data_7HZS
# 
_entry.id   7HZS 
# 
_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   7HZS         pdb_00007hzs 10.2210/pdb7hzs/pdb 
WWPDB D_1001408136 ?            ?                   
# 
_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                        7HZS 
_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 2   3.4.22.29 ? ? ? 
2 non-polymer syn 'ZINC ION'                                                               65.409    2   ?         ? ? ? 
3 non-polymer syn '(3S)-1-(1H-pyrazolo[3,4-b]pyridine-4-carbonyl)piperidine-3-carboxamide' 273.291   1   ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                     78.133    3   ?         ? ? ? 
5 water       nat water                                                                    18.015    307 ?         ? ? ? 
# 
_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,C 
_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 '(3S)-1-(1H-pyrazolo[3,4-b]pyridine-4-carbonyl)piperidine-3-carboxamide' A1BQ7 
4 'DIMETHYL SULFOXIDE'                                                     DMS   
5 water                                                                    HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   GLY n 
1 3   ALA n 
1 4   ILE n 
1 5   TYR n 
1 6   VAL n 
1 7   GLY n 
1 8   ASN n 
1 9   TYR n 
1 10  ARG n 
1 11  VAL n 
1 12  VAL n 
1 13  ASN n 
1 14  ARG n 
1 15  HIS n 
1 16  LEU n 
1 17  ALA n 
1 18  THR n 
1 19  HIS n 
1 20  ASN n 
1 21  ASP n 
1 22  TRP n 
1 23  ALA n 
1 24  ASN n 
1 25  LEU n 
1 26  VAL n 
1 27  TRP n 
1 28  GLU n 
1 29  ASP n 
1 30  SER n 
1 31  SER n 
1 32  ARG n 
1 33  ASP n 
1 34  LEU n 
1 35  LEU n 
1 36  VAL n 
1 37  SER n 
1 38  SER n 
1 39  THR n 
1 40  THR n 
1 41  ALA n 
1 42  GLN n 
1 43  GLY n 
1 44  CYS n 
1 45  ASP n 
1 46  THR n 
1 47  ILE n 
1 48  ALA n 
1 49  ARG n 
1 50  CYS n 
1 51  ASP n 
1 52  CYS n 
1 53  GLN n 
1 54  THR n 
1 55  GLY n 
1 56  VAL n 
1 57  TYR n 
1 58  TYR n 
1 59  CYS n 
1 60  SER n 
1 61  SER n 
1 62  ARG n 
1 63  ARG n 
1 64  LYS n 
1 65  HIS n 
1 66  TYR n 
1 67  PRO n 
1 68  VAL n 
1 69  SER n 
1 70  PHE n 
1 71  SER n 
1 72  LYS n 
1 73  PRO n 
1 74  SER n 
1 75  LEU n 
1 76  ILE n 
1 77  PHE n 
1 78  VAL n 
1 79  GLU n 
1 80  ALA n 
1 81  SER n 
1 82  GLU n 
1 83  TYR n 
1 84  TYR n 
1 85  PRO n 
1 86  ALA n 
1 87  ARG n 
1 88  TYR n 
1 89  GLN n 
1 90  SER n 
1 91  HIS n 
1 92  LEU n 
1 93  MET n 
1 94  LEU n 
1 95  ALA n 
1 96  VAL n 
1 97  GLY n 
1 98  HIS n 
1 99  SER n 
1 100 GLU n 
1 101 PRO n 
1 102 GLY n 
1 103 ASP n 
1 104 CYS n 
1 105 GLY n 
1 106 GLY n 
1 107 ILE n 
1 108 LEU n 
1 109 ARG n 
1 110 CYS n 
1 111 GLN n 
1 112 HIS n 
1 113 GLY n 
1 114 VAL n 
1 115 VAL n 
1 116 GLY n 
1 117 ILE n 
1 118 VAL n 
1 119 SER n 
1 120 THR n 
1 121 GLY n 
1 122 GLY n 
1 123 ASN n 
1 124 GLY n 
1 125 LEU n 
1 126 VAL n 
1 127 GLY n 
1 128 PHE n 
1 129 ALA n 
1 130 ASP n 
1 131 VAL n 
1 132 ARG n 
1 133 ASP n 
1 134 LEU n 
1 135 LEU n 
1 136 TRP n 
1 137 LEU n 
1 138 ASP n 
1 139 GLU n 
1 140 GLU n 
1 141 ALA n 
1 142 MET n 
1 143 GLU n 
1 144 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   144 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Coxsackievirus A16' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     31704 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1BQ7 non-polymer         . '(3S)-1-(1H-pyrazolo[3,4-b]pyridine-4-carbonyl)piperidine-3-carboxamide' ? 'C13 H15 N5 O2'  273.291 
ALA   'L-peptide linking' y ALANINE                                                                  ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                                 ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                               ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                          ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                 ? 'C3 H7 N O2 S'   121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                     ? 'C2 H6 O S'      78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                                ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                          ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                                  ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                                    ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                               ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                                  ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                                   ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                               ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                            ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                                  ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                                   ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                                ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                               ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                                                 ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                                   ? 'C5 H11 N O2'    117.146 
ZN    non-polymer         . 'ZINC ION'                                                               ? 'Zn 2'           65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   7   7   SER SER A . n 
A 1 2   GLY 2   8   8   GLY GLY A . n 
A 1 3   ALA 3   9   9   ALA ALA A . n 
A 1 4   ILE 4   10  10  ILE ILE A . n 
A 1 5   TYR 5   11  11  TYR TYR A . n 
A 1 6   VAL 6   12  12  VAL VAL A . n 
A 1 7   GLY 7   13  13  GLY GLY A . n 
A 1 8   ASN 8   14  14  ASN ASN A . n 
A 1 9   TYR 9   15  15  TYR TYR A . n 
A 1 10  ARG 10  16  16  ARG ARG A . n 
A 1 11  VAL 11  17  17  VAL VAL A . n 
A 1 12  VAL 12  18  18  VAL VAL A . n 
A 1 13  ASN 13  19  19  ASN ASN A . n 
A 1 14  ARG 14  20  20  ARG ARG A . n 
A 1 15  HIS 15  21  21  HIS HIS A . n 
A 1 16  LEU 16  22  22  LEU LEU A . n 
A 1 17  ALA 17  23  23  ALA ALA A . n 
A 1 18  THR 18  24  24  THR THR A . n 
A 1 19  HIS 19  25  25  HIS HIS A . n 
A 1 20  ASN 20  26  26  ASN ASN A . n 
A 1 21  ASP 21  27  27  ASP ASP A . n 
A 1 22  TRP 22  28  28  TRP TRP A . n 
A 1 23  ALA 23  29  29  ALA ALA A . n 
A 1 24  ASN 24  30  30  ASN ASN A . n 
A 1 25  LEU 25  31  31  LEU LEU A . n 
A 1 26  VAL 26  32  32  VAL VAL A . n 
A 1 27  TRP 27  33  33  TRP TRP A . n 
A 1 28  GLU 28  34  34  GLU GLU A . n 
A 1 29  ASP 29  35  35  ASP ASP A . n 
A 1 30  SER 30  36  36  SER SER A . n 
A 1 31  SER 31  37  37  SER SER A . n 
A 1 32  ARG 32  38  38  ARG ARG A . n 
A 1 33  ASP 33  39  39  ASP ASP A . n 
A 1 34  LEU 34  40  40  LEU LEU A . n 
A 1 35  LEU 35  41  41  LEU LEU A . n 
A 1 36  VAL 36  42  42  VAL VAL A . n 
A 1 37  SER 37  43  43  SER SER A . n 
A 1 38  SER 38  44  44  SER SER A . n 
A 1 39  THR 39  45  45  THR THR A . n 
A 1 40  THR 40  46  46  THR THR A . n 
A 1 41  ALA 41  47  47  ALA ALA A . n 
A 1 42  GLN 42  48  48  GLN GLN A . n 
A 1 43  GLY 43  49  49  GLY GLY A . n 
A 1 44  CYS 44  50  50  CYS CYS A . n 
A 1 45  ASP 45  51  51  ASP ASP A . n 
A 1 46  THR 46  52  52  THR THR A . n 
A 1 47  ILE 47  53  53  ILE ILE A . n 
A 1 48  ALA 48  54  54  ALA ALA A . n 
A 1 49  ARG 49  55  55  ARG ARG A . n 
A 1 50  CYS 50  56  56  CYS CYS A . n 
A 1 51  ASP 51  57  57  ASP ASP A . n 
A 1 52  CYS 52  58  58  CYS CYS A . n 
A 1 53  GLN 53  59  59  GLN GLN A . n 
A 1 54  THR 54  60  60  THR THR A . n 
A 1 55  GLY 55  61  61  GLY GLY A . n 
A 1 56  VAL 56  62  62  VAL VAL A . n 
A 1 57  TYR 57  63  63  TYR TYR A . n 
A 1 58  TYR 58  64  64  TYR TYR A . n 
A 1 59  CYS 59  65  65  CYS CYS A . n 
A 1 60  SER 60  66  66  SER SER A . n 
A 1 61  SER 61  67  67  SER SER A . n 
A 1 62  ARG 62  68  68  ARG ARG A . n 
A 1 63  ARG 63  69  69  ARG ARG A . n 
A 1 64  LYS 64  70  70  LYS LYS A . n 
A 1 65  HIS 65  71  71  HIS HIS A . n 
A 1 66  TYR 66  72  72  TYR TYR A . n 
A 1 67  PRO 67  73  73  PRO PRO A . n 
A 1 68  VAL 68  74  74  VAL VAL A . n 
A 1 69  SER 69  75  75  SER SER A . n 
A 1 70  PHE 70  76  76  PHE PHE A . n 
A 1 71  SER 71  77  77  SER SER A . n 
A 1 72  LYS 72  78  78  LYS LYS A . n 
A 1 73  PRO 73  79  79  PRO PRO A . n 
A 1 74  SER 74  80  80  SER SER A . n 
A 1 75  LEU 75  81  81  LEU LEU A . n 
A 1 76  ILE 76  82  82  ILE ILE A . n 
A 1 77  PHE 77  83  83  PHE PHE A . n 
A 1 78  VAL 78  84  84  VAL VAL A . n 
A 1 79  GLU 79  85  85  GLU GLU A . n 
A 1 80  ALA 80  86  86  ALA ALA A . n 
A 1 81  SER 81  87  87  SER SER A . n 
A 1 82  GLU 82  88  88  GLU GLU A . n 
A 1 83  TYR 83  89  89  TYR TYR A . n 
A 1 84  TYR 84  90  90  TYR TYR A . n 
A 1 85  PRO 85  91  91  PRO PRO A . n 
A 1 86  ALA 86  92  92  ALA ALA A . n 
A 1 87  ARG 87  93  93  ARG ARG A . n 
A 1 88  TYR 88  94  94  TYR TYR A . n 
A 1 89  GLN 89  95  95  GLN GLN A . n 
A 1 90  SER 90  96  96  SER SER A . n 
A 1 91  HIS 91  97  97  HIS HIS A . n 
A 1 92  LEU 92  98  98  LEU LEU A . n 
A 1 93  MET 93  99  99  MET MET A . n 
A 1 94  LEU 94  100 100 LEU LEU A . n 
A 1 95  ALA 95  101 101 ALA ALA A . n 
A 1 96  VAL 96  102 102 VAL VAL A . n 
A 1 97  GLY 97  103 103 GLY GLY A . n 
A 1 98  HIS 98  104 104 HIS HIS A . n 
A 1 99  SER 99  105 105 SER SER A . n 
A 1 100 GLU 100 106 106 GLU GLU A . n 
A 1 101 PRO 101 107 107 PRO PRO A . n 
A 1 102 GLY 102 108 108 GLY GLY A . n 
A 1 103 ASP 103 109 109 ASP ASP A . n 
A 1 104 CYS 104 110 110 CYS CYS A . n 
A 1 105 GLY 105 111 111 GLY GLY A . n 
A 1 106 GLY 106 112 112 GLY GLY A . n 
A 1 107 ILE 107 113 113 ILE ILE A . n 
A 1 108 LEU 108 114 114 LEU LEU A . n 
A 1 109 ARG 109 115 115 ARG ARG A . n 
A 1 110 CYS 110 116 116 CYS CYS A . n 
A 1 111 GLN 111 117 117 GLN GLN A . n 
A 1 112 HIS 112 118 118 HIS HIS A . n 
A 1 113 GLY 113 119 119 GLY GLY A . n 
A 1 114 VAL 114 120 120 VAL VAL A . n 
A 1 115 VAL 115 121 121 VAL VAL A . n 
A 1 116 GLY 116 122 122 GLY GLY A . n 
A 1 117 ILE 117 123 123 ILE ILE A . n 
A 1 118 VAL 118 124 124 VAL VAL A . n 
A 1 119 SER 119 125 125 SER SER A . n 
A 1 120 THR 120 126 126 THR THR A . n 
A 1 121 GLY 121 127 127 GLY GLY A . n 
A 1 122 GLY 122 128 128 GLY GLY A . n 
A 1 123 ASN 123 129 129 ASN ASN A . n 
A 1 124 GLY 124 130 130 GLY GLY A . n 
A 1 125 LEU 125 131 131 LEU LEU A . n 
A 1 126 VAL 126 132 132 VAL VAL A . n 
A 1 127 GLY 127 133 133 GLY GLY A . n 
A 1 128 PHE 128 134 134 PHE PHE A . n 
A 1 129 ALA 129 135 135 ALA ALA A . n 
A 1 130 ASP 130 136 136 ASP ASP A . n 
A 1 131 VAL 131 137 137 VAL VAL A . n 
A 1 132 ARG 132 138 138 ARG ARG A . n 
A 1 133 ASP 133 139 139 ASP ASP A . n 
A 1 134 LEU 134 140 140 LEU LEU A . n 
A 1 135 LEU 135 141 141 LEU LEU A . n 
A 1 136 TRP 136 142 142 TRP TRP A . n 
A 1 137 LEU 137 143 143 LEU LEU A . n 
A 1 138 ASP 138 144 144 ASP ASP A . n 
A 1 139 GLU 139 145 145 GLU GLU A . n 
A 1 140 GLU 140 146 146 GLU GLU A . n 
A 1 141 ALA 141 147 ?   ?   ?   A . n 
A 1 142 MET 142 148 ?   ?   ?   A . n 
A 1 143 GLU 143 149 ?   ?   ?   A . n 
A 1 144 GLN 144 150 ?   ?   ?   A . n 
B 1 1   SER 1   7   7   SER SER C . n 
B 1 2   GLY 2   8   8   GLY GLY C . n 
B 1 3   ALA 3   9   9   ALA ALA C . n 
B 1 4   ILE 4   10  10  ILE ILE C . n 
B 1 5   TYR 5   11  11  TYR TYR C . n 
B 1 6   VAL 6   12  12  VAL VAL C . n 
B 1 7   GLY 7   13  13  GLY GLY C . n 
B 1 8   ASN 8   14  14  ASN ASN C . n 
B 1 9   TYR 9   15  15  TYR TYR C . n 
B 1 10  ARG 10  16  16  ARG ARG C . n 
B 1 11  VAL 11  17  17  VAL VAL C . n 
B 1 12  VAL 12  18  18  VAL VAL C . n 
B 1 13  ASN 13  19  19  ASN ASN C . n 
B 1 14  ARG 14  20  20  ARG ARG C . n 
B 1 15  HIS 15  21  21  HIS HIS C . n 
B 1 16  LEU 16  22  22  LEU LEU C . n 
B 1 17  ALA 17  23  23  ALA ALA C . n 
B 1 18  THR 18  24  24  THR THR C . n 
B 1 19  HIS 19  25  25  HIS HIS C . n 
B 1 20  ASN 20  26  26  ASN ASN C . n 
B 1 21  ASP 21  27  27  ASP ASP C . n 
B 1 22  TRP 22  28  28  TRP TRP C . n 
B 1 23  ALA 23  29  29  ALA ALA C . n 
B 1 24  ASN 24  30  30  ASN ASN C . n 
B 1 25  LEU 25  31  31  LEU LEU C . n 
B 1 26  VAL 26  32  32  VAL VAL C . n 
B 1 27  TRP 27  33  33  TRP TRP C . n 
B 1 28  GLU 28  34  34  GLU GLU C . n 
B 1 29  ASP 29  35  35  ASP ASP C . n 
B 1 30  SER 30  36  36  SER SER C . n 
B 1 31  SER 31  37  37  SER SER C . n 
B 1 32  ARG 32  38  38  ARG ARG C . n 
B 1 33  ASP 33  39  39  ASP ASP C . n 
B 1 34  LEU 34  40  40  LEU LEU C . n 
B 1 35  LEU 35  41  41  LEU LEU C . n 
B 1 36  VAL 36  42  42  VAL VAL C . n 
B 1 37  SER 37  43  43  SER SER C . n 
B 1 38  SER 38  44  44  SER SER C . n 
B 1 39  THR 39  45  45  THR THR C . n 
B 1 40  THR 40  46  46  THR THR C . n 
B 1 41  ALA 41  47  47  ALA ALA C . n 
B 1 42  GLN 42  48  48  GLN GLN C . n 
B 1 43  GLY 43  49  49  GLY GLY C . n 
B 1 44  CYS 44  50  50  CYS CYS C . n 
B 1 45  ASP 45  51  51  ASP ASP C . n 
B 1 46  THR 46  52  52  THR THR C . n 
B 1 47  ILE 47  53  53  ILE ILE C . n 
B 1 48  ALA 48  54  54  ALA ALA C . n 
B 1 49  ARG 49  55  55  ARG ARG C . n 
B 1 50  CYS 50  56  56  CYS CYS C . n 
B 1 51  ASP 51  57  57  ASP ASP C . n 
B 1 52  CYS 52  58  58  CYS CYS C . n 
B 1 53  GLN 53  59  59  GLN GLN C . n 
B 1 54  THR 54  60  60  THR THR C . n 
B 1 55  GLY 55  61  61  GLY GLY C . n 
B 1 56  VAL 56  62  62  VAL VAL C . n 
B 1 57  TYR 57  63  63  TYR TYR C . n 
B 1 58  TYR 58  64  64  TYR TYR C . n 
B 1 59  CYS 59  65  65  CYS CYS C . n 
B 1 60  SER 60  66  66  SER SER C . n 
B 1 61  SER 61  67  67  SER SER C . n 
B 1 62  ARG 62  68  68  ARG ARG C . n 
B 1 63  ARG 63  69  69  ARG ARG C . n 
B 1 64  LYS 64  70  70  LYS LYS C . n 
B 1 65  HIS 65  71  71  HIS HIS C . n 
B 1 66  TYR 66  72  72  TYR TYR C . n 
B 1 67  PRO 67  73  73  PRO PRO C . n 
B 1 68  VAL 68  74  74  VAL VAL C . n 
B 1 69  SER 69  75  75  SER SER C . n 
B 1 70  PHE 70  76  76  PHE PHE C . n 
B 1 71  SER 71  77  77  SER SER C . n 
B 1 72  LYS 72  78  78  LYS LYS C . n 
B 1 73  PRO 73  79  79  PRO PRO C . n 
B 1 74  SER 74  80  80  SER SER C . n 
B 1 75  LEU 75  81  81  LEU LEU C . n 
B 1 76  ILE 76  82  82  ILE ILE C . n 
B 1 77  PHE 77  83  83  PHE PHE C . n 
B 1 78  VAL 78  84  84  VAL VAL C . n 
B 1 79  GLU 79  85  85  GLU GLU C . n 
B 1 80  ALA 80  86  86  ALA ALA C . n 
B 1 81  SER 81  87  87  SER SER C . n 
B 1 82  GLU 82  88  88  GLU GLU C . n 
B 1 83  TYR 83  89  89  TYR TYR C . n 
B 1 84  TYR 84  90  90  TYR TYR C . n 
B 1 85  PRO 85  91  91  PRO PRO C . n 
B 1 86  ALA 86  92  92  ALA ALA C . n 
B 1 87  ARG 87  93  93  ARG ARG C . n 
B 1 88  TYR 88  94  94  TYR TYR C . n 
B 1 89  GLN 89  95  95  GLN GLN C . n 
B 1 90  SER 90  96  96  SER SER C . n 
B 1 91  HIS 91  97  97  HIS HIS C . n 
B 1 92  LEU 92  98  98  LEU LEU C . n 
B 1 93  MET 93  99  99  MET MET C . n 
B 1 94  LEU 94  100 100 LEU LEU C . n 
B 1 95  ALA 95  101 101 ALA ALA C . n 
B 1 96  VAL 96  102 102 VAL VAL C . n 
B 1 97  GLY 97  103 103 GLY GLY C . n 
B 1 98  HIS 98  104 104 HIS HIS C . n 
B 1 99  SER 99  105 105 SER SER C . n 
B 1 100 GLU 100 106 106 GLU GLU C . n 
B 1 101 PRO 101 107 107 PRO PRO C . n 
B 1 102 GLY 102 108 108 GLY GLY C . n 
B 1 103 ASP 103 109 109 ASP ASP C . n 
B 1 104 CYS 104 110 110 CYS CYS C . n 
B 1 105 GLY 105 111 111 GLY GLY C . n 
B 1 106 GLY 106 112 112 GLY GLY C . n 
B 1 107 ILE 107 113 113 ILE ILE C . n 
B 1 108 LEU 108 114 114 LEU LEU C . n 
B 1 109 ARG 109 115 115 ARG ARG C . n 
B 1 110 CYS 110 116 116 CYS CYS C . n 
B 1 111 GLN 111 117 117 GLN GLN C . n 
B 1 112 HIS 112 118 118 HIS HIS C . n 
B 1 113 GLY 113 119 119 GLY GLY C . n 
B 1 114 VAL 114 120 120 VAL VAL C . n 
B 1 115 VAL 115 121 121 VAL VAL C . n 
B 1 116 GLY 116 122 122 GLY GLY C . n 
B 1 117 ILE 117 123 123 ILE ILE C . n 
B 1 118 VAL 118 124 124 VAL VAL C . n 
B 1 119 SER 119 125 125 SER SER C . n 
B 1 120 THR 120 126 126 THR THR C . n 
B 1 121 GLY 121 127 127 GLY GLY C . n 
B 1 122 GLY 122 128 128 GLY GLY C . n 
B 1 123 ASN 123 129 129 ASN ASN C . n 
B 1 124 GLY 124 130 130 GLY GLY C . n 
B 1 125 LEU 125 131 131 LEU LEU C . n 
B 1 126 VAL 126 132 132 VAL VAL C . n 
B 1 127 GLY 127 133 133 GLY GLY C . n 
B 1 128 PHE 128 134 134 PHE PHE C . n 
B 1 129 ALA 129 135 135 ALA ALA C . n 
B 1 130 ASP 130 136 136 ASP ASP C . n 
B 1 131 VAL 131 137 137 VAL VAL C . n 
B 1 132 ARG 132 138 138 ARG ARG C . n 
B 1 133 ASP 133 139 139 ASP ASP C . n 
B 1 134 LEU 134 140 140 LEU LEU C . n 
B 1 135 LEU 135 141 141 LEU LEU C . n 
B 1 136 TRP 136 142 142 TRP TRP C . n 
B 1 137 LEU 137 143 143 LEU LEU C . n 
B 1 138 ASP 138 144 144 ASP ASP C . n 
B 1 139 GLU 139 145 145 GLU GLU C . n 
B 1 140 GLU 140 146 146 GLU GLU C . n 
B 1 141 ALA 141 147 ?   ?   ?   C . n 
B 1 142 MET 142 148 ?   ?   ?   C . n 
B 1 143 GLU 143 149 ?   ?   ?   C . n 
B 1 144 GLN 144 150 ?   ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BQ7 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BQ7 
_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 
C 2 ZN    1   201 1   ZN    ZN  A . 
D 3 A1BQ7 1   202 301 A1BQ7 LIG A . 
E 4 DMS   1   203 6   DMS   DMS A . 
F 4 DMS   1   201 1   DMS   DMS C . 
G 2 ZN    1   202 1   ZN    ZN  C . 
H 4 DMS   1   203 1   DMS   DMS C . 
I 5 HOH   1   301 150 HOH   HOH A . 
I 5 HOH   2   302 301 HOH   HOH A . 
I 5 HOH   3   303 98  HOH   HOH A . 
I 5 HOH   4   304 175 HOH   HOH A . 
I 5 HOH   5   305 79  HOH   HOH A . 
I 5 HOH   6   306 159 HOH   HOH A . 
I 5 HOH   7   307 268 HOH   HOH A . 
I 5 HOH   8   308 243 HOH   HOH A . 
I 5 HOH   9   309 162 HOH   HOH A . 
I 5 HOH   10  310 133 HOH   HOH A . 
I 5 HOH   11  311 276 HOH   HOH A . 
I 5 HOH   12  312 171 HOH   HOH A . 
I 5 HOH   13  313 97  HOH   HOH A . 
I 5 HOH   14  314 236 HOH   HOH A . 
I 5 HOH   15  315 69  HOH   HOH A . 
I 5 HOH   16  316 81  HOH   HOH A . 
I 5 HOH   17  317 16  HOH   HOH A . 
I 5 HOH   18  318 215 HOH   HOH A . 
I 5 HOH   19  319 197 HOH   HOH A . 
I 5 HOH   20  320 158 HOH   HOH A . 
I 5 HOH   21  321 205 HOH   HOH A . 
I 5 HOH   22  322 63  HOH   HOH A . 
I 5 HOH   23  323 184 HOH   HOH A . 
I 5 HOH   24  324 284 HOH   HOH A . 
I 5 HOH   25  325 214 HOH   HOH A . 
I 5 HOH   26  326 102 HOH   HOH A . 
I 5 HOH   27  327 62  HOH   HOH A . 
I 5 HOH   28  328 143 HOH   HOH A . 
I 5 HOH   29  329 253 HOH   HOH A . 
I 5 HOH   30  330 103 HOH   HOH A . 
I 5 HOH   31  331 86  HOH   HOH A . 
I 5 HOH   32  332 121 HOH   HOH A . 
I 5 HOH   33  333 106 HOH   HOH A . 
I 5 HOH   34  334 9   HOH   HOH A . 
I 5 HOH   35  335 208 HOH   HOH A . 
I 5 HOH   36  336 77  HOH   HOH A . 
I 5 HOH   37  337 190 HOH   HOH A . 
I 5 HOH   38  338 37  HOH   HOH A . 
I 5 HOH   39  339 112 HOH   HOH A . 
I 5 HOH   40  340 155 HOH   HOH A . 
I 5 HOH   41  341 82  HOH   HOH A . 
I 5 HOH   42  342 157 HOH   HOH A . 
I 5 HOH   43  343 1   HOH   HOH A . 
I 5 HOH   44  344 3   HOH   HOH A . 
I 5 HOH   45  345 27  HOH   HOH A . 
I 5 HOH   46  346 123 HOH   HOH A . 
I 5 HOH   47  347 207 HOH   HOH A . 
I 5 HOH   48  348 89  HOH   HOH A . 
I 5 HOH   49  349 307 HOH   HOH A . 
I 5 HOH   50  350 34  HOH   HOH A . 
I 5 HOH   51  351 15  HOH   HOH A . 
I 5 HOH   52  352 95  HOH   HOH A . 
I 5 HOH   53  353 139 HOH   HOH A . 
I 5 HOH   54  354 287 HOH   HOH A . 
I 5 HOH   55  355 188 HOH   HOH A . 
I 5 HOH   56  356 160 HOH   HOH A . 
I 5 HOH   57  357 7   HOH   HOH A . 
I 5 HOH   58  358 84  HOH   HOH A . 
I 5 HOH   59  359 43  HOH   HOH A . 
I 5 HOH   60  360 288 HOH   HOH A . 
I 5 HOH   61  361 56  HOH   HOH A . 
I 5 HOH   62  362 124 HOH   HOH A . 
I 5 HOH   63  363 41  HOH   HOH A . 
I 5 HOH   64  364 60  HOH   HOH A . 
I 5 HOH   65  365 21  HOH   HOH A . 
I 5 HOH   66  366 55  HOH   HOH A . 
I 5 HOH   67  367 304 HOH   HOH A . 
I 5 HOH   68  368 29  HOH   HOH A . 
I 5 HOH   69  369 272 HOH   HOH A . 
I 5 HOH   70  370 148 HOH   HOH A . 
I 5 HOH   71  371 295 HOH   HOH A . 
I 5 HOH   72  372 36  HOH   HOH A . 
I 5 HOH   73  373 131 HOH   HOH A . 
I 5 HOH   74  374 108 HOH   HOH A . 
I 5 HOH   75  375 92  HOH   HOH A . 
I 5 HOH   76  376 18  HOH   HOH A . 
I 5 HOH   77  377 258 HOH   HOH A . 
I 5 HOH   78  378 237 HOH   HOH A . 
I 5 HOH   79  379 113 HOH   HOH A . 
I 5 HOH   80  380 285 HOH   HOH A . 
I 5 HOH   81  381 26  HOH   HOH A . 
I 5 HOH   82  382 64  HOH   HOH A . 
I 5 HOH   83  383 269 HOH   HOH A . 
I 5 HOH   84  384 165 HOH   HOH A . 
I 5 HOH   85  385 71  HOH   HOH A . 
I 5 HOH   86  386 104 HOH   HOH A . 
I 5 HOH   87  387 122 HOH   HOH A . 
I 5 HOH   88  388 267 HOH   HOH A . 
I 5 HOH   89  389 203 HOH   HOH A . 
I 5 HOH   90  390 263 HOH   HOH A . 
I 5 HOH   91  391 248 HOH   HOH A . 
I 5 HOH   92  392 33  HOH   HOH A . 
I 5 HOH   93  393 189 HOH   HOH A . 
I 5 HOH   94  394 169 HOH   HOH A . 
I 5 HOH   95  395 101 HOH   HOH A . 
I 5 HOH   96  396 164 HOH   HOH A . 
I 5 HOH   97  397 218 HOH   HOH A . 
I 5 HOH   98  398 28  HOH   HOH A . 
I 5 HOH   99  399 219 HOH   HOH A . 
I 5 HOH   100 400 257 HOH   HOH A . 
I 5 HOH   101 401 141 HOH   HOH A . 
I 5 HOH   102 402 6   HOH   HOH A . 
I 5 HOH   103 403 235 HOH   HOH A . 
I 5 HOH   104 404 5   HOH   HOH A . 
I 5 HOH   105 405 216 HOH   HOH A . 
I 5 HOH   106 406 200 HOH   HOH A . 
I 5 HOH   107 407 255 HOH   HOH A . 
I 5 HOH   108 408 254 HOH   HOH A . 
I 5 HOH   109 409 115 HOH   HOH A . 
I 5 HOH   110 410 120 HOH   HOH A . 
I 5 HOH   111 411 206 HOH   HOH A . 
I 5 HOH   112 412 116 HOH   HOH A . 
I 5 HOH   113 413 17  HOH   HOH A . 
I 5 HOH   114 414 153 HOH   HOH A . 
I 5 HOH   115 415 45  HOH   HOH A . 
I 5 HOH   116 416 72  HOH   HOH A . 
I 5 HOH   117 417 181 HOH   HOH A . 
I 5 HOH   118 418 53  HOH   HOH A . 
I 5 HOH   119 419 48  HOH   HOH A . 
I 5 HOH   120 420 266 HOH   HOH A . 
I 5 HOH   121 421 8   HOH   HOH A . 
I 5 HOH   122 422 68  HOH   HOH A . 
I 5 HOH   123 423 260 HOH   HOH A . 
I 5 HOH   124 424 294 HOH   HOH A . 
I 5 HOH   125 425 183 HOH   HOH A . 
I 5 HOH   126 426 212 HOH   HOH A . 
I 5 HOH   127 427 271 HOH   HOH A . 
I 5 HOH   128 428 202 HOH   HOH A . 
I 5 HOH   129 429 223 HOH   HOH A . 
I 5 HOH   130 430 185 HOH   HOH A . 
I 5 HOH   131 431 306 HOH   HOH A . 
I 5 HOH   132 432 210 HOH   HOH A . 
I 5 HOH   133 433 88  HOH   HOH A . 
I 5 HOH   134 434 154 HOH   HOH A . 
I 5 HOH   135 435 177 HOH   HOH A . 
I 5 HOH   136 436 305 HOH   HOH A . 
I 5 HOH   137 437 140 HOH   HOH A . 
I 5 HOH   138 438 261 HOH   HOH A . 
I 5 HOH   139 439 100 HOH   HOH A . 
I 5 HOH   140 440 117 HOH   HOH A . 
I 5 HOH   141 441 196 HOH   HOH A . 
I 5 HOH   142 442 244 HOH   HOH A . 
I 5 HOH   143 443 125 HOH   HOH A . 
I 5 HOH   144 444 262 HOH   HOH A . 
I 5 HOH   145 445 252 HOH   HOH A . 
I 5 HOH   146 446 270 HOH   HOH A . 
I 5 HOH   147 447 274 HOH   HOH A . 
J 5 HOH   1   301 110 HOH   HOH C . 
J 5 HOH   2   302 283 HOH   HOH C . 
J 5 HOH   3   303 225 HOH   HOH C . 
J 5 HOH   4   304 234 HOH   HOH C . 
J 5 HOH   5   305 80  HOH   HOH C . 
J 5 HOH   6   306 144 HOH   HOH C . 
J 5 HOH   7   307 161 HOH   HOH C . 
J 5 HOH   8   308 180 HOH   HOH C . 
J 5 HOH   9   309 75  HOH   HOH C . 
J 5 HOH   10  310 67  HOH   HOH C . 
J 5 HOH   11  311 142 HOH   HOH C . 
J 5 HOH   12  312 279 HOH   HOH C . 
J 5 HOH   13  313 85  HOH   HOH C . 
J 5 HOH   14  314 11  HOH   HOH C . 
J 5 HOH   15  315 99  HOH   HOH C . 
J 5 HOH   16  316 289 HOH   HOH C . 
J 5 HOH   17  317 182 HOH   HOH C . 
J 5 HOH   18  318 126 HOH   HOH C . 
J 5 HOH   19  319 231 HOH   HOH C . 
J 5 HOH   20  320 127 HOH   HOH C . 
J 5 HOH   21  321 199 HOH   HOH C . 
J 5 HOH   22  322 173 HOH   HOH C . 
J 5 HOH   23  323 2   HOH   HOH C . 
J 5 HOH   24  324 58  HOH   HOH C . 
J 5 HOH   25  325 40  HOH   HOH C . 
J 5 HOH   26  326 90  HOH   HOH C . 
J 5 HOH   27  327 44  HOH   HOH C . 
J 5 HOH   28  328 4   HOH   HOH C . 
J 5 HOH   29  329 35  HOH   HOH C . 
J 5 HOH   30  330 302 HOH   HOH C . 
J 5 HOH   31  331 264 HOH   HOH C . 
J 5 HOH   32  332 265 HOH   HOH C . 
J 5 HOH   33  333 192 HOH   HOH C . 
J 5 HOH   34  334 174 HOH   HOH C . 
J 5 HOH   35  335 54  HOH   HOH C . 
J 5 HOH   36  336 191 HOH   HOH C . 
J 5 HOH   37  337 12  HOH   HOH C . 
J 5 HOH   38  338 217 HOH   HOH C . 
J 5 HOH   39  339 50  HOH   HOH C . 
J 5 HOH   40  340 176 HOH   HOH C . 
J 5 HOH   41  341 51  HOH   HOH C . 
J 5 HOH   42  342 151 HOH   HOH C . 
J 5 HOH   43  343 213 HOH   HOH C . 
J 5 HOH   44  344 91  HOH   HOH C . 
J 5 HOH   45  345 239 HOH   HOH C . 
J 5 HOH   46  346 22  HOH   HOH C . 
J 5 HOH   47  347 224 HOH   HOH C . 
J 5 HOH   48  348 186 HOH   HOH C . 
J 5 HOH   49  349 52  HOH   HOH C . 
J 5 HOH   50  350 135 HOH   HOH C . 
J 5 HOH   51  351 149 HOH   HOH C . 
J 5 HOH   52  352 87  HOH   HOH C . 
J 5 HOH   53  353 170 HOH   HOH C . 
J 5 HOH   54  354 25  HOH   HOH C . 
J 5 HOH   55  355 114 HOH   HOH C . 
J 5 HOH   56  356 156 HOH   HOH C . 
J 5 HOH   57  357 240 HOH   HOH C . 
J 5 HOH   58  358 76  HOH   HOH C . 
J 5 HOH   59  359 83  HOH   HOH C . 
J 5 HOH   60  360 47  HOH   HOH C . 
J 5 HOH   61  361 297 HOH   HOH C . 
J 5 HOH   62  362 222 HOH   HOH C . 
J 5 HOH   63  363 303 HOH   HOH C . 
J 5 HOH   64  364 78  HOH   HOH C . 
J 5 HOH   65  365 241 HOH   HOH C . 
J 5 HOH   66  366 201 HOH   HOH C . 
J 5 HOH   67  367 232 HOH   HOH C . 
J 5 HOH   68  368 242 HOH   HOH C . 
J 5 HOH   69  369 129 HOH   HOH C . 
J 5 HOH   70  370 168 HOH   HOH C . 
J 5 HOH   71  371 14  HOH   HOH C . 
J 5 HOH   72  372 293 HOH   HOH C . 
J 5 HOH   73  373 119 HOH   HOH C . 
J 5 HOH   74  374 167 HOH   HOH C . 
J 5 HOH   75  375 31  HOH   HOH C . 
J 5 HOH   76  376 111 HOH   HOH C . 
J 5 HOH   77  377 19  HOH   HOH C . 
J 5 HOH   78  378 105 HOH   HOH C . 
J 5 HOH   79  379 66  HOH   HOH C . 
J 5 HOH   80  380 42  HOH   HOH C . 
J 5 HOH   81  381 30  HOH   HOH C . 
J 5 HOH   82  382 74  HOH   HOH C . 
J 5 HOH   83  383 24  HOH   HOH C . 
J 5 HOH   84  384 147 HOH   HOH C . 
J 5 HOH   85  385 163 HOH   HOH C . 
J 5 HOH   86  386 57  HOH   HOH C . 
J 5 HOH   87  387 73  HOH   HOH C . 
J 5 HOH   88  388 211 HOH   HOH C . 
J 5 HOH   89  389 221 HOH   HOH C . 
J 5 HOH   90  390 107 HOH   HOH C . 
J 5 HOH   91  391 195 HOH   HOH C . 
J 5 HOH   92  392 152 HOH   HOH C . 
J 5 HOH   93  393 137 HOH   HOH C . 
J 5 HOH   94  394 118 HOH   HOH C . 
J 5 HOH   95  395 96  HOH   HOH C . 
J 5 HOH   96  396 49  HOH   HOH C . 
J 5 HOH   97  397 275 HOH   HOH C . 
J 5 HOH   98  398 59  HOH   HOH C . 
J 5 HOH   99  399 179 HOH   HOH C . 
J 5 HOH   100 400 187 HOH   HOH C . 
J 5 HOH   101 401 20  HOH   HOH C . 
J 5 HOH   102 402 166 HOH   HOH C . 
J 5 HOH   103 403 61  HOH   HOH C . 
J 5 HOH   104 404 93  HOH   HOH C . 
J 5 HOH   105 405 38  HOH   HOH C . 
J 5 HOH   106 406 204 HOH   HOH C . 
J 5 HOH   107 407 220 HOH   HOH C . 
J 5 HOH   108 408 228 HOH   HOH C . 
J 5 HOH   109 409 194 HOH   HOH C . 
J 5 HOH   110 410 238 HOH   HOH C . 
J 5 HOH   111 411 145 HOH   HOH C . 
J 5 HOH   112 412 277 HOH   HOH C . 
J 5 HOH   113 413 94  HOH   HOH C . 
J 5 HOH   114 414 65  HOH   HOH C . 
J 5 HOH   115 415 46  HOH   HOH C . 
J 5 HOH   116 416 39  HOH   HOH C . 
J 5 HOH   117 417 226 HOH   HOH C . 
J 5 HOH   118 418 70  HOH   HOH C . 
J 5 HOH   119 419 130 HOH   HOH C . 
J 5 HOH   120 420 172 HOH   HOH C . 
J 5 HOH   121 421 251 HOH   HOH C . 
J 5 HOH   122 422 134 HOH   HOH C . 
J 5 HOH   123 423 13  HOH   HOH C . 
J 5 HOH   124 424 32  HOH   HOH C . 
J 5 HOH   125 425 23  HOH   HOH C . 
J 5 HOH   126 426 292 HOH   HOH C . 
J 5 HOH   127 427 193 HOH   HOH C . 
J 5 HOH   128 428 230 HOH   HOH C . 
J 5 HOH   129 429 227 HOH   HOH C . 
J 5 HOH   130 430 298 HOH   HOH C . 
J 5 HOH   131 431 249 HOH   HOH C . 
J 5 HOH   132 432 128 HOH   HOH C . 
J 5 HOH   133 433 10  HOH   HOH C . 
J 5 HOH   134 434 136 HOH   HOH C . 
J 5 HOH   135 435 278 HOH   HOH C . 
J 5 HOH   136 436 138 HOH   HOH C . 
J 5 HOH   137 437 132 HOH   HOH C . 
J 5 HOH   138 438 308 HOH   HOH C . 
J 5 HOH   139 439 280 HOH   HOH C . 
J 5 HOH   140 440 273 HOH   HOH C . 
J 5 HOH   141 441 281 HOH   HOH C . 
J 5 HOH   142 442 229 HOH   HOH C . 
J 5 HOH   143 443 282 HOH   HOH C . 
J 5 HOH   144 444 198 HOH   HOH C . 
J 5 HOH   145 445 246 HOH   HOH C . 
J 5 HOH   146 446 286 HOH   HOH C . 
J 5 HOH   147 447 291 HOH   HOH C . 
J 5 HOH   148 448 259 HOH   HOH C . 
J 5 HOH   149 449 146 HOH   HOH C . 
J 5 HOH   150 450 178 HOH   HOH C . 
J 5 HOH   151 451 233 HOH   HOH C . 
J 5 HOH   152 452 296 HOH   HOH C . 
J 5 HOH   153 453 109 HOH   HOH C . 
J 5 HOH   154 454 209 HOH   HOH C . 
J 5 HOH   155 455 250 HOH   HOH C . 
J 5 HOH   156 456 245 HOH   HOH C . 
J 5 HOH   157 457 299 HOH   HOH C . 
J 5 HOH   158 458 290 HOH   HOH C . 
J 5 HOH   159 459 256 HOH   HOH C . 
J 5 HOH   160 460 247 HOH   HOH C . 
# 
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           7HZS 
_cell.length_a           86.733 
_cell.length_b           57.149 
_cell.length_c           64.871 
_cell.angle_alpha        90.00 
_cell.angle_beta         94.64 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HZS 
_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          7HZS 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.52 
_exptl_crystal.density_percent_sol   51.20 
_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   2024-10-10 
_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   0.92208 
_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        0.92208 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HZS 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             64.66 
_reflns.d_resolution_high            1.23 
_reflns.number_obs                   80442 
_reflns.percent_possible_obs         87.7 
_reflns.pdbx_Rmerge_I_obs            0.064 
_reflns.pdbx_netI_over_sigmaI        16.0 
_reflns.pdbx_redundancy              5.6 
_reflns.pdbx_Rrim_I_all              0.070 
_reflns.pdbx_Rpim_I_all              0.028 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_number_measured_all     447418 
_reflns.pdbx_chi_squared             1.04 
_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                  1.23 
_reflns_shell.d_res_low                   1.25 
_reflns_shell.number_measured_all         3308 
_reflns_shell.number_unique_obs           1654 
_reflns_shell.Rmerge_I_obs                0.922 
_reflns_shell.pdbx_chi_squared            0.39 
_reflns_shell.pdbx_redundancy             2.0 
_reflns_shell.percent_possible_obs        36.3 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.6 
_reflns_shell.pdbx_Rrim_I_all             1.227 
_reflns_shell.pdbx_Rpim_I_all             0.799 
_reflns_shell.pdbx_CC_half                0.384 
_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                                 7HZS 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     76524 
_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                             64.66 
_refine.ls_d_res_high                            1.23 
_refine.ls_percent_reflns_obs                    87.69 
_refine.ls_R_factor_obs                          0.18998 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.18916 
_refine.ls_R_factor_R_free                       0.20573 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.8 
_refine.ls_number_reflns_R_free                  3860 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.965 
_refine.correlation_coeff_Fo_to_Fc_free          0.964 
_refine.B_iso_mean                               16.713 
_refine.aniso_B[1][1]                            -0.21 
_refine.aniso_B[2][2]                            0.25 
_refine.aniso_B[3][3]                            -0.10 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            0.37 
_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                       0.060 
_refine.pdbx_overall_ESU_R_Free                  0.059 
_refine.overall_SU_ML                            0.051 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             1.263 
_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        2166 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         34 
_refine_hist.number_atoms_solvent             307 
_refine_hist.number_atoms_total               2507 
_refine_hist.d_res_high                       1.23 
_refine_hist.d_res_low                        64.66 
# 
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             0.010  0.014  ? 4019 'X-RAY DIFFRACTION' ? 
r_bond_other_d               0.001  0.015  ? 2751 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.776  1.627  ? 4302 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            1.449  1.587  ? 6338 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       6.677  5.000  ? 410  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       35.025 21.288 ? 163  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       12.914 15.000 ? 437  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       19.716 15.000 ? 21   'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.088  0.200  ? 378  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.011  0.020  ? 3885 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           0.003  0.020  ? 777  '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  1.654  ? 2198 'X-RAY DIFFRACTION' ? 
r_mcbond_other               1.302  1.498  ? 1890 'X-RAY DIFFRACTION' ? 
r_mcangle_it                 2.155  2.225  ? 2014 'X-RAY DIFFRACTION' ? 
r_mcangle_other              2.155  2.227  ? 2015 'X-RAY DIFFRACTION' ? 
r_scbond_it                  2.265  1.813  ? 1821 'X-RAY DIFFRACTION' ? 
r_scbond_other               2.264  1.819  ? 1822 'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              3.330  2.623  ? 2289 'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       6.085  19.783 ? 3633 'X-RAY DIFFRACTION' ? 
r_long_range_B_other         6.140  19.345 ? 3552 '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                       1.230 
_refine_ls_shell.d_res_low                        1.262 
_refine_ls_shell.number_reflns_R_work             2479 
_refine_ls_shell.R_factor_R_work                  0.350 
_refine_ls_shell.percent_reflns_obs               37.67 
_refine_ls_shell.R_factor_R_free                  0.323 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             78 
_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                  7HZS 
_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-0031972-001 (A71EV2A-x3223)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HZS 
_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 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 4 ? 
G N N 2 ? 
H N N 4 ? 
I N N 5 ? 
J N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    POLG_CX16G 
_struct_ref.pdbx_db_accession          Q65900 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_struct_ref.pdbx_align_begin           869 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HZS A 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
2 1 7HZS C 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,I 
2 1 B,F,G,H,J 
# 
_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 SER A 30  ? ARG A 32  ? SER A 36  ARG A 38  5 ? 3 
HELX_P HELX_P4  AA4 SER A 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
HELX_P HELX_P5  AA5 LEU A 134 ? GLU A 139 ? LEU A 140 GLU A 145 5 ? 6 
HELX_P HELX_P6  AA6 HIS B 15  ? ALA B 17  ? HIS C 21  ALA C 23  5 ? 3 
HELX_P HELX_P7  AA7 THR B 18  ? ASN B 24  ? THR C 24  ASN C 30  1 ? 7 
HELX_P HELX_P8  AA8 SER B 30  ? ARG B 32  ? SER C 36  ARG C 38  5 ? 3 
HELX_P HELX_P9  AA9 SER B 60  ? ARG B 63  ? SER C 66  ARG C 69  5 ? 4 
HELX_P HELX_P10 AB1 GLU B 100 ? CYS B 104 ? GLU C 106 CYS C 110 5 ? 5 
HELX_P HELX_P11 AB2 LEU B 134 ? GLU B 139 ? LEU C 140 GLU C 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 C ZN . ZN ? ? A CYS 56  A ZN 201 1_555 ? ? ? ? ? ? ? 2.421 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 58  A ZN 201 1_555 ? ? ? ? ? ? ? 2.316 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 116 A ZN 201 1_555 ? ? ? ? ? ? ? 2.228 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 C ZN . ZN ? ? A HIS 118 A ZN 201 1_555 ? ? ? ? ? ? ? 1.990 ? ? 
metalc5 metalc ? ? B CYS 50  SG  ? ? ? 1_555 G ZN . ZN ? ? C CYS 56  C ZN 202 1_555 ? ? ? ? ? ? ? 2.355 ? ? 
metalc6 metalc ? ? B CYS 52  SG  ? ? ? 1_555 G ZN . ZN ? ? C CYS 58  C ZN 202 1_555 ? ? ? ? ? ? ? 2.336 ? ? 
metalc7 metalc ? ? B CYS 110 SG  ? ? ? 1_555 G ZN . ZN ? ? C CYS 116 C ZN 202 1_555 ? ? ? ? ? ? ? 2.284 ? ? 
metalc8 metalc ? ? B HIS 112 ND1 ? ? ? 1_555 G ZN . ZN ? ? C HIS 118 C ZN 202 1_555 ? ? ? ? ? ? ? 2.085 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 201 ? 1_555 SG  ? A CYS 52  ? A CYS 58  ? 1_555 109.0 ? 
2  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 201 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 105.0 ? 
3  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? C ZN . ? A ZN 201 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 117.5 ? 
4  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 201 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 98.6  ? 
5  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? C ZN . ? A ZN 201 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 102.3 ? 
6  SG ? A CYS 110 ? A CYS 116 ? 1_555 ZN ? C ZN . ? A ZN 201 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 122.4 ? 
7  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? G ZN . ? C ZN 202 ? 1_555 SG  ? B CYS 52  ? C CYS 58  ? 1_555 109.7 ? 
8  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? G ZN . ? C ZN 202 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 106.5 ? 
9  SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? G ZN . ? C ZN 202 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 118.6 ? 
10 SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? G ZN . ? C ZN 202 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 105.3 ? 
11 SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? G ZN . ? C ZN 202 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 101.2 ? 
12 SG ? B CYS 110 ? C CYS 116 ? 1_555 ZN ? G ZN . ? C ZN 202 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 114.8 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 7 ? 
AA3 ? 3 ? 
AA4 ? 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 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA1 2 LEU A 34  ? CYS A 44  ? LEU A 40  CYS A 50  
AA1 3 ILE A 4   ? ASN A 13  ? ILE A 10  ASN A 19  
AA2 1 LYS A 64  ? SER A 69  ? LYS A 70  SER A 75  
AA2 2 THR A 54  ? CYS A 59  ? THR A 60  CYS A 65  
AA2 3 ILE A 107 ? CYS A 110 ? ILE A 113 CYS A 116 
AA2 4 GLY A 113 ? THR A 120 ? GLY A 119 THR A 126 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
AA3 1 LEU B 25  ? ASP B 29  ? LEU C 31  ASP C 35  
AA3 2 LEU B 34  ? CYS B 44  ? LEU C 40  CYS C 50  
AA3 3 ILE B 4   ? ASN B 13  ? ILE C 10  ASN C 19  
AA4 1 LYS B 64  ? SER B 69  ? LYS C 70  SER C 75  
AA4 2 THR B 54  ? CYS B 59  ? THR C 60  CYS C 65  
AA4 3 ILE B 107 ? CYS B 110 ? ILE C 113 CYS C 116 
AA4 4 GLY B 113 ? GLY B 122 ? GLY C 119 GLY C 128 
AA4 5 LEU B 125 ? ASP B 130 ? LEU C 131 ASP C 136 
AA4 6 ARG B 87  ? VAL B 96  ? ARG C 93  VAL C 102 
AA4 7 SER B 74  ? VAL B 78  ? SER C 80  VAL C 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 26  ? N VAL A 32  O VAL A 36  ? O VAL A 42  
AA1 2 3 N LEU A 35  ? N LEU A 41  O VAL A 12  ? O VAL A 18  
AA2 1 2 O 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  
AA3 1 2 N TRP B 27  ? N TRP C 33  O VAL B 36  ? O VAL C 42  
AA3 2 3 N LEU B 35  ? N LEU C 41  O VAL B 12  ? O VAL C 18  
AA4 1 2 O LYS B 64  ? O LYS C 70  N CYS B 59  ? N CYS C 65  
AA4 2 3 N VAL B 56  ? N VAL C 62  O ARG B 109 ? O ARG C 115 
AA4 3 4 N LEU B 108 ? N LEU C 114 O VAL B 115 ? O VAL C 121 
AA4 4 5 N SER B 119 ? N SER C 125 O GLY B 127 ? O GLY C 133 
AA4 5 6 O PHE B 128 ? O PHE C 134 N MET B 93  ? N MET C 99  
AA4 6 7 O ARG B 87  ? O ARG C 93  N VAL B 78  ? N VAL C 84  
# 
_pdbx_entry_details.entry_id                   7HZS 
_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 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   CB 
_pdbx_validate_close_contact.auth_asym_id_1   C 
_pdbx_validate_close_contact.auth_comp_id_1   SER 
_pdbx_validate_close_contact.auth_seq_id_1    66 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   C 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    302 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.63 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 NE A ARG 93  ? ? CZ A ARG 93  ? ? NH1 A ARG 93  ? ? 123.53 120.30 3.23  0.50 N 
2 1 NE A ARG 93  ? ? CZ A ARG 93  ? ? NH2 A ARG 93  ? ? 116.58 120.30 -3.72 0.50 N 
3 1 CB A ASP 136 ? ? CG A ASP 136 ? ? OD2 A ASP 136 ? ? 112.14 118.30 -6.16 0.90 N 
4 1 NE A ARG 138 ? ? CZ A ARG 138 ? ? NH2 A ARG 138 ? ? 116.55 120.30 -3.75 0.50 N 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    SER 
_pdbx_validate_torsion.auth_asym_id    C 
_pdbx_validate_torsion.auth_seq_id     125 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -132.73 
_pdbx_validate_torsion.psi             -30.15 
# 
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 
5 1 Y 1 C ALA 147 ? B ALA 141 
6 1 Y 1 C MET 148 ? B MET 142 
7 1 Y 1 C GLU 149 ? B GLU 143 
8 1 Y 1 C GLN 150 ? B 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 
A1BQ7 N1   N  N N 1   
A1BQ7 N3   N  Y N 2   
A1BQ7 C4   C  N N 3   
A1BQ7 C5   C  N N 4   
A1BQ7 C6   C  Y N 5   
A1BQ7 C7   C  Y N 6   
A1BQ7 C8   C  Y N 7   
A1BQ7 C10  C  Y N 8   
A1BQ7 N    N  N N 9   
A1BQ7 C    C  N N 10  
A1BQ7 O    O  N N 11  
A1BQ7 C1   C  N S 12  
A1BQ7 C11  C  Y N 13  
A1BQ7 C12  C  N N 14  
A1BQ7 C2   C  N N 15  
A1BQ7 C3   C  N N 16  
A1BQ7 C9   C  Y N 17  
A1BQ7 N2   N  Y N 18  
A1BQ7 N4   N  Y N 19  
A1BQ7 O1   O  N N 20  
A1BQ7 H1   H  N N 21  
A1BQ7 H9   H  N N 22  
A1BQ7 H8   H  N N 23  
A1BQ7 H10  H  N N 24  
A1BQ7 H11  H  N N 25  
A1BQ7 H12  H  N N 26  
A1BQ7 H2   H  N N 27  
A1BQ7 H3   H  N N 28  
A1BQ7 H    H  N N 29  
A1BQ7 H14  H  N N 30  
A1BQ7 H13  H  N N 31  
A1BQ7 H5   H  N N 32  
A1BQ7 H4   H  N N 33  
A1BQ7 H7   H  N N 34  
A1BQ7 H6   H  N N 35  
ALA   N    N  N N 36  
ALA   CA   C  N S 37  
ALA   C    C  N N 38  
ALA   O    O  N N 39  
ALA   CB   C  N N 40  
ALA   OXT  O  N N 41  
ALA   H    H  N N 42  
ALA   H2   H  N N 43  
ALA   HA   H  N N 44  
ALA   HB1  H  N N 45  
ALA   HB2  H  N N 46  
ALA   HB3  H  N N 47  
ALA   HXT  H  N N 48  
ARG   N    N  N N 49  
ARG   CA   C  N S 50  
ARG   C    C  N N 51  
ARG   O    O  N N 52  
ARG   CB   C  N N 53  
ARG   CG   C  N N 54  
ARG   CD   C  N N 55  
ARG   NE   N  N N 56  
ARG   CZ   C  N N 57  
ARG   NH1  N  N N 58  
ARG   NH2  N  N N 59  
ARG   OXT  O  N N 60  
ARG   H    H  N N 61  
ARG   H2   H  N N 62  
ARG   HA   H  N N 63  
ARG   HB2  H  N N 64  
ARG   HB3  H  N N 65  
ARG   HG2  H  N N 66  
ARG   HG3  H  N N 67  
ARG   HD2  H  N N 68  
ARG   HD3  H  N N 69  
ARG   HE   H  N N 70  
ARG   HH11 H  N N 71  
ARG   HH12 H  N N 72  
ARG   HH21 H  N N 73  
ARG   HH22 H  N N 74  
ARG   HXT  H  N N 75  
ASN   N    N  N N 76  
ASN   CA   C  N S 77  
ASN   C    C  N N 78  
ASN   O    O  N N 79  
ASN   CB   C  N N 80  
ASN   CG   C  N N 81  
ASN   OD1  O  N N 82  
ASN   ND2  N  N N 83  
ASN   OXT  O  N N 84  
ASN   H    H  N N 85  
ASN   H2   H  N N 86  
ASN   HA   H  N N 87  
ASN   HB2  H  N N 88  
ASN   HB3  H  N N 89  
ASN   HD21 H  N N 90  
ASN   HD22 H  N N 91  
ASN   HXT  H  N N 92  
ASP   N    N  N N 93  
ASP   CA   C  N S 94  
ASP   C    C  N N 95  
ASP   O    O  N N 96  
ASP   CB   C  N N 97  
ASP   CG   C  N N 98  
ASP   OD1  O  N N 99  
ASP   OD2  O  N N 100 
ASP   OXT  O  N N 101 
ASP   H    H  N N 102 
ASP   H2   H  N N 103 
ASP   HA   H  N N 104 
ASP   HB2  H  N N 105 
ASP   HB3  H  N N 106 
ASP   HD2  H  N N 107 
ASP   HXT  H  N N 108 
CYS   N    N  N N 109 
CYS   CA   C  N R 110 
CYS   C    C  N N 111 
CYS   O    O  N N 112 
CYS   CB   C  N N 113 
CYS   SG   S  N N 114 
CYS   OXT  O  N N 115 
CYS   H    H  N N 116 
CYS   H2   H  N N 117 
CYS   HA   H  N N 118 
CYS   HB2  H  N N 119 
CYS   HB3  H  N N 120 
CYS   HG   H  N N 121 
CYS   HXT  H  N N 122 
DMS   S    S  N N 123 
DMS   O    O  N N 124 
DMS   C1   C  N N 125 
DMS   C2   C  N N 126 
DMS   H11  H  N N 127 
DMS   H12  H  N N 128 
DMS   H13  H  N N 129 
DMS   H21  H  N N 130 
DMS   H22  H  N N 131 
DMS   H23  H  N N 132 
GLN   N    N  N N 133 
GLN   CA   C  N S 134 
GLN   C    C  N N 135 
GLN   O    O  N N 136 
GLN   CB   C  N N 137 
GLN   CG   C  N N 138 
GLN   CD   C  N N 139 
GLN   OE1  O  N N 140 
GLN   NE2  N  N N 141 
GLN   OXT  O  N N 142 
GLN   H    H  N N 143 
GLN   H2   H  N N 144 
GLN   HA   H  N N 145 
GLN   HB2  H  N N 146 
GLN   HB3  H  N N 147 
GLN   HG2  H  N N 148 
GLN   HG3  H  N N 149 
GLN   HE21 H  N N 150 
GLN   HE22 H  N N 151 
GLN   HXT  H  N N 152 
GLU   N    N  N N 153 
GLU   CA   C  N S 154 
GLU   C    C  N N 155 
GLU   O    O  N N 156 
GLU   CB   C  N N 157 
GLU   CG   C  N N 158 
GLU   CD   C  N N 159 
GLU   OE1  O  N N 160 
GLU   OE2  O  N N 161 
GLU   OXT  O  N N 162 
GLU   H    H  N N 163 
GLU   H2   H  N N 164 
GLU   HA   H  N N 165 
GLU   HB2  H  N N 166 
GLU   HB3  H  N N 167 
GLU   HG2  H  N N 168 
GLU   HG3  H  N N 169 
GLU   HE2  H  N N 170 
GLU   HXT  H  N N 171 
GLY   N    N  N N 172 
GLY   CA   C  N N 173 
GLY   C    C  N N 174 
GLY   O    O  N N 175 
GLY   OXT  O  N N 176 
GLY   H    H  N N 177 
GLY   H2   H  N N 178 
GLY   HA2  H  N N 179 
GLY   HA3  H  N N 180 
GLY   HXT  H  N N 181 
HIS   N    N  N N 182 
HIS   CA   C  N S 183 
HIS   C    C  N N 184 
HIS   O    O  N N 185 
HIS   CB   C  N N 186 
HIS   CG   C  Y N 187 
HIS   ND1  N  Y N 188 
HIS   CD2  C  Y N 189 
HIS   CE1  C  Y N 190 
HIS   NE2  N  Y N 191 
HIS   OXT  O  N N 192 
HIS   H    H  N N 193 
HIS   H2   H  N N 194 
HIS   HA   H  N N 195 
HIS   HB2  H  N N 196 
HIS   HB3  H  N N 197 
HIS   HD1  H  N N 198 
HIS   HD2  H  N N 199 
HIS   HE1  H  N N 200 
HIS   HE2  H  N N 201 
HIS   HXT  H  N N 202 
HOH   O    O  N N 203 
HOH   H1   H  N N 204 
HOH   H2   H  N N 205 
ILE   N    N  N N 206 
ILE   CA   C  N S 207 
ILE   C    C  N N 208 
ILE   O    O  N N 209 
ILE   CB   C  N S 210 
ILE   CG1  C  N N 211 
ILE   CG2  C  N N 212 
ILE   CD1  C  N N 213 
ILE   OXT  O  N N 214 
ILE   H    H  N N 215 
ILE   H2   H  N N 216 
ILE   HA   H  N N 217 
ILE   HB   H  N N 218 
ILE   HG12 H  N N 219 
ILE   HG13 H  N N 220 
ILE   HG21 H  N N 221 
ILE   HG22 H  N N 222 
ILE   HG23 H  N N 223 
ILE   HD11 H  N N 224 
ILE   HD12 H  N N 225 
ILE   HD13 H  N N 226 
ILE   HXT  H  N N 227 
LEU   N    N  N N 228 
LEU   CA   C  N S 229 
LEU   C    C  N N 230 
LEU   O    O  N N 231 
LEU   CB   C  N N 232 
LEU   CG   C  N N 233 
LEU   CD1  C  N N 234 
LEU   CD2  C  N N 235 
LEU   OXT  O  N N 236 
LEU   H    H  N N 237 
LEU   H2   H  N N 238 
LEU   HA   H  N N 239 
LEU   HB2  H  N N 240 
LEU   HB3  H  N N 241 
LEU   HG   H  N N 242 
LEU   HD11 H  N N 243 
LEU   HD12 H  N N 244 
LEU   HD13 H  N N 245 
LEU   HD21 H  N N 246 
LEU   HD22 H  N N 247 
LEU   HD23 H  N N 248 
LEU   HXT  H  N N 249 
LYS   N    N  N N 250 
LYS   CA   C  N S 251 
LYS   C    C  N N 252 
LYS   O    O  N N 253 
LYS   CB   C  N N 254 
LYS   CG   C  N N 255 
LYS   CD   C  N N 256 
LYS   CE   C  N N 257 
LYS   NZ   N  N N 258 
LYS   OXT  O  N N 259 
LYS   H    H  N N 260 
LYS   H2   H  N N 261 
LYS   HA   H  N N 262 
LYS   HB2  H  N N 263 
LYS   HB3  H  N N 264 
LYS   HG2  H  N N 265 
LYS   HG3  H  N N 266 
LYS   HD2  H  N N 267 
LYS   HD3  H  N N 268 
LYS   HE2  H  N N 269 
LYS   HE3  H  N N 270 
LYS   HZ1  H  N N 271 
LYS   HZ2  H  N N 272 
LYS   HZ3  H  N N 273 
LYS   HXT  H  N N 274 
MET   N    N  N N 275 
MET   CA   C  N S 276 
MET   C    C  N N 277 
MET   O    O  N N 278 
MET   CB   C  N N 279 
MET   CG   C  N N 280 
MET   SD   S  N N 281 
MET   CE   C  N N 282 
MET   OXT  O  N N 283 
MET   H    H  N N 284 
MET   H2   H  N N 285 
MET   HA   H  N N 286 
MET   HB2  H  N N 287 
MET   HB3  H  N N 288 
MET   HG2  H  N N 289 
MET   HG3  H  N N 290 
MET   HE1  H  N N 291 
MET   HE2  H  N N 292 
MET   HE3  H  N N 293 
MET   HXT  H  N N 294 
PHE   N    N  N N 295 
PHE   CA   C  N S 296 
PHE   C    C  N N 297 
PHE   O    O  N N 298 
PHE   CB   C  N N 299 
PHE   CG   C  Y N 300 
PHE   CD1  C  Y N 301 
PHE   CD2  C  Y N 302 
PHE   CE1  C  Y N 303 
PHE   CE2  C  Y N 304 
PHE   CZ   C  Y N 305 
PHE   OXT  O  N N 306 
PHE   H    H  N N 307 
PHE   H2   H  N N 308 
PHE   HA   H  N N 309 
PHE   HB2  H  N N 310 
PHE   HB3  H  N N 311 
PHE   HD1  H  N N 312 
PHE   HD2  H  N N 313 
PHE   HE1  H  N N 314 
PHE   HE2  H  N N 315 
PHE   HZ   H  N N 316 
PHE   HXT  H  N N 317 
PRO   N    N  N N 318 
PRO   CA   C  N S 319 
PRO   C    C  N N 320 
PRO   O    O  N N 321 
PRO   CB   C  N N 322 
PRO   CG   C  N N 323 
PRO   CD   C  N N 324 
PRO   OXT  O  N N 325 
PRO   H    H  N N 326 
PRO   HA   H  N N 327 
PRO   HB2  H  N N 328 
PRO   HB3  H  N N 329 
PRO   HG2  H  N N 330 
PRO   HG3  H  N N 331 
PRO   HD2  H  N N 332 
PRO   HD3  H  N N 333 
PRO   HXT  H  N N 334 
SER   N    N  N N 335 
SER   CA   C  N S 336 
SER   C    C  N N 337 
SER   O    O  N N 338 
SER   CB   C  N N 339 
SER   OG   O  N N 340 
SER   OXT  O  N N 341 
SER   H    H  N N 342 
SER   H2   H  N N 343 
SER   HA   H  N N 344 
SER   HB2  H  N N 345 
SER   HB3  H  N N 346 
SER   HG   H  N N 347 
SER   HXT  H  N N 348 
THR   N    N  N N 349 
THR   CA   C  N S 350 
THR   C    C  N N 351 
THR   O    O  N N 352 
THR   CB   C  N R 353 
THR   OG1  O  N N 354 
THR   CG2  C  N N 355 
THR   OXT  O  N N 356 
THR   H    H  N N 357 
THR   H2   H  N N 358 
THR   HA   H  N N 359 
THR   HB   H  N N 360 
THR   HG1  H  N N 361 
THR   HG21 H  N N 362 
THR   HG22 H  N N 363 
THR   HG23 H  N N 364 
THR   HXT  H  N N 365 
TRP   N    N  N N 366 
TRP   CA   C  N S 367 
TRP   C    C  N N 368 
TRP   O    O  N N 369 
TRP   CB   C  N N 370 
TRP   CG   C  Y N 371 
TRP   CD1  C  Y N 372 
TRP   CD2  C  Y N 373 
TRP   NE1  N  Y N 374 
TRP   CE2  C  Y N 375 
TRP   CE3  C  Y N 376 
TRP   CZ2  C  Y N 377 
TRP   CZ3  C  Y N 378 
TRP   CH2  C  Y N 379 
TRP   OXT  O  N N 380 
TRP   H    H  N N 381 
TRP   H2   H  N N 382 
TRP   HA   H  N N 383 
TRP   HB2  H  N N 384 
TRP   HB3  H  N N 385 
TRP   HD1  H  N N 386 
TRP   HE1  H  N N 387 
TRP   HE3  H  N N 388 
TRP   HZ2  H  N N 389 
TRP   HZ3  H  N N 390 
TRP   HH2  H  N N 391 
TRP   HXT  H  N N 392 
TYR   N    N  N N 393 
TYR   CA   C  N S 394 
TYR   C    C  N N 395 
TYR   O    O  N N 396 
TYR   CB   C  N N 397 
TYR   CG   C  Y N 398 
TYR   CD1  C  Y N 399 
TYR   CD2  C  Y N 400 
TYR   CE1  C  Y N 401 
TYR   CE2  C  Y N 402 
TYR   CZ   C  Y N 403 
TYR   OH   O  N N 404 
TYR   OXT  O  N N 405 
TYR   H    H  N N 406 
TYR   H2   H  N N 407 
TYR   HA   H  N N 408 
TYR   HB2  H  N N 409 
TYR   HB3  H  N N 410 
TYR   HD1  H  N N 411 
TYR   HD2  H  N N 412 
TYR   HE1  H  N N 413 
TYR   HE2  H  N N 414 
TYR   HH   H  N N 415 
TYR   HXT  H  N N 416 
VAL   N    N  N N 417 
VAL   CA   C  N S 418 
VAL   C    C  N N 419 
VAL   O    O  N N 420 
VAL   CB   C  N N 421 
VAL   CG1  C  N N 422 
VAL   CG2  C  N N 423 
VAL   OXT  O  N N 424 
VAL   H    H  N N 425 
VAL   H2   H  N N 426 
VAL   HA   H  N N 427 
VAL   HB   H  N N 428 
VAL   HG11 H  N N 429 
VAL   HG12 H  N N 430 
VAL   HG13 H  N N 431 
VAL   HG21 H  N N 432 
VAL   HG22 H  N N 433 
VAL   HG23 H  N N 434 
VAL   HXT  H  N N 435 
ZN    ZN   ZN N N 436 
# 
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 
A1BQ7 N   C    sing N N 1   
A1BQ7 O   C    doub N N 2   
A1BQ7 C   C1   sing N N 3   
A1BQ7 C1  C2   sing N N 4   
A1BQ7 C2  C3   sing N N 5   
A1BQ7 C3  C4   sing N N 6   
A1BQ7 C4  N1   sing N N 7   
A1BQ7 N1  C5   sing N N 8   
A1BQ7 C5  O1   doub N N 9   
A1BQ7 C6  C5   sing N N 10  
A1BQ7 C6  C7   doub Y N 11  
A1BQ7 C7  C8   sing Y N 12  
A1BQ7 C8  N2   doub Y N 13  
A1BQ7 N2  C9   sing Y N 14  
A1BQ7 C9  N3   sing Y N 15  
A1BQ7 N3  N4   sing Y N 16  
A1BQ7 N4  C10  doub Y N 17  
A1BQ7 C10 C11  sing Y N 18  
A1BQ7 C11 C6   sing Y N 19  
A1BQ7 C9  C11  doub Y N 20  
A1BQ7 C12 N1   sing N N 21  
A1BQ7 C1  C12  sing N N 22  
A1BQ7 N3  H1   sing N N 23  
A1BQ7 C4  H9   sing N N 24  
A1BQ7 C4  H8   sing N N 25  
A1BQ7 C7  H10  sing N N 26  
A1BQ7 C8  H11  sing N N 27  
A1BQ7 C10 H12  sing N N 28  
A1BQ7 N   H2   sing N N 29  
A1BQ7 N   H3   sing N N 30  
A1BQ7 C1  H    sing N N 31  
A1BQ7 C12 H14  sing N N 32  
A1BQ7 C12 H13  sing N N 33  
A1BQ7 C2  H5   sing N N 34  
A1BQ7 C2  H4   sing N N 35  
A1BQ7 C3  H7   sing N N 36  
A1BQ7 C3  H6   sing N N 37  
ALA   N   CA   sing N N 38  
ALA   N   H    sing N N 39  
ALA   N   H2   sing N N 40  
ALA   CA  C    sing N N 41  
ALA   CA  CB   sing N N 42  
ALA   CA  HA   sing N N 43  
ALA   C   O    doub N N 44  
ALA   C   OXT  sing N N 45  
ALA   CB  HB1  sing N N 46  
ALA   CB  HB2  sing N N 47  
ALA   CB  HB3  sing N N 48  
ALA   OXT HXT  sing N N 49  
ARG   N   CA   sing N N 50  
ARG   N   H    sing N N 51  
ARG   N   H2   sing N N 52  
ARG   CA  C    sing N N 53  
ARG   CA  CB   sing N N 54  
ARG   CA  HA   sing N N 55  
ARG   C   O    doub N N 56  
ARG   C   OXT  sing N N 57  
ARG   CB  CG   sing N N 58  
ARG   CB  HB2  sing N N 59  
ARG   CB  HB3  sing N N 60  
ARG   CG  CD   sing N N 61  
ARG   CG  HG2  sing N N 62  
ARG   CG  HG3  sing N N 63  
ARG   CD  NE   sing N N 64  
ARG   CD  HD2  sing N N 65  
ARG   CD  HD3  sing N N 66  
ARG   NE  CZ   sing N N 67  
ARG   NE  HE   sing N N 68  
ARG   CZ  NH1  sing N N 69  
ARG   CZ  NH2  doub N N 70  
ARG   NH1 HH11 sing N N 71  
ARG   NH1 HH12 sing N N 72  
ARG   NH2 HH21 sing N N 73  
ARG   NH2 HH22 sing N N 74  
ARG   OXT HXT  sing N N 75  
ASN   N   CA   sing N N 76  
ASN   N   H    sing N N 77  
ASN   N   H2   sing N N 78  
ASN   CA  C    sing N N 79  
ASN   CA  CB   sing N N 80  
ASN   CA  HA   sing N N 81  
ASN   C   O    doub N N 82  
ASN   C   OXT  sing N N 83  
ASN   CB  CG   sing N N 84  
ASN   CB  HB2  sing N N 85  
ASN   CB  HB3  sing N N 86  
ASN   CG  OD1  doub N N 87  
ASN   CG  ND2  sing N N 88  
ASN   ND2 HD21 sing N N 89  
ASN   ND2 HD22 sing N N 90  
ASN   OXT HXT  sing N N 91  
ASP   N   CA   sing N N 92  
ASP   N   H    sing N N 93  
ASP   N   H2   sing N N 94  
ASP   CA  C    sing N N 95  
ASP   CA  CB   sing N N 96  
ASP   CA  HA   sing N N 97  
ASP   C   O    doub N N 98  
ASP   C   OXT  sing N N 99  
ASP   CB  CG   sing N N 100 
ASP   CB  HB2  sing N N 101 
ASP   CB  HB3  sing N N 102 
ASP   CG  OD1  doub N N 103 
ASP   CG  OD2  sing N N 104 
ASP   OD2 HD2  sing N N 105 
ASP   OXT HXT  sing N N 106 
CYS   N   CA   sing N N 107 
CYS   N   H    sing N N 108 
CYS   N   H2   sing N N 109 
CYS   CA  C    sing N N 110 
CYS   CA  CB   sing N N 111 
CYS   CA  HA   sing N N 112 
CYS   C   O    doub N N 113 
CYS   C   OXT  sing N N 114 
CYS   CB  SG   sing N N 115 
CYS   CB  HB2  sing N N 116 
CYS   CB  HB3  sing N N 117 
CYS   SG  HG   sing N N 118 
CYS   OXT HXT  sing N N 119 
DMS   S   O    doub N N 120 
DMS   S   C1   sing N N 121 
DMS   S   C2   sing N N 122 
DMS   C1  H11  sing N N 123 
DMS   C1  H12  sing N N 124 
DMS   C1  H13  sing N N 125 
DMS   C2  H21  sing N N 126 
DMS   C2  H22  sing N N 127 
DMS   C2  H23  sing N N 128 
GLN   N   CA   sing N N 129 
GLN   N   H    sing N N 130 
GLN   N   H2   sing N N 131 
GLN   CA  C    sing N N 132 
GLN   CA  CB   sing N N 133 
GLN   CA  HA   sing N N 134 
GLN   C   O    doub N N 135 
GLN   C   OXT  sing N N 136 
GLN   CB  CG   sing N N 137 
GLN   CB  HB2  sing N N 138 
GLN   CB  HB3  sing N N 139 
GLN   CG  CD   sing N N 140 
GLN   CG  HG2  sing N N 141 
GLN   CG  HG3  sing N N 142 
GLN   CD  OE1  doub N N 143 
GLN   CD  NE2  sing N N 144 
GLN   NE2 HE21 sing N N 145 
GLN   NE2 HE22 sing N N 146 
GLN   OXT HXT  sing N N 147 
GLU   N   CA   sing N N 148 
GLU   N   H    sing N N 149 
GLU   N   H2   sing N N 150 
GLU   CA  C    sing N N 151 
GLU   CA  CB   sing N N 152 
GLU   CA  HA   sing N N 153 
GLU   C   O    doub N N 154 
GLU   C   OXT  sing N N 155 
GLU   CB  CG   sing N N 156 
GLU   CB  HB2  sing N N 157 
GLU   CB  HB3  sing N N 158 
GLU   CG  CD   sing N N 159 
GLU   CG  HG2  sing N N 160 
GLU   CG  HG3  sing N N 161 
GLU   CD  OE1  doub N N 162 
GLU   CD  OE2  sing N N 163 
GLU   OE2 HE2  sing N N 164 
GLU   OXT HXT  sing N N 165 
GLY   N   CA   sing N N 166 
GLY   N   H    sing N N 167 
GLY   N   H2   sing N N 168 
GLY   CA  C    sing N N 169 
GLY   CA  HA2  sing N N 170 
GLY   CA  HA3  sing N N 171 
GLY   C   O    doub N N 172 
GLY   C   OXT  sing N N 173 
GLY   OXT HXT  sing N N 174 
HIS   N   CA   sing N N 175 
HIS   N   H    sing N N 176 
HIS   N   H2   sing N N 177 
HIS   CA  C    sing N N 178 
HIS   CA  CB   sing N N 179 
HIS   CA  HA   sing N N 180 
HIS   C   O    doub N N 181 
HIS   C   OXT  sing N N 182 
HIS   CB  CG   sing N N 183 
HIS   CB  HB2  sing N N 184 
HIS   CB  HB3  sing N N 185 
HIS   CG  ND1  sing Y N 186 
HIS   CG  CD2  doub Y N 187 
HIS   ND1 CE1  doub Y N 188 
HIS   ND1 HD1  sing N N 189 
HIS   CD2 NE2  sing Y N 190 
HIS   CD2 HD2  sing N N 191 
HIS   CE1 NE2  sing Y N 192 
HIS   CE1 HE1  sing N N 193 
HIS   NE2 HE2  sing N N 194 
HIS   OXT HXT  sing N N 195 
HOH   O   H1   sing N N 196 
HOH   O   H2   sing N N 197 
ILE   N   CA   sing N N 198 
ILE   N   H    sing N N 199 
ILE   N   H2   sing N N 200 
ILE   CA  C    sing N N 201 
ILE   CA  CB   sing N N 202 
ILE   CA  HA   sing N N 203 
ILE   C   O    doub N N 204 
ILE   C   OXT  sing N N 205 
ILE   CB  CG1  sing N N 206 
ILE   CB  CG2  sing N N 207 
ILE   CB  HB   sing N N 208 
ILE   CG1 CD1  sing N N 209 
ILE   CG1 HG12 sing N N 210 
ILE   CG1 HG13 sing N N 211 
ILE   CG2 HG21 sing N N 212 
ILE   CG2 HG22 sing N N 213 
ILE   CG2 HG23 sing N N 214 
ILE   CD1 HD11 sing N N 215 
ILE   CD1 HD12 sing N N 216 
ILE   CD1 HD13 sing N N 217 
ILE   OXT HXT  sing N N 218 
LEU   N   CA   sing N N 219 
LEU   N   H    sing N N 220 
LEU   N   H2   sing N N 221 
LEU   CA  C    sing N N 222 
LEU   CA  CB   sing N N 223 
LEU   CA  HA   sing N N 224 
LEU   C   O    doub N N 225 
LEU   C   OXT  sing N N 226 
LEU   CB  CG   sing N N 227 
LEU   CB  HB2  sing N N 228 
LEU   CB  HB3  sing N N 229 
LEU   CG  CD1  sing N N 230 
LEU   CG  CD2  sing N N 231 
LEU   CG  HG   sing N N 232 
LEU   CD1 HD11 sing N N 233 
LEU   CD1 HD12 sing N N 234 
LEU   CD1 HD13 sing N N 235 
LEU   CD2 HD21 sing N N 236 
LEU   CD2 HD22 sing N N 237 
LEU   CD2 HD23 sing N N 238 
LEU   OXT HXT  sing N N 239 
LYS   N   CA   sing N N 240 
LYS   N   H    sing N N 241 
LYS   N   H2   sing N N 242 
LYS   CA  C    sing N N 243 
LYS   CA  CB   sing N N 244 
LYS   CA  HA   sing N N 245 
LYS   C   O    doub N N 246 
LYS   C   OXT  sing N N 247 
LYS   CB  CG   sing N N 248 
LYS   CB  HB2  sing N N 249 
LYS   CB  HB3  sing N N 250 
LYS   CG  CD   sing N N 251 
LYS   CG  HG2  sing N N 252 
LYS   CG  HG3  sing N N 253 
LYS   CD  CE   sing N N 254 
LYS   CD  HD2  sing N N 255 
LYS   CD  HD3  sing N N 256 
LYS   CE  NZ   sing N N 257 
LYS   CE  HE2  sing N N 258 
LYS   CE  HE3  sing N N 259 
LYS   NZ  HZ1  sing N N 260 
LYS   NZ  HZ2  sing N N 261 
LYS   NZ  HZ3  sing N N 262 
LYS   OXT HXT  sing N N 263 
MET   N   CA   sing N N 264 
MET   N   H    sing N N 265 
MET   N   H2   sing N N 266 
MET   CA  C    sing N N 267 
MET   CA  CB   sing N N 268 
MET   CA  HA   sing N N 269 
MET   C   O    doub N N 270 
MET   C   OXT  sing N N 271 
MET   CB  CG   sing N N 272 
MET   CB  HB2  sing N N 273 
MET   CB  HB3  sing N N 274 
MET   CG  SD   sing N N 275 
MET   CG  HG2  sing N N 276 
MET   CG  HG3  sing N N 277 
MET   SD  CE   sing N N 278 
MET   CE  HE1  sing N N 279 
MET   CE  HE2  sing N N 280 
MET   CE  HE3  sing N N 281 
MET   OXT HXT  sing N N 282 
PHE   N   CA   sing N N 283 
PHE   N   H    sing N N 284 
PHE   N   H2   sing N N 285 
PHE   CA  C    sing N N 286 
PHE   CA  CB   sing N N 287 
PHE   CA  HA   sing N N 288 
PHE   C   O    doub N N 289 
PHE   C   OXT  sing N N 290 
PHE   CB  CG   sing N N 291 
PHE   CB  HB2  sing N N 292 
PHE   CB  HB3  sing N N 293 
PHE   CG  CD1  doub Y N 294 
PHE   CG  CD2  sing Y N 295 
PHE   CD1 CE1  sing Y N 296 
PHE   CD1 HD1  sing N N 297 
PHE   CD2 CE2  doub Y N 298 
PHE   CD2 HD2  sing N N 299 
PHE   CE1 CZ   doub Y N 300 
PHE   CE1 HE1  sing N N 301 
PHE   CE2 CZ   sing Y N 302 
PHE   CE2 HE2  sing N N 303 
PHE   CZ  HZ   sing N N 304 
PHE   OXT HXT  sing N N 305 
PRO   N   CA   sing N N 306 
PRO   N   CD   sing N N 307 
PRO   N   H    sing N N 308 
PRO   CA  C    sing N N 309 
PRO   CA  CB   sing N N 310 
PRO   CA  HA   sing N N 311 
PRO   C   O    doub N N 312 
PRO   C   OXT  sing N N 313 
PRO   CB  CG   sing N N 314 
PRO   CB  HB2  sing N N 315 
PRO   CB  HB3  sing N N 316 
PRO   CG  CD   sing N N 317 
PRO   CG  HG2  sing N N 318 
PRO   CG  HG3  sing N N 319 
PRO   CD  HD2  sing N N 320 
PRO   CD  HD3  sing N N 321 
PRO   OXT HXT  sing N N 322 
SER   N   CA   sing N N 323 
SER   N   H    sing N N 324 
SER   N   H2   sing N N 325 
SER   CA  C    sing N N 326 
SER   CA  CB   sing N N 327 
SER   CA  HA   sing N N 328 
SER   C   O    doub N N 329 
SER   C   OXT  sing N N 330 
SER   CB  OG   sing N N 331 
SER   CB  HB2  sing N N 332 
SER   CB  HB3  sing N N 333 
SER   OG  HG   sing N N 334 
SER   OXT HXT  sing N N 335 
THR   N   CA   sing N N 336 
THR   N   H    sing N N 337 
THR   N   H2   sing N N 338 
THR   CA  C    sing N N 339 
THR   CA  CB   sing N N 340 
THR   CA  HA   sing N N 341 
THR   C   O    doub N N 342 
THR   C   OXT  sing N N 343 
THR   CB  OG1  sing N N 344 
THR   CB  CG2  sing N N 345 
THR   CB  HB   sing N N 346 
THR   OG1 HG1  sing N N 347 
THR   CG2 HG21 sing N N 348 
THR   CG2 HG22 sing N N 349 
THR   CG2 HG23 sing N N 350 
THR   OXT HXT  sing N N 351 
TRP   N   CA   sing N N 352 
TRP   N   H    sing N N 353 
TRP   N   H2   sing N N 354 
TRP   CA  C    sing N N 355 
TRP   CA  CB   sing N N 356 
TRP   CA  HA   sing N N 357 
TRP   C   O    doub N N 358 
TRP   C   OXT  sing N N 359 
TRP   CB  CG   sing N N 360 
TRP   CB  HB2  sing N N 361 
TRP   CB  HB3  sing N N 362 
TRP   CG  CD1  doub Y N 363 
TRP   CG  CD2  sing Y N 364 
TRP   CD1 NE1  sing Y N 365 
TRP   CD1 HD1  sing N N 366 
TRP   CD2 CE2  doub Y N 367 
TRP   CD2 CE3  sing Y N 368 
TRP   NE1 CE2  sing Y N 369 
TRP   NE1 HE1  sing N N 370 
TRP   CE2 CZ2  sing Y N 371 
TRP   CE3 CZ3  doub Y N 372 
TRP   CE3 HE3  sing N N 373 
TRP   CZ2 CH2  doub Y N 374 
TRP   CZ2 HZ2  sing N N 375 
TRP   CZ3 CH2  sing Y N 376 
TRP   CZ3 HZ3  sing N N 377 
TRP   CH2 HH2  sing N N 378 
TRP   OXT HXT  sing N N 379 
TYR   N   CA   sing N N 380 
TYR   N   H    sing N N 381 
TYR   N   H2   sing N N 382 
TYR   CA  C    sing N N 383 
TYR   CA  CB   sing N N 384 
TYR   CA  HA   sing N N 385 
TYR   C   O    doub N N 386 
TYR   C   OXT  sing N N 387 
TYR   CB  CG   sing N N 388 
TYR   CB  HB2  sing N N 389 
TYR   CB  HB3  sing N N 390 
TYR   CG  CD1  doub Y N 391 
TYR   CG  CD2  sing Y N 392 
TYR   CD1 CE1  sing Y N 393 
TYR   CD1 HD1  sing N N 394 
TYR   CD2 CE2  doub Y N 395 
TYR   CD2 HD2  sing N N 396 
TYR   CE1 CZ   doub Y N 397 
TYR   CE1 HE1  sing N N 398 
TYR   CE2 CZ   sing Y N 399 
TYR   CE2 HE2  sing N N 400 
TYR   CZ  OH   sing N N 401 
TYR   OH  HH   sing N N 402 
TYR   OXT HXT  sing N N 403 
VAL   N   CA   sing N N 404 
VAL   N   H    sing N N 405 
VAL   N   H2   sing N N 406 
VAL   CA  C    sing N N 407 
VAL   CA  CB   sing N N 408 
VAL   CA  HA   sing N N 409 
VAL   C   O    doub N N 410 
VAL   C   OXT  sing N N 411 
VAL   CB  CG1  sing N N 412 
VAL   CB  CG2  sing N N 413 
VAL   CB  HB   sing N N 414 
VAL   CG1 HG11 sing N N 415 
VAL   CG1 HG12 sing N N 416 
VAL   CG1 HG13 sing N N 417 
VAL   CG2 HG21 sing N N 418 
VAL   CG2 HG22 sing N N 419 
VAL   CG2 HG23 sing N N 420 
VAL   OXT HXT  sing N N 421 
# 
_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                    7HZS 
_atom_sites.fract_transf_matrix[1][1]   0.011530 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000936 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017498 
_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]   0.015466 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER   A 1 1   ? 17.674 8.068   24.819 1.00 17.93  ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 18.928 8.192   24.027 1.00 17.83  ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 19.063 6.982   23.102 1.00 16.22  ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 18.317 5.999   23.293 1.00 17.09  ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 20.129 8.284   24.930 1.00 21.31  ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 20.251 7.067   25.631 1.00 22.74  ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 19.990 7.031   22.155 1.00 14.30  ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 20.261 5.925   21.229 1.00 12.77  ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 20.625 6.394   19.833 1.00 11.62  ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 20.355 7.544   19.480 1.00 13.77  ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 21.324 5.566   19.116 1.00 11.46  ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 21.860 5.893   17.778 1.00 10.96  ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 21.775 4.675   16.872 1.00 11.15  ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 21.691 3.544   17.349 1.00 11.83  ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.275 6.400   17.883 1.00 12.51  ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 21.834 4.918   15.584 1.00 10.52  ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.072 3.880   14.547 1.00 10.52  ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 23.540 3.981   14.181 1.00 11.81  ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.017 5.099   13.886 1.00 11.42  ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.190 4.047   13.312 1.00 10.54  ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 19.697 4.263   13.653 1.00 11.67  ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.429 2.860   12.377 1.00 11.60  ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 18.905 4.790   12.443 1.00 11.81  ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.260 2.846   14.197 1.00 11.23  ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 25.684 2.796   13.785 1.00 13.17  ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 25.790 1.990   12.496 1.00 13.52  ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 25.754 0.726   12.541 1.00 13.53  ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 26.548 2.239   14.914 1.00 14.22  ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 26.582 3.149   16.105 1.00 12.89  ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 27.476 4.234   16.179 1.00 13.46  ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 25.797 2.912   17.222 1.00 14.29  ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 27.471 5.121   17.253 1.00 13.85  ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 25.809 3.777   18.319 1.00 14.60  ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 26.635 4.899   18.324 1.00 14.82  ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 26.654 5.746   19.413 1.00 16.86  ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 25.805 2.642   11.361 1.00 12.74  ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 25.874 2.021   10.021 1.00 12.72  ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.127 2.516   9.313  1.00 15.47  ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.377 3.750   9.261  1.00 13.60  ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.601 2.311   9.190  1.00 14.36  ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.242 3.783   9.119  1.00 14.07  ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.722 1.707   7.826  1.00 14.81  ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 27.971 1.599   8.818  1.00 15.80  ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.251 2.011   8.200  1.00 15.67  ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.051 2.904   9.132  1.00 14.15  ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.185 2.587   10.319 1.00 14.69  ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.531 4.046   8.611  1.00 14.96  ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.238 5.052   9.442  1.00 14.53  ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.317 6.225   9.731  1.00 13.74  ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.837 7.362   9.903  1.00 14.12  ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.602 5.495   8.898  1.00 15.34  ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.663 4.413   9.020  1.00 18.53  ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.361 4.314   10.036 1.00 22.68  ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.677 3.583   8.009  1.00 18.49  ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.047 5.941   9.978  1.00 12.39  ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.057 6.979   10.355 1.00 11.73  ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.405 6.651   11.689 1.00 11.65  ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.137 5.465   12.039 1.00 12.23  ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.977 7.094   9.279  1.00 13.44  ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.498 7.472   7.913  1.00 12.52  ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 28.153 8.682   7.712  1.00 14.33  ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.273 6.658   6.802  1.00 15.47  ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.637 9.048   6.467  1.00 15.59  ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.704 7.038   5.540  1.00 16.46  ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 28.357 8.252   5.375  1.00 17.08  ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.818 8.629   4.127  1.00 20.89  ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.083 7.697   12.440 1.00 10.52  ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.268 7.669   13.673 1.00 10.30  ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.023 8.520   13.430 1.00 10.98  ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.195 9.741   13.125 1.00 11.45  ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.084 8.196   14.869 1.00 11.20  ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.324 8.496   16.144 1.00 12.32  ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.243 8.940   17.275 1.00 13.40  ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 26.690 9.963   18.154 1.00 14.44  ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 26.021 9.766   19.283 1.00 15.60  ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 25.741 8.542   19.683 1.00 16.60  ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 25.552 10.797  19.959 1.00 16.71  ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 23.837 7.908   13.497 1.00 9.95   ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.530 8.606   13.241 1.00 9.97   ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 21.866 8.814   14.581 1.00 10.99  ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 21.578 7.845   15.274 1.00 11.50  ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.634 7.817   12.278 1.00 10.77  ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.424 8.682   11.954 1.00 10.98  ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.355 7.367   11.017 1.00 12.41  ? 17  VAL   A CG2 1 
ATOM   85   N  N   A VAL   A 1 12  ? 21.630 10.079  14.941 0.36 9.30   ? 18  VAL   A N   1 
ATOM   86   N  N   B VAL   A 1 12  ? 21.633 10.079  14.947 0.36 10.89  ? 18  VAL   A N   1 
ATOM   87   C  CA  A VAL   A 1 12  ? 21.000 10.442  16.244 0.36 10.01  ? 18  VAL   A CA  1 
ATOM   88   C  CA  B VAL   A 1 12  ? 21.105 10.479  16.288 0.36 12.94  ? 18  VAL   A CA  1 
ATOM   89   C  C   A VAL   A 1 12  ? 19.853 11.412  16.003 0.36 10.62  ? 18  VAL   A C   1 
ATOM   90   C  C   B VAL   A 1 12  ? 19.969 11.480  16.080 0.36 12.16  ? 18  VAL   A C   1 
ATOM   91   O  O   A VAL   A 1 12  ? 19.669 11.974  14.871 0.36 10.71  ? 18  VAL   A O   1 
ATOM   92   O  O   B VAL   A 1 12  ? 19.934 12.157  15.026 0.36 12.67  ? 18  VAL   A O   1 
ATOM   93   C  CB  A VAL   A 1 12  ? 22.002 11.068  17.235 0.36 9.29   ? 18  VAL   A CB  1 
ATOM   94   C  CB  B VAL   A 1 12  ? 22.211 11.118  17.151 0.36 14.73  ? 18  VAL   A CB  1 
ATOM   95   C  CG1 A VAL   A 1 12  ? 22.936 10.012  17.789 0.36 9.29   ? 18  VAL   A CG1 1 
ATOM   96   C  CG1 B VAL   A 1 12  ? 21.848 11.194  18.619 0.36 15.69  ? 18  VAL   A CG1 1 
ATOM   97   C  CG2 A VAL   A 1 12  ? 22.763 12.266  16.615 0.36 8.63   ? 18  VAL   A CG2 1 
ATOM   98   C  CG2 B VAL   A 1 12  ? 23.541 10.433  16.974 0.36 16.86  ? 18  VAL   A CG2 1 
ATOM   99   N  N   . ASN   A 1 13  ? 19.061 11.585  17.051 1.00 11.46  ? 19  ASN   A N   1 
ATOM   100  C  CA  . ASN   A 1 13  ? 18.086 12.694  17.069 1.00 11.57  ? 19  ASN   A CA  1 
ATOM   101  C  C   . ASN   A 1 13  ? 18.896 14.003  17.077 1.00 10.77  ? 19  ASN   A C   1 
ATOM   102  O  O   . ASN   A 1 13  ? 19.825 14.190  17.875 1.00 11.99  ? 19  ASN   A O   1 
ATOM   103  C  CB  . ASN   A 1 13  ? 17.247 12.659  18.337 1.00 12.21  ? 19  ASN   A CB  1 
ATOM   104  C  CG  . ASN   A 1 13  ? 16.368 11.418  18.431 1.00 11.82  ? 19  ASN   A CG  1 
ATOM   105  O  OD1 . ASN   A 1 13  ? 16.794 10.410  19.037 1.00 12.94  ? 19  ASN   A OD1 1 
ATOM   106  N  ND2 . ASN   A 1 13  ? 15.202 11.444  17.824 1.00 12.58  ? 19  ASN   A ND2 1 
ATOM   107  N  N   . ARG   A 1 14  ? 18.527 14.921  16.163 1.00 12.09  ? 20  ARG   A N   1 
ATOM   108  C  CA  . ARG   A 1 14  ? 19.263 16.235  16.101 1.00 12.41  ? 20  ARG   A CA  1 
ATOM   109  C  C   . ARG   A 1 14  ? 19.208 16.899  17.466 1.00 13.45  ? 20  ARG   A C   1 
ATOM   110  O  O   . ARG   A 1 14  ? 20.238 17.427  17.912 1.00 14.27  ? 20  ARG   A O   1 
ATOM   111  C  CB  . ARG   A 1 14  ? 18.644 17.127  15.040 1.00 13.01  ? 20  ARG   A CB  1 
ATOM   112  C  CG  . ARG   A 1 14  ? 19.424 18.416  14.761 1.00 13.84  ? 20  ARG   A CG  1 
ATOM   113  C  CD  . ARG   A 1 14  ? 18.677 19.299  13.785 1.00 15.63  ? 20  ARG   A CD  1 
ATOM   114  N  NE  . ARG   A 1 14  ? 19.410 20.508  13.362 1.00 16.43  ? 20  ARG   A NE  1 
ATOM   115  C  CZ  . ARG   A 1 14  ? 19.405 21.665  14.002 1.00 20.06  ? 20  ARG   A CZ  1 
ATOM   116  N  NH1 . ARG   A 1 14  ? 18.846 21.769  15.190 1.00 19.57  ? 20  ARG   A NH1 1 
ATOM   117  N  NH2 . ARG   A 1 14  ? 20.010 22.716  13.448 1.00 20.59  ? 20  ARG   A NH2 1 
ATOM   118  N  N   . HIS   A 1 15  ? 18.082 16.779  18.175 1.00 13.79  ? 21  HIS   A N   1 
ATOM   119  C  CA  . HIS   A 1 15  ? 17.895 17.508  19.448 1.00 15.68  ? 21  HIS   A CA  1 
ATOM   120  C  C   . HIS   A 1 15  ? 18.757 16.922  20.563 1.00 16.77  ? 21  HIS   A C   1 
ATOM   121  O  O   . HIS   A 1 15  ? 18.904 17.552  21.650 1.00 19.52  ? 21  HIS   A O   1 
ATOM   122  C  CB  . HIS   A 1 15  ? 16.420 17.631  19.844 1.00 17.75  ? 21  HIS   A CB  1 
ATOM   123  C  CG  . HIS   A 1 15  ? 15.756 16.384  20.336 1.00 16.50  ? 21  HIS   A CG  1 
ATOM   124  N  ND1 . HIS   A 1 15  ? 15.064 15.544  19.480 1.00 16.22  ? 21  HIS   A ND1 1 
ATOM   125  C  CD2 . HIS   A 1 15  ? 15.530 15.930  21.593 1.00 17.96  ? 21  HIS   A CD2 1 
ATOM   126  C  CE1 . HIS   A 1 15  ? 14.488 14.575  20.193 1.00 16.58  ? 21  HIS   A CE1 1 
ATOM   127  N  NE2 . HIS   A 1 15  ? 14.769 14.790  21.480 1.00 16.38  ? 21  HIS   A NE2 1 
ATOM   128  N  N   . LEU   A 1 16  ? 19.292 15.699  20.412 1.00 15.55  ? 22  LEU   A N   1 
ATOM   129  C  CA  . LEU   A 1 16  ? 20.194 15.028  21.381 1.00 14.66  ? 22  LEU   A CA  1 
ATOM   130  C  C   . LEU   A 1 16  ? 21.653 14.998  20.908 1.00 15.14  ? 22  LEU   A C   1 
ATOM   131  O  O   . LEU   A 1 16  ? 22.485 14.371  21.557 1.00 16.59  ? 22  LEU   A O   1 
ATOM   132  C  CB  . LEU   A 1 16  ? 19.649 13.624  21.686 1.00 15.65  ? 22  LEU   A CB  1 
ATOM   133  C  CG  . LEU   A 1 16  ? 18.236 13.575  22.282 1.00 15.87  ? 22  LEU   A CG  1 
ATOM   134  C  CD1 . LEU   A 1 16  ? 17.827 12.123  22.577 1.00 16.57  ? 22  LEU   A CD1 1 
ATOM   135  C  CD2 . LEU   A 1 16  ? 18.174 14.395  23.572 1.00 18.61  ? 22  LEU   A CD2 1 
ATOM   136  N  N   . ALA   A 1 17  ? 21.993 15.608  19.758 1.00 15.83  ? 23  ALA   A N   1 
ATOM   137  C  CA  . ALA   A 1 17  ? 23.368 15.570  19.243 1.00 14.74  ? 23  ALA   A CA  1 
ATOM   138  C  C   . ALA   A 1 17  ? 24.348 16.213  20.243 1.00 16.91  ? 23  ALA   A C   1 
ATOM   139  O  O   . ALA   A 1 17  ? 24.016 17.254  20.863 1.00 18.41  ? 23  ALA   A O   1 
ATOM   140  C  CB  . ALA   A 1 17  ? 23.452 16.215  17.873 1.00 14.37  ? 23  ALA   A CB  1 
ATOM   141  N  N   . THR   A 1 18  ? 25.498 15.594  20.403 1.00 15.69  ? 24  THR   A N   1 
ATOM   142  C  CA  . THR   A 1 18  ? 26.579 16.096  21.308 1.00 15.78  ? 24  THR   A CA  1 
ATOM   143  C  C   . THR   A 1 18  ? 27.476 17.100  20.585 1.00 16.84  ? 24  THR   A C   1 
ATOM   144  O  O   . THR   A 1 18  ? 27.446 17.220  19.301 1.00 14.93  ? 24  THR   A O   1 
ATOM   145  C  CB  . THR   A 1 18  ? 27.446 14.931  21.796 1.00 17.67  ? 24  THR   A CB  1 
ATOM   146  O  OG1 . THR   A 1 18  ? 28.186 14.408  20.689 1.00 17.53  ? 24  THR   A OG1 1 
ATOM   147  C  CG2 . THR   A 1 18  ? 26.665 13.815  22.455 1.00 18.26  ? 24  THR   A CG2 1 
ATOM   148  N  N   . HIS   A 1 19  ? 28.347 17.798  21.335 1.00 17.31  ? 25  HIS   A N   1 
ATOM   149  C  CA  . HIS   A 1 19  ? 29.389 18.636  20.711 1.00 18.82  ? 25  HIS   A CA  1 
ATOM   150  C  C   . HIS   A 1 19  ? 30.249 17.807  19.741 1.00 16.90  ? 25  HIS   A C   1 
ATOM   151  O  O   . HIS   A 1 19  ? 30.583 18.291  18.646 1.00 16.62  ? 25  HIS   A O   1 
ATOM   152  C  CB  . HIS   A 1 19  ? 30.290 19.319  21.775 1.00 19.41  ? 25  HIS   A CB  1 
ATOM   153  C  CG  . HIS   A 1 19  ? 31.490 20.027  21.190 1.00 25.07  ? 25  HIS   A CG  1 
ATOM   154  N  ND1 . HIS   A 1 19  ? 31.383 21.224  20.490 1.00 34.34  ? 25  HIS   A ND1 1 
ATOM   155  C  CD2 . HIS   A 1 19  ? 32.792 19.654  21.056 1.00 36.07  ? 25  HIS   A CD2 1 
ATOM   156  C  CE1 . HIS   A 1 19  ? 32.564 21.609  20.050 1.00 31.56  ? 25  HIS   A CE1 1 
ATOM   157  N  NE2 . HIS   A 1 19  ? 33.456 20.652  20.350 1.00 40.70  ? 25  HIS   A NE2 1 
ATOM   158  N  N   . ASN   A 1 20  ? 30.646 16.586  20.118 1.00 17.02  ? 26  ASN   A N   1 
ATOM   159  C  CA  . ASN   A 1 20  ? 31.466 15.765  19.218 1.00 16.65  ? 26  ASN   A CA  1 
ATOM   160  C  C   . ASN   A 1 20  ? 30.706 15.483  17.893 1.00 14.24  ? 26  ASN   A C   1 
ATOM   161  O  O   . ASN   A 1 20  ? 31.314 15.519  16.825 1.00 15.52  ? 26  ASN   A O   1 
ATOM   162  C  CB  . ASN   A 1 20  ? 31.903 14.440  19.851 1.00 18.43  ? 26  ASN   A CB  1 
ATOM   163  C  CG  . ASN   A 1 20  ? 32.889 13.741  18.954 1.00 23.85  ? 26  ASN   A CG  1 
ATOM   164  O  OD1 . ASN   A 1 20  ? 34.027 14.190  18.820 1.00 30.47  ? 26  ASN   A OD1 1 
ATOM   165  N  ND2 . ASN   A 1 20  ? 32.439 12.704  18.258 1.00 26.47  ? 26  ASN   A ND2 1 
ATOM   166  N  N   . ASP   A 1 21  ? 29.396 15.234  17.983 1.00 14.18  ? 27  ASP   A N   1 
ATOM   167  C  CA  . ASP   A 1 21  ? 28.571 15.078  16.753 1.00 13.69  ? 27  ASP   A CA  1 
ATOM   168  C  C   . ASP   A 1 21  ? 28.645 16.327  15.844 1.00 12.81  ? 27  ASP   A C   1 
ATOM   169  O  O   . ASP   A 1 21  ? 28.870 16.212  14.626 1.00 12.74  ? 27  ASP   A O   1 
ATOM   170  C  CB  . ASP   A 1 21  ? 27.118 14.777  17.096 1.00 13.34  ? 27  ASP   A CB  1 
ATOM   171  C  CG  . ASP   A 1 21  ? 26.873 13.404  17.697 1.00 14.06  ? 27  ASP   A CG  1 
ATOM   172  O  OD1 . ASP   A 1 21  ? 27.540 12.441  17.263 1.00 15.44  ? 27  ASP   A OD1 1 
ATOM   173  O  OD2 . ASP   A 1 21  ? 26.038 13.331  18.624 1.00 14.75  ? 27  ASP   A OD2 1 
ATOM   174  N  N   . TRP   A 1 22  ? 28.425 17.515  16.412 1.00 13.73  ? 28  TRP   A N   1 
ATOM   175  C  CA  . TRP   A 1 22  ? 28.491 18.789  15.646 1.00 13.04  ? 28  TRP   A CA  1 
ATOM   176  C  C   . TRP   A 1 22  ? 29.904 19.039  15.091 1.00 13.96  ? 28  TRP   A C   1 
ATOM   177  O  O   . TRP   A 1 22  ? 29.989 19.583  14.002 1.00 13.98  ? 28  TRP   A O   1 
ATOM   178  C  CB  . TRP   A 1 22  ? 28.022 19.934  16.569 1.00 13.59  ? 28  TRP   A CB  1 
ATOM   179  C  CG  . TRP   A 1 22  ? 26.539 20.025  16.692 1.00 12.31  ? 28  TRP   A CG  1 
ATOM   180  C  CD1 . TRP   A 1 22  ? 25.776 19.744  17.786 1.00 14.03  ? 28  TRP   A CD1 1 
ATOM   181  C  CD2 . TRP   A 1 22  ? 25.589 20.464  15.697 1.00 12.80  ? 28  TRP   A CD2 1 
ATOM   182  N  NE1 . TRP   A 1 22  ? 24.462 19.925  17.530 1.00 13.36  ? 28  TRP   A NE1 1 
ATOM   183  C  CE2 . TRP   A 1 22  ? 24.300 20.389  16.249 1.00 13.54  ? 28  TRP   A CE2 1 
ATOM   184  C  CE3 . TRP   A 1 22  ? 25.720 20.885  14.372 1.00 15.39  ? 28  TRP   A CE3 1 
ATOM   185  C  CZ2 . TRP   A 1 22  ? 23.147 20.756  15.545 1.00 15.14  ? 28  TRP   A CZ2 1 
ATOM   186  C  CZ3 . TRP   A 1 22  ? 24.585 21.208  13.668 1.00 16.35  ? 28  TRP   A CZ3 1 
ATOM   187  C  CH2 . TRP   A 1 22  ? 23.328 21.209  14.258 1.00 16.10  ? 28  TRP   A CH2 1 
ATOM   188  N  N   . ALA   A 1 23  ? 30.959 18.608  15.791 1.00 13.13  ? 29  ALA   A N   1 
ATOM   189  C  CA  . ALA   A 1 23  ? 32.349 18.816  15.324 1.00 14.50  ? 29  ALA   A CA  1 
ATOM   190  C  C   . ALA   A 1 23  ? 32.767 17.805  14.252 1.00 15.27  ? 29  ALA   A C   1 
ATOM   191  O  O   . ALA   A 1 23  ? 33.788 17.961  13.598 1.00 15.30  ? 29  ALA   A O   1 
ATOM   192  C  CB  . ALA   A 1 23  ? 33.277 18.825  16.512 1.00 16.96  ? 29  ALA   A CB  1 
ATOM   193  N  N   . ASN   A 1 24  ? 31.934 16.773  14.043 1.00 14.72  ? 30  ASN   A N   1 
ATOM   194  C  CA  . ASN   A 1 24  ? 32.217 15.684  13.077 1.00 15.27  ? 30  ASN   A CA  1 
ATOM   195  C  C   . ASN   A 1 24  ? 30.984 15.530  12.202 1.00 14.43  ? 30  ASN   A C   1 
ATOM   196  O  O   . ASN   A 1 24  ? 30.608 14.365  11.872 1.00 14.44  ? 30  ASN   A O   1 
ATOM   197  C  CB  . ASN   A 1 24  ? 32.669 14.378  13.755 1.00 16.35  ? 30  ASN   A CB  1 
ATOM   198  C  CG  . ASN   A 1 24  ? 34.000 14.577  14.453 1.00 16.44  ? 30  ASN   A CG  1 
ATOM   199  O  OD1 . ASN   A 1 24  ? 35.012 14.521  13.765 1.00 20.96  ? 30  ASN   A OD1 1 
ATOM   200  N  ND2 . ASN   A 1 24  ? 33.972 14.881  15.750 1.00 17.81  ? 30  ASN   A ND2 1 
ATOM   201  N  N   . LEU   A 1 25  ? 30.361 16.620  11.793 1.00 13.88  ? 31  LEU   A N   1 
ATOM   202  C  CA  . LEU   A 1 25  ? 29.040 16.591  11.161 1.00 12.58  ? 31  LEU   A CA  1 
ATOM   203  C  C   . LEU   A 1 25  ? 29.111 16.105  9.729  1.00 13.31  ? 31  LEU   A C   1 
ATOM   204  O  O   . LEU   A 1 25  ? 29.982 16.589  8.959  1.00 14.45  ? 31  LEU   A O   1 
ATOM   205  C  CB  . LEU   A 1 25  ? 28.465 18.011  11.199 1.00 13.24  ? 31  LEU   A CB  1 
ATOM   206  C  CG  . LEU   A 1 25  ? 27.066 18.173  10.622 1.00 14.45  ? 31  LEU   A CG  1 
ATOM   207  C  CD1 . LEU   A 1 25  ? 26.019 17.397  11.406 1.00 14.12  ? 31  LEU   A CD1 1 
ATOM   208  C  CD2 . LEU   A 1 25  ? 26.670 19.648  10.561 1.00 15.83  ? 31  LEU   A CD2 1 
ATOM   209  N  N   . VAL   A 1 26  ? 28.175 15.230  9.324  1.00 11.91  ? 32  VAL   A N   1 
ATOM   210  C  CA  . VAL   A 1 26  ? 27.980 14.814  7.910  1.00 12.70  ? 32  VAL   A CA  1 
ATOM   211  C  C   . VAL   A 1 26  ? 26.765 15.567  7.354  1.00 12.46  ? 32  VAL   A C   1 
ATOM   212  O  O   . VAL   A 1 26  ? 26.842 16.069  6.207  1.00 14.88  ? 32  VAL   A O   1 
ATOM   213  C  CB  . VAL   A 1 26  ? 27.878 13.277  7.806  1.00 12.53  ? 32  VAL   A CB  1 
ATOM   214  C  CG1 . VAL   A 1 26  ? 27.543 12.848  6.381  1.00 13.61  ? 32  VAL   A CG1 1 
ATOM   215  C  CG2 . VAL   A 1 26  ? 29.148 12.637  8.358  1.00 13.30  ? 32  VAL   A CG2 1 
ATOM   216  N  N   . TRP   A 1 27  ? 25.615 15.533  8.066  1.00 12.83  ? 33  TRP   A N   1 
ATOM   217  C  CA  . TRP   A 1 27  ? 24.313 16.026  7.547  1.00 12.66  ? 33  TRP   A CA  1 
ATOM   218  C  C   . TRP   A 1 27  ? 23.365 16.246  8.708  1.00 13.79  ? 33  TRP   A C   1 
ATOM   219  O  O   . TRP   A 1 27  ? 23.427 15.476  9.682  1.00 12.99  ? 33  TRP   A O   1 
ATOM   220  C  CB  . TRP   A 1 27  ? 23.737 15.029  6.539  1.00 14.15  ? 33  TRP   A CB  1 
ATOM   221  C  CG  . TRP   A 1 27  ? 22.340 15.285  6.084  1.00 15.34  ? 33  TRP   A CG  1 
ATOM   222  C  CD1 . TRP   A 1 27  ? 21.946 16.102  5.062  1.00 17.55  ? 33  TRP   A CD1 1 
ATOM   223  C  CD2 . TRP   A 1 27  ? 21.140 14.671  6.585  1.00 15.14  ? 33  TRP   A CD2 1 
ATOM   224  N  NE1 . TRP   A 1 27  ? 20.580 16.060  4.942  1.00 20.82  ? 33  TRP   A NE1 1 
ATOM   225  C  CE2 . TRP   A 1 27  ? 20.058 15.177  5.846  1.00 17.58  ? 33  TRP   A CE2 1 
ATOM   226  C  CE3 . TRP   A 1 27  ? 20.869 13.744  7.590  1.00 15.82  ? 33  TRP   A CE3 1 
ATOM   227  C  CZ2 . TRP   A 1 27  ? 18.740 14.756  6.068  1.00 18.88  ? 33  TRP   A CZ2 1 
ATOM   228  C  CZ3 . TRP   A 1 27  ? 19.576 13.327  7.807  1.00 16.34  ? 33  TRP   A CZ3 1 
ATOM   229  C  CH2 . TRP   A 1 27  ? 18.523 13.839  7.067  1.00 17.83  ? 33  TRP   A CH2 1 
ATOM   230  N  N   . GLU   A 1 28  ? 22.563 17.314  8.670  1.00 14.23  ? 34  GLU   A N   1 
ATOM   231  C  CA  . GLU   A 1 28  ? 21.545 17.514  9.704  1.00 14.21  ? 34  GLU   A CA  1 
ATOM   232  C  C   . GLU   A 1 28  ? 20.320 18.155  9.072  1.00 16.20  ? 34  GLU   A C   1 
ATOM   233  O  O   . GLU   A 1 28  ? 20.448 18.927  8.091  1.00 15.96  ? 34  GLU   A O   1 
ATOM   234  C  CB  . GLU   A 1 28  ? 22.094 18.342  10.838 1.00 14.89  ? 34  GLU   A CB  1 
ATOM   235  C  CG  . GLU   A 1 28  ? 22.653 19.711  10.443 1.00 16.08  ? 34  GLU   A CG  1 
ATOM   236  C  CD  . GLU   A 1 28  ? 21.662 20.848  10.235 1.00 17.98  ? 34  GLU   A CD  1 
ATOM   237  O  OE1 . GLU   A 1 28  ? 22.012 21.824  9.477  1.00 19.46  ? 34  GLU   A OE1 1 
ATOM   238  O  OE2 . GLU   A 1 28  ? 20.564 20.812  10.813 1.00 15.89  ? 34  GLU   A OE2 1 
ATOM   239  N  N   . ASP   A 1 29  ? 19.147 17.821  9.587  1.00 14.35  ? 35  ASP   A N   1 
ATOM   240  C  CA  . ASP   A 1 29  ? 17.857 18.352  9.081  1.00 14.74  ? 35  ASP   A CA  1 
ATOM   241  C  C   . ASP   A 1 29  ? 16.925 18.527  10.269 1.00 15.32  ? 35  ASP   A C   1 
ATOM   242  O  O   . ASP   A 1 29  ? 16.400 17.539  10.826 1.00 14.84  ? 35  ASP   A O   1 
ATOM   243  C  CB  . ASP   A 1 29  ? 17.308 17.479  7.957  1.00 15.56  ? 35  ASP   A CB  1 
ATOM   244  C  CG  . ASP   A 1 29  ? 16.039 17.988  7.292  1.00 16.23  ? 35  ASP   A CG  1 
ATOM   245  O  OD1 . ASP   A 1 29  ? 15.226 18.571  8.027  1.00 21.20  ? 35  ASP   A OD1 1 
ATOM   246  O  OD2 . ASP   A 1 29  ? 15.863 17.686  6.106  1.00 22.76  ? 35  ASP   A OD2 1 
ATOM   247  N  N   . SER   A 1 30  ? 16.717 19.781  10.671 0.72 15.71  ? 36  SER   A N   1 
ATOM   248  C  CA  . SER   A 1 30  ? 15.837 20.154  11.802 0.72 16.88  ? 36  SER   A CA  1 
ATOM   249  C  C   . SER   A 1 30  ? 14.398 19.687  11.518 0.72 16.84  ? 36  SER   A C   1 
ATOM   250  O  O   . SER   A 1 30  ? 13.786 19.086  12.441 0.72 19.05  ? 36  SER   A O   1 
ATOM   251  C  CB  . SER   A 1 30  ? 15.937 21.649  12.091 0.72 18.75  ? 36  SER   A CB  1 
ATOM   252  O  OG  . SER   A 1 30  ? 15.035 22.027  13.117 0.72 19.96  ? 36  SER   A OG  1 
ATOM   253  N  N   . SER   A 1 31  ? 13.904 19.859  10.289 1.00 17.94  ? 37  SER   A N   1 
ATOM   254  C  CA  . SER   A 1 31  ? 12.529 19.443  9.893  1.00 18.52  ? 37  SER   A CA  1 
ATOM   255  C  C   . SER   A 1 31  ? 12.279 17.946  10.118 1.00 19.26  ? 37  SER   A C   1 
ATOM   256  O  O   . SER   A 1 31  ? 11.126 17.582  10.368 1.00 20.65  ? 37  SER   A O   1 
ATOM   257  C  CB  . SER   A 1 31  ? 12.185 19.841  8.470  1.00 19.54  ? 37  SER   A CB  1 
ATOM   258  O  OG  . SER   A 1 31  ? 12.714 18.983  7.483  1.00 23.31  ? 37  SER   A OG  1 
ATOM   259  N  N   . ARG   A 1 32  ? 13.326 17.116  10.149 1.00 15.51  ? 38  ARG   A N   1 
ATOM   260  C  CA  . ARG   A 1 32  ? 13.229 15.634  10.315 1.00 14.95  ? 38  ARG   A CA  1 
ATOM   261  C  C   . ARG   A 1 32  ? 13.691 15.213  11.718 1.00 12.90  ? 38  ARG   A C   1 
ATOM   262  O  O   . ARG   A 1 32  ? 13.578 13.968  12.009 1.00 13.42  ? 38  ARG   A O   1 
ATOM   263  C  CB  . ARG   A 1 32  ? 14.073 14.956  9.232  1.00 14.97  ? 38  ARG   A CB  1 
ATOM   264  C  CG  . ARG   A 1 32  ? 13.501 15.040  7.828  1.00 15.45  ? 38  ARG   A CG  1 
ATOM   265  C  CD  . ARG   A 1 32  ? 14.401 14.427  6.803  1.00 16.79  ? 38  ARG   A CD  1 
ATOM   266  N  NE  . ARG   A 1 32  ? 14.339 12.963  6.900  1.00 14.02  ? 38  ARG   A NE  1 
ATOM   267  C  CZ  . ARG   A 1 32  ? 14.482 12.134  5.892  1.00 15.98  ? 38  ARG   A CZ  1 
ATOM   268  N  NH1 . ARG   A 1 32  ? 14.719 12.565  4.659  1.00 17.21  ? 38  ARG   A NH1 1 
ATOM   269  N  NH2 . ARG   A 1 32  ? 14.378 10.825  6.076  1.00 15.00  ? 38  ARG   A NH2 1 
ATOM   270  N  N   . ASP   A 1 33  ? 14.238 16.111  12.529 1.00 12.93  ? 39  ASP   A N   1 
ATOM   271  C  CA  . ASP   A 1 33  ? 14.885 15.803  13.821 1.00 12.71  ? 39  ASP   A CA  1 
ATOM   272  C  C   . ASP   A 1 33  ? 16.038 14.794  13.635 1.00 12.92  ? 39  ASP   A C   1 
ATOM   273  O  O   . ASP   A 1 33  ? 16.260 13.945  14.561 1.00 13.26  ? 39  ASP   A O   1 
ATOM   274  C  CB  . ASP   A 1 33  ? 13.872 15.317  14.860 1.00 13.84  ? 39  ASP   A CB  1 
ATOM   275  C  CG  . ASP   A 1 33  ? 14.486 15.088  16.222 1.00 13.82  ? 39  ASP   A CG  1 
ATOM   276  O  OD1 . ASP   A 1 33  ? 15.346 15.879  16.711 1.00 14.64  ? 39  ASP   A OD1 1 
ATOM   277  O  OD2 . ASP   A 1 33  ? 14.113 14.044  16.863 1.00 15.82  ? 39  ASP   A OD2 1 
ATOM   278  N  N   . LEU   A 1 34  ? 16.851 14.917  12.587 1.00 12.21  ? 40  LEU   A N   1 
ATOM   279  C  CA  . LEU   A 1 34  ? 17.950 13.946  12.339 1.00 11.29  ? 40  LEU   A CA  1 
ATOM   280  C  C   . LEU   A 1 34  ? 19.298 14.668  12.250 1.00 11.57  ? 40  LEU   A C   1 
ATOM   281  O  O   . LEU   A 1 34  ? 19.358 15.797  11.656 1.00 12.58  ? 40  LEU   A O   1 
ATOM   282  C  CB  . LEU   A 1 34  ? 17.678 13.163  11.065 1.00 11.30  ? 40  LEU   A CB  1 
ATOM   283  C  CG  . LEU   A 1 34  ? 16.631 12.034  11.116 1.00 12.86  ? 40  LEU   A CG  1 
ATOM   284  C  CD1 . LEU   A 1 34  ? 16.548 11.355  9.774  1.00 13.32  ? 40  LEU   A CD1 1 
ATOM   285  C  CD2 . LEU   A 1 34  ? 16.907 11.008  12.246 1.00 12.16  ? 40  LEU   A CD2 1 
ATOM   286  N  N   . LEU   A 1 35  ? 20.348 14.028  12.745 1.00 11.44  ? 41  LEU   A N   1 
ATOM   287  C  CA  . LEU   A 1 35  ? 21.722 14.468  12.539 1.00 10.50  ? 41  LEU   A CA  1 
ATOM   288  C  C   . LEU   A 1 35  ? 22.587 13.236  12.370 1.00 10.66  ? 41  LEU   A C   1 
ATOM   289  O  O   . LEU   A 1 35  ? 22.363 12.204  13.086 1.00 10.71  ? 41  LEU   A O   1 
ATOM   290  C  CB  . LEU   A 1 35  ? 22.164 15.329  13.737 1.00 11.06  ? 41  LEU   A CB  1 
ATOM   291  C  CG  . LEU   A 1 35  ? 23.585 15.903  13.622 1.00 11.06  ? 41  LEU   A CG  1 
ATOM   292  C  CD1 . LEU   A 1 35  ? 23.687 17.289  14.281 1.00 12.42  ? 41  LEU   A CD1 1 
ATOM   293  C  CD2 . LEU   A 1 35  ? 24.619 14.999  14.249 1.00 11.46  ? 41  LEU   A CD2 1 
ATOM   294  N  N   . VAL   A 1 36  ? 23.535 13.312  11.448 1.00 10.54  ? 42  VAL   A N   1 
ATOM   295  C  CA  . VAL   A 1 36  ? 24.498 12.215  11.181 1.00 10.25  ? 42  VAL   A CA  1 
ATOM   296  C  C   . VAL   A 1 36  ? 25.903 12.751  11.350 1.00 10.95  ? 42  VAL   A C   1 
ATOM   297  O  O   . VAL   A 1 36  ? 26.234 13.815  10.765 1.00 12.04  ? 42  VAL   A O   1 
ATOM   298  C  CB  . VAL   A 1 36  ? 24.268 11.604  9.785  1.00 10.28  ? 42  VAL   A CB  1 
ATOM   299  C  CG1 . VAL   A 1 36  ? 25.286 10.512  9.526  1.00 12.21  ? 42  VAL   A CG1 1 
ATOM   300  C  CG2 . VAL   A 1 36  ? 22.847 11.092  9.629  1.00 11.31  ? 42  VAL   A CG2 1 
ATOM   301  N  N   . SER   A 1 37  ? 26.703 12.046  12.133 1.00 11.32  ? 43  SER   A N   1 
ATOM   302  C  CA  . SER   A 1 37  ? 28.134 12.375  12.328 1.00 11.60  ? 43  SER   A CA  1 
ATOM   303  C  C   . SER   A 1 37  ? 28.993 11.189  11.896 1.00 11.97  ? 43  SER   A C   1 
ATOM   304  O  O   . SER   A 1 37  ? 28.489 10.065  11.623 1.00 12.65  ? 43  SER   A O   1 
ATOM   305  C  CB  . SER   A 1 37  ? 28.412 12.729  13.775 1.00 12.52  ? 43  SER   A CB  1 
ATOM   306  O  OG  . SER   A 1 37  ? 28.087 11.666  14.664 1.00 13.36  ? 43  SER   A OG  1 
ATOM   307  N  N   . SER   A 1 38  ? 30.274 11.461  11.664 1.00 13.68  ? 44  SER   A N   1 
ATOM   308  C  CA  . SER   A 1 38  ? 31.251 10.436  11.245 1.00 14.67  ? 44  SER   A CA  1 
ATOM   309  C  C   . SER   A 1 38  ? 31.857 9.700   12.448 1.00 15.54  ? 44  SER   A C   1 
ATOM   310  O  O   . SER   A 1 38  ? 32.002 10.284  13.542 1.00 17.96  ? 44  SER   A O   1 
ATOM   311  C  CB  . SER   A 1 38  ? 32.303 11.048  10.354 1.00 16.12  ? 44  SER   A CB  1 
ATOM   312  O  OG  . SER   A 1 38  ? 32.978 12.068  11.080 1.00 18.44  ? 44  SER   A OG  1 
ATOM   313  N  N   . THR   A 1 39  ? 32.175 8.419   12.274 1.00 16.66  ? 45  THR   A N   1 
ATOM   314  C  CA  . THR   A 1 39  ? 32.758 7.553   13.328 1.00 18.02  ? 45  THR   A CA  1 
ATOM   315  C  C   . THR   A 1 39  ? 34.106 7.006   12.841 1.00 19.86  ? 45  THR   A C   1 
ATOM   316  O  O   . THR   A 1 39  ? 34.303 6.810   11.626 1.00 18.57  ? 45  THR   A O   1 
ATOM   317  C  CB  . THR   A 1 39  ? 31.827 6.380   13.683 1.00 18.40  ? 45  THR   A CB  1 
ATOM   318  O  OG1 . THR   A 1 39  ? 31.711 5.534   12.551 1.00 19.09  ? 45  THR   A OG1 1 
ATOM   319  C  CG2 . THR   A 1 39  ? 30.432 6.815   14.066 1.00 20.45  ? 45  THR   A CG2 1 
ATOM   320  N  N   . THR   A 1 40  ? 34.962 6.706   13.814 1.00 21.58  ? 46  THR   A N   1 
ATOM   321  C  CA  . THR   A 1 40  ? 36.264 6.058   13.543 1.00 24.27  ? 46  THR   A CA  1 
ATOM   322  C  C   . THR   A 1 40  ? 36.035 4.556   13.338 1.00 21.21  ? 46  THR   A C   1 
ATOM   323  O  O   . THR   A 1 40  ? 36.552 4.047   12.337 1.00 25.84  ? 46  THR   A O   1 
ATOM   324  C  CB  . THR   A 1 40  ? 37.274 6.426   14.641 1.00 27.74  ? 46  THR   A CB  1 
ATOM   325  O  OG1 . THR   A 1 40  ? 36.766 6.043   15.909 1.00 34.24  ? 46  THR   A OG1 1 
ATOM   326  C  CG2 . THR   A 1 40  ? 37.561 7.906   14.705 1.00 29.15  ? 46  THR   A CG2 1 
ATOM   327  N  N   . ALA   A 1 41  ? 35.226 3.921   14.183 1.00 23.56  ? 47  ALA   A N   1 
ATOM   328  C  CA  . ALA   A 1 41  ? 34.920 2.467   14.089 1.00 25.00  ? 47  ALA   A CA  1 
ATOM   329  C  C   . ALA   A 1 41  ? 33.714 2.210   13.160 1.00 25.95  ? 47  ALA   A C   1 
ATOM   330  O  O   . ALA   A 1 41  ? 32.775 3.042   13.135 1.00 24.31  ? 47  ALA   A O   1 
ATOM   331  C  CB  . ALA   A 1 41  ? 34.651 1.918   15.461 1.00 28.77  ? 47  ALA   A CB  1 
ATOM   332  N  N   . GLN   A 1 42  ? 33.713 1.095   12.420 1.00 24.00  ? 48  GLN   A N   1 
ATOM   333  C  CA  . GLN   A 1 42  ? 32.571 0.678   11.574 1.00 25.26  ? 48  GLN   A CA  1 
ATOM   334  C  C   . GLN   A 1 42  ? 31.479 0.050   12.443 1.00 22.10  ? 48  GLN   A C   1 
ATOM   335  O  O   . GLN   A 1 42  ? 31.774 -0.698  13.374 1.00 21.70  ? 48  GLN   A O   1 
ATOM   336  C  CB  . GLN   A 1 42  ? 33.027 -0.272  10.493 1.00 28.63  ? 48  GLN   A CB  1 
ATOM   337  C  CG  . GLN   A 1 42  ? 33.983 0.401   9.518  1.00 32.50  ? 48  GLN   A CG  1 
ATOM   338  C  CD  . GLN   A 1 42  ? 34.394 -0.612  8.490  1.00 36.16  ? 48  GLN   A CD  1 
ATOM   339  O  OE1 . GLN   A 1 42  ? 35.144 -1.546  8.789  1.00 35.65  ? 48  GLN   A OE1 1 
ATOM   340  N  NE2 . GLN   A 1 42  ? 33.801 -0.501  7.315  1.00 38.27  ? 48  GLN   A NE2 1 
ATOM   341  N  N   . GLY   A 1 43  ? 30.234 0.457   12.218 1.00 17.98  ? 49  GLY   A N   1 
ATOM   342  C  CA  . GLY   A 1 43  ? 29.070 -0.070  12.944 1.00 16.57  ? 49  GLY   A CA  1 
ATOM   343  C  C   . GLY   A 1 43  ? 28.472 -1.347  12.330 1.00 14.97  ? 49  GLY   A C   1 
ATOM   344  O  O   . GLY   A 1 43  ? 28.748 -1.669  11.130 1.00 16.38  ? 49  GLY   A O   1 
ATOM   345  N  N   . CYS   A 1 44  ? 27.541 -1.932  13.098 1.00 14.57  ? 50  CYS   A N   1 
ATOM   346  C  CA  . CYS   A 1 44  ? 26.939 -3.247  12.744 1.00 16.01  ? 50  CYS   A CA  1 
ATOM   347  C  C   . CYS   A 1 44  ? 25.481 -3.172  12.341 1.00 16.07  ? 50  CYS   A C   1 
ATOM   348  O  O   . CYS   A 1 44  ? 24.943 -4.194  11.883 1.00 15.66  ? 50  CYS   A O   1 
ATOM   349  C  CB  . CYS   A 1 44  ? 27.064 -4.222  13.899 1.00 15.27  ? 50  CYS   A CB  1 
ATOM   350  S  SG  . CYS   A 1 44  ? 28.796 -4.640  14.210 1.00 19.74  ? 50  CYS   A SG  1 
ATOM   351  N  N   . ASP   A 1 45  ? 24.825 -2.009  12.432 1.00 14.42  ? 51  ASP   A N   1 
ATOM   352  C  CA  . ASP   A 1 45  ? 23.431 -1.870  11.963 1.00 13.77  ? 51  ASP   A CA  1 
ATOM   353  C  C   . ASP   A 1 45  ? 23.378 -1.798  10.442 1.00 14.24  ? 51  ASP   A C   1 
ATOM   354  O  O   . ASP   A 1 45  ? 24.312 -1.264  9.807  1.00 15.63  ? 51  ASP   A O   1 
ATOM   355  C  CB  . ASP   A 1 45  ? 22.776 -0.635  12.570 1.00 12.23  ? 51  ASP   A CB  1 
ATOM   356  C  CG  . ASP   A 1 45  ? 22.669 -0.689  14.073 1.00 13.28  ? 51  ASP   A CG  1 
ATOM   357  O  OD1 . ASP   A 1 45  ? 22.347 -1.808  14.627 1.00 13.98  ? 51  ASP   A OD1 1 
ATOM   358  O  OD2 . ASP   A 1 45  ? 22.910 0.332   14.729 1.00 14.07  ? 51  ASP   A OD2 1 
ATOM   359  N  N   . THR   A 1 46  ? 22.363 -2.385  9.856  1.00 15.63  ? 52  THR   A N   1 
ATOM   360  C  CA  . THR   A 1 46  ? 22.030 -2.325  8.408  1.00 17.06  ? 52  THR   A CA  1 
ATOM   361  C  C   . THR   A 1 46  ? 20.724 -1.549  8.232  1.00 15.61  ? 52  THR   A C   1 
ATOM   362  O  O   . THR   A 1 46  ? 19.820 -1.684  9.110  1.00 16.48  ? 52  THR   A O   1 
ATOM   363  C  CB  . THR   A 1 46  ? 21.863 -3.742  7.839  1.00 20.64  ? 52  THR   A CB  1 
ATOM   364  O  OG1 . THR   A 1 46  ? 23.129 -4.408  8.006  1.00 30.37  ? 52  THR   A OG1 1 
ATOM   365  C  CG2 . THR   A 1 46  ? 21.482 -3.747  6.379  1.00 29.24  ? 52  THR   A CG2 1 
ATOM   366  N  N   . ILE   A 1 47  ? 20.567 -0.775  7.172  1.00 13.96  ? 53  ILE   A N   1 
ATOM   367  C  CA  . ILE   A 1 47  ? 19.337 -0.001  6.950  1.00 13.25  ? 53  ILE   A CA  1 
ATOM   368  C  C   . ILE   A 1 47  ? 18.380 -0.787  6.060  1.00 13.85  ? 53  ILE   A C   1 
ATOM   369  O  O   . ILE   A 1 47  ? 18.764 -1.285  5.002  1.00 14.67  ? 53  ILE   A O   1 
ATOM   370  C  CB  . ILE   A 1 47  ? 19.665 1.380   6.353  1.00 13.25  ? 53  ILE   A CB  1 
ATOM   371  C  CG1 . ILE   A 1 47  ? 20.753 2.127   7.141  1.00 13.23  ? 53  ILE   A CG1 1 
ATOM   372  C  CG2 . ILE   A 1 47  ? 18.426 2.273   6.151  1.00 12.22  ? 53  ILE   A CG2 1 
ATOM   373  C  CD1 . ILE   A 1 47  ? 20.395 2.464   8.586  1.00 13.90  ? 53  ILE   A CD1 1 
ATOM   374  N  N   . ALA   A 1 48  ? 17.125 -0.798  6.448  1.00 12.64  ? 54  ALA   A N   1 
ATOM   375  C  CA  . ALA   A 1 48  ? 16.020 -1.370  5.644  1.00 13.08  ? 54  ALA   A CA  1 
ATOM   376  C  C   . ALA   A 1 48  ? 15.764 -0.521  4.395  1.00 12.93  ? 54  ALA   A C   1 
ATOM   377  O  O   . ALA   A 1 48  ? 15.764 0.729   4.451  1.00 13.49  ? 54  ALA   A O   1 
ATOM   378  C  CB  . ALA   A 1 48  ? 14.783 -1.438  6.496  1.00 12.28  ? 54  ALA   A CB  1 
ATOM   379  N  N   . ARG   A 1 49  ? 15.536 -1.174  3.234  1.00 15.64  ? 55  ARG   A N   1 
ATOM   380  C  CA  . ARG   A 1 49  ? 15.157 -0.527  1.966  1.00 16.78  ? 55  ARG   A CA  1 
ATOM   381  C  C   . ARG   A 1 49  ? 13.841 -1.147  1.478  1.00 18.68  ? 55  ARG   A C   1 
ATOM   382  O  O   . ARG   A 1 49  ? 13.959 -2.180  0.737  1.00 21.58  ? 55  ARG   A O   1 
ATOM   383  C  CB  . ARG   A 1 49  ? 16.347 -0.689  1.003  1.00 18.18  ? 55  ARG   A CB  1 
ATOM   384  C  CG  . ARG   A 1 49  ? 17.656 -0.104  1.518  1.00 17.52  ? 55  ARG   A CG  1 
ATOM   385  C  CD  . ARG   A 1 49  ? 17.685 1.411   1.795  1.00 15.12  ? 55  ARG   A CD  1 
ATOM   386  N  NE  . ARG   A 1 49  ? 19.011 1.859   2.256  1.00 15.19  ? 55  ARG   A NE  1 
ATOM   387  C  CZ  . ARG   A 1 49  ? 19.255 2.994   2.881  1.00 15.39  ? 55  ARG   A CZ  1 
ATOM   388  N  NH1 . ARG   A 1 49  ? 18.314 3.890   3.066  1.00 15.23  ? 55  ARG   A NH1 1 
ATOM   389  N  NH2 . ARG   A 1 49  ? 20.494 3.274   3.288  1.00 18.01  ? 55  ARG   A NH2 1 
ATOM   390  N  N   . CYS   A 1 50  ? 12.718 -0.543  1.895  1.00 19.70  ? 56  CYS   A N   1 
ATOM   391  C  CA  . CYS   A 1 50  ? 11.341 -1.159  1.872  1.00 20.95  ? 56  CYS   A CA  1 
ATOM   392  C  C   . CYS   A 1 50  ? 10.229 -0.170  2.200  1.00 19.56  ? 56  CYS   A C   1 
ATOM   393  O  O   . CYS   A 1 50  ? 10.452 0.963   2.591  1.00 21.50  ? 56  CYS   A O   1 
ATOM   394  C  CB  . CYS   A 1 50  ? 11.368 -2.341  2.813  1.00 19.15  ? 56  CYS   A CB  1 
ATOM   395  S  SG  . CYS   A 1 50  ? 11.380 -1.859  4.574  1.00 20.00  ? 56  CYS   A SG  1 
ATOM   396  N  N   . ASP   A 1 51  ? 8.937  -0.622  2.133  1.00 25.59  ? 57  ASP   A N   1 
ATOM   397  C  CA  . ASP   A 1 51  ? 7.771  0.164   2.609  1.00 28.48  ? 57  ASP   A CA  1 
ATOM   398  C  C   . ASP   A 1 51  ? 6.999  -0.705  3.617  1.00 28.49  ? 57  ASP   A C   1 
ATOM   399  O  O   . ASP   A 1 51  ? 5.781  -0.490  3.745  1.00 31.68  ? 57  ASP   A O   1 
ATOM   400  C  CB  . ASP   A 1 51  ? 6.893  0.689   1.456  1.00 35.59  ? 57  ASP   A CB  1 
ATOM   401  C  CG  . ASP   A 1 51  ? 6.234  -0.452  0.722  1.00 38.88  ? 57  ASP   A CG  1 
ATOM   402  O  OD1 . ASP   A 1 51  ? 6.726  -1.627  0.903  1.00 37.54  ? 57  ASP   A OD1 1 
ATOM   403  O  OD2 . ASP   A 1 51  ? 5.252  -0.171  -0.008 1.00 44.27  ? 57  ASP   A OD2 1 
ATOM   404  N  N   . CYS   A 1 52  ? 7.690  -1.578  4.365  1.00 23.77  ? 58  CYS   A N   1 
ATOM   405  C  CA  . CYS   A 1 52  ? 7.139  -2.178  5.627  1.00 20.25  ? 58  CYS   A CA  1 
ATOM   406  C  C   . CYS   A 1 52  ? 6.390  -1.129  6.436  1.00 20.33  ? 58  CYS   A C   1 
ATOM   407  O  O   . CYS   A 1 52  ? 6.827  0.038   6.639  1.00 19.08  ? 58  CYS   A O   1 
ATOM   408  C  CB  . CYS   A 1 52  ? 8.220  -2.862  6.450  1.00 22.25  ? 58  CYS   A CB  1 
ATOM   409  S  SG  . CYS   A 1 52  ? 8.808  -4.447  5.822  1.00 20.49  ? 58  CYS   A SG  1 
ATOM   410  N  N   . GLN   A 1 53  ? 5.237  -1.540  6.974  1.00 17.34  ? 59  GLN   A N   1 
ATOM   411  C  CA  . GLN   A 1 53  ? 4.451  -0.729  7.902  1.00 17.57  ? 59  GLN   A CA  1 
ATOM   412  C  C   . GLN   A 1 53  ? 4.226  -1.517  9.208  1.00 13.19  ? 59  GLN   A C   1 
ATOM   413  O  O   . GLN   A 1 53  ? 3.381  -1.109  9.984  1.00 14.30  ? 59  GLN   A O   1 
ATOM   414  C  CB  . GLN   A 1 53  ? 3.102  -0.255  7.324  1.00 20.33  ? 59  GLN   A CB  1 
ATOM   415  C  CG  . GLN   A 1 53  ? 3.127  0.953   6.374  1.00 23.70  ? 59  GLN   A CG  1 
ATOM   416  C  CD  . GLN   A 1 53  ? 1.742  1.501   6.042  1.00 27.85  ? 59  GLN   A CD  1 
ATOM   417  O  OE1 . GLN   A 1 53  ? 1.193  1.290   4.959  1.00 29.02  ? 59  GLN   A OE1 1 
ATOM   418  N  NE2 . GLN   A 1 53  ? 1.140  2.225   6.963  1.00 24.69  ? 59  GLN   A NE2 1 
ATOM   419  N  N   . THR   A 1 54  ? 4.924  -2.617  9.411  1.00 12.37  ? 60  THR   A N   1 
ATOM   420  C  CA  . THR   A 1 54  ? 4.993  -3.312  10.713 1.00 13.32  ? 60  THR   A CA  1 
ATOM   421  C  C   . THR   A 1 54  ? 6.449  -3.564  11.082 1.00 12.80  ? 60  THR   A C   1 
ATOM   422  O  O   . THR   A 1 54  ? 7.314  -3.755  10.219 1.00 13.43  ? 60  THR   A O   1 
ATOM   423  C  CB  . THR   A 1 54  ? 4.216  -4.625  10.702 1.00 15.37  ? 60  THR   A CB  1 
ATOM   424  O  OG1 . THR   A 1 54  ? 4.831  -5.561  9.847  1.00 21.83  ? 60  THR   A OG1 1 
ATOM   425  C  CG2 . THR   A 1 54  ? 2.787  -4.509  10.257 1.00 15.21  ? 60  THR   A CG2 1 
ATOM   426  N  N   . GLY   A 1 55  ? 6.718  -3.541  12.367 1.00 10.74  ? 61  GLY   A N   1 
ATOM   427  C  CA  . GLY   A 1 55  ? 8.075  -3.739  12.858 1.00 10.90  ? 61  GLY   A CA  1 
ATOM   428  C  C   . GLY   A 1 55  ? 8.098  -3.810  14.372 1.00 10.08  ? 61  GLY   A C   1 
ATOM   429  O  O   . GLY   A 1 55  ? 7.027  -3.993  14.998 1.00 10.72  ? 61  GLY   A O   1 
ATOM   430  N  N   . VAL   A 1 56  ? 9.268  -3.590  14.948 1.00 9.30   ? 62  VAL   A N   1 
ATOM   431  C  CA  . VAL   A 1 56  ? 9.449  -3.697  16.405 1.00 9.13   ? 62  VAL   A CA  1 
ATOM   432  C  C   . VAL   A 1 56  ? 10.295 -2.512  16.849 1.00 8.91   ? 62  VAL   A C   1 
ATOM   433  O  O   . VAL   A 1 56  ? 11.299 -2.221  16.172 1.00 10.54  ? 62  VAL   A O   1 
ATOM   434  C  CB  . VAL   A 1 56  ? 10.111 -5.027  16.777 1.00 10.93  ? 62  VAL   A CB  1 
ATOM   435  C  CG1 . VAL   A 1 56  ? 10.489 -5.147  18.249 1.00 13.37  ? 62  VAL   A CG1 1 
ATOM   436  C  CG2 . VAL   A 1 56  ? 9.234  -6.185  16.363 1.00 10.82  ? 62  VAL   A CG2 1 
ATOM   437  N  N   . TYR   A 1 57  ? 9.949  -1.829  17.943 1.00 9.60   ? 63  TYR   A N   1 
ATOM   438  C  CA  . TYR   A 1 57  ? 10.783 -0.719  18.446 1.00 9.08   ? 63  TYR   A CA  1 
ATOM   439  C  C   . TYR   A 1 57  ? 11.241 -0.962  19.894 1.00 10.50  ? 63  TYR   A C   1 
ATOM   440  O  O   . TYR   A 1 57  ? 10.508 -1.604  20.692 1.00 10.70  ? 63  TYR   A O   1 
ATOM   441  C  CB  . TYR   A 1 57  ? 10.104 0.654   18.296 1.00 9.21   ? 63  TYR   A CB  1 
ATOM   442  C  CG  . TYR   A 1 57  ? 9.149  1.086   19.395 1.00 9.23   ? 63  TYR   A CG  1 
ATOM   443  C  CD1 . TYR   A 1 57  ? 7.868  0.567   19.454 1.00 10.39  ? 63  TYR   A CD1 1 
ATOM   444  C  CD2 . TYR   A 1 57  ? 9.516  1.990   20.364 1.00 10.23  ? 63  TYR   A CD2 1 
ATOM   445  C  CE1 . TYR   A 1 57  ? 6.972  0.920   20.459 1.00 11.47  ? 63  TYR   A CE1 1 
ATOM   446  C  CE2 . TYR   A 1 57  ? 8.645  2.360   21.380 1.00 11.27  ? 63  TYR   A CE2 1 
ATOM   447  C  CZ  . TYR   A 1 57  ? 7.353  1.858   21.383 1.00 12.08  ? 63  TYR   A CZ  1 
ATOM   448  O  OH  . TYR   A 1 57  ? 6.406  2.165   22.368 1.00 14.04  ? 63  TYR   A OH  1 
ATOM   449  N  N   . TYR   A 1 58  ? 12.360 -0.354  20.250 1.00 9.60   ? 64  TYR   A N   1 
ATOM   450  C  CA  . TYR   A 1 58  ? 12.855 -0.358  21.646 1.00 10.23  ? 64  TYR   A CA  1 
ATOM   451  C  C   . TYR   A 1 58  ? 12.384 0.866   22.424 1.00 10.50  ? 64  TYR   A C   1 
ATOM   452  O  O   . TYR   A 1 58  ? 12.608 1.998   22.041 1.00 9.86   ? 64  TYR   A O   1 
ATOM   453  C  CB  . TYR   A 1 58  ? 14.385 -0.452  21.703 1.00 10.44  ? 64  TYR   A CB  1 
ATOM   454  C  CG  . TYR   A 1 58  ? 14.860 -0.592  23.128 1.00 11.56  ? 64  TYR   A CG  1 
ATOM   455  C  CD1 . TYR   A 1 58  ? 14.529 -1.709  23.859 1.00 12.81  ? 64  TYR   A CD1 1 
ATOM   456  C  CD2 . TYR   A 1 58  ? 15.626 0.408   23.722 1.00 11.08  ? 64  TYR   A CD2 1 
ATOM   457  C  CE1 . TYR   A 1 58  ? 14.884 -1.808  25.202 1.00 13.80  ? 64  TYR   A CE1 1 
ATOM   458  C  CE2 . TYR   A 1 58  ? 15.953 0.337   25.064 1.00 11.96  ? 64  TYR   A CE2 1 
ATOM   459  C  CZ  . TYR   A 1 58  ? 15.656 -0.817  25.762 1.00 13.55  ? 64  TYR   A CZ  1 
ATOM   460  O  OH  . TYR   A 1 58  ? 16.018 -0.916  27.099 1.00 16.51  ? 64  TYR   A OH  1 
ATOM   461  N  N   . CYS   A 1 59  ? 11.767 0.559   23.570 1.00 10.06  ? 65  CYS   A N   1 
ATOM   462  C  CA  . CYS   A 1 59  ? 11.231 1.554   24.532 1.00 11.03  ? 65  CYS   A CA  1 
ATOM   463  C  C   . CYS   A 1 59  ? 12.049 1.543   25.819 1.00 11.12  ? 65  CYS   A C   1 
ATOM   464  O  O   . CYS   A 1 59  ? 11.876 0.596   26.647 1.00 11.44  ? 65  CYS   A O   1 
ATOM   465  C  CB  . CYS   A 1 59  ? 9.791  1.245   24.833 1.00 10.62  ? 65  CYS   A CB  1 
ATOM   466  S  SG  . CYS   A 1 59  ? 9.040  2.360   26.060 1.00 11.83  ? 65  CYS   A SG  1 
ATOM   467  N  N   . SER   A 1 60  ? 12.969 2.487   25.993 1.00 11.02  ? 66  SER   A N   1 
ATOM   468  C  CA  . SER   A 1 60  ? 13.879 2.529   27.178 1.00 12.68  ? 66  SER   A CA  1 
ATOM   469  C  C   . SER   A 1 60  ? 13.125 2.701   28.497 1.00 11.37  ? 66  SER   A C   1 
ATOM   470  O  O   . SER   A 1 60  ? 13.552 2.031   29.479 1.00 13.74  ? 66  SER   A O   1 
ATOM   471  C  CB  . SER   A 1 60  ? 14.968 3.551   27.009 1.00 13.78  ? 66  SER   A CB  1 
ATOM   472  O  OG  . SER   A 1 60  ? 14.545 4.881   27.121 1.00 17.19  ? 66  SER   A OG  1 
ATOM   473  N  N   . SER   A 1 61  ? 12.001 3.401   28.501 1.00 10.37  ? 67  SER   A N   1 
ATOM   474  C  CA  . SER   A 1 61  ? 11.192 3.626   29.717 1.00 11.45  ? 67  SER   A CA  1 
ATOM   475  C  C   . SER   A 1 61  ? 10.417 2.387   30.126 1.00 12.54  ? 67  SER   A C   1 
ATOM   476  O  O   . SER   A 1 61  ? 9.777  2.421   31.185 1.00 12.05  ? 67  SER   A O   1 
ATOM   477  C  CB  . SER   A 1 61  ? 10.310 4.810   29.560 1.00 12.64  ? 67  SER   A CB  1 
ATOM   478  O  OG  . SER   A 1 61  ? 9.319  4.614   28.599 1.00 12.38  ? 67  SER   A OG  1 
ATOM   479  N  N   . ARG   A 1 62  ? 10.510 1.281   29.391 1.00 12.54  ? 68  ARG   A N   1 
ATOM   480  C  CA  . ARG   A 1 62  ? 9.914  -0.032  29.742 1.00 12.20  ? 68  ARG   A CA  1 
ATOM   481  C  C   . ARG   A 1 62  ? 10.941 -1.160  29.695 1.00 13.36  ? 68  ARG   A C   1 
ATOM   482  O  O   . ARG   A 1 62  ? 10.549 -2.329  29.947 1.00 14.26  ? 68  ARG   A O   1 
ATOM   483  C  CB  . ARG   A 1 62  ? 8.702  -0.299  28.826 1.00 12.14  ? 68  ARG   A CB  1 
ATOM   484  C  CG  . ARG   A 1 62  ? 7.557  0.683   28.947 1.00 12.96  ? 68  ARG   A CG  1 
ATOM   485  C  CD  . ARG   A 1 62  ? 6.771  0.358   30.230 1.00 12.38  ? 68  ARG   A CD  1 
ATOM   486  N  NE  . ARG   A 1 62  ? 5.644  1.264   30.386 1.00 15.04  ? 68  ARG   A NE  1 
ATOM   487  C  CZ  . ARG   A 1 62  ? 5.668  2.405   31.072 1.00 13.72  ? 68  ARG   A CZ  1 
ATOM   488  N  NH1 . ARG   A 1 62  ? 6.808  2.879   31.581 1.00 14.91  ? 68  ARG   A NH1 1 
ATOM   489  N  NH2 . ARG   A 1 62  ? 4.565  3.141   31.164 1.00 15.13  ? 68  ARG   A NH2 1 
ATOM   490  N  N   . ARG   A 1 63  ? 12.150 -0.898  29.244 1.00 13.75  ? 69  ARG   A N   1 
ATOM   491  C  CA  . ARG   A 1 63  ? 13.134 -1.965  28.881 1.00 13.99  ? 69  ARG   A CA  1 
ATOM   492  C  C   . ARG   A 1 63  ? 12.471 -3.069  28.057 1.00 15.81  ? 69  ARG   A C   1 
ATOM   493  O  O   . ARG   A 1 63  ? 12.619 -4.272  28.348 1.00 19.26  ? 69  ARG   A O   1 
ATOM   494  C  CB  . ARG   A 1 63  ? 13.768 -2.607  30.125 1.00 16.19  ? 69  ARG   A CB  1 
ATOM   495  C  CG  . ARG   A 1 63  ? 14.750 -1.674  30.794 1.00 15.81  ? 69  ARG   A CG  1 
ATOM   496  C  CD  . ARG   A 1 63  ? 15.554 -2.472  31.838 1.00 15.63  ? 69  ARG   A CD  1 
ATOM   497  N  NE  . ARG   A 1 63  ? 16.323 -1.520  32.605 1.00 17.20  ? 69  ARG   A NE  1 
ATOM   498  C  CZ  . ARG   A 1 63  ? 15.998 -1.093  33.837 1.00 15.83  ? 69  ARG   A CZ  1 
ATOM   499  N  NH1 . ARG   A 1 63  ? 14.949 -1.575  34.488 1.00 18.82  ? 69  ARG   A NH1 1 
ATOM   500  N  NH2 . ARG   A 1 63  ? 16.767 -0.198  34.405 1.00 17.66  ? 69  ARG   A NH2 1 
ATOM   501  N  N   . LYS   A 1 64  ? 11.761 -2.695  27.035 1.00 14.37  ? 70  LYS   A N   1 
ATOM   502  C  CA  . LYS   A 1 64  ? 10.962 -3.662  26.254 1.00 14.48  ? 70  LYS   A CA  1 
ATOM   503  C  C   . LYS   A 1 64  ? 11.030 -3.282  24.783 1.00 13.78  ? 70  LYS   A C   1 
ATOM   504  O  O   . LYS   A 1 64  ? 10.947 -2.073  24.467 1.00 13.52  ? 70  LYS   A O   1 
ATOM   505  C  CB  . LYS   A 1 64  ? 9.518  -3.707  26.770 1.00 17.76  ? 70  LYS   A CB  1 
ATOM   506  C  CG  . LYS   A 1 64  ? 9.351  -4.568  28.024 1.00 27.46  ? 70  LYS   A CG  1 
ATOM   507  C  CD  . LYS   A 1 64  ? 7.951  -5.023  28.365 1.00 35.70  ? 70  LYS   A CD  1 
ATOM   508  C  CE  . LYS   A 1 64  ? 7.880  -5.840  29.655 1.00 42.00  ? 70  LYS   A CE  1 
ATOM   509  N  NZ  . LYS   A 1 64  ? 8.466  -5.132  30.829 1.00 45.23  ? 70  LYS   A NZ  1 
ATOM   510  N  N   . HIS   A 1 65  ? 11.003 -4.305  23.942 1.00 12.56  ? 71  HIS   A N   1 
ATOM   511  C  CA  . HIS   A 1 65  ? 10.772 -4.188  22.473 1.00 11.93  ? 71  HIS   A CA  1 
ATOM   512  C  C   . HIS   A 1 65  ? 9.304  -4.493  22.236 1.00 13.13  ? 71  HIS   A C   1 
ATOM   513  O  O   . HIS   A 1 65  ? 8.826  -5.546  22.709 1.00 16.27  ? 71  HIS   A O   1 
ATOM   514  C  CB  . HIS   A 1 65  ? 11.691 -5.129  21.701 1.00 11.27  ? 71  HIS   A CB  1 
ATOM   515  C  CG  . HIS   A 1 65  ? 13.138 -4.787  21.827 1.00 12.03  ? 71  HIS   A CG  1 
ATOM   516  N  ND1 . HIS   A 1 65  ? 13.923 -4.151  20.853 1.00 15.31  ? 71  HIS   A ND1 1 
ATOM   517  C  CD2 . HIS   A 1 65  ? 13.977 -5.112  22.837 1.00 11.34  ? 71  HIS   A CD2 1 
ATOM   518  C  CE1 . HIS   A 1 65  ? 15.195 -4.093  21.301 1.00 12.76  ? 71  HIS   A CE1 1 
ATOM   519  N  NE2 . HIS   A 1 65  ? 15.217 -4.681  22.478 1.00 15.73  ? 71  HIS   A NE2 1 
ATOM   520  N  N   . TYR   A 1 66  ? 8.621  -3.637  21.498 1.00 11.15  ? 72  TYR   A N   1 
ATOM   521  C  CA  . TYR   A 1 66  ? 7.178  -3.788  21.208 1.00 12.06  ? 72  TYR   A CA  1 
ATOM   522  C  C   . TYR   A 1 66  ? 6.974  -3.918  19.716 1.00 10.68  ? 72  TYR   A C   1 
ATOM   523  O  O   . TYR   A 1 66  ? 7.466  -3.075  18.947 1.00 10.68  ? 72  TYR   A O   1 
ATOM   524  C  CB  . TYR   A 1 66  ? 6.393  -2.553  21.691 1.00 11.38  ? 72  TYR   A CB  1 
ATOM   525  C  CG  . TYR   A 1 66  ? 6.294  -2.350  23.196 1.00 12.64  ? 72  TYR   A CG  1 
ATOM   526  C  CD1 . TYR   A 1 66  ? 5.484  -3.180  23.968 1.00 14.51  ? 72  TYR   A CD1 1 
ATOM   527  C  CD2 . TYR   A 1 66  ? 7.070  -1.419  23.848 1.00 13.57  ? 72  TYR   A CD2 1 
ATOM   528  C  CE1 . TYR   A 1 66  ? 5.381  -3.009  25.347 1.00 15.88  ? 72  TYR   A CE1 1 
ATOM   529  C  CE2 . TYR   A 1 66  ? 6.976  -1.227  25.219 1.00 15.48  ? 72  TYR   A CE2 1 
ATOM   530  C  CZ  . TYR   A 1 66  ? 6.127  -2.027  25.966 1.00 15.18  ? 72  TYR   A CZ  1 
ATOM   531  O  OH  . TYR   A 1 66  ? 6.013  -1.809  27.337 1.00 17.40  ? 72  TYR   A OH  1 
ATOM   532  N  N   . PRO   A 1 67  ? 6.138  -4.886  19.288 1.00 11.36  ? 73  PRO   A N   1 
ATOM   533  C  CA  . PRO   A 1 67  ? 5.694  -4.907  17.906 1.00 11.25  ? 73  PRO   A CA  1 
ATOM   534  C  C   . PRO   A 1 67  ? 4.652  -3.821  17.656 1.00 12.09  ? 73  PRO   A C   1 
ATOM   535  O  O   . PRO   A 1 67  ? 3.712  -3.709  18.451 1.00 13.59  ? 73  PRO   A O   1 
ATOM   536  C  CB  . PRO   A 1 67  ? 5.082  -6.304  17.712 1.00 12.97  ? 73  PRO   A CB  1 
ATOM   537  C  CG  . PRO   A 1 67  ? 4.675  -6.695  19.099 1.00 13.89  ? 73  PRO   A CG  1 
ATOM   538  C  CD  . PRO   A 1 67  ? 5.589  -5.983  20.099 1.00 11.82  ? 73  PRO   A CD  1 
ATOM   539  N  N   . VAL   A 1 68  ? 4.781  -3.157  16.535 1.00 10.95  ? 74  VAL   A N   1 
ATOM   540  C  CA  . VAL   A 1 68  ? 3.878  -2.030  16.147 1.00 12.05  ? 74  VAL   A CA  1 
ATOM   541  C  C   . VAL   A 1 68  ? 3.525  -2.133  14.663 1.00 11.85  ? 74  VAL   A C   1 
ATOM   542  O  O   . VAL   A 1 68  ? 4.373  -2.427  13.836 1.00 12.41  ? 74  VAL   A O   1 
ATOM   543  C  CB  . VAL   A 1 68  ? 4.472  -0.661  16.511 1.00 14.52  ? 74  VAL   A CB  1 
ATOM   544  C  CG1 . VAL   A 1 68  ? 4.391  -0.501  18.020 1.00 15.09  ? 74  VAL   A CG1 1 
ATOM   545  C  CG2 . VAL   A 1 68  ? 5.886  -0.488  15.980 1.00 14.38  ? 74  VAL   A CG2 1 
ATOM   546  N  N   . SER   A 1 69  ? 2.348  -1.557  14.354 1.00 12.20  ? 75  SER   A N   1 
ATOM   547  C  CA  . SER   A 1 69  ? 1.928  -1.062  13.032 1.00 12.96  ? 75  SER   A CA  1 
ATOM   548  C  C   . SER   A 1 69  ? 2.157  0.430   12.989 1.00 12.28  ? 75  SER   A C   1 
ATOM   549  O  O   . SER   A 1 69  ? 1.812  1.109   13.944 1.00 13.06  ? 75  SER   A O   1 
ATOM   550  C  CB  . SER   A 1 69  ? 0.455  -1.331  12.825 1.00 15.78  ? 75  SER   A CB  1 
ATOM   551  O  OG  . SER   A 1 69  ? 0.236  -2.707  12.766 1.00 23.87  ? 75  SER   A OG  1 
ATOM   552  N  N   . PHE   A 1 70  ? 2.738  0.968   11.906 1.00 12.34  ? 76  PHE   A N   1 
ATOM   553  C  CA  . PHE   A 1 70  ? 3.070  2.408   11.831 1.00 13.11  ? 76  PHE   A CA  1 
ATOM   554  C  C   . PHE   A 1 70  ? 2.666  2.954   10.469 1.00 12.39  ? 76  PHE   A C   1 
ATOM   555  O  O   . PHE   A 1 70  ? 2.606  2.228   9.490  1.00 14.90  ? 76  PHE   A O   1 
ATOM   556  C  CB  . PHE   A 1 70  ? 4.548  2.651   12.183 1.00 13.46  ? 76  PHE   A CB  1 
ATOM   557  C  CG  . PHE   A 1 70  ? 5.553  1.839   11.408 1.00 12.89  ? 76  PHE   A CG  1 
ATOM   558  C  CD1 . PHE   A 1 70  ? 5.990  0.600   11.852 1.00 12.62  ? 76  PHE   A CD1 1 
ATOM   559  C  CD2 . PHE   A 1 70  ? 6.149  2.355   10.250 1.00 11.66  ? 76  PHE   A CD2 1 
ATOM   560  C  CE1 . PHE   A 1 70  ? 6.925  -0.124  11.155 1.00 12.52  ? 76  PHE   A CE1 1 
ATOM   561  C  CE2 . PHE   A 1 70  ? 7.078  1.615   9.536  1.00 12.47  ? 76  PHE   A CE2 1 
ATOM   562  C  CZ  . PHE   A 1 70  ? 7.440  0.365   9.963  1.00 12.43  ? 76  PHE   A CZ  1 
ATOM   563  N  N   . SER   A 1 71  ? 2.373  4.238   10.464 1.00 13.64  ? 77  SER   A N   1 
ATOM   564  C  CA  . SER   A 1 71  ? 1.959  4.969   9.243  1.00 14.39  ? 77  SER   A CA  1 
ATOM   565  C  C   . SER   A 1 71  ? 3.150  5.173   8.306  1.00 15.85  ? 77  SER   A C   1 
ATOM   566  O  O   . SER   A 1 71  ? 4.303  5.042   8.708  1.00 15.29  ? 77  SER   A O   1 
ATOM   567  C  CB  . SER   A 1 71  ? 1.290  6.269   9.657  1.00 15.53  ? 77  SER   A CB  1 
ATOM   568  O  OG  . SER   A 1 71  ? 2.140  7.196   10.293 1.00 16.95  ? 77  SER   A OG  1 
ATOM   569  N  N   . LYS   A 1 72  ? 2.865  5.448   7.053  1.00 15.54  ? 78  LYS   A N   1 
ATOM   570  C  CA  . LYS   A 1 72  ? 3.938  5.798   6.093  1.00 14.81  ? 78  LYS   A CA  1 
ATOM   571  C  C   . LYS   A 1 72  ? 4.539  7.147   6.443  1.00 15.77  ? 78  LYS   A C   1 
ATOM   572  O  O   . LYS   A 1 72  ? 3.882  8.036   6.979  1.00 15.56  ? 78  LYS   A O   1 
ATOM   573  C  CB  . LYS   A 1 72  ? 3.353  5.720   4.674  1.00 18.06  ? 78  LYS   A CB  1 
ATOM   574  C  CG  . LYS   A 1 72  ? 2.923  4.329   4.245  1.00 19.95  ? 78  LYS   A CG  1 
ATOM   575  C  CD  . LYS   A 1 72  ? 2.541  4.212   2.774  1.00 25.54  ? 78  LYS   A CD  1 
ATOM   576  C  CE  . LYS   A 1 72  ? 2.267  2.809   2.312  1.00 32.18  ? 78  LYS   A CE  1 
ATOM   577  N  NZ  . LYS   A 1 72  ? 2.297  2.745   0.838  1.00 39.04  ? 78  LYS   A NZ  1 
ATOM   578  N  N   . PRO   A 1 73  ? 5.811  7.410   6.106  1.00 16.02  ? 79  PRO   A N   1 
ATOM   579  C  CA  . PRO   A 1 73  ? 6.427  8.669   6.444  1.00 15.99  ? 79  PRO   A CA  1 
ATOM   580  C  C   . PRO   A 1 73  ? 5.637  9.851   5.841  1.00 15.91  ? 79  PRO   A C   1 
ATOM   581  O  O   . PRO   A 1 73  ? 5.294  9.844   4.647  1.00 19.49  ? 79  PRO   A O   1 
ATOM   582  C  CB  . PRO   A 1 73  ? 7.851  8.569   5.882  1.00 17.75  ? 79  PRO   A CB  1 
ATOM   583  C  CG  . PRO   A 1 73  ? 7.896  7.327   5.060  1.00 22.22  ? 79  PRO   A CG  1 
ATOM   584  C  CD  . PRO   A 1 73  ? 6.715  6.462   5.428  1.00 17.35  ? 79  PRO   A CD  1 
ATOM   585  N  N   . SER   A 1 74  ? 5.394  10.832  6.663  1.00 15.91  ? 80  SER   A N   1 
ATOM   586  C  CA  . SER   A 1 74  ? 4.429  11.927  6.381  1.00 19.34  ? 80  SER   A CA  1 
ATOM   587  C  C   . SER   A 1 74  ? 4.894  13.207  7.057  1.00 16.98  ? 80  SER   A C   1 
ATOM   588  O  O   . SER   A 1 74  ? 5.734  13.247  7.985  1.00 16.90  ? 80  SER   A O   1 
ATOM   589  C  CB  . SER   A 1 74  ? 2.982  11.635  6.872  1.00 21.31  ? 80  SER   A CB  1 
ATOM   590  O  OG  . SER   A 1 74  ? 2.685  10.261  6.844  1.00 35.82  ? 80  SER   A OG  1 
ATOM   591  N  N   . LEU   A 1 75  ? 4.189  14.293  6.715  1.00 18.82  ? 81  LEU   A N   1 
ATOM   592  C  CA  . LEU   A 1 75  ? 4.324  15.604  7.372  1.00 18.16  ? 81  LEU   A CA  1 
ATOM   593  C  C   . LEU   A 1 75  ? 3.251  15.687  8.468  1.00 20.15  ? 81  LEU   A C   1 
ATOM   594  O  O   . LEU   A 1 75  ? 2.036  15.656  8.132  1.00 22.14  ? 81  LEU   A O   1 
ATOM   595  C  CB  . LEU   A 1 75  ? 4.116  16.679  6.285  1.00 22.23  ? 81  LEU   A CB  1 
ATOM   596  C  CG  . LEU   A 1 75  ? 4.533  18.098  6.627  1.00 24.80  ? 81  LEU   A CG  1 
ATOM   597  C  CD1 . LEU   A 1 75  ? 6.026  18.226  6.898  1.00 27.60  ? 81  LEU   A CD1 1 
ATOM   598  C  CD2 . LEU   A 1 75  ? 4.155  19.060  5.485  1.00 27.46  ? 81  LEU   A CD2 1 
ATOM   599  N  N   . ILE   A 1 76  ? 3.672  15.561  9.719  0.72 19.54  ? 82  ILE   A N   1 
ATOM   600  C  CA  . ILE   A 1 76  ? 2.788  15.343  10.895 0.72 21.65  ? 82  ILE   A CA  1 
ATOM   601  C  C   . ILE   A 1 76  ? 2.963  16.548  11.809 0.72 21.39  ? 82  ILE   A C   1 
ATOM   602  O  O   . ILE   A 1 76  ? 4.123  16.926  12.113 0.72 21.24  ? 82  ILE   A O   1 
ATOM   603  C  CB  . ILE   A 1 76  ? 3.138  14.046  11.655 0.72 22.23  ? 82  ILE   A CB  1 
ATOM   604  C  CG1 . ILE   A 1 76  ? 2.889  12.764  10.851 0.72 25.27  ? 82  ILE   A CG1 1 
ATOM   605  C  CG2 . ILE   A 1 76  ? 2.413  14.010  12.994 0.72 23.71  ? 82  ILE   A CG2 1 
ATOM   606  C  CD1 . ILE   A 1 76  ? 1.463  12.281  10.872 0.72 26.06  ? 82  ILE   A CD1 1 
ATOM   607  N  N   . PHE   A 1 77  ? 1.860  17.140  12.253 0.72 22.29  ? 83  PHE   A N   1 
ATOM   608  C  CA  . PHE   A 1 77  ? 1.917  18.231  13.246 0.72 21.70  ? 83  PHE   A CA  1 
ATOM   609  C  C   . PHE   A 1 77  ? 2.462  17.665  14.550 0.72 21.53  ? 83  PHE   A C   1 
ATOM   610  O  O   . PHE   A 1 77  ? 1.961  16.644  15.067 0.72 22.04  ? 83  PHE   A O   1 
ATOM   611  C  CB  . PHE   A 1 77  ? 0.561  18.890  13.491 0.72 23.70  ? 83  PHE   A CB  1 
ATOM   612  C  CG  . PHE   A 1 77  ? 0.666  19.965  14.537 0.72 23.94  ? 83  PHE   A CG  1 
ATOM   613  C  CD1 . PHE   A 1 77  ? 1.189  21.207  14.223 0.72 27.65  ? 83  PHE   A CD1 1 
ATOM   614  C  CD2 . PHE   A 1 77  ? 0.298  19.714  15.847 0.72 25.20  ? 83  PHE   A CD2 1 
ATOM   615  C  CE1 . PHE   A 1 77  ? 1.301  22.189  15.194 0.72 26.92  ? 83  PHE   A CE1 1 
ATOM   616  C  CE2 . PHE   A 1 77  ? 0.416  20.695  16.819 0.72 25.64  ? 83  PHE   A CE2 1 
ATOM   617  C  CZ  . PHE   A 1 77  ? 0.914  21.929  16.488 0.72 25.99  ? 83  PHE   A CZ  1 
ATOM   618  N  N   . VAL   A 1 78  ? 3.507  18.315  15.054 0.72 21.49  ? 84  VAL   A N   1 
ATOM   619  C  CA  . VAL   A 1 78  ? 4.105  17.979  16.372 0.72 20.34  ? 84  VAL   A CA  1 
ATOM   620  C  C   . VAL   A 1 78  ? 4.014  19.192  17.298 0.72 21.02  ? 84  VAL   A C   1 
ATOM   621  O  O   . VAL   A 1 78  ? 4.506  20.270  16.912 0.72 20.09  ? 84  VAL   A O   1 
ATOM   622  C  CB  . VAL   A 1 78  ? 5.562  17.503  16.218 0.72 18.19  ? 84  VAL   A CB  1 
ATOM   623  C  CG1 . VAL   A 1 78  ? 6.154  17.153  17.570 0.72 17.30  ? 84  VAL   A CG1 1 
ATOM   624  C  CG2 . VAL   A 1 78  ? 5.664  16.331  15.250 0.72 18.50  ? 84  VAL   A CG2 1 
ATOM   625  N  N   . GLU   A 1 79  ? 3.478  18.970  18.502 0.72 21.82  ? 85  GLU   A N   1 
ATOM   626  C  CA  . GLU   A 1 79  ? 3.254  20.021  19.527 0.72 24.40  ? 85  GLU   A CA  1 
ATOM   627  C  C   . GLU   A 1 79  ? 4.595  20.564  20.021 0.72 24.23  ? 85  GLU   A C   1 
ATOM   628  O  O   . GLU   A 1 79  ? 5.585  19.795  20.049 0.72 20.80  ? 85  GLU   A O   1 
ATOM   629  C  CB  . GLU   A 1 79  ? 2.468  19.477  20.720 0.72 26.11  ? 85  GLU   A CB  1 
ATOM   630  C  CG  . GLU   A 1 79  ? 2.013  20.563  21.680 0.72 30.42  ? 85  GLU   A CG  1 
ATOM   631  C  CD  . GLU   A 1 79  ? 1.328  21.774  21.058 0.72 31.67  ? 85  GLU   A CD  1 
ATOM   632  O  OE1 . GLU   A 1 79  ? 1.894  22.897  21.182 0.72 31.75  ? 85  GLU   A OE1 1 
ATOM   633  O  OE2 . GLU   A 1 79  ? 0.236  21.602  20.451 0.72 29.70  ? 85  GLU   A OE2 1 
ATOM   634  N  N   . ALA   A 1 80  ? 4.604  21.842  20.409 0.72 25.32  ? 86  ALA   A N   1 
ATOM   635  C  CA  . ALA   A 1 80  ? 5.752  22.537  21.031 0.72 24.23  ? 86  ALA   A CA  1 
ATOM   636  C  C   . ALA   A 1 80  ? 6.279  21.675  22.177 0.72 24.33  ? 86  ALA   A C   1 
ATOM   637  O  O   . ALA   A 1 80  ? 5.452  21.096  22.910 0.72 26.90  ? 86  ALA   A O   1 
ATOM   638  C  CB  . ALA   A 1 80  ? 5.348  23.907  21.516 0.72 24.65  ? 86  ALA   A CB  1 
ATOM   639  N  N   . SER   A 1 81  ? 7.608  21.560  22.268 0.72 24.07  ? 87  SER   A N   1 
ATOM   640  C  CA  . SER   A 1 81  ? 8.365  20.867  23.341 0.72 23.45  ? 87  SER   A CA  1 
ATOM   641  C  C   . SER   A 1 81  ? 9.522  21.774  23.767 0.72 23.38  ? 87  SER   A C   1 
ATOM   642  O  O   . SER   A 1 81  ? 9.632  22.908  23.196 0.72 23.69  ? 87  SER   A O   1 
ATOM   643  C  CB  . SER   A 1 81  ? 8.858  19.519  22.882 0.72 22.46  ? 87  SER   A CB  1 
ATOM   644  O  OG  . SER   A 1 81  ? 9.955  19.640  21.971 0.72 20.55  ? 87  SER   A OG  1 
ATOM   645  N  N   . GLU   A 1 82  ? 10.360 21.287  24.692 0.72 25.44  ? 88  GLU   A N   1 
ATOM   646  C  CA  . GLU   A 1 82  ? 11.567 22.012  25.170 0.72 25.03  ? 88  GLU   A CA  1 
ATOM   647  C  C   . GLU   A 1 82  ? 12.621 22.029  24.055 0.72 21.88  ? 88  GLU   A C   1 
ATOM   648  O  O   . GLU   A 1 82  ? 13.524 22.865  24.163 0.72 19.84  ? 88  GLU   A O   1 
ATOM   649  C  CB  . GLU   A 1 82  ? 12.091 21.450  26.497 0.72 28.16  ? 88  GLU   A CB  1 
ATOM   650  C  CG  . GLU   A 1 82  ? 12.781 20.103  26.420 0.72 29.26  ? 88  GLU   A CG  1 
ATOM   651  C  CD  . GLU   A 1 82  ? 13.406 19.663  27.732 0.72 35.62  ? 88  GLU   A CD  1 
ATOM   652  O  OE1 . GLU   A 1 82  ? 12.725 18.945  28.499 0.72 38.88  ? 88  GLU   A OE1 1 
ATOM   653  O  OE2 . GLU   A 1 82  ? 14.574 20.042  27.992 0.72 39.76  ? 88  GLU   A OE2 1 
ATOM   654  N  N   . TYR   A 1 83  ? 12.447 21.244  22.974 0.72 19.79  ? 89  TYR   A N   1 
ATOM   655  C  CA  . TYR   A 1 83  ? 13.428 21.144  21.852 0.72 17.74  ? 89  TYR   A CA  1 
ATOM   656  C  C   . TYR   A 1 83  ? 12.972 21.866  20.572 0.72 16.58  ? 89  TYR   A C   1 
ATOM   657  O  O   . TYR   A 1 83  ? 13.858 22.317  19.825 0.72 15.55  ? 89  TYR   A O   1 
ATOM   658  C  CB  . TYR   A 1 83  ? 13.731 19.665  21.581 0.72 18.17  ? 89  TYR   A CB  1 
ATOM   659  C  CG  . TYR   A 1 83  ? 14.377 18.962  22.751 0.72 18.01  ? 89  TYR   A CG  1 
ATOM   660  C  CD1 . TYR   A 1 83  ? 15.687 19.221  23.111 0.72 18.93  ? 89  TYR   A CD1 1 
ATOM   661  C  CD2 . TYR   A 1 83  ? 13.665 18.064  23.535 0.72 19.86  ? 89  TYR   A CD2 1 
ATOM   662  C  CE1 . TYR   A 1 83  ? 16.293 18.574  24.173 0.72 20.10  ? 89  TYR   A CE1 1 
ATOM   663  C  CE2 . TYR   A 1 83  ? 14.251 17.414  24.608 0.72 19.65  ? 89  TYR   A CE2 1 
ATOM   664  C  CZ  . TYR   A 1 83  ? 15.567 17.679  24.941 0.72 20.73  ? 89  TYR   A CZ  1 
ATOM   665  O  OH  . TYR   A 1 83  ? 16.184 17.051  25.991 0.72 24.51  ? 89  TYR   A OH  1 
ATOM   666  N  N   . TYR   A 1 84  ? 11.672 21.918  20.259 0.72 17.42  ? 90  TYR   A N   1 
ATOM   667  C  CA  . TYR   A 1 84  ? 11.144 22.552  19.020 0.72 17.21  ? 90  TYR   A CA  1 
ATOM   668  C  C   . TYR   A 1 84  ? 9.824  23.262  19.323 0.72 18.97  ? 90  TYR   A C   1 
ATOM   669  O  O   . TYR   A 1 84  ? 9.047  22.798  20.164 0.72 20.55  ? 90  TYR   A O   1 
ATOM   670  C  CB  . TYR   A 1 84  ? 10.860 21.541  17.897 0.72 16.32  ? 90  TYR   A CB  1 
ATOM   671  C  CG  . TYR   A 1 84  ? 12.023 20.722  17.376 0.72 13.78  ? 90  TYR   A CG  1 
ATOM   672  C  CD1 . TYR   A 1 84  ? 12.939 21.246  16.478 0.72 14.08  ? 90  TYR   A CD1 1 
ATOM   673  C  CD2 . TYR   A 1 84  ? 12.175 19.399  17.755 0.72 13.75  ? 90  TYR   A CD2 1 
ATOM   674  C  CE1 . TYR   A 1 84  ? 13.997 20.489  15.996 0.72 12.96  ? 90  TYR   A CE1 1 
ATOM   675  C  CE2 . TYR   A 1 84  ? 13.223 18.626  17.276 0.72 13.54  ? 90  TYR   A CE2 1 
ATOM   676  C  CZ  . TYR   A 1 84  ? 14.138 19.168  16.393 0.72 12.41  ? 90  TYR   A CZ  1 
ATOM   677  O  OH  . TYR   A 1 84  ? 15.198 18.430  15.923 0.72 12.19  ? 90  TYR   A OH  1 
ATOM   678  N  N   . PRO   A 1 85  ? 9.522  24.362  18.593 0.72 21.52  ? 91  PRO   A N   1 
ATOM   679  C  CA  . PRO   A 1 85  ? 8.187  24.961  18.604 0.72 22.52  ? 91  PRO   A CA  1 
ATOM   680  C  C   . PRO   A 1 85  ? 7.200  24.076  17.835 0.72 24.02  ? 91  PRO   A C   1 
ATOM   681  O  O   . PRO   A 1 85  ? 7.647  23.176  17.108 0.72 24.75  ? 91  PRO   A O   1 
ATOM   682  C  CB  . PRO   A 1 85  ? 8.387  26.309  17.885 0.72 22.17  ? 91  PRO   A CB  1 
ATOM   683  C  CG  . PRO   A 1 85  ? 9.560  26.073  16.959 0.72 22.17  ? 91  PRO   A CG  1 
ATOM   684  C  CD  . PRO   A 1 85  ? 10.436 25.063  17.676 0.72 20.87  ? 91  PRO   A CD  1 
ATOM   685  N  N   . ALA   A 1 86  ? 5.900  24.332  17.998 0.72 23.95  ? 92  ALA   A N   1 
ATOM   686  C  CA  . ALA   A 1 86  ? 4.824  23.667  17.230 0.72 25.19  ? 92  ALA   A CA  1 
ATOM   687  C  C   . ALA   A 1 86  ? 5.171  23.794  15.747 0.72 24.27  ? 92  ALA   A C   1 
ATOM   688  O  O   . ALA   A 1 86  ? 5.420  24.911  15.296 0.72 27.00  ? 92  ALA   A O   1 
ATOM   689  C  CB  . ALA   A 1 86  ? 3.486  24.297  17.541 0.72 26.40  ? 92  ALA   A CB  1 
ATOM   690  N  N   . ARG   A 1 87  ? 5.246  22.682  15.018 0.72 24.16  ? 93  ARG   A N   1 
ATOM   691  C  CA  . ARG   A 1 87  ? 5.680  22.706  13.602 0.72 23.98  ? 93  ARG   A CA  1 
ATOM   692  C  C   . ARG   A 1 87  ? 5.285  21.388  12.946 0.72 23.17  ? 93  ARG   A C   1 
ATOM   693  O  O   . ARG   A 1 87  ? 4.860  20.454  13.666 0.72 23.93  ? 93  ARG   A O   1 
ATOM   694  C  CB  . ARG   A 1 87  ? 7.193  22.936  13.519 0.72 24.33  ? 93  ARG   A CB  1 
ATOM   695  C  CG  . ARG   A 1 87  ? 8.020  21.655  13.502 0.72 24.33  ? 93  ARG   A CG  1 
ATOM   696  C  CD  . ARG   A 1 87  ? 9.272  21.735  14.337 0.72 20.70  ? 93  ARG   A CD  1 
ATOM   697  N  NE  . ARG   A 1 87  ? 10.191 20.642  14.032 0.72 19.02  ? 93  ARG   A NE  1 
ATOM   698  C  CZ  . ARG   A 1 87  ? 10.223 19.429  14.593 0.72 19.75  ? 93  ARG   A CZ  1 
ATOM   699  N  NH1 . ARG   A 1 87  ? 9.383  19.039  15.558 0.72 20.30  ? 93  ARG   A NH1 1 
ATOM   700  N  NH2 . ARG   A 1 87  ? 11.151 18.596  14.150 0.72 16.58  ? 93  ARG   A NH2 1 
ATOM   701  N  N   . TYR   A 1 88  ? 5.418  21.335  11.626 0.72 23.49  ? 94  TYR   A N   1 
ATOM   702  C  CA  . TYR   A 1 88  ? 5.284  20.102  10.826 0.72 24.22  ? 94  TYR   A CA  1 
ATOM   703  C  C   . TYR   A 1 88  ? 6.666  19.451  10.771 0.72 21.18  ? 94  TYR   A C   1 
ATOM   704  O  O   . TYR   A 1 88  ? 7.650  20.052  10.285 0.72 20.97  ? 94  TYR   A O   1 
ATOM   705  C  CB  . TYR   A 1 88  ? 4.617  20.401  9.484  0.72 26.83  ? 94  TYR   A CB  1 
ATOM   706  C  CG  . TYR   A 1 88  ? 3.154  20.706  9.655  0.72 29.70  ? 94  TYR   A CG  1 
ATOM   707  C  CD1 . TYR   A 1 88  ? 2.211  19.690  9.634  0.72 29.63  ? 94  TYR   A CD1 1 
ATOM   708  C  CD2 . TYR   A 1 88  ? 2.723  21.992  9.940  0.72 31.77  ? 94  TYR   A CD2 1 
ATOM   709  C  CE1 . TYR   A 1 88  ? 0.865  19.952  9.827  0.72 31.16  ? 94  TYR   A CE1 1 
ATOM   710  C  CE2 . TYR   A 1 88  ? 1.381  22.270  10.143 0.72 31.79  ? 94  TYR   A CE2 1 
ATOM   711  C  CZ  . TYR   A 1 88  ? 0.452  21.245  10.098 0.72 32.63  ? 94  TYR   A CZ  1 
ATOM   712  O  OH  . TYR   A 1 88  ? -0.867 21.516  10.300 0.72 34.07  ? 94  TYR   A OH  1 
ATOM   713  N  N   . GLN   A 1 89  ? 6.736  18.247  11.341 1.00 19.25  ? 95  GLN   A N   1 
ATOM   714  C  CA  . GLN   A 1 89  ? 7.942  17.381  11.192 1.00 17.55  ? 95  GLN   A CA  1 
ATOM   715  C  C   . GLN   A 1 89  ? 7.720  16.512  9.975  1.00 17.29  ? 95  GLN   A C   1 
ATOM   716  O  O   . GLN   A 1 89  ? 6.627  15.894  9.834  1.00 17.40  ? 95  GLN   A O   1 
ATOM   717  C  CB  . GLN   A 1 89  ? 8.169  16.607  12.493 1.00 17.38  ? 95  GLN   A CB  1 
ATOM   718  C  CG  . GLN   A 1 89  ? 9.481  15.857  12.459 1.00 16.82  ? 95  GLN   A CG  1 
ATOM   719  C  CD  . GLN   A 1 89  ? 9.997  15.349  13.791 1.00 15.27  ? 95  GLN   A CD  1 
ATOM   720  O  OE1 . GLN   A 1 89  ? 10.061 16.009  14.818 1.00 18.46  ? 95  GLN   A OE1 1 
ATOM   721  N  NE2 . GLN   A 1 89  ? 10.414 14.081  13.749 1.00 16.52  ? 95  GLN   A NE2 1 
ATOM   722  N  N   . SER   A 1 90  ? 8.686  16.422  9.054  1.00 15.17  ? 96  SER   A N   1 
ATOM   723  C  CA  . SER   A 1 90  ? 8.610  15.614  7.848  1.00 16.03  ? 96  SER   A CA  1 
ATOM   724  C  C   . SER   A 1 90  ? 9.219  14.238  8.094  1.00 14.46  ? 96  SER   A C   1 
ATOM   725  O  O   . SER   A 1 90  ? 9.986  14.086  9.100  1.00 16.16  ? 96  SER   A O   1 
ATOM   726  C  CB  . SER   A 1 90  ? 9.312  16.280  6.704  1.00 18.76  ? 96  SER   A CB  1 
ATOM   727  O  OG  . SER   A 1 90  ? 10.676 16.451  7.059  1.00 21.86  ? 96  SER   A OG  1 
ATOM   728  N  N   . HIS   A 1 91  ? 8.822  13.320  7.241  1.00 15.97  ? 97  HIS   A N   1 
ATOM   729  C  CA  . HIS   A 1 91  ? 9.334  11.936  7.196  1.00 16.01  ? 97  HIS   A CA  1 
ATOM   730  C  C   . HIS   A 1 91  ? 9.074  11.277  8.561  1.00 15.16  ? 97  HIS   A C   1 
ATOM   731  O  O   . HIS   A 1 91  ? 9.871  10.379  8.960  1.00 15.15  ? 97  HIS   A O   1 
ATOM   732  C  CB  . HIS   A 1 91  ? 10.837 11.929  6.807  1.00 17.76  ? 97  HIS   A CB  1 
ATOM   733  C  CG  . HIS   A 1 91  ? 11.115 12.484  5.436  1.00 17.65  ? 97  HIS   A CG  1 
ATOM   734  N  ND1 . HIS   A 1 91  ? 11.225 11.698  4.336  1.00 20.55  ? 97  HIS   A ND1 1 
ATOM   735  C  CD2 . HIS   A 1 91  ? 11.268 13.755  5.029  1.00 20.58  ? 97  HIS   A CD2 1 
ATOM   736  C  CE1 . HIS   A 1 91  ? 11.450 12.468  3.269  1.00 20.74  ? 97  HIS   A CE1 1 
ATOM   737  N  NE2 . HIS   A 1 91  ? 11.475 13.722  3.667  1.00 19.10  ? 97  HIS   A NE2 1 
ATOM   738  N  N   . LEU   A 1 92  ? 7.958  11.573  9.198  1.00 13.63  ? 98  LEU   A N   1 
ATOM   739  C  CA  . LEU   A 1 92  ? 7.591  11.031  10.548 1.00 14.20  ? 98  LEU   A CA  1 
ATOM   740  C  C   . LEU   A 1 92  ? 6.532  9.954   10.360 1.00 14.39  ? 98  LEU   A C   1 
ATOM   741  O  O   . LEU   A 1 92  ? 5.606  10.115  9.554  1.00 15.05  ? 98  LEU   A O   1 
ATOM   742  C  CB  . LEU   A 1 92  ? 7.063  12.153  11.432 1.00 16.13  ? 98  LEU   A CB  1 
ATOM   743  C  CG  . LEU   A 1 92  ? 6.755  11.772  12.891 1.00 17.53  ? 98  LEU   A CG  1 
ATOM   744  C  CD1 . LEU   A 1 92  ? 8.004  11.390  13.633 1.00 16.85  ? 98  LEU   A CD1 1 
ATOM   745  C  CD2 . LEU   A 1 92  ? 6.034  12.886  13.644 1.00 19.08  ? 98  LEU   A CD2 1 
ATOM   746  N  N   . MET   A 1 93  ? 6.654  8.853   11.098 1.00 13.46  ? 99  MET   A N   1 
ATOM   747  C  CA  . MET   A 1 93  ? 5.710  7.715   11.067 1.00 14.08  ? 99  MET   A CA  1 
ATOM   748  C  C   . MET   A 1 93  ? 5.131  7.574   12.476 1.00 13.92  ? 99  MET   A C   1 
ATOM   749  O  O   . MET   A 1 93  ? 5.896  7.658   13.482 1.00 14.59  ? 99  MET   A O   1 
ATOM   750  C  CB  . MET   A 1 93  ? 6.441  6.425   10.718 1.00 14.31  ? 99  MET   A CB  1 
ATOM   751  C  CG  . MET   A 1 93  ? 7.115  6.548   9.319  1.00 15.93  ? 99  MET   A CG  1 
ATOM   752  S  SD  . MET   A 1 93  ? 8.191  5.167   8.845  1.00 18.30  ? 99  MET   A SD  1 
ATOM   753  C  CE  . MET   A 1 93  ? 9.438  5.293   10.103 1.00 22.80  ? 99  MET   A CE  1 
ATOM   754  N  N   . LEU   A 1 94  ? 3.836  7.333   12.598 1.00 12.55  ? 100 LEU   A N   1 
ATOM   755  C  CA  . LEU   A 1 94  ? 3.180  7.259   13.915 1.00 14.45  ? 100 LEU   A CA  1 
ATOM   756  C  C   . LEU   A 1 94  ? 2.705  5.823   14.163 1.00 11.48  ? 100 LEU   A C   1 
ATOM   757  O  O   . LEU   A 1 94  ? 2.282  5.086   13.246 1.00 13.54  ? 100 LEU   A O   1 
ATOM   758  C  CB  . LEU   A 1 94  ? 1.981  8.217   13.951 1.00 16.51  ? 100 LEU   A CB  1 
ATOM   759  C  CG  . LEU   A 1 94  ? 2.257  9.708   14.018 1.00 19.01  ? 100 LEU   A CG  1 
ATOM   760  C  CD1 . LEU   A 1 94  ? 0.974  10.504  14.317 1.00 21.99  ? 100 LEU   A CD1 1 
ATOM   761  C  CD2 . LEU   A 1 94  ? 3.304  10.046  15.068 1.00 21.14  ? 100 LEU   A CD2 1 
ATOM   762  N  N   . ALA   A 1 95  ? 2.742  5.422   15.453 1.00 12.54  ? 101 ALA   A N   1 
ATOM   763  C  CA  . ALA   A 1 95  ? 2.208  4.151   15.946 1.00 11.98  ? 101 ALA   A CA  1 
ATOM   764  C  C   . ALA   A 1 95  ? 1.608  4.392   17.333 1.00 11.20  ? 101 ALA   A C   1 
ATOM   765  O  O   . ALA   A 1 95  ? 1.896  5.397   17.987 1.00 12.68  ? 101 ALA   A O   1 
ATOM   766  C  CB  . ALA   A 1 95  ? 3.282  3.056   16.033 1.00 12.67  ? 101 ALA   A CB  1 
ATOM   767  N  N   . VAL   A 1 96  ? 0.851  3.396   17.769 1.00 12.25  ? 102 VAL   A N   1 
ATOM   768  C  CA  . VAL   A 1 96  ? 0.311  3.391   19.139 1.00 11.63  ? 102 VAL   A CA  1 
ATOM   769  C  C   . VAL   A 1 96  ? 1.341  2.671   20.044 1.00 12.90  ? 102 VAL   A C   1 
ATOM   770  O  O   . VAL   A 1 96  ? 1.650  1.523   19.768 1.00 14.82  ? 102 VAL   A O   1 
ATOM   771  C  CB  . VAL   A 1 96  ? -1.045 2.683   19.191 1.00 12.95  ? 102 VAL   A CB  1 
ATOM   772  C  CG1 . VAL   A 1 96  ? -1.551 2.515   20.625 1.00 12.56  ? 102 VAL   A CG1 1 
ATOM   773  C  CG2 . VAL   A 1 96  ? -2.047 3.434   18.307 1.00 12.88  ? 102 VAL   A CG2 1 
ATOM   774  N  N   . GLY   A 1 97  ? 1.858  3.391   21.035 1.00 13.54  ? 103 GLY   A N   1 
ATOM   775  C  CA  . GLY   A 1 97  ? 2.864  2.812   21.944 1.00 13.79  ? 103 GLY   A CA  1 
ATOM   776  C  C   . GLY   A 1 97  ? 3.322  3.843   22.917 1.00 13.57  ? 103 GLY   A C   1 
ATOM   777  O  O   . GLY   A 1 97  ? 2.985  5.015   22.785 1.00 16.49  ? 103 GLY   A O   1 
ATOM   778  N  N   . HIS   A 1 98  ? 3.924  3.279   23.960 0.72 15.34  ? 104 HIS   A N   1 
ATOM   779  C  CA  . HIS   A 1 98  ? 4.487  4.037   25.076 0.72 16.90  ? 104 HIS   A CA  1 
ATOM   780  C  C   . HIS   A 1 98  ? 5.764  4.712   24.601 0.72 16.13  ? 104 HIS   A C   1 
ATOM   781  O  O   . HIS   A 1 98  ? 6.667  4.025   24.100 0.72 15.55  ? 104 HIS   A O   1 
ATOM   782  C  CB  . HIS   A 1 98  ? 4.722  3.139   26.296 0.72 16.92  ? 104 HIS   A CB  1 
ATOM   783  C  CG  . HIS   A 1 98  ? 5.046  4.009   27.454 0.72 17.84  ? 104 HIS   A CG  1 
ATOM   784  N  ND1 . HIS   A 1 98  ? 4.097  4.828   28.019 0.72 17.10  ? 104 HIS   A ND1 1 
ATOM   785  C  CD2 . HIS   A 1 98  ? 6.218  4.301   28.062 0.72 17.93  ? 104 HIS   A CD2 1 
ATOM   786  C  CE1 . HIS   A 1 98  ? 4.660  5.560   28.964 0.72 18.93  ? 104 HIS   A CE1 1 
ATOM   787  N  NE2 . HIS   A 1 98  ? 5.962  5.247   29.009 0.72 18.40  ? 104 HIS   A NE2 1 
ATOM   788  N  N   . SER   A 1 99  ? 5.802  6.030   24.721 0.72 16.18  ? 105 SER   A N   1 
ATOM   789  C  CA  . SER   A 1 99  ? 6.995  6.864   24.471 0.72 16.52  ? 105 SER   A CA  1 
ATOM   790  C  C   . SER   A 1 99  ? 6.915  8.061   25.418 0.72 19.26  ? 105 SER   A C   1 
ATOM   791  O  O   . SER   A 1 99  ? 5.937  8.839   25.310 0.72 18.05  ? 105 SER   A O   1 
ATOM   792  C  CB  . SER   A 1 99  ? 7.071  7.239   23.002 0.72 17.37  ? 105 SER   A CB  1 
ATOM   793  O  OG  . SER   A 1 99  ? 8.130  8.146   22.747 0.72 18.54  ? 105 SER   A OG  1 
ATOM   794  N  N   . GLU   A 1 100 ? 7.885  8.181   26.322 0.72 18.47  ? 106 GLU   A N   1 
ATOM   795  C  CA  . GLU   A 1 100 ? 7.968  9.313   27.276 0.72 21.76  ? 106 GLU   A CA  1 
ATOM   796  C  C   . GLU   A 1 100 ? 9.321  9.986   27.077 0.72 23.01  ? 106 GLU   A C   1 
ATOM   797  O  O   . GLU   A 1 100 ? 10.183 9.493   26.342 0.72 23.55  ? 106 GLU   A O   1 
ATOM   798  C  CB  . GLU   A 1 100 ? 7.616  8.841   28.702 0.72 22.03  ? 106 GLU   A CB  1 
ATOM   799  C  CG  . GLU   A 1 100 ? 8.562  7.816   29.300 0.72 21.79  ? 106 GLU   A CG  1 
ATOM   800  C  CD  . GLU   A 1 100 ? 8.183  7.329   30.694 0.72 21.71  ? 106 GLU   A CD  1 
ATOM   801  O  OE1 . GLU   A 1 100 ? 8.522  8.019   31.665 0.72 24.51  ? 106 GLU   A OE1 1 
ATOM   802  O  OE2 . GLU   A 1 100 ? 7.518  6.295   30.798 0.72 21.22  ? 106 GLU   A OE2 1 
ATOM   803  N  N   . PRO   A 1 101 ? 9.495  11.213  27.626 0.72 26.22  ? 107 PRO   A N   1 
ATOM   804  C  CA  . PRO   A 1 101 ? 10.763 11.927  27.542 0.72 26.14  ? 107 PRO   A CA  1 
ATOM   805  C  C   . PRO   A 1 101 ? 11.952 11.099  28.049 0.72 25.80  ? 107 PRO   A C   1 
ATOM   806  O  O   . PRO   A 1 101 ? 12.054 10.808  29.288 0.72 26.34  ? 107 PRO   A O   1 
ATOM   807  C  CB  . PRO   A 1 101 ? 10.507 13.177  28.396 0.72 27.43  ? 107 PRO   A CB  1 
ATOM   808  C  CG  . PRO   A 1 101 ? 9.038  13.420  28.170 0.72 27.52  ? 107 PRO   A CG  1 
ATOM   809  C  CD  . PRO   A 1 101 ? 8.449  12.025  28.276 0.72 26.62  ? 107 PRO   A CD  1 
ATOM   810  N  N   . GLY   A 1 102 ? 12.832 10.794  27.088 0.72 20.61  ? 108 GLY   A N   1 
ATOM   811  C  CA  . GLY   A 1 102 ? 13.996 9.900   27.240 0.72 18.63  ? 108 GLY   A CA  1 
ATOM   812  C  C   . GLY   A 1 102 ? 13.973 8.717   26.274 0.72 15.39  ? 108 GLY   A C   1 
ATOM   813  O  O   . GLY   A 1 102 ? 15.001 8.061   26.146 0.72 15.68  ? 108 GLY   A O   1 
ATOM   814  N  N   . ASP   A 1 103 ? 12.827 8.409   25.655 0.72 13.76  ? 109 ASP   A N   1 
ATOM   815  C  CA  . ASP   A 1 103 ? 12.691 7.248   24.740 0.72 12.98  ? 109 ASP   A CA  1 
ATOM   816  C  C   . ASP   A 1 103 ? 13.209 7.587   23.338 0.72 12.52  ? 109 ASP   A C   1 
ATOM   817  O  O   . ASP   A 1 103 ? 13.421 6.651   22.555 0.72 11.57  ? 109 ASP   A O   1 
ATOM   818  C  CB  . ASP   A 1 103 ? 11.253 6.729   24.695 0.72 12.72  ? 109 ASP   A CB  1 
ATOM   819  C  CG  . ASP   A 1 103 ? 10.898 5.906   25.921 0.72 12.05  ? 109 ASP   A CG  1 
ATOM   820  O  OD1 . ASP   A 1 103 ? 11.822 5.267   26.444 0.72 13.35  ? 109 ASP   A OD1 1 
ATOM   821  O  OD2 . ASP   A 1 103 ? 9.710  5.919   26.342 0.72 11.37  ? 109 ASP   A OD2 1 
ATOM   822  N  N   . CYS   A 1 104 ? 13.425 8.856   23.014 0.72 11.51  ? 110 CYS   A N   1 
ATOM   823  C  CA  . CYS   A 1 104 ? 13.979 9.204   21.676 0.72 11.90  ? 110 CYS   A CA  1 
ATOM   824  C  C   . CYS   A 1 104 ? 15.309 8.462   21.489 0.72 11.71  ? 110 CYS   A C   1 
ATOM   825  O  O   . CYS   A 1 104 ? 16.103 8.342   22.431 0.72 12.06  ? 110 CYS   A O   1 
ATOM   826  C  CB  . CYS   A 1 104 ? 14.097 10.709  21.495 0.72 12.45  ? 110 CYS   A CB  1 
ATOM   827  S  SG  . CYS   A 1 104 ? 12.476 11.498  21.259 0.72 15.20  ? 110 CYS   A SG  1 
ATOM   828  N  N   . GLY   A 1 105 ? 15.535 7.947   20.274 0.72 10.85  ? 111 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 105 ? 16.781 7.271   19.875 0.72 10.52  ? 111 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 105 ? 16.640 5.753   19.790 0.72 10.67  ? 111 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 105 ? 17.520 5.103   19.229 0.72 11.36  ? 111 GLY   A O   1 
ATOM   832  N  N   . GLY   A 1 106 ? 15.605 5.210   20.412 1.00 10.58  ? 112 GLY   A N   1 
ATOM   833  C  CA  . GLY   A 1 106 ? 15.293 3.783   20.322 1.00 9.59   ? 112 GLY   A CA  1 
ATOM   834  C  C   . GLY   A 1 106 ? 15.087 3.358   18.865 1.00 9.72   ? 112 GLY   A C   1 
ATOM   835  O  O   . GLY   A 1 106 ? 14.400 4.079   18.136 1.00 9.64   ? 112 GLY   A O   1 
ATOM   836  N  N   . ILE   A 1 107 ? 15.601 2.226   18.446 1.00 9.83   ? 113 ILE   A N   1 
ATOM   837  C  CA  . ILE   A 1 107 ? 15.458 1.767   17.039 1.00 8.99   ? 113 ILE   A CA  1 
ATOM   838  C  C   . ILE   A 1 107 ? 14.101 1.122   16.790 1.00 9.08   ? 113 ILE   A C   1 
ATOM   839  O  O   . ILE   A 1 107 ? 13.647 0.277   17.582 1.00 9.25   ? 113 ILE   A O   1 
ATOM   840  C  CB  . ILE   A 1 107 ? 16.624 0.821   16.706 1.00 9.86   ? 113 ILE   A CB  1 
ATOM   841  C  CG1 . ILE   A 1 107 ? 17.897 1.668   16.482 1.00 10.71  ? 113 ILE   A CG1 1 
ATOM   842  C  CG2 . ILE   A 1 107 ? 16.323 -0.082  15.515 1.00 10.21  ? 113 ILE   A CG2 1 
ATOM   843  C  CD1 . ILE   A 1 107 ? 19.155 0.875   16.286 1.00 13.57  ? 113 ILE   A CD1 1 
ATOM   844  N  N   . LEU   A 1 108 ? 13.532 1.486   15.634 1.00 8.55   ? 114 LEU   A N   1 
ATOM   845  C  CA  . LEU   A 1 108 ? 12.436 0.751   14.978 1.00 8.77   ? 114 LEU   A CA  1 
ATOM   846  C  C   . LEU   A 1 108 ? 13.056 -0.073  13.857 1.00 8.58   ? 114 LEU   A C   1 
ATOM   847  O  O   . LEU   A 1 108 ? 13.815 0.468   13.012 1.00 9.98   ? 114 LEU   A O   1 
ATOM   848  C  CB  . LEU   A 1 108 ? 11.412 1.765   14.405 1.00 8.96   ? 114 LEU   A CB  1 
ATOM   849  C  CG  . LEU   A 1 108 ? 10.307 1.147   13.533 1.00 10.00  ? 114 LEU   A CG  1 
ATOM   850  C  CD1 . LEU   A 1 108 ? 9.347  0.324   14.369 1.00 10.80  ? 114 LEU   A CD1 1 
ATOM   851  C  CD2 . LEU   A 1 108 ? 9.551  2.222   12.734 1.00 10.94  ? 114 LEU   A CD2 1 
ATOM   852  N  N   . ARG   A 1 109 ? 12.742 -1.364  13.827 1.00 8.64   ? 115 ARG   A N   1 
ATOM   853  C  CA  . ARG   A 1 109 ? 13.312 -2.269  12.773 1.00 9.60   ? 115 ARG   A CA  1 
ATOM   854  C  C   . ARG   A 1 109 ? 12.240 -3.202  12.240 1.00 10.24  ? 115 ARG   A C   1 
ATOM   855  O  O   . ARG   A 1 109 ? 11.192 -3.466  12.889 1.00 10.33  ? 115 ARG   A O   1 
ATOM   856  C  CB  . ARG   A 1 109 ? 14.448 -3.119  13.347 1.00 11.34  ? 115 ARG   A CB  1 
ATOM   857  C  CG  . ARG   A 1 109 ? 14.023 -4.124  14.425 1.00 11.73  ? 115 ARG   A CG  1 
ATOM   858  C  CD  . ARG   A 1 109 ? 15.224 -4.831  15.032 1.00 12.58  ? 115 ARG   A CD  1 
ATOM   859  N  NE  . ARG   A 1 109 ? 16.032 -3.975  15.871 1.00 13.47  ? 115 ARG   A NE  1 
ATOM   860  C  CZ  . ARG   A 1 109 ? 17.339 -3.745  15.781 1.00 14.20  ? 115 ARG   A CZ  1 
ATOM   861  N  NH1 . ARG   A 1 109 ? 18.052 -4.158  14.741 1.00 14.95  ? 115 ARG   A NH1 1 
ATOM   862  N  NH2 . ARG   A 1 109 ? 17.956 -3.017  16.693 1.00 14.85  ? 115 ARG   A NH2 1 
ATOM   863  N  N   . CYS   A 1 110 ? 12.452 -3.643  11.009 1.00 12.87  ? 116 CYS   A N   1 
ATOM   864  C  CA  . CYS   A 1 110 ? 11.563 -4.591  10.284 1.00 16.57  ? 116 CYS   A CA  1 
ATOM   865  C  C   . CYS   A 1 110 ? 12.437 -5.767  9.878  1.00 18.64  ? 116 CYS   A C   1 
ATOM   866  O  O   . CYS   A 1 110 ? 13.606 -5.899  10.299 1.00 17.35  ? 116 CYS   A O   1 
ATOM   867  C  CB  . CYS   A 1 110 ? 10.858 -3.909  9.123  1.00 14.84  ? 116 CYS   A CB  1 
ATOM   868  S  SG  . CYS   A 1 110 ? 12.038 -3.552  7.787  1.00 15.59  ? 116 CYS   A SG  1 
ATOM   869  N  N   . GLN   A 1 111 ? 11.802 -6.678  9.122  1.00 22.87  ? 117 GLN   A N   1 
ATOM   870  C  CA  . GLN   A 1 111 ? 12.487 -7.880  8.596  1.00 25.16  ? 117 GLN   A CA  1 
ATOM   871  C  C   . GLN   A 1 111 ? 13.752 -7.507  7.782  1.00 25.94  ? 117 GLN   A C   1 
ATOM   872  O  O   . GLN   A 1 111 ? 14.712 -8.288  7.761  1.00 28.47  ? 117 GLN   A O   1 
ATOM   873  C  CB  . GLN   A 1 111 ? 11.479 -8.718  7.776  1.00 29.89  ? 117 GLN   A CB  1 
ATOM   874  C  CG  . GLN   A 1 111 ? 10.925 -8.004  6.549  1.00 31.08  ? 117 GLN   A CG  1 
ATOM   875  C  CD  . GLN   A 1 111 ? 10.037 -8.902  5.723  1.00 37.12  ? 117 GLN   A CD  1 
ATOM   876  O  OE1 . GLN   A 1 111 ? 8.848  -8.653  5.586  1.00 37.94  ? 117 GLN   A OE1 1 
ATOM   877  N  NE2 . GLN   A 1 111 ? 10.616 -9.965  5.179  1.00 35.41  ? 117 GLN   A NE2 1 
ATOM   878  N  N   . HIS   A 1 112 ? 13.785 -6.325  7.192  1.00 20.29  ? 118 HIS   A N   1 
ATOM   879  C  CA  . HIS   A 1 112 ? 14.885 -5.915  6.259  1.00 18.57  ? 118 HIS   A CA  1 
ATOM   880  C  C   . HIS   A 1 112 ? 16.012 -5.192  6.992  1.00 18.92  ? 118 HIS   A C   1 
ATOM   881  O  O   . HIS   A 1 112 ? 17.074 -5.009  6.398  1.00 22.22  ? 118 HIS   A O   1 
ATOM   882  C  CB  . HIS   A 1 112 ? 14.249 -5.082  5.189  1.00 17.89  ? 118 HIS   A CB  1 
ATOM   883  C  CG  . HIS   A 1 112 ? 13.054 -5.775  4.597  1.00 18.47  ? 118 HIS   A CG  1 
ATOM   884  N  ND1 . HIS   A 1 112 ? 11.798 -5.187  4.479  1.00 21.57  ? 118 HIS   A ND1 1 
ATOM   885  C  CD2 . HIS   A 1 112 ? 13.041 -6.926  3.867  1.00 28.90  ? 118 HIS   A CD2 1 
ATOM   886  C  CE1 . HIS   A 1 112 ? 11.010 -6.036  3.817  1.00 29.04  ? 118 HIS   A CE1 1 
ATOM   887  N  NE2 . HIS   A 1 112 ? 11.757 -7.103  3.448  1.00 28.39  ? 118 HIS   A NE2 1 
ATOM   888  N  N   . GLY   A 1 113 ? 15.795 -4.704  8.220  1.00 16.36  ? 119 GLY   A N   1 
ATOM   889  C  CA  . GLY   A 1 113 ? 16.834 -3.938  8.903  1.00 15.54  ? 119 GLY   A CA  1 
ATOM   890  C  C   . GLY   A 1 113 ? 16.245 -2.766  9.687  1.00 13.39  ? 119 GLY   A C   1 
ATOM   891  O  O   . GLY   A 1 113 ? 15.056 -2.757  10.014 1.00 13.23  ? 119 GLY   A O   1 
ATOM   892  N  N   . VAL   A 1 114 ? 17.092 -1.770  9.984  1.00 12.45  ? 120 VAL   A N   1 
ATOM   893  C  CA  . VAL   A 1 114 ? 16.670 -0.552  10.753 1.00 11.81  ? 120 VAL   A CA  1 
ATOM   894  C  C   . VAL   A 1 114 ? 15.809 0.357   9.884  1.00 10.80  ? 120 VAL   A C   1 
ATOM   895  O  O   . VAL   A 1 114 ? 16.244 0.730   8.741  1.00 10.86  ? 120 VAL   A O   1 
ATOM   896  C  CB  . VAL   A 1 114 ? 17.893 0.210   11.296 1.00 10.68  ? 120 VAL   A CB  1 
ATOM   897  C  CG1 . VAL   A 1 114 ? 17.444 1.521   11.945 1.00 12.34  ? 120 VAL   A CG1 1 
ATOM   898  C  CG2 . VAL   A 1 114 ? 18.670 -0.658  12.262 1.00 11.66  ? 120 VAL   A CG2 1 
ATOM   899  N  N   . VAL   A 1 115 ? 14.674 0.776   10.399 1.00 9.60   ? 121 VAL   A N   1 
ATOM   900  C  CA  . VAL   A 1 115 ? 13.706 1.639   9.703  1.00 10.50  ? 121 VAL   A CA  1 
ATOM   901  C  C   . VAL   A 1 115 ? 13.894 3.080   10.119 1.00 10.48  ? 121 VAL   A C   1 
ATOM   902  O  O   . VAL   A 1 115 ? 13.708 4.020   9.333  1.00 11.62  ? 121 VAL   A O   1 
ATOM   903  C  CB  . VAL   A 1 115 ? 12.270 1.135   9.971  1.00 11.67  ? 121 VAL   A CB  1 
ATOM   904  C  CG1 . VAL   A 1 115 ? 11.194 2.113   9.491  1.00 13.08  ? 121 VAL   A CG1 1 
ATOM   905  C  CG2 . VAL   A 1 115 ? 12.094 -0.245  9.409  1.00 12.22  ? 121 VAL   A CG2 1 
ATOM   906  N  N   . GLY   A 1 116 ? 14.041 3.329   11.424 1.00 10.45  ? 122 GLY   A N   1 
ATOM   907  C  CA  . GLY   A 1 116 ? 14.162 4.693   11.938 1.00 10.99  ? 122 GLY   A CA  1 
ATOM   908  C  C   . GLY   A 1 116 ? 14.377 4.686   13.430 1.00 10.19  ? 122 GLY   A C   1 
ATOM   909  O  O   . GLY   A 1 116 ? 14.716 3.619   14.007 1.00 9.84   ? 122 GLY   A O   1 
ATOM   910  N  N   . ILE   A 1 117 ? 14.289 5.860   14.043 0.72 9.83   ? 123 ILE   A N   1 
ATOM   911  C  CA  . ILE   A 1 117 ? 14.505 6.030   15.510 0.72 9.71   ? 123 ILE   A CA  1 
ATOM   912  C  C   . ILE   A 1 117 ? 13.294 6.727   16.110 0.72 9.91   ? 123 ILE   A C   1 
ATOM   913  O  O   . ILE   A 1 117 ? 12.637 7.536   15.410 0.72 9.54   ? 123 ILE   A O   1 
ATOM   914  C  CB  . ILE   A 1 117 ? 15.793 6.796   15.860 0.72 10.04  ? 123 ILE   A CB  1 
ATOM   915  C  CG1 . ILE   A 1 117 ? 15.942 8.104   15.076 0.72 10.86  ? 123 ILE   A CG1 1 
ATOM   916  C  CG2 . ILE   A 1 117 ? 16.989 5.868   15.719 0.72 10.28  ? 123 ILE   A CG2 1 
ATOM   917  C  CD1 . ILE   A 1 117 ? 17.108 8.956   15.545 0.72 11.35  ? 123 ILE   A CD1 1 
ATOM   918  N  N   . VAL   A 1 118 ? 13.048 6.484   17.382 0.72 10.16  ? 124 VAL   A N   1 
ATOM   919  C  CA  . VAL   A 1 118 ? 11.987 7.220   18.116 0.72 10.93  ? 124 VAL   A CA  1 
ATOM   920  C  C   . VAL   A 1 118 ? 12.326 8.714   18.046 0.72 10.71  ? 124 VAL   A C   1 
ATOM   921  O  O   . VAL   A 1 118 ? 13.476 9.083   18.352 0.72 11.40  ? 124 VAL   A O   1 
ATOM   922  C  CB  . VAL   A 1 118 ? 11.845 6.752   19.570 0.72 10.63  ? 124 VAL   A CB  1 
ATOM   923  C  CG1 . VAL   A 1 118 ? 10.768 7.550   20.300 0.72 10.81  ? 124 VAL   A CG1 1 
ATOM   924  C  CG2 . VAL   A 1 118 ? 11.587 5.244   19.677 0.72 10.57  ? 124 VAL   A CG2 1 
ATOM   925  N  N   . SER   A 1 119 ? 11.336 9.544   17.700 0.72 11.84  ? 125 SER   A N   1 
ATOM   926  C  CA  . SER   A 1 119 ? 11.438 11.026  17.581 0.72 12.52  ? 125 SER   A CA  1 
ATOM   927  C  C   . SER   A 1 119 ? 10.281 11.732  18.330 0.72 14.11  ? 125 SER   A C   1 
ATOM   928  O  O   . SER   A 1 119 ? 10.517 12.884  18.722 0.72 15.48  ? 125 SER   A O   1 
ATOM   929  C  CB  . SER   A 1 119 ? 11.561 11.397  16.112 0.72 13.18  ? 125 SER   A CB  1 
ATOM   930  O  OG  . SER   A 1 119 ? 11.690 12.804  15.906 0.72 13.05  ? 125 SER   A OG  1 
ATOM   931  N  N   . THR   A 1 120 ? 9.111  11.094  18.570 0.72 15.01  ? 126 THR   A N   1 
ATOM   932  C  CA  . THR   A 1 120 ? 7.962  11.728  19.315 0.72 16.30  ? 126 THR   A CA  1 
ATOM   933  C  C   . THR   A 1 120 ? 7.238  10.741  20.249 0.72 17.57  ? 126 THR   A C   1 
ATOM   934  O  O   . THR   A 1 120 ? 7.452  9.534   20.108 0.72 16.38  ? 126 THR   A O   1 
ATOM   935  C  CB  . THR   A 1 120 ? 6.911  12.356  18.388 0.72 16.52  ? 126 THR   A CB  1 
ATOM   936  O  OG1 . THR   A 1 120 ? 6.121  11.362  17.744 0.72 16.60  ? 126 THR   A OG1 1 
ATOM   937  C  CG2 . THR   A 1 120 ? 7.504  13.219  17.302 0.72 16.29  ? 126 THR   A CG2 1 
ATOM   938  N  N   . GLY   A 1 121 ? 6.370  11.229  21.160 0.72 16.93  ? 127 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 121 ? 5.623  10.340  22.074 0.72 18.58  ? 127 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 121 ? 4.425  10.998  22.738 0.72 21.00  ? 127 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 121 ? 3.910  11.977  22.196 0.72 18.94  ? 127 GLY   A O   1 
ATOM   942  N  N   . GLY   A 1 122 ? 4.006  10.463  23.888 0.72 22.10  ? 128 GLY   A N   1 
ATOM   943  C  CA  . GLY   A 1 122 ? 2.860  10.975  24.671 0.72 23.56  ? 128 GLY   A CA  1 
ATOM   944  C  C   . GLY   A 1 122 ? 1.525  10.517  24.110 0.72 27.17  ? 128 GLY   A C   1 
ATOM   945  O  O   . GLY   A 1 122 ? 1.458  10.090  22.928 0.72 28.84  ? 128 GLY   A O   1 
ATOM   946  N  N   . ASN   A 1 123 ? 0.469  10.603  24.918 0.72 29.65  ? 129 ASN   A N   1 
ATOM   947  C  CA  . ASN   A 1 123 ? -0.926 10.385  24.450 0.72 31.60  ? 129 ASN   A CA  1 
ATOM   948  C  C   . ASN   A 1 123 ? -1.100 8.922   24.010 0.72 28.92  ? 129 ASN   A C   1 
ATOM   949  O  O   . ASN   A 1 123 ? -2.126 8.630   23.351 0.72 29.04  ? 129 ASN   A O   1 
ATOM   950  C  CB  . ASN   A 1 123 ? -1.298 11.358  23.319 0.72 33.69  ? 129 ASN   A CB  1 
ATOM   951  C  CG  . ASN   A 1 123 ? -1.311 12.818  23.732 0.72 36.49  ? 129 ASN   A CG  1 
ATOM   952  O  OD1 . ASN   A 1 123 ? -1.216 13.144  24.914 0.72 39.41  ? 129 ASN   A OD1 1 
ATOM   953  N  ND2 . ASN   A 1 123 ? -1.474 13.713  22.768 0.72 34.91  ? 129 ASN   A ND2 1 
ATOM   954  N  N   . GLY   A 1 124 ? -0.175 8.024   24.381 0.72 23.81  ? 130 GLY   A N   1 
ATOM   955  C  CA  . GLY   A 1 124 ? -0.167 6.623   23.930 0.72 21.45  ? 130 GLY   A CA  1 
ATOM   956  C  C   . GLY   A 1 124 ? 0.123  6.527   22.440 0.72 16.99  ? 130 GLY   A C   1 
ATOM   957  O  O   . GLY   A 1 124 ? -0.361 5.570   21.830 0.72 15.43  ? 130 GLY   A O   1 
ATOM   958  N  N   . LEU   A 1 125 ? 0.875  7.518   21.917 0.72 17.03  ? 131 LEU   A N   1 
ATOM   959  C  CA  . LEU   A 1 125 ? 1.478  7.511   20.549 0.72 16.10  ? 131 LEU   A CA  1 
ATOM   960  C  C   . LEU   A 1 125 ? 3.004  7.446   20.638 0.72 15.03  ? 131 LEU   A C   1 
ATOM   961  O  O   . LEU   A 1 125 ? 3.602  7.931   21.629 0.72 14.81  ? 131 LEU   A O   1 
ATOM   962  C  CB  . LEU   A 1 125 ? 1.050  8.747   19.761 0.72 15.93  ? 131 LEU   A CB  1 
ATOM   963  C  CG  . LEU   A 1 125 ? -0.461 8.853   19.556 0.72 16.34  ? 131 LEU   A CG  1 
ATOM   964  C  CD1 . LEU   A 1 125 ? -0.881 10.262  19.191 0.72 17.61  ? 131 LEU   A CD1 1 
ATOM   965  C  CD2 . LEU   A 1 125 ? -0.943 7.868   18.501 0.72 16.25  ? 131 LEU   A CD2 1 
ATOM   966  N  N   . VAL   A 1 126 ? 3.602  6.910   19.580 0.72 13.57  ? 132 VAL   A N   1 
ATOM   967  C  CA  . VAL   A 1 126 ? 5.068  6.983   19.358 0.72 13.01  ? 132 VAL   A CA  1 
ATOM   968  C  C   . VAL   A 1 126 ? 5.305  7.301   17.884 0.72 11.94  ? 132 VAL   A C   1 
ATOM   969  O  O   . VAL   A 1 126 ? 4.647  6.686   17.023 0.72 13.18  ? 132 VAL   A O   1 
ATOM   970  C  CB  . VAL   A 1 126 ? 5.743  5.679   19.804 0.72 12.80  ? 132 VAL   A CB  1 
ATOM   971  C  CG1 . VAL   A 1 126 ? 5.153  4.435   19.142 0.72 12.55  ? 132 VAL   A CG1 1 
ATOM   972  C  CG2 . VAL   A 1 126 ? 7.248  5.748   19.593 0.72 13.14  ? 132 VAL   A CG2 1 
ATOM   973  N  N   . GLY   A 1 127 ? 6.185  8.264   17.626 0.72 11.57  ? 133 GLY   A N   1 
ATOM   974  C  CA  . GLY   A 1 127 ? 6.570  8.679   16.270 0.72 11.40  ? 133 GLY   A CA  1 
ATOM   975  C  C   . GLY   A 1 127 ? 8.009  8.304   15.999 0.72 11.65  ? 133 GLY   A C   1 
ATOM   976  O  O   . GLY   A 1 127 ? 8.847  8.407   16.924 0.72 12.78  ? 133 GLY   A O   1 
ATOM   977  N  N   . PHE   A 1 128 ? 8.269  7.881   14.771 0.72 10.99  ? 134 PHE   A N   1 
ATOM   978  C  CA  . PHE   A 1 128 ? 9.626  7.449   14.325 0.72 11.03  ? 134 PHE   A CA  1 
ATOM   979  C  C   . PHE   A 1 128 ? 10.137 8.319   13.169 0.72 11.44  ? 134 PHE   A C   1 
ATOM   980  O  O   . PHE   A 1 128 ? 9.360  8.463   12.186 0.72 11.46  ? 134 PHE   A O   1 
ATOM   981  C  CB  . PHE   A 1 128 ? 9.558  5.979   13.917 0.72 10.76  ? 134 PHE   A CB  1 
ATOM   982  C  CG  . PHE   A 1 128 ? 8.942  5.074   14.959 0.72 10.75  ? 134 PHE   A CG  1 
ATOM   983  C  CD1 . PHE   A 1 128 ? 9.674  4.611   16.044 0.72 10.20  ? 134 PHE   A CD1 1 
ATOM   984  C  CD2 . PHE   A 1 128 ? 7.643  4.620   14.803 0.72 10.66  ? 134 PHE   A CD2 1 
ATOM   985  C  CE1 . PHE   A 1 128 ? 9.094  3.742   16.960 0.72 9.81   ? 134 PHE   A CE1 1 
ATOM   986  C  CE2 . PHE   A 1 128 ? 7.086  3.739   15.711 0.72 10.17  ? 134 PHE   A CE2 1 
ATOM   987  C  CZ  . PHE   A 1 128 ? 7.812  3.300   16.790 0.72 9.91   ? 134 PHE   A CZ  1 
ATOM   988  N  N   . ALA   A 1 129 ? 11.359 8.871   13.298 1.00 11.36  ? 135 ALA   A N   1 
ATOM   989  C  CA  . ALA   A 1 129 ? 12.024 9.548   12.159 1.00 11.85  ? 135 ALA   A CA  1 
ATOM   990  C  C   . ALA   A 1 129 ? 12.483 8.481   11.195 1.00 11.46  ? 135 ALA   A C   1 
ATOM   991  O  O   . ALA   A 1 129 ? 13.362 7.659   11.577 1.00 11.96  ? 135 ALA   A O   1 
ATOM   992  C  CB  . ALA   A 1 129 ? 13.100 10.417  12.694 1.00 11.27  ? 135 ALA   A CB  1 
ATOM   993  N  N   . ASP   A 1 130 ? 11.916 8.377   10.007 1.00 11.87  ? 136 ASP   A N   1 
ATOM   994  C  CA  . ASP   A 1 130 ? 12.319 7.429   8.953  1.00 12.92  ? 136 ASP   A CA  1 
ATOM   995  C  C   . ASP   A 1 130 ? 13.731 7.721   8.451  1.00 12.97  ? 136 ASP   A C   1 
ATOM   996  O  O   . ASP   A 1 130 ? 14.132 8.902   8.377  1.00 13.93  ? 136 ASP   A O   1 
ATOM   997  C  CB  . ASP   A 1 130 ? 11.322 7.473   7.793  1.00 14.64  ? 136 ASP   A CB  1 
ATOM   998  C  CG  . ASP   A 1 130 ? 11.606 6.448   6.764  1.00 17.82  ? 136 ASP   A CG  1 
ATOM   999  O  OD1 . ASP   A 1 130 ? 11.724 5.226   7.043  1.00 16.23  ? 136 ASP   A OD1 1 
ATOM   1000 O  OD2 . ASP   A 1 130 ? 11.872 6.965   5.633  1.00 25.76  ? 136 ASP   A OD2 1 
ATOM   1001 N  N   . VAL   A 1 131 ? 14.481 6.658   8.184  1.00 11.41  ? 137 VAL   A N   1 
ATOM   1002 C  CA  . VAL   A 1 131 ? 15.817 6.803   7.531  1.00 11.74  ? 137 VAL   A CA  1 
ATOM   1003 C  C   . VAL   A 1 131 ? 15.915 5.981   6.252  1.00 12.25  ? 137 VAL   A C   1 
ATOM   1004 O  O   . VAL   A 1 131 ? 17.003 5.980   5.606  1.00 11.51  ? 137 VAL   A O   1 
ATOM   1005 C  CB  . VAL   A 1 131 ? 16.972 6.470   8.491  1.00 10.89  ? 137 VAL   A CB  1 
ATOM   1006 C  CG1 . VAL   A 1 131 ? 17.013 7.370   9.724  1.00 11.79  ? 137 VAL   A CG1 1 
ATOM   1007 C  CG2 . VAL   A 1 131 ? 17.045 5.010   8.872  1.00 11.75  ? 137 VAL   A CG2 1 
ATOM   1008 N  N   . ARG   A 1 132 ? 14.843 5.313   5.827  1.00 12.35  ? 138 ARG   A N   1 
ATOM   1009 C  CA  . ARG   A 1 132 ? 14.943 4.376   4.688  1.00 12.05  ? 138 ARG   A CA  1 
ATOM   1010 C  C   . ARG   A 1 132 ? 15.194 5.076   3.334  1.00 13.21  ? 138 ARG   A C   1 
ATOM   1011 O  O   . ARG   A 1 132 ? 15.686 4.366   2.410  1.00 14.54  ? 138 ARG   A O   1 
ATOM   1012 C  CB  . ARG   A 1 132 ? 13.684 3.517   4.610  1.00 13.09  ? 138 ARG   A CB  1 
ATOM   1013 C  CG  . ARG   A 1 132 ? 13.546 2.549   5.793  1.00 12.86  ? 138 ARG   A CG  1 
ATOM   1014 C  CD  . ARG   A 1 132 ? 12.249 1.761   5.629  1.00 13.38  ? 138 ARG   A CD  1 
ATOM   1015 N  NE  . ARG   A 1 132 ? 11.100 2.596   5.874  1.00 13.65  ? 138 ARG   A NE  1 
ATOM   1016 C  CZ  . ARG   A 1 132 ? 9.827  2.186   5.985  1.00 13.81  ? 138 ARG   A CZ  1 
ATOM   1017 N  NH1 . ARG   A 1 132 ? 9.491  0.964   5.693  1.00 17.67  ? 138 ARG   A NH1 1 
ATOM   1018 N  NH2 . ARG   A 1 132 ? 8.935  3.108   6.301  1.00 16.50  ? 138 ARG   A NH2 1 
ATOM   1019 N  N   . ASP   A 1 133 ? 14.877 6.355   3.220  1.00 13.78  ? 139 ASP   A N   1 
ATOM   1020 C  CA  . ASP   A 1 133 ? 15.164 7.083   1.949  1.00 15.20  ? 139 ASP   A CA  1 
ATOM   1021 C  C   . ASP   A 1 133 ? 16.610 7.597   1.895  1.00 15.87  ? 139 ASP   A C   1 
ATOM   1022 O  O   . ASP   A 1 133 ? 16.987 8.067   0.821  1.00 15.95  ? 139 ASP   A O   1 
ATOM   1023 C  CB  . ASP   A 1 133 ? 14.199 8.262   1.810  1.00 16.68  ? 139 ASP   A CB  1 
ATOM   1024 C  CG  . ASP   A 1 133 ? 14.387 9.313   2.895  1.00 18.39  ? 139 ASP   A CG  1 
ATOM   1025 O  OD1 . ASP   A 1 133 ? 14.463 8.949   4.127  1.00 18.22  ? 139 ASP   A OD1 1 
ATOM   1026 O  OD2 . ASP   A 1 133 ? 14.435 10.512  2.615  1.00 21.54  ? 139 ASP   A OD2 1 
ATOM   1027 N  N   . LEU   A 1 134 ? 17.386 7.574   2.975  1.00 12.96  ? 140 LEU   A N   1 
ATOM   1028 C  CA  . LEU   A 1 134 ? 18.772 8.095   3.021  1.00 13.11  ? 140 LEU   A CA  1 
ATOM   1029 C  C   . LEU   A 1 134 ? 19.713 7.011   2.472  1.00 12.50  ? 140 LEU   A C   1 
ATOM   1030 O  O   . LEU   A 1 134 ? 20.380 6.298   3.200  1.00 12.15  ? 140 LEU   A O   1 
ATOM   1031 C  CB  . LEU   A 1 134 ? 19.109 8.535   4.457  1.00 12.58  ? 140 LEU   A CB  1 
ATOM   1032 C  CG  . LEU   A 1 134 ? 18.139 9.545   5.084  1.00 14.27  ? 140 LEU   A CG  1 
ATOM   1033 C  CD1 . LEU   A 1 134 ? 18.502 9.767   6.539  1.00 14.64  ? 140 LEU   A CD1 1 
ATOM   1034 C  CD2 . LEU   A 1 134 ? 18.091 10.846  4.327  1.00 14.93  ? 140 LEU   A CD2 1 
ATOM   1035 N  N   . LEU   A 1 135 ? 19.787 6.898   1.141  1.00 12.35  ? 141 LEU   A N   1 
ATOM   1036 C  CA  . LEU   A 1 135 ? 20.506 5.801   0.470  1.00 12.94  ? 141 LEU   A CA  1 
ATOM   1037 C  C   . LEU   A 1 135 ? 22.010 5.937   0.678  1.00 12.69  ? 141 LEU   A C   1 
ATOM   1038 O  O   . LEU   A 1 135 ? 22.689 4.906   0.764  1.00 14.95  ? 141 LEU   A O   1 
ATOM   1039 C  CB  . LEU   A 1 135 ? 20.160 5.725   -1.034 1.00 14.72  ? 141 LEU   A CB  1 
ATOM   1040 C  CG  . LEU   A 1 135 ? 18.660 5.695   -1.346 1.00 16.15  ? 141 LEU   A CG  1 
ATOM   1041 C  CD1 . LEU   A 1 135 ? 18.451 5.351   -2.819 1.00 17.86  ? 141 LEU   A CD1 1 
ATOM   1042 C  CD2 . LEU   A 1 135 ? 17.852 4.729   -0.492 1.00 17.20  ? 141 LEU   A CD2 1 
ATOM   1043 N  N   . TRP   A 1 136 ? 22.463 7.176   0.876  1.00 13.12  ? 142 TRP   A N   1 
ATOM   1044 C  CA  . TRP   A 1 136 ? 23.897 7.441   1.065  1.00 12.95  ? 142 TRP   A CA  1 
ATOM   1045 C  C   . TRP   A 1 136 ? 24.415 6.840   2.365  1.00 13.66  ? 142 TRP   A C   1 
ATOM   1046 O  O   . TRP   A 1 136 ? 25.636 6.676   2.485  1.00 14.79  ? 142 TRP   A O   1 
ATOM   1047 C  CB  . TRP   A 1 136 ? 24.152 8.936   0.948  1.00 13.35  ? 142 TRP   A CB  1 
ATOM   1048 C  CG  . TRP   A 1 136 ? 23.381 9.762   1.904  1.00 13.35  ? 142 TRP   A CG  1 
ATOM   1049 C  CD1 . TRP   A 1 136 ? 22.243 10.446  1.592  1.00 13.94  ? 142 TRP   A CD1 1 
ATOM   1050 C  CD2 . TRP   A 1 136 ? 23.713 10.082  3.270  1.00 13.44  ? 142 TRP   A CD2 1 
ATOM   1051 N  NE1 . TRP   A 1 136 ? 21.780 11.108  2.704  1.00 16.04  ? 142 TRP   A NE1 1 
ATOM   1052 C  CE2 . TRP   A 1 136 ? 22.695 10.955  3.712  1.00 14.28  ? 142 TRP   A CE2 1 
ATOM   1053 C  CE3 . TRP   A 1 136 ? 24.757 9.770   4.133  1.00 14.39  ? 142 TRP   A CE3 1 
ATOM   1054 C  CZ2 . TRP   A 1 136 ? 22.680 11.469  5.021  1.00 15.17  ? 142 TRP   A CZ2 1 
ATOM   1055 C  CZ3 . TRP   A 1 136 ? 24.761 10.313  5.406  1.00 15.59  ? 142 TRP   A CZ3 1 
ATOM   1056 C  CH2 . TRP   A 1 136 ? 23.730 11.136  5.824  1.00 13.91  ? 142 TRP   A CH2 1 
ATOM   1057 N  N   . LEU   A 1 137 ? 23.562 6.494   3.352  1.00 13.49  ? 143 LEU   A N   1 
ATOM   1058 C  CA  . LEU   A 1 137 ? 24.048 5.841   4.597  1.00 14.37  ? 143 LEU   A CA  1 
ATOM   1059 C  C   . LEU   A 1 137 ? 24.762 4.524   4.269  1.00 15.91  ? 143 LEU   A C   1 
ATOM   1060 O  O   . LEU   A 1 137 ? 25.581 4.078   5.095  1.00 17.66  ? 143 LEU   A O   1 
ATOM   1061 C  CB  . LEU   A 1 137 ? 22.886 5.576   5.544  1.00 14.36  ? 143 LEU   A CB  1 
ATOM   1062 C  CG  . LEU   A 1 137 ? 22.339 6.809   6.247  1.00 14.08  ? 143 LEU   A CG  1 
ATOM   1063 C  CD1 . LEU   A 1 137 ? 21.113 6.468   7.042  1.00 14.92  ? 143 LEU   A CD1 1 
ATOM   1064 C  CD2 . LEU   A 1 137 ? 23.383 7.420   7.182  1.00 15.30  ? 143 LEU   A CD2 1 
ATOM   1065 N  N   . ASP   A 1 138 ? 24.492 3.929   3.098  1.00 19.12  ? 144 ASP   A N   1 
ATOM   1066 C  CA  . ASP   A 1 138 ? 25.056 2.596   2.710  1.00 22.70  ? 144 ASP   A CA  1 
ATOM   1067 C  C   . ASP   A 1 138 ? 26.403 2.690   1.982  1.00 27.44  ? 144 ASP   A C   1 
ATOM   1068 O  O   . ASP   A 1 138 ? 26.962 1.619   1.654  1.00 28.72  ? 144 ASP   A O   1 
ATOM   1069 C  CB  . ASP   A 1 138 ? 24.132 1.822   1.765  1.00 23.89  ? 144 ASP   A CB  1 
ATOM   1070 C  CG  . ASP   A 1 138 ? 22.776 1.494   2.323  1.00 24.29  ? 144 ASP   A CG  1 
ATOM   1071 O  OD1 . ASP   A 1 138 ? 22.613 1.553   3.581  1.00 28.20  ? 144 ASP   A OD1 1 
ATOM   1072 O  OD2 . ASP   A 1 138 ? 21.860 1.226   1.508  1.00 33.59  ? 144 ASP   A OD2 1 
ATOM   1073 N  N   . GLU   A 1 139 ? 26.954 3.875   1.715  1.00 31.19  ? 145 GLU   A N   1 
ATOM   1074 C  CA  . GLU   A 1 139 ? 28.282 3.917   1.014  1.00 40.62  ? 145 GLU   A CA  1 
ATOM   1075 C  C   . GLU   A 1 139 ? 29.188 5.031   1.547  1.00 42.29  ? 145 GLU   A C   1 
ATOM   1076 O  O   . GLU   A 1 139 ? 28.761 5.752   2.463  1.00 34.68  ? 145 GLU   A O   1 
ATOM   1077 C  CB  . GLU   A 1 139 ? 28.131 4.033   -0.502 1.00 49.90  ? 145 GLU   A CB  1 
ATOM   1078 C  CG  . GLU   A 1 139 ? 27.370 5.257   -0.964 1.00 54.93  ? 145 GLU   A CG  1 
ATOM   1079 C  CD  . GLU   A 1 139 ? 25.936 4.959   -1.347 1.00 59.31  ? 145 GLU   A CD  1 
ATOM   1080 O  OE1 . GLU   A 1 139 ? 25.358 5.737   -2.139 1.00 63.12  ? 145 GLU   A OE1 1 
ATOM   1081 O  OE2 . GLU   A 1 139 ? 25.400 3.948   -0.849 1.00 64.37  ? 145 GLU   A OE2 1 
ATOM   1082 N  N   . GLU   A 1 140 ? 30.413 5.082   0.996  1.00 48.60  ? 146 GLU   A N   1 
ATOM   1083 C  CA  . GLU   A 1 140 ? 31.448 6.154   1.115  1.00 55.34  ? 146 GLU   A CA  1 
ATOM   1084 C  C   . GLU   A 1 140 ? 32.244 5.896   2.392  1.00 54.79  ? 146 GLU   A C   1 
ATOM   1085 O  O   . GLU   A 1 140 ? 33.239 5.190   2.223  1.00 57.86  ? 146 GLU   A O   1 
ATOM   1086 C  CB  . GLU   A 1 140 ? 30.850 7.562   1.008  1.00 54.97  ? 146 GLU   A CB  1 
ATOM   1087 C  CG  . GLU   A 1 140 ? 31.503 8.615   1.902  1.00 63.03  ? 146 GLU   A CG  1 
ATOM   1088 C  CD  . GLU   A 1 140 ? 31.962 9.870   1.168  1.00 63.18  ? 146 GLU   A CD  1 
ATOM   1089 O  OE1 . GLU   A 1 140 ? 31.108 10.718  0.817  1.00 64.22  ? 146 GLU   A OE1 1 
ATOM   1090 O  OE2 . GLU   A 1 140 ? 33.177 9.979   0.918  1.00 66.77  ? 146 GLU   A OE2 1 
ATOM   1091 N  N   . SER   B 1 1   ? 21.921 -21.291 7.662  1.00 19.09  ? 7   SER   C N   1 
ATOM   1092 C  CA  . SER   B 1 1   ? 20.775 -21.092 8.585  1.00 18.96  ? 7   SER   C CA  1 
ATOM   1093 C  C   . SER   B 1 1   ? 20.753 -22.197 9.650  1.00 16.73  ? 7   SER   C C   1 
ATOM   1094 O  O   . SER   B 1 1   ? 21.427 -23.265 9.459  1.00 19.34  ? 7   SER   C O   1 
ATOM   1095 C  CB  . SER   B 1 1   ? 19.490 -21.128 7.811  1.00 21.93  ? 7   SER   C CB  1 
ATOM   1096 O  OG  . SER   B 1 1   ? 19.339 -22.400 7.209  1.00 23.13  ? 7   SER   C OG  1 
ATOM   1097 N  N   . GLY   B 1 2   ? 19.993 -21.977 10.721 1.00 16.86  ? 8   GLY   C N   1 
ATOM   1098 C  CA  . GLY   B 1 2   ? 19.815 -22.996 11.774 1.00 16.32  ? 8   GLY   C CA  1 
ATOM   1099 C  C   . GLY   B 1 2   ? 19.530 -22.374 13.115 1.00 14.35  ? 8   GLY   C C   1 
ATOM   1100 O  O   . GLY   B 1 2   ? 19.915 -21.228 13.379 1.00 16.01  ? 8   GLY   C O   1 
ATOM   1101 N  N   . ALA   B 1 3   ? 18.881 -23.100 13.998 1.00 13.98  ? 9   ALA   C N   1 
ATOM   1102 C  CA  . ALA   B 1 3   ? 18.527 -22.632 15.342 1.00 13.24  ? 9   ALA   C CA  1 
ATOM   1103 C  C   . ALA   B 1 3   ? 18.663 -23.764 16.363 1.00 11.63  ? 9   ALA   C C   1 
ATOM   1104 O  O   . ALA   B 1 3   ? 18.715 -24.966 15.979 1.00 13.27  ? 9   ALA   C O   1 
ATOM   1105 C  CB  . ALA   B 1 3   ? 17.135 -22.086 15.310 1.00 15.52  ? 9   ALA   C CB  1 
ATOM   1106 N  N   . ILE   B 1 4   ? 18.623 -23.363 17.615 1.00 12.12  ? 10  ILE   C N   1 
ATOM   1107 C  CA  . ILE   B 1 4   ? 18.566 -24.293 18.765 1.00 13.10  ? 10  ILE   C CA  1 
ATOM   1108 C  C   . ILE   B 1 4   ? 17.161 -24.120 19.346 1.00 13.20  ? 10  ILE   C C   1 
ATOM   1109 O  O   . ILE   B 1 4   ? 16.758 -22.948 19.572 1.00 13.41  ? 10  ILE   C O   1 
ATOM   1110 C  CB  . ILE   B 1 4   ? 19.617 -23.988 19.834 1.00 12.54  ? 10  ILE   C CB  1 
ATOM   1111 C  CG1 . ILE   B 1 4   ? 21.040 -23.811 19.281 1.00 13.53  ? 10  ILE   C CG1 1 
ATOM   1112 C  CG2 . ILE   B 1 4   ? 19.562 -25.040 20.905 1.00 13.73  ? 10  ILE   C CG2 1 
ATOM   1113 C  CD1 . ILE   B 1 4   ? 21.990 -23.212 20.283 1.00 13.35  ? 10  ILE   C CD1 1 
ATOM   1114 N  N   . TYR   B 1 5   ? 16.479 -25.203 19.672 1.00 12.26  ? 11  TYR   C N   1 
ATOM   1115 C  CA  . TYR   B 1 5   ? 15.123 -25.173 20.249 1.00 13.17  ? 11  TYR   C CA  1 
ATOM   1116 C  C   . TYR   B 1 5   ? 15.203 -25.819 21.619 1.00 13.88  ? 11  TYR   C C   1 
ATOM   1117 O  O   . TYR   B 1 5   ? 15.320 -27.068 21.663 1.00 15.45  ? 11  TYR   C O   1 
ATOM   1118 C  CB  . TYR   B 1 5   ? 14.123 -25.865 19.333 1.00 14.02  ? 11  TYR   C CB  1 
ATOM   1119 C  CG  . TYR   B 1 5   ? 13.903 -25.113 18.054 1.00 15.50  ? 11  TYR   C CG  1 
ATOM   1120 C  CD1 . TYR   B 1 5   ? 13.126 -23.975 18.014 1.00 14.80  ? 11  TYR   C CD1 1 
ATOM   1121 C  CD2 . TYR   B 1 5   ? 14.571 -25.456 16.902 1.00 15.06  ? 11  TYR   C CD2 1 
ATOM   1122 C  CE1 . TYR   B 1 5   ? 12.983 -23.234 16.852 1.00 16.51  ? 11  TYR   C CE1 1 
ATOM   1123 C  CE2 . TYR   B 1 5   ? 14.458 -24.735 15.729 1.00 16.83  ? 11  TYR   C CE2 1 
ATOM   1124 C  CZ  . TYR   B 1 5   ? 13.639 -23.631 15.711 1.00 16.51  ? 11  TYR   C CZ  1 
ATOM   1125 O  OH  . TYR   B 1 5   ? 13.576 -22.898 14.556 1.00 19.84  ? 11  TYR   C OH  1 
ATOM   1126 N  N   . VAL   B 1 6   ? 15.226 -25.056 22.687 1.00 14.22  ? 12  VAL   C N   1 
ATOM   1127 C  CA  . VAL   B 1 6   ? 15.298 -25.599 24.073 1.00 15.10  ? 12  VAL   C CA  1 
ATOM   1128 C  C   . VAL   B 1 6   ? 14.132 -25.006 24.868 1.00 16.05  ? 12  VAL   C C   1 
ATOM   1129 O  O   . VAL   B 1 6   ? 13.972 -23.776 24.905 1.00 14.25  ? 12  VAL   C O   1 
ATOM   1130 C  CB  . VAL   B 1 6   ? 16.681 -25.344 24.710 1.00 15.56  ? 12  VAL   C CB  1 
ATOM   1131 C  CG1 . VAL   B 1 6   ? 17.096 -23.860 24.701 1.00 15.56  ? 12  VAL   C CG1 1 
ATOM   1132 C  CG2 . VAL   B 1 6   ? 16.674 -25.887 26.109 1.00 17.23  ? 12  VAL   C CG2 1 
ATOM   1133 N  N   . GLY   B 1 7   ? 13.337 -25.842 25.551 1.00 17.25  ? 13  GLY   C N   1 
ATOM   1134 C  CA  . GLY   B 1 7   ? 12.194 -25.323 26.289 1.00 17.15  ? 13  GLY   C CA  1 
ATOM   1135 C  C   . GLY   B 1 7   ? 11.304 -24.459 25.413 1.00 15.62  ? 13  GLY   C C   1 
ATOM   1136 O  O   . GLY   B 1 7   ? 11.006 -24.867 24.301 1.00 16.96  ? 13  GLY   C O   1 
ATOM   1137 N  N   . ASN   B 1 8   ? 10.939 -23.288 25.882 1.00 16.94  ? 14  ASN   C N   1 
ATOM   1138 C  CA  . ASN   B 1 8   ? 10.152 -22.345 25.054 1.00 18.99  ? 14  ASN   C CA  1 
ATOM   1139 C  C   . ASN   B 1 8   ? 11.068 -21.241 24.535 1.00 16.50  ? 14  ASN   C C   1 
ATOM   1140 O  O   . ASN   B 1 8   ? 10.602 -20.121 24.338 1.00 16.19  ? 14  ASN   C O   1 
ATOM   1141 C  CB  . ASN   B 1 8   ? 8.928  -21.800 25.792 1.00 20.57  ? 14  ASN   C CB  1 
ATOM   1142 C  CG  . ASN   B 1 8   ? 7.845  -22.858 25.903 1.00 26.90  ? 14  ASN   C CG  1 
ATOM   1143 O  OD1 . ASN   B 1 8   ? 6.962  -22.939 25.057 1.00 29.67  ? 14  ASN   C OD1 1 
ATOM   1144 N  ND2 . ASN   B 1 8   ? 8.011  -23.765 26.841 1.00 27.94  ? 14  ASN   C ND2 1 
ATOM   1145 N  N   . TYR   B 1 9   ? 12.274 -21.622 24.149 1.00 14.49  ? 15  TYR   C N   1 
ATOM   1146 C  CA  . TYR   B 1 9   ? 13.278 -20.667 23.565 1.00 14.63  ? 15  TYR   C CA  1 
ATOM   1147 C  C   . TYR   B 1 9   ? 13.765 -21.133 22.193 1.00 13.70  ? 15  TYR   C C   1 
ATOM   1148 O  O   . TYR   B 1 9   ? 13.906 -22.343 21.966 1.00 14.38  ? 15  TYR   C O   1 
ATOM   1149 C  CB  . TYR   B 1 9   ? 14.486 -20.496 24.474 1.00 14.67  ? 15  TYR   C CB  1 
ATOM   1150 C  CG  . TYR   B 1 9   ? 14.197 -19.992 25.869 1.00 15.10  ? 15  TYR   C CG  1 
ATOM   1151 C  CD1 . TYR   B 1 9   ? 13.660 -18.727 26.068 1.00 16.49  ? 15  TYR   C CD1 1 
ATOM   1152 C  CD2 . TYR   B 1 9   ? 14.474 -20.760 26.990 1.00 16.43  ? 15  TYR   C CD2 1 
ATOM   1153 C  CE1 . TYR   B 1 9   ? 13.401 -18.238 27.346 1.00 19.37  ? 15  TYR   C CE1 1 
ATOM   1154 C  CE2 . TYR   B 1 9   ? 14.256 -20.257 28.273 1.00 19.44  ? 15  TYR   C CE2 1 
ATOM   1155 C  CZ  . TYR   B 1 9   ? 13.702 -19.003 28.442 1.00 21.88  ? 15  TYR   C CZ  1 
ATOM   1156 O  OH  . TYR   B 1 9   ? 13.454 -18.489 29.698 1.00 27.70  ? 15  TYR   C OH  1 
ATOM   1157 N  N   . ARG   B 1 10  ? 13.968 -20.174 21.275 1.00 12.74  ? 16  ARG   C N   1 
ATOM   1158 C  CA  . ARG   B 1 10  ? 14.598 -20.370 19.949 1.00 12.75  ? 16  ARG   C CA  1 
ATOM   1159 C  C   . ARG   B 1 10  ? 15.862 -19.503 19.957 1.00 13.57  ? 16  ARG   C C   1 
ATOM   1160 O  O   . ARG   B 1 10  ? 15.790 -18.278 20.203 1.00 12.89  ? 16  ARG   C O   1 
ATOM   1161 C  CB  . ARG   B 1 10  ? 13.659 -19.940 18.805 1.00 14.50  ? 16  ARG   C CB  1 
ATOM   1162 C  CG  . ARG   B 1 10  ? 14.282 -19.795 17.426 1.00 14.33  ? 16  ARG   C CG  1 
ATOM   1163 C  CD  . ARG   B 1 10  ? 13.205 -19.466 16.404 1.00 14.69  ? 16  ARG   C CD  1 
ATOM   1164 N  NE  . ARG   B 1 10  ? 13.622 -18.566 15.332 1.00 15.45  ? 16  ARG   C NE  1 
ATOM   1165 C  CZ  . ARG   B 1 10  ? 14.166 -18.877 14.164 1.00 14.91  ? 16  ARG   C CZ  1 
ATOM   1166 N  NH1 . ARG   B 1 10  ? 14.386 -20.133 13.785 1.00 17.24  ? 16  ARG   C NH1 1 
ATOM   1167 N  NH2 . ARG   B 1 10  ? 14.479 -17.901 13.326 1.00 17.11  ? 16  ARG   C NH2 1 
ATOM   1168 N  N   . VAL   B 1 11  ? 17.032 -20.113 19.759 1.00 12.11  ? 17  VAL   C N   1 
ATOM   1169 C  CA  . VAL   B 1 11  ? 18.337 -19.406 19.688 1.00 11.30  ? 17  VAL   C CA  1 
ATOM   1170 C  C   . VAL   B 1 11  ? 18.811 -19.374 18.251 1.00 11.06  ? 17  VAL   C C   1 
ATOM   1171 O  O   . VAL   B 1 11  ? 18.952 -20.435 17.621 1.00 11.66  ? 17  VAL   C O   1 
ATOM   1172 C  CB  . VAL   B 1 11  ? 19.402 -20.123 20.545 1.00 12.25  ? 17  VAL   C CB  1 
ATOM   1173 C  CG1 . VAL   B 1 11  ? 20.623 -19.255 20.648 1.00 13.54  ? 17  VAL   C CG1 1 
ATOM   1174 C  CG2 . VAL   B 1 11  ? 18.852 -20.528 21.890 1.00 13.61  ? 17  VAL   C CG2 1 
ATOM   1175 N  N   A VAL   B 1 12  ? 19.030 -18.169 17.701 0.25 10.35  ? 18  VAL   C N   1 
ATOM   1176 N  N   B VAL   B 1 12  ? 19.104 -18.167 17.751 0.25 12.13  ? 18  VAL   C N   1 
ATOM   1177 C  CA  A VAL   B 1 12  ? 19.504 -17.962 16.302 0.25 10.17  ? 18  VAL   C CA  1 
ATOM   1178 C  CA  B VAL   B 1 12  ? 19.468 -17.907 16.331 0.25 13.00  ? 18  VAL   C CA  1 
ATOM   1179 C  C   A VAL   B 1 12  ? 20.645 -16.935 16.276 0.25 10.17  ? 18  VAL   C C   1 
ATOM   1180 C  C   B VAL   B 1 12  ? 20.627 -16.902 16.269 0.25 11.72  ? 18  VAL   C C   1 
ATOM   1181 O  O   A VAL   B 1 12  ? 20.835 -16.184 17.265 0.25 10.87  ? 18  VAL   C O   1 
ATOM   1182 O  O   B VAL   B 1 12  ? 20.801 -16.110 17.236 0.25 12.37  ? 18  VAL   C O   1 
ATOM   1183 C  CB  A VAL   B 1 12  ? 18.370 -17.471 15.377 0.25 9.47   ? 18  VAL   C CB  1 
ATOM   1184 C  CB  B VAL   B 1 12  ? 18.252 -17.341 15.575 0.25 14.53  ? 18  VAL   C CB  1 
ATOM   1185 C  CG1 A VAL   B 1 12  ? 17.383 -18.584 15.082 0.25 9.15   ? 18  VAL   C CG1 1 
ATOM   1186 C  CG1 B VAL   B 1 12  ? 18.396 -17.503 14.077 0.25 14.99  ? 18  VAL   C CG1 1 
ATOM   1187 C  CG2 A VAL   B 1 12  ? 17.691 -16.201 15.912 0.25 8.64   ? 18  VAL   C CG2 1 
ATOM   1188 C  CG2 B VAL   B 1 12  ? 16.956 -17.946 16.059 0.25 16.54  ? 18  VAL   C CG2 1 
ATOM   1189 N  N   . ASN   B 1 13  ? 21.363 -16.896 15.151 1.00 10.83  ? 19  ASN   C N   1 
ATOM   1190 C  CA  . ASN   B 1 13  ? 22.343 -15.834 14.897 1.00 11.04  ? 19  ASN   C CA  1 
ATOM   1191 C  C   . ASN   B 1 13  ? 21.544 -14.507 14.889 1.00 11.34  ? 19  ASN   C C   1 
ATOM   1192 O  O   . ASN   B 1 13  ? 20.537 -14.457 14.175 1.00 11.33  ? 19  ASN   C O   1 
ATOM   1193 C  CB  . ASN   B 1 13  ? 23.055 -16.028 13.557 1.00 11.28  ? 19  ASN   C CB  1 
ATOM   1194 C  CG  . ASN   B 1 13  ? 23.884 -17.303 13.504 1.00 10.50  ? 19  ASN   C CG  1 
ATOM   1195 O  OD1 . ASN   B 1 13  ? 23.405 -18.356 13.040 1.00 11.66  ? 19  ASN   C OD1 1 
ATOM   1196 N  ND2 . ASN   B 1 13  ? 25.106 -17.179 13.953 1.00 12.05  ? 19  ASN   C ND2 1 
ATOM   1197 N  N   . ARG   B 1 14  ? 22.038 -13.498 15.596 1.00 11.56  ? 20  ARG   C N   1 
ATOM   1198 C  CA  . ARG   B 1 14  ? 21.327 -12.182 15.608 1.00 11.13  ? 20  ARG   C CA  1 
ATOM   1199 C  C   . ARG   B 1 14  ? 21.162 -11.698 14.161 1.00 12.58  ? 20  ARG   C C   1 
ATOM   1200 O  O   . ARG   B 1 14  ? 20.091 -11.140 13.808 1.00 13.09  ? 20  ARG   C O   1 
ATOM   1201 C  CB  . ARG   B 1 14  ? 22.048 -11.177 16.478 1.00 11.43  ? 20  ARG   C CB  1 
ATOM   1202 C  CG  . ARG   B 1 14  ? 21.252 -9.875  16.639 1.00 11.96  ? 20  ARG   C CG  1 
ATOM   1203 C  CD  . ARG   B 1 14  ? 22.056 -8.892  17.421 1.00 12.76  ? 20  ARG   C CD  1 
ATOM   1204 N  NE  . ARG   B 1 14  ? 21.417 -7.644  17.866 1.00 13.50  ? 20  ARG   C NE  1 
ATOM   1205 C  CZ  . ARG   B 1 14  ? 21.314 -6.548  17.100 1.00 12.65  ? 20  ARG   C CZ  1 
ATOM   1206 N  NH1 . ARG   B 1 14  ? 21.672 -6.574  15.839 1.00 13.39  ? 20  ARG   C NH1 1 
ATOM   1207 N  NH2 . ARG   B 1 14  ? 20.824 -5.439  17.625 1.00 13.53  ? 20  ARG   C NH2 1 
ATOM   1208 N  N   . HIS   B 1 15  ? 22.143 -11.891 13.278 1.00 12.01  ? 21  HIS   C N   1 
ATOM   1209 C  CA  . HIS   B 1 15  ? 22.079 -11.326 11.909 1.00 12.24  ? 21  HIS   C CA  1 
ATOM   1210 C  C   . HIS   B 1 15  ? 21.067 -12.054 11.016 1.00 14.18  ? 21  HIS   C C   1 
ATOM   1211 O  O   . HIS   B 1 15  ? 20.755 -11.525 9.929  1.00 15.53  ? 21  HIS   C O   1 
ATOM   1212 C  CB  . HIS   B 1 15  ? 23.478 -11.218 11.260 1.00 12.66  ? 21  HIS   C CB  1 
ATOM   1213 C  CG  . HIS   B 1 15  ? 24.058 -12.515 10.806 1.00 12.51  ? 21  HIS   C CG  1 
ATOM   1214 N  ND1 . HIS   B 1 15  ? 24.767 -13.340 11.665 1.00 13.15  ? 21  HIS   C ND1 1 
ATOM   1215 C  CD2 . HIS   B 1 15  ? 24.050 -13.100 9.589  1.00 13.16  ? 21  HIS   C CD2 1 
ATOM   1216 C  CE1 . HIS   B 1 15  ? 25.163 -14.393 10.960 1.00 14.29  ? 21  HIS   C CE1 1 
ATOM   1217 N  NE2 . HIS   B 1 15  ? 24.734 -14.299 9.695  1.00 13.81  ? 21  HIS   C NE2 1 
ATOM   1218 N  N   . LEU   B 1 16  ? 20.534 -13.213 11.437 1.00 12.49  ? 22  LEU   C N   1 
ATOM   1219 C  CA  . LEU   B 1 16  ? 19.496 -13.987 10.693 1.00 13.57  ? 22  LEU   C CA  1 
ATOM   1220 C  C   . LEU   B 1 16  ? 18.120 -13.895 11.388 1.00 12.57  ? 22  LEU   C C   1 
ATOM   1221 O  O   . LEU   B 1 16  ? 17.192 -14.632 10.947 1.00 15.21  ? 22  LEU   C O   1 
ATOM   1222 C  CB  . LEU   B 1 16  ? 19.969 -15.428 10.488 1.00 13.32  ? 22  LEU   C CB  1 
ATOM   1223 C  CG  . LEU   B 1 16  ? 21.269 -15.583 9.708  1.00 13.12  ? 22  LEU   C CG  1 
ATOM   1224 C  CD1 . LEU   B 1 16  ? 21.707 -17.053 9.679  1.00 14.65  ? 22  LEU   C CD1 1 
ATOM   1225 C  CD2 . LEU   B 1 16  ? 21.181 -14.974 8.328  1.00 13.86  ? 22  LEU   C CD2 1 
ATOM   1226 N  N   . ALA   B 1 17  ? 17.985 -13.153 12.483 1.00 13.64  ? 23  ALA   C N   1 
ATOM   1227 C  CA  . ALA   B 1 17  ? 16.708 -13.064 13.243 1.00 13.79  ? 23  ALA   C CA  1 
ATOM   1228 C  C   . ALA   B 1 17  ? 15.599 -12.529 12.327 1.00 15.03  ? 23  ALA   C C   1 
ATOM   1229 O  O   . ALA   B 1 17  ? 15.840 -11.580 11.513 1.00 16.36  ? 23  ALA   C O   1 
ATOM   1230 C  CB  . ALA   B 1 17  ? 16.844 -12.216 14.462 1.00 14.61  ? 23  ALA   C CB  1 
ATOM   1231 N  N   . THR   B 1 18  ? 14.404 -13.076 12.501 1.00 14.44  ? 24  THR   C N   1 
ATOM   1232 C  CA  . THR   B 1 18  ? 13.223 -12.683 11.703 1.00 16.20  ? 24  THR   C CA  1 
ATOM   1233 C  C   . THR   B 1 18  ? 12.432 -11.598 12.444 1.00 14.27  ? 24  THR   C C   1 
ATOM   1234 O  O   . THR   B 1 18  ? 12.662 -11.260 13.630 1.00 14.66  ? 24  THR   C O   1 
ATOM   1235 C  CB  . THR   B 1 18  ? 12.314 -13.903 11.449 1.00 16.94  ? 24  THR   C CB  1 
ATOM   1236 O  OG1 . THR   B 1 18  ? 11.807 -14.284 12.723 1.00 15.93  ? 24  THR   C OG1 1 
ATOM   1237 C  CG2 . THR   B 1 18  ? 13.003 -15.072 10.776 1.00 18.05  ? 24  THR   C CG2 1 
ATOM   1238 N  N   . HIS   B 1 19  ? 11.431 -11.004 11.753 1.00 17.13  ? 25  HIS   C N   1 
ATOM   1239 C  CA  . HIS   B 1 19  ? 10.458 -10.112 12.441 1.00 19.19  ? 25  HIS   C CA  1 
ATOM   1240 C  C   . HIS   B 1 19  ? 9.781  -10.836 13.607 1.00 13.66  ? 25  HIS   C C   1 
ATOM   1241 O  O   . HIS   B 1 19  ? 9.727  -10.267 14.690 1.00 16.46  ? 25  HIS   C O   1 
ATOM   1242 C  CB  . HIS   B 1 19  ? 9.396  -9.577  11.462 1.00 19.76  ? 25  HIS   C CB  1 
ATOM   1243 C  CG  . HIS   B 1 19  ? 8.244  -8.900  12.159 1.00 20.46  ? 25  HIS   C CG  1 
ATOM   1244 N  ND1 . HIS   B 1 19  ? 8.334  -7.615  12.677 1.00 23.76  ? 25  HIS   C ND1 1 
ATOM   1245 C  CD2 . HIS   B 1 19  ? 7.034  -9.350  12.568 1.00 22.58  ? 25  HIS   C CD2 1 
ATOM   1246 C  CE1 . HIS   B 1 19  ? 7.210  -7.265  13.269 1.00 22.97  ? 25  HIS   C CE1 1 
ATOM   1247 N  NE2 . HIS   B 1 19  ? 6.391  -8.327  13.241 1.00 22.45  ? 25  HIS   C NE2 1 
ATOM   1248 N  N   . ASN   B 1 20  ? 9.371  -12.076 13.413 1.00 16.33  ? 26  ASN   C N   1 
ATOM   1249 C  CA  . ASN   B 1 20  ? 8.710  -12.839 14.488 1.00 17.50  ? 26  ASN   C CA  1 
ATOM   1250 C  C   . ASN   B 1 20  ? 9.651  -12.998 15.685 1.00 14.95  ? 26  ASN   C C   1 
ATOM   1251 O  O   . ASN   B 1 20  ? 9.240  -12.905 16.857 1.00 15.00  ? 26  ASN   C O   1 
ATOM   1252 C  CB  . ASN   B 1 20  ? 8.167  -14.167 13.969 1.00 17.96  ? 26  ASN   C CB  1 
ATOM   1253 C  CG  . ASN   B 1 20  ? 7.391  -14.889 15.057 1.00 25.20  ? 26  ASN   C CG  1 
ATOM   1254 O  OD1 . ASN   B 1 20  ? 6.344  -14.400 15.510 1.00 28.43  ? 26  ASN   C OD1 1 
ATOM   1255 N  ND2 . ASN   B 1 20  ? 7.973  -15.942 15.603 1.00 26.90  ? 26  ASN   C ND2 1 
ATOM   1256 N  N   . ASP   B 1 21  ? 10.964 -13.187 15.401 1.00 15.07  ? 27  ASP   C N   1 
ATOM   1257 C  CA  . ASP   B 1 21  ? 11.918 -13.298 16.512 1.00 14.56  ? 27  ASP   C CA  1 
ATOM   1258 C  C   . ASP   B 1 21  ? 11.947 -12.003 17.325 1.00 12.46  ? 27  ASP   C C   1 
ATOM   1259 O  O   . ASP   B 1 21  ? 11.899 -12.020 18.518 1.00 15.21  ? 27  ASP   C O   1 
ATOM   1260 C  CB  . ASP   B 1 21  ? 13.325 -13.610 16.000 1.00 13.96  ? 27  ASP   C CB  1 
ATOM   1261 C  CG  . ASP   B 1 21  ? 13.553 -15.037 15.523 1.00 14.83  ? 27  ASP   C CG  1 
ATOM   1262 O  OD1 . ASP   B 1 21  ? 12.947 -15.976 16.139 1.00 15.63  ? 27  ASP   C OD1 1 
ATOM   1263 O  OD2 . ASP   B 1 21  ? 14.233 -15.227 14.480 1.00 14.59  ? 27  ASP   C OD2 1 
ATOM   1264 N  N   . TRP   B 1 22  ? 12.011 -10.830 16.646 1.00 13.83  ? 28  TRP   C N   1 
ATOM   1265 C  CA  . TRP   B 1 22  ? 12.108 -9.540  17.368 1.00 13.98  ? 28  TRP   C CA  1 
ATOM   1266 C  C   . TRP   B 1 22  ? 10.778 -9.199  18.084 1.00 12.25  ? 28  TRP   C C   1 
ATOM   1267 O  O   . TRP   B 1 22  ? 10.818 -8.595  19.141 1.00 14.16  ? 28  TRP   C O   1 
ATOM   1268 C  CB  . TRP   B 1 22  ? 12.529 -8.430  16.412 1.00 14.47  ? 28  TRP   C CB  1 
ATOM   1269 C  CG  . TRP   B 1 22  ? 14.008 -8.374  16.159 1.00 14.24  ? 28  TRP   C CG  1 
ATOM   1270 C  CD1 . TRP   B 1 22  ? 14.644 -8.859  15.080 1.00 15.19  ? 28  TRP   C CD1 1 
ATOM   1271 C  CD2 . TRP   B 1 22  ? 14.998 -7.780  17.002 1.00 11.69  ? 28  TRP   C CD2 1 
ATOM   1272 N  NE1 . TRP   B 1 22  ? 15.981 -8.572  15.161 1.00 13.73  ? 28  TRP   C NE1 1 
ATOM   1273 C  CE2 . TRP   B 1 22  ? 16.236 -7.918  16.339 1.00 13.36  ? 28  TRP   C CE2 1 
ATOM   1274 C  CE3 . TRP   B 1 22  ? 14.953 -7.086  18.204 1.00 14.19  ? 28  TRP   C CE3 1 
ATOM   1275 C  CZ2 . TRP   B 1 22  ? 17.409 -7.362  16.837 1.00 12.91  ? 28  TRP   C CZ2 1 
ATOM   1276 C  CZ3 . TRP   B 1 22  ? 16.132 -6.562  18.707 1.00 15.44  ? 28  TRP   C CZ3 1 
ATOM   1277 C  CH2 . TRP   B 1 22  ? 17.344 -6.734  18.036 1.00 14.85  ? 28  TRP   C CH2 1 
ATOM   1278 N  N   . ALA   B 1 23  ? 9.674  -9.669  17.515 1.00 16.10  ? 29  ALA   C N   1 
ATOM   1279 C  CA  . ALA   B 1 23  ? 8.298  -9.454  18.042 1.00 15.37  ? 29  ALA   C CA  1 
ATOM   1280 C  C   . ALA   B 1 23  ? 8.074  -10.357 19.265 1.00 18.41  ? 29  ALA   C C   1 
ATOM   1281 O  O   . ALA   B 1 23  ? 7.106  -10.138 20.015 1.00 18.09  ? 29  ALA   C O   1 
ATOM   1282 C  CB  . ALA   B 1 23  ? 7.267  -9.743  16.997 1.00 15.83  ? 29  ALA   C CB  1 
ATOM   1283 N  N   . ASN   B 1 24  ? 8.915  -11.387 19.475 1.00 17.13  ? 30  ASN   C N   1 
ATOM   1284 C  CA  . ASN   B 1 24  ? 8.852  -12.314 20.642 1.00 15.57  ? 30  ASN   C CA  1 
ATOM   1285 C  C   . ASN   B 1 24  ? 10.224 -12.346 21.324 1.00 17.22  ? 30  ASN   C C   1 
ATOM   1286 O  O   . ASN   B 1 24  ? 10.628 -13.408 21.855 1.00 15.00  ? 30  ASN   C O   1 
ATOM   1287 C  CB  . ASN   B 1 24  ? 8.385  -13.697 20.202 1.00 17.73  ? 30  ASN   C CB  1 
ATOM   1288 C  CG  . ASN   B 1 24  ? 6.956  -13.648 19.695 1.00 17.49  ? 30  ASN   C CG  1 
ATOM   1289 O  OD1 . ASN   B 1 24  ? 6.016  -13.625 20.510 1.00 19.57  ? 30  ASN   C OD1 1 
ATOM   1290 N  ND2 . ASN   B 1 24  ? 6.784  -13.559 18.398 1.00 18.30  ? 30  ASN   C ND2 1 
ATOM   1291 N  N   . LEU   B 1 25  ? 10.903 -11.212 21.421 1.00 17.77  ? 31  LEU   C N   1 
ATOM   1292 C  CA  . LEU   B 1 25  ? 12.303 -11.191 21.934 1.00 15.55  ? 31  LEU   C CA  1 
ATOM   1293 C  C   . LEU   B 1 25  ? 12.386 -11.555 23.404 1.00 17.02  ? 31  LEU   C C   1 
ATOM   1294 O  O   . LEU   B 1 25  ? 11.638 -11.019 24.249 1.00 17.61  ? 31  LEU   C O   1 
ATOM   1295 C  CB  . LEU   B 1 25  ? 12.840 -9.779  21.714 1.00 17.41  ? 31  LEU   C CB  1 
ATOM   1296 C  CG  . LEU   B 1 25  ? 14.312 -9.615  22.038 1.00 16.67  ? 31  LEU   C CG  1 
ATOM   1297 C  CD1 . LEU   B 1 25  ? 15.186 -10.493 21.143 1.00 15.87  ? 31  LEU   C CD1 1 
ATOM   1298 C  CD2 . LEU   B 1 25  ? 14.709 -8.149  21.885 1.00 17.45  ? 31  LEU   C CD2 1 
ATOM   1299 N  N   . VAL   B 1 26  ? 13.385 -12.366 23.740 1.00 14.93  ? 32  VAL   C N   1 
ATOM   1300 C  CA  . VAL   B 1 26  ? 13.782 -12.605 25.147 1.00 15.42  ? 32  VAL   C CA  1 
ATOM   1301 C  C   . VAL   B 1 26  ? 15.086 -11.872 25.460 1.00 15.63  ? 32  VAL   C C   1 
ATOM   1302 O  O   . VAL   B 1 26  ? 15.199 -11.230 26.505 1.00 17.88  ? 32  VAL   C O   1 
ATOM   1303 C  CB  . VAL   B 1 26  ? 13.891 -14.114 25.394 1.00 15.72  ? 32  VAL   C CB  1 
ATOM   1304 C  CG1 . VAL   B 1 26  ? 14.455 -14.417 26.769 1.00 17.52  ? 32  VAL   C CG1 1 
ATOM   1305 C  CG2 . VAL   B 1 26  ? 12.550 -14.830 25.167 1.00 15.86  ? 32  VAL   C CG2 1 
ATOM   1306 N  N   . TRP   B 1 27  ? 16.101 -12.029 24.586 1.00 14.86  ? 33  TRP   C N   1 
ATOM   1307 C  CA  . TRP   B 1 27  ? 17.448 -11.493 24.858 1.00 14.97  ? 33  TRP   C CA  1 
ATOM   1308 C  C   . TRP   B 1 27  ? 18.243 -11.445 23.559 1.00 13.96  ? 33  TRP   C C   1 
ATOM   1309 O  O   . TRP   B 1 27  ? 17.998 -12.301 22.690 1.00 14.33  ? 33  TRP   C O   1 
ATOM   1310 C  CB  . TRP   B 1 27  ? 18.149 -12.331 25.921 1.00 15.94  ? 33  TRP   C CB  1 
ATOM   1311 C  CG  . TRP   B 1 27  ? 19.614 -12.085 26.093 1.00 15.99  ? 33  TRP   C CG  1 
ATOM   1312 C  CD1 . TRP   B 1 27  ? 20.217 -11.175 26.905 1.00 18.97  ? 33  TRP   C CD1 1 
ATOM   1313 C  CD2 . TRP   B 1 27  ? 20.686 -12.803 25.453 1.00 15.48  ? 33  TRP   C CD2 1 
ATOM   1314 N  NE1 . TRP   B 1 27  ? 21.586 -11.299 26.850 1.00 20.92  ? 33  TRP   C NE1 1 
ATOM   1315 C  CE2 . TRP   B 1 27  ? 21.902 -12.287 25.956 1.00 17.97  ? 33  TRP   C CE2 1 
ATOM   1316 C  CE3 . TRP   B 1 27  ? 20.743 -13.837 24.519 1.00 15.57  ? 33  TRP   C CE3 1 
ATOM   1317 C  CZ2 . TRP   B 1 27  ? 23.156 -12.792 25.577 1.00 17.74  ? 33  TRP   C CZ2 1 
ATOM   1318 C  CZ3 . TRP   B 1 27  ? 21.985 -14.329 24.136 1.00 17.99  ? 33  TRP   C CZ3 1 
ATOM   1319 C  CH2 . TRP   B 1 27  ? 23.157 -13.789 24.640 1.00 17.19  ? 33  TRP   C CH2 1 
ATOM   1320 N  N   . GLU   B 1 28  ? 19.086 -10.428 23.425 1.00 14.95  ? 34  GLU   C N   1 
ATOM   1321 C  CA  . GLU   B 1 28  ? 19.956 -10.346 22.239 1.00 16.39  ? 34  GLU   C CA  1 
ATOM   1322 C  C   . GLU   B 1 28  ? 21.244 -9.635  22.590 1.00 15.38  ? 34  GLU   C C   1 
ATOM   1323 O  O   . GLU   B 1 28  ? 21.253 -8.750  23.489 1.00 15.12  ? 34  GLU   C O   1 
ATOM   1324 C  CB  . GLU   B 1 28  ? 19.226 -9.687  21.083 1.00 16.19  ? 34  GLU   C CB  1 
ATOM   1325 C  CG  . GLU   B 1 28  ? 18.686 -8.301  21.305 1.00 16.92  ? 34  GLU   C CG  1 
ATOM   1326 C  CD  . GLU   B 1 28  ? 19.645 -7.135  21.240 1.00 18.28  ? 34  GLU   C CD  1 
ATOM   1327 O  OE1 . GLU   B 1 28  ? 19.373 -6.116  21.897 1.00 20.54  ? 34  GLU   C OE1 1 
ATOM   1328 O  OE2 . GLU   B 1 28  ? 20.678 -7.197  20.504 1.00 16.99  ? 34  GLU   C OE2 1 
ATOM   1329 N  N   . ASP   B 1 29  ? 22.311 -9.979  21.867 1.00 14.30  ? 35  ASP   C N   1 
ATOM   1330 C  CA  . ASP   B 1 29  ? 23.629 -9.343  22.102 1.00 14.15  ? 35  ASP   C CA  1 
ATOM   1331 C  C   . ASP   B 1 29  ? 24.389 -9.332  20.791 1.00 14.74  ? 35  ASP   C C   1 
ATOM   1332 O  O   . ASP   B 1 29  ? 24.808 -10.400 20.314 1.00 13.92  ? 35  ASP   C O   1 
ATOM   1333 C  CB  . ASP   B 1 29  ? 24.359 -10.099 23.210 1.00 13.96  ? 35  ASP   C CB  1 
ATOM   1334 C  CG  . ASP   B 1 29  ? 25.709 -9.557  23.605 1.00 16.88  ? 35  ASP   C CG  1 
ATOM   1335 O  OD1 . ASP   B 1 29  ? 26.429 -9.127  22.736 1.00 19.00  ? 35  ASP   C OD1 1 
ATOM   1336 O  OD2 . ASP   B 1 29  ? 26.056 -9.692  24.780 1.00 20.50  ? 35  ASP   C OD2 1 
ATOM   1337 N  N   A SER   B 1 30  ? 24.532 -8.138  20.201 0.36 13.19  ? 36  SER   C N   1 
ATOM   1338 N  N   B SER   B 1 30  ? 24.554 -8.151  20.186 0.36 13.66  ? 36  SER   C N   1 
ATOM   1339 C  CA  A SER   B 1 30  ? 25.260 -7.907  18.929 0.36 13.75  ? 36  SER   C CA  1 
ATOM   1340 C  CA  B SER   B 1 30  ? 25.235 -8.010  18.877 0.36 14.48  ? 36  SER   C CA  1 
ATOM   1341 C  C   A SER   B 1 30  ? 26.706 -8.431  19.009 0.36 13.52  ? 36  SER   C C   1 
ATOM   1342 C  C   B SER   B 1 30  ? 26.723 -8.413  18.985 0.36 13.88  ? 36  SER   C C   1 
ATOM   1343 O  O   A SER   B 1 30  ? 27.179 -9.031  18.032 0.36 13.63  ? 36  SER   C O   1 
ATOM   1344 O  O   B SER   B 1 30  ? 27.239 -8.975  18.009 0.36 13.86  ? 36  SER   C O   1 
ATOM   1345 C  CB  A SER   B 1 30  ? 25.260 -6.436  18.546 0.36 13.14  ? 36  SER   C CB  1 
ATOM   1346 C  CB  B SER   B 1 30  ? 25.058 -6.616  18.306 0.36 14.48  ? 36  SER   C CB  1 
ATOM   1347 O  OG  A SER   B 1 30  ? 26.208 -6.203  17.509 0.36 13.86  ? 36  SER   C OG  1 
ATOM   1348 O  OG  B SER   B 1 30  ? 25.488 -5.640  19.228 0.36 16.62  ? 36  SER   C OG  1 
ATOM   1349 N  N   . SER   B 1 31  ? 27.380 -8.159  20.120 1.00 14.64  ? 37  SER   C N   1 
ATOM   1350 C  CA  . SER   B 1 31  ? 28.815 -8.531  20.267 1.00 14.58  ? 37  SER   C CA  1 
ATOM   1351 C  C   . SER   B 1 31  ? 28.985 -10.057 20.271 1.00 14.28  ? 37  SER   C C   1 
ATOM   1352 O  O   . SER   B 1 31  ? 30.067 -10.467 19.853 1.00 15.72  ? 37  SER   C O   1 
ATOM   1353 C  CB  . SER   B 1 31  ? 29.397 -7.950  21.479 1.00 16.19  ? 37  SER   C CB  1 
ATOM   1354 O  OG  . SER   B 1 31  ? 29.081 -8.681  22.620 1.00 20.89  ? 37  SER   C OG  1 
ATOM   1355 N  N   . ARG   B 1 32  ? 27.939 -10.846 20.570 1.00 13.70  ? 38  ARG   C N   1 
ATOM   1356 C  CA  . ARG   B 1 32  ? 28.001 -12.329 20.512 1.00 13.02  ? 38  ARG   C CA  1 
ATOM   1357 C  C   . ARG   B 1 32  ? 27.374 -12.880 19.219 1.00 12.27  ? 38  ARG   C C   1 
ATOM   1358 O  O   . ARG   B 1 32  ? 27.399 -14.119 18.997 1.00 12.60  ? 38  ARG   C O   1 
ATOM   1359 C  CB  . ARG   B 1 32  ? 27.253 -12.893 21.705 1.00 14.48  ? 38  ARG   C CB  1 
ATOM   1360 C  CG  . ARG   B 1 32  ? 27.943 -12.583 23.016 1.00 15.05  ? 38  ARG   C CG  1 
ATOM   1361 C  CD  . ARG   B 1 32  ? 27.205 -13.082 24.216 1.00 13.95  ? 38  ARG   C CD  1 
ATOM   1362 N  NE  . ARG   B 1 32  ? 27.244 -14.560 24.282 1.00 13.22  ? 38  ARG   C NE  1 
ATOM   1363 C  CZ  . ARG   B 1 32  ? 27.208 -15.286 25.384 1.00 13.40  ? 38  ARG   C CZ  1 
ATOM   1364 N  NH1 . ARG   B 1 32  ? 27.085 -14.758 26.579 1.00 14.94  ? 38  ARG   C NH1 1 
ATOM   1365 N  NH2 . ARG   B 1 32  ? 27.313 -16.623 25.303 1.00 13.95  ? 38  ARG   C NH2 1 
ATOM   1366 N  N   . ASP   B 1 33  ? 26.691 -12.049 18.416 1.00 11.51  ? 39  ASP   C N   1 
ATOM   1367 C  CA  . ASP   B 1 33  ? 25.879 -12.512 17.278 1.00 12.30  ? 39  ASP   C CA  1 
ATOM   1368 C  C   . ASP   B 1 33  ? 24.768 -13.494 17.720 1.00 10.77  ? 39  ASP   C C   1 
ATOM   1369 O  O   . ASP   B 1 33  ? 24.487 -14.422 16.932 1.00 11.21  ? 39  ASP   C O   1 
ATOM   1370 C  CB  . ASP   B 1 33  ? 26.714 -13.123 16.164 1.00 11.64  ? 39  ASP   C CB  1 
ATOM   1371 C  CG  . ASP   B 1 33  ? 25.948 -13.447 14.887 1.00 12.98  ? 39  ASP   C CG  1 
ATOM   1372 O  OD1 . ASP   B 1 33  ? 25.049 -12.634 14.502 1.00 12.62  ? 39  ASP   C OD1 1 
ATOM   1373 O  OD2 . ASP   B 1 33  ? 26.225 -14.464 14.223 1.00 12.44  ? 39  ASP   C OD2 1 
ATOM   1374 N  N   . LEU   B 1 34  ? 24.129 -13.280 18.870 1.00 11.01  ? 40  LEU   C N   1 
ATOM   1375 C  CA  . LEU   B 1 34  ? 23.016 -14.149 19.312 1.00 11.16  ? 40  LEU   C CA  1 
ATOM   1376 C  C   . LEU   B 1 34  ? 21.725 -13.366 19.545 1.00 11.37  ? 40  LEU   C C   1 
ATOM   1377 O  O   . LEU   B 1 34  ? 21.788 -12.223 20.052 1.00 12.49  ? 40  LEU   C O   1 
ATOM   1378 C  CB  . LEU   B 1 34  ? 23.414 -14.867 20.609 1.00 11.63  ? 40  LEU   C CB  1 
ATOM   1379 C  CG  . LEU   B 1 34  ? 24.493 -15.976 20.517 1.00 12.01  ? 40  LEU   C CG  1 
ATOM   1380 C  CD1 . LEU   B 1 34  ? 24.780 -16.593 21.926 1.00 13.36  ? 40  LEU   C CD1 1 
ATOM   1381 C  CD2 . LEU   B 1 34  ? 24.068 -17.071 19.565 1.00 12.73  ? 40  LEU   C CD2 1 
ATOM   1382 N  N   . LEU   B 1 35  ? 20.625 -14.059 19.288 1.00 10.81  ? 41  LEU   C N   1 
ATOM   1383 C  CA  . LEU   B 1 35  ? 19.284 -13.570 19.700 1.00 11.41  ? 41  LEU   C CA  1 
ATOM   1384 C  C   . LEU   B 1 35  ? 18.481 -14.805 20.104 1.00 11.64  ? 41  LEU   C C   1 
ATOM   1385 O  O   . LEU   B 1 35  ? 18.584 -15.854 19.483 1.00 12.21  ? 41  LEU   C O   1 
ATOM   1386 C  CB  . LEU   B 1 35  ? 18.646 -12.836 18.504 1.00 12.03  ? 41  LEU   C CB  1 
ATOM   1387 C  CG  . LEU   B 1 35  ? 17.243 -12.261 18.750 1.00 11.70  ? 41  LEU   C CG  1 
ATOM   1388 C  CD1 . LEU   B 1 35  ? 16.997 -10.931 18.025 1.00 12.66  ? 41  LEU   C CD1 1 
ATOM   1389 C  CD2 . LEU   B 1 35  ? 16.158 -13.273 18.410 1.00 13.09  ? 41  LEU   C CD2 1 
ATOM   1390 N  N   . VAL   B 1 36  ? 17.711 -14.650 21.164 1.00 12.62  ? 42  VAL   C N   1 
ATOM   1391 C  CA  . VAL   B 1 36  ? 16.752 -15.640 21.703 1.00 12.58  ? 42  VAL   C CA  1 
ATOM   1392 C  C   . VAL   B 1 36  ? 15.347 -15.052 21.660 1.00 11.96  ? 42  VAL   C C   1 
ATOM   1393 O  O   . VAL   B 1 36  ? 15.156 -13.921 22.180 1.00 14.60  ? 42  VAL   C O   1 
ATOM   1394 C  CB  . VAL   B 1 36  ? 17.174 -16.067 23.106 1.00 12.95  ? 42  VAL   C CB  1 
ATOM   1395 C  CG1 . VAL   B 1 36  ? 16.233 -17.122 23.643 1.00 13.85  ? 42  VAL   C CG1 1 
ATOM   1396 C  CG2 . VAL   B 1 36  ? 18.629 -16.591 23.069 1.00 14.08  ? 42  VAL   C CG2 1 
ATOM   1397 N  N   . SER   B 1 37  ? 14.432 -15.821 21.103 1.00 12.49  ? 43  SER   C N   1 
ATOM   1398 C  CA  . SER   B 1 37  ? 12.985 -15.493 21.028 1.00 13.27  ? 43  SER   C CA  1 
ATOM   1399 C  C   . SER   B 1 37  ? 12.176 -16.580 21.733 1.00 14.88  ? 43  SER   C C   1 
ATOM   1400 O  O   . SER   B 1 37  ? 12.692 -17.685 22.010 1.00 13.96  ? 43  SER   C O   1 
ATOM   1401 C  CB  . SER   B 1 37  ? 12.552 -15.279 19.622 1.00 13.28  ? 43  SER   C CB  1 
ATOM   1402 O  OG  . SER   B 1 37  ? 12.677 -16.412 18.810 1.00 14.18  ? 43  SER   C OG  1 
ATOM   1403 N  N   . SER   B 1 38  ? 10.945 -16.273 22.121 1.00 15.51  ? 44  SER   C N   1 
ATOM   1404 C  CA  . SER   B 1 38  ? 10.049 -17.245 22.805 1.00 16.13  ? 44  SER   C CA  1 
ATOM   1405 C  C   . SER   B 1 38  ? 9.258  -18.031 21.766 1.00 17.96  ? 44  SER   C C   1 
ATOM   1406 O  O   . SER   B 1 38  ? 8.957  -17.491 20.686 1.00 18.85  ? 44  SER   C O   1 
ATOM   1407 C  CB  . SER   B 1 38  ? 9.147  -16.553 23.804 1.00 18.15  ? 44  SER   C CB  1 
ATOM   1408 O  OG  . SER   B 1 38  ? 8.353  -15.599 23.107 1.00 22.63  ? 44  SER   C OG  1 
ATOM   1409 N  N   . THR   B 1 39  ? 8.918  -19.288 22.097 1.00 18.17  ? 45  THR   C N   1 
ATOM   1410 C  CA  . THR   B 1 39  ? 8.168  -20.227 21.230 1.00 17.91  ? 45  THR   C CA  1 
ATOM   1411 C  C   . THR   B 1 39  ? 6.842  -20.616 21.940 1.00 20.42  ? 45  THR   C C   1 
ATOM   1412 O  O   . THR   B 1 39  ? 6.796  -20.666 23.169 1.00 19.85  ? 45  THR   C O   1 
ATOM   1413 C  CB  . THR   B 1 39  ? 9.026  -21.464 20.888 1.00 18.41  ? 45  THR   C CB  1 
ATOM   1414 O  OG1 . THR   B 1 39  ? 9.323  -22.165 22.096 1.00 19.75  ? 45  THR   C OG1 1 
ATOM   1415 C  CG2 . THR   B 1 39  ? 10.350 -21.151 20.227 1.00 17.64  ? 45  THR   C CG2 1 
ATOM   1416 N  N   . THR   B 1 40  ? 5.830  -20.977 21.163 1.00 25.02  ? 46  THR   C N   1 
ATOM   1417 C  CA  . THR   B 1 40  ? 4.568  -21.579 21.685 1.00 25.28  ? 46  THR   C CA  1 
ATOM   1418 C  C   . THR   B 1 40  ? 4.830  -23.059 22.016 1.00 25.45  ? 46  THR   C C   1 
ATOM   1419 O  O   . THR   B 1 40  ? 4.525  -23.472 23.169 1.00 27.77  ? 46  THR   C O   1 
ATOM   1420 C  CB  . THR   B 1 40  ? 3.432  -21.273 20.711 1.00 28.61  ? 46  THR   C CB  1 
ATOM   1421 O  OG1 . THR   B 1 40  ? 3.828  -21.837 19.477 1.00 33.63  ? 46  THR   C OG1 1 
ATOM   1422 C  CG2 . THR   B 1 40  ? 3.234  -19.795 20.466 1.00 28.94  ? 46  THR   C CG2 1 
ATOM   1423 N  N   . ALA   B 1 41  ? 5.483  -23.785 21.107 1.00 22.73  ? 47  ALA   C N   1 
ATOM   1424 C  CA  . ALA   B 1 41  ? 5.771  -25.225 21.277 1.00 23.40  ? 47  ALA   C CA  1 
ATOM   1425 C  C   . ALA   B 1 41  ? 7.078  -25.439 22.047 1.00 22.05  ? 47  ALA   C C   1 
ATOM   1426 O  O   . ALA   B 1 41  ? 8.008  -24.654 21.880 1.00 21.89  ? 47  ALA   C O   1 
ATOM   1427 C  CB  . ALA   B 1 41  ? 5.847  -25.878 19.917 1.00 24.64  ? 47  ALA   C CB  1 
ATOM   1428 N  N   . GLN   B 1 42  ? 7.153  -26.470 22.877 1.00 22.72  ? 48  GLN   C N   1 
ATOM   1429 C  CA  . GLN   B 1 42  ? 8.383  -26.918 23.579 1.00 24.83  ? 48  GLN   C CA  1 
ATOM   1430 C  C   . GLN   B 1 42  ? 9.392  -27.504 22.586 1.00 22.29  ? 48  GLN   C C   1 
ATOM   1431 O  O   . GLN   B 1 42  ? 8.997  -28.295 21.715 1.00 23.62  ? 48  GLN   C O   1 
ATOM   1432 C  CB  . GLN   B 1 42  ? 8.034  -27.933 24.659 1.00 30.94  ? 48  GLN   C CB  1 
ATOM   1433 C  CG  . GLN   B 1 42  ? 7.551  -27.255 25.927 1.00 38.61  ? 48  GLN   C CG  1 
ATOM   1434 C  CD  . GLN   B 1 42  ? 7.666  -28.238 27.058 1.00 44.17  ? 48  GLN   C CD  1 
ATOM   1435 O  OE1 . GLN   B 1 42  ? 6.679  -28.851 27.468 1.00 57.53  ? 48  GLN   C OE1 1 
ATOM   1436 N  NE2 . GLN   B 1 42  ? 8.891  -28.421 27.534 1.00 48.32  ? 48  GLN   C NE2 1 
ATOM   1437 N  N   . GLY   B 1 43  ? 10.659 -27.120 22.746 1.00 18.93  ? 49  GLY   C N   1 
ATOM   1438 C  CA  . GLY   B 1 43  ? 11.796 -27.661 21.977 1.00 19.65  ? 49  GLY   C CA  1 
ATOM   1439 C  C   . GLY   B 1 43  ? 12.386 -28.849 22.694 1.00 18.14  ? 49  GLY   C C   1 
ATOM   1440 O  O   . GLY   B 1 43  ? 12.145 -28.981 23.921 1.00 21.67  ? 49  GLY   C O   1 
ATOM   1441 N  N   . CYS   B 1 44  ? 13.252 -29.560 22.012 1.00 17.95  ? 50  CYS   C N   1 
ATOM   1442 C  CA  . CYS   B 1 44  ? 13.802 -30.820 22.565 1.00 18.81  ? 50  CYS   C CA  1 
ATOM   1443 C  C   . CYS   B 1 44  ? 15.319 -30.826 22.632 1.00 19.05  ? 50  CYS   C C   1 
ATOM   1444 O  O   . CYS   B 1 44  ? 15.886 -31.856 23.077 1.00 22.70  ? 50  CYS   C O   1 
ATOM   1445 C  CB  . CYS   B 1 44  ? 13.313 -31.995 21.726 1.00 18.85  ? 50  CYS   C CB  1 
ATOM   1446 S  SG  . CYS   B 1 44  ? 11.487 -32.038 21.703 1.00 27.48  ? 50  CYS   C SG  1 
ATOM   1447 N  N   . ASP   B 1 45  ? 16.019 -29.769 22.239 1.00 15.23  ? 51  ASP   C N   1 
ATOM   1448 C  CA  . ASP   B 1 45  ? 17.500 -29.755 22.278 1.00 15.35  ? 51  ASP   C CA  1 
ATOM   1449 C  C   . ASP   B 1 45  ? 17.912 -29.566 23.751 1.00 14.83  ? 51  ASP   C C   1 
ATOM   1450 O  O   . ASP   B 1 45  ? 17.192 -28.921 24.565 1.00 16.39  ? 51  ASP   C O   1 
ATOM   1451 C  CB  . ASP   B 1 45  ? 18.067 -28.618 21.418 1.00 16.41  ? 51  ASP   C CB  1 
ATOM   1452 C  CG  . ASP   B 1 45  ? 17.890 -28.763 19.920 1.00 19.74  ? 51  ASP   C CG  1 
ATOM   1453 O  OD1 . ASP   B 1 45  ? 17.861 -29.892 19.458 1.00 20.41  ? 51  ASP   C OD1 1 
ATOM   1454 O  OD2 . ASP   B 1 45  ? 17.776 -27.710 19.189 1.00 18.44  ? 51  ASP   C OD2 1 
ATOM   1455 N  N   . THR   B 1 46  ? 19.001 -30.207 24.115 1.00 13.97  ? 52  THR   C N   1 
ATOM   1456 C  CA  . THR   B 1 46  ? 19.663 -30.039 25.412 1.00 14.45  ? 52  THR   C CA  1 
ATOM   1457 C  C   . THR   B 1 46  ? 20.912 -29.170 25.233 1.00 12.44  ? 52  THR   C C   1 
ATOM   1458 O  O   . THR   B 1 46  ? 21.755 -29.510 24.361 1.00 13.72  ? 52  THR   C O   1 
ATOM   1459 C  CB  . THR   B 1 46  ? 20.078 -31.387 25.993 1.00 16.43  ? 52  THR   C CB  1 
ATOM   1460 O  OG1 . THR   B 1 46  ? 18.866 -32.145 26.159 1.00 19.69  ? 52  THR   C OG1 1 
ATOM   1461 C  CG2 . THR   B 1 46  ? 20.821 -31.228 27.301 1.00 19.48  ? 52  THR   C CG2 1 
ATOM   1462 N  N   . ILE   B 1 47  ? 21.105 -28.144 26.070 1.00 13.56  ? 53  ILE   C N   1 
ATOM   1463 C  CA  . ILE   B 1 47  ? 22.301 -27.285 26.010 1.00 12.84  ? 53  ILE   C CA  1 
ATOM   1464 C  C   . ILE   B 1 47  ? 23.390 -27.995 26.816 1.00 12.23  ? 53  ILE   C C   1 
ATOM   1465 O  O   . ILE   B 1 47  ? 23.133 -28.480 27.944 1.00 14.08  ? 53  ILE   C O   1 
ATOM   1466 C  CB  . ILE   B 1 47  ? 22.053 -25.877 26.560 1.00 14.08  ? 53  ILE   C CB  1 
ATOM   1467 C  CG1 . ILE   B 1 47  ? 20.846 -25.195 25.900 1.00 14.40  ? 53  ILE   C CG1 1 
ATOM   1468 C  CG2 . ILE   B 1 47  ? 23.306 -25.023 26.465 1.00 14.39  ? 53  ILE   C CG2 1 
ATOM   1469 C  CD1 . ILE   B 1 47  ? 21.089 -24.985 24.427 1.00 15.69  ? 53  ILE   C CD1 1 
ATOM   1470 N  N   . ALA   B 1 48  ? 24.591 -28.088 26.279 1.00 11.18  ? 54  ALA   C N   1 
ATOM   1471 C  CA  . ALA   B 1 48  ? 25.728 -28.639 27.030 1.00 10.93  ? 54  ALA   C CA  1 
ATOM   1472 C  C   . ALA   B 1 48  ? 26.046 -27.711 28.212 1.00 11.74  ? 54  ALA   C C   1 
ATOM   1473 O  O   . ALA   B 1 48  ? 26.014 -26.478 28.088 1.00 11.70  ? 54  ALA   C O   1 
ATOM   1474 C  CB  . ALA   B 1 48  ? 26.919 -28.720 26.116 1.00 11.35  ? 54  ALA   C CB  1 
ATOM   1475 N  N   . ARG   B 1 49  ? 26.416 -28.311 29.355 1.00 11.97  ? 55  ARG   C N   1 
ATOM   1476 C  CA  . ARG   B 1 49  ? 26.907 -27.563 30.539 1.00 11.68  ? 55  ARG   C CA  1 
ATOM   1477 C  C   . ARG   B 1 49  ? 28.241 -28.206 30.922 1.00 12.11  ? 55  ARG   C C   1 
ATOM   1478 O  O   . ARG   B 1 49  ? 28.214 -29.278 31.592 1.00 13.47  ? 55  ARG   C O   1 
ATOM   1479 C  CB  . ARG   B 1 49  ? 25.845 -27.568 31.642 1.00 12.64  ? 55  ARG   C CB  1 
ATOM   1480 C  CG  . ARG   B 1 49  ? 24.501 -26.981 31.236 1.00 12.45  ? 55  ARG   C CG  1 
ATOM   1481 C  CD  . ARG   B 1 49  ? 24.505 -25.505 30.930 1.00 13.37  ? 55  ARG   C CD  1 
ATOM   1482 N  NE  . ARG   B 1 49  ? 23.170 -25.061 30.520 1.00 14.15  ? 55  ARG   C NE  1 
ATOM   1483 C  CZ  . ARG   B 1 49  ? 22.920 -23.978 29.785 1.00 14.25  ? 55  ARG   C CZ  1 
ATOM   1484 N  NH1 . ARG   B 1 49  ? 23.883 -23.167 29.465 1.00 13.30  ? 55  ARG   C NH1 1 
ATOM   1485 N  NH2 . ARG   B 1 49  ? 21.683 -23.683 29.410 1.00 14.98  ? 55  ARG   C NH2 1 
ATOM   1486 N  N   . CYS   B 1 50  ? 29.324 -27.629 30.448 1.00 11.18  ? 56  CYS   C N   1 
ATOM   1487 C  CA  . CYS   B 1 50  ? 30.655 -28.300 30.430 1.00 11.63  ? 56  CYS   C CA  1 
ATOM   1488 C  C   . CYS   B 1 50  ? 31.709 -27.330 29.921 1.00 11.36  ? 56  CYS   C C   1 
ATOM   1489 O  O   . CYS   B 1 50  ? 31.370 -26.211 29.480 1.00 12.30  ? 56  CYS   C O   1 
ATOM   1490 C  CB  . CYS   B 1 50  ? 30.654 -29.506 29.497 1.00 10.50  ? 56  CYS   C CB  1 
ATOM   1491 S  SG  . CYS   B 1 50  ? 30.442 -29.048 27.744 1.00 12.27  ? 56  CYS   C SG  1 
ATOM   1492 N  N   . ASP   B 1 51  ? 32.977 -27.744 29.969 1.00 13.41  ? 57  ASP   C N   1 
ATOM   1493 C  CA  . ASP   B 1 51  ? 34.110 -27.052 29.331 1.00 15.42  ? 57  ASP   C CA  1 
ATOM   1494 C  C   . ASP   B 1 51  ? 34.762 -27.937 28.250 1.00 14.31  ? 57  ASP   C C   1 
ATOM   1495 O  O   . ASP   B 1 51  ? 35.976 -27.768 27.999 1.00 14.88  ? 57  ASP   C O   1 
ATOM   1496 C  CB  . ASP   B 1 51  ? 35.133 -26.592 30.374 1.00 17.24  ? 57  ASP   C CB  1 
ATOM   1497 C  CG  . ASP   B 1 51  ? 35.807 -27.711 31.115 1.00 19.69  ? 57  ASP   C CG  1 
ATOM   1498 O  OD1 . ASP   B 1 51  ? 35.514 -28.864 30.883 1.00 19.78  ? 57  ASP   C OD1 1 
ATOM   1499 O  OD2 . ASP   B 1 51  ? 36.708 -27.351 31.924 1.00 28.71  ? 57  ASP   C OD2 1 
ATOM   1500 N  N   . CYS   B 1 52  ? 34.007 -28.825 27.576 1.00 12.87  ? 58  CYS   C N   1 
ATOM   1501 C  CA  . CYS   B 1 52  ? 34.555 -29.566 26.404 1.00 12.20  ? 58  CYS   C CA  1 
ATOM   1502 C  C   . CYS   B 1 52  ? 35.220 -28.642 25.406 1.00 12.51  ? 58  CYS   C C   1 
ATOM   1503 O  O   . CYS   B 1 52  ? 34.775 -27.495 25.179 1.00 12.84  ? 58  CYS   C O   1 
ATOM   1504 C  CB  . CYS   B 1 52  ? 33.516 -30.392 25.670 1.00 12.20  ? 58  CYS   C CB  1 
ATOM   1505 S  SG  . CYS   B 1 52  ? 32.885 -31.793 26.643 1.00 13.38  ? 58  CYS   C SG  1 
ATOM   1506 N  N   . GLN   B 1 53  ? 36.251 -29.148 24.774 1.00 12.54  ? 59  GLN   C N   1 
ATOM   1507 C  CA  . GLN   B 1 53  ? 36.988 -28.546 23.645 1.00 12.93  ? 59  GLN   C CA  1 
ATOM   1508 C  C   . GLN   B 1 53  ? 37.062 -29.523 22.484 1.00 11.51  ? 59  GLN   C C   1 
ATOM   1509 O  O   . GLN   B 1 53  ? 37.823 -29.262 21.521 1.00 12.22  ? 59  GLN   C O   1 
ATOM   1510 C  CB  . GLN   B 1 53  ? 38.398 -28.103 24.045 1.00 13.34  ? 59  GLN   C CB  1 
ATOM   1511 C  CG  . GLN   B 1 53  ? 38.381 -26.876 24.925 1.00 15.74  ? 59  GLN   C CG  1 
ATOM   1512 C  CD  . GLN   B 1 53  ? 39.750 -26.296 25.146 1.00 18.03  ? 59  GLN   C CD  1 
ATOM   1513 O  OE1 . GLN   B 1 53  ? 40.253 -26.298 26.270 1.00 20.52  ? 59  GLN   C OE1 1 
ATOM   1514 N  NE2 . GLN   B 1 53  ? 40.371 -25.745 24.116 1.00 17.43  ? 59  GLN   C NE2 1 
ATOM   1515 N  N   . THR   B 1 54  ? 36.277 -30.584 22.518 1.00 11.47  ? 60  THR   C N   1 
ATOM   1516 C  CA  . THR   B 1 54  ? 36.130 -31.432 21.326 1.00 12.54  ? 60  THR   C CA  1 
ATOM   1517 C  C   . THR   B 1 54  ? 34.657 -31.717 21.074 1.00 12.04  ? 60  THR   C C   1 
ATOM   1518 O  O   . THR   B 1 54  ? 33.864 -31.807 22.003 1.00 11.97  ? 60  THR   C O   1 
ATOM   1519 C  CB  . THR   B 1 54  ? 36.913 -32.725 21.393 1.00 15.22  ? 60  THR   C CB  1 
ATOM   1520 O  OG1 . THR   B 1 54  ? 36.377 -33.497 22.410 1.00 19.30  ? 60  THR   C OG1 1 
ATOM   1521 C  CG2 . THR   B 1 54  ? 38.386 -32.524 21.655 1.00 15.03  ? 60  THR   C CG2 1 
ATOM   1522 N  N   . GLY   B 1 55  ? 34.250 -31.759 19.792 1.00 10.52  ? 61  GLY   C N   1 
ATOM   1523 C  CA  . GLY   B 1 55  ? 32.851 -31.993 19.455 1.00 10.32  ? 61  GLY   C CA  1 
ATOM   1524 C  C   . GLY   B 1 55  ? 32.715 -32.154 17.957 1.00 9.57   ? 61  GLY   C C   1 
ATOM   1525 O  O   . GLY   B 1 55  ? 33.703 -32.501 17.293 1.00 10.74  ? 61  GLY   C O   1 
ATOM   1526 N  N   . VAL   B 1 56  ? 31.490 -32.066 17.504 1.00 9.68   ? 62  VAL   C N   1 
ATOM   1527 C  CA  . VAL   B 1 56  ? 31.189 -32.289 16.067 1.00 9.07   ? 62  VAL   C CA  1 
ATOM   1528 C  C   . VAL   B 1 56  ? 30.300 -31.125 15.630 1.00 8.83   ? 62  VAL   C C   1 
ATOM   1529 O  O   . VAL   B 1 56  ? 29.342 -30.839 16.338 1.00 10.87  ? 62  VAL   C O   1 
ATOM   1530 C  CB  . VAL   B 1 56  ? 30.473 -33.646 15.877 1.00 10.17  ? 62  VAL   C CB  1 
ATOM   1531 C  CG1 . VAL   B 1 56  ? 29.941 -33.825 14.448 1.00 11.22  ? 62  VAL   C CG1 1 
ATOM   1532 C  CG2 . VAL   B 1 56  ? 31.343 -34.851 16.276 1.00 10.31  ? 62  VAL   C CG2 1 
ATOM   1533 N  N   . TYR   B 1 57  ? 30.552 -30.567 14.446 1.00 9.48   ? 63  TYR   C N   1 
ATOM   1534 C  CA  . TYR   B 1 57  ? 29.672 -29.476 13.923 1.00 8.27   ? 63  TYR   C CA  1 
ATOM   1535 C  C   . TYR   B 1 57  ? 29.099 -29.871 12.558 1.00 9.49   ? 63  TYR   C C   1 
ATOM   1536 O  O   . TYR   B 1 57  ? 29.792 -30.535 11.796 1.00 11.15  ? 63  TYR   C O   1 
ATOM   1537 C  CB  . TYR   B 1 57  ? 30.347 -28.084 13.904 1.00 8.79   ? 63  TYR   C CB  1 
ATOM   1538 C  CG  . TYR   B 1 57  ? 31.213 -27.762 12.700 1.00 10.03  ? 63  TYR   C CG  1 
ATOM   1539 C  CD1 . TYR   B 1 57  ? 32.485 -28.263 12.591 1.00 10.60  ? 63  TYR   C CD1 1 
ATOM   1540 C  CD2 . TYR   B 1 57  ? 30.741 -26.915 11.687 1.00 9.98   ? 63  TYR   C CD2 1 
ATOM   1541 C  CE1 . TYR   B 1 57  ? 33.312 -27.969 11.507 1.00 11.40  ? 63  TYR   C CE1 1 
ATOM   1542 C  CE2 . TYR   B 1 57  ? 31.551 -26.620 10.593 1.00 10.53  ? 63  TYR   C CE2 1 
ATOM   1543 C  CZ  . TYR   B 1 57  ? 32.827 -27.126 10.512 1.00 10.73  ? 63  TYR   C CZ  1 
ATOM   1544 O  OH  . TYR   B 1 57  ? 33.700 -26.837 9.453  1.00 13.11  ? 63  TYR   C OH  1 
ATOM   1545 N  N   . TYR   B 1 58  ? 27.951 -29.283 12.267 1.00 9.40   ? 64  TYR   C N   1 
ATOM   1546 C  CA  . TYR   B 1 58  ? 27.328 -29.449 10.922 1.00 10.57  ? 64  TYR   C CA  1 
ATOM   1547 C  C   . TYR   B 1 58  ? 27.710 -28.269 10.034 1.00 9.99   ? 64  TYR   C C   1 
ATOM   1548 O  O   . TYR   B 1 58  ? 27.483 -27.096 10.330 1.00 10.85  ? 64  TYR   C O   1 
ATOM   1549 C  CB  . TYR   B 1 58  ? 25.818 -29.570 10.981 1.00 10.99  ? 64  TYR   C CB  1 
ATOM   1550 C  CG  . TYR   B 1 58  ? 25.236 -29.847 9.617  1.00 12.43  ? 64  TYR   C CG  1 
ATOM   1551 C  CD1 . TYR   B 1 58  ? 25.569 -31.006 8.955  1.00 12.93  ? 64  TYR   C CD1 1 
ATOM   1552 C  CD2 . TYR   B 1 58  ? 24.390 -28.934 9.019  1.00 12.68  ? 64  TYR   C CD2 1 
ATOM   1553 C  CE1 . TYR   B 1 58  ? 25.115 -31.236 7.662  1.00 13.98  ? 64  TYR   C CE1 1 
ATOM   1554 C  CE2 . TYR   B 1 58  ? 23.876 -29.184 7.737  1.00 13.58  ? 64  TYR   C CE2 1 
ATOM   1555 C  CZ  . TYR   B 1 58  ? 24.205 -30.364 7.119  1.00 12.61  ? 64  TYR   C CZ  1 
ATOM   1556 O  OH  . TYR   B 1 58  ? 23.753 -30.605 5.807  1.00 17.13  ? 64  TYR   C OH  1 
ATOM   1557 N  N   . CYS   B 1 59  ? 28.231 -28.651 8.859  1.00 10.04  ? 65  CYS   C N   1 
ATOM   1558 C  CA  . CYS   B 1 59  ? 28.665 -27.731 7.753  1.00 10.92  ? 65  CYS   C CA  1 
ATOM   1559 C  C   . CYS   B 1 59  ? 27.752 -27.919 6.527  1.00 11.48  ? 65  CYS   C C   1 
ATOM   1560 O  O   . CYS   B 1 59  ? 27.895 -28.875 5.744  1.00 12.82  ? 65  CYS   C O   1 
ATOM   1561 C  CB  . CYS   B 1 59  ? 30.109 -28.006 7.404  1.00 10.22  ? 65  CYS   C CB  1 
ATOM   1562 S  SG  . CYS   B 1 59  ? 30.681 -26.939 6.034  1.00 13.08  ? 65  CYS   C SG  1 
ATOM   1563 N  N   . SER   B 1 60  ? 26.759 -27.048 6.400  1.00 12.67  ? 66  SER   C N   1 
ATOM   1564 C  CA  . SER   B 1 60  ? 25.736 -27.179 5.337  1.00 14.68  ? 66  SER   C CA  1 
ATOM   1565 C  C   . SER   B 1 60  ? 26.350 -27.072 3.922  1.00 13.31  ? 66  SER   C C   1 
ATOM   1566 O  O   . SER   B 1 60  ? 25.953 -27.877 3.069  1.00 14.97  ? 66  SER   C O   1 
ATOM   1567 C  CB  . SER   B 1 60  ? 24.655 -26.185 5.627  1.00 17.62  ? 66  SER   C CB  1 
ATOM   1568 O  OG  . SER   B 1 60  ? 25.014 -24.848 5.408  1.00 29.41  ? 66  SER   C OG  1 
ATOM   1569 N  N   . SER   B 1 61  ? 27.372 -26.261 3.761  1.00 12.96  ? 67  SER   C N   1 
ATOM   1570 C  CA  . SER   B 1 61  ? 28.034 -26.084 2.434  1.00 13.37  ? 67  SER   C CA  1 
ATOM   1571 C  C   . SER   B 1 61  ? 28.822 -27.328 2.038  1.00 16.43  ? 67  SER   C C   1 
ATOM   1572 O  O   . SER   B 1 61  ? 29.281 -27.380 0.874  1.00 18.56  ? 67  SER   C O   1 
ATOM   1573 C  CB  . SER   B 1 61  ? 28.896 -24.852 2.432  1.00 14.46  ? 67  SER   C CB  1 
ATOM   1574 O  OG  . SER   B 1 61  ? 30.014 -24.962 3.285  1.00 14.39  ? 67  SER   C OG  1 
ATOM   1575 N  N   . ARG   B 1 62  ? 29.024 -28.323 2.893  1.00 13.12  ? 68  ARG   C N   1 
ATOM   1576 C  CA  . ARG   B 1 62  ? 29.668 -29.596 2.516  1.00 14.72  ? 68  ARG   C CA  1 
ATOM   1577 C  C   . ARG   B 1 62  ? 28.723 -30.773 2.751  1.00 13.98  ? 68  ARG   C C   1 
ATOM   1578 O  O   . ARG   B 1 62  ? 29.162 -31.934 2.589  1.00 15.40  ? 68  ARG   C O   1 
ATOM   1579 C  CB  . ARG   B 1 62  ? 30.972 -29.789 3.298  1.00 13.50  ? 68  ARG   C CB  1 
ATOM   1580 C  CG  . ARG   B 1 62  ? 31.978 -28.662 3.129  1.00 17.97  ? 68  ARG   C CG  1 
ATOM   1581 C  CD  . ARG   B 1 62  ? 32.642 -28.864 1.800  1.00 17.13  ? 68  ARG   C CD  1 
ATOM   1582 N  NE  . ARG   B 1 62  ? 33.661 -27.820 1.562  1.00 19.30  ? 68  ARG   C NE  1 
ATOM   1583 C  CZ  . ARG   B 1 62  ? 33.451 -26.628 1.006  1.00 19.61  ? 68  ARG   C CZ  1 
ATOM   1584 N  NH1 . ARG   B 1 62  ? 32.260 -26.288 0.536  1.00 22.80  ? 68  ARG   C NH1 1 
ATOM   1585 N  NH2 . ARG   B 1 62  ? 34.483 -25.807 0.774  1.00 21.90  ? 68  ARG   C NH2 1 
ATOM   1586 N  N   . ARG   B 1 63  ? 27.548 -30.493 3.294  1.00 15.17  ? 69  ARG   C N   1 
ATOM   1587 C  CA  . ARG   B 1 63  ? 26.580 -31.549 3.690  1.00 17.81  ? 69  ARG   C CA  1 
ATOM   1588 C  C   . ARG   B 1 63  ? 27.287 -32.579 4.573  1.00 16.63  ? 69  ARG   C C   1 
ATOM   1589 O  O   . ARG   B 1 63  ? 27.096 -33.797 4.396  1.00 18.94  ? 69  ARG   C O   1 
ATOM   1590 C  CB  . ARG   B 1 63  ? 25.954 -32.244 2.474  1.00 20.31  ? 69  ARG   C CB  1 
ATOM   1591 C  CG  . ARG   B 1 63  ? 25.106 -31.284 1.663  1.00 23.19  ? 69  ARG   C CG  1 
ATOM   1592 C  CD  . ARG   B 1 63  ? 23.648 -31.567 1.660  1.00 34.24  ? 69  ARG   C CD  1 
ATOM   1593 N  NE  . ARG   B 1 63  ? 22.903 -30.356 1.344  1.00 32.28  ? 69  ARG   C NE  1 
ATOM   1594 C  CZ  . ARG   B 1 63  ? 22.242 -30.109 0.217  1.00 44.31  ? 69  ARG   C CZ  1 
ATOM   1595 N  NH1 . ARG   B 1 63  ? 22.252 -30.956 -0.801 1.00 46.77  ? 69  ARG   C NH1 1 
ATOM   1596 N  NH2 . ARG   B 1 63  ? 21.592 -28.966 0.109  1.00 38.71  ? 69  ARG   C NH2 1 
ATOM   1597 N  N   . LYS   B 1 64  ? 28.052 -32.113 5.567  1.00 15.06  ? 70  LYS   C N   1 
ATOM   1598 C  CA  . LYS   B 1 64  ? 28.896 -33.026 6.365  1.00 16.22  ? 70  LYS   C CA  1 
ATOM   1599 C  C   . LYS   B 1 64  ? 28.909 -32.545 7.812  1.00 14.19  ? 70  LYS   C C   1 
ATOM   1600 O  O   . LYS   B 1 64  ? 29.007 -31.316 8.047  1.00 14.17  ? 70  LYS   C O   1 
ATOM   1601 C  CB  . LYS   B 1 64  ? 30.317 -33.005 5.807  1.00 19.63  ? 70  LYS   C CB  1 
ATOM   1602 C  CG  . LYS   B 1 64  ? 30.671 -34.086 4.805  1.00 31.67  ? 70  LYS   C CG  1 
ATOM   1603 C  CD  . LYS   B 1 64  ? 32.186 -34.323 4.769  1.00 35.36  ? 70  LYS   C CD  1 
ATOM   1604 C  CE  . LYS   B 1 64  ? 32.613 -35.333 3.727  1.00 42.55  ? 70  LYS   C CE  1 
ATOM   1605 N  NZ  . LYS   B 1 64  ? 31.981 -35.085 2.412  1.00 48.53  ? 70  LYS   C NZ  1 
ATOM   1606 N  N   . HIS   B 1 65  ? 29.047 -33.497 8.720  1.00 13.27  ? 71  HIS   C N   1 
ATOM   1607 C  CA  . HIS   B 1 65  ? 29.368 -33.265 10.151 1.00 13.20  ? 71  HIS   C CA  1 
ATOM   1608 C  C   . HIS   B 1 65  ? 30.832 -33.528 10.348 1.00 13.22  ? 71  HIS   C C   1 
ATOM   1609 O  O   . HIS   B 1 65  ? 31.320 -34.643 10.021 1.00 17.61  ? 71  HIS   C O   1 
ATOM   1610 C  CB  . HIS   B 1 65  ? 28.530 -34.168 11.042 1.00 12.69  ? 71  HIS   C CB  1 
ATOM   1611 C  CG  . HIS   B 1 65  ? 27.074 -33.883 10.980 1.00 12.10  ? 71  HIS   C CG  1 
ATOM   1612 N  ND1 . HIS   B 1 65  ? 26.366 -33.098 11.904 1.00 14.23  ? 71  HIS   C ND1 1 
ATOM   1613 C  CD2 . HIS   B 1 65  ? 26.160 -34.303 10.071 1.00 11.50  ? 71  HIS   C CD2 1 
ATOM   1614 C  CE1 . HIS   B 1 65  ? 25.088 -33.105 11.570 1.00 12.29  ? 71  HIS   C CE1 1 
ATOM   1615 N  NE2 . HIS   B 1 65  ? 24.927 -33.814 10.495 1.00 14.85  ? 71  HIS   C NE2 1 
ATOM   1616 N  N   . TYR   B 1 66  ? 31.585 -32.586 10.889 1.00 11.61  ? 72  TYR   C N   1 
ATOM   1617 C  CA  . TYR   B 1 66  ? 33.048 -32.723 11.035 1.00 11.61  ? 72  TYR   C CA  1 
ATOM   1618 C  C   . TYR   B 1 66  ? 33.407 -32.754 12.524 1.00 11.34  ? 72  TYR   C C   1 
ATOM   1619 O  O   . TYR   B 1 66  ? 32.943 -31.886 13.300 1.00 11.26  ? 72  TYR   C O   1 
ATOM   1620 C  CB  . TYR   B 1 66  ? 33.798 -31.518 10.482 1.00 11.85  ? 72  TYR   C CB  1 
ATOM   1621 C  CG  . TYR   B 1 66  ? 33.764 -31.402 8.971  1.00 13.01  ? 72  TYR   C CG  1 
ATOM   1622 C  CD1 . TYR   B 1 66  ? 34.627 -32.150 8.180  1.00 15.44  ? 72  TYR   C CD1 1 
ATOM   1623 C  CD2 . TYR   B 1 66  ? 32.958 -30.495 8.318  1.00 13.90  ? 72  TYR   C CD2 1 
ATOM   1624 C  CE1 . TYR   B 1 66  ? 34.658 -32.042 6.791  1.00 16.21  ? 72  TYR   C CE1 1 
ATOM   1625 C  CE2 . TYR   B 1 66  ? 32.971 -30.361 6.930  1.00 16.06  ? 72  TYR   C CE2 1 
ATOM   1626 C  CZ  . TYR   B 1 66  ? 33.825 -31.137 6.180  1.00 15.09  ? 72  TYR   C CZ  1 
ATOM   1627 O  OH  . TYR   B 1 66  ? 33.776 -30.944 4.802  1.00 17.57  ? 72  TYR   C OH  1 
ATOM   1628 N  N   . PRO   B 1 67  ? 34.201 -33.750 12.971 1.00 11.32  ? 73  PRO   C N   1 
ATOM   1629 C  CA  . PRO   B 1 67  ? 34.758 -33.735 14.323 1.00 10.91  ? 73  PRO   C CA  1 
ATOM   1630 C  C   . PRO   B 1 67  ? 35.852 -32.677 14.424 1.00 11.41  ? 73  PRO   C C   1 
ATOM   1631 O  O   . PRO   B 1 67  ? 36.749 -32.598 13.540 1.00 13.92  ? 73  PRO   C O   1 
ATOM   1632 C  CB  . PRO   B 1 67  ? 35.298 -35.152 14.523 1.00 12.26  ? 73  PRO   C CB  1 
ATOM   1633 C  CG  . PRO   B 1 67  ? 35.532 -35.680 13.143 1.00 14.56  ? 73  PRO   C CG  1 
ATOM   1634 C  CD  . PRO   B 1 67  ? 34.629 -34.936 12.184 1.00 12.22  ? 73  PRO   C CD  1 
ATOM   1635 N  N   . VAL   B 1 68  ? 35.822 -31.861 15.467 1.00 11.08  ? 74  VAL   C N   1 
ATOM   1636 C  CA  . VAL   B 1 68  ? 36.779 -30.752 15.616 1.00 11.02  ? 74  VAL   C CA  1 
ATOM   1637 C  C   . VAL   B 1 68  ? 37.205 -30.617 17.067 1.00 11.13  ? 74  VAL   C C   1 
ATOM   1638 O  O   . VAL   B 1 68  ? 36.425 -30.877 17.987 1.00 11.08  ? 74  VAL   C O   1 
ATOM   1639 C  CB  . VAL   B 1 68  ? 36.191 -29.412 15.126 1.00 13.05  ? 74  VAL   C CB  1 
ATOM   1640 C  CG1 . VAL   B 1 68  ? 36.076 -29.354 13.603 1.00 14.78  ? 74  VAL   C CG1 1 
ATOM   1641 C  CG2 . VAL   B 1 68  ? 34.878 -29.077 15.817 1.00 13.65  ? 74  VAL   C CG2 1 
ATOM   1642 N  N   . SER   B 1 69  ? 38.406 -30.086 17.231 1.00 11.23  ? 75  SER   C N   1 
ATOM   1643 C  CA  . SER   B 1 69  ? 38.871 -29.380 18.443 1.00 11.41  ? 75  SER   C CA  1 
ATOM   1644 C  C   . SER   B 1 69  ? 38.572 -27.891 18.348 1.00 10.72  ? 75  SER   C C   1 
ATOM   1645 O  O   . SER   B 1 69  ? 38.731 -27.310 17.260 1.00 11.54  ? 75  SER   C O   1 
ATOM   1646 C  CB  . SER   B 1 69  ? 40.369 -29.574 18.634 1.00 14.66  ? 75  SER   C CB  1 
ATOM   1647 O  OG  . SER   B 1 69  ? 40.625 -30.949 18.779 1.00 18.74  ? 75  SER   C OG  1 
ATOM   1648 N  N   . PHE   B 1 70  ? 38.120 -27.284 19.428 1.00 10.59  ? 76  PHE   C N   1 
ATOM   1649 C  CA  . PHE   B 1 70  ? 37.738 -25.856 19.400 1.00 10.51  ? 76  PHE   C CA  1 
ATOM   1650 C  C   . PHE   B 1 70  ? 38.227 -25.169 20.658 1.00 11.54  ? 76  PHE   C C   1 
ATOM   1651 O  O   . PHE   B 1 70  ? 38.380 -25.769 21.718 1.00 11.23  ? 76  PHE   C O   1 
ATOM   1652 C  CB  . PHE   B 1 70  ? 36.229 -25.657 19.175 1.00 10.92  ? 76  PHE   C CB  1 
ATOM   1653 C  CG  . PHE   B 1 70  ? 35.307 -26.343 20.154 1.00 10.27  ? 76  PHE   C CG  1 
ATOM   1654 C  CD1 . PHE   B 1 70  ? 34.906 -27.657 19.973 1.00 10.43  ? 76  PHE   C CD1 1 
ATOM   1655 C  CD2 . PHE   B 1 70  ? 34.897 -25.686 21.302 1.00 10.85  ? 76  PHE   C CD2 1 
ATOM   1656 C  CE1 . PHE   B 1 70  ? 34.077 -28.266 20.896 1.00 9.77   ? 76  PHE   C CE1 1 
ATOM   1657 C  CE2 . PHE   B 1 70  ? 34.074 -26.313 22.220 1.00 10.16  ? 76  PHE   C CE2 1 
ATOM   1658 C  CZ  . PHE   B 1 70  ? 33.666 -27.590 22.027 1.00 10.08  ? 76  PHE   C CZ  1 
ATOM   1659 N  N   . SER   B 1 71  ? 38.487 -23.874 20.546 1.00 10.56  ? 77  SER   C N   1 
ATOM   1660 C  CA  . SER   B 1 71  ? 39.119 -23.051 21.571 1.00 12.15  ? 77  SER   C CA  1 
ATOM   1661 C  C   . SER   B 1 71  ? 38.125 -22.676 22.662 1.00 13.62  ? 77  SER   C C   1 
ATOM   1662 O  O   . SER   B 1 71  ? 36.928 -22.946 22.608 1.00 13.68  ? 77  SER   C O   1 
ATOM   1663 C  CB  . SER   B 1 71  ? 39.821 -21.871 20.943 1.00 12.88  ? 77  SER   C CB  1 
ATOM   1664 O  OG  . SER   B 1 71  ? 38.906 -20.939 20.353 1.00 14.41  ? 77  SER   C OG  1 
ATOM   1665 N  N   . LYS   B 1 72  ? 38.641 -22.036 23.698 1.00 15.94  ? 78  LYS   C N   1 
ATOM   1666 C  CA  . LYS   B 1 72  ? 37.813 -21.591 24.837 1.00 16.21  ? 78  LYS   C CA  1 
ATOM   1667 C  C   . LYS   B 1 72  ? 37.058 -20.321 24.423 1.00 14.52  ? 78  LYS   C C   1 
ATOM   1668 O  O   . LYS   B 1 72  ? 37.588 -19.525 23.674 1.00 16.16  ? 78  LYS   C O   1 
ATOM   1669 C  CB  . LYS   B 1 72  ? 38.769 -21.288 26.002 1.00 21.89  ? 78  LYS   C CB  1 
ATOM   1670 C  CG  . LYS   B 1 72  ? 39.565 -22.501 26.467 1.00 25.98  ? 78  LYS   C CG  1 
ATOM   1671 C  CD  . LYS   B 1 72  ? 39.700 -22.659 28.000 1.00 38.61  ? 78  LYS   C CD  1 
ATOM   1672 C  CE  . LYS   B 1 72  ? 39.686 -24.120 28.435 1.00 43.66  ? 78  LYS   C CE  1 
ATOM   1673 N  NZ  . LYS   B 1 72  ? 39.495 -24.280 29.898 1.00 48.21  ? 78  LYS   C NZ  1 
ATOM   1674 N  N   . PRO   B 1 73  ? 35.800 -20.066 24.881 1.00 13.66  ? 79  PRO   C N   1 
ATOM   1675 C  CA  . PRO   B 1 73  ? 35.055 -18.853 24.492 1.00 13.62  ? 79  PRO   C CA  1 
ATOM   1676 C  C   . PRO   B 1 73  ? 35.814 -17.572 24.848 1.00 14.02  ? 79  PRO   C C   1 
ATOM   1677 O  O   . PRO   B 1 73  ? 36.201 -17.442 26.024 1.00 16.70  ? 79  PRO   C O   1 
ATOM   1678 C  CB  . PRO   B 1 73  ? 33.744 -18.914 25.290 1.00 15.04  ? 79  PRO   C CB  1 
ATOM   1679 C  CG  . PRO   B 1 73  ? 33.644 -20.312 25.801 1.00 17.59  ? 79  PRO   C CG  1 
ATOM   1680 C  CD  . PRO   B 1 73  ? 35.035 -20.901 25.819 1.00 15.05  ? 79  PRO   C CD  1 
ATOM   1681 N  N   . SER   B 1 74  ? 36.073 -16.710 23.877 1.00 13.21  ? 80  SER   C N   1 
ATOM   1682 C  CA  . SER   B 1 74  ? 36.966 -15.551 24.066 1.00 14.67  ? 80  SER   C CA  1 
ATOM   1683 C  C   . SER   B 1 74  ? 36.500 -14.377 23.206 1.00 14.83  ? 80  SER   C C   1 
ATOM   1684 O  O   . SER   B 1 74  ? 35.648 -14.545 22.332 1.00 13.99  ? 80  SER   C O   1 
ATOM   1685 C  CB  . SER   B 1 74  ? 38.395 -15.906 23.705 1.00 17.29  ? 80  SER   C CB  1 
ATOM   1686 O  OG  . SER   B 1 74  ? 38.817 -17.067 24.420 1.00 24.16  ? 80  SER   C OG  1 
ATOM   1687 N  N   . LEU   B 1 75  ? 37.192 -13.258 23.375 1.00 14.59  ? 81  LEU   C N   1 
ATOM   1688 C  CA  . LEU   B 1 75  ? 37.011 -12.024 22.584 1.00 15.56  ? 81  LEU   C CA  1 
ATOM   1689 C  C   . LEU   B 1 75  ? 38.017 -12.059 21.433 1.00 17.42  ? 81  LEU   C C   1 
ATOM   1690 O  O   . LEU   B 1 75  ? 39.265 -12.014 21.724 1.00 19.56  ? 81  LEU   C O   1 
ATOM   1691 C  CB  . LEU   B 1 75  ? 37.210 -10.813 23.511 1.00 18.51  ? 81  LEU   C CB  1 
ATOM   1692 C  CG  . LEU   B 1 75  ? 37.015 -9.442  22.871 1.00 20.41  ? 81  LEU   C CG  1 
ATOM   1693 C  CD1 . LEU   B 1 75  ? 35.561 -9.187  22.528 1.00 21.26  ? 81  LEU   C CD1 1 
ATOM   1694 C  CD2 . LEU   B 1 75  ? 37.507 -8.336  23.819 1.00 22.82  ? 81  LEU   C CD2 1 
ATOM   1695 N  N   . ILE   B 1 76  ? 37.569 -12.290 20.206 1.00 17.85  ? 82  ILE   C N   1 
ATOM   1696 C  CA  . ILE   B 1 76  ? 38.406 -12.602 19.019 1.00 19.50  ? 82  ILE   C CA  1 
ATOM   1697 C  C   . ILE   B 1 76  ? 38.146 -11.472 18.017 1.00 21.62  ? 82  ILE   C C   1 
ATOM   1698 O  O   . ILE   B 1 76  ? 36.943 -11.160 17.758 1.00 17.67  ? 82  ILE   C O   1 
ATOM   1699 C  CB  . ILE   B 1 76  ? 38.014 -13.973 18.431 1.00 22.42  ? 82  ILE   C CB  1 
ATOM   1700 C  CG1 . ILE   B 1 76  ? 38.251 -15.150 19.378 1.00 26.32  ? 82  ILE   C CG1 1 
ATOM   1701 C  CG2 . ILE   B 1 76  ? 38.685 -14.225 17.080 1.00 24.88  ? 82  ILE   C CG2 1 
ATOM   1702 C  CD1 . ILE   B 1 76  ? 39.696 -15.429 19.638 1.00 27.17  ? 82  ILE   C CD1 1 
ATOM   1703 N  N   . PHE   B 1 77  ? 39.181 -10.909 17.395 1.00 20.24  ? 83  PHE   C N   1 
ATOM   1704 C  CA  . PHE   B 1 77  ? 38.995 -10.044 16.204 1.00 19.39  ? 83  PHE   C CA  1 
ATOM   1705 C  C   . PHE   B 1 77  ? 38.629 -10.918 14.991 1.00 20.04  ? 83  PHE   C C   1 
ATOM   1706 O  O   . PHE   B 1 77  ? 39.365 -11.845 14.625 1.00 23.23  ? 83  PHE   C O   1 
ATOM   1707 C  CB  . PHE   B 1 77  ? 40.243 -9.188  15.934 1.00 21.22  ? 83  PHE   C CB  1 
ATOM   1708 C  CG  . PHE   B 1 77  ? 39.970 -8.018  15.013 1.00 20.19  ? 83  PHE   C CG  1 
ATOM   1709 C  CD1 . PHE   B 1 77  ? 39.251 -6.913  15.446 1.00 20.72  ? 83  PHE   C CD1 1 
ATOM   1710 C  CD2 . PHE   B 1 77  ? 40.332 -8.095  13.674 1.00 22.13  ? 83  PHE   C CD2 1 
ATOM   1711 C  CE1 . PHE   B 1 77  ? 38.986 -5.866  14.578 1.00 22.17  ? 83  PHE   C CE1 1 
ATOM   1712 C  CE2 . PHE   B 1 77  ? 40.067 -7.046  12.805 1.00 21.29  ? 83  PHE   C CE2 1 
ATOM   1713 C  CZ  . PHE   B 1 77  ? 39.373 -5.946  13.259 1.00 21.36  ? 83  PHE   C CZ  1 
ATOM   1714 N  N   . VAL   B 1 78  ? 37.521 -10.570 14.307 1.00 17.37  ? 84  VAL   C N   1 
ATOM   1715 C  CA  . VAL   B 1 78  ? 36.942 -11.267 13.136 1.00 16.77  ? 84  VAL   C CA  1 
ATOM   1716 C  C   . VAL   B 1 78  ? 37.052 -10.320 11.934 1.00 16.94  ? 84  VAL   C C   1 
ATOM   1717 O  O   . VAL   B 1 78  ? 36.587 -9.150  12.045 1.00 16.76  ? 84  VAL   C O   1 
ATOM   1718 C  CB  . VAL   B 1 78  ? 35.477 -11.686 13.453 1.00 16.17  ? 84  VAL   C CB  1 
ATOM   1719 C  CG1 . VAL   B 1 78  ? 34.866 -12.494 12.334 1.00 16.24  ? 84  VAL   C CG1 1 
ATOM   1720 C  CG2 . VAL   B 1 78  ? 35.382 -12.447 14.763 1.00 17.01  ? 84  VAL   C CG2 1 
ATOM   1721 N  N   . GLU   B 1 79  ? 37.573 -10.784 10.798 1.00 16.37  ? 85  GLU   C N   1 
ATOM   1722 C  CA  . GLU   B 1 79  ? 37.601 -10.005 9.539  1.00 18.53  ? 85  GLU   C CA  1 
ATOM   1723 C  C   . GLU   B 1 79  ? 36.182 -9.746  9.027  1.00 16.37  ? 85  GLU   C C   1 
ATOM   1724 O  O   . GLU   B 1 79  ? 35.209 -10.427 9.453  1.00 15.30  ? 85  GLU   C O   1 
ATOM   1725 C  CB  . GLU   B 1 79  ? 38.470 -10.692 8.483  1.00 22.68  ? 85  GLU   C CB  1 
ATOM   1726 C  CG  . GLU   B 1 79  ? 39.952 -10.713 8.887  1.00 27.05  ? 85  GLU   C CG  1 
ATOM   1727 C  CD  . GLU   B 1 79  ? 40.573 -9.339  9.150  1.00 29.99  ? 85  GLU   C CD  1 
ATOM   1728 O  OE1 . GLU   B 1 79  ? 40.292 -8.380  8.373  1.00 35.92  ? 85  GLU   C OE1 1 
ATOM   1729 O  OE2 . GLU   B 1 79  ? 41.285 -9.183  10.163 1.00 33.97  ? 85  GLU   C OE2 1 
ATOM   1730 N  N   . ALA   B 1 80  ? 36.036 -8.737  8.200  1.00 16.65  ? 86  ALA   C N   1 
ATOM   1731 C  CA  . ALA   B 1 80  ? 34.729 -8.388  7.638  1.00 17.67  ? 86  ALA   C CA  1 
ATOM   1732 C  C   . ALA   B 1 80  ? 34.134 -9.609  6.952  1.00 19.06  ? 86  ALA   C C   1 
ATOM   1733 O  O   . ALA   B 1 80  ? 34.863 -10.408 6.331  1.00 19.43  ? 86  ALA   C O   1 
ATOM   1734 C  CB  . ALA   B 1 80  ? 34.898 -7.268  6.620  1.00 19.52  ? 86  ALA   C CB  1 
ATOM   1735 N  N   . SER   B 1 81  ? 32.831 -9.763  7.076  1.00 15.87  ? 87  SER   C N   1 
ATOM   1736 C  CA  . SER   B 1 81  ? 32.089 -10.820 6.389  1.00 18.17  ? 87  SER   C CA  1 
ATOM   1737 C  C   . SER   B 1 81  ? 30.998 -10.173 5.556  1.00 17.79  ? 87  SER   C C   1 
ATOM   1738 O  O   . SER   B 1 81  ? 30.854 -8.935  5.572  1.00 18.28  ? 87  SER   C O   1 
ATOM   1739 C  CB  . SER   B 1 81  ? 31.515 -11.749 7.412  1.00 16.61  ? 87  SER   C CB  1 
ATOM   1740 O  OG  . SER   B 1 81  ? 30.465 -11.096 8.136  1.00 16.00  ? 87  SER   C OG  1 
ATOM   1741 N  N   . GLU   B 1 82  ? 30.168 -10.953 4.920  1.00 20.27  ? 88  GLU   C N   1 
ATOM   1742 C  CA  . GLU   B 1 82  ? 29.077 -10.308 4.151  1.00 21.47  ? 88  GLU   C CA  1 
ATOM   1743 C  C   . GLU   B 1 82  ? 28.027 -9.698  5.095  1.00 22.58  ? 88  GLU   C C   1 
ATOM   1744 O  O   . GLU   B 1 82  ? 27.265 -8.844  4.632  1.00 22.79  ? 88  GLU   C O   1 
ATOM   1745 C  CB  . GLU   B 1 82  ? 28.540 -11.269 3.103  1.00 26.15  ? 88  GLU   C CB  1 
ATOM   1746 C  CG  . GLU   B 1 82  ? 27.701 -12.381 3.642  1.00 32.82  ? 88  GLU   C CG  1 
ATOM   1747 C  CD  . GLU   B 1 82  ? 26.995 -13.179 2.554  1.00 33.93  ? 88  GLU   C CD  1 
ATOM   1748 O  OE1 . GLU   B 1 82  ? 27.640 -13.450 1.522  1.00 37.01  ? 88  GLU   C OE1 1 
ATOM   1749 O  OE2 . GLU   B 1 82  ? 25.802 -13.521 2.758  1.00 37.14  ? 88  GLU   C OE2 1 
ATOM   1750 N  N   . TYR   B 1 83  ? 28.046 -9.979  6.387  1.00 18.15  ? 89  TYR   C N   1 
ATOM   1751 C  CA  . TYR   B 1 83  ? 26.990 -9.527  7.316  1.00 17.13  ? 89  TYR   C CA  1 
ATOM   1752 C  C   . TYR   B 1 83  ? 27.512 -8.693  8.499  1.00 18.02  ? 89  TYR   C C   1 
ATOM   1753 O  O   . TYR   B 1 83  ? 26.682 -8.118  9.227  1.00 17.68  ? 89  TYR   C O   1 
ATOM   1754 C  CB  . TYR   B 1 83  ? 26.174 -10.741 7.800  1.00 16.84  ? 89  TYR   C CB  1 
ATOM   1755 C  CG  . TYR   B 1 83  ? 26.986 -11.939 8.267  1.00 16.03  ? 89  TYR   C CG  1 
ATOM   1756 C  CD1 . TYR   B 1 83  ? 27.377 -12.956 7.384  1.00 16.00  ? 89  TYR   C CD1 1 
ATOM   1757 C  CD2 . TYR   B 1 83  ? 27.406 -12.058 9.584  1.00 14.56  ? 89  TYR   C CD2 1 
ATOM   1758 C  CE1 . TYR   B 1 83  ? 28.154 -14.045 7.793  1.00 14.50  ? 89  TYR   C CE1 1 
ATOM   1759 C  CE2 . TYR   B 1 83  ? 28.165 -13.128 10.010 1.00 14.98  ? 89  TYR   C CE2 1 
ATOM   1760 C  CZ  . TYR   B 1 83  ? 28.567 -14.118 9.111  1.00 15.29  ? 89  TYR   C CZ  1 
ATOM   1761 O  OH  . TYR   B 1 83  ? 29.350 -15.178 9.526  1.00 16.19  ? 89  TYR   C OH  1 
ATOM   1762 N  N   . TYR   B 1 84  ? 28.822 -8.572  8.767  1.00 15.29  ? 90  TYR   C N   1 
ATOM   1763 C  CA  . TYR   B 1 84  ? 29.396 -7.669  9.787  1.00 14.98  ? 90  TYR   C CA  1 
ATOM   1764 C  C   . TYR   B 1 84  ? 30.685 -7.040  9.262  1.00 14.50  ? 90  TYR   C C   1 
ATOM   1765 O  O   . TYR   B 1 84  ? 31.404 -7.667  8.487  1.00 15.51  ? 90  TYR   C O   1 
ATOM   1766 C  CB  . TYR   B 1 84  ? 29.739 -8.419  11.091 1.00 13.74  ? 90  TYR   C CB  1 
ATOM   1767 C  CG  . TYR   B 1 84  ? 28.566 -8.822  11.959 1.00 13.68  ? 90  TYR   C CG  1 
ATOM   1768 C  CD1 . TYR   B 1 84  ? 27.646 -7.910  12.478 1.00 14.87  ? 90  TYR   C CD1 1 
ATOM   1769 C  CD2 . TYR   B 1 84  ? 28.359 -10.140 12.281 1.00 13.15  ? 90  TYR   C CD2 1 
ATOM   1770 C  CE1 . TYR   B 1 84  ? 26.586 -8.296  13.295 1.00 13.80  ? 90  TYR   C CE1 1 
ATOM   1771 C  CE2 . TYR   B 1 84  ? 27.301 -10.547 13.077 1.00 13.07  ? 90  TYR   C CE2 1 
ATOM   1772 C  CZ  . TYR   B 1 84  ? 26.383 -9.642  13.559 1.00 13.10  ? 90  TYR   C CZ  1 
ATOM   1773 O  OH  . TYR   B 1 84  ? 25.328 -10.033 14.350 1.00 13.94  ? 90  TYR   C OH  1 
ATOM   1774 N  N   . PRO   B 1 85  ? 31.068 -5.829  9.742  1.00 16.23  ? 91  PRO   C N   1 
ATOM   1775 C  CA  . PRO   B 1 85  ? 32.406 -5.320  9.440  1.00 16.40  ? 91  PRO   C CA  1 
ATOM   1776 C  C   . PRO   B 1 85  ? 33.429 -6.121  10.240 1.00 17.27  ? 91  PRO   C C   1 
ATOM   1777 O  O   . PRO   B 1 85  ? 33.077 -6.896  11.154 1.00 15.57  ? 91  PRO   C O   1 
ATOM   1778 C  CB  . PRO   B 1 85  ? 32.308 -3.870  9.932  1.00 16.27  ? 91  PRO   C CB  1 
ATOM   1779 C  CG  . PRO   B 1 85  ? 31.391 -3.941  11.099 1.00 15.76  ? 91  PRO   C CG  1 
ATOM   1780 C  CD  . PRO   B 1 85  ? 30.353 -5.006  10.748 1.00 16.54  ? 91  PRO   C CD  1 
ATOM   1781 N  N   . ALA   B 1 86  ? 34.717 -5.847  9.990  1.00 16.67  ? 92  ALA   C N   1 
ATOM   1782 C  CA  . ALA   B 1 86  ? 35.775 -6.371  10.871 1.00 16.84  ? 92  ALA   C CA  1 
ATOM   1783 C  C   . ALA   B 1 86  ? 35.558 -5.800  12.278 1.00 17.56  ? 92  ALA   C C   1 
ATOM   1784 O  O   . ALA   B 1 86  ? 35.344 -4.543  12.408 1.00 19.32  ? 92  ALA   C O   1 
ATOM   1785 C  CB  . ALA   B 1 86  ? 37.126 -5.998  10.280 1.00 16.92  ? 92  ALA   C CB  1 
ATOM   1786 N  N   . ARG   B 1 87  ? 35.592 -6.628  13.312 1.00 15.65  ? 93  ARG   C N   1 
ATOM   1787 C  CA  . ARG   B 1 87  ? 35.266 -6.220  14.694 1.00 15.87  ? 93  ARG   C CA  1 
ATOM   1788 C  C   . ARG   B 1 87  ? 35.691 -7.309  15.663 1.00 16.25  ? 93  ARG   C C   1 
ATOM   1789 O  O   . ARG   B 1 87  ? 35.938 -8.450  15.245 1.00 16.59  ? 93  ARG   C O   1 
ATOM   1790 C  CB  . ARG   B 1 87  ? 33.777 -5.935  14.873 1.00 16.54  ? 93  ARG   C CB  1 
ATOM   1791 C  CG  . ARG   B 1 87  ? 32.948 -7.211  14.744 1.00 16.06  ? 93  ARG   C CG  1 
ATOM   1792 C  CD  . ARG   B 1 87  ? 31.450 -6.953  14.830 1.00 16.39  ? 93  ARG   C CD  1 
ATOM   1793 N  NE  . ARG   B 1 87  ? 30.733 -8.213  15.076 1.00 16.63  ? 93  ARG   C NE  1 
ATOM   1794 C  CZ  . ARG   B 1 87  ? 29.643 -8.383  15.825 1.00 16.95  ? 93  ARG   C CZ  1 
ATOM   1795 N  NH1 . ARG   B 1 87  ? 29.026 -7.366  16.405 1.00 17.66  ? 93  ARG   C NH1 1 
ATOM   1796 N  NH2 . ARG   B 1 87  ? 29.204 -9.615  15.996 1.00 17.39  ? 93  ARG   C NH2 1 
ATOM   1797 N  N   . TYR   B 1 88  ? 35.710 -6.967  16.951 1.00 18.07  ? 94  TYR   C N   1 
ATOM   1798 C  CA  . TYR   B 1 88  ? 35.780 -7.937  18.063 1.00 19.74  ? 94  TYR   C CA  1 
ATOM   1799 C  C   . TYR   B 1 88  ? 34.398 -8.572  18.262 1.00 18.55  ? 94  TYR   C C   1 
ATOM   1800 O  O   . TYR   B 1 88  ? 33.379 -7.873  18.342 1.00 19.20  ? 94  TYR   C O   1 
ATOM   1801 C  CB  . TYR   B 1 88  ? 36.247 -7.232  19.336 1.00 25.04  ? 94  TYR   C CB  1 
ATOM   1802 C  CG  . TYR   B 1 88  ? 37.712 -6.880  19.294 1.00 26.09  ? 94  TYR   C CG  1 
ATOM   1803 C  CD1 . TYR   B 1 88  ? 38.678 -7.846  19.499 1.00 28.44  ? 94  TYR   C CD1 1 
ATOM   1804 C  CD2 . TYR   B 1 88  ? 38.114 -5.585  18.982 1.00 29.54  ? 94  TYR   C CD2 1 
ATOM   1805 C  CE1 . TYR   B 1 88  ? 40.034 -7.535  19.446 1.00 29.75  ? 94  TYR   C CE1 1 
ATOM   1806 C  CE2 . TYR   B 1 88  ? 39.453 -5.262  18.913 1.00 31.59  ? 94  TYR   C CE2 1 
ATOM   1807 C  CZ  . TYR   B 1 88  ? 40.409 -6.233  19.150 1.00 33.80  ? 94  TYR   C CZ  1 
ATOM   1808 O  OH  . TYR   B 1 88  ? 41.729 -5.886  19.070 1.00 39.19  ? 94  TYR   C OH  1 
ATOM   1809 N  N   . GLN   B 1 89  ? 34.370 -9.897  18.339 1.00 16.40  ? 95  GLN   C N   1 
ATOM   1810 C  CA  . GLN   B 1 89  ? 33.167 -10.694 18.715 1.00 14.91  ? 95  GLN   C CA  1 
ATOM   1811 C  C   . GLN   B 1 89  ? 33.486 -11.400 20.014 1.00 14.02  ? 95  GLN   C C   1 
ATOM   1812 O  O   . GLN   B 1 89  ? 34.588 -12.012 20.096 1.00 15.41  ? 95  GLN   C O   1 
ATOM   1813 C  CB  . GLN   B 1 89  ? 32.800 -11.612 17.549 1.00 15.43  ? 95  GLN   C CB  1 
ATOM   1814 C  CG  . GLN   B 1 89  ? 31.531 -12.388 17.788 1.00 16.35  ? 95  GLN   C CG  1 
ATOM   1815 C  CD  . GLN   B 1 89  ? 30.841 -12.937 16.573 1.00 14.39  ? 95  GLN   C CD  1 
ATOM   1816 O  OE1 . GLN   B 1 89  ? 30.824 -12.380 15.479 1.00 14.97  ? 95  GLN   C OE1 1 
ATOM   1817 N  NE2 . GLN   B 1 89  ? 30.266 -14.101 16.786 1.00 14.85  ? 95  GLN   C NE2 1 
ATOM   1818 N  N   . SER   B 1 90  ? 32.610 -11.372 20.946 1.00 12.67  ? 96  SER   C N   1 
ATOM   1819 C  CA  . SER   B 1 90  ? 32.764 -11.973 22.262 1.00 13.27  ? 96  SER   C CA  1 
ATOM   1820 C  C   . SER   B 1 90  ? 32.181 -13.405 22.290 1.00 12.76  ? 96  SER   C C   1 
ATOM   1821 O  O   . SER   B 1 90  ? 31.336 -13.761 21.486 1.00 12.52  ? 96  SER   C O   1 
ATOM   1822 C  CB  . SER   B 1 90  ? 32.181 -11.075 23.364 1.00 16.02  ? 96  SER   C CB  1 
ATOM   1823 O  OG  . SER   B 1 90  ? 30.788 -11.112 23.255 1.00 16.36  ? 96  SER   C OG  1 
ATOM   1824 N  N   . HIS   B 1 91  ? 32.595 -14.191 23.294 1.00 12.24  ? 97  HIS   C N   1 
ATOM   1825 C  CA  . HIS   B 1 91  ? 32.117 -15.579 23.586 1.00 12.61  ? 97  HIS   C CA  1 
ATOM   1826 C  C   . HIS   B 1 91  ? 32.249 -16.447 22.328 1.00 12.88  ? 97  HIS   C C   1 
ATOM   1827 O  O   . HIS   B 1 91  ? 31.329 -17.261 22.079 1.00 13.18  ? 97  HIS   C O   1 
ATOM   1828 C  CB  . HIS   B 1 91  ? 30.675 -15.536 24.148 1.00 13.47  ? 97  HIS   C CB  1 
ATOM   1829 C  CG  . HIS   B 1 91  ? 30.534 -14.779 25.439 1.00 14.24  ? 97  HIS   C CG  1 
ATOM   1830 N  ND1 . HIS   B 1 91  ? 30.557 -15.380 26.662 1.00 16.14  ? 97  HIS   C ND1 1 
ATOM   1831 C  CD2 . HIS   B 1 91  ? 30.449 -13.432 25.666 1.00 14.99  ? 97  HIS   C CD2 1 
ATOM   1832 C  CE1 . HIS   B 1 91  ? 30.451 -14.439 27.608 1.00 16.40  ? 97  HIS   C CE1 1 
ATOM   1833 N  NE2 . HIS   B 1 91  ? 30.371 -13.227 27.019 1.00 16.09  ? 97  HIS   C NE2 1 
ATOM   1834 N  N   . LEU   B 1 92  ? 33.321 -16.299 21.578 1.00 11.15  ? 98  LEU   C N   1 
ATOM   1835 C  CA  . LEU   B 1 92  ? 33.548 -16.993 20.303 1.00 12.13  ? 98  LEU   C CA  1 
ATOM   1836 C  C   . LEU   B 1 92  ? 34.616 -18.066 20.519 1.00 11.69  ? 98  LEU   C C   1 
ATOM   1837 O  O   . LEU   B 1 92  ? 35.580 -17.810 21.202 1.00 12.37  ? 98  LEU   C O   1 
ATOM   1838 C  CB  . LEU   B 1 92  ? 34.015 -16.006 19.218 1.00 13.86  ? 98  LEU   C CB  1 
ATOM   1839 C  CG  . LEU   B 1 92  ? 34.114 -16.536 17.795 1.00 14.39  ? 98  LEU   C CG  1 
ATOM   1840 C  CD1 . LEU   B 1 92  ? 32.757 -16.885 17.242 1.00 15.05  ? 98  LEU   C CD1 1 
ATOM   1841 C  CD2 . LEU   B 1 92  ? 34.796 -15.557 16.863 1.00 14.79  ? 98  LEU   C CD2 1 
ATOM   1842 N  N   . MET   B 1 93  ? 34.419 -19.205 19.862 1.00 11.45  ? 99  MET   C N   1 
ATOM   1843 C  CA  . MET   B 1 93  ? 35.354 -20.353 19.906 1.00 11.00  ? 99  MET   C CA  1 
ATOM   1844 C  C   . MET   B 1 93  ? 35.750 -20.653 18.457 1.00 12.11  ? 99  MET   C C   1 
ATOM   1845 O  O   . MET   B 1 93  ? 34.875 -20.699 17.590 1.00 12.00  ? 99  MET   C O   1 
ATOM   1846 C  CB  . MET   B 1 93  ? 34.639 -21.554 20.508 1.00 12.57  ? 99  MET   C CB  1 
ATOM   1847 C  CG  . MET   B 1 93  ? 34.160 -21.294 21.923 1.00 14.12  ? 99  MET   C CG  1 
ATOM   1848 S  SD  . MET   B 1 93  ? 33.124 -22.621 22.532 1.00 14.68  ? 99  MET   C SD  1 
ATOM   1849 C  CE  . MET   B 1 93  ? 31.674 -22.438 21.482 1.00 15.05  ? 99  MET   C CE  1 
ATOM   1850 N  N   . LEU   B 1 94  ? 37.025 -20.906 18.164 1.00 11.51  ? 100 LEU   C N   1 
ATOM   1851 C  CA  . LEU   B 1 94  ? 37.495 -21.198 16.800 1.00 12.22  ? 100 LEU   C CA  1 
ATOM   1852 C  C   . LEU   B 1 94  ? 37.929 -22.667 16.685 1.00 11.61  ? 100 LEU   C C   1 
ATOM   1853 O  O   . LEU   B 1 94  ? 38.450 -23.248 17.665 1.00 12.75  ? 100 LEU   C O   1 
ATOM   1854 C  CB  . LEU   B 1 94  ? 38.727 -20.367 16.414 1.00 13.15  ? 100 LEU   C CB  1 
ATOM   1855 C  CG  . LEU   B 1 94  ? 38.559 -18.859 16.389 1.00 14.69  ? 100 LEU   C CG  1 
ATOM   1856 C  CD1 . LEU   B 1 94  ? 39.844 -18.177 15.973 1.00 19.08  ? 100 LEU   C CD1 1 
ATOM   1857 C  CD2 . LEU   B 1 94  ? 37.440 -18.436 15.466 1.00 16.24  ? 100 LEU   C CD2 1 
ATOM   1858 N  N   . ALA   B 1 95  ? 37.747 -23.220 15.503 1.00 11.80  ? 101 ALA   C N   1 
ATOM   1859 C  CA  . ALA   B 1 95  ? 38.304 -24.514 15.081 1.00 12.08  ? 101 ALA   C CA  1 
ATOM   1860 C  C   . ALA   B 1 95  ? 38.884 -24.362 13.688 1.00 12.42  ? 101 ALA   C C   1 
ATOM   1861 O  O   . ALA   B 1 95  ? 38.501 -23.461 12.928 1.00 12.00  ? 101 ALA   C O   1 
ATOM   1862 C  CB  . ALA   B 1 95  ? 37.239 -25.595 15.062 1.00 12.53  ? 101 ALA   C CB  1 
ATOM   1863 N  N   . VAL   B 1 96  ? 39.757 -25.277 13.301 1.00 11.93  ? 102 VAL   C N   1 
ATOM   1864 C  CA  . VAL   B 1 96  ? 40.202 -25.410 11.901 1.00 12.56  ? 102 VAL   C CA  1 
ATOM   1865 C  C   . VAL   B 1 96  ? 39.134 -26.142 11.095 1.00 13.15  ? 102 VAL   C C   1 
ATOM   1866 O  O   . VAL   B 1 96  ? 38.799 -27.318 11.374 1.00 14.33  ? 102 VAL   C O   1 
ATOM   1867 C  CB  . VAL   B 1 96  ? 41.580 -26.097 11.870 1.00 13.61  ? 102 VAL   C CB  1 
ATOM   1868 C  CG1 . VAL   B 1 96  ? 42.067 -26.246 10.434 1.00 14.70  ? 102 VAL   C CG1 1 
ATOM   1869 C  CG2 . VAL   B 1 96  ? 42.560 -25.314 12.694 1.00 15.53  ? 102 VAL   C CG2 1 
ATOM   1870 N  N   . GLY   B 1 97  ? 38.551 -25.476 10.108 1.00 13.27  ? 103 GLY   C N   1 
ATOM   1871 C  CA  . GLY   B 1 97  ? 37.490 -26.082 9.319  1.00 13.61  ? 103 GLY   C CA  1 
ATOM   1872 C  C   . GLY   B 1 97  ? 36.805 -25.095 8.399  1.00 13.60  ? 103 GLY   C C   1 
ATOM   1873 O  O   . GLY   B 1 97  ? 37.120 -23.864 8.454  1.00 17.20  ? 103 GLY   C O   1 
ATOM   1874 N  N   . HIS   B 1 98  ? 35.918 -25.623 7.577  1.00 14.85  ? 104 HIS   C N   1 
ATOM   1875 C  CA  . HIS   B 1 98  ? 35.208 -24.817 6.563  1.00 14.90  ? 104 HIS   C CA  1 
ATOM   1876 C  C   . HIS   B 1 98  ? 33.976 -24.101 7.142  1.00 15.37  ? 104 HIS   C C   1 
ATOM   1877 O  O   . HIS   B 1 98  ? 33.134 -24.756 7.852  1.00 14.07  ? 104 HIS   C O   1 
ATOM   1878 C  CB  . HIS   B 1 98  ? 34.859 -25.681 5.377  1.00 17.89  ? 104 HIS   C CB  1 
ATOM   1879 C  CG  . HIS   B 1 98  ? 34.348 -24.831 4.278  1.00 20.67  ? 104 HIS   C CG  1 
ATOM   1880 N  ND1 . HIS   B 1 98  ? 35.180 -23.880 3.666  1.00 22.29  ? 104 HIS   C ND1 1 
ATOM   1881 C  CD2 . HIS   B 1 98  ? 33.102 -24.663 3.794  1.00 22.77  ? 104 HIS   C CD2 1 
ATOM   1882 C  CE1 . HIS   B 1 98  ? 34.432 -23.172 2.821  1.00 25.40  ? 104 HIS   C CE1 1 
ATOM   1883 N  NE2 . HIS   B 1 98  ? 33.168 -23.662 2.843  1.00 25.22  ? 104 HIS   C NE2 1 
ATOM   1884 N  N   . SER   B 1 99  ? 33.768 -22.845 6.747  1.00 14.43  ? 105 SER   C N   1 
ATOM   1885 C  CA  . SER   B 1 99  ? 32.556 -22.069 7.119  1.00 15.39  ? 105 SER   C CA  1 
ATOM   1886 C  C   . SER   B 1 99  ? 32.320 -20.947 6.104  1.00 15.89  ? 105 SER   C C   1 
ATOM   1887 O  O   . SER   B 1 99  ? 33.154 -20.039 6.042  1.00 18.25  ? 105 SER   C O   1 
ATOM   1888 C  CB  . SER   B 1 99  ? 32.781 -21.488 8.493  1.00 16.76  ? 105 SER   C CB  1 
ATOM   1889 O  OG  . SER   B 1 99  ? 31.671 -20.701 8.879  1.00 16.95  ? 105 SER   C OG  1 
ATOM   1890 N  N   . GLU   B 1 100 ? 31.213 -21.005 5.418  1.00 16.41  ? 106 GLU   C N   1 
ATOM   1891 C  CA  . GLU   B 1 100 ? 30.772 -19.904 4.527  1.00 18.07  ? 106 GLU   C CA  1 
ATOM   1892 C  C   . GLU   B 1 100 ? 29.584 -19.240 5.190  1.00 15.17  ? 106 GLU   C C   1 
ATOM   1893 O  O   . GLU   B 1 100 ? 29.027 -19.714 6.175  1.00 14.14  ? 106 GLU   C O   1 
ATOM   1894 C  CB  . GLU   B 1 100 ? 30.371 -20.481 3.201  1.00 22.36  ? 106 GLU   C CB  1 
ATOM   1895 C  CG  . GLU   B 1 100 ? 31.543 -20.509 2.225  1.00 33.74  ? 106 GLU   C CG  1 
ATOM   1896 C  CD  . GLU   B 1 100 ? 31.337 -21.664 1.280  1.00 29.27  ? 106 GLU   C CD  1 
ATOM   1897 O  OE1 . GLU   B 1 100 ? 30.221 -22.163 1.273  1.00 38.48  ? 106 GLU   C OE1 1 
ATOM   1898 O  OE2 . GLU   B 1 100 ? 32.271 -22.081 0.631  1.00 29.54  ? 106 GLU   C OE2 1 
ATOM   1899 N  N   . PRO   B 1 101 ? 29.147 -18.072 4.677  1.00 15.88  ? 107 PRO   C N   1 
ATOM   1900 C  CA  . PRO   B 1 101 ? 28.076 -17.364 5.367  1.00 14.96  ? 107 PRO   C CA  1 
ATOM   1901 C  C   . PRO   B 1 101 ? 26.823 -18.222 5.527  1.00 14.58  ? 107 PRO   C C   1 
ATOM   1902 O  O   . PRO   B 1 101 ? 26.177 -18.113 6.588  1.00 15.02  ? 107 PRO   C O   1 
ATOM   1903 C  CB  . PRO   B 1 101 ? 27.826 -16.149 4.426  1.00 17.78  ? 107 PRO   C CB  1 
ATOM   1904 C  CG  . PRO   B 1 101 ? 29.132 -15.974 3.711  1.00 22.67  ? 107 PRO   C CG  1 
ATOM   1905 C  CD  . PRO   B 1 101 ? 29.786 -17.328 3.565  1.00 18.79  ? 107 PRO   C CD  1 
ATOM   1906 N  N   . GLY   B 1 102 ? 26.476 -19.050 4.551  1.00 14.02  ? 108 GLY   C N   1 
ATOM   1907 C  CA  . GLY   B 1 102 ? 25.239 -19.855 4.673  1.00 14.03  ? 108 GLY   C CA  1 
ATOM   1908 C  C   . GLY   B 1 102 ? 25.364 -20.960 5.711  1.00 13.85  ? 108 GLY   C C   1 
ATOM   1909 O  O   . GLY   B 1 102 ? 24.341 -21.618 6.029  1.00 14.74  ? 108 GLY   C O   1 
ATOM   1910 N  N   . ASP   B 1 103 ? 26.572 -21.222 6.224  1.00 12.59  ? 109 ASP   C N   1 
ATOM   1911 C  CA  . ASP   B 1 103 ? 26.742 -22.274 7.258  1.00 12.03  ? 109 ASP   C CA  1 
ATOM   1912 C  C   . ASP   B 1 103 ? 26.354 -21.752 8.634  1.00 12.16  ? 109 ASP   C C   1 
ATOM   1913 O  O   . ASP   B 1 103 ? 26.244 -22.532 9.610  1.00 11.74  ? 109 ASP   C O   1 
ATOM   1914 C  CB  . ASP   B 1 103 ? 28.180 -22.769 7.272  1.00 13.23  ? 109 ASP   C CB  1 
ATOM   1915 C  CG  . ASP   B 1 103 ? 28.491 -23.541 6.016  1.00 12.37  ? 109 ASP   C CG  1 
ATOM   1916 O  OD1 . ASP   B 1 103 ? 27.654 -24.295 5.591  1.00 14.03  ? 109 ASP   C OD1 1 
ATOM   1917 O  OD2 . ASP   B 1 103 ? 29.666 -23.403 5.562  1.00 15.09  ? 109 ASP   C OD2 1 
ATOM   1918 N  N   . CYS   B 1 104 ? 26.164 -20.445 8.840  1.00 10.98  ? 110 CYS   C N   1 
ATOM   1919 C  CA  . CYS   B 1 104 ? 25.724 -19.866 10.109 1.00 10.84  ? 110 CYS   C CA  1 
ATOM   1920 C  C   . CYS   B 1 104 ? 24.481 -20.585 10.601 1.00 12.00  ? 110 CYS   C C   1 
ATOM   1921 O  O   . CYS   B 1 104 ? 23.549 -20.839 9.821  1.00 12.43  ? 110 CYS   C O   1 
ATOM   1922 C  CB  . CYS   B 1 104 ? 25.504 -18.358 10.030 1.00 11.47  ? 110 CYS   C CB  1 
ATOM   1923 S  SG  . CYS   B 1 104 ? 27.047 -17.407 9.962  1.00 13.45  ? 110 CYS   C SG  1 
ATOM   1924 N  N   . GLY   B 1 105 ? 24.487 -20.903 11.895 1.00 9.87   ? 111 GLY   C N   1 
ATOM   1925 C  CA  . GLY   B 1 105 ? 23.359 -21.596 12.544 1.00 10.82  ? 111 GLY   C CA  1 
ATOM   1926 C  C   . GLY   B 1 105 ? 23.575 -23.110 12.657 1.00 10.57  ? 111 GLY   C C   1 
ATOM   1927 O  O   . GLY   B 1 105 ? 22.798 -23.744 13.386 1.00 11.98  ? 111 GLY   C O   1 
ATOM   1928 N  N   . GLY   B 1 106 ? 24.588 -23.673 11.998 1.00 10.87  ? 112 GLY   C N   1 
ATOM   1929 C  CA  . GLY   B 1 106 ? 24.917 -25.102 12.167 1.00 11.60  ? 112 GLY   C CA  1 
ATOM   1930 C  C   . GLY   B 1 106 ? 25.317 -25.400 13.620 1.00 10.40  ? 112 GLY   C C   1 
ATOM   1931 O  O   . GLY   B 1 106 ? 26.028 -24.614 14.243 1.00 10.41  ? 112 GLY   C O   1 
ATOM   1932 N  N   . ILE   B 1 107 ? 24.855 -26.525 14.128 1.00 10.81  ? 113 ILE   C N   1 
ATOM   1933 C  CA  . ILE   B 1 107 ? 25.108 -26.891 15.555 1.00 10.53  ? 113 ILE   C CA  1 
ATOM   1934 C  C   . ILE   B 1 107 ? 26.508 -27.513 15.715 1.00 10.39  ? 113 ILE   C C   1 
ATOM   1935 O  O   . ILE   B 1 107 ? 26.895 -28.353 14.936 1.00 10.65  ? 113 ILE   C O   1 
ATOM   1936 C  CB  . ILE   B 1 107 ? 23.968 -27.824 16.050 1.00 12.52  ? 113 ILE   C CB  1 
ATOM   1937 C  CG1 . ILE   B 1 107 ? 22.786 -26.924 16.463 1.00 15.50  ? 113 ILE   C CG1 1 
ATOM   1938 C  CG2 . ILE   B 1 107 ? 24.413 -28.699 17.220 1.00 12.06  ? 113 ILE   C CG2 1 
ATOM   1939 C  CD1 . ILE   B 1 107 ? 21.516 -27.611 16.837 1.00 19.14  ? 113 ILE   C CD1 1 
ATOM   1940 N  N   . LEU   B 1 108 ? 27.163 -27.065 16.797 1.00 9.18   ? 114 LEU   C N   1 
ATOM   1941 C  CA  . LEU   B 1 108 ? 28.332 -27.748 17.421 1.00 8.52   ? 114 LEU   C CA  1 
ATOM   1942 C  C   . LEU   B 1 108 ? 27.808 -28.495 18.649 1.00 9.20   ? 114 LEU   C C   1 
ATOM   1943 O  O   . LEU   B 1 108 ? 27.190 -27.871 19.531 1.00 8.91   ? 114 LEU   C O   1 
ATOM   1944 C  CB  . LEU   B 1 108 ? 29.369 -26.710 17.799 1.00 9.19   ? 114 LEU   C CB  1 
ATOM   1945 C  CG  . LEU   B 1 108 ? 30.583 -27.236 18.603 1.00 9.79   ? 114 LEU   C CG  1 
ATOM   1946 C  CD1 . LEU   B 1 108 ? 31.422 -28.161 17.744 1.00 10.72  ? 114 LEU   C CD1 1 
ATOM   1947 C  CD2 . LEU   B 1 108 ? 31.405 -26.062 19.101 1.00 10.31  ? 114 LEU   C CD2 1 
ATOM   1948 N  N   . ARG   B 1 109 ? 28.089 -29.803 18.704 1.00 9.00   ? 115 ARG   C N   1 
ATOM   1949 C  CA  . ARG   B 1 109 ? 27.605 -30.673 19.835 1.00 9.99   ? 115 ARG   C CA  1 
ATOM   1950 C  C   . ARG   B 1 109 ? 28.782 -31.457 20.418 1.00 10.19  ? 115 ARG   C C   1 
ATOM   1951 O  O   . ARG   B 1 109 ? 29.682 -31.852 19.692 1.00 10.93  ? 115 ARG   C O   1 
ATOM   1952 C  CB  . ARG   B 1 109 ? 26.507 -31.623 19.353 1.00 12.90  ? 115 ARG   C CB  1 
ATOM   1953 C  CG  . ARG   B 1 109 ? 26.971 -32.581 18.275 1.00 17.10  ? 115 ARG   C CG  1 
ATOM   1954 C  CD  . ARG   B 1 109 ? 25.871 -33.511 17.789 1.00 22.05  ? 115 ARG   C CD  1 
ATOM   1955 N  NE  . ARG   B 1 109 ? 24.969 -32.848 16.863 1.00 27.47  ? 115 ARG   C NE  1 
ATOM   1956 C  CZ  . ARG   B 1 109 ? 23.651 -32.796 16.961 1.00 32.20  ? 115 ARG   C CZ  1 
ATOM   1957 N  NH1 . ARG   B 1 109 ? 23.031 -33.350 17.989 1.00 36.84  ? 115 ARG   C NH1 1 
ATOM   1958 N  NH2 . ARG   B 1 109 ? 22.968 -32.182 16.007 1.00 35.05  ? 115 ARG   C NH2 1 
ATOM   1959 N  N   . CYS   B 1 110 ? 28.680 -31.682 21.728 1.00 10.02  ? 116 CYS   C N   1 
ATOM   1960 C  CA  . CYS   B 1 110 ? 29.628 -32.581 22.464 1.00 11.18  ? 116 CYS   C CA  1 
ATOM   1961 C  C   . CYS   B 1 110 ? 28.769 -33.664 23.123 1.00 13.14  ? 116 CYS   C C   1 
ATOM   1962 O  O   . CYS   B 1 110 ? 27.536 -33.748 22.898 1.00 12.89  ? 116 CYS   C O   1 
ATOM   1963 C  CB  . CYS   B 1 110 ? 30.434 -31.788 23.485 1.00 10.60  ? 116 CYS   C CB  1 
ATOM   1964 S  SG  . CYS   B 1 110 ? 29.415 -31.119 24.831 1.00 10.91  ? 116 CYS   C SG  1 
ATOM   1965 N  N   . GLN   B 1 111 ? 29.378 -34.521 23.978 1.00 14.49  ? 117 GLN   C N   1 
ATOM   1966 C  CA  . GLN   B 1 111 ? 28.610 -35.569 24.688 1.00 16.05  ? 117 GLN   C CA  1 
ATOM   1967 C  C   . GLN   B 1 111 ? 27.545 -34.987 25.606 1.00 15.88  ? 117 GLN   C C   1 
ATOM   1968 O  O   . GLN   B 1 111 ? 26.590 -35.714 25.946 1.00 17.02  ? 117 GLN   C O   1 
ATOM   1969 C  CB  . GLN   B 1 111 ? 29.552 -36.495 25.477 1.00 18.07  ? 117 GLN   C CB  1 
ATOM   1970 C  CG  . GLN   B 1 111 ? 30.147 -35.853 26.706 1.00 20.58  ? 117 GLN   C CG  1 
ATOM   1971 C  CD  . GLN   B 1 111 ? 31.182 -36.733 27.369 1.00 28.45  ? 117 GLN   C CD  1 
ATOM   1972 O  OE1 . GLN   B 1 111 ? 32.365 -36.709 27.025 1.00 33.45  ? 117 GLN   C OE1 1 
ATOM   1973 N  NE2 . GLN   B 1 111 ? 30.742 -37.439 28.385 1.00 29.07  ? 117 GLN   C NE2 1 
ATOM   1974 N  N   . HIS   B 1 112 ? 27.642 -33.716 26.004 1.00 13.61  ? 118 HIS   C N   1 
ATOM   1975 C  CA  . HIS   B 1 112 ? 26.684 -33.119 26.960 1.00 13.41  ? 118 HIS   C CA  1 
ATOM   1976 C  C   . HIS   B 1 112 ? 25.514 -32.395 26.271 1.00 13.83  ? 118 HIS   C C   1 
ATOM   1977 O  O   . HIS   B 1 112 ? 24.563 -31.995 26.961 1.00 15.85  ? 118 HIS   C O   1 
ATOM   1978 C  CB  . HIS   B 1 112 ? 27.430 -32.152 27.861 1.00 14.24  ? 118 HIS   C CB  1 
ATOM   1979 C  CG  . HIS   B 1 112 ? 28.610 -32.780 28.519 1.00 13.90  ? 118 HIS   C CG  1 
ATOM   1980 N  ND1 . HIS   B 1 112 ? 29.928 -32.515 28.199 1.00 12.17  ? 118 HIS   C ND1 1 
ATOM   1981 C  CD2 . HIS   B 1 112 ? 28.647 -33.619 29.596 1.00 17.02  ? 118 HIS   C CD2 1 
ATOM   1982 C  CE1 . HIS   B 1 112 ? 30.722 -33.241 29.000 1.00 15.54  ? 118 HIS   C CE1 1 
ATOM   1983 N  NE2 . HIS   B 1 112 ? 29.960 -33.873 29.854 1.00 16.91  ? 118 HIS   C NE2 1 
ATOM   1984 N  N   . GLY   B 1 113 ? 25.578 -32.217 24.950 1.00 12.82  ? 119 GLY   C N   1 
ATOM   1985 C  CA  . GLY   B 1 113 ? 24.519 -31.474 24.234 1.00 12.96  ? 119 GLY   C CA  1 
ATOM   1986 C  C   . GLY   B 1 113 ? 25.081 -30.413 23.292 1.00 11.22  ? 119 GLY   C C   1 
ATOM   1987 O  O   . GLY   B 1 113 ? 26.195 -30.542 22.792 1.00 11.82  ? 119 GLY   C O   1 
ATOM   1988 N  N   . VAL   B 1 114 ? 24.249 -29.396 23.033 1.00 11.39  ? 120 VAL   C N   1 
ATOM   1989 C  CA  . VAL   B 1 114 ? 24.573 -28.317 22.073 1.00 10.78  ? 120 VAL   C CA  1 
ATOM   1990 C  C   . VAL   B 1 114 ? 25.515 -27.327 22.746 1.00 10.40  ? 120 VAL   C C   1 
ATOM   1991 O  O   . VAL   B 1 114 ? 25.196 -26.788 23.833 1.00 11.84  ? 120 VAL   C O   1 
ATOM   1992 C  CB  . VAL   B 1 114 ? 23.289 -27.626 21.590 1.00 12.08  ? 120 VAL   C CB  1 
ATOM   1993 C  CG1 . VAL   B 1 114 ? 23.642 -26.446 20.688 1.00 13.08  ? 120 VAL   C CG1 1 
ATOM   1994 C  CG2 . VAL   B 1 114 ? 22.390 -28.622 20.886 1.00 13.75  ? 120 VAL   C CG2 1 
ATOM   1995 N  N   . VAL   B 1 115 ? 26.687 -27.125 22.161 1.00 9.52   ? 121 VAL   C N   1 
ATOM   1996 C  CA  . VAL   B 1 115 ? 27.723 -26.190 22.664 1.00 10.10  ? 121 VAL   C CA  1 
ATOM   1997 C  C   . VAL   B 1 115 ? 27.459 -24.776 22.137 1.00 10.86  ? 121 VAL   C C   1 
ATOM   1998 O  O   . VAL   B 1 115 ? 27.703 -23.785 22.845 1.00 11.20  ? 121 VAL   C O   1 
ATOM   1999 C  CB  . VAL   B 1 115 ? 29.118 -26.710 22.265 1.00 10.23  ? 121 VAL   C CB  1 
ATOM   2000 C  CG1 . VAL   B 1 115 ? 30.182 -25.729 22.642 1.00 11.16  ? 121 VAL   C CG1 1 
ATOM   2001 C  CG2 . VAL   B 1 115 ? 29.360 -28.111 22.805 1.00 11.66  ? 121 VAL   C CG2 1 
ATOM   2002 N  N   . GLY   B 1 116 ? 27.111 -24.666 20.850 1.00 10.10  ? 122 GLY   C N   1 
ATOM   2003 C  CA  . GLY   B 1 116 ? 26.932 -23.347 20.230 1.00 11.74  ? 122 GLY   C CA  1 
ATOM   2004 C  C   . GLY   B 1 116 ? 26.574 -23.520 18.777 1.00 9.43   ? 122 GLY   C C   1 
ATOM   2005 O  O   . GLY   B 1 116 ? 26.263 -24.656 18.350 1.00 10.55  ? 122 GLY   C O   1 
ATOM   2006 N  N   . ILE   B 1 117 ? 26.548 -22.397 18.029 1.00 9.29   ? 123 ILE   C N   1 
ATOM   2007 C  CA  . ILE   B 1 117 ? 26.176 -22.399 16.594 1.00 9.67   ? 123 ILE   C CA  1 
ATOM   2008 C  C   . ILE   B 1 117 ? 27.250 -21.678 15.782 1.00 8.94   ? 123 ILE   C C   1 
ATOM   2009 O  O   . ILE   B 1 117 ? 27.871 -20.732 16.280 1.00 9.65   ? 123 ILE   C O   1 
ATOM   2010 C  CB  . ILE   B 1 117 ? 24.781 -21.769 16.345 1.00 10.50  ? 123 ILE   C CB  1 
ATOM   2011 C  CG1 . ILE   B 1 117 ? 24.654 -20.367 16.937 1.00 11.77  ? 123 ILE   C CG1 1 
ATOM   2012 C  CG2 . ILE   B 1 117 ? 23.678 -22.695 16.773 1.00 12.37  ? 123 ILE   C CG2 1 
ATOM   2013 C  CD1 . ILE   B 1 117 ? 23.308 -19.668 16.543 1.00 11.86  ? 123 ILE   C CD1 1 
ATOM   2014 N  N   . VAL   B 1 118 ? 27.410 -22.088 14.528 1.00 9.55   ? 124 VAL   C N   1 
ATOM   2015 C  CA  . VAL   B 1 118 ? 28.342 -21.422 13.601 1.00 10.27  ? 124 VAL   C CA  1 
ATOM   2016 C  C   . VAL   B 1 118 ? 27.984 -19.942 13.518 1.00 10.78  ? 124 VAL   C C   1 
ATOM   2017 O  O   . VAL   B 1 118 ? 26.768 -19.616 13.323 1.00 11.07  ? 124 VAL   C O   1 
ATOM   2018 C  CB  . VAL   B 1 118 ? 28.333 -22.082 12.226 1.00 10.18  ? 124 VAL   C CB  1 
ATOM   2019 C  CG1 . VAL   B 1 118 ? 29.200 -21.352 11.228 1.00 10.77  ? 124 VAL   C CG1 1 
ATOM   2020 C  CG2 . VAL   B 1 118 ? 28.785 -23.532 12.310 1.00 10.10  ? 124 VAL   C CG2 1 
ATOM   2021 N  N   . SER   B 1 119 ? 28.977 -19.063 13.626 1.00 10.16  ? 125 SER   C N   1 
ATOM   2022 C  CA  . SER   B 1 119 ? 28.799 -17.587 13.515 1.00 10.74  ? 125 SER   C CA  1 
ATOM   2023 C  C   . SER   B 1 119 ? 29.833 -16.938 12.588 1.00 11.95  ? 125 SER   C C   1 
ATOM   2024 O  O   . SER   B 1 119 ? 29.479 -15.856 12.044 1.00 11.80  ? 125 SER   C O   1 
ATOM   2025 C  CB  . SER   B 1 119 ? 28.805 -17.009 14.891 1.00 11.52  ? 125 SER   C CB  1 
ATOM   2026 O  OG  . SER   B 1 119 ? 28.680 -15.552 14.853 1.00 12.58  ? 125 SER   C OG  1 
ATOM   2027 N  N   . THR   B 1 120 ? 31.061 -17.447 12.440 1.00 11.59  ? 126 THR   C N   1 
ATOM   2028 C  CA  . THR   B 1 120 ? 32.118 -16.790 11.653 1.00 11.34  ? 126 THR   C CA  1 
ATOM   2029 C  C   . THR   B 1 120 ? 32.790 -17.815 10.766 1.00 11.16  ? 126 THR   C C   1 
ATOM   2030 O  O   . THR   B 1 120 ? 32.691 -19.048 10.969 1.00 10.68  ? 126 THR   C O   1 
ATOM   2031 C  CB  . THR   B 1 120 ? 33.163 -16.047 12.497 1.00 10.84  ? 126 THR   C CB  1 
ATOM   2032 O  OG1 . THR   B 1 120 ? 34.000 -17.027 13.145 1.00 12.60  ? 126 THR   C OG1 1 
ATOM   2033 C  CG2 . THR   B 1 120 ? 32.573 -15.138 13.544 1.00 12.29  ? 126 THR   C CG2 1 
ATOM   2034 N  N   . GLY   B 1 121 ? 33.483 -17.306 9.775  1.00 12.59  ? 127 GLY   C N   1 
ATOM   2035 C  CA  . GLY   B 1 121 ? 34.249 -18.127 8.836  1.00 14.33  ? 127 GLY   C CA  1 
ATOM   2036 C  C   . GLY   B 1 121 ? 35.307 -17.306 8.135  1.00 18.30  ? 127 GLY   C C   1 
ATOM   2037 O  O   . GLY   B 1 121 ? 35.076 -16.163 7.810  1.00 21.67  ? 127 GLY   C O   1 
ATOM   2038 N  N   . GLY   B 1 122 ? 36.346 -17.968 7.693  1.00 25.76  ? 128 GLY   C N   1 
ATOM   2039 C  CA  . GLY   B 1 122 ? 37.362 -17.325 6.838  1.00 29.16  ? 128 GLY   C CA  1 
ATOM   2040 C  C   . GLY   B 1 122 ? 38.733 -17.763 7.249  1.00 26.19  ? 128 GLY   C C   1 
ATOM   2041 O  O   . GLY   B 1 122 ? 38.896 -18.241 8.337  1.00 23.74  ? 128 GLY   C O   1 
ATOM   2042 N  N   . ASN   B 1 123 ? 39.702 -17.645 6.351  1.00 24.88  ? 129 ASN   C N   1 
ATOM   2043 C  CA  . ASN   B 1 123 ? 41.123 -18.010 6.627  1.00 24.32  ? 129 ASN   C CA  1 
ATOM   2044 C  C   . ASN   B 1 123 ? 41.199 -19.457 7.108  1.00 20.70  ? 129 ASN   C C   1 
ATOM   2045 O  O   . ASN   B 1 123 ? 42.099 -19.728 7.892  1.00 25.36  ? 129 ASN   C O   1 
ATOM   2046 C  CB  . ASN   B 1 123 ? 41.826 -17.076 7.631  1.00 29.77  ? 129 ASN   C CB  1 
ATOM   2047 C  CG  . ASN   B 1 123 ? 42.746 -16.080 6.951  1.00 37.32  ? 129 ASN   C CG  1 
ATOM   2048 O  OD1 . ASN   B 1 123 ? 43.028 -16.209 5.761  1.00 42.88  ? 129 ASN   C OD1 1 
ATOM   2049 N  ND2 . ASN   B 1 123 ? 43.193 -15.070 7.673  1.00 43.52  ? 129 ASN   C ND2 1 
ATOM   2050 N  N   . GLY   B 1 124 ? 40.312 -20.346 6.651  1.00 18.52  ? 130 GLY   C N   1 
ATOM   2051 C  CA  . GLY   B 1 124 ? 40.319 -21.783 7.019  1.00 17.85  ? 130 GLY   C CA  1 
ATOM   2052 C  C   . GLY   B 1 124 ? 39.930 -22.026 8.462  1.00 17.43  ? 130 GLY   C C   1 
ATOM   2053 O  O   . GLY   B 1 124 ? 40.152 -23.145 8.936  1.00 15.18  ? 130 GLY   C O   1 
ATOM   2054 N  N   . LEU   B 1 125 ? 39.298 -21.075 9.109  1.00 15.43  ? 131 LEU   C N   1 
ATOM   2055 C  CA  . LEU   B 1 125 ? 38.801 -21.230 10.488 1.00 14.12  ? 131 LEU   C CA  1 
ATOM   2056 C  C   . LEU   B 1 125 ? 37.272 -21.134 10.484 1.00 14.62  ? 131 LEU   C C   1 
ATOM   2057 O  O   . LEU   B 1 125 ? 36.680 -20.402 9.641  1.00 18.01  ? 131 LEU   C O   1 
ATOM   2058 C  CB  . LEU   B 1 125 ? 39.420 -20.161 11.380 1.00 16.76  ? 131 LEU   C CB  1 
ATOM   2059 C  CG  . LEU   B 1 125 ? 40.954 -20.174 11.364 1.00 18.47  ? 131 LEU   C CG  1 
ATOM   2060 C  CD1 . LEU   B 1 125 ? 41.556 -18.903 11.918 1.00 24.13  ? 131 LEU   C CD1 1 
ATOM   2061 C  CD2 . LEU   B 1 125 ? 41.457 -21.390 12.095 1.00 19.17  ? 131 LEU   C CD2 1 
ATOM   2062 N  N   . VAL   B 1 126 ? 36.654 -21.812 11.413 1.00 11.45  ? 132 VAL   C N   1 
ATOM   2063 C  CA  . VAL   B 1 126 ? 35.203 -21.698 11.695 1.00 11.04  ? 132 VAL   C CA  1 
ATOM   2064 C  C   . VAL   B 1 126 ? 35.061 -21.227 13.143 1.00 10.83  ? 132 VAL   C C   1 
ATOM   2065 O  O   . VAL   B 1 126 ? 35.741 -21.729 14.048 1.00 11.21  ? 132 VAL   C O   1 
ATOM   2066 C  CB  . VAL   B 1 126 ? 34.466 -23.025 11.432 1.00 10.99  ? 132 VAL   C CB  1 
ATOM   2067 C  CG1 . VAL   B 1 126 ? 35.096 -24.206 12.096 1.00 11.74  ? 132 VAL   C CG1 1 
ATOM   2068 C  CG2 . VAL   B 1 126 ? 32.982 -22.922 11.784 1.00 11.85  ? 132 VAL   C CG2 1 
ATOM   2069 N  N   . GLY   B 1 127 ? 34.177 -20.245 13.357 1.00 10.23  ? 133 GLY   C N   1 
ATOM   2070 C  CA  . GLY   B 1 127 ? 33.906 -19.734 14.697 1.00 9.76   ? 133 GLY   C CA  1 
ATOM   2071 C  C   . GLY   B 1 127 ? 32.480 -20.050 15.140 1.00 10.41  ? 133 GLY   C C   1 
ATOM   2072 O  O   . GLY   B 1 127 ? 31.541 -19.892 14.342 1.00 10.70  ? 133 GLY   C O   1 
ATOM   2073 N  N   . PHE   B 1 128 ? 32.358 -20.422 16.395 1.00 9.22   ? 134 PHE   C N   1 
ATOM   2074 C  CA  . PHE   B 1 128 ? 31.079 -20.795 17.040 1.00 9.68   ? 134 PHE   C CA  1 
ATOM   2075 C  C   . PHE   B 1 128 ? 30.754 -19.860 18.178 1.00 10.79  ? 134 PHE   C C   1 
ATOM   2076 O  O   . PHE   B 1 128 ? 31.589 -19.598 19.030 1.00 10.85  ? 134 PHE   C O   1 
ATOM   2077 C  CB  . PHE   B 1 128 ? 31.129 -22.227 17.578 1.00 10.04  ? 134 PHE   C CB  1 
ATOM   2078 C  CG  . PHE   B 1 128 ? 31.660 -23.215 16.559 1.00 9.91   ? 134 PHE   C CG  1 
ATOM   2079 C  CD1 . PHE   B 1 128 ? 30.842 -23.851 15.638 1.00 10.13  ? 134 PHE   C CD1 1 
ATOM   2080 C  CD2 . PHE   B 1 128 ? 32.994 -23.582 16.579 1.00 10.77  ? 134 PHE   C CD2 1 
ATOM   2081 C  CE1 . PHE   B 1 128 ? 31.326 -24.809 14.772 1.00 10.84  ? 134 PHE   C CE1 1 
ATOM   2082 C  CE2 . PHE   B 1 128 ? 33.500 -24.538 15.708 1.00 10.74  ? 134 PHE   C CE2 1 
ATOM   2083 C  CZ  . PHE   B 1 128 ? 32.683 -25.154 14.812 1.00 11.24  ? 134 PHE   C CZ  1 
ATOM   2084 N  N   . ALA   B 1 129 ? 29.517 -19.342 18.177 1.00 10.36  ? 135 ALA   C N   1 
ATOM   2085 C  CA  . ALA   B 1 129 ? 28.978 -18.581 19.322 1.00 10.11  ? 135 ALA   C CA  1 
ATOM   2086 C  C   . ALA   B 1 129 ? 28.584 -19.570 20.429 1.00 10.24  ? 135 ALA   C C   1 
ATOM   2087 O  O   . ALA   B 1 129 ? 27.696 -20.396 20.258 1.00 10.48  ? 135 ALA   C O   1 
ATOM   2088 C  CB  . ALA   B 1 129 ? 27.775 -17.754 18.875 1.00 10.21  ? 135 ALA   C CB  1 
ATOM   2089 N  N   . ASP   B 1 130 ? 29.278 -19.487 21.546 1.00 10.96  ? 136 ASP   C N   1 
ATOM   2090 C  CA  . ASP   B 1 130 ? 29.014 -20.366 22.700 1.00 11.74  ? 136 ASP   C CA  1 
ATOM   2091 C  C   . ASP   B 1 130 ? 27.648 -20.036 23.303 1.00 12.12  ? 136 ASP   C C   1 
ATOM   2092 O  O   . ASP   B 1 130 ? 27.260 -18.817 23.334 1.00 12.54  ? 136 ASP   C O   1 
ATOM   2093 C  CB  . ASP   B 1 130 ? 30.069 -20.124 23.783 1.00 12.46  ? 136 ASP   C CB  1 
ATOM   2094 C  CG  . ASP   B 1 130 ? 29.984 -21.041 24.986 1.00 13.81  ? 136 ASP   C CG  1 
ATOM   2095 O  OD1 . ASP   B 1 130 ? 29.838 -22.247 24.802 1.00 14.01  ? 136 ASP   C OD1 1 
ATOM   2096 O  OD2 . ASP   B 1 130 ? 29.918 -20.490 26.101 1.00 17.48  ? 136 ASP   C OD2 1 
ATOM   2097 N  N   . VAL   B 1 131 ? 26.948 -21.023 23.788 1.00 11.22  ? 137 VAL   C N   1 
ATOM   2098 C  CA  . VAL   B 1 131 ? 25.705 -20.846 24.583 1.00 11.33  ? 137 VAL   C CA  1 
ATOM   2099 C  C   . VAL   B 1 131 ? 25.789 -21.519 25.950 1.00 12.33  ? 137 VAL   C C   1 
ATOM   2100 O  O   . VAL   B 1 131 ? 24.788 -21.468 26.715 1.00 12.21  ? 137 VAL   C O   1 
ATOM   2101 C  CB  . VAL   B 1 131 ? 24.454 -21.305 23.812 1.00 11.80  ? 137 VAL   C CB  1 
ATOM   2102 C  CG1 . VAL   B 1 131 ? 24.235 -20.470 22.537 1.00 11.36  ? 137 VAL   C CG1 1 
ATOM   2103 C  CG2 . VAL   B 1 131 ? 24.504 -22.753 23.472 1.00 11.16  ? 137 VAL   C CG2 1 
ATOM   2104 N  N   . ARG   B 1 132 ? 26.904 -22.140 26.303 1.00 11.71  ? 138 ARG   C N   1 
ATOM   2105 C  CA  . ARG   B 1 132 ? 26.987 -22.961 27.558 1.00 12.25  ? 138 ARG   C CA  1 
ATOM   2106 C  C   . ARG   B 1 132 ? 26.910 -22.103 28.813 1.00 12.42  ? 138 ARG   C C   1 
ATOM   2107 O  O   . ARG   B 1 132 ? 26.570 -22.646 29.880 1.00 14.17  ? 138 ARG   C O   1 
ATOM   2108 C  CB  . ARG   B 1 132 ? 28.256 -23.784 27.501 1.00 11.73  ? 138 ARG   C CB  1 
ATOM   2109 C  CG  . ARG   B 1 132 ? 28.224 -24.820 26.394 1.00 11.60  ? 138 ARG   C CG  1 
ATOM   2110 C  CD  . ARG   B 1 132 ? 29.531 -25.615 26.405 1.00 11.09  ? 138 ARG   C CD  1 
ATOM   2111 N  NE  . ARG   B 1 132 ? 30.663 -24.784 26.044 1.00 11.11  ? 138 ARG   C NE  1 
ATOM   2112 C  CZ  . ARG   B 1 132 ? 31.901 -25.160 25.887 1.00 12.30  ? 138 ARG   C CZ  1 
ATOM   2113 N  NH1 . ARG   B 1 132 ? 32.253 -26.393 26.242 1.00 12.99  ? 138 ARG   C NH1 1 
ATOM   2114 N  NH2 . ARG   B 1 132 ? 32.783 -24.299 25.421 1.00 12.71  ? 138 ARG   C NH2 1 
ATOM   2115 N  N   . ASP   B 1 133 ? 27.181 -20.809 28.731 1.00 12.03  ? 139 ASP   C N   1 
ATOM   2116 C  CA  . ASP   B 1 133 ? 27.136 -19.902 29.905 1.00 12.74  ? 139 ASP   C CA  1 
ATOM   2117 C  C   . ASP   B 1 133 ? 25.696 -19.383 30.105 1.00 14.36  ? 139 ASP   C C   1 
ATOM   2118 O  O   . ASP   B 1 133 ? 25.472 -18.742 31.153 1.00 15.82  ? 139 ASP   C O   1 
ATOM   2119 C  CB  . ASP   B 1 133 ? 28.098 -18.736 29.747 1.00 13.44  ? 139 ASP   C CB  1 
ATOM   2120 C  CG  . ASP   B 1 133 ? 27.727 -17.805 28.595 1.00 15.09  ? 139 ASP   C CG  1 
ATOM   2121 O  OD1 . ASP   B 1 133 ? 27.371 -18.324 27.523 1.00 15.30  ? 139 ASP   C OD1 1 
ATOM   2122 O  OD2 . ASP   B 1 133 ? 27.792 -16.540 28.774 1.00 18.14  ? 139 ASP   C OD2 1 
ATOM   2123 N  N   . LEU   B 1 134 ? 24.754 -19.625 29.176 1.00 12.82  ? 140 LEU   C N   1 
ATOM   2124 C  CA  . LEU   B 1 134 ? 23.375 -19.053 29.244 1.00 13.09  ? 140 LEU   C CA  1 
ATOM   2125 C  C   . LEU   B 1 134 ? 22.490 -20.032 30.021 1.00 12.43  ? 140 LEU   C C   1 
ATOM   2126 O  O   . LEU   B 1 134 ? 21.673 -20.770 29.452 1.00 12.89  ? 140 LEU   C O   1 
ATOM   2127 C  CB  . LEU   B 1 134 ? 22.831 -18.806 27.832 1.00 12.37  ? 140 LEU   C CB  1 
ATOM   2128 C  CG  . LEU   B 1 134 ? 23.671 -17.859 26.963 1.00 13.98  ? 140 LEU   C CG  1 
ATOM   2129 C  CD1 . LEU   B 1 134 ? 23.094 -17.729 25.542 1.00 14.58  ? 140 LEU   C CD1 1 
ATOM   2130 C  CD2 . LEU   B 1 134 ? 23.840 -16.477 27.587 1.00 15.35  ? 140 LEU   C CD2 1 
ATOM   2131 N  N   . LEU   B 1 135 ? 22.708 -20.075 31.361 1.00 14.05  ? 141 LEU   C N   1 
ATOM   2132 C  CA  . LEU   B 1 135 ? 22.120 -21.127 32.224 1.00 14.39  ? 141 LEU   C CA  1 
ATOM   2133 C  C   . LEU   B 1 135 ? 20.596 -20.998 32.272 1.00 13.34  ? 141 LEU   C C   1 
ATOM   2134 O  O   . LEU   B 1 135 ? 19.889 -21.999 32.394 1.00 15.70  ? 141 LEU   C O   1 
ATOM   2135 C  CB  . LEU   B 1 135 ? 22.708 -21.103 33.646 1.00 14.66  ? 141 LEU   C CB  1 
ATOM   2136 C  CG  . LEU   B 1 135 ? 24.236 -21.124 33.756 1.00 16.61  ? 141 LEU   C CG  1 
ATOM   2137 C  CD1 . LEU   B 1 135 ? 24.721 -21.186 35.222 1.00 17.32  ? 141 LEU   C CD1 1 
ATOM   2138 C  CD2 . LEU   B 1 135 ? 24.918 -22.185 32.913 1.00 16.39  ? 141 LEU   C CD2 1 
ATOM   2139 N  N   . TRP   B 1 136 ? 20.115 -19.782 32.057 1.00 14.62  ? 142 TRP   C N   1 
ATOM   2140 C  CA  . TRP   B 1 136 ? 18.656 -19.476 32.108 1.00 16.05  ? 142 TRP   C CA  1 
ATOM   2141 C  C   . TRP   B 1 136 ? 17.903 -20.184 30.973 1.00 15.90  ? 142 TRP   C C   1 
ATOM   2142 O  O   . TRP   B 1 136 ? 16.663 -20.340 31.029 1.00 17.69  ? 142 TRP   C O   1 
ATOM   2143 C  CB  . TRP   B 1 136 ? 18.441 -17.963 32.075 1.00 16.29  ? 142 TRP   C CB  1 
ATOM   2144 C  CG  . TRP   B 1 136 ? 19.113 -17.218 30.964 1.00 15.70  ? 142 TRP   C CG  1 
ATOM   2145 C  CD1 . TRP   B 1 136 ? 20.303 -16.554 31.022 1.00 16.73  ? 142 TRP   C CD1 1 
ATOM   2146 C  CD2 . TRP   B 1 136 ? 18.590 -16.994 29.634 1.00 15.83  ? 142 TRP   C CD2 1 
ATOM   2147 N  NE1 . TRP   B 1 136 ? 20.577 -15.957 29.811 1.00 16.57  ? 142 TRP   C NE1 1 
ATOM   2148 C  CE2 . TRP   B 1 136 ? 19.557 -16.250 28.935 1.00 16.89  ? 142 TRP   C CE2 1 
ATOM   2149 C  CE3 . TRP   B 1 136 ? 17.436 -17.402 28.979 1.00 15.69  ? 142 TRP   C CE3 1 
ATOM   2150 C  CZ2 . TRP   B 1 136 ? 19.333 -15.838 27.616 1.00 16.51  ? 142 TRP   C CZ2 1 
ATOM   2151 C  CZ3 . TRP   B 1 136 ? 17.209 -16.997 27.685 1.00 17.04  ? 142 TRP   C CZ3 1 
ATOM   2152 C  CH2 . TRP   B 1 136 ? 18.168 -16.250 27.017 1.00 16.08  ? 142 TRP   C CH2 1 
ATOM   2153 N  N   . LEU   B 1 137 ? 18.592 -20.667 29.930 1.00 15.44  ? 143 LEU   C N   1 
ATOM   2154 C  CA  . LEU   B 1 137 ? 17.909 -21.421 28.855 1.00 15.95  ? 143 LEU   C CA  1 
ATOM   2155 C  C   . LEU   B 1 137 ? 17.299 -22.703 29.421 1.00 17.73  ? 143 LEU   C C   1 
ATOM   2156 O  O   . LEU   B 1 137 ? 16.394 -23.228 28.774 1.00 20.53  ? 143 LEU   C O   1 
ATOM   2157 C  CB  . LEU   B 1 137 ? 18.861 -21.726 27.691 1.00 15.29  ? 143 LEU   C CB  1 
ATOM   2158 C  CG  . LEU   B 1 137 ? 19.304 -20.557 26.805 1.00 14.31  ? 143 LEU   C CG  1 
ATOM   2159 C  CD1 . LEU   B 1 137 ? 20.496 -20.986 25.942 1.00 15.65  ? 143 LEU   C CD1 1 
ATOM   2160 C  CD2 . LEU   B 1 137 ? 18.173 -20.033 25.912 1.00 16.33  ? 143 LEU   C CD2 1 
ATOM   2161 N  N   . ASP   B 1 138 ? 17.828 -23.205 30.550 1.00 18.88  ? 144 ASP   C N   1 
ATOM   2162 C  CA  . ASP   B 1 138 ? 17.399 -24.496 31.156 1.00 21.00  ? 144 ASP   C CA  1 
ATOM   2163 C  C   . ASP   B 1 138 ? 16.115 -24.307 31.992 1.00 24.00  ? 144 ASP   C C   1 
ATOM   2164 O  O   . ASP   B 1 138 ? 15.613 -25.339 32.468 1.00 25.90  ? 144 ASP   C O   1 
ATOM   2165 C  CB  . ASP   B 1 138 ? 18.509 -25.136 32.006 1.00 20.08  ? 144 ASP   C CB  1 
ATOM   2166 C  CG  . ASP   B 1 138 ? 19.751 -25.558 31.230 1.00 19.11  ? 144 ASP   C CG  1 
ATOM   2167 O  OD1 . ASP   B 1 138 ? 19.682 -25.604 29.993 1.00 21.76  ? 144 ASP   C OD1 1 
ATOM   2168 O  OD2 . ASP   B 1 138 ? 20.781 -25.818 31.888 1.00 23.24  ? 144 ASP   C OD2 1 
ATOM   2169 N  N   . GLU   B 1 139 ? 15.549 -23.106 32.124 1.00 24.27  ? 145 GLU   C N   1 
ATOM   2170 C  CA  . GLU   B 1 139 ? 14.384 -22.912 33.040 1.00 30.27  ? 145 GLU   C CA  1 
ATOM   2171 C  C   . GLU   B 1 139 ? 13.363 -21.907 32.484 1.00 35.40  ? 145 GLU   C C   1 
ATOM   2172 O  O   . GLU   B 1 139 ? 13.663 -21.225 31.489 1.00 32.53  ? 145 GLU   C O   1 
ATOM   2173 C  CB  . GLU   B 1 139 ? 14.937 -22.447 34.389 1.00 36.91  ? 145 GLU   C CB  1 
ATOM   2174 C  CG  . GLU   B 1 139 ? 15.493 -21.039 34.343 1.00 42.04  ? 145 GLU   C CG  1 
ATOM   2175 C  CD  . GLU   B 1 139 ? 16.411 -20.604 35.481 1.00 48.41  ? 145 GLU   C CD  1 
ATOM   2176 O  OE1 . GLU   B 1 139 ? 16.790 -19.397 35.492 1.00 48.56  ? 145 GLU   C OE1 1 
ATOM   2177 O  OE2 . GLU   B 1 139 ? 16.743 -21.453 36.350 1.00 46.72  ? 145 GLU   C OE2 1 
ATOM   2178 N  N   . GLU   B 1 140 ? 12.227 -21.748 33.184 1.00 39.16  ? 146 GLU   C N   1 
ATOM   2179 C  CA  . GLU   B 1 140 ? 11.349 -20.532 33.162 1.00 44.49  ? 146 GLU   C CA  1 
ATOM   2180 C  C   . GLU   B 1 140 ? 10.805 -20.325 31.753 1.00 46.52  ? 146 GLU   C C   1 
ATOM   2181 O  O   . GLU   B 1 140 ? 10.297 -19.239 31.476 1.00 51.11  ? 146 GLU   C O   1 
ATOM   2182 C  CB  . GLU   B 1 140 ? 12.101 -19.307 33.709 1.00 45.15  ? 146 GLU   C CB  1 
ATOM   2183 C  CG  . GLU   B 1 140 ? 11.765 -17.936 33.092 1.00 52.65  ? 146 GLU   C CG  1 
ATOM   2184 C  CD  . GLU   B 1 140 ? 10.478 -17.205 33.497 1.00 52.76  ? 146 GLU   C CD  1 
ATOM   2185 O  OE1 . GLU   B 1 140 ? 10.440 -15.962 33.344 1.00 58.37  ? 146 GLU   C OE1 1 
ATOM   2186 O  OE2 . GLU   B 1 140 ? 9.509  -17.857 33.952 1.00 56.15  ? 146 GLU   C OE2 1 
HETATM 2187 ZN ZN  . ZN    C 2 .   ? 11.061 -3.912  5.817  1.00 19.12  ? 201 ZN    A ZN  1 
HETATM 2188 N  N1  . A1BQ7 D 3 .   ? 8.488  15.408  21.508 0.72 24.48  ? 202 A1BQ7 A N1  1 
HETATM 2189 N  N3  . A1BQ7 D 3 .   ? 5.459  13.105  25.816 0.72 30.00  ? 202 A1BQ7 A N3  1 
HETATM 2190 C  C4  . A1BQ7 D 3 .   ? 9.484  15.848  22.503 0.72 23.08  ? 202 A1BQ7 A C4  1 
HETATM 2191 C  C5  . A1BQ7 D 3 .   ? 7.539  14.485  21.729 0.72 22.97  ? 202 A1BQ7 A C5  1 
HETATM 2192 C  C6  . A1BQ7 D 3 .   ? 7.539  13.738  23.033 0.72 27.29  ? 202 A1BQ7 A C6  1 
HETATM 2193 C  C7  . A1BQ7 D 3 .   ? 8.595  12.863  23.294 0.72 26.17  ? 202 A1BQ7 A C7  1 
HETATM 2194 C  C8  . A1BQ7 D 3 .   ? 8.519  12.019  24.393 0.72 26.86  ? 202 A1BQ7 A C8  1 
HETATM 2195 C  C10 . A1BQ7 D 3 .   ? 5.289  14.519  24.206 0.72 29.78  ? 202 A1BQ7 A C10 1 
HETATM 2196 N  N   . A1BQ7 D 3 .   ? 10.801 15.468  17.387 0.72 19.92  ? 202 A1BQ7 A N   1 
HETATM 2197 C  C   . A1BQ7 D 3 .   ? 10.167 16.299  18.203 0.72 23.64  ? 202 A1BQ7 A C   1 
HETATM 2198 O  O   . A1BQ7 D 3 .   ? 9.732  17.394  17.833 0.72 24.04  ? 202 A1BQ7 A O   1 
HETATM 2199 C  C1  . A1BQ7 D 3 .   ? 9.991  15.826  19.635 0.72 22.07  ? 202 A1BQ7 A C1  1 
HETATM 2200 C  C11 . A1BQ7 D 3 .   ? 6.466  13.774  23.945 0.72 28.40  ? 202 A1BQ7 A C11 1 
HETATM 2201 C  C12 . A1BQ7 D 3 .   ? 8.623  16.129  20.239 0.72 23.25  ? 202 A1BQ7 A C12 1 
HETATM 2202 C  C2  . A1BQ7 D 3 .   ? 11.019 16.446  20.593 0.72 23.39  ? 202 A1BQ7 A C2  1 
HETATM 2203 C  C3  . A1BQ7 D 3 .   ? 10.907 15.778  21.964 0.72 25.05  ? 202 A1BQ7 A C3  1 
HETATM 2204 C  C9  . A1BQ7 D 3 .   ? 6.520  12.868  25.017 0.72 28.01  ? 202 A1BQ7 A C9  1 
HETATM 2205 N  N2  . A1BQ7 D 3 .   ? 7.487  11.977  25.246 0.72 25.39  ? 202 A1BQ7 A N2  1 
HETATM 2206 N  N4  . A1BQ7 D 3 .   ? 4.701  14.127  25.321 0.72 31.52  ? 202 A1BQ7 A N4  1 
HETATM 2207 O  O1  . A1BQ7 D 3 .   ? 6.657  14.261  20.933 0.72 26.91  ? 202 A1BQ7 A O1  1 
HETATM 2208 S  S   . DMS   E 4 .   ? 28.793 -2.853  6.703  1.00 126.57 ? 203 DMS   A S   1 
HETATM 2209 O  O   . DMS   E 4 .   ? 28.039 -3.457  7.856  1.00 121.83 ? 203 DMS   A O   1 
HETATM 2210 C  C1  . DMS   E 4 .   ? 27.644 -1.786  5.861  1.00 119.15 ? 203 DMS   A C1  1 
HETATM 2211 C  C2  . DMS   E 4 .   ? 29.849 -1.603  7.396  1.00 115.13 ? 203 DMS   A C2  1 
HETATM 2212 S  S   . DMS   F 4 .   ? 18.690 -4.644  25.169 1.00 71.68  ? 201 DMS   C S   1 
HETATM 2213 O  O   . DMS   F 4 .   ? 18.557 -3.290  24.482 1.00 64.04  ? 201 DMS   C O   1 
HETATM 2214 C  C1  . DMS   F 4 .   ? 17.856 -5.863  24.142 1.00 38.89  ? 201 DMS   C C1  1 
HETATM 2215 C  C2  . DMS   F 4 .   ? 20.363 -5.178  24.852 1.00 70.52  ? 201 DMS   C C2  1 
HETATM 2216 ZN ZN  . ZN    G 2 .   ? 30.634 -31.180 26.762 1.00 12.19  ? 202 ZN    C ZN  1 
HETATM 2217 S  S   . DMS   H 4 .   ? 20.950 -32.505 10.028 1.00 63.48  ? 203 DMS   C S   1 
HETATM 2218 O  O   . DMS   H 4 .   ? 21.342 -31.211 9.373  1.00 63.86  ? 203 DMS   C O   1 
HETATM 2219 C  C1  . DMS   H 4 .   ? 21.717 -32.466 11.616 1.00 62.65  ? 203 DMS   C C1  1 
HETATM 2220 C  C2  . DMS   H 4 .   ? 19.263 -32.268 10.564 1.00 67.26  ? 203 DMS   C C2  1 
HETATM 2221 O  O   . HOH   I 5 .   ? 3.005  9.527   8.971  0.72 21.65  ? 301 HOH   A O   1 
HETATM 2222 O  O   . HOH   I 5 .   ? 8.403  24.828  23.755 0.72 27.05  ? 302 HOH   A O   1 
HETATM 2223 O  O   . HOH   I 5 .   ? 11.212 8.908   4.366  1.00 23.87  ? 303 HOH   A O   1 
HETATM 2224 O  O   . HOH   I 5 .   ? 20.164 19.855  5.824  0.72 34.54  ? 304 HOH   A O   1 
HETATM 2225 O  O   . HOH   I 5 .   ? 35.351 -3.843  7.864  0.72 17.88  ? 305 HOH   A O   1 
HETATM 2226 O  O   . HOH   I 5 .   ? 30.494 10.447  15.550 0.72 25.27  ? 306 HOH   A O   1 
HETATM 2227 O  O   . HOH   I 5 .   ? 23.278 3.598   -2.199 1.00 41.91  ? 307 HOH   A O   1 
HETATM 2228 O  O   . HOH   I 5 .   ? 13.980 17.370  4.365  0.72 31.68  ? 308 HOH   A O   1 
HETATM 2229 O  O   . HOH   I 5 .   ? 8.380  -2.789  31.951 0.72 19.51  ? 309 HOH   A O   1 
HETATM 2230 O  O   . HOH   I 5 .   ? 13.854 2.953   1.211  1.00 23.60  ? 310 HOH   A O   1 
HETATM 2231 O  O   . HOH   I 5 .   ? 23.062 13.076  23.750 0.72 38.55  ? 311 HOH   A O   1 
HETATM 2232 O  O   . HOH   I 5 .   ? 33.830 -2.301  13.540 0.72 27.74  ? 312 HOH   A O   1 
HETATM 2233 O  O   . HOH   I 5 .   ? 17.471 0.962   28.197 0.72 19.85  ? 313 HOH   A O   1 
HETATM 2234 O  O   . HOH   I 5 .   ? 27.764 8.033   1.620  1.00 33.27  ? 314 HOH   A O   1 
HETATM 2235 O  O   . HOH   I 5 .   ? 5.999  2.317   5.624  1.00 24.36  ? 315 HOH   A O   1 
HETATM 2236 O  O   . HOH   I 5 .   ? 23.498 21.694  7.304  0.72 17.71  ? 316 HOH   A O   1 
HETATM 2237 O  O   . HOH   I 5 .   ? 19.337 10.090  19.657 0.72 9.07   ? 317 HOH   A O   1 
HETATM 2238 O  O   . HOH   I 5 .   ? 28.100 3.334   4.853  1.00 30.21  ? 318 HOH   A O   1 
HETATM 2239 O  O   . HOH   I 5 .   ? 33.803 14.210  9.769  0.72 27.06  ? 319 HOH   A O   1 
HETATM 2240 O  O   . HOH   I 5 .   ? 4.588  -3.490  28.819 0.72 21.44  ? 320 HOH   A O   1 
HETATM 2241 O  O   . HOH   I 5 .   ? 18.812 17.301  26.342 0.72 34.01  ? 321 HOH   A O   1 
HETATM 2242 O  O   . HOH   I 5 .   ? 8.451  6.525   33.877 0.72 14.48  ? 322 HOH   A O   1 
HETATM 2243 O  O   . HOH   I 5 .   ? 17.526 -4.839  12.211 0.72 27.22  ? 323 HOH   A O   1 
HETATM 2244 O  O   . HOH   I 5 .   ? 20.038 18.061  24.024 0.72 34.86  ? 324 HOH   A O   1 
HETATM 2245 O  O   . HOH   I 5 .   ? 21.937 2.309   -0.942 1.00 28.56  ? 325 HOH   A O   1 
HETATM 2246 O  O   . HOH   I 5 .   ? 29.979 11.637  18.428 0.72 22.80  ? 326 HOH   A O   1 
HETATM 2247 O  O   . HOH   I 5 .   ? 3.135  7.228   24.320 0.72 19.16  ? 327 HOH   A O   1 
HETATM 2248 O  O   . HOH   I 5 .   ? 3.725  11.504  18.978 0.72 31.21  ? 328 HOH   A O   1 
HETATM 2249 O  O   . HOH   I 5 .   ? 3.255  20.897  24.466 0.72 36.97  ? 329 HOH   A O   1 
HETATM 2250 O  O   . HOH   I 5 .   ? 18.415 21.916  9.603  0.72 16.65  ? 330 HOH   A O   1 
HETATM 2251 O  O   . HOH   I 5 .   ? 0.446  -0.871  19.413 0.72 17.28  ? 331 HOH   A O   1 
HETATM 2252 O  O   . HOH   I 5 .   ? 2.223  14.628  16.855 0.72 26.22  ? 332 HOH   A O   1 
HETATM 2253 O  O   . HOH   I 5 .   ? 2.656  -2.776  20.763 0.72 18.84  ? 333 HOH   A O   1 
HETATM 2254 O  O   . HOH   I 5 .   ? -0.059 1.332   15.895 0.72 8.30   ? 334 HOH   A O   1 
HETATM 2255 O  O   . HOH   I 5 .   ? 36.400 17.988  14.335 0.72 24.91  ? 335 HOH   A O   1 
HETATM 2256 O  O   . HOH   I 5 .   ? 10.493 10.264  31.444 0.72 17.41  ? 336 HOH   A O   1 
HETATM 2257 O  O   . HOH   I 5 .   ? 26.826 -1.197  8.773  0.72 20.51  ? 337 HOH   A O   1 
HETATM 2258 O  O   . HOH   I 5 .   ? 20.983 -4.128  14.197 0.72 11.24  ? 338 HOH   A O   1 
HETATM 2259 O  O   . HOH   I 5 .   ? 8.622  19.213  19.540 0.72 17.09  ? 339 HOH   A O   1 
HETATM 2260 O  O   . HOH   I 5 .   ? 6.627  -6.805  23.742 0.72 19.86  ? 340 HOH   A O   1 
HETATM 2261 O  O   . HOH   I 5 .   ? 15.117 14.545  26.313 0.72 26.52  ? 341 HOH   A O   1 
HETATM 2262 O  O   . HOH   I 5 .   ? 26.567 -5.471  10.075 0.72 17.43  ? 342 HOH   A O   1 
HETATM 2263 O  O   . HOH   I 5 .   ? 13.731 4.016   23.531 0.72 7.85   ? 343 HOH   A O   1 
HETATM 2264 O  O   . HOH   I 5 .   ? 22.655 0.885   17.410 0.72 11.23  ? 344 HOH   A O   1 
HETATM 2265 O  O   . HOH   I 5 .   ? 16.590 3.892   23.663 0.72 13.16  ? 345 HOH   A O   1 
HETATM 2266 O  O   . HOH   I 5 .   ? 5.687  5.538   32.707 0.72 16.53  ? 346 HOH   A O   1 
HETATM 2267 O  O   . HOH   I 5 .   ? 23.294 11.767  21.930 0.72 30.45  ? 347 HOH   A O   1 
HETATM 2268 O  O   . HOH   I 5 .   ? 28.926 15.861  4.419  0.72 23.38  ? 348 HOH   A O   1 
HETATM 2269 O  O   . HOH   I 5 .   ? 4.484  11.377  27.737 0.72 40.49  ? 349 HOH   A O   1 
HETATM 2270 O  O   . HOH   I 5 .   ? 11.264 12.711  11.175 0.72 11.77  ? 350 HOH   A O   1 
HETATM 2271 O  O   . HOH   I 5 .   ? 13.970 13.833  23.945 0.72 16.76  ? 351 HOH   A O   1 
HETATM 2272 O  O   . HOH   I 5 .   ? 31.619 19.973  11.803 1.00 21.99  ? 352 HOH   A O   1 
HETATM 2273 O  O   . HOH   I 5 .   ? 24.847 5.106   21.420 0.72 26.09  ? 353 HOH   A O   1 
HETATM 2274 O  O   . HOH   I 5 .   ? 24.028 -3.572  15.982 0.72 26.61  ? 354 HOH   A O   1 
HETATM 2275 O  O   . HOH   I 5 .   ? 32.747 16.607  9.345  0.72 24.78  ? 355 HOH   A O   1 
HETATM 2276 O  O   . HOH   I 5 .   ? 33.701 11.226  15.561 0.72 27.75  ? 356 HOH   A O   1 
HETATM 2277 O  O   . HOH   I 5 .   ? 28.906 3.393   12.697 0.72 11.46  ? 357 HOH   A O   1 
HETATM 2278 O  O   . HOH   I 5 .   ? 29.400 11.921  21.146 0.72 25.53  ? 358 HOH   A O   1 
HETATM 2279 O  O   . HOH   I 5 .   ? 20.754 -2.541  16.822 0.72 10.70  ? 359 HOH   A O   1 
HETATM 2280 O  O   . HOH   I 5 .   ? 3.110  -0.451  2.874  1.00 46.60  ? 360 HOH   A O   1 
HETATM 2281 O  O   . HOH   I 5 .   ? 3.930  -3.870  6.073  1.00 28.39  ? 361 HOH   A O   1 
HETATM 2282 O  O   . HOH   I 5 .   ? 2.593  16.360  19.097 0.72 23.32  ? 362 HOH   A O   1 
HETATM 2283 O  O   . HOH   I 5 .   ? 22.793 -0.650  5.335  1.00 21.30  ? 363 HOH   A O   1 
HETATM 2284 O  O   . HOH   I 5 .   ? 30.517 2.954   14.836 0.72 17.09  ? 364 HOH   A O   1 
HETATM 2285 O  O   . HOH   I 5 .   ? 17.523 19.987  16.946 0.72 13.07  ? 365 HOH   A O   1 
HETATM 2286 O  O   . HOH   I 5 .   ? 13.210 11.430  9.254  0.72 9.51   ? 366 HOH   A O   1 
HETATM 2287 O  O   . HOH   I 5 .   ? 9.301  19.089  26.129 0.72 38.94  ? 367 HOH   A O   1 
HETATM 2288 O  O   . HOH   I 5 .   ? 14.406 -2.436  17.914 0.72 13.11  ? 368 HOH   A O   1 
HETATM 2289 O  O   . HOH   I 5 .   ? 18.096 17.948  4.376  0.72 29.23  ? 369 HOH   A O   1 
HETATM 2290 O  O   . HOH   I 5 .   ? 0.214  5.686   6.057  1.00 26.55  ? 370 HOH   A O   1 
HETATM 2291 O  O   . HOH   I 5 .   ? 34.028 18.755  10.877 1.00 25.19  ? 371 HOH   A O   1 
HETATM 2292 O  O   . HOH   I 5 .   ? 27.297 -1.281  15.860 0.72 18.29  ? 372 HOH   A O   1 
HETATM 2293 O  O   . HOH   I 5 .   ? 17.129 6.040   26.787 0.72 22.71  ? 373 HOH   A O   1 
HETATM 2294 O  O   . HOH   I 5 .   ? 7.373  20.357  17.473 0.72 18.95  ? 374 HOH   A O   1 
HETATM 2295 O  O   . HOH   I 5 .   ? 16.283 9.360   -1.630 1.00 22.93  ? 375 HOH   A O   1 
HETATM 2296 O  O   . HOH   I 5 .   ? 9.740  4.037   33.546 0.72 9.76   ? 376 HOH   A O   1 
HETATM 2297 O  O   . HOH   I 5 .   ? 4.085  8.942   27.491 0.72 27.21  ? 377 HOH   A O   1 
HETATM 2298 O  O   . HOH   I 5 .   ? 30.777 15.753  22.856 0.72 23.01  ? 378 HOH   A O   1 
HETATM 2299 O  O   . HOH   I 5 .   ? 17.681 10.652  26.074 0.72 20.75  ? 379 HOH   A O   1 
HETATM 2300 O  O   . HOH   I 5 .   ? 35.868 15.073  11.076 0.72 30.56  ? 380 HOH   A O   1 
HETATM 2301 O  O   . HOH   I 5 .   ? 4.228  0.408   23.974 0.72 12.91  ? 381 HOH   A O   1 
HETATM 2302 O  O   . HOH   I 5 .   ? 19.442 2.949   19.388 0.72 14.40  ? 382 HOH   A O   1 
HETATM 2303 O  O   . HOH   I 5 .   ? 32.162 2.097   6.044  1.00 35.29  ? 383 HOH   A O   1 
HETATM 2304 O  O   . HOH   I 5 .   ? 25.250 17.915  4.635  0.72 27.99  ? 384 HOH   A O   1 
HETATM 2305 O  O   . HOH   I 5 .   ? 30.300 4.629   5.774  1.00 22.15  ? 385 HOH   A O   1 
HETATM 2306 O  O   . HOH   I 5 .   ? 1.149  11.743  27.504 0.72 25.89  ? 386 HOH   A O   1 
HETATM 2307 O  O   . HOH   I 5 .   ? 32.001 8.777   7.645  1.00 22.99  ? 387 HOH   A O   1 
HETATM 2308 O  O   . HOH   I 5 .   ? 17.019 -3.568  27.790 0.72 27.66  ? 388 HOH   A O   1 
HETATM 2309 O  O   . HOH   I 5 .   ? 16.488 21.229  19.160 0.72 19.67  ? 389 HOH   A O   1 
HETATM 2310 O  O   . HOH   I 5 .   ? 10.972 -6.366  13.201 1.00 26.46  ? 390 HOH   A O   1 
HETATM 2311 O  O   . HOH   I 5 .   ? 30.922 -2.313  15.661 0.72 32.87  ? 391 HOH   A O   1 
HETATM 2312 O  O   . HOH   I 5 .   ? 10.734 5.485   3.374  1.00 26.71  ? 392 HOH   A O   1 
HETATM 2313 O  O   . HOH   I 5 .   ? 33.979 5.144   16.540 0.72 26.21  ? 393 HOH   A O   1 
HETATM 2314 O  O   . HOH   I 5 .   ? 35.232 10.666  12.338 0.72 33.48  ? 394 HOH   A O   1 
HETATM 2315 O  O   . HOH   I 5 .   ? 15.177 15.178  3.363  0.72 25.71  ? 395 HOH   A O   1 
HETATM 2316 O  O   . HOH   I 5 .   ? 0.521  -1.323  9.276  1.00 38.32  ? 396 HOH   A O   1 
HETATM 2317 O  O   . HOH   I 5 .   ? 25.478 19.671  21.730 1.00 27.11  ? 397 HOH   A O   1 
HETATM 2318 O  O   . HOH   I 5 .   ? 7.261  13.743  4.763  1.00 22.83  ? 398 HOH   A O   1 
HETATM 2319 O  O   . HOH   I 5 .   ? 5.676  16.972  21.669 0.72 32.13  ? 399 HOH   A O   1 
HETATM 2320 O  O   . HOH   I 5 .   ? 21.396 4.512   24.581 0.72 34.16  ? 400 HOH   A O   1 
HETATM 2321 O  O   . HOH   I 5 .   ? 36.304 -0.401  12.589 0.72 25.19  ? 401 HOH   A O   1 
HETATM 2322 O  O   . HOH   I 5 .   ? 0.449  -1.267  16.679 0.72 12.86  ? 402 HOH   A O   1 
HETATM 2323 O  O   . HOH   I 5 .   ? 15.162 -4.931  0.450  1.00 37.47  ? 403 HOH   A O   1 
HETATM 2324 O  O   . HOH   I 5 .   ? 17.452 0.657   20.241 0.72 13.49  ? 404 HOH   A O   1 
HETATM 2325 O  O   . HOH   I 5 .   ? 31.007 19.428  9.087  0.72 31.69  ? 405 HOH   A O   1 
HETATM 2326 O  O   . HOH   I 5 .   ? 5.278  26.758  19.689 0.72 28.67  ? 406 HOH   A O   1 
HETATM 2327 O  O   . HOH   I 5 .   ? 34.126 7.793   16.513 0.72 28.77  ? 407 HOH   A O   1 
HETATM 2328 O  O   . HOH   I 5 .   ? 9.922  10.581  22.907 0.72 24.10  ? 408 HOH   A O   1 
HETATM 2329 O  O   . HOH   I 5 .   ? 3.422  -0.273  21.455 0.72 15.79  ? 409 HOH   A O   1 
HETATM 2330 O  O   . HOH   I 5 .   ? 22.220 19.553  19.550 1.00 34.34  ? 410 HOH   A O   1 
HETATM 2331 O  O   . HOH   I 5 .   ? 19.662 -0.420  33.479 0.66 29.82  ? 411 HOH   A O   1 
HETATM 2332 O  O   . HOH   I 5 .   ? 19.722 13.301  2.172  0.66 23.78  ? 412 HOH   A O   1 
HETATM 2333 O  O   . HOH   I 5 .   ? 23.244 19.125  6.303  0.72 14.19  ? 413 HOH   A O   1 
HETATM 2334 O  O   . HOH   I 5 .   ? 16.752 -3.953  2.789  1.00 29.71  ? 414 HOH   A O   1 
HETATM 2335 O  O   . HOH   I 5 .   ? 15.770 21.527  7.346  0.72 21.62  ? 415 HOH   A O   1 
HETATM 2336 O  O   . HOH   I 5 .   ? 22.734 3.428   20.837 0.72 16.22  ? 416 HOH   A O   1 
HETATM 2337 O  O   . HOH   I 5 .   ? 1.589  7.703   26.895 0.72 36.45  ? 417 HOH   A O   1 
HETATM 2338 O  O   . HOH   I 5 .   ? 17.139 -2.475  19.645 0.72 14.13  ? 418 HOH   A O   1 
HETATM 2339 O  O   . HOH   I 5 .   ? 23.339 8.231   21.635 0.72 19.56  ? 419 HOH   A O   1 
HETATM 2340 O  O   . HOH   I 5 .   ? 36.668 2.218   9.789  0.72 36.72  ? 420 HOH   A O   1 
HETATM 2341 O  O   . HOH   I 5 .   ? 21.062 9.961   21.887 0.72 13.60  ? 421 HOH   A O   1 
HETATM 2342 O  O   . HOH   I 5 .   ? 20.069 -4.229  10.974 0.72 24.79  ? 422 HOH   A O   1 
HETATM 2343 O  O   . HOH   I 5 .   ? 5.510  18.143  24.037 0.72 38.30  ? 423 HOH   A O   1 
HETATM 2344 O  O   . HOH   I 5 .   ? 1.226  4.099   26.339 0.72 24.64  ? 424 HOH   A O   1 
HETATM 2345 O  O   . HOH   I 5 .   ? 31.768 7.099   5.281  1.00 31.20  ? 425 HOH   A O   1 
HETATM 2346 O  O   . HOH   I 5 .   ? 19.324 -2.946  33.809 0.66 31.14  ? 426 HOH   A O   1 
HETATM 2347 O  O   . HOH   I 5 .   ? 6.474  3.202   3.276  1.00 35.32  ? 427 HOH   A O   1 
HETATM 2348 O  O   . HOH   I 5 .   ? 18.532 3.234   26.008 0.72 31.47  ? 428 HOH   A O   1 
HETATM 2349 O  O   . HOH   I 5 .   ? 18.463 2.174   22.562 0.72 30.02  ? 429 HOH   A O   1 
HETATM 2350 O  O   . HOH   I 5 .   ? 16.913 -4.970  34.319 1.00 32.67  ? 430 HOH   A O   1 
HETATM 2351 O  O   . HOH   I 5 .   ? 7.154  21.308  26.913 0.72 33.57  ? 431 HOH   A O   1 
HETATM 2352 O  O   . HOH   I 5 .   ? 29.584 0.630   16.508 0.72 26.97  ? 432 HOH   A O   1 
HETATM 2353 O  O   . HOH   I 5 .   ? 8.651  12.154  31.725 0.72 29.35  ? 433 HOH   A O   1 
HETATM 2354 O  O   . HOH   I 5 .   ? 23.767 0.983   19.902 0.72 26.15  ? 434 HOH   A O   1 
HETATM 2355 O  O   . HOH   I 5 .   ? 30.355 7.094   17.686 0.72 25.66  ? 435 HOH   A O   1 
HETATM 2356 O  O   . HOH   I 5 .   ? 8.068  16.732  26.057 0.72 32.66  ? 436 HOH   A O   1 
HETATM 2357 O  O   . HOH   I 5 .   ? 12.550 -4.991  33.204 1.00 26.51  ? 437 HOH   A O   1 
HETATM 2358 O  O   . HOH   I 5 .   ? 21.228 11.264  24.557 0.72 29.71  ? 438 HOH   A O   1 
HETATM 2359 O  O   . HOH   I 5 .   ? 21.188 -1.004  18.988 0.72 23.15  ? 439 HOH   A O   1 
HETATM 2360 O  O   . HOH   I 5 .   ? 31.178 4.539   17.021 0.72 20.53  ? 440 HOH   A O   1 
HETATM 2361 O  O   . HOH   I 5 .   ? 37.767 -4.505  6.723  0.72 25.76  ? 441 HOH   A O   1 
HETATM 2362 O  O   . HOH   I 5 .   ? 2.542  -5.007  22.603 0.72 25.93  ? 442 HOH   A O   1 
HETATM 2363 O  O   . HOH   I 5 .   ? 10.441 15.461  26.034 0.72 66.14  ? 443 HOH   A O   1 
HETATM 2364 O  O   . HOH   I 5 .   ? 28.677 1.347   19.048 0.72 35.92  ? 444 HOH   A O   1 
HETATM 2365 O  O   . HOH   I 5 .   ? 4.077  -6.761  23.290 0.72 37.08  ? 445 HOH   A O   1 
HETATM 2366 O  O   . HOH   I 5 .   ? 26.371 0.473   20.048 0.72 36.73  ? 446 HOH   A O   1 
HETATM 2367 O  O   . HOH   I 5 .   ? 1.678  -4.238  25.332 0.72 37.50  ? 447 HOH   A O   1 
HETATM 2368 O  O   . HOH   J 5 .   ? 23.456 -28.155 1.521  1.00 30.74  ? 301 HOH   C O   1 
HETATM 2369 O  O   . HOH   J 5 .   ? 23.672 -26.402 4.343  1.00 21.57  ? 302 HOH   C O   1 
HETATM 2370 O  O   . HOH   J 5 .   ? 28.207 -5.202  18.552 0.72 28.99  ? 303 HOH   C O   1 
HETATM 2371 O  O   . HOH   J 5 .   ? 17.745 -33.200 23.986 1.00 37.06  ? 304 HOH   C O   1 
HETATM 2372 O  O   . HOH   J 5 .   ? 38.324 -7.412  7.067  0.72 17.04  ? 305 HOH   C O   1 
HETATM 2373 O  O   . HOH   J 5 .   ? 39.035 -18.677 21.533 1.00 25.04  ? 306 HOH   C O   1 
HETATM 2374 O  O   . HOH   J 5 .   ? 36.196 -26.035 34.075 1.00 33.12  ? 307 HOH   C O   1 
HETATM 2375 O  O   . HOH   J 5 .   ? 14.732 -23.863 12.429 1.00 32.17  ? 308 HOH   C O   1 
HETATM 2376 O  O   . HOH   J 5 .   ? 19.762 -4.161  20.172 0.72 17.11  ? 309 HOH   C O   1 
HETATM 2377 O  O   . HOH   J 5 .   ? 22.922 -5.996  21.208 0.72 13.78  ? 310 HOH   C O   1 
HETATM 2378 O  O   . HOH   J 5 .   ? 22.690 -29.460 -2.940 1.00 27.78  ? 311 HOH   C O   1 
HETATM 2379 O  O   . HOH   J 5 .   ? 14.746 -18.657 32.003 1.00 39.30  ? 312 HOH   C O   1 
HETATM 2380 O  O   . HOH   J 5 .   ? 30.779 -18.125 26.924 0.72 13.75  ? 313 HOH   C O   1 
HETATM 2381 O  O   . HOH   J 5 .   ? 20.779 -18.772 12.828 1.00 13.73  ? 314 HOH   C O   1 
HETATM 2382 O  O   . HOH   J 5 .   ? 36.153 -17.572 11.657 0.72 21.50  ? 315 HOH   C O   1 
HETATM 2383 O  O   . HOH   J 5 .   ? 16.862 -9.471  27.653 0.72 29.79  ? 316 HOH   C O   1 
HETATM 2384 O  O   . HOH   J 5 .   ? 10.240 -20.163 28.958 1.00 33.00  ? 317 HOH   C O   1 
HETATM 2385 O  O   . HOH   J 5 .   ? 13.315 -11.278 28.416 0.72 29.56  ? 318 HOH   C O   1 
HETATM 2386 O  O   . HOH   J 5 .   ? 36.289 -2.420  11.061 0.72 24.10  ? 319 HOH   C O   1 
HETATM 2387 O  O   . HOH   J 5 .   ? 10.274 -17.563 18.336 1.00 26.83  ? 320 HOH   C O   1 
HETATM 2388 O  O   . HOH   J 5 .   ? 13.361 -29.639 19.315 1.00 32.10  ? 321 HOH   C O   1 
HETATM 2389 O  O   . HOH   J 5 .   ? 18.631 -8.869  13.743 0.72 23.32  ? 322 HOH   C O   1 
HETATM 2390 O  O   . HOH   J 5 .   ? 40.579 -27.246 15.279 1.00 12.28  ? 323 HOH   C O   1 
HETATM 2391 O  O   . HOH   J 5 .   ? 17.873 -27.535 16.486 1.00 19.14  ? 324 HOH   C O   1 
HETATM 2392 O  O   . HOH   J 5 .   ? 40.089 -29.653 11.947 1.00 21.04  ? 325 HOH   C O   1 
HETATM 2393 O  O   . HOH   J 5 .   ? 41.519 -24.935 7.395  0.66 23.40  ? 326 HOH   C O   1 
HETATM 2394 O  O   . HOH   J 5 .   ? 10.433 -16.971 15.018 1.00 28.85  ? 327 HOH   C O   1 
HETATM 2395 O  O   . HOH   J 5 .   ? 26.100 -25.292 8.809  1.00 12.34  ? 328 HOH   C O   1 
HETATM 2396 O  O   . HOH   J 5 .   ? 37.329 -31.983 10.935 1.00 24.05  ? 329 HOH   C O   1 
HETATM 2397 O  O   . HOH   J 5 .   ? 7.257  -30.398 21.972 0.72 29.20  ? 330 HOH   C O   1 
HETATM 2398 O  O   . HOH   J 5 .   ? 24.663 -5.972  15.254 0.72 22.72  ? 331 HOH   C O   1 
HETATM 2399 O  O   . HOH   J 5 .   ? 39.956 -25.218 7.147  0.66 30.08  ? 332 HOH   C O   1 
HETATM 2400 O  O   . HOH   J 5 .   ? 37.268 -18.715 28.210 0.72 24.49  ? 333 HOH   C O   1 
HETATM 2401 O  O   . HOH   J 5 .   ? 24.380 -9.353  26.929 0.72 31.04  ? 334 HOH   C O   1 
HETATM 2402 O  O   . HOH   J 5 .   ? 29.784 -13.093 13.035 0.72 10.11  ? 335 HOH   C O   1 
HETATM 2403 O  O   . HOH   J 5 .   ? 17.571 -24.012 8.567  1.00 39.26  ? 336 HOH   C O   1 
HETATM 2404 O  O   . HOH   J 5 .   ? 30.966 -21.521 28.428 0.72 12.31  ? 337 HOH   C O   1 
HETATM 2405 O  O   . HOH   J 5 .   ? 35.156 -32.851 3.374  1.00 30.50  ? 338 HOH   C O   1 
HETATM 2406 O  O   . HOH   J 5 .   ? 32.508 -23.726 29.145 0.72 11.85  ? 339 HOH   C O   1 
HETATM 2407 O  O   . HOH   J 5 .   ? 34.869 -34.855 18.135 1.00 33.37  ? 340 HOH   C O   1 
HETATM 2408 O  O   . HOH   J 5 .   ? 24.848 -15.780 7.367  1.00 17.21  ? 341 HOH   C O   1 
HETATM 2409 O  O   . HOH   J 5 .   ? 14.641 -28.963 25.624 1.00 33.52  ? 342 HOH   C O   1 
HETATM 2410 O  O   . HOH   J 5 .   ? 42.647 -11.353 11.220 0.72 26.58  ? 343 HOH   C O   1 
HETATM 2411 O  O   . HOH   J 5 .   ? 22.041 -28.703 4.734  1.00 25.56  ? 344 HOH   C O   1 
HETATM 2412 O  O   . HOH   J 5 .   ? 29.977 -10.619 27.885 0.72 30.99  ? 345 HOH   C O   1 
HETATM 2413 O  O   . HOH   J 5 .   ? 29.938 -15.279 19.622 1.00 13.37  ? 346 HOH   C O   1 
HETATM 2414 O  O   . HOH   J 5 .   ? 13.879 -24.245 29.387 1.00 32.62  ? 347 HOH   C O   1 
HETATM 2415 O  O   . HOH   J 5 .   ? 39.044 -16.067 4.156  0.66 30.45  ? 348 HOH   C O   1 
HETATM 2416 O  O   . HOH   J 5 .   ? 35.185 -13.132 8.773  0.72 14.74  ? 349 HOH   C O   1 
HETATM 2417 O  O   . HOH   J 5 .   ? 31.457 -13.383 4.443  0.72 27.20  ? 350 HOH   C O   1 
HETATM 2418 O  O   . HOH   J 5 .   ? 21.780 -26.329 34.444 0.72 22.61  ? 351 HOH   C O   1 
HETATM 2419 O  O   . HOH   J 5 .   ? 23.897 -8.197  9.424  0.72 16.93  ? 352 HOH   C O   1 
HETATM 2420 O  O   . HOH   J 5 .   ? 26.287 -15.298 30.774 0.72 29.00  ? 353 HOH   C O   1 
HETATM 2421 O  O   . HOH   J 5 .   ? 11.920 -24.304 21.721 1.00 16.25  ? 354 HOH   C O   1 
HETATM 2422 O  O   . HOH   J 5 .   ? 9.274  -8.056  21.408 0.72 17.98  ? 355 HOH   C O   1 
HETATM 2423 O  O   . HOH   J 5 .   ? 27.053 -35.547 20.813 1.00 25.75  ? 356 HOH   C O   1 
HETATM 2424 O  O   . HOH   J 5 .   ? 31.999 -34.754 24.925 1.00 26.50  ? 357 HOH   C O   1 
HETATM 2425 O  O   . HOH   J 5 .   ? 4.342  -10.450 19.637 0.72 23.61  ? 358 HOH   C O   1 
HETATM 2426 O  O   . HOH   J 5 .   ? 9.838  -8.894  23.893 0.72 20.51  ? 359 HOH   C O   1 
HETATM 2427 O  O   . HOH   J 5 .   ? 19.216 -27.717 28.203 1.00 18.01  ? 360 HOH   C O   1 
HETATM 2428 O  O   . HOH   J 5 .   ? 25.858 -37.846 24.267 1.00 30.90  ? 361 HOH   C O   1 
HETATM 2429 O  O   . HOH   J 5 .   ? 11.161 -21.689 13.765 1.00 38.85  ? 362 HOH   C O   1 
HETATM 2430 O  O   . HOH   J 5 .   ? 10.369 -30.856 25.042 0.72 32.29  ? 363 HOH   C O   1 
HETATM 2431 O  O   . HOH   J 5 .   ? 32.012 -10.441 13.816 0.72 13.58  ? 364 HOH   C O   1 
HETATM 2432 O  O   . HOH   J 5 .   ? 22.361 -23.658 6.197  1.00 37.37  ? 365 HOH   C O   1 
HETATM 2433 O  O   . HOH   J 5 .   ? 23.710 -3.453  19.090 0.72 29.59  ? 366 HOH   C O   1 
HETATM 2434 O  O   . HOH   J 5 .   ? 6.820  -9.202  22.665 0.72 28.92  ? 367 HOH   C O   1 
HETATM 2435 O  O   . HOH   J 5 .   ? 37.315 -10.374 4.906  0.72 27.35  ? 368 HOH   C O   1 
HETATM 2436 O  O   . HOH   J 5 .   ? 20.780 -25.687 13.866 1.00 22.53  ? 369 HOH   C O   1 
HETATM 2437 O  O   . HOH   J 5 .   ? 23.580 -33.565 29.122 1.00 25.55  ? 370 HOH   C O   1 
HETATM 2438 O  O   . HOH   J 5 .   ? 22.926 -8.531  14.069 0.72 11.78  ? 371 HOH   C O   1 
HETATM 2439 O  O   . HOH   J 5 .   ? 28.923 -36.219 7.894  0.72 15.25  ? 372 HOH   C O   1 
HETATM 2440 O  O   . HOH   J 5 .   ? 31.115 -23.913 -1.219 1.00 22.79  ? 373 HOH   C O   1 
HETATM 2441 O  O   . HOH   J 5 .   ? 38.489 -13.490 10.740 0.72 30.43  ? 374 HOH   C O   1 
HETATM 2442 O  O   . HOH   J 5 .   ? 23.234 -25.418 8.925  1.00 18.56  ? 375 HOH   C O   1 
HETATM 2443 O  O   . HOH   J 5 .   ? 36.351 -21.323 6.944  0.66 18.40  ? 376 HOH   C O   1 
HETATM 2444 O  O   . HOH   J 5 .   ? 32.976 -9.820  11.159 0.72 10.45  ? 377 HOH   C O   1 
HETATM 2445 O  O   . HOH   J 5 .   ? 30.387 -18.165 8.423  0.72 18.66  ? 378 HOH   C O   1 
HETATM 2446 O  O   . HOH   J 5 .   ? 37.443 -31.587 25.740 1.00 29.07  ? 379 HOH   C O   1 
HETATM 2447 O  O   . HOH   J 5 .   ? 31.301 -12.169 10.679 0.72 10.34  ? 380 HOH   C O   1 
HETATM 2448 O  O   . HOH   J 5 .   ? 22.978 -28.136 12.640 1.00 20.49  ? 381 HOH   C O   1 
HETATM 2449 O  O   . HOH   J 5 .   ? 22.793 -33.310 5.463  1.00 31.15  ? 382 HOH   C O   1 
HETATM 2450 O  O   . HOH   J 5 .   ? 28.132 -16.354 22.093 1.00 12.06  ? 383 HOH   C O   1 
HETATM 2451 O  O   . HOH   J 5 .   ? 11.439 -22.367 28.581 1.00 28.43  ? 384 HOH   C O   1 
HETATM 2452 O  O   . HOH   J 5 .   ? 3.869  -8.292  14.688 0.72 21.97  ? 385 HOH   C O   1 
HETATM 2453 O  O   . HOH   J 5 .   ? 26.006 -31.047 30.907 1.00 16.43  ? 386 HOH   C O   1 
HETATM 2454 O  O   . HOH   J 5 .   ? 26.406 -31.225 14.891 1.00 18.94  ? 387 HOH   C O   1 
HETATM 2455 O  O   . HOH   J 5 .   ? 31.388 -35.466 31.835 1.00 37.13  ? 388 HOH   C O   1 
HETATM 2456 O  O   . HOH   J 5 .   ? 37.922 -23.457 4.581  0.66 31.26  ? 389 HOH   C O   1 
HETATM 2457 O  O   . HOH   J 5 .   ? 36.942 -29.260 10.213 1.00 20.93  ? 390 HOH   C O   1 
HETATM 2458 O  O   . HOH   J 5 .   ? 20.456 -23.638 34.755 1.00 31.31  ? 391 HOH   C O   1 
HETATM 2459 O  O   . HOH   J 5 .   ? 14.743 -18.493 10.465 1.00 39.89  ? 392 HOH   C O   1 
HETATM 2460 O  O   . HOH   J 5 .   ? 34.679 -23.287 -0.725 1.00 32.92  ? 393 HOH   C O   1 
HETATM 2461 O  O   . HOH   J 5 .   ? 26.703 -11.990 27.492 0.72 23.55  ? 394 HOH   C O   1 
HETATM 2462 O  O   . HOH   J 5 .   ? 8.859  -13.312 10.795 1.00 24.17  ? 395 HOH   C O   1 
HETATM 2463 O  O   . HOH   J 5 .   ? 10.072 -24.858 19.792 1.00 20.23  ? 396 HOH   C O   1 
HETATM 2464 O  O   . HOH   J 5 .   ? 4.733  -28.117 23.198 1.00 36.67  ? 397 HOH   C O   1 
HETATM 2465 O  O   . HOH   J 5 .   ? 43.267 -25.271 23.839 0.72 18.31  ? 398 HOH   C O   1 
HETATM 2466 O  O   . HOH   J 5 .   ? 38.859 -14.523 13.481 0.72 27.41  ? 399 HOH   C O   1 
HETATM 2467 O  O   . HOH   J 5 .   ? 31.159 -6.013  5.906  1.00 36.52  ? 400 HOH   C O   1 
HETATM 2468 O  O   . HOH   J 5 .   ? 34.390 -13.430 25.521 0.72 15.48  ? 401 HOH   C O   1 
HETATM 2469 O  O   . HOH   J 5 .   ? 21.729 -18.890 5.939  1.00 27.04  ? 402 HOH   C O   1 
HETATM 2470 O  O   . HOH   J 5 .   ? 33.070 -30.311 31.735 1.00 18.54  ? 403 HOH   C O   1 
HETATM 2471 O  O   . HOH   J 5 .   ? 41.736 -12.281 18.035 1.00 28.00  ? 404 HOH   C O   1 
HETATM 2472 O  O   . HOH   J 5 .   ? 35.651 -24.632 24.714 0.72 14.71  ? 405 HOH   C O   1 
HETATM 2473 O  O   . HOH   J 5 .   ? 38.896 -13.019 25.799 0.72 21.64  ? 406 HOH   C O   1 
HETATM 2474 O  O   . HOH   J 5 .   ? 23.425 -31.029 13.303 1.00 33.73  ? 407 HOH   C O   1 
HETATM 2475 O  O   . HOH   J 5 .   ? 10.838 -11.870 8.969  1.00 31.44  ? 408 HOH   C O   1 
HETATM 2476 O  O   . HOH   J 5 .   ? 22.644 -13.812 29.856 0.72 28.11  ? 409 HOH   C O   1 
HETATM 2477 O  O   . HOH   J 5 .   ? 33.699 -36.036 8.891  1.00 40.79  ? 410 HOH   C O   1 
HETATM 2478 O  O   . HOH   J 5 .   ? 20.359 -32.159 22.313 1.00 30.56  ? 411 HOH   C O   1 
HETATM 2479 O  O   . HOH   J 5 .   ? 37.877 -20.467 4.918  0.66 28.02  ? 412 HOH   C O   1 
HETATM 2480 O  O   . HOH   J 5 .   ? 16.439 -20.594 11.657 1.00 26.11  ? 413 HOH   C O   1 
HETATM 2481 O  O   . HOH   J 5 .   ? 35.775 -28.609 7.835  1.00 18.31  ? 414 HOH   C O   1 
HETATM 2482 O  O   . HOH   J 5 .   ? 18.665 -8.309  25.518 0.72 15.87  ? 415 HOH   C O   1 
HETATM 2483 O  O   . HOH   J 5 .   ? 26.651 -6.063  22.168 0.72 21.71  ? 416 HOH   C O   1 
HETATM 2484 O  O   . HOH   J 5 .   ? 24.553 -13.634 5.509  1.00 38.75  ? 417 HOH   C O   1 
HETATM 2485 O  O   . HOH   J 5 .   ? 17.224 -25.328 12.786 1.00 22.80  ? 418 HOH   C O   1 
HETATM 2486 O  O   . HOH   J 5 .   ? 34.096 -15.532 27.087 0.72 24.55  ? 419 HOH   C O   1 
HETATM 2487 O  O   . HOH   J 5 .   ? 34.975 -4.127  17.746 0.72 23.39  ? 420 HOH   C O   1 
HETATM 2488 O  O   . HOH   J 5 .   ? 18.742 -11.786 7.658  1.00 47.32  ? 421 HOH   C O   1 
HETATM 2489 O  O   . HOH   J 5 .   ? 6.544  -22.944 18.365 1.00 31.54  ? 422 HOH   C O   1 
HETATM 2490 O  O   . HOH   J 5 .   ? 40.052 -29.900 14.658 1.00 16.15  ? 423 HOH   C O   1 
HETATM 2491 O  O   . HOH   J 5 .   ? 32.822 -14.330 9.508  0.72 10.23  ? 424 HOH   C O   1 
HETATM 2492 O  O   . HOH   J 5 .   ? 18.846 -19.139 10.846 1.00 18.60  ? 425 HOH   C O   1 
HETATM 2493 O  O   . HOH   J 5 .   ? 9.690  -11.801 26.492 0.72 39.75  ? 426 HOH   C O   1 
HETATM 2494 O  O   . HOH   J 5 .   ? 35.170 -13.550 6.175  0.72 31.36  ? 427 HOH   C O   1 
HETATM 2495 O  O   . HOH   J 5 .   ? 15.179 -29.967 17.905 1.00 41.44  ? 428 HOH   C O   1 
HETATM 2496 O  O   . HOH   J 5 .   ? 5.859  -17.141 22.029 1.00 40.38  ? 429 HOH   C O   1 
HETATM 2497 O  O   . HOH   J 5 .   ? 6.567  -20.047 18.242 1.00 30.68  ? 430 HOH   C O   1 
HETATM 2498 O  O   . HOH   J 5 .   ? 33.621 -32.853 0.872  1.00 43.32  ? 431 HOH   C O   1 
HETATM 2499 O  O   . HOH   J 5 .   ? 31.594 -15.726 7.264  0.72 19.87  ? 432 HOH   C O   1 
HETATM 2500 O  O   . HOH   J 5 .   ? 23.340 -17.586 33.351 0.72 19.58  ? 433 HOH   C O   1 
HETATM 2501 O  O   . HOH   J 5 .   ? 41.890 -31.465 15.810 0.72 24.36  ? 434 HOH   C O   1 
HETATM 2502 O  O   . HOH   J 5 .   ? 36.681 -24.488 27.197 0.72 29.87  ? 435 HOH   C O   1 
HETATM 2503 O  O   . HOH   J 5 .   ? 34.230 -31.818 29.564 1.00 24.29  ? 436 HOH   C O   1 
HETATM 2504 O  O   . HOH   J 5 .   ? 23.788 -15.705 31.483 0.72 28.30  ? 437 HOH   C O   1 
HETATM 2505 O  O   . HOH   J 5 .   ? 42.488 -11.941 20.310 0.72 43.95  ? 438 HOH   C O   1 
HETATM 2506 O  O   . HOH   J 5 .   ? 33.829 -20.622 -2.306 1.00 38.49  ? 439 HOH   C O   1 
HETATM 2507 O  O   . HOH   J 5 .   ? 3.886  -23.593 26.947 1.00 60.81  ? 440 HOH   C O   1 
HETATM 2508 O  O   . HOH   J 5 .   ? 21.618 -26.871 10.226 1.00 33.97  ? 441 HOH   C O   1 
HETATM 2509 O  O   . HOH   J 5 .   ? 8.985  -19.210 17.066 1.00 37.71  ? 442 HOH   C O   1 
HETATM 2510 O  O   . HOH   J 5 .   ? 20.721 -7.276  26.964 0.72 37.46  ? 443 HOH   C O   1 
HETATM 2511 O  O   . HOH   J 5 .   ? 16.474 -27.478 14.161 1.00 33.85  ? 444 HOH   C O   1 
HETATM 2512 O  O   . HOH   J 5 .   ? 2.519  -8.962  12.447 0.72 40.02  ? 445 HOH   C O   1 
HETATM 2513 O  O   . HOH   J 5 .   ? 40.942 -28.451 8.139  1.00 46.87  ? 446 HOH   C O   1 
HETATM 2514 O  O   . HOH   J 5 .   ? 43.528 -20.338 4.135  1.00 46.63  ? 447 HOH   C O   1 
HETATM 2515 O  O   . HOH   J 5 .   ? 18.477 -26.004 10.208 1.00 38.13  ? 448 HOH   C O   1 
HETATM 2516 O  O   . HOH   J 5 .   ? 32.557 -19.327 29.049 0.72 23.77  ? 449 HOH   C O   1 
HETATM 2517 O  O   . HOH   J 5 .   ? 18.144 -18.019 8.519  1.00 31.38  ? 450 HOH   C O   1 
HETATM 2518 O  O   . HOH   J 5 .   ? 17.194 -28.946 28.855 1.00 36.73  ? 451 HOH   C O   1 
HETATM 2519 O  O   . HOH   J 5 .   ? 22.820 -11.888 6.185  1.00 36.71  ? 452 HOH   C O   1 
HETATM 2520 O  O   . HOH   J 5 .   ? 22.371 -7.869  11.515 0.72 25.99  ? 453 HOH   C O   1 
HETATM 2521 O  O   . HOH   J 5 .   ? 35.217 -23.167 28.942 0.72 23.38  ? 454 HOH   C O   1 
HETATM 2522 O  O   . HOH   J 5 .   ? 9.092  -23.418 17.734 1.00 33.54  ? 455 HOH   C O   1 
HETATM 2523 O  O   . HOH   J 5 .   ? 3.258  -8.913  22.058 0.72 32.65  ? 456 HOH   C O   1 
HETATM 2524 O  O   . HOH   J 5 .   ? 39.229 -2.625  11.002 0.72 29.46  ? 457 HOH   C O   1 
HETATM 2525 O  O   . HOH   J 5 .   ? 34.321 -10.731 26.671 0.72 40.95  ? 458 HOH   C O   1 
HETATM 2526 O  O   . HOH   J 5 .   ? 19.352 -17.680 5.969  1.00 37.72  ? 459 HOH   C O   1 
HETATM 2527 O  O   . HOH   J 5 .   ? 3.215  -9.340  17.062 0.72 26.67  ? 460 HOH   C O   1 
# 
