data_7HY5
# 
_entry.id   7HY5 
# 
_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   7HY5         pdb_00007hy5 10.2210/pdb7hy5/pdb 
WWPDB D_1001408077 ?            ?                   
# 
_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       2025-02-26 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.entry_id                        7HY5 
_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   2025-01-10 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frank.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lithgo, R.M.'        1  ? 
'Fairhead, M.'        2  ? 
'Koekemoer, L.'       3  ? 
'Balcomb, B.H.'       4  ? 
'Capkin, E.'          5  ? 
'Chandran, A.V.'      6  ? 
'Golding, M.'         7  ? 
'Godoy, A.S.'         8  ? 
'Aschenbrenner, J.C.' 9  ? 
'Marples, P.G.'       10 ? 
'Ni, X.'              11 ? 
'Thompson, W.'        12 ? 
'Tomlinson, C.W.E.'   13 ? 
'Wild, C.'            14 ? 
'Winokan, M.'         15 ? 
'Xavier, M.-A.E.'     16 ? 
'Kenton, N.'          17 ? 
'Tucker, J.'          18 ? 
'DiPoto, M.'          19 ? 
'Lee, A.'             20 ? 
'Fearon, D.'          21 ? 
'von Delft, F.'       22 ? 
# 
_citation.id                        primary 
_citation.title                     
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Lithgo, R.M.'        ? 1  
primary 'Fairhead, M.'        ? 2  
primary 'Koekemoer, L.'       ? 3  
primary 'Balcomb, B.H.'       ? 4  
primary 'Capkin, E.'          ? 5  
primary 'Chandran, A.V.'      ? 6  
primary 'Golding, M.'         ? 7  
primary 'Godoy, A.S.'         ? 8  
primary 'Aschenbrenner, J.C.' ? 9  
primary 'Marples, P.G.'       ? 10 
primary 'Ni, X.'              ? 11 
primary 'Thompson, W.'        ? 12 
primary 'Tomlinson, C.W.E.'   ? 13 
primary 'Wild, C.'            ? 14 
primary 'Winokan, M.'         ? 15 
primary 'Xavier, M.-A.E.'     ? 16 
primary 'Kenton, N.'          ? 17 
primary 'Tucker, J.'          ? 18 
primary 'DiPoto, M.'          ? 19 
primary 'Lee, A.'             ? 20 
primary 'Fearon, D.'          ? 21 
primary 'von Delft, F.'       ? 22 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Protease 2A'                                                 15892.732 1  3.4.22.29 ? ? ? 
2 non-polymer syn '(3S)-1-[(2,3-dichlorophenyl)acetyl]piperidine-3-carboxamide' 315.195   1  ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                    65.409    1  ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                          78.133    1  ?         ? ? ? 
5 water       nat water                                                         18.015    69 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'P2A,Picornain 2A,Protein 2A' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '(3S)-1-[(2,3-dichlorophenyl)acetyl]piperidine-3-carboxamide' A1BR0 
3 'ZINC ION'                                                    ZN    
4 'DIMETHYL SULFOXIDE'                                          DMS   
5 water                                                         HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   GLY n 
1 3   ALA n 
1 4   ILE n 
1 5   TYR n 
1 6   VAL n 
1 7   GLY n 
1 8   ASN n 
1 9   TYR n 
1 10  ARG n 
1 11  VAL n 
1 12  VAL n 
1 13  ASN n 
1 14  ARG n 
1 15  HIS n 
1 16  LEU n 
1 17  ALA n 
1 18  THR n 
1 19  HIS n 
1 20  ASN n 
1 21  ASP n 
1 22  TRP n 
1 23  ALA n 
1 24  ASN n 
1 25  LEU n 
1 26  VAL n 
1 27  TRP n 
1 28  GLU n 
1 29  ASP n 
1 30  SER n 
1 31  SER n 
1 32  ARG n 
1 33  ASP n 
1 34  LEU n 
1 35  LEU n 
1 36  VAL n 
1 37  SER n 
1 38  SER n 
1 39  THR n 
1 40  THR n 
1 41  ALA n 
1 42  GLN n 
1 43  GLY n 
1 44  CYS n 
1 45  ASP n 
1 46  THR n 
1 47  ILE n 
1 48  ALA n 
1 49  ARG n 
1 50  CYS n 
1 51  ASP n 
1 52  CYS n 
1 53  GLN n 
1 54  THR n 
1 55  GLY n 
1 56  VAL n 
1 57  TYR n 
1 58  TYR n 
1 59  CYS n 
1 60  SER n 
1 61  SER n 
1 62  ARG n 
1 63  ARG n 
1 64  LYS n 
1 65  HIS n 
1 66  TYR n 
1 67  PRO n 
1 68  VAL n 
1 69  SER n 
1 70  PHE n 
1 71  SER n 
1 72  LYS n 
1 73  PRO n 
1 74  SER n 
1 75  LEU n 
1 76  ILE n 
1 77  PHE n 
1 78  VAL n 
1 79  GLU n 
1 80  ALA n 
1 81  SER n 
1 82  GLU n 
1 83  TYR n 
1 84  TYR n 
1 85  PRO n 
1 86  ALA n 
1 87  ARG n 
1 88  TYR n 
1 89  GLN n 
1 90  SER n 
1 91  HIS n 
1 92  LEU n 
1 93  MET n 
1 94  LEU n 
1 95  ALA n 
1 96  VAL n 
1 97  GLY n 
1 98  HIS n 
1 99  SER n 
1 100 GLU n 
1 101 PRO n 
1 102 GLY n 
1 103 ASP n 
1 104 CYS n 
1 105 GLY n 
1 106 GLY n 
1 107 ILE n 
1 108 LEU n 
1 109 ARG n 
1 110 CYS n 
1 111 GLN n 
1 112 HIS n 
1 113 GLY n 
1 114 VAL n 
1 115 VAL n 
1 116 GLY n 
1 117 ILE n 
1 118 VAL n 
1 119 SER n 
1 120 THR n 
1 121 GLY n 
1 122 GLY n 
1 123 ASN n 
1 124 GLY n 
1 125 LEU n 
1 126 VAL n 
1 127 GLY n 
1 128 PHE n 
1 129 ALA n 
1 130 ASP n 
1 131 VAL n 
1 132 ARG n 
1 133 ASP n 
1 134 LEU n 
1 135 LEU n 
1 136 TRP n 
1 137 LEU n 
1 138 ASP n 
1 139 GLU n 
1 140 GLU n 
1 141 ALA n 
1 142 MET n 
1 143 GLU n 
1 144 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   144 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Coxsackievirus A16' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     31704 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1BR0 non-polymer         . '(3S)-1-[(2,3-dichlorophenyl)acetyl]piperidine-3-carboxamide' ? 'C14 H16 Cl2 N2 O2' 315.195 
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 ?   ?   ?   A . n 
A 1 141 ALA 141 147 ?   ?   ?   A . n 
A 1 142 MET 142 148 ?   ?   ?   A . n 
A 1 143 GLU 143 149 ?   ?   ?   A . n 
A 1 144 GLN 144 150 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BR0 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BR0 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 A1BR0 1  201 201 A1BR0 LIG A . 
C 3 ZN    1  202 1   ZN    ZN  A . 
D 4 DMS   1  203 6   DMS   DMS A . 
E 5 HOH   1  301 9   HOH   HOH A . 
E 5 HOH   2  302 59  HOH   HOH A . 
E 5 HOH   3  303 47  HOH   HOH A . 
E 5 HOH   4  304 36  HOH   HOH A . 
E 5 HOH   5  305 22  HOH   HOH A . 
E 5 HOH   6  306 42  HOH   HOH A . 
E 5 HOH   7  307 37  HOH   HOH A . 
E 5 HOH   8  308 18  HOH   HOH A . 
E 5 HOH   9  309 34  HOH   HOH A . 
E 5 HOH   10 310 14  HOH   HOH A . 
E 5 HOH   11 311 25  HOH   HOH A . 
E 5 HOH   12 312 12  HOH   HOH A . 
E 5 HOH   13 313 16  HOH   HOH A . 
E 5 HOH   14 314 7   HOH   HOH A . 
E 5 HOH   15 315 29  HOH   HOH A . 
E 5 HOH   16 316 35  HOH   HOH A . 
E 5 HOH   17 317 33  HOH   HOH A . 
E 5 HOH   18 318 27  HOH   HOH A . 
E 5 HOH   19 319 2   HOH   HOH A . 
E 5 HOH   20 320 54  HOH   HOH A . 
E 5 HOH   21 321 23  HOH   HOH A . 
E 5 HOH   22 322 45  HOH   HOH A . 
E 5 HOH   23 323 51  HOH   HOH A . 
E 5 HOH   24 324 24  HOH   HOH A . 
E 5 HOH   25 325 40  HOH   HOH A . 
E 5 HOH   26 326 53  HOH   HOH A . 
E 5 HOH   27 327 50  HOH   HOH A . 
E 5 HOH   28 328 4   HOH   HOH A . 
E 5 HOH   29 329 11  HOH   HOH A . 
E 5 HOH   30 330 8   HOH   HOH A . 
E 5 HOH   31 331 48  HOH   HOH A . 
E 5 HOH   32 332 49  HOH   HOH A . 
E 5 HOH   33 333 19  HOH   HOH A . 
E 5 HOH   34 334 13  HOH   HOH A . 
E 5 HOH   35 335 20  HOH   HOH A . 
E 5 HOH   36 336 64  HOH   HOH A . 
E 5 HOH   37 337 46  HOH   HOH A . 
E 5 HOH   38 338 28  HOH   HOH A . 
E 5 HOH   39 339 39  HOH   HOH A . 
E 5 HOH   40 340 30  HOH   HOH A . 
E 5 HOH   41 341 10  HOH   HOH A . 
E 5 HOH   42 342 73  HOH   HOH A . 
E 5 HOH   43 343 17  HOH   HOH A . 
E 5 HOH   44 344 60  HOH   HOH A . 
E 5 HOH   45 345 21  HOH   HOH A . 
E 5 HOH   46 346 26  HOH   HOH A . 
E 5 HOH   47 347 67  HOH   HOH A . 
E 5 HOH   48 348 15  HOH   HOH A . 
E 5 HOH   49 349 5   HOH   HOH A . 
E 5 HOH   50 350 3   HOH   HOH A . 
E 5 HOH   51 351 32  HOH   HOH A . 
E 5 HOH   52 352 66  HOH   HOH A . 
E 5 HOH   53 353 65  HOH   HOH A . 
E 5 HOH   54 354 55  HOH   HOH A . 
E 5 HOH   55 355 6   HOH   HOH A . 
E 5 HOH   56 356 70  HOH   HOH A . 
E 5 HOH   57 357 56  HOH   HOH A . 
E 5 HOH   58 358 41  HOH   HOH A . 
E 5 HOH   59 359 43  HOH   HOH A . 
E 5 HOH   60 360 68  HOH   HOH A . 
E 5 HOH   61 361 31  HOH   HOH A . 
E 5 HOH   62 362 58  HOH   HOH A . 
E 5 HOH   63 363 71  HOH   HOH A . 
E 5 HOH   64 364 61  HOH   HOH A . 
E 5 HOH   65 365 52  HOH   HOH A . 
E 5 HOH   66 366 44  HOH   HOH A . 
E 5 HOH   67 367 69  HOH   HOH A . 
E 5 HOH   68 368 62  HOH   HOH A . 
E 5 HOH   69 369 72  HOH   HOH A . 
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       BUSTER  '2.10.4 (23-JAN-2024)' ? 1 
'data scaling'   Aimless .                      ? 2 
phasing          PHASER  .                      ? 3 
'data reduction' XDS     .                      ? 4 
# 
_cell.entry_id           7HY5 
_cell.length_a           73.820 
_cell.length_b           62.933 
_cell.length_c           33.252 
_cell.angle_alpha        90.00 
_cell.angle_beta         93.09 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HY5 
_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          7HY5 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.43 
_exptl_crystal.density_percent_sol   49.31 
_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   2024-12-02 
_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   0.92203 
_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        0.92203 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HY5 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             47.98 
_reflns.d_resolution_high            1.92 
_reflns.number_obs                   11748 
_reflns.percent_possible_obs         98.7 
_reflns.pdbx_Rmerge_I_obs            0.271 
_reflns.pdbx_netI_over_sigmaI        5.3 
_reflns.pdbx_redundancy              6.7 
_reflns.pdbx_Rrim_I_all              0.295 
_reflns.pdbx_Rpim_I_all              0.114 
_reflns.pdbx_CC_half                 0.987 
_reflns.pdbx_number_measured_all     78974 
_reflns.pdbx_chi_squared             0.59 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.92 
_reflns_shell.d_res_low                   1.97 
_reflns_shell.number_measured_all         4916 
_reflns_shell.number_unique_obs           703 
_reflns_shell.Rmerge_I_obs                4.335 
_reflns_shell.pdbx_chi_squared            0.22 
_reflns_shell.pdbx_redundancy             7.0 
_reflns_shell.percent_possible_obs        82.2 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.4 
_reflns_shell.pdbx_Rrim_I_all             4.697 
_reflns_shell.pdbx_Rpim_I_all             1.786 
_reflns_shell.pdbx_CC_half                0.272 
_reflns_shell.percent_possible_all        ? 
_reflns_shell.pdbx_Rsym_value             ? 
_reflns_shell.meanI_over_sigI_obs         ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 7HY5 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     11555 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             47.86 
_refine.ls_d_res_high                            1.920 
_refine.ls_percent_reflns_obs                    98.9 
_refine.ls_R_factor_obs                          0.2536 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2519 
_refine.ls_R_factor_R_free                       0.2856 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.040 
_refine.ls_number_reflns_R_free                  582 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.941 
_refine.correlation_coeff_Fo_to_Fc_free          0.905 
_refine.B_iso_mean                               42.89 
_refine.aniso_B[1][1]                            -6.81960 
_refine.aniso_B[2][2]                            4.23810 
_refine.aniso_B[3][3]                            2.58140 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -0.35460 
_refine.aniso_B[2][3]                            0.00000 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             0.199 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.174 
_refine.pdbx_overall_SU_R_Blow_DPI               0.201 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.174 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HY5 
_refine_analyze.Luzzati_coordinate_error_obs    0.35 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1074 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         21 
_refine_hist.number_atoms_solvent             69 
_refine_hist.number_atoms_total               1164 
_refine_hist.d_res_high                       1.920 
_refine_hist.d_res_low                        47.86 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
t_bond_d                  0.009 ? 2.00  1128 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               0.91  ? 2.00  1535 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  376  'X-RAY DIFFRACTION' SINUSOIDAL   
t_incorr_chiral_ct        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_pseud_angle             ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_trig_c_planes           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_gen_planes              ?     ? 5.00  204  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1125 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           3.44  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           17.15 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  138  'X-RAY DIFFRACTION' SEMIHARMONIC 
t_sum_occupancies         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_distance        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_angle           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_torsion         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_ideal_dist_contact      ?     ? 4.00  725  'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   30 
_refine_ls_shell.d_res_high                       1.92 
_refine_ls_shell.d_res_low                        1.95 
_refine_ls_shell.number_reflns_R_work             379 
_refine_ls_shell.R_factor_R_work                  0.4065 
_refine_ls_shell.percent_reflns_obs               76.64 
_refine_ls_shell.R_factor_R_free                  0.4099 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            5.01 
_refine_ls_shell.number_reflns_R_free             20 
_refine_ls_shell.number_reflns_all                399 
_refine_ls_shell.R_factor_all                     0.4066 
# 
_struct.entry_id                  7HY5 
_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-0035275-001 (A71EV2A-x4336)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HY5 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN, HYDROLASE
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    POLG_CX16G 
_struct_ref.pdbx_db_accession          Q65900 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_struct_ref.pdbx_align_begin           869 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              7HY5 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 144 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q65900 
_struct_ref_seq.db_align_beg                  869 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1012 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       7 
_struct_ref_seq.pdbx_auth_seq_align_end       150 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_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 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
HELX_P HELX_P4 AA4 LEU A 134 ? ASP A 138 ? LEU A 140 ASP A 144 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 50  SG  ? ? ? 1_555 C ZN  . ZN ? ? A CYS 56  A ZN  202 1_555 ? ? ? ? ? ? ? 2.344 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 C ZN  . ZN ? ? A CYS 58  A ZN  202 1_555 ? ? ? ? ? ? ? 2.461 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 C ZN  . ZN ? ? A CYS 116 A ZN  202 1_555 ? ? ? ? ? ? ? 2.575 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 C ZN  . ZN ? ? A HIS 118 A ZN  202 1_555 ? ? ? ? ? ? ? 2.063 ? ? 
metalc5 metalc ? ? C ZN  .   ZN  ? ? ? 1_555 E HOH . O  ? ? A ZN  202 A HOH 344 1_555 ? ? ? ? ? ? ? 2.533 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  SG  ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 52  ? A CYS 58  ? 1_555 107.0 ? 
2  SG  ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 107.5 ? 
3  SG  ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 116.8 ? 
4  SG  ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 120.9 ? 
5  SG  ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 104.4 ? 
6  SG  ? A CYS 110 ? A CYS 116 ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 100.8 ? 
7  SG  ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 O   ? E HOH .   ? A HOH 344 ? 1_555 52.3  ? 
8  SG  ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 O   ? E HOH .   ? A HOH 344 ? 1_555 158.9 ? 
9  SG  ? A CYS 110 ? A CYS 116 ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 O   ? E HOH .   ? A HOH 344 ? 1_555 78.1  ? 
10 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 O   ? E HOH .   ? A HOH 344 ? 1_555 86.2  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA1 2 LEU A 34  ? CYS A 44  ? LEU A 40  CYS A 50  
AA1 3 ILE A 4   ? ASN A 13  ? ILE A 10  ASN A 19  
AA2 1 LYS A 64  ? SER A 69  ? LYS A 70  SER A 75  
AA2 2 THR A 54  ? CYS A 59  ? THR A 60  CYS A 65  
AA2 3 ILE A 107 ? CYS A 110 ? ILE A 113 CYS A 116 
AA2 4 GLY A 113 ? GLY A 122 ? GLY A 119 GLY A 128 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N TRP A 27  ? N TRP A 33  O VAL A 36  ? O VAL A 42  
AA1 2 3 N SER A 37  ? N SER A 43  O ARG A 10  ? O ARG A 16  
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 THR A 120 ? N THR A 126 O GLY A 127 ? O GLY A 133 
AA2 5 6 O PHE A 128 ? O PHE A 134 N MET A 93  ? N MET A 99  
AA2 6 7 O ARG A 87  ? O ARG A 93  N VAL A 78  ? N VAL A 84  
# 
_pdbx_entry_details.entry_id                   7HY5 
_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   SG 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   CYS 
_pdbx_validate_close_contact.auth_seq_id_1    56 
_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   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    344 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.16 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 14  ? ? -89.78  36.20   
2 1 CYS A 116 ? ? -116.05 -168.20 
3 1 SER A 125 ? ? -141.15 -24.60  
# 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         15.2952 
_pdbx_refine_tls.origin_y         6.7158 
_pdbx_refine_tls.origin_z         14.5202 
_pdbx_refine_tls.T[1][1]          -0.0194 
_pdbx_refine_tls.T[2][2]          0.0280 
_pdbx_refine_tls.T[3][3]          -0.1185 
_pdbx_refine_tls.T[1][2]          0.0323 
_pdbx_refine_tls.T[1][3]          -0.0107 
_pdbx_refine_tls.T[2][3]          -0.0146 
_pdbx_refine_tls.L[1][1]          2.2014 
_pdbx_refine_tls.L[2][2]          10.0437 
_pdbx_refine_tls.L[3][3]          1.7876 
_pdbx_refine_tls.L[1][2]          3.1796 
_pdbx_refine_tls.L[1][3]          -0.9309 
_pdbx_refine_tls.L[2][3]          -2.9025 
_pdbx_refine_tls.S[1][1]          -0.1282 
_pdbx_refine_tls.S[1][2]          0.0940 
_pdbx_refine_tls.S[1][3]          0.0980 
_pdbx_refine_tls.S[2][1]          0.3810 
_pdbx_refine_tls.S[2][2]          0.1631 
_pdbx_refine_tls.S[2][3]          -0.2952 
_pdbx_refine_tls.S[3][1]          -0.0749 
_pdbx_refine_tls.S[3][2]          -0.1985 
_pdbx_refine_tls.S[3][3]          -0.0349 
# 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   '{ A|* }' 
# 
loop_
_pdbx_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 GLU 146 ? A GLU 140 
2 1 Y 1 A ALA 147 ? A ALA 141 
3 1 Y 1 A MET 148 ? A MET 142 
4 1 Y 1 A GLU 149 ? A GLU 143 
5 1 Y 1 A GLN 150 ? A GLN 144 
6 1 N 0 A DMS 203 ? D DMS ?   
# 
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 
A1BR0 N1   N  N N 1   
A1BR0 C4   C  N N 2   
A1BR0 C5   C  N N 3   
A1BR0 C6   C  N N 4   
A1BR0 C7   C  Y N 5   
A1BR0 C8   C  Y N 6   
A1BR0 C10  C  Y N 7   
A1BR0 C13  C  N N 8   
A1BR0 CL1  CL N N 9   
A1BR0 C12  C  Y N 10  
A1BR0 C11  C  Y N 11  
A1BR0 CL   CL N N 12  
A1BR0 C9   C  Y N 13  
A1BR0 O1   O  N N 14  
A1BR0 C3   C  N N 15  
A1BR0 C2   C  N N 16  
A1BR0 C1   C  N S 17  
A1BR0 C    C  N N 18  
A1BR0 O    O  N N 19  
A1BR0 N    N  N N 20  
A1BR0 H7   H  N N 21  
A1BR0 H8   H  N N 22  
A1BR0 H9   H  N N 23  
A1BR0 H10  H  N N 24  
A1BR0 H11  H  N N 25  
A1BR0 H13  H  N N 26  
A1BR0 H15  H  N N 27  
A1BR0 H14  H  N N 28  
A1BR0 H12  H  N N 29  
A1BR0 H6   H  N N 30  
A1BR0 H5   H  N N 31  
A1BR0 H4   H  N N 32  
A1BR0 H3   H  N N 33  
A1BR0 H    H  N N 34  
A1BR0 H1   H  N N 35  
A1BR0 H2   H  N N 36  
ALA   N    N  N N 37  
ALA   CA   C  N S 38  
ALA   C    C  N N 39  
ALA   O    O  N N 40  
ALA   CB   C  N N 41  
ALA   OXT  O  N N 42  
ALA   H    H  N N 43  
ALA   H2   H  N N 44  
ALA   HA   H  N N 45  
ALA   HB1  H  N N 46  
ALA   HB2  H  N N 47  
ALA   HB3  H  N N 48  
ALA   HXT  H  N N 49  
ARG   N    N  N N 50  
ARG   CA   C  N S 51  
ARG   C    C  N N 52  
ARG   O    O  N N 53  
ARG   CB   C  N N 54  
ARG   CG   C  N N 55  
ARG   CD   C  N N 56  
ARG   NE   N  N N 57  
ARG   CZ   C  N N 58  
ARG   NH1  N  N N 59  
ARG   NH2  N  N N 60  
ARG   OXT  O  N N 61  
ARG   H    H  N N 62  
ARG   H2   H  N N 63  
ARG   HA   H  N N 64  
ARG   HB2  H  N N 65  
ARG   HB3  H  N N 66  
ARG   HG2  H  N N 67  
ARG   HG3  H  N N 68  
ARG   HD2  H  N N 69  
ARG   HD3  H  N N 70  
ARG   HE   H  N N 71  
ARG   HH11 H  N N 72  
ARG   HH12 H  N N 73  
ARG   HH21 H  N N 74  
ARG   HH22 H  N N 75  
ARG   HXT  H  N N 76  
ASN   N    N  N N 77  
ASN   CA   C  N S 78  
ASN   C    C  N N 79  
ASN   O    O  N N 80  
ASN   CB   C  N N 81  
ASN   CG   C  N N 82  
ASN   OD1  O  N N 83  
ASN   ND2  N  N N 84  
ASN   OXT  O  N N 85  
ASN   H    H  N N 86  
ASN   H2   H  N N 87  
ASN   HA   H  N N 88  
ASN   HB2  H  N N 89  
ASN   HB3  H  N N 90  
ASN   HD21 H  N N 91  
ASN   HD22 H  N N 92  
ASN   HXT  H  N N 93  
ASP   N    N  N N 94  
ASP   CA   C  N S 95  
ASP   C    C  N N 96  
ASP   O    O  N N 97  
ASP   CB   C  N N 98  
ASP   CG   C  N N 99  
ASP   OD1  O  N N 100 
ASP   OD2  O  N N 101 
ASP   OXT  O  N N 102 
ASP   H    H  N N 103 
ASP   H2   H  N N 104 
ASP   HA   H  N N 105 
ASP   HB2  H  N N 106 
ASP   HB3  H  N N 107 
ASP   HD2  H  N N 108 
ASP   HXT  H  N N 109 
CYS   N    N  N N 110 
CYS   CA   C  N R 111 
CYS   C    C  N N 112 
CYS   O    O  N N 113 
CYS   CB   C  N N 114 
CYS   SG   S  N N 115 
CYS   OXT  O  N N 116 
CYS   H    H  N N 117 
CYS   H2   H  N N 118 
CYS   HA   H  N N 119 
CYS   HB2  H  N N 120 
CYS   HB3  H  N N 121 
CYS   HG   H  N N 122 
CYS   HXT  H  N N 123 
DMS   S    S  N N 124 
DMS   O    O  N N 125 
DMS   C1   C  N N 126 
DMS   C2   C  N N 127 
DMS   H11  H  N N 128 
DMS   H12  H  N N 129 
DMS   H13  H  N N 130 
DMS   H21  H  N N 131 
DMS   H22  H  N N 132 
DMS   H23  H  N N 133 
GLN   N    N  N N 134 
GLN   CA   C  N S 135 
GLN   C    C  N N 136 
GLN   O    O  N N 137 
GLN   CB   C  N N 138 
GLN   CG   C  N N 139 
GLN   CD   C  N N 140 
GLN   OE1  O  N N 141 
GLN   NE2  N  N N 142 
GLN   OXT  O  N N 143 
GLN   H    H  N N 144 
GLN   H2   H  N N 145 
GLN   HA   H  N N 146 
GLN   HB2  H  N N 147 
GLN   HB3  H  N N 148 
GLN   HG2  H  N N 149 
GLN   HG3  H  N N 150 
GLN   HE21 H  N N 151 
GLN   HE22 H  N N 152 
GLN   HXT  H  N N 153 
GLU   N    N  N N 154 
GLU   CA   C  N S 155 
GLU   C    C  N N 156 
GLU   O    O  N N 157 
GLU   CB   C  N N 158 
GLU   CG   C  N N 159 
GLU   CD   C  N N 160 
GLU   OE1  O  N N 161 
GLU   OE2  O  N N 162 
GLU   OXT  O  N N 163 
GLU   H    H  N N 164 
GLU   H2   H  N N 165 
GLU   HA   H  N N 166 
GLU   HB2  H  N N 167 
GLU   HB3  H  N N 168 
GLU   HG2  H  N N 169 
GLU   HG3  H  N N 170 
GLU   HE2  H  N N 171 
GLU   HXT  H  N N 172 
GLY   N    N  N N 173 
GLY   CA   C  N N 174 
GLY   C    C  N N 175 
GLY   O    O  N N 176 
GLY   OXT  O  N N 177 
GLY   H    H  N N 178 
GLY   H2   H  N N 179 
GLY   HA2  H  N N 180 
GLY   HA3  H  N N 181 
GLY   HXT  H  N N 182 
HIS   N    N  N N 183 
HIS   CA   C  N S 184 
HIS   C    C  N N 185 
HIS   O    O  N N 186 
HIS   CB   C  N N 187 
HIS   CG   C  Y N 188 
HIS   ND1  N  Y N 189 
HIS   CD2  C  Y N 190 
HIS   CE1  C  Y N 191 
HIS   NE2  N  Y N 192 
HIS   OXT  O  N N 193 
HIS   H    H  N N 194 
HIS   H2   H  N N 195 
HIS   HA   H  N N 196 
HIS   HB2  H  N N 197 
HIS   HB3  H  N N 198 
HIS   HD1  H  N N 199 
HIS   HD2  H  N N 200 
HIS   HE1  H  N N 201 
HIS   HE2  H  N N 202 
HIS   HXT  H  N N 203 
HOH   O    O  N N 204 
HOH   H1   H  N N 205 
HOH   H2   H  N N 206 
ILE   N    N  N N 207 
ILE   CA   C  N S 208 
ILE   C    C  N N 209 
ILE   O    O  N N 210 
ILE   CB   C  N S 211 
ILE   CG1  C  N N 212 
ILE   CG2  C  N N 213 
ILE   CD1  C  N N 214 
ILE   OXT  O  N N 215 
ILE   H    H  N N 216 
ILE   H2   H  N N 217 
ILE   HA   H  N N 218 
ILE   HB   H  N N 219 
ILE   HG12 H  N N 220 
ILE   HG13 H  N N 221 
ILE   HG21 H  N N 222 
ILE   HG22 H  N N 223 
ILE   HG23 H  N N 224 
ILE   HD11 H  N N 225 
ILE   HD12 H  N N 226 
ILE   HD13 H  N N 227 
ILE   HXT  H  N N 228 
LEU   N    N  N N 229 
LEU   CA   C  N S 230 
LEU   C    C  N N 231 
LEU   O    O  N N 232 
LEU   CB   C  N N 233 
LEU   CG   C  N N 234 
LEU   CD1  C  N N 235 
LEU   CD2  C  N N 236 
LEU   OXT  O  N N 237 
LEU   H    H  N N 238 
LEU   H2   H  N N 239 
LEU   HA   H  N N 240 
LEU   HB2  H  N N 241 
LEU   HB3  H  N N 242 
LEU   HG   H  N N 243 
LEU   HD11 H  N N 244 
LEU   HD12 H  N N 245 
LEU   HD13 H  N N 246 
LEU   HD21 H  N N 247 
LEU   HD22 H  N N 248 
LEU   HD23 H  N N 249 
LEU   HXT  H  N N 250 
LYS   N    N  N N 251 
LYS   CA   C  N S 252 
LYS   C    C  N N 253 
LYS   O    O  N N 254 
LYS   CB   C  N N 255 
LYS   CG   C  N N 256 
LYS   CD   C  N N 257 
LYS   CE   C  N N 258 
LYS   NZ   N  N N 259 
LYS   OXT  O  N N 260 
LYS   H    H  N N 261 
LYS   H2   H  N N 262 
LYS   HA   H  N N 263 
LYS   HB2  H  N N 264 
LYS   HB3  H  N N 265 
LYS   HG2  H  N N 266 
LYS   HG3  H  N N 267 
LYS   HD2  H  N N 268 
LYS   HD3  H  N N 269 
LYS   HE2  H  N N 270 
LYS   HE3  H  N N 271 
LYS   HZ1  H  N N 272 
LYS   HZ2  H  N N 273 
LYS   HZ3  H  N N 274 
LYS   HXT  H  N N 275 
MET   N    N  N N 276 
MET   CA   C  N S 277 
MET   C    C  N N 278 
MET   O    O  N N 279 
MET   CB   C  N N 280 
MET   CG   C  N N 281 
MET   SD   S  N N 282 
MET   CE   C  N N 283 
MET   OXT  O  N N 284 
MET   H    H  N N 285 
MET   H2   H  N N 286 
MET   HA   H  N N 287 
MET   HB2  H  N N 288 
MET   HB3  H  N N 289 
MET   HG2  H  N N 290 
MET   HG3  H  N N 291 
MET   HE1  H  N N 292 
MET   HE2  H  N N 293 
MET   HE3  H  N N 294 
MET   HXT  H  N N 295 
PHE   N    N  N N 296 
PHE   CA   C  N S 297 
PHE   C    C  N N 298 
PHE   O    O  N N 299 
PHE   CB   C  N N 300 
PHE   CG   C  Y N 301 
PHE   CD1  C  Y N 302 
PHE   CD2  C  Y N 303 
PHE   CE1  C  Y N 304 
PHE   CE2  C  Y N 305 
PHE   CZ   C  Y N 306 
PHE   OXT  O  N N 307 
PHE   H    H  N N 308 
PHE   H2   H  N N 309 
PHE   HA   H  N N 310 
PHE   HB2  H  N N 311 
PHE   HB3  H  N N 312 
PHE   HD1  H  N N 313 
PHE   HD2  H  N N 314 
PHE   HE1  H  N N 315 
PHE   HE2  H  N N 316 
PHE   HZ   H  N N 317 
PHE   HXT  H  N N 318 
PRO   N    N  N N 319 
PRO   CA   C  N S 320 
PRO   C    C  N N 321 
PRO   O    O  N N 322 
PRO   CB   C  N N 323 
PRO   CG   C  N N 324 
PRO   CD   C  N N 325 
PRO   OXT  O  N N 326 
PRO   H    H  N N 327 
PRO   HA   H  N N 328 
PRO   HB2  H  N N 329 
PRO   HB3  H  N N 330 
PRO   HG2  H  N N 331 
PRO   HG3  H  N N 332 
PRO   HD2  H  N N 333 
PRO   HD3  H  N N 334 
PRO   HXT  H  N N 335 
SER   N    N  N N 336 
SER   CA   C  N S 337 
SER   C    C  N N 338 
SER   O    O  N N 339 
SER   CB   C  N N 340 
SER   OG   O  N N 341 
SER   OXT  O  N N 342 
SER   H    H  N N 343 
SER   H2   H  N N 344 
SER   HA   H  N N 345 
SER   HB2  H  N N 346 
SER   HB3  H  N N 347 
SER   HG   H  N N 348 
SER   HXT  H  N N 349 
THR   N    N  N N 350 
THR   CA   C  N S 351 
THR   C    C  N N 352 
THR   O    O  N N 353 
THR   CB   C  N R 354 
THR   OG1  O  N N 355 
THR   CG2  C  N N 356 
THR   OXT  O  N N 357 
THR   H    H  N N 358 
THR   H2   H  N N 359 
THR   HA   H  N N 360 
THR   HB   H  N N 361 
THR   HG1  H  N N 362 
THR   HG21 H  N N 363 
THR   HG22 H  N N 364 
THR   HG23 H  N N 365 
THR   HXT  H  N N 366 
TRP   N    N  N N 367 
TRP   CA   C  N S 368 
TRP   C    C  N N 369 
TRP   O    O  N N 370 
TRP   CB   C  N N 371 
TRP   CG   C  Y N 372 
TRP   CD1  C  Y N 373 
TRP   CD2  C  Y N 374 
TRP   NE1  N  Y N 375 
TRP   CE2  C  Y N 376 
TRP   CE3  C  Y N 377 
TRP   CZ2  C  Y N 378 
TRP   CZ3  C  Y N 379 
TRP   CH2  C  Y N 380 
TRP   OXT  O  N N 381 
TRP   H    H  N N 382 
TRP   H2   H  N N 383 
TRP   HA   H  N N 384 
TRP   HB2  H  N N 385 
TRP   HB3  H  N N 386 
TRP   HD1  H  N N 387 
TRP   HE1  H  N N 388 
TRP   HE3  H  N N 389 
TRP   HZ2  H  N N 390 
TRP   HZ3  H  N N 391 
TRP   HH2  H  N N 392 
TRP   HXT  H  N N 393 
TYR   N    N  N N 394 
TYR   CA   C  N S 395 
TYR   C    C  N N 396 
TYR   O    O  N N 397 
TYR   CB   C  N N 398 
TYR   CG   C  Y N 399 
TYR   CD1  C  Y N 400 
TYR   CD2  C  Y N 401 
TYR   CE1  C  Y N 402 
TYR   CE2  C  Y N 403 
TYR   CZ   C  Y N 404 
TYR   OH   O  N N 405 
TYR   OXT  O  N N 406 
TYR   H    H  N N 407 
TYR   H2   H  N N 408 
TYR   HA   H  N N 409 
TYR   HB2  H  N N 410 
TYR   HB3  H  N N 411 
TYR   HD1  H  N N 412 
TYR   HD2  H  N N 413 
TYR   HE1  H  N N 414 
TYR   HE2  H  N N 415 
TYR   HH   H  N N 416 
TYR   HXT  H  N N 417 
VAL   N    N  N N 418 
VAL   CA   C  N S 419 
VAL   C    C  N N 420 
VAL   O    O  N N 421 
VAL   CB   C  N N 422 
VAL   CG1  C  N N 423 
VAL   CG2  C  N N 424 
VAL   OXT  O  N N 425 
VAL   H    H  N N 426 
VAL   H2   H  N N 427 
VAL   HA   H  N N 428 
VAL   HB   H  N N 429 
VAL   HG11 H  N N 430 
VAL   HG12 H  N N 431 
VAL   HG13 H  N N 432 
VAL   HG21 H  N N 433 
VAL   HG22 H  N N 434 
VAL   HG23 H  N N 435 
VAL   HXT  H  N N 436 
ZN    ZN   ZN N N 437 
# 
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 
A1BR0 N   C    sing N N 1   
A1BR0 O   C    doub N N 2   
A1BR0 C   C1   sing N N 3   
A1BR0 C1  C2   sing N N 4   
A1BR0 C2  C3   sing N N 5   
A1BR0 C3  C4   sing N N 6   
A1BR0 C4  N1   sing N N 7   
A1BR0 N1  C5   sing N N 8   
A1BR0 O1  C5   doub N N 9   
A1BR0 C5  C6   sing N N 10  
A1BR0 C6  C7   sing N N 11  
A1BR0 C7  C8   doub Y N 12  
A1BR0 C8  C9   sing Y N 13  
A1BR0 C9  C10  doub Y N 14  
A1BR0 C10 C11  sing Y N 15  
A1BR0 CL  C11  sing N N 16  
A1BR0 C11 C12  doub Y N 17  
A1BR0 C7  C12  sing Y N 18  
A1BR0 C12 CL1  sing N N 19  
A1BR0 C13 N1   sing N N 20  
A1BR0 C1  C13  sing N N 21  
A1BR0 C4  H7   sing N N 22  
A1BR0 C4  H8   sing N N 23  
A1BR0 C6  H9   sing N N 24  
A1BR0 C6  H10  sing N N 25  
A1BR0 C8  H11  sing N N 26  
A1BR0 C10 H13  sing N N 27  
A1BR0 C13 H15  sing N N 28  
A1BR0 C13 H14  sing N N 29  
A1BR0 C9  H12  sing N N 30  
A1BR0 C3  H6   sing N N 31  
A1BR0 C3  H5   sing N N 32  
A1BR0 C2  H4   sing N N 33  
A1BR0 C2  H3   sing N N 34  
A1BR0 C1  H    sing N N 35  
A1BR0 N   H1   sing N N 36  
A1BR0 N   H2   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_1002329 
_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.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8POA 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    7HY5 
_atom_sites.fract_transf_matrix[1][1]   0.013546 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000731 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.015890 
_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]   0.030117 
_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  
CL 
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   ? 19.129 6.195   24.842 1.00 49.20 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 20.316 6.280   23.978 1.00 49.44 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 20.370 5.164   22.902 1.00 47.91 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 19.659 4.165   23.015 1.00 47.57 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 21.586 6.283   24.825 1.00 51.30 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 21.570 5.212   25.755 1.00 54.24 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 21.183 5.366   21.860 1.00 46.75 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 21.330 4.390   20.778 1.00 45.92 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 21.647 4.968   19.406 1.00 44.38 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 21.317 6.132   19.126 1.00 44.37 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 22.288 4.147   18.535 1.00 42.65 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 22.690 4.553   17.181 1.00 42.25 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 22.779 3.390   16.144 1.00 42.09 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 22.850 2.212   16.524 1.00 41.61 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 24.030 5.279   17.257 1.00 42.33 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 22.788 3.727   14.829 1.00 42.02 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.954 2.748   13.751 1.00 42.61 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 24.354 2.939   13.161 1.00 44.23 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.754 4.065   12.847 1.00 43.92 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.895 2.900   12.630 1.00 42.42 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 20.468 3.048   13.187 1.00 42.29 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 22.003 1.760   11.612 1.00 42.91 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.484 3.457   12.139 1.00 43.02 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 25.095 1.848   13.005 1.00 45.38 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 26.443 1.903   12.453 1.00 46.90 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 26.512 1.104   11.160 1.00 48.36 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 26.604 -0.127  11.211 1.00 48.75 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.450 1.346   13.473 1.00 47.04 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.597 2.221   14.697 1.00 47.45 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 28.390 3.363   14.671 1.00 48.16 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 26.938 1.914   15.878 1.00 48.02 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 28.525 4.172   15.790 1.00 48.53 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 27.065 2.718   17.004 1.00 48.82 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 27.862 3.846   16.955 1.00 49.54 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 28.012 4.624   18.072 1.00 51.21 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 26.445 1.795   10.007 1.00 48.77 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 26.504 1.172   8.684  1.00 49.65 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.635 1.786   7.881  1.00 50.54 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.624 2.986   7.598  1.00 50.65 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 25.157 1.203   7.918  1.00 50.28 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.582 2.620   7.826  1.00 50.55 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 25.306 0.580   6.539  1.00 50.74 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.647 0.972   7.573  1.00 50.59 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.823 1.422   6.850  1.00 51.51 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.551 2.490   7.636  1.00 52.37 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.589 2.421   8.872  1.00 53.12 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 31.001 3.543   6.959  1.00 51.99 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.669 4.643   7.649  1.00 52.02 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.679 5.738   8.111  1.00 50.29 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 31.026 6.923   8.122  1.00 50.41 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.812 5.198   6.812  1.00 54.29 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.903 4.168   6.606  1.00 60.47 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.194 3.363   7.497  1.00 63.58 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 34.519 4.151   5.429  1.00 61.00 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.474 5.329   8.534  1.00 48.40 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.447 6.262   9.006  1.00 47.02 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.875 5.863   10.365 1.00 44.98 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.808 4.679   10.699 1.00 44.98 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 27.288 6.384   7.998  1.00 46.96 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.669 6.979   6.661  1.00 47.70 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 28.283 8.220   6.581  1.00 48.80 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.359 6.329   5.476  1.00 48.58 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.615 8.784   5.355  1.00 50.07 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.670 6.888   4.244  1.00 49.93 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 28.307 8.114   4.186  1.00 51.44 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.635 8.670   2.968  1.00 53.78 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.440 6.868   11.129 1.00 42.88 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.791 6.722   12.428 1.00 41.36 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.474 7.524   12.362 1.00 39.65 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.495 8.725   12.076 1.00 39.61 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.707 7.253   13.557 1.00 42.20 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 27.021 7.422   14.922 1.00 44.10 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 28.009 7.780   16.019 1.00 46.10 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 27.513 8.818   16.930 1.00 47.62 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 27.058 8.585   18.158 1.00 49.25 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 26.999 7.344   18.630 1.00 49.31 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 26.631 9.588   18.915 1.00 48.55 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 24.335 6.869   12.597 1.00 37.93 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 23.036 7.542   12.561 1.00 36.91 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.495 7.674   13.974 1.00 35.78 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 22.309 6.667   14.645 1.00 36.24 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 22.004 6.819   11.659 1.00 37.55 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.789 7.712   11.412 1.00 37.74 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.625 6.366   10.339 1.00 37.93 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 22.204 8.895   14.421 1.00 34.22 ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 21.673 9.144   15.767 1.00 33.39 ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 20.473 10.102  15.707 1.00 32.34 ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 20.270 10.767  14.686 1.00 31.40 ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 22.767 9.757   16.693 1.00 33.77 ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 23.755 8.712   17.151 1.00 34.75 ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 23.465 10.944  16.034 1.00 34.06 ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 19.714 10.229  16.831 1.00 31.84 ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 18.649 11.227  16.974 1.00 32.11 ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 19.356 12.586  16.939 1.00 32.85 ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 20.372 12.753  17.611 1.00 33.55 ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.919 11.088  18.329 1.00 32.87 ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 17.271 9.738   18.590 1.00 34.43 ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.869 8.841   19.210 1.00 35.30 ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 16.045 9.563   18.145 1.00 33.44 ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 18.881 13.529  16.120 1.00 32.96 ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 19.517 14.844  16.007 1.00 33.07 ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 19.565 15.567  17.352 1.00 34.64 ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 20.562 16.236  17.638 1.00 35.15 ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 18.829 15.729  14.946 1.00 32.10 ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.596 17.015  14.570 1.00 31.79 ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 18.688 17.982  13.832 1.00 32.09 ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.337 19.200  13.313 1.00 32.15 ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.454 20.340  13.992 1.00 32.48 ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 19.045 20.415  15.253 1.00 31.20 ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 19.982 21.412  13.416 1.00 31.83 ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 18.528 15.407  18.200 1.00 35.42 ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 18.512 16.112  19.494 1.00 36.69 ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 19.470 15.516  20.548 1.00 38.34 ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 19.701 16.144  21.575 1.00 38.16 ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 17.090 16.268  20.055 1.00 37.12 ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 16.476 15.004  20.566 1.00 38.22 ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 15.912 14.082  19.708 1.00 38.99 ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 16.338 14.560  21.839 1.00 39.12 ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 15.456 13.102  20.472 1.00 39.75 ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 15.693 13.338  21.764 1.00 39.93 ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 20.079 14.358  20.259 1.00 39.44 ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 21.034 13.723  21.157 1.00 40.77 ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 22.474 13.698  20.592 1.00 42.80 ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 23.326 13.012  21.157 1.00 43.40 ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 20.581 12.274  21.439 1.00 40.72 ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 19.252 12.091  22.183 1.00 42.01 ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 18.918 10.598  22.351 1.00 42.11 ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 19.273 12.812  23.546 1.00 42.46 ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 22.746 14.404  19.483 1.00 43.88 ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 24.060 14.414  18.835 1.00 45.41 ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 25.169 15.020  19.707 1.00 46.72 ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 24.918 16.000  20.401 1.00 46.76 ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 23.974 15.150  17.502 1.00 45.67 ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 26.391 14.415  19.683 1.00 47.67 ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 27.565 14.862  20.457 1.00 49.04 ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 28.407 15.944  19.710 1.00 50.08 ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 28.100 16.277  18.564 1.00 50.11 ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 28.442 13.645  20.841 1.00 50.59 ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 29.091 13.143  19.671 1.00 51.30 ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 27.674 12.564  21.566 1.00 51.25 ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 29.451 16.509  20.368 1.00 50.82 ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 30.346 17.480  19.751 1.00 51.70 ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 31.062 16.846  18.566 1.00 51.06 ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 31.231 17.506  17.542 1.00 50.96 ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 31.387 17.969  20.761 1.00 54.24 ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 30.893 19.047  21.660 1.00 58.83 ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 30.254 20.160  21.158 1.00 61.58 ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 30.996 19.167  23.005 1.00 61.03 ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 29.979 20.922  22.205 1.00 62.46 ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 30.412 20.370  23.339 1.00 62.46 ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 31.473 15.567  18.698 1.00 50.25 ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 32.149 14.840  17.622 1.00 50.36 ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 31.279 14.685  16.388 1.00 48.89 ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 31.747 15.004  15.292 1.00 49.29 ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 32.685 13.485  18.086 1.00 52.83 ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 33.834 13.007  17.229 1.00 58.12 ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.741 13.776  16.899 1.00 60.25 ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 33.817 11.737  16.833 1.00 59.30 ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 30.004 14.257  16.562 1.00 47.03 ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 29.012 14.139  15.479 1.00 45.50 ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 28.892 15.457  14.681 1.00 44.33 ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 28.859 15.428  13.456 1.00 44.17 ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 27.623 13.754  16.042 1.00 45.67 ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 27.533 12.353  16.619 1.00 47.71 ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 28.122 11.431  16.028 1.00 47.42 ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 26.872 12.184  17.664 1.00 49.25 ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 28.841 16.603  15.369 1.00 43.46 ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.754 17.911  14.700 1.00 43.37 ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 30.060 18.332  13.986 1.00 43.82 ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 30.011 19.062  13.006 1.00 44.00 ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 28.274 19.006  15.678 1.00 42.51 ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 26.782 19.069  15.796 1.00 41.80 ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 26.012 18.503  16.770 1.00 42.28 ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 25.872 19.611  14.829 1.00 41.49 ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 24.679 18.705  16.495 1.00 42.37 ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 24.566 19.382  15.307 1.00 42.03 ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 26.035 20.287  13.614 1.00 41.69 ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 23.436 19.831  14.625 1.00 42.07 ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.910 20.701  12.928 1.00 42.18 ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 23.631 20.472  13.433 1.00 42.02 ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 31.209 17.867  14.469 1.00 44.15 ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.515 18.171  13.870 1.00 45.33 ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.867 17.232  12.678 1.00 46.36 ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.852 17.482  11.969 1.00 46.96 ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 33.612 18.090  14.935 1.00 45.09 ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 32.105 16.125  12.507 1.00 45.71 ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 32.269 15.153  11.420 1.00 44.64 ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.902 14.910  10.730 1.00 42.34 ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.567 13.779  10.374 1.00 41.42 ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.870 13.857  11.959 1.00 46.88 ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 34.354 13.949  12.248 1.00 51.88 ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 35.146 14.460  11.438 1.00 54.15 ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 34.765 13.457  13.409 1.00 51.86 ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 30.102 15.998  10.594 1.00 40.72 ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.762 16.035  10.036 1.00 39.22 ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.724 15.654  8.575  1.00 38.77 ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.465 16.228  7.796  1.00 39.04 ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 28.209 17.467  10.186 1.00 38.85 ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.814 17.757  9.573  1.00 38.96 ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.713 17.004  10.318 1.00 38.96 ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.517 19.252  9.561  1.00 38.64 ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.812 14.738  8.185  1.00 37.92 ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.591 14.384  6.787  1.00 37.15 ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 26.245 15.018  6.323  1.00 35.70 ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 26.197 15.733  5.322  1.00 36.41 ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.603 12.855  6.563  1.00 38.14 ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 27.152 12.515  5.150  1.00 38.76 ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 28.981 12.266  6.847  1.00 38.45 ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 25.178 14.808  7.095  1.00 33.95 ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 23.821 15.291  6.795  1.00 32.11 ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 22.980 15.388  8.085  1.00 30.53 ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 23.151 14.586  8.986  1.00 30.14 ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 23.151 14.317  5.791  1.00 31.59 ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.674 14.498  5.580  1.00 31.80 ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 21.058 15.492  4.875  1.00 32.59 ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.624 13.699  6.148  1.00 31.49 ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.691 15.340  4.942  1.00 32.79 ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.398 14.255  5.726  1.00 32.17 ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.601 12.597  7.014  1.00 31.30 ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 18.168 13.696  6.075  1.00 32.66 ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.383 12.041  7.353  1.00 31.79 ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 18.183 12.601  6.905  1.00 32.01 ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 22.063 16.360  8.163  1.00 29.34 ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 21.164 16.501  9.303  1.00 28.83 ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 19.800 17.103  8.842  1.00 28.65 ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 19.762 17.886  7.889  1.00 28.33 ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 21.812 17.324  10.444 1.00 29.58 ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.389 18.671  10.013 1.00 29.48 ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.444 19.861  9.911  1.00 33.00 ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 21.740 20.784  9.115  1.00 36.23 ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 20.407 19.873  10.612 1.00 31.15 ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 18.695 16.717  9.504  1.00 28.33 ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.348 17.216  9.195  1.00 28.12 ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.505 17.349  10.486 1.00 27.09 ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 16.051 16.337  11.028 1.00 26.79 ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.660 16.304  8.151  1.00 30.61 ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.378 16.830  7.525  1.00 36.38 ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 14.735 17.704  8.125  1.00 36.66 ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 15.008 16.346  6.442  1.00 40.74 ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.275 18.608  10.951 1.00 26.32 ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 15.478 18.927  12.145 0.50 26.59 ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 15.504 18.836  12.169 0.50 26.64 ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 14.053 18.380  12.047 1.00 27.00 ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 13.478 17.979  13.050 1.00 26.81 ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 15.389 20.440  12.348 0.50 27.17 ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 15.572 20.298  12.595 0.50 27.40 ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 16.620 21.048  12.695 0.50 28.43 ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 15.083 21.109  11.543 0.50 28.78 ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 13.456 18.425  10.834 1.00 27.37 ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 12.077 17.946  10.646 1.00 28.04 ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 11.945 16.419  10.757 1.00 27.69 ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 10.840 15.933  10.945 1.00 28.22 ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 11.479 18.457  9.337  1.00 30.87 ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 12.064 17.826  8.210  1.00 34.75 ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 13.053 15.669  10.637 1.00 26.53 ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 13.065 14.207  10.780 1.00 25.97 ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 13.695 13.737  12.105 1.00 26.40 ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 13.592 12.555  12.412 1.00 25.94 ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 13.845 13.546  9.619  1.00 25.55 ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 13.222 13.758  8.255  1.00 26.26 ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 13.998 13.081  7.142  1.00 28.72 ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 13.990 11.619  7.244  1.00 30.47 ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 14.135 10.794  6.204  1.00 32.73 ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 14.286 11.280  4.977  1.00 32.39 ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 14.120 9.479   6.383  1.00 31.89 ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 14.408 14.642  12.845 1.00 27.05 ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 15.141 14.379  14.094 1.00 26.91 ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 16.303 13.409  13.795 1.00 27.99 ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 16.564 12.502  14.587 1.00 27.68 ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 14.206 13.820  15.205 1.00 27.29 ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 14.850 13.600  16.570 1.00 30.20 ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 15.661 14.450  16.992 1.00 28.85 ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 14.551 12.566  17.207 1.00 33.81 ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 16.984 13.576  12.641 1.00 28.34 ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 18.121 12.719  12.293 1.00 28.91 ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 19.423 13.531  12.090 1.00 29.48 ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 19.402 14.709  11.729 1.00 29.95 ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.845 11.913  11.005 1.00 29.35 ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 16.818 10.772  11.034 1.00 30.96 ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 16.735 10.123  9.644  1.00 31.45 ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 17.191 9.702   12.076 1.00 30.72 ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 20.550 12.885  12.335 1.00 29.41 ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 21.874 13.442  12.086 1.00 30.56 ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 22.783 12.240  11.751 1.00 31.85 ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 22.695 11.201  12.406 1.00 31.92 ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 22.413 14.271  13.291 1.00 30.58 ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 23.726 15.028  13.054 1.00 31.83 ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 23.729 16.355  13.759 1.00 32.30 ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 24.907 14.229  13.524 1.00 32.49 ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 23.589 12.357  10.693 1.00 33.06 ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 24.518 11.315  10.259 1.00 35.27 ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 25.944 11.860  10.323 1.00 37.74 ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 26.221 12.908  9.739  1.00 37.44 ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 24.186 10.772  8.846  1.00 35.68 ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 25.294 9.848   8.339  1.00 36.31 ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 22.835 10.054  8.841  1.00 36.01 ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 26.841 11.161  11.027 1.00 39.78 ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 28.235 11.594  11.119 1.00 42.82 ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 29.202 10.503  10.611 1.00 46.16 ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 28.846 9.321   10.587 1.00 45.67 ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 28.575 12.012  12.548 1.00 43.79 ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 28.350 10.958  13.473 1.00 45.53 ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 30.424 10.902  10.216 1.00 49.00 ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 31.438 9.978   9.697  1.00 52.76 ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 32.200 9.238   10.799 1.00 56.30 ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 32.301 9.738   11.914 1.00 56.58 ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 32.410 10.714  8.783  1.00 54.46 ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 32.908 11.875  9.424  1.00 56.79 ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 32.693 8.027   10.510 1.00 59.35 ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 33.432 7.231   11.501 1.00 62.79 ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 34.736 6.695   10.928 1.00 66.72 ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 34.834 6.475   9.722  1.00 67.75 ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 32.586 6.065   12.061 1.00 64.11 ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 32.484 5.020   11.097 1.00 65.49 ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 31.198 6.494   12.522 1.00 64.29 ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? 35.727 6.442   11.790 1.00 68.77 ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? 37.004 5.906   11.343 1.00 71.14 ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? 36.944 4.384   11.137 1.00 72.56 ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? 37.686 3.848   10.311 1.00 73.64 ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? 38.113 6.287   12.333 1.00 73.63 ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? 37.740 5.829   13.635 1.00 75.57 ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? 38.380 7.787   12.369 1.00 73.82 ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? 36.096 3.686   11.910 1.00 72.07 ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? 35.959 2.244   11.814 1.00 71.96 ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 34.691 1.859   11.067 1.00 71.38 ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 33.674 2.554   11.144 1.00 71.06 ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? 35.952 1.628   13.200 1.00 72.27 ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 34.770 0.756   10.330 1.00 71.35 ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 33.679 0.191   9.533  1.00 72.06 ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 32.557 -0.391  10.425 1.00 71.53 ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 32.837 -1.077  11.406 1.00 72.05 ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 34.262 -0.884  8.575  1.00 74.65 ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 33.250 -1.784  7.866  1.00 79.53 ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 32.623 -1.149  6.643  1.00 85.67 ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 33.013 -0.058  6.184  1.00 87.59 ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 31.631 -1.834  6.084  1.00 86.28 ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 31.306 -0.090  10.082 1.00 70.28 ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 30.127 -0.588  10.783 1.00 69.49 ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 29.503 -1.763  10.053 1.00 68.21 ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 29.680 -1.899  8.839  1.00 68.24 ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 28.752 -2.611  10.769 1.00 67.13 ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 28.190 -3.802  10.126 1.00 66.76 ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 26.694 -4.042  10.385 1.00 63.81 ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 26.267 -5.200  10.458 1.00 64.27 ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 29.021 -5.041  10.450 1.00 69.61 ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 29.548 -5.169  12.182 1.00 78.08 ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 25.888 -2.963  10.418 1.00 60.43 ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 24.435 -3.077  10.529 1.00 57.77 ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 23.881 -3.093  9.095  1.00 54.81 ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 24.282 -2.264  8.278  1.00 54.42 ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 23.833 -1.850  11.259 1.00 59.06 ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 23.714 -1.958  12.764 1.00 62.47 ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 23.282 -3.022  13.248 1.00 63.65 ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 24.021 -0.960  13.458 1.00 63.54 ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 22.950 -3.993  8.793  1.00 52.70 ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 22.309 -4.036  7.480  1.00 51.83 ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 21.051 -3.140  7.500  1.00 49.86 ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 20.197 -3.302  8.374  1.00 49.84 ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 21.921 -5.490  7.130  1.00 54.44 ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 23.111 -6.233  6.844  1.00 56.53 ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 20.970 -5.576  5.930  1.00 54.69 ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 20.928 -2.217  6.543  1.00 47.85 ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 19.748 -1.365  6.451  1.00 46.48 ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 18.731 -2.076  5.578  1.00 45.83 ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 19.097 -2.664  4.551  1.00 46.35 ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 20.093 0.025   5.882  1.00 46.24 ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 21.186 0.702   6.721  1.00 46.71 ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 18.836 0.897   5.753  1.00 46.32 ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 20.779 1.027   8.157  1.00 47.52 ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 17.464 -2.052  5.983  1.00 44.39 ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 16.421 -2.726  5.224  1.00 43.88 ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 15.857 -1.844  4.087  1.00 43.34 ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 15.777 -0.630  4.231  1.00 43.02 ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 15.326 -3.155  6.162  1.00 43.24 ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 15.481 -2.457  2.960  1.00 43.28 ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 14.894 -1.760  1.808  1.00 43.41 ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 13.563 -2.472  1.481  1.00 43.88 ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 13.548 -3.437  0.699  1.00 45.30 ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 15.853 -1.798  0.610  1.00 44.32 ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 17.251 -1.190  0.849  1.00 44.61 ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 17.249 0.249   1.353  1.00 45.47 ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 18.617 0.730   1.587  1.00 44.48 ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 18.923 1.850   2.233  1.00 42.55 ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 17.966 2.628   2.716  1.00 39.99 ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 20.192 2.199   2.405  1.00 40.99 ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 12.451 -2.010  2.095  1.00 42.26 ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 11.144 -2.667  1.989  1.00 41.73 ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 10.001 -1.694  2.352  1.00 42.20 ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 10.242 -0.534  2.671  1.00 41.35 ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 11.138 -3.843  2.963  1.00 41.57 ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 11.101 -3.327  4.721  1.00 43.80 ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 8.762  -2.239  2.463  1.00 43.11 ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 7.602  -1.509  2.957  1.00 44.11 ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 6.894  -2.328  4.074  1.00 43.58 ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 5.669  -2.299  4.172  1.00 44.46 ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 6.663  -1.056  1.810  1.00 47.50 ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 5.669  -2.067  1.265  1.00 56.23 ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 5.938  -3.293  1.365  1.00 58.22 ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 4.612  -1.638  0.751  1.00 59.91 ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 7.674  -3.079  4.901  1.00 41.82 ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 7.158  -3.905  6.012  1.00 39.64 ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 6.402  -3.006  6.997  1.00 37.22 ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 6.841  -1.892  7.259  1.00 37.10 ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 8.292  -4.644  6.731  1.00 39.55 ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 8.833  -6.201  5.958  1.00 38.68 ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 5.276  -3.470  7.512  1.00 35.63 ? 59  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 53  ? 4.526  -2.724  8.522  1.00 35.04 ? 59  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 53  ? 4.423  -3.485  9.857  1.00 33.63 ? 59  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 53  ? 3.518  -3.189  10.631 1.00 33.27 ? 59  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 53  ? 3.128  -2.303  8.037  1.00 36.21 ? 59  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 53  ? 3.060  -1.019  7.213  1.00 39.67 ? 59  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 53  ? 1.616  -0.728  6.829  1.00 43.37 ? 59  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 53  ? 1.205  -0.846  5.664  1.00 45.86 ? 59  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 53  ? 0.800  -0.360  7.810  1.00 42.80 ? 59  GLN   A NE2 1 
ATOM   415  N  N   . THR   A 1 54  ? 5.315  -4.495  10.096 1.00 32.65 ? 60  THR   A N   1 
ATOM   416  C  CA  . THR   A 1 54  ? 5.473  -5.268  11.338 1.00 32.27 ? 60  THR   A CA  1 
ATOM   417  C  C   . THR   A 1 54  ? 6.983  -5.496  11.585 1.00 31.43 ? 60  THR   A C   1 
ATOM   418  O  O   . THR   A 1 54  ? 7.748  -5.686  10.627 1.00 31.19 ? 60  THR   A O   1 
ATOM   419  C  CB  . THR   A 1 54  ? 4.754  -6.646  11.331 1.00 34.21 ? 60  THR   A CB  1 
ATOM   420  O  OG1 . THR   A 1 54  ? 5.464  -7.577  10.505 1.00 34.69 ? 60  THR   A OG1 1 
ATOM   421  C  CG2 . THR   A 1 54  ? 3.289  -6.569  10.917 1.00 35.50 ? 60  THR   A CG2 1 
ATOM   422  N  N   . GLY   A 1 55  ? 7.371  -5.534  12.857 1.00 29.97 ? 61  GLY   A N   1 
ATOM   423  C  CA  . GLY   A 1 55  ? 8.754  -5.732  13.268 1.00 29.94 ? 61  GLY   A CA  1 
ATOM   424  C  C   . GLY   A 1 55  ? 8.916  -5.906  14.772 1.00 29.35 ? 61  GLY   A C   1 
ATOM   425  O  O   . GLY   A 1 55  ? 7.939  -6.215  15.450 1.00 29.52 ? 61  GLY   A O   1 
ATOM   426  N  N   . VAL   A 1 56  ? 10.163 -5.738  15.295 1.00 28.77 ? 62  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 56  ? 10.553 -5.878  16.713 1.00 29.19 ? 62  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 56  ? 11.445 -4.697  17.128 1.00 29.06 ? 62  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 56  ? 12.402 -4.385  16.422 1.00 29.31 ? 62  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 56  ? 11.297 -7.227  16.949 1.00 30.50 ? 62  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 56  ? 11.867 -7.323  18.365 1.00 31.25 ? 62  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 56  ? 10.388 -8.418  16.660 1.00 31.52 ? 62  VAL   A CG2 1 
ATOM   433  N  N   . TYR   A 1 57  ? 11.137 -4.033  18.249 1.00 29.09 ? 63  TYR   A N   1 
ATOM   434  C  CA  . TYR   A 1 57  ? 11.973 -2.929  18.738 1.00 29.32 ? 63  TYR   A CA  1 
ATOM   435  C  C   . TYR   A 1 57  ? 12.531 -3.182  20.167 1.00 28.93 ? 63  TYR   A C   1 
ATOM   436  O  O   . TYR   A 1 57  ? 11.927 -3.912  20.942 1.00 28.91 ? 63  TYR   A O   1 
ATOM   437  C  CB  . TYR   A 1 57  ? 11.240 -1.571  18.633 1.00 29.37 ? 63  TYR   A CB  1 
ATOM   438  C  CG  . TYR   A 1 57  ? 10.289 -1.271  19.770 1.00 31.00 ? 63  TYR   A CG  1 
ATOM   439  C  CD1 . TYR   A 1 57  ? 9.051  -1.897  19.852 1.00 31.99 ? 63  TYR   A CD1 1 
ATOM   440  C  CD2 . TYR   A 1 57  ? 10.597 -0.308  20.725 1.00 32.90 ? 63  TYR   A CD2 1 
ATOM   441  C  CE1 . TYR   A 1 57  ? 8.157  -1.594  20.875 1.00 33.60 ? 63  TYR   A CE1 1 
ATOM   442  C  CE2 . TYR   A 1 57  ? 9.723  -0.020  21.773 1.00 33.89 ? 63  TYR   A CE2 1 
ATOM   443  C  CZ  . TYR   A 1 57  ? 8.505  -0.674  21.848 1.00 34.65 ? 63  TYR   A CZ  1 
ATOM   444  O  OH  . TYR   A 1 57  ? 7.614  -0.382  22.853 1.00 35.84 ? 63  TYR   A OH  1 
ATOM   445  N  N   . TYR   A 1 58  ? 13.682 -2.593  20.497 1.00 28.86 ? 64  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 58  ? 14.271 -2.721  21.823 1.00 30.37 ? 64  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 58  ? 13.836 -1.559  22.751 1.00 30.41 ? 64  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 58  ? 13.993 -0.392  22.385 1.00 29.21 ? 64  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 58  ? 15.811 -2.812  21.745 1.00 31.32 ? 64  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 58  ? 16.448 -2.928  23.113 1.00 33.08 ? 64  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 58  ? 16.250 -4.054  23.900 1.00 34.10 ? 64  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 58  ? 17.181 -1.879  23.651 1.00 34.36 ? 64  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 58  ? 16.784 -4.143  25.179 1.00 36.07 ? 64  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 58  ? 17.711 -1.949  24.931 1.00 35.83 ? 64  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 58  ? 17.515 -3.084  25.694 1.00 37.79 ? 64  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 58  ? 18.033 -3.145  26.969 1.00 41.18 ? 64  TYR   A OH  1 
ATOM   457  N  N   . CYS   A 1 59  ? 13.319 -1.879  23.958 1.00 31.68 ? 65  CYS   A N   1 
ATOM   458  C  CA  . CYS   A 1 59  ? 12.876 -0.861  24.920 1.00 33.69 ? 65  CYS   A CA  1 
ATOM   459  C  C   . CYS   A 1 59  ? 13.752 -0.876  26.184 1.00 35.90 ? 65  CYS   A C   1 
ATOM   460  O  O   . CYS   A 1 59  ? 13.572 -1.754  27.032 1.00 35.39 ? 65  CYS   A O   1 
ATOM   461  C  CB  . CYS   A 1 59  ? 11.396 -1.064  25.247 1.00 34.82 ? 65  CYS   A CB  1 
ATOM   462  S  SG  . CYS   A 1 59  ? 10.803 -0.171  26.714 1.00 37.63 ? 65  CYS   A SG  1 
ATOM   463  N  N   . SER   A 1 60  ? 14.697 0.098   26.307 1.00 37.34 ? 66  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 60  ? 15.619 0.176   27.443 1.00 39.52 ? 66  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 60  ? 14.932 0.291   28.797 1.00 40.90 ? 66  SER   A C   1 
ATOM   466  O  O   . SER   A 1 60  ? 15.360 -0.378  29.734 1.00 42.17 ? 66  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 60  ? 16.641 1.299   27.272 1.00 41.75 ? 66  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 60  ? 16.004 2.538   27.008 1.00 45.20 ? 66  SER   A OG  1 
ATOM   469  N  N   . SER   A 1 61  ? 13.832 1.062   28.890 1.00 40.92 ? 67  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 61  ? 13.048 1.241   30.121 1.00 41.96 ? 67  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 61  ? 12.437 -0.063  30.683 1.00 42.60 ? 67  SER   A C   1 
ATOM   472  O  O   . SER   A 1 61  ? 12.045 -0.106  31.860 1.00 42.91 ? 67  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 61  ? 11.975 2.309   29.929 1.00 43.20 ? 67  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 61  ? 10.823 1.825   29.258 1.00 44.79 ? 67  SER   A OG  1 
ATOM   475  N  N   . ARG   A 1 62  ? 12.412 -1.138  29.879 1.00 41.71 ? 68  ARG   A N   1 
ATOM   476  C  CA  . ARG   A 1 62  ? 11.934 -2.437  30.364 1.00 42.30 ? 68  ARG   A CA  1 
ATOM   477  C  C   . ARG   A 1 62  ? 12.968 -3.563  30.182 1.00 43.63 ? 68  ARG   A C   1 
ATOM   478  O  O   . ARG   A 1 62  ? 12.673 -4.703  30.531 1.00 44.01 ? 68  ARG   A O   1 
ATOM   479  C  CB  . ARG   A 1 62  ? 10.661 -2.843  29.609 1.00 43.31 ? 68  ARG   A CB  1 
ATOM   480  C  CG  . ARG   A 1 62  ? 9.444  -1.978  29.868 1.00 45.73 ? 68  ARG   A CG  1 
ATOM   481  C  CD  . ARG   A 1 62  ? 8.781  -2.346  31.187 1.00 48.24 ? 68  ARG   A CD  1 
ATOM   482  N  NE  . ARG   A 1 62  ? 7.553  -1.582  31.411 1.00 50.72 ? 68  ARG   A NE  1 
ATOM   483  C  CZ  . ARG   A 1 62  ? 7.510  -0.365  31.945 1.00 52.11 ? 68  ARG   A CZ  1 
ATOM   484  N  NH1 . ARG   A 1 62  ? 8.629  0.242   32.326 1.00 51.14 ? 68  ARG   A NH1 1 
ATOM   485  N  NH2 . ARG   A 1 62  ? 6.346  0.256   32.104 1.00 52.08 ? 68  ARG   A NH2 1 
ATOM   486  N  N   . ARG   A 1 63  ? 14.135 -3.273  29.570 1.00 44.43 ? 69  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 63  ? 15.161 -4.251  29.183 1.00 44.70 ? 69  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 63  ? 14.556 -5.420  28.382 1.00 43.39 ? 69  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 63  ? 14.887 -6.590  28.620 1.00 43.50 ? 69  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 63  ? 15.999 -4.715  30.371 1.00 47.21 ? 69  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 63  ? 17.045 -3.698  30.805 1.00 53.21 ? 69  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 63  ? 17.787 -4.220  32.009 1.00 60.32 ? 69  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 63  ? 18.011 -3.168  32.996 1.00 67.97 ? 69  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 63  ? 18.438 -3.378  34.239 1.00 72.65 ? 69  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 63  ? 18.683 -4.613  34.666 1.00 72.34 ? 69  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 63  ? 18.621 -2.356  35.066 1.00 74.55 ? 69  ARG   A NH2 1 
ATOM   497  N  N   . LYS   A 1 64  ? 13.649 -5.091  27.434 1.00 41.39 ? 70  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 64  ? 12.927 -6.095  26.649 1.00 39.81 ? 70  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 64  ? 12.765 -5.696  25.172 1.00 36.94 ? 70  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 64  ? 12.700 -4.510  24.868 1.00 36.33 ? 70  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 64  ? 11.511 -6.280  27.228 1.00 41.24 ? 70  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 64  ? 11.361 -7.368  28.264 1.00 46.04 ? 70  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 64  ? 9.884  -7.548  28.586 1.00 51.77 ? 70  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 64  ? 9.616  -8.573  29.661 1.00 56.42 ? 70  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 64  ? 9.816  -8.025  31.031 1.00 58.24 ? 70  LYS   A NZ  1 
ATOM   506  N  N   . HIS   A 1 65  ? 12.637 -6.703  24.275 1.00 34.95 ? 71  HIS   A N   1 
ATOM   507  C  CA  . HIS   A 1 65  ? 12.345 -6.550  22.837 1.00 33.52 ? 71  HIS   A CA  1 
ATOM   508  C  C   . HIS   A 1 65  ? 10.842 -6.823  22.675 1.00 33.10 ? 71  HIS   A C   1 
ATOM   509  O  O   . HIS   A 1 65  ? 10.324 -7.789  23.257 1.00 33.72 ? 71  HIS   A O   1 
ATOM   510  C  CB  . HIS   A 1 65  ? 13.135 -7.562  21.979 1.00 33.19 ? 71  HIS   A CB  1 
ATOM   511  C  CG  . HIS   A 1 65  ? 14.611 -7.309  21.915 1.00 33.85 ? 71  HIS   A CG  1 
ATOM   512  N  ND1 . HIS   A 1 65  ? 15.179 -6.583  20.880 1.00 35.71 ? 71  HIS   A ND1 1 
ATOM   513  C  CD2 . HIS   A 1 65  ? 15.584 -7.660  22.779 1.00 34.51 ? 71  HIS   A CD2 1 
ATOM   514  C  CE1 . HIS   A 1 65  ? 16.466 -6.512  21.159 1.00 35.78 ? 71  HIS   A CE1 1 
ATOM   515  N  NE2 . HIS   A 1 65  ? 16.756 -7.152  22.286 1.00 35.63 ? 71  HIS   A NE2 1 
ATOM   516  N  N   . TYR   A 1 66  ? 10.130 -5.961  21.949 1.00 31.62 ? 72  TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 66  ? 8.683  -6.116  21.772 1.00 31.34 ? 72  TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 66  ? 8.265  -6.148  20.279 1.00 30.62 ? 72  TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 66  ? 8.697  -5.314  19.475 1.00 29.82 ? 72  TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 66  ? 7.913  -4.957  22.467 1.00 31.57 ? 72  TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 66  ? 7.993  -4.889  23.979 1.00 33.18 ? 72  TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 66  ? 7.296  -5.790  24.775 1.00 34.60 ? 72  TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 66  ? 8.657  -3.847  24.610 1.00 34.63 ? 72  TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 66  ? 7.328  -5.703  26.167 1.00 36.42 ? 72  TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 66  ? 8.673  -3.732  25.996 1.00 36.08 ? 72  TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 66  ? 8.003  -4.659  26.772 1.00 37.88 ? 72  TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 66  ? 8.028  -4.541  28.138 1.00 41.89 ? 72  TYR   A OH  1 
ATOM   528  N  N   . PRO   A 1 67  ? 7.362  -7.077  19.912 1.00 30.50 ? 73  PRO   A N   1 
ATOM   529  C  CA  . PRO   A 1 67  ? 6.853  -7.089  18.523 1.00 30.32 ? 73  PRO   A CA  1 
ATOM   530  C  C   . PRO   A 1 67  ? 5.733  -6.041  18.324 1.00 30.52 ? 73  PRO   A C   1 
ATOM   531  O  O   . PRO   A 1 67  ? 4.916  -5.830  19.238 1.00 30.62 ? 73  PRO   A O   1 
ATOM   532  C  CB  . PRO   A 1 67  ? 6.355  -8.523  18.336 1.00 31.06 ? 73  PRO   A CB  1 
ATOM   533  C  CG  . PRO   A 1 67  ? 6.032  -9.022  19.755 1.00 31.45 ? 73  PRO   A CG  1 
ATOM   534  C  CD  . PRO   A 1 67  ? 6.743  -8.128  20.757 1.00 29.90 ? 73  PRO   A CD  1 
ATOM   535  N  N   . VAL   A 1 68  ? 5.742  -5.329  17.169 1.00 29.80 ? 74  VAL   A N   1 
ATOM   536  C  CA  . VAL   A 1 68  ? 4.804  -4.239  16.882 1.00 29.98 ? 74  VAL   A CA  1 
ATOM   537  C  C   . VAL   A 1 68  ? 4.282  -4.222  15.440 1.00 30.94 ? 74  VAL   A C   1 
ATOM   538  O  O   . VAL   A 1 68  ? 4.943  -4.691  14.513 1.00 31.23 ? 74  VAL   A O   1 
ATOM   539  C  CB  . VAL   A 1 68  ? 5.470  -2.845  17.162 1.00 30.08 ? 74  VAL   A CB  1 
ATOM   540  C  CG1 . VAL   A 1 68  ? 5.567  -2.527  18.654 1.00 30.51 ? 74  VAL   A CG1 1 
ATOM   541  C  CG2 . VAL   A 1 68  ? 6.829  -2.734  16.485 1.00 30.16 ? 74  VAL   A CG2 1 
ATOM   542  N  N   . SER   A 1 69  ? 3.109  -3.608  15.252 1.00 30.91 ? 75  SER   A N   1 
ATOM   543  C  CA  . SER   A 1 69  ? 2.551  -3.264  13.954 1.00 31.48 ? 75  SER   A CA  1 
ATOM   544  C  C   . SER   A 1 69  ? 2.758  -1.743  13.914 1.00 31.35 ? 75  SER   A C   1 
ATOM   545  O  O   . SER   A 1 69  ? 2.557  -1.074  14.939 1.00 31.58 ? 75  SER   A O   1 
ATOM   546  C  CB  . SER   A 1 69  ? 1.060  -3.576  13.881 1.00 33.65 ? 75  SER   A CB  1 
ATOM   547  O  OG  . SER   A 1 69  ? 0.832  -4.901  13.434 1.00 36.91 ? 75  SER   A OG  1 
ATOM   548  N  N   . PHE   A 1 70  ? 3.214  -1.207  12.787 1.00 30.50 ? 76  PHE   A N   1 
ATOM   549  C  CA  . PHE   A 1 70  ? 3.467  0.228   12.714 1.00 31.19 ? 76  PHE   A CA  1 
ATOM   550  C  C   . PHE   A 1 70  ? 2.944  0.844   11.414 1.00 33.39 ? 76  PHE   A C   1 
ATOM   551  O  O   . PHE   A 1 70  ? 2.774  0.153   10.418 1.00 33.93 ? 76  PHE   A O   1 
ATOM   552  C  CB  . PHE   A 1 70  ? 4.950  0.545   12.990 1.00 30.33 ? 76  PHE   A CB  1 
ATOM   553  C  CG  . PHE   A 1 70  ? 5.932  -0.224  12.143 1.00 30.04 ? 76  PHE   A CG  1 
ATOM   554  C  CD1 . PHE   A 1 70  ? 6.454  -1.428  12.581 1.00 29.93 ? 76  PHE   A CD1 1 
ATOM   555  C  CD2 . PHE   A 1 70  ? 6.339  0.263   10.908 1.00 30.80 ? 76  PHE   A CD2 1 
ATOM   556  C  CE1 . PHE   A 1 70  ? 7.366  -2.129  11.804 1.00 30.56 ? 76  PHE   A CE1 1 
ATOM   557  C  CE2 . PHE   A 1 70  ? 7.252  -0.440  10.132 1.00 31.54 ? 76  PHE   A CE2 1 
ATOM   558  C  CZ  . PHE   A 1 70  ? 7.755  -1.636  10.582 1.00 30.90 ? 76  PHE   A CZ  1 
ATOM   559  N  N   . SER   A 1 71  ? 2.637  2.139   11.450 1.00 34.63 ? 77  SER   A N   1 
ATOM   560  C  CA  . SER   A 1 71  ? 2.054  2.836   10.319 1.00 36.59 ? 77  SER   A CA  1 
ATOM   561  C  C   . SER   A 1 71  ? 3.084  3.204   9.224  1.00 38.37 ? 77  SER   A C   1 
ATOM   562  O  O   . SER   A 1 71  ? 4.286  3.015   9.413  1.00 38.77 ? 77  SER   A O   1 
ATOM   563  C  CB  . SER   A 1 71  ? 1.283  4.063   10.809 1.00 37.54 ? 77  SER   A CB  1 
ATOM   564  O  OG  . SER   A 1 71  ? 2.155  5.135   11.127 1.00 39.70 ? 77  SER   A OG  1 
ATOM   565  N  N   . LYS   A 1 72  ? 2.609  3.692   8.076  1.00 39.58 ? 78  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 72  ? 3.479  4.116   6.969  1.00 41.68 ? 78  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 72  ? 4.105  5.487   7.298  1.00 42.34 ? 78  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 72  ? 3.433  6.317   7.903  1.00 43.12 ? 78  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 72  ? 2.668  4.206   5.648  1.00 44.38 ? 78  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 72  ? 1.649  3.081   5.469  1.00 50.67 ? 78  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 72  ? 1.779  2.405   4.117  1.00 56.79 ? 78  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 72  ? 3.083  1.653   3.987  1.00 60.74 ? 78  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 72  ? 3.399  1.376   2.559  1.00 62.69 ? 78  LYS   A NZ  1 
ATOM   574  N  N   . PRO   A 1 73  ? 5.373  5.754   6.914  1.00 42.18 ? 79  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 73  ? 5.986  7.060   7.237  1.00 42.32 ? 79  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 73  ? 5.179  8.272   6.786  1.00 42.88 ? 79  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 73  ? 4.767  8.351   5.620  1.00 43.25 ? 79  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 73  ? 7.344  7.001   6.538  1.00 42.94 ? 79  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 73  ? 7.632  5.555   6.391  1.00 43.41 ? 79  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 73  ? 6.320  4.869   6.212  1.00 41.68 ? 79  PRO   A CD  1 
ATOM   581  N  N   . SER   A 1 74  ? 4.958  9.226   7.706  1.00 42.75 ? 80  SER   A N   1 
ATOM   582  C  CA  . SER   A 1 74  ? 4.143  10.397  7.406  1.00 43.60 ? 80  SER   A CA  1 
ATOM   583  C  C   . SER   A 1 74  ? 4.438  11.619  8.310  1.00 43.56 ? 80  SER   A C   1 
ATOM   584  O  O   . SER   A 1 74  ? 5.295  11.547  9.191  1.00 42.84 ? 80  SER   A O   1 
ATOM   585  C  CB  . SER   A 1 74  ? 2.663  10.009  7.466  1.00 46.26 ? 80  SER   A CB  1 
ATOM   586  O  OG  . SER   A 1 74  ? 2.308  9.435   8.715  1.00 49.34 ? 80  SER   A OG  1 
ATOM   587  N  N   . LEU   A 1 75  ? 3.749  12.757  8.051  1.00 44.32 ? 81  LEU   A N   1 
ATOM   588  C  CA  . LEU   A 1 75  ? 3.873  14.003  8.804  1.00 45.79 ? 81  LEU   A CA  1 
ATOM   589  C  C   . LEU   A 1 75  ? 2.961  13.922  10.013 1.00 47.36 ? 81  LEU   A C   1 
ATOM   590  O  O   . LEU   A 1 75  ? 1.738  13.882  9.854  1.00 48.17 ? 81  LEU   A O   1 
ATOM   591  C  CB  . LEU   A 1 75  ? 3.431  15.202  7.949  1.00 46.00 ? 81  LEU   A CB  1 
ATOM   592  C  CG  . LEU   A 1 75  ? 4.475  15.784  7.027  1.00 47.58 ? 81  LEU   A CG  1 
ATOM   593  C  CD1 . LEU   A 1 75  ? 3.830  16.614  5.952  1.00 48.84 ? 81  LEU   A CD1 1 
ATOM   594  C  CD2 . LEU   A 1 75  ? 5.464  16.624  7.800  1.00 48.26 ? 81  LEU   A CD2 1 
ATOM   595  N  N   . ILE   A 1 76  ? 3.544  13.929  11.215 1.00 47.62 ? 82  ILE   A N   1 
ATOM   596  C  CA  . ILE   A 1 76  ? 2.798  13.842  12.461 1.00 48.80 ? 82  ILE   A CA  1 
ATOM   597  C  C   . ILE   A 1 76  ? 3.172  15.003  13.388 1.00 50.41 ? 82  ILE   A C   1 
ATOM   598  O  O   . ILE   A 1 76  ? 4.354  15.265  13.602 1.00 49.99 ? 82  ILE   A O   1 
ATOM   599  C  CB  . ILE   A 1 76  ? 3.052  12.455  13.115 1.00 48.97 ? 82  ILE   A CB  1 
ATOM   600  C  CG1 . ILE   A 1 76  ? 2.497  11.317  12.236 1.00 49.76 ? 82  ILE   A CG1 1 
ATOM   601  C  CG2 . ILE   A 1 76  ? 2.487  12.386  14.535 1.00 49.25 ? 82  ILE   A CG2 1 
ATOM   602  C  CD1 . ILE   A 1 76  ? 3.071  10.015  12.533 1.00 51.06 ? 82  ILE   A CD1 1 
ATOM   603  N  N   . PHE   A 1 77  ? 2.166  15.703  13.934 1.00 52.00 ? 83  PHE   A N   1 
ATOM   604  C  CA  . PHE   A 1 77  ? 2.402  16.816  14.849 1.00 53.80 ? 83  PHE   A CA  1 
ATOM   605  C  C   . PHE   A 1 77  ? 3.049  16.368  16.177 1.00 54.55 ? 83  PHE   A C   1 
ATOM   606  O  O   . PHE   A 1 77  ? 2.600  15.411  16.811 1.00 54.24 ? 83  PHE   A O   1 
ATOM   607  C  CB  . PHE   A 1 77  ? 1.102  17.565  15.112 1.00 54.70 ? 83  PHE   A CB  1 
ATOM   608  C  CG  . PHE   A 1 77  ? 1.259  18.779  15.989 1.00 56.12 ? 83  PHE   A CG  1 
ATOM   609  C  CD1 . PHE   A 1 77  ? 1.755  19.961  15.477 1.00 57.21 ? 83  PHE   A CD1 1 
ATOM   610  C  CD2 . PHE   A 1 77  ? 0.873  18.749  17.316 1.00 57.35 ? 83  PHE   A CD2 1 
ATOM   611  C  CE1 . PHE   A 1 77  ? 1.893  21.080  16.282 1.00 58.16 ? 83  PHE   A CE1 1 
ATOM   612  C  CE2 . PHE   A 1 77  ? 1.005  19.872  18.119 1.00 58.09 ? 83  PHE   A CE2 1 
ATOM   613  C  CZ  . PHE   A 1 77  ? 1.525  21.027  17.599 1.00 58.13 ? 83  PHE   A CZ  1 
ATOM   614  N  N   . VAL   A 1 78  ? 4.136  17.051  16.564 1.00 55.00 ? 84  VAL   A N   1 
ATOM   615  C  CA  . VAL   A 1 78  ? 4.878  16.795  17.789 1.00 55.88 ? 84  VAL   A CA  1 
ATOM   616  C  C   . VAL   A 1 78  ? 4.857  18.059  18.660 1.00 57.19 ? 84  VAL   A C   1 
ATOM   617  O  O   . VAL   A 1 78  ? 5.200  19.156  18.197 1.00 57.15 ? 84  VAL   A O   1 
ATOM   618  C  CB  . VAL   A 1 78  ? 6.325  16.286  17.523 1.00 56.21 ? 84  VAL   A CB  1 
ATOM   619  C  CG1 . VAL   A 1 78  ? 7.017  15.881  18.821 1.00 56.49 ? 84  VAL   A CG1 1 
ATOM   620  C  CG2 . VAL   A 1 78  ? 6.324  15.119  16.547 1.00 56.58 ? 84  VAL   A CG2 1 
ATOM   621  N  N   . GLU   A 1 79  ? 4.413  17.891  19.913 1.00 58.01 ? 85  GLU   A N   1 
ATOM   622  C  CA  . GLU   A 1 79  ? 4.306  18.929  20.933 1.00 59.21 ? 85  GLU   A CA  1 
ATOM   623  C  C   . GLU   A 1 79  ? 5.645  19.587  21.209 1.00 59.24 ? 85  GLU   A C   1 
ATOM   624  O  O   . GLU   A 1 79  ? 6.673  18.915  21.159 1.00 59.19 ? 85  GLU   A O   1 
ATOM   625  C  CB  . GLU   A 1 79  ? 3.797  18.300  22.233 1.00 62.64 ? 85  GLU   A CB  1 
ATOM   626  C  CG  . GLU   A 1 79  ? 2.301  18.429  22.420 1.00 70.04 ? 85  GLU   A CG  1 
ATOM   627  C  CD  . GLU   A 1 79  ? 1.923  19.308  23.592 1.00 78.15 ? 85  GLU   A CD  1 
ATOM   628  O  OE1 . GLU   A 1 79  ? 1.539  18.752  24.646 1.00 80.35 ? 85  GLU   A OE1 1 
ATOM   629  O  OE2 . GLU   A 1 79  ? 2.013  20.550  23.461 1.00 81.27 ? 85  GLU   A OE2 1 
ATOM   630  N  N   . ALA   A 1 80  ? 5.638  20.889  21.546 1.00 59.04 ? 86  ALA   A N   1 
ATOM   631  C  CA  . ALA   A 1 80  ? 6.867  21.621  21.864 1.00 59.74 ? 86  ALA   A CA  1 
ATOM   632  C  C   . ALA   A 1 80  ? 7.698  20.935  22.962 1.00 60.54 ? 86  ALA   A C   1 
ATOM   633  O  O   . ALA   A 1 80  ? 7.141  20.336  23.877 1.00 61.56 ? 86  ALA   A O   1 
ATOM   634  C  CB  . ALA   A 1 80  ? 6.532  23.034  22.288 1.00 59.90 ? 86  ALA   A CB  1 
ATOM   635  N  N   . SER   A 1 81  ? 9.018  21.006  22.859 1.00 60.07 ? 87  SER   A N   1 
ATOM   636  C  CA  . SER   A 1 81  ? 9.912  20.387  23.833 1.00 60.18 ? 87  SER   A CA  1 
ATOM   637  C  C   . SER   A 1 81  ? 11.121 21.304  24.113 1.00 60.86 ? 87  SER   A C   1 
ATOM   638  O  O   . SER   A 1 81  ? 11.200 22.419  23.578 1.00 61.37 ? 87  SER   A O   1 
ATOM   639  C  CB  . SER   A 1 81  ? 10.368 19.017  23.321 1.00 60.78 ? 87  SER   A CB  1 
ATOM   640  O  OG  . SER   A 1 81  ? 11.363 19.123  22.315 1.00 62.06 ? 87  SER   A OG  1 
ATOM   641  N  N   . GLU   A 1 82  ? 12.060 20.848  24.956 1.00 60.55 ? 88  GLU   A N   1 
ATOM   642  C  CA  . GLU   A 1 82  ? 13.278 21.618  25.227 1.00 60.64 ? 88  GLU   A CA  1 
ATOM   643  C  C   . GLU   A 1 82  ? 14.211 21.670  23.989 1.00 58.71 ? 88  GLU   A C   1 
ATOM   644  O  O   . GLU   A 1 82  ? 15.063 22.556  23.909 1.00 59.36 ? 88  GLU   A O   1 
ATOM   645  C  CB  . GLU   A 1 82  ? 14.042 21.094  26.478 1.00 64.84 ? 88  GLU   A CB  1 
ATOM   646  C  CG  . GLU   A 1 82  ? 13.513 19.806  27.114 1.00 71.75 ? 88  GLU   A CG  1 
ATOM   647  C  CD  . GLU   A 1 82  ? 14.304 19.294  28.307 1.00 81.13 ? 88  GLU   A CD  1 
ATOM   648  O  OE1 . GLU   A 1 82  ? 15.221 18.467  28.089 1.00 83.13 ? 88  GLU   A OE1 1 
ATOM   649  O  OE2 . GLU   A 1 82  ? 14.008 19.709  29.454 1.00 83.81 ? 88  GLU   A OE2 1 
ATOM   650  N  N   . TYR   A 1 83  ? 14.029 20.746  23.019 1.00 56.16 ? 89  TYR   A N   1 
ATOM   651  C  CA  . TYR   A 1 83  ? 14.852 20.653  21.817 1.00 54.14 ? 89  TYR   A CA  1 
ATOM   652  C  C   . TYR   A 1 83  ? 14.230 21.319  20.582 1.00 51.66 ? 89  TYR   A C   1 
ATOM   653  O  O   . TYR   A 1 83  ? 14.969 21.792  19.724 1.00 51.52 ? 89  TYR   A O   1 
ATOM   654  C  CB  . TYR   A 1 83  ? 15.174 19.181  21.485 1.00 54.16 ? 89  TYR   A CB  1 
ATOM   655  C  CG  . TYR   A 1 83  ? 15.594 18.354  22.677 1.00 54.95 ? 89  TYR   A CG  1 
ATOM   656  C  CD1 . TYR   A 1 83  ? 16.850 18.504  23.245 1.00 55.94 ? 89  TYR   A CD1 1 
ATOM   657  C  CD2 . TYR   A 1 83  ? 14.720 17.451  23.263 1.00 55.83 ? 89  TYR   A CD2 1 
ATOM   658  C  CE1 . TYR   A 1 83  ? 17.230 17.771  24.363 1.00 56.96 ? 89  TYR   A CE1 1 
ATOM   659  C  CE2 . TYR   A 1 83  ? 15.090 16.707  24.375 1.00 56.94 ? 89  TYR   A CE2 1 
ATOM   660  C  CZ  . TYR   A 1 83  ? 16.347 16.870  24.926 1.00 57.96 ? 89  TYR   A CZ  1 
ATOM   661  O  OH  . TYR   A 1 83  ? 16.721 16.128  26.022 1.00 59.53 ? 89  TYR   A OH  1 
ATOM   662  N  N   . TYR   A 1 84  ? 12.893 21.299  20.448 1.00 49.43 ? 90  TYR   A N   1 
ATOM   663  C  CA  . TYR   A 1 84  ? 12.237 21.863  19.264 1.00 47.80 ? 90  TYR   A CA  1 
ATOM   664  C  C   . TYR   A 1 84  ? 10.968 22.642  19.623 1.00 48.35 ? 90  TYR   A C   1 
ATOM   665  O  O   . TYR   A 1 84  ? 10.291 22.285  20.586 1.00 48.59 ? 90  TYR   A O   1 
ATOM   666  C  CB  . TYR   A 1 84  ? 11.789 20.722  18.311 1.00 46.13 ? 90  TYR   A CB  1 
ATOM   667  C  CG  . TYR   A 1 84  ? 12.857 19.754  17.847 1.00 44.57 ? 90  TYR   A CG  1 
ATOM   668  C  CD1 . TYR   A 1 84  ? 12.825 18.419  18.228 1.00 44.17 ? 90  TYR   A CD1 1 
ATOM   669  C  CD2 . TYR   A 1 84  ? 13.826 20.145  16.936 1.00 44.30 ? 90  TYR   A CD2 1 
ATOM   670  C  CE1 . TYR   A 1 84  ? 13.767 17.510  17.760 1.00 44.40 ? 90  TYR   A CE1 1 
ATOM   671  C  CE2 . TYR   A 1 84  ? 14.781 19.250  16.470 1.00 44.32 ? 90  TYR   A CE2 1 
ATOM   672  C  CZ  . TYR   A 1 84  ? 14.745 17.929  16.876 1.00 44.64 ? 90  TYR   A CZ  1 
ATOM   673  O  OH  . TYR   A 1 84  ? 15.702 17.054  16.419 1.00 43.98 ? 90  TYR   A OH  1 
ATOM   674  N  N   . PRO   A 1 85  ? 10.549 23.630  18.804 1.00 48.33 ? 91  PRO   A N   1 
ATOM   675  C  CA  . PRO   A 1 85  ? 9.219  24.239  19.036 1.00 48.64 ? 91  PRO   A CA  1 
ATOM   676  C  C   . PRO   A 1 85  ? 8.108  23.249  18.578 1.00 48.90 ? 91  PRO   A C   1 
ATOM   677  O  O   . PRO   A 1 85  ? 8.418  22.140  18.109 1.00 48.56 ? 91  PRO   A O   1 
ATOM   678  C  CB  . PRO   A 1 85  ? 9.267  25.503  18.166 1.00 49.23 ? 91  PRO   A CB  1 
ATOM   679  C  CG  . PRO   A 1 85  ? 10.161 25.113  17.019 1.00 49.34 ? 91  PRO   A CG  1 
ATOM   680  C  CD  . PRO   A 1 85  ? 11.189 24.155  17.576 1.00 47.49 ? 91  PRO   A CD  1 
ATOM   681  N  N   . ALA   A 1 86  ? 6.822  23.624  18.709 1.00 48.97 ? 92  ALA   A N   1 
ATOM   682  C  CA  . ALA   A 1 86  ? 5.733  22.747  18.258 1.00 49.33 ? 92  ALA   A CA  1 
ATOM   683  C  C   . ALA   A 1 86  ? 5.788  22.688  16.720 1.00 48.14 ? 92  ALA   A C   1 
ATOM   684  O  O   . ALA   A 1 86  ? 5.829  23.745  16.080 1.00 48.52 ? 92  ALA   A O   1 
ATOM   685  C  CB  . ALA   A 1 86  ? 4.394  23.290  18.727 1.00 50.41 ? 92  ALA   A CB  1 
ATOM   686  N  N   . ARG   A 1 87  ? 5.847  21.468  16.131 1.00 45.85 ? 93  ARG   A N   1 
ATOM   687  C  CA  . ARG   A 1 87  ? 5.993  21.339  14.674 1.00 44.59 ? 93  ARG   A CA  1 
ATOM   688  C  C   . ARG   A 1 87  ? 5.504  19.961  14.107 1.00 44.08 ? 93  ARG   A C   1 
ATOM   689  O  O   . ARG   A 1 87  ? 5.130  19.077  14.872 1.00 43.72 ? 93  ARG   A O   1 
ATOM   690  C  CB  . ARG   A 1 87  ? 7.492  21.581  14.314 1.00 44.37 ? 93  ARG   A CB  1 
ATOM   691  C  CG  . ARG   A 1 87  ? 8.373  20.309  14.330 1.00 42.92 ? 93  ARG   A CG  1 
ATOM   692  C  CD  . ARG   A 1 87  ? 9.645  20.370  15.141 1.00 40.86 ? 93  ARG   A CD  1 
ATOM   693  N  NE  . ARG   A 1 87  ? 10.550 19.279  14.765 1.00 38.12 ? 93  ARG   A NE  1 
ATOM   694  C  CZ  . ARG   A 1 87  ? 10.551 18.071  15.318 1.00 36.58 ? 93  ARG   A CZ  1 
ATOM   695  N  NH1 . ARG   A 1 87  ? 11.401 17.140  14.895 1.00 33.86 ? 93  ARG   A NH1 1 
ATOM   696  N  NH2 . ARG   A 1 87  ? 9.702  17.781  16.297 1.00 34.80 ? 93  ARG   A NH2 1 
ATOM   697  N  N   . TYR   A 1 88  ? 5.539  19.780  12.770 1.00 43.86 ? 94  TYR   A N   1 
ATOM   698  C  CA  . TYR   A 1 88  ? 5.247  18.493  12.138 1.00 43.83 ? 94  TYR   A CA  1 
ATOM   699  C  C   . TYR   A 1 88  ? 6.566  17.763  11.894 1.00 41.25 ? 94  TYR   A C   1 
ATOM   700  O  O   . TYR   A 1 88  ? 7.489  18.337  11.322 1.00 41.04 ? 94  TYR   A O   1 
ATOM   701  C  CB  . TYR   A 1 88  ? 4.563  18.679  10.784 1.00 45.41 ? 94  TYR   A CB  1 
ATOM   702  C  CG  . TYR   A 1 88  ? 3.111  19.075  10.889 1.00 47.87 ? 94  TYR   A CG  1 
ATOM   703  C  CD1 . TYR   A 1 88  ? 2.124  18.125  11.112 1.00 49.53 ? 94  TYR   A CD1 1 
ATOM   704  C  CD2 . TYR   A 1 88  ? 2.722  20.399  10.754 1.00 49.52 ? 94  TYR   A CD2 1 
ATOM   705  C  CE1 . TYR   A 1 88  ? 0.785  18.484  11.197 1.00 51.26 ? 94  TYR   A CE1 1 
ATOM   706  C  CE2 . TYR   A 1 88  ? 1.397  20.772  10.863 1.00 51.13 ? 94  TYR   A CE2 1 
ATOM   707  C  CZ  . TYR   A 1 88  ? 0.427  19.816  11.076 1.00 52.80 ? 94  TYR   A CZ  1 
ATOM   708  O  OH  . TYR   A 1 88  ? -0.881 20.239  11.140 1.00 56.27 ? 94  TYR   A OH  1 
ATOM   709  N  N   . GLN   A 1 89  ? 6.656  16.512  12.325 1.00 38.75 ? 95  GLN   A N   1 
ATOM   710  C  CA  . GLN   A 1 89  ? 7.850  15.710  12.113 1.00 36.81 ? 95  GLN   A CA  1 
ATOM   711  C  C   . GLN   A 1 89  ? 7.549  14.769  10.964 1.00 35.75 ? 95  GLN   A C   1 
ATOM   712  O  O   . GLN   A 1 89  ? 6.556  14.051  10.992 1.00 36.23 ? 95  GLN   A O   1 
ATOM   713  C  CB  . GLN   A 1 89  ? 8.271  14.946  13.383 1.00 36.50 ? 95  GLN   A CB  1 
ATOM   714  C  CG  . GLN   A 1 89  ? 9.455  13.985  13.150 1.00 36.75 ? 95  GLN   A CG  1 
ATOM   715  C  CD  . GLN   A 1 89  ? 10.179 13.586  14.425 1.00 37.86 ? 95  GLN   A CD  1 
ATOM   716  O  OE1 . GLN   A 1 89  ? 10.396 14.401  15.338 1.00 39.40 ? 95  GLN   A OE1 1 
ATOM   717  N  NE2 . GLN   A 1 89  ? 10.598 12.324  14.499 1.00 34.74 ? 95  GLN   A NE2 1 
ATOM   718  N  N   . SER   A 1 90  ? 8.350  14.837  9.918  1.00 34.35 ? 96  SER   A N   1 
ATOM   719  C  CA  . SER   A 1 90  ? 8.160  14.028  8.719  1.00 33.59 ? 96  SER   A CA  1 
ATOM   720  C  C   . SER   A 1 90  ? 8.876  12.672  8.842  1.00 33.12 ? 96  SER   A C   1 
ATOM   721  O  O   . SER   A 1 90  ? 9.769  12.512  9.696  1.00 33.54 ? 96  SER   A O   1 
ATOM   722  C  CB  . SER   A 1 90  ? 8.674  14.793  7.499  1.00 34.02 ? 96  SER   A CB  1 
ATOM   723  O  OG  . SER   A 1 90  ? 10.059 15.074  7.635  1.00 35.89 ? 96  SER   A OG  1 
ATOM   724  N  N   . HIS   A 1 91  ? 8.454  11.696  8.013  1.00 31.78 ? 97  HIS   A N   1 
ATOM   725  C  CA  . HIS   A 1 91  ? 9.013  10.336  7.933  1.00 31.38 ? 97  HIS   A CA  1 
ATOM   726  C  C   . HIS   A 1 91  ? 8.861  9.533   9.253  1.00 30.97 ? 97  HIS   A C   1 
ATOM   727  O  O   . HIS   A 1 91  ? 9.657  8.634   9.538  1.00 30.66 ? 97  HIS   A O   1 
ATOM   728  C  CB  . HIS   A 1 91  ? 10.476 10.370  7.433  1.00 31.01 ? 97  HIS   A CB  1 
ATOM   729  C  CG  . HIS   A 1 91  ? 10.648 11.028  6.082  1.00 33.33 ? 97  HIS   A CG  1 
ATOM   730  N  ND1 . HIS   A 1 91  ? 10.717 10.279  4.911  1.00 34.90 ? 97  HIS   A ND1 1 
ATOM   731  C  CD2 . HIS   A 1 91  ? 10.747 12.343  5.757  1.00 34.00 ? 97  HIS   A CD2 1 
ATOM   732  C  CE1 . HIS   A 1 91  ? 10.874 11.159  3.929  1.00 35.30 ? 97  HIS   A CE1 1 
ATOM   733  N  NE2 . HIS   A 1 91  ? 10.881 12.411  4.389  1.00 34.90 ? 97  HIS   A NE2 1 
ATOM   734  N  N   . LEU   A 1 92  ? 7.815  9.847   10.039 1.00 31.21 ? 98  LEU   A N   1 
ATOM   735  C  CA  . LEU   A 1 92  ? 7.567  9.217   11.344 1.00 31.68 ? 98  LEU   A CA  1 
ATOM   736  C  C   . LEU   A 1 92  ? 6.548  8.075   11.274 1.00 31.35 ? 98  LEU   A C   1 
ATOM   737  O  O   . LEU   A 1 92  ? 5.543  8.197   10.581 1.00 32.14 ? 98  LEU   A O   1 
ATOM   738  C  CB  . LEU   A 1 92  ? 7.119  10.301  12.355 1.00 31.97 ? 98  LEU   A CB  1 
ATOM   739  C  CG  . LEU   A 1 92  ? 6.963  9.869   13.817 1.00 34.25 ? 98  LEU   A CG  1 
ATOM   740  C  CD1 . LEU   A 1 92  ? 8.307  9.480   14.413 1.00 35.27 ? 98  LEU   A CD1 1 
ATOM   741  C  CD2 . LEU   A 1 92  ? 6.285  10.973  14.654 1.00 34.92 ? 98  LEU   A CD2 1 
ATOM   742  N  N   . MET   A 1 93  ? 6.797  6.981   12.008 1.00 30.86 ? 99  MET   A N   1 
ATOM   743  C  CA  . MET   A 1 93  ? 5.928  5.796   12.038 1.00 30.89 ? 99  MET   A CA  1 
ATOM   744  C  C   . MET   A 1 93  ? 5.438  5.511   13.465 1.00 31.86 ? 99  MET   A C   1 
ATOM   745  O  O   . MET   A 1 93  ? 6.260  5.443   14.374 1.00 32.57 ? 99  MET   A O   1 
ATOM   746  C  CB  . MET   A 1 93  ? 6.693  4.576   11.477 1.00 30.61 ? 99  MET   A CB  1 
ATOM   747  C  CG  . MET   A 1 93  ? 7.113  4.749   10.012 1.00 31.57 ? 99  MET   A CG  1 
ATOM   748  S  SD  . MET   A 1 93  ? 8.177  3.432   9.369  1.00 34.56 ? 99  MET   A SD  1 
ATOM   749  C  CE  . MET   A 1 93  ? 9.512  3.479   10.504 1.00 32.60 ? 99  MET   A CE  1 
ATOM   750  N  N   . LEU   A 1 94  ? 4.117  5.344   13.677 1.00 31.78 ? 100 LEU   A N   1 
ATOM   751  C  CA  . LEU   A 1 94  ? 3.594  5.074   15.023 1.00 32.37 ? 100 LEU   A CA  1 
ATOM   752  C  C   . LEU   A 1 94  ? 3.169  3.613   15.232 1.00 32.02 ? 100 LEU   A C   1 
ATOM   753  O  O   . LEU   A 1 94  ? 2.723  2.963   14.289 1.00 31.11 ? 100 LEU   A O   1 
ATOM   754  C  CB  . LEU   A 1 94  ? 2.397  5.996   15.384 1.00 33.09 ? 100 LEU   A CB  1 
ATOM   755  C  CG  . LEU   A 1 94  ? 2.661  7.507   15.477 1.00 35.71 ? 100 LEU   A CG  1 
ATOM   756  C  CD1 . LEU   A 1 94  ? 1.441  8.240   16.018 1.00 36.12 ? 100 LEU   A CD1 1 
ATOM   757  C  CD2 . LEU   A 1 94  ? 3.849  7.821   16.365 1.00 36.78 ? 100 LEU   A CD2 1 
ATOM   758  N  N   . ALA   A 1 95  ? 3.248  3.143   16.494 1.00 32.30 ? 101 ALA   A N   1 
ATOM   759  C  CA  . ALA   A 1 95  ? 2.831  1.812   16.944 1.00 33.56 ? 101 ALA   A CA  1 
ATOM   760  C  C   . ALA   A 1 95  ? 2.288  1.882   18.374 1.00 34.76 ? 101 ALA   A C   1 
ATOM   761  O  O   . ALA   A 1 95  ? 2.650  2.771   19.137 1.00 34.49 ? 101 ALA   A O   1 
ATOM   762  C  CB  . ALA   A 1 95  ? 4.027  0.862   16.919 1.00 33.58 ? 101 ALA   A CB  1 
ATOM   763  N  N   . VAL   A 1 96  ? 1.455  0.916   18.751 1.00 35.94 ? 102 VAL   A N   1 
ATOM   764  C  CA  . VAL   A 1 96  ? 0.955  0.793   20.107 1.00 37.54 ? 102 VAL   A CA  1 
ATOM   765  C  C   . VAL   A 1 96  ? 2.036  0.016   20.868 1.00 39.28 ? 102 VAL   A C   1 
ATOM   766  O  O   . VAL   A 1 96  ? 2.478  -1.046  20.424 1.00 39.59 ? 102 VAL   A O   1 
ATOM   767  C  CB  . VAL   A 1 96  ? -0.428 0.097   20.134 1.00 38.49 ? 102 VAL   A CB  1 
ATOM   768  C  CG1 . VAL   A 1 96  ? -0.867 -0.220  21.564 1.00 38.65 ? 102 VAL   A CG1 1 
ATOM   769  C  CG2 . VAL   A 1 96  ? -1.481 0.966   19.428 1.00 38.78 ? 102 VAL   A CG2 1 
ATOM   770  N  N   . GLY   A 1 97  ? 2.555  0.625   21.918 1.00 40.13 ? 103 GLY   A N   1 
ATOM   771  C  CA  . GLY   A 1 97  ? 3.644  0.043   22.686 1.00 41.76 ? 103 GLY   A CA  1 
ATOM   772  C  C   . GLY   A 1 97  ? 4.171  0.989   23.750 1.00 43.20 ? 103 GLY   A C   1 
ATOM   773  O  O   . GLY   A 1 97  ? 3.946  2.202   23.680 1.00 44.40 ? 103 GLY   A O   1 
ATOM   774  N  N   . HIS   A 1 98  ? 4.885  0.446   24.745 1.00 42.67 ? 104 HIS   A N   1 
ATOM   775  C  CA  . HIS   A 1 98  ? 5.439  1.262   25.813 1.00 42.75 ? 104 HIS   A CA  1 
ATOM   776  C  C   . HIS   A 1 98  ? 6.738  1.998   25.434 1.00 41.72 ? 104 HIS   A C   1 
ATOM   777  O  O   . HIS   A 1 98  ? 7.641  1.425   24.830 1.00 40.65 ? 104 HIS   A O   1 
ATOM   778  C  CB  . HIS   A 1 98  ? 5.639  0.426   27.096 1.00 44.33 ? 104 HIS   A CB  1 
ATOM   779  C  CG  . HIS   A 1 98  ? 6.276  1.201   28.212 1.00 47.38 ? 104 HIS   A CG  1 
ATOM   780  N  ND1 . HIS   A 1 98  ? 5.571  2.158   28.916 1.00 49.87 ? 104 HIS   A ND1 1 
ATOM   781  C  CD2 . HIS   A 1 98  ? 7.558  1.193   28.645 1.00 48.56 ? 104 HIS   A CD2 1 
ATOM   782  C  CE1 . HIS   A 1 98  ? 6.438  2.687   29.764 1.00 50.40 ? 104 HIS   A CE1 1 
ATOM   783  N  NE2 . HIS   A 1 98  ? 7.650  2.145   29.623 1.00 50.15 ? 104 HIS   A NE2 1 
ATOM   784  N  N   . SER   A 1 99  ? 6.850  3.242   25.879 1.00 41.96 ? 105 SER   A N   1 
ATOM   785  C  CA  . SER   A 1 99  ? 8.057  4.032   25.716 1.00 43.05 ? 105 SER   A CA  1 
ATOM   786  C  C   . SER   A 1 99  ? 8.067  5.221   26.690 1.00 44.76 ? 105 SER   A C   1 
ATOM   787  O  O   . SER   A 1 99  ? 7.016  5.741   27.059 1.00 44.66 ? 105 SER   A O   1 
ATOM   788  C  CB  . SER   A 1 99  ? 8.217  4.515   24.276 1.00 43.21 ? 105 SER   A CB  1 
ATOM   789  O  OG  . SER   A 1 99  ? 7.177  5.402   23.901 1.00 45.20 ? 105 SER   A OG  1 
ATOM   790  N  N   . GLU   A 1 100 ? 9.255  5.625   27.120 1.00 46.06 ? 106 GLU   A N   1 
ATOM   791  C  CA  . GLU   A 1 100 ? 9.460  6.817   27.947 1.00 47.97 ? 106 GLU   A CA  1 
ATOM   792  C  C   . GLU   A 1 100 ? 10.749 7.551   27.492 1.00 49.28 ? 106 GLU   A C   1 
ATOM   793  O  O   . GLU   A 1 100 ? 11.564 6.922   26.811 1.00 49.78 ? 106 GLU   A O   1 
ATOM   794  C  CB  . GLU   A 1 100 ? 9.391  6.531   29.465 1.00 50.96 ? 106 GLU   A CB  1 
ATOM   795  C  CG  . GLU   A 1 100 ? 10.029 5.235   29.917 1.00 56.50 ? 106 GLU   A CG  1 
ATOM   796  C  CD  . GLU   A 1 100 ? 9.829  4.973   31.398 1.00 60.63 ? 106 GLU   A CD  1 
ATOM   797  O  OE1 . GLU   A 1 100 ? 10.441 5.696   32.215 1.00 60.37 ? 106 GLU   A OE1 1 
ATOM   798  O  OE2 . GLU   A 1 100 ? 9.053  4.056   31.746 1.00 62.07 ? 106 GLU   A OE2 1 
ATOM   799  N  N   . PRO   A 1 101 ? 10.944 8.885   27.736 1.00 49.99 ? 107 PRO   A N   1 
ATOM   800  C  CA  . PRO   A 1 101 ? 12.196 9.530   27.265 1.00 50.08 ? 107 PRO   A CA  1 
ATOM   801  C  C   . PRO   A 1 101 ? 13.367 8.854   27.967 1.00 50.09 ? 107 PRO   A C   1 
ATOM   802  O  O   . PRO   A 1 101 ? 13.330 8.631   29.191 1.00 52.32 ? 107 PRO   A O   1 
ATOM   803  C  CB  . PRO   A 1 101 ? 12.014 11.007  27.625 1.00 51.12 ? 107 PRO   A CB  1 
ATOM   804  C  CG  . PRO   A 1 101 ? 11.005 11.028  28.733 1.00 51.54 ? 107 PRO   A CG  1 
ATOM   805  C  CD  . PRO   A 1 101 ? 10.106 9.819   28.519 1.00 49.70 ? 107 PRO   A CD  1 
ATOM   806  N  N   . GLY   A 1 102 ? 14.296 8.394   27.160 1.00 47.71 ? 108 GLY   A N   1 
ATOM   807  C  CA  . GLY   A 1 102 ? 15.392 7.518   27.558 1.00 45.82 ? 108 GLY   A CA  1 
ATOM   808  C  C   . GLY   A 1 102 ? 15.440 6.309   26.622 1.00 43.37 ? 108 GLY   A C   1 
ATOM   809  O  O   . GLY   A 1 102 ? 16.491 5.683   26.442 1.00 43.42 ? 108 GLY   A O   1 
ATOM   810  N  N   . ASP   A 1 103 ? 14.280 5.978   25.998 1.00 40.79 ? 109 ASP   A N   1 
ATOM   811  C  CA  . ASP   A 1 103 ? 14.146 4.919   25.021 1.00 38.42 ? 109 ASP   A CA  1 
ATOM   812  C  C   . ASP   A 1 103 ? 14.564 5.356   23.618 1.00 35.85 ? 109 ASP   A C   1 
ATOM   813  O  O   . ASP   A 1 103 ? 14.856 4.485   22.808 1.00 34.10 ? 109 ASP   A O   1 
ATOM   814  C  CB  . ASP   A 1 103 ? 12.736 4.329   25.021 1.00 38.80 ? 109 ASP   A CB  1 
ATOM   815  C  CG  . ASP   A 1 103 ? 12.480 3.523   26.263 1.00 41.09 ? 109 ASP   A CG  1 
ATOM   816  O  OD1 . ASP   A 1 103 ? 13.407 2.807   26.702 1.00 40.83 ? 109 ASP   A OD1 1 
ATOM   817  O  OD2 . ASP   A 1 103 ? 11.362 3.617   26.806 1.00 41.67 ? 109 ASP   A OD2 1 
ATOM   818  N  N   . CYS   A 1 104 ? 14.691 6.691   23.352 1.00 35.03 ? 110 CYS   A N   1 
ATOM   819  C  CA  . CYS   A 1 104 ? 15.165 7.221   22.055 1.00 35.05 ? 110 CYS   A CA  1 
ATOM   820  C  C   . CYS   A 1 104 ? 16.505 6.588   21.697 1.00 34.05 ? 110 CYS   A C   1 
ATOM   821  O  O   . CYS   A 1 104 ? 17.339 6.405   22.585 1.00 34.36 ? 110 CYS   A O   1 
ATOM   822  C  CB  . CYS   A 1 104 ? 15.265 8.745   22.080 1.00 36.08 ? 110 CYS   A CB  1 
ATOM   823  S  SG  . CYS   A 1 104 ? 13.672 9.589   21.955 1.00 42.34 ? 110 CYS   A SG  1 
ATOM   824  N  N   . GLY   A 1 105 ? 16.656 6.172   20.450 1.00 32.91 ? 111 GLY   A N   1 
ATOM   825  C  CA  . GLY   A 1 105 ? 17.861 5.486   20.004 1.00 32.62 ? 111 GLY   A CA  1 
ATOM   826  C  C   . GLY   A 1 105 ? 17.691 3.981   19.875 1.00 32.44 ? 111 GLY   A C   1 
ATOM   827  O  O   . GLY   A 1 105 ? 18.503 3.315   19.227 1.00 33.24 ? 111 GLY   A O   1 
ATOM   828  N  N   . GLY   A 1 106 ? 16.637 3.424   20.474 1.00 31.23 ? 112 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 106 ? 16.352 1.995   20.351 1.00 30.11 ? 112 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 106 ? 16.037 1.630   18.912 1.00 28.86 ? 112 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 106 ? 15.364 2.388   18.217 1.00 28.78 ? 112 GLY   A O   1 
ATOM   832  N  N   . ILE   A 1 107 ? 16.559 0.498   18.437 1.00 27.85 ? 113 ILE   A N   1 
ATOM   833  C  CA  . ILE   A 1 107 ? 16.427 0.065   17.058 1.00 27.34 ? 113 ILE   A CA  1 
ATOM   834  C  C   . ILE   A 1 107 ? 15.141 -0.718  16.791 1.00 26.39 ? 113 ILE   A C   1 
ATOM   835  O  O   . ILE   A 1 107 ? 14.736 -1.533  17.628 1.00 27.14 ? 113 ILE   A O   1 
ATOM   836  C  CB  . ILE   A 1 107 ? 17.729 -0.740  16.711 1.00 28.56 ? 113 ILE   A CB  1 
ATOM   837  C  CG1 . ILE   A 1 107 ? 18.861 0.207   16.254 1.00 29.93 ? 113 ILE   A CG1 1 
ATOM   838  C  CG2 . ILE   A 1 107 ? 17.517 -1.879  15.706 1.00 29.09 ? 113 ILE   A CG2 1 
ATOM   839  C  CD1 . ILE   A 1 107 ? 20.218 -0.447  16.266 1.00 31.62 ? 113 ILE   A CD1 1 
ATOM   840  N  N   . LEU   A 1 108 ? 14.508 -0.463  15.633 1.00 25.09 ? 114 LEU   A N   1 
ATOM   841  C  CA  . LEU   A 1 108 ? 13.351 -1.189  15.108 1.00 25.50 ? 114 LEU   A CA  1 
ATOM   842  C  C   . LEU   A 1 108 ? 13.866 -1.993  13.879 1.00 25.89 ? 114 LEU   A C   1 
ATOM   843  O  O   . LEU   A 1 108 ? 14.614 -1.470  13.042 1.00 24.18 ? 114 LEU   A O   1 
ATOM   844  C  CB  . LEU   A 1 108 ? 12.206 -0.231  14.719 1.00 25.93 ? 114 LEU   A CB  1 
ATOM   845  C  CG  . LEU   A 1 108 ? 11.091 -0.789  13.795 1.00 26.74 ? 114 LEU   A CG  1 
ATOM   846  C  CD1 . LEU   A 1 108 ? 10.231 -1.838  14.509 1.00 27.67 ? 114 LEU   A CD1 1 
ATOM   847  C  CD2 . LEU   A 1 108 ? 10.174 0.323   13.348 1.00 26.73 ? 114 LEU   A CD2 1 
ATOM   848  N  N   . ARG   A 1 109 ? 13.540 -3.284  13.841 1.00 27.12 ? 115 ARG   A N   1 
ATOM   849  C  CA  . ARG   A 1 109 ? 14.025 -4.213  12.841 1.00 28.62 ? 115 ARG   A CA  1 
ATOM   850  C  C   . ARG   A 1 109 ? 12.915 -5.104  12.337 1.00 29.97 ? 115 ARG   A C   1 
ATOM   851  O  O   . ARG   A 1 109 ? 12.088 -5.559  13.116 1.00 28.96 ? 115 ARG   A O   1 
ATOM   852  C  CB  . ARG   A 1 109 ? 15.053 -5.166  13.467 1.00 31.00 ? 115 ARG   A CB  1 
ATOM   853  C  CG  . ARG   A 1 109 ? 16.460 -4.646  13.662 1.00 37.55 ? 115 ARG   A CG  1 
ATOM   854  C  CD  . ARG   A 1 109 ? 17.403 -5.764  14.127 1.00 42.63 ? 115 ARG   A CD  1 
ATOM   855  N  NE  . ARG   A 1 109 ? 17.419 -6.861  13.161 1.00 47.59 ? 115 ARG   A NE  1 
ATOM   856  C  CZ  . ARG   A 1 109 ? 18.213 -6.917  12.094 1.00 49.71 ? 115 ARG   A CZ  1 
ATOM   857  N  NH1 . ARG   A 1 109 ? 18.117 -7.930  11.241 1.00 49.26 ? 115 ARG   A NH1 1 
ATOM   858  N  NH2 . ARG   A 1 109 ? 19.110 -5.963  11.875 1.00 48.77 ? 115 ARG   A NH2 1 
ATOM   859  N  N   . CYS   A 1 110 ? 12.970 -5.440  11.043 1.00 31.56 ? 116 CYS   A N   1 
ATOM   860  C  CA  . CYS   A 1 110 ? 12.075 -6.406  10.413 1.00 33.83 ? 116 CYS   A CA  1 
ATOM   861  C  C   . CYS   A 1 110 ? 12.986 -7.581  9.950  1.00 36.63 ? 116 CYS   A C   1 
ATOM   862  O  O   . CYS   A 1 110 ? 14.167 -7.612  10.321 1.00 36.56 ? 116 CYS   A O   1 
ATOM   863  C  CB  . CYS   A 1 110 ? 11.362 -5.754  9.231  1.00 34.15 ? 116 CYS   A CB  1 
ATOM   864  S  SG  . CYS   A 1 110 ? 12.491 -5.173  7.949  1.00 35.71 ? 116 CYS   A SG  1 
ATOM   865  N  N   . GLN   A 1 111 ? 12.473 -8.521  9.116  1.00 38.83 ? 117 GLN   A N   1 
ATOM   866  C  CA  . GLN   A 1 111 ? 13.278 -9.641  8.605  1.00 41.27 ? 117 GLN   A CA  1 
ATOM   867  C  C   . GLN   A 1 111 ? 14.377 -9.217  7.604  1.00 42.90 ? 117 GLN   A C   1 
ATOM   868  O  O   . GLN   A 1 111 ? 15.265 -10.016 7.304  1.00 43.80 ? 117 GLN   A O   1 
ATOM   869  C  CB  . GLN   A 1 111 ? 12.380 -10.700 7.941  1.00 43.84 ? 117 GLN   A CB  1 
ATOM   870  C  CG  . GLN   A 1 111 ? 11.769 -10.239 6.618  1.00 48.33 ? 117 GLN   A CG  1 
ATOM   871  C  CD  . GLN   A 1 111 ? 10.849 -11.275 6.035  1.00 54.04 ? 117 GLN   A CD  1 
ATOM   872  O  OE1 . GLN   A 1 111 ? 9.627  -11.218 6.215  1.00 56.43 ? 117 GLN   A OE1 1 
ATOM   873  N  NE2 . GLN   A 1 111 ? 11.416 -12.239 5.311  1.00 54.19 ? 117 GLN   A NE2 1 
ATOM   874  N  N   . HIS   A 1 112 ? 14.299 -8.000  7.056  1.00 43.02 ? 118 HIS   A N   1 
ATOM   875  C  CA  . HIS   A 1 112 ? 15.296 -7.536  6.081  1.00 43.23 ? 118 HIS   A CA  1 
ATOM   876  C  C   . HIS   A 1 112 ? 16.393 -6.650  6.667  1.00 41.99 ? 118 HIS   A C   1 
ATOM   877  O  O   . HIS   A 1 112 ? 17.300 -6.255  5.924  1.00 42.77 ? 118 HIS   A O   1 
ATOM   878  C  CB  . HIS   A 1 112 ? 14.643 -6.749  4.946  1.00 45.31 ? 118 HIS   A CB  1 
ATOM   879  C  CG  . HIS   A 1 112 ? 13.393 -7.345  4.382  1.00 50.03 ? 118 HIS   A CG  1 
ATOM   880  N  ND1 . HIS   A 1 112 ? 12.153 -7.012  4.886  1.00 52.69 ? 118 HIS   A ND1 1 
ATOM   881  C  CD2 . HIS   A 1 112 ? 13.228 -8.156  3.312  1.00 52.06 ? 118 HIS   A CD2 1 
ATOM   882  C  CE1 . HIS   A 1 112 ? 11.275 -7.647  4.121  1.00 53.72 ? 118 HIS   A CE1 1 
ATOM   883  N  NE2 . HIS   A 1 112 ? 11.877 -8.370  3.180  1.00 53.58 ? 118 HIS   A NE2 1 
ATOM   884  N  N   . GLY   A 1 113 ? 16.276 -6.274  7.944  1.00 39.58 ? 119 GLY   A N   1 
ATOM   885  C  CA  . GLY   A 1 113 ? 17.265 -5.410  8.567  1.00 38.14 ? 119 GLY   A CA  1 
ATOM   886  C  C   . GLY   A 1 113 ? 16.698 -4.252  9.367  1.00 36.32 ? 119 GLY   A C   1 
ATOM   887  O  O   . GLY   A 1 113 ? 15.581 -4.324  9.873  1.00 35.77 ? 119 GLY   A O   1 
ATOM   888  N  N   . VAL   A 1 114 ? 17.494 -3.184  9.508  1.00 35.28 ? 120 VAL   A N   1 
ATOM   889  C  CA  . VAL   A 1 114 ? 17.143 -2.002  10.286 1.00 34.72 ? 120 VAL   A CA  1 
ATOM   890  C  C   . VAL   A 1 114 ? 16.105 -1.146  9.569  1.00 33.70 ? 120 VAL   A C   1 
ATOM   891  O  O   . VAL   A 1 114 ? 16.316 -0.747  8.422  1.00 33.62 ? 120 VAL   A O   1 
ATOM   892  C  CB  . VAL   A 1 114 ? 18.424 -1.190  10.611 1.00 35.66 ? 120 VAL   A CB  1 
ATOM   893  C  CG1 . VAL   A 1 114 ? 18.094 0.179   11.201 1.00 36.27 ? 120 VAL   A CG1 1 
ATOM   894  C  CG2 . VAL   A 1 114 ? 19.337 -1.975  11.544 1.00 36.15 ? 120 VAL   A CG2 1 
ATOM   895  N  N   . VAL   A 1 115 ? 14.995 -0.852  10.252 1.00 32.34 ? 121 VAL   A N   1 
ATOM   896  C  CA  . VAL   A 1 115 ? 13.930 -0.013  9.712  1.00 32.06 ? 121 VAL   A CA  1 
ATOM   897  C  C   . VAL   A 1 115 ? 14.095 1.441   10.177 1.00 31.58 ? 121 VAL   A C   1 
ATOM   898  O  O   . VAL   A 1 115 ? 13.895 2.376   9.399  1.00 31.63 ? 121 VAL   A O   1 
ATOM   899  C  CB  . VAL   A 1 115 ? 12.546 -0.570  10.127 1.00 32.82 ? 121 VAL   A CB  1 
ATOM   900  C  CG1 . VAL   A 1 115 ? 11.415 0.353   9.672  1.00 33.43 ? 121 VAL   A CG1 1 
ATOM   901  C  CG2 . VAL   A 1 115 ? 12.350 -1.974  9.583  1.00 33.15 ? 121 VAL   A CG2 1 
ATOM   902  N  N   . GLY   A 1 116 ? 14.442 1.618   11.448 1.00 30.72 ? 122 GLY   A N   1 
ATOM   903  C  CA  . GLY   A 1 116 ? 14.588 2.948   12.033 1.00 30.07 ? 122 GLY   A CA  1 
ATOM   904  C  C   . GLY   A 1 116 ? 14.894 2.941   13.523 1.00 28.61 ? 122 GLY   A C   1 
ATOM   905  O  O   . GLY   A 1 116 ? 15.264 1.897   14.076 1.00 28.17 ? 122 GLY   A O   1 
ATOM   906  N  N   . ILE   A 1 117 ? 14.815 4.127   14.168 1.00 27.11 ? 123 ILE   A N   1 
ATOM   907  C  CA  . ILE   A 1 117 ? 15.110 4.316   15.599 1.00 26.15 ? 123 ILE   A CA  1 
ATOM   908  C  C   . ILE   A 1 117 ? 13.997 5.075   16.350 1.00 24.59 ? 123 ILE   A C   1 
ATOM   909  O  O   . ILE   A 1 117 ? 13.365 5.958   15.760 1.00 23.07 ? 123 ILE   A O   1 
ATOM   910  C  CB  . ILE   A 1 117 ? 16.487 5.018   15.817 1.00 27.39 ? 123 ILE   A CB  1 
ATOM   911  C  CG1 . ILE   A 1 117 ? 16.651 6.265   14.922 1.00 28.62 ? 123 ILE   A CG1 1 
ATOM   912  C  CG2 . ILE   A 1 117 ? 17.666 4.048   15.649 1.00 28.08 ? 123 ILE   A CG2 1 
ATOM   913  C  CD1 . ILE   A 1 117 ? 17.632 7.313   15.498 1.00 29.86 ? 123 ILE   A CD1 1 
ATOM   914  N  N   . VAL   A 1 118 ? 13.821 4.790   17.684 1.00 24.00 ? 124 VAL   A N   1 
ATOM   915  C  CA  . VAL   A 1 118 ? 12.822 5.472   18.541 1.00 23.90 ? 124 VAL   A CA  1 
ATOM   916  C  C   . VAL   A 1 118 ? 13.122 6.973   18.565 1.00 23.11 ? 124 VAL   A C   1 
ATOM   917  O  O   . VAL   A 1 118 ? 14.284 7.367   18.644 1.00 21.43 ? 124 VAL   A O   1 
ATOM   918  C  CB  . VAL   A 1 118 ? 12.713 4.881   19.978 1.00 25.07 ? 124 VAL   A CB  1 
ATOM   919  C  CG1 . VAL   A 1 118 ? 11.733 5.679   20.837 1.00 25.44 ? 124 VAL   A CG1 1 
ATOM   920  C  CG2 . VAL   A 1 118 ? 12.302 3.402   19.942 1.00 25.91 ? 124 VAL   A CG2 1 
ATOM   921  N  N   . SER   A 1 119 ? 12.082 7.809   18.442 1.00 24.33 ? 125 SER   A N   1 
ATOM   922  C  CA  . SER   A 1 119 ? 12.283 9.245   18.374 1.00 27.02 ? 125 SER   A CA  1 
ATOM   923  C  C   . SER   A 1 119 ? 11.215 10.039  19.142 1.00 29.56 ? 125 SER   A C   1 
ATOM   924  O  O   . SER   A 1 119 ? 11.482 11.180  19.520 1.00 29.15 ? 125 SER   A O   1 
ATOM   925  C  CB  . SER   A 1 119 ? 12.359 9.686   16.906 1.00 28.72 ? 125 SER   A CB  1 
ATOM   926  O  OG  . SER   A 1 119 ? 12.089 11.073  16.739 1.00 30.33 ? 125 SER   A OG  1 
ATOM   927  N  N   . THR   A 1 120 ? 10.011 9.457   19.334 1.00 31.74 ? 126 THR   A N   1 
ATOM   928  C  CA  . THR   A 1 120 ? 8.898  10.051  20.078 1.00 35.17 ? 126 THR   A CA  1 
ATOM   929  C  C   . THR   A 1 120 ? 8.046  8.938   20.744 1.00 38.35 ? 126 THR   A C   1 
ATOM   930  O  O   . THR   A 1 120 ? 8.311  7.761   20.525 1.00 37.87 ? 126 THR   A O   1 
ATOM   931  C  CB  . THR   A 1 120 ? 8.100  11.048  19.218 1.00 37.00 ? 126 THR   A CB  1 
ATOM   932  O  OG1 . THR   A 1 120 ? 7.338  11.879  20.106 1.00 39.39 ? 126 THR   A OG1 1 
ATOM   933  C  CG2 . THR   A 1 120 ? 7.179  10.371  18.233 1.00 36.77 ? 126 THR   A CG2 1 
ATOM   934  N  N   . GLY   A 1 121 ? 7.074  9.305   21.572 1.00 40.88 ? 127 GLY   A N   1 
ATOM   935  C  CA  . GLY   A 1 121 ? 6.210  8.342   22.246 1.00 44.09 ? 127 GLY   A CA  1 
ATOM   936  C  C   . GLY   A 1 121 ? 5.333  8.954   23.327 1.00 47.36 ? 127 GLY   A C   1 
ATOM   937  O  O   . GLY   A 1 121 ? 5.286  10.177  23.480 1.00 47.55 ? 127 GLY   A O   1 
ATOM   938  N  N   . GLY   A 1 122 ? 4.643  8.099   24.075 1.00 49.74 ? 128 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 122 ? 3.739  8.510   25.147 1.00 52.45 ? 128 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 122 ? 2.308  8.048   24.924 1.00 54.93 ? 128 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 122 ? 1.963  7.612   23.826 1.00 56.23 ? 128 GLY   A O   1 
ATOM   942  N  N   . ASN   A 1 123 ? 1.479  8.093   25.965 1.00 55.41 ? 129 ASN   A N   1 
ATOM   943  C  CA  . ASN   A 1 123 ? 0.060  7.697   25.935 1.00 56.03 ? 129 ASN   A CA  1 
ATOM   944  C  C   . ASN   A 1 123 ? -0.203 6.247   25.486 1.00 54.52 ? 129 ASN   A C   1 
ATOM   945  O  O   . ASN   A 1 123 ? -1.331 5.920   25.116 1.00 55.62 ? 129 ASN   A O   1 
ATOM   946  C  CB  . ASN   A 1 123 ? -0.761 8.673   25.087 1.00 58.97 ? 129 ASN   A CB  1 
ATOM   947  C  CG  . ASN   A 1 123 ? -0.875 10.028  25.718 1.00 64.52 ? 129 ASN   A CG  1 
ATOM   948  O  OD1 . ASN   A 1 123 ? -1.189 10.147  26.914 1.00 65.99 ? 129 ASN   A OD1 1 
ATOM   949  N  ND2 . ASN   A 1 123 ? -0.637 11.079  24.927 1.00 66.00 ? 129 ASN   A ND2 1 
ATOM   950  N  N   . GLY   A 1 124 ? 0.799  5.389   25.590 1.00 51.44 ? 130 GLY   A N   1 
ATOM   951  C  CA  . GLY   A 1 124 ? 0.667  4.008   25.153 1.00 49.72 ? 130 GLY   A CA  1 
ATOM   952  C  C   . GLY   A 1 124 ? 1.078  3.808   23.701 1.00 47.86 ? 130 GLY   A C   1 
ATOM   953  O  O   . GLY   A 1 124 ? 0.755  2.782   23.103 1.00 48.06 ? 130 GLY   A O   1 
ATOM   954  N  N   . LEU   A 1 125 ? 1.811  4.775   23.119 1.00 45.83 ? 131 LEU   A N   1 
ATOM   955  C  CA  . LEU   A 1 125 ? 2.277  4.756   21.741 1.00 44.68 ? 131 LEU   A CA  1 
ATOM   956  C  C   . LEU   A 1 125 ? 3.788  5.007   21.662 1.00 42.66 ? 131 LEU   A C   1 
ATOM   957  O  O   . LEU   A 1 125 ? 4.375  5.538   22.607 1.00 43.86 ? 131 LEU   A O   1 
ATOM   958  C  CB  . LEU   A 1 125 ? 1.532  5.836   20.928 1.00 45.39 ? 131 LEU   A CB  1 
ATOM   959  C  CG  . LEU   A 1 125 ? 0.017  5.623   20.822 1.00 47.42 ? 131 LEU   A CG  1 
ATOM   960  C  CD1 . LEU   A 1 125 ? -0.697 6.886   20.476 1.00 47.73 ? 131 LEU   A CD1 1 
ATOM   961  C  CD2 . LEU   A 1 125 ? -0.304 4.515   19.838 1.00 48.18 ? 131 LEU   A CD2 1 
ATOM   962  N  N   . VAL   A 1 126 ? 4.414  4.604   20.541 1.00 39.12 ? 132 VAL   A N   1 
ATOM   963  C  CA  . VAL   A 1 126 ? 5.827  4.818   20.274 1.00 36.46 ? 132 VAL   A CA  1 
ATOM   964  C  C   . VAL   A 1 126 ? 6.014  5.268   18.811 1.00 34.83 ? 132 VAL   A C   1 
ATOM   965  O  O   . VAL   A 1 126 ? 5.337  4.757   17.912 1.00 34.78 ? 132 VAL   A O   1 
ATOM   966  C  CB  . VAL   A 1 126 ? 6.696  3.588   20.679 1.00 35.68 ? 132 VAL   A CB  1 
ATOM   967  C  CG1 . VAL   A 1 126 ? 6.160  2.294   20.094 1.00 35.75 ? 132 VAL   A CG1 1 
ATOM   968  C  CG2 . VAL   A 1 126 ? 8.165  3.786   20.333 1.00 35.29 ? 132 VAL   A CG2 1 
ATOM   969  N  N   . GLY   A 1 127 ? 6.889  6.253   18.604 1.00 33.22 ? 133 GLY   A N   1 
ATOM   970  C  CA  . GLY   A 1 127 ? 7.241  6.816   17.309 1.00 31.88 ? 133 GLY   A CA  1 
ATOM   971  C  C   . GLY   A 1 127 ? 8.659  6.490   16.856 1.00 30.92 ? 133 GLY   A C   1 
ATOM   972  O  O   . GLY   A 1 127 ? 9.614  6.613   17.636 1.00 30.93 ? 133 GLY   A O   1 
ATOM   973  N  N   . PHE   A 1 128 ? 8.798  6.048   15.583 1.00 29.18 ? 134 PHE   A N   1 
ATOM   974  C  CA  . PHE   A 1 128 ? 10.062 5.631   14.956 1.00 27.69 ? 134 PHE   A CA  1 
ATOM   975  C  C   . PHE   A 1 128 ? 10.415 6.481   13.716 1.00 26.55 ? 134 PHE   A C   1 
ATOM   976  O  O   . PHE   A 1 128 ? 9.624  6.600   12.788 1.00 26.50 ? 134 PHE   A O   1 
ATOM   977  C  CB  . PHE   A 1 128 ? 10.023 4.134   14.551 1.00 27.03 ? 134 PHE   A CB  1 
ATOM   978  C  CG  . PHE   A 1 128 ? 9.601  3.128   15.612 1.00 27.25 ? 134 PHE   A CG  1 
ATOM   979  C  CD1 . PHE   A 1 128 ? 10.506 2.665   16.553 1.00 27.37 ? 134 PHE   A CD1 1 
ATOM   980  C  CD2 . PHE   A 1 128 ? 8.329  2.574   15.602 1.00 27.95 ? 134 PHE   A CD2 1 
ATOM   981  C  CE1 . PHE   A 1 128 ? 10.128 1.722   17.503 1.00 28.04 ? 134 PHE   A CE1 1 
ATOM   982  C  CE2 . PHE   A 1 128 ? 7.951  1.632   16.558 1.00 28.36 ? 134 PHE   A CE2 1 
ATOM   983  C  CZ  . PHE   A 1 128 ? 8.849  1.219   17.510 1.00 27.88 ? 134 PHE   A CZ  1 
ATOM   984  N  N   . ALA   A 1 129 ? 11.625 7.051   13.701 1.00 25.73 ? 135 ALA   A N   1 
ATOM   985  C  CA  . ALA   A 1 129 ? 12.151 7.815   12.578 1.00 25.99 ? 135 ALA   A CA  1 
ATOM   986  C  C   . ALA   A 1 129 ? 12.664 6.843   11.498 1.00 27.28 ? 135 ALA   A C   1 
ATOM   987  O  O   . ALA   A 1 129 ? 13.689 6.192   11.700 1.00 26.71 ? 135 ALA   A O   1 
ATOM   988  C  CB  . ALA   A 1 129 ? 13.290 8.710   13.053 1.00 26.06 ? 135 ALA   A CB  1 
ATOM   989  N  N   . ASP   A 1 130 ? 11.946 6.724   10.366 1.00 28.95 ? 136 ASP   A N   1 
ATOM   990  C  CA  . ASP   A 1 130 ? 12.319 5.806   9.272  1.00 30.53 ? 136 ASP   A CA  1 
ATOM   991  C  C   . ASP   A 1 130 ? 13.677 6.135   8.648  1.00 31.85 ? 136 ASP   A C   1 
ATOM   992  O  O   . ASP   A 1 130 ? 14.013 7.311   8.581  1.00 32.34 ? 136 ASP   A O   1 
ATOM   993  C  CB  . ASP   A 1 130 ? 11.235 5.871   8.200  1.00 32.11 ? 136 ASP   A CB  1 
ATOM   994  C  CG  . ASP   A 1 130 ? 11.375 4.844   7.106  1.00 36.96 ? 136 ASP   A CG  1 
ATOM   995  O  OD1 . ASP   A 1 130 ? 11.453 3.636   7.430  1.00 36.23 ? 136 ASP   A OD1 1 
ATOM   996  O  OD2 . ASP   A 1 130 ? 11.387 5.244   5.918  1.00 40.84 ? 136 ASP   A OD2 1 
ATOM   997  N  N   . VAL   A 1 131 ? 14.467 5.109   8.219  1.00 32.29 ? 137 VAL   A N   1 
ATOM   998  C  CA  . VAL   A 1 131 ? 15.759 5.297   7.515  1.00 32.92 ? 137 VAL   A CA  1 
ATOM   999  C  C   . VAL   A 1 131 ? 15.832 4.523   6.158  1.00 33.12 ? 137 VAL   A C   1 
ATOM   1000 O  O   . VAL   A 1 131 ? 16.850 4.602   5.458  1.00 32.99 ? 137 VAL   A O   1 
ATOM   1001 C  CB  . VAL   A 1 131 ? 17.018 4.972   8.375  1.00 33.45 ? 137 VAL   A CB  1 
ATOM   1002 C  CG1 . VAL   A 1 131 ? 17.081 5.828   9.636  1.00 34.49 ? 137 VAL   A CG1 1 
ATOM   1003 C  CG2 . VAL   A 1 131 ? 17.112 3.477   8.702  1.00 33.17 ? 137 VAL   A CG2 1 
ATOM   1004 N  N   . ARG   A 1 132 ? 14.787 3.751   5.808  1.00 32.85 ? 138 ARG   A N   1 
ATOM   1005 C  CA  . ARG   A 1 132 ? 14.802 2.918   4.603  1.00 33.64 ? 138 ARG   A CA  1 
ATOM   1006 C  C   . ARG   A 1 132 ? 14.911 3.688   3.257  1.00 34.34 ? 138 ARG   A C   1 
ATOM   1007 O  O   . ARG   A 1 132 ? 15.359 3.093   2.283  1.00 34.19 ? 138 ARG   A O   1 
ATOM   1008 C  CB  . ARG   A 1 132 ? 13.596 1.963   4.582  1.00 33.50 ? 138 ARG   A CB  1 
ATOM   1009 C  CG  . ARG   A 1 132 ? 13.519 1.077   5.801  1.00 32.78 ? 138 ARG   A CG  1 
ATOM   1010 C  CD  . ARG   A 1 132 ? 12.259 0.238   5.760  1.00 33.14 ? 138 ARG   A CD  1 
ATOM   1011 N  NE  . ARG   A 1 132 ? 11.096 1.050   6.124  1.00 33.04 ? 138 ARG   A NE  1 
ATOM   1012 C  CZ  . ARG   A 1 132 ? 9.852  0.595   6.174  1.00 31.48 ? 138 ARG   A CZ  1 
ATOM   1013 N  NH1 . ARG   A 1 132 ? 9.587  -0.669  5.862  1.00 30.83 ? 138 ARG   A NH1 1 
ATOM   1014 N  NH2 . ARG   A 1 132 ? 8.859  1.401   6.529  1.00 27.95 ? 138 ARG   A NH2 1 
ATOM   1015 N  N   . ASP   A 1 133 ? 14.589 4.996   3.223  1.00 35.05 ? 139 ASP   A N   1 
ATOM   1016 C  CA  . ASP   A 1 133 ? 14.678 5.824   2.006  1.00 36.43 ? 139 ASP   A CA  1 
ATOM   1017 C  C   . ASP   A 1 133 ? 16.080 6.417   1.746  1.00 37.60 ? 139 ASP   A C   1 
ATOM   1018 O  O   . ASP   A 1 133 ? 16.372 6.860   0.617  1.00 38.11 ? 139 ASP   A O   1 
ATOM   1019 C  CB  . ASP   A 1 133 ? 13.640 6.957   2.052  1.00 37.68 ? 139 ASP   A CB  1 
ATOM   1020 C  CG  . ASP   A 1 133 ? 13.863 7.957   3.173  1.00 40.75 ? 139 ASP   A CG  1 
ATOM   1021 O  OD1 . ASP   A 1 133 ? 14.129 7.520   4.321  1.00 41.86 ? 139 ASP   A OD1 1 
ATOM   1022 O  OD2 . ASP   A 1 133 ? 13.754 9.172   2.911  1.00 41.78 ? 139 ASP   A OD2 1 
ATOM   1023 N  N   . LEU   A 1 134 ? 16.941 6.450   2.782  1.00 37.53 ? 140 LEU   A N   1 
ATOM   1024 C  CA  . LEU   A 1 134 ? 18.294 7.009   2.642  1.00 37.71 ? 140 LEU   A CA  1 
ATOM   1025 C  C   . LEU   A 1 134 ? 19.225 5.973   1.995  1.00 38.60 ? 140 LEU   A C   1 
ATOM   1026 O  O   . LEU   A 1 134 ? 19.996 5.322   2.702  1.00 38.23 ? 140 LEU   A O   1 
ATOM   1027 C  CB  . LEU   A 1 134 ? 18.845 7.455   4.009  1.00 37.36 ? 140 LEU   A CB  1 
ATOM   1028 C  CG  . LEU   A 1 134 ? 17.914 8.333   4.851  1.00 37.89 ? 140 LEU   A CG  1 
ATOM   1029 C  CD1 . LEU   A 1 134 ? 18.384 8.424   6.292  1.00 37.91 ? 140 LEU   A CD1 1 
ATOM   1030 C  CD2 . LEU   A 1 134 ? 17.725 9.690   4.222  1.00 38.34 ? 140 LEU   A CD2 1 
ATOM   1031 N  N   . LEU   A 1 135 ? 19.155 5.823   0.648  1.00 39.81 ? 141 LEU   A N   1 
ATOM   1032 C  CA  . LEU   A 1 135 ? 19.939 4.813   -0.077 1.00 41.65 ? 141 LEU   A CA  1 
ATOM   1033 C  C   . LEU   A 1 135 ? 21.452 5.040   -0.051 1.00 44.09 ? 141 LEU   A C   1 
ATOM   1034 O  O   . LEU   A 1 135 ? 22.205 4.074   -0.238 1.00 44.69 ? 141 LEU   A O   1 
ATOM   1035 C  CB  . LEU   A 1 135 ? 19.466 4.656   -1.539 1.00 41.76 ? 141 LEU   A CB  1 
ATOM   1036 C  CG  . LEU   A 1 135 ? 17.963 4.598   -1.812 1.00 42.45 ? 141 LEU   A CG  1 
ATOM   1037 C  CD1 . LEU   A 1 135 ? 17.697 4.395   -3.288 1.00 42.36 ? 141 LEU   A CD1 1 
ATOM   1038 C  CD2 . LEU   A 1 135 ? 17.290 3.523   -0.991 1.00 43.60 ? 141 LEU   A CD2 1 
ATOM   1039 N  N   . TRP   A 1 136 ? 21.901 6.306   0.161  1.00 44.88 ? 142 TRP   A N   1 
ATOM   1040 C  CA  . TRP   A 1 136 ? 23.327 6.679   0.174  1.00 46.11 ? 142 TRP   A CA  1 
ATOM   1041 C  C   . TRP   A 1 136 ? 24.131 6.084   1.335  1.00 48.80 ? 142 TRP   A C   1 
ATOM   1042 O  O   . TRP   A 1 136 ? 25.361 6.084   1.297  1.00 48.71 ? 142 TRP   A O   1 
ATOM   1043 C  CB  . TRP   A 1 136 ? 23.520 8.198   0.117  1.00 45.40 ? 142 TRP   A CB  1 
ATOM   1044 C  CG  . TRP   A 1 136 ? 22.749 8.981   1.144  1.00 44.97 ? 142 TRP   A CG  1 
ATOM   1045 C  CD1 . TRP   A 1 136 ? 21.511 9.534   0.995  1.00 45.41 ? 142 TRP   A CD1 1 
ATOM   1046 C  CD2 . TRP   A 1 136 ? 23.204 9.362   2.450  1.00 44.62 ? 142 TRP   A CD2 1 
ATOM   1047 N  NE1 . TRP   A 1 136 ? 21.165 10.230  2.130  1.00 45.49 ? 142 TRP   A NE1 1 
ATOM   1048 C  CE2 . TRP   A 1 136 ? 22.182 10.132  3.042  1.00 45.24 ? 142 TRP   A CE2 1 
ATOM   1049 C  CE3 . TRP   A 1 136 ? 24.367 9.109   3.187  1.00 45.10 ? 142 TRP   A CE3 1 
ATOM   1050 C  CZ2 . TRP   A 1 136 ? 22.295 10.657  4.330  1.00 45.78 ? 142 TRP   A CZ2 1 
ATOM   1051 C  CZ3 . TRP   A 1 136 ? 24.481 9.644   4.458  1.00 45.78 ? 142 TRP   A CZ3 1 
ATOM   1052 C  CH2 . TRP   A 1 136 ? 23.458 10.417  5.011  1.00 45.82 ? 142 TRP   A CH2 1 
ATOM   1053 N  N   . LEU   A 1 137 ? 23.439 5.569   2.363  1.00 50.77 ? 143 LEU   A N   1 
ATOM   1054 C  CA  . LEU   A 1 137 ? 24.072 4.919   3.500  1.00 52.96 ? 143 LEU   A CA  1 
ATOM   1055 C  C   . LEU   A 1 137 ? 24.800 3.633   3.081  1.00 56.62 ? 143 LEU   A C   1 
ATOM   1056 O  O   . LEU   A 1 137 ? 25.743 3.235   3.755  1.00 56.78 ? 143 LEU   A O   1 
ATOM   1057 C  CB  . LEU   A 1 137 ? 22.998 4.582   4.541  1.00 52.29 ? 143 LEU   A CB  1 
ATOM   1058 C  CG  . LEU   A 1 137 ? 22.344 5.779   5.209  1.00 52.61 ? 143 LEU   A CG  1 
ATOM   1059 C  CD1 . LEU   A 1 137 ? 21.169 5.345   6.047  1.00 53.22 ? 143 LEU   A CD1 1 
ATOM   1060 C  CD2 . LEU   A 1 137 ? 23.332 6.526   6.063  1.00 52.60 ? 143 LEU   A CD2 1 
ATOM   1061 N  N   . ASP   A 1 138 ? 24.357 2.987   1.979  1.00 59.42 ? 144 ASP   A N   1 
ATOM   1062 C  CA  . ASP   A 1 138 ? 24.904 1.737   1.461  1.00 62.82 ? 144 ASP   A CA  1 
ATOM   1063 C  C   . ASP   A 1 138 ? 25.954 1.897   0.407  1.00 65.77 ? 144 ASP   A C   1 
ATOM   1064 O  O   . ASP   A 1 138 ? 26.844 1.060   0.328  1.00 66.40 ? 144 ASP   A O   1 
ATOM   1065 C  CB  . ASP   A 1 138 ? 23.784 0.891   0.849  1.00 65.21 ? 144 ASP   A CB  1 
ATOM   1066 C  CG  . ASP   A 1 138 ? 22.959 0.181   1.874  1.00 70.17 ? 144 ASP   A CG  1 
ATOM   1067 O  OD1 . ASP   A 1 138 ? 23.518 -0.195  2.922  1.00 71.00 ? 144 ASP   A OD1 1 
ATOM   1068 O  OD2 . ASP   A 1 138 ? 21.755 -0.003  1.632  1.00 73.14 ? 144 ASP   A OD2 1 
ATOM   1069 N  N   . GLU   A 1 139 ? 25.811 2.898   -0.468 1.00 67.76 ? 145 GLU   A N   1 
ATOM   1070 C  CA  . GLU   A 1 139 ? 26.731 3.089   -1.581 1.00 70.06 ? 145 GLU   A CA  1 
ATOM   1071 C  C   . GLU   A 1 139 ? 28.030 3.779   -1.194 1.00 70.96 ? 145 GLU   A C   1 
ATOM   1072 O  O   . GLU   A 1 139 ? 29.029 3.607   -1.892 1.00 71.54 ? 145 GLU   A O   1 
ATOM   1073 C  CB  . GLU   A 1 139 ? 26.039 3.839   -2.725 1.00 73.85 ? 145 GLU   A CB  1 
ATOM   1074 C  CG  . GLU   A 1 139 ? 25.492 5.188   -2.298 1.00 80.96 ? 145 GLU   A CG  1 
ATOM   1075 C  CD  . GLU   A 1 139 ? 24.476 5.778   -3.256 1.00 89.64 ? 145 GLU   A CD  1 
ATOM   1076 O  OE1 . GLU   A 1 139 ? 24.388 7.027   -3.333 1.00 90.91 ? 145 GLU   A OE1 1 
ATOM   1077 O  OE2 . GLU   A 1 139 ? 23.766 4.992   -3.927 1.00 92.46 ? 145 GLU   A OE2 1 
HETATM 1078 N  N1  . A1BR0 B 2 .   ? 9.904  14.157  22.765 1.00 45.94 ? 201 A1BR0 A N1  1 
HETATM 1079 C  C4  . A1BR0 B 2 .   ? 10.948 14.856  23.531 1.00 45.07 ? 201 A1BR0 A C4  1 
HETATM 1080 C  C5  . A1BR0 B 2 .   ? 9.127  13.154  23.229 1.00 47.37 ? 201 A1BR0 A C5  1 
HETATM 1081 C  C6  . A1BR0 B 2 .   ? 9.344  12.721  24.667 1.00 48.78 ? 201 A1BR0 A C6  1 
HETATM 1082 C  C7  . A1BR0 B 2 .   ? 9.107  11.236  24.828 1.00 49.87 ? 201 A1BR0 A C7  1 
HETATM 1083 C  C8  . A1BR0 B 2 .   ? 8.077  10.791  25.655 1.00 50.07 ? 201 A1BR0 A C8  1 
HETATM 1084 C  C10 . A1BR0 B 2 .   ? 8.473  8.511   25.005 1.00 50.15 ? 201 A1BR0 A C10 1 
HETATM 1085 C  C13 . A1BR0 B 2 .   ? 9.795  14.619  21.379 1.00 44.88 ? 201 A1BR0 A C13 1 
HETATM 1086 CL CL1 . A1BR0 B 2 .   ? 11.139 10.796  23.103 1.00 51.97 ? 201 A1BR0 A CL1 1 
HETATM 1087 C  C12 . A1BR0 B 2 .   ? 9.835  10.284  24.111 1.00 50.63 ? 201 A1BR0 A C12 1 
HETATM 1088 C  C11 . A1BR0 B 2 .   ? 9.516  8.935   24.204 1.00 49.99 ? 201 A1BR0 A C11 1 
HETATM 1089 CL CL  . A1BR0 B 2 .   ? 10.448 7.749   23.347 1.00 49.74 ? 201 A1BR0 A CL  1 
HETATM 1090 C  C9  . A1BR0 B 2 .   ? 7.761  9.444   25.740 1.00 50.22 ? 201 A1BR0 A C9  1 
HETATM 1091 O  O1  . A1BR0 B 2 .   ? 8.316  12.576  22.516 1.00 47.19 ? 201 A1BR0 A O1  1 
HETATM 1092 C  C3  . A1BR0 B 2 .   ? 12.309 14.695  22.861 1.00 44.46 ? 201 A1BR0 A C3  1 
HETATM 1093 C  C2  . A1BR0 B 2 .   ? 12.247 15.070  21.374 1.00 43.98 ? 201 A1BR0 A C2  1 
HETATM 1094 C  C1  . A1BR0 B 2 .   ? 11.108 14.339  20.643 1.00 43.80 ? 201 A1BR0 A C1  1 
HETATM 1095 C  C   . A1BR0 B 2 .   ? 11.039 14.731  19.176 1.00 42.48 ? 201 A1BR0 A C   1 
HETATM 1096 O  O   . A1BR0 B 2 .   ? 10.704 15.869  18.835 1.00 41.69 ? 201 A1BR0 A O   1 
HETATM 1097 N  N   . A1BR0 B 2 .   ? 11.354 13.783  18.308 1.00 41.74 ? 201 A1BR0 A N   1 
HETATM 1098 ZN ZN  . ZN    C 3 .   ? 11.161 -5.428  5.759  1.00 41.14 2 202 ZN    A ZN  1 
HETATM 1099 S  S   . DMS   D 4 .   ? 20.168 -0.951  20.346 0.00 32.71 ? 203 DMS   A S   1 
HETATM 1100 O  O   . DMS   D 4 .   ? 18.688 -0.943  20.101 0.00 17.46 ? 203 DMS   A O   1 
HETATM 1101 C  C1  . DMS   D 4 .   ? 20.427 -0.732  22.127 0.00 31.57 ? 203 DMS   A C1  1 
HETATM 1102 C  C2  . DMS   D 4 .   ? 20.808 0.676   19.867 0.00 31.97 ? 203 DMS   A C2  1 
HETATM 1103 O  O   . HOH   E 5 .   ? 20.201 8.373   19.350 1.00 27.93 ? 301 HOH   A O   1 
HETATM 1104 O  O   . HOH   E 5 .   ? 23.214 -1.993  4.639  1.00 43.42 ? 302 HOH   A O   1 
HETATM 1105 O  O   . HOH   E 5 .   ? 8.323  19.635  18.274 1.00 43.14 ? 303 HOH   A O   1 
HETATM 1106 O  O   . HOH   E 5 .   ? 8.110  -4.456  0.681  1.00 44.99 ? 304 HOH   A O   1 
HETATM 1107 O  O   . HOH   E 5 .   ? 9.197  1.795   2.976  1.00 40.18 ? 305 HOH   A O   1 
HETATM 1108 O  O   . HOH   E 5 .   ? 31.091 20.513  11.170 1.00 39.09 ? 306 HOH   A O   1 
HETATM 1109 O  O   . HOH   E 5 .   ? 20.098 22.401  7.889  1.00 31.47 ? 307 HOH   A O   1 
HETATM 1110 O  O   . HOH   E 5 .   ? 10.485 7.533   5.020  1.00 50.66 ? 308 HOH   A O   1 
HETATM 1111 O  O   . HOH   E 5 .   ? 17.992 2.159   23.492 1.00 35.68 ? 309 HOH   A O   1 
HETATM 1112 O  O   . HOH   E 5 .   ? 17.983 20.770  10.003 1.00 47.26 ? 310 HOH   A O   1 
HETATM 1113 O  O   . HOH   E 5 .   ? 10.491 4.301   3.569  1.00 38.87 ? 311 HOH   A O   1 
HETATM 1114 O  O   . HOH   E 5 .   ? 15.375 1.931   23.632 1.00 34.43 ? 312 HOH   A O   1 
HETATM 1115 O  O   . HOH   E 5 .   ? 11.378 11.149  11.569 1.00 26.44 ? 313 HOH   A O   1 
HETATM 1116 O  O   . HOH   E 5 .   ? 11.409 1.353   34.110 1.00 38.93 ? 314 HOH   A O   1 
HETATM 1117 O  O   . HOH   E 5 .   ? 24.050 21.697  7.901  1.00 49.26 ? 315 HOH   A O   1 
HETATM 1118 O  O   . HOH   E 5 .   ? 30.620 10.872  19.258 1.00 43.60 ? 316 HOH   A O   1 
HETATM 1119 O  O   . HOH   E 5 .   ? 16.912 23.202  14.433 1.00 49.76 ? 317 HOH   A O   1 
HETATM 1120 O  O   . HOH   E 5 .   ? 9.554  18.092  20.054 1.00 36.84 ? 318 HOH   A O   1 
HETATM 1121 O  O   . HOH   E 5 .   ? 13.210 9.793   9.570  1.00 22.40 ? 319 HOH   A O   1 
HETATM 1122 O  O   . HOH   E 5 .   ? 0.260  0.613   24.789 1.00 43.09 ? 320 HOH   A O   1 
HETATM 1123 O  O   . HOH   E 5 .   ? 18.099 18.572  17.164 1.00 34.22 ? 321 HOH   A O   1 
HETATM 1124 O  O   . HOH   E 5 .   ? 31.308 20.262  16.941 1.00 40.60 ? 322 HOH   A O   1 
HETATM 1125 O  O   . HOH   E 5 .   ? 23.070 18.133  20.244 1.00 55.84 ? 323 HOH   A O   1 
HETATM 1126 O  O   . HOH   E 5 .   ? 10.034 3.437   34.377 1.00 38.06 ? 324 HOH   A O   1 
HETATM 1127 O  O   . HOH   E 5 .   ? 7.044  2.735   33.433 1.00 42.57 ? 325 HOH   A O   1 
HETATM 1128 O  O   . HOH   E 5 .   ? 30.611 4.243   4.168  1.00 55.94 ? 326 HOH   A O   1 
HETATM 1129 O  O   . HOH   E 5 .   ? 16.152 -11.931 5.306  1.00 55.85 ? 327 HOH   A O   1 
HETATM 1130 O  O   . HOH   E 5 .   ? 5.560  -2.383  24.760 1.00 34.72 ? 328 HOH   A O   1 
HETATM 1131 O  O   . HOH   E 5 .   ? 4.958  7.079   28.645 1.00 43.43 ? 329 HOH   A O   1 
HETATM 1132 O  O   . HOH   E 5 .   ? 0.307  -1.013  16.811 1.00 32.24 ? 330 HOH   A O   1 
HETATM 1133 O  O   . HOH   E 5 .   ? 6.614  -6.595  29.672 1.00 49.15 ? 331 HOH   A O   1 
HETATM 1134 O  O   . HOH   E 5 .   ? 19.029 12.282  2.018  1.00 48.53 ? 332 HOH   A O   1 
HETATM 1135 O  O   . HOH   E 5 .   ? 15.012 -5.391  17.406 1.00 32.27 ? 333 HOH   A O   1 
HETATM 1136 O  O   . HOH   E 5 .   ? 11.170 16.351  5.182  1.00 58.36 ? 334 HOH   A O   1 
HETATM 1137 O  O   . HOH   E 5 .   ? 1.797  -2.816  17.828 1.00 38.72 ? 335 HOH   A O   1 
HETATM 1138 O  O   . HOH   E 5 .   ? 24.954 6.513   20.677 1.00 60.44 ? 336 HOH   A O   1 
HETATM 1139 O  O   . HOH   E 5 .   ? 7.208  25.694  14.137 1.00 44.21 ? 337 HOH   A O   1 
HETATM 1140 O  O   . HOH   E 5 .   ? 4.942  -2.005  29.823 1.00 49.71 ? 338 HOH   A O   1 
HETATM 1141 O  O   . HOH   E 5 .   ? 9.403  -8.594  9.464  1.00 52.47 ? 339 HOH   A O   1 
HETATM 1142 O  O   . HOH   E 5 .   ? 14.527 14.126  3.778  1.00 44.49 ? 340 HOH   A O   1 
HETATM 1143 O  O   . HOH   E 5 .   ? 5.791  1.026   6.234  1.00 54.06 ? 341 HOH   A O   1 
HETATM 1144 O  O   . HOH   E 5 .   ? 22.050 -6.256  10.729 1.00 38.97 ? 342 HOH   A O   1 
HETATM 1145 O  O   . HOH   E 5 .   ? 14.917 11.940  24.476 1.00 45.41 ? 343 HOH   A O   1 
HETATM 1146 O  O   . HOH   E 5 .   ? 13.124 -4.010  5.017  1.00 46.23 ? 344 HOH   A O   1 
HETATM 1147 O  O   . HOH   E 5 .   ? 4.368  -6.418  6.808  1.00 40.99 ? 345 HOH   A O   1 
HETATM 1148 O  O   . HOH   E 5 .   ? 12.246 -8.699  13.537 1.00 54.08 ? 346 HOH   A O   1 
HETATM 1149 O  O   . HOH   E 5 .   ? 19.627 23.668  15.622 1.00 28.26 ? 347 HOH   A O   1 
HETATM 1150 O  O   . HOH   E 5 .   ? 22.144 8.410   21.531 1.00 38.04 ? 348 HOH   A O   1 
HETATM 1151 O  O   . HOH   E 5 .   ? 22.489 18.642  5.935  1.00 29.45 ? 349 HOH   A O   1 
HETATM 1152 O  O   . HOH   E 5 .   ? 16.065 -5.524  2.168  1.00 36.44 ? 350 HOH   A O   1 
HETATM 1153 O  O   . HOH   E 5 .   ? 3.891  -3.420  22.105 1.00 63.12 ? 351 HOH   A O   1 
HETATM 1154 O  O   . HOH   E 5 .   ? 7.239  -5.879  2.867  1.00 54.59 ? 352 HOH   A O   1 
HETATM 1155 O  O   . HOH   E 5 .   ? 12.046 13.309  1.448  1.00 51.53 ? 353 HOH   A O   1 
HETATM 1156 O  O   . HOH   E 5 .   ? 9.405  20.990  10.748 1.00 50.01 ? 354 HOH   A O   1 
HETATM 1157 O  O   . HOH   E 5 .   ? 11.692 20.975  12.146 1.00 35.03 ? 355 HOH   A O   1 
HETATM 1158 O  O   . HOH   E 5 .   ? 28.595 22.044  18.956 1.00 41.45 ? 356 HOH   A O   1 
HETATM 1159 O  O   . HOH   E 5 .   ? 1.916  12.427  5.219  1.00 56.37 ? 357 HOH   A O   1 
HETATM 1160 O  O   . HOH   E 5 .   ? 36.982 6.319   6.921  1.00 49.69 ? 358 HOH   A O   1 
HETATM 1161 O  O   . HOH   E 5 .   ? 0.714  -4.790  17.646 1.00 43.85 ? 359 HOH   A O   1 
HETATM 1162 O  O   . HOH   E 5 .   ? 3.817  11.774  19.237 1.00 43.91 ? 360 HOH   A O   1 
HETATM 1163 O  O   . HOH   E 5 .   ? 20.707 22.023  18.117 1.00 46.84 ? 361 HOH   A O   1 
HETATM 1164 O  O   . HOH   E 5 .   ? -1.894 7.035   28.789 1.00 46.75 ? 362 HOH   A O   1 
HETATM 1165 O  O   . HOH   E 5 .   ? 13.881 13.520  26.384 1.00 51.47 ? 363 HOH   A O   1 
HETATM 1166 O  O   . HOH   E 5 .   ? 1.948  1.194   27.532 1.00 39.09 ? 364 HOH   A O   1 
HETATM 1167 O  O   . HOH   E 5 .   ? 11.740 23.057  13.953 1.00 46.28 ? 365 HOH   A O   1 
HETATM 1168 O  O   . HOH   E 5 .   ? 8.856  6.700   2.553  1.00 50.44 ? 366 HOH   A O   1 
HETATM 1169 O  O   . HOH   E 5 .   ? 9.550  -9.632  12.838 1.00 41.59 ? 367 HOH   A O   1 
HETATM 1170 O  O   . HOH   E 5 .   ? 9.577  24.682  13.532 1.00 51.94 ? 368 HOH   A O   1 
HETATM 1171 O  O   . HOH   E 5 .   ? 10.252 14.478  28.557 1.00 56.07 ? 369 HOH   A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . SER   A 1   ? 0.8980 0.5360 0.4354 -0.0574 -0.2131 0.0094  7   SER   A N   
2    C  CA  . SER   A 1   ? 0.8474 0.5401 0.4910 -0.0536 -0.2391 0.0229  7   SER   A CA  
3    C  C   . SER   A 1   ? 0.7685 0.5387 0.5133 -0.0347 -0.2205 0.0263  7   SER   A C   
4    O  O   . SER   A 1   ? 0.7663 0.5437 0.4974 -0.0296 -0.2029 0.0226  7   SER   A O   
5    C  CB  . SER   A 1   ? 0.8872 0.5351 0.5269 -0.0820 -0.3046 0.0468  7   SER   A CB  
6    O  OG  . SER   A 1   ? 0.9512 0.5607 0.5490 -0.0990 -0.3318 0.0593  7   SER   A OG  
7    N  N   . GLY   A 2   ? 0.7056 0.5259 0.5446 -0.0260 -0.2201 0.0321  8   GLY   A N   
8    C  CA  . GLY   A 2   ? 0.6470 0.5256 0.5720 -0.0116 -0.1957 0.0331  8   GLY   A CA  
9    C  C   . GLY   A 2   ? 0.5917 0.5147 0.5799 0.0006  -0.1682 0.0272  8   GLY   A C   
10   O  O   . GLY   A 2   ? 0.6022 0.5223 0.5612 0.0033  -0.1581 0.0177  8   GLY   A O   
11   N  N   . ALA   A 3   ? 0.5300 0.4878 0.6026 0.0069  -0.1522 0.0329  9   ALA   A N   
12   C  CA  . ALA   A 3   ? 0.4964 0.4855 0.6235 0.0147  -0.1207 0.0277  9   ALA   A CA  
13   C  C   . ALA   A 3   ? 0.4705 0.4823 0.6466 0.0210  -0.0811 0.0234  9   ALA   A C   
14   O  O   . ALA   A 3   ? 0.4592 0.4675 0.6542 0.0207  -0.0837 0.0295  9   ALA   A O   
15   C  CB  . ALA   A 3   ? 0.4751 0.4631 0.6702 0.0093  -0.1463 0.0451  9   ALA   A CB  
16   N  N   . ILE   A 4   ? 0.4604 0.4869 0.6494 0.0240  -0.0434 0.0131  10  ILE   A N   
17   C  CA  . ILE   A 4   ? 0.4561 0.4868 0.6762 0.0250  0.0007  0.0066  10  ILE   A CA  
18   C  C   . ILE   A 4   ? 0.4444 0.4780 0.7582 0.0267  0.0188  0.0173  10  ILE   A C   
19   O  O   . ILE   A 4   ? 0.4350 0.4730 0.7606 0.0259  0.0157  0.0194  10  ILE   A O   
20   C  CB  . ILE   A 4   ? 0.4768 0.5073 0.6276 0.0201  0.0322  -0.0115 10  ILE   A CB  
21   C  CG1 . ILE   A 4   ? 0.4994 0.5330 0.5745 0.0195  0.0132  -0.0169 10  ILE   A CG1 
22   C  CG2 . ILE   A 4   ? 0.4853 0.5021 0.6431 0.0147  0.0769  -0.0202 10  ILE   A CG2 
23   C  CD1 . ILE   A 4   ? 0.5245 0.5620 0.5479 0.0123  0.0309  -0.0256 10  ILE   A CD1 
24   N  N   . TYR   A 5   ? 0.4357 0.4655 0.8229 0.0297  0.0412  0.0253  11  TYR   A N   
25   C  CA  . TYR   A 5   ? 0.4183 0.4496 0.9139 0.0331  0.0677  0.0386  11  TYR   A CA  
26   C  C   . TYR   A 5   ? 0.4427 0.4525 0.9423 0.0324  0.1391  0.0232  11  TYR   A C   
27   O  O   . TYR   A 5   ? 0.4410 0.4398 0.9716 0.0353  0.1600  0.0247  11  TYR   A O   
28   C  CB  . TYR   A 5   ? 0.3812 0.4207 0.9852 0.0366  0.0328  0.0694  11  TYR   A CB  
29   C  CG  . TYR   A 5   ? 0.3874 0.4324 0.9830 0.0299  -0.0389 0.0873  11  TYR   A CG  
30   C  CD1 . TYR   A 5   ? 0.3781 0.4303 1.0213 0.0266  -0.0575 0.1007  11  TYR   A CD1 
31   C  CD2 . TYR   A 5   ? 0.4201 0.4542 0.9503 0.0238  -0.0860 0.0903  11  TYR   A CD2 
32   C  CE1 . TYR   A 5   ? 0.3927 0.4373 1.0140 0.0155  -0.1240 0.1163  11  TYR   A CE1 
33   C  CE2 . TYR   A 5   ? 0.4441 0.4653 0.9456 0.0123  -0.1482 0.1047  11  TYR   A CE2 
34   C  CZ  . TYR   A 5   ? 0.4377 0.4623 0.9823 0.0071  -0.1683 0.1174  11  TYR   A CZ  
35   O  OH  . TYR   A 5   ? 0.4799 0.4803 0.9857 -0.0091 -0.2308 0.1315  11  TYR   A OH  
36   N  N   . VAL   A 6   ? 0.4660 0.4618 0.9253 0.0260  0.1772  0.0083  12  VAL   A N   
37   C  CA  . VAL   A 6   ? 0.4977 0.4546 0.9341 0.0183  0.2491  -0.0088 12  VAL   A CA  
38   C  C   . VAL   A 6   ? 0.4898 0.4347 0.9957 0.0189  0.2924  -0.0034 12  VAL   A C   
39   O  O   . VAL   A 6   ? 0.4964 0.4503 0.9778 0.0150  0.2787  -0.0037 12  VAL   A O   
40   C  CB  . VAL   A 6   ? 0.5608 0.4944 0.8552 0.0013  0.2581  -0.0326 12  VAL   A CB  
41   C  CG1 . VAL   A 6   ? 0.5779 0.5294 0.8133 -0.0037 0.2240  -0.0337 12  VAL   A CG1 
42   C  CG2 . VAL   A 6   ? 0.5993 0.4754 0.8533 -0.0141 0.3311  -0.0499 12  VAL   A CG2 
43   N  N   . GLY   A 7   ? 0.4643 0.3894 1.0687 0.0251  0.3459  0.0041  13  GLY   A N   
44   C  CA  . GLY   A 7   ? 0.4512 0.3623 1.1436 0.0276  0.3978  0.0124  13  GLY   A CA  
45   C  C   . GLY   A 7   ? 0.4146 0.3734 1.2019 0.0363  0.3430  0.0399  13  GLY   A C   
46   O  O   . GLY   A 7   ? 0.3964 0.3913 1.2307 0.0430  0.2761  0.0603  13  GLY   A O   
47   N  N   . ASN   A 8   ? 0.4094 0.3631 1.2030 0.0320  0.3639  0.0394  14  ASN   A N   
48   C  CA  . ASN   A 8   ? 0.3693 0.3634 1.2437 0.0368  0.3103  0.0647  14  ASN   A CA  
49   C  C   . ASN   A 8   ? 0.3798 0.3919 1.1393 0.0299  0.2443  0.0550  14  ASN   A C   
50   O  O   . ASN   A 8   ? 0.3716 0.3969 1.1466 0.0277  0.2232  0.0631  14  ASN   A O   
51   C  CB  . ASN   A 8   ? 0.3708 0.3536 1.3384 0.0377  0.3661  0.0748  14  ASN   A CB  
52   C  CG  . ASN   A 8   ? 0.4026 0.3740 1.5208 0.0484  0.4260  0.0932  14  ASN   A CG  
53   O  OD1 . ASN   A 8   ? 0.4042 0.3988 1.6129 0.0575  0.3943  0.1155  14  ASN   A OD1 
54   N  ND2 . ASN   A 8   ? 0.4129 0.3431 1.5617 0.0466  0.5171  0.0855  14  ASN   A ND2 
55   N  N   . TYR   A 9   ? 0.3907 0.4027 1.0456 0.0272  0.2140  0.0400  15  TYR   A N   
56   C  CA  . TYR   A 9   ? 0.4027 0.4276 0.9562 0.0227  0.1606  0.0315  15  TYR   A CA  
57   C  C   . TYR   A 9   ? 0.3789 0.4190 0.9112 0.0261  0.1014  0.0379  15  TYR   A C   
58   O  O   . TYR   A 9   ? 0.3738 0.4105 0.9247 0.0293  0.1065  0.0398  15  TYR   A O   
59   C  CB  . TYR   A 9   ? 0.4524 0.4543 0.8775 0.0119  0.1885  0.0058  15  TYR   A CB  
60   C  CG  . TYR   A 9   ? 0.4756 0.4513 0.8853 0.0020  0.2395  -0.0018 15  TYR   A CG  
61   C  CD1 . TYR   A 9   ? 0.4730 0.4608 0.9205 0.0030  0.2285  0.0083  15  TYR   A CD1 
62   C  CD2 . TYR   A 9   ? 0.5242 0.4549 0.8667 -0.0120 0.2973  -0.0195 15  TYR   A CD2 
63   C  CE1 . TYR   A 9   ? 0.5055 0.4649 0.9319 -0.0078 0.2763  0.0018  15  TYR   A CE1 
64   C  CE2 . TYR   A 9   ? 0.5650 0.4588 0.8733 -0.0261 0.3445  -0.0267 15  TYR   A CE2 
65   C  CZ  . TYR   A 9   ? 0.5636 0.4738 0.9170 -0.0230 0.3351  -0.0158 15  TYR   A CZ  
66   O  OH  . TYR   A 9   ? 0.6190 0.4887 0.9358 -0.0382 0.3840  -0.0221 15  TYR   A OH  
67   N  N   . ARG   A 10  ? 0.3647 0.4143 0.8502 0.0241  0.0496  0.0400  16  ARG   A N   
68   C  CA  . ARG   A 10  ? 0.3608 0.4111 0.7995 0.0236  -0.0029 0.0430  16  ARG   A CA  
69   C  C   . ARG   A 10  ? 0.3783 0.4244 0.7040 0.0217  -0.0101 0.0245  16  ARG   A C   
70   O  O   . ARG   A 10  ? 0.3828 0.4296 0.6928 0.0200  -0.0139 0.0229  16  ARG   A O   
71   C  CB  . ARG   A 10  ? 0.3510 0.4026 0.8500 0.0192  -0.0590 0.0683  16  ARG   A CB  
72   C  CG  . ARG   A 10  ? 0.4070 0.4410 0.8277 0.0125  -0.1133 0.0690  16  ARG   A CG  
73   C  CD  . ARG   A 10  ? 0.4194 0.4411 0.8911 0.0001  -0.1732 0.0972  16  ARG   A CD  
74   N  NE  . ARG   A 10  ? 0.4807 0.4707 0.8579 -0.0112 -0.2144 0.0924  16  ARG   A NE  
75   C  CZ  . ARG   A 10  ? 0.5376 0.4923 0.8414 -0.0227 -0.2535 0.0946  16  ARG   A CZ  
76   N  NH1 . ARG   A 10  ? 0.5348 0.4880 0.8508 -0.0236 -0.2618 0.1029  16  ARG   A NH1 
77   N  NH2 . ARG   A 10  ? 0.5733 0.4871 0.7845 -0.0343 -0.2799 0.0876  16  ARG   A NH2 
78   N  N   . VAL   A 11  ? 0.3805 0.4231 0.6377 0.0224  -0.0099 0.0132  17  VAL   A N   
79   C  CA  . VAL   A 11  ? 0.3970 0.4384 0.5672 0.0218  -0.0141 0.0011  17  VAL   A CA  
80   C  C   . VAL   A 11  ? 0.4003 0.4301 0.5292 0.0230  -0.0517 0.0035  17  VAL   A C   
81   O  O   . VAL   A 11  ? 0.4098 0.4338 0.5332 0.0230  -0.0605 0.0055  17  VAL   A O   
82   C  CB  . VAL   A 11  ? 0.4209 0.4634 0.5423 0.0181  0.0172  -0.0114 17  VAL   A CB  
83   C  CG1 . VAL   A 11  ? 0.4430 0.4897 0.5012 0.0164  0.0122  -0.0160 17  VAL   A CG1 
84   C  CG2 . VAL   A 11  ? 0.4200 0.4542 0.5671 0.0115  0.0604  -0.0156 17  VAL   A CG2 
85   N  N   . VAL   A 12  ? 0.3961 0.4150 0.4893 0.0228  -0.0696 0.0027  18  VAL   A N   
86   C  CA  . VAL   A 12  ? 0.4136 0.4043 0.4509 0.0209  -0.0968 0.0025  18  VAL   A CA  
87   C  C   . VAL   A 12  ? 0.4216 0.4061 0.4011 0.0258  -0.0839 -0.0069 18  VAL   A C   
88   O  O   . VAL   A 12  ? 0.3996 0.4030 0.3905 0.0287  -0.0663 -0.0089 18  VAL   A O   
89   C  CB  . VAL   A 12  ? 0.4220 0.3855 0.4756 0.0110  -0.1371 0.0151  18  VAL   A CB  
90   C  CG1 . VAL   A 12  ? 0.4149 0.3788 0.5267 0.0045  -0.1604 0.0315  18  VAL   A CG1 
91   C  CG2 . VAL   A 12  ? 0.4110 0.3827 0.5006 0.0103  -0.1365 0.0184  18  VAL   A CG2 
92   N  N   . ASN   A 13  ? 0.4462 0.3982 0.3654 0.0255  -0.0912 -0.0107 19  ASN   A N   
93   C  CA  . ASN   A 13  ? 0.4688 0.4064 0.3450 0.0316  -0.0749 -0.0168 19  ASN   A CA  
94   C  C   . ASN   A 13  ? 0.4822 0.4030 0.3631 0.0283  -0.0871 -0.0153 19  ASN   A C   
95   O  O   . ASN   A 13  ? 0.5016 0.3937 0.3794 0.0173  -0.1166 -0.0109 19  ASN   A O   
96   C  CB  . ASN   A 13  ? 0.5170 0.4067 0.3253 0.0296  -0.0739 -0.0216 19  ASN   A CB  
97   C  CG  . ASN   A 13  ? 0.5368 0.4358 0.3355 0.0311  -0.0646 -0.0221 19  ASN   A CG  
98   O  OD1 . ASN   A 13  ? 0.5549 0.4396 0.3469 0.0226  -0.0855 -0.0188 19  ASN   A OD1 
99   N  ND2 . ASN   A 13  ? 0.5150 0.4376 0.3179 0.0406  -0.0364 -0.0231 19  ASN   A ND2 
100  N  N   . ARG   A 14  ? 0.4736 0.4119 0.3667 0.0355  -0.0691 -0.0158 20  ARG   A N   
101  C  CA  . ARG   A 14  ? 0.4779 0.4011 0.3774 0.0328  -0.0785 -0.0144 20  ARG   A CA  
102  C  C   . ARG   A 14  ? 0.5397 0.3985 0.3778 0.0258  -0.0916 -0.0194 20  ARG   A C   
103  O  O   . ARG   A 14  ? 0.5545 0.3885 0.3927 0.0148  -0.1169 -0.0163 20  ARG   A O   
104  C  CB  . ARG   A 14  ? 0.4508 0.3996 0.3693 0.0412  -0.0569 -0.0118 20  ARG   A CB  
105  C  CG  . ARG   A 14  ? 0.4436 0.3849 0.3795 0.0382  -0.0654 -0.0090 20  ARG   A CG  
106  C  CD  . ARG   A 14  ? 0.4406 0.3948 0.3841 0.0464  -0.0461 -0.0043 20  ARG   A CD  
107  N  NE  . ARG   A 14  ? 0.4359 0.3871 0.3986 0.0438  -0.0517 -0.0005 20  ARG   A NE  
108  C  CZ  . ARG   A 14  ? 0.4610 0.3718 0.4012 0.0442  -0.0556 -0.0038 20  ARG   A CZ  
109  N  NH1 . ARG   A 14  ? 0.4786 0.3398 0.3672 0.0447  -0.0528 -0.0125 20  ARG   A NH1 
110  N  NH2 . ARG   A 14  ? 0.4452 0.3572 0.4071 0.0419  -0.0598 0.0010  20  ARG   A NH2 
111  N  N   . HIS   A 15  ? 0.5800 0.4041 0.3616 0.0290  -0.0738 -0.0264 21  HIS   A N   
112  C  CA  . HIS   A 15  ? 0.6497 0.3931 0.3512 0.0184  -0.0778 -0.0341 21  HIS   A CA  
113  C  C   . HIS   A 15  ? 0.7008 0.3975 0.3584 -0.0043 -0.1193 -0.0312 21  HIS   A C   
114  O  O   . HIS   A 15  ? 0.7507 0.3690 0.3301 -0.0217 -0.1327 -0.0358 21  HIS   A O   
115  C  CB  . HIS   A 15  ? 0.6819 0.3918 0.3369 0.0287  -0.0345 -0.0424 21  HIS   A CB  
116  C  CG  . HIS   A 15  ? 0.7037 0.4124 0.3363 0.0292  -0.0249 -0.0437 21  HIS   A CG  
117  N  ND1 . HIS   A 15  ? 0.6703 0.4481 0.3630 0.0416  -0.0133 -0.0371 21  HIS   A ND1 
118  C  CD2 . HIS   A 15  ? 0.7654 0.4055 0.3156 0.0159  -0.0256 -0.0503 21  HIS   A CD2 
119  C  CE1 . HIS   A 15  ? 0.6998 0.4559 0.3546 0.0383  -0.0066 -0.0398 21  HIS   A CE1 
120  N  NE2 . HIS   A 15  ? 0.7583 0.4321 0.3267 0.0232  -0.0129 -0.0476 21  HIS   A NE2 
121  N  N   . LEU   A 16  ? 0.6837 0.4229 0.3919 -0.0067 -0.1415 -0.0214 22  LEU   A N   
122  C  CA  . LEU   A 16  ? 0.7185 0.4231 0.4076 -0.0285 -0.1873 -0.0109 22  LEU   A CA  
123  C  C   . LEU   A 16  ? 0.7021 0.4438 0.4804 -0.0356 -0.2238 0.0068  22  LEU   A C   
124  O  O   . LEU   A 16  ? 0.7086 0.4372 0.5032 -0.0521 -0.2649 0.0229  22  LEU   A O   
125  C  CB  . LEU   A 16  ? 0.7145 0.4328 0.4000 -0.0257 -0.1821 -0.0096 22  LEU   A CB  
126  C  CG  . LEU   A 16  ? 0.7723 0.4491 0.3749 -0.0218 -0.1479 -0.0231 22  LEU   A CG  
127  C  CD1 . LEU   A 16  ? 0.7640 0.4613 0.3748 -0.0198 -0.1468 -0.0194 22  LEU   A CD1 
128  C  CD2 . LEU   A 16  ? 0.8512 0.4236 0.3383 -0.0445 -0.1592 -0.0291 22  LEU   A CD2 
129  N  N   . ALA   A 17  ? 0.6796 0.4663 0.5214 -0.0240 -0.2081 0.0068  23  ALA   A N   
130  C  CA  . ALA   A 17  ? 0.6553 0.4785 0.5917 -0.0280 -0.2298 0.0235  23  ALA   A CA  
131  C  C   . ALA   A 17  ? 0.6894 0.4657 0.6201 -0.0534 -0.2840 0.0396  23  ALA   A C   
132  O  O   . ALA   A 17  ? 0.7373 0.4535 0.5860 -0.0656 -0.2944 0.0320  23  ALA   A O   
133  C  CB  . ALA   A 17  ? 0.6279 0.4957 0.6118 -0.0129 -0.1964 0.0182  23  ALA   A CB  
134  N  N   . THR   A 18  ? 0.6637 0.4630 0.6846 -0.0631 -0.3182 0.0642  24  THR   A N   
135  C  CA  . THR   A 18  ? 0.6875 0.4493 0.7265 -0.0914 -0.3806 0.0890  24  THR   A CA  
136  C  C   . THR   A 18  ? 0.6690 0.4535 0.7802 -0.0917 -0.3832 0.0977  24  THR   A C   
137  O  O   . THR   A 18  ? 0.6427 0.4722 0.7891 -0.0695 -0.3345 0.0844  24  THR   A O   
138  C  CB  . THR   A 18  ? 0.6750 0.4526 0.7944 -0.1022 -0.4194 0.1185  24  THR   A CB  
139  O  OG1 . THR   A 18  ? 0.6134 0.4642 0.8715 -0.0828 -0.3900 0.1290  24  THR   A OG1 
140  C  CG2 . THR   A 18  ? 0.7139 0.4685 0.7649 -0.1034 -0.4189 0.1120  24  THR   A CG2 
141  N  N   . HIS   A 19  ? 0.6847 0.4333 0.8130 -0.1200 -0.4429 0.1218  25  HIS   A N   
142  C  CA  . HIS   A 19  ? 0.6631 0.4319 0.8694 -0.1235 -0.4513 0.1348  25  HIS   A CA  
143  C  C   . HIS   A 19  ? 0.5771 0.4262 0.9369 -0.1033 -0.4200 0.1493  25  HIS   A C   
144  O  O   . HIS   A 19  ? 0.5490 0.4311 0.9561 -0.0897 -0.3836 0.1432  25  HIS   A O   
145  C  CB  . HIS   A 19  ? 0.7128 0.4280 0.9199 -0.1628 -0.5312 0.1653  25  HIS   A CB  
146  C  CG  . HIS   A 19  ? 0.8516 0.4760 0.9078 -0.1865 -0.5535 0.1489  25  HIS   A CG  
147  N  ND1 . HIS   A 19  ? 0.9075 0.5227 0.9095 -0.1720 -0.5097 0.1213  25  HIS   A ND1 
148  C  CD2 . HIS   A 19  ? 0.9457 0.4782 0.8949 -0.2259 -0.6135 0.1581  25  HIS   A CD2 
149  C  CE1 . HIS   A 19  ? 0.9955 0.5140 0.8638 -0.2000 -0.5376 0.1123  25  HIS   A CE1 
150  N  NE2 . HIS   A 19  ? 1.0297 0.4906 0.8527 -0.2351 -0.6001 0.1326  25  HIS   A NE2 
151  N  N   . ASN   A 20  ? 0.5337 0.4078 0.9678 -0.1021 -0.4296 0.1685  26  ASN   A N   
152  C  CA  . ASN   A 20  ? 0.4655 0.4042 1.0439 -0.0832 -0.3902 0.1815  26  ASN   A CA  
153  C  C   . ASN   A 20  ? 0.4442 0.4157 0.9976 -0.0550 -0.3114 0.1489  26  ASN   A C   
154  O  O   . ASN   A 20  ? 0.4147 0.4176 1.0404 -0.0447 -0.2719 0.1496  26  ASN   A O   
155  C  CB  . ASN   A 20  ? 0.4657 0.4172 1.1243 -0.0871 -0.4135 0.2082  26  ASN   A CB  
156  C  CG  . ASN   A 20  ? 0.4555 0.4585 1.2943 -0.0772 -0.3897 0.2359  26  ASN   A CG  
157  O  OD1 . ASN   A 20  ? 0.4503 0.4648 1.3740 -0.0840 -0.4004 0.2557  26  ASN   A OD1 
158  N  ND2 . ASN   A 20  ? 0.4394 0.4707 1.3429 -0.0606 -0.3513 0.2377  26  ASN   A ND2 
159  N  N   . ASP   A 21  ? 0.4605 0.4192 0.9071 -0.0458 -0.2904 0.1223  27  ASP   A N   
160  C  CA  . ASP   A 21  ? 0.4468 0.4291 0.8529 -0.0251 -0.2269 0.0942  27  ASP   A CA  
161  C  C   . ASP   A 21  ? 0.4367 0.4222 0.8254 -0.0215 -0.2051 0.0836  27  ASP   A C   
162  O  O   . ASP   A 21  ? 0.4160 0.4285 0.8337 -0.0107 -0.1574 0.0760  27  ASP   A O   
163  C  CB  . ASP   A 21  ? 0.4947 0.4549 0.7858 -0.0210 -0.2221 0.0728  27  ASP   A CB  
164  C  CG  . ASP   A 21  ? 0.5177 0.4784 0.8167 -0.0214 -0.2311 0.0788  27  ASP   A CG  
165  O  OD1 . ASP   A 21  ? 0.4739 0.4660 0.8620 -0.0147 -0.2108 0.0888  27  ASP   A OD1 
166  O  OD2 . ASP   A 21  ? 0.5772 0.5020 0.7919 -0.0288 -0.2545 0.0734  27  ASP   A OD2 
167  N  N   . TRP   A 22  ? 0.4553 0.4055 0.7905 -0.0332 -0.2395 0.0834  28  TRP   A N   
168  C  CA  . TRP   A 22  ? 0.4588 0.4088 0.7802 -0.0305 -0.2229 0.0756  28  TRP   A CA  
169  C  C   . TRP   A 22  ? 0.4194 0.3940 0.8517 -0.0346 -0.2210 0.0954  28  TRP   A C   
170  O  O   . TRP   A 22  ? 0.4144 0.4028 0.8546 -0.0281 -0.1885 0.0887  28  TRP   A O   
171  C  CB  . TRP   A 22  ? 0.4980 0.3937 0.7233 -0.0417 -0.2535 0.0675  28  TRP   A CB  
172  C  CG  . TRP   A 22  ? 0.5270 0.4067 0.6545 -0.0297 -0.2255 0.0439  28  TRP   A CG  
173  C  CD1 . TRP   A 22  ? 0.5690 0.4157 0.6218 -0.0320 -0.2331 0.0352  28  TRP   A CD1 
174  C  CD2 . TRP   A 22  ? 0.5228 0.4230 0.6307 -0.0137 -0.1832 0.0303  28  TRP   A CD2 
175  N  NE1 . TRP   A 22  ? 0.5886 0.4359 0.5854 -0.0165 -0.1953 0.0173  28  TRP   A NE1 
176  C  CE2 . TRP   A 22  ? 0.5610 0.4425 0.5934 -0.0058 -0.1680 0.0159  28  TRP   A CE2 
177  C  CE3 . TRP   A 22  ? 0.5024 0.4316 0.6499 -0.0074 -0.1584 0.0316  28  TRP   A CE3 
178  C  CZ2 . TRP   A 22  ? 0.5646 0.4601 0.5738 0.0083  -0.1336 0.0069  28  TRP   A CZ2 
179  C  CZ3 . TRP   A 22  ? 0.5175 0.4565 0.6286 0.0042  -0.1274 0.0216  28  TRP   A CZ3 
180  C  CH2 . TRP   A 22  ? 0.5407 0.4657 0.5902 0.0122  -0.1174 0.0112  28  TRP   A CH2 
181  N  N   . ALA   A 23  ? 0.3918 0.3710 0.9147 -0.0462 -0.2551 0.1224  29  ALA   A N   
182  C  CA  . ALA   A 23  ? 0.3559 0.3603 1.0063 -0.0500 -0.2517 0.1466  29  ALA   A CA  
183  C  C   . ALA   A 23  ? 0.3258 0.3699 1.0656 -0.0337 -0.1878 0.1477  29  ALA   A C   
184  O  O   . ALA   A 23  ? 0.2920 0.3554 1.1370 -0.0334 -0.1651 0.1641  29  ALA   A O   
185  C  CB  . ALA   A 23  ? 0.3322 0.3239 1.0571 -0.0720 -0.3201 0.1823  29  ALA   A CB  
186  N  N   . ASN   A 24  ? 0.3293 0.3791 1.0284 -0.0223 -0.1575 0.1313  30  ASN   A N   
187  C  CA  . ASN   A 24  ? 0.2904 0.3610 1.0447 -0.0099 -0.0925 0.1269  30  ASN   A CA  
188  C  C   . ASN   A 24  ? 0.3029 0.3667 0.9392 -0.0015 -0.0519 0.0943  30  ASN   A C   
189  O  O   . ASN   A 24  ? 0.2922 0.3588 0.9227 0.0045  -0.0186 0.0856  30  ASN   A O   
190  C  CB  . ASN   A 24  ? 0.2855 0.3666 1.1291 -0.0088 -0.1026 0.1473  30  ASN   A CB  
191  C  CG  . ASN   A 24  ? 0.2916 0.3877 1.2918 -0.0160 -0.1262 0.1866  30  ASN   A CG  
192  O  OD1 . ASN   A 24  ? 0.2892 0.3969 1.3716 -0.0141 -0.0912 0.1959  30  ASN   A OD1 
193  N  ND2 . ASN   A 24  ? 0.2761 0.3702 1.3242 -0.0266 -0.1874 0.2137  30  ASN   A ND2 
194  N  N   . LEU   A 25  ? 0.3161 0.3688 0.8621 -0.0030 -0.0590 0.0793  31  LEU   A N   
195  C  CA  . LEU   A 25  ? 0.3337 0.3808 0.7757 0.0016  -0.0347 0.0562  31  LEU   A CA  
196  C  C   . LEU   A 25  ? 0.3280 0.3765 0.7686 0.0015  0.0251  0.0476  31  LEU   A C   
197  O  O   . LEU   A 25  ? 0.3178 0.3648 0.8007 -0.0023 0.0497  0.0535  31  LEU   A O   
198  C  CB  . LEU   A 25  ? 0.3536 0.3888 0.7337 -0.0004 -0.0563 0.0509  31  LEU   A CB  
199  C  CG  . LEU   A 25  ? 0.3858 0.4182 0.6764 0.0033  -0.0364 0.0348  31  LEU   A CG  
200  C  CD1 . LEU   A 25  ? 0.4065 0.4355 0.6384 0.0085  -0.0476 0.0255  31  LEU   A CD1 
201  C  CD2 . LEU   A 25  ? 0.3955 0.4173 0.6554 0.0023  -0.0498 0.0349  31  LEU   A CD2 
202  N  N   . VAL   A 26  ? 0.3388 0.3829 0.7190 0.0025  0.0482  0.0335  32  VAL   A N   
203  C  CA  . VAL   A 26  ? 0.3458 0.3746 0.6910 -0.0049 0.1013  0.0234  32  VAL   A CA  
204  C  C   . VAL   A 26  ? 0.3636 0.3861 0.6067 -0.0108 0.0925  0.0142  32  VAL   A C   
205  O  O   . VAL   A 26  ? 0.3869 0.3961 0.6004 -0.0207 0.1112  0.0141  32  VAL   A O   
206  C  CB  . VAL   A 26  ? 0.3591 0.3786 0.7115 -0.0052 0.1348  0.0170  32  VAL   A CB  
207  C  CG1 . VAL   A 26  ? 0.4017 0.3885 0.6826 -0.0198 0.1857  0.0038  32  VAL   A CG1 
208  C  CG2 . VAL   A 26  ? 0.3208 0.3464 0.7935 0.0011  0.1503  0.0312  32  VAL   A CG2 
209  N  N   . TRP   A 27  ? 0.3537 0.3851 0.5511 -0.0053 0.0626  0.0101  33  TRP   A N   
210  C  CA  . TRP   A 27  ? 0.3555 0.3864 0.4783 -0.0090 0.0519  0.0074  33  TRP   A CA  
211  C  C   . TRP   A 27  ? 0.3378 0.3789 0.4432 0.0027  0.0168  0.0069  33  TRP   A C   
212  O  O   . TRP   A 27  ? 0.3268 0.3700 0.4484 0.0086  0.0066  0.0047  33  TRP   A O   
213  C  CB  . TRP   A 27  ? 0.3716 0.3881 0.4404 -0.0228 0.0787  0.0014  33  TRP   A CB  
214  C  CG  . TRP   A 27  ? 0.3940 0.4140 0.4003 -0.0288 0.0607  0.0047  33  TRP   A CG  
215  C  CD1 . TRP   A 27  ? 0.4158 0.4323 0.3900 -0.0383 0.0517  0.0143  33  TRP   A CD1 
216  C  CD2 . TRP   A 27  ? 0.3944 0.4251 0.3771 -0.0251 0.0463  0.0034  33  TRP   A CD2 
217  N  NE1 . TRP   A 27  ? 0.4262 0.4525 0.3674 -0.0411 0.0318  0.0217  33  TRP   A NE1 
218  C  CE2 . TRP   A 27  ? 0.4138 0.4491 0.3594 -0.0327 0.0299  0.0143  33  TRP   A CE2 
219  C  CE3 . TRP   A 27  ? 0.3855 0.4227 0.3812 -0.0162 0.0443  -0.0033 33  TRP   A CE3 
220  C  CZ2 . TRP   A 27  ? 0.4221 0.4695 0.3492 -0.0320 0.0154  0.0191  33  TRP   A CZ2 
221  C  CZ3 . TRP   A 27  ? 0.3989 0.4449 0.3642 -0.0159 0.0316  -0.0018 33  TRP   A CZ3 
222  C  CH2 . TRP   A 27  ? 0.4095 0.4618 0.3448 -0.0231 0.0182  0.0096  33  TRP   A CH2 
223  N  N   . GLU   A 28  ? 0.3330 0.3755 0.4061 0.0053  0.0022  0.0102  34  GLU   A N   
224  C  CA  . GLU   A 28  ? 0.3339 0.3761 0.3855 0.0159  -0.0182 0.0089  34  GLU   A CA  
225  C  C   . GLU   A 28  ? 0.3395 0.3878 0.3614 0.0162  -0.0180 0.0161  34  GLU   A C   
226  O  O   . GLU   A 28  ? 0.3355 0.3848 0.3562 0.0089  -0.0143 0.0241  34  GLU   A O   
227  C  CB  . GLU   A 28  ? 0.3440 0.3697 0.4103 0.0219  -0.0401 0.0085  34  GLU   A CB  
228  C  CG  . GLU   A 28  ? 0.3388 0.3586 0.4226 0.0193  -0.0431 0.0138  34  GLU   A CG  
229  C  CD  . GLU   A 28  ? 0.3938 0.4074 0.4525 0.0241  -0.0438 0.0173  34  GLU   A CD  
230  O  OE1 . GLU   A 28  ? 0.4299 0.4450 0.5016 0.0200  -0.0400 0.0237  34  GLU   A OE1 
231  O  OE2 . GLU   A 28  ? 0.3821 0.3877 0.4136 0.0323  -0.0449 0.0152  34  GLU   A OE2 
232  N  N   . ASP   A 29  ? 0.3401 0.3918 0.3446 0.0234  -0.0219 0.0164  35  ASP   A N   
233  C  CA  . ASP   A 29  ? 0.3362 0.3974 0.3348 0.0252  -0.0225 0.0292  35  ASP   A CA  
234  C  C   . ASP   A 29  ? 0.3274 0.3789 0.3229 0.0407  -0.0212 0.0272  35  ASP   A C   
235  O  O   . ASP   A 29  ? 0.3266 0.3801 0.3109 0.0430  -0.0181 0.0229  35  ASP   A O   
236  C  CB  . ASP   A 29  ? 0.3681 0.4437 0.3514 0.0099  -0.0206 0.0378  35  ASP   A CB  
237  C  CG  . ASP   A 29  ? 0.4347 0.5232 0.4245 0.0045  -0.0302 0.0604  35  ASP   A CG  
238  O  OD1 . ASP   A 29  ? 0.4284 0.5198 0.4448 0.0192  -0.0312 0.0689  35  ASP   A OD1 
239  O  OD2 . ASP   A 29  ? 0.4961 0.5869 0.4648 -0.0166 -0.0366 0.0714  35  ASP   A OD2 
240  N  N   . SER   A 30  ? 0.3210 0.3558 0.3233 0.0505  -0.0188 0.0302  36  SER   A N   
241  C  CA  A SER   A 30  ? 0.3358 0.3458 0.3287 0.0642  -0.0061 0.0273  36  SER   A CA  
242  C  CA  B SER   A 30  ? 0.3369 0.3471 0.3283 0.0638  -0.0064 0.0266  36  SER   A CA  
243  C  C   . SER   A 30  ? 0.3273 0.3587 0.3399 0.0691  0.0053  0.0409  36  SER   A C   
244  O  O   . SER   A 30  ? 0.3354 0.3486 0.3346 0.0776  0.0204  0.0351  36  SER   A O   
245  C  CB  A SER   A 30  ? 0.3483 0.3341 0.3499 0.0720  0.0014  0.0308  36  SER   A CB  
246  C  CB  B SER   A 30  ? 0.3568 0.3356 0.3486 0.0714  0.0005  0.0262  36  SER   A CB  
247  O  OG  A SER   A 30  ? 0.3806 0.3378 0.3617 0.0669  -0.0100 0.0189  36  SER   A OG  
248  O  OG  B SER   A 30  ? 0.3530 0.3565 0.3842 0.0718  0.0004  0.0454  36  SER   A OG  
249  N  N   . SER   A 31  ? 0.3100 0.3755 0.3545 0.0613  -0.0033 0.0619  37  SER   A N   
250  C  CA  . SER   A 31  ? 0.2995 0.3894 0.3764 0.0620  -0.0004 0.0823  37  SER   A CA  
251  C  C   . SER   A 31  ? 0.2990 0.3994 0.3537 0.0543  -0.0034 0.0752  37  SER   A C   
252  O  O   . SER   A 31  ? 0.2925 0.4071 0.3725 0.0572  0.0021  0.0887  37  SER   A O   
253  C  CB  . SER   A 31  ? 0.3143 0.4310 0.4277 0.0493  -0.0189 0.1122  37  SER   A CB  
254  O  OG  . SER   A 31  ? 0.3722 0.4969 0.4512 0.0253  -0.0386 0.1118  37  SER   A OG  
255  N  N   . ARG   A 32  ? 0.2994 0.3927 0.3157 0.0449  -0.0102 0.0564  38  ARG   A N   
256  C  CA  . ARG   A 32  ? 0.2977 0.3960 0.2929 0.0383  -0.0108 0.0479  38  ARG   A CA  
257  C  C   . ARG   A 32  ? 0.3199 0.3929 0.2901 0.0483  -0.0034 0.0272  38  ARG   A C   
258  O  O   . ARG   A 32  ? 0.3180 0.3931 0.2747 0.0454  -0.0025 0.0216  38  ARG   A O   
259  C  CB  . ARG   A 32  ? 0.2981 0.4007 0.2721 0.0182  -0.0191 0.0442  38  ARG   A CB  
260  C  CG  . ARG   A 32  ? 0.3030 0.4174 0.2774 -0.0015 -0.0317 0.0652  38  ARG   A CG  
261  C  CD  . ARG   A 32  ? 0.3526 0.4522 0.2863 -0.0249 -0.0306 0.0579  38  ARG   A CD  
262  N  NE  . ARG   A 32  ? 0.3845 0.4787 0.2945 -0.0321 -0.0237 0.0469  38  ARG   A NE  
263  C  CZ  . ARG   A 32  ? 0.4341 0.5087 0.3008 -0.0576 -0.0202 0.0449  38  ARG   A CZ  
264  N  NH1 . ARG   A 32  ? 0.4472 0.5022 0.2814 -0.0810 -0.0241 0.0537  38  ARG   A NH1 
265  N  NH2 . ARG   A 32  ? 0.4323 0.4990 0.2803 -0.0623 -0.0112 0.0342  38  ARG   A NH2 
266  N  N   . ASP   A 33  ? 0.3413 0.3858 0.3007 0.0560  -0.0025 0.0174  39  ASP   A N   
267  C  CA  . ASP   A 33  ? 0.3624 0.3713 0.2886 0.0582  -0.0057 0.0019  39  ASP   A CA  
268  C  C   . ASP   A 33  ? 0.3721 0.3902 0.3012 0.0483  -0.0203 -0.0043 39  ASP   A C   
269  O  O   . ASP   A 33  ? 0.3785 0.3829 0.2905 0.0468  -0.0258 -0.0104 39  ASP   A O   
270  C  CB  . ASP   A 33  ? 0.3826 0.3705 0.2838 0.0649  0.0096  -0.0011 39  ASP   A CB  
271  C  CG  . ASP   A 33  ? 0.4536 0.3908 0.3029 0.0616  0.0031  -0.0145 39  ASP   A CG  
272  O  OD1 . ASP   A 33  ? 0.4549 0.3582 0.2830 0.0575  -0.0084 -0.0200 39  ASP   A OD1 
273  O  OD2 . ASP   A 33  ? 0.5101 0.4380 0.3367 0.0599  0.0059  -0.0178 39  ASP   A OD2 
274  N  N   . LEU   A 34  ? 0.3621 0.3996 0.3152 0.0410  -0.0231 -0.0011 40  LEU   A N   
275  C  CA  . LEU   A 34  ? 0.3625 0.4045 0.3315 0.0334  -0.0262 -0.0055 40  LEU   A CA  
276  C  C   . LEU   A 34  ? 0.3632 0.3979 0.3589 0.0307  -0.0337 -0.0050 40  LEU   A C   
277  O  O   . LEU   A 34  ? 0.3689 0.4019 0.3672 0.0315  -0.0341 -0.0014 40  LEU   A O   
278  C  CB  . LEU   A 34  ? 0.3614 0.4224 0.3315 0.0230  -0.0124 -0.0032 40  LEU   A CB  
279  C  CG  . LEU   A 34  ? 0.3852 0.4546 0.3364 0.0203  -0.0078 -0.0025 40  LEU   A CG  
280  C  CD1 . LEU   A 34  ? 0.3947 0.4676 0.3328 0.0027  0.0035  -0.0007 40  LEU   A CD1 
281  C  CD2 . LEU   A 34  ? 0.3854 0.4454 0.3364 0.0252  -0.0111 -0.0100 40  LEU   A CD2 
282  N  N   . LEU   A 35  ? 0.3538 0.3853 0.3785 0.0274  -0.0401 -0.0057 41  LEU   A N   
283  C  CA  . LEU   A 35  ? 0.3541 0.3835 0.4237 0.0236  -0.0459 -0.0009 41  LEU   A CA  
284  C  C   . LEU   A 35  ? 0.3514 0.3894 0.4695 0.0203  -0.0343 0.0013  41  LEU   A C   
285  O  O   . LEU   A 35  ? 0.3532 0.3888 0.4708 0.0215  -0.0409 0.0010  41  LEU   A O   
286  C  CB  . LEU   A 35  ? 0.3642 0.3674 0.4305 0.0226  -0.0774 0.0026  41  LEU   A CB  
287  C  CG  . LEU   A 35  ? 0.3629 0.3649 0.4817 0.0168  -0.0890 0.0115  41  LEU   A CG  
288  C  CD1 . LEU   A 35  ? 0.3891 0.3612 0.4769 0.0138  -0.1116 0.0118  41  LEU   A CD1 
289  C  CD2 . LEU   A 35  ? 0.3507 0.3536 0.5304 0.0110  -0.1071 0.0232  41  LEU   A CD2 
290  N  N   . VAL   A 36  ? 0.3510 0.3949 0.5102 0.0161  -0.0114 0.0039  42  VAL   A N   
291  C  CA  . VAL   A 36  ? 0.3591 0.4050 0.5758 0.0141  0.0123  0.0067  42  VAL   A CA  
292  C  C   . VAL   A 36  ? 0.3622 0.4101 0.6616 0.0136  0.0067  0.0202  42  VAL   A C   
293  O  O   . VAL   A 36  ? 0.3574 0.4044 0.6608 0.0108  0.0130  0.0217  42  VAL   A O   
294  C  CB  . VAL   A 36  ? 0.3763 0.4148 0.5645 0.0062  0.0578  -0.0026 42  VAL   A CB  
295  C  CG1 . VAL   A 36  ? 0.3656 0.3950 0.6189 0.0047  0.0952  -0.0007 42  VAL   A CG1 
296  C  CG2 . VAL   A 36  ? 0.4040 0.4416 0.5228 0.0034  0.0567  -0.0110 42  VAL   A CG2 
297  N  N   . SER   A 37  ? 0.3630 0.4140 0.7347 0.0151  -0.0077 0.0335  43  SER   A N   
298  C  CA  . SER   A 37  ? 0.3665 0.4229 0.8374 0.0130  -0.0173 0.0532  43  SER   A CA  
299  C  C   . SER   A 37  ? 0.3735 0.4359 0.9446 0.0161  0.0204  0.0638  43  SER   A C   
300  O  O   . SER   A 37  ? 0.3716 0.4309 0.9326 0.0194  0.0387  0.0575  43  SER   A O   
301  C  CB  . SER   A 37  ? 0.3775 0.4269 0.8594 0.0073  -0.0813 0.0692  43  SER   A CB  
302  O  OG  . SER   A 37  ? 0.4046 0.4483 0.8771 0.0068  -0.1050 0.0735  43  SER   A OG  
303  N  N   . SER   A 38  ? 0.3732 0.4420 1.0466 0.0154  0.0352  0.0809  44  SER   A N   
304  C  CA  . SER   A 38  ? 0.3814 0.4528 1.1704 0.0201  0.0810  0.0942  44  SER   A CA  
305  C  C   . SER   A 38  ? 0.3867 0.4721 1.2805 0.0216  0.0393  0.1236  44  SER   A C   
306  O  O   . SER   A 38  ? 0.3892 0.4791 1.2814 0.0141  -0.0304 0.1395  44  SER   A O   
307  C  CB  . SER   A 38  ? 0.3776 0.4486 1.2431 0.0188  0.1201  0.1033  44  SER   A CB  
308  O  OG  . SER   A 38  ? 0.3911 0.4758 1.2909 0.0133  0.0653  0.1216  44  SER   A OG  
309  N  N   . THR   A 39  ? 0.3975 0.4827 1.3747 0.0289  0.0805  0.1316  45  THR   A N   
310  C  CA  . THR   A 39  ? 0.3987 0.4980 1.4892 0.0299  0.0407  0.1649  45  THR   A CA  
311  C  C   . THR   A 39  ? 0.3871 0.4947 1.6531 0.0379  0.0919  0.1911  45  THR   A C   
312  O  O   . THR   A 39  ? 0.4047 0.4946 1.6748 0.0444  0.1760  0.1731  45  THR   A O   
313  C  CB  . THR   A 39  ? 0.4402 0.5312 1.4644 0.0324  0.0302  0.1535  45  THR   A CB  
314  O  OG1 . THR   A 39  ? 0.4599 0.5366 1.4919 0.0414  0.1086  0.1365  45  THR   A OG1 
315  C  CG2 . THR   A 39  ? 0.5018 0.5820 1.3588 0.0266  -0.0053 0.1268  45  THR   A CG2 
316  N  N   . THR   A 40  ? 0.3578 0.4863 1.7689 0.0355  0.0430  0.2355  46  THR   A N   
317  C  CA  . THR   A 40  ? 0.3187 0.4592 1.9251 0.0448  0.0905  0.2679  46  THR   A CA  
318  C  C   . THR   A 40  ? 0.3264 0.4555 1.9749 0.0574  0.1431  0.2649  46  THR   A C   
319  O  O   . THR   A 40  ? 0.3030 0.4243 2.0706 0.0692  0.2242  0.2727  46  THR   A O   
320  C  CB  . THR   A 40  ? 0.2894 0.4583 2.0500 0.0342  0.0106  0.3242  46  THR   A CB  
321  O  OG1 . THR   A 40  ? 0.3250 0.4939 2.0527 0.0233  -0.0733 0.3408  46  THR   A OG1 
322  C  CG2 . THR   A 40  ? 0.2987 0.4731 2.0331 0.0206  -0.0323 0.3288  46  THR   A CG2 
323  N  N   . ALA   A 41  ? 0.3528 0.4767 1.9087 0.0546  0.1005  0.2550  47  ALA   A N   
324  C  CA  . ALA   A 41  ? 0.3456 0.4573 1.9312 0.0650  0.1421  0.2520  47  ALA   A CA  
325  C  C   . ALA   A 41  ? 0.4081 0.4869 1.8170 0.0665  0.1959  0.1989  47  ALA   A C   
326  O  O   . ALA   A 41  ? 0.4581 0.5318 1.7099 0.0580  0.1676  0.1707  47  ALA   A O   
327  C  CB  . ALA   A 41  ? 0.3337 0.4598 1.9522 0.0584  0.0562  0.2835  47  ALA   A CB  
328  N  N   . GLN   A 42  ? 0.4059 0.4587 1.8466 0.0759  0.2746  0.1879  48  GLN   A N   
329  C  CA  . GLN   A 42  ? 0.4793 0.4918 1.7669 0.0733  0.3305  0.1422  48  GLN   A CA  
330  C  C   . GLN   A 42  ? 0.5082 0.5264 1.6832 0.0687  0.2708  0.1310  48  GLN   A C   
331  O  O   . GLN   A 42  ? 0.4841 0.5209 1.7328 0.0721  0.2231  0.1586  48  GLN   A O   
332  C  CB  . GLN   A 42  ? 0.4981 0.4707 1.8674 0.0823  0.4337  0.1382  48  GLN   A CB  
333  C  CG  . GLN   A 42  ? 0.6266 0.5465 1.8487 0.0755  0.4897  0.0960  48  GLN   A CG  
334  C  CD  . GLN   A 42  ? 0.7682 0.6425 1.8444 0.0603  0.5428  0.0580  48  GLN   A CD  
335  O  OE1 . GLN   A 42  ? 0.7869 0.6661 1.8749 0.0571  0.5506  0.0606  48  GLN   A OE1 
336  N  NE2 . GLN   A 42  ? 0.8399 0.6653 1.7729 0.0475  0.5772  0.0240  48  GLN   A NE2 
337  N  N   . GLY   A 43  ? 0.5555 0.5568 1.5580 0.0595  0.2724  0.0942  49  GLY   A N   
338  C  CA  . GLY   A 43  ? 0.5830 0.5859 1.4716 0.0549  0.2285  0.0803  49  GLY   A CA  
339  C  C   . GLY   A 43  ? 0.5998 0.5648 1.4269 0.0529  0.2892  0.0549  49  GLY   A C   
340  O  O   . GLY   A 43  ? 0.6182 0.5446 1.4302 0.0491  0.3650  0.0369  49  GLY   A O   
341  N  N   . CYS   A 44  ? 0.6008 0.5685 1.3813 0.0524  0.2580  0.0525  50  CYS   A N   
342  C  CA  . CYS   A 44  ? 0.6269 0.5557 1.3538 0.0487  0.3123  0.0306  50  CYS   A CA  
343  C  C   . CYS   A 44  ? 0.6395 0.5650 1.2198 0.0380  0.2824  0.0087  50  CYS   A C   
344  O  O   . CYS   A 44  ? 0.6607 0.5654 1.2160 0.0359  0.3004  0.0006  50  CYS   A O   
345  C  CB  . CYS   A 44  ? 0.6209 0.5455 1.4786 0.0607  0.3319  0.0529  50  CYS   A CB  
346  S  SG  . CYS   A 44  ? 0.6820 0.6548 1.6297 0.0676  0.2344  0.0951  50  CYS   A SG  
347  N  N   . ASP   A 45  ? 0.6217 0.5644 1.1100 0.0307  0.2437  -0.0004 51  ASP   A N   
348  C  CA  . ASP   A 45  ? 0.6303 0.5715 0.9930 0.0205  0.2209  -0.0178 51  ASP   A CA  
349  C  C   . ASP   A 45  ? 0.6375 0.5380 0.9071 0.0028  0.2719  -0.0429 51  ASP   A C   
350  O  O   . ASP   A 45  ? 0.6381 0.5265 0.9029 -0.0024 0.2964  -0.0472 51  ASP   A O   
351  C  CB  . ASP   A 45  ? 0.6509 0.6250 0.9680 0.0211  0.1605  -0.0130 51  ASP   A CB  
352  C  CG  . ASP   A 45  ? 0.6798 0.6757 1.0180 0.0280  0.1022  0.0045  51  ASP   A CG  
353  O  OD1 . ASP   A 45  ? 0.6986 0.6888 1.0309 0.0285  0.0978  0.0059  51  ASP   A OD1 
354  O  OD2 . ASP   A 45  ? 0.6841 0.6959 1.0341 0.0301  0.0608  0.0164  51  ASP   A OD2 
355  N  N   . THR   A 46  ? 0.6459 0.5208 0.8355 -0.0100 0.2840  -0.0575 52  THR   A N   
356  C  CA  . THR   A 46  ? 0.6865 0.5137 0.7690 -0.0349 0.3202  -0.0782 52  THR   A CA  
357  C  C   . THR   A 46  ? 0.6826 0.5346 0.6772 -0.0461 0.2712  -0.0788 52  THR   A C   
358  O  O   . THR   A 46  ? 0.6761 0.5601 0.6574 -0.0408 0.2281  -0.0727 52  THR   A O   
359  C  CB  . THR   A 46  ? 0.7498 0.5293 0.7892 -0.0479 0.3558  -0.0914 52  THR   A CB  
360  O  OG1 . THR   A 46  ? 0.7624 0.5053 0.8802 -0.0400 0.4179  -0.0926 52  THR   A OG1 
361  C  CG2 . THR   A 46  ? 0.8165 0.5433 0.7183 -0.0823 0.3718  -0.1096 52  THR   A CG2 
362  N  N   . ILE   A 47  ? 0.6813 0.5158 0.6211 -0.0617 0.2804  -0.0840 53  ILE   A N   
363  C  CA  . ILE   A 47  ? 0.6800 0.5358 0.5501 -0.0730 0.2370  -0.0801 53  ILE   A CA  
364  C  C   . ILE   A 47  ? 0.7204 0.5329 0.4881 -0.1045 0.2445  -0.0888 53  ILE   A C   
365  O  O   . ILE   A 47  ? 0.7653 0.5124 0.4833 -0.1262 0.2922  -0.1023 53  ILE   A O   
366  C  CB  . ILE   A 47  ? 0.6774 0.5365 0.5431 -0.0761 0.2360  -0.0767 53  ILE   A CB  
367  C  CG1 . ILE   A 47  ? 0.6367 0.5324 0.6056 -0.0488 0.2282  -0.0669 53  ILE   A CG1 
368  C  CG2 . ILE   A 47  ? 0.6908 0.5722 0.4969 -0.0872 0.1914  -0.0684 53  ILE   A CG2 
369  C  CD1 . ILE   A 47  ? 0.6171 0.5642 0.6242 -0.0286 0.1748  -0.0548 53  ILE   A CD1 
370  N  N   . ALA   A 48  ? 0.7033 0.5450 0.4384 -0.1094 0.1997  -0.0801 54  ALA   A N   
371  C  CA  . ALA   A 48  ? 0.7394 0.5439 0.3841 -0.1426 0.1953  -0.0824 54  ALA   A CA  
372  C  C   . ALA   A 48  ? 0.7666 0.5459 0.3343 -0.1738 0.1815  -0.0762 54  ALA   A C   
373  O  O   . ALA   A 48  ? 0.7413 0.5575 0.3357 -0.1634 0.1573  -0.0647 54  ALA   A O   
374  C  CB  . ALA   A 48  ? 0.7125 0.5600 0.3705 -0.1349 0.1550  -0.0714 54  ALA   A CB  
375  N  N   . ARG   A 49  ? 0.8223 0.5321 0.2901 -0.2149 0.1958  -0.0826 55  ARG   A N   
376  C  CA  . ARG   A 49  ? 0.8665 0.5383 0.2445 -0.2543 0.1764  -0.0730 55  ARG   A CA  
377  C  C   . ARG   A 49  ? 0.9029 0.5543 0.2101 -0.2904 0.1390  -0.0613 55  ARG   A C   
378  O  O   . ARG   A 49  ? 0.9779 0.5495 0.1937 -0.3260 0.1637  -0.0743 55  ARG   A O   
379  C  CB  . ARG   A 49  ? 0.9327 0.5150 0.2364 -0.2799 0.2336  -0.0917 55  ARG   A CB  
380  C  CG  . ARG   A 49  ? 0.9045 0.5019 0.2885 -0.2464 0.2770  -0.1014 55  ARG   A CG  
381  C  CD  . ARG   A 49  ? 0.8691 0.5382 0.3204 -0.2221 0.2388  -0.0844 55  ARG   A CD  
382  N  NE  . ARG   A 49  ? 0.8264 0.5066 0.3569 -0.1937 0.2777  -0.0918 55  ARG   A NE  
383  C  CZ  . ARG   A 49  ? 0.7558 0.4973 0.3635 -0.1659 0.2529  -0.0807 55  ARG   A CZ  
384  N  NH1 . ARG   A 49  ? 0.7033 0.4974 0.3189 -0.1602 0.1965  -0.0638 55  ARG   A NH1 
385  N  NH2 . ARG   A 49  ? 0.7094 0.4566 0.3914 -0.1444 0.2863  -0.0848 55  ARG   A NH2 
386  N  N   . CYS   A 50  ? 0.8445 0.5638 0.1974 -0.2822 0.0824  -0.0359 56  CYS   A N   
387  C  CA  . CYS   A 50  ? 0.8502 0.5671 0.1680 -0.3109 0.0418  -0.0183 56  CYS   A CA  
388  C  C   . CYS   A 50  ? 0.8135 0.6003 0.1897 -0.3054 -0.0166 0.0168  56  CYS   A C   
389  O  O   . CYS   A 50  ? 0.7692 0.5994 0.2025 -0.2797 -0.0222 0.0241  56  CYS   A O   
390  C  CB  . CYS   A 50  ? 0.8272 0.5640 0.1883 -0.2878 0.0576  -0.0301 56  CYS   A CB  
391  S  SG  . CYS   A 50  ? 0.7755 0.6158 0.2727 -0.2272 0.0443  -0.0220 56  CYS   A SG  
392  N  N   . ASP   A 51  ? 0.8192 0.6212 0.1976 -0.3244 -0.0559 0.0389  57  ASP   A N   
393  C  CA  . ASP   A 51  ? 0.7818 0.6539 0.2404 -0.3144 -0.1032 0.0750  57  ASP   A CA  
394  C  C   . ASP   A 51  ? 0.7380 0.6561 0.2618 -0.2925 -0.1069 0.0797  57  ASP   A C   
395  O  O   . ASP   A 51  ? 0.7249 0.6753 0.2890 -0.3047 -0.1464 0.1124  57  ASP   A O   
396  C  CB  . ASP   A 51  ? 0.8484 0.6963 0.2603 -0.3657 -0.1573 0.1111  57  ASP   A CB  
397  C  CG  . ASP   A 51  ? 0.9886 0.8013 0.3464 -0.4147 -0.1946 0.1305  57  ASP   A CG  
398  O  OD1 . ASP   A 51  ? 1.0435 0.8169 0.3519 -0.4218 -0.1680 0.1057  57  ASP   A OD1 
399  O  OD2 . ASP   A 51  ? 1.0274 0.8512 0.3978 -0.4470 -0.2529 0.1733  57  ASP   A OD2 
400  N  N   . CYS   A 52  ? 0.7109 0.6294 0.2488 -0.2621 -0.0659 0.0498  58  CYS   A N   
401  C  CA  . CYS   A 52  ? 0.6543 0.6078 0.2439 -0.2409 -0.0637 0.0508  58  CYS   A CA  
402  C  C   . CYS   A 52  ? 0.5685 0.5924 0.2535 -0.2097 -0.0802 0.0740  58  CYS   A C   
403  O  O   . CYS   A 52  ? 0.5485 0.5941 0.2668 -0.1862 -0.0737 0.0730  58  CYS   A O   
404  C  CB  . CYS   A 52  ? 0.6562 0.5968 0.2495 -0.2127 -0.0201 0.0184  58  CYS   A CB  
405  S  SG  . CYS   A 52  ? 0.7016 0.5617 0.2065 -0.2441 0.0093  -0.0065 58  CYS   A SG  
406  N  N   . GLN   A 53  ? 0.5239 0.5777 0.2522 -0.2108 -0.0974 0.0949  59  GLN   A N   
407  C  CA  . GLN   A 53  ? 0.4665 0.5777 0.2873 -0.1801 -0.0999 0.1154  59  GLN   A CA  
408  C  C   . GLN   A 53  ? 0.4330 0.5601 0.2849 -0.1522 -0.0752 0.1044  59  GLN   A C   
409  O  O   . GLN   A 53  ? 0.3938 0.5570 0.3134 -0.1359 -0.0742 0.1245  59  GLN   A O   
410  C  CB  . GLN   A 53  ? 0.4546 0.5943 0.3270 -0.2029 -0.1402 0.1604  59  GLN   A CB  
411  C  CG  . GLN   A 53  ? 0.4918 0.6381 0.3776 -0.2132 -0.1640 0.1815  59  GLN   A CG  
412  C  CD  . GLN   A 53  ? 0.5043 0.6826 0.4611 -0.2361 -0.2082 0.2335  59  GLN   A CD  
413  O  OE1 . GLN   A 53  ? 0.5573 0.7109 0.4743 -0.2833 -0.2533 0.2576  59  GLN   A OE1 
414  N  NE2 . GLN   A 53  ? 0.4442 0.6730 0.5089 -0.2060 -0.1961 0.2546  59  GLN   A NE2 
415  N  N   . THR   A 54  ? 0.4469 0.5426 0.2512 -0.1489 -0.0535 0.0749  60  THR   A N   
416  C  CA  . THR   A 54  ? 0.4355 0.5357 0.2551 -0.1248 -0.0315 0.0619  60  THR   A CA  
417  C  C   . THR   A 54  ? 0.4444 0.5166 0.2331 -0.1093 -0.0078 0.0312  60  THR   A C   
418  O  O   . THR   A 54  ? 0.4666 0.5060 0.2126 -0.1257 -0.0026 0.0179  60  THR   A O   
419  C  CB  . THR   A 54  ? 0.4674 0.5582 0.2744 -0.1448 -0.0378 0.0677  60  THR   A CB  
420  O  OG1 . THR   A 54  ? 0.5118 0.5549 0.2514 -0.1684 -0.0331 0.0483  60  THR   A OG1 
421  C  CG2 . THR   A 54  ? 0.4625 0.5791 0.3074 -0.1673 -0.0673 0.1032  60  THR   A CG2 
422  N  N   . GLY   A 55  ? 0.4163 0.4959 0.2267 -0.0810 0.0066  0.0228  61  GLY   A N   
423  C  CA  . GLY   A 55  ? 0.4261 0.4847 0.2268 -0.0660 0.0214  0.0021  61  GLY   A CA  
424  C  C   . GLY   A 55  ? 0.4130 0.4735 0.2288 -0.0433 0.0268  0.0001  61  GLY   A C   
425  O  O   . GLY   A 55  ? 0.4092 0.4798 0.2326 -0.0412 0.0271  0.0104  61  GLY   A O   
426  N  N   . VAL   A 56  ? 0.4093 0.4553 0.2285 -0.0293 0.0300  -0.0108 62  VAL   A N   
427  C  CA  . VAL   A 56  ? 0.4183 0.4525 0.2382 -0.0141 0.0273  -0.0111 62  VAL   A CA  
428  C  C   . VAL   A 56  ? 0.4166 0.4452 0.2424 -0.0021 0.0200  -0.0135 62  VAL   A C   
429  O  O   . VAL   A 56  ? 0.4145 0.4428 0.2564 -0.0029 0.0198  -0.0189 62  VAL   A O   
430  C  CB  . VAL   A 56  ? 0.4404 0.4549 0.2637 -0.0163 0.0288  -0.0161 62  VAL   A CB  
431  C  CG1 . VAL   A 56  ? 0.4571 0.4530 0.2774 -0.0059 0.0166  -0.0120 62  VAL   A CG1 
432  C  CG2 . VAL   A 56  ? 0.4572 0.4715 0.2688 -0.0294 0.0356  -0.0144 62  VAL   A CG2 
433  N  N   . TYR   A 57  ? 0.4263 0.4439 0.2352 0.0067  0.0170  -0.0098 63  TYR   A N   
434  C  CA  . TYR   A 57  ? 0.4360 0.4384 0.2396 0.0139  0.0068  -0.0117 63  TYR   A CA  
435  C  C   . TYR   A 57  ? 0.4542 0.4176 0.2276 0.0142  -0.0081 -0.0096 63  TYR   A C   
436  O  O   . TYR   A 57  ? 0.4686 0.4152 0.2149 0.0116  -0.0037 -0.0067 63  TYR   A O   
437  C  CB  . TYR   A 57  ? 0.4351 0.4459 0.2350 0.0195  0.0164  -0.0095 63  TYR   A CB  
438  C  CG  . TYR   A 57  ? 0.4732 0.4613 0.2432 0.0245  0.0311  -0.0059 63  TYR   A CG  
439  C  CD1 . TYR   A 57  ? 0.4792 0.4794 0.2567 0.0233  0.0483  0.0016  63  TYR   A CD1 
440  C  CD2 . TYR   A 57  ? 0.5229 0.4716 0.2557 0.0284  0.0318  -0.0093 63  TYR   A CD2 
441  C  CE1 . TYR   A 57  ? 0.5154 0.4900 0.2711 0.0288  0.0724  0.0054  63  TYR   A CE1 
442  C  CE2 . TYR   A 57  ? 0.5600 0.4730 0.2545 0.0312  0.0560  -0.0083 63  TYR   A CE2 
443  C  CZ  . TYR   A 57  ? 0.5601 0.4869 0.2696 0.0327  0.0797  -0.0011 63  TYR   A CZ  
444  O  OH  . TYR   A 57  ? 0.5985 0.4865 0.2768 0.0364  0.1137  0.0005  63  TYR   A OH  
445  N  N   . TYR   A 58  ? 0.4583 0.4039 0.2344 0.0141  -0.0287 -0.0085 64  TYR   A N   
446  C  CA  . TYR   A 58  ? 0.5045 0.4048 0.2445 0.0073  -0.0533 -0.0019 64  TYR   A CA  
447  C  C   . TYR   A 58  ? 0.5408 0.3991 0.2154 0.0051  -0.0504 -0.0047 64  TYR   A C   
448  O  O   . TYR   A 58  ? 0.5220 0.3854 0.2025 0.0093  -0.0476 -0.0087 64  TYR   A O   
449  C  CB  . TYR   A 58  ? 0.5016 0.4004 0.2878 0.0037  -0.0837 0.0070  64  TYR   A CB  
450  C  CG  . TYR   A 58  ? 0.5535 0.4015 0.3019 -0.0096 -0.1211 0.0203  64  TYR   A CG  
451  C  CD1 . TYR   A 58  ? 0.5827 0.4069 0.3060 -0.0174 -0.1307 0.0284  64  TYR   A CD1 
452  C  CD2 . TYR   A 58  ? 0.5874 0.4038 0.3142 -0.0184 -0.1495 0.0261  64  TYR   A CD2 
453  C  CE1 . TYR   A 58  ? 0.6427 0.4105 0.3173 -0.0355 -0.1702 0.0435  64  TYR   A CE1 
454  C  CE2 . TYR   A 58  ? 0.6428 0.4004 0.3180 -0.0382 -0.1904 0.0408  64  TYR   A CE2 
455  C  CZ  . TYR   A 58  ? 0.6856 0.4175 0.3326 -0.0477 -0.2020 0.0503  64  TYR   A CZ  
456  O  OH  . TYR   A 58  ? 0.7722 0.4366 0.3558 -0.0728 -0.2476 0.0676  64  TYR   A OH  
457  N  N   . CYS   A 59  ? 0.5959 0.4048 0.2031 -0.0030 -0.0479 -0.0030 65  CYS   A N   
458  C  CA  . CYS   A 59  ? 0.6670 0.4167 0.1962 -0.0082 -0.0353 -0.0080 65  CYS   A CA  
459  C  C   . CYS   A 59  ? 0.7444 0.4197 0.1998 -0.0300 -0.0731 -0.0009 65  CYS   A C   
460  O  O   . CYS   A 59  ? 0.7667 0.4037 0.1740 -0.0418 -0.0792 0.0048  65  CYS   A O   
461  C  CB  . CYS   A 59  ? 0.6933 0.4342 0.1956 -0.0024 0.0101  -0.0119 65  CYS   A CB  
462  S  SG  . CYS   A 59  ? 0.8001 0.4415 0.1880 -0.0123 0.0400  -0.0189 65  CYS   A SG  
463  N  N   . SER   A 60  ? 0.7744 0.4259 0.2187 -0.0384 -0.1020 0.0012  66  SER   A N   
464  C  CA  . SER   A 60  ? 0.8497 0.4271 0.2249 -0.0655 -0.1496 0.0130  66  SER   A CA  
465  C  C   . SER   A 60  ? 0.9442 0.4241 0.1859 -0.0850 -0.1346 0.0077  66  SER   A C   
466  O  O   . SER   A 60  ? 0.9982 0.4225 0.1815 -0.1092 -0.1705 0.0210  66  SER   A O   
467  C  CB  . SER   A 60  ? 0.8765 0.4451 0.2645 -0.0727 -0.1813 0.0167  66  SER   A CB  
468  O  OG  . SER   A 60  ? 0.9304 0.4927 0.2944 -0.0620 -0.1430 -0.0004 66  SER   A OG  
469  N  N   . SER   A 61  ? 0.9673 0.4236 0.1640 -0.0752 -0.0783 -0.0097 67  SER   A N   
470  C  CA  . SER   A 61  ? 1.0573 0.4120 0.1249 -0.0916 -0.0449 -0.0182 67  SER   A CA  
471  C  C   . SER   A 61  ? 1.0801 0.4198 0.1187 -0.0968 -0.0322 -0.0131 67  SER   A C   
472  O  O   . SER   A 61  ? 1.1582 0.3980 0.0742 -0.1184 -0.0143 -0.0168 67  SER   A O   
473  C  CB  . SER   A 61  ? 1.0792 0.4241 0.1381 -0.0739 0.0224  -0.0352 67  SER   A CB  
474  O  OG  . SER   A 61  ? 1.0485 0.4647 0.1887 -0.0473 0.0702  -0.0365 67  SER   A OG  
475  N  N   . ARG   A 62  ? 1.0052 0.4335 0.1462 -0.0807 -0.0419 -0.0048 68  ARG   A N   
476  C  CA  . ARG   A 62  ? 1.0222 0.4410 0.1441 -0.0862 -0.0360 0.0018  68  ARG   A CA  
477  C  C   . ARG   A 62  ? 1.0086 0.4627 0.1866 -0.0934 -0.0946 0.0205  68  ARG   A C   
478  O  O   . ARG   A 62  ? 1.0175 0.4672 0.1875 -0.0980 -0.0950 0.0278  68  ARG   A O   
479  C  CB  . ARG   A 62  ? 0.9878 0.4755 0.1824 -0.0600 0.0190  -0.0047 68  ARG   A CB  
480  C  CG  . ARG   A 62  ? 1.0407 0.4962 0.2007 -0.0509 0.0854  -0.0165 68  ARG   A CG  
481  C  CD  . ARG   A 62  ? 1.1421 0.5016 0.1891 -0.0684 0.1185  -0.0185 68  ARG   A CD  
482  N  NE  . ARG   A 62  ? 1.1886 0.5180 0.2203 -0.0565 0.1943  -0.0282 68  ARG   A NE  
483  C  CZ  . ARG   A 62  ? 1.2566 0.5091 0.2140 -0.0627 0.2239  -0.0398 68  ARG   A CZ  
484  N  NH1 . ARG   A 62  ? 1.2884 0.4843 0.1703 -0.0838 0.1777  -0.0432 68  ARG   A NH1 
485  N  NH2 . ARG   A 62  ? 1.2622 0.4911 0.2254 -0.0485 0.3008  -0.0461 68  ARG   A NH2 
486  N  N   . ARG   A 63  ? 0.9824 0.4756 0.2301 -0.0919 -0.1382 0.0291  69  ARG   A N   
487  C  CA  . ARG   A 63  ? 0.9420 0.4799 0.2765 -0.0927 -0.1844 0.0483  69  ARG   A CA  
488  C  C   . ARG   A 63  ? 0.8766 0.4838 0.2883 -0.0725 -0.1552 0.0452  69  ARG   A C   
489  O  O   . ARG   A 63  ? 0.8696 0.4785 0.3046 -0.0787 -0.1779 0.0598  69  ARG   A O   
490  C  CB  . ARG   A 63  ? 1.0184 0.4836 0.2918 -0.1251 -0.2440 0.0722  69  ARG   A CB  
491  C  CG  . ARG   A 63  ? 1.1220 0.5385 0.3612 -0.1476 -0.2939 0.0836  69  ARG   A CG  
492  C  CD  . ARG   A 63  ? 1.2598 0.5984 0.4338 -0.1860 -0.3607 0.1129  69  ARG   A CD  
493  N  NE  . ARG   A 63  ? 1.4349 0.6700 0.4774 -0.2206 -0.3889 0.1143  69  ARG   A NE  
494  C  CZ  . ARG   A 63  ? 1.5663 0.6987 0.4953 -0.2646 -0.4427 0.1357  69  ARG   A CZ  
495  N  NH1 . ARG   A 63  ? 1.5613 0.6866 0.5007 -0.2770 -0.4752 0.1595  69  ARG   A NH1 
496  N  NH2 . ARG   A 63  ? 1.6689 0.6977 0.4659 -0.2995 -0.4655 0.1342  69  ARG   A NH2 
497  N  N   . LYS   A 64  ? 0.8209 0.4809 0.2707 -0.0509 -0.1073 0.0282  70  LYS   A N   
498  C  CA  . LYS   A 64  ? 0.7623 0.4792 0.2709 -0.0369 -0.0796 0.0246  70  LYS   A CA  
499  C  C   . LYS   A 64  ? 0.6761 0.4637 0.2639 -0.0190 -0.0583 0.0149  70  LYS   A C   
500  O  O   . LYS   A 64  ? 0.6676 0.4600 0.2527 -0.0135 -0.0488 0.0079  70  LYS   A O   
501  C  CB  . LYS   A 64  ? 0.8082 0.5001 0.2588 -0.0370 -0.0384 0.0184  70  LYS   A CB  
502  C  CG  . LYS   A 64  ? 0.9031 0.5473 0.2988 -0.0521 -0.0478 0.0280  70  LYS   A CG  
503  C  CD  . LYS   A 64  ? 0.9913 0.6234 0.3522 -0.0484 0.0031  0.0217  70  LYS   A CD  
504  C  CE  . LYS   A 64  ? 1.0901 0.6678 0.3857 -0.0645 0.0006  0.0303  70  LYS   A CE  
505  N  NZ  . LYS   A 64  ? 1.1890 0.6639 0.3600 -0.0873 -0.0057 0.0315  70  LYS   A NZ  
506  N  N   . HIS   A 65  ? 0.6150 0.4493 0.2636 -0.0127 -0.0495 0.0148  71  HIS   A N   
507  C  CA  . HIS   A 65  ? 0.5595 0.4489 0.2652 -0.0029 -0.0289 0.0065  71  HIS   A CA  
508  C  C   . HIS   A 65  ? 0.5528 0.4579 0.2471 -0.0012 0.0018  0.0040  71  HIS   A C   
509  O  O   . HIS   A 65  ? 0.5721 0.4626 0.2465 -0.0059 0.0070  0.0082  71  HIS   A O   
510  C  CB  . HIS   A 65  ? 0.5270 0.4408 0.2934 -0.0027 -0.0349 0.0079  71  HIS   A CB  
511  C  CG  . HIS   A 65  ? 0.5230 0.4321 0.3308 -0.0021 -0.0592 0.0145  71  HIS   A CG  
512  N  ND1 . HIS   A 65  ? 0.5247 0.4583 0.3737 0.0033  -0.0521 0.0087  71  HIS   A ND1 
513  C  CD2 . HIS   A 65  ? 0.5372 0.4189 0.3550 -0.0082 -0.0920 0.0299  71  HIS   A CD2 
514  C  CE1 . HIS   A 65  ? 0.5154 0.4388 0.4053 0.0024  -0.0770 0.0204  71  HIS   A CE1 
515  N  NE2 . HIS   A 65  ? 0.5278 0.4215 0.4045 -0.0051 -0.1048 0.0352  71  HIS   A NE2 
516  N  N   . TYR   A 66  ? 0.5189 0.4521 0.2303 0.0044  0.0199  0.0008  72  TYR   A N   
517  C  CA  . TYR   A 66  ? 0.5062 0.4587 0.2261 0.0050  0.0451  0.0054  72  TYR   A CA  
518  C  C   . TYR   A 66  ? 0.4651 0.4651 0.2331 0.0016  0.0464  0.0073  72  TYR   A C   
519  O  O   . TYR   A 66  ? 0.4440 0.4596 0.2294 0.0032  0.0404  0.0043  72  TYR   A O   
520  C  CB  . TYR   A 66  ? 0.5230 0.4557 0.2206 0.0120  0.0685  0.0073  72  TYR   A CB  
521  C  CG  . TYR   A 66  ? 0.5885 0.4569 0.2153 0.0091  0.0763  0.0053  72  TYR   A CG  
522  C  CD1 . TYR   A 66  ? 0.6239 0.4681 0.2227 0.0041  0.0927  0.0098  72  TYR   A CD1 
523  C  CD2 . TYR   A 66  ? 0.6373 0.4615 0.2171 0.0083  0.0700  -0.0006 72  TYR   A CD2 
524  C  CE1 . TYR   A 66  ? 0.6985 0.4701 0.2151 -0.0033 0.1026  0.0078  72  TYR   A CE1 
525  C  CE2 . TYR   A 66  ? 0.7091 0.4582 0.2037 -0.0010 0.0773  -0.0025 72  TYR   A CE2 
526  C  CZ  . TYR   A 66  ? 0.7534 0.4736 0.2125 -0.0073 0.0949  0.0014  72  TYR   A CZ  
527  O  OH  . TYR   A 66  ? 0.8666 0.4997 0.2252 -0.0212 0.1036  -0.0008 72  TYR   A OH  
528  N  N   . PRO   A 67  ? 0.4526 0.4702 0.2361 -0.0066 0.0527  0.0140  73  PRO   A N   
529  C  CA  . PRO   A 67  ? 0.4288 0.4798 0.2434 -0.0176 0.0481  0.0193  73  PRO   A CA  
530  C  C   . PRO   A 67  ? 0.4124 0.4880 0.2593 -0.0145 0.0566  0.0345  73  PRO   A C   
531  O  O   . PRO   A 67  ? 0.4129 0.4831 0.2673 -0.0059 0.0764  0.0430  73  PRO   A O   
532  C  CB  . PRO   A 67  ? 0.4381 0.4899 0.2521 -0.0311 0.0473  0.0227  73  PRO   A CB  
533  C  CG  . PRO   A 67  ? 0.4561 0.4866 0.2523 -0.0233 0.0592  0.0253  73  PRO   A CG  
534  C  CD  . PRO   A 67  ? 0.4551 0.4577 0.2234 -0.0097 0.0619  0.0190  73  PRO   A CD  
535  N  N   . VAL   A 68  ? 0.3893 0.4866 0.2565 -0.0215 0.0447  0.0391  74  VAL   A N   
536  C  CA  . VAL   A 68  ? 0.3687 0.4912 0.2792 -0.0186 0.0479  0.0578  74  VAL   A CA  
537  C  C   . VAL   A 68  ? 0.3644 0.5124 0.2989 -0.0410 0.0243  0.0740  74  VAL   A C   
538  O  O   . VAL   A 68  ? 0.3831 0.5197 0.2838 -0.0579 0.0091  0.0638  74  VAL   A O   
539  C  CB  . VAL   A 68  ? 0.3750 0.4877 0.2801 -0.0023 0.0544  0.0497  74  VAL   A CB  
540  C  CG1 . VAL   A 68  ? 0.4000 0.4795 0.2799 0.0149  0.0785  0.0417  74  VAL   A CG1 
541  C  CG2 . VAL   A 68  ? 0.3888 0.4916 0.2654 -0.0067 0.0384  0.0329  74  VAL   A CG2 
542  N  N   . SER   A 69  ? 0.3349 0.5115 0.3282 -0.0427 0.0224  0.1015  75  SER   A N   
543  C  CA  . SER   A 69  ? 0.3251 0.5240 0.3468 -0.0659 -0.0075 0.1249  75  SER   A CA  
544  C  C   . SER   A 69  ? 0.3120 0.5195 0.3595 -0.0499 -0.0021 0.1288  75  SER   A C   
545  O  O   . SER   A 69  ? 0.3060 0.5127 0.3811 -0.0244 0.0272  0.1283  75  SER   A O   
546  C  CB  . SER   A 69  ? 0.3193 0.5483 0.4112 -0.0777 -0.0166 0.1610  75  SER   A CB  
547  O  OG  . SER   A 69  ? 0.3726 0.5933 0.4366 -0.1043 -0.0359 0.1627  75  SER   A OG  
548  N  N   . PHE   A 70  ? 0.3077 0.5142 0.3368 -0.0656 -0.0262 0.1303  76  PHE   A N   
549  C  CA  . PHE   A 70  ? 0.3065 0.5198 0.3586 -0.0511 -0.0222 0.1337  76  PHE   A CA  
550  C  C   . PHE   A 70  ? 0.3196 0.5503 0.3989 -0.0756 -0.0571 0.1631  76  PHE   A C   
551  O  O   . PHE   A 70  ? 0.3396 0.5621 0.3875 -0.1090 -0.0872 0.1719  76  PHE   A O   
552  C  CB  . PHE   A 70  ? 0.3243 0.5092 0.3188 -0.0372 -0.0091 0.0994  76  PHE   A CB  
553  C  CG  . PHE   A 70  ? 0.3492 0.5106 0.2816 -0.0571 -0.0210 0.0802  76  PHE   A CG  
554  C  CD1 . PHE   A 70  ? 0.3660 0.5074 0.2637 -0.0570 -0.0109 0.0608  76  PHE   A CD1 
555  C  CD2 . PHE   A 70  ? 0.3695 0.5226 0.2784 -0.0762 -0.0379 0.0823  76  PHE   A CD2 
556  C  CE1 . PHE   A 70  ? 0.3991 0.5134 0.2485 -0.0733 -0.0122 0.0436  76  PHE   A CE1 
557  C  CE2 . PHE   A 70  ? 0.4097 0.5301 0.2586 -0.0946 -0.0370 0.0630  76  PHE   A CE2 
558  C  CZ  . PHE   A 70  ? 0.4163 0.5176 0.2401 -0.0919 -0.0217 0.0437  76  PHE   A CZ  
559  N  N   . SER   A 71  ? 0.3108 0.5593 0.4456 -0.0615 -0.0538 0.1804  77  SER   A N   
560  C  CA  . SER   A 71  ? 0.3168 0.5835 0.4899 -0.0840 -0.0902 0.2154  77  SER   A CA  
561  C  C   . SER   A 71  ? 0.3732 0.6133 0.4714 -0.1036 -0.1105 0.2004  77  SER   A C   
562  O  O   . SER   A 71  ? 0.4091 0.6219 0.4422 -0.0941 -0.0905 0.1632  77  SER   A O   
563  C  CB  . SER   A 71  ? 0.2859 0.5809 0.5594 -0.0597 -0.0745 0.2425  77  SER   A CB  
564  O  OG  . SER   A 71  ? 0.3254 0.6050 0.5779 -0.0366 -0.0521 0.2201  77  SER   A OG  
565  N  N   . LYS   A 72  ? 0.3831 0.6280 0.4929 -0.1333 -0.1506 0.2323  78  LYS   A N   
566  C  CA  . LYS   A 72  ? 0.4454 0.6579 0.4803 -0.1560 -0.1677 0.2220  78  LYS   A CA  
567  C  C   . LYS   A 72  ? 0.4427 0.6628 0.5032 -0.1261 -0.1473 0.2129  78  LYS   A C   
568  O  O   . LYS   A 72  ? 0.4130 0.6646 0.5607 -0.1024 -0.1385 0.2337  78  LYS   A O   
569  C  CB  . LYS   A 72  ? 0.4833 0.6897 0.5132 -0.2042 -0.2237 0.2642  78  LYS   A CB  
570  C  CG  . LYS   A 72  ? 0.5581 0.7685 0.5987 -0.2334 -0.2527 0.2886  78  LYS   A CG  
571  C  CD  . LYS   A 72  ? 0.6899 0.8452 0.6229 -0.2919 -0.2933 0.2937  78  LYS   A CD  
572  C  CE  . LYS   A 72  ? 0.7980 0.8972 0.6125 -0.2945 -0.2573 0.2408  78  LYS   A CE  
573  N  NZ  . LYS   A 72  ? 0.8867 0.9148 0.5804 -0.3516 -0.2854 0.2418  78  LYS   A NZ  
574  N  N   . PRO   A 73  ? 0.4743 0.6633 0.4652 -0.1269 -0.1358 0.1833  79  PRO   A N   
575  C  CA  . PRO   A 73  ? 0.4660 0.6608 0.4812 -0.1003 -0.1189 0.1754  79  PRO   A CA  
576  C  C   . PRO   A 73  ? 0.4423 0.6612 0.5256 -0.1035 -0.1426 0.2151  79  PRO   A C   
577  O  O   . PRO   A 73  ? 0.4539 0.6664 0.5230 -0.1396 -0.1825 0.2435  79  PRO   A O   
578  C  CB  . PRO   A 73  ? 0.5143 0.6705 0.4466 -0.1127 -0.1115 0.1465  79  PRO   A CB  
579  C  CG  . PRO   A 73  ? 0.5491 0.6790 0.4214 -0.1295 -0.1047 0.1270  79  PRO   A CG  
580  C  CD  . PRO   A 73  ? 0.5157 0.6595 0.4084 -0.1509 -0.1320 0.1557  79  PRO   A CD  
581  N  N   . SER   A 74  ? 0.4105 0.6500 0.5639 -0.0683 -0.1182 0.2184  80  SER   A N   
582  C  CA  . SER   A 74  ? 0.3850 0.6489 0.6226 -0.0656 -0.1336 0.2583  80  SER   A CA  
583  C  C   . SER   A 74  ? 0.3708 0.6347 0.6496 -0.0271 -0.0961 0.2467  80  SER   A C   
584  O  O   . SER   A 74  ? 0.3836 0.6258 0.6183 -0.0056 -0.0628 0.2081  80  SER   A O   
585  C  CB  . SER   A 74  ? 0.3778 0.6750 0.7049 -0.0728 -0.1503 0.3012  80  SER   A CB  
586  O  OG  . SER   A 74  ? 0.4036 0.7084 0.7626 -0.0451 -0.1102 0.2875  80  SER   A OG  
587  N  N   . LEU   A 75  ? 0.3467 0.6295 0.7077 -0.0220 -0.1048 0.2823  81  LEU   A N   
588  C  CA  . LEU   A 75  ? 0.3527 0.6294 0.7579 0.0112  -0.0687 0.2765  81  LEU   A CA  
589  C  C   . LEU   A 75  ? 0.3462 0.6294 0.8237 0.0393  -0.0254 0.2823  81  LEU   A C   
590  O  O   . LEU   A 75  ? 0.3131 0.6275 0.8895 0.0365  -0.0336 0.3249  81  LEU   A O   
591  C  CB  . LEU   A 75  ? 0.3266 0.6201 0.8009 0.0036  -0.0950 0.3176  81  LEU   A CB  
592  C  CG  . LEU   A 75  ? 0.3763 0.6502 0.7812 -0.0131 -0.1184 0.3063  81  LEU   A CG  
593  C  CD1 . LEU   A 75  ? 0.3649 0.6568 0.8340 -0.0322 -0.1593 0.3569  81  LEU   A CD1 
594  C  CD2 . LEU   A 75  ? 0.4047 0.6517 0.7773 0.0156  -0.0786 0.2680  81  LEU   A CD2 
595  N  N   . ILE   A 76  ? 0.3767 0.6259 0.8067 0.0638  0.0204  0.2427  82  ILE   A N   
596  C  CA  . ILE   A 76  ? 0.3811 0.6181 0.8549 0.0885  0.0713  0.2416  82  ILE   A CA  
597  C  C   . ILE   A 76  ? 0.4204 0.6125 0.8825 0.1150  0.1194  0.2204  82  ILE   A C   
598  O  O   . ILE   A 76  ? 0.4557 0.6141 0.8295 0.1151  0.1182  0.1856  82  ILE   A O   
599  C  CB  . ILE   A 76  ? 0.4106 0.6343 0.8159 0.0844  0.0794  0.2142  82  ILE   A CB  
600  C  CG1 . ILE   A 76  ? 0.4006 0.6633 0.8266 0.0577  0.0374  0.2388  82  ILE   A CG1 
601  C  CG2 . ILE   A 76  ? 0.4200 0.6122 0.8391 0.1085  0.1390  0.2041  82  ILE   A CG2 
602  C  CD1 . ILE   A 76  ? 0.4489 0.6977 0.7936 0.0486  0.0344  0.2094  82  ILE   A CD1 
603  N  N   . PHE   A 77  ? 0.4115 0.5986 0.9656 0.1361  0.1633  0.2431  83  PHE   A N   
604  C  CA  . PHE   A 77  ? 0.4581 0.5892 0.9971 0.1594  0.2172  0.2234  83  PHE   A CA  
605  C  C   . PHE   A 77  ? 0.5288 0.5926 0.9515 0.1653  0.2549  0.1762  83  PHE   A C   
606  O  O   . PHE   A 77  ? 0.5314 0.5875 0.9419 0.1658  0.2752  0.1714  83  PHE   A O   
607  C  CB  . PHE   A 77  ? 0.4232 0.5593 1.0956 0.1806  0.2646  0.2605  83  PHE   A CB  
608  C  CG  . PHE   A 77  ? 0.4682 0.5371 1.1271 0.2033  0.3269  0.2419  83  PHE   A CG  
609  C  CD1 . PHE   A 77  ? 0.4813 0.5449 1.1474 0.2055  0.3132  0.2447  83  PHE   A CD1 
610  C  CD2 . PHE   A 77  ? 0.5138 0.5171 1.1482 0.2203  0.4022  0.2223  83  PHE   A CD2 
611  C  CE1 . PHE   A 77  ? 0.5225 0.5167 1.1705 0.2243  0.3717  0.2268  83  PHE   A CE1 
612  C  CE2 . PHE   A 77  ? 0.5579 0.4840 1.1652 0.2371  0.4636  0.2035  83  PHE   A CE2 
613  C  CZ  . PHE   A 77  ? 0.5572 0.4797 1.1716 0.2391  0.4471  0.2053  83  PHE   A CZ  
614  N  N   . VAL   A 78  ? 0.5806 0.5939 0.9154 0.1659  0.2582  0.1440  84  VAL   A N   
615  C  CA  . VAL   A 78  ? 0.6561 0.5957 0.8713 0.1650  0.2825  0.1029  84  VAL   A CA  
616  C  C   . VAL   A 78  ? 0.7065 0.5688 0.8975 0.1790  0.3372  0.0896  84  VAL   A C   
617  O  O   . VAL   A 78  ? 0.6998 0.5607 0.9109 0.1825  0.3298  0.0937  84  VAL   A O   
618  C  CB  . VAL   A 78  ? 0.6909 0.6319 0.8129 0.1461  0.2296  0.0771  84  VAL   A CB  
619  C  CG1 . VAL   A 78  ? 0.7577 0.6243 0.7645 0.1405  0.2450  0.0428  84  VAL   A CG1 
620  C  CG2 . VAL   A 78  ? 0.6649 0.6736 0.8111 0.1318  0.1836  0.0900  84  VAL   A CG2 
621  N  N   . GLU   A 79  ? 0.7563 0.5478 0.9000 0.1854  0.3956  0.0739  85  GLU   A N   
622  C  CA  . GLU   A 79  ? 0.8203 0.5134 0.9159 0.1948  0.4613  0.0564  85  GLU   A CA  
623  C  C   . GLU   A 79  ? 0.8790 0.5130 0.8586 0.1804  0.4355  0.0256  85  GLU   A C   
624  O  O   . GLU   A 79  ? 0.8998 0.5435 0.8054 0.1618  0.3808  0.0097  85  GLU   A O   
625  C  CB  . GLU   A 79  ? 0.9112 0.5296 0.9393 0.1944  0.5194  0.0397  85  GLU   A CB  
626  C  CG  . GLU   A 79  ? 0.9676 0.5849 1.1086 0.2169  0.5946  0.0656  85  GLU   A CG  
627  C  CD  . GLU   A 79  ? 1.1312 0.6251 1.2130 0.2254  0.6846  0.0457  85  GLU   A CD  
628  O  OE1 . GLU   A 79  ? 1.2092 0.6254 1.2183 0.2220  0.7412  0.0291  85  GLU   A OE1 
629  O  OE2 . GLU   A 79  ? 1.1733 0.6405 1.2741 0.2336  0.7011  0.0458  85  GLU   A OE2 
630  N  N   . ALA   A 80  ? 0.9027 0.4709 0.8697 0.1882  0.4769  0.0185  86  ALA   A N   
631  C  CA  . ALA   A 80  ? 0.9699 0.4729 0.8272 0.1722  0.4539  -0.0088 86  ALA   A CA  
632  C  C   . ALA   A 80  ? 1.0584 0.4819 0.7600 0.1468  0.4394  -0.0407 86  ALA   A C   
633  O  O   . ALA   A 80  ? 1.1072 0.4746 0.7573 0.1447  0.4824  -0.0496 86  ALA   A O   
634  C  CB  . ALA   A 80  ? 0.9989 0.4224 0.8546 0.1836  0.5161  -0.0137 86  ALA   A CB  
635  N  N   . SER   A 81  ? 1.0767 0.4956 0.7100 0.1263  0.3776  -0.0541 87  SER   A N   
636  C  CA  . SER   A 81  ? 1.1470 0.4953 0.6441 0.0983  0.3495  -0.0769 87  SER   A CA  
637  C  C   . SER   A 81  ? 1.2060 0.4893 0.6169 0.0766  0.3154  -0.0926 87  SER   A C   
638  O  O   . SER   A 81  ? 1.1957 0.4864 0.6496 0.0857  0.3215  -0.0886 87  SER   A O   
639  C  CB  . SER   A 81  ? 1.1166 0.5504 0.6426 0.0919  0.2911  -0.0682 87  SER   A CB  
640  O  OG  . SER   A 81  ? 1.0941 0.5985 0.6655 0.0875  0.2296  -0.0609 87  SER   A OG  
641  N  N   . GLU   A 82  ? 1.2632 0.4817 0.5559 0.0459  0.2762  -0.1072 88  GLU   A N   
642  C  CA  . GLU   A 82  ? 1.3099 0.4692 0.5250 0.0197  0.2319  -0.1171 88  GLU   A CA  
643  C  C   . GLU   A 82  ? 1.2155 0.4841 0.5312 0.0249  0.1700  -0.1016 88  GLU   A C   
644  O  O   . GLU   A 82  ? 1.2396 0.4813 0.5346 0.0126  0.1436  -0.1045 88  GLU   A O   
645  C  CB  . GLU   A 82  ? 1.4405 0.5084 0.5146 -0.0192 0.1928  -0.1284 88  GLU   A CB  
646  C  CG  . GLU   A 82  ? 1.5575 0.5914 0.5773 -0.0230 0.2208  -0.1326 88  GLU   A CG  
647  C  CD  . GLU   A 82  ? 1.7543 0.6952 0.6331 -0.0655 0.1741  -0.1392 88  GLU   A CD  
648  O  OE1 . GLU   A 82  ? 1.7457 0.7519 0.6611 -0.0752 0.1051  -0.1253 88  GLU   A OE1 
649  O  OE2 . GLU   A 82  ? 1.8858 0.6827 0.6161 -0.0910 0.2072  -0.1566 88  GLU   A OE2 
650  N  N   . TYR   A 83  ? 1.1107 0.4940 0.5290 0.0410  0.1504  -0.0856 89  TYR   A N   
651  C  CA  . TYR   A 83  ? 1.0245 0.5032 0.5294 0.0440  0.1007  -0.0720 89  TYR   A CA  
652  C  C   . TYR   A 83  ? 0.9328 0.4851 0.5449 0.0685  0.1210  -0.0576 89  TYR   A C   
653  O  O   . TYR   A 83  ? 0.9015 0.4973 0.5586 0.0670  0.0899  -0.0504 89  TYR   A O   
654  C  CB  . TYR   A 83  ? 0.9914 0.5373 0.5292 0.0408  0.0654  -0.0642 89  TYR   A CB  
655  C  CG  . TYR   A 83  ? 1.0544 0.5349 0.4984 0.0182  0.0459  -0.0726 89  TYR   A CG  
656  C  CD1 . TYR   A 83  ? 1.1033 0.5340 0.4882 -0.0095 -0.0041 -0.0744 89  TYR   A CD1 
657  C  CD2 . TYR   A 83  ? 1.0805 0.5450 0.4958 0.0219  0.0750  -0.0757 89  TYR   A CD2 
658  C  CE1 . TYR   A 83  ? 1.1681 0.5325 0.4635 -0.0351 -0.0295 -0.0772 89  TYR   A CE1 
659  C  CE2 . TYR   A 83  ? 1.1479 0.5459 0.4695 -0.0017 0.0555  -0.0817 89  TYR   A CE2 
660  C  CZ  . TYR   A 83  ? 1.1988 0.5452 0.4581 -0.0312 0.0010  -0.0816 89  TYR   A CZ  
661  O  OH  . TYR   A 83  ? 1.2733 0.5502 0.4386 -0.0589 -0.0261 -0.0825 89  TYR   A OH  
662  N  N   . TYR   A 84  ? 0.8826 0.4524 0.5431 0.0891  0.1694  -0.0493 90  TYR   A N   
663  C  CA  . TYR   A 84  ? 0.8019 0.4432 0.5712 0.1086  0.1803  -0.0282 90  TYR   A CA  
664  C  C   . TYR   A 84  ? 0.8109 0.4155 0.6107 0.1276  0.2445  -0.0222 90  TYR   A C   
665  O  O   . TYR   A 84  ? 0.8458 0.3958 0.6047 0.1303  0.2876  -0.0308 90  TYR   A O   
666  C  CB  . TYR   A 84  ? 0.7240 0.4601 0.5688 0.1141  0.1614  -0.0098 90  TYR   A CB  
667  C  CG  . TYR   A 84  ? 0.6942 0.4723 0.5269 0.0990  0.1102  -0.0131 90  TYR   A CG  
668  C  CD1 . TYR   A 84  ? 0.6942 0.4809 0.5030 0.0931  0.1018  -0.0175 90  TYR   A CD1 
669  C  CD2 . TYR   A 84  ? 0.6713 0.4835 0.5283 0.0921  0.0756  -0.0092 90  TYR   A CD2 
670  C  CE1 . TYR   A 84  ? 0.6837 0.5084 0.4948 0.0814  0.0616  -0.0185 90  TYR   A CE1 
671  C  CE2 . TYR   A 84  ? 0.6591 0.5072 0.5177 0.0802  0.0393  -0.0107 90  TYR   A CE2 
672  C  CZ  . TYR   A 84  ? 0.6677 0.5222 0.5064 0.0755  0.0332  -0.0151 90  TYR   A CZ  
673  O  OH  . TYR   A 84  ? 0.6453 0.5312 0.4945 0.0653  0.0032  -0.0155 90  TYR   A OH  
674  N  N   . PRO   A 85  ? 0.7715 0.4095 0.6554 0.1419  0.2549  -0.0036 91  PRO   A N   
675  C  CA  . PRO   A 85  ? 0.7611 0.3789 0.7082 0.1636  0.3186  0.0104  91  PRO   A CA  
676  C  C   . PRO   A 85  ? 0.7095 0.4009 0.7475 0.1747  0.3249  0.0361  91  PRO   A C   
677  O  O   . PRO   A 85  ? 0.6865 0.4357 0.7227 0.1639  0.2804  0.0389  91  PRO   A O   
678  C  CB  . PRO   A 85  ? 0.7363 0.3795 0.7547 0.1722  0.3123  0.0279  91  PRO   A CB  
679  C  CG  . PRO   A 85  ? 0.7065 0.4272 0.7408 0.1587  0.2425  0.0356  91  PRO   A CG  
680  C  CD  . PRO   A 85  ? 0.7226 0.4224 0.6593 0.1391  0.2110  0.0101  91  PRO   A CD  
681  N  N   . ALA   A 86  ? 0.6836 0.3711 0.8059 0.1950  0.3807  0.0566  92  ALA   A N   
682  C  CA  . ALA   A 86  ? 0.6313 0.3899 0.8529 0.2033  0.3827  0.0867  92  ALA   A CA  
683  C  C   . ALA   A 86  ? 0.5536 0.4121 0.8634 0.1976  0.3200  0.1190  92  ALA   A C   
684  O  O   . ALA   A 86  ? 0.5367 0.4074 0.8993 0.2025  0.3130  0.1354  92  ALA   A O   
685  C  CB  . ALA   A 86  ? 0.6248 0.3557 0.9350 0.2266  0.4585  0.1064  92  ALA   A CB  
686  N  N   . ARG   A 87  ? 0.5033 0.4232 0.8156 0.1838  0.2743  0.1265  93  ARG   A N   
687  C  CA  . ARG   A 87  ? 0.4444 0.4404 0.8093 0.1707  0.2144  0.1530  93  ARG   A CA  
688  C  C   . ARG   A 87  ? 0.4093 0.4644 0.8011 0.1575  0.1821  0.1707  93  ARG   A C   
689  O  O   . ARG   A 87  ? 0.4153 0.4578 0.7881 0.1606  0.2049  0.1610  93  ARG   A O   
690  C  CB  . ARG   A 87  ? 0.4742 0.4587 0.7530 0.1556  0.1757  0.1272  93  ARG   A CB  
691  C  CG  . ARG   A 87  ? 0.4793 0.4726 0.6788 0.1383  0.1434  0.1039  93  ARG   A CG  
692  C  CD  . ARG   A 87  ? 0.5048 0.4431 0.6045 0.1325  0.1415  0.0672  93  ARG   A CD  
693  N  NE  . ARG   A 87  ? 0.4758 0.4392 0.5333 0.1158  0.1031  0.0556  93  ARG   A NE  
694  C  CZ  . ARG   A 87  ? 0.4694 0.4291 0.4915 0.1114  0.1028  0.0445  93  ARG   A CZ  
695  N  NH1 . ARG   A 87  ? 0.4363 0.4182 0.4319 0.0975  0.0712  0.0362  93  ARG   A NH1 
696  N  NH2 . ARG   A 87  ? 0.4590 0.3891 0.4741 0.1208  0.1383  0.0422  93  ARG   A NH2 
697  N  N   . TYR   A 88  ? 0.3771 0.4879 0.8013 0.1394  0.1290  0.1953  94  TYR   A N   
698  C  CA  . TYR   A 88  ? 0.3615 0.5158 0.7879 0.1201  0.0931  0.2082  94  TYR   A CA  
699  C  C   . TYR   A 88  ? 0.3673 0.5125 0.6877 0.1025  0.0647  0.1745  94  TYR   A C   
700  O  O   . TYR   A 88  ? 0.3782 0.5172 0.6640 0.0946  0.0450  0.1655  94  TYR   A O   
701  C  CB  . TYR   A 88  ? 0.3383 0.5434 0.8437 0.1028  0.0491  0.2555  94  TYR   A CB  
702  C  CG  . TYR   A 88  ? 0.3169 0.5470 0.9549 0.1156  0.0668  0.3008  94  TYR   A CG  
703  C  CD1 . TYR   A 88  ? 0.3122 0.5675 1.0023 0.1134  0.0703  0.3207  94  TYR   A CD1 
704  C  CD2 . TYR   A 88  ? 0.3098 0.5395 1.0321 0.1298  0.0806  0.3273  94  TYR   A CD2 
705  C  CE1 . TYR   A 88  ? 0.2780 0.5599 1.1095 0.1254  0.0877  0.3679  94  TYR   A CE1 
706  C  CE2 . TYR   A 88  ? 0.2749 0.5289 1.1389 0.1434  0.1006  0.3736  94  TYR   A CE2 
707  C  CZ  . TYR   A 88  ? 0.2672 0.5488 1.1902 0.1411  0.1040  0.3952  94  TYR   A CZ  
708  O  OH  . TYR   A 88  ? 0.2484 0.5577 1.3318 0.1547  0.1242  0.4470  94  TYR   A OH  
709  N  N   . GLN   A 89  ? 0.3504 0.4943 0.6277 0.0971  0.0652  0.1581  95  GLN   A N   
710  C  CA  . GLN   A 89  ? 0.3559 0.4924 0.5502 0.0820  0.0427  0.1303  95  GLN   A CA  
711  C  C   . GLN   A 89  ? 0.3285 0.5012 0.5285 0.0576  0.0074  0.1485  95  GLN   A C   
712  O  O   . GLN   A 89  ? 0.3154 0.5089 0.5525 0.0541  0.0061  0.1671  95  GLN   A O   
713  C  CB  . GLN   A 89  ? 0.3834 0.4851 0.5185 0.0900  0.0653  0.0995  95  GLN   A CB  
714  C  CG  . GLN   A 89  ? 0.4088 0.5081 0.4794 0.0752  0.0418  0.0768  95  GLN   A CG  
715  C  CD  . GLN   A 89  ? 0.4570 0.5136 0.4679 0.0813  0.0552  0.0489  95  GLN   A CD  
716  O  OE1 . GLN   A 89  ? 0.4987 0.5125 0.4859 0.0912  0.0739  0.0377  95  GLN   A OE1 
717  N  NE2 . GLN   A 89  ? 0.4262 0.4871 0.4068 0.0722  0.0436  0.0383  95  GLN   A NE2 
718  N  N   . SER   A 90  ? 0.3223 0.4970 0.4858 0.0385  -0.0196 0.1454  96  SER   A N   
719  C  CA  . SER   A 90  ? 0.3132 0.5039 0.4590 0.0085  -0.0519 0.1604  96  SER   A CA  
720  C  C   . SER   A 90  ? 0.3336 0.5106 0.4141 -0.0008 -0.0490 0.1324  96  SER   A C   
721  O  O   . SER   A 90  ? 0.3553 0.5131 0.4058 0.0141  -0.0295 0.1030  96  SER   A O   
722  C  CB  . SER   A 90  ? 0.3265 0.5122 0.4541 -0.0105 -0.0750 0.1704  96  SER   A CB  
723  O  OG  . SER   A 90  ? 0.3740 0.5358 0.4537 -0.0043 -0.0613 0.1391  96  SER   A OG  
724  N  N   . HIS   A 91  ? 0.3212 0.5043 0.3820 -0.0274 -0.0703 0.1443  97  HIS   A N   
725  C  CA  . HIS   A 91  ? 0.3410 0.5080 0.3433 -0.0400 -0.0667 0.1217  97  HIS   A CA  
726  C  C   . HIS   A 91  ? 0.3321 0.5014 0.3431 -0.0191 -0.0452 0.1058  97  HIS   A C   
727  O  O   . HIS   A 91  ? 0.3474 0.5002 0.3175 -0.0192 -0.0352 0.0813  97  HIS   A O   
728  C  CB  . HIS   A 91  ? 0.3638 0.5031 0.3111 -0.0467 -0.0583 0.0961  97  HIS   A CB  
729  C  CG  . HIS   A 91  ? 0.4057 0.5322 0.3284 -0.0718 -0.0754 0.1100  97  HIS   A CG  
730  N  ND1 . HIS   A 91  ? 0.4558 0.5544 0.3157 -0.1077 -0.0860 0.1120  97  HIS   A ND1 
731  C  CD2 . HIS   A 91  ? 0.4054 0.5358 0.3506 -0.0681 -0.0825 0.1227  97  HIS   A CD2 
732  C  CE1 . HIS   A 91  ? 0.4721 0.5561 0.3130 -0.1259 -0.0996 0.1257  97  HIS   A CE1 
733  N  NE2 . HIS   A 91  ? 0.4409 0.5477 0.3373 -0.1021 -0.0997 0.1339  97  HIS   A NE2 
734  N  N   . LEU   A 92  ? 0.3109 0.4972 0.3779 -0.0022 -0.0356 0.1220  98  LEU   A N   
735  C  CA  . LEU   A 92  ? 0.3180 0.4979 0.3876 0.0164  -0.0108 0.1089  98  LEU   A CA  
736  C  C   . LEU   A 92  ? 0.3021 0.4996 0.3897 0.0045  -0.0180 0.1246  98  LEU   A C   
737  O  O   . LEU   A 92  ? 0.2883 0.5099 0.4228 -0.0096 -0.0380 0.1571  98  LEU   A O   
738  C  CB  . LEU   A 92  ? 0.3102 0.4829 0.4214 0.0424  0.0168  0.1133  98  LEU   A CB  
739  C  CG  . LEU   A 92  ? 0.3533 0.5004 0.4478 0.0599  0.0493  0.0968  98  LEU   A CG  
740  C  CD1 . LEU   A 92  ? 0.4016 0.5153 0.4231 0.0606  0.0487  0.0641  98  LEU   A CD1 
741  C  CD2 . LEU   A 92  ? 0.3544 0.4837 0.4888 0.0813  0.0849  0.1047  98  LEU   A CD2 
742  N  N   . MET   A 93  ? 0.3112 0.4957 0.3655 0.0083  -0.0053 0.1050  99  MET   A N   
743  C  CA  . MET   A 93  ? 0.3034 0.5009 0.3694 -0.0028 -0.0101 0.1166  99  MET   A CA  
744  C  C   . MET   A 93  ? 0.3134 0.5026 0.3947 0.0189  0.0219  0.1110  99  MET   A C   
745  O  O   . MET   A 93  ? 0.3473 0.5067 0.3836 0.0318  0.0390  0.0848  99  MET   A O   
746  C  CB  . MET   A 93  ? 0.3260 0.5081 0.3289 -0.0231 -0.0230 0.0981  99  MET   A CB  
747  C  CG  . MET   A 93  ? 0.3509 0.5261 0.3227 -0.0500 -0.0472 0.1027  99  MET   A CG  
748  S  SD  . MET   A 93  ? 0.4263 0.5665 0.3202 -0.0717 -0.0451 0.0762  99  MET   A SD  
749  C  CE  . MET   A 93  ? 0.4083 0.5350 0.2954 -0.0421 -0.0185 0.0452  99  MET   A CE  
750  N  N   . LEU   A 94  ? 0.2841 0.4949 0.4285 0.0204  0.0299  0.1376  100 LEU   A N   
751  C  CA  . LEU   A 94  ? 0.2935 0.4881 0.4481 0.0394  0.0686  0.1325  100 LEU   A CA  
752  C  C   . LEU   A 94  ? 0.2906 0.4908 0.4351 0.0285  0.0654  0.1334  100 LEU   A C   
753  O  O   . LEU   A 94  ? 0.2642 0.4905 0.4274 0.0061  0.0346  0.1515  100 LEU   A O   
754  C  CB  . LEU   A 94  ? 0.2688 0.4752 0.5132 0.0558  0.0982  0.1606  100 LEU   A CB  
755  C  CG  . LEU   A 94  ? 0.3011 0.4935 0.5622 0.0717  0.1142  0.1599  100 LEU   A CG  
756  C  CD1 . LEU   A 94  ? 0.2749 0.4692 0.6284 0.0910  0.1578  0.1857  100 LEU   A CD1 
757  C  CD2 . LEU   A 94  ? 0.3627 0.5029 0.5318 0.0818  0.1308  0.1207  100 LEU   A CD2 
758  N  N   . ALA   A 95  ? 0.3158 0.4849 0.4265 0.0417  0.0969  0.1157  101 ALA   A N   
759  C  CA  . ALA   A 95  ? 0.3358 0.5036 0.4358 0.0352  0.1019  0.1152  101 ALA   A CA  
760  C  C   . ALA   A 95  ? 0.3628 0.4971 0.4610 0.0534  0.1508  0.1116  101 ALA   A C   
761  O  O   . ALA   A 95  ? 0.3827 0.4778 0.4500 0.0678  0.1778  0.0976  101 ALA   A O   
762  C  CB  . ALA   A 95  ? 0.3692 0.5166 0.3903 0.0254  0.0822  0.0878  101 ALA   A CB  
763  N  N   . VAL   A 96  ? 0.3675 0.5089 0.4891 0.0499  0.1639  0.1230  102 VAL   A N   
764  C  CA  . VAL   A 96  ? 0.4064 0.5067 0.5131 0.0631  0.2146  0.1182  102 VAL   A CA  
765  C  C   . VAL   A 96  ? 0.4803 0.5337 0.4786 0.0582  0.2072  0.0867  102 VAL   A C   
766  O  O   . VAL   A 96  ? 0.4860 0.5556 0.4625 0.0445  0.1740  0.0815  102 VAL   A O   
767  C  CB  . VAL   A 96  ? 0.3811 0.5118 0.5695 0.0603  0.2314  0.1477  102 VAL   A CB  
768  C  CG1 . VAL   A 96  ? 0.4109 0.4897 0.5679 0.0710  0.2885  0.1392  102 VAL   A CG1 
769  C  CG2 . VAL   A 96  ? 0.3275 0.5051 0.6408 0.0645  0.2349  0.1863  102 VAL   A CG2 
770  N  N   . GLY   A 97  ? 0.5344 0.5261 0.4641 0.0666  0.2336  0.0673  103 GLY   A N   
771  C  CA  . GLY   A 97  ? 0.6050 0.5472 0.4346 0.0588  0.2188  0.0432  103 GLY   A CA  
772  C  C   . GLY   A 97  ? 0.6746 0.5415 0.4251 0.0626  0.2415  0.0259  103 GLY   A C   
773  O  O   . GLY   A 97  ? 0.6859 0.5440 0.4570 0.0725  0.2630  0.0276  103 GLY   A O   
774  N  N   . HIS   A 98  ? 0.7197 0.5261 0.3755 0.0517  0.2340  0.0109  104 HIS   A N   
775  C  CA  . HIS   A 98  ? 0.7817 0.5013 0.3411 0.0467  0.2478  -0.0047 104 HIS   A CA  
776  C  C   . HIS   A 98  ? 0.7756 0.4948 0.3146 0.0424  0.2044  -0.0140 104 HIS   A C   
777  O  O   . HIS   A 98  ? 0.7432 0.5014 0.3001 0.0367  0.1568  -0.0139 104 HIS   A O   
778  C  CB  . HIS   A 98  ? 0.8612 0.5052 0.3181 0.0305  0.2514  -0.0124 104 HIS   A CB  
779  C  CG  . HIS   A 98  ? 0.9743 0.5146 0.3114 0.0163  0.2568  -0.0271 104 HIS   A CG  
780  N  ND1 . HIS   A 98  ? 1.0449 0.5133 0.3365 0.0195  0.3185  -0.0337 104 HIS   A ND1 
781  C  CD2 . HIS   A 98  ? 1.0289 0.5260 0.2900 -0.0027 0.2061  -0.0338 104 HIS   A CD2 
782  C  CE1 . HIS   A 98  ? 1.1219 0.4984 0.2947 -0.0007 0.3023  -0.0470 104 HIS   A CE1 
783  N  NE2 . HIS   A 98  ? 1.1185 0.5129 0.2742 -0.0151 0.2305  -0.0452 104 HIS   A NE2 
784  N  N   . SER   A 99  ? 0.8102 0.4761 0.3080 0.0441  0.2255  -0.0222 105 SER   A N   
785  C  CA  . SER   A 99  ? 0.8385 0.4901 0.3073 0.0376  0.1878  -0.0306 105 SER   A CA  
786  C  C   . SER   A 99  ? 0.9211 0.4767 0.3030 0.0320  0.2196  -0.0427 105 SER   A C   
787  O  O   . SER   A 99  ? 0.9305 0.4536 0.3127 0.0419  0.2801  -0.0431 105 SER   A O   
788  C  CB  . SER   A 99  ? 0.7792 0.5160 0.3465 0.0500  0.1680  -0.0229 105 SER   A CB  
789  O  OG  . SER   A 99  ? 0.7797 0.5337 0.4041 0.0658  0.2095  -0.0151 105 SER   A OG  
790  N  N   . GLU   A 100 ? 0.9784 0.4840 0.2877 0.0145  0.1801  -0.0510 106 GLU   A N   
791  C  CA  . GLU   A 100 ? 1.0667 0.4741 0.2819 0.0033  0.1998  -0.0636 106 GLU   A CA  
792  C  C   . GLU   A 100 ? 1.0775 0.4969 0.2981 -0.0045 0.1454  -0.0646 106 GLU   A C   
793  O  O   . GLU   A 100 ? 1.0418 0.5289 0.3208 -0.0053 0.0938  -0.0558 106 GLU   A O   
794  C  CB  . GLU   A 100 ? 1.1949 0.4777 0.2637 -0.0226 0.2174  -0.0730 106 GLU   A CB  
795  C  CG  . GLU   A 100 ? 1.2807 0.5572 0.3087 -0.0430 0.1668  -0.0659 106 GLU   A CG  
796  C  CD  . GLU   A 100 ? 1.4278 0.5735 0.3025 -0.0716 0.1874  -0.0732 106 GLU   A CD  
797  O  OE1 . GLU   A 100 ? 1.5000 0.5400 0.2539 -0.0993 0.1730  -0.0813 106 GLU   A OE1 
798  O  OE2 . GLU   A 100 ? 1.4494 0.5915 0.3175 -0.0694 0.2176  -0.0704 106 GLU   A OE2 
799  N  N   . PRO   A 101 ? 1.1209 0.4823 0.2962 -0.0084 0.1596  -0.0740 107 PRO   A N   
800  C  CA  . PRO   A 101 ? 1.1112 0.4900 0.3016 -0.0167 0.1050  -0.0723 107 PRO   A CA  
801  C  C   . PRO   A 101 ? 1.1491 0.4841 0.2699 -0.0474 0.0413  -0.0673 107 PRO   A C   
802  O  O   . PRO   A 101 ? 1.2523 0.4848 0.2510 -0.0728 0.0432  -0.0721 107 PRO   A O   
803  C  CB  . PRO   A 101 ? 1.1663 0.4724 0.3035 -0.0179 0.1403  -0.0842 107 PRO   A CB  
804  C  CG  . PRO   A 101 ? 1.2367 0.4432 0.2782 -0.0236 0.2048  -0.0954 107 PRO   A CG  
805  C  CD  . PRO   A 101 ? 1.1727 0.4400 0.2756 -0.0081 0.2273  -0.0865 107 PRO   A CD  
806  N  N   . GLY   A 102 ? 1.0646 0.4784 0.2697 -0.0448 -0.0105 -0.0550 108 GLY   A N   
807  C  CA  . GLY   A 102 ? 1.0484 0.4531 0.2395 -0.0675 -0.0736 -0.0417 108 GLY   A CA  
808  C  C   . GLY   A 102 ? 0.9463 0.4531 0.2486 -0.0497 -0.0835 -0.0314 108 GLY   A C   
809  O  O   . GLY   A 102 ? 0.9223 0.4572 0.2704 -0.0583 -0.1326 -0.0171 108 GLY   A O   
810  N  N   . ASP   A 103 ? 0.8797 0.4396 0.2306 -0.0260 -0.0352 -0.0368 109 ASP   A N   
811  C  CA  . ASP   A 103 ? 0.7893 0.4372 0.2335 -0.0110 -0.0366 -0.0299 109 ASP   A CA  
812  C  C   . ASP   A 103 ? 0.6991 0.4239 0.2390 0.0035  -0.0424 -0.0278 109 ASP   A C   
813  O  O   . ASP   A 103 ? 0.6355 0.4183 0.2417 0.0087  -0.0531 -0.0221 109 ASP   A O   
814  C  CB  . ASP   A 103 ? 0.7878 0.4505 0.2358 0.0014  0.0104  -0.0328 109 ASP   A CB  
815  C  CG  . ASP   A 103 ? 0.8665 0.4632 0.2314 -0.0141 0.0125  -0.0326 109 ASP   A CG  
816  O  OD1 . ASP   A 103 ? 0.8761 0.4547 0.2206 -0.0309 -0.0325 -0.0246 109 ASP   A OD1 
817  O  OD2 . ASP   A 103 ? 0.8994 0.4602 0.2235 -0.0103 0.0601  -0.0381 109 ASP   A OD2 
818  N  N   . CYS   A 104 ? 0.6914 0.4081 0.2316 0.0072  -0.0358 -0.0323 110 CYS   A N   
819  C  CA  . CYS   A 104 ? 0.6442 0.4235 0.2639 0.0175  -0.0423 -0.0297 110 CYS   A CA  
820  C  C   . CYS   A 104 ? 0.6076 0.4122 0.2741 0.0096  -0.0826 -0.0209 110 CYS   A C   
821  O  O   . CYS   A 104 ? 0.6371 0.3979 0.2707 -0.0069 -0.1173 -0.0145 110 CYS   A O   
822  C  CB  . CYS   A 104 ? 0.6730 0.4243 0.2736 0.0185  -0.0355 -0.0346 110 CYS   A CB  
823  S  SG  . CYS   A 104 ? 0.7538 0.5021 0.3529 0.0359  0.0217  -0.0393 110 CYS   A SG  
824  N  N   . GLY   A 105 ? 0.5472 0.4154 0.2879 0.0189  -0.0763 -0.0185 111 GLY   A N   
825  C  CA  . GLY   A 105 ? 0.5157 0.4083 0.3152 0.0146  -0.1003 -0.0100 111 GLY   A CA  
826  C  C   . GLY   A 105 ? 0.4996 0.4122 0.3206 0.0155  -0.0953 -0.0073 111 GLY   A C   
827  O  O   . GLY   A 105 ? 0.4805 0.4192 0.3632 0.0158  -0.0999 -0.0016 111 GLY   A O   
828  N  N   . GLY   A 106 ? 0.5049 0.4025 0.2791 0.0160  -0.0811 -0.0111 112 GLY   A N   
829  C  CA  . GLY   A 106 ? 0.4795 0.3946 0.2701 0.0163  -0.0748 -0.0091 112 GLY   A CA  
830  C  C   . GLY   A 106 ? 0.4313 0.3954 0.2697 0.0229  -0.0508 -0.0133 112 GLY   A C   
831  O  O   . GLY   A 106 ? 0.4244 0.4069 0.2623 0.0273  -0.0337 -0.0172 112 GLY   A O   
832  N  N   . ILE   A 107 ? 0.4005 0.3794 0.2783 0.0210  -0.0500 -0.0111 113 ILE   A N   
833  C  CA  . ILE   A 107 ? 0.3746 0.3821 0.2821 0.0208  -0.0265 -0.0164 113 ILE   A CA  
834  C  C   . ILE   A 107 ? 0.3678 0.3853 0.2496 0.0178  -0.0099 -0.0194 113 ILE   A C   
835  O  O   . ILE   A 107 ? 0.3875 0.3932 0.2506 0.0172  -0.0139 -0.0170 113 ILE   A O   
836  C  CB  . ILE   A 107 ? 0.3710 0.3781 0.3361 0.0196  -0.0265 -0.0124 113 ILE   A CB  
837  C  CG1 . ILE   A 107 ? 0.3724 0.3834 0.3814 0.0214  -0.0302 -0.0091 113 ILE   A CG1 
838  C  CG2 . ILE   A 107 ? 0.3719 0.3853 0.3480 0.0153  0.0021  -0.0192 113 ILE   A CG2 
839  C  CD1 . ILE   A 107 ? 0.3698 0.3778 0.4538 0.0221  -0.0337 0.0018  113 ILE   A CD1 
840  N  N   . LEU   A 108 ? 0.3457 0.3819 0.2257 0.0128  0.0051  -0.0221 114 LEU   A N   
841  C  CA  . LEU   A 108 ? 0.3529 0.3996 0.2164 0.0040  0.0152  -0.0208 114 LEU   A CA  
842  C  C   . LEU   A 108 ? 0.3585 0.3988 0.2266 -0.0089 0.0294  -0.0274 114 LEU   A C   
843  O  O   . LEU   A 108 ? 0.3351 0.3710 0.2126 -0.0123 0.0374  -0.0314 114 LEU   A O   
844  C  CB  . LEU   A 108 ? 0.3546 0.4193 0.2115 0.0025  0.0154  -0.0129 114 LEU   A CB  
845  C  CG  . LEU   A 108 ? 0.3627 0.4407 0.2127 -0.0138 0.0172  -0.0051 114 LEU   A CG  
846  C  CD1 . LEU   A 108 ? 0.3756 0.4547 0.2212 -0.0145 0.0193  -0.0007 114 LEU   A CD1 
847  C  CD2 . LEU   A 108 ? 0.3515 0.4494 0.2147 -0.0156 0.0114  0.0093  114 LEU   A CD2 
848  N  N   . ARG   A 109 ? 0.3801 0.4119 0.2384 -0.0165 0.0365  -0.0294 115 ARG   A N   
849  C  CA  . ARG   A 109 ? 0.4079 0.4184 0.2611 -0.0299 0.0570  -0.0380 115 ARG   A CA  
850  C  C   . ARG   A 109 ? 0.4396 0.4435 0.2556 -0.0486 0.0595  -0.0373 115 ARG   A C   
851  O  O   . ARG   A 109 ? 0.4234 0.4391 0.2377 -0.0455 0.0488  -0.0306 115 ARG   A O   
852  C  CB  . ARG   A 109 ? 0.4307 0.4269 0.3202 -0.0204 0.0645  -0.0403 115 ARG   A CB  
853  C  CG  . ARG   A 109 ? 0.4972 0.4912 0.4385 -0.0085 0.0655  -0.0384 115 ARG   A CG  
854  C  CD  . ARG   A 109 ? 0.5491 0.5291 0.5414 -0.0023 0.0726  -0.0345 115 ARG   A CD  
855  N  NE  . ARG   A 109 ? 0.6234 0.5774 0.6074 -0.0134 0.1090  -0.0450 115 ARG   A NE  
856  C  CZ  . ARG   A 109 ? 0.6524 0.5821 0.6543 -0.0184 0.1464  -0.0532 115 ARG   A CZ  
857  N  NH1 . ARG   A 109 ? 0.6682 0.5601 0.6434 -0.0323 0.1838  -0.0652 115 ARG   A NH1 
858  N  NH2 . ARG   A 109 ? 0.6247 0.5611 0.6671 -0.0112 0.1502  -0.0498 115 ARG   A NH2 
859  N  N   . CYS   A 110 ? 0.4803 0.4565 0.2623 -0.0708 0.0757  -0.0443 116 CYS   A N   
860  C  CA  . CYS   A 110 ? 0.5311 0.4868 0.2675 -0.0962 0.0766  -0.0442 116 CYS   A CA  
861  C  C   . CYS   A 110 ? 0.5859 0.4945 0.3112 -0.1034 0.1115  -0.0605 116 CYS   A C   
862  O  O   . CYS   A 110 ? 0.5706 0.4759 0.3427 -0.0842 0.1296  -0.0662 116 CYS   A O   
863  C  CB  . CYS   A 110 ? 0.5536 0.5002 0.2436 -0.1237 0.0642  -0.0368 116 CYS   A CB  
864  S  SG  . CYS   A 110 ? 0.5990 0.5020 0.2557 -0.1371 0.0913  -0.0503 116 CYS   A SG  
865  N  N   . GLN   A 111 ? 0.6469 0.5143 0.3141 -0.1326 0.1220  -0.0663 117 GLN   A N   
866  C  CA  . GLN   A 111 ? 0.7022 0.5131 0.3527 -0.1413 0.1641  -0.0835 117 GLN   A CA  
867  C  C   . GLN   A 111 ? 0.7420 0.5091 0.3789 -0.1475 0.2036  -0.0969 117 GLN   A C   
868  O  O   . GLN   A 111 ? 0.7645 0.4869 0.4128 -0.1461 0.2493  -0.1103 117 GLN   A O   
869  C  CB  . GLN   A 111 ? 0.7746 0.5408 0.3502 -0.1765 0.1649  -0.0872 117 GLN   A CB  
870  C  CG  . GLN   A 111 ? 0.8740 0.6012 0.3613 -0.2172 0.1547  -0.0857 117 GLN   A CG  
871  C  CD  . GLN   A 111 ? 0.9872 0.6685 0.3977 -0.2569 0.1446  -0.0848 117 GLN   A CD  
872  O  OE1 . GLN   A 111 ? 1.0074 0.7218 0.4149 -0.2701 0.0994  -0.0642 117 GLN   A OE1 
873  N  NE2 . GLN   A 111 ? 1.0364 0.6364 0.3863 -0.2782 0.1885  -0.1059 117 GLN   A NE2 
874  N  N   . HIS   A 112 ? 0.7480 0.5235 0.3629 -0.1552 0.1907  -0.0923 118 HIS   A N   
875  C  CA  . HIS   A 112 ? 0.7718 0.5026 0.3681 -0.1632 0.2302  -0.1042 118 HIS   A CA  
876  C  C   . HIS   A 112 ? 0.7130 0.4831 0.3992 -0.1293 0.2362  -0.1005 118 HIS   A C   
877  O  O   . HIS   A 112 ? 0.7338 0.4701 0.4212 -0.1324 0.2740  -0.1089 118 HIS   A O   
878  C  CB  . HIS   A 112 ? 0.8358 0.5403 0.3455 -0.1977 0.2139  -0.1004 118 HIS   A CB  
879  C  CG  . HIS   A 112 ? 0.9345 0.6086 0.3578 -0.2368 0.1879  -0.0948 118 HIS   A CG  
880  N  ND1 . HIS   A 112 ? 0.9438 0.6745 0.3837 -0.2371 0.1324  -0.0724 118 HIS   A ND1 
881  C  CD2 . HIS   A 112 ? 1.0233 0.6114 0.3432 -0.2794 0.2100  -0.1065 118 HIS   A CD2 
882  C  CE1 . HIS   A 112 ? 0.9996 0.6847 0.3568 -0.2797 0.1165  -0.0678 118 HIS   A CE1 
883  N  NE2 . HIS   A 112 ? 1.0552 0.6506 0.3300 -0.3080 0.1599  -0.0891 118 HIS   A NE2 
884  N  N   . GLY   A 113 ? 0.6389 0.4731 0.3916 -0.1012 0.1992  -0.0871 119 GLY   A N   
885  C  CA  . GLY   A 113 ? 0.5837 0.4510 0.4145 -0.0741 0.1951  -0.0807 119 GLY   A CA  
886  C  C   . GLY   A 113 ? 0.5384 0.4582 0.3833 -0.0607 0.1490  -0.0674 119 GLY   A C   
887  O  O   . GLY   A 113 ? 0.5315 0.4737 0.3539 -0.0622 0.1203  -0.0604 119 GLY   A O   
888  N  N   . VAL   A 114 ? 0.5060 0.4420 0.3924 -0.0474 0.1458  -0.0634 120 VAL   A N   
889  C  CA  . VAL   A 114 ? 0.4813 0.4565 0.3815 -0.0342 0.1090  -0.0529 120 VAL   A CA  
890  C  C   . VAL   A 114 ? 0.4840 0.4654 0.3310 -0.0490 0.0955  -0.0494 120 VAL   A C   
891  O  O   . VAL   A 114 ? 0.5005 0.4591 0.3179 -0.0651 0.1116  -0.0533 120 VAL   A O   
892  C  CB  . VAL   A 114 ? 0.4691 0.4531 0.4325 -0.0185 0.1091  -0.0487 120 VAL   A CB  
893  C  CG1 . VAL   A 114 ? 0.4685 0.4792 0.4302 -0.0097 0.0770  -0.0409 120 VAL   A CG1 
894  C  CG2 . VAL   A 114 ? 0.4528 0.4382 0.4826 -0.0044 0.1064  -0.0423 120 VAL   A CG2 
895  N  N   . VAL   A 115 ? 0.4604 0.4693 0.2991 -0.0444 0.0673  -0.0397 121 VAL   A N   
896  C  CA  . VAL   A 115 ? 0.4616 0.4836 0.2728 -0.0560 0.0500  -0.0289 121 VAL   A CA  
897  C  C   . VAL   A 115 ? 0.4386 0.4833 0.2781 -0.0393 0.0367  -0.0224 121 VAL   A C   
898  O  O   . VAL   A 115 ? 0.4423 0.4888 0.2705 -0.0483 0.0314  -0.0159 121 VAL   A O   
899  C  CB  . VAL   A 115 ? 0.4695 0.5073 0.2702 -0.0609 0.0335  -0.0183 121 VAL   A CB  
900  C  CG1 . VAL   A 115 ? 0.4717 0.5293 0.2691 -0.0707 0.0124  0.0005  121 VAL   A CG1 
901  C  CG2 . VAL   A 115 ? 0.4946 0.5048 0.2601 -0.0814 0.0444  -0.0245 121 VAL   A CG2 
902  N  N   . GLY   A 116 ? 0.4141 0.4692 0.2836 -0.0181 0.0298  -0.0233 122 GLY   A N   
903  C  CA  . GLY   A 116 ? 0.3968 0.4624 0.2833 -0.0041 0.0183  -0.0190 122 GLY   A CA  
904  C  C   . GLY   A 116 ? 0.3767 0.4368 0.2735 0.0115  0.0084  -0.0201 122 GLY   A C   
905  O  O   . GLY   A 116 ? 0.3729 0.4236 0.2738 0.0125  0.0081  -0.0231 122 GLY   A O   
906  N  N   . ILE   A 117 ? 0.3588 0.4168 0.2546 0.0210  -0.0003 -0.0172 123 ILE   A N   
907  C  CA  . ILE   A 117 ? 0.3581 0.3937 0.2418 0.0293  -0.0118 -0.0183 123 ILE   A CA  
908  C  C   . ILE   A 117 ? 0.3502 0.3759 0.2084 0.0362  -0.0056 -0.0153 123 ILE   A C   
909  O  O   . ILE   A 117 ? 0.3222 0.3626 0.1917 0.0386  0.0022  -0.0101 123 ILE   A O   
910  C  CB  . ILE   A 117 ? 0.3723 0.3943 0.2742 0.0302  -0.0268 -0.0189 123 ILE   A CB  
911  C  CG1 . ILE   A 117 ? 0.3795 0.4131 0.2949 0.0308  -0.0223 -0.0182 123 ILE   A CG1 
912  C  CG2 . ILE   A 117 ? 0.3681 0.3905 0.3082 0.0264  -0.0312 -0.0177 123 ILE   A CG2 
913  C  CD1 . ILE   A 117 ? 0.3994 0.4136 0.3215 0.0325  -0.0397 -0.0171 123 ILE   A CD1 
914  N  N   . VAL   A 118 ? 0.3649 0.3583 0.1886 0.0383  -0.0071 -0.0174 124 VAL   A N   
915  C  CA  . VAL   A 118 ? 0.3824 0.3503 0.1754 0.0446  0.0104  -0.0167 124 VAL   A CA  
916  C  C   . VAL   A 118 ? 0.3795 0.3306 0.1678 0.0485  0.0109  -0.0185 124 VAL   A C   
917  O  O   . VAL   A 118 ? 0.3647 0.3013 0.1482 0.0436  -0.0103 -0.0218 124 VAL   A O   
918  C  CB  . VAL   A 118 ? 0.4317 0.3512 0.1698 0.0409  0.0116  -0.0204 124 VAL   A CB  
919  C  CG1 . VAL   A 118 ? 0.4619 0.3419 0.1627 0.0466  0.0421  -0.0219 124 VAL   A CG1 
920  C  CG2 . VAL   A 118 ? 0.4335 0.3711 0.1798 0.0377  0.0128  -0.0176 124 VAL   A CG2 
921  N  N   . SER   A 119 ? 0.3898 0.3447 0.1899 0.0572  0.0349  -0.0134 125 SER   A N   
922  C  CA  . SER   A 119 ? 0.4289 0.3681 0.2295 0.0618  0.0389  -0.0143 125 SER   A CA  
923  C  C   . SER   A 119 ? 0.4778 0.3817 0.2634 0.0716  0.0749  -0.0130 125 SER   A C   
924  O  O   . SER   A 119 ? 0.4929 0.3590 0.2556 0.0738  0.0823  -0.0184 125 SER   A O   
925  C  CB  . SER   A 119 ? 0.4156 0.4050 0.2707 0.0620  0.0301  -0.0053 125 SER   A CB  
926  O  OG  . SER   A 119 ? 0.4334 0.4161 0.3030 0.0693  0.0410  -0.0007 125 SER   A OG  
927  N  N   . THR   A 120 ? 0.4958 0.4101 0.2999 0.0773  0.1008  -0.0049 126 THR   A N   
928  C  CA  . THR   A 120 ? 0.5508 0.4307 0.3548 0.0883  0.1466  -0.0012 126 THR   A CA  
929  C  C   . THR   A 120 ? 0.5969 0.4686 0.3915 0.0883  0.1689  0.0015  126 THR   A C   
930  O  O   . THR   A 120 ? 0.5835 0.4810 0.3743 0.0798  0.1442  0.0011  126 THR   A O   
931  C  CB  . THR   A 120 ? 0.5342 0.4522 0.4196 0.1003  0.1619  0.0176  126 THR   A CB  
932  O  OG1 . THR   A 120 ? 0.5839 0.4497 0.4633 0.1123  0.2130  0.0172  126 THR   A OG1 
933  C  CG2 . THR   A 120 ? 0.4815 0.4687 0.4467 0.1000  0.1533  0.0414  126 THR   A CG2 
934  N  N   . GLY   A 121 ? 0.6441 0.4748 0.4344 0.0975  0.2194  0.0037  127 GLY   A N   
935  C  CA  . GLY   A 121 ? 0.6911 0.5088 0.4751 0.0980  0.2482  0.0074  127 GLY   A CA  
936  C  C   . GLY   A 121 ? 0.7643 0.5111 0.5241 0.1071  0.3154  0.0046  127 GLY   A C   
937  O  O   . GLY   A 121 ? 0.7800 0.4899 0.5367 0.1146  0.3426  0.0012  127 GLY   A O   
938  N  N   . GLY   A 122 ? 0.8088 0.5309 0.5500 0.1058  0.3469  0.0057  128 GLY   A N   
939  C  CA  . GLY   A 122 ? 0.8776 0.5233 0.5922 0.1131  0.4224  0.0028  128 GLY   A CA  
940  C  C   . GLY   A 122 ? 0.8557 0.5491 0.6822 0.1273  0.4632  0.0290  128 GLY   A C   
941  O  O   . GLY   A 122 ? 0.8059 0.5942 0.7366 0.1305  0.4279  0.0525  128 GLY   A O   
942  N  N   . ASN   A 123 ? 0.8937 0.5163 0.6955 0.1325  0.5370  0.0266  129 ASN   A N   
943  C  CA  . ASN   A 123 ? 0.8519 0.5093 0.7675 0.1466  0.5875  0.0540  129 ASN   A CA  
944  C  C   . ASN   A 123 ? 0.7936 0.5246 0.7535 0.1384  0.5461  0.0691  129 ASN   A C   
945  O  O   . ASN   A 123 ? 0.7478 0.5347 0.8308 0.1479  0.5666  0.0998  129 ASN   A O   
946  C  CB  . ASN   A 123 ? 0.8182 0.5345 0.8878 0.1673  0.6077  0.0848  129 ASN   A CB  
947  C  CG  . ASN   A 123 ? 0.9258 0.5572 0.9684 0.1793  0.6753  0.0732  129 ASN   A CG  
948  O  OD1 . ASN   A 123 ? 1.0053 0.5333 0.9688 0.1793  0.7499  0.0560  129 ASN   A OD1 
949  N  ND2 . ASN   A 123 ? 0.9135 0.5790 1.0151 0.1880  0.6543  0.0822  129 ASN   A ND2 
950  N  N   . GLY   A 124 ? 0.7889 0.5134 0.6522 0.1203  0.4918  0.0498  130 GLY   A N   
951  C  CA  . GLY   A 124 ? 0.7364 0.5224 0.6304 0.1112  0.4520  0.0607  130 GLY   A CA  
952  C  C   . GLY   A 124 ? 0.6597 0.5389 0.6198 0.1064  0.3806  0.0728  130 GLY   A C   
953  O  O   . GLY   A 124 ? 0.6285 0.5641 0.6335 0.0986  0.3505  0.0867  130 GLY   A O   
954  N  N   . LEU   A 125 ? 0.6319 0.5202 0.5893 0.1085  0.3546  0.0668  131 LEU   A N   
955  C  CA  . LEU   A 125 ? 0.5773 0.5380 0.5822 0.1020  0.2942  0.0761  131 LEU   A CA  
956  C  C   . LEU   A 125 ? 0.5883 0.5251 0.5073 0.0937  0.2549  0.0503  131 LEU   A C   
957  O  O   . LEU   A 125 ? 0.6546 0.5211 0.4909 0.0939  0.2723  0.0300  131 LEU   A O   
958  C  CB  . LEU   A 125 ? 0.5358 0.5395 0.6495 0.1130  0.3026  0.1029  131 LEU   A CB  
959  C  CG  . LEU   A 125 ? 0.5096 0.5507 0.7414 0.1201  0.3331  0.1387  131 LEU   A CG  
960  C  CD1 . LEU   A 125 ? 0.4739 0.5317 0.8077 0.1351  0.3585  0.1645  131 LEU   A CD1 
961  C  CD2 . LEU   A 125 ? 0.4800 0.5894 0.7611 0.1028  0.2822  0.1597  131 LEU   A CD2 
962  N  N   . VAL   A 126 ? 0.5199 0.5093 0.4571 0.0838  0.2032  0.0526  132 VAL   A N   
963  C  CA  . VAL   A 126 ? 0.5078 0.4865 0.3911 0.0768  0.1670  0.0339  132 VAL   A CA  
964  C  C   . VAL   A 126 ? 0.4497 0.4843 0.3893 0.0731  0.1358  0.0457  132 VAL   A C   
965  O  O   . VAL   A 126 ? 0.4149 0.4972 0.4092 0.0658  0.1219  0.0647  132 VAL   A O   
966  C  CB  . VAL   A 126 ? 0.5244 0.4856 0.3455 0.0649  0.1423  0.0188  132 VAL   A CB  
967  C  CG1 . VAL   A 126 ? 0.4988 0.5036 0.3557 0.0572  0.1305  0.0297  132 VAL   A CG1 
968  C  CG2 . VAL   A 126 ? 0.5312 0.4880 0.3217 0.0584  0.1058  0.0056  132 VAL   A CG2 
969  N  N   . GLY   A 127 ? 0.4399 0.4615 0.3607 0.0751  0.1247  0.0362  133 GLY   A N   
970  C  CA  . GLY   A 127 ? 0.3979 0.4585 0.3551 0.0700  0.0980  0.0445  133 GLY   A CA  
971  C  C   . GLY   A 127 ? 0.3996 0.4580 0.3172 0.0598  0.0674  0.0279  133 GLY   A C   
972  O  O   . GLY   A 127 ? 0.4284 0.4488 0.2979 0.0613  0.0647  0.0111  133 GLY   A O   
973  N  N   . PHE   A 128 ? 0.3589 0.4529 0.2970 0.0467  0.0448  0.0349  134 PHE   A N   
974  C  CA  . PHE   A 128 ? 0.3487 0.4413 0.2623 0.0365  0.0255  0.0217  134 PHE   A CA  
975  C  C   . PHE   A 128 ? 0.3237 0.4320 0.2531 0.0290  0.0134  0.0276  134 PHE   A C   
976  O  O   . PHE   A 128 ? 0.3076 0.4388 0.2604 0.0184  0.0056  0.0453  134 PHE   A O   
977  C  CB  . PHE   A 128 ? 0.3405 0.4422 0.2443 0.0232  0.0187  0.0200  134 PHE   A CB  
978  C  CG  . PHE   A 128 ? 0.3522 0.4415 0.2416 0.0273  0.0282  0.0169  134 PHE   A CG  
979  C  CD1 . PHE   A 128 ? 0.3738 0.4341 0.2318 0.0312  0.0266  0.0027  134 PHE   A CD1 
980  C  CD2 . PHE   A 128 ? 0.3483 0.4546 0.2590 0.0239  0.0351  0.0314  134 PHE   A CD2 
981  C  CE1 . PHE   A 128 ? 0.3944 0.4385 0.2324 0.0321  0.0334  0.0014  134 PHE   A CE1 
982  C  CE2 . PHE   A 128 ? 0.3630 0.4558 0.2588 0.0268  0.0463  0.0286  134 PHE   A CE2 
983  C  CZ  . PHE   A 128 ? 0.3817 0.4414 0.2361 0.0308  0.0461  0.0126  134 PHE   A CZ  
984  N  N   . ALA   A 129 ? 0.3227 0.4160 0.2390 0.0316  0.0091  0.0154  135 ALA   A N   
985  C  CA  . ALA   A 129 ? 0.3204 0.4219 0.2450 0.0238  0.0011  0.0185  135 ALA   A CA  
986  C  C   . ALA   A 129 ? 0.3418 0.4443 0.2505 0.0052  -0.0022 0.0141  135 ALA   A C   
987  O  O   . ALA   A 129 ? 0.3417 0.4306 0.2425 0.0057  0.0023  0.0004  135 ALA   A O   
988  C  CB  . ALA   A 129 ? 0.3291 0.4113 0.2497 0.0327  -0.0002 0.0077  135 ALA   A CB  
989  N  N   . ASP   A 130 ? 0.3614 0.4738 0.2647 -0.0134 -0.0096 0.0276  136 ASP   A N   
990  C  CA  . ASP   A 130 ? 0.3984 0.4949 0.2669 -0.0370 -0.0078 0.0223  136 ASP   A CA  
991  C  C   . ASP   A 130 ? 0.4260 0.5017 0.2826 -0.0407 0.0048  0.0091  136 ASP   A C   
992  O  O   . ASP   A 130 ? 0.4255 0.5057 0.2977 -0.0335 0.0016  0.0123  136 ASP   A O   
993  C  CB  . ASP   A 130 ? 0.4215 0.5224 0.2762 -0.0623 -0.0260 0.0439  136 ASP   A CB  
994  C  CG  . ASP   A 130 ? 0.5122 0.5818 0.3103 -0.0938 -0.0246 0.0391  136 ASP   A CG  
995  O  OD1 . ASP   A 130 ? 0.5111 0.5703 0.2951 -0.0949 -0.0136 0.0273  136 ASP   A OD1 
996  O  OD2 . ASP   A 130 ? 0.5809 0.6290 0.3417 -0.1199 -0.0336 0.0476  136 ASP   A OD2 
997  N  N   . VAL   A 131 ? 0.4469 0.4979 0.2822 -0.0509 0.0232  -0.0051 137 VAL   A N   
998  C  CA  . VAL   A 131 ? 0.4639 0.4905 0.2964 -0.0558 0.0453  -0.0160 137 VAL   A CA  
999  C  C   . VAL   A 131 ? 0.5003 0.4840 0.2741 -0.0866 0.0665  -0.0219 137 VAL   A C   
1000 O  O   . VAL   A 131 ? 0.5114 0.4649 0.2773 -0.0934 0.0951  -0.0314 137 VAL   A O   
1001 C  CB  . VAL   A 131 ? 0.4546 0.4817 0.3346 -0.0356 0.0582  -0.0268 137 VAL   A CB  
1002 C  CG1 . VAL   A 131 ? 0.4482 0.4986 0.3637 -0.0135 0.0360  -0.0218 137 VAL   A CG1 
1003 C  CG2 . VAL   A 131 ? 0.4547 0.4708 0.3349 -0.0363 0.0707  -0.0344 137 VAL   A CG2 
1004 N  N   . ARG   A 132 ? 0.5146 0.4884 0.2452 -0.1069 0.0554  -0.0163 138 ARG   A N   
1005 C  CA  . ARG   A 132 ? 0.5677 0.4863 0.2242 -0.1416 0.0742  -0.0232 138 ARG   A CA  
1006 C  C   . ARG   A 132 ? 0.6102 0.4889 0.2057 -0.1717 0.0768  -0.0182 138 ARG   A C   
1007 O  O   . ARG   A 132 ? 0.6520 0.4674 0.1797 -0.1989 0.1080  -0.0306 138 ARG   A O   
1008 C  CB  . ARG   A 132 ? 0.5779 0.4942 0.2008 -0.1605 0.0529  -0.0146 138 ARG   A CB  
1009 C  CG  . ARG   A 132 ? 0.5441 0.4880 0.2133 -0.1357 0.0556  -0.0208 138 ARG   A CG  
1010 C  CD  . ARG   A 132 ? 0.5577 0.5021 0.1992 -0.1552 0.0333  -0.0095 138 ARG   A CD  
1011 N  NE  . ARG   A 132 ? 0.5295 0.5195 0.2062 -0.1505 -0.0040 0.0161  138 ARG   A NE  
1012 C  CZ  . ARG   A 132 ? 0.5045 0.5088 0.1828 -0.1645 -0.0299 0.0350  138 ARG   A CZ  
1013 N  NH1 . ARG   A 132 ? 0.5210 0.4951 0.1554 -0.1869 -0.0271 0.0296  138 ARG   A NH1 
1014 N  NH2 . ARG   A 132 ? 0.4284 0.4753 0.1583 -0.1565 -0.0566 0.0609  138 ARG   A NH2 
1015 N  N   . ASP   A 133 ? 0.6023 0.5101 0.2194 -0.1670 0.0495  -0.0010 139 ASP   A N   
1016 C  CA  . ASP   A 133 ? 0.6503 0.5220 0.2118 -0.1955 0.0465  0.0075  139 ASP   A CA  
1017 C  C   . ASP   A 133 ? 0.6671 0.5195 0.2420 -0.1848 0.0853  -0.0078 139 ASP   A C   
1018 O  O   . ASP   A 133 ? 0.7110 0.5143 0.2229 -0.2129 0.0981  -0.0069 139 ASP   A O   
1019 C  CB  . ASP   A 133 ? 0.6437 0.5556 0.2323 -0.1958 -0.0013 0.0372  139 ASP   A CB  
1020 C  CG  . ASP   A 133 ? 0.6336 0.6024 0.3122 -0.1535 -0.0060 0.0392  139 ASP   A CG  
1021 O  OD1 . ASP   A 133 ? 0.6226 0.6180 0.3500 -0.1237 0.0053  0.0265  139 ASP   A OD1 
1022 O  OD2 . ASP   A 133 ? 0.6374 0.6181 0.3319 -0.1527 -0.0223 0.0545  139 ASP   A OD2 
1023 N  N   . LEU   A 134 ? 0.6276 0.5149 0.2837 -0.1473 0.1018  -0.0190 140 LEU   A N   
1024 C  CA  . LEU   A 134 ? 0.6220 0.4986 0.3123 -0.1357 0.1348  -0.0286 140 LEU   A CA  
1025 C  C   . LEU   A 134 ? 0.6609 0.4801 0.3255 -0.1483 0.1911  -0.0474 140 LEU   A C   
1026 O  O   . LEU   A 134 ? 0.6301 0.4619 0.3606 -0.1257 0.2131  -0.0563 140 LEU   A O   
1027 C  CB  . LEU   A 134 ? 0.5673 0.4979 0.3542 -0.0966 0.1227  -0.0280 140 LEU   A CB  
1028 C  CG  . LEU   A 134 ? 0.5502 0.5277 0.3619 -0.0811 0.0780  -0.0133 140 LEU   A CG  
1029 C  CD1 . LEU   A 134 ? 0.5169 0.5273 0.3961 -0.0501 0.0680  -0.0163 140 LEU   A CD1 
1030 C  CD2 . LEU   A 134 ? 0.5595 0.5379 0.3595 -0.0890 0.0643  -0.0008 140 LEU   A CD2 
1031 N  N   . LEU   A 135 ? 0.7321 0.4812 0.2993 -0.1867 0.2158  -0.0517 141 LEU   A N   
1032 C  CA  . LEU   A 135 ? 0.7935 0.4696 0.3192 -0.2035 0.2802  -0.0715 141 LEU   A CA  
1033 C  C   . LEU   A 135 ? 0.8012 0.4706 0.4032 -0.1828 0.3342  -0.0804 141 LEU   A C   
1034 O  O   . LEU   A 135 ? 0.8186 0.4456 0.4339 -0.1823 0.3918  -0.0949 141 LEU   A O   
1035 C  CB  . LEU   A 135 ? 0.8736 0.4590 0.2542 -0.2565 0.2941  -0.0743 141 LEU   A CB  
1036 C  CG  . LEU   A 135 ? 0.9090 0.4933 0.2106 -0.2875 0.2326  -0.0569 141 LEU   A CG  
1037 C  CD1 . LEU   A 135 ? 0.9946 0.4724 0.1426 -0.3468 0.2471  -0.0590 141 LEU   A CD1 
1038 C  CD2 . LEU   A 135 ? 0.9029 0.5210 0.2327 -0.2756 0.2113  -0.0576 141 LEU   A CD2 
1039 N  N   . TRP   A 136 ? 0.7798 0.4880 0.4375 -0.1666 0.3181  -0.0698 142 TRP   A N   
1040 C  CA  . TRP   A 136 ? 0.7677 0.4748 0.5096 -0.1487 0.3630  -0.0726 142 TRP   A CA  
1041 C  C   . TRP   A 136 ? 0.7440 0.4966 0.6138 -0.1132 0.3691  -0.0713 142 TRP   A C   
1042 O  O   . TRP   A 136 ? 0.7178 0.4630 0.6701 -0.1010 0.4128  -0.0709 142 TRP   A O   
1043 C  CB  . TRP   A 136 ? 0.7411 0.4773 0.5065 -0.1433 0.3379  -0.0599 142 TRP   A CB  
1044 C  CG  . TRP   A 136 ? 0.6994 0.5082 0.5011 -0.1233 0.2671  -0.0456 142 TRP   A CG  
1045 C  CD1 . TRP   A 136 ? 0.7215 0.5422 0.4617 -0.1364 0.2201  -0.0349 142 TRP   A CD1 
1046 C  CD2 . TRP   A 136 ? 0.6391 0.5096 0.5467 -0.0893 0.2391  -0.0385 142 TRP   A CD2 
1047 N  NE1 . TRP   A 136 ? 0.6803 0.5644 0.4837 -0.1094 0.1739  -0.0245 142 TRP   A NE1 
1048 C  CE2 . TRP   A 136 ? 0.6379 0.5483 0.5326 -0.0826 0.1834  -0.0281 142 TRP   A CE2 
1049 C  CE3 . TRP   A 136 ? 0.6034 0.4941 0.6160 -0.0666 0.2542  -0.0373 142 TRP   A CE3 
1050 C  CZ2 . TRP   A 136 ? 0.6058 0.5641 0.5694 -0.0561 0.1482  -0.0215 142 TRP   A CZ2 
1051 C  CZ3 . TRP   A 136 ? 0.5720 0.5140 0.6533 -0.0434 0.2082  -0.0270 142 TRP   A CZ3 
1052 C  CH2 . TRP   A 136 ? 0.5745 0.5444 0.6218 -0.0393 0.1586  -0.0216 142 TRP   A CH2 
1053 N  N   . LEU   A 137 ? 0.7473 0.5445 0.6373 -0.0986 0.3246  -0.0677 143 LEU   A N   
1054 C  CA  . LEU   A 137 ? 0.7271 0.5614 0.7236 -0.0706 0.3205  -0.0633 143 LEU   A CA  
1055 C  C   . LEU   A 137 ? 0.7817 0.5684 0.8012 -0.0737 0.3853  -0.0737 143 LEU   A C   
1056 O  O   . LEU   A 137 ? 0.7385 0.5470 0.8717 -0.0519 0.3968  -0.0653 143 LEU   A O   
1057 C  CB  . LEU   A 137 ? 0.7092 0.5852 0.6924 -0.0614 0.2644  -0.0591 143 LEU   A CB  
1058 C  CG  . LEU   A 137 ? 0.6977 0.6206 0.6808 -0.0518 0.2071  -0.0479 143 LEU   A CG  
1059 C  CD1 . LEU   A 137 ? 0.7063 0.6548 0.6611 -0.0475 0.1672  -0.0457 143 LEU   A CD1 
1060 C  CD2 . LEU   A 137 ? 0.6546 0.6108 0.7333 -0.0299 0.1904  -0.0373 143 LEU   A CD2 
1061 N  N   . ASP   A 138 ? 0.8764 0.5930 0.7884 -0.1031 0.4263  -0.0897 144 ASP   A N   
1062 C  CA  . ASP   A 138 ? 0.9409 0.5946 0.8515 -0.1106 0.4967  -0.1035 144 ASP   A CA  
1063 C  C   . ASP   A 138 ? 0.9987 0.5869 0.9133 -0.1214 0.5768  -0.1114 144 ASP   A C   
1064 O  O   . ASP   A 138 ? 0.9951 0.5507 0.9770 -0.1125 0.6410  -0.1159 144 ASP   A O   
1065 C  CB  . ASP   A 138 ? 1.0353 0.6337 0.8085 -0.1426 0.4979  -0.1180 144 ASP   A CB  
1066 C  CG  . ASP   A 138 ? 1.0768 0.7231 0.8663 -0.1301 0.4475  -0.1133 144 ASP   A CG  
1067 O  OD1 . ASP   A 138 ? 1.0329 0.7274 0.9374 -0.0990 0.4390  -0.1046 144 ASP   A OD1 
1068 O  OD2 . ASP   A 138 ? 1.1521 0.7856 0.8413 -0.1534 0.4147  -0.1157 144 ASP   A OD2 
1069 N  N   . GLU   A 139 ? 1.0591 0.6188 0.8966 -0.1429 0.5794  -0.1130 145 GLU   A N   
1070 C  CA  . GLU   A 139 ? 1.1195 0.6034 0.9390 -0.1585 0.6617  -0.1220 145 GLU   A CA  
1071 C  C   . GLU   A 139 ? 1.0640 0.5931 1.0391 -0.1285 0.6809  -0.1065 145 GLU   A C   
1072 O  O   . GLU   A 139 ? 1.0791 0.5512 1.0878 -0.1318 0.7646  -0.1117 145 GLU   A O   
1073 C  CB  . GLU   A 139 ? 1.2416 0.6644 0.8999 -0.2001 0.6562  -0.1285 145 GLU   A CB  
1074 C  CG  . GLU   A 139 ? 1.3044 0.8015 0.9701 -0.1930 0.5738  -0.1104 145 GLU   A CG  
1075 C  CD  . GLU   A 139 ? 1.4832 0.9314 0.9912 -0.2356 0.5454  -0.1098 145 GLU   A CD  
1076 O  OE1 . GLU   A 139 ? 1.4885 0.9662 0.9993 -0.2357 0.5109  -0.0965 145 GLU   A OE1 
1077 O  OE2 . GLU   A 139 ? 1.5844 0.9621 0.9666 -0.2713 0.5542  -0.1204 145 GLU   A OE2 
1078 N  N1  . A1BR0 B .   ? 0.8429 0.4610 0.4417 0.0849  0.2172  -0.0450 201 A1BR0 A N1  
1079 C  C4  . A1BR0 B .   ? 0.8925 0.4277 0.3920 0.0664  0.1994  -0.0620 201 A1BR0 A C4  
1080 C  C5  . A1BR0 B .   ? 0.8632 0.4794 0.4573 0.0867  0.2405  -0.0423 201 A1BR0 A C5  
1081 C  C6  . A1BR0 B .   ? 0.9561 0.4724 0.4249 0.0683  0.2523  -0.0594 201 A1BR0 A C6  
1082 C  C7  . A1BR0 B .   ? 0.9600 0.5049 0.4302 0.0639  0.2408  -0.0546 201 A1BR0 A C7  
1083 C  C8  . A1BR0 B .   ? 0.9874 0.4869 0.4281 0.0666  0.2938  -0.0559 201 A1BR0 A C8  
1084 C  C10 . A1BR0 B .   ? 0.9376 0.5409 0.4272 0.0588  0.2266  -0.0433 201 A1BR0 A C10 
1085 C  C13 . A1BR0 B .   ? 0.7657 0.4697 0.4700 0.0978  0.2017  -0.0281 201 A1BR0 A C13 
1086 CL CL1 . A1BR0 B .   ? 0.9201 0.5860 0.4684 0.0551  0.1290  -0.0461 201 A1BR0 A CL1 
1087 C  C12 . A1BR0 B .   ? 0.9330 0.5492 0.4416 0.0587  0.1846  -0.0480 201 A1BR0 A C12 
1088 C  C11 . A1BR0 B .   ? 0.9132 0.5559 0.4302 0.0563  0.1790  -0.0430 201 A1BR0 A C11 
1089 CL CL  . A1BR0 B .   ? 0.8701 0.5880 0.4320 0.0496  0.1189  -0.0366 201 A1BR0 A CL  
1090 C  C9  . A1BR0 B .   ? 0.9754 0.5059 0.4268 0.0640  0.2857  -0.0496 201 A1BR0 A C9  
1091 O  O1  . A1BR0 B .   ? 0.8077 0.4961 0.4892 0.0988  0.2470  -0.0253 201 A1BR0 A O1  
1092 C  C3  . A1BR0 B .   ? 0.8638 0.4451 0.3803 0.0549  0.1328  -0.0595 201 A1BR0 A C3  
1093 C  C2  . A1BR0 B .   ? 0.7899 0.4649 0.4164 0.0705  0.1220  -0.0453 201 A1BR0 A C2  
1094 C  C1  . A1BR0 B .   ? 0.7366 0.4829 0.4447 0.0858  0.1415  -0.0296 201 A1BR0 A C1  
1095 C  C   . A1BR0 B .   ? 0.6636 0.4881 0.4623 0.0937  0.1255  -0.0133 201 A1BR0 A C   
1096 O  O   . A1BR0 B .   ? 0.6422 0.4664 0.4756 0.1031  0.1425  -0.0061 201 A1BR0 A O   
1097 N  N   . A1BR0 B .   ? 0.6234 0.5076 0.4548 0.0879  0.0943  -0.0068 201 A1BR0 A N   
# 
