   ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 18.967 13.070  17.222 1.00 8.04   ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 19.959 13.178  17.984 1.00 8.28   ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.422 11.641  18.566 1.00 7.68   ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 16.623 10.347  18.649 1.00 7.58   ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.087 9.334   19.173 1.00 8.15   ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 15.456 10.392  18.093 1.00 8.11   ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 18.567 14.056  16.382 1.00 10.25  ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 19.254 15.393  16.413 1.00 11.30  ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 19.392 15.947  17.867 1.00 12.82  ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 20.478 16.447  18.199 1.00 12.33  ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 18.549 16.390  15.491 1.00 12.76  ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.389 17.633  15.194 1.00 12.89  ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 18.556 18.642  14.437 1.00 14.56  ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.215 19.914  14.128 1.00 15.79  ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.316 20.956  14.965 1.00 15.80  ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 18.904 20.894  16.217 1.00 17.66  ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 19.881 22.082  14.549 1.00 15.54  ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 18.441 15.762  18.804 1.00 14.21  ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 18.525 16.321  20.198 1.00 14.69  ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 19.484 15.586  21.163 1.00 15.82  ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 19.771 16.128  22.253 1.00 16.97  ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 17.137 16.436  20.879 1.00 16.12  ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 16.542 15.151  21.349 1.00 16.81  ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 15.667 14.446  20.575 1.00 19.17  ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 16.705 14.445  22.490 1.00 17.71  ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 15.283 13.367  21.233 1.00 17.14  ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 15.944 13.316  22.398 1.00 18.25  ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 19.943 14.369  20.875 1.00 13.71  ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 20.929 13.640  21.718 1.00 15.89  ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 22.311 13.703  21.087 1.00 14.28  ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 23.257 13.056  21.620 1.00 17.62  ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 20.466 12.195  21.879 1.00 15.84  ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 19.133 12.060  22.599 1.00 16.01  ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 18.674 10.606  22.649 1.00 15.75  ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 19.206 12.657  24.001 1.00 15.94  ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 22.425 14.378  19.943 1.00 14.20  ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 23.686 14.483  19.175 1.00 14.20  ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 24.717 15.144  20.102 1.00 14.74  ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 24.341 16.138  20.785 1.00 15.84  ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 23.492 15.263  17.880 1.00 12.99  ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 25.918 14.579  20.136 1.00 16.95  ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 27.056 14.989  20.996 1.00 18.44  ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 27.889 16.048  20.264 1.00 18.28  ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 27.685 16.274  19.046 1.00 14.68  ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 27.916 13.762  21.325 1.00 19.67  ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 28.446 13.282  20.093 1.00 21.90  ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 27.144 12.662  22.030 1.00 20.02  ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 28.821 16.695  20.968 1.00 20.15  ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 29.843 17.566  20.336 1.00 20.69  ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 30.590 16.783  19.246 1.00 18.90  ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 30.738 17.320  18.141 1.00 15.26  ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 30.824 18.177  21.347 1.00 22.29  ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 31.991 18.799  20.653 1.00 23.08  ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 31.874 19.995  19.978 1.00 23.13  ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 33.235 18.336  20.391 1.00 23.31  ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 33.013 20.279  19.382 1.00 21.49  ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 33.874 19.287  19.632 1.00 22.36  ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 31.025 15.539  19.517 1.00 18.76  ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 31.734 14.700  18.520 1.00 21.31  ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 30.837 14.541  17.284 1.00 16.30  ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 31.325 14.661  16.158 1.00 15.58  ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 32.131 13.335  19.090 1.00 22.37  ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 33.146 12.615  18.219 1.00 26.32  ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.347 12.687  18.479 1.00 27.23  ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 32.693 11.921  17.182 1.00 24.82  ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 29.533 14.306  17.492 1.00 16.31  ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 28.597 14.118  16.362 1.00 15.18  ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 28.607 15.388  15.524 1.00 12.76  ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 28.708 15.308  14.338 1.00 10.48  ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 27.159 13.863  16.812 1.00 14.03  ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 26.883 12.475  17.380 1.00 13.41  ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 27.478 11.490  16.860 1.00 15.64  ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 26.130 12.381  18.354 1.00 14.42  ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 28.485 16.549  16.173 1.00 12.19  ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.503 17.844  15.450 1.00 11.62  ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 29.913 18.141  14.904 1.00 12.16  ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 29.943 18.660  13.858 1.00 10.47  ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 27.988 18.984  16.331 1.00 11.70  ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 26.500 19.099  16.486 1.00 10.98  ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 25.781 18.739  17.584 1.00 11.99  ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 25.564 19.627  15.532 1.00 11.44  ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 24.464 19.045  17.387 1.00 10.83  ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 24.287 19.535  16.121 1.00 10.71  ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 25.679 20.178  14.268 1.00 11.30  ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 23.148 20.072  15.524 1.00 11.42  ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.538 20.613  13.633 1.00 13.12  ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 23.292 20.541  14.244 1.00 12.50  ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 30.998 17.618  15.489 1.00 12.57  ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.396 17.905  15.076 1.00 15.24  ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.795 16.903  13.999 1.00 16.12  ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.849 17.069  13.365 1.00 17.78  ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 33.303 17.845  16.278 1.00 15.95  ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 31.956 15.880  13.790 1.00 18.05  ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 32.127 14.933  12.654 1.00 19.15  ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.777 14.743  11.955 1.00 18.06  ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.390 13.559  11.768 1.00 17.54  ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.713 13.601  13.123 1.00 21.10  ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 34.003 13.752  13.905 1.00 21.43  ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 35.092 13.537  13.368 1.00 24.05  ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 33.888 14.076  15.182 1.00 23.95  ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 30.122 15.834  11.531 1.00 18.32  ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.734 15.843  10.985 1.00 19.62  ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.755 15.359  9.533  1.00 21.47  ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.854 15.411  8.933  1.00 19.96  ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 28.153 17.259  11.078 1.00 18.70  ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.765 17.452  10.455 1.00 19.12  ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.702 16.673  11.215 1.00 18.71  ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.367 18.911  10.384 1.00 20.47  ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.589 14.907  9.026  1.00 24.50  ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.329 14.471  7.618  1.00 26.74  ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 26.068 15.180  7.102  1.00 28.87  ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 26.153 15.780  6.027  1.00 30.99  ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.210 12.937  7.502  1.00 28.75  ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 27.049 12.465  6.064  1.00 28.94  ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 28.377 12.222  8.149  1.00 27.48  ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 24.938 15.099  7.822  1.00 25.06  ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 23.644 15.756  7.486  1.00 24.59  ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 22.779 15.813  8.755  1.00 20.67  ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 23.007 14.895  9.606  1.00 16.44  ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 22.967 14.992  6.330  1.00 25.71  ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.490 15.199  6.202  1.00 28.34  ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 20.838 16.178  5.508  1.00 28.30  ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.465 14.368  6.777  1.00 27.93  ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.482 16.032  5.633  1.00 29.61  ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.223 14.933  6.409  1.00 28.42  ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.481 13.227  7.590  1.00 28.15  ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 18.009 14.369  6.804  1.00 30.30  ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.282 12.672  7.977  1.00 28.79  ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 18.065 13.242  7.593  1.00 28.24  ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 21.853 16.791  8.855  1.00 19.23  ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 20.961 17.027  10.038 1.00 21.32  ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 19.640 17.776  9.712  1.00 20.55  ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 19.679 18.713  8.886  1.00 20.26  ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 21.746 17.795  11.102 1.00 21.91  ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.177 19.203  10.676 1.00 21.87  ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.132 20.310  10.761 1.00 23.46  ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 21.325 21.341  10.082 1.00 26.03  ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 20.149 20.177  11.521 1.00 24.31  ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 18.515 17.472  10.406 1.00 18.59  ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.173 18.111  10.198 1.00 19.36  ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.342 18.167  11.495 1.00 19.26  ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 15.950 17.118  12.041 1.00 18.55  ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.424 17.383  9.085  1.00 19.51  ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.064 17.952  8.702  1.00 21.44  ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 14.359 18.529  9.576  1.00 22.33  ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 14.706 17.771  7.547  1.00 23.89  ? 35  ASP   A OD2 1 
ATOM   240  N  N   A SER   A 1 30  ? 16.056 19.381  11.971 0.22 17.91  ? 36  SER   A N   1 
ATOM   241  N  N   B SER   A 1 30  ? 16.058 19.387  11.952 0.22 18.51  ? 36  SER   A N   1 
ATOM   242  C  CA  A SER   A 1 30  ? 15.334 19.640  13.246 0.22 17.97  ? 36  SER   A CA  1 
ATOM   243  C  CA  B SER   A 1 30  ? 15.339 19.698  13.217 0.22 18.90  ? 36  SER   A CA  1 
ATOM   244  C  C   A SER   A 1 30  ? 13.877 19.169  13.160 0.22 17.97  ? 36  SER   A C   1 
ATOM   245  C  C   B SER   A 1 30  ? 13.887 19.203  13.161 0.22 18.50  ? 36  SER   A C   1 
ATOM   246  O  O   A SER   A 1 30  ? 13.394 18.596  14.162 0.22 17.69  ? 36  SER   A O   1 
ATOM   247  O  O   B SER   A 1 30  ? 13.423 18.634  14.175 0.22 18.17  ? 36  SER   A O   1 
ATOM   248  C  CB  A SER   A 1 30  ? 15.398 21.091  13.639 0.22 17.62  ? 36  SER   A CB  1 
ATOM   249  C  CB  B SER   A 1 30  ? 15.407 21.176  13.506 0.22 19.05  ? 36  SER   A CB  1 
ATOM   250  O  OG  A SER   A 1 30  ? 14.581 21.328  14.779 0.22 17.87  ? 36  SER   A OG  1 
ATOM   251  O  OG  B SER   A 1 30  ? 15.126 21.933  12.338 0.22 20.43  ? 36  SER   A OG  1 
ATOM   252  N  N   . SER   A 1 31  ? 13.206 19.419  12.030 1.00 18.93  ? 37  SER   A N   1 
ATOM   253  C  CA  . SER   A 1 31  ? 11.806 18.977  11.799 1.00 20.17  ? 37  SER   A CA  1 
ATOM   254  C  C   . SER   A 1 31  ? 11.675 17.450  11.922 1.00 18.38  ? 37  SER   A C   1 
ATOM   255  O  O   . SER   A 1 31  ? 10.586 17.008  12.280 1.00 19.03  ? 37  SER   A O   1 
ATOM   256  C  CB  . SER   A 1 31  ? 11.276 19.440  10.470 1.00 22.18  ? 37  SER   A CB  1 
ATOM   257  O  OG  . SER   A 1 31  ? 12.007 18.878  9.396  1.00 26.12  ? 37  SER   A OG  1 
ATOM   258  N  N   . ARG   A 1 32  ? 12.738 16.672  11.642 1.00 17.94  ? 38  ARG   A N   1 
ATOM   259  C  CA  . ARG   A 1 32  ? 12.748 15.186  11.705 1.00 18.11  ? 38  ARG   A CA  1 
ATOM   260  C  C   . ARG   A 1 32  ? 13.455 14.679  12.969 1.00 17.58  ? 38  ARG   A C   1 
ATOM   261  O  O   . ARG   A 1 32  ? 13.320 13.461  13.254 1.00 18.18  ? 38  ARG   A O   1 
ATOM   262  C  CB  . ARG   A 1 32  ? 13.477 14.611  10.486 1.00 15.29  ? 38  ARG   A CB  1 
ATOM   263  C  CG  . ARG   A 1 32  ? 12.921 15.045  9.137  1.00 17.20  ? 38  ARG   A CG  1 
ATOM   264  C  CD  . ARG   A 1 32  ? 13.573 14.359  7.956  1.00 16.59  ? 38  ARG   A CD  1 
ATOM   265  N  NE  . ARG   A 1 32  ? 13.443 12.918  8.030  1.00 17.84  ? 38  ARG   A NE  1 
ATOM   266  C  CZ  . ARG   A 1 32  ? 13.575 12.088  7.009  1.00 18.43  ? 38  ARG   A CZ  1 
ATOM   267  N  NH1 . ARG   A 1 32  ? 13.785 12.545  5.784  1.00 20.52  ? 38  ARG   A NH1 1 
ATOM   268  N  NH2 . ARG   A 1 32  ? 13.390 10.800  7.227  1.00 18.02  ? 38  ARG   A NH2 1 
ATOM   269  N  N   . ASP   A 1 33  ? 14.195 15.521  13.699 1.00 17.50  ? 39  ASP   A N   1 
ATOM   270  C  CA  . ASP   A 1 33  ? 15.046 15.062  14.823 1.00 15.40  ? 39  ASP   A CA  1 
ATOM   271  C  C   . ASP   A 1 33  ? 16.067 14.026  14.333 1.00 14.26  ? 39  ASP   A C   1 
ATOM   272  O  O   . ASP   A 1 33  ? 16.238 13.084  15.091 1.00 14.18  ? 39  ASP   A O   1 
ATOM   273  C  CB  . ASP   A 1 33  ? 14.209 14.358  15.903 1.00 14.11  ? 39  ASP   A CB  1 
ATOM   274  C  CG  . ASP   A 1 33  ? 14.851 14.159  17.268 1.00 16.50  ? 39  ASP   A CG  1 
ATOM   275  O  OD1 . ASP   A 1 33  ? 15.691 14.947  17.641 1.00 13.82  ? 39  ASP   A OD1 1 
ATOM   276  O  OD2 . ASP   A 1 33  ? 14.474 13.210  17.982 1.00 14.74  ? 39  ASP   A OD2 1 
ATOM   277  N  N   . LEU   A 1 34  ? 16.659 14.133  13.127 1.00 12.24  ? 40  LEU   A N   1 
ATOM   278  C  CA  . LEU   A 1 34  ? 17.759 13.220  12.676 1.00 12.25  ? 40  LEU   A CA  1 
ATOM   279  C  C   . LEU   A 1 34  ? 19.089 13.980  12.533 1.00 11.05  ? 40  LEU   A C   1 
ATOM   280  O  O   . LEU   A 1 34  ? 19.080 15.159  12.044 1.00 14.94  ? 40  LEU   A O   1 
ATOM   281  C  CB  . LEU   A 1 34  ? 17.436 12.518  11.353 1.00 12.16  ? 40  LEU   A CB  1 
ATOM   282  C  CG  . LEU   A 1 34  ? 16.448 11.335  11.428 1.00 14.02  ? 40  LEU   A CG  1 
ATOM   283  C  CD1 . LEU   A 1 34  ? 16.279 10.683  10.071 1.00 14.87  ? 40  LEU   A CD1 1 
ATOM   284  C  CD2 . LEU   A 1 34  ? 16.834 10.294  12.482 1.00 14.64  ? 40  LEU   A CD2 1 
ATOM   285  N  N   . LEU   A 1 35  ? 20.182 13.267  12.815 1.00 9.54   ? 41  LEU   A N   1 
ATOM   286  C  CA  . LEU   A 1 35  ? 21.583 13.711  12.568 1.00 9.44   ? 41  LEU   A CA  1 
ATOM   287  C  C   . LEU   A 1 35  ? 22.454 12.471  12.320 1.00 9.72   ? 41  LEU   A C   1 
ATOM   288  O  O   . LEU   A 1 35  ? 22.255 11.414  13.023 1.00 10.46  ? 41  LEU   A O   1 
ATOM   289  C  CB  . LEU   A 1 35  ? 22.086 14.526  13.767 1.00 8.05   ? 41  LEU   A CB  1 
ATOM   290  C  CG  . LEU   A 1 35  ? 23.480 15.144  13.621 1.00 8.43   ? 41  LEU   A CG  1 
ATOM   291  C  CD1 . LEU   A 1 35  ? 23.575 16.495  14.283 1.00 8.19   ? 41  LEU   A CD1 1 
ATOM   292  C  CD2 . LEU   A 1 35  ? 24.544 14.225  14.149 1.00 8.56   ? 41  LEU   A CD2 1 
ATOM   293  N  N   . VAL   A 1 36  ? 23.335 12.525  11.305 1.00 11.87  ? 42  VAL   A N   1 
ATOM   294  C  CA  . VAL   A 1 36  ? 24.339 11.437  11.051 1.00 12.47  ? 42  VAL   A CA  1 
ATOM   295  C  C   . VAL   A 1 36  ? 25.767 11.999  11.155 1.00 11.76  ? 42  VAL   A C   1 
ATOM   296  O  O   . VAL   A 1 36  ? 26.001 13.095  10.597 1.00 16.19  ? 42  VAL   A O   1 
ATOM   297  C  CB  . VAL   A 1 36  ? 24.138 10.716  9.704  1.00 12.18  ? 42  VAL   A CB  1 
ATOM   298  C  CG1 . VAL   A 1 36  ? 25.161 9.602   9.486  1.00 12.52  ? 42  VAL   A CG1 1 
ATOM   299  C  CG2 . VAL   A 1 36  ? 22.704 10.182  9.626  1.00 12.20  ? 42  VAL   A CG2 1 
ATOM   300  N  N   . SER   A 1 37  ? 26.607 11.283  11.896 1.00 13.52  ? 43  SER   A N   1 
ATOM   301  C  CA  . SER   A 1 37  ? 28.048 11.574  12.164 1.00 15.84  ? 43  SER   A CA  1 
ATOM   302  C  C   . SER   A 1 37  ? 28.933 10.392  11.724 1.00 16.70  ? 43  SER   A C   1 
ATOM   303  O  O   . SER   A 1 37  ? 28.428 9.227   11.572 1.00 14.60  ? 43  SER   A O   1 
ATOM   304  C  CB  . SER   A 1 37  ? 28.262 11.885  13.617 1.00 15.30  ? 43  SER   A CB  1 
ATOM   305  O  OG  . SER   A 1 37  ? 28.033 10.766  14.459 1.00 15.71  ? 43  SER   A OG  1 
ATOM   306  N  N   . SER   A 1 38  ? 30.222 10.678  11.507 1.00 19.84  ? 44  SER   A N   1 
ATOM   307  C  CA  . SER   A 1 38  ? 31.227 9.729   10.948 1.00 23.29  ? 44  SER   A CA  1 
ATOM   308  C  C   . SER   A 1 38  ? 31.838 8.868   12.062 1.00 26.85  ? 44  SER   A C   1 
ATOM   309  O  O   . SER   A 1 38  ? 31.998 9.339   13.224 1.00 25.38  ? 44  SER   A O   1 
ATOM   310  C  CB  . SER   A 1 38  ? 32.289 10.450  10.155 1.00 25.23  ? 44  SER   A CB  1 
ATOM   311  O  OG  . SER   A 1 38  ? 32.979 11.375  10.985 1.00 25.47  ? 44  SER   A OG  1 
ATOM   312  N  N   . THR   A 1 39  ? 32.204 7.636   11.705 1.00 31.11  ? 45  THR   A N   1 
ATOM   313  C  CA  . THR   A 1 39  ? 32.855 6.665   12.614 1.00 35.78  ? 45  THR   A CA  1 
ATOM   314  C  C   . THR   A 1 39  ? 34.112 6.135   11.915 1.00 38.01  ? 45  THR   A C   1 
ATOM   315  O  O   . THR   A 1 39  ? 34.256 6.340   10.690 1.00 38.25  ? 45  THR   A O   1 
ATOM   316  C  CB  . THR   A 1 39  ? 31.852 5.602   13.091 1.00 36.73  ? 45  THR   A CB  1 
ATOM   317  O  OG1 . THR   A 1 39  ? 31.798 4.497   12.188 1.00 36.58  ? 45  THR   A OG1 1 
ATOM   318  C  CG2 . THR   A 1 39  ? 30.454 6.157   13.261 1.00 36.17  ? 45  THR   A CG2 1 
ATOM   319  N  N   . THR   A 1 40  ? 35.012 5.549   12.699 1.00 44.57  ? 46  THR   A N   1 
ATOM   320  C  CA  . THR   A 1 40  ? 36.350 5.070   12.262 1.00 47.98  ? 46  THR   A CA  1 
ATOM   321  C  C   . THR   A 1 40  ? 36.319 3.541   12.132 1.00 51.18  ? 46  THR   A C   1 
ATOM   322  O  O   . THR   A 1 40  ? 37.073 3.010   11.292 1.00 53.50  ? 46  THR   A O   1 
ATOM   323  C  CB  . THR   A 1 40  ? 37.429 5.590   13.221 1.00 48.12  ? 46  THR   A CB  1 
ATOM   324  O  OG1 . THR   A 1 40  ? 37.071 5.249   14.562 1.00 48.37  ? 46  THR   A OG1 1 
ATOM   325  C  CG2 . THR   A 1 40  ? 37.609 7.088   13.127 1.00 48.98  ? 46  THR   A CG2 1 
ATOM   326  N  N   . ALA   A 1 41  ? 35.479 2.876   12.935 1.00 52.80  ? 47  ALA   A N   1 
ATOM   327  C  CA  . ALA   A 1 41  ? 35.148 1.433   12.857 1.00 53.02  ? 47  ALA   A CA  1 
ATOM   328  C  C   . ALA   A 1 41  ? 33.713 1.269   12.343 1.00 54.22  ? 47  ALA   A C   1 
ATOM   329  O  O   . ALA   A 1 41  ? 32.832 2.018   12.824 1.00 50.70  ? 47  ALA   A O   1 
ATOM   330  C  CB  . ALA   A 1 41  ? 35.312 0.798   14.214 1.00 52.80  ? 47  ALA   A CB  1 
ATOM   331  N  N   . GLN   A 1 42  ? 33.487 0.310   11.434 1.00 55.92  ? 48  GLN   A N   1 
ATOM   332  C  CA  . GLN   A 1 42  ? 32.181 0.098   10.747 1.00 54.64  ? 48  GLN   A CA  1 
ATOM   333  C  C   . GLN   A 1 42  ? 31.152 -0.474  11.731 1.00 54.12  ? 48  GLN   A C   1 
ATOM   334  O  O   . GLN   A 1 42  ? 31.548 -0.887  12.841 1.00 52.76  ? 48  GLN   A O   1 
ATOM   335  C  CB  . GLN   A 1 42  ? 32.328 -0.805  9.521  1.00 57.58  ? 48  GLN   A CB  1 
ATOM   336  C  CG  . GLN   A 1 42  ? 32.725 -0.048  8.262  1.00 57.63  ? 48  GLN   A CG  1 
ATOM   337  C  CD  . GLN   A 1 42  ? 32.641 -0.903  7.022  1.00 60.85  ? 48  GLN   A CD  1 
ATOM   338  O  OE1 . GLN   A 1 42  ? 33.275 -1.953  6.931  1.00 65.94  ? 48  GLN   A OE1 1 
ATOM   339  N  NE2 . GLN   A 1 42  ? 31.860 -0.459  6.049  1.00 60.50  ? 48  GLN   A NE2 1 
ATOM   340  N  N   . GLY   A 1 43  ? 29.876 -0.484  11.323 1.00 53.10  ? 49  GLY   A N   1 
ATOM   341  C  CA  . GLY   A 1 43  ? 28.721 -0.892  12.149 1.00 51.41  ? 49  GLY   A CA  1 
ATOM   342  C  C   . GLY   A 1 43  ? 28.155 -2.236  11.723 1.00 49.05  ? 49  GLY   A C   1 
ATOM   343  O  O   . GLY   A 1 43  ? 28.776 -2.895  10.876 1.00 46.37  ? 49  GLY   A O   1 
ATOM   344  N  N   . CYS   A 1 44  ? 26.991 -2.613  12.261 1.00 48.75  ? 50  CYS   A N   1 
ATOM   345  C  CA  . CYS   A 1 44  ? 26.379 -3.958  12.081 1.00 47.33  ? 50  CYS   A CA  1 
ATOM   346  C  C   . CYS   A 1 44  ? 24.967 -3.882  11.455 1.00 43.49  ? 50  CYS   A C   1 
ATOM   347  O  O   . CYS   A 1 44  ? 24.263 -4.901  11.583 1.00 45.92  ? 50  CYS   A O   1 
ATOM   348  C  CB  . CYS   A 1 44  ? 26.349 -4.690  13.424 1.00 50.04  ? 50  CYS   A CB  1 
ATOM   349  S  SG  . CYS   A 1 44  ? 27.956 -5.350  13.947 1.00 55.72  ? 50  CYS   A SG  1 
ATOM   350  N  N   . ASP   A 1 45  ? 24.588 -2.805  10.727 1.00 37.52  ? 51  ASP   A N   1 
ATOM   351  C  CA  . ASP   A 1 45  ? 23.160 -2.447  10.453 1.00 29.62  ? 51  ASP   A CA  1 
ATOM   352  C  C   . ASP   A 1 45  ? 22.837 -2.140  8.978  1.00 25.43  ? 51  ASP   A C   1 
ATOM   353  O  O   . ASP   A 1 45  ? 23.500 -1.276  8.344  1.00 27.18  ? 51  ASP   A O   1 
ATOM   354  C  CB  . ASP   A 1 45  ? 22.716 -1.234  11.277 1.00 29.81  ? 51  ASP   A CB  1 
ATOM   355  C  CG  . ASP   A 1 45  ? 22.731 -1.473  12.773 1.00 28.19  ? 51  ASP   A CG  1 
ATOM   356  O  OD1 . ASP   A 1 45  ? 22.583 -2.627  13.175 1.00 33.22  ? 51  ASP   A OD1 1 
ATOM   357  O  OD2 . ASP   A 1 45  ? 22.915 -0.493  13.527 1.00 34.17  ? 51  ASP   A OD2 1 
ATOM   358  N  N   . THR   A 1 46  ? 21.774 -2.774  8.478  1.00 19.48  ? 52  THR   A N   1 
ATOM   359  C  CA  . THR   A 1 46  ? 21.117 -2.502  7.166  1.00 19.74  ? 52  THR   A CA  1 
ATOM   360  C  C   . THR   A 1 46  ? 19.832 -1.691  7.354  1.00 17.72  ? 52  THR   A C   1 
ATOM   361  O  O   . THR   A 1 46  ? 19.014 -2.056  8.229  1.00 19.43  ? 52  THR   A O   1 
ATOM   362  C  CB  . THR   A 1 46  ? 20.762 -3.813  6.455  1.00 19.64  ? 52  THR   A CB  1 
ATOM   363  O  OG1 . THR   A 1 46  ? 21.928 -4.637  6.422  1.00 19.91  ? 52  THR   A OG1 1 
ATOM   364  C  CG2 . THR   A 1 46  ? 20.262 -3.614  5.039  1.00 20.83  ? 52  THR   A CG2 1 
ATOM   365  N  N   . ILE   A 1 47  ? 19.602 -0.698  6.510  1.00 17.06  ? 53  ILE   A N   1 
ATOM   366  C  CA  . ILE   A 1 47  ? 18.397 0.167   6.505  1.00 16.02  ? 53  ILE   A CA  1 
ATOM   367  C  C   . ILE   A 1 47  ? 17.321 -0.463  5.614  1.00 14.84  ? 53  ILE   A C   1 
ATOM   368  O  O   . ILE   A 1 47  ? 17.626 -0.916  4.489  1.00 14.49  ? 53  ILE   A O   1 
ATOM   369  C  CB  . ILE   A 1 47  ? 18.727 1.584   6.026  1.00 15.71  ? 53  ILE   A CB  1 
ATOM   370  C  CG1 . ILE   A 1 47  ? 19.923 2.196   6.776  1.00 16.76  ? 53  ILE   A CG1 1 
ATOM   371  C  CG2 . ILE   A 1 47  ? 17.496 2.457   6.109  1.00 15.75  ? 53  ILE   A CG2 1 
ATOM   372  C  CD1 . ILE   A 1 47  ? 19.987 1.873   8.291  1.00 16.59  ? 53  ILE   A CD1 1 
ATOM   373  N  N   . ALA   A 1 48  ? 16.080 -0.470  6.093  1.00 13.93  ? 54  ALA   A N   1 
ATOM   374  C  CA  . ALA   A 1 48  ? 14.929 -1.029  5.345  1.00 15.75  ? 54  ALA   A CA  1 
ATOM   375  C  C   . ALA   A 1 48  ? 14.640 -0.156  4.119  1.00 14.92  ? 54  ALA   A C   1 
ATOM   376  O  O   . ALA   A 1 48  ? 14.562 1.100   4.296  1.00 15.74  ? 54  ALA   A O   1 
ATOM   377  C  CB  . ALA   A 1 48  ? 13.737 -1.100  6.256  1.00 15.47  ? 54  ALA   A CB  1 
ATOM   378  N  N   . ARG   A 1 49  ? 14.471 -0.759  2.932  1.00 15.60  ? 55  ARG   A N   1 
ATOM   379  C  CA  . ARG   A 1 49  ? 13.941 -0.043  1.752  1.00 15.93  ? 55  ARG   A CA  1 
ATOM   380  C  C   . ARG   A 1 49  ? 12.623 -0.717  1.387  1.00 15.93  ? 55  ARG   A C   1 
ATOM   381  O  O   . ARG   A 1 49  ? 12.661 -1.740  0.673  1.00 18.46  ? 55  ARG   A O   1 
ATOM   382  C  CB  . ARG   A 1 49  ? 14.993 -0.002  0.644  1.00 16.97  ? 55  ARG   A CB  1 
ATOM   383  C  CG  . ARG   A 1 49  ? 16.349 0.525   1.102  1.00 17.38  ? 55  ARG   A CG  1 
ATOM   384  C  CD  . ARG   A 1 49  ? 16.378 1.968   1.561  1.00 18.44  ? 55  ARG   A CD  1 
ATOM   385  N  NE  . ARG   A 1 49  ? 17.705 2.381   2.027  1.00 18.93  ? 55  ARG   A NE  1 
ATOM   386  C  CZ  . ARG   A 1 49  ? 17.962 3.497   2.726  1.00 17.24  ? 55  ARG   A CZ  1 
ATOM   387  N  NH1 . ARG   A 1 49  ? 16.991 4.364   2.973  1.00 16.80  ? 55  ARG   A NH1 1 
ATOM   388  N  NH2 . ARG   A 1 49  ? 19.195 3.806   3.106  1.00 19.56  ? 55  ARG   A NH2 1 
ATOM   389  N  N   . CYS   A 1 50  ? 11.531 -0.133  1.872  1.00 15.35  ? 56  CYS   A N   1 
ATOM   390  C  CA  . CYS   A 1 50  ? 10.199 -0.784  1.934  1.00 14.19  ? 56  CYS   A CA  1 
ATOM   391  C  C   . CYS   A 1 50  ? 9.083  0.158   2.425  1.00 14.66  ? 56  CYS   A C   1 
ATOM   392  O  O   . CYS   A 1 50  ? 9.348  1.338   2.844  1.00 12.98  ? 56  CYS   A O   1 
ATOM   393  C  CB  . CYS   A 1 50  ? 10.271 -1.994  2.860  1.00 14.27  ? 56  CYS   A CB  1 
ATOM   394  S  SG  . CYS   A 1 50  ? 10.255 -1.480  4.596  1.00 14.07  ? 56  CYS   A SG  1 
ATOM   395  N  N   A ASP   A 1 51  ? 7.830  -0.308  2.361  0.25 14.80  ? 57  ASP   A N   1 
ATOM   396  N  N   B ASP   A 1 51  ? 7.885  -0.428  2.417  0.25 15.39  ? 57  ASP   A N   1 
ATOM   397  C  CA  A ASP   A 1 51  ? 6.635  0.432   2.858  0.25 15.75  ? 57  ASP   A CA  1 
ATOM   398  C  CA  B ASP   A 1 51  ? 6.555  0.182   2.648  0.25 16.72  ? 57  ASP   A CA  1 
ATOM   399  C  C   A ASP   A 1 51  ? 5.933  -0.393  3.944  0.25 16.14  ? 57  ASP   A C   1 
ATOM   400  C  C   B ASP   A 1 51  ? 5.941  -0.384  3.937  0.25 16.64  ? 57  ASP   A C   1 
ATOM   401  O  O   A ASP   A 1 51  ? 4.718  -0.211  4.128  0.25 17.15  ? 57  ASP   A O   1 
ATOM   402  O  O   B ASP   A 1 51  ? 4.798  -0.008  4.255  0.25 17.36  ? 57  ASP   A O   1 
ATOM   403  C  CB  A ASP   A 1 51  ? 5.661  0.775   1.724  0.25 15.92  ? 57  ASP   A CB  1 
ATOM   404  C  CB  B ASP   A 1 51  ? 5.683  -0.155  1.438  0.25 17.41  ? 57  ASP   A CB  1 
ATOM   405  C  CG  A ASP   A 1 51  ? 5.058  -0.438  1.034  0.25 16.60  ? 57  ASP   A CG  1 
ATOM   406  C  CG  B ASP   A 1 51  ? 4.582  0.840   1.135  0.25 17.82  ? 57  ASP   A CG  1 
ATOM   407  O  OD1 A ASP   A 1 51  ? 5.275  -1.563  1.524  0.25 16.58  ? 57  ASP   A OD1 1 
ATOM   408  O  OD1 B ASP   A 1 51  ? 4.592  1.927   1.739  0.25 19.04  ? 57  ASP   A OD1 1 
ATOM   409  O  OD2 A ASP   A 1 51  ? 4.375  -0.245  0.009  0.25 16.94  ? 57  ASP   A OD2 1 
ATOM   410  O  OD2 B ASP   A 1 51  ? 3.724  0.515   0.290  0.25 17.93  ? 57  ASP   A OD2 1 
ATOM   411  N  N   . CYS   A 1 52  ? 6.672  -1.246  4.656  1.00 17.24  ? 58  CYS   A N   1 
ATOM   412  C  CA  . CYS   A 1 52  ? 6.126  -2.023  5.803  1.00 16.54  ? 58  CYS   A CA  1 
ATOM   413  C  C   . CYS   A 1 52  ? 5.513  -1.113  6.851  1.00 15.70  ? 58  CYS   A C   1 
ATOM   414  O  O   . CYS   A 1 52  ? 6.103  -0.039  7.115  1.00 15.66  ? 58  CYS   A O   1 
ATOM   415  C  CB  . CYS   A 1 52  ? 7.187  -2.746  6.585  1.00 15.89  ? 58  CYS   A CB  1 
ATOM   416  S  SG  . CYS   A 1 52  ? 7.749  -4.208  5.706  1.00 15.45  ? 58  CYS   A SG  1 
ATOM   417  N  N   . GLN   A 1 53  ? 4.436  -1.606  7.460  1.00 14.37  ? 59  GLN   A N   1 
ATOM   418  C  CA  . GLN   A 1 53  ? 3.726  -0.976  8.590  1.00 15.20  ? 59  GLN   A CA  1 
ATOM   419  C  C   . GLN   A 1 53  ? 3.665  -2.004  9.723  1.00 11.35  ? 59  GLN   A C   1 
ATOM   420  O  O   . GLN   A 1 53  ? 2.915  -1.729  10.646 1.00 14.37  ? 59  GLN   A O   1 
ATOM   421  C  CB  . GLN   A 1 53  ? 2.340  -0.475  8.177  1.00 14.40  ? 59  GLN   A CB  1 
ATOM   422  C  CG  . GLN   A 1 53  ? 2.381  0.792   7.357  1.00 15.62  ? 59  GLN   A CG  1 
ATOM   423  C  CD  . GLN   A 1 53  ? 1.026  1.366   7.047  1.00 15.32  ? 59  GLN   A CD  1 
ATOM   424  O  OE1 . GLN   A 1 53  ? 0.599  1.369   5.894  1.00 21.21  ? 59  GLN   A OE1 1 
ATOM   425  N  NE2 . GLN   A 1 53  ? 0.380  1.936   8.059  1.00 17.89  ? 59  GLN   A NE2 1 
ATOM   426  N  N   . THR   A 1 54  ? 4.512  -3.054  9.674  1.00 11.62  ? 60  THR   A N   1 
ATOM   427  C  CA  . THR   A 1 54  ? 4.702  -3.984  10.828 1.00 12.30  ? 60  THR   A CA  1 
ATOM   428  C  C   . THR   A 1 54  ? 6.191  -4.173  11.156 1.00 11.01  ? 60  THR   A C   1 
ATOM   429  O  O   . THR   A 1 54  ? 6.994  -4.369  10.253 1.00 11.59  ? 60  THR   A O   1 
ATOM   430  C  CB  . THR   A 1 54  ? 4.027  -5.348  10.617 1.00 14.12  ? 60  THR   A CB  1 
ATOM   431  O  OG1 . THR   A 1 54  ? 4.657  -6.005  9.525  1.00 20.87  ? 60  THR   A OG1 1 
ATOM   432  C  CG2 . THR   A 1 54  ? 2.536  -5.232  10.371 1.00 14.26  ? 60  THR   A CG2 1 
ATOM   433  N  N   . GLY   A 1 55  ? 6.535  -4.230  12.441 1.00 9.36   ? 61  GLY   A N   1 
ATOM   434  C  CA  . GLY   A 1 55  ? 7.918  -4.470  12.864 1.00 7.93   ? 61  GLY   A CA  1 
ATOM   435  C  C   . GLY   A 1 55  ? 7.984  -4.593  14.367 1.00 6.71   ? 61  GLY   A C   1 
ATOM   436  O  O   . GLY   A 1 55  ? 6.966  -4.930  14.987 1.00 7.39   ? 61  GLY   A O   1 
ATOM   437  N  N   . VAL   A 1 56  ? 9.202  -4.483  14.875 1.00 6.13   ? 62  VAL   A N   1 
ATOM   438  C  CA  . VAL   A 1 56  ? 9.435  -4.657  16.333 1.00 5.86   ? 62  VAL   A CA  1 
ATOM   439  C  C   . VAL   A 1 56  ? 10.300 -3.497  16.806 1.00 6.05   ? 62  VAL   A C   1 
ATOM   440  O  O   . VAL   A 1 56  ? 11.253 -3.170  16.110 1.00 6.45   ? 62  VAL   A O   1 
ATOM   441  C  CB  . VAL   A 1 56  ? 10.128 -6.006  16.595 1.00 6.07   ? 62  VAL   A CB  1 
ATOM   442  C  CG1 . VAL   A 1 56  ? 10.500 -6.173  18.061 1.00 6.41   ? 62  VAL   A CG1 1 
ATOM   443  C  CG2 . VAL   A 1 56  ? 9.241  -7.140  16.127 1.00 6.62   ? 62  VAL   A CG2 1 
ATOM   444  N  N   . TYR   A 1 57  ? 9.966  -2.838  17.901 1.00 6.00   ? 63  TYR   A N   1 
ATOM   445  C  CA  . TYR   A 1 57  ? 10.837 -1.740  18.422 1.00 6.60   ? 63  TYR   A CA  1 
ATOM   446  C  C   . TYR   A 1 57  ? 11.324 -2.078  19.842 1.00 7.58   ? 63  TYR   A C   1 
ATOM   447  O  O   . TYR   A 1 57  ? 10.675 -2.758  20.647 1.00 8.73   ? 63  TYR   A O   1 
ATOM   448  C  CB  . TYR   A 1 57  ? 10.135 -0.368  18.386 1.00 7.25   ? 63  TYR   A CB  1 
ATOM   449  C  CG  . TYR   A 1 57  ? 9.207  -0.026  19.534 1.00 7.99   ? 63  TYR   A CG  1 
ATOM   450  C  CD1 . TYR   A 1 57  ? 7.928  -0.536  19.584 1.00 9.15   ? 63  TYR   A CD1 1 
ATOM   451  C  CD2 . TYR   A 1 57  ? 9.585  0.869   20.535 1.00 9.45   ? 63  TYR   A CD2 1 
ATOM   452  C  CE1 . TYR   A 1 57  ? 7.049  -0.194  20.590 1.00 9.81   ? 63  TYR   A CE1 1 
ATOM   453  C  CE2 . TYR   A 1 57  ? 8.724  1.205   21.570 1.00 10.99  ? 63  TYR   A CE2 1 
ATOM   454  C  CZ  . TYR   A 1 57  ? 7.458  0.658   21.588 1.00 10.94  ? 63  TYR   A CZ  1 
ATOM   455  O  OH  . TYR   A 1 57  ? 6.542  0.953   22.537 1.00 13.27  ? 63  TYR   A OH  1 
ATOM   456  N  N   . TYR   A 1 58  ? 12.466 -1.504  20.185 1.00 8.13   ? 64  TYR   A N   1 
ATOM   457  C  CA  . TYR   A 1 58  ? 12.999 -1.577  21.573 1.00 9.86   ? 64  TYR   A CA  1 
ATOM   458  C  C   . TYR   A 1 58  ? 12.535 -0.362  22.366 1.00 11.37  ? 64  TYR   A C   1 
ATOM   459  O  O   . TYR   A 1 58  ? 12.782 0.767   21.948 1.00 11.64  ? 64  TYR   A O   1 
ATOM   460  C  CB  . TYR   A 1 58  ? 14.524 -1.657  21.538 1.00 12.14  ? 64  TYR   A CB  1 
ATOM   461  C  CG  . TYR   A 1 58  ? 15.075 -1.785  22.938 1.00 15.70  ? 64  TYR   A CG  1 
ATOM   462  C  CD1 . TYR   A 1 58  ? 14.790 -2.924  23.674 1.00 17.11  ? 64  TYR   A CD1 1 
ATOM   463  C  CD2 . TYR   A 1 58  ? 15.738 -0.735  23.568 1.00 17.90  ? 64  TYR   A CD2 1 
ATOM   464  C  CE1 . TYR   A 1 58  ? 15.210 -3.052  24.987 1.00 19.97  ? 64  TYR   A CE1 1 
ATOM   465  C  CE2 . TYR   A 1 58  ? 16.169 -0.856  24.883 1.00 20.16  ? 64  TYR   A CE2 1 
ATOM   466  C  CZ  . TYR   A 1 58  ? 15.922 -2.026  25.582 1.00 22.36  ? 64  TYR   A CZ  1 
ATOM   467  O  OH  . TYR   A 1 58  ? 16.305 -2.180  26.885 1.00 23.78  ? 64  TYR   A OH  1 
ATOM   468  N  N   . CYS   A 1 59  ? 11.939 -0.600  23.550 1.00 11.24  ? 65  CYS   A N   1 
ATOM   469  C  CA  . CYS   A 1 59  ? 11.353 0.432   24.465 1.00 12.78  ? 65  CYS   A CA  1 
ATOM   470  C  C   . CYS   A 1 59  ? 12.064 0.444   25.819 1.00 13.33  ? 65  CYS   A C   1 
ATOM   471  O  O   . CYS   A 1 59  ? 11.749 -0.420  26.655 1.00 13.64  ? 65  CYS   A O   1 
ATOM   472  C  CB  . CYS   A 1 59  ? 9.877  0.186   24.733 1.00 12.14  ? 65  CYS   A CB  1 
ATOM   473  S  SG  . CYS   A 1 59  ? 9.195  1.198   26.085 1.00 15.98  ? 65  CYS   A SG  1 
ATOM   474  N  N   . SER   A 1 60  ? 13.004 1.373   25.999 1.00 14.23  ? 66  SER   A N   1 
ATOM   475  C  CA  . SER   A 1 60  ? 13.955 1.402   27.142 1.00 14.15  ? 66  SER   A CA  1 
ATOM   476  C  C   . SER   A 1 60  ? 13.178 1.620   28.442 1.00 12.81  ? 66  SER   A C   1 
ATOM   477  O  O   . SER   A 1 60  ? 13.577 1.056   29.476 1.00 17.65  ? 66  SER   A O   1 
ATOM   478  C  CB  . SER   A 1 60  ? 15.085 2.417   26.980 1.00 15.06  ? 66  SER   A CB  1 
ATOM   479  O  OG  . SER   A 1 60  ? 14.637 3.743   27.123 1.00 15.78  ? 66  SER   A OG  1 
ATOM   480  N  N   . SER   A 1 61  ? 12.072 2.361   28.415 1.00 13.83  ? 67  SER   A N   1 
ATOM   481  C  CA  . SER   A 1 61  ? 11.282 2.627   29.654 1.00 13.73  ? 67  SER   A CA  1 
ATOM   482  C  C   . SER   A 1 61  ? 10.470 1.379   30.043 1.00 14.49  ? 67  SER   A C   1 
ATOM   483  O  O   . SER   A 1 61  ? 9.756  1.441   31.037 1.00 14.35  ? 67  SER   A O   1 
ATOM   484  C  CB  . SER   A 1 61  ? 10.375 3.850   29.532 1.00 14.86  ? 67  SER   A CB  1 
ATOM   485  O  OG  . SER   A 1 61  ? 9.397  3.671   28.528 1.00 15.30  ? 67  SER   A OG  1 
ATOM   486  N  N   . ARG   A 1 62  ? 10.592 0.261   29.316 1.00 14.57  ? 68  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 62  ? 9.984  -1.037  29.716 1.00 14.28  ? 68  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 62  ? 10.982 -2.202  29.646 1.00 13.02  ? 68  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 62  ? 10.524 -3.316  29.964 1.00 16.63  ? 68  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 62  ? 8.803  -1.398  28.813 1.00 13.99  ? 68  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 62  ? 7.627  -0.444  28.938 1.00 15.39  ? 68  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 62  ? 6.906  -0.675  30.266 1.00 15.01  ? 68  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 62  ? 5.705  0.138   30.346 1.00 15.34  ? 68  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 62  ? 5.601  1.324   30.973 1.00 14.68  ? 68  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 62  ? 6.660  1.900   31.531 1.00 14.63  ? 68  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 62  ? 4.443  1.965   30.973 1.00 18.01  ? 68  ARG   A NH2 1 
ATOM   497  N  N   . ARG   A 1 63  ? 12.198 -2.018  29.102 1.00 16.64  ? 69  ARG   A N   1 
ATOM   498  C  CA  . ARG   A 1 63  ? 13.226 -3.064  28.829 1.00 17.33  ? 69  ARG   A CA  1 
ATOM   499  C  C   . ARG   A 1 63  ? 12.689 -4.195  27.925 1.00 21.02  ? 69  ARG   A C   1 
ATOM   500  O  O   . ARG   A 1 63  ? 13.115 -5.358  28.106 1.00 20.21  ? 69  ARG   A O   1 
ATOM   501  C  CB  . ARG   A 1 63  ? 13.775 -3.619  30.146 1.00 20.05  ? 69  ARG   A CB  1 
ATOM   502  C  CG  . ARG   A 1 63  ? 14.911 -2.788  30.721 1.00 21.83  ? 69  ARG   A CG  1 
ATOM   503  C  CD  . ARG   A 1 63  ? 15.452 -3.431  31.980 1.00 22.70  ? 69  ARG   A CD  1 
ATOM   504  N  NE  . ARG   A 1 63  ? 16.220 -2.460  32.750 1.00 24.01  ? 69  ARG   A NE  1 
ATOM   505  C  CZ  . ARG   A 1 63  ? 15.967 -2.064  34.002 1.00 24.47  ? 69  ARG   A CZ  1 
ATOM   506  N  NH1 . ARG   A 1 63  ? 14.981 -2.593  34.710 1.00 23.34  ? 69  ARG   A NH1 1 
ATOM   507  N  NH2 . ARG   A 1 63  ? 16.759 -1.170  34.566 1.00 23.81  ? 69  ARG   A NH2 1 
ATOM   508  N  N   . LYS   A 1 64  ? 11.865 -3.890  26.922 1.00 20.53  ? 70  LYS   A N   1 
ATOM   509  C  CA  . LYS   A 1 64  ? 11.191 -4.920  26.082 1.00 20.17  ? 70  LYS   A CA  1 
ATOM   510  C  C   . LYS   A 1 64  ? 11.254 -4.546  24.593 1.00 17.56  ? 70  LYS   A C   1 
ATOM   511  O  O   . LYS   A 1 64  ? 11.181 -3.327  24.266 1.00 18.31  ? 70  LYS   A O   1 
ATOM   512  C  CB  . LYS   A 1 64  ? 9.733  -5.040  26.528 1.00 20.78  ? 70  LYS   A CB  1 
ATOM   513  C  CG  . LYS   A 1 64  ? 9.482  -6.099  27.594 1.00 23.90  ? 70  LYS   A CG  1 
ATOM   514  C  CD  . LYS   A 1 64  ? 8.014  -6.404  27.806 1.00 25.35  ? 70  LYS   A CD  1 
ATOM   515  C  CE  . LYS   A 1 64  ? 7.764  -7.472  28.850 1.00 27.68  ? 70  LYS   A CE  1 
ATOM   516  N  NZ  . LYS   A 1 64  ? 8.259  -7.066  30.184 1.00 28.79  ? 70  LYS   A NZ  1 
ATOM   517  N  N   . HIS   A 1 65  ? 11.326 -5.553  23.730 1.00 17.07  ? 71  HIS   A N   1 
ATOM   518  C  CA  . HIS   A 1 65  ? 11.020 -5.382  22.287 1.00 14.61  ? 71  HIS   A CA  1 
ATOM   519  C  C   . HIS   A 1 65  ? 9.523  -5.657  22.122 1.00 12.57  ? 71  HIS   A C   1 
ATOM   520  O  O   . HIS   A 1 65  ? 8.998  -6.680  22.674 1.00 15.22  ? 71  HIS   A O   1 
ATOM   521  C  CB  . HIS   A 1 65  ? 11.882 -6.272  21.417 1.00 14.45  ? 71  HIS   A CB  1 
ATOM   522  C  CG  . HIS   A 1 65  ? 13.332 -5.950  21.534 1.00 14.41  ? 71  HIS   A CG  1 
ATOM   523  N  ND1 . HIS   A 1 65  ? 14.074 -5.346  20.517 1.00 14.86  ? 71  HIS   A ND1 1 
ATOM   524  C  CD2 . HIS   A 1 65  ? 14.180 -6.122  22.568 1.00 15.70  ? 71  HIS   A CD2 1 
ATOM   525  C  CE1 . HIS   A 1 65  ? 15.313 -5.206  20.928 1.00 14.77  ? 71  HIS   A CE1 1 
ATOM   526  N  NE2 . HIS   A 1 65  ? 15.380 -5.599  22.190 1.00 16.57  ? 71  HIS   A NE2 1 
ATOM   527  N  N   . TYR   A 1 66  ? 8.790  -4.747  21.506 1.00 11.36  ? 72  TYR   A N   1 
ATOM   528  C  CA  . TYR   A 1 66  ? 7.340  -4.925  21.270 1.00 9.77   ? 72  TYR   A CA  1 
ATOM   529  C  C   . TYR   A 1 66  ? 7.071  -5.014  19.780 1.00 9.09   ? 72  TYR   A C   1 
ATOM   530  O  O   . TYR   A 1 66  ? 7.523  -4.133  19.015 1.00 7.88   ? 72  TYR   A O   1 
ATOM   531  C  CB  . TYR   A 1 66  ? 6.527  -3.732  21.758 1.00 10.37  ? 72  TYR   A CB  1 
ATOM   532  C  CG  . TYR   A 1 66  ? 6.483  -3.524  23.262 1.00 11.40  ? 72  TYR   A CG  1 
ATOM   533  C  CD1 . TYR   A 1 66  ? 5.680  -4.340  24.056 1.00 11.71  ? 72  TYR   A CD1 1 
ATOM   534  C  CD2 . TYR   A 1 66  ? 7.249  -2.561  23.917 1.00 12.00  ? 72  TYR   A CD2 1 
ATOM   535  C  CE1 . TYR   A 1 66  ? 5.609  -4.186  25.436 1.00 12.15  ? 72  TYR   A CE1 1 
ATOM   536  C  CE2 . TYR   A 1 66  ? 7.183  -2.393  25.295 1.00 12.30  ? 72  TYR   A CE2 1 
ATOM   537  C  CZ  . TYR   A 1 66  ? 6.352  -3.193  26.048 1.00 12.60  ? 72  TYR   A CZ  1 
ATOM   538  O  OH  . TYR   A 1 66  ? 6.361  -2.999  27.407 1.00 14.84  ? 72  TYR   A OH  1 
ATOM   539  N  N   . PRO   A 1 67  ? 6.250  -6.003  19.347 1.00 8.86   ? 73  PRO   A N   1 
ATOM   540  C  CA  . PRO   A 1 67  ? 5.767  -6.000  17.966 1.00 9.25   ? 73  PRO   A CA  1 
ATOM   541  C  C   . PRO   A 1 67  ? 4.679  -4.936  17.776 1.00 9.52   ? 73  PRO   A C   1 
ATOM   542  O  O   . PRO   A 1 67  ? 3.743  -4.855  18.577 1.00 11.56  ? 73  PRO   A O   1 
ATOM   543  C  CB  . PRO   A 1 67  ? 5.157  -7.390  17.787 1.00 9.31   ? 73  PRO   A CB  1 
ATOM   544  C  CG  . PRO   A 1 67  ? 4.792  -7.821  19.189 1.00 9.65   ? 73  PRO   A CG  1 
ATOM   545  C  CD  . PRO   A 1 67  ? 5.727  -7.125  20.156 1.00 9.63   ? 73  PRO   A CD  1 
ATOM   546  N  N   . VAL   A 1 68  ? 4.739  -4.195  16.687 1.00 8.94   ? 74  VAL   A N   1 
ATOM   547  C  CA  . VAL   A 1 68  ? 3.808  -3.066  16.409 1.00 9.61   ? 74  VAL   A CA  1 
ATOM   548  C  C   . VAL   A 1 68  ? 3.487  -2.986  14.917 1.00 10.36  ? 74  VAL   A C   1 
ATOM   549  O  O   . VAL   A 1 68  ? 4.311  -3.318  14.056 1.00 9.06   ? 74  VAL   A O   1 
ATOM   550  C  CB  . VAL   A 1 68  ? 4.407  -1.723  16.867 1.00 11.38  ? 74  VAL   A CB  1 
ATOM   551  C  CG1 . VAL   A 1 68  ? 4.464  -1.622  18.373 1.00 11.89  ? 74  VAL   A CG1 1 
ATOM   552  C  CG2 . VAL   A 1 68  ? 5.802  -1.491  16.273 1.00 11.45  ? 74  VAL   A CG2 1 
ATOM   553  N  N   . SER   A 1 69  ? 2.262  -2.511  14.670 1.00 9.60   ? 75  SER   A N   1 
ATOM   554  C  CA  . SER   A 1 69  ? 1.789  -1.833  13.445 1.00 10.56  ? 75  SER   A CA  1 
ATOM   555  C  C   . SER   A 1 69  ? 2.101  -0.348  13.575 1.00 10.60  ? 75  SER   A C   1 
ATOM   556  O  O   . SER   A 1 69  ? 1.840  0.229   14.635 1.00 13.06  ? 75  SER   A O   1 
ATOM   557  C  CB  . SER   A 1 69  ? 0.332  -2.036  13.210 1.00 12.10  ? 75  SER   A CB  1 
ATOM   558  O  OG  . SER   A 1 69  ? 0.041  -3.404  13.228 1.00 14.19  ? 75  SER   A OG  1 
ATOM   559  N  N   . PHE   A 1 70  ? 2.583  0.252   12.494 1.00 12.81  ? 76  PHE   A N   1 
ATOM   560  C  CA  . PHE   A 1 70  ? 2.989  1.679   12.558 1.00 13.54  ? 76  PHE   A CA  1 
ATOM   561  C  C   . PHE   A 1 70  ? 2.500  2.360   11.301 1.00 15.79  ? 76  PHE   A C   1 
ATOM   562  O  O   . PHE   A 1 70  ? 2.425  1.731   10.271 1.00 14.20  ? 76  PHE   A O   1 
ATOM   563  C  CB  . PHE   A 1 70  ? 4.486  1.854   12.854 1.00 12.51  ? 76  PHE   A CB  1 
ATOM   564  C  CG  . PHE   A 1 70  ? 5.410  1.122   11.913 1.00 10.98  ? 76  PHE   A CG  1 
ATOM   565  C  CD1 . PHE   A 1 70  ? 5.870  -0.166  12.157 1.00 11.05  ? 76  PHE   A CD1 1 
ATOM   566  C  CD2 . PHE   A 1 70  ? 5.836  1.783   10.767 1.00 12.79  ? 76  PHE   A CD2 1 
ATOM   567  C  CE1 . PHE   A 1 70  ? 6.719  -0.776  11.257 1.00 10.56  ? 76  PHE   A CE1 1 
ATOM   568  C  CE2 . PHE   A 1 70  ? 6.644  1.146   9.857  1.00 10.82  ? 76  PHE   A CE2 1 
ATOM   569  C  CZ  . PHE   A 1 70  ? 7.134  -0.116  10.112 1.00 10.38  ? 76  PHE   A CZ  1 
ATOM   570  N  N   . SER   A 1 71  ? 2.187  3.638   11.456 1.00 15.42  ? 77  SER   A N   1 
ATOM   571  C  CA  . SER   A 1 71  ? 1.565  4.501   10.412 1.00 17.70  ? 77  SER   A CA  1 
ATOM   572  C  C   . SER   A 1 71  ? 2.624  4.886   9.372  1.00 19.13  ? 77  SER   A C   1 
ATOM   573  O  O   . SER   A 1 71  ? 3.796  4.694   9.677  1.00 15.57  ? 77  SER   A O   1 
ATOM   574  C  CB  . SER   A 1 71  ? 0.982  5.717   11.029 1.00 19.27  ? 77  SER   A CB  1 
ATOM   575  O  OG  . SER   A 1 71  ? 1.953  6.755   11.084 1.00 21.45  ? 77  SER   A OG  1 
ATOM   576  N  N   . LYS   A 1 72  ? 2.261  5.458   8.218  1.00 21.53  ? 78  LYS   A N   1 
ATOM   577  C  CA  . LYS   A 1 72  ? 3.297  5.847   7.214  1.00 23.94  ? 78  LYS   A CA  1 
ATOM   578  C  C   . LYS   A 1 72  ? 3.869  7.210   7.615  1.00 19.95  ? 78  LYS   A C   1 
ATOM   579  O  O   . LYS   A 1 72  ? 3.223  7.975   8.351  1.00 20.45  ? 78  LYS   A O   1 
ATOM   580  C  CB  . LYS   A 1 72  ? 2.798  5.736   5.762  1.00 26.79  ? 78  LYS   A CB  1 
ATOM   581  C  CG  . LYS   A 1 72  ? 3.101  4.397   5.088  1.00 29.32  ? 78  LYS   A CG  1 
ATOM   582  C  CD  . LYS   A 1 72  ? 2.595  4.245   3.666  1.00 32.50  ? 78  LYS   A CD  1 
ATOM   583  C  CE  . LYS   A 1 72  ? 2.201  2.821   3.332  1.00 34.12  ? 78  LYS   A CE  1 
ATOM   584  N  NZ  . LYS   A 1 72  ? 2.015  2.611   1.879  1.00 36.18  ? 78  LYS   A NZ  1 
ATOM   585  N  N   . PRO   A 1 73  ? 5.149  7.486   7.254  1.00 19.10  ? 79  PRO   A N   1 
ATOM   586  C  CA  . PRO   A 1 73  ? 5.881  8.679   7.691  1.00 19.79  ? 79  PRO   A CA  1 
ATOM   587  C  C   . PRO   A 1 73  ? 5.143  9.919   7.197  1.00 19.51  ? 79  PRO   A C   1 
ATOM   588  O  O   . PRO   A 1 73  ? 4.873  10.011  6.046  1.00 20.76  ? 79  PRO   A O   1 
ATOM   589  C  CB  . PRO   A 1 73  ? 7.236  8.614   6.977  1.00 20.00  ? 79  PRO   A CB  1 
ATOM   590  C  CG  . PRO   A 1 73  ? 7.361  7.205   6.474  1.00 18.52  ? 79  PRO   A CG  1 
ATOM   591  C  CD  . PRO   A 1 73  ? 5.952  6.668   6.325  1.00 17.43  ? 79  PRO   A CD  1 
ATOM   592  N  N   A SER   A 1 74  ? 4.806  10.832  8.112  0.22 19.46  ? 80  SER   A N   1 
ATOM   593  N  N   B SER   A 1 74  ? 4.818  10.843  8.105  0.22 19.66  ? 80  SER   A N   1 
ATOM   594  C  CA  A SER   A 1 74  ? 3.944  12.013  7.833  0.22 19.91  ? 80  SER   A CA  1 
ATOM   595  C  CA  B SER   A 1 74  ? 3.965  12.026  7.811  0.22 20.20  ? 80  SER   A CA  1 
ATOM   596  C  C   A SER   A 1 74  ? 4.292  13.177  8.769  0.22 19.67  ? 80  SER   A C   1 
ATOM   597  C  C   B SER   A 1 74  ? 4.145  13.118  8.872  0.22 19.81  ? 80  SER   A C   1 
ATOM   598  O  O   A SER   A 1 74  ? 5.258  13.054  9.553  0.22 19.29  ? 80  SER   A O   1 
ATOM   599  O  O   B SER   A 1 74  ? 4.862  12.878  9.867  0.22 19.59  ? 80  SER   A O   1 
ATOM   600  C  CB  A SER   A 1 74  ? 2.489  11.635  7.944  0.22 20.32  ? 80  SER   A CB  1 
ATOM   601  C  CB  B SER   A 1 74  ? 2.527  11.601  7.699  0.22 20.74  ? 80  SER   A CB  1 
ATOM   602  O  OG  A SER   A 1 74  ? 2.304  10.263  7.645  0.22 20.37  ? 80  SER   A OG  1 
ATOM   603  O  OG  B SER   A 1 74  ? 2.386  10.590  6.715  0.22 21.01  ? 80  SER   A OG  1 
ATOM   604  N  N   . LEU   A 1 75  ? 3.521  14.265  8.681  0.44 18.20  ? 81  LEU   A N   1 
ATOM   605  C  CA  . LEU   A 1 75  ? 3.647  15.456  9.558  0.44 17.97  ? 81  LEU   A CA  1 
ATOM   606  C  C   . LEU   A 1 75  ? 2.633  15.344  10.702 0.44 17.58  ? 81  LEU   A C   1 
ATOM   607  O  O   . LEU   A 1 75  ? 1.417  15.424  10.425 0.44 17.49  ? 81  LEU   A O   1 
ATOM   608  C  CB  . LEU   A 1 75  ? 3.407  16.715  8.722  0.44 18.35  ? 81  LEU   A CB  1 
ATOM   609  C  CG  . LEU   A 1 75  ? 3.575  18.032  9.478  0.44 18.35  ? 81  LEU   A CG  1 
ATOM   610  C  CD1 . LEU   A 1 75  ? 4.818  18.772  9.005  0.44 18.85  ? 81  LEU   A CD1 1 
ATOM   611  C  CD2 . LEU   A 1 75  ? 2.335  18.896  9.327  0.44 19.03  ? 81  LEU   A CD2 1 
ATOM   612  N  N   . ILE   A 1 76  ? 3.126  15.206  11.936 0.44 16.96  ? 82  ILE   A N   1 
ATOM   613  C  CA  . ILE   A 1 76  ? 2.324  14.869  13.150 0.44 17.32  ? 82  ILE   A CA  1 
ATOM   614  C  C   . ILE   A 1 76  ? 2.596  15.919  14.231 0.44 17.54  ? 82  ILE   A C   1 
ATOM   615  O  O   . ILE   A 1 76  ? 3.781  16.236  14.473 0.44 16.77  ? 82  ILE   A O   1 
ATOM   616  C  CB  . ILE   A 1 76  ? 2.674  13.459  13.667 0.44 17.13  ? 82  ILE   A CB  1 
ATOM   617  C  CG1 . ILE   A 1 76  ? 2.573  12.385  12.580 0.44 17.58  ? 82  ILE   A CG1 1 
ATOM   618  C  CG2 . ILE   A 1 76  ? 1.836  13.114  14.892 0.44 16.95  ? 82  ILE   A CG2 1 
ATOM   619  C  CD1 . ILE   A 1 76  ? 1.200  12.225  11.980 0.44 17.64  ? 82  ILE   A CD1 1 
ATOM   620  N  N   . PHE   A 1 77  ? 1.544  16.416  14.884 0.44 17.92  ? 83  PHE   A N   1 
ATOM   621  C  CA  . PHE   A 1 77  ? 1.669  17.299  16.070 0.44 17.96  ? 83  PHE   A CA  1 
ATOM   622  C  C   . PHE   A 1 77  ? 2.006  16.424  17.286 0.44 17.66  ? 83  PHE   A C   1 
ATOM   623  O  O   . PHE   A 1 77  ? 1.282  15.437  17.556 0.44 16.81  ? 83  PHE   A O   1 
ATOM   624  C  CB  . PHE   A 1 77  ? 0.412  18.148  16.276 0.44 18.59  ? 83  PHE   A CB  1 
ATOM   625  C  CG  . PHE   A 1 77  ? 0.675  19.380  17.100 0.44 18.92  ? 83  PHE   A CG  1 
ATOM   626  C  CD1 . PHE   A 1 77  ? 1.107  20.552  16.500 0.44 19.46  ? 83  PHE   A CD1 1 
ATOM   627  C  CD2 . PHE   A 1 77  ? 0.554  19.352  18.480 0.44 19.31  ? 83  PHE   A CD2 1 
ATOM   628  C  CE1 . PHE   A 1 77  ? 1.383  21.680  17.256 0.44 19.39  ? 83  PHE   A CE1 1 
ATOM   629  C  CE2 . PHE   A 1 77  ? 0.833  20.480  19.237 0.44 19.23  ? 83  PHE   A CE2 1 
ATOM   630  C  CZ  . PHE   A 1 77  ? 1.245  21.642  18.624 0.44 19.32  ? 83  PHE   A CZ  1 
ATOM   631  N  N   . VAL   A 1 78  ? 3.109  16.750  17.969 0.44 17.50  ? 84  VAL   A N   1 
ATOM   632  C  CA  . VAL   A 1 78  ? 3.587  16.034  19.189 0.44 17.56  ? 84  VAL   A CA  1 
ATOM   633  C  C   . VAL   A 1 78  ? 3.654  17.049  20.340 0.44 17.72  ? 84  VAL   A C   1 
ATOM   634  O  O   . VAL   A 1 78  ? 4.088  18.200  20.111 0.44 18.12  ? 84  VAL   A O   1 
ATOM   635  C  CB  . VAL   A 1 78  ? 4.916  15.287  18.932 0.44 17.62  ? 84  VAL   A CB  1 
ATOM   636  C  CG1 . VAL   A 1 78  ? 5.876  16.065  18.047 0.44 17.21  ? 84  VAL   A CG1 1 
ATOM   637  C  CG2 . VAL   A 1 78  ? 5.605  14.860  20.220 0.44 17.89  ? 84  VAL   A CG2 1 
ATOM   638  N  N   . GLU   A 1 79  ? 3.174  16.648  21.523 0.44 17.34  ? 85  GLU   A N   1 
ATOM   639  C  CA  . GLU   A 1 79  ? 3.050  17.524  22.720 0.44 17.66  ? 85  GLU   A CA  1 
ATOM   640  C  C   . GLU   A 1 79  ? 4.442  17.769  23.320 0.44 17.31  ? 85  GLU   A C   1 
ATOM   641  O  O   . GLU   A 1 79  ? 5.394  17.046  22.952 0.44 16.28  ? 85  GLU   A O   1 
ATOM   642  C  CB  . GLU   A 1 79  ? 2.109  16.907  23.759 0.44 17.88  ? 85  GLU   A CB  1 
ATOM   643  C  CG  . GLU   A 1 79  ? 0.699  16.658  23.249 0.44 18.38  ? 85  GLU   A CG  1 
ATOM   644  C  CD  . GLU   A 1 79  ? -0.188 17.890  23.224 0.44 18.06  ? 85  GLU   A CD  1 
ATOM   645  O  OE1 . GLU   A 1 79  ? -0.481 18.424  24.310 0.44 18.39  ? 85  GLU   A OE1 1 
ATOM   646  O  OE2 . GLU   A 1 79  ? -0.577 18.311  22.120 0.44 19.06  ? 85  GLU   A OE2 1 
ATOM   647  N  N   . ALA   A 1 80  ? 4.535  18.741  24.233 0.44 17.79  ? 86  ALA   A N   1 
ATOM   648  C  CA  . ALA   A 1 80  ? 5.791  19.242  24.845 0.44 18.56  ? 86  ALA   A CA  1 
ATOM   649  C  C   . ALA   A 1 80  ? 6.541  18.117  25.571 0.44 19.20  ? 86  ALA   A C   1 
ATOM   650  O  O   . ALA   A 1 80  ? 5.911  17.096  25.928 0.44 17.89  ? 86  ALA   A O   1 
ATOM   651  C  CB  . ALA   A 1 80  ? 5.477  20.371  25.798 0.44 18.80  ? 86  ALA   A CB  1 
ATOM   652  N  N   . SER   A 1 81  ? 7.846  18.329  25.780 0.44 20.29  ? 87  SER   A N   1 
ATOM   653  C  CA  . SER   A 1 81  ? 8.783  17.460  26.543 0.44 21.21  ? 87  SER   A CA  1 
ATOM   654  C  C   . SER   A 1 81  ? 10.029 18.274  26.924 0.44 22.00  ? 87  SER   A C   1 
ATOM   655  O  O   . SER   A 1 81  ? 10.042 19.487  26.644 0.44 22.38  ? 87  SER   A O   1 
ATOM   656  C  CB  . SER   A 1 81  ? 9.137  16.222  25.755 0.44 21.07  ? 87  SER   A CB  1 
ATOM   657  O  OG  . SER   A 1 81  ? 9.969  16.536  24.646 0.44 21.16  ? 87  SER   A OG  1 
ATOM   658  N  N   . GLU   A 1 82  ? 11.038 17.634  27.528 0.44 23.55  ? 88  GLU   A N   1 
ATOM   659  C  CA  . GLU   A 1 82  ? 12.278 18.295  28.025 0.44 24.40  ? 88  GLU   A CA  1 
ATOM   660  C  C   . GLU   A 1 82  ? 13.091 18.855  26.849 0.44 24.57  ? 88  GLU   A C   1 
ATOM   661  O  O   . GLU   A 1 82  ? 13.875 19.793  27.083 0.44 24.67  ? 88  GLU   A O   1 
ATOM   662  C  CB  . GLU   A 1 82  ? 13.143 17.312  28.822 0.44 25.19  ? 88  GLU   A CB  1 
ATOM   663  C  CG  . GLU   A 1 82  ? 14.192 17.988  29.695 0.44 25.85  ? 88  GLU   A CG  1 
ATOM   664  C  CD  . GLU   A 1 82  ? 15.399 17.134  30.049 0.44 26.48  ? 88  GLU   A CD  1 
ATOM   665  O  OE1 . GLU   A 1 82  ? 15.709 17.021  31.253 0.44 27.70  ? 88  GLU   A OE1 1 
ATOM   666  O  OE2 . GLU   A 1 82  ? 16.041 16.604  29.122 0.44 26.44  ? 88  GLU   A OE2 1 
ATOM   667  N  N   . TYR   A 1 83  ? 12.910 18.305  25.642 0.44 24.67  ? 89  TYR   A N   1 
ATOM   668  C  CA  . TYR   A 1 83  ? 13.836 18.463  24.488 0.44 24.08  ? 89  TYR   A CA  1 
ATOM   669  C  C   . TYR   A 1 83  ? 13.253 19.380  23.403 0.44 23.78  ? 89  TYR   A C   1 
ATOM   670  O  O   . TYR   A 1 83  ? 14.046 20.070  22.736 0.44 23.71  ? 89  TYR   A O   1 
ATOM   671  C  CB  . TYR   A 1 83  ? 14.221 17.080  23.960 0.44 24.05  ? 89  TYR   A CB  1 
ATOM   672  C  CG  . TYR   A 1 83  ? 15.270 16.409  24.807 0.44 23.66  ? 89  TYR   A CG  1 
ATOM   673  C  CD1 . TYR   A 1 83  ? 16.614 16.670  24.602 0.44 23.45  ? 89  TYR   A CD1 1 
ATOM   674  C  CD2 . TYR   A 1 83  ? 14.928 15.560  25.846 0.44 23.29  ? 89  TYR   A CD2 1 
ATOM   675  C  CE1 . TYR   A 1 83  ? 17.595 16.079  25.380 0.44 23.82  ? 89  TYR   A CE1 1 
ATOM   676  C  CE2 . TYR   A 1 83  ? 15.896 14.959  26.635 0.44 23.19  ? 89  TYR   A CE2 1 
ATOM   677  C  CZ  . TYR   A 1 83  ? 17.235 15.221  26.401 0.44 23.48  ? 89  TYR   A CZ  1 
ATOM   678  O  OH  . TYR   A 1 83  ? 18.203 14.642  27.167 0.44 24.74  ? 89  TYR   A OH  1 
ATOM   679  N  N   . TYR   A 1 84  ? 11.930 19.388  23.216 0.44 23.22  ? 90  TYR   A N   1 
ATOM   680  C  CA  . TYR   A 1 84  ? 11.234 20.229  22.206 0.44 22.52  ? 90  TYR   A CA  1 
ATOM   681  C  C   . TYR   A 1 84  ? 9.973  20.831  22.825 0.44 22.50  ? 90  TYR   A C   1 
ATOM   682  O  O   . TYR   A 1 84  ? 9.506  20.370  23.865 0.44 22.01  ? 90  TYR   A O   1 
ATOM   683  C  CB  . TYR   A 1 84  ? 10.920 19.403  20.954 0.44 21.90  ? 90  TYR   A CB  1 
ATOM   684  C  CG  . TYR   A 1 84  ? 12.133 18.876  20.227 0.44 21.34  ? 90  TYR   A CG  1 
ATOM   685  C  CD1 . TYR   A 1 84  ? 13.035 19.739  19.624 0.44 20.96  ? 90  TYR   A CD1 1 
ATOM   686  C  CD2 . TYR   A 1 84  ? 12.389 17.516  20.141 0.44 21.09  ? 90  TYR   A CD2 1 
ATOM   687  C  CE1 . TYR   A 1 84  ? 14.155 19.269  18.955 0.44 20.86  ? 90  TYR   A CE1 1 
ATOM   688  C  CE2 . TYR   A 1 84  ? 13.504 17.028  19.477 0.44 21.17  ? 90  TYR   A CE2 1 
ATOM   689  C  CZ  . TYR   A 1 84  ? 14.393 17.907  18.883 0.44 20.67  ? 90  TYR   A CZ  1 
ATOM   690  O  OH  . TYR   A 1 84  ? 15.491 17.443  18.218 0.44 20.28  ? 90  TYR   A OH  1 
ATOM   691  N  N   . PRO   A 1 85  ? 9.415  21.913  22.234 0.44 22.23  ? 91  PRO   A N   1 
ATOM   692  C  CA  . PRO   A 1 85  ? 8.067  22.372  22.569 0.44 22.01  ? 91  PRO   A CA  1 
ATOM   693  C  C   . PRO   A 1 85  ? 7.007  21.574  21.792 0.44 22.05  ? 91  PRO   A C   1 
ATOM   694  O  O   . PRO   A 1 85  ? 7.379  20.701  21.032 0.44 21.53  ? 91  PRO   A O   1 
ATOM   695  C  CB  . PRO   A 1 85  ? 8.107  23.841  22.126 0.44 22.21  ? 91  PRO   A CB  1 
ATOM   696  C  CG  . PRO   A 1 85  ? 9.005  23.814  20.908 0.44 22.28  ? 91  PRO   A CG  1 
ATOM   697  C  CD  . PRO   A 1 85  ? 10.061 22.774  21.229 0.44 22.14  ? 91  PRO   A CD  1 
ATOM   698  N  N   . ALA   A 1 86  ? 5.726  21.904  21.984 0.44 21.33  ? 92  ALA   A N   1 
ATOM   699  C  CA  . ALA   A 1 86  ? 4.578  21.303  21.264 0.44 21.10  ? 92  ALA   A CA  1 
ATOM   700  C  C   . ALA   A 1 86  ? 4.585  21.789  19.811 0.44 20.55  ? 92  ALA   A C   1 
ATOM   701  O  O   . ALA   A 1 86  ? 4.115  22.922  19.560 0.44 20.80  ? 92  ALA   A O   1 
ATOM   702  C  CB  . ALA   A 1 86  ? 3.283  21.659  21.951 0.44 21.28  ? 92  ALA   A CB  1 
ATOM   703  N  N   . ARG   A 1 87  ? 5.094  20.956  18.895 0.44 19.66  ? 93  ARG   A N   1 
ATOM   704  C  CA  . ARG   A 1 87  ? 5.330  21.321  17.474 0.44 18.89  ? 93  ARG   A CA  1 
ATOM   705  C  C   . ARG   A 1 87  ? 4.920  20.167  16.553 0.44 18.09  ? 93  ARG   A C   1 
ATOM   706  O  O   . ARG   A 1 87  ? 4.586  19.070  17.065 0.44 16.65  ? 93  ARG   A O   1 
ATOM   707  C  CB  . ARG   A 1 87  ? 6.813  21.643  17.257 0.44 18.80  ? 93  ARG   A CB  1 
ATOM   708  C  CG  . ARG   A 1 87  ? 7.724  20.432  17.415 0.44 18.88  ? 93  ARG   A CG  1 
ATOM   709  C  CD  . ARG   A 1 87  ? 9.195  20.735  17.197 0.44 19.04  ? 93  ARG   A CD  1 
ATOM   710  N  NE  . ARG   A 1 87  ? 10.003 19.523  17.292 0.44 19.14  ? 93  ARG   A NE  1 
ATOM   711  C  CZ  . ARG   A 1 87  ? 11.271 19.404  16.898 0.44 19.17  ? 93  ARG   A CZ  1 
ATOM   712  N  NH1 . ARG   A 1 87  ? 11.920 20.424  16.360 0.44 20.08  ? 93  ARG   A NH1 1 
ATOM   713  N  NH2 . ARG   A 1 87  ? 11.889 18.247  17.038 0.44 19.06  ? 93  ARG   A NH2 1 
ATOM   714  N  N   . TYR   A 1 88  ? 4.973  20.414  15.240 0.44 18.44  ? 94  TYR   A N   1 
ATOM   715  C  CA  . TYR   A 1 88  ? 4.903  19.383  14.172 0.44 18.55  ? 94  TYR   A CA  1 
ATOM   716  C  C   . TYR   A 1 88  ? 6.304  18.827  13.914 0.44 18.16  ? 94  TYR   A C   1 
ATOM   717  O  O   . TYR   A 1 88  ? 7.216  19.624  13.609 0.44 18.12  ? 94  TYR   A O   1 
ATOM   718  C  CB  . TYR   A 1 88  ? 4.332  19.967  12.880 0.44 19.14  ? 94  TYR   A CB  1 
ATOM   719  C  CG  . TYR   A 1 88  ? 2.880  20.349  12.983 0.44 19.56  ? 94  TYR   A CG  1 
ATOM   720  C  CD1 . TYR   A 1 88  ? 1.883  19.404  12.799 0.44 19.97  ? 94  TYR   A CD1 1 
ATOM   721  C  CD2 . TYR   A 1 88  ? 2.504  21.647  13.284 0.44 20.16  ? 94  TYR   A CD2 1 
ATOM   722  C  CE1 . TYR   A 1 88  ? 0.544  19.742  12.903 0.44 20.03  ? 94  TYR   A CE1 1 
ATOM   723  C  CE2 . TYR   A 1 88  ? 1.171  22.002  13.389 0.44 20.35  ? 94  TYR   A CE2 1 
ATOM   724  C  CZ  . TYR   A 1 88  ? 0.189  21.047  13.197 0.44 20.69  ? 94  TYR   A CZ  1 
ATOM   725  O  OH  . TYR   A 1 88  ? -1.117 21.417  13.300 0.44 21.50  ? 94  TYR   A OH  1 
ATOM   726  N  N   . GLN   A 1 89  ? 6.459  17.507  14.042 0.44 17.61  ? 95  GLN   A N   1 
ATOM   727  C  CA  . GLN   A 1 89  ? 7.645  16.745  13.571 0.44 17.10  ? 95  GLN   A CA  1 
ATOM   728  C  C   . GLN   A 1 89  ? 7.264  16.048  12.260 0.44 16.87  ? 95  GLN   A C   1 
ATOM   729  O  O   . GLN   A 1 89  ? 6.185  15.415  12.225 0.44 16.68  ? 95  GLN   A O   1 
ATOM   730  C  CB  . GLN   A 1 89  ? 8.085  15.750  14.646 0.44 16.73  ? 95  GLN   A CB  1 
ATOM   731  C  CG  . GLN   A 1 89  ? 9.545  15.321  14.553 0.44 16.59  ? 95  GLN   A CG  1 
ATOM   732  C  CD  . GLN   A 1 89  ? 10.066 14.790  15.865 0.44 16.22  ? 95  GLN   A CD  1 
ATOM   733  O  OE1 . GLN   A 1 89  ? 9.982  15.447  16.902 0.44 16.55  ? 95  GLN   A OE1 1 
ATOM   734  N  NE2 . GLN   A 1 89  ? 10.626 13.590  15.831 0.44 15.89  ? 95  GLN   A NE2 1 
ATOM   735  N  N   . SER   A 1 90  ? 8.093  16.193  11.221 1.00 16.03  ? 96  SER   A N   1 
ATOM   736  C  CA  . SER   A 1 90  ? 7.886  15.557  9.890  1.00 17.59  ? 96  SER   A CA  1 
ATOM   737  C  C   . SER   A 1 90  ? 8.457  14.134  9.861  1.00 18.38  ? 96  SER   A C   1 
ATOM   738  O  O   . SER   A 1 90  ? 9.326  13.814  10.694 1.00 18.81  ? 96  SER   A O   1 
ATOM   739  C  CB  . SER   A 1 90  ? 8.470  16.392  8.791  1.00 19.33  ? 96  SER   A CB  1 
ATOM   740  O  OG  . SER   A 1 90  ? 9.876  16.430  8.881  1.00 20.35  ? 96  SER   A OG  1 
ATOM   741  N  N   . HIS   A 1 91  ? 8.007  13.334  8.893  1.00 17.06  ? 97  HIS   A N   1 
ATOM   742  C  CA  . HIS   A 1 91  ? 8.513  11.958  8.634  1.00 17.38  ? 97  HIS   A CA  1 
ATOM   743  C  C   . HIS   A 1 91  ? 8.424  11.162  9.948  1.00 15.87  ? 97  HIS   A C   1 
ATOM   744  O  O   . HIS   A 1 91  ? 9.360  10.416  10.249 1.00 14.75  ? 97  HIS   A O   1 
ATOM   745  C  CB  . HIS   A 1 91  ? 9.950  11.997  8.058  1.00 17.74  ? 97  HIS   A CB  1 
ATOM   746  C  CG  . HIS   A 1 91  ? 10.130 12.720  6.759  1.00 18.93  ? 97  HIS   A CG  1 
ATOM   747  N  ND1 . HIS   A 1 91  ? 10.427 12.052  5.585  1.00 21.52  ? 97  HIS   A ND1 1 
ATOM   748  C  CD2 . HIS   A 1 91  ? 10.138 14.040  6.456  1.00 20.59  ? 97  HIS   A CD2 1 
ATOM   749  C  CE1 . HIS   A 1 91  ? 10.571 12.926  4.603  1.00 21.48  ? 97  HIS   A CE1 1 
ATOM   750  N  NE2 . HIS   A 1 91  ? 10.388 14.152  5.112  1.00 19.78  ? 97  HIS   A NE2 1 
ATOM   751  N  N   . LEU   A 1 92  ? 7.356  11.355  10.722 1.00 14.99  ? 98  LEU   A N   1 
ATOM   752  C  CA  . LEU   A 1 92  ? 7.092  10.636  11.980 1.00 15.63  ? 98  LEU   A CA  1 
ATOM   753  C  C   . LEU   A 1 92  ? 6.083  9.527   11.699 1.00 14.64  ? 98  LEU   A C   1 
ATOM   754  O  O   . LEU   A 1 92  ? 5.098  9.771   10.984 1.00 15.61  ? 98  LEU   A O   1 
ATOM   755  C  CB  . LEU   A 1 92  ? 6.525  11.593  13.021 1.00 15.37  ? 98  LEU   A CB  1 
ATOM   756  C  CG  . LEU   A 1 92  ? 6.392  11.015  14.414 1.00 17.43  ? 98  LEU   A CG  1 
ATOM   757  C  CD1 . LEU   A 1 92  ? 7.778  10.678  14.922 1.00 16.98  ? 98  LEU   A CD1 1 
ATOM   758  C  CD2 . LEU   A 1 92  ? 5.619  12.009  15.256 1.00 16.88  ? 98  LEU   A CD2 1 
ATOM   759  N  N   . MET   A 1 93  ? 6.318  8.368   12.306 1.00 17.18  ? 99  MET   A N   1 
ATOM   760  C  CA  . MET   A 1 93  ? 5.404  7.200   12.219 1.00 17.06  ? 99  MET   A CA  1 
ATOM   761  C  C   . MET   A 1 93  ? 4.934  6.896   13.622 1.00 19.30  ? 99  MET   A C   1 
ATOM   762  O  O   . MET   A 1 93  ? 5.752  6.770   14.511 1.00 19.70  ? 99  MET   A O   1 
ATOM   763  C  CB  . MET   A 1 93  ? 6.114  5.986   11.626 1.00 16.75  ? 99  MET   A CB  1 
ATOM   764  C  CG  . MET   A 1 93  ? 6.627  6.251   10.268 1.00 17.25  ? 99  MET   A CG  1 
ATOM   765  S  SD  . MET   A 1 93  ? 7.678  4.946   9.693  1.00 18.58  ? 99  MET   A SD  1 
ATOM   766  C  CE  . MET   A 1 93  ? 9.160  5.050   10.696 1.00 17.54  ? 99  MET   A CE  1 
ATOM   767  N  N   . LEU   A 1 94  ? 3.620  6.821   13.785 1.00 19.90  ? 100 LEU   A N   1 
ATOM   768  C  CA  . LEU   A 1 94  ? 3.017  6.460   15.065 1.00 20.48  ? 100 LEU   A CA  1 
ATOM   769  C  C   . LEU   A 1 94  ? 2.690  4.979   14.968 1.00 19.07  ? 100 LEU   A C   1 
ATOM   770  O  O   . LEU   A 1 94  ? 2.326  4.457   13.884 1.00 20.67  ? 100 LEU   A O   1 
ATOM   771  C  CB  . LEU   A 1 94  ? 1.793  7.330   15.349 1.00 21.56  ? 100 LEU   A CB  1 
ATOM   772  C  CG  . LEU   A 1 94  ? 2.101  8.818   15.478 1.00 23.88  ? 100 LEU   A CG  1 
ATOM   773  C  CD1 . LEU   A 1 94  ? 0.833  9.649   15.361 1.00 27.22  ? 100 LEU   A CD1 1 
ATOM   774  C  CD2 . LEU   A 1 94  ? 2.858  9.124   16.758 1.00 25.36  ? 100 LEU   A CD2 1 
ATOM   775  N  N   . ALA   A 1 95  ? 2.978  4.346   16.061 1.00 18.08  ? 101 ALA   A N   1 
ATOM   776  C  CA  . ALA   A 1 95  ? 2.418  3.040   16.379 1.00 17.97  ? 101 ALA   A CA  1 
ATOM   777  C  C   . ALA   A 1 95  ? 1.679  3.326   17.653 1.00 17.60  ? 101 ALA   A C   1 
ATOM   778  O  O   . ALA   A 1 95  ? 1.957  4.345   18.281 1.00 17.12  ? 101 ALA   A O   1 
ATOM   779  C  CB  . ALA   A 1 95  ? 3.495  2.009   16.576 1.00 17.31  ? 101 ALA   A CB  1 
ATOM   780  N  N   . VAL   A 1 96  ? 0.802  2.408   18.009 1.00 19.59  ? 102 VAL   A N   1 
ATOM   781  C  CA  . VAL   A 1 96  ? 0.262  2.356   19.379 1.00 18.34  ? 102 VAL   A CA  1 
ATOM   782  C  C   . VAL   A 1 96  ? 1.271  1.587   20.220 1.00 19.11  ? 102 VAL   A C   1 
ATOM   783  O  O   . VAL   A 1 96  ? 1.586  0.413   19.878 1.00 20.25  ? 102 VAL   A O   1 
ATOM   784  C  CB  . VAL   A 1 96  ? -1.121 1.692   19.381 1.00 19.68  ? 102 VAL   A CB  1 
ATOM   785  C  CG1 . VAL   A 1 96  ? -1.668 1.573   20.785 1.00 21.14  ? 102 VAL   A CG1 1 
ATOM   786  C  CG2 . VAL   A 1 96  ? -2.092 2.445   18.480 1.00 19.27  ? 102 VAL   A CG2 1 
ATOM   787  N  N   . GLY   A 1 97  ? 1.754  2.199   21.290 0.44 18.18  ? 103 GLY   A N   1 
ATOM   788  C  CA  . GLY   A 1 97  ? 2.778  1.580   22.141 0.44 17.94  ? 103 GLY   A CA  1 
ATOM   789  C  C   . GLY   A 1 97  ? 3.288  2.578   23.141 0.44 17.75  ? 103 GLY   A C   1 
ATOM   790  O  O   . GLY   A 1 97  ? 3.223  3.792   22.856 0.44 18.02  ? 103 GLY   A O   1 
ATOM   791  N  N   . HIS   A 1 98  ? 3.757  2.085   24.279 0.44 16.37  ? 104 HIS   A N   1 
ATOM   792  C  CA  . HIS   A 1 98  ? 4.288  2.940   25.359 0.44 16.49  ? 104 HIS   A CA  1 
ATOM   793  C  C   . HIS   A 1 98  ? 5.580  3.597   24.874 0.44 15.69  ? 104 HIS   A C   1 
ATOM   794  O  O   . HIS   A 1 98  ? 6.381  2.922   24.202 0.44 15.73  ? 104 HIS   A O   1 
ATOM   795  C  CB  . HIS   A 1 98  ? 4.500  2.161   26.654 0.44 16.44  ? 104 HIS   A CB  1 
ATOM   796  C  CG  . HIS   A 1 98  ? 5.045  3.050   27.710 0.44 16.47  ? 104 HIS   A CG  1 
ATOM   797  N  ND1 . HIS   A 1 98  ? 4.323  4.116   28.205 0.44 15.76  ? 104 HIS   A ND1 1 
ATOM   798  C  CD2 . HIS   A 1 98  ? 6.260  3.103   28.289 0.44 15.96  ? 104 HIS   A CD2 1 
ATOM   799  C  CE1 . HIS   A 1 98  ? 5.051  4.755   29.093 0.44 16.02  ? 104 HIS   A CE1 1 
ATOM   800  N  NE2 . HIS   A 1 98  ? 6.245  4.157   29.157 0.44 15.63  ? 104 HIS   A NE2 1 
ATOM   801  N  N   . SER   A 1 99  ? 5.765  4.869   25.220 0.44 14.68  ? 105 SER   A N   1 
ATOM   802  C  CA  . SER   A 1 99  ? 7.011  5.634   24.976 0.44 14.08  ? 105 SER   A CA  1 
ATOM   803  C  C   . SER   A 1 99  ? 7.041  6.847   25.909 0.44 14.08  ? 105 SER   A C   1 
ATOM   804  O  O   . SER   A 1 99  ? 5.948  7.354   26.267 0.44 13.82  ? 105 SER   A O   1 
ATOM   805  C  CB  . SER   A 1 99  ? 7.150  6.023   23.522 0.44 13.74  ? 105 SER   A CB  1 
ATOM   806  O  OG  . SER   A 1 99  ? 6.288  7.100   23.194 0.44 12.59  ? 105 SER   A OG  1 
ATOM   807  N  N   . GLU   A 1 100 ? 8.253  7.226   26.318 0.44 14.70  ? 106 GLU   A N   1 
ATOM   808  C  CA  . GLU   A 1 100 ? 8.595  8.432   27.119 0.44 15.30  ? 106 GLU   A CA  1 
ATOM   809  C  C   . GLU   A 1 100 ? 9.785  9.097   26.427 0.44 15.61  ? 106 GLU   A C   1 
ATOM   810  O  O   . GLU   A 1 100 ? 10.361 8.510   25.519 0.44 15.07  ? 106 GLU   A O   1 
ATOM   811  C  CB  . GLU   A 1 100 ? 8.880  8.019   28.567 0.44 15.52  ? 106 GLU   A CB  1 
ATOM   812  C  CG  . GLU   A 1 100 ? 7.769  7.195   29.201 0.44 15.95  ? 106 GLU   A CG  1 
ATOM   813  C  CD  . GLU   A 1 100 ? 8.105  6.599   30.559 0.44 16.20  ? 106 GLU   A CD  1 
ATOM   814  O  OE1 . GLU   A 1 100 ? 8.936  7.194   31.267 0.44 16.55  ? 106 GLU   A OE1 1 
ATOM   815  O  OE2 . GLU   A 1 100 ? 7.537  5.541   30.903 0.44 16.27  ? 106 GLU   A OE2 1 
ATOM   816  N  N   . PRO   A 1 101 ? 10.210 10.328  26.799 0.44 15.76  ? 107 PRO   A N   1 
ATOM   817  C  CA  . PRO   A 1 101 ? 11.308 11.002  26.097 0.44 16.01  ? 107 PRO   A CA  1 
ATOM   818  C  C   . PRO   A 1 101 ? 12.584 10.164  25.918 0.44 16.17  ? 107 PRO   A C   1 
ATOM   819  O  O   . PRO   A 1 101 ? 13.049 10.083  24.795 0.44 15.88  ? 107 PRO   A O   1 
ATOM   820  C  CB  . PRO   A 1 101 ? 11.609 12.213  26.991 0.44 16.28  ? 107 PRO   A CB  1 
ATOM   821  C  CG  . PRO   A 1 101 ? 10.281 12.509  27.645 0.44 16.41  ? 107 PRO   A CG  1 
ATOM   822  C  CD  . PRO   A 1 101 ? 9.671  11.145  27.897 0.44 16.19  ? 107 PRO   A CD  1 
ATOM   823  N  N   . GLY   A 1 102 ? 13.092 9.571   27.004 0.44 15.81  ? 108 GLY   A N   1 
ATOM   824  C  CA  . GLY   A 1 102 ? 14.363 8.821   27.066 0.44 15.72  ? 108 GLY   A CA  1 
ATOM   825  C  C   . GLY   A 1 102 ? 14.386 7.577   26.187 0.44 15.46  ? 108 GLY   A C   1 
ATOM   826  O  O   . GLY   A 1 102 ? 15.482 7.023   26.006 0.44 15.25  ? 108 GLY   A O   1 
ATOM   827  N  N   . ASP   A 1 103 ? 13.232 7.128   25.677 0.44 15.84  ? 109 ASP   A N   1 
ATOM   828  C  CA  . ASP   A 1 103 ? 13.123 5.933   24.792 0.44 15.33  ? 109 ASP   A CA  1 
ATOM   829  C  C   . ASP   A 1 103 ? 13.718 6.242   23.416 0.44 15.26  ? 109 ASP   A C   1 
ATOM   830  O  O   . ASP   A 1 103 ? 13.915 5.297   22.626 0.44 14.18  ? 109 ASP   A O   1 
ATOM   831  C  CB  . ASP   A 1 103 ? 11.673 5.466   24.677 0.44 15.40  ? 109 ASP   A CB  1 
ATOM   832  C  CG  . ASP   A 1 103 ? 11.208 4.716   25.907 0.44 15.40  ? 109 ASP   A CG  1 
ATOM   833  O  OD1 . ASP   A 1 103 ? 12.033 3.982   26.474 0.44 14.87  ? 109 ASP   A OD1 1 
ATOM   834  O  OD2 . ASP   A 1 103 ? 10.027 4.875   26.279 0.44 16.19  ? 109 ASP   A OD2 1 
ATOM   835  N  N   . CYS   A 1 104 ? 13.974 7.520   23.143 1.00 15.42  ? 110 CYS   A N   1 
ATOM   836  C  CA  . CYS   A 1 104 ? 14.581 7.979   21.889 1.00 14.57  ? 110 CYS   A CA  1 
ATOM   837  C  C   . CYS   A 1 104 ? 15.823 7.214   21.584 1.00 11.46  ? 110 CYS   A C   1 
ATOM   838  O  O   . CYS   A 1 104 ? 16.658 7.053   22.450 1.00 15.34  ? 110 CYS   A O   1 
ATOM   839  C  CB  . CYS   A 1 104 ? 15.043 9.397   21.985 1.00 15.93  ? 110 CYS   A CB  1 
ATOM   840  S  SG  . CYS   A 1 104 ? 13.551 10.314  22.272 1.00 18.49  ? 110 CYS   A SG  1 
ATOM   841  N  N   . GLY   A 1 105 ? 15.907 6.843   20.306 1.00 8.89   ? 111 GLY   A N   1 
ATOM   842  C  CA  . GLY   A 1 105 ? 17.090 6.148   19.814 1.00 8.69   ? 111 GLY   A CA  1 
ATOM   843  C  C   . GLY   A 1 105 ? 16.837 4.656   19.655 1.00 8.80   ? 111 GLY   A C   1 
ATOM   844  O  O   . GLY   A 1 105 ? 17.700 3.972   19.090 1.00 8.25   ? 111 GLY   A O   1 
ATOM   845  N  N   . GLY   A 1 106 ? 15.836 4.095   20.348 1.00 8.24   ? 112 GLY   A N   1 
ATOM   846  C  CA  . GLY   A 1 106 ? 15.391 2.687   20.206 1.00 7.43   ? 112 GLY   A CA  1 
ATOM   847  C  C   . GLY   A 1 106 ? 15.166 2.325   18.756 1.00 6.04   ? 112 GLY   A C   1 
ATOM   848  O  O   . GLY   A 1 106 ? 14.426 3.076   18.096 1.00 5.82   ? 112 GLY   A O   1 
ATOM   849  N  N   . ILE   A 1 107 ? 15.631 1.173   18.328 1.00 6.36   ? 113 ILE   A N   1 
ATOM   850  C  CA  . ILE   A 1 107 ? 15.458 0.780   16.907 1.00 6.34   ? 113 ILE   A CA  1 
ATOM   851  C  C   . ILE   A 1 107 ? 14.108 0.130   16.667 1.00 5.62   ? 113 ILE   A C   1 
ATOM   852  O  O   . ILE   A 1 107 ? 13.656 -0.710  17.491 1.00 5.08   ? 113 ILE   A O   1 
ATOM   853  C  CB  . ILE   A 1 107 ? 16.600 -0.171  16.530 1.00 7.96   ? 113 ILE   A CB  1 
ATOM   854  C  CG1 . ILE   A 1 107 ? 17.830 0.712   16.306 1.00 9.51   ? 113 ILE   A CG1 1 
ATOM   855  C  CG2 . ILE   A 1 107 ? 16.284 -0.987  15.301 1.00 8.11   ? 113 ILE   A CG2 1 
ATOM   856  C  CD1 . ILE   A 1 107 ? 19.172 -0.007  16.114 1.00 10.47  ? 113 ILE   A CD1 1 
ATOM   857  N  N   . LEU   A 1 108 ? 13.480 0.554   15.568 1.00 5.04   ? 114 LEU   A N   1 
ATOM   858  C  CA  . LEU   A 1 108 ? 12.333 -0.136  14.920 1.00 5.39   ? 114 LEU   A CA  1 
ATOM   859  C  C   . LEU   A 1 108 ? 12.914 -0.943  13.767 1.00 5.77   ? 114 LEU   A C   1 
ATOM   860  O  O   . LEU   A 1 108 ? 13.607 -0.366  12.918 1.00 5.91   ? 114 LEU   A O   1 
ATOM   861  C  CB  . LEU   A 1 108 ? 11.326 0.891   14.423 1.00 5.21   ? 114 LEU   A CB  1 
ATOM   862  C  CG  . LEU   A 1 108 ? 10.113 0.341   13.664 1.00 5.97   ? 114 LEU   A CG  1 
ATOM   863  C  CD1 . LEU   A 1 108 ? 9.270  -0.576  14.543 1.00 5.98   ? 114 LEU   A CD1 1 
ATOM   864  C  CD2 . LEU   A 1 108 ? 9.267  1.491   13.122 1.00 6.40   ? 114 LEU   A CD2 1 
ATOM   865  N  N   . ARG   A 1 109 ? 12.650 -2.255  13.754 1.00 5.68   ? 115 ARG   A N   1 
ATOM   866  C  CA  . ARG   A 1 109 ? 13.137 -3.149  12.635 1.00 6.46   ? 115 ARG   A CA  1 
ATOM   867  C  C   . ARG   A 1 109 ? 11.991 -3.966  12.022 1.00 7.69   ? 115 ARG   A C   1 
ATOM   868  O  O   . ARG   A 1 109 ? 11.079 -4.312  12.722 1.00 7.93   ? 115 ARG   A O   1 
ATOM   869  C  CB  . ARG   A 1 109 ? 14.279 -4.056  13.110 1.00 7.98   ? 115 ARG   A CB  1 
ATOM   870  C  CG  . ARG   A 1 109 ? 13.917 -4.952  14.286 1.00 9.77   ? 115 ARG   A CG  1 
ATOM   871  C  CD  . ARG   A 1 109 ? 15.089 -5.707  14.909 1.00 11.57  ? 115 ARG   A CD  1 
ATOM   872  N  NE  . ARG   A 1 109 ? 15.903 -4.956  15.859 1.00 13.55  ? 115 ARG   A NE  1 
ATOM   873  C  CZ  . ARG   A 1 109 ? 17.217 -4.701  15.742 1.00 15.50  ? 115 ARG   A CZ  1 
ATOM   874  N  NH1 . ARG   A 1 109 ? 17.903 -5.042  14.655 1.00 16.81  ? 115 ARG   A NH1 1 
ATOM   875  N  NH2 . ARG   A 1 109 ? 17.820 -3.975  16.665 1.00 15.90  ? 115 ARG   A NH2 1 
ATOM   876  N  N   . CYS   A 1 110 ? 12.074 -4.237  10.709 1.00 9.14   ? 116 CYS   A N   1 
ATOM   877  C  CA  . CYS   A 1 110 ? 11.111 -5.066  9.913  1.00 10.44  ? 116 CYS   A CA  1 
ATOM   878  C  C   . CYS   A 1 110 ? 11.954 -6.132  9.234  1.00 12.85  ? 116 CYS   A C   1 
ATOM   879  O  O   . CYS   A 1 110 ? 13.172 -6.246  9.551  1.00 12.19  ? 116 CYS   A O   1 
ATOM   880  C  CB  . CYS   A 1 110 ? 10.285 -4.268  8.916  1.00 9.65   ? 116 CYS   A CB  1 
ATOM   881  S  SG  . CYS   A 1 110 ? 11.314 -3.644  7.566  1.00 11.66  ? 116 CYS   A SG  1 
ATOM   882  N  N   . GLN   A 1 111 ? 11.370 -6.911  8.328  1.00 15.92  ? 117 GLN   A N   1 
ATOM   883  C  CA  . GLN   A 1 111 ? 12.117 -8.034  7.703  1.00 16.43  ? 117 GLN   A CA  1 
ATOM   884  C  C   . GLN   A 1 111 ? 13.213 -7.455  6.791  1.00 16.12  ? 117 GLN   A C   1 
ATOM   885  O  O   . GLN   A 1 111 ? 14.148 -8.190  6.434  1.00 19.01  ? 117 GLN   A O   1 
ATOM   886  C  CB  . GLN   A 1 111 ? 11.157 -8.974  6.965  1.00 18.72  ? 117 GLN   A CB  1 
ATOM   887  C  CG  . GLN   A 1 111 ? 10.514 -8.356  5.736  1.00 21.39  ? 117 GLN   A CG  1 
ATOM   888  C  CD  . GLN   A 1 111 ? 9.575  -9.346  5.091  1.00 24.74  ? 117 GLN   A CD  1 
ATOM   889  O  OE1 . GLN   A 1 111 ? 8.365  -9.265  5.248  1.00 29.84  ? 117 GLN   A OE1 1 
ATOM   890  N  NE2 . GLN   A 1 111 ? 10.145 -10.304 4.373  1.00 26.25  ? 117 GLN   A NE2 1 
ATOM   891  N  N   . HIS   A 1 112 ? 13.078 -6.191  6.395  1.00 15.49  ? 118 HIS   A N   1 
ATOM   892  C  CA  . HIS   A 1 112 ? 13.989 -5.527  5.427  1.00 14.37  ? 118 HIS   A CA  1 
ATOM   893  C  C   . HIS   A 1 112 ? 15.156 -4.820  6.132  1.00 15.66  ? 118 HIS   A C   1 
ATOM   894  O  O   . HIS   A 1 112 ? 16.019 -4.286  5.394  1.00 15.97  ? 118 HIS   A O   1 
ATOM   895  C  CB  . HIS   A 1 112 ? 13.171 -4.532  4.624  1.00 14.21  ? 118 HIS   A CB  1 
ATOM   896  C  CG  . HIS   A 1 112 ? 12.055 -5.164  3.864  1.00 14.77  ? 118 HIS   A CG  1 
ATOM   897  N  ND1 . HIS   A 1 112 ? 10.731 -4.836  4.041  1.00 12.10  ? 118 HIS   A ND1 1 
ATOM   898  C  CD2 . HIS   A 1 112 ? 12.085 -6.049  2.843  1.00 14.54  ? 118 HIS   A CD2 1 
ATOM   899  C  CE1 . HIS   A 1 112 ? 9.995  -5.573  3.228  1.00 15.02  ? 118 HIS   A CE1 1 
ATOM   900  N  NE2 . HIS   A 1 112 ? 10.805 -6.307  2.474  1.00 16.66  ? 118 HIS   A NE2 1 
ATOM   901  N  N   . GLY   A 1 113 ? 15.181 -4.795  7.477  1.00 16.78  ? 119 GLY   A N   1 
ATOM   902  C  CA  . GLY   A 1 113 ? 16.276 -4.235  8.312  1.00 16.97  ? 119 GLY   A CA  1 
ATOM   903  C  C   . GLY   A 1 113 ? 15.824 -3.212  9.346  1.00 18.56  ? 119 GLY   A C   1 
ATOM   904  O  O   . GLY   A 1 113 ? 14.662 -3.282  9.853  1.00 15.30  ? 119 GLY   A O   1 
ATOM   905  N  N   . VAL   A 1 114 ? 16.688 -2.232  9.614  1.00 16.35  ? 120 VAL   A N   1 
ATOM   906  C  CA  . VAL   A 1 114 ? 16.367 -1.101  10.522 1.00 13.52  ? 120 VAL   A CA  1 
ATOM   907  C  C   . VAL   A 1 114 ? 15.444 -0.174  9.765  1.00 13.00  ? 120 VAL   A C   1 
ATOM   908  O  O   . VAL   A 1 114 ? 15.826 0.255   8.641  1.00 16.12  ? 120 VAL   A O   1 
ATOM   909  C  CB  . VAL   A 1 114 ? 17.615 -0.333  10.968 1.00 13.18  ? 120 VAL   A CB  1 
ATOM   910  C  CG1 . VAL   A 1 114 ? 17.248 0.895   11.773 1.00 12.64  ? 120 VAL   A CG1 1 
ATOM   911  C  CG2 . VAL   A 1 114 ? 18.526 -1.207  11.749 1.00 12.76  ? 120 VAL   A CG2 1 
ATOM   912  N  N   . VAL   A 1 115 ? 14.272 0.130   10.321 1.00 11.35  ? 121 VAL   A N   1 
ATOM   913  C  CA  . VAL   A 1 115 ? 13.253 1.041   9.725  1.00 11.63  ? 121 VAL   A CA  1 
ATOM   914  C  C   . VAL   A 1 115 ? 13.507 2.485   10.169 1.00 11.08  ? 121 VAL   A C   1 
ATOM   915  O  O   . VAL   A 1 115 ? 13.307 3.413   9.387  1.00 12.13  ? 121 VAL   A O   1 
ATOM   916  C  CB  . VAL   A 1 115 ? 11.818 0.599   10.092 1.00 11.31  ? 121 VAL   A CB  1 
ATOM   917  C  CG1 . VAL   A 1 115 ? 10.763 1.609   9.660  1.00 11.52  ? 121 VAL   A CG1 1 
ATOM   918  C  CG2 . VAL   A 1 115 ? 11.547 -0.811  9.575  1.00 11.99  ? 121 VAL   A CG2 1 
ATOM   919  N  N   . GLY   A 1 116 ? 13.794 2.668   11.448 1.00 10.13  ? 122 GLY   A N   1 
ATOM   920  C  CA  . GLY   A 1 116 ? 13.917 4.004   11.996 1.00 8.77   ? 122 GLY   A CA  1 
ATOM   921  C  C   . GLY   A 1 116 ? 14.213 3.922   13.466 1.00 7.38   ? 122 GLY   A C   1 
ATOM   922  O  O   . GLY   A 1 116 ? 14.508 2.783   13.969 1.00 8.20   ? 122 GLY   A O   1 
ATOM   923  N  N   . ILE   A 1 117 ? 14.268 5.076   14.120 0.44 7.45   ? 123 ILE   A N   1 
ATOM   924  C  CA  . ILE   A 1 117 ? 14.529 5.155   15.579 0.44 7.18   ? 123 ILE   A CA  1 
ATOM   925  C  C   . ILE   A 1 117 ? 13.359 5.906   16.200 0.44 7.02   ? 123 ILE   A C   1 
ATOM   926  O  O   . ILE   A 1 117 ? 12.711 6.689   15.480 0.44 7.18   ? 123 ILE   A O   1 
ATOM   927  C  CB  . ILE   A 1 117 ? 15.889 5.810   15.906 0.44 7.34   ? 123 ILE   A CB  1 
ATOM   928  C  CG1 . ILE   A 1 117 ? 16.120 7.134   15.167 0.44 7.58   ? 123 ILE   A CG1 1 
ATOM   929  C  CG2 . ILE   A 1 117 ? 17.027 4.825   15.680 0.44 7.39   ? 123 ILE   A CG2 1 
ATOM   930  C  CD1 . ILE   A 1 117 ? 17.279 7.943   15.721 0.44 7.57   ? 123 ILE   A CD1 1 
ATOM   931  N  N   . VAL   A 1 118 ? 13.112 5.671   17.487 0.44 7.08   ? 124 VAL   A N   1 
ATOM   932  C  CA  . VAL   A 1 118 ? 12.037 6.365   18.248 0.44 6.86   ? 124 VAL   A CA  1 
ATOM   933  C  C   . VAL   A 1 118 ? 12.395 7.850   18.240 0.44 7.03   ? 124 VAL   A C   1 
ATOM   934  O  O   . VAL   A 1 118 ? 13.570 8.187   18.449 0.44 6.73   ? 124 VAL   A O   1 
ATOM   935  C  CB  . VAL   A 1 118 ? 11.879 5.821   19.681 0.44 6.81   ? 124 VAL   A CB  1 
ATOM   936  C  CG1 . VAL   A 1 118 ? 10.992 6.718   20.541 0.44 6.87   ? 124 VAL   A CG1 1 
ATOM   937  C  CG2 . VAL   A 1 118 ? 11.346 4.395   19.665 0.44 6.83   ? 124 VAL   A CG2 1 
ATOM   938  N  N   . SER   A 1 119 ? 11.436 8.714   17.926 0.44 7.25   ? 125 SER   A N   1 
ATOM   939  C  CA  . SER   A 1 119 ? 11.680 10.180  17.889 0.44 7.93   ? 125 SER   A CA  1 
ATOM   940  C  C   . SER   A 1 119 ? 10.575 10.960  18.616 0.44 8.10   ? 125 SER   A C   1 
ATOM   941  O  O   . SER   A 1 119 ? 10.929 11.943  19.321 0.44 8.99   ? 125 SER   A O   1 
ATOM   942  C  CB  . SER   A 1 119 ? 11.868 10.656  16.483 0.44 8.34   ? 125 SER   A CB  1 
ATOM   943  O  OG  . SER   A 1 119 ? 12.291 12.008  16.471 0.44 9.31   ? 125 SER   A OG  1 
ATOM   944  N  N   . THR   A 1 120 ? 9.306  10.561  18.483 0.44 8.63   ? 126 THR   A N   1 
ATOM   945  C  CA  . THR   A 1 120 ? 8.159  11.246  19.151 0.44 8.88   ? 126 THR   A CA  1 
ATOM   946  C  C   . THR   A 1 120 ? 7.257  10.235  19.866 0.44 9.31   ? 126 THR   A C   1 
ATOM   947  O  O   . THR   A 1 120 ? 7.542  9.029   19.769 0.44 9.00   ? 126 THR   A O   1 
ATOM   948  C  CB  . THR   A 1 120 ? 7.285  12.000  18.145 0.44 8.97   ? 126 THR   A CB  1 
ATOM   949  O  OG1 . THR   A 1 120 ? 6.503  10.988  17.512 0.44 9.38   ? 126 THR   A OG1 1 
ATOM   950  C  CG2 . THR   A 1 120 ? 8.083  12.836  17.170 0.44 9.18   ? 126 THR   A CG2 1 
ATOM   951  N  N   . GLY   A 1 121 ? 6.193  10.720  20.516 0.44 9.90   ? 127 GLY   A N   1 
ATOM   952  C  CA  . GLY   A 1 121 ? 5.131  9.863   21.084 0.44 10.58  ? 127 GLY   A CA  1 
ATOM   953  C  C   . GLY   A 1 121 ? 4.332  10.564  22.166 0.44 11.62  ? 127 GLY   A C   1 
ATOM   954  O  O   . GLY   A 1 121 ? 4.430  11.803  22.261 0.44 12.26  ? 127 GLY   A O   1 
ATOM   955  N  N   . GLY   A 1 122 ? 3.591  9.772   22.953 0.44 11.87  ? 128 GLY   A N   1 
ATOM   956  C  CA  . GLY   A 1 122 ? 2.679  10.220  24.027 0.44 12.26  ? 128 GLY   A CA  1 
ATOM   957  C  C   . GLY   A 1 122 ? 1.296  9.590   23.897 0.44 13.03  ? 128 GLY   A C   1 
ATOM   958  O  O   . GLY   A 1 122 ? 0.887  9.301   22.750 0.44 12.84  ? 128 GLY   A O   1 
ATOM   959  N  N   . ASN   A 1 123 ? 0.595  9.406   25.024 0.44 13.89  ? 129 ASN   A N   1 
ATOM   960  C  CA  . ASN   A 1 123 ? -0.820 8.945   25.102 0.44 14.23  ? 129 ASN   A CA  1 
ATOM   961  C  C   . ASN   A 1 123 ? -0.969 7.572   24.434 0.44 14.33  ? 129 ASN   A C   1 
ATOM   962  O  O   . ASN   A 1 123 ? -1.975 7.351   23.717 0.44 14.15  ? 129 ASN   A O   1 
ATOM   963  C  CB  . ASN   A 1 123 ? -1.768 9.974   24.483 0.44 14.96  ? 129 ASN   A CB  1 
ATOM   964  C  CG  . ASN   A 1 123 ? -1.645 11.341  25.120 0.44 15.54  ? 129 ASN   A CG  1 
ATOM   965  O  OD1 . ASN   A 1 123 ? -1.391 11.448  26.319 0.44 16.89  ? 129 ASN   A OD1 1 
ATOM   966  N  ND2 . ASN   A 1 123 ? -1.808 12.387  24.325 0.44 16.22  ? 129 ASN   A ND2 1 
ATOM   967  N  N   . GLY   A 1 124 ? -0.007 6.680   24.673 0.44 14.06  ? 130 GLY   A N   1 
ATOM   968  C  CA  . GLY   A 1 124 ? 0.013  5.315   24.119 0.44 13.67  ? 130 GLY   A CA  1 
ATOM   969  C  C   . GLY   A 1 124 ? 0.380  5.304   22.644 0.44 13.36  ? 130 GLY   A C   1 
ATOM   970  O  O   . GLY   A 1 124 ? 0.046  4.324   21.954 0.44 13.39  ? 130 GLY   A O   1 
ATOM   971  N  N   . LEU   A 1 125 ? 1.061  6.354   22.174 0.44 13.05  ? 131 LEU   A N   1 
ATOM   972  C  CA  . LEU   A 1 125 ? 1.589  6.442   20.791 0.44 12.79  ? 131 LEU   A CA  1 
ATOM   973  C  C   . LEU   A 1 125 ? 3.114  6.478   20.849 0.44 11.83  ? 131 LEU   A C   1 
ATOM   974  O  O   . LEU   A 1 125 ? 3.680  6.797   21.924 0.44 12.51  ? 131 LEU   A O   1 
ATOM   975  C  CB  . LEU   A 1 125 ? 1.038  7.685   20.091 0.44 13.07  ? 131 LEU   A CB  1 
ATOM   976  C  CG  . LEU   A 1 125 ? -0.484 7.750   19.988 0.44 13.37  ? 131 LEU   A CG  1 
ATOM   977  C  CD1 . LEU   A 1 125 ? -0.928 8.988   19.225 0.44 13.36  ? 131 LEU   A CD1 1 
ATOM   978  C  CD2 . LEU   A 1 125 ? -1.026 6.495   19.331 0.44 13.76  ? 131 LEU   A CD2 1 
ATOM   979  N  N   . VAL   A 1 126 ? 3.735  6.130   19.727 0.44 10.77  ? 132 VAL   A N   1 
ATOM   980  C  CA  . VAL   A 1 126 ? 5.209  6.184   19.534 0.44 10.06  ? 132 VAL   A CA  1 
ATOM   981  C  C   . VAL   A 1 126 ? 5.449  6.517   18.065 0.44 9.74   ? 132 VAL   A C   1 
ATOM   982  O  O   . VAL   A 1 126 ? 4.841  5.868   17.197 0.44 9.57   ? 132 VAL   A O   1 
ATOM   983  C  CB  . VAL   A 1 126 ? 5.873  4.866   19.976 0.44 9.87   ? 132 VAL   A CB  1 
ATOM   984  C  CG1 . VAL   A 1 126 ? 5.333  3.676   19.201 0.44 9.72   ? 132 VAL   A CG1 1 
ATOM   985  C  CG2 . VAL   A 1 126 ? 7.390  4.945   19.886 0.44 9.83   ? 132 VAL   A CG2 1 
ATOM   986  N  N   . GLY   A 1 127 ? 6.260  7.544   17.822 0.44 9.33   ? 133 GLY   A N   1 
ATOM   987  C  CA  . GLY   A 1 127 ? 6.627  8.018   16.483 0.44 9.62   ? 133 GLY   A CA  1 
ATOM   988  C  C   . GLY   A 1 127 ? 8.052  7.621   16.171 0.44 9.57   ? 133 GLY   A C   1 
ATOM   989  O  O   . GLY   A 1 127 ? 8.927  7.905   16.996 0.44 9.72   ? 133 GLY   A O   1 
ATOM   990  N  N   . PHE   A 1 128 ? 8.286  6.971   15.036 0.44 9.78   ? 134 PHE   A N   1 
ATOM   991  C  CA  . PHE   A 1 128 ? 9.659  6.576   14.641 0.44 10.24  ? 134 PHE   A CA  1 
ATOM   992  C  C   . PHE   A 1 128 ? 10.093 7.505   13.512 0.44 10.94  ? 134 PHE   A C   1 
ATOM   993  O  O   . PHE   A 1 128 ? 9.385  7.597   12.480 0.44 11.71  ? 134 PHE   A O   1 
ATOM   994  C  CB  . PHE   A 1 128 ? 9.740  5.096   14.268 0.44 10.05  ? 134 PHE   A CB  1 
ATOM   995  C  CG  . PHE   A 1 128 ? 9.071  4.168   15.242 0.44 9.61   ? 134 PHE   A CG  1 
ATOM   996  C  CD1 . PHE   A 1 128 ? 9.751  3.676   16.342 0.44 9.26   ? 134 PHE   A CD1 1 
ATOM   997  C  CD2 . PHE   A 1 128 ? 7.756  3.774   15.042 0.44 9.48   ? 134 PHE   A CD2 1 
ATOM   998  C  CE1 . PHE   A 1 128 ? 9.132  2.802   17.221 0.44 9.07   ? 134 PHE   A CE1 1 
ATOM   999  C  CE2 . PHE   A 1 128 ? 7.135  2.908   15.928 0.44 9.36   ? 134 PHE   A CE2 1 
ATOM   1000 C  CZ  . PHE   A 1 128 ? 7.821  2.429   17.022 0.44 9.26   ? 134 PHE   A CZ  1 
ATOM   1001 N  N   . ALA   A 1 129 ? 11.212 8.202   13.721 0.44 11.65  ? 135 ALA   A N   1 
ATOM   1002 C  CA  . ALA   A 1 129 ? 11.896 8.963   12.661 0.44 12.34  ? 135 ALA   A CA  1 
ATOM   1003 C  C   . ALA   A 1 129 ? 12.277 7.948   11.589 0.44 12.68  ? 135 ALA   A C   1 
ATOM   1004 O  O   . ALA   A 1 129 ? 13.200 7.119   11.804 0.44 13.63  ? 135 ALA   A O   1 
ATOM   1005 C  CB  . ALA   A 1 129 ? 13.081 9.719   13.196 0.44 11.91  ? 135 ALA   A CB  1 
ATOM   1006 N  N   . ASP   A 1 130 ? 11.517 7.956   10.502 1.00 13.97  ? 136 ASP   A N   1 
ATOM   1007 C  CA  . ASP   A 1 130 ? 11.781 7.067   9.389  1.00 13.45  ? 136 ASP   A CA  1 
ATOM   1008 C  C   . ASP   A 1 130 ? 13.178 7.422   8.857  1.00 14.53  ? 136 ASP   A C   1 
ATOM   1009 O  O   . ASP   A 1 130 ? 13.552 8.652   8.957  1.00 15.11  ? 136 ASP   A O   1 
ATOM   1010 C  CB  . ASP   A 1 130 ? 10.696 7.302   8.351  1.00 15.30  ? 136 ASP   A CB  1 
ATOM   1011 C  CG  . ASP   A 1 130 ? 10.963 6.448   7.148  1.00 15.58  ? 136 ASP   A CG  1 
ATOM   1012 O  OD1 . ASP   A 1 130 ? 11.164 5.236   7.342  1.00 17.08  ? 136 ASP   A OD1 1 
ATOM   1013 O  OD2 . ASP   A 1 130 ? 10.981 7.007   6.011  1.00 17.62  ? 136 ASP   A OD2 1 
ATOM   1014 N  N   . VAL   A 1 131 ? 13.950 6.431   8.429  1.00 13.28  ? 137 VAL   A N   1 
ATOM   1015 C  CA  . VAL   A 1 131 ? 15.268 6.617   7.746  1.00 14.30  ? 137 VAL   A CA  1 
ATOM   1016 C  C   . VAL   A 1 131 ? 15.122 6.015   6.350  1.00 14.45  ? 137 VAL   A C   1 
ATOM   1017 O  O   . VAL   A 1 131 ? 16.089 6.047   5.630  1.00 15.93  ? 137 VAL   A O   1 
ATOM   1018 C  CB  . VAL   A 1 131 ? 16.475 6.027   8.515  1.00 12.88  ? 137 VAL   A CB  1 
ATOM   1019 C  CG1 . VAL   A 1 131 ? 16.718 6.783   9.825  1.00 12.60  ? 137 VAL   A CG1 1 
ATOM   1020 C  CG2 . VAL   A 1 131 ? 16.347 4.547   8.833  1.00 12.31  ? 137 VAL   A CG2 1 
ATOM   1021 N  N   . ARG   A 1 132 ? 13.955 5.475   5.992  1.00 13.46  ? 138 ARG   A N   1 
ATOM   1022 C  CA  . ARG   A 1 132 ? 13.830 4.627   4.788  1.00 13.09  ? 138 ARG   A CA  1 
ATOM   1023 C  C   . ARG   A 1 132 ? 13.986 5.483   3.541  1.00 15.15  ? 138 ARG   A C   1 
ATOM   1024 O  O   . ARG   A 1 132 ? 14.393 4.919   2.553  1.00 16.39  ? 138 ARG   A O   1 
ATOM   1025 C  CB  . ARG   A 1 132 ? 12.510 3.857   4.825  1.00 11.90  ? 138 ARG   A CB  1 
ATOM   1026 C  CG  . ARG   A 1 132 ? 12.498 2.773   5.892  1.00 11.31  ? 138 ARG   A CG  1 
ATOM   1027 C  CD  . ARG   A 1 132 ? 11.237 1.907   5.868  1.00 10.34  ? 138 ARG   A CD  1 
ATOM   1028 N  NE  . ARG   A 1 132 ? 10.120 2.731   6.261  1.00 13.01  ? 138 ARG   A NE  1 
ATOM   1029 C  CZ  . ARG   A 1 132 ? 8.857  2.348   6.345  1.00 11.13  ? 138 ARG   A CZ  1 
ATOM   1030 N  NH1 . ARG   A 1 132 ? 8.488  1.132   5.963  1.00 12.63  ? 138 ARG   A NH1 1 
ATOM   1031 N  NH2 . ARG   A 1 132 ? 7.963  3.201   6.806  1.00 12.84  ? 138 ARG   A NH2 1 
ATOM   1032 N  N   . ASP   A 1 133 ? 13.598 6.759   3.579  1.00 16.34  ? 139 ASP   A N   1 
ATOM   1033 C  CA  . ASP   A 1 133 ? 13.639 7.663   2.390  1.00 15.71  ? 139 ASP   A CA  1 
ATOM   1034 C  C   . ASP   A 1 133 ? 15.063 8.189   2.192  1.00 16.13  ? 139 ASP   A C   1 
ATOM   1035 O  O   . ASP   A 1 133 ? 15.298 8.768   1.111  1.00 16.81  ? 139 ASP   A O   1 
ATOM   1036 C  CB  . ASP   A 1 133 ? 12.654 8.827   2.540  1.00 17.11  ? 139 ASP   A CB  1 
ATOM   1037 C  CG  . ASP   A 1 133 ? 13.025 9.755   3.679  1.00 17.11  ? 139 ASP   A CG  1 
ATOM   1038 O  OD1 . ASP   A 1 133 ? 13.494 9.244   4.711  1.00 16.11  ? 139 ASP   A OD1 1 
ATOM   1039 O  OD2 . ASP   A 1 133 ? 12.854 10.984  3.531  1.00 18.34  ? 139 ASP   A OD2 1 
ATOM   1040 N  N   . LEU   A 1 134 ? 15.964 7.990   3.166  1.00 15.71  ? 140 LEU   A N   1 
ATOM   1041 C  CA  . LEU   A 1 134 ? 17.371 8.495   3.156  1.00 15.45  ? 140 LEU   A CA  1 
ATOM   1042 C  C   . LEU   A 1 134 ? 18.213 7.463   2.387  1.00 14.63  ? 140 LEU   A C   1 
ATOM   1043 O  O   . LEU   A 1 134 ? 19.035 6.777   2.983  1.00 12.72  ? 140 LEU   A O   1 
ATOM   1044 C  CB  . LEU   A 1 134 ? 17.884 8.737   4.601  1.00 13.71  ? 140 LEU   A CB  1 
ATOM   1045 C  CG  . LEU   A 1 134 ? 17.099 9.737   5.471  1.00 14.41  ? 140 LEU   A CG  1 
ATOM   1046 C  CD1 . LEU   A 1 134 ? 17.682 9.872   6.881  1.00 14.32  ? 140 LEU   A CD1 1 
ATOM   1047 C  CD2 . LEU   A 1 134 ? 16.972 11.094  4.784  1.00 15.66  ? 140 LEU   A CD2 1 
ATOM   1048 N  N   . LEU   A 1 135 ? 17.980 7.343   1.069  1.00 16.40  ? 141 LEU   A N   1 
ATOM   1049 C  CA  . LEU   A 1 135 ? 18.609 6.293   0.210  1.00 17.59  ? 141 LEU   A CA  1 
ATOM   1050 C  C   . LEU   A 1 135 ? 20.134 6.445   0.163  1.00 19.17  ? 141 LEU   A C   1 
ATOM   1051 O  O   . LEU   A 1 135 ? 20.813 5.447   -0.139 1.00 21.73  ? 141 LEU   A O   1 
ATOM   1052 C  CB  . LEU   A 1 135 ? 18.026 6.333   -1.208 1.00 18.36  ? 141 LEU   A CB  1 
ATOM   1053 C  CG  . LEU   A 1 135 ? 16.500 6.412   -1.342 1.00 18.09  ? 141 LEU   A CG  1 
ATOM   1054 C  CD1 . LEU   A 1 135 ? 16.071 6.216   -2.799 1.00 18.22  ? 141 LEU   A CD1 1 
ATOM   1055 C  CD2 . LEU   A 1 135 ? 15.813 5.386   -0.452 1.00 17.43  ? 141 LEU   A CD2 1 
ATOM   1056 N  N   . TRP   A 1 136 ? 20.654 7.640   0.442  1.00 19.53  ? 142 TRP   A N   1 
ATOM   1057 C  CA  . TRP   A 1 136 ? 22.108 7.935   0.346  1.00 20.30  ? 142 TRP   A CA  1 
ATOM   1058 C  C   . TRP   A 1 136 ? 22.902 7.234   1.454  1.00 21.00  ? 142 TRP   A C   1 
ATOM   1059 O  O   . TRP   A 1 136 ? 24.120 7.134   1.284  1.00 22.62  ? 142 TRP   A O   1 
ATOM   1060 C  CB  . TRP   A 1 136 ? 22.358 9.445   0.331  1.00 19.42  ? 142 TRP   A CB  1 
ATOM   1061 C  CG  . TRP   A 1 136 ? 21.671 10.228  1.409  1.00 19.50  ? 142 TRP   A CG  1 
ATOM   1062 C  CD1 . TRP   A 1 136 ? 20.542 10.987  1.265  1.00 18.70  ? 142 TRP   A CD1 1 
ATOM   1063 C  CD2 . TRP   A 1 136 ? 22.105 10.411  2.771  1.00 17.69  ? 142 TRP   A CD2 1 
ATOM   1064 N  NE1 . TRP   A 1 136 ? 20.244 11.628  2.441  1.00 19.13  ? 142 TRP   A NE1 1 
ATOM   1065 C  CE2 . TRP   A 1 136 ? 21.182 11.288  3.380  1.00 19.00  ? 142 TRP   A CE2 1 
ATOM   1066 C  CE3 . TRP   A 1 136 ? 23.191 9.952   3.527  1.00 18.15  ? 142 TRP   A CE3 1 
ATOM   1067 C  CZ2 . TRP   A 1 136 ? 21.301 11.670  4.716  1.00 18.17  ? 142 TRP   A CZ2 1 
ATOM   1068 C  CZ3 . TRP   A 1 136 ? 23.303 10.331  4.845  1.00 19.74  ? 142 TRP   A CZ3 1 
ATOM   1069 C  CH2 . TRP   A 1 136 ? 22.368 11.173  5.427  1.00 19.21  ? 142 TRP   A CH2 1 
ATOM   1070 N  N   . LEU   A 1 137 ? 22.255 6.750   2.524  1.00 20.43  ? 143 LEU   A N   1 
ATOM   1071 C  CA  . LEU   A 1 137 ? 22.937 6.074   3.661  1.00 19.83  ? 143 LEU   A CA  1 
ATOM   1072 C  C   . LEU   A 1 137 ? 23.665 4.808   3.206  1.00 22.34  ? 143 LEU   A C   1 
ATOM   1073 O  O   . LEU   A 1 137 ? 24.571 4.367   3.933  1.00 26.51  ? 143 LEU   A O   1 
ATOM   1074 C  CB  . LEU   A 1 137 ? 21.907 5.721   4.742  1.00 18.79  ? 143 LEU   A CB  1 
ATOM   1075 C  CG  . LEU   A 1 137 ? 21.391 6.887   5.584  1.00 17.77  ? 143 LEU   A CG  1 
ATOM   1076 C  CD1 . LEU   A 1 137 ? 20.122 6.500   6.319  1.00 17.89  ? 143 LEU   A CD1 1 
ATOM   1077 C  CD2 . LEU   A 1 137 ? 22.446 7.368   6.562  1.00 18.52  ? 143 LEU   A CD2 1 
ATOM   1078 N  N   . ASP   A 1 138 ? 23.218 4.173   2.116  1.00 29.38  ? 144 ASP   A N   1 
ATOM   1079 C  CA  . ASP   A 1 138 ? 23.654 2.793   1.760  1.00 34.22  ? 144 ASP   A CA  1 
ATOM   1080 C  C   . ASP   A 1 138 ? 25.098 2.823   1.234  1.00 41.32  ? 144 ASP   A C   1 
ATOM   1081 O  O   . ASP   A 1 138 ? 25.811 1.812   1.430  1.00 41.69  ? 144 ASP   A O   1 
ATOM   1082 C  CB  . ASP   A 1 138 ? 22.653 2.133   0.805  1.00 34.61  ? 144 ASP   A CB  1 
ATOM   1083 C  CG  . ASP   A 1 138 ? 21.409 1.576   1.495  1.00 33.42  ? 144 ASP   A CG  1 
ATOM   1084 O  OD1 . ASP   A 1 138 ? 21.075 2.036   2.614  1.00 29.69  ? 144 ASP   A OD1 1 
ATOM   1085 O  OD2 . ASP   A 1 138 ? 20.784 0.666   0.917  1.00 36.95  ? 144 ASP   A OD2 1 
ATOM   1086 N  N   . GLU   A 1 139 ? 25.535 3.960   0.673  1.00 47.76  ? 145 GLU   A N   1 
ATOM   1087 C  CA  . GLU   A 1 139 ? 26.842 4.116   -0.031 1.00 52.51  ? 145 GLU   A CA  1 
ATOM   1088 C  C   . GLU   A 1 139 ? 27.631 5.318   0.513  1.00 56.90  ? 145 GLU   A C   1 
ATOM   1089 O  O   . GLU   A 1 139 ? 27.074 6.078   1.336  1.00 60.70  ? 145 GLU   A O   1 
ATOM   1090 C  CB  . GLU   A 1 139 ? 26.586 4.292   -1.528 1.00 52.05  ? 145 GLU   A CB  1 
ATOM   1091 C  CG  . GLU   A 1 139 ? 25.857 5.584   -1.871 1.00 53.57  ? 145 GLU   A CG  1 
ATOM   1092 C  CD  . GLU   A 1 139 ? 24.697 5.447   -2.845 1.00 54.71  ? 145 GLU   A CD  1 
ATOM   1093 O  OE1 . GLU   A 1 139 ? 24.257 6.480   -3.385 1.00 57.83  ? 145 GLU   A OE1 1 
ATOM   1094 O  OE2 . GLU   A 1 139 ? 24.229 4.311   -3.055 1.00 53.89  ? 145 GLU   A OE2 1 
ATOM   1095 N  N   . GLU   A 1 140 ? 28.882 5.472   0.050  1.00 60.08  ? 146 GLU   A N   1 
ATOM   1096 C  CA  . GLU   A 1 140 ? 29.760 6.655   0.279  1.00 61.19  ? 146 GLU   A CA  1 
ATOM   1097 C  C   . GLU   A 1 140 ? 29.966 6.847   1.787  1.00 63.21  ? 146 GLU   A C   1 
ATOM   1098 O  O   . GLU   A 1 140 ? 31.027 7.259   2.267  1.00 64.08  ? 146 GLU   A O   1 
ATOM   1099 C  CB  . GLU   A 1 140 ? 29.148 7.883   -0.407 1.00 61.35  ? 146 GLU   A CB  1 
ATOM   1100 C  CG  . GLU   A 1 140 ? 29.570 9.224   0.174  1.00 61.77  ? 146 GLU   A CG  1 
ATOM   1101 C  CD  . GLU   A 1 140 ? 30.940 9.725   -0.250 1.00 63.07  ? 146 GLU   A CD  1 
ATOM   1102 O  OE1 . GLU   A 1 140 ? 31.026 10.884  -0.711 1.00 62.99  ? 146 GLU   A OE1 1 
ATOM   1103 O  OE2 . GLU   A 1 140 ? 31.918 8.964   -0.107 1.00 63.13  ? 146 GLU   A OE2 1 
HETATM 1104 ZN ZN  . ZN    B 2 .   ? 10.072 -3.638  5.593  1.00 13.45  ? 201 ZN    A ZN  1 
HETATM 1105 S  S   . DMS   C 3 .   ? 17.799 -7.375  8.062  1.00 105.26 ? 202 DMS   A S   1 
HETATM 1106 O  O   . DMS   C 3 .   ? 18.403 -8.304  7.048  1.00 107.51 ? 202 DMS   A O   1 
HETATM 1107 C  C1  . DMS   C 3 .   ? 16.539 -8.305  8.887  1.00 103.13 ? 202 DMS   A C1  1 
HETATM 1108 C  C2  . DMS   C 3 .   ? 18.952 -7.295  9.407  1.00 105.02 ? 202 DMS   A C2  1 
HETATM 1109 S  S   . DMS   D 3 .   ? 14.878 21.491  8.126  1.00 82.07  ? 203 DMS   A S   1 
HETATM 1110 O  O   . DMS   D 3 .   ? 14.500 21.271  9.564  1.00 79.11  ? 203 DMS   A O   1 
HETATM 1111 C  C1  . DMS   D 3 .   ? 13.399 22.040  7.312  1.00 81.42  ? 203 DMS   A C1  1 
HETATM 1112 C  C2  . DMS   D 3 .   ? 15.766 23.026  8.082  1.00 79.96  ? 203 DMS   A C2  1 
HETATM 1113 S  S   . DMS   E 3 .   ? 19.578 -3.476  23.967 1.00 90.04  ? 204 DMS   A S   1 
HETATM 1114 O  O   . DMS   E 3 .   ? 19.074 -4.601  24.830 1.00 89.88  ? 204 DMS   A O   1 
HETATM 1115 C  C1  . DMS   E 3 .   ? 20.952 -4.140  23.058 1.00 90.81  ? 204 DMS   A C1  1 
HETATM 1116 C  C2  . DMS   E 3 .   ? 18.430 -3.339  22.624 1.00 87.43  ? 204 DMS   A C2  1 
HETATM 1117 S  S   . DMS   F 3 .   ? -0.488 -1.332  23.600 1.00 50.69  ? 205 DMS   A S   1 
HETATM 1118 O  O   . DMS   F 3 .   ? -0.920 -0.997  24.995 1.00 48.95  ? 205 DMS   A O   1 
HETATM 1119 C  C1  . DMS   F 3 .   ? 0.575  -2.747  23.746 1.00 48.53  ? 205 DMS   A C1  1 
HETATM 1120 C  C2  . DMS   F 3 .   ? -1.870 -2.160  22.844 1.00 49.61  ? 205 DMS   A C2  1 
HETATM 1121 S  S   . SO4   G 4 .   ? -2.006 24.786  14.001 1.00 103.41 ? 206 SO4   A S   1 
HETATM 1122 O  O1  . SO4   G 4 .   ? -2.301 24.372  12.655 1.00 101.69 ? 206 SO4   A O1  1 
HETATM 1123 O  O2  . SO4   G 4 .   ? -3.227 25.116  14.685 1.00 101.47 ? 206 SO4   A O2  1 
HETATM 1124 O  O3  . SO4   G 4 .   ? -1.340 23.721  14.699 1.00 103.09 ? 206 SO4   A O3  1 
HETATM 1125 O  O4  . SO4   G 4 .   ? -1.150 25.941  13.966 1.00 106.28 ? 206 SO4   A O4  1 
HETATM 1126 N  N1  . A1BQ3 H 5 .   ? 9.537  11.253  22.212 0.44 12.36  ? 207 A1BQ3 A N1  1 
HETATM 1127 C  C4  . A1BQ3 H 5 .   ? 7.148  12.939  24.412 0.44 13.15  ? 207 A1BQ3 A C4  1 
HETATM 1128 C  C5  . A1BQ3 H 5 .   ? 6.218  12.288  25.192 0.44 13.08  ? 207 A1BQ3 A C5  1 
HETATM 1129 C  C6  . A1BQ3 H 5 .   ? 6.067  10.921  25.229 0.44 13.12  ? 207 A1BQ3 A C6  1 
HETATM 1130 C  C7  . A1BQ3 H 5 .   ? 6.905  10.140  24.452 0.44 12.95  ? 207 A1BQ3 A C7  1 
HETATM 1131 C  C8  . A1BQ3 H 5 .   ? 7.856  10.762  23.658 0.44 12.88  ? 207 A1BQ3 A C8  1 
HETATM 1132 N  N   . A1BQ3 H 5 .   ? 8.790  10.257  22.803 0.44 12.85  ? 207 A1BQ3 A N   1 
HETATM 1133 C  C   . A1BQ3 H 5 .   ? 9.014  8.867   22.443 0.44 12.86  ? 207 A1BQ3 A C   1 
HETATM 1134 O  O   . A1BQ3 H 5 .   ? 9.139  14.759  22.784 0.44 12.87  ? 207 A1BQ3 A O   1 
HETATM 1135 C  C1  . A1BQ3 H 5 .   ? 9.062  12.399  22.703 0.44 12.41  ? 207 A1BQ3 A C1  1 
HETATM 1136 C  C2  . A1BQ3 H 5 .   ? 9.636  13.718  22.330 0.44 12.83  ? 207 A1BQ3 A C2  1 
HETATM 1137 C  C3  . A1BQ3 H 5 .   ? 7.987  12.153  23.626 0.44 12.78  ? 207 A1BQ3 A C3  1 
HETATM 1138 F  F   . A1BQ3 H 5 .   ? 5.420  13.042  25.990 0.44 14.04  ? 207 A1BQ3 A F   1 
HETATM 1139 N  N2  . A1BQ3 H 5 .   ? 10.700 13.721  21.533 0.44 12.52  ? 207 A1BQ3 A N2  1 
HETATM 1140 O  O   . HOH   I 6 .   ? 24.980 17.175  4.960  1.00 24.92  ? 301 HOH   A O   1 
HETATM 1141 O  O   . HOH   I 6 .   ? 27.576 9.556   2.409  1.00 27.27  ? 302 HOH   A O   1 
HETATM 1142 O  O   . HOH   I 6 .   ? 4.127  6.246   25.103 1.00 18.77  ? 303 HOH   A O   1 
HETATM 1143 O  O   . HOH   I 6 .   ? 36.084 4.482   8.968  1.00 24.24  ? 304 HOH   A O   1 
HETATM 1144 O  O   . HOH   I 6 .   ? 22.158 4.091   24.556 1.00 34.82  ? 305 HOH   A O   1 
HETATM 1145 O  O   . HOH   I 6 .   ? 12.162 17.921  7.371  1.00 37.38  ? 306 HOH   A O   1 
HETATM 1146 O  O   . HOH   I 6 .   ? 22.495 -6.227  12.154 1.00 28.93  ? 307 HOH   A O   1 
HETATM 1147 O  O   . HOH   I 6 .   ? 22.690 -0.010  15.827 1.00 22.30  ? 308 HOH   A O   1 
HETATM 1148 O  O   . HOH   I 6 .   ? 26.556 -2.956  9.356  1.00 28.73  ? 309 HOH   A O   1 
HETATM 1149 O  O   . HOH   I 6 .   ? 23.764 8.816   -3.083 1.00 29.72  ? 310 HOH   A O   1 
HETATM 1150 O  O   . HOH   I 6 .   ? 19.590 9.081   -1.169 1.00 52.24  ? 311 HOH   A O   1 
HETATM 1151 O  O   . HOH   I 6 .   ? 3.847  8.718   4.285  1.00 34.06  ? 312 HOH   A O   1 
HETATM 1152 O  O   . HOH   I 6 .   ? 11.759 8.457   23.365 0.44 31.27  ? 313 HOH   A O   1 
HETATM 1153 O  O   . HOH   I 6 .   ? 0.092  0.433   16.311 1.00 16.26  ? 314 HOH   A O   1 
HETATM 1154 O  O   . HOH   I 6 .   ? 16.044 16.635  5.865  1.00 25.27  ? 315 HOH   A O   1 
HETATM 1155 O  O   . HOH   I 6 .   ? 19.753 20.225  6.949  1.00 31.89  ? 316 HOH   A O   1 
HETATM 1156 O  O   . HOH   I 6 .   ? 22.189 -1.359  0.784  1.00 31.22  ? 317 HOH   A O   1 
HETATM 1157 O  O   . HOH   I 6 .   ? 18.338 -1.082  27.768 1.00 24.09  ? 318 HOH   A O   1 
HETATM 1158 O  O   . HOH   I 6 .   ? 29.673 4.126   6.168  1.00 22.50  ? 319 HOH   A O   1 
HETATM 1159 O  O   . HOH   I 6 .   ? 33.952 3.604   14.768 1.00 41.01  ? 320 HOH   A O   1 
HETATM 1160 O  O   . HOH   I 6 .   ? 25.428 3.925   20.025 1.00 64.69  ? 321 HOH   A O   1 
HETATM 1161 O  O   . HOH   I 6 .   ? 22.909 -5.570  8.523  1.00 22.47  ? 322 HOH   A O   1 
HETATM 1162 O  O   . HOH   I 6 .   ? 25.576 8.683   -0.036 1.00 30.02  ? 323 HOH   A O   1 
HETATM 1163 O  O   . HOH   I 6 .   ? 31.921 7.716   7.984  1.00 25.67  ? 324 HOH   A O   1 
HETATM 1164 O  O   . HOH   I 6 .   ? 28.746 -3.930  8.550  1.00 137.16 ? 325 HOH   A O   1 
HETATM 1165 O  O   . HOH   I 6 .   ? 10.245 9.374   5.428  1.00 23.87  ? 326 HOH   A O   1 
HETATM 1166 O  O   . HOH   I 6 .   ? 17.941 -1.974  30.934 1.00 23.08  ? 327 HOH   A O   1 
HETATM 1167 O  O   . HOH   I 6 .   ? -3.269 8.721   22.001 1.00 52.68  ? 328 HOH   A O   1 
HETATM 1168 O  O   . HOH   I 6 .   ? 2.615  9.196   10.668 1.00 28.20  ? 329 HOH   A O   1 
HETATM 1169 O  O   . HOH   I 6 .   ? 5.687  2.195   5.911  1.00 34.35  ? 330 HOH   A O   1 
HETATM 1170 O  O   . HOH   I 6 .   ? 23.934 10.573  21.527 1.00 22.99  ? 331 HOH   A O   1 
HETATM 1171 O  O   . HOH   I 6 .   ? 9.950  15.579  19.475 0.44 17.45  ? 332 HOH   A O   1 
HETATM 1172 O  O   . HOH   I 6 .   ? 21.937 0.134   4.124  1.00 28.50  ? 333 HOH   A O   1 
HETATM 1173 O  O   . HOH   I 6 .   ? 8.779  21.706  26.225 1.00 42.39  ? 334 HOH   A O   1 
HETATM 1174 O  O   . HOH   I 6 .   ? 35.880 1.260   9.584  1.00 84.37  ? 335 HOH   A O   1 
HETATM 1175 O  O   . HOH   I 6 .   ? 19.461 0.232   -1.279 1.00 32.60  ? 336 HOH   A O   1 
HETATM 1176 O  O   . HOH   I 6 .   ? 19.638 8.992   19.569 1.00 10.92  ? 337 HOH   A O   1 
HETATM 1177 O  O   . HOH   I 6 .   ? 6.777  -5.478  31.627 1.00 25.14  ? 338 HOH   A O   1 
HETATM 1178 O  O   . HOH   I 6 .   ? 21.058 23.299  11.789 1.00 20.83  ? 339 HOH   A O   1 
HETATM 1179 O  O   . HOH   I 6 .   ? 29.746 21.210  19.067 1.00 19.63  ? 340 HOH   A O   1 
HETATM 1180 O  O   . HOH   I 6 .   ? 31.830 2.899   5.419  1.00 75.02  ? 341 HOH   A O   1 
HETATM 1181 O  O   . HOH   I 6 .   ? 7.563  19.400  11.019 1.00 25.96  ? 342 HOH   A O   1 
HETATM 1182 O  O   . HOH   I 6 .   ? 4.779  8.492   28.321 1.00 33.33  ? 343 HOH   A O   1 
HETATM 1183 O  O   . HOH   I 6 .   ? 0.114  19.293  26.715 1.00 82.81  ? 344 HOH   A O   1 
HETATM 1184 O  O   . HOH   I 6 .   ? 13.945 2.796   23.428 1.00 14.27  ? 345 HOH   A O   1 
HETATM 1185 O  O   . HOH   I 6 .   ? 15.634 21.294  28.333 1.00 80.08  ? 346 HOH   A O   1 
HETATM 1186 O  O   . HOH   I 6 .   ? -0.870 14.808  11.583 1.00 22.10  ? 347 HOH   A O   1 
HETATM 1187 O  O   . HOH   I 6 .   ? 25.452 8.803   21.913 1.00 25.89  ? 348 HOH   A O   1 
HETATM 1188 O  O   . HOH   I 6 .   ? 21.792 7.391   -3.696 1.00 40.09  ? 349 HOH   A O   1 
HETATM 1189 O  O   . HOH   I 6 .   ? 24.687 -0.606  1.636  1.00 31.44  ? 350 HOH   A O   1 
HETATM 1190 O  O   . HOH   I 6 .   ? -1.314 14.932  17.980 1.00 33.88  ? 351 HOH   A O   1 
HETATM 1191 O  O   . HOH   I 6 .   ? 8.695  17.153  18.520 1.00 20.36  ? 352 HOH   A O   1 
HETATM 1192 O  O   . HOH   I 6 .   ? 11.113 11.967  11.563 1.00 18.04  ? 353 HOH   A O   1 
HETATM 1193 O  O   . HOH   I 6 .   ? 13.560 9.479   -0.812 1.00 34.96  ? 354 HOH   A O   1 
HETATM 1194 O  O   . HOH   I 6 .   ? 16.268 18.581  27.292 1.00 66.64  ? 355 HOH   A O   1 
HETATM 1195 O  O   . HOH   I 6 .   ? 36.454 17.166  12.698 1.00 26.50  ? 356 HOH   A O   1 
HETATM 1196 O  O   . HOH   I 6 .   ? 3.240  -4.272  21.156 1.00 25.02  ? 357 HOH   A O   1 
HETATM 1197 O  O   . HOH   I 6 .   ? 0.279  -1.947  19.782 1.00 23.18  ? 358 HOH   A O   1 
HETATM 1198 O  O   . HOH   I 6 .   ? -1.980 20.652  23.924 1.00 39.56  ? 359 HOH   A O   1 
HETATM 1199 O  O   . HOH   I 6 .   ? 17.658 19.065  18.022 1.00 17.01  ? 360 HOH   A O   1 
HETATM 1200 O  O   . HOH   I 6 .   ? 9.680  6.062   3.815  1.00 19.42  ? 361 HOH   A O   1 
HETATM 1201 O  O   . HOH   I 6 .   ? 20.668 13.566  26.692 1.00 43.98  ? 362 HOH   A O   1 
HETATM 1202 O  O   . HOH   I 6 .   ? 4.804  -4.660  28.922 1.00 19.86  ? 363 HOH   A O   1 
HETATM 1203 O  O   . HOH   I 6 .   ? 25.400 18.554  21.509 1.00 21.49  ? 364 HOH   A O   1 
HETATM 1204 O  O   . HOH   I 6 .   ? 25.623 -1.640  14.421 1.00 28.62  ? 365 HOH   A O   1 
HETATM 1205 O  O   . HOH   I 6 .   ? 1.306  -5.705  17.666 1.00 31.81  ? 366 HOH   A O   1 
HETATM 1206 O  O   . HOH   I 6 .   ? 23.073 21.403  7.970  1.00 21.98  ? 367 HOH   A O   1 
HETATM 1207 O  O   . HOH   I 6 .   ? 16.687 19.337  22.897 1.00 24.59  ? 368 HOH   A O   1 
HETATM 1208 O  O   . HOH   I 6 .   ? 2.036  8.750   27.272 1.00 52.40  ? 369 HOH   A O   1 
HETATM 1209 O  O   . HOH   I 6 .   ? 16.808 2.763   23.710 1.00 18.90  ? 370 HOH   A O   1 
HETATM 1210 O  O   . HOH   I 6 .   ? -0.323 2.338   23.832 1.00 26.06  ? 371 HOH   A O   1 
HETATM 1211 O  O   . HOH   I 6 .   ? 13.721 -8.049  11.566 1.00 21.69  ? 372 HOH   A O   1 
HETATM 1212 O  O   . HOH   I 6 .   ? 2.466  1.418   29.119 1.00 49.71  ? 373 HOH   A O   1 
HETATM 1213 O  O   . HOH   I 6 .   ? 22.154 17.659  21.526 1.00 27.00  ? 374 HOH   A O   1 
HETATM 1214 O  O   . HOH   I 6 .   ? 12.429 10.175  29.620 1.00 25.39  ? 375 HOH   A O   1 
HETATM 1215 O  O   . HOH   I 6 .   ? 12.466 22.625  11.940 1.00 27.68  ? 376 HOH   A O   1 
HETATM 1216 O  O   . HOH   I 6 .   ? 6.352  14.065  6.774  1.00 16.51  ? 377 HOH   A O   1 
HETATM 1217 O  O   . HOH   I 6 .   ? 14.277 -3.558  17.651 1.00 14.95  ? 378 HOH   A O   1 
HETATM 1218 O  O   . HOH   I 6 .   ? 17.669 21.521  11.133 1.00 19.11  ? 379 HOH   A O   1 
HETATM 1219 O  O   . HOH   I 6 .   ? 2.934  14.504  5.954  1.00 63.10  ? 380 HOH   A O   1 
HETATM 1220 O  O   . HOH   I 6 .   ? 30.280 9.606   15.674 1.00 19.74  ? 381 HOH   A O   1 
HETATM 1221 O  O   . HOH   I 6 .   ? 6.636  -7.812  23.683 1.00 23.09  ? 382 HOH   A O   1 
HETATM 1222 O  O   . HOH   I 6 .   ? 15.701 11.755  24.721 1.00 21.02  ? 383 HOH   A O   1 
HETATM 1223 O  O   . HOH   I 6 .   ? 1.172  7.746   6.441  1.00 30.55  ? 384 HOH   A O   1 
HETATM 1224 O  O   . HOH   I 6 .   ? 30.231 10.699  17.831 1.00 22.41  ? 385 HOH   A O   1 
HETATM 1225 O  O   . HOH   I 6 .   ? 1.901  14.201  20.916 1.00 30.97  ? 386 HOH   A O   1 
HETATM 1226 O  O   . HOH   I 6 .   ? 19.475 1.793   19.391 1.00 22.97  ? 387 HOH   A O   1 
HETATM 1227 O  O   . HOH   I 6 .   ? 18.293 9.166   26.274 1.00 29.29  ? 388 HOH   A O   1 
HETATM 1228 O  O   . HOH   I 6 .   ? 18.446 3.153   -0.596 1.00 47.13  ? 389 HOH   A O   1 
HETATM 1229 O  O   . HOH   I 6 .   ? 5.759  4.309   32.734 1.00 24.92  ? 390 HOH   A O   1 
HETATM 1230 O  O   . HOH   I 6 .   ? 7.695  -2.816  0.712  1.00 14.91  ? 391 HOH   A O   1 
HETATM 1231 O  O   . HOH   I 6 .   ? 12.659 11.080  10.142 1.00 13.19  ? 392 HOH   A O   1 
HETATM 1232 O  O   . HOH   I 6 .   ? 29.572 10.674  19.872 1.00 26.90  ? 393 HOH   A O   1 
HETATM 1233 O  O   . HOH   I 6 .   ? 23.846 6.858   21.096 1.00 26.17  ? 394 HOH   A O   1 
HETATM 1234 O  O   . HOH   I 6 .   ? 2.356  20.281  25.248 1.00 17.26  ? 395 HOH   A O   1 
HETATM 1235 O  O   . HOH   I 6 .   ? 1.874  -0.862  4.643  1.00 39.59  ? 396 HOH   A O   1 
HETATM 1236 O  O   . HOH   I 6 .   ? 11.720 -8.291  24.459 1.00 16.26  ? 397 HOH   A O   1 
HETATM 1237 O  O   . HOH   I 6 .   ? 1.399  -5.612  14.444 1.00 26.16  ? 398 HOH   A O   1 
HETATM 1238 O  O   . HOH   I 6 .   ? 9.565  -8.281  0.811  1.00 25.08  ? 399 HOH   A O   1 
HETATM 1239 O  O   . HOH   I 6 .   ? 16.444 22.056  17.113 1.00 33.85  ? 400 HOH   A O   1 
HETATM 1240 O  O   . HOH   I 6 .   ? 14.103 -10.567 8.032  1.00 34.22  ? 401 HOH   A O   1 
HETATM 1241 O  O   . HOH   I 6 .   ? 5.226  3.042   7.641  1.00 22.99  ? 402 HOH   A O   1 
HETATM 1242 O  O   . HOH   I 6 .   ? 1.533  4.186   27.512 1.00 29.05  ? 403 HOH   A O   1 
HETATM 1243 O  O   . HOH   I 6 .   ? 8.033  3.885   3.134  1.00 19.64  ? 404 HOH   A O   1 
HETATM 1244 O  O   . HOH   I 6 .   ? -4.186 24.867  10.533 1.00 36.62  ? 405 HOH   A O   1 
HETATM 1245 O  O   . HOH   I 6 .   ? 33.052 -4.787  6.453  1.00 47.56  ? 406 HOH   A O   1 
HETATM 1246 O  O   . HOH   I 6 .   ? 13.387 -7.024  30.449 1.00 30.47  ? 407 HOH   A O   1 
HETATM 1247 O  O   . HOH   I 6 .   ? 8.351  5.593   33.675 1.00 20.65  ? 408 HOH   A O   1 
HETATM 1248 O  O   . HOH   I 6 .   ? 20.673 -3.550  16.836 1.00 16.53  ? 409 HOH   A O   1 
HETATM 1249 O  O   . HOH   I 6 .   ? 33.820 17.985  10.623 1.00 21.68  ? 410 HOH   A O   1 
HETATM 1250 O  O   . HOH   I 6 .   ? 14.821 -3.508  1.445  1.00 15.93  ? 411 HOH   A O   1 
HETATM 1251 O  O   . HOH   I 6 .   ? -1.370 2.715   4.250  1.00 45.41  ? 412 HOH   A O   1 
HETATM 1252 O  O   . HOH   I 6 .   ? 6.771  22.502  13.787 1.00 75.14  ? 413 HOH   A O   1 
HETATM 1253 O  O   . HOH   I 6 .   ? 14.289 12.228  1.310  1.00 27.41  ? 414 HOH   A O   1 
HETATM 1254 O  O   . HOH   I 6 .   ? 28.863 2.393   12.575 1.00 18.70  ? 415 HOH   A O   1 
HETATM 1255 O  O   . HOH   I 6 .   ? 6.699  12.042  4.984  1.00 21.90  ? 416 HOH   A O   1 
HETATM 1256 O  O   . HOH   I 6 .   ? 7.485  -6.902  8.835  1.00 26.60  ? 417 HOH   A O   1 
HETATM 1257 O  O   . HOH   I 6 .   ? 16.889 -5.883  3.075  1.00 32.16  ? 418 HOH   A O   1 
HETATM 1258 O  O   . HOH   I 6 .   ? -1.316 16.829  19.672 1.00 94.24  ? 419 HOH   A O   1 
HETATM 1259 O  O   . HOH   I 6 .   ? 33.599 13.413  8.929  1.00 33.56  ? 420 HOH   A O   1 
HETATM 1260 O  O   . HOH   I 6 .   ? 17.347 -0.503  20.067 1.00 14.60  ? 421 HOH   A O   1 
HETATM 1261 O  O   . HOH   I 6 .   ? 31.661 19.289  11.521 1.00 22.42  ? 422 HOH   A O   1 
HETATM 1262 O  O   . HOH   I 6 .   ? 12.406 3.168   1.212  1.00 15.92  ? 423 HOH   A O   1 
HETATM 1263 O  O   . HOH   I 6 .   ? 23.752 13.183  24.544 1.00 25.30  ? 424 HOH   A O   1 
HETATM 1264 O  O   . HOH   I 6 .   ? 3.295  -1.009  29.010 1.00 25.52  ? 425 HOH   A O   1 
HETATM 1265 O  O   . HOH   I 6 .   ? 4.954  -6.930  14.043 1.00 30.48  ? 426 HOH   A O   1 
HETATM 1266 O  O   . HOH   I 6 .   ? 4.370  14.416  23.961 0.44 20.47  ? 427 HOH   A O   1 
HETATM 1267 O  O   . HOH   I 6 .   ? -3.024 19.055  25.771 1.00 27.32  ? 428 HOH   A O   1 
HETATM 1268 O  O   . HOH   I 6 .   ? 18.205 3.944   26.108 1.00 30.67  ? 429 HOH   A O   1 
HETATM 1269 O  O   . HOH   I 6 .   ? 21.532 15.931  24.697 1.00 32.91  ? 430 HOH   A O   1 
HETATM 1270 O  O   . HOH   I 6 .   ? 0.578  16.707  26.559 1.00 30.89  ? 431 HOH   A O   1 
HETATM 1271 O  O   . HOH   I 6 .   ? 35.045 9.931   12.652 1.00 30.46  ? 432 HOH   A O   1 
HETATM 1272 O  O   . HOH   I 6 .   ? 10.746 -3.950  -0.146 1.00 23.63  ? 433 HOH   A O   1 
HETATM 1273 O  O   . HOH   I 6 .   ? 17.314 9.948   -0.859 1.00 23.46  ? 434 HOH   A O   1 
HETATM 1274 O  O   . HOH   I 6 .   ? 30.417 2.103   14.727 1.00 23.00  ? 435 HOH   A O   1 
HETATM 1275 O  O   . HOH   I 6 .   ? 20.945 -5.215  14.203 1.00 17.19  ? 436 HOH   A O   1 
HETATM 1276 O  O   . HOH   I 6 .   ? 17.930 13.661  2.523  1.00 21.62  ? 437 HOH   A O   1 
HETATM 1277 O  O   . HOH   I 6 .   ? 17.272 -3.409  19.650 1.00 18.36  ? 438 HOH   A O   1 
HETATM 1278 O  O   . HOH   I 6 .   ? 36.451 19.036  17.935 1.00 26.59  ? 439 HOH   A O   1 
HETATM 1279 O  O   . HOH   I 6 .   ? 30.748 15.023  22.738 1.00 23.92  ? 440 HOH   A O   1 
HETATM 1280 O  O   . HOH   I 6 .   ? 1.958  11.218  20.460 1.00 31.71  ? 441 HOH   A O   1 
HETATM 1281 O  O   . HOH   I 6 .   ? 17.243 -5.972  26.946 1.00 35.99  ? 442 HOH   A O   1 
HETATM 1282 O  O   . HOH   I 6 .   ? 14.710 12.721  25.197 1.00 29.18  ? 443 HOH   A O   1 
HETATM 1283 O  O   . HOH   I 6 .   ? 23.226 2.188   19.970 1.00 24.30  ? 444 HOH   A O   1 
HETATM 1284 O  O   . HOH   I 6 .   ? 4.593  -0.945  24.367 1.00 17.52  ? 445 HOH   A O   1 
HETATM 1285 O  O   . HOH   I 6 .   ? 5.300  23.686  24.559 1.00 21.54  ? 446 HOH   A O   1 
HETATM 1286 O  O   . HOH   I 6 .   ? 0.545  -2.257  17.315 1.00 13.27  ? 447 HOH   A O   1 
HETATM 1287 O  O   . HOH   I 6 .   ? 3.437  -1.386  21.715 1.00 20.90  ? 448 HOH   A O   1 
HETATM 1288 O  O   . HOH   I 6 .   ? 35.141 -2.304  9.490  1.00 29.50  ? 449 HOH   A O   1 
HETATM 1289 O  O   . HOH   I 6 .   ? 1.275  11.097  28.038 1.00 39.54  ? 450 HOH   A O   1 
HETATM 1290 O  O   . HOH   I 6 .   ? -0.209 12.613  17.471 1.00 29.28  ? 451 HOH   A O   1 
HETATM 1291 O  O   . HOH   I 6 .   ? 12.522 23.653  14.017 1.00 28.14  ? 452 HOH   A O   1 
HETATM 1292 O  O   . HOH   I 6 .   ? 22.005 18.921  19.559 1.00 22.31  ? 453 HOH   A O   1 
HETATM 1293 O  O   . HOH   I 6 .   ? 0.072  4.540   5.814  1.00 25.93  ? 454 HOH   A O   1 
HETATM 1294 O  O   . HOH   I 6 .   ? 30.289 -3.195  6.733  1.00 30.75  ? 455 HOH   A O   1 
HETATM 1295 O  O   . HOH   I 6 .   ? 21.426 8.838   21.543 1.00 19.56  ? 456 HOH   A O   1 
HETATM 1296 O  O   . HOH   I 6 .   ? 16.738 -6.547  12.017 1.00 30.78  ? 457 HOH   A O   1 
HETATM 1297 O  O   . HOH   I 6 .   ? 0.862  2.340   25.783 1.00 39.78  ? 458 HOH   A O   1 
HETATM 1298 O  O   . HOH   I 6 .   ? 4.057  -5.256  6.392  1.00 29.35  ? 459 HOH   A O   1 
HETATM 1299 O  O   . HOH   I 6 .   ? 0.336  13.313  22.026 1.00 27.86  ? 460 HOH   A O   1 
HETATM 1300 O  O   . HOH   I 6 .   ? 3.863  -4.526  1.596  1.00 30.79  ? 461 HOH   A O   1 
HETATM 1301 O  O   . HOH   I 6 .   ? 2.451  12.395  17.986 0.44 64.49  ? 462 HOH   A O   1 
HETATM 1302 O  O   . HOH   I 6 .   ? 34.567 8.235   14.973 1.00 48.27  ? 463 HOH   A O   1 
HETATM 1303 O  O   . HOH   I 6 .   ? 16.628 20.069  30.367 1.00 57.06  ? 464 HOH   A O   1 
HETATM 1304 O  O   . HOH   I 6 .   ? 15.444 14.372  3.576  1.00 29.14  ? 465 HOH   A O   1 
HETATM 1305 O  O   . HOH   I 6 .   ? 29.388 4.835   3.846  1.00 26.43  ? 466 HOH   A O   1 
HETATM 1306 O  O   . HOH   I 6 .   ? 17.266 11.518  26.489 1.00 30.40  ? 467 HOH   A O   1 
HETATM 1307 O  O   . HOH   I 6 .   ? 5.120  23.738  15.403 1.00 29.61  ? 468 HOH   A O   1 
HETATM 1308 O  O   . HOH   I 6 .   ? 30.584 18.654  8.571  1.00 22.14  ? 469 HOH   A O   1 
HETATM 1309 O  O   . HOH   I 6 .   ? 22.926 18.469  6.169  1.00 31.63  ? 470 HOH   A O   1 
HETATM 1310 O  O   . HOH   I 6 .   ? 36.226 -1.538  12.018 1.00 32.96  ? 471 HOH   A O   1 
HETATM 1311 O  O   . HOH   I 6 .   ? 20.226 -4.752  10.724 1.00 25.10  ? 472 HOH   A O   1 
HETATM 1312 O  O   . HOH   I 6 .   ? 30.787 6.232   6.483  1.00 64.01  ? 473 HOH   A O   1 
HETATM 1313 O  O   . HOH   I 6 .   ? 28.955 15.193  4.173  1.00 37.25  ? 474 HOH   A O   1 
HETATM 1314 O  O   . HOH   I 6 .   ? 3.267  15.597  27.485 1.00 49.63  ? 475 HOH   A O   1 
HETATM 1315 O  O   . HOH   I 6 .   ? 16.861 11.819  0.878  1.00 32.54  ? 476 HOH   A O   1 
HETATM 1316 O  O   . HOH   I 6 .   ? 19.380 -7.193  3.932  1.00 38.80  ? 477 HOH   A O   1 
HETATM 1317 O  O   . HOH   I 6 .   ? -0.020 12.848  19.490 1.00 32.93  ? 478 HOH   A O   1 
HETATM 1318 O  O   . HOH   I 6 .   ? 28.008 16.298  24.368 1.00 26.95  ? 479 HOH   A O   1 
HETATM 1319 O  O   . HOH   I 6 .   ? 38.174 -0.018  12.836 1.00 35.11  ? 480 HOH   A O   1 
HETATM 1320 O  O   . HOH   I 6 .   ? 0.085  21.838  22.324 1.00 75.85  ? 481 HOH   A O   1 
HETATM 1321 O  O   . HOH   I 6 .   ? 7.232  -7.590  2.198  1.00 23.81  ? 482 HOH   A O   1 
HETATM 1322 O  O   . HOH   I 6 .   ? 13.608 22.816  29.177 1.00 43.37  ? 483 HOH   A O   1 
HETATM 1323 O  O   . HOH   I 6 .   ? 8.252  10.522  3.027  1.00 35.09  ? 484 HOH   A O   1 
HETATM 1324 O  O   . HOH   I 6 .   ? 9.337  20.178  7.157  1.00 42.40  ? 485 HOH   A O   1 
HETATM 1325 O  O   . HOH   I 6 .   ? 27.925 8.563   22.425 1.00 25.17  ? 486 HOH   A O   1 
HETATM 1326 O  O   . HOH   I 6 .   ? 6.559  -4.863  2.809  1.00 36.41  ? 487 HOH   A O   1 
HETATM 1327 O  O   . HOH   I 6 .   ? 7.848  14.675  28.085 1.00 38.61  ? 488 HOH   A O   1 
HETATM 1328 O  O   . HOH   I 6 .   ? 30.398 6.192   17.346 1.00 29.32  ? 489 HOH   A O   1 
HETATM 1329 O  O   . HOH   I 6 .   ? 5.145  -3.726  30.933 1.00 32.31  ? 490 HOH   A O   1 
HETATM 1330 O  O   . HOH   I 6 .   ? 14.420 -8.267  24.792 1.00 28.62  ? 491 HOH   A O   1 
HETATM 1331 O  O   . HOH   I 6 .   ? 22.599 9.721   23.514 1.00 27.77  ? 492 HOH   A O   1 
HETATM 1332 O  O   . HOH   I 6 .   ? 2.397  18.497  27.531 1.00 47.90  ? 493 HOH   A O   1 
HETATM 1333 O  O   . HOH   I 6 .   ? 21.414 14.181  -0.346 1.00 33.18  ? 494 HOH   A O   1 
HETATM 1334 O  O   . HOH   I 6 .   ? 2.882  -1.169  26.467 1.00 35.12  ? 495 HOH   A O   1 
HETATM 1335 O  O   . HOH   I 6 .   ? 23.785 13.537  2.180  1.00 27.80  ? 496 HOH   A O   1 
HETATM 1336 O  O   . HOH   I 6 .   ? 8.810  11.194  31.795 1.00 27.42  ? 497 HOH   A O   1 
HETATM 1337 O  O   . HOH   I 6 .   ? 26.589 -2.424  16.283 1.00 30.19  ? 498 HOH   A O   1 
HETATM 1338 O  O   . HOH   I 6 .   ? 30.326 6.405   19.919 1.00 31.04  ? 499 HOH   A O   1 
HETATM 1339 O  O   . HOH   I 6 .   ? 23.531 -5.291  2.717  1.00 31.42  ? 500 HOH   A O   1 
HETATM 1340 O  O   . HOH   I 6 .   ? 18.947 11.653  29.866 1.00 28.42  ? 501 HOH   A O   1 
HETATM 1341 O  O   . HOH   I 6 .   ? 19.927 10.984  26.393 1.00 25.70  ? 502 HOH   A O   1 
HETATM 1342 O  O   . HOH   I 6 .   ? 30.518 -4.647  14.239 1.00 28.98  ? 503 HOH   A O   1 
HETATM 1343 O  O   . HOH   I 6 .   ? 22.432 -9.265  7.237  1.00 32.44  ? 504 HOH   A O   1 
HETATM 1344 O  O   . HOH   I 6 .   ? 8.415  7.771   2.807  1.00 32.03  ? 505 HOH   A O   1 
HETATM 1345 O  O   . HOH   I 6 .   ? 29.502 -0.306  16.481 1.00 26.89  ? 506 HOH   A O   1 
HETATM 1346 O  O   . HOH   I 6 .   ? 25.527 10.445  24.034 1.00 47.03  ? 507 HOH   A O   1 
HETATM 1347 O  O   . HOH   I 6 .   ? 37.278 -0.896  9.632  1.00 36.10  ? 508 HOH   A O   1 
HETATM 1348 O  O   . HOH   I 6 .   ? 12.256 -6.003  32.782 1.00 21.86  ? 509 HOH   A O   1 
HETATM 1349 O  O   . HOH   I 6 .   ? 2.221  -3.894  26.908 1.00 33.26  ? 510 HOH   A O   1 
HETATM 1350 O  O   . HOH   I 6 .   ? 37.711 18.552  14.831 1.00 23.87  ? 511 HOH   A O   1 
HETATM 1351 O  O   . HOH   I 6 .   ? 31.209 3.595   16.601 1.00 29.85  ? 512 HOH   A O   1 
HETATM 1352 O  O   . HOH   I 6 .   ? 16.882 10.218  29.201 1.00 26.21  ? 513 HOH   A O   1 
HETATM 1353 O  O   . HOH   I 6 .   ? 33.802 -3.109  15.960 1.00 36.01  ? 514 HOH   A O   1 
HETATM 1354 O  O   . HOH   I 6 .   ? 2.400  -5.764  22.715 1.00 24.76  ? 515 HOH   A O   1 
HETATM 1355 O  O   . HOH   I 6 .   ? 5.009  7.179   2.450  1.00 21.84  ? 516 HOH   A O   1 
HETATM 1356 O  O   . HOH   I 6 .   ? 16.184 -7.733  30.630 1.00 33.27  ? 517 HOH   A O   1 
HETATM 1357 O  O   . HOH   I 6 .   ? 25.381 11.131  -0.731 1.00 27.74  ? 518 HOH   A O   1 
HETATM 1358 O  O   . HOH   I 6 .   ? -2.692 7.279   28.628 1.00 24.24  ? 519 HOH   A O   1 
HETATM 1359 O  O   . HOH   I 6 .   ? 4.565  -12.074 6.442  1.00 27.37  ? 520 HOH   A O   1 
HETATM 1360 O  O   . HOH   I 6 .   ? 13.629 13.420  -0.621 1.00 45.57  ? 521 HOH   A O   1 
HETATM 1361 O  O   . HOH   I 6 .   ? 3.714  -6.999  23.448 1.00 23.02  ? 522 HOH   A O   1 
HETATM 1362 O  O   . HOH   I 6 .   ? 2.411  21.759  9.794  1.00 27.34  ? 523 HOH   A O   1 
HETATM 1363 O  O   . HOH   I 6 .   ? 5.192  22.717  10.072 1.00 34.78  ? 524 HOH   A O   1 
HETATM 1364 O  O   . HOH   I 6 .   ? 4.702  -7.584  25.772 1.00 22.48  ? 525 HOH   A O   1 
HETATM 1365 O  O   . HOH   I 6 .   ? 14.485 -12.289 2.404  1.00 27.18  ? 526 HOH   A O   1 
HETATM 1366 O  O   . HOH   I 6 .   ? 4.994  21.959  6.576  1.00 50.00  ? 527 HOH   A O   1 
HETATM 1367 O  O   . HOH   I 6 .   ? 43.790 -4.796  5.045  1.00 37.65  ? 528 HOH   A O   1 
# 
