data_7HXO
# 
_entry.id   7HXO 
# 
_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   7HXO         pdb_00007hxo 10.2210/pdb7hxo/pdb 
WWPDB D_1001408060 ?            ?                   
# 
_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                        7HXO 
_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)-N~1~-[2-(2,2,2-trifluoroethoxy)phenyl]piperidine-1,3-dicarboxamide' 345.317   1   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                                65.409    1   ?         ? ? ? 
4 water       nat water                                                                     18.015    200 ?         ? ? ? 
# 
_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)-N~1~-[2-(2,2,2-trifluoroethoxy)phenyl]piperidine-1,3-dicarboxamide' A1BRI 
3 'ZINC ION'                                                                ZN    
4 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 
A1BRI non-polymer         . '(3S)-N~1~-[2-(2,2,2-trifluoroethoxy)phenyl]piperidine-1,3-dicarboxamide' ? 'C15 H18 F3 N3 O3' 345.317 
ALA   'L-peptide linking' y ALANINE                                                                   ? 'C3 H7 N O2'       89.093  
ARG   'L-peptide linking' y ARGININE                                                                  ? 'C6 H15 N4 O2 1'   175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                ? 'C4 H8 N2 O3'      132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                           ? 'C4 H7 N O4'       133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                  ? 'C3 H7 N O2 S'     121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                 ? 'C5 H10 N2 O3'     146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                           ? 'C5 H9 N O4'       147.129 
GLY   'peptide linking'   y GLYCINE                                                                   ? 'C2 H5 N O2'       75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                 ? 'C6 H10 N3 O2 1'   156.162 
HOH   non-polymer         . WATER                                                                     ? 'H2 O'             18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                ? 'C6 H13 N O2'      131.173 
LEU   'L-peptide linking' y LEUCINE                                                                   ? 'C6 H13 N O2'      131.173 
LYS   'L-peptide linking' y LYSINE                                                                    ? 'C6 H15 N2 O2 1'   147.195 
MET   'L-peptide linking' y METHIONINE                                                                ? 'C5 H11 N O2 S'    149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                             ? 'C9 H11 N O2'      165.189 
PRO   'L-peptide linking' y PROLINE                                                                   ? 'C5 H9 N O2'       115.130 
SER   'L-peptide linking' y SERINE                                                                    ? 'C3 H7 N O3'       105.093 
THR   'L-peptide linking' y THREONINE                                                                 ? 'C4 H9 N O3'       119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                ? 'C11 H12 N2 O2'    204.225 
TYR   'L-peptide linking' y TYROSINE                                                                  ? 'C9 H11 N O3'      181.189 
VAL   'L-peptide linking' y VALINE                                                                    ? 'C5 H11 N O2'      117.146 
ZN    non-polymer         . 'ZINC ION'                                                                ? 'Zn 2'             65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   7   7   SER SER A . n 
A 1 2   GLY 2   8   8   GLY GLY A . n 
A 1 3   ALA 3   9   9   ALA ALA A . n 
A 1 4   ILE 4   10  10  ILE ILE A . n 
A 1 5   TYR 5   11  11  TYR TYR A . n 
A 1 6   VAL 6   12  12  VAL VAL A . n 
A 1 7   GLY 7   13  13  GLY GLY A . n 
A 1 8   ASN 8   14  14  ASN ASN A . n 
A 1 9   TYR 9   15  15  TYR TYR A . n 
A 1 10  ARG 10  16  16  ARG ARG A . n 
A 1 11  VAL 11  17  17  VAL VAL A . n 
A 1 12  VAL 12  18  18  VAL VAL A . n 
A 1 13  ASN 13  19  19  ASN ASN A . n 
A 1 14  ARG 14  20  20  ARG ARG A . n 
A 1 15  HIS 15  21  21  HIS HIS A . n 
A 1 16  LEU 16  22  22  LEU LEU A . n 
A 1 17  ALA 17  23  23  ALA ALA A . n 
A 1 18  THR 18  24  24  THR THR A . n 
A 1 19  HIS 19  25  25  HIS HIS A . n 
A 1 20  ASN 20  26  26  ASN ASN A . n 
A 1 21  ASP 21  27  27  ASP ASP A . n 
A 1 22  TRP 22  28  28  TRP TRP A . n 
A 1 23  ALA 23  29  29  ALA ALA A . n 
A 1 24  ASN 24  30  30  ASN ASN A . n 
A 1 25  LEU 25  31  31  LEU LEU A . n 
A 1 26  VAL 26  32  32  VAL VAL A . n 
A 1 27  TRP 27  33  33  TRP TRP A . n 
A 1 28  GLU 28  34  34  GLU GLU A . n 
A 1 29  ASP 29  35  35  ASP ASP A . n 
A 1 30  SER 30  36  36  SER SER A . n 
A 1 31  SER 31  37  37  SER SER A . n 
A 1 32  ARG 32  38  38  ARG ARG A . n 
A 1 33  ASP 33  39  39  ASP ASP A . n 
A 1 34  LEU 34  40  40  LEU LEU A . n 
A 1 35  LEU 35  41  41  LEU LEU A . n 
A 1 36  VAL 36  42  42  VAL VAL A . n 
A 1 37  SER 37  43  43  SER SER A . n 
A 1 38  SER 38  44  44  SER SER A . n 
A 1 39  THR 39  45  45  THR THR A . n 
A 1 40  THR 40  46  46  THR THR A . n 
A 1 41  ALA 41  47  47  ALA ALA A . n 
A 1 42  GLN 42  48  48  GLN GLN A . n 
A 1 43  GLY 43  49  49  GLY GLY A . n 
A 1 44  CYS 44  50  50  CYS CYS A . n 
A 1 45  ASP 45  51  51  ASP ASP A . n 
A 1 46  THR 46  52  52  THR THR A . n 
A 1 47  ILE 47  53  53  ILE ILE A . n 
A 1 48  ALA 48  54  54  ALA ALA A . n 
A 1 49  ARG 49  55  55  ARG ARG A . n 
A 1 50  CYS 50  56  56  CYS CYS A . n 
A 1 51  ASP 51  57  57  ASP ASP A . n 
A 1 52  CYS 52  58  58  CYS CYS A . n 
A 1 53  GLN 53  59  59  GLN GLN A . n 
A 1 54  THR 54  60  60  THR THR A . n 
A 1 55  GLY 55  61  61  GLY GLY A . n 
A 1 56  VAL 56  62  62  VAL VAL A . n 
A 1 57  TYR 57  63  63  TYR TYR A . n 
A 1 58  TYR 58  64  64  TYR TYR A . n 
A 1 59  CYS 59  65  65  CYS CYS A . n 
A 1 60  SER 60  66  66  SER SER A . n 
A 1 61  SER 61  67  67  SER SER A . n 
A 1 62  ARG 62  68  68  ARG ARG A . n 
A 1 63  ARG 63  69  69  ARG ARG A . n 
A 1 64  LYS 64  70  70  LYS LYS A . n 
A 1 65  HIS 65  71  71  HIS HIS A . n 
A 1 66  TYR 66  72  72  TYR TYR A . n 
A 1 67  PRO 67  73  73  PRO PRO A . n 
A 1 68  VAL 68  74  74  VAL VAL A . n 
A 1 69  SER 69  75  75  SER SER A . n 
A 1 70  PHE 70  76  76  PHE PHE A . n 
A 1 71  SER 71  77  77  SER SER A . n 
A 1 72  LYS 72  78  78  LYS LYS A . n 
A 1 73  PRO 73  79  79  PRO PRO A . n 
A 1 74  SER 74  80  80  SER SER A . n 
A 1 75  LEU 75  81  81  LEU LEU A . n 
A 1 76  ILE 76  82  82  ILE ILE A . n 
A 1 77  PHE 77  83  83  PHE PHE A . n 
A 1 78  VAL 78  84  84  VAL VAL A . n 
A 1 79  GLU 79  85  85  GLU GLU A . n 
A 1 80  ALA 80  86  86  ALA ALA A . n 
A 1 81  SER 81  87  87  SER SER A . n 
A 1 82  GLU 82  88  88  GLU GLU A . n 
A 1 83  TYR 83  89  89  TYR TYR A . n 
A 1 84  TYR 84  90  90  TYR TYR A . n 
A 1 85  PRO 85  91  91  PRO PRO A . n 
A 1 86  ALA 86  92  92  ALA ALA A . n 
A 1 87  ARG 87  93  93  ARG ARG A . n 
A 1 88  TYR 88  94  94  TYR TYR A . n 
A 1 89  GLN 89  95  95  GLN GLN A . n 
A 1 90  SER 90  96  96  SER SER A . n 
A 1 91  HIS 91  97  97  HIS HIS A . n 
A 1 92  LEU 92  98  98  LEU LEU A . n 
A 1 93  MET 93  99  99  MET MET A . n 
A 1 94  LEU 94  100 100 LEU LEU A . n 
A 1 95  ALA 95  101 101 ALA ALA A . n 
A 1 96  VAL 96  102 102 VAL VAL A . n 
A 1 97  GLY 97  103 103 GLY GLY A . n 
A 1 98  HIS 98  104 104 HIS HIS A . n 
A 1 99  SER 99  105 105 SER SER A . n 
A 1 100 GLU 100 106 106 GLU GLU A . n 
A 1 101 PRO 101 107 107 PRO PRO A . n 
A 1 102 GLY 102 108 108 GLY GLY A . n 
A 1 103 ASP 103 109 109 ASP ASP A . n 
A 1 104 CYS 104 110 110 CYS CYS A . n 
A 1 105 GLY 105 111 111 GLY GLY A . n 
A 1 106 GLY 106 112 112 GLY GLY A . n 
A 1 107 ILE 107 113 113 ILE ILE A . n 
A 1 108 LEU 108 114 114 LEU LEU A . n 
A 1 109 ARG 109 115 115 ARG ARG A . n 
A 1 110 CYS 110 116 116 CYS CYS A . n 
A 1 111 GLN 111 117 117 GLN GLN A . n 
A 1 112 HIS 112 118 118 HIS HIS A . n 
A 1 113 GLY 113 119 119 GLY GLY A . n 
A 1 114 VAL 114 120 120 VAL VAL A . n 
A 1 115 VAL 115 121 121 VAL VAL A . n 
A 1 116 GLY 116 122 122 GLY GLY A . n 
A 1 117 ILE 117 123 123 ILE ILE A . n 
A 1 118 VAL 118 124 124 VAL VAL A . n 
A 1 119 SER 119 125 125 SER SER A . n 
A 1 120 THR 120 126 126 THR THR A . n 
A 1 121 GLY 121 127 127 GLY GLY A . n 
A 1 122 GLY 122 128 128 GLY GLY A . n 
A 1 123 ASN 123 129 129 ASN ASN A . n 
A 1 124 GLY 124 130 130 GLY GLY A . n 
A 1 125 LEU 125 131 131 LEU LEU A . n 
A 1 126 VAL 126 132 132 VAL VAL A . n 
A 1 127 GLY 127 133 133 GLY GLY A . n 
A 1 128 PHE 128 134 134 PHE PHE A . n 
A 1 129 ALA 129 135 135 ALA ALA A . n 
A 1 130 ASP 130 136 136 ASP ASP A . n 
A 1 131 VAL 131 137 137 VAL VAL A . n 
A 1 132 ARG 132 138 138 ARG ARG A . n 
A 1 133 ASP 133 139 139 ASP ASP A . n 
A 1 134 LEU 134 140 140 LEU LEU A . n 
A 1 135 LEU 135 141 141 LEU LEU A . n 
A 1 136 TRP 136 142 142 TRP TRP A . n 
A 1 137 LEU 137 143 143 LEU LEU A . n 
A 1 138 ASP 138 144 144 ASP ASP A . n 
A 1 139 GLU 139 145 145 GLU GLU A . n 
A 1 140 GLU 140 146 146 GLU GLU A . n 
A 1 141 ALA 141 147 ?   ?   ?   A . n 
A 1 142 MET 142 148 ?   ?   ?   A . n 
A 1 143 GLU 143 149 ?   ?   ?   A . n 
A 1 144 GLN 144 150 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BRI 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BRI 
_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 A1BRI 1   201 201 A1BRI LIG A . 
C 3 ZN    1   202 1   ZN    ZN  A . 
D 4 HOH   1   301 82  HOH   HOH A . 
D 4 HOH   2   302 245 HOH   HOH A . 
D 4 HOH   3   303 30  HOH   HOH A . 
D 4 HOH   4   304 104 HOH   HOH A . 
D 4 HOH   5   305 59  HOH   HOH A . 
D 4 HOH   6   306 181 HOH   HOH A . 
D 4 HOH   7   307 258 HOH   HOH A . 
D 4 HOH   8   308 36  HOH   HOH A . 
D 4 HOH   9   309 26  HOH   HOH A . 
D 4 HOH   10  310 211 HOH   HOH A . 
D 4 HOH   11  311 267 HOH   HOH A . 
D 4 HOH   12  312 266 HOH   HOH A . 
D 4 HOH   13  313 136 HOH   HOH A . 
D 4 HOH   14  314 277 HOH   HOH A . 
D 4 HOH   15  315 63  HOH   HOH A . 
D 4 HOH   16  316 13  HOH   HOH A . 
D 4 HOH   17  317 57  HOH   HOH A . 
D 4 HOH   18  318 24  HOH   HOH A . 
D 4 HOH   19  319 34  HOH   HOH A . 
D 4 HOH   20  320 205 HOH   HOH A . 
D 4 HOH   21  321 4   HOH   HOH A . 
D 4 HOH   22  322 68  HOH   HOH A . 
D 4 HOH   23  323 186 HOH   HOH A . 
D 4 HOH   24  324 250 HOH   HOH A . 
D 4 HOH   25  325 137 HOH   HOH A . 
D 4 HOH   26  326 28  HOH   HOH A . 
D 4 HOH   27  327 264 HOH   HOH A . 
D 4 HOH   28  328 147 HOH   HOH A . 
D 4 HOH   29  329 210 HOH   HOH A . 
D 4 HOH   30  330 35  HOH   HOH A . 
D 4 HOH   31  331 79  HOH   HOH A . 
D 4 HOH   32  332 144 HOH   HOH A . 
D 4 HOH   33  333 42  HOH   HOH A . 
D 4 HOH   34  334 16  HOH   HOH A . 
D 4 HOH   35  335 219 HOH   HOH A . 
D 4 HOH   36  336 256 HOH   HOH A . 
D 4 HOH   37  337 254 HOH   HOH A . 
D 4 HOH   38  338 21  HOH   HOH A . 
D 4 HOH   39  339 107 HOH   HOH A . 
D 4 HOH   40  340 15  HOH   HOH A . 
D 4 HOH   41  341 191 HOH   HOH A . 
D 4 HOH   42  342 2   HOH   HOH A . 
D 4 HOH   43  343 265 HOH   HOH A . 
D 4 HOH   44  344 90  HOH   HOH A . 
D 4 HOH   45  345 9   HOH   HOH A . 
D 4 HOH   46  346 70  HOH   HOH A . 
D 4 HOH   47  347 49  HOH   HOH A . 
D 4 HOH   48  348 33  HOH   HOH A . 
D 4 HOH   49  349 5   HOH   HOH A . 
D 4 HOH   50  350 52  HOH   HOH A . 
D 4 HOH   51  351 55  HOH   HOH A . 
D 4 HOH   52  352 169 HOH   HOH A . 
D 4 HOH   53  353 61  HOH   HOH A . 
D 4 HOH   54  354 20  HOH   HOH A . 
D 4 HOH   55  355 37  HOH   HOH A . 
D 4 HOH   56  356 275 HOH   HOH A . 
D 4 HOH   57  357 269 HOH   HOH A . 
D 4 HOH   58  358 260 HOH   HOH A . 
D 4 HOH   59  359 146 HOH   HOH A . 
D 4 HOH   60  360 77  HOH   HOH A . 
D 4 HOH   61  361 148 HOH   HOH A . 
D 4 HOH   62  362 174 HOH   HOH A . 
D 4 HOH   63  363 119 HOH   HOH A . 
D 4 HOH   64  364 91  HOH   HOH A . 
D 4 HOH   65  365 167 HOH   HOH A . 
D 4 HOH   66  366 7   HOH   HOH A . 
D 4 HOH   67  367 46  HOH   HOH A . 
D 4 HOH   68  368 11  HOH   HOH A . 
D 4 HOH   69  369 272 HOH   HOH A . 
D 4 HOH   70  370 249 HOH   HOH A . 
D 4 HOH   71  371 72  HOH   HOH A . 
D 4 HOH   72  372 253 HOH   HOH A . 
D 4 HOH   73  373 262 HOH   HOH A . 
D 4 HOH   74  374 161 HOH   HOH A . 
D 4 HOH   75  375 177 HOH   HOH A . 
D 4 HOH   76  376 27  HOH   HOH A . 
D 4 HOH   77  377 182 HOH   HOH A . 
D 4 HOH   78  378 117 HOH   HOH A . 
D 4 HOH   79  379 17  HOH   HOH A . 
D 4 HOH   80  380 29  HOH   HOH A . 
D 4 HOH   81  381 98  HOH   HOH A . 
D 4 HOH   82  382 50  HOH   HOH A . 
D 4 HOH   83  383 60  HOH   HOH A . 
D 4 HOH   84  384 85  HOH   HOH A . 
D 4 HOH   85  385 62  HOH   HOH A . 
D 4 HOH   86  386 12  HOH   HOH A . 
D 4 HOH   87  387 106 HOH   HOH A . 
D 4 HOH   88  388 156 HOH   HOH A . 
D 4 HOH   89  389 76  HOH   HOH A . 
D 4 HOH   90  390 259 HOH   HOH A . 
D 4 HOH   91  391 257 HOH   HOH A . 
D 4 HOH   92  392 78  HOH   HOH A . 
D 4 HOH   93  393 263 HOH   HOH A . 
D 4 HOH   94  394 126 HOH   HOH A . 
D 4 HOH   95  395 105 HOH   HOH A . 
D 4 HOH   96  396 103 HOH   HOH A . 
D 4 HOH   97  397 100 HOH   HOH A . 
D 4 HOH   98  398 168 HOH   HOH A . 
D 4 HOH   99  399 8   HOH   HOH A . 
D 4 HOH   100 400 84  HOH   HOH A . 
D 4 HOH   101 401 131 HOH   HOH A . 
D 4 HOH   102 402 25  HOH   HOH A . 
D 4 HOH   103 403 18  HOH   HOH A . 
D 4 HOH   104 404 95  HOH   HOH A . 
D 4 HOH   105 405 40  HOH   HOH A . 
D 4 HOH   106 406 89  HOH   HOH A . 
D 4 HOH   107 407 214 HOH   HOH A . 
D 4 HOH   108 408 43  HOH   HOH A . 
D 4 HOH   109 409 96  HOH   HOH A . 
D 4 HOH   110 410 255 HOH   HOH A . 
D 4 HOH   111 411 179 HOH   HOH A . 
D 4 HOH   112 412 10  HOH   HOH A . 
D 4 HOH   113 413 234 HOH   HOH A . 
D 4 HOH   114 414 47  HOH   HOH A . 
D 4 HOH   115 415 220 HOH   HOH A . 
D 4 HOH   116 416 197 HOH   HOH A . 
D 4 HOH   117 417 39  HOH   HOH A . 
D 4 HOH   118 418 123 HOH   HOH A . 
D 4 HOH   119 419 206 HOH   HOH A . 
D 4 HOH   120 420 51  HOH   HOH A . 
D 4 HOH   121 421 110 HOH   HOH A . 
D 4 HOH   122 422 248 HOH   HOH A . 
D 4 HOH   123 423 203 HOH   HOH A . 
D 4 HOH   124 424 142 HOH   HOH A . 
D 4 HOH   125 425 41  HOH   HOH A . 
D 4 HOH   126 426 69  HOH   HOH A . 
D 4 HOH   127 427 154 HOH   HOH A . 
D 4 HOH   128 428 102 HOH   HOH A . 
D 4 HOH   129 429 23  HOH   HOH A . 
D 4 HOH   130 430 80  HOH   HOH A . 
D 4 HOH   131 431 271 HOH   HOH A . 
D 4 HOH   132 432 215 HOH   HOH A . 
D 4 HOH   133 433 128 HOH   HOH A . 
D 4 HOH   134 434 101 HOH   HOH A . 
D 4 HOH   135 435 19  HOH   HOH A . 
D 4 HOH   136 436 155 HOH   HOH A . 
D 4 HOH   137 437 14  HOH   HOH A . 
D 4 HOH   138 438 114 HOH   HOH A . 
D 4 HOH   139 439 192 HOH   HOH A . 
D 4 HOH   140 440 67  HOH   HOH A . 
D 4 HOH   141 441 135 HOH   HOH A . 
D 4 HOH   142 442 133 HOH   HOH A . 
D 4 HOH   143 443 270 HOH   HOH A . 
D 4 HOH   144 444 112 HOH   HOH A . 
D 4 HOH   145 445 213 HOH   HOH A . 
D 4 HOH   146 446 178 HOH   HOH A . 
D 4 HOH   147 447 212 HOH   HOH A . 
D 4 HOH   148 448 140 HOH   HOH A . 
D 4 HOH   149 449 224 HOH   HOH A . 
D 4 HOH   150 450 207 HOH   HOH A . 
D 4 HOH   151 451 216 HOH   HOH A . 
D 4 HOH   152 452 159 HOH   HOH A . 
D 4 HOH   153 453 229 HOH   HOH A . 
D 4 HOH   154 454 175 HOH   HOH A . 
D 4 HOH   155 455 233 HOH   HOH A . 
D 4 HOH   156 456 247 HOH   HOH A . 
D 4 HOH   157 457 121 HOH   HOH A . 
D 4 HOH   158 458 65  HOH   HOH A . 
D 4 HOH   159 459 151 HOH   HOH A . 
D 4 HOH   160 460 83  HOH   HOH A . 
D 4 HOH   161 461 198 HOH   HOH A . 
D 4 HOH   162 462 38  HOH   HOH A . 
D 4 HOH   163 463 200 HOH   HOH A . 
D 4 HOH   164 464 279 HOH   HOH A . 
D 4 HOH   165 465 240 HOH   HOH A . 
D 4 HOH   166 466 164 HOH   HOH A . 
D 4 HOH   167 467 243 HOH   HOH A . 
D 4 HOH   168 468 120 HOH   HOH A . 
D 4 HOH   169 469 48  HOH   HOH A . 
D 4 HOH   170 470 122 HOH   HOH A . 
D 4 HOH   171 471 201 HOH   HOH A . 
D 4 HOH   172 472 232 HOH   HOH A . 
D 4 HOH   173 473 261 HOH   HOH A . 
D 4 HOH   174 474 238 HOH   HOH A . 
D 4 HOH   175 475 162 HOH   HOH A . 
D 4 HOH   176 476 86  HOH   HOH A . 
D 4 HOH   177 477 278 HOH   HOH A . 
D 4 HOH   178 478 152 HOH   HOH A . 
D 4 HOH   179 479 221 HOH   HOH A . 
D 4 HOH   180 480 99  HOH   HOH A . 
D 4 HOH   181 481 276 HOH   HOH A . 
D 4 HOH   182 482 125 HOH   HOH A . 
D 4 HOH   183 483 73  HOH   HOH A . 
D 4 HOH   184 484 230 HOH   HOH A . 
D 4 HOH   185 485 202 HOH   HOH A . 
D 4 HOH   186 486 129 HOH   HOH A . 
D 4 HOH   187 487 153 HOH   HOH A . 
D 4 HOH   188 488 165 HOH   HOH A . 
D 4 HOH   189 489 56  HOH   HOH A . 
D 4 HOH   190 490 199 HOH   HOH A . 
D 4 HOH   191 491 208 HOH   HOH A . 
D 4 HOH   192 492 209 HOH   HOH A . 
D 4 HOH   193 493 274 HOH   HOH A . 
D 4 HOH   194 494 222 HOH   HOH A . 
D 4 HOH   195 495 92  HOH   HOH A . 
D 4 HOH   196 496 273 HOH   HOH A . 
D 4 HOH   197 497 87  HOH   HOH A . 
D 4 HOH   198 498 244 HOH   HOH A . 
D 4 HOH   199 499 225 HOH   HOH A . 
D 4 HOH   200 500 160 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           7HXO 
_cell.length_a           88.986 
_cell.length_b           57.845 
_cell.length_c           32.785 
_cell.angle_alpha        90.00 
_cell.angle_beta         93.36 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HXO 
_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          7HXO 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.65 
_exptl_crystal.density_percent_sol   53.59 
_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                     7HXO 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             48.47 
_reflns.d_resolution_high            1.55 
_reflns.number_obs                   23957 
_reflns.percent_possible_obs         99.6 
_reflns.pdbx_Rmerge_I_obs            0.139 
_reflns.pdbx_netI_over_sigmaI        5.8 
_reflns.pdbx_redundancy              6.3 
_reflns.pdbx_Rrim_I_all              0.151 
_reflns.pdbx_Rpim_I_all              0.059 
_reflns.pdbx_CC_half                 0.992 
_reflns.pdbx_number_measured_all     151581 
_reflns.pdbx_chi_squared             0.80 
_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                  1.55 
_reflns_shell.d_res_low                   1.64 
_reflns_shell.number_measured_all         17362 
_reflns_shell.number_unique_obs           3441 
_reflns_shell.Rmerge_I_obs                1.857 
_reflns_shell.pdbx_chi_squared            0.61 
_reflns_shell.pdbx_redundancy             5.0 
_reflns_shell.percent_possible_obs        98.9 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.8 
_reflns_shell.pdbx_Rrim_I_all             2.064 
_reflns_shell.pdbx_Rpim_I_all             0.884 
_reflns_shell.pdbx_CC_half                0.446 
_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                                 7HXO 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     23775 
_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                             48.47 
_refine.ls_d_res_high                            1.552 
_refine.ls_percent_reflns_obs                    98.7 
_refine.ls_R_factor_obs                          0.2000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1983 
_refine.ls_R_factor_R_free                       0.2312 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.120 
_refine.ls_number_reflns_R_free                  1218 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.955 
_refine.correlation_coeff_Fo_to_Fc_free          0.936 
_refine.B_iso_mean                               30.49 
_refine.aniso_B[1][1]                            -3.90720 
_refine.aniso_B[2][2]                            -0.17040 
_refine.aniso_B[3][3]                            4.07760 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -3.88940 
_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             0.082 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.085 
_refine.pdbx_overall_SU_R_Blow_DPI               0.089 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.090 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HXO 
_refine_analyze.Luzzati_coordinate_error_obs    0.22 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1083 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         25 
_refine_hist.number_atoms_solvent             204 
_refine_hist.number_atoms_total               1312 
_refine_hist.d_res_high                       1.552 
_refine_hist.d_res_low                        48.47 
# 
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                  0.010 ? 2.00  1145 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               0.98  ? 2.00  1561 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  386  '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  207  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1145 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           4.25  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           15.99 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  140  '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  1064 'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   51 
_refine_ls_shell.d_res_high                       1.55 
_refine_ls_shell.d_res_low                        1.56 
_refine_ls_shell.number_reflns_R_work             454 
_refine_ls_shell.R_factor_R_work                  0.3676 
_refine_ls_shell.percent_reflns_obs               85.77 
_refine_ls_shell.R_factor_R_free                  0.4414 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            4.62 
_refine_ls_shell.number_reflns_R_free             22 
_refine_ls_shell.number_reflns_all                476 
_refine_ls_shell.R_factor_all                     0.3710 
# 
_struct.entry_id                  7HXO 
_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-0035279-001 (A71EV2A-x4306)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HXO 
_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 ? 
# 
_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              7HXO 
_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 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2 AA2 THR A 18  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
HELX_P HELX_P3 AA3 SER A 30  ? ARG A 32  ? SER A 36  ARG A 38  5 ? 3 
HELX_P HELX_P4 AA4 SER A 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
HELX_P HELX_P5 AA5 LEU A 134 ? GLU A 139 ? LEU A 140 GLU A 145 5 ? 6 
# 
_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 ? ? ? ? ? ? ? 2.315 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.250 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.323 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 C ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.129 ? ? 
# 
_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_555 111.4 ? 
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_555 107.8 ? 
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_555 117.9 ? 
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_555 108.7 ? 
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_555 100.2 ? 
6 SG ? A CYS 110 ? A CYS 116 ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 110.4 ? 
# 
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 LEU A 35  ? N LEU A 41  O VAL A 12  ? O VAL A 18  
AA2 1 2 O LYS A 64  ? O LYS A 70  N CYS A 59  ? N CYS A 65  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N LEU A 108 ? N LEU A 114 O VAL A 115 ? O VAL A 121 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O PHE A 128 ? O PHE A 134 N MET A 93  ? N MET A 99  
AA2 6 7 O ARG A 87  ? O ARG A 93  N VAL A 78  ? N VAL A 84  
# 
_pdbx_entry_details.entry_id                   7HXO 
_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   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    303 
_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    315 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.96 
# 
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  ? ? -103.37 43.99  
2 1 SER A 125 ? ? -134.10 -31.59 
# 
_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         14.9708 
_pdbx_refine_tls.origin_y         7.6731 
_pdbx_refine_tls.origin_z         14.1689 
_pdbx_refine_tls.T[1][1]          -0.0044 
_pdbx_refine_tls.T[2][2]          -0.0425 
_pdbx_refine_tls.T[3][3]          -0.0152 
_pdbx_refine_tls.T[1][2]          -0.0096 
_pdbx_refine_tls.T[1][3]          0.0182 
_pdbx_refine_tls.T[2][3]          -0.0119 
_pdbx_refine_tls.L[1][1]          0.9929 
_pdbx_refine_tls.L[2][2]          3.2486 
_pdbx_refine_tls.L[3][3]          0.7083 
_pdbx_refine_tls.L[1][2]          0.2182 
_pdbx_refine_tls.L[1][3]          -0.2350 
_pdbx_refine_tls.L[2][3]          0.7468 
_pdbx_refine_tls.S[1][1]          -0.0243 
_pdbx_refine_tls.S[1][2]          0.0281 
_pdbx_refine_tls.S[1][3]          0.0714 
_pdbx_refine_tls.S[2][1]          -0.0492 
_pdbx_refine_tls.S[2][2]          0.1743 
_pdbx_refine_tls.S[2][3]          -0.1904 
_pdbx_refine_tls.S[3][1]          -0.0670 
_pdbx_refine_tls.S[3][2]          -0.0351 
_pdbx_refine_tls.S[3][3]          -0.1500 
# 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   '{ A|* }' 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 498 ? 5.90 . 
2 1 O ? A HOH 499 ? 7.11 . 
3 1 O ? A HOH 500 ? 8.52 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A ALA 147 ? A ALA 141 
2 1 Y 1 A MET 148 ? A MET 142 
3 1 Y 1 A GLU 149 ? A GLU 143 
4 1 Y 1 A GLN 150 ? A GLN 144 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1BRI N1   N  N N 1   
A1BRI C4   C  N N 2   
A1BRI C5   C  N N 3   
A1BRI C6   C  Y N 4   
A1BRI C7   C  Y N 5   
A1BRI C8   C  Y N 6   
A1BRI C10  C  Y N 7   
A1BRI C13  C  N N 8   
A1BRI F2   F  N N 9   
A1BRI F    F  N N 10  
A1BRI F1   F  N N 11  
A1BRI C12  C  N N 12  
A1BRI O2   O  N N 13  
A1BRI C11  C  Y N 14  
A1BRI C9   C  Y N 15  
A1BRI N2   N  N N 16  
A1BRI O1   O  N N 17  
A1BRI C3   C  N N 18  
A1BRI C2   C  N N 19  
A1BRI C14  C  N N 20  
A1BRI C1   C  N S 21  
A1BRI C    C  N N 22  
A1BRI O    O  N N 23  
A1BRI N    N  N N 24  
A1BRI H8   H  N N 25  
A1BRI H7   H  N N 26  
A1BRI H10  H  N N 27  
A1BRI H11  H  N N 28  
A1BRI H13  H  N N 29  
A1BRI H14  H  N N 30  
A1BRI H15  H  N N 31  
A1BRI H12  H  N N 32  
A1BRI H9   H  N N 33  
A1BRI H6   H  N N 34  
A1BRI H5   H  N N 35  
A1BRI H4   H  N N 36  
A1BRI H3   H  N N 37  
A1BRI H17  H  N N 38  
A1BRI H16  H  N N 39  
A1BRI H    H  N N 40  
A1BRI H1   H  N N 41  
A1BRI H2   H  N N 42  
ALA   N    N  N N 43  
ALA   CA   C  N S 44  
ALA   C    C  N N 45  
ALA   O    O  N N 46  
ALA   CB   C  N N 47  
ALA   OXT  O  N N 48  
ALA   H    H  N N 49  
ALA   H2   H  N N 50  
ALA   HA   H  N N 51  
ALA   HB1  H  N N 52  
ALA   HB2  H  N N 53  
ALA   HB3  H  N N 54  
ALA   HXT  H  N N 55  
ARG   N    N  N N 56  
ARG   CA   C  N S 57  
ARG   C    C  N N 58  
ARG   O    O  N N 59  
ARG   CB   C  N N 60  
ARG   CG   C  N N 61  
ARG   CD   C  N N 62  
ARG   NE   N  N N 63  
ARG   CZ   C  N N 64  
ARG   NH1  N  N N 65  
ARG   NH2  N  N N 66  
ARG   OXT  O  N N 67  
ARG   H    H  N N 68  
ARG   H2   H  N N 69  
ARG   HA   H  N N 70  
ARG   HB2  H  N N 71  
ARG   HB3  H  N N 72  
ARG   HG2  H  N N 73  
ARG   HG3  H  N N 74  
ARG   HD2  H  N N 75  
ARG   HD3  H  N N 76  
ARG   HE   H  N N 77  
ARG   HH11 H  N N 78  
ARG   HH12 H  N N 79  
ARG   HH21 H  N N 80  
ARG   HH22 H  N N 81  
ARG   HXT  H  N N 82  
ASN   N    N  N N 83  
ASN   CA   C  N S 84  
ASN   C    C  N N 85  
ASN   O    O  N N 86  
ASN   CB   C  N N 87  
ASN   CG   C  N N 88  
ASN   OD1  O  N N 89  
ASN   ND2  N  N N 90  
ASN   OXT  O  N N 91  
ASN   H    H  N N 92  
ASN   H2   H  N N 93  
ASN   HA   H  N N 94  
ASN   HB2  H  N N 95  
ASN   HB3  H  N N 96  
ASN   HD21 H  N N 97  
ASN   HD22 H  N N 98  
ASN   HXT  H  N N 99  
ASP   N    N  N N 100 
ASP   CA   C  N S 101 
ASP   C    C  N N 102 
ASP   O    O  N N 103 
ASP   CB   C  N N 104 
ASP   CG   C  N N 105 
ASP   OD1  O  N N 106 
ASP   OD2  O  N N 107 
ASP   OXT  O  N N 108 
ASP   H    H  N N 109 
ASP   H2   H  N N 110 
ASP   HA   H  N N 111 
ASP   HB2  H  N N 112 
ASP   HB3  H  N N 113 
ASP   HD2  H  N N 114 
ASP   HXT  H  N N 115 
CYS   N    N  N N 116 
CYS   CA   C  N R 117 
CYS   C    C  N N 118 
CYS   O    O  N N 119 
CYS   CB   C  N N 120 
CYS   SG   S  N N 121 
CYS   OXT  O  N N 122 
CYS   H    H  N N 123 
CYS   H2   H  N N 124 
CYS   HA   H  N N 125 
CYS   HB2  H  N N 126 
CYS   HB3  H  N N 127 
CYS   HG   H  N N 128 
CYS   HXT  H  N N 129 
GLN   N    N  N N 130 
GLN   CA   C  N S 131 
GLN   C    C  N N 132 
GLN   O    O  N N 133 
GLN   CB   C  N N 134 
GLN   CG   C  N N 135 
GLN   CD   C  N N 136 
GLN   OE1  O  N N 137 
GLN   NE2  N  N N 138 
GLN   OXT  O  N N 139 
GLN   H    H  N N 140 
GLN   H2   H  N N 141 
GLN   HA   H  N N 142 
GLN   HB2  H  N N 143 
GLN   HB3  H  N N 144 
GLN   HG2  H  N N 145 
GLN   HG3  H  N N 146 
GLN   HE21 H  N N 147 
GLN   HE22 H  N N 148 
GLN   HXT  H  N N 149 
GLU   N    N  N N 150 
GLU   CA   C  N S 151 
GLU   C    C  N N 152 
GLU   O    O  N N 153 
GLU   CB   C  N N 154 
GLU   CG   C  N N 155 
GLU   CD   C  N N 156 
GLU   OE1  O  N N 157 
GLU   OE2  O  N N 158 
GLU   OXT  O  N N 159 
GLU   H    H  N N 160 
GLU   H2   H  N N 161 
GLU   HA   H  N N 162 
GLU   HB2  H  N N 163 
GLU   HB3  H  N N 164 
GLU   HG2  H  N N 165 
GLU   HG3  H  N N 166 
GLU   HE2  H  N N 167 
GLU   HXT  H  N N 168 
GLY   N    N  N N 169 
GLY   CA   C  N N 170 
GLY   C    C  N N 171 
GLY   O    O  N N 172 
GLY   OXT  O  N N 173 
GLY   H    H  N N 174 
GLY   H2   H  N N 175 
GLY   HA2  H  N N 176 
GLY   HA3  H  N N 177 
GLY   HXT  H  N N 178 
HIS   N    N  N N 179 
HIS   CA   C  N S 180 
HIS   C    C  N N 181 
HIS   O    O  N N 182 
HIS   CB   C  N N 183 
HIS   CG   C  Y N 184 
HIS   ND1  N  Y N 185 
HIS   CD2  C  Y N 186 
HIS   CE1  C  Y N 187 
HIS   NE2  N  Y N 188 
HIS   OXT  O  N N 189 
HIS   H    H  N N 190 
HIS   H2   H  N N 191 
HIS   HA   H  N N 192 
HIS   HB2  H  N N 193 
HIS   HB3  H  N N 194 
HIS   HD1  H  N N 195 
HIS   HD2  H  N N 196 
HIS   HE1  H  N N 197 
HIS   HE2  H  N N 198 
HIS   HXT  H  N N 199 
HOH   O    O  N N 200 
HOH   H1   H  N N 201 
HOH   H2   H  N N 202 
ILE   N    N  N N 203 
ILE   CA   C  N S 204 
ILE   C    C  N N 205 
ILE   O    O  N N 206 
ILE   CB   C  N S 207 
ILE   CG1  C  N N 208 
ILE   CG2  C  N N 209 
ILE   CD1  C  N N 210 
ILE   OXT  O  N N 211 
ILE   H    H  N N 212 
ILE   H2   H  N N 213 
ILE   HA   H  N N 214 
ILE   HB   H  N N 215 
ILE   HG12 H  N N 216 
ILE   HG13 H  N N 217 
ILE   HG21 H  N N 218 
ILE   HG22 H  N N 219 
ILE   HG23 H  N N 220 
ILE   HD11 H  N N 221 
ILE   HD12 H  N N 222 
ILE   HD13 H  N N 223 
ILE   HXT  H  N N 224 
LEU   N    N  N N 225 
LEU   CA   C  N S 226 
LEU   C    C  N N 227 
LEU   O    O  N N 228 
LEU   CB   C  N N 229 
LEU   CG   C  N N 230 
LEU   CD1  C  N N 231 
LEU   CD2  C  N N 232 
LEU   OXT  O  N N 233 
LEU   H    H  N N 234 
LEU   H2   H  N N 235 
LEU   HA   H  N N 236 
LEU   HB2  H  N N 237 
LEU   HB3  H  N N 238 
LEU   HG   H  N N 239 
LEU   HD11 H  N N 240 
LEU   HD12 H  N N 241 
LEU   HD13 H  N N 242 
LEU   HD21 H  N N 243 
LEU   HD22 H  N N 244 
LEU   HD23 H  N N 245 
LEU   HXT  H  N N 246 
LYS   N    N  N N 247 
LYS   CA   C  N S 248 
LYS   C    C  N N 249 
LYS   O    O  N N 250 
LYS   CB   C  N N 251 
LYS   CG   C  N N 252 
LYS   CD   C  N N 253 
LYS   CE   C  N N 254 
LYS   NZ   N  N N 255 
LYS   OXT  O  N N 256 
LYS   H    H  N N 257 
LYS   H2   H  N N 258 
LYS   HA   H  N N 259 
LYS   HB2  H  N N 260 
LYS   HB3  H  N N 261 
LYS   HG2  H  N N 262 
LYS   HG3  H  N N 263 
LYS   HD2  H  N N 264 
LYS   HD3  H  N N 265 
LYS   HE2  H  N N 266 
LYS   HE3  H  N N 267 
LYS   HZ1  H  N N 268 
LYS   HZ2  H  N N 269 
LYS   HZ3  H  N N 270 
LYS   HXT  H  N N 271 
MET   N    N  N N 272 
MET   CA   C  N S 273 
MET   C    C  N N 274 
MET   O    O  N N 275 
MET   CB   C  N N 276 
MET   CG   C  N N 277 
MET   SD   S  N N 278 
MET   CE   C  N N 279 
MET   OXT  O  N N 280 
MET   H    H  N N 281 
MET   H2   H  N N 282 
MET   HA   H  N N 283 
MET   HB2  H  N N 284 
MET   HB3  H  N N 285 
MET   HG2  H  N N 286 
MET   HG3  H  N N 287 
MET   HE1  H  N N 288 
MET   HE2  H  N N 289 
MET   HE3  H  N N 290 
MET   HXT  H  N N 291 
PHE   N    N  N N 292 
PHE   CA   C  N S 293 
PHE   C    C  N N 294 
PHE   O    O  N N 295 
PHE   CB   C  N N 296 
PHE   CG   C  Y N 297 
PHE   CD1  C  Y N 298 
PHE   CD2  C  Y N 299 
PHE   CE1  C  Y N 300 
PHE   CE2  C  Y N 301 
PHE   CZ   C  Y N 302 
PHE   OXT  O  N N 303 
PHE   H    H  N N 304 
PHE   H2   H  N N 305 
PHE   HA   H  N N 306 
PHE   HB2  H  N N 307 
PHE   HB3  H  N N 308 
PHE   HD1  H  N N 309 
PHE   HD2  H  N N 310 
PHE   HE1  H  N N 311 
PHE   HE2  H  N N 312 
PHE   HZ   H  N N 313 
PHE   HXT  H  N N 314 
PRO   N    N  N N 315 
PRO   CA   C  N S 316 
PRO   C    C  N N 317 
PRO   O    O  N N 318 
PRO   CB   C  N N 319 
PRO   CG   C  N N 320 
PRO   CD   C  N N 321 
PRO   OXT  O  N N 322 
PRO   H    H  N N 323 
PRO   HA   H  N N 324 
PRO   HB2  H  N N 325 
PRO   HB3  H  N N 326 
PRO   HG2  H  N N 327 
PRO   HG3  H  N N 328 
PRO   HD2  H  N N 329 
PRO   HD3  H  N N 330 
PRO   HXT  H  N N 331 
SER   N    N  N N 332 
SER   CA   C  N S 333 
SER   C    C  N N 334 
SER   O    O  N N 335 
SER   CB   C  N N 336 
SER   OG   O  N N 337 
SER   OXT  O  N N 338 
SER   H    H  N N 339 
SER   H2   H  N N 340 
SER   HA   H  N N 341 
SER   HB2  H  N N 342 
SER   HB3  H  N N 343 
SER   HG   H  N N 344 
SER   HXT  H  N N 345 
THR   N    N  N N 346 
THR   CA   C  N S 347 
THR   C    C  N N 348 
THR   O    O  N N 349 
THR   CB   C  N R 350 
THR   OG1  O  N N 351 
THR   CG2  C  N N 352 
THR   OXT  O  N N 353 
THR   H    H  N N 354 
THR   H2   H  N N 355 
THR   HA   H  N N 356 
THR   HB   H  N N 357 
THR   HG1  H  N N 358 
THR   HG21 H  N N 359 
THR   HG22 H  N N 360 
THR   HG23 H  N N 361 
THR   HXT  H  N N 362 
TRP   N    N  N N 363 
TRP   CA   C  N S 364 
TRP   C    C  N N 365 
TRP   O    O  N N 366 
TRP   CB   C  N N 367 
TRP   CG   C  Y N 368 
TRP   CD1  C  Y N 369 
TRP   CD2  C  Y N 370 
TRP   NE1  N  Y N 371 
TRP   CE2  C  Y N 372 
TRP   CE3  C  Y N 373 
TRP   CZ2  C  Y N 374 
TRP   CZ3  C  Y N 375 
TRP   CH2  C  Y N 376 
TRP   OXT  O  N N 377 
TRP   H    H  N N 378 
TRP   H2   H  N N 379 
TRP   HA   H  N N 380 
TRP   HB2  H  N N 381 
TRP   HB3  H  N N 382 
TRP   HD1  H  N N 383 
TRP   HE1  H  N N 384 
TRP   HE3  H  N N 385 
TRP   HZ2  H  N N 386 
TRP   HZ3  H  N N 387 
TRP   HH2  H  N N 388 
TRP   HXT  H  N N 389 
TYR   N    N  N N 390 
TYR   CA   C  N S 391 
TYR   C    C  N N 392 
TYR   O    O  N N 393 
TYR   CB   C  N N 394 
TYR   CG   C  Y N 395 
TYR   CD1  C  Y N 396 
TYR   CD2  C  Y N 397 
TYR   CE1  C  Y N 398 
TYR   CE2  C  Y N 399 
TYR   CZ   C  Y N 400 
TYR   OH   O  N N 401 
TYR   OXT  O  N N 402 
TYR   H    H  N N 403 
TYR   H2   H  N N 404 
TYR   HA   H  N N 405 
TYR   HB2  H  N N 406 
TYR   HB3  H  N N 407 
TYR   HD1  H  N N 408 
TYR   HD2  H  N N 409 
TYR   HE1  H  N N 410 
TYR   HE2  H  N N 411 
TYR   HH   H  N N 412 
TYR   HXT  H  N N 413 
VAL   N    N  N N 414 
VAL   CA   C  N S 415 
VAL   C    C  N N 416 
VAL   O    O  N N 417 
VAL   CB   C  N N 418 
VAL   CG1  C  N N 419 
VAL   CG2  C  N N 420 
VAL   OXT  O  N N 421 
VAL   H    H  N N 422 
VAL   H2   H  N N 423 
VAL   HA   H  N N 424 
VAL   HB   H  N N 425 
VAL   HG11 H  N N 426 
VAL   HG12 H  N N 427 
VAL   HG13 H  N N 428 
VAL   HG21 H  N N 429 
VAL   HG22 H  N N 430 
VAL   HG23 H  N N 431 
VAL   HXT  H  N N 432 
ZN    ZN   ZN N N 433 
# 
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 
A1BRI N   C    sing N N 1   
A1BRI O   C    doub N N 2   
A1BRI C   C1   sing N N 3   
A1BRI C1  C2   sing N N 4   
A1BRI C2  C3   sing N N 5   
A1BRI C3  C4   sing N N 6   
A1BRI C4  N1   sing N N 7   
A1BRI N1  C5   sing N N 8   
A1BRI O1  C5   doub N N 9   
A1BRI C5  N2   sing N N 10  
A1BRI N2  C6   sing N N 11  
A1BRI C6  C7   doub Y N 12  
A1BRI C7  C8   sing Y N 13  
A1BRI C8  C9   doub Y N 14  
A1BRI C9  C10  sing Y N 15  
A1BRI C10 C11  doub Y N 16  
A1BRI C6  C11  sing Y N 17  
A1BRI C11 O2   sing N N 18  
A1BRI O2  C12  sing N N 19  
A1BRI C12 C13  sing N N 20  
A1BRI F   C13  sing N N 21  
A1BRI F1  C13  sing N N 22  
A1BRI C13 F2   sing N N 23  
A1BRI C14 N1   sing N N 24  
A1BRI C1  C14  sing N N 25  
A1BRI C4  H8   sing N N 26  
A1BRI C4  H7   sing N N 27  
A1BRI C7  H10  sing N N 28  
A1BRI C8  H11  sing N N 29  
A1BRI C10 H13  sing N N 30  
A1BRI C12 H14  sing N N 31  
A1BRI C12 H15  sing N N 32  
A1BRI C9  H12  sing N N 33  
A1BRI N2  H9   sing N N 34  
A1BRI C3  H6   sing N N 35  
A1BRI C3  H5   sing N N 36  
A1BRI C2  H4   sing N N 37  
A1BRI C2  H3   sing N N 38  
A1BRI C14 H17  sing N N 39  
A1BRI C14 H16  sing N N 40  
A1BRI C1  H    sing N N 41  
A1BRI N   H1   sing N N 42  
A1BRI N   H2   sing N N 43  
ALA   N   CA   sing N N 44  
ALA   N   H    sing N N 45  
ALA   N   H2   sing N N 46  
ALA   CA  C    sing N N 47  
ALA   CA  CB   sing N N 48  
ALA   CA  HA   sing N N 49  
ALA   C   O    doub N N 50  
ALA   C   OXT  sing N N 51  
ALA   CB  HB1  sing N N 52  
ALA   CB  HB2  sing N N 53  
ALA   CB  HB3  sing N N 54  
ALA   OXT HXT  sing N N 55  
ARG   N   CA   sing N N 56  
ARG   N   H    sing N N 57  
ARG   N   H2   sing N N 58  
ARG   CA  C    sing N N 59  
ARG   CA  CB   sing N N 60  
ARG   CA  HA   sing N N 61  
ARG   C   O    doub N N 62  
ARG   C   OXT  sing N N 63  
ARG   CB  CG   sing N N 64  
ARG   CB  HB2  sing N N 65  
ARG   CB  HB3  sing N N 66  
ARG   CG  CD   sing N N 67  
ARG   CG  HG2  sing N N 68  
ARG   CG  HG3  sing N N 69  
ARG   CD  NE   sing N N 70  
ARG   CD  HD2  sing N N 71  
ARG   CD  HD3  sing N N 72  
ARG   NE  CZ   sing N N 73  
ARG   NE  HE   sing N N 74  
ARG   CZ  NH1  sing N N 75  
ARG   CZ  NH2  doub N N 76  
ARG   NH1 HH11 sing N N 77  
ARG   NH1 HH12 sing N N 78  
ARG   NH2 HH21 sing N N 79  
ARG   NH2 HH22 sing N N 80  
ARG   OXT HXT  sing N N 81  
ASN   N   CA   sing N N 82  
ASN   N   H    sing N N 83  
ASN   N   H2   sing N N 84  
ASN   CA  C    sing N N 85  
ASN   CA  CB   sing N N 86  
ASN   CA  HA   sing N N 87  
ASN   C   O    doub N N 88  
ASN   C   OXT  sing N N 89  
ASN   CB  CG   sing N N 90  
ASN   CB  HB2  sing N N 91  
ASN   CB  HB3  sing N N 92  
ASN   CG  OD1  doub N N 93  
ASN   CG  ND2  sing N N 94  
ASN   ND2 HD21 sing N N 95  
ASN   ND2 HD22 sing N N 96  
ASN   OXT HXT  sing N N 97  
ASP   N   CA   sing N N 98  
ASP   N   H    sing N N 99  
ASP   N   H2   sing N N 100 
ASP   CA  C    sing N N 101 
ASP   CA  CB   sing N N 102 
ASP   CA  HA   sing N N 103 
ASP   C   O    doub N N 104 
ASP   C   OXT  sing N N 105 
ASP   CB  CG   sing N N 106 
ASP   CB  HB2  sing N N 107 
ASP   CB  HB3  sing N N 108 
ASP   CG  OD1  doub N N 109 
ASP   CG  OD2  sing N N 110 
ASP   OD2 HD2  sing N N 111 
ASP   OXT HXT  sing N N 112 
CYS   N   CA   sing N N 113 
CYS   N   H    sing N N 114 
CYS   N   H2   sing N N 115 
CYS   CA  C    sing N N 116 
CYS   CA  CB   sing N N 117 
CYS   CA  HA   sing N N 118 
CYS   C   O    doub N N 119 
CYS   C   OXT  sing N N 120 
CYS   CB  SG   sing N N 121 
CYS   CB  HB2  sing N N 122 
CYS   CB  HB3  sing N N 123 
CYS   SG  HG   sing N N 124 
CYS   OXT HXT  sing N N 125 
GLN   N   CA   sing N N 126 
GLN   N   H    sing N N 127 
GLN   N   H2   sing N N 128 
GLN   CA  C    sing N N 129 
GLN   CA  CB   sing N N 130 
GLN   CA  HA   sing N N 131 
GLN   C   O    doub N N 132 
GLN   C   OXT  sing N N 133 
GLN   CB  CG   sing N N 134 
GLN   CB  HB2  sing N N 135 
GLN   CB  HB3  sing N N 136 
GLN   CG  CD   sing N N 137 
GLN   CG  HG2  sing N N 138 
GLN   CG  HG3  sing N N 139 
GLN   CD  OE1  doub N N 140 
GLN   CD  NE2  sing N N 141 
GLN   NE2 HE21 sing N N 142 
GLN   NE2 HE22 sing N N 143 
GLN   OXT HXT  sing N N 144 
GLU   N   CA   sing N N 145 
GLU   N   H    sing N N 146 
GLU   N   H2   sing N N 147 
GLU   CA  C    sing N N 148 
GLU   CA  CB   sing N N 149 
GLU   CA  HA   sing N N 150 
GLU   C   O    doub N N 151 
GLU   C   OXT  sing N N 152 
GLU   CB  CG   sing N N 153 
GLU   CB  HB2  sing N N 154 
GLU   CB  HB3  sing N N 155 
GLU   CG  CD   sing N N 156 
GLU   CG  HG2  sing N N 157 
GLU   CG  HG3  sing N N 158 
GLU   CD  OE1  doub N N 159 
GLU   CD  OE2  sing N N 160 
GLU   OE2 HE2  sing N N 161 
GLU   OXT HXT  sing N N 162 
GLY   N   CA   sing N N 163 
GLY   N   H    sing N N 164 
GLY   N   H2   sing N N 165 
GLY   CA  C    sing N N 166 
GLY   CA  HA2  sing N N 167 
GLY   CA  HA3  sing N N 168 
GLY   C   O    doub N N 169 
GLY   C   OXT  sing N N 170 
GLY   OXT HXT  sing N N 171 
HIS   N   CA   sing N N 172 
HIS   N   H    sing N N 173 
HIS   N   H2   sing N N 174 
HIS   CA  C    sing N N 175 
HIS   CA  CB   sing N N 176 
HIS   CA  HA   sing N N 177 
HIS   C   O    doub N N 178 
HIS   C   OXT  sing N N 179 
HIS   CB  CG   sing N N 180 
HIS   CB  HB2  sing N N 181 
HIS   CB  HB3  sing N N 182 
HIS   CG  ND1  sing Y N 183 
HIS   CG  CD2  doub Y N 184 
HIS   ND1 CE1  doub Y N 185 
HIS   ND1 HD1  sing N N 186 
HIS   CD2 NE2  sing Y N 187 
HIS   CD2 HD2  sing N N 188 
HIS   CE1 NE2  sing Y N 189 
HIS   CE1 HE1  sing N N 190 
HIS   NE2 HE2  sing N N 191 
HIS   OXT HXT  sing N N 192 
HOH   O   H1   sing N N 193 
HOH   O   H2   sing N N 194 
ILE   N   CA   sing N N 195 
ILE   N   H    sing N N 196 
ILE   N   H2   sing N N 197 
ILE   CA  C    sing N N 198 
ILE   CA  CB   sing N N 199 
ILE   CA  HA   sing N N 200 
ILE   C   O    doub N N 201 
ILE   C   OXT  sing N N 202 
ILE   CB  CG1  sing N N 203 
ILE   CB  CG2  sing N N 204 
ILE   CB  HB   sing N N 205 
ILE   CG1 CD1  sing N N 206 
ILE   CG1 HG12 sing N N 207 
ILE   CG1 HG13 sing N N 208 
ILE   CG2 HG21 sing N N 209 
ILE   CG2 HG22 sing N N 210 
ILE   CG2 HG23 sing N N 211 
ILE   CD1 HD11 sing N N 212 
ILE   CD1 HD12 sing N N 213 
ILE   CD1 HD13 sing N N 214 
ILE   OXT HXT  sing N N 215 
LEU   N   CA   sing N N 216 
LEU   N   H    sing N N 217 
LEU   N   H2   sing N N 218 
LEU   CA  C    sing N N 219 
LEU   CA  CB   sing N N 220 
LEU   CA  HA   sing N N 221 
LEU   C   O    doub N N 222 
LEU   C   OXT  sing N N 223 
LEU   CB  CG   sing N N 224 
LEU   CB  HB2  sing N N 225 
LEU   CB  HB3  sing N N 226 
LEU   CG  CD1  sing N N 227 
LEU   CG  CD2  sing N N 228 
LEU   CG  HG   sing N N 229 
LEU   CD1 HD11 sing N N 230 
LEU   CD1 HD12 sing N N 231 
LEU   CD1 HD13 sing N N 232 
LEU   CD2 HD21 sing N N 233 
LEU   CD2 HD22 sing N N 234 
LEU   CD2 HD23 sing N N 235 
LEU   OXT HXT  sing N N 236 
LYS   N   CA   sing N N 237 
LYS   N   H    sing N N 238 
LYS   N   H2   sing N N 239 
LYS   CA  C    sing N N 240 
LYS   CA  CB   sing N N 241 
LYS   CA  HA   sing N N 242 
LYS   C   O    doub N N 243 
LYS   C   OXT  sing N N 244 
LYS   CB  CG   sing N N 245 
LYS   CB  HB2  sing N N 246 
LYS   CB  HB3  sing N N 247 
LYS   CG  CD   sing N N 248 
LYS   CG  HG2  sing N N 249 
LYS   CG  HG3  sing N N 250 
LYS   CD  CE   sing N N 251 
LYS   CD  HD2  sing N N 252 
LYS   CD  HD3  sing N N 253 
LYS   CE  NZ   sing N N 254 
LYS   CE  HE2  sing N N 255 
LYS   CE  HE3  sing N N 256 
LYS   NZ  HZ1  sing N N 257 
LYS   NZ  HZ2  sing N N 258 
LYS   NZ  HZ3  sing N N 259 
LYS   OXT HXT  sing N N 260 
MET   N   CA   sing N N 261 
MET   N   H    sing N N 262 
MET   N   H2   sing N N 263 
MET   CA  C    sing N N 264 
MET   CA  CB   sing N N 265 
MET   CA  HA   sing N N 266 
MET   C   O    doub N N 267 
MET   C   OXT  sing N N 268 
MET   CB  CG   sing N N 269 
MET   CB  HB2  sing N N 270 
MET   CB  HB3  sing N N 271 
MET   CG  SD   sing N N 272 
MET   CG  HG2  sing N N 273 
MET   CG  HG3  sing N N 274 
MET   SD  CE   sing N N 275 
MET   CE  HE1  sing N N 276 
MET   CE  HE2  sing N N 277 
MET   CE  HE3  sing N N 278 
MET   OXT HXT  sing N N 279 
PHE   N   CA   sing N N 280 
PHE   N   H    sing N N 281 
PHE   N   H2   sing N N 282 
PHE   CA  C    sing N N 283 
PHE   CA  CB   sing N N 284 
PHE   CA  HA   sing N N 285 
PHE   C   O    doub N N 286 
PHE   C   OXT  sing N N 287 
PHE   CB  CG   sing N N 288 
PHE   CB  HB2  sing N N 289 
PHE   CB  HB3  sing N N 290 
PHE   CG  CD1  doub Y N 291 
PHE   CG  CD2  sing Y N 292 
PHE   CD1 CE1  sing Y N 293 
PHE   CD1 HD1  sing N N 294 
PHE   CD2 CE2  doub Y N 295 
PHE   CD2 HD2  sing N N 296 
PHE   CE1 CZ   doub Y N 297 
PHE   CE1 HE1  sing N N 298 
PHE   CE2 CZ   sing Y N 299 
PHE   CE2 HE2  sing N N 300 
PHE   CZ  HZ   sing N N 301 
PHE   OXT HXT  sing N N 302 
PRO   N   CA   sing N N 303 
PRO   N   CD   sing N N 304 
PRO   N   H    sing N N 305 
PRO   CA  C    sing N N 306 
PRO   CA  CB   sing N N 307 
PRO   CA  HA   sing N N 308 
PRO   C   O    doub N N 309 
PRO   C   OXT  sing N N 310 
PRO   CB  CG   sing N N 311 
PRO   CB  HB2  sing N N 312 
PRO   CB  HB3  sing N N 313 
PRO   CG  CD   sing N N 314 
PRO   CG  HG2  sing N N 315 
PRO   CG  HG3  sing N N 316 
PRO   CD  HD2  sing N N 317 
PRO   CD  HD3  sing N N 318 
PRO   OXT HXT  sing N N 319 
SER   N   CA   sing N N 320 
SER   N   H    sing N N 321 
SER   N   H2   sing N N 322 
SER   CA  C    sing N N 323 
SER   CA  CB   sing N N 324 
SER   CA  HA   sing N N 325 
SER   C   O    doub N N 326 
SER   C   OXT  sing N N 327 
SER   CB  OG   sing N N 328 
SER   CB  HB2  sing N N 329 
SER   CB  HB3  sing N N 330 
SER   OG  HG   sing N N 331 
SER   OXT HXT  sing N N 332 
THR   N   CA   sing N N 333 
THR   N   H    sing N N 334 
THR   N   H2   sing N N 335 
THR   CA  C    sing N N 336 
THR   CA  CB   sing N N 337 
THR   CA  HA   sing N N 338 
THR   C   O    doub N N 339 
THR   C   OXT  sing N N 340 
THR   CB  OG1  sing N N 341 
THR   CB  CG2  sing N N 342 
THR   CB  HB   sing N N 343 
THR   OG1 HG1  sing N N 344 
THR   CG2 HG21 sing N N 345 
THR   CG2 HG22 sing N N 346 
THR   CG2 HG23 sing N N 347 
THR   OXT HXT  sing N N 348 
TRP   N   CA   sing N N 349 
TRP   N   H    sing N N 350 
TRP   N   H2   sing N N 351 
TRP   CA  C    sing N N 352 
TRP   CA  CB   sing N N 353 
TRP   CA  HA   sing N N 354 
TRP   C   O    doub N N 355 
TRP   C   OXT  sing N N 356 
TRP   CB  CG   sing N N 357 
TRP   CB  HB2  sing N N 358 
TRP   CB  HB3  sing N N 359 
TRP   CG  CD1  doub Y N 360 
TRP   CG  CD2  sing Y N 361 
TRP   CD1 NE1  sing Y N 362 
TRP   CD1 HD1  sing N N 363 
TRP   CD2 CE2  doub Y N 364 
TRP   CD2 CE3  sing Y N 365 
TRP   NE1 CE2  sing Y N 366 
TRP   NE1 HE1  sing N N 367 
TRP   CE2 CZ2  sing Y N 368 
TRP   CE3 CZ3  doub Y N 369 
TRP   CE3 HE3  sing N N 370 
TRP   CZ2 CH2  doub Y N 371 
TRP   CZ2 HZ2  sing N N 372 
TRP   CZ3 CH2  sing Y N 373 
TRP   CZ3 HZ3  sing N N 374 
TRP   CH2 HH2  sing N N 375 
TRP   OXT HXT  sing N N 376 
TYR   N   CA   sing N N 377 
TYR   N   H    sing N N 378 
TYR   N   H2   sing N N 379 
TYR   CA  C    sing N N 380 
TYR   CA  CB   sing N N 381 
TYR   CA  HA   sing N N 382 
TYR   C   O    doub N N 383 
TYR   C   OXT  sing N N 384 
TYR   CB  CG   sing N N 385 
TYR   CB  HB2  sing N N 386 
TYR   CB  HB3  sing N N 387 
TYR   CG  CD1  doub Y N 388 
TYR   CG  CD2  sing Y N 389 
TYR   CD1 CE1  sing Y N 390 
TYR   CD1 HD1  sing N N 391 
TYR   CD2 CE2  doub Y N 392 
TYR   CD2 HD2  sing N N 393 
TYR   CE1 CZ   doub Y N 394 
TYR   CE1 HE1  sing N N 395 
TYR   CE2 CZ   sing Y N 396 
TYR   CE2 HE2  sing N N 397 
TYR   CZ  OH   sing N N 398 
TYR   OH  HH   sing N N 399 
TYR   OXT HXT  sing N N 400 
VAL   N   CA   sing N N 401 
VAL   N   H    sing N N 402 
VAL   N   H2   sing N N 403 
VAL   CA  C    sing N N 404 
VAL   CA  CB   sing N N 405 
VAL   CA  HA   sing N N 406 
VAL   C   O    doub N N 407 
VAL   C   OXT  sing N N 408 
VAL   CB  CG1  sing N N 409 
VAL   CB  CG2  sing N N 410 
VAL   CB  HB   sing N N 411 
VAL   CG1 HG11 sing N N 412 
VAL   CG1 HG12 sing N N 413 
VAL   CG1 HG13 sing N N 414 
VAL   CG2 HG21 sing N N 415 
VAL   CG2 HG22 sing N N 416 
VAL   CG2 HG23 sing N N 417 
VAL   OXT HXT  sing N N 418 
# 
_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                    7HXO 
_atom_sites.fract_transf_matrix[1][1]   0.011238 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000660 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017288 
_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]   0.030554 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
F  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER   A 1 1   ? 18.643 6.957   24.332 1.00 29.63  ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 19.895 7.113   23.608 1.00 29.56  ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 20.077 5.984   22.570 1.00 29.02  ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 19.493 4.899   22.725 1.00 29.33  ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 21.066 7.113   24.587 1.00 32.75  ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 21.033 5.917   25.348 1.00 37.41  ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 20.832 6.262   21.507 1.00 27.24  ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 21.079 5.264   20.470 1.00 26.15  ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 21.362 5.803   19.070 1.00 25.87  ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 20.943 6.902   18.707 1.00 24.88  ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 22.055 5.003   18.243 1.00 25.03  ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 22.408 5.429   16.892 1.00 25.54  ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 22.385 4.255   15.908 1.00 25.59  ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 22.349 3.086   16.339 1.00 26.29  ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.814 6.049   16.918 1.00 26.15  ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 22.356 4.562   14.580 1.00 24.77  ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.472 3.593   13.493 1.00 24.32  ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 23.910 3.742   12.911 1.00 27.30  ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.364 4.871   12.689 1.00 27.70  ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.432 3.843   12.367 1.00 23.34  ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 19.989 3.848   12.870 1.00 22.32  ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.615 2.818   11.220 1.00 23.98  ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.047 4.475   11.803 1.00 20.68  ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.638 2.628   12.665 1.00 28.40  ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 25.995 2.713   12.116 1.00 29.83  ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 26.037 1.958   10.794 1.00 30.34  ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 26.035 0.730   10.804 1.00 31.05  ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.039 2.153   13.111 1.00 29.86  ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.140 2.966   14.382 1.00 31.41  ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 27.931 4.109   14.443 1.00 32.14  ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 26.431 2.607   15.519 1.00 32.69  ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 27.995 4.881   15.598 1.00 33.09  ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 26.481 3.376   16.674 1.00 33.93  ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 27.290 4.496   16.719 1.00 34.19  ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 27.331 5.246   17.862 1.00 36.96  ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 25.967 2.672   9.657  1.00 30.70  ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 25.963 2.092   8.300  1.00 30.86  ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.112 2.685   7.479  1.00 32.35  ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.257 3.913   7.424  1.00 32.19  ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.583 2.283   7.599  1.00 31.85  ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.112 3.739   7.666  1.00 31.63  ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.601 1.760   6.156  1.00 32.35  ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 27.999 1.836   6.925  1.00 33.06  ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.176 2.333   6.209  1.00 34.46  ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.004 3.297   7.050  1.00 36.32  ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.251 3.022   8.228  1.00 37.09  ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.326 4.493   6.511  1.00 36.22  ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.055 5.479   7.291  1.00 36.46  ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.101 6.586   7.778  1.00 35.24  ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.442 7.769   7.739  1.00 35.27  ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.278 6.031   6.548  1.00 38.66  ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.382 4.994   6.411  1.00 44.95  ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.265 4.858   7.270  1.00 47.39  ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.338 4.214   5.341  1.00 45.83  ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 28.920 6.195   8.268  1.00 33.67  ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 27.918 7.148   8.741  1.00 32.37  ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.370 6.754   10.135 1.00 30.08  ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.251 5.573   10.432 1.00 29.92  ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.734 7.185   7.747  1.00 32.62  ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.088 7.695   6.365  1.00 34.44  ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 27.694 8.931   6.192  1.00 35.87  ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 26.784 6.956   5.229  1.00 35.50  ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.010 9.409   4.926  1.00 37.12  ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.099 7.423   3.959  1.00 37.09  ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 27.709 8.651   3.811  1.00 38.83  ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.022 9.118   2.553  1.00 42.37  ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.037 7.746   10.977 1.00 28.71  ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.411 7.552   12.295 1.00 27.96  ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.120 8.382   12.243 1.00 26.19  ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.185 9.588   12.017 1.00 26.30  ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.321 8.034   13.453 1.00 29.53  ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.582 8.298   14.784 1.00 32.69  ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.558 8.616   15.910 1.00 34.82  ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 27.069 9.660   16.815 1.00 37.68  ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 26.530 9.427   18.007 1.00 38.26  ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 26.355 8.181   18.434 1.00 35.91  ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 26.132 10.436  18.767 1.00 39.67  ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 23.964 7.741   12.394 1.00 24.15  ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.685 8.432   12.332 1.00 22.76  ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.139 8.548   13.756 1.00 22.76  ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 21.915 7.526   14.419 1.00 23.33  ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.668 7.651   11.472 1.00 22.66  ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.379 8.450   11.278 1.00 22.66  ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.264 7.222   10.123 1.00 22.44  ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 21.886 9.753   14.199 1.00 21.18  ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 21.365 9.987   15.551 1.00 22.55  ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 20.172 10.922  15.501 1.00 21.27  ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 19.948 11.606  14.503 1.00 22.05  ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 22.443 10.593  16.499 1.00 25.11  ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 23.552 9.610   16.759 1.00 28.10  ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 22.983 11.921  15.958 1.00 25.73  ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 19.395 11.000  16.622 1.00 21.00  ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 18.358 12.035  16.748 1.00 19.45  ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 19.101 13.377  16.777 1.00 20.67  ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 20.075 13.515  17.542 1.00 20.83  ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.624 11.883  18.091 1.00 19.43  ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 16.802 10.619  18.166 1.00 19.30  ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.277 9.601   18.652 1.00 21.50  ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 15.564 10.635  17.642 1.00 19.19  ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 18.665 14.355  15.990 1.00 20.48  ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 19.367 15.658  15.924 1.00 21.73  ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 19.421 16.322  17.279 1.00 22.41  ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 20.469 16.865  17.655 1.00 23.66  ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 18.673 16.586  14.917 1.00 22.72  ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.441 17.884  14.567 1.00 23.68  ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 18.471 18.773  13.806 1.00 24.64  ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.058 20.020  13.297 1.00 26.20  ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.033 21.180  13.952 1.00 28.94  ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 18.520 21.253  15.180 1.00 26.25  ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 19.531 22.279  13.390 1.00 31.52  ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 18.335 16.187  18.062 1.00 22.49  ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 18.276 16.807  19.386 1.00 22.48  ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 19.263 16.196  20.400 1.00 23.64  ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 19.515 16.809  21.437 1.00 24.54  ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 16.847 16.863  19.928 1.00 22.47  ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 16.294 15.566  20.443 1.00 21.06  ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 15.621 14.687  19.615 1.00 22.04  ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 16.236 15.101  21.717 1.00 21.72  ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 15.184 13.712  20.399 1.00 23.56  ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 15.528 13.917  21.676 1.00 22.39  ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 19.847 15.027  20.080 1.00 23.48  ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 20.813 14.366  20.961 1.00 25.26  ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 22.262 14.358  20.385 1.00 28.28  ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 23.135 13.694  20.943 1.00 29.72  ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 20.346 12.919  21.263 1.00 24.45  ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 19.015 12.787  22.031 1.00 25.39  ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 18.703 11.325  22.363 1.00 25.54  ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 19.018 13.621  23.348 1.00 25.67  ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 22.487 15.005  19.226 1.00 28.67  ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 23.796 15.066  18.584 1.00 29.44  ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 24.792 15.776  19.509 1.00 32.05  ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 24.405 16.730  20.193 1.00 32.45  ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 23.687 15.834  17.269 1.00 28.67  ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 26.027 15.253  19.600 1.00 33.98  ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 27.111 15.853  20.398 1.00 36.82  ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 27.788 16.974  19.563 1.00 38.46  ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 27.573 17.039  18.343 1.00 38.55  ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 28.090 14.765  20.847 1.00 39.11  ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 28.761 14.223  19.709 1.00 41.15  ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 27.410 13.642  21.593 1.00 39.40  ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 28.587 17.882  20.197 1.00 38.92  ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 29.239 18.963  19.419 1.00 39.87  ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 30.185 18.416  18.336 1.00 39.57  ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 30.350 19.056  17.295 1.00 40.35  ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 29.943 20.003  20.329 1.00 42.10  ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 31.302 19.593  20.792 1.00 46.03  ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 32.427 20.355  20.492 1.00 48.94  ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 31.678 18.527  21.534 1.00 47.51  ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 33.447 19.720  21.045 1.00 49.82  ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 33.053 18.604  21.666 1.00 49.36  ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 30.753 17.212  18.569 1.00 38.02  ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 31.626 16.454  17.669 1.00 38.71  ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 30.882 15.877  16.467 1.00 38.49  ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 31.516 15.573  15.451 1.00 38.46  ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 32.257 15.287  18.414 1.00 40.91  ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 33.206 15.727  19.498 1.00 48.01  ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 33.952 16.717  19.368 1.00 50.03  ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 33.206 14.991  20.595 1.00 50.28  ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 29.550 15.622  16.613 1.00 37.10  ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 28.728 15.157  15.502 1.00 35.19  ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 28.596 16.358  14.544 1.00 34.59  ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 28.716 16.163  13.341 1.00 34.72  ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 27.320 14.685  15.966 1.00 33.56  ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 27.229 13.295  16.600 1.00 34.43  ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 27.797 12.334  16.024 1.00 33.86  ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 26.565 13.162  17.653 1.00 32.74  ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 28.366 17.600  15.076 1.00 34.01  ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.267 18.822  14.273 1.00 34.80  ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 29.594 19.129  13.537 1.00 35.47  ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 29.574 19.481  12.350 1.00 35.46  ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 27.848 20.013  15.131 1.00 34.31  ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 26.395 19.981  15.466 1.00 33.75  ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 25.828 19.593  16.643 1.00 34.24  ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 25.318 20.361  14.602 1.00 33.56  ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 24.457 19.699  16.562 1.00 34.21  ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 24.117 20.138  15.306 1.00 33.86  ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 25.251 20.839  13.286 1.00 33.76  ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 22.866 20.390  14.744 1.00 34.25  ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.011 21.122  12.743 1.00 34.32  ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 22.835 20.863  13.457 1.00 34.49  ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 30.736 18.902  14.202 1.00 35.63  ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.037 19.092  13.556 1.00 38.08  ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.194 18.124  12.368 1.00 39.43  ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 32.816 18.474  11.357 1.00 41.14  ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 33.158 18.854  14.563 1.00 38.66  ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 31.636 16.890  12.500 1.00 37.68  ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 31.712 15.867  11.473 1.00 37.88  ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.394 15.698  10.699 1.00 36.79  ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.109 14.615  10.180 1.00 36.85  ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.124 14.548  12.120 1.00 40.52  ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 33.522 14.620  12.680 1.00 46.78  ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 34.478 14.928  11.966 1.00 49.45  ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 33.676 14.367  13.972 1.00 47.99  ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 29.600 16.768  10.615 1.00 34.95  ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.316 16.738  9.923  1.00 33.70  ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.410 16.362  8.439  1.00 33.66  ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.260 16.894  7.702  1.00 33.69  ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 27.656 18.114  10.044 1.00 32.28  ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.289 18.262  9.383  1.00 32.24  ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.247 17.423  10.156 1.00 32.57  ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 25.839 19.748  9.351  1.00 31.29  ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.481 15.487  7.998  1.00 32.60  ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.295 15.103  6.615  1.00 32.30  ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 25.944 15.719  6.133  1.00 32.43  ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 25.873 16.329  5.062  1.00 33.12  ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.297 13.554  6.478  1.00 33.21  ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 26.838 13.130  5.090  1.00 33.55  ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 28.679 12.990  6.776  1.00 33.84  ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 24.869 15.547  6.945  1.00 30.81  ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 23.527 16.044  6.623  1.00 30.06  ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 22.671 16.129  7.881  1.00 29.52  ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 22.792 15.282  8.758  1.00 29.03  ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 22.865 15.108  5.610  1.00 30.16  ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.394 15.298  5.358  1.00 30.28  ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 20.817 16.109  4.425  1.00 32.00  ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.313 14.609  6.018  1.00 29.77  ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.446 15.940  4.433  1.00 32.32  ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.110 15.057  5.431  1.00 30.69  ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.249 13.669  7.053  1.00 29.22  ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 17.868 14.551  5.804  1.00 30.03  ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.015 13.178  7.427  1.00 28.44  ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 17.842 13.644  6.829  1.00 28.96  ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 21.796 17.139  7.959  1.00 28.19  ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 20.873 17.250  9.089  1.00 27.57  ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 19.567 17.882  8.637  1.00 27.80  ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 19.566 18.699  7.702  1.00 29.26  ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 21.504 17.971  10.284 1.00 27.90  ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.066 19.370  9.979  1.00 30.20  ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.078 20.525  9.996  1.00 33.34  ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 21.396 21.575  9.389  1.00 32.76  ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 19.991 20.394  10.607 1.00 31.07  ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 18.450 17.489  9.261  1.00 25.80  ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.157 18.070  8.953  1.00 25.05  ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.378 18.173  10.268 1.00 24.60  ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 15.948 17.157  10.814 1.00 24.13  ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.438 17.251  7.874  1.00 26.42  ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.117 17.811  7.377  1.00 31.35  ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 14.544 18.685  8.064  1.00 33.58  ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 14.638 17.348  6.308  1.00 32.41  ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.227 19.402  10.789 1.00 24.28  ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 15.502 19.671  12.018 0.50 24.28  ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 15.516 19.591  12.050 0.50 24.83  ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 14.048 19.164  11.919 1.00 24.36  ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 13.506 18.596  12.874 1.00 24.97  ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 15.496 21.174  12.283 0.50 24.90  ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 15.637 21.026  12.562 0.50 27.14  ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 14.892 21.425  13.535 0.50 25.87  ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 14.680 21.876  11.963 0.50 30.27  ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 13.415 19.369  10.731 1.00 24.01  ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 12.025 18.924  10.560 1.00 24.68  ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 11.871 17.400  10.691 1.00 23.17  ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 10.783 16.940  10.982 1.00 24.73  ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 11.425 19.394  9.241  1.00 28.20  ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 11.870 18.587  8.162  1.00 33.17  ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 12.938 16.642  10.477 1.00 21.87  ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 12.912 15.180  10.637 1.00 21.09  ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 13.491 14.682  11.964 1.00 21.77  ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 13.393 13.470  12.244 1.00 21.50  ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 13.680 14.525  9.496  1.00 21.81  ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 13.077 14.787  8.145  1.00 24.11  ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 13.903 14.111  7.071  1.00 24.03  ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 13.793 12.647  7.173  1.00 24.60  ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 13.850 11.828  6.123  1.00 25.56  ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 14.014 12.319  4.893  1.00 26.16  ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 13.695 10.519  6.287  1.00 23.96  ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 14.122 15.571  12.770 1.00 21.15  ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 14.839 15.202  14.010 1.00 19.85  ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 15.979 14.240  13.680 1.00 20.08  ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 16.271 13.376  14.498 1.00 19.57  ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 13.910 14.603  15.142 1.00 20.43  ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 14.661 14.333  16.460 1.00 19.08  ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 15.535 15.146  16.817 1.00 18.07  ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 14.384 13.284  17.124 1.00 19.57  ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 16.681 14.395  12.507 1.00 20.46  ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 17.790 13.481  12.175 1.00 21.28  ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 19.092 14.240  11.943 1.00 22.41  ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 19.068 15.365  11.434 1.00 22.67  ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.497 12.690  10.895 1.00 22.06  ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 16.431 11.590  11.010 1.00 22.99  ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 16.284 10.886  9.667  1.00 22.66  ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 16.806 10.570  12.096 1.00 23.70  ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 20.208 13.625  12.323 1.00 22.45  ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 21.548 14.151  12.055 1.00 23.70  ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 22.450 12.985  11.687 1.00 24.22  ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 22.369 11.923  12.313 1.00 24.32  ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 22.107 14.918  13.261 1.00 23.84  ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 23.465 15.618  13.013 1.00 25.17  ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 23.519 16.961  13.723 1.00 25.12  ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 24.612 14.744  13.507 1.00 26.62  ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 23.232 13.132  10.612 1.00 24.02  ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 24.162 12.087  10.181 1.00 25.36  ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 25.567 12.669  10.262 1.00 27.36  ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 25.801 13.743  9.714  1.00 27.63  ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 23.833 11.604  8.755  1.00 27.37  ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 24.919 10.655  8.229  1.00 28.94  ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 22.463 10.912  8.712  1.00 27.68  ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 26.482 12.001  10.963 1.00 28.13  ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 27.881 12.436  11.000 1.00 29.78  ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 28.771 11.339  10.340 1.00 32.15  ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 28.363 10.185  10.222 1.00 31.25  ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 28.346 12.696  12.427 1.00 30.77  ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 28.078 11.615  13.308 1.00 32.05  ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 29.975 11.716  9.912  1.00 33.90  ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 30.964 10.816  9.313  1.00 35.46  ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 31.685 10.034  10.427 1.00 36.76  ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 31.870 10.565  11.524 1.00 37.51  ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 31.994 11.644  8.550  1.00 37.11  ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 32.601 12.567  9.441  1.00 39.88  ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 32.099 8.791   10.154 1.00 37.66  ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 32.809 7.965   11.143 1.00 39.49  ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 34.144 7.439   10.570 1.00 42.11  ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 34.245 7.227   9.361  1.00 42.65  ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 31.951 6.742   11.579 1.00 39.42  ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 31.896 5.782   10.528 1.00 39.58  ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 30.549 7.123   12.038 1.00 38.91  ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? 35.124 7.136   11.440 1.00 44.14  ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? 36.401 6.590   10.973 1.00 46.92  ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? 36.284 5.104   10.655 1.00 48.08  ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? 36.780 4.642   9.622  1.00 48.78  ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? 37.514 6.856   11.992 1.00 49.78  ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? 37.073 6.408   13.278 1.00 52.07  ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? 37.901 8.322   12.058 1.00 50.16  ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? 35.632 4.351   11.543 1.00 47.65  ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? 35.445 2.921   11.332 1.00 47.57  ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 34.155 2.639   10.567 1.00 46.32  ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 33.183 3.378   10.683 1.00 45.38  ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? 35.416 2.197   12.668 1.00 48.31  ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 34.139 1.543   9.814  1.00 45.62  ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 32.956 1.148   9.060  1.00 44.97  ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 31.941 0.427   9.985  1.00 42.46  ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 32.339 -0.347  10.854 1.00 42.79  ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 33.363 0.289   7.850  1.00 47.83  ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 32.283 0.166   6.780  1.00 53.69  ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 32.794 -0.536  5.547  1.00 60.85  ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 33.987 -0.463  5.207  1.00 63.50  ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 31.904 -1.236  4.848  1.00 61.75  ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 30.662 0.766   9.827  1.00 40.01  ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 29.539 0.219   10.579 1.00 38.23  ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 28.913 -0.972  9.881  1.00 36.13  ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 29.178 -1.211  8.700  1.00 36.71  ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 28.105 -1.769  10.612 1.00 33.85  ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 27.575 -3.005  10.055 1.00 32.60  ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 26.044 -3.110  10.013 1.00 30.62  ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 25.536 -4.200  9.780  1.00 30.72  ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 28.180 -4.200  10.779 1.00 33.29  ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 29.989 -4.177  10.847 1.00 35.85  ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 25.312 -2.009  10.243 1.00 28.78  ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 23.853 -2.062  10.150 1.00 28.25  ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 23.479 -1.958  8.673  1.00 28.21  ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 24.157 -1.277  7.881  1.00 29.38  ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 23.199 -0.887  10.933 1.00 28.94  ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 23.363 -0.980  12.448 1.00 32.55  ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 23.378 -2.107  12.970 1.00 33.98  ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 23.480 0.088   13.111 1.00 33.09  ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 22.393 -2.599  8.319  1.00 27.51  ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 21.833 -2.552  6.968  1.00 28.78  ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 20.536 -1.756  7.025  1.00 27.33  ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 19.719 -2.038  7.892  1.00 27.37  ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 21.522 -3.994  6.516  1.00 32.07  ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 22.772 -4.652  6.327  1.00 34.05  ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 20.711 -4.048  5.205  1.00 33.06  ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 20.347 -0.776  6.138  1.00 26.38  ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 19.116 0.009   6.103  1.00 25.46  ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 18.077 -0.752  5.260  1.00 25.69  ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 18.407 -1.266  4.191  1.00 26.93  ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 19.373 1.424   5.522  1.00 25.76  ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 20.525 2.161   6.275  1.00 26.10  ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 18.105 2.279   5.520  1.00 25.57  ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 20.285 2.294   7.806  1.00 27.79  ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 16.836 -0.814  5.717  1.00 24.59  ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 15.758 -1.463  4.977  1.00 23.90  ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 15.396 -0.624  3.749  1.00 22.67  ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 15.343 0.593   3.866  1.00 21.90  ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 14.532 -1.580  5.852  1.00 23.17  ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 15.089 -1.266  2.591  1.00 21.60  ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 14.604 -0.529  1.421  1.00 23.16  ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 13.300 -1.227  1.025  1.00 23.84  ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 13.302 -2.212  0.274  1.00 24.50  ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 15.635 -0.515  0.295  1.00 23.91  ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 16.986 0.093   0.715  1.00 25.87  ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 16.941 1.548   1.135  1.00 28.59  ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 18.271 2.003   1.581  1.00 29.77  ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 18.501 3.149   2.214  1.00 31.19  ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 17.504 3.980   2.480  1.00 29.78  ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 19.719 3.447   2.634  1.00 32.36  ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 12.195 -0.777  1.646  1.00 24.57  ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 10.902 -1.471  1.594  1.00 23.41  ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 9.751  -0.514  2.040  1.00 22.45  ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 10.013 0.618   2.428  1.00 21.92  ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 10.992 -2.650  2.565  1.00 23.69  ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 11.071 -2.108  4.302  1.00 21.24  ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 8.479  -1.017  2.003  1.00 23.35  ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 7.316  -0.294  2.516  1.00 24.00  ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 6.669  -1.137  3.644  1.00 23.43  ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 5.452  -1.079  3.805  1.00 24.49  ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 6.264  0.035   1.425  1.00 27.58  ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 5.612  -1.155  0.752  1.00 35.82  ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 6.117  -2.279  0.918  1.00 38.28  ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 4.593  -0.960  0.055  1.00 39.28  ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 7.463  -1.890  4.435  1.00 21.40  ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 6.928  -2.680  5.575  1.00 20.40  ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 6.181  -1.727  6.531  1.00 20.11  ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 6.609  -0.583  6.739  1.00 19.05  ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 8.060  -3.367  6.339  1.00 20.34  ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 8.772  -4.832  5.532  1.00 23.96  ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 5.109  -2.224  7.146  1.00 20.02  ? 59  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 53  ? 4.402  -1.496  8.189  1.00 21.04  ? 59  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 53  ? 4.344  -2.323  9.492  1.00 20.76  ? 59  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 53  ? 3.550  -1.998  10.373 1.00 21.30  ? 59  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 53  ? 2.976  -1.088  7.746  1.00 22.94  ? 59  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 53  ? 2.898  0.245   7.055  1.00 26.55  ? 59  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 53  ? 1.459  0.642   6.795  1.00 30.53  ? 59  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 53  ? 0.919  0.408   5.705  1.00 31.20  ? 59  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 53  ? 0.791  1.251   7.796  1.00 29.14  ? 59  GLN   A NE2 1 
ATOM   415  N  N   . THR   A 1 54  ? 5.134  -3.434  9.597  1.00 19.50  ? 60  THR   A N   1 
ATOM   416  C  CA  . THR   A 1 54  ? 5.232  -4.242  10.817 1.00 19.45  ? 60  THR   A CA  1 
ATOM   417  C  C   . THR   A 1 54  ? 6.723  -4.443  11.077 1.00 19.33  ? 60  THR   A C   1 
ATOM   418  O  O   . THR   A 1 54  ? 7.534  -4.490  10.148 1.00 19.73  ? 60  THR   A O   1 
ATOM   419  C  CB  . THR   A 1 54  ? 4.410  -5.550  10.757 1.00 21.95  ? 60  THR   A CB  1 
ATOM   420  O  OG1 . THR   A 1 54  ? 5.013  -6.426  9.813  1.00 24.98  ? 60  THR   A OG1 1 
ATOM   421  C  CG2 . THR   A 1 54  ? 2.924  -5.320  10.408 1.00 22.48  ? 60  THR   A CG2 1 
ATOM   422  N  N   . GLY   A 1 55  ? 7.088  -4.443  12.340 1.00 18.97  ? 61  GLY   A N   1 
ATOM   423  C  CA  . GLY   A 1 55  ? 8.488  -4.538  12.736 1.00 17.72  ? 61  GLY   A CA  1 
ATOM   424  C  C   . GLY   A 1 55  ? 8.640  -4.699  14.232 1.00 17.83  ? 61  GLY   A C   1 
ATOM   425  O  O   . GLY   A 1 55  ? 7.708  -5.123  14.899 1.00 19.26  ? 61  GLY   A O   1 
ATOM   426  N  N   . VAL   A 1 56  ? 9.858  -4.534  14.723 1.00 17.60  ? 62  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 56  ? 10.165 -4.719  16.143 1.00 17.91  ? 62  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 56  ? 11.002 -3.545  16.600 1.00 18.70  ? 62  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 56  ? 11.942 -3.216  15.915 1.00 18.40  ? 62  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 56  ? 10.940 -6.035  16.350 1.00 18.73  ? 62  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 56  ? 11.461 -6.137  17.797 1.00 19.94  ? 62  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 56  ? 10.057 -7.222  16.045 1.00 18.85  ? 62  VAL   A CG2 1 
ATOM   433  N  N   . TYR   A 1 57  ? 10.660 -2.900  17.756 1.00 18.53  ? 63  TYR   A N   1 
ATOM   434  C  CA  . TYR   A 1 57  ? 11.480 -1.772  18.206 1.00 18.21  ? 63  TYR   A CA  1 
ATOM   435  C  C   . TYR   A 1 57  ? 12.064 -2.014  19.577 1.00 17.84  ? 63  TYR   A C   1 
ATOM   436  O  O   . TYR   A 1 57  ? 11.480 -2.739  20.370 1.00 19.38  ? 63  TYR   A O   1 
ATOM   437  C  CB  . TYR   A 1 57  ? 10.720 -0.426  18.144 1.00 17.22  ? 63  TYR   A CB  1 
ATOM   438  C  CG  . TYR   A 1 57  ? 9.796  -0.167  19.321 1.00 18.91  ? 63  TYR   A CG  1 
ATOM   439  C  CD1 . TYR   A 1 57  ? 8.538  -0.763  19.393 1.00 19.90  ? 63  TYR   A CD1 1 
ATOM   440  C  CD2 . TYR   A 1 57  ? 10.163 0.699   20.339 1.00 19.64  ? 63  TYR   A CD2 1 
ATOM   441  C  CE1 . TYR   A 1 57  ? 7.682  -0.523  20.466 1.00 21.72  ? 63  TYR   A CE1 1 
ATOM   442  C  CE2 . TYR   A 1 57  ? 9.305  0.961   21.413 1.00 20.27  ? 63  TYR   A CE2 1 
ATOM   443  C  CZ  . TYR   A 1 57  ? 8.072  0.329   21.484 1.00 22.17  ? 63  TYR   A CZ  1 
ATOM   444  O  OH  . TYR   A 1 57  ? 7.182  0.587   22.508 1.00 23.38  ? 63  TYR   A OH  1 
ATOM   445  N  N   . TYR   A 1 58  ? 13.195 -1.351  19.875 1.00 17.27  ? 64  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 58  ? 13.783 -1.454  21.200 1.00 18.87  ? 64  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 58  ? 13.264 -0.308  22.091 1.00 19.99  ? 64  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 58  ? 13.323 0.864   21.685 1.00 19.81  ? 64  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 58  ? 15.298 -1.418  21.145 1.00 19.01  ? 64  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 58  ? 15.889 -1.561  22.532 1.00 20.59  ? 64  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 58  ? 15.618 -2.679  23.310 1.00 22.15  ? 64  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 58  ? 16.640 -0.537  23.098 1.00 21.75  ? 64  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 58  ? 16.128 -2.803  24.606 1.00 23.51  ? 64  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 58  ? 17.137 -0.639  24.394 1.00 23.69  ? 64  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 58  ? 16.856 -1.764  25.154 1.00 25.22  ? 64  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 58  ? 17.349 -1.900  26.434 1.00 26.37  ? 64  TYR   A OH  1 
ATOM   457  N  N   . CYS   A 1 59  ? 12.785 -0.663  23.325 1.00 20.39  ? 65  CYS   A N   1 
ATOM   458  C  CA  . CYS   A 1 59  ? 12.251 0.296   24.325 1.00 21.37  ? 65  CYS   A CA  1 
ATOM   459  C  C   . CYS   A 1 59  ? 13.180 0.268   25.558 1.00 21.67  ? 65  CYS   A C   1 
ATOM   460  O  O   . CYS   A 1 59  ? 13.068 -0.638  26.391 1.00 22.07  ? 65  CYS   A O   1 
ATOM   461  C  CB  . CYS   A 1 59  ? 10.822 -0.073  24.710 1.00 23.06  ? 65  CYS   A CB  1 
ATOM   462  S  SG  . CYS   A 1 59  ? 10.128 0.965   26.031 1.00 24.52  ? 65  CYS   A SG  1 
ATOM   463  N  N   . SER   A 1 60  ? 14.116 1.223   25.647 1.00 21.02  ? 66  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 60  ? 15.098 1.199   26.734 1.00 23.21  ? 66  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 60  ? 14.455 1.333   28.119 1.00 23.93  ? 66  SER   A C   1 
ATOM   466  O  O   . SER   A 1 60  ? 14.975 0.770   29.076 1.00 25.40  ? 66  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 60  ? 16.142 2.296   26.548 1.00 26.68  ? 66  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 60  ? 15.568 3.571   26.769 1.00 31.13  ? 66  SER   A OG  1 
ATOM   469  N  N   . SER   A 1 61  ? 13.313 2.036   28.215 1.00 22.55  ? 67  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 61  ? 12.600 2.240   29.491 1.00 22.18  ? 67  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 61  ? 11.904 0.969   30.057 1.00 24.18  ? 67  SER   A C   1 
ATOM   472  O  O   . SER   A 1 61  ? 11.405 0.981   31.190 1.00 26.32  ? 67  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 61  ? 11.609 3.391   29.383 1.00 22.46  ? 67  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 61  ? 10.544 3.122   28.488 1.00 23.24  ? 67  SER   A OG  1 
ATOM   475  N  N   . ARG   A 1 62  ? 11.848 -0.097  29.261 1.00 23.34  ? 68  ARG   A N   1 
ATOM   476  C  CA  . ARG   A 1 62  ? 11.323 -1.391  29.694 1.00 23.64  ? 68  ARG   A CA  1 
ATOM   477  C  C   . ARG   A 1 62  ? 12.390 -2.478  29.499 1.00 24.78  ? 68  ARG   A C   1 
ATOM   478  O  O   . ARG   A 1 62  ? 12.099 -3.648  29.761 1.00 25.74  ? 68  ARG   A O   1 
ATOM   479  C  CB  . ARG   A 1 62  ? 10.096 -1.760  28.850 1.00 25.44  ? 68  ARG   A CB  1 
ATOM   480  C  CG  . ARG   A 1 62  ? 8.917  -0.807  29.055 1.00 27.05  ? 68  ARG   A CG  1 
ATOM   481  C  CD  . ARG   A 1 62  ? 8.200  -1.136  30.362 1.00 29.19  ? 68  ARG   A CD  1 
ATOM   482  N  NE  . ARG   A 1 62  ? 7.031  -0.287  30.588 1.00 29.16  ? 68  ARG   A NE  1 
ATOM   483  C  CZ  . ARG   A 1 62  ? 7.066  0.871   31.243 1.00 31.17  ? 68  ARG   A CZ  1 
ATOM   484  N  NH1 . ARG   A 1 62  ? 8.211  1.323   31.752 1.00 30.84  ? 68  ARG   A NH1 1 
ATOM   485  N  NH2 . ARG   A 1 62  ? 5.951  1.573   31.423 1.00 29.53  ? 68  ARG   A NH2 1 
ATOM   486  N  N   . ARG   A 1 63  ? 13.580 -2.150  28.900 1.00 24.81  ? 69  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 63  ? 14.624 -3.147  28.590 1.00 26.05  ? 69  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 63  ? 14.020 -4.296  27.759 1.00 25.53  ? 69  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 63  ? 14.295 -5.470  28.019 1.00 26.89  ? 69  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 63  ? 15.247 -3.701  29.894 1.00 27.41  ? 69  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 63  ? 16.101 -2.690  30.645 1.00 31.89  ? 69  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 63  ? 16.805 -3.333  31.817 1.00 34.86  ? 69  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 63  ? 17.558 -2.354  32.594 1.00 36.81  ? 69  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 63  ? 17.488 -2.228  33.920 1.00 38.63  ? 69  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 63  ? 16.704 -3.033  34.632 1.00 37.18  ? 69  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 63  ? 18.199 -1.294  34.541 1.00 37.84  ? 69  ARG   A NH2 1 
ATOM   497  N  N   . LYS   A 1 64  ? 13.136 -3.937  26.791 1.00 24.96  ? 70  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 64  ? 12.453 -4.939  25.998 1.00 25.09  ? 70  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 64  ? 12.261 -4.516  24.535 1.00 23.55  ? 70  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 64  ? 12.108 -3.324  24.236 1.00 24.24  ? 70  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 64  ? 11.065 -5.182  26.605 1.00 28.58  ? 70  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 64  ? 10.452 -6.516  26.259 1.00 37.65  ? 70  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 64  ? 9.121  -6.715  26.963 1.00 46.03  ? 70  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 64  ? 9.262  -7.185  28.387 1.00 52.18  ? 70  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 64  ? 7.941  -7.213  29.085 1.00 55.62  ? 70  LYS   A NZ  1 
ATOM   506  N  N   . HIS   A 1 65  ? 12.232 -5.499  23.643 1.00 21.85  ? 71  HIS   A N   1 
ATOM   507  C  CA  . HIS   A 1 65  ? 11.922 -5.290  22.233 1.00 21.30  ? 71  HIS   A CA  1 
ATOM   508  C  C   . HIS   A 1 65  ? 10.428 -5.614  22.092 1.00 22.57  ? 71  HIS   A C   1 
ATOM   509  O  O   . HIS   A 1 65  ? 9.935  -6.583  22.716 1.00 24.90  ? 71  HIS   A O   1 
ATOM   510  C  CB  . HIS   A 1 65  ? 12.785 -6.229  21.333 1.00 21.13  ? 71  HIS   A CB  1 
ATOM   511  C  CG  . HIS   A 1 65  ? 14.258 -5.973  21.452 1.00 20.97  ? 71  HIS   A CG  1 
ATOM   512  N  ND1 . HIS   A 1 65  ? 14.935 -5.196  20.518 1.00 21.88  ? 71  HIS   A ND1 1 
ATOM   513  C  CD2 . HIS   A 1 65  ? 15.123 -6.334  22.429 1.00 21.82  ? 71  HIS   A CD2 1 
ATOM   514  C  CE1 . HIS   A 1 65  ? 16.193 -5.141  20.938 1.00 22.51  ? 71  HIS   A CE1 1 
ATOM   515  N  NE2 . HIS   A 1 65  ? 16.351 -5.783  22.093 1.00 23.78  ? 71  HIS   A NE2 1 
ATOM   516  N  N   . TYR   A 1 66  ? 9.682  -4.812  21.327 1.00 21.14  ? 72  TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 66  ? 8.256  -5.096  21.118 1.00 21.42  ? 72  TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 66  ? 7.895  -5.175  19.639 1.00 21.34  ? 72  TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 66  ? 8.244  -4.278  18.885 1.00 19.31  ? 72  TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 66  ? 7.378  -3.992  21.719 1.00 21.57  ? 72  TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 66  ? 7.441  -3.886  23.222 1.00 22.49  ? 72  TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 66  ? 6.665  -4.710  24.027 1.00 24.01  ? 72  TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 66  ? 8.222  -2.917  23.837 1.00 23.18  ? 72  TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 66  ? 6.651  -4.562  25.417 1.00 24.94  ? 72  TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 66  ? 8.213  -2.753  25.224 1.00 24.18  ? 72  TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 66  ? 7.435  -3.589  26.012 1.00 26.34  ? 72  TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 66  ? 7.417  -3.467  27.396 1.00 28.98  ? 72  TYR   A OH  1 
ATOM   528  N  N   . PRO   A 1 67  ? 7.097  -6.169  19.248 1.00 21.83  ? 73  PRO   A N   1 
ATOM   529  C  CA  . PRO   A 1 67  ? 6.565  -6.200  17.866 1.00 22.12  ? 73  PRO   A CA  1 
ATOM   530  C  C   . PRO   A 1 67  ? 5.472  -5.119  17.700 1.00 24.71  ? 73  PRO   A C   1 
ATOM   531  O  O   . PRO   A 1 67  ? 4.630  -4.952  18.587 1.00 26.86  ? 73  PRO   A O   1 
ATOM   532  C  CB  . PRO   A 1 67  ? 5.949  -7.601  17.770 1.00 22.75  ? 73  PRO   A CB  1 
ATOM   533  C  CG  . PRO   A 1 67  ? 5.540  -7.923  19.181 1.00 23.07  ? 73  PRO   A CG  1 
ATOM   534  C  CD  . PRO   A 1 67  ? 6.582  -7.291  20.072 1.00 21.41  ? 73  PRO   A CD  1 
ATOM   535  N  N   . VAL   A 1 68  ? 5.513  -4.342  16.602 1.00 23.54  ? 74  VAL   A N   1 
ATOM   536  C  CA  . VAL   A 1 68  ? 4.522  -3.284  16.387 1.00 23.98  ? 74  VAL   A CA  1 
ATOM   537  C  C   . VAL   A 1 68  ? 4.108  -3.159  14.944 1.00 22.78  ? 74  VAL   A C   1 
ATOM   538  O  O   . VAL   A 1 68  ? 4.888  -3.488  14.036 1.00 21.17  ? 74  VAL   A O   1 
ATOM   539  C  CB  . VAL   A 1 68  ? 5.067  -1.897  16.830 1.00 26.35  ? 74  VAL   A CB  1 
ATOM   540  C  CG1 . VAL   A 1 68  ? 5.016  -1.718  18.336 1.00 27.08  ? 74  VAL   A CG1 1 
ATOM   541  C  CG2 . VAL   A 1 68  ? 6.460  -1.606  16.255 1.00 26.10  ? 74  VAL   A CG2 1 
ATOM   542  N  N   . SER   A 1 69  ? 2.863  -2.653  14.741 1.00 21.58  ? 75  SER   A N   1 
ATOM   543  C  CA  . SER   A 1 69  ? 2.365  -2.185  13.456 1.00 22.10  ? 75  SER   A CA  1 
ATOM   544  C  C   . SER   A 1 69  ? 2.611  -0.662  13.503 1.00 20.72  ? 75  SER   A C   1 
ATOM   545  O  O   . SER   A 1 69  ? 2.392  -0.032  14.545 1.00 21.01  ? 75  SER   A O   1 
ATOM   546  C  CB  . SER   A 1 69  ? 0.876  -2.443  13.308 1.00 26.43  ? 75  SER   A CB  1 
ATOM   547  O  OG  . SER   A 1 69  ? 0.661  -3.838  13.394 1.00 34.53  ? 75  SER   A OG  1 
ATOM   548  N  N   . PHE   A 1 70  ? 3.001  -0.063  12.386 1.00 19.20  ? 76  PHE   A N   1 
ATOM   549  C  CA  . PHE   A 1 70  ? 3.265  1.387   12.367 1.00 17.87  ? 76  PHE   A CA  1 
ATOM   550  C  C   . PHE   A 1 70  ? 2.743  2.040   11.099 1.00 19.56  ? 76  PHE   A C   1 
ATOM   551  O  O   . PHE   A 1 70  ? 2.679  1.394   10.053 1.00 20.37  ? 76  PHE   A O   1 
ATOM   552  C  CB  . PHE   A 1 70  ? 4.760  1.704   12.645 1.00 17.02  ? 76  PHE   A CB  1 
ATOM   553  C  CG  . PHE   A 1 70  ? 5.753  0.986   11.745 1.00 16.15  ? 76  PHE   A CG  1 
ATOM   554  C  CD1 . PHE   A 1 70  ? 6.255  -0.267  12.093 1.00 16.33  ? 76  PHE   A CD1 1 
ATOM   555  C  CD2 . PHE   A 1 70  ? 6.168  1.553   10.538 1.00 16.70  ? 76  PHE   A CD2 1 
ATOM   556  C  CE1 . PHE   A 1 70  ? 7.116  -0.952  11.230 1.00 17.12  ? 76  PHE   A CE1 1 
ATOM   557  C  CE2 . PHE   A 1 70  ? 7.051  0.874   9.704  1.00 17.45  ? 76  PHE   A CE2 1 
ATOM   558  C  CZ  . PHE   A 1 70  ? 7.518  -0.362  10.046 1.00 16.40  ? 76  PHE   A CZ  1 
ATOM   559  N  N   . SER   A 1 71  ? 2.357  3.340   11.196 1.00 19.13  ? 77  SER   A N   1 
ATOM   560  C  CA  . SER   A 1 71  ? 1.807  4.089   10.087 1.00 19.95  ? 77  SER   A CA  1 
ATOM   561  C  C   . SER   A 1 71  ? 2.884  4.465   9.038  1.00 20.35  ? 77  SER   A C   1 
ATOM   562  O  O   . SER   A 1 71  ? 4.079  4.347   9.321  1.00 20.61  ? 77  SER   A O   1 
ATOM   563  C  CB  . SER   A 1 71  ? 1.105  5.348   10.626 1.00 21.07  ? 77  SER   A CB  1 
ATOM   564  O  OG  . SER   A 1 71  ? 2.049  6.219   11.247 1.00 21.95  ? 77  SER   A OG  1 
ATOM   565  N  N   . LYS   A 1 72  ? 2.479  4.866   7.819  1.00 20.90  ? 78  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 72  ? 3.461  5.263   6.803  1.00 22.71  ? 78  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 72  ? 4.122  6.622   7.144  1.00 22.20  ? 78  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 72  ? 3.490  7.460   7.762  1.00 23.06  ? 78  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 72  ? 2.808  5.328   5.391  1.00 26.69  ? 78  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 72  ? 2.690  3.936   4.774  1.00 32.14  ? 78  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 72  ? 2.212  3.919   3.322  1.00 37.39  ? 78  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 72  ? 2.574  2.569   2.719  1.00 41.65  ? 78  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 72  ? 1.663  2.158   1.611  1.00 44.27  ? 78  LYS   A NZ  1 
ATOM   574  N  N   . PRO   A 1 73  ? 5.364  6.883   6.692  1.00 22.85  ? 79  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 73  ? 6.022  8.183   7.010  1.00 23.10  ? 79  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 73  ? 5.184  9.378   6.573  1.00 23.12  ? 79  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 73  ? 4.708  9.439   5.426  1.00 23.64  ? 79  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 73  ? 7.359  8.098   6.277  1.00 24.30  ? 79  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 73  ? 7.622  6.597   6.175  1.00 25.94  ? 79  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 73  ? 6.262  5.998   5.920  1.00 23.03  ? 79  PRO   A CD  1 
ATOM   581  N  N   A SER   A 1 74  ? 4.921  10.297  7.510  0.50 22.57  ? 80  SER   A N   1 
ATOM   582  N  N   B SER   A 1 74  ? 4.940  10.306  7.504  0.50 22.43  ? 80  SER   A N   1 
ATOM   583  C  CA  A SER   A 1 74  ? 4.007  11.412  7.243  0.50 23.77  ? 80  SER   A CA  1 
ATOM   584  C  CA  B SER   A 1 74  ? 4.051  11.430  7.227  0.50 23.54  ? 80  SER   A CA  1 
ATOM   585  C  C   A SER   A 1 74  ? 4.377  12.659  8.071  0.50 24.30  ? 80  SER   A C   1 
ATOM   586  C  C   B SER   A 1 74  ? 4.369  12.662  8.089  0.50 24.23  ? 80  SER   A C   1 
ATOM   587  O  O   A SER   A 1 74  ? 5.282  12.599  8.904  0.50 24.28  ? 80  SER   A O   1 
ATOM   588  O  O   B SER   A 1 74  ? 5.252  12.601  8.946  0.50 24.26  ? 80  SER   A O   1 
ATOM   589  C  CB  A SER   A 1 74  ? 2.562  11.009  7.574  0.50 26.44  ? 80  SER   A CB  1 
ATOM   590  C  CB  B SER   A 1 74  ? 2.600  10.991  7.419  0.50 25.87  ? 80  SER   A CB  1 
ATOM   591  O  OG  A SER   A 1 74  ? 2.309  9.616   7.642  0.50 30.15  ? 80  SER   A OG  1 
ATOM   592  O  OG  B SER   A 1 74  ? 2.199  10.174  6.334  0.50 29.04  ? 80  SER   A OG  1 
ATOM   593  N  N   . LEU   A 1 75  ? 3.679  13.790  7.831  1.00 24.91  ? 81  LEU   A N   1 
ATOM   594  C  CA  . LEU   A 1 75  ? 3.875  15.048  8.559  1.00 26.68  ? 81  LEU   A CA  1 
ATOM   595  C  C   . LEU   A 1 75  ? 2.910  14.960  9.760  1.00 27.35  ? 81  LEU   A C   1 
ATOM   596  O  O   . LEU   A 1 75  ? 1.695  14.877  9.563  1.00 27.39  ? 81  LEU   A O   1 
ATOM   597  C  CB  . LEU   A 1 75  ? 3.443  16.184  7.597  1.00 27.77  ? 81  LEU   A CB  1 
ATOM   598  C  CG  . LEU   A 1 75  ? 3.936  17.622  7.794  1.00 31.67  ? 81  LEU   A CG  1 
ATOM   599  C  CD1 . LEU   A 1 75  ? 5.436  17.709  7.819  1.00 32.51  ? 81  LEU   A CD1 1 
ATOM   600  C  CD2 . LEU   A 1 75  ? 3.417  18.511  6.657  1.00 32.02  ? 81  LEU   A CD2 1 
ATOM   601  N  N   . ILE   A 1 76  ? 3.444  14.904  10.992 1.00 27.26  ? 82  ILE   A N   1 
ATOM   602  C  CA  . ILE   A 1 76  ? 2.662  14.703  12.204 1.00 28.45  ? 82  ILE   A CA  1 
ATOM   603  C  C   . ILE   A 1 76  ? 2.969  15.797  13.203 1.00 28.85  ? 82  ILE   A C   1 
ATOM   604  O  O   . ILE   A 1 76  ? 4.146  16.093  13.422 1.00 28.48  ? 82  ILE   A O   1 
ATOM   605  C  CB  . ILE   A 1 76  ? 3.088  13.342  12.821 1.00 29.95  ? 82  ILE   A CB  1 
ATOM   606  C  CG1 . ILE   A 1 76  ? 2.816  12.149  11.880 1.00 31.03  ? 82  ILE   A CG1 1 
ATOM   607  C  CG2 . ILE   A 1 76  ? 2.478  13.129  14.212 1.00 30.72  ? 82  ILE   A CG2 1 
ATOM   608  C  CD1 . ILE   A 1 76  ? 1.435  11.904  11.645 1.00 32.47  ? 82  ILE   A CD1 1 
ATOM   609  N  N   . PHE   A 1 77  ? 1.930  16.321  13.885 1.00 29.39  ? 83  PHE   A N   1 
ATOM   610  C  CA  . PHE   A 1 77  ? 2.100  17.366  14.878 1.00 30.00  ? 83  PHE   A CA  1 
ATOM   611  C  C   . PHE   A 1 77  ? 2.750  16.835  16.123 1.00 28.67  ? 83  PHE   A C   1 
ATOM   612  O  O   . PHE   A 1 77  ? 2.296  15.840  16.695 1.00 29.36  ? 83  PHE   A O   1 
ATOM   613  C  CB  . PHE   A 1 77  ? 0.754  17.996  15.258 1.00 32.20  ? 83  PHE   A CB  1 
ATOM   614  C  CG  . PHE   A 1 77  ? 0.950  19.242  16.092 1.00 35.12  ? 83  PHE   A CG  1 
ATOM   615  C  CD1 . PHE   A 1 77  ? 1.328  20.434  15.504 1.00 36.36  ? 83  PHE   A CD1 1 
ATOM   616  C  CD2 . PHE   A 1 77  ? 0.774  19.213  17.462 1.00 36.83  ? 83  PHE   A CD2 1 
ATOM   617  C  CE1 . PHE   A 1 77  ? 1.496  21.584  16.267 1.00 38.01  ? 83  PHE   A CE1 1 
ATOM   618  C  CE2 . PHE   A 1 77  ? 0.962  20.360  18.225 1.00 38.18  ? 83  PHE   A CE2 1 
ATOM   619  C  CZ  . PHE   A 1 77  ? 1.315  21.538  17.621 1.00 38.01  ? 83  PHE   A CZ  1 
ATOM   620  N  N   . VAL   A 1 78  ? 3.819  17.497  16.565 1.00 26.96  ? 84  VAL   A N   1 
ATOM   621  C  CA  . VAL   A 1 78  ? 4.511  17.079  17.781 1.00 26.31  ? 84  VAL   A CA  1 
ATOM   622  C  C   . VAL   A 1 78  ? 4.483  18.233  18.785 1.00 26.94  ? 84  VAL   A C   1 
ATOM   623  O  O   . VAL   A 1 78  ? 4.882  19.352  18.434 1.00 27.35  ? 84  VAL   A O   1 
ATOM   624  C  CB  . VAL   A 1 78  ? 5.946  16.637  17.468 1.00 25.03  ? 84  VAL   A CB  1 
ATOM   625  C  CG1 . VAL   A 1 78  ? 6.690  16.273  18.758 1.00 25.19  ? 84  VAL   A CG1 1 
ATOM   626  C  CG2 . VAL   A 1 78  ? 5.960  15.468  16.480 1.00 25.07  ? 84  VAL   A CG2 1 
ATOM   627  N  N   . GLU   A 1 79  ? 4.034  17.965  20.014 1.00 27.57  ? 85  GLU   A N   1 
ATOM   628  C  CA  . GLU   A 1 79  ? 3.942  18.988  21.063 1.00 28.59  ? 85  GLU   A CA  1 
ATOM   629  C  C   . GLU   A 1 79  ? 5.300  19.614  21.403 1.00 28.17  ? 85  GLU   A C   1 
ATOM   630  O  O   . GLU   A 1 79  ? 6.345  18.995  21.213 1.00 26.59  ? 85  GLU   A O   1 
ATOM   631  C  CB  . GLU   A 1 79  ? 3.302  18.414  22.335 1.00 31.22  ? 85  GLU   A CB  1 
ATOM   632  C  CG  . GLU   A 1 79  ? 1.898  17.890  22.104 1.00 39.47  ? 85  GLU   A CG  1 
ATOM   633  C  CD  . GLU   A 1 79  ? 1.025  17.887  23.341 1.00 50.89  ? 85  GLU   A CD  1 
ATOM   634  O  OE1 . GLU   A 1 79  ? 1.074  18.881  24.103 1.00 55.31  ? 85  GLU   A OE1 1 
ATOM   635  O  OE2 . GLU   A 1 79  ? 0.275  16.902  23.536 1.00 53.38  ? 85  GLU   A OE2 1 
ATOM   636  N  N   . ALA   A 1 80  ? 5.275  20.845  21.922 1.00 28.90  ? 86  ALA   A N   1 
ATOM   637  C  CA  . ALA   A 1 80  ? 6.498  21.513  22.337 1.00 29.57  ? 86  ALA   A CA  1 
ATOM   638  C  C   . ALA   A 1 80  ? 7.218  20.736  23.436 1.00 29.03  ? 86  ALA   A C   1 
ATOM   639  O  O   . ALA   A 1 80  ? 6.596  20.047  24.264 1.00 30.38  ? 86  ALA   A O   1 
ATOM   640  C  CB  . ALA   A 1 80  ? 6.205  22.932  22.792 1.00 30.27  ? 86  ALA   A CB  1 
ATOM   641  N  N   . SER   A 1 81  ? 8.543  20.788  23.384 1.00 27.21  ? 87  SER   A N   1 
ATOM   642  C  CA  . SER   A 1 81  ? 9.409  20.157  24.379 1.00 26.71  ? 87  SER   A CA  1 
ATOM   643  C  C   . SER   A 1 81  ? 10.613 21.118  24.596 1.00 26.84  ? 87  SER   A C   1 
ATOM   644  O  O   . SER   A 1 81  ? 10.636 22.229  24.066 1.00 27.15  ? 87  SER   A O   1 
ATOM   645  C  CB  . SER   A 1 81  ? 9.899  18.795  23.869 1.00 27.09  ? 87  SER   A CB  1 
ATOM   646  O  OG  . SER   A 1 81  ? 10.902 18.955  22.870 1.00 27.06  ? 87  SER   A OG  1 
ATOM   647  N  N   . GLU   A 1 82  ? 11.596 20.686  25.387 1.00 27.34  ? 88  GLU   A N   1 
ATOM   648  C  CA  . GLU   A 1 82  ? 12.798 21.485  25.612 1.00 28.45  ? 88  GLU   A CA  1 
ATOM   649  C  C   . GLU   A 1 82  ? 13.707 21.494  24.373 1.00 27.81  ? 88  GLU   A C   1 
ATOM   650  O  O   . GLU   A 1 82  ? 14.624 22.303  24.341 1.00 28.10  ? 88  GLU   A O   1 
ATOM   651  C  CB  . GLU   A 1 82  ? 13.597 20.965  26.810 1.00 33.03  ? 88  GLU   A CB  1 
ATOM   652  C  CG  . GLU   A 1 82  ? 12.734 20.368  27.909 1.00 42.92  ? 88  GLU   A CG  1 
ATOM   653  C  CD  . GLU   A 1 82  ? 12.532 18.873  27.718 1.00 52.87  ? 88  GLU   A CD  1 
ATOM   654  O  OE1 . GLU   A 1 82  ? 11.468 18.470  27.188 1.00 51.66  ? 88  GLU   A OE1 1 
ATOM   655  O  OE2 . GLU   A 1 82  ? 13.458 18.108  28.081 1.00 57.59  ? 88  GLU   A OE2 1 
ATOM   656  N  N   . TYR   A 1 83  ? 13.466 20.598  23.374 1.00 26.12  ? 89  TYR   A N   1 
ATOM   657  C  CA  . TYR   A 1 83  ? 14.272 20.490  22.165 1.00 25.19  ? 89  TYR   A CA  1 
ATOM   658  C  C   . TYR   A 1 83  ? 13.703 21.192  20.962 1.00 24.66  ? 89  TYR   A C   1 
ATOM   659  O  O   . TYR   A 1 83  ? 14.471 21.725  20.161 1.00 24.85  ? 89  TYR   A O   1 
ATOM   660  C  CB  . TYR   A 1 83  ? 14.546 19.027  21.840 1.00 25.00  ? 89  TYR   A CB  1 
ATOM   661  C  CG  . TYR   A 1 83  ? 15.235 18.336  22.992 1.00 26.44  ? 89  TYR   A CG  1 
ATOM   662  C  CD1 . TYR   A 1 83  ? 16.570 18.587  23.282 1.00 27.01  ? 89  TYR   A CD1 1 
ATOM   663  C  CD2 . TYR   A 1 83  ? 14.536 17.475  23.832 1.00 28.64  ? 89  TYR   A CD2 1 
ATOM   664  C  CE1 . TYR   A 1 83  ? 17.204 17.962  24.350 1.00 28.30  ? 89  TYR   A CE1 1 
ATOM   665  C  CE2 . TYR   A 1 83  ? 15.170 16.811  24.871 1.00 29.49  ? 89  TYR   A CE2 1 
ATOM   666  C  CZ  . TYR   A 1 83  ? 16.501 17.066  25.137 1.00 30.60  ? 89  TYR   A CZ  1 
ATOM   667  O  OH  . TYR   A 1 83  ? 17.127 16.391  26.160 1.00 33.76  ? 89  TYR   A OH  1 
ATOM   668  N  N   . TYR   A 1 84  ? 12.372 21.203  20.827 1.00 24.72  ? 90  TYR   A N   1 
ATOM   669  C  CA  . TYR   A 1 84  ? 11.722 21.899  19.721 1.00 24.76  ? 90  TYR   A CA  1 
ATOM   670  C  C   . TYR   A 1 84  ? 10.464 22.630  20.192 1.00 26.30  ? 90  TYR   A C   1 
ATOM   671  O  O   . TYR   A 1 84  ? 9.736  22.139  21.079 1.00 26.68  ? 90  TYR   A O   1 
ATOM   672  C  CB  . TYR   A 1 84  ? 11.288 20.914  18.607 1.00 23.24  ? 90  TYR   A CB  1 
ATOM   673  C  CG  . TYR   A 1 84  ? 12.405 20.083  18.016 1.00 21.71  ? 90  TYR   A CG  1 
ATOM   674  C  CD1 . TYR   A 1 84  ? 13.231 20.594  17.017 1.00 21.82  ? 90  TYR   A CD1 1 
ATOM   675  C  CD2 . TYR   A 1 84  ? 12.631 18.784  18.447 1.00 21.17  ? 90  TYR   A CD2 1 
ATOM   676  C  CE1 . TYR   A 1 84  ? 14.245 19.818  16.455 1.00 21.37  ? 90  TYR   A CE1 1 
ATOM   677  C  CE2 . TYR   A 1 84  ? 13.650 18.001  17.896 1.00 20.47  ? 90  TYR   A CE2 1 
ATOM   678  C  CZ  . TYR   A 1 84  ? 14.420 18.507  16.865 1.00 21.01  ? 90  TYR   A CZ  1 
ATOM   679  O  OH  . TYR   A 1 84  ? 15.455 17.762  16.353 1.00 21.56  ? 90  TYR   A OH  1 
ATOM   680  N  N   . PRO   A 1 85  ? 10.096 23.711  19.491 1.00 27.61  ? 91  PRO   A N   1 
ATOM   681  C  CA  . PRO   A 1 85  ? 8.763  24.285  19.712 1.00 28.68  ? 91  PRO   A CA  1 
ATOM   682  C  C   . PRO   A 1 85  ? 7.706  23.372  19.042 1.00 29.54  ? 91  PRO   A C   1 
ATOM   683  O  O   . PRO   A 1 85  ? 8.042  22.428  18.292 1.00 29.72  ? 91  PRO   A O   1 
ATOM   684  C  CB  . PRO   A 1 85  ? 8.847  25.639  19.001 1.00 29.79  ? 91  PRO   A CB  1 
ATOM   685  C  CG  . PRO   A 1 85  ? 9.769  25.379  17.840 1.00 30.73  ? 91  PRO   A CG  1 
ATOM   686  C  CD  . PRO   A 1 85  ? 10.804 24.384  18.373 1.00 28.65  ? 91  PRO   A CD  1 
ATOM   687  N  N   . ALA   A 1 86  ? 6.416  23.651  19.283 1.00 30.30  ? 92  ALA   A N   1 
ATOM   688  C  CA  . ALA   A 1 86  ? 5.310  22.914  18.664 1.00 31.25  ? 92  ALA   A CA  1 
ATOM   689  C  C   . ALA   A 1 86  ? 5.425  23.021  17.145 1.00 31.10  ? 92  ALA   A C   1 
ATOM   690  O  O   . ALA   A 1 86  ? 5.626  24.120  16.627 1.00 30.86  ? 92  ALA   A O   1 
ATOM   691  C  CB  . ALA   A 1 86  ? 3.987  23.491  19.117 1.00 31.89  ? 92  ALA   A CB  1 
ATOM   692  N  N   . ARG   A 1 87  ? 5.482  21.858  16.448 1.00 29.79  ? 93  ARG   A N   1 
ATOM   693  C  CA  . ARG   A 1 87  ? 5.688  21.889  15.001 1.00 28.89  ? 93  ARG   A CA  1 
ATOM   694  C  C   . ARG   A 1 87  ? 5.223  20.576  14.335 1.00 29.36  ? 93  ARG   A C   1 
ATOM   695  O  O   . ARG   A 1 87  ? 4.877  19.628  15.036 1.00 29.32  ? 93  ARG   A O   1 
ATOM   696  C  CB  . ARG   A 1 87  ? 7.193  22.117  14.718 1.00 30.25  ? 93  ARG   A CB  1 
ATOM   697  C  CG  . ARG   A 1 87  ? 8.036  20.814  14.745 1.00 32.15  ? 93  ARG   A CG  1 
ATOM   698  C  CD  . ARG   A 1 87  ? 9.347  20.915  15.477 1.00 31.54  ? 93  ARG   A CD  1 
ATOM   699  N  NE  . ARG   A 1 87  ? 10.325 19.954  14.967 1.00 29.16  ? 93  ARG   A NE  1 
ATOM   700  C  CZ  . ARG   A 1 87  ? 10.455 18.705  15.400 1.00 29.61  ? 93  ARG   A CZ  1 
ATOM   701  N  NH1 . ARG   A 1 87  ? 9.661  18.239  16.376 1.00 27.05  ? 93  ARG   A NH1 1 
ATOM   702  N  NH2 . ARG   A 1 87  ? 11.406 17.916  14.895 1.00 24.50  ? 93  ARG   A NH2 1 
ATOM   703  N  N   . TYR   A 1 88  ? 5.252  20.519  12.983 1.00 29.58  ? 94  TYR   A N   1 
ATOM   704  C  CA  . TYR   A 1 88  ? 4.987  19.258  12.305 1.00 30.37  ? 94  TYR   A CA  1 
ATOM   705  C  C   . TYR   A 1 88  ? 6.327  18.645  12.034 1.00 27.39  ? 94  TYR   A C   1 
ATOM   706  O  O   . TYR   A 1 88  ? 7.197  19.286  11.428 1.00 28.03  ? 94  TYR   A O   1 
ATOM   707  C  CB  . TYR   A 1 88  ? 4.312  19.450  10.959 1.00 32.89  ? 94  TYR   A CB  1 
ATOM   708  C  CG  . TYR   A 1 88  ? 2.876  19.871  11.070 1.00 36.48  ? 94  TYR   A CG  1 
ATOM   709  C  CD1 . TYR   A 1 88  ? 1.872  18.936  11.276 1.00 38.41  ? 94  TYR   A CD1 1 
ATOM   710  C  CD2 . TYR   A 1 88  ? 2.507  21.195  10.884 1.00 38.83  ? 94  TYR   A CD2 1 
ATOM   711  C  CE1 . TYR   A 1 88  ? 0.537  19.311  11.318 1.00 40.50  ? 94  TYR   A CE1 1 
ATOM   712  C  CE2 . TYR   A 1 88  ? 1.177  21.584  10.943 1.00 40.67  ? 94  TYR   A CE2 1 
ATOM   713  C  CZ  . TYR   A 1 88  ? 0.195  20.639  11.162 1.00 42.12  ? 94  TYR   A CZ  1 
ATOM   714  O  OH  . TYR   A 1 88  ? -1.119 21.032  11.205 1.00 45.30  ? 94  TYR   A OH  1 
ATOM   715  N  N   . GLN   A 1 89  ? 6.512  17.407  12.490 1.00 24.49  ? 95  GLN   A N   1 
ATOM   716  C  CA  . GLN   A 1 89  ? 7.752  16.692  12.191 1.00 23.76  ? 95  GLN   A CA  1 
ATOM   717  C  C   . GLN   A 1 89  ? 7.455  15.833  10.962 1.00 23.03  ? 95  GLN   A C   1 
ATOM   718  O  O   . GLN   A 1 89  ? 6.436  15.148  10.947 1.00 22.66  ? 95  GLN   A O   1 
ATOM   719  C  CB  . GLN   A 1 89  ? 8.200  15.846  13.384 1.00 24.76  ? 95  GLN   A CB  1 
ATOM   720  C  CG  . GLN   A 1 89  ? 9.448  15.011  13.087 1.00 25.37  ? 95  GLN   A CG  1 
ATOM   721  C  CD  . GLN   A 1 89  ? 10.123 14.501  14.350 1.00 24.39  ? 95  GLN   A CD  1 
ATOM   722  O  OE1 . GLN   A 1 89  ? 10.251 15.219  15.348 1.00 23.24  ? 95  GLN   A OE1 1 
ATOM   723  N  NE2 . GLN   A 1 89  ? 10.637 13.275  14.299 1.00 23.67  ? 95  GLN   A NE2 1 
ATOM   724  N  N   . SER   A 1 90  ? 8.307  15.883  9.925  1.00 22.22  ? 96  SER   A N   1 
ATOM   725  C  CA  . SER   A 1 90  ? 8.058  15.091  8.716  1.00 22.12  ? 96  SER   A CA  1 
ATOM   726  C  C   . SER   A 1 90  ? 8.719  13.699  8.785  1.00 20.55  ? 96  SER   A C   1 
ATOM   727  O  O   . SER   A 1 90  ? 9.612  13.486  9.614  1.00 20.24  ? 96  SER   A O   1 
ATOM   728  C  CB  . SER   A 1 90  ? 8.571  15.841  7.485  1.00 23.40  ? 96  SER   A CB  1 
ATOM   729  O  OG  . SER   A 1 90  ? 9.958  16.084  7.654  1.00 24.58  ? 96  SER   A OG  1 
ATOM   730  N  N   . HIS   A 1 91  ? 8.297  12.778  7.883  1.00 19.80  ? 97  HIS   A N   1 
ATOM   731  C  CA  . HIS   A 1 91  ? 8.833  11.411  7.754  1.00 19.88  ? 97  HIS   A CA  1 
ATOM   732  C  C   . HIS   A 1 91  ? 8.693  10.609  9.059  1.00 19.63  ? 97  HIS   A C   1 
ATOM   733  O  O   . HIS   A 1 91  ? 9.545  9.760   9.350  1.00 20.33  ? 97  HIS   A O   1 
ATOM   734  C  CB  . HIS   A 1 91  ? 10.294 11.458  7.276  1.00 20.36  ? 97  HIS   A CB  1 
ATOM   735  C  CG  . HIS   A 1 91  ? 10.440 12.109  5.929  1.00 22.88  ? 97  HIS   A CG  1 
ATOM   736  N  ND1 . HIS   A 1 91  ? 10.487 11.359  4.773  1.00 25.60  ? 97  HIS   A ND1 1 
ATOM   737  C  CD2 . HIS   A 1 91  ? 10.534 13.428  5.605  1.00 24.88  ? 97  HIS   A CD2 1 
ATOM   738  C  CE1 . HIS   A 1 91  ? 10.639 12.237  3.780  1.00 26.47  ? 97  HIS   A CE1 1 
ATOM   739  N  NE2 . HIS   A 1 91  ? 10.669 13.496  4.234  1.00 26.43  ? 97  HIS   A NE2 1 
ATOM   740  N  N   . LEU   A 1 92  ? 7.644  10.921  9.837  1.00 17.72  ? 98  LEU   A N   1 
ATOM   741  C  CA  . LEU   A 1 92  ? 7.396  10.294  11.126 1.00 18.33  ? 98  LEU   A CA  1 
ATOM   742  C  C   . LEU   A 1 92  ? 6.348  9.193   10.977 1.00 18.10  ? 98  LEU   A C   1 
ATOM   743  O  O   . LEU   A 1 92  ? 5.358  9.359   10.219 1.00 19.48  ? 98  LEU   A O   1 
ATOM   744  C  CB  . LEU   A 1 92  ? 6.918  11.381  12.129 1.00 19.05  ? 98  LEU   A CB  1 
ATOM   745  C  CG  . LEU   A 1 92  ? 6.834  10.940  13.600 1.00 20.79  ? 98  LEU   A CG  1 
ATOM   746  C  CD1 . LEU   A 1 92  ? 8.202  10.573  14.146 1.00 21.96  ? 98  LEU   A CD1 1 
ATOM   747  C  CD2 . LEU   A 1 92  ? 6.239  12.062  14.473 1.00 21.49  ? 98  LEU   A CD2 1 
ATOM   748  N  N   . MET   A 1 93  ? 6.549  8.088   11.719 1.00 17.82  ? 99  MET   A N   1 
ATOM   749  C  CA  . MET   A 1 93  ? 5.663  6.926   11.747 1.00 17.19  ? 99  MET   A CA  1 
ATOM   750  C  C   . MET   A 1 93  ? 5.219  6.666   13.171 1.00 18.99  ? 99  MET   A C   1 
ATOM   751  O  O   . MET   A 1 93  ? 6.044  6.723   14.072 1.00 19.65  ? 99  MET   A O   1 
ATOM   752  C  CB  . MET   A 1 93  ? 6.446  5.705   11.227 1.00 17.37  ? 99  MET   A CB  1 
ATOM   753  C  CG  . MET   A 1 93  ? 6.936  5.921   9.774  1.00 17.49  ? 99  MET   A CG  1 
ATOM   754  S  SD  . MET   A 1 93  ? 7.928  4.538   9.214  1.00 21.39  ? 99  MET   A SD  1 
ATOM   755  C  CE  . MET   A 1 93  ? 9.350  4.686   10.172 1.00 19.94  ? 99  MET   A CE  1 
ATOM   756  N  N   . LEU   A 1 94  ? 3.922  6.452   13.391 1.00 19.72  ? 100 LEU   A N   1 
ATOM   757  C  CA  . LEU   A 1 94  ? 3.429  6.194   14.743 1.00 18.74  ? 100 LEU   A CA  1 
ATOM   758  C  C   . LEU   A 1 94  ? 3.026  4.749   14.941 1.00 19.27  ? 100 LEU   A C   1 
ATOM   759  O  O   . LEU   A 1 94  ? 2.544  4.091   14.008 1.00 19.74  ? 100 LEU   A O   1 
ATOM   760  C  CB  . LEU   A 1 94  ? 2.201  7.085   15.123 1.00 20.06  ? 100 LEU   A CB  1 
ATOM   761  C  CG  . LEU   A 1 94  ? 2.416  8.582   15.101 1.00 23.38  ? 100 LEU   A CG  1 
ATOM   762  C  CD1 . LEU   A 1 94  ? 1.152  9.315   15.614 1.00 24.64  ? 100 LEU   A CD1 1 
ATOM   763  C  CD2 . LEU   A 1 94  ? 3.600  8.960   15.991 1.00 25.35  ? 100 LEU   A CD2 1 
ATOM   764  N  N   . ALA   A 1 95  ? 3.192  4.276   16.173 1.00 18.29  ? 101 ALA   A N   1 
ATOM   765  C  CA  . ALA   A 1 95  ? 2.747  2.949   16.637 1.00 17.98  ? 101 ALA   A CA  1 
ATOM   766  C  C   . ALA   A 1 95  ? 2.118  3.099   18.050 1.00 19.52  ? 101 ALA   A C   1 
ATOM   767  O  O   . ALA   A 1 95  ? 2.410  4.060   18.760 1.00 19.42  ? 101 ALA   A O   1 
ATOM   768  C  CB  . ALA   A 1 95  ? 3.936  1.980   16.733 1.00 18.60  ? 101 ALA   A CB  1 
ATOM   769  N  N   . VAL   A 1 96  ? 1.273  2.134   18.423 1.00 20.08  ? 102 VAL   A N   1 
ATOM   770  C  CA  . VAL   A 1 96  ? 0.703  1.990   19.762 1.00 21.36  ? 102 VAL   A CA  1 
ATOM   771  C  C   . VAL   A 1 96  ? 1.759  1.170   20.503 1.00 23.15  ? 102 VAL   A C   1 
ATOM   772  O  O   . VAL   A 1 96  ? 2.068  0.020   20.144 1.00 23.94  ? 102 VAL   A O   1 
ATOM   773  C  CB  . VAL   A 1 96  ? -0.672 1.291   19.726 1.00 23.95  ? 102 VAL   A CB  1 
ATOM   774  C  CG1 . VAL   A 1 96  ? -1.187 1.026   21.146 1.00 25.13  ? 102 VAL   A CG1 1 
ATOM   775  C  CG2 . VAL   A 1 96  ? -1.681 2.138   18.953 1.00 23.62  ? 102 VAL   A CG2 1 
ATOM   776  N  N   . GLY   A 1 97  ? 2.390  1.803   21.457 1.00 24.17  ? 103 GLY   A N   1 
ATOM   777  C  CA  . GLY   A 1 97  ? 3.472  1.178   22.211 1.00 25.30  ? 103 GLY   A CA  1 
ATOM   778  C  C   . GLY   A 1 97  ? 3.992  2.115   23.277 1.00 26.12  ? 103 GLY   A C   1 
ATOM   779  O  O   . GLY   A 1 97  ? 3.683  3.318   23.264 1.00 27.17  ? 103 GLY   A O   1 
ATOM   780  N  N   . HIS   A 1 98  ? 4.733  1.565   24.260 1.00 25.43  ? 104 HIS   A N   1 
ATOM   781  C  CA  . HIS   A 1 98  ? 5.265  2.409   25.313 1.00 24.58  ? 104 HIS   A CA  1 
ATOM   782  C  C   . HIS   A 1 98  ? 6.467  3.160   24.854 1.00 23.35  ? 104 HIS   A C   1 
ATOM   783  O  O   . HIS   A 1 98  ? 7.382  2.607   24.253 1.00 23.72  ? 104 HIS   A O   1 
ATOM   784  C  CB  . HIS   A 1 98  ? 5.623  1.631   26.589 1.00 25.72  ? 104 HIS   A CB  1 
ATOM   785  C  CG  . HIS   A 1 98  ? 6.182  2.506   27.681 1.00 26.68  ? 104 HIS   A CG  1 
ATOM   786  N  ND1 . HIS   A 1 98  ? 5.393  3.443   28.330 1.00 27.85  ? 104 HIS   A ND1 1 
ATOM   787  C  CD2 . HIS   A 1 98  ? 7.452  2.627   28.130 1.00 27.51  ? 104 HIS   A CD2 1 
ATOM   788  C  CE1 . HIS   A 1 98  ? 6.204  4.098   29.153 1.00 28.13  ? 104 HIS   A CE1 1 
ATOM   789  N  NE2 . HIS   A 1 98  ? 7.439  3.601   29.110 1.00 28.14  ? 104 HIS   A NE2 1 
ATOM   790  N  N   . SER   A 1 99  ? 6.512  4.426   25.207 1.00 22.17  ? 105 SER   A N   1 
ATOM   791  C  CA  . SER   A 1 99  ? 7.681  5.258   25.073 1.00 21.79  ? 105 SER   A CA  1 
ATOM   792  C  C   . SER   A 1 99  ? 7.613  6.373   26.107 1.00 25.18  ? 105 SER   A C   1 
ATOM   793  O  O   . SER   A 1 99  ? 6.521  6.770   26.542 1.00 25.64  ? 105 SER   A O   1 
ATOM   794  C  CB  . SER   A 1 99  ? 7.872  5.818   23.659 1.00 22.60  ? 105 SER   A CB  1 
ATOM   795  O  OG  . SER   A 1 99  ? 6.833  6.725   23.343 1.00 24.27  ? 105 SER   A OG  1 
ATOM   796  N  N   . GLU   A 1 100 ? 8.800  6.835   26.524 1.00 25.58  ? 106 GLU   A N   1 
ATOM   797  C  CA  . GLU   A 1 100 ? 8.966  7.909   27.501 1.00 26.82  ? 106 GLU   A CA  1 
ATOM   798  C  C   . GLU   A 1 100 ? 10.195 8.711   27.107 1.00 27.96  ? 106 GLU   A C   1 
ATOM   799  O  O   . GLU   A 1 100 ? 11.102 8.154   26.499 1.00 28.40  ? 106 GLU   A O   1 
ATOM   800  C  CB  . GLU   A 1 100 ? 9.372  7.279   28.849 1.00 27.91  ? 106 GLU   A CB  1 
ATOM   801  C  CG  . GLU   A 1 100 ? 8.281  6.824   29.749 1.00 35.07  ? 106 GLU   A CG  1 
ATOM   802  C  CD  . GLU   A 1 100 ? 8.951  6.055   30.877 1.00 34.15  ? 106 GLU   A CD  1 
ATOM   803  O  OE1 . GLU   A 1 100 ? 9.602  6.695   31.734 1.00 32.29  ? 106 GLU   A OE1 1 
ATOM   804  O  OE2 . GLU   A 1 100 ? 8.881  4.812   30.857 1.00 33.12  ? 106 GLU   A OE2 1 
ATOM   805  N  N   . PRO   A 1 101 ? 10.345 9.980   27.565 1.00 28.87  ? 107 PRO   A N   1 
ATOM   806  C  CA  . PRO   A 1 101 ? 11.627 10.663  27.375 1.00 29.18  ? 107 PRO   A CA  1 
ATOM   807  C  C   . PRO   A 1 101 ? 12.791 9.808   27.922 1.00 27.92  ? 107 PRO   A C   1 
ATOM   808  O  O   . PRO   A 1 101 ? 12.771 9.389   29.096 1.00 29.15  ? 107 PRO   A O   1 
ATOM   809  C  CB  . PRO   A 1 101 ? 11.462 11.941  28.198 1.00 30.92  ? 107 PRO   A CB  1 
ATOM   810  C  CG  . PRO   A 1 101 ? 9.972  12.175  28.258 1.00 31.50  ? 107 PRO   A CG  1 
ATOM   811  C  CD  . PRO   A 1 101 ? 9.404  10.791  28.362 1.00 29.39  ? 107 PRO   A CD  1 
ATOM   812  N  N   . GLY   A 1 102 ? 13.765 9.537   27.058 1.00 25.72  ? 108 GLY   A N   1 
ATOM   813  C  CA  . GLY   A 1 102 ? 14.925 8.686   27.313 1.00 24.10  ? 108 GLY   A CA  1 
ATOM   814  C  C   . GLY   A 1 102 ? 15.043 7.519   26.325 1.00 23.50  ? 108 GLY   A C   1 
ATOM   815  O  O   . GLY   A 1 102 ? 16.119 6.924   26.145 1.00 23.74  ? 108 GLY   A O   1 
ATOM   816  N  N   . ASP   A 1 103 ? 13.925 7.199   25.625 1.00 21.70  ? 109 ASP   A N   1 
ATOM   817  C  CA  . ASP   A 1 103 ? 13.835 6.097   24.668 1.00 20.65  ? 109 ASP   A CA  1 
ATOM   818  C  C   . ASP   A 1 103 ? 14.274 6.469   23.218 1.00 19.72  ? 109 ASP   A C   1 
ATOM   819  O  O   . ASP   A 1 103 ? 14.386 5.575   22.347 1.00 19.04  ? 109 ASP   A O   1 
ATOM   820  C  CB  . ASP   A 1 103 ? 12.398 5.540   24.624 1.00 21.78  ? 109 ASP   A CB  1 
ATOM   821  C  CG  . ASP   A 1 103 ? 12.072 4.718   25.860 1.00 22.25  ? 109 ASP   A CG  1 
ATOM   822  O  OD1 . ASP   A 1 103 ? 12.992 4.072   26.394 1.00 21.26  ? 109 ASP   A OD1 1 
ATOM   823  O  OD2 . ASP   A 1 103 ? 10.896 4.730   26.285 1.00 22.37  ? 109 ASP   A OD2 1 
ATOM   824  N  N   . CYS   A 1 104 ? 14.551 7.767   22.953 1.00 19.45  ? 110 CYS   A N   1 
ATOM   825  C  CA  . CYS   A 1 104 ? 14.994 8.137   21.583 1.00 20.00  ? 110 CYS   A CA  1 
ATOM   826  C  C   . CYS   A 1 104 ? 16.246 7.383   21.181 1.00 20.98  ? 110 CYS   A C   1 
ATOM   827  O  O   . CYS   A 1 104 ? 17.121 7.167   22.028 1.00 22.31  ? 110 CYS   A O   1 
ATOM   828  C  CB  . CYS   A 1 104 ? 15.218 9.636   21.478 1.00 21.02  ? 110 CYS   A CB  1 
ATOM   829  S  SG  . CYS   A 1 104 ? 13.690 10.590  21.452 1.00 22.42  ? 110 CYS   A SG  1 
ATOM   830  N  N   . GLY   A 1 105 ? 16.359 7.040   19.908 1.00 19.05  ? 111 GLY   A N   1 
ATOM   831  C  CA  . GLY   A 1 105 ? 17.544 6.332   19.428 1.00 19.04  ? 111 GLY   A CA  1 
ATOM   832  C  C   . GLY   A 1 105 ? 17.376 4.826   19.319 1.00 20.41  ? 111 GLY   A C   1 
ATOM   833  O  O   . GLY   A 1 105 ? 18.204 4.147   18.681 1.00 21.14  ? 111 GLY   A O   1 
ATOM   834  N  N   . GLY   A 1 106 ? 16.341 4.269   19.977 1.00 20.31  ? 112 GLY   A N   1 
ATOM   835  C  CA  . GLY   A 1 106 ? 16.071 2.835   19.859 1.00 19.22  ? 112 GLY   A CA  1 
ATOM   836  C  C   . GLY   A 1 106 ? 15.733 2.446   18.427 1.00 18.78  ? 112 GLY   A C   1 
ATOM   837  O  O   . GLY   A 1 106 ? 14.997 3.156   17.751 1.00 18.73  ? 112 GLY   A O   1 
ATOM   838  N  N   . ILE   A 1 107 ? 16.331 1.342   17.911 1.00 18.55  ? 113 ILE   A N   1 
ATOM   839  C  CA  . ILE   A 1 107 ? 16.078 0.950   16.538 1.00 19.04  ? 113 ILE   A CA  1 
ATOM   840  C  C   . ILE   A 1 107 ? 14.709 0.280   16.333 1.00 16.85  ? 113 ILE   A C   1 
ATOM   841  O  O   . ILE   A 1 107 ? 14.284 -0.587  17.132 1.00 18.21  ? 113 ILE   A O   1 
ATOM   842  C  CB  . ILE   A 1 107 ? 17.262 0.072   16.030 1.00 22.51  ? 113 ILE   A CB  1 
ATOM   843  C  CG1 . ILE   A 1 107 ? 18.404 0.974   15.520 1.00 25.63  ? 113 ILE   A CG1 1 
ATOM   844  C  CG2 . ILE   A 1 107 ? 16.828 -0.930  14.908 1.00 23.32  ? 113 ILE   A CG2 1 
ATOM   845  C  CD1 . ILE   A 1 107 ? 19.714 0.266   15.443 1.00 28.86  ? 113 ILE   A CD1 1 
ATOM   846  N  N   . LEU   A 1 108 ? 14.059 0.645   15.227 1.00 15.34  ? 114 LEU   A N   1 
ATOM   847  C  CA  . LEU   A 1 108 ? 12.879 -0.048  14.689 1.00 14.40  ? 114 LEU   A CA  1 
ATOM   848  C  C   . LEU   A 1 108 ? 13.409 -0.913  13.496 1.00 15.33  ? 114 LEU   A C   1 
ATOM   849  O  O   . LEU   A 1 108 ? 14.071 -0.385  12.594 1.00 16.30  ? 114 LEU   A O   1 
ATOM   850  C  CB  . LEU   A 1 108 ? 11.809 0.925   14.189 1.00 13.91  ? 114 LEU   A CB  1 
ATOM   851  C  CG  . LEU   A 1 108 ? 10.639 0.300   13.426 1.00 14.70  ? 114 LEU   A CG  1 
ATOM   852  C  CD1 . LEU   A 1 108 ? 9.768  -0.587  14.341 1.00 15.32  ? 114 LEU   A CD1 1 
ATOM   853  C  CD2 . LEU   A 1 108 ? 9.729  1.386   12.758 1.00 16.00  ? 114 LEU   A CD2 1 
ATOM   854  N  N   . ARG   A 1 109 ? 13.143 -2.235  13.512 1.00 15.02  ? 115 ARG   A N   1 
ATOM   855  C  CA  . ARG   A 1 109 ? 13.655 -3.109  12.431 1.00 16.36  ? 115 ARG   A CA  1 
ATOM   856  C  C   . ARG   A 1 109 ? 12.562 -3.980  11.822 1.00 17.26  ? 115 ARG   A C   1 
ATOM   857  O  O   . ARG   A 1 109 ? 11.658 -4.365  12.532 1.00 17.32  ? 115 ARG   A O   1 
ATOM   858  C  CB  . ARG   A 1 109 ? 14.781 -3.993  13.006 1.00 19.56  ? 115 ARG   A CB  1 
ATOM   859  C  CG  . ARG   A 1 109 ? 14.283 -5.080  13.964 1.00 26.41  ? 115 ARG   A CG  1 
ATOM   860  C  CD  . ARG   A 1 109 ? 15.409 -5.897  14.577 1.00 33.22  ? 115 ARG   A CD  1 
ATOM   861  N  NE  . ARG   A 1 109 ? 16.009 -5.176  15.699 1.00 37.71  ? 115 ARG   A NE  1 
ATOM   862  C  CZ  . ARG   A 1 109 ? 17.296 -5.223  16.023 1.00 40.75  ? 115 ARG   A CZ  1 
ATOM   863  N  NH1 . ARG   A 1 109 ? 18.139 -5.969  15.319 1.00 42.53  ? 115 ARG   A NH1 1 
ATOM   864  N  NH2 . ARG   A 1 109 ? 17.745 -4.542  17.060 1.00 39.55  ? 115 ARG   A NH2 1 
ATOM   865  N  N   . CYS   A 1 110 ? 12.681 -4.323  10.528 1.00 18.30  ? 116 CYS   A N   1 
ATOM   866  C  CA  . CYS   A 1 110 ? 11.764 -5.239  9.863  1.00 19.37  ? 116 CYS   A CA  1 
ATOM   867  C  C   . CYS   A 1 110 ? 12.655 -6.392  9.297  1.00 20.90  ? 116 CYS   A C   1 
ATOM   868  O  O   . CYS   A 1 110 ? 13.867 -6.440  9.575  1.00 21.88  ? 116 CYS   A O   1 
ATOM   869  C  CB  . CYS   A 1 110 ? 11.021 -4.516  8.738  1.00 21.62  ? 116 CYS   A CB  1 
ATOM   870  S  SG  . CYS   A 1 110 ? 12.109 -3.958  7.390  1.00 21.95  ? 116 CYS   A SG  1 
ATOM   871  N  N   . GLN   A 1 111 ? 12.077 -7.289  8.479  1.00 22.57  ? 117 GLN   A N   1 
ATOM   872  C  CA  . GLN   A 1 111 ? 12.903 -8.346  7.850  1.00 24.42  ? 117 GLN   A CA  1 
ATOM   873  C  C   . GLN   A 1 111 ? 14.023 -7.821  6.944  1.00 26.11  ? 117 GLN   A C   1 
ATOM   874  O  O   . GLN   A 1 111 ? 14.968 -8.562  6.647  1.00 28.89  ? 117 GLN   A O   1 
ATOM   875  C  CB  . GLN   A 1 111 ? 12.026 -9.314  7.048  1.00 27.58  ? 117 GLN   A CB  1 
ATOM   876  C  CG  . GLN   A 1 111 ? 11.279 -8.646  5.930  1.00 31.01  ? 117 GLN   A CG  1 
ATOM   877  C  CD  . GLN   A 1 111 ? 10.335 -9.590  5.264  1.00 37.49  ? 117 GLN   A CD  1 
ATOM   878  O  OE1 . GLN   A 1 111 ? 9.106  -9.406  5.301  1.00 38.41  ? 117 GLN   A OE1 1 
ATOM   879  N  NE2 . GLN   A 1 111 ? 10.895 -10.625 4.638  1.00 39.18  ? 117 GLN   A NE2 1 
ATOM   880  N  N   . HIS   A 1 112 ? 13.906 -6.599  6.448  1.00 24.99  ? 118 HIS   A N   1 
ATOM   881  C  CA  . HIS   A 1 112 ? 14.871 -6.036  5.508  1.00 25.02  ? 118 HIS   A CA  1 
ATOM   882  C  C   . HIS   A 1 112 ? 16.021 -5.277  6.155  1.00 25.64  ? 118 HIS   A C   1 
ATOM   883  O  O   . HIS   A 1 112 ? 16.985 -4.928  5.465  1.00 26.80  ? 118 HIS   A O   1 
ATOM   884  C  CB  . HIS   A 1 112 ? 14.158 -5.151  4.471  1.00 25.09  ? 118 HIS   A CB  1 
ATOM   885  C  CG  . HIS   A 1 112 ? 13.026 -5.850  3.782  1.00 24.62  ? 118 HIS   A CG  1 
ATOM   886  N  ND1 . HIS   A 1 112 ? 11.733 -5.657  4.172  1.00 25.27  ? 118 HIS   A ND1 1 
ATOM   887  C  CD2 . HIS   A 1 112 ? 13.050 -6.718  2.740  1.00 25.66  ? 118 HIS   A CD2 1 
ATOM   888  C  CE1 . HIS   A 1 112 ? 10.986 -6.395  3.374  1.00 26.08  ? 118 HIS   A CE1 1 
ATOM   889  N  NE2 . HIS   A 1 112 ? 11.740 -7.081  2.499  1.00 26.52  ? 118 HIS   A NE2 1 
ATOM   890  N  N   . GLY   A 1 113 ? 15.892 -4.951  7.446  1.00 24.00  ? 119 GLY   A N   1 
ATOM   891  C  CA  . GLY   A 1 113 ? 16.938 -4.210  8.132  1.00 23.21  ? 119 GLY   A CA  1 
ATOM   892  C  C   . GLY   A 1 113 ? 16.367 -3.107  9.001  1.00 22.09  ? 119 GLY   A C   1 
ATOM   893  O  O   . GLY   A 1 113 ? 15.218 -3.198  9.452  1.00 22.00  ? 119 GLY   A O   1 
ATOM   894  N  N   . VAL   A 1 114 ? 17.171 -2.059  9.204  1.00 20.77  ? 120 VAL   A N   1 
ATOM   895  C  CA  . VAL   A 1 114 ? 16.800 -0.908  10.038 1.00 20.53  ? 120 VAL   A CA  1 
ATOM   896  C  C   . VAL   A 1 114 ? 15.806 -0.045  9.275  1.00 20.83  ? 120 VAL   A C   1 
ATOM   897  O  O   . VAL   A 1 114 ? 16.132 0.416   8.180  1.00 21.56  ? 120 VAL   A O   1 
ATOM   898  C  CB  . VAL   A 1 114 ? 18.044 -0.068  10.438 1.00 21.32  ? 120 VAL   A CB  1 
ATOM   899  C  CG1 . VAL   A 1 114 ? 17.607 1.188   11.193 1.00 21.72  ? 120 VAL   A CG1 1 
ATOM   900  C  CG2 . VAL   A 1 114 ? 19.002 -0.890  11.294 1.00 22.23  ? 120 VAL   A CG2 1 
ATOM   901  N  N   . VAL   A 1 115 ? 14.641 0.259   9.893  1.00 19.36  ? 121 VAL   A N   1 
ATOM   902  C  CA  . VAL   A 1 115 ? 13.594 1.109   9.310  1.00 19.23  ? 121 VAL   A CA  1 
ATOM   903  C  C   . VAL   A 1 115 ? 13.769 2.560   9.790  1.00 19.37  ? 121 VAL   A C   1 
ATOM   904  O  O   . VAL   A 1 115 ? 13.613 3.507   9.024  1.00 19.80  ? 121 VAL   A O   1 
ATOM   905  C  CB  . VAL   A 1 115 ? 12.207 0.557   9.711  1.00 18.76  ? 121 VAL   A CB  1 
ATOM   906  C  CG1 . VAL   A 1 115 ? 11.062 1.478   9.268  1.00 18.41  ? 121 VAL   A CG1 1 
ATOM   907  C  CG2 . VAL   A 1 115 ? 11.991 -0.874  9.200  1.00 19.47  ? 121 VAL   A CG2 1 
ATOM   908  N  N   . GLY   A 1 116 ? 14.060 2.712   11.082 1.00 17.18  ? 122 GLY   A N   1 
ATOM   909  C  CA  . GLY   A 1 116 ? 14.159 4.048   11.675 1.00 16.79  ? 122 GLY   A CA  1 
ATOM   910  C  C   . GLY   A 1 116 ? 14.558 4.006   13.135 1.00 16.86  ? 122 GLY   A C   1 
ATOM   911  O  O   . GLY   A 1 116 ? 14.982 2.958   13.634 1.00 17.87  ? 122 GLY   A O   1 
ATOM   912  N  N   . ILE   A 1 117 ? 14.477 5.149   13.797 1.00 16.64  ? 123 ILE   A N   1 
ATOM   913  C  CA  . ILE   A 1 117 ? 14.808 5.188   15.248 1.00 16.52  ? 123 ILE   A CA  1 
ATOM   914  C  C   . ILE   A 1 117 ? 13.714 5.901   16.015 1.00 17.64  ? 123 ILE   A C   1 
ATOM   915  O  O   . ILE   A 1 117 ? 13.061 6.805   15.479 1.00 18.23  ? 123 ILE   A O   1 
ATOM   916  C  CB  . ILE   A 1 117 ? 16.191 5.871   15.547 1.00 18.32  ? 123 ILE   A CB  1 
ATOM   917  C  CG1 . ILE   A 1 117 ? 16.295 7.217   14.833 1.00 20.48  ? 123 ILE   A CG1 1 
ATOM   918  C  CG2 . ILE   A 1 117 ? 17.409 4.947   15.256 1.00 20.04  ? 123 ILE   A CG2 1 
ATOM   919  C  CD1 . ILE   A 1 117 ? 17.560 8.024   15.124 1.00 22.01  ? 123 ILE   A CD1 1 
ATOM   920  N  N   . VAL   A 1 118 ? 13.511 5.527   17.299 1.00 15.54  ? 124 VAL   A N   1 
ATOM   921  C  CA  . VAL   A 1 118 ? 12.525 6.262   18.128 1.00 15.16  ? 124 VAL   A CA  1 
ATOM   922  C  C   . VAL   A 1 118 ? 12.840 7.762   18.145 1.00 15.46  ? 124 VAL   A C   1 
ATOM   923  O  O   . VAL   A 1 118 ? 13.990 8.149   18.399 1.00 17.04  ? 124 VAL   A O   1 
ATOM   924  C  CB  . VAL   A 1 118 ? 12.464 5.722   19.588 1.00 16.76  ? 124 VAL   A CB  1 
ATOM   925  C  CG1 . VAL   A 1 118 ? 11.495 6.546   20.446 1.00 17.52  ? 124 VAL   A CG1 1 
ATOM   926  C  CG2 . VAL   A 1 118 ? 12.087 4.250   19.610 1.00 17.39  ? 124 VAL   A CG2 1 
ATOM   927  N  N   . SER   A 1 119 ? 11.816 8.605   17.995 1.00 14.92  ? 125 SER   A N   1 
ATOM   928  C  CA  . SER   A 1 119 ? 12.006 10.066  17.981 1.00 15.17  ? 125 SER   A CA  1 
ATOM   929  C  C   . SER   A 1 119 ? 10.981 10.784  18.862 1.00 17.89  ? 125 SER   A C   1 
ATOM   930  O  O   . SER   A 1 119 ? 11.287 11.840  19.374 1.00 19.31  ? 125 SER   A O   1 
ATOM   931  C  CB  . SER   A 1 119 ? 11.947 10.605  16.538 1.00 16.57  ? 125 SER   A CB  1 
ATOM   932  O  OG  . SER   A 1 119 ? 12.127 12.022  16.465 1.00 19.57  ? 125 SER   A OG  1 
ATOM   933  N  N   . THR   A 1 120 ? 9.746  10.253  19.001 1.00 18.36  ? 126 THR   A N   1 
ATOM   934  C  CA  . THR   A 1 120 ? 8.698  10.952  19.774 1.00 18.62  ? 126 THR   A CA  1 
ATOM   935  C  C   . THR   A 1 120 ? 7.821  9.888   20.541 1.00 19.46  ? 126 THR   A C   1 
ATOM   936  O  O   . THR   A 1 120 ? 8.026  8.681   20.371 1.00 19.04  ? 126 THR   A O   1 
ATOM   937  C  CB  . THR   A 1 120 ? 7.734  11.722  18.764 1.00 19.94  ? 126 THR   A CB  1 
ATOM   938  O  OG1 . THR   A 1 120 ? 6.887  10.779  18.113 1.00 21.11  ? 126 THR   A OG1 1 
ATOM   939  C  CG2 . THR   A 1 120 ? 8.423  12.558  17.730 1.00 19.65  ? 126 THR   A CG2 1 
ATOM   940  N  N   . GLY   A 1 121 ? 6.828  10.351  21.308 1.00 20.99  ? 127 GLY   A N   1 
ATOM   941  C  CA  . GLY   A 1 121 ? 5.879  9.455   21.929 1.00 23.82  ? 127 GLY   A CA  1 
ATOM   942  C  C   . GLY   A 1 121 ? 4.664  10.184  22.458 1.00 26.86  ? 127 GLY   A C   1 
ATOM   943  O  O   . GLY   A 1 121 ? 4.503  11.389  22.256 1.00 28.44  ? 127 GLY   A O   1 
ATOM   944  N  N   . GLY   A 1 122 ? 3.773  9.425   23.064 1.00 27.09  ? 128 GLY   A N   1 
ATOM   945  C  CA  . GLY   A 1 122 ? 2.560  9.983   23.648 1.00 28.52  ? 128 GLY   A CA  1 
ATOM   946  C  C   . GLY   A 1 122 ? 1.973  9.012   24.636 1.00 31.25  ? 128 GLY   A C   1 
ATOM   947  O  O   . GLY   A 1 122 ? 2.660  8.082   25.083 1.00 32.55  ? 128 GLY   A O   1 
ATOM   948  N  N   . ASN   A 1 123 ? 0.692  9.204   24.990 1.00 31.85  ? 129 ASN   A N   1 
ATOM   949  C  CA  . ASN   A 1 123 ? 0.050  8.284   25.909 1.00 32.41  ? 129 ASN   A CA  1 
ATOM   950  C  C   . ASN   A 1 123 ? -0.243 6.995   25.191 1.00 31.62  ? 129 ASN   A C   1 
ATOM   951  O  O   . ASN   A 1 123 ? -1.282 6.852   24.524 1.00 32.74  ? 129 ASN   A O   1 
ATOM   952  C  CB  . ASN   A 1 123 ? -1.210 8.881   26.502 1.00 33.76  ? 129 ASN   A CB  1 
ATOM   953  C  CG  . ASN   A 1 123 ? -1.690 8.161   27.740 1.00 37.65  ? 129 ASN   A CG  1 
ATOM   954  O  OD1 . ASN   A 1 123 ? -1.154 7.114   28.145 1.00 40.03  ? 129 ASN   A OD1 1 
ATOM   955  N  ND2 . ASN   A 1 123 ? -2.705 8.722   28.370 1.00 36.67  ? 129 ASN   A ND2 1 
ATOM   956  N  N   . GLY   A 1 124 ? 0.652  6.032   25.375 1.00 28.22  ? 130 GLY   A N   1 
ATOM   957  C  CA  . GLY   A 1 124 ? 0.499  4.741   24.743 1.00 27.55  ? 130 GLY   A CA  1 
ATOM   958  C  C   . GLY   A 1 124 ? 0.922  4.766   23.286 1.00 25.18  ? 130 GLY   A C   1 
ATOM   959  O  O   . GLY   A 1 124 ? 0.600  3.834   22.561 1.00 25.81  ? 130 GLY   A O   1 
ATOM   960  N  N   . LEU   A 1 125 ? 1.663  5.802   22.869 1.00 23.81  ? 131 LEU   A N   1 
ATOM   961  C  CA  . LEU   A 1 125 ? 2.165  5.944   21.490 1.00 23.38  ? 131 LEU   A CA  1 
ATOM   962  C  C   . LEU   A 1 125 ? 3.696  6.071   21.444 1.00 23.25  ? 131 LEU   A C   1 
ATOM   963  O  O   . LEU   A 1 125 ? 4.326  6.537   22.408 1.00 23.92  ? 131 LEU   A O   1 
ATOM   964  C  CB  . LEU   A 1 125 ? 1.565  7.191   20.828 1.00 24.24  ? 131 LEU   A CB  1 
ATOM   965  C  CG  . LEU   A 1 125 ? 0.035  7.200   20.634 1.00 25.27  ? 131 LEU   A CG  1 
ATOM   966  C  CD1 . LEU   A 1 125 ? -0.450 8.624   20.385 1.00 26.91  ? 131 LEU   A CD1 1 
ATOM   967  C  CD2 . LEU   A 1 125 ? -0.366 6.286   19.509 1.00 25.22  ? 131 LEU   A CD2 1 
ATOM   968  N  N   . VAL   A 1 126 ? 4.300  5.651   20.317 1.00 20.99  ? 132 VAL   A N   1 
ATOM   969  C  CA  . VAL   A 1 126 ? 5.732  5.812   20.085 1.00 20.47  ? 132 VAL   A CA  1 
ATOM   970  C  C   . VAL   A 1 126 ? 5.880  6.214   18.602 1.00 19.92  ? 132 VAL   A C   1 
ATOM   971  O  O   . VAL   A 1 126 ? 5.133  5.712   17.759 1.00 20.98  ? 132 VAL   A O   1 
ATOM   972  C  CB  . VAL   A 1 126 ? 6.491  4.498   20.390 1.00 20.98  ? 132 VAL   A CB  1 
ATOM   973  C  CG1 . VAL   A 1 126 ? 5.899  3.333   19.626 1.00 23.00  ? 132 VAL   A CG1 1 
ATOM   974  C  CG2 . VAL   A 1 126 ? 7.988  4.626   20.149 1.00 20.19  ? 132 VAL   A CG2 1 
ATOM   975  N  N   . GLY   A 1 127 ? 6.729  7.203   18.312 1.00 18.04  ? 133 GLY   A N   1 
ATOM   976  C  CA  . GLY   A 1 127 ? 6.960  7.686   16.951 1.00 18.98  ? 133 GLY   A CA  1 
ATOM   977  C  C   . GLY   A 1 127 ? 8.377  7.399   16.514 1.00 18.22  ? 133 GLY   A C   1 
ATOM   978  O  O   . GLY   A 1 127 ? 9.311  7.564   17.308 1.00 17.98  ? 133 GLY   A O   1 
ATOM   979  N  N   . PHE   A 1 128 ? 8.543  7.027   15.241 1.00 16.87  ? 134 PHE   A N   1 
ATOM   980  C  CA  . PHE   A 1 128 ? 9.844  6.635   14.686 1.00 16.54  ? 134 PHE   A CA  1 
ATOM   981  C  C   . PHE   A 1 128 ? 10.203 7.540   13.518 1.00 17.00  ? 134 PHE   A C   1 
ATOM   982  O  O   . PHE   A 1 128 ? 9.380  7.754   12.634 1.00 16.54  ? 134 PHE   A O   1 
ATOM   983  C  CB  . PHE   A 1 128 ? 9.790  5.203   14.156 1.00 15.83  ? 134 PHE   A CB  1 
ATOM   984  C  CG  . PHE   A 1 128 ? 9.302  4.213   15.196 1.00 15.64  ? 134 PHE   A CG  1 
ATOM   985  C  CD1 . PHE   A 1 128 ? 10.169 3.708   16.153 1.00 14.98  ? 134 PHE   A CD1 1 
ATOM   986  C  CD2 . PHE   A 1 128 ? 7.982  3.768   15.200 1.00 15.63  ? 134 PHE   A CD2 1 
ATOM   987  C  CE1 . PHE   A 1 128 ? 9.718  2.793   17.122 1.00 15.21  ? 134 PHE   A CE1 1 
ATOM   988  C  CE2 . PHE   A 1 128 ? 7.531  2.860   16.175 1.00 16.25  ? 134 PHE   A CE2 1 
ATOM   989  C  CZ  . PHE   A 1 128 ? 8.409  2.357   17.103 1.00 15.05  ? 134 PHE   A CZ  1 
ATOM   990  N  N   . ALA   A 1 129 ? 11.428 8.024   13.513 1.00 16.14  ? 135 ALA   A N   1 
ATOM   991  C  CA  . ALA   A 1 129 ? 11.924 8.815   12.381 1.00 16.90  ? 135 ALA   A CA  1 
ATOM   992  C  C   . ALA   A 1 129 ? 12.348 7.828   11.269 1.00 17.61  ? 135 ALA   A C   1 
ATOM   993  O  O   . ALA   A 1 129 ? 13.280 7.055   11.479 1.00 17.90  ? 135 ALA   A O   1 
ATOM   994  C  CB  . ALA   A 1 129 ? 13.132 9.650   12.821 1.00 16.69  ? 135 ALA   A CB  1 
ATOM   995  N  N   . ASP   A 1 130 ? 11.674 7.831   10.106 1.00 17.44  ? 136 ASP   A N   1 
ATOM   996  C  CA  . ASP   A 1 130 ? 12.055 6.904   8.999  1.00 17.83  ? 136 ASP   A CA  1 
ATOM   997  C  C   . ASP   A 1 130 ? 13.442 7.251   8.403  1.00 19.11  ? 136 ASP   A C   1 
ATOM   998  O  O   . ASP   A 1 130 ? 13.803 8.425   8.316  1.00 20.21  ? 136 ASP   A O   1 
ATOM   999  C  CB  . ASP   A 1 130 ? 11.004 7.052   7.867  1.00 20.65  ? 136 ASP   A CB  1 
ATOM   1000 C  CG  . ASP   A 1 130 ? 11.114 6.019   6.772  1.00 25.64  ? 136 ASP   A CG  1 
ATOM   1001 O  OD1 . ASP   A 1 130 ? 11.146 4.832   7.091  1.00 26.07  ? 136 ASP   A OD1 1 
ATOM   1002 O  OD2 . ASP   A 1 130 ? 11.171 6.412   5.592  1.00 28.22  ? 136 ASP   A OD2 1 
ATOM   1003 N  N   . VAL   A 1 131 ? 14.218 6.232   7.991  1.00 18.77  ? 137 VAL   A N   1 
ATOM   1004 C  CA  . VAL   A 1 131 ? 15.502 6.445   7.323  1.00 20.30  ? 137 VAL   A CA  1 
ATOM   1005 C  C   . VAL   A 1 131 ? 15.541 5.676   5.954  1.00 20.87  ? 137 VAL   A C   1 
ATOM   1006 O  O   . VAL   A 1 131 ? 16.523 5.809   5.229  1.00 21.73  ? 137 VAL   A O   1 
ATOM   1007 C  CB  . VAL   A 1 131 ? 16.736 6.100   8.195  1.00 20.86  ? 137 VAL   A CB  1 
ATOM   1008 C  CG1 . VAL   A 1 131 ? 16.708 6.863   9.530  1.00 20.45  ? 137 VAL   A CG1 1 
ATOM   1009 C  CG2 . VAL   A 1 131 ? 16.866 4.585   8.421  1.00 21.55  ? 137 VAL   A CG2 1 
ATOM   1010 N  N   . ARG   A 1 132 ? 14.457 4.938   5.591  1.00 20.64  ? 138 ARG   A N   1 
ATOM   1011 C  CA  . ARG   A 1 132 ? 14.416 4.137   4.366  1.00 20.63  ? 138 ARG   A CA  1 
ATOM   1012 C  C   . ARG   A 1 132 ? 14.485 4.936   3.038  1.00 22.49  ? 138 ARG   A C   1 
ATOM   1013 O  O   . ARG   A 1 132 ? 14.846 4.356   2.017  1.00 23.57  ? 138 ARG   A O   1 
ATOM   1014 C  CB  . ARG   A 1 132 ? 13.214 3.203   4.334  1.00 20.49  ? 138 ARG   A CB  1 
ATOM   1015 C  CG  . ARG   A 1 132 ? 13.149 2.259   5.536  1.00 20.48  ? 138 ARG   A CG  1 
ATOM   1016 C  CD  . ARG   A 1 132 ? 11.838 1.487   5.467  1.00 20.54  ? 138 ARG   A CD  1 
ATOM   1017 N  NE  . ARG   A 1 132 ? 10.697 2.327   5.846  1.00 20.04  ? 138 ARG   A NE  1 
ATOM   1018 C  CZ  . ARG   A 1 132 ? 9.453  1.874   5.968  1.00 19.90  ? 138 ARG   A CZ  1 
ATOM   1019 N  NH1 . ARG   A 1 132 ? 9.165  0.611   5.660  1.00 20.04  ? 138 ARG   A NH1 1 
ATOM   1020 N  NH2 . ARG   A 1 132 ? 8.489  2.676   6.408  1.00 19.73  ? 138 ARG   A NH2 1 
ATOM   1021 N  N   . ASP   A 1 133 ? 14.116 6.228   3.036  1.00 23.78  ? 139 ASP   A N   1 
ATOM   1022 C  CA  . ASP   A 1 133 ? 14.244 7.074   1.843  1.00 24.48  ? 139 ASP   A CA  1 
ATOM   1023 C  C   . ASP   A 1 133 ? 15.678 7.646   1.662  1.00 25.57  ? 139 ASP   A C   1 
ATOM   1024 O  O   . ASP   A 1 133 ? 15.952 8.260   0.632  1.00 26.83  ? 139 ASP   A O   1 
ATOM   1025 C  CB  . ASP   A 1 133 ? 13.251 8.245   1.873  1.00 25.92  ? 139 ASP   A CB  1 
ATOM   1026 C  CG  . ASP   A 1 133 ? 13.538 9.230   3.007  1.00 29.28  ? 139 ASP   A CG  1 
ATOM   1027 O  OD1 . ASP   A 1 133 ? 13.881 8.776   4.110  1.00 29.30  ? 139 ASP   A OD1 1 
ATOM   1028 O  OD2 . ASP   A 1 133 ? 13.426 10.466  2.781  1.00 30.06  ? 139 ASP   A OD2 1 
ATOM   1029 N  N   . LEU   A 1 134 ? 16.572 7.492   2.662  1.00 24.33  ? 140 LEU   A N   1 
ATOM   1030 C  CA  . LEU   A 1 134 ? 17.920 8.070   2.581  1.00 25.14  ? 140 LEU   A CA  1 
ATOM   1031 C  C   . LEU   A 1 134 ? 18.831 7.095   1.870  1.00 26.77  ? 140 LEU   A C   1 
ATOM   1032 O  O   . LEU   A 1 134 ? 19.696 6.457   2.490  1.00 26.12  ? 140 LEU   A O   1 
ATOM   1033 C  CB  . LEU   A 1 134 ? 18.389 8.380   4.039  1.00 24.46  ? 140 LEU   A CB  1 
ATOM   1034 C  CG  . LEU   A 1 134 ? 17.514 9.368   4.818  1.00 25.03  ? 140 LEU   A CG  1 
ATOM   1035 C  CD1 . LEU   A 1 134 ? 18.076 9.604   6.227  1.00 25.03  ? 140 LEU   A CD1 1 
ATOM   1036 C  CD2 . LEU   A 1 134 ? 17.380 10.696  4.085  1.00 25.44  ? 140 LEU   A CD2 1 
ATOM   1037 N  N   . LEU   A 1 135 ? 18.584 6.935   0.537  1.00 27.56  ? 141 LEU   A N   1 
ATOM   1038 C  CA  . LEU   A 1 135 ? 19.286 5.959   -0.284 1.00 28.83  ? 141 LEU   A CA  1 
ATOM   1039 C  C   . LEU   A 1 135 ? 20.781 6.153   -0.280 1.00 30.65  ? 141 LEU   A C   1 
ATOM   1040 O  O   . LEU   A 1 135 ? 21.523 5.176   -0.398 1.00 31.90  ? 141 LEU   A O   1 
ATOM   1041 C  CB  . LEU   A 1 135 ? 18.736 5.898   -1.736 1.00 29.47  ? 141 LEU   A CB  1 
ATOM   1042 C  CG  . LEU   A 1 135 ? 17.210 5.855   -1.893 1.00 31.70  ? 141 LEU   A CG  1 
ATOM   1043 C  CD1 . LEU   A 1 135 ? 16.807 5.580   -3.342 1.00 32.70  ? 141 LEU   A CD1 1 
ATOM   1044 C  CD2 . LEU   A 1 135 ? 16.566 4.778   -1.025 1.00 32.08  ? 141 LEU   A CD2 1 
ATOM   1045 N  N   . TRP   A 1 136 ? 21.228 7.404   -0.146 1.00 31.34  ? 142 TRP   A N   1 
ATOM   1046 C  CA  . TRP   A 1 136 ? 22.642 7.730   -0.135 1.00 32.31  ? 142 TRP   A CA  1 
ATOM   1047 C  C   . TRP   A 1 136 ? 23.400 7.108   1.038  1.00 33.41  ? 142 TRP   A C   1 
ATOM   1048 O  O   . TRP   A 1 136 ? 24.618 7.032   0.974  1.00 35.07  ? 142 TRP   A O   1 
ATOM   1049 C  CB  . TRP   A 1 136 ? 22.836 9.250   -0.189 1.00 31.56  ? 142 TRP   A CB  1 
ATOM   1050 C  CG  . TRP   A 1 136 ? 22.126 10.005  0.895  1.00 31.12  ? 142 TRP   A CG  1 
ATOM   1051 C  CD1 . TRP   A 1 136 ? 20.886 10.568  0.831  1.00 31.70  ? 142 TRP   A CD1 1 
ATOM   1052 C  CD2 . TRP   A 1 136 ? 22.647 10.328  2.188  1.00 30.46  ? 142 TRP   A CD2 1 
ATOM   1053 N  NE1 . TRP   A 1 136 ? 20.602 11.222  2.006  1.00 32.04  ? 142 TRP   A NE1 1 
ATOM   1054 C  CE2 . TRP   A 1 136 ? 21.670 11.090  2.857  1.00 31.16  ? 142 TRP   A CE2 1 
ATOM   1055 C  CE3 . TRP   A 1 136 ? 23.848 10.041  2.850  1.00 30.60  ? 142 TRP   A CE3 1 
ATOM   1056 C  CZ2 . TRP   A 1 136 ? 21.843 11.546  4.160  1.00 30.80  ? 142 TRP   A CZ2 1 
ATOM   1057 C  CZ3 . TRP   A 1 136 ? 24.031 10.527  4.127  1.00 30.57  ? 142 TRP   A CZ3 1 
ATOM   1058 C  CH2 . TRP   A 1 136 ? 23.027 11.249  4.777  1.00 30.66  ? 142 TRP   A CH2 1 
ATOM   1059 N  N   . LEU   A 1 137 ? 22.704 6.639   2.102  1.00 32.98  ? 143 LEU   A N   1 
ATOM   1060 C  CA  . LEU   A 1 137 ? 23.396 6.004   3.232  1.00 33.23  ? 143 LEU   A CA  1 
ATOM   1061 C  C   . LEU   A 1 137 ? 24.152 4.732   2.810  1.00 35.23  ? 143 LEU   A C   1 
ATOM   1062 O  O   . LEU   A 1 137 ? 25.052 4.308   3.530  1.00 34.97  ? 143 LEU   A O   1 
ATOM   1063 C  CB  . LEU   A 1 137 ? 22.398 5.646   4.352  1.00 32.04  ? 143 LEU   A CB  1 
ATOM   1064 C  CG  . LEU   A 1 137 ? 21.863 6.817   5.159  1.00 31.67  ? 143 LEU   A CG  1 
ATOM   1065 C  CD1 . LEU   A 1 137 ? 20.728 6.348   6.093  1.00 32.44  ? 143 LEU   A CD1 1 
ATOM   1066 C  CD2 . LEU   A 1 137 ? 22.980 7.466   5.967  1.00 31.96  ? 143 LEU   A CD2 1 
ATOM   1067 N  N   . ASP   A 1 138 ? 23.749 4.111   1.674  1.00 37.08  ? 144 ASP   A N   1 
ATOM   1068 C  CA  . ASP   A 1 138 ? 24.333 2.882   1.101  1.00 39.87  ? 144 ASP   A CA  1 
ATOM   1069 C  C   . ASP   A 1 138 ? 25.496 3.156   0.134  1.00 43.11  ? 144 ASP   A C   1 
ATOM   1070 O  O   . ASP   A 1 138 ? 26.007 2.206   -0.467 1.00 43.44  ? 144 ASP   A O   1 
ATOM   1071 C  CB  . ASP   A 1 138 ? 23.269 2.111   0.312  1.00 41.30  ? 144 ASP   A CB  1 
ATOM   1072 C  CG  . ASP   A 1 138 ? 22.047 1.678   1.089  1.00 46.89  ? 144 ASP   A CG  1 
ATOM   1073 O  OD1 . ASP   A 1 138 ? 22.111 1.663   2.336  1.00 46.92  ? 144 ASP   A OD1 1 
ATOM   1074 O  OD2 . ASP   A 1 138 ? 21.014 1.367   0.447  1.00 50.09  ? 144 ASP   A OD2 1 
ATOM   1075 N  N   . GLU   A 1 139 ? 25.887 4.421   -0.064 1.00 45.48  ? 145 GLU   A N   1 
ATOM   1076 C  CA  . GLU   A 1 139 ? 26.967 4.730   -1.002 1.00 48.62  ? 145 GLU   A CA  1 
ATOM   1077 C  C   . GLU   A 1 139 ? 27.898 5.817   -0.518 1.00 51.72  ? 145 GLU   A C   1 
ATOM   1078 O  O   . GLU   A 1 139 ? 27.487 6.686   0.259  1.00 52.76  ? 145 GLU   A O   1 
ATOM   1079 C  CB  . GLU   A 1 139 ? 26.406 5.057   -2.395 1.00 51.26  ? 145 GLU   A CB  1 
ATOM   1080 C  CG  . GLU   A 1 139 ? 25.389 6.183   -2.402 1.00 57.02  ? 145 GLU   A CG  1 
ATOM   1081 C  CD  . GLU   A 1 139 ? 24.293 6.016   -3.438 1.00 66.06  ? 145 GLU   A CD  1 
ATOM   1082 O  OE1 . GLU   A 1 139 ? 24.375 6.671   -4.501 1.00 68.68  ? 145 GLU   A OE1 1 
ATOM   1083 O  OE2 . GLU   A 1 139 ? 23.351 5.229   -3.188 1.00 68.38  ? 145 GLU   A OE2 1 
ATOM   1084 N  N   . GLU   A 1 140 ? 29.162 5.757   -0.993 1.00 53.26  ? 146 GLU   A N   1 
ATOM   1085 C  CA  . GLU   A 1 140 ? 30.254 6.699   -0.739 1.00 55.05  ? 146 GLU   A CA  1 
ATOM   1086 C  C   . GLU   A 1 140 ? 30.272 7.257   0.692  1.00 56.37  ? 146 GLU   A C   1 
ATOM   1087 O  O   . GLU   A 1 140 ? 31.053 8.155   1.025  1.00 57.17  ? 146 GLU   A O   1 
ATOM   1088 C  CB  . GLU   A 1 140 ? 30.245 7.823   -1.794 1.00 58.01  ? 146 GLU   A CB  1 
ATOM   1089 C  CG  . GLU   A 1 140 ? 29.315 8.998   -1.521 1.00 63.53  ? 146 GLU   A CG  1 
ATOM   1090 C  CD  . GLU   A 1 140 ? 30.031 10.324  -1.317 1.00 70.68  ? 146 GLU   A CD  1 
ATOM   1091 O  OE1 . GLU   A 1 140 ? 29.395 11.270  -0.794 1.00 71.11  ? 146 GLU   A OE1 1 
ATOM   1092 O  OE2 . GLU   A 1 140 ? 31.232 10.414  -1.665 1.00 73.38  ? 146 GLU   A OE2 1 
HETATM 1093 N  N1  . A1BRI B 2 .   ? 9.437  14.316  22.517 1.00 26.68  ? 201 A1BRI A N1  1 
HETATM 1094 C  C4  . A1BRI B 2 .   ? 10.475 14.838  23.423 1.00 26.53  ? 201 A1BRI A C4  1 
HETATM 1095 C  C5  . A1BRI B 2 .   ? 8.422  13.490  22.898 1.00 27.04  ? 201 A1BRI A C5  1 
HETATM 1096 C  C6  . A1BRI B 2 .   ? 7.342  12.406  24.845 1.00 30.43  ? 201 A1BRI A C6  1 
HETATM 1097 C  C7  . A1BRI B 2 .   ? 6.240  12.812  25.599 1.00 31.13  ? 201 A1BRI A C7  1 
HETATM 1098 C  C8  . A1BRI B 2 .   ? 5.411  11.859  26.173 1.00 31.31  ? 201 A1BRI A C8  1 
HETATM 1099 C  C10 . A1BRI B 2 .   ? 6.765  10.094  25.269 1.00 31.08  ? 201 A1BRI A C10 1 
HETATM 1100 C  C13 . A1BRI B 2 .   ? 10.489 9.441   23.195 1.00 29.98  ? 201 A1BRI A C13 1 
HETATM 1101 F  F2  . A1BRI B 2 .   ? 11.320 10.144  23.937 1.00 30.18  ? 201 A1BRI A F2  1 
HETATM 1102 F  F   . A1BRI B 2 .   ? 10.502 10.009  21.995 1.00 29.69  ? 201 A1BRI A F   1 
HETATM 1103 F  F1  . A1BRI B 2 .   ? 11.021 8.233   23.048 1.00 29.50  ? 201 A1BRI A F1  1 
HETATM 1104 C  C12 . A1BRI B 2 .   ? 9.144  9.400   23.799 1.00 30.89  ? 201 A1BRI A C12 1 
HETATM 1105 O  O2  . A1BRI B 2 .   ? 8.705  10.764  23.930 1.00 31.14  ? 201 A1BRI A O2  1 
HETATM 1106 C  C11 . A1BRI B 2 .   ? 7.597  11.043  24.690 1.00 30.76  ? 201 A1BRI A C11 1 
HETATM 1107 C  C9  . A1BRI B 2 .   ? 5.668  10.511  26.004 1.00 31.11  ? 201 A1BRI A C9  1 
HETATM 1108 N  N2  . A1BRI B 2 .   ? 8.273  13.291  24.247 1.00 28.97  ? 201 A1BRI A N2  1 
HETATM 1109 O  O1  . A1BRI B 2 .   ? 7.656  13.014  22.077 1.00 26.31  ? 201 A1BRI A O1  1 
HETATM 1110 C  C3  . A1BRI B 2 .   ? 11.857 14.797  22.775 1.00 26.76  ? 201 A1BRI A C3  1 
HETATM 1111 C  C2  . A1BRI B 2 .   ? 11.822 15.426  21.383 1.00 26.86  ? 201 A1BRI A C2  1 
HETATM 1112 C  C14 . A1BRI B 2 .   ? 9.411  14.941  21.189 1.00 26.53  ? 201 A1BRI A C14 1 
HETATM 1113 C  C1  . A1BRI B 2 .   ? 10.763 14.746  20.493 1.00 26.62  ? 201 A1BRI A C1  1 
HETATM 1114 C  C   . A1BRI B 2 .   ? 10.772 15.320  19.085 1.00 25.49  ? 201 A1BRI A C   1 
HETATM 1115 O  O   . A1BRI B 2 .   ? 10.257 16.417  18.841 1.00 26.07  ? 201 A1BRI A O   1 
HETATM 1116 N  N   . A1BRI B 2 .   ? 11.349 14.574  18.154 1.00 24.20  ? 201 A1BRI A N   1 
HETATM 1117 ZN ZN  . ZN    C 3 .   ? 10.907 -4.134  5.410  1.00 20.74  2 202 ZN    A ZN  1 
HETATM 1118 O  O   . HOH   D 4 .   ? 14.536 9.738   30.865 1.00 33.56  ? 301 HOH   A O   1 
HETATM 1119 O  O   . HOH   D 4 .   ? 31.386 8.490   3.529  1.00 58.76  ? 302 HOH   A O   1 
HETATM 1120 O  O   . HOH   D 4 .   ? 2.947  8.511   10.079 1.00 48.02  ? 303 HOH   A O   1 
HETATM 1121 O  O   . HOH   D 4 .   ? 3.772  -4.944  21.007 1.00 35.26  ? 304 HOH   A O   1 
HETATM 1122 O  O   . HOH   D 4 .   ? 10.353 8.664   4.644  1.00 30.85  ? 305 HOH   A O   1 
HETATM 1123 O  O   . HOH   D 4 .   ? 23.687 22.751  9.171  1.00 35.37  ? 306 HOH   A O   1 
HETATM 1124 O  O   . HOH   D 4 .   ? 9.687  24.633  24.114 1.00 33.53  ? 307 HOH   A O   1 
HETATM 1125 O  O   . HOH   D 4 .   ? 22.295 -0.320  4.037  1.00 30.22  ? 308 HOH   A O   1 
HETATM 1126 O  O   . HOH   D 4 .   ? 29.049 3.655   10.503 1.00 30.02  ? 309 HOH   A O   1 
HETATM 1127 O  O   . HOH   D 4 .   ? 17.451 0.798   29.964 1.00 40.09  ? 310 HOH   A O   1 
HETATM 1128 O  O   . HOH   D 4 .   ? 7.074  25.703  15.099 1.00 38.39  ? 311 HOH   A O   1 
HETATM 1129 O  O   . HOH   D 4 .   ? 4.506  20.511  25.799 1.00 43.55  ? 312 HOH   A O   1 
HETATM 1130 O  O   . HOH   D 4 .   ? 15.874 19.042  28.592 1.00 52.13  ? 313 HOH   A O   1 
HETATM 1131 O  O   . HOH   D 4 .   ? 15.082 23.454  18.259 1.00 35.14  ? 314 HOH   A O   1 
HETATM 1132 O  O   . HOH   D 4 .   ? 1.031  8.458   9.652  1.00 35.58  ? 315 HOH   A O   1 
HETATM 1133 O  O   . HOH   D 4 .   ? 0.017  14.572  17.159 1.00 50.25  ? 316 HOH   A O   1 
HETATM 1134 O  O   . HOH   D 4 .   ? 17.996 -6.210  3.378  1.00 35.38  ? 317 HOH   A O   1 
HETATM 1135 O  O   . HOH   D 4 .   ? 10.023 5.419   3.418  1.00 26.99  ? 318 HOH   A O   1 
HETATM 1136 O  O   . HOH   D 4 .   ? 18.922 0.091   27.248 1.00 35.19  ? 319 HOH   A O   1 
HETATM 1137 O  O   . HOH   D 4 .   ? 19.227 -0.705  31.328 1.00 45.02  ? 320 HOH   A O   1 
HETATM 1138 O  O   . HOH   D 4 .   ? 19.857 9.286   19.261 1.00 23.89  ? 321 HOH   A O   1 
HETATM 1139 O  O   . HOH   D 4 .   ? 6.171  -5.197  29.037 1.00 36.57  ? 322 HOH   A O   1 
HETATM 1140 O  O   . HOH   D 4 .   ? 15.847 23.585  14.819 1.00 47.56  ? 323 HOH   A O   1 
HETATM 1141 O  O   . HOH   D 4 .   ? 15.011 24.360  26.050 1.00 42.63  ? 324 HOH   A O   1 
HETATM 1142 O  O   . HOH   D 4 .   ? 12.195 7.423   30.877 1.00 126.25 ? 325 HOH   A O   1 
HETATM 1143 O  O   . HOH   D 4 .   ? 11.205 12.035  11.518 1.00 21.04  ? 326 HOH   A O   1 
HETATM 1144 O  O   . HOH   D 4 .   ? 5.574  -5.808  7.228  1.00 45.26  ? 327 HOH   A O   1 
HETATM 1145 O  O   . HOH   D 4 .   ? 10.692 18.057  5.772  1.00 52.07  ? 328 HOH   A O   1 
HETATM 1146 O  O   . HOH   D 4 .   ? 16.639 13.717  26.250 1.00 40.25  ? 329 HOH   A O   1 
HETATM 1147 O  O   . HOH   D 4 .   ? 14.440 21.408  8.124  1.00 51.25  ? 330 HOH   A O   1 
HETATM 1148 O  O   . HOH   D 4 .   ? 10.316 -4.381  31.695 1.00 51.34  ? 331 HOH   A O   1 
HETATM 1149 O  O   . HOH   D 4 .   ? 4.770  7.832   28.349 1.00 36.79  ? 332 HOH   A O   1 
HETATM 1150 O  O   . HOH   D 4 .   ? 7.993  -8.383  23.405 1.00 34.78  ? 333 HOH   A O   1 
HETATM 1151 O  O   . HOH   D 4 .   ? 17.752 21.547  9.528  1.00 29.79  ? 334 HOH   A O   1 
HETATM 1152 O  O   . HOH   D 4 .   ? 3.949  7.955   3.245  1.00 35.59  ? 335 HOH   A O   1 
HETATM 1153 O  O   . HOH   D 4 .   ? 18.668 19.628  5.279  1.00 42.83  ? 336 HOH   A O   1 
HETATM 1154 O  O   . HOH   D 4 .   ? 7.799  19.702  18.517 1.00 24.43  ? 337 HOH   A O   1 
HETATM 1155 O  O   . HOH   D 4 .   ? 14.992 12.814  24.141 1.00 24.85  ? 338 HOH   A O   1 
HETATM 1156 O  O   . HOH   D 4 .   ? 25.876 4.428   20.053 1.00 43.96  ? 339 HOH   A O   1 
HETATM 1157 O  O   . HOH   D 4 .   ? 14.918 -3.432  17.532 1.00 29.70  ? 340 HOH   A O   1 
HETATM 1158 O  O   . HOH   D 4 .   ? 23.993 12.287  23.154 1.00 47.22  ? 341 HOH   A O   1 
HETATM 1159 O  O   . HOH   D 4 .   ? 14.611 2.959   23.202 1.00 22.72  ? 342 HOH   A O   1 
HETATM 1160 O  O   . HOH   D 4 .   ? 2.655  3.492   27.938 1.00 36.91  ? 343 HOH   A O   1 
HETATM 1161 O  O   . HOH   D 4 .   ? 20.137 2.180   18.425 1.00 33.15  ? 344 HOH   A O   1 
HETATM 1162 O  O   . HOH   D 4 .   ? 11.076 2.526   33.470 1.00 22.69  ? 345 HOH   A O   1 
HETATM 1163 O  O   . HOH   D 4 .   ? 31.442 9.487   5.802  1.00 43.83  ? 346 HOH   A O   1 
HETATM 1164 O  O   . HOH   D 4 .   ? 20.472 23.722  10.891 1.00 39.67  ? 347 HOH   A O   1 
HETATM 1165 O  O   . HOH   D 4 .   ? 0.496  0.007   16.578 1.00 23.08  ? 348 HOH   A O   1 
HETATM 1166 O  O   . HOH   D 4 .   ? 34.462 5.667   13.883 1.00 52.62  ? 349 HOH   A O   1 
HETATM 1167 O  O   . HOH   D 4 .   ? 28.014 16.978  3.408  1.00 53.80  ? 350 HOH   A O   1 
HETATM 1168 O  O   . HOH   D 4 .   ? 9.428  18.518  20.469 1.00 24.89  ? 351 HOH   A O   1 
HETATM 1169 O  O   . HOH   D 4 .   ? 8.475  -3.662  0.365  1.00 27.82  ? 352 HOH   A O   1 
HETATM 1170 O  O   . HOH   D 4 .   ? 18.137 -3.162  19.467 1.00 50.22  ? 353 HOH   A O   1 
HETATM 1171 O  O   . HOH   D 4 .   ? 9.641  4.877   33.870 1.00 30.23  ? 354 HOH   A O   1 
HETATM 1172 O  O   . HOH   D 4 .   ? 0.591  -2.362  19.976 1.00 34.38  ? 355 HOH   A O   1 
HETATM 1173 O  O   . HOH   D 4 .   ? 7.272  7.918   32.740 1.00 39.04  ? 356 HOH   A O   1 
HETATM 1174 O  O   . HOH   D 4 .   ? 0.888  14.520  22.162 1.00 48.69  ? 357 HOH   A O   1 
HETATM 1175 O  O   . HOH   D 4 .   ? 6.831  16.568  22.559 1.00 32.38  ? 358 HOH   A O   1 
HETATM 1176 O  O   . HOH   D 4 .   ? 31.108 18.890  8.440  1.00 40.92  ? 359 HOH   A O   1 
HETATM 1177 O  O   . HOH   D 4 .   ? 23.252 0.448   15.922 1.00 33.39  ? 360 HOH   A O   1 
HETATM 1178 O  O   . HOH   D 4 .   ? 13.800 -6.910  30.395 1.00 51.63  ? 361 HOH   A O   1 
HETATM 1179 O  O   . HOH   D 4 .   ? 6.986  3.903   32.742 1.00 29.66  ? 362 HOH   A O   1 
HETATM 1180 O  O   . HOH   D 4 .   ? 21.708 -4.379  12.793 1.00 39.37  ? 363 HOH   A O   1 
HETATM 1181 O  O   . HOH   D 4 .   ? 20.470 -3.854  16.739 1.00 54.45  ? 364 HOH   A O   1 
HETATM 1182 O  O   . HOH   D 4 .   ? 5.248  14.464  22.395 1.00 30.86  ? 365 HOH   A O   1 
HETATM 1183 O  O   . HOH   D 4 .   ? 8.709  3.127   2.670  1.00 27.07  ? 366 HOH   A O   1 
HETATM 1184 O  O   . HOH   D 4 .   ? 30.579 10.977  14.492 1.00 57.64  ? 367 HOH   A O   1 
HETATM 1185 O  O   . HOH   D 4 .   ? 5.075  -1.255  24.154 1.00 24.77  ? 368 HOH   A O   1 
HETATM 1186 O  O   . HOH   D 4 .   ? 11.583 15.671  26.689 1.00 43.21  ? 369 HOH   A O   1 
HETATM 1187 O  O   . HOH   D 4 .   ? 24.430 11.157  20.963 1.00 42.95  ? 370 HOH   A O   1 
HETATM 1188 O  O   . HOH   D 4 .   ? 3.248  -2.846  3.412  1.00 49.53  ? 371 HOH   A O   1 
HETATM 1189 O  O   . HOH   D 4 .   ? 6.699  17.394  25.311 1.00 38.02  ? 372 HOH   A O   1 
HETATM 1190 O  O   . HOH   D 4 .   ? 15.243 10.189  24.705 1.00 21.94  ? 373 HOH   A O   1 
HETATM 1191 O  O   . HOH   D 4 .   ? 3.383  0.779   30.448 1.00 45.84  ? 374 HOH   A O   1 
HETATM 1192 O  O   . HOH   D 4 .   ? 0.017  4.263   6.488  1.00 41.20  ? 375 HOH   A O   1 
HETATM 1193 O  O   . HOH   D 4 .   ? 21.694 19.422  18.106 1.00 49.35  ? 376 HOH   A O   1 
HETATM 1194 O  O   . HOH   D 4 .   ? 29.965 5.168   3.738  1.00 41.50  ? 377 HOH   A O   1 
HETATM 1195 O  O   . HOH   D 4 .   ? 11.876 21.474  13.078 1.00 32.12  ? 378 HOH   A O   1 
HETATM 1196 O  O   . HOH   D 4 .   ? 31.214 14.294  22.555 1.00 44.06  ? 379 HOH   A O   1 
HETATM 1197 O  O   . HOH   D 4 .   ? 17.514 2.840   23.129 1.00 26.62  ? 380 HOH   A O   1 
HETATM 1198 O  O   . HOH   D 4 .   ? 10.613 9.357   31.270 1.00 31.14  ? 381 HOH   A O   1 
HETATM 1199 O  O   . HOH   D 4 .   ? 17.789 19.286  17.165 1.00 23.01  ? 382 HOH   A O   1 
HETATM 1200 O  O   . HOH   D 4 .   ? 24.702 -6.765  10.829 1.00 55.94  ? 383 HOH   A O   1 
HETATM 1201 O  O   . HOH   D 4 .   ? 17.056 20.545  19.609 1.00 32.49  ? 384 HOH   A O   1 
HETATM 1202 O  O   . HOH   D 4 .   ? 13.149 -8.116  24.484 1.00 28.05  ? 385 HOH   A O   1 
HETATM 1203 O  O   . HOH   D 4 .   ? 12.932 10.965  9.406  1.00 19.69  ? 386 HOH   A O   1 
HETATM 1204 O  O   . HOH   D 4 .   ? 3.902  -4.665  6.149  1.00 34.61  ? 387 HOH   A O   1 
HETATM 1205 O  O   . HOH   D 4 .   ? 28.258 -1.361  13.479 1.00 44.37  ? 388 HOH   A O   1 
HETATM 1206 O  O   . HOH   D 4 .   ? 6.749  -3.465  -1.657 1.00 52.30  ? 389 HOH   A O   1 
HETATM 1207 O  O   . HOH   D 4 .   ? 2.679  22.035  22.484 1.00 38.45  ? 390 HOH   A O   1 
HETATM 1208 O  O   . HOH   D 4 .   ? -1.142 10.915  23.511 1.00 39.44  ? 391 HOH   A O   1 
HETATM 1209 O  O   . HOH   D 4 .   ? 23.304 16.800  22.892 1.00 49.86  ? 392 HOH   A O   1 
HETATM 1210 O  O   . HOH   D 4 .   ? 5.656  22.943  11.414 1.00 36.57  ? 393 HOH   A O   1 
HETATM 1211 O  O   . HOH   D 4 .   ? 6.600  -7.753  14.284 1.00 33.21  ? 394 HOH   A O   1 
HETATM 1212 O  O   . HOH   D 4 .   ? 14.381 14.997  3.783  1.00 31.99  ? 395 HOH   A O   1 
HETATM 1213 O  O   . HOH   D 4 .   ? 27.225 -0.956  6.536  1.00 44.64  ? 396 HOH   A O   1 
HETATM 1214 O  O   . HOH   D 4 .   ? 18.388 13.100  1.642  1.00 48.45  ? 397 HOH   A O   1 
HETATM 1215 O  O   . HOH   D 4 .   ? -0.798 15.442  13.294 1.00 35.01  ? 398 HOH   A O   1 
HETATM 1216 O  O   . HOH   D 4 .   ? 6.538  13.405  5.629  1.00 29.91  ? 399 HOH   A O   1 
HETATM 1217 O  O   . HOH   D 4 .   ? 18.172 9.431   25.827 1.00 31.63  ? 400 HOH   A O   1 
HETATM 1218 O  O   . HOH   D 4 .   ? 30.842 -3.088  7.179  1.00 49.74  ? 401 HOH   A O   1 
HETATM 1219 O  O   . HOH   D 4 .   ? 0.220  1.419   24.192 1.00 29.64  ? 402 HOH   A O   1 
HETATM 1220 O  O   . HOH   D 4 .   ? 4.252  11.472  19.227 1.00 35.49  ? 403 HOH   A O   1 
HETATM 1221 O  O   . HOH   D 4 .   ? 20.846 -4.226  10.232 1.00 39.26  ? 404 HOH   A O   1 
HETATM 1222 O  O   . HOH   D 4 .   ? 15.679 -3.932  1.454  1.00 26.94  ? 405 HOH   A O   1 
HETATM 1223 O  O   . HOH   D 4 .   ? 23.626 2.898   19.608 1.00 35.69  ? 406 HOH   A O   1 
HETATM 1224 O  O   . HOH   D 4 .   ? 18.226 4.877   26.651 1.00 41.16  ? 407 HOH   A O   1 
HETATM 1225 O  O   . HOH   D 4 .   ? 3.693  5.310   25.473 1.00 31.22  ? 408 HOH   A O   1 
HETATM 1226 O  O   . HOH   D 4 .   ? 2.151  13.855  5.280  1.00 36.96  ? 409 HOH   A O   1 
HETATM 1227 O  O   . HOH   D 4 .   ? 5.806  26.025  20.983 1.00 31.94  ? 410 HOH   A O   1 
HETATM 1228 O  O   . HOH   D 4 .   ? 8.505  15.324  26.422 1.00 30.85  ? 411 HOH   A O   1 
HETATM 1229 O  O   . HOH   D 4 .   ? 21.669 9.123   21.272 1.00 34.24  ? 412 HOH   A O   1 
HETATM 1230 O  O   . HOH   D 4 .   ? 24.642 9.467   -3.461 1.00 62.21  ? 413 HOH   A O   1 
HETATM 1231 O  O   . HOH   D 4 .   ? 30.682 3.397   12.349 1.00 40.59  ? 414 HOH   A O   1 
HETATM 1232 O  O   . HOH   D 4 .   ? 31.751 2.897   3.146  1.00 54.14  ? 415 HOH   A O   1 
HETATM 1233 O  O   . HOH   D 4 .   ? 25.487 -2.385  5.415  1.00 53.06  ? 416 HOH   A O   1 
HETATM 1234 O  O   . HOH   D 4 .   ? 36.696 0.161   8.981  1.00 58.15  ? 417 HOH   A O   1 
HETATM 1235 O  O   . HOH   D 4 .   ? 9.087  -7.429  7.967  1.00 41.53  ? 418 HOH   A O   1 
HETATM 1236 O  O   . HOH   D 4 .   ? 35.905 14.876  15.974 1.00 54.41  ? 419 HOH   A O   1 
HETATM 1237 O  O   . HOH   D 4 .   ? 18.288 -0.135  19.709 1.00 27.77  ? 420 HOH   A O   1 
HETATM 1238 O  O   . HOH   D 4 .   ? 7.876  -5.221  31.397 1.00 78.42  ? 421 HOH   A O   1 
HETATM 1239 O  O   . HOH   D 4 .   ? 25.950 -1.918  14.643 1.00 48.84  ? 422 HOH   A O   1 
HETATM 1240 O  O   . HOH   D 4 .   ? 3.201  15.034  20.572 1.00 31.34  ? 423 HOH   A O   1 
HETATM 1241 O  O   . HOH   D 4 .   ? 13.679 -10.672 3.274  1.00 51.81  ? 424 HOH   A O   1 
HETATM 1242 O  O   . HOH   D 4 .   ? 2.091  6.058   28.136 1.00 35.32  ? 425 HOH   A O   1 
HETATM 1243 O  O   . HOH   D 4 .   ? 24.259 7.550   20.658 1.00 50.79  ? 426 HOH   A O   1 
HETATM 1244 O  O   . HOH   D 4 .   ? 14.997 -8.116  26.513 1.00 47.73  ? 427 HOH   A O   1 
HETATM 1245 O  O   . HOH   D 4 .   ? 27.893 17.867  23.259 1.00 47.02  ? 428 HOH   A O   1 
HETATM 1246 O  O   . HOH   D 4 .   ? 22.236 19.284  5.701  1.00 32.12  ? 429 HOH   A O   1 
HETATM 1247 O  O   . HOH   D 4 .   ? 1.219  -2.416  17.415 1.00 32.80  ? 430 HOH   A O   1 
HETATM 1248 O  O   . HOH   D 4 .   ? 0.600  -2.665  9.477  1.00 40.79  ? 431 HOH   A O   1 
HETATM 1249 O  O   . HOH   D 4 .   ? 18.177 -4.591  27.890 1.00 57.44  ? 432 HOH   A O   1 
HETATM 1250 O  O   . HOH   D 4 .   ? 6.928  11.219  3.980  1.00 42.53  ? 433 HOH   A O   1 
HETATM 1251 O  O   . HOH   D 4 .   ? 34.897 11.303  12.218 1.00 51.35  ? 434 HOH   A O   1 
HETATM 1252 O  O   . HOH   D 4 .   ? 5.359  2.336   7.141  1.00 36.97  ? 435 HOH   A O   1 
HETATM 1253 O  O   . HOH   D 4 .   ? 4.443  -1.234  28.959 1.00 68.78  ? 436 HOH   A O   1 
HETATM 1254 O  O   . HOH   D 4 .   ? 2.951  13.137  18.316 1.00 45.24  ? 437 HOH   A O   1 
HETATM 1255 O  O   . HOH   D 4 .   ? 32.312 14.772  7.088  1.00 47.73  ? 438 HOH   A O   1 
HETATM 1256 O  O   . HOH   D 4 .   ? 34.763 8.220   14.662 1.00 65.35  ? 439 HOH   A O   1 
HETATM 1257 O  O   . HOH   D 4 .   ? 18.851 -7.048  7.065  1.00 47.48  ? 440 HOH   A O   1 
HETATM 1258 O  O   . HOH   D 4 .   ? 23.986 17.202  2.547  1.00 52.83  ? 441 HOH   A O   1 
HETATM 1259 O  O   . HOH   D 4 .   ? 30.181 11.395  18.142 1.00 51.47  ? 442 HOH   A O   1 
HETATM 1260 O  O   . HOH   D 4 .   ? 3.131  14.022  23.757 1.00 50.68  ? 443 HOH   A O   1 
HETATM 1261 O  O   . HOH   D 4 .   ? 36.683 17.077  13.389 1.00 48.63  ? 444 HOH   A O   1 
HETATM 1262 O  O   . HOH   D 4 .   ? 2.407  -6.329  14.967 1.00 53.76  ? 445 HOH   A O   1 
HETATM 1263 O  O   . HOH   D 4 .   ? 29.597 11.003  20.589 1.00 63.59  ? 446 HOH   A O   1 
HETATM 1264 O  O   . HOH   D 4 .   ? 18.644 -4.930  12.073 1.00 55.52  ? 447 HOH   A O   1 
HETATM 1265 O  O   . HOH   D 4 .   ? 17.462 21.297  26.094 1.00 54.21  ? 448 HOH   A O   1 
HETATM 1266 O  O   . HOH   D 4 .   ? 21.370 -1.968  33.157 1.00 51.16  ? 449 HOH   A O   1 
HETATM 1267 O  O   . HOH   D 4 .   ? 19.050 9.504   -2.005 1.00 43.51  ? 450 HOH   A O   1 
HETATM 1268 O  O   . HOH   D 4 .   ? 10.498 10.479  0.726  1.00 53.53  ? 451 HOH   A O   1 
HETATM 1269 O  O   . HOH   D 4 .   ? 17.011 11.659  0.220  1.00 52.73  ? 452 HOH   A O   1 
HETATM 1270 O  O   . HOH   D 4 .   ? 25.878 10.791  -1.387 1.00 49.18  ? 453 HOH   A O   1 
HETATM 1271 O  O   . HOH   D 4 .   ? 7.552  -5.192  2.527  1.00 32.81  ? 454 HOH   A O   1 
HETATM 1272 O  O   . HOH   D 4 .   ? 18.617 8.260   28.529 1.00 35.03  ? 455 HOH   A O   1 
HETATM 1273 O  O   . HOH   D 4 .   ? 24.856 -0.704  3.290  1.00 66.15  ? 456 HOH   A O   1 
HETATM 1274 O  O   . HOH   D 4 .   ? 27.855 1.022   2.593  1.00 57.57  ? 457 HOH   A O   1 
HETATM 1275 O  O   . HOH   D 4 .   ? 1.727  1.505   26.587 1.00 35.68  ? 458 HOH   A O   1 
HETATM 1276 O  O   . HOH   D 4 .   ? 18.019 -6.606  34.589 1.00 53.39  ? 459 HOH   A O   1 
HETATM 1277 O  O   . HOH   D 4 .   ? 30.955 0.567   14.289 1.00 58.24  ? 460 HOH   A O   1 
HETATM 1278 O  O   . HOH   D 4 .   ? 8.224  -7.762  1.136  1.00 55.38  ? 461 HOH   A O   1 
HETATM 1279 O  O   . HOH   D 4 .   ? 3.660  -2.718  22.302 1.00 49.34  ? 462 HOH   A O   1 
HETATM 1280 O  O   . HOH   D 4 .   ? 36.811 18.410  22.473 1.00 54.09  ? 463 HOH   A O   1 
HETATM 1281 O  O   . HOH   D 4 .   ? 11.540 23.609  14.770 1.00 30.00  ? 464 HOH   A O   1 
HETATM 1282 O  O   . HOH   D 4 .   ? 19.951 15.451  0.618  1.00 43.94  ? 465 HOH   A O   1 
HETATM 1283 O  O   . HOH   D 4 .   ? 19.115 13.184  27.062 1.00 38.11  ? 466 HOH   A O   1 
HETATM 1284 O  O   . HOH   D 4 .   ? -2.425 20.324  25.051 1.00 59.33  ? 467 HOH   A O   1 
HETATM 1285 O  O   . HOH   D 4 .   ? 30.011 2.505   18.621 1.00 69.99  ? 468 HOH   A O   1 
HETATM 1286 O  O   . HOH   D 4 .   ? 2.541  10.340  28.296 1.00 45.29  ? 469 HOH   A O   1 
HETATM 1287 O  O   . HOH   D 4 .   ? 30.851 6.632   16.755 1.00 46.85  ? 470 HOH   A O   1 
HETATM 1288 O  O   . HOH   D 4 .   ? 4.621  -4.998  3.371  1.00 48.05  ? 471 HOH   A O   1 
HETATM 1289 O  O   . HOH   D 4 .   ? 8.449  19.917  6.681  1.00 48.15  ? 472 HOH   A O   1 
HETATM 1290 O  O   . HOH   D 4 .   ? 0.715  -1.499  23.558 1.00 40.20  ? 473 HOH   A O   1 
HETATM 1291 O  O   . HOH   D 4 .   ? 37.781 6.225   5.982  1.00 58.74  ? 474 HOH   A O   1 
HETATM 1292 O  O   . HOH   D 4 .   ? 20.708 -4.440  34.172 1.00 57.28  ? 475 HOH   A O   1 
HETATM 1293 O  O   . HOH   D 4 .   ? 8.574  7.527   2.596  1.00 34.73  ? 476 HOH   A O   1 
HETATM 1294 O  O   . HOH   D 4 .   ? 13.751 24.714  15.819 1.00 39.61  ? 477 HOH   A O   1 
HETATM 1295 O  O   . HOH   D 4 .   ? 6.076  3.282   3.016  1.00 38.22  ? 478 HOH   A O   1 
HETATM 1296 O  O   . HOH   D 4 .   ? 5.743  6.297   2.425  1.00 44.16  ? 479 HOH   A O   1 
HETATM 1297 O  O   . HOH   D 4 .   ? 3.278  -1.740  26.656 1.00 65.74  ? 480 HOH   A O   1 
HETATM 1298 O  O   . HOH   D 4 .   ? 5.178  7.156   31.117 1.00 43.25  ? 481 HOH   A O   1 
HETATM 1299 O  O   . HOH   D 4 .   ? 33.365 19.023  7.003  1.00 79.57  ? 482 HOH   A O   1 
HETATM 1300 O  O   . HOH   D 4 .   ? 31.780 4.898   14.875 1.00 48.90  ? 483 HOH   A O   1 
HETATM 1301 O  O   . HOH   D 4 .   ? 37.535 19.015  18.109 1.00 69.26  ? 484 HOH   A O   1 
HETATM 1302 O  O   . HOH   D 4 .   ? 0.390  12.312  18.609 1.00 70.19  ? 485 HOH   A O   1 
HETATM 1303 O  O   . HOH   D 4 .   ? 15.575 -6.301  0.326  1.00 49.33  ? 486 HOH   A O   1 
HETATM 1304 O  O   . HOH   D 4 .   ? 20.342 10.698  26.126 1.00 33.76  ? 487 HOH   A O   1 
HETATM 1305 O  O   . HOH   D 4 .   ? 16.560 -7.174  31.514 1.00 56.61  ? 488 HOH   A O   1 
HETATM 1306 O  O   . HOH   D 4 .   ? 22.151 10.361  23.851 1.00 35.03  ? 489 HOH   A O   1 
HETATM 1307 O  O   . HOH   D 4 .   ? 25.053 15.877  24.673 1.00 53.60  ? 490 HOH   A O   1 
HETATM 1308 O  O   . HOH   D 4 .   ? 3.346  -6.809  22.682 1.00 45.05  ? 491 HOH   A O   1 
HETATM 1309 O  O   . HOH   D 4 .   ? 2.873  -4.587  27.538 1.00 80.04  ? 492 HOH   A O   1 
HETATM 1310 O  O   . HOH   D 4 .   ? 7.128  14.559  28.619 1.00 48.72  ? 493 HOH   A O   1 
HETATM 1311 O  O   . HOH   D 4 .   ? 20.645 12.099  -2.615 1.00 52.04  ? 494 HOH   A O   1 
HETATM 1312 O  O   . HOH   D 4 .   ? 5.500  -7.962  23.653 1.00 54.35  ? 495 HOH   A O   1 
HETATM 1313 O  O   . HOH   D 4 .   ? 5.794  11.346  29.672 1.00 55.09  ? 496 HOH   A O   1 
HETATM 1314 O  O   . HOH   D 4 .   ? 39.157 0.343   7.894  1.00 91.37  ? 497 HOH   A O   1 
HETATM 1315 O  O   . HOH   D 4 .   ? 3.133  22.297  7.318  1.00 61.24  ? 498 HOH   A O   1 
HETATM 1316 O  O   . HOH   D 4 .   ? 0.649  28.910  18.313 1.00 87.96  ? 499 HOH   A O   1 
HETATM 1317 O  O   . HOH   D 4 .   ? 41.506 -4.374  4.366  1.00 72.97  ? 500 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   ? 0.4287 0.3291 0.3679 0.0236  -0.0519 -0.0439 7   SER   A N   
2    C CA  . SER   A 1   ? 0.4130 0.3253 0.3849 0.0226  -0.0571 -0.0525 7   SER   A CA  
3    C C   . SER   A 1   ? 0.3975 0.3194 0.3857 0.0204  -0.0542 -0.0503 7   SER   A C   
4    O O   . SER   A 1   ? 0.4084 0.3247 0.3813 0.0214  -0.0546 -0.0435 7   SER   A O   
5    C CB  . SER   A 1   ? 0.4554 0.3586 0.4301 0.0274  -0.0763 -0.0619 7   SER   A CB  
6    O OG  . SER   A 1   ? 0.5263 0.4152 0.4800 0.0318  -0.0881 -0.0582 7   SER   A OG  
7    N N   . GLY   A 2   ? 0.3608 0.2956 0.3786 0.0168  -0.0492 -0.0561 8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.3392 0.2820 0.3726 0.0140  -0.0447 -0.0558 8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.3249 0.2788 0.3791 0.0075  -0.0307 -0.0587 8   GLY   A C   
10   O O   . GLY   A 2   ? 0.3131 0.2685 0.3637 0.0047  -0.0215 -0.0567 8   GLY   A O   
11   N N   . ALA   A 3   ? 0.3057 0.2652 0.3800 0.0049  -0.0281 -0.0632 9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.3048 0.2707 0.3950 -0.0021 -0.0132 -0.0667 9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.3032 0.2717 0.3972 -0.0058 -0.0068 -0.0658 9   ALA   A C   
14   O O   . ALA   A 3   ? 0.3133 0.2802 0.4055 -0.0022 -0.0154 -0.0645 9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.3005 0.2699 0.4230 -0.0030 -0.0143 -0.0800 9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.2920 0.2618 0.3876 -0.0130 0.0088  -0.0659 10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.2848 0.2553 0.3840 -0.0180 0.0174  -0.0673 10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.3110 0.2837 0.4426 -0.0223 0.0261  -0.0808 10  ILE   A C   
19   O O   . ILE   A 4   ? 0.3137 0.2853 0.4536 -0.0254 0.0337  -0.0850 10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.2819 0.2486 0.3562 -0.0238 0.0288  -0.0587 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.2776 0.2437 0.3266 -0.0202 0.0220  -0.0469 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.2902 0.2552 0.3656 -0.0297 0.0378  -0.0616 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.2650 0.2272 0.2937 -0.0249 0.0304  -0.0394 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.3171 0.2923 0.4696 -0.0227 0.0261  -0.0883 11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.3224 0.3003 0.5107 -0.0271 0.0361  -0.1025 11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.3308 0.3050 0.5168 -0.0348 0.0526  -0.1048 11  TYR   A C   
27   O O   . TYR   A 5   ? 0.3378 0.3134 0.5286 -0.0328 0.0480  -0.1056 11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.3089 0.2930 0.5328 -0.0198 0.0201  -0.1126 11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.3276 0.3128 0.5529 -0.0130 0.0036  -0.1125 11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.3283 0.3164 0.5765 -0.0152 0.0075  -0.1218 11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.3529 0.3342 0.5548 -0.0051 -0.0147 -0.1036 11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.3407 0.3285 0.5880 -0.0094 -0.0078 -0.1223 11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.3709 0.3500 0.5684 0.0005  -0.0288 -0.1037 11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.3650 0.3479 0.5861 -0.0014 -0.0264 -0.1136 11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.4029 0.3828 0.6184 0.0038  -0.0409 -0.1146 11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.3423 0.3089 0.5154 -0.0436 0.0716  -0.1047 12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.3505 0.3090 0.5131 -0.0523 0.0892  -0.1069 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.3638 0.3168 0.5484 -0.0609 0.1106  -0.1195 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.3642 0.3127 0.5461 -0.0634 0.1171  -0.1191 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.3820 0.3309 0.4972 -0.0556 0.0917  -0.0930 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.3871 0.3309 0.4839 -0.0557 0.0926  -0.0856 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.3977 0.3346 0.4967 -0.0652 0.1092  -0.0959 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.3641 0.3172 0.5748 -0.0651 0.1220  -0.1317 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.3745 0.3225 0.6124 -0.0737 0.1447  -0.1459 13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.3828 0.3399 0.6571 -0.0703 0.1396  -0.1536 13  GLY   A C   
46   O O   . GLY   A 7   ? 0.3795 0.3502 0.6794 -0.0606 0.1180  -0.1557 13  GLY   A O   
47   N N   . ASN   A 8   ? 0.3858 0.3333 0.6572 -0.0779 0.1575  -0.1562 14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.3749 0.3304 0.6800 -0.0754 0.1529  -0.1637 14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.3723 0.3239 0.6426 -0.0718 0.1425  -0.1496 14  ASN   A C   
50   O O   . ASN   A 8   ? 0.3722 0.3190 0.6489 -0.0756 0.1518  -0.1525 14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.3931 0.3430 0.7328 -0.0859 0.1799  -0.1799 14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.4527 0.4118 0.8432 -0.0870 0.1860  -0.1972 14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.4606 0.4360 0.9040 -0.0810 0.1728  -0.2095 14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.4724 0.4207 0.8482 -0.0944 0.2046  -0.1988 14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.3630 0.3167 0.5996 -0.0645 0.1240  -0.1352 15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.3583 0.3087 0.5631 -0.0606 0.1144  -0.1219 15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.3256 0.2878 0.5295 -0.0489 0.0875  -0.1161 15  TYR   A C   
58   O O   . TYR   A 9   ? 0.3207 0.2886 0.5275 -0.0446 0.0770  -0.1157 15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.3830 0.3189 0.5376 -0.0649 0.1223  -0.1078 15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.4166 0.3341 0.5579 -0.0765 0.1483  -0.1104 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.4342 0.3435 0.5852 -0.0815 0.1620  -0.1151 15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.4428 0.3481 0.5581 -0.0829 0.1596  -0.1081 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.4629 0.3507 0.5968 -0.0927 0.1875  -0.1168 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.4765 0.3601 0.5727 -0.0940 0.1841  -0.1102 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.4990 0.3729 0.6034 -0.0990 0.1986  -0.1142 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.5602 0.4083 0.6415 -0.1106 0.2246  -0.1157 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.3099 0.2732 0.5076 -0.0444 0.0776  -0.1119 16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.3014 0.2710 0.4897 -0.0344 0.0549  -0.1056 16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.2942 0.2567 0.4443 -0.0339 0.0558  -0.0915 16  ARG   A C   
70   O O   . ARG   A 10  ? 0.2981 0.2549 0.4463 -0.0371 0.0646  -0.0915 16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.3086 0.2850 0.5284 -0.0293 0.0418  -0.1163 16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.3553 0.3318 0.5550 -0.0207 0.0222  -0.1089 16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.3709 0.3521 0.5998 -0.0156 0.0065  -0.1208 16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.4142 0.3914 0.6261 -0.0121 -0.0014 -0.1172 16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.4296 0.4034 0.6207 -0.0045 -0.0194 -0.1122 16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.4028 0.3760 0.5856 0.0006  -0.0316 -0.1088 16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.4540 0.4229 0.6304 -0.0024 -0.0238 -0.1105 16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.2775 0.2398 0.4002 -0.0302 0.0479  -0.0800 17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.2721 0.2291 0.3637 -0.0292 0.0479  -0.0674 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.2726 0.2335 0.3586 -0.0209 0.0321  -0.0638 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.2795 0.2440 0.3630 -0.0164 0.0211  -0.0624 17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.2802 0.2341 0.3465 -0.0314 0.0508  -0.0579 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.2910 0.2394 0.3304 -0.0304 0.0505  -0.0459 17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.2788 0.2266 0.3472 -0.0397 0.0655  -0.0628 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.2551 0.2131 0.3365 -0.0194 0.0320  -0.0620 18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.2750 0.2337 0.3479 -0.0124 0.0194  -0.0594 18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.2673 0.2215 0.3195 -0.0116 0.0234  -0.0496 18  VAL   A C   
88   O O   . VAL   A 12  ? 0.2803 0.2299 0.3275 -0.0158 0.0340  -0.0459 18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.3001 0.2598 0.3942 -0.0101 0.0121  -0.0708 18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.3284 0.2931 0.4461 -0.0089 0.0037  -0.0808 18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.3047 0.2613 0.4116 -0.0150 0.0239  -0.0758 18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.2683 0.2217 0.3077 -0.0060 0.0151  -0.0456 19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.2543 0.2039 0.2807 -0.0044 0.0190  -0.0387 19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.2670 0.2127 0.3056 -0.0061 0.0237  -0.0451 19  ASN   A C   
95   O O   . ASN   A 13  ? 0.2643 0.2106 0.3166 -0.0050 0.0177  -0.0550 19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.2589 0.2067 0.2725 0.0012  0.0113  -0.0365 19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.2606 0.2106 0.2622 0.0025  0.0084  -0.0300 19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.2885 0.2383 0.2901 0.0038  0.0012  -0.0331 19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.2615 0.2131 0.2546 0.0021  0.0134  -0.0213 19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.2678 0.2084 0.3020 -0.0084 0.0330  -0.0399 20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.2815 0.2164 0.3275 -0.0108 0.0395  -0.0457 20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.2894 0.2236 0.3385 -0.0065 0.0329  -0.0512 20  ARG   A C   
103  O O   . ARG   A 14  ? 0.2998 0.2333 0.3660 -0.0080 0.0323  -0.0618 20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.3007 0.2266 0.3358 -0.0129 0.0494  -0.0368 20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.3125 0.2291 0.3581 -0.0170 0.0595  -0.0416 20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.3339 0.2392 0.3631 -0.0166 0.0655  -0.0303 20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.3563 0.2485 0.3905 -0.0209 0.0770  -0.0323 20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.3901 0.2779 0.4315 -0.0187 0.0783  -0.0349 20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.3526 0.2481 0.3965 -0.0126 0.0693  -0.0368 20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.4263 0.3002 0.4711 -0.0231 0.0900  -0.0359 20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.2958 0.2298 0.3291 -0.0014 0.0278  -0.0454 21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.2979 0.2280 0.3283 0.0024  0.0227  -0.0506 21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.3107 0.2416 0.3459 0.0040  0.0105  -0.0609 21  HIS   A C   
114  O O   . HIS   A 15  ? 0.3246 0.2500 0.3580 0.0061  0.0052  -0.0678 21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.3045 0.2322 0.3172 0.0065  0.0237  -0.0425 21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.2903 0.2203 0.2896 0.0089  0.0178  -0.0389 21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.3020 0.2376 0.2980 0.0079  0.0197  -0.0307 21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.3048 0.2295 0.2908 0.0119  0.0109  -0.0422 21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.3255 0.2604 0.3095 0.0102  0.0151  -0.0293 21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.3161 0.2431 0.2916 0.0127  0.0100  -0.0356 21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.3047 0.2411 0.3463 0.0030  0.0053  -0.0625 22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.3250 0.2614 0.3732 0.0054  -0.0088 -0.0719 22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.3507 0.2932 0.4307 0.0017  -0.0093 -0.0828 22  LEU   A C   
124  O O   . LEU   A 16  ? 0.3644 0.3087 0.4561 0.0040  -0.0223 -0.0910 22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.3201 0.2564 0.3524 0.0085  -0.0161 -0.0659 22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.3441 0.2731 0.3473 0.0118  -0.0154 -0.0574 22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.3516 0.2784 0.3406 0.0140  -0.0220 -0.0526 22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.3558 0.2737 0.3461 0.0148  -0.0209 -0.0628 22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.3504 0.2949 0.4441 -0.0040 0.0052  -0.0826 23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.3481 0.2972 0.4734 -0.0090 0.0097  -0.0934 23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.3739 0.3230 0.5209 -0.0079 0.0005  -0.1074 23  ALA   A C   
132  O O   . ALA   A 17  ? 0.3845 0.3276 0.5209 -0.0061 -0.0011 -0.1075 23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.3391 0.2842 0.4662 -0.0157 0.0292  -0.0893 23  ALA   A CB  
134  N N   . THR   A 18  ? 0.3859 0.3416 0.5635 -0.0084 -0.0072 -0.1198 24  THR   A N   
135  C CA  . THR   A 18  ? 0.4122 0.3694 0.6173 -0.0077 -0.0181 -0.1354 24  THR   A CA  
136  C C   . THR   A 18  ? 0.4234 0.3813 0.6568 -0.0157 0.0000  -0.1431 24  THR   A C   
137  O O   . THR   A 18  ? 0.4257 0.3820 0.6569 -0.0216 0.0194  -0.1368 24  THR   A O   
138  C CB  . THR   A 18  ? 0.4312 0.3950 0.6599 -0.0040 -0.0359 -0.1453 24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.4447 0.4166 0.7022 -0.0093 -0.0235 -0.1493 24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.4467 0.4060 0.6443 0.0034  -0.0516 -0.1364 24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.4210 0.3791 0.6788 -0.0165 -0.0058 -0.1568 25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.4240 0.3811 0.7097 -0.0250 0.0134  -0.1645 25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.4067 0.3705 0.7264 -0.0316 0.0267  -0.1717 25  HIS   A C   
144  O O   . HIS   A 19  ? 0.4160 0.3741 0.7432 -0.0398 0.0499  -0.1712 25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.4448 0.4013 0.7535 -0.0250 0.0043  -0.1794 25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.4761 0.4431 0.8299 -0.0244 -0.0109 -0.1981 25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.4956 0.4670 0.8967 -0.0314 -0.0019 -0.2145 25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.4908 0.4638 0.8505 -0.0175 -0.0348 -0.2029 25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.4912 0.4730 0.9286 -0.0282 -0.0214 -0.2294 25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.4932 0.4757 0.9066 -0.0195 -0.0423 -0.2226 25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.3780 0.3513 0.7154 -0.0280 0.0129  -0.1776 26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.3732 0.3538 0.7439 -0.0329 0.0233  -0.1852 26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.3816 0.3567 0.7241 -0.0368 0.0418  -0.1710 26  ASN   A C   
154  O O   . ASN   A 20  ? 0.3735 0.3497 0.7380 -0.0439 0.0593  -0.1766 26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.3903 0.3811 0.7829 -0.0256 -0.0008 -0.1936 26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.4669 0.4631 0.8942 -0.0221 -0.0214 -0.2105 26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.4805 0.4788 0.9415 -0.0280 -0.0125 -0.2233 26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.4980 0.4951 0.9171 -0.0124 -0.0501 -0.2112 26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.3818 0.3511 0.6767 -0.0320 0.0370  -0.1537 27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.3695 0.3327 0.6348 -0.0354 0.0520  -0.1400 27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.3686 0.3196 0.6262 -0.0436 0.0752  -0.1366 27  ASP   A C   
162  O O   . ASP   A 21  ? 0.3735 0.3180 0.6278 -0.0507 0.0939  -0.1345 27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.3643 0.3249 0.5859 -0.0283 0.0403  -0.1239 27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.3741 0.3416 0.5925 -0.0216 0.0224  -0.1229 27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.3595 0.3319 0.5951 -0.0237 0.0255  -0.1273 27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.3603 0.3263 0.5573 -0.0145 0.0066  -0.1174 27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.3645 0.3101 0.6175 -0.0427 0.0744  -0.1363 28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.3815 0.3131 0.6275 -0.0497 0.0951  -0.1329 28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.3779 0.3075 0.6621 -0.0597 0.1142  -0.1474 28  TRP   A C   
170  O O   . TRP   A 22  ? 0.3867 0.3018 0.6588 -0.0677 0.1368  -0.1426 28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.3791 0.3065 0.6181 -0.0462 0.0887  -0.1318 28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.3867 0.3104 0.5851 -0.0392 0.0800  -0.1158 28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.3947 0.3251 0.5813 -0.0308 0.0605  -0.1138 28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.3995 0.3108 0.5650 -0.0402 0.0909  -0.0999 28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.4078 0.3323 0.5599 -0.0270 0.0606  -0.0985 28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.4108 0.3248 0.5510 -0.0321 0.0774  -0.0898 28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.4110 0.3071 0.5646 -0.0471 0.1103  -0.0934 28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.4287 0.3339 0.5387 -0.0303 0.0814  -0.0744 28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.4335 0.3184 0.5521 -0.0448 0.1123  -0.0771 28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.4397 0.3309 0.5397 -0.0362 0.0973  -0.0681 28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.3605 0.3034 0.6897 -0.0592 0.1051  -0.1650 29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.3767 0.3202 0.7501 -0.0687 0.1236  -0.1809 29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.3962 0.3364 0.7657 -0.0744 0.1402  -0.1788 29  ALA   A C   
184  O O   . ALA   A 23  ? 0.4170 0.3467 0.7995 -0.0850 0.1664  -0.1845 29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.3608 0.3218 0.7863 -0.0653 0.1056  -0.2006 29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.3779 0.3252 0.7284 -0.0678 0.1259  -0.1710 30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.3833 0.3280 0.7281 -0.0723 0.1388  -0.1692 30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.3935 0.3239 0.6804 -0.0725 0.1445  -0.1491 30  ASN   A C   
189  O O   . ASN   A 24  ? 0.3989 0.3299 0.6715 -0.0724 0.1450  -0.1445 30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.4026 0.3648 0.7723 -0.0653 0.1190  -0.1765 30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.4567 0.4322 0.8884 -0.0657 0.1138  -0.1979 30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.4797 0.4531 0.9461 -0.0751 0.1357  -0.2108 30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.4630 0.4507 0.9098 -0.0558 0.0849  -0.2026 30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.3848 0.3023 0.6406 -0.0726 0.1481  -0.1377 31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.3909 0.2947 0.5948 -0.0718 0.1506  -0.1190 31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.4023 0.2896 0.5869 -0.0812 0.1728  -0.1161 31  LEU   A C   
197  O O   . LEU   A 25  ? 0.4025 0.2771 0.6003 -0.0911 0.1958  -0.1242 31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.3842 0.2754 0.5668 -0.0709 0.1526  -0.1100 31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.4053 0.2819 0.5379 -0.0691 0.1526  -0.0908 31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.4097 0.3006 0.5274 -0.0589 0.1296  -0.0824 31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.4035 0.2644 0.5212 -0.0693 0.1583  -0.0837 31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.4010 0.2861 0.5514 -0.0786 0.1665  -0.1043 32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.4135 0.2800 0.5336 -0.0864 0.1835  -0.0989 32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.4379 0.2871 0.5071 -0.0842 0.1797  -0.0801 32  VAL   A C   
205  O O   . VAL   A 26  ? 0.4646 0.2885 0.5055 -0.0915 0.1967  -0.0746 32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.4203 0.2981 0.5436 -0.0850 0.1771  -0.1016 32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.4451 0.3022 0.5275 -0.0921 0.1909  -0.0940 32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.4063 0.2979 0.5814 -0.0876 0.1825  -0.1205 32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.4168 0.2786 0.4751 -0.0739 0.1572  -0.0705 33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.4247 0.2745 0.4430 -0.0701 0.1500  -0.0538 33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.4103 0.2774 0.4340 -0.0591 0.1286  -0.0488 33  TRP   A C   
212  O O   . TRP   A 27  ? 0.3913 0.2776 0.4343 -0.0544 0.1165  -0.0543 33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.4398 0.2809 0.4251 -0.0723 0.1497  -0.0459 33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.4555 0.2895 0.4054 -0.0668 0.1366  -0.0299 33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.4974 0.3064 0.4120 -0.0691 0.1414  -0.0190 33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.4440 0.2953 0.3918 -0.0582 0.1163  -0.0235 33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.5075 0.3190 0.4014 -0.0620 0.1237  -0.0068 33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.4708 0.3088 0.3863 -0.0555 0.1094  -0.0098 33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.4218 0.2966 0.3917 -0.0525 0.1037  -0.0282 33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.4606 0.3105 0.3701 -0.0482 0.0917  -0.0021 33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.4124 0.2964 0.3717 -0.0457 0.0880  -0.0196 33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.4316 0.3047 0.3639 -0.0437 0.0826  -0.0073 33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.4024 0.2606 0.4081 -0.0553 0.1246  -0.0384 34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.3890 0.2610 0.3974 -0.0455 0.1071  -0.0335 34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.4056 0.2656 0.3851 -0.0418 0.1025  -0.0188 34  GLU   A C   
226  O O   . GLU   A 28  ? 0.4374 0.2759 0.3985 -0.0460 0.1127  -0.0133 34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.3807 0.2618 0.4176 -0.0429 0.1047  -0.0431 34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.4134 0.2789 0.4553 -0.0476 0.1188  -0.0456 34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.4631 0.3167 0.4868 -0.0434 0.1169  -0.0346 34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.4637 0.2985 0.4824 -0.0482 0.1303  -0.0332 34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.4342 0.2962 0.4500 -0.0355 0.1031  -0.0274 34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.3776 0.2496 0.3531 -0.0341 0.0874  -0.0124 35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.3774 0.2412 0.3333 -0.0293 0.0809  0.0002  35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.3620 0.2415 0.3313 -0.0209 0.0694  0.0007  35  ASP   A C   
235  O O   . ASP   A 29  ? 0.3497 0.2439 0.3230 -0.0178 0.0607  -0.0001 35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.4050 0.2627 0.3362 -0.0308 0.0763  0.0085  35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.4772 0.3249 0.3891 -0.0258 0.0673  0.0213  35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.5014 0.3516 0.4229 -0.0196 0.0629  0.0243  35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.5021 0.3391 0.3900 -0.0279 0.0636  0.0279  35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.3574 0.2320 0.3331 -0.0177 0.0711  0.0012  36  SER   A N   
241  C CA  A SER   A 30  ? 0.3501 0.2357 0.3366 -0.0105 0.0633  0.0009  36  SER   A CA  
242  C CA  B SER   A 30  ? 0.3567 0.2432 0.3435 -0.0105 0.0630  0.0005  36  SER   A CA  
243  C C   . SER   A 30  ? 0.3522 0.2434 0.3301 -0.0050 0.0534  0.0103  36  SER   A C   
244  O O   . SER   A 30  ? 0.3529 0.2574 0.3383 -0.0009 0.0473  0.0084  36  SER   A O   
245  C CB  A SER   A 30  ? 0.3599 0.2347 0.3515 -0.0087 0.0685  0.0012  36  SER   A CB  
246  C CB  B SER   A 30  ? 0.3858 0.2644 0.3811 -0.0086 0.0679  -0.0014 36  SER   A CB  
247  O OG  A SER   A 30  ? 0.3656 0.2499 0.3675 -0.0025 0.0631  -0.0012 36  SER   A OG  
248  O OG  B SER   A 30  ? 0.4330 0.2994 0.4177 -0.0053 0.0673  0.0092  36  SER   A OG  
249  N N   . SER   A 31  ? 0.3572 0.2364 0.3186 -0.0053 0.0517  0.0202  37  SER   A N   
250  C CA  . SER   A 31  ? 0.3650 0.2501 0.3227 -0.0002 0.0407  0.0282  37  SER   A CA  
251  C C   . SER   A 31  ? 0.3407 0.2406 0.2992 -0.0015 0.0355  0.0257  37  SER   A C   
252  O O   . SER   A 31  ? 0.3553 0.2651 0.3191 0.0027  0.0277  0.0289  37  SER   A O   
253  C CB  . SER   A 31  ? 0.4218 0.2896 0.3603 0.0001  0.0366  0.0388  37  SER   A CB  
254  O OG  . SER   A 31  ? 0.4938 0.3540 0.4126 -0.0063 0.0376  0.0398  37  SER   A OG  
255  N N   . ARG   A 32  ? 0.3248 0.2256 0.2804 -0.0075 0.0404  0.0195  38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.3102 0.2236 0.2676 -0.0088 0.0363  0.0165  38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.3097 0.2353 0.2823 -0.0075 0.0366  0.0078  38  ARG   A C   
258  O O   . ARG   A 32  ? 0.3026 0.2375 0.2767 -0.0077 0.0326  0.0059  38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.3263 0.2318 0.2706 -0.0160 0.0410  0.0149  38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.3680 0.2582 0.2897 -0.0178 0.0387  0.0237  38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.3758 0.2557 0.2817 -0.0259 0.0459  0.0207  38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.3771 0.2703 0.2872 -0.0271 0.0414  0.0171  38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.3975 0.2833 0.2902 -0.0325 0.0422  0.0173  38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.4214 0.2849 0.2877 -0.0375 0.0473  0.0211  38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.3711 0.2693 0.2699 -0.0332 0.0379  0.0139  38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.2991 0.2231 0.2816 -0.0063 0.0405  0.0022  39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.2764 0.2079 0.2701 -0.0051 0.0389  -0.0068 39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.2768 0.2110 0.2750 -0.0098 0.0400  -0.0136 39  ASP   A C   
269  O O   . ASP   A 33  ? 0.2662 0.2076 0.2698 -0.0082 0.0345  -0.0183 39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.2810 0.2208 0.2743 0.0000  0.0325  -0.0056 39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.2616 0.2037 0.2597 0.0016  0.0294  -0.0143 39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.2477 0.1857 0.2530 0.0010  0.0311  -0.0210 39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.2680 0.2142 0.2616 0.0033  0.0246  -0.0145 39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.2850 0.2113 0.2812 -0.0158 0.0479  -0.0145 40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.2916 0.2206 0.2965 -0.0205 0.0510  -0.0224 40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.3032 0.2260 0.3224 -0.0254 0.0609  -0.0312 40  LEU   A C   
277  O O   . LEU   A 34  ? 0.3122 0.2236 0.3257 -0.0275 0.0688  -0.0284 40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.3079 0.2325 0.2978 -0.0250 0.0541  -0.0176 40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.3199 0.2525 0.3011 -0.0220 0.0447  -0.0118 40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.3229 0.2491 0.2890 -0.0274 0.0480  -0.0089 40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.3206 0.2646 0.3152 -0.0191 0.0382  -0.0179 40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.2946 0.2243 0.3341 -0.0269 0.0604  -0.0421 41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.3047 0.2308 0.3651 -0.0324 0.0707  -0.0530 41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.3042 0.2358 0.3801 -0.0360 0.0731  -0.0614 41  LEU   A C   
285  O O   . LEU   A 35  ? 0.3007 0.2422 0.3810 -0.0317 0.0616  -0.0626 41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.2983 0.2289 0.3787 -0.0289 0.0648  -0.0613 41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.3072 0.2347 0.4145 -0.0349 0.0758  -0.0738 41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.3056 0.2295 0.4194 -0.0332 0.0752  -0.0765 41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.3115 0.2505 0.4495 -0.0347 0.0694  -0.0872 41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.3027 0.2256 0.3843 -0.0442 0.0893  -0.0664 42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.3121 0.2393 0.4123 -0.0484 0.0948  -0.0760 42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.3252 0.2531 0.4611 -0.0530 0.1048  -0.0907 42  VAL   A C   
293  O O   . VAL   A 36  ? 0.3337 0.2493 0.4667 -0.0586 0.1192  -0.0911 42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.3500 0.2647 0.4251 -0.0552 0.1076  -0.0705 42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.3618 0.2787 0.4591 -0.0610 0.1178  -0.0825 42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.3631 0.2797 0.4089 -0.0506 0.0954  -0.0578 42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.3191 0.2602 0.4896 -0.0504 0.0966  -0.1029 43  SER   A N   
298  C CA  . SER   A 37  ? 0.3251 0.2691 0.5373 -0.0550 0.1054  -0.1192 43  SER   A CA  
299  C C   . SER   A 37  ? 0.3456 0.2933 0.5825 -0.0597 0.1147  -0.1297 43  SER   A C   
300  O O   . SER   A 37  ? 0.3369 0.2881 0.5623 -0.0571 0.1082  -0.1253 43  SER   A O   
301  C CB  . SER   A 37  ? 0.3246 0.2808 0.5637 -0.0476 0.0861  -0.1274 43  SER   A CB  
302  O OG  . SER   A 37  ? 0.3381 0.3040 0.5756 -0.0391 0.0649  -0.1256 43  SER   A OG  
303  N N   . SER   A 38  ? 0.3563 0.3028 0.6290 -0.0670 0.1312  -0.1442 44  SER   A N   
304  C CA  . SER   A 38  ? 0.3641 0.3142 0.6688 -0.0722 0.1430  -0.1572 44  SER   A CA  
305  C C   . SER   A 38  ? 0.3597 0.3292 0.7077 -0.0638 0.1209  -0.1686 44  SER   A C   
306  O O   . SER   A 38  ? 0.3612 0.3388 0.7252 -0.0574 0.1034  -0.1720 44  SER   A O   
307  C CB  . SER   A 38  ? 0.3793 0.3204 0.7103 -0.0834 0.1699  -0.1697 44  SER   A CB  
308  O OG  . SER   A 38  ? 0.4003 0.3498 0.7650 -0.0811 0.1621  -0.1789 44  SER   A OG  
309  N N   . THR   A 39  ? 0.3632 0.3385 0.7293 -0.0634 0.1209  -0.1746 45  THR   A N   
310  C CA  . THR   A 39  ? 0.3672 0.3585 0.7745 -0.0548 0.0988  -0.1851 45  THR   A CA  
311  C C   . THR   A 39  ? 0.3802 0.3774 0.8425 -0.0603 0.1135  -0.2042 45  THR   A C   
312  O O   . THR   A 39  ? 0.3923 0.3800 0.8482 -0.0700 0.1397  -0.2060 45  THR   A O   
313  C CB  . THR   A 39  ? 0.3750 0.3685 0.7543 -0.0463 0.0795  -0.1734 45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.3806 0.3697 0.7538 -0.0517 0.0951  -0.1732 45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.3882 0.3756 0.7145 -0.0417 0.0686  -0.1549 45  THR   A CG2 
316  N N   . THR   A 40  ? 0.3835 0.3952 0.8985 -0.0538 0.0955  -0.2186 46  THR   A N   
317  C CA  . THR   A 40  ? 0.3961 0.4155 0.9713 -0.0579 0.1077  -0.2382 46  THR   A CA  
318  C C   . THR   A 40  ? 0.4109 0.4315 0.9846 -0.0550 0.1053  -0.2366 46  THR   A C   
319  O O   . THR   A 40  ? 0.4148 0.4321 1.0066 -0.0634 0.1301  -0.2454 46  THR   A O   
320  C CB  . THR   A 40  ? 0.4067 0.4413 1.0434 -0.0517 0.0875  -0.2553 46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.4393 0.4785 1.0605 -0.0379 0.0507  -0.2473 46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.4070 0.4404 1.0584 -0.0578 0.0976  -0.2622 46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.4119 0.4354 0.9631 -0.0435 0.0768  -0.2257 47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.4120 0.4357 0.9597 -0.0400 0.0726  -0.2230 47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.4215 0.4324 0.9060 -0.0447 0.0850  -0.2054 47  ALA   A C   
326  O O   . ALA   A 41  ? 0.4272 0.4312 0.8658 -0.0451 0.0833  -0.1914 47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.4170 0.4471 0.9714 -0.0256 0.0363  -0.2201 47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.4139 0.4217 0.8979 -0.0477 0.0961  -0.2068 48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.4284 0.4243 0.8559 -0.0521 0.1059  -0.1919 48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.4067 0.4040 0.8027 -0.0415 0.0790  -0.1770 48  GLN   A C   
331  O O   . GLN   A 42  ? 0.4000 0.4043 0.8216 -0.0321 0.0584  -0.1806 48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.4628 0.4530 0.9014 -0.0608 0.1302  -0.2009 48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.5616 0.5363 0.9418 -0.0687 0.1457  -0.1885 48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.6520 0.6180 1.0419 -0.0788 0.1725  -0.1995 48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 0.6690 0.6375 1.1062 -0.0838 0.1894  -0.2170 48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.6816 0.6366 1.0281 -0.0825 0.1778  -0.1906 48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.3962 0.3855 0.7384 -0.0428 0.0793  -0.1606 49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.3856 0.3740 0.6931 -0.0350 0.0592  -0.1457 49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.3676 0.3509 0.6543 -0.0376 0.0651  -0.1405 49  GLY   A C   
340  O O   . GLY   A 43  ? 0.3760 0.3542 0.6647 -0.0466 0.0862  -0.1466 49  GLY   A O   
341  N N   . CYS   A 44  ? 0.3455 0.3286 0.6121 -0.0302 0.0473  -0.1301 50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.3357 0.3146 0.5882 -0.0322 0.0511  -0.1266 50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.3284 0.3021 0.5330 -0.0327 0.0476  -0.1107 50  CYS   A C   
344  O O   . CYS   A 44  ? 0.3340 0.3050 0.5281 -0.0330 0.0467  -0.1073 50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.3336 0.3157 0.6155 -0.0241 0.0362  -0.1319 50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.3415 0.3317 0.6890 -0.0225 0.0377  -0.1524 50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.3139 0.2866 0.4929 -0.0327 0.0456  -0.1017 51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.3216 0.2906 0.4610 -0.0333 0.0429  -0.0879 51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.3300 0.2922 0.4496 -0.0433 0.0605  -0.0877 51  ASP   A C   
350  O O   . ASP   A 45  ? 0.3441 0.3021 0.4700 -0.0497 0.0753  -0.0947 51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.3360 0.3058 0.4579 -0.0293 0.0347  -0.0792 51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.3780 0.3503 0.5084 -0.0196 0.0163  -0.0778 51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.3951 0.3662 0.5298 -0.0151 0.0069  -0.0773 51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.3845 0.3577 0.5151 -0.0167 0.0113  -0.0774 51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.3306 0.2898 0.4248 -0.0449 0.0587  -0.0798 52  THR   A N   
356  C CA  . THR   A 46  ? 0.3584 0.3088 0.4264 -0.0537 0.0710  -0.0781 52  THR   A CA  
357  C C   . THR   A 46  ? 0.3505 0.2997 0.3884 -0.0526 0.0643  -0.0655 52  THR   A C   
358  O O   . THR   A 46  ? 0.3504 0.3054 0.3842 -0.0467 0.0517  -0.0580 52  THR   A O   
359  C CB  . THR   A 46  ? 0.4017 0.3503 0.4666 -0.0562 0.0716  -0.0798 52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.4167 0.3654 0.5116 -0.0577 0.0800  -0.0926 52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.4286 0.3669 0.4605 -0.0646 0.0796  -0.0769 52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.3481 0.2884 0.3658 -0.0581 0.0730  -0.0632 53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.3457 0.2842 0.3375 -0.0567 0.0660  -0.0516 53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.3581 0.2917 0.3261 -0.0606 0.0635  -0.0474 53  ILE   A C   
365  O O   . ILE   A 47  ? 0.3804 0.3042 0.3387 -0.0679 0.0733  -0.0531 53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.3570 0.2853 0.3365 -0.0602 0.0748  -0.0504 53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.3505 0.2835 0.3576 -0.0575 0.0786  -0.0571 53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.3632 0.2893 0.3192 -0.0574 0.0660  -0.0385 53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.3625 0.3085 0.3851 -0.0479 0.0635  -0.0537 53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.3450 0.2847 0.3045 -0.0564 0.0512  -0.0385 54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.3436 0.2803 0.2842 -0.0598 0.0465  -0.0349 54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.3425 0.2649 0.2539 -0.0650 0.0493  -0.0316 54  ALA   A C   
373  O O   . ALA   A 48  ? 0.3357 0.2550 0.2416 -0.0627 0.0489  -0.0268 54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.3295 0.2770 0.2737 -0.0538 0.0338  -0.0270 54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.3397 0.2513 0.2299 -0.0718 0.0509  -0.0339 55  ARG   A N   
376  C CA  . ARG   A 49  ? 0.3766 0.2708 0.2325 -0.0763 0.0501  -0.0295 55  ARG   A CA  
377  C C   . ARG   A 49  ? 0.3886 0.2848 0.2326 -0.0768 0.0361  -0.0261 55  ARG   A C   
378  O O   . ARG   A 49  ? 0.4028 0.2922 0.2359 -0.0829 0.0382  -0.0318 55  ARG   A O   
379  C CB  . ARG   A 49  ? 0.3994 0.2731 0.2361 -0.0854 0.0672  -0.0371 55  ARG   A CB  
380  C CG  . ARG   A 49  ? 0.4174 0.2913 0.2740 -0.0855 0.0823  -0.0428 55  ARG   A CG  
381  C CD  . ARG   A 49  ? 0.4526 0.3254 0.3084 -0.0811 0.0804  -0.0357 55  ARG   A CD  
382  N NE  . ARG   A 49  ? 0.4587 0.3335 0.3390 -0.0817 0.0944  -0.0432 55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.4721 0.3501 0.3630 -0.0775 0.0943  -0.0401 55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.4581 0.3369 0.3367 -0.0723 0.0822  -0.0293 55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.4769 0.3583 0.3943 -0.0782 0.1055  -0.0486 55  ARG   A NH2 
386  N N   . CYS   A 50  ? 0.3915 0.2990 0.2431 -0.0702 0.0220  -0.0179 56  CYS   A N   
387  C CA  . CYS   A 50  ? 0.3735 0.2890 0.2271 -0.0692 0.0079  -0.0155 56  CYS   A CA  
388  C C   . CYS   A 50  ? 0.3570 0.2800 0.2161 -0.0623 -0.0054 -0.0063 56  CYS   A C   
389  O O   . CYS   A 50  ? 0.3503 0.2720 0.2106 -0.0583 -0.0030 -0.0020 56  CYS   A O   
390  C CB  . CYS   A 50  ? 0.3623 0.2936 0.2442 -0.0674 0.0100  -0.0197 56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.3163 0.2637 0.2269 -0.0582 0.0101  -0.0152 56  CYS   A SG  
392  N N   . ASP   A 51  ? 0.3630 0.2947 0.2292 -0.0612 -0.0189 -0.0046 57  ASP   A N   
393  C CA  . ASP   A 51  ? 0.3631 0.3051 0.2435 -0.0545 -0.0308 0.0022  57  ASP   A CA  
394  C C   . ASP   A 51  ? 0.3388 0.3004 0.2512 -0.0517 -0.0314 0.0007  57  ASP   A C   
395  O O   . ASP   A 51  ? 0.3441 0.3151 0.2711 -0.0490 -0.0419 0.0031  57  ASP   A O   
396  C CB  . ASP   A 51  ? 0.4172 0.3506 0.2802 -0.0552 -0.0477 0.0054  57  ASP   A CB  
397  C CG  . ASP   A 51  ? 0.5220 0.4563 0.3827 -0.0603 -0.0566 0.0001  57  ASP   A CG  
398  O OD1 . ASP   A 51  ? 0.5499 0.4879 0.4167 -0.0648 -0.0474 -0.0064 57  ASP   A OD1 
399  O OD2 . ASP   A 51  ? 0.5692 0.5002 0.4232 -0.0597 -0.0738 0.0022  57  ASP   A OD2 
400  N N   . CYS   A 52  ? 0.3076 0.2740 0.2314 -0.0523 -0.0201 -0.0032 58  CYS   A N   
401  C CA  . CYS   A 52  ? 0.2820 0.2620 0.2310 -0.0499 -0.0187 -0.0037 58  CYS   A CA  
402  C C   . CYS   A 52  ? 0.2703 0.2591 0.2346 -0.0432 -0.0211 0.0020  58  CYS   A C   
403  O O   . CYS   A 52  ? 0.2599 0.2451 0.2187 -0.0395 -0.0192 0.0054  58  CYS   A O   
404  C CB  . CYS   A 52  ? 0.2797 0.2590 0.2341 -0.0499 -0.0076 -0.0073 58  CYS   A CB  
405  S SG  . CYS   A 52  ? 0.3300 0.3025 0.2779 -0.0573 -0.0028 -0.0156 58  CYS   A SG  
406  N N   . GLN   A 53  ? 0.2589 0.2583 0.2435 -0.0421 -0.0233 0.0023  59  GLN   A N   
407  C CA  . GLN   A 53  ? 0.2635 0.2707 0.2652 -0.0365 -0.0219 0.0061  59  GLN   A CA  
408  C C   . GLN   A 53  ? 0.2543 0.2653 0.2692 -0.0360 -0.0120 0.0050  59  GLN   A C   
409  O O   . GLN   A 53  ? 0.2541 0.2708 0.2843 -0.0329 -0.0088 0.0069  59  GLN   A O   
410  C CB  . GLN   A 53  ? 0.2798 0.2949 0.2968 -0.0352 -0.0330 0.0075  59  GLN   A CB  
411  C CG  . GLN   A 53  ? 0.3307 0.3406 0.3373 -0.0317 -0.0419 0.0118  59  GLN   A CG  
412  C CD  . GLN   A 53  ? 0.3713 0.3899 0.3990 -0.0289 -0.0543 0.0129  59  GLN   A CD  
413  O OE1 . GLN   A 53  ? 0.3816 0.3985 0.4052 -0.0312 -0.0682 0.0117  59  GLN   A OE1 
414  N NE2 . GLN   A 53  ? 0.3425 0.3702 0.3943 -0.0238 -0.0499 0.0145  59  GLN   A NE2 
415  N N   . THR   A 54  ? 0.2422 0.2481 0.2507 -0.0392 -0.0068 0.0018  60  THR   A N   
416  C CA  . THR   A 54  ? 0.2400 0.2442 0.2547 -0.0384 0.0018  0.0018  60  THR   A CA  
417  C C   . THR   A 54  ? 0.2460 0.2411 0.2475 -0.0372 0.0053  0.0004  60  THR   A C   
418  O O   . THR   A 54  ? 0.2550 0.2469 0.2478 -0.0396 0.0034  -0.0026 60  THR   A O   
419  C CB  . THR   A 54  ? 0.2666 0.2738 0.2936 -0.0432 0.0031  -0.0010 60  THR   A CB  
420  O OG1 . THR   A 54  ? 0.3088 0.3123 0.3280 -0.0478 0.0006  -0.0053 60  THR   A OG1 
421  C CG2 . THR   A 54  ? 0.2632 0.2813 0.3095 -0.0445 -0.0020 -0.0014 60  THR   A CG2 
422  N N   . GLY   A 55  ? 0.2436 0.2337 0.2437 -0.0333 0.0104  0.0023  61  GLY   A N   
423  C CA  . GLY   A 55  ? 0.2331 0.2152 0.2248 -0.0309 0.0113  0.0007  61  GLY   A CA  
424  C C   . GLY   A 55  ? 0.2387 0.2125 0.2261 -0.0266 0.0146  0.0033  61  GLY   A C   
425  O O   . GLY   A 55  ? 0.2568 0.2287 0.2462 -0.0271 0.0190  0.0058  61  GLY   A O   
426  N N   . VAL   A 56  ? 0.2402 0.2070 0.2215 -0.0229 0.0124  0.0018  62  VAL   A N   
427  C CA  . VAL   A 56  ? 0.2512 0.2060 0.2231 -0.0183 0.0126  0.0040  62  VAL   A CA  
428  C C   . VAL   A 56  ? 0.2632 0.2164 0.2308 -0.0137 0.0090  0.0029  62  VAL   A C   
429  O O   . VAL   A 56  ? 0.2560 0.2132 0.2297 -0.0139 0.0059  -0.0013 62  VAL   A O   
430  C CB  . VAL   A 56  ? 0.2652 0.2104 0.2359 -0.0179 0.0102  0.0023  62  VAL   A CB  
431  C CG1 . VAL   A 56  ? 0.2907 0.2197 0.2471 -0.0121 0.0068  0.0047  62  VAL   A CG1 
432  C CG2 . VAL   A 56  ? 0.2655 0.2105 0.2401 -0.0227 0.0149  0.0034  62  VAL   A CG2 
433  N N   . TYR   A 57  ? 0.2669 0.2130 0.2240 -0.0102 0.0106  0.0058  63  TYR   A N   
434  C CA  . TYR   A 57  ? 0.2648 0.2088 0.2182 -0.0060 0.0064  0.0036  63  TYR   A CA  
435  C C   . TYR   A 57  ? 0.2709 0.1983 0.2085 -0.0013 0.0017  0.0039  63  TYR   A C   
436  O O   . TYR   A 57  ? 0.2989 0.2143 0.2231 -0.0012 0.0049  0.0077  63  TYR   A O   
437  C CB  . TYR   A 57  ? 0.2494 0.2002 0.2046 -0.0059 0.0107  0.0053  63  TYR   A CB  
438  C CG  . TYR   A 57  ? 0.2773 0.2197 0.2215 -0.0042 0.0168  0.0086  63  TYR   A CG  
439  C CD1 . TYR   A 57  ? 0.2887 0.2320 0.2356 -0.0072 0.0246  0.0117  63  TYR   A CD1 
440  C CD2 . TYR   A 57  ? 0.2937 0.2268 0.2258 -0.0003 0.0159  0.0076  63  TYR   A CD2 
441  C CE1 . TYR   A 57  ? 0.3177 0.2520 0.2557 -0.0066 0.0335  0.0137  63  TYR   A CE1 
442  C CE2 . TYR   A 57  ? 0.3092 0.2322 0.2287 0.0004  0.0238  0.0098  63  TYR   A CE2 
443  C CZ  . TYR   A 57  ? 0.3323 0.2553 0.2547 -0.0029 0.0336  0.0129  63  TYR   A CZ  
444  O OH  . TYR   A 57  ? 0.3547 0.2671 0.2667 -0.0031 0.0448  0.0141  63  TYR   A OH  
445  N N   . TYR   A 58  ? 0.2643 0.1895 0.2025 0.0024  -0.0060 -0.0004 64  TYR   A N   
446  C CA  . TYR   A 58  ? 0.2960 0.2039 0.2171 0.0076  -0.0137 -0.0007 64  TYR   A CA  
447  C C   . TYR   A 58  ? 0.3173 0.2188 0.2233 0.0093  -0.0102 0.0005  64  TYR   A C   
448  O O   . TYR   A 58  ? 0.3082 0.2202 0.2243 0.0088  -0.0084 -0.0021 64  TYR   A O   
449  C CB  . TYR   A 58  ? 0.2938 0.2019 0.2264 0.0110  -0.0258 -0.0074 64  TYR   A CB  
450  C CG  . TYR   A 58  ? 0.3269 0.2151 0.2402 0.0171  -0.0376 -0.0078 64  TYR   A CG  
451  C CD1 . TYR   A 58  ? 0.3600 0.2293 0.2524 0.0189  -0.0403 -0.0026 64  TYR   A CD1 
452  C CD2 . TYR   A 58  ? 0.3428 0.2284 0.2553 0.0206  -0.0459 -0.0130 64  TYR   A CD2 
453  C CE1 . TYR   A 58  ? 0.3929 0.2393 0.2610 0.0247  -0.0526 -0.0022 64  TYR   A CE1 
454  C CE2 . TYR   A 58  ? 0.3815 0.2464 0.2723 0.0262  -0.0588 -0.0136 64  TYR   A CE2 
455  C CZ  . TYR   A 58  ? 0.4160 0.2601 0.2821 0.0284  -0.0624 -0.0077 64  TYR   A CZ  
456  O OH  . TYR   A 58  ? 0.4480 0.2671 0.2868 0.0342  -0.0768 -0.0076 64  TYR   A OH  
457  N N   . CYS   A 59  ? 0.3378 0.2194 0.2175 0.0109  -0.0085 0.0043  65  CYS   A N   
458  C CA  . CYS   A 59  ? 0.3602 0.2310 0.2208 0.0121  -0.0032 0.0049  65  CYS   A CA  
459  C C   . CYS   A 59  ? 0.3800 0.2282 0.2152 0.0173  -0.0159 0.0029  65  CYS   A C   
460  O O   . CYS   A 59  ? 0.4008 0.2272 0.2105 0.0185  -0.0174 0.0068  65  CYS   A O   
461  C CB  . CYS   A 59  ? 0.3877 0.2515 0.2370 0.0086  0.0121  0.0102  65  CYS   A CB  
462  S SG  . CYS   A 59  ? 0.4206 0.2670 0.2442 0.0093  0.0221  0.0100  65  CYS   A SG  
463  N N   . SER   A 60  ? 0.3683 0.2203 0.2101 0.0203  -0.0258 -0.0034 66  SER   A N   
464  C CA  . SER   A 60  ? 0.4096 0.2414 0.2308 0.0257  -0.0418 -0.0067 66  SER   A CA  
465  C C   . SER   A 60  ? 0.4419 0.2460 0.2212 0.0265  -0.0376 -0.0035 66  SER   A C   
466  O O   . SER   A 60  ? 0.4782 0.2574 0.2294 0.0304  -0.0500 -0.0028 66  SER   A O   
467  C CB  . SER   A 60  ? 0.4436 0.2863 0.2838 0.0278  -0.0518 -0.0154 66  SER   A CB  
468  O OG  . SER   A 60  ? 0.5006 0.3456 0.3364 0.0262  -0.0423 -0.0168 66  SER   A OG  
469  N N   . SER   A 61  ? 0.4254 0.2316 0.1998 0.0228  -0.0200 -0.0017 67  SER   A N   
470  C CA  . SER   A 61  ? 0.4428 0.2220 0.1779 0.0222  -0.0112 0.0003  67  SER   A CA  
471  C C   . SER   A 61  ? 0.4850 0.2414 0.1923 0.0202  -0.0029 0.0077  67  SER   A C   
472  O O   . SER   A 61  ? 0.5346 0.2625 0.2031 0.0194  0.0050  0.0096  67  SER   A O   
473  C CB  . SER   A 61  ? 0.4397 0.2294 0.1842 0.0189  0.0063  -0.0012 67  SER   A CB  
474  O OG  . SER   A 61  ? 0.4349 0.2436 0.2046 0.0146  0.0213  0.0027  67  SER   A OG  
475  N N   . ARG   A 62  ? 0.4643 0.2318 0.1905 0.0189  -0.0030 0.0115  68  ARG   A N   
476  C CA  . ARG   A 62  ? 0.4828 0.2292 0.1864 0.0169  0.0037  0.0183  68  ARG   A CA  
477  C C   . ARG   A 62  ? 0.4983 0.2396 0.2038 0.0212  -0.0151 0.0197  68  ARG   A C   
478  O O   . ARG   A 62  ? 0.5218 0.2454 0.2110 0.0201  -0.0117 0.0256  68  ARG   A O   
479  C CB  . ARG   A 62  ? 0.4906 0.2560 0.2200 0.0105  0.0230  0.0212  68  ARG   A CB  
480  C CG  . ARG   A 62  ? 0.5086 0.2785 0.2408 0.0066  0.0426  0.0198  68  ARG   A CG  
481  C CD  . ARG   A 62  ? 0.5611 0.2962 0.2516 0.0040  0.0574  0.0231  68  ARG   A CD  
482  N NE  . ARG   A 62  ? 0.5575 0.2964 0.2541 -0.0002 0.0786  0.0207  68  ARG   A NE  
483  C CZ  . ARG   A 62  ? 0.5903 0.3214 0.2726 0.0012  0.0812  0.0163  68  ARG   A CZ  
484  N NH1 . ARG   A 62  ? 0.5978 0.3166 0.2575 0.0065  0.0629  0.0137  68  ARG   A NH1 
485  N NH2 . ARG   A 62  ? 0.5652 0.2999 0.2570 -0.0026 0.1020  0.0137  68  ARG   A NH2 
486  N N   . ARG   A 63  ? 0.4840 0.2431 0.2156 0.0253  -0.0328 0.0138  69  ARG   A N   
487  C CA  . ARG   A 63  ? 0.4961 0.2545 0.2391 0.0295  -0.0499 0.0133  69  ARG   A CA  
488  C C   . ARG   A 63  ? 0.4810 0.2485 0.2404 0.0252  -0.0392 0.0180  69  ARG   A C   
489  O O   . ARG   A 63  ? 0.5077 0.2582 0.2557 0.0273  -0.0457 0.0219  69  ARG   A O   
490  C CB  . ARG   A 63  ? 0.5394 0.2606 0.2414 0.0356  -0.0664 0.0159  69  ARG   A CB  
491  C CG  . ARG   A 63  ? 0.6033 0.3157 0.2925 0.0407  -0.0830 0.0095  69  ARG   A CG  
492  C CD  . ARG   A 63  ? 0.6665 0.3417 0.3164 0.0476  -0.1038 0.0119  69  ARG   A CD  
493  N NE  . ARG   A 63  ? 0.6996 0.3645 0.3348 0.0522  -0.1209 0.0050  69  ARG   A NE  
494  C CZ  . ARG   A 63  ? 0.7532 0.3800 0.3346 0.0546  -0.1278 0.0072  69  ARG   A CZ  
495  N NH1 . ARG   A 63  ? 0.7613 0.3547 0.2968 0.0526  -0.1174 0.0168  69  ARG   A NH1 
496  N NH2 . ARG   A 63  ? 0.7488 0.3687 0.3204 0.0584  -0.1444 -0.0006 69  ARG   A NH2 
497  N N   . LYS   A 64  ? 0.4570 0.2498 0.2418 0.0192  -0.0231 0.0175  70  LYS   A N   
498  C CA  . LYS   A 64  ? 0.4503 0.2522 0.2507 0.0143  -0.0127 0.0208  70  LYS   A CA  
499  C C   . LYS   A 64  ? 0.4068 0.2423 0.2458 0.0104  -0.0077 0.0168  70  LYS   A C   
500  O O   . LYS   A 64  ? 0.4072 0.2572 0.2566 0.0097  -0.0048 0.0138  70  LYS   A O   
501  C CB  . LYS   A 64  ? 0.5062 0.2938 0.2858 0.0094  0.0060  0.0265  70  LYS   A CB  
502  C CG  . LYS   A 64  ? 0.6208 0.4049 0.4049 0.0052  0.0146  0.0307  70  LYS   A CG  
503  C CD  . LYS   A 64  ? 0.7387 0.5066 0.5037 -0.0002 0.0349  0.0351  70  LYS   A CD  
504  C CE  . LYS   A 64  ? 0.8461 0.5730 0.5635 0.0021  0.0349  0.0404  70  LYS   A CE  
505  N NZ  . LYS   A 64  ? 0.9013 0.6117 0.6004 -0.0042 0.0587  0.0434  70  LYS   A NZ  
506  N N   . HIS   A 65  ? 0.3759 0.2209 0.2332 0.0076  -0.0065 0.0170  71  HIS   A N   
507  C CA  . HIS   A 65  ? 0.3500 0.2219 0.2374 0.0030  -0.0012 0.0140  71  HIS   A CA  
508  C C   . HIS   A 65  ? 0.3649 0.2394 0.2532 -0.0029 0.0138  0.0178  71  HIS   A C   
509  O O   . HIS   A 65  ? 0.4049 0.2624 0.2786 -0.0043 0.0196  0.0220  71  HIS   A O   
510  C CB  . HIS   A 65  ? 0.3393 0.2181 0.2454 0.0028  -0.0083 0.0105  71  HIS   A CB  
511  C CG  . HIS   A 65  ? 0.3356 0.2132 0.2481 0.0084  -0.0225 0.0053  71  HIS   A CG  
512  N ND1 . HIS   A 65  ? 0.3335 0.2295 0.2686 0.0075  -0.0244 -0.0013 71  HIS   A ND1 
513  C CD2 . HIS   A 65  ? 0.3570 0.2158 0.2564 0.0147  -0.0352 0.0053  71  HIS   A CD2 
514  C CE1 . HIS   A 65  ? 0.3416 0.2321 0.2816 0.0130  -0.0371 -0.0060 71  HIS   A CE1 
515  N NE2 . HIS   A 65  ? 0.3719 0.2406 0.2912 0.0179  -0.0456 -0.0023 71  HIS   A NE2 
516  N N   . TYR   A 66  ? 0.3347 0.2286 0.2401 -0.0062 0.0202  0.0164  72  TYR   A N   
517  C CA  . TYR   A 66  ? 0.3336 0.2330 0.2473 -0.0115 0.0328  0.0185  72  TYR   A CA  
518  C C   . TYR   A 66  ? 0.3164 0.2382 0.2562 -0.0157 0.0319  0.0158  72  TYR   A C   
519  O O   . TYR   A 66  ? 0.2830 0.2181 0.2326 -0.0148 0.0267  0.0133  72  TYR   A O   
520  C CB  . TYR   A 66  ? 0.3364 0.2361 0.2469 -0.0114 0.0418  0.0193  72  TYR   A CB  
521  C CG  . TYR   A 66  ? 0.3665 0.2410 0.2468 -0.0088 0.0462  0.0218  72  TYR   A CG  
522  C CD1 . TYR   A 66  ? 0.3970 0.2530 0.2622 -0.0119 0.0585  0.0252  72  TYR   A CD1 
523  C CD2 . TYR   A 66  ? 0.3826 0.2501 0.2481 -0.0039 0.0391  0.0202  72  TYR   A CD2 
524  C CE1 . TYR   A 66  ? 0.4291 0.2578 0.2606 -0.0102 0.0642  0.0275  72  TYR   A CE1 
525  C CE2 . TYR   A 66  ? 0.4144 0.2564 0.2479 -0.0019 0.0429  0.0219  72  TYR   A CE2 
526  C CZ  . TYR   A 66  ? 0.4551 0.2764 0.2693 -0.0051 0.0555  0.0259  72  TYR   A CZ  
527  O OH  . TYR   A 66  ? 0.5115 0.3024 0.2873 -0.0038 0.0605  0.0278  72  TYR   A OH  
528  N N   . PRO   A 67  ? 0.3186 0.2428 0.2680 -0.0206 0.0376  0.0162  73  PRO   A N   
529  C CA  . PRO   A 67  ? 0.3083 0.2522 0.2801 -0.0250 0.0359  0.0133  73  PRO   A CA  
530  C C   . PRO   A 67  ? 0.3327 0.2890 0.3173 -0.0256 0.0398  0.0134  73  PRO   A C   
531  O O   . PRO   A 67  ? 0.3620 0.3127 0.3457 -0.0259 0.0496  0.0151  73  PRO   A O   
532  C CB  . PRO   A 67  ? 0.3156 0.2555 0.2932 -0.0300 0.0415  0.0133  73  PRO   A CB  
533  C CG  . PRO   A 67  ? 0.3313 0.2521 0.2932 -0.0294 0.0517  0.0173  73  PRO   A CG  
534  C CD  . PRO   A 67  ? 0.3225 0.2297 0.2615 -0.0229 0.0463  0.0193  73  PRO   A CD  
535  N N   . VAL   A 68  ? 0.3094 0.2802 0.3048 -0.0256 0.0327  0.0115  74  VAL   A N   
536  C CA  . VAL   A 68  ? 0.3067 0.2886 0.3159 -0.0250 0.0338  0.0119  74  VAL   A CA  
537  C C   . VAL   A 68  ? 0.2821 0.2779 0.3056 -0.0276 0.0255  0.0100  74  VAL   A C   
538  O O   . VAL   A 68  ? 0.2637 0.2598 0.2810 -0.0293 0.0188  0.0083  74  VAL   A O   
539  C CB  . VAL   A 68  ? 0.3405 0.3200 0.3408 -0.0198 0.0324  0.0130  74  VAL   A CB  
540  C CG1 . VAL   A 68  ? 0.3587 0.3245 0.3457 -0.0173 0.0413  0.0145  74  VAL   A CG1 
541  C CG2 . VAL   A 68  ? 0.3410 0.3193 0.3314 -0.0181 0.0240  0.0117  74  VAL   A CG2 
542  N N   . SER   A 69  ? 0.2571 0.2631 0.2999 -0.0280 0.0258  0.0099  75  SER   A N   
543  C CA  . SER   A 69  ? 0.2559 0.2733 0.3104 -0.0287 0.0149  0.0089  75  SER   A CA  
544  C C   . SER   A 69  ? 0.2399 0.2573 0.2901 -0.0234 0.0122  0.0115  75  SER   A C   
545  O O   . SER   A 69  ? 0.2437 0.2586 0.2962 -0.0202 0.0201  0.0127  75  SER   A O   
546  C CB  . SER   A 69  ? 0.2979 0.3261 0.3801 -0.0310 0.0151  0.0068  75  SER   A CB  
547  O OG  . SER   A 69  ? 0.3995 0.4261 0.4862 -0.0364 0.0198  0.0041  75  SER   A OG  
548  N N   . PHE   A 70  ? 0.2227 0.2412 0.2658 -0.0229 0.0021  0.0123  76  PHE   A N   
549  C CA  . PHE   A 70  ? 0.2080 0.2245 0.2465 -0.0182 -0.0002 0.0151  76  PHE   A CA  
550  C C   . PHE   A 70  ? 0.2271 0.2471 0.2690 -0.0176 -0.0125 0.0167  76  PHE   A C   
551  O O   . PHE   A 70  ? 0.2390 0.2590 0.2761 -0.0215 -0.0204 0.0154  76  PHE   A O   
552  C CB  . PHE   A 70  ? 0.2074 0.2142 0.2252 -0.0171 0.0031  0.0151  76  PHE   A CB  
553  C CG  . PHE   A 70  ? 0.2025 0.2047 0.2065 -0.0211 -0.0001 0.0129  76  PHE   A CG  
554  C CD1 . PHE   A 70  ? 0.2066 0.2061 0.2077 -0.0238 0.0037  0.0101  76  PHE   A CD1 
555  C CD2 . PHE   A 70  ? 0.2142 0.2128 0.2076 -0.0225 -0.0059 0.0134  76  PHE   A CD2 
556  C CE1 . PHE   A 70  ? 0.2210 0.2166 0.2131 -0.0277 0.0019  0.0070  76  PHE   A CE1 
557  C CE2 . PHE   A 70  ? 0.2298 0.2227 0.2106 -0.0271 -0.0061 0.0102  76  PHE   A CE2 
558  C CZ  . PHE   A 70  ? 0.2161 0.2087 0.1983 -0.0296 -0.0021 0.0066  76  PHE   A CZ  
559  N N   . SER   A 71  ? 0.2193 0.2400 0.2678 -0.0126 -0.0147 0.0196  77  SER   A N   
560  C CA  . SER   A 71  ? 0.2288 0.2497 0.2794 -0.0107 -0.0279 0.0223  77  SER   A CA  
561  C C   . SER   A 71  ? 0.2480 0.2560 0.2693 -0.0125 -0.0328 0.0245  77  SER   A C   
562  O O   . SER   A 71  ? 0.2587 0.2601 0.2642 -0.0143 -0.0244 0.0232  77  SER   A O   
563  C CB  . SER   A 71  ? 0.2361 0.2602 0.3044 -0.0044 -0.0273 0.0246  77  SER   A CB  
564  O OG  . SER   A 71  ? 0.2546 0.2706 0.3090 -0.0019 -0.0190 0.0261  77  SER   A OG  
565  N N   . LYS   A 72  ? 0.2593 0.2621 0.2728 -0.0122 -0.0463 0.0272  78  LYS   A N   
566  C CA  . LYS   A 72  ? 0.2981 0.2846 0.2801 -0.0148 -0.0484 0.0294  78  LYS   A CA  
567  C C   . LYS   A 72  ? 0.2971 0.2751 0.2715 -0.0109 -0.0423 0.0330  78  LYS   A C   
568  O O   . LYS   A 72  ? 0.3003 0.2835 0.2923 -0.0052 -0.0429 0.0353  78  LYS   A O   
569  C CB  . LYS   A 72  ? 0.3556 0.3339 0.3247 -0.0158 -0.0656 0.0319  78  LYS   A CB  
570  C CG  . LYS   A 72  ? 0.4258 0.4059 0.3897 -0.0222 -0.0697 0.0270  78  LYS   A CG  
571  C CD  . LYS   A 72  ? 0.5032 0.4711 0.4464 -0.0242 -0.0872 0.0284  78  LYS   A CD  
572  C CE  . LYS   A 72  ? 0.5629 0.5278 0.4919 -0.0322 -0.0859 0.0223  78  LYS   A CE  
573  N NZ  . LYS   A 72  ? 0.5999 0.5605 0.5218 -0.0342 -0.1055 0.0210  78  LYS   A NZ  
574  N N   . PRO   A 73  ? 0.3179 0.2822 0.2680 -0.0143 -0.0358 0.0329  79  PRO   A N   
575  C CA  . PRO   A 73  ? 0.3256 0.2815 0.2706 -0.0113 -0.0292 0.0354  79  PRO   A CA  
576  C C   . PRO   A 73  ? 0.3278 0.2772 0.2734 -0.0059 -0.0392 0.0421  79  PRO   A C   
577  O O   . PRO   A 73  ? 0.3428 0.2821 0.2733 -0.0065 -0.0514 0.0459  79  PRO   A O   
578  C CB  . PRO   A 73  ? 0.3542 0.2953 0.2739 -0.0174 -0.0215 0.0333  79  PRO   A CB  
579  C CG  . PRO   A 73  ? 0.3729 0.3202 0.2925 -0.0226 -0.0196 0.0276  79  PRO   A CG  
580  C CD  . PRO   A 73  ? 0.3299 0.2859 0.2591 -0.0214 -0.0322 0.0292  79  PRO   A CD  
581  N N   A SER   A 74  ? 0.3131 0.2677 0.2766 -0.0002 -0.0354 0.0432  80  SER   A N   
582  N N   B SER   A 74  ? 0.3115 0.2659 0.2747 -0.0002 -0.0353 0.0432  80  SER   A N   
583  C CA  A SER   A 74  ? 0.3271 0.2776 0.2985 0.0062  -0.0451 0.0491  80  SER   A CA  
584  C CA  B SER   A 74  ? 0.3247 0.2746 0.2951 0.0061  -0.0449 0.0491  80  SER   A CA  
585  C C   A SER   A 74  ? 0.3324 0.2798 0.3111 0.0105  -0.0358 0.0499  80  SER   A C   
586  C C   B SER   A 74  ? 0.3312 0.2789 0.3103 0.0105  -0.0358 0.0498  80  SER   A C   
587  O O   A SER   A 74  ? 0.3313 0.2812 0.3099 0.0084  -0.0231 0.0452  80  SER   A O   
588  O O   B SER   A 74  ? 0.3306 0.2809 0.3101 0.0085  -0.0230 0.0452  80  SER   A O   
589  C CB  A SER   A 74  ? 0.3453 0.3124 0.3470 0.0103  -0.0543 0.0482  80  SER   A CB  
590  C CB  B SER   A 74  ? 0.3396 0.3050 0.3381 0.0099  -0.0553 0.0486  80  SER   A CB  
591  O OG  A SER   A 74  ? 0.3861 0.3647 0.3945 0.0059  -0.0547 0.0435  80  SER   A OG  
592  O OG  B SER   A 74  ? 0.3841 0.3472 0.3720 0.0067  -0.0684 0.0492  80  SER   A OG  
593  N N   . LEU   A 75  ? 0.3400 0.2812 0.3254 0.0166  -0.0434 0.0553  81  LEU   A N   
594  C CA  . LEU   A 75  ? 0.3606 0.2980 0.3550 0.0211  -0.0355 0.0560  81  LEU   A CA  
595  C C   . LEU   A 75  ? 0.3515 0.3074 0.3804 0.0257  -0.0324 0.0519  81  LEU   A C   
596  O O   . LEU   A 75  ? 0.3424 0.3063 0.3921 0.0298  -0.0428 0.0534  81  LEU   A O   
597  C CB  . LEU   A 75  ? 0.3833 0.3033 0.3685 0.0258  -0.0470 0.0645  81  LEU   A CB  
598  C CG  . LEU   A 75  ? 0.4389 0.3446 0.4200 0.0288  -0.0399 0.0674  81  LEU   A CG  
599  C CD1 . LEU   A 75  ? 0.4604 0.3557 0.4194 0.0219  -0.0255 0.0644  81  LEU   A CD1 
600  C CD2 . LEU   A 75  ? 0.4547 0.3400 0.4220 0.0333  -0.0543 0.0772  81  LEU   A CD2 
601  N N   . ILE   A 76  ? 0.3463 0.3083 0.3812 0.0245  -0.0182 0.0460  82  ILE   A N   
602  C CA  . ILE   A 76  ? 0.3482 0.3238 0.4089 0.0271  -0.0114 0.0412  82  ILE   A CA  
603  C C   . ILE   A 76  ? 0.3531 0.3243 0.4189 0.0302  -0.0005 0.0386  82  ILE   A C   
604  O O   . ILE   A 76  ? 0.3571 0.3198 0.4051 0.0275  0.0058  0.0367  82  ILE   A O   
605  C CB  . ILE   A 76  ? 0.3666 0.3499 0.4215 0.0216  -0.0044 0.0359  82  ILE   A CB  
606  C CG1 . ILE   A 76  ? 0.3802 0.3681 0.4306 0.0178  -0.0139 0.0372  82  ILE   A CG1 
607  C CG2 . ILE   A 76  ? 0.3674 0.3592 0.4407 0.0230  0.0065  0.0307  82  ILE   A CG2 
608  C CD1 . ILE   A 76  ? 0.3870 0.3850 0.4618 0.0205  -0.0220 0.0379  82  ILE   A CD1 
609  N N   . PHE   A 77  ? 0.3492 0.3265 0.4411 0.0353  0.0028  0.0369  83  PHE   A N   
610  C CA  . PHE   A 77  ? 0.3566 0.3290 0.4542 0.0381  0.0139  0.0334  83  PHE   A CA  
611  C C   . PHE   A 77  ? 0.3431 0.3161 0.4301 0.0342  0.0267  0.0264  83  PHE   A C   
612  O O   . PHE   A 77  ? 0.3475 0.3283 0.4396 0.0321  0.0312  0.0232  83  PHE   A O   
613  C CB  . PHE   A 77  ? 0.3714 0.3500 0.5022 0.0443  0.0154  0.0324  83  PHE   A CB  
614  C CG  . PHE   A 77  ? 0.4095 0.3802 0.5447 0.0475  0.0260  0.0291  83  PHE   A CG  
615  C CD1 . PHE   A 77  ? 0.4309 0.3896 0.5611 0.0508  0.0213  0.0337  83  PHE   A CD1 
616  C CD2 . PHE   A 77  ? 0.4283 0.4010 0.5699 0.0467  0.0415  0.0213  83  PHE   A CD2 
617  C CE1 . PHE   A 77  ? 0.4525 0.4036 0.5882 0.0535  0.0314  0.0300  83  PHE   A CE1 
618  C CE2 . PHE   A 77  ? 0.4476 0.4115 0.5915 0.0492  0.0513  0.0173  83  PHE   A CE2 
619  C CZ  . PHE   A 77  ? 0.4490 0.4034 0.5919 0.0527  0.0460  0.0214  83  PHE   A CZ  
620  N N   . VAL   A 78  ? 0.3298 0.2931 0.4015 0.0332  0.0323  0.0237  84  VAL   A N   
621  C CA  . VAL   A 78  ? 0.3267 0.2876 0.3855 0.0302  0.0415  0.0168  84  VAL   A CA  
622  C C   . VAL   A 78  ? 0.3355 0.2892 0.3988 0.0331  0.0510  0.0118  84  VAL   A C   
623  O O   . VAL   A 78  ? 0.3428 0.2895 0.4070 0.0350  0.0499  0.0130  84  VAL   A O   
624  C CB  . VAL   A 78  ? 0.3191 0.2755 0.3564 0.0257  0.0380  0.0158  84  VAL   A CB  
625  C CG1 . VAL   A 78  ? 0.3269 0.2790 0.3511 0.0237  0.0441  0.0085  84  VAL   A CG1 
626  C CG2 . VAL   A 78  ? 0.3193 0.2816 0.3516 0.0225  0.0301  0.0198  84  VAL   A CG2 
627  N N   . GLU   A 79  ? 0.3434 0.2966 0.4075 0.0329  0.0612  0.0062  85  GLU   A N   
628  C CA  . GLU   A 79  ? 0.3586 0.3032 0.4245 0.0350  0.0719  0.0001  85  GLU   A CA  
629  C C   . GLU   A 79  ? 0.3631 0.2970 0.4101 0.0334  0.0710  -0.0041 85  GLU   A C   
630  O O   . GLU   A 79  ? 0.3489 0.2820 0.3795 0.0300  0.0647  -0.0044 85  GLU   A O   
631  C CB  . GLU   A 79  ? 0.3939 0.3359 0.4565 0.0335  0.0845  -0.0056 85  GLU   A CB  
632  C CG  . GLU   A 79  ? 0.4863 0.4393 0.5743 0.0346  0.0882  -0.0035 85  GLU   A CG  
633  C CD  . GLU   A 79  ? 0.6307 0.5785 0.7244 0.0341  0.1061  -0.0103 85  GLU   A CD  
634  O OE1 . GLU   A 79  ? 0.6908 0.6285 0.7821 0.0356  0.1155  -0.0158 85  GLU   A OE1 
635  O OE2 . GLU   A 79  ? 0.6583 0.6111 0.7590 0.0316  0.1120  -0.0106 85  GLU   A OE2 
636  N N   . ALA   A 80  ? 0.3734 0.2993 0.4255 0.0358  0.0776  -0.0084 86  ALA   A N   
637  C CA  . ALA   A 80  ? 0.3900 0.3058 0.4277 0.0341  0.0772  -0.0141 86  ALA   A CA  
638  C C   . ALA   A 80  ? 0.3933 0.3029 0.4067 0.0307  0.0778  -0.0210 86  ALA   A C   
639  O O   . ALA   A 80  ? 0.4138 0.3213 0.4190 0.0301  0.0840  -0.0229 86  ALA   A O   
640  C CB  . ALA   A 80  ? 0.3981 0.3056 0.4464 0.0371  0.0853  -0.0183 86  ALA   A CB  
641  N N   . SER   A 81  ? 0.3753 0.2811 0.3775 0.0283  0.0707  -0.0244 87  SER   A N   
642  C CA  . SER   A 81  ? 0.3789 0.2772 0.3588 0.0259  0.0669  -0.0314 87  SER   A CA  
643  C C   . SER   A 81  ? 0.3833 0.2744 0.3620 0.0249  0.0632  -0.0392 87  SER   A C   
644  O O   . SER   A 81  ? 0.3823 0.2732 0.3759 0.0257  0.0664  -0.0387 87  SER   A O   
645  C CB  . SER   A 81  ? 0.3834 0.2889 0.3569 0.0237  0.0579  -0.0275 87  SER   A CB  
646  O OG  . SER   A 81  ? 0.3785 0.2891 0.3607 0.0220  0.0508  -0.0267 87  SER   A OG  
647  N N   . GLU   A 82  ? 0.3975 0.2819 0.3593 0.0232  0.0559  -0.0465 88  GLU   A N   
648  C CA  . GLU   A 82  ? 0.4126 0.2916 0.3767 0.0218  0.0506  -0.0555 88  GLU   A CA  
649  C C   . GLU   A 82  ? 0.3953 0.2839 0.3774 0.0195  0.0454  -0.0533 88  GLU   A C   
650  O O   . GLU   A 82  ? 0.3969 0.2824 0.3882 0.0178  0.0438  -0.0603 88  GLU   A O   
651  C CB  . GLU   A 82  ? 0.4817 0.3499 0.4234 0.0213  0.0411  -0.0645 88  GLU   A CB  
652  C CG  . GLU   A 82  ? 0.6197 0.4763 0.5348 0.0225  0.0456  -0.0640 88  GLU   A CG  
653  C CD  . GLU   A 82  ? 0.7474 0.6084 0.6531 0.0224  0.0413  -0.0570 88  GLU   A CD  
654  O OE1 . GLU   A 82  ? 0.7269 0.5958 0.6403 0.0227  0.0499  -0.0486 88  GLU   A OE1 
655  O OE2 . GLU   A 82  ? 0.8129 0.6695 0.7059 0.0221  0.0283  -0.0603 88  GLU   A OE2 
656  N N   . TYR   A 83  ? 0.3691 0.2678 0.3557 0.0188  0.0439  -0.0445 89  TYR   A N   
657  C CA  . TYR   A 83  ? 0.3508 0.2560 0.3503 0.0158  0.0413  -0.0425 89  TYR   A CA  
658  C C   . TYR   A 83  ? 0.3400 0.2466 0.3504 0.0158  0.0481  -0.0340 89  TYR   A C   
659  O O   . TYR   A 83  ? 0.3400 0.2447 0.3595 0.0127  0.0498  -0.0349 89  TYR   A O   
660  C CB  . TYR   A 83  ? 0.3476 0.2601 0.3423 0.0146  0.0344  -0.0397 89  TYR   A CB  
661  C CG  . TYR   A 83  ? 0.3710 0.2793 0.3541 0.0152  0.0253  -0.0477 89  TYR   A CG  
662  C CD1 . TYR   A 83  ? 0.3765 0.2827 0.3672 0.0137  0.0180  -0.0579 89  TYR   A CD1 
663  C CD2 . TYR   A 83  ? 0.4065 0.3108 0.3707 0.0173  0.0236  -0.0453 89  TYR   A CD2 
664  C CE1 . TYR   A 83  ? 0.3985 0.2990 0.3778 0.0152  0.0062  -0.0651 89  TYR   A CE1 
665  C CE2 . TYR   A 83  ? 0.4252 0.3215 0.3737 0.0183  0.0137  -0.0515 89  TYR   A CE2 
666  C CZ  . TYR   A 83  ? 0.4377 0.3319 0.3932 0.0177  0.0035  -0.0612 89  TYR   A CZ  
667  O OH  . TYR   A 83  ? 0.4862 0.3709 0.4256 0.0195  -0.0095 -0.0671 89  TYR   A OH  
668  N N   . TYR   A 84  ? 0.3404 0.2487 0.3502 0.0190  0.0518  -0.0263 90  TYR   A N   
669  C CA  . TYR   A 84  ? 0.3382 0.2456 0.3571 0.0203  0.0553  -0.0176 90  TYR   A CA  
670  C C   . TYR   A 84  ? 0.3563 0.2614 0.3817 0.0252  0.0607  -0.0154 90  TYR   A C   
671  O O   . TYR   A 84  ? 0.3613 0.2691 0.3834 0.0271  0.0627  -0.0172 90  TYR   A O   
672  C CB  . TYR   A 84  ? 0.3172 0.2319 0.3340 0.0195  0.0509  -0.0085 90  TYR   A CB  
673  C CG  . TYR   A 84  ? 0.2987 0.2158 0.3105 0.0145  0.0472  -0.0104 90  TYR   A CG  
674  C CD1 . TYR   A 84  ? 0.3015 0.2125 0.3152 0.0107  0.0498  -0.0098 90  TYR   A CD1 
675  C CD2 . TYR   A 84  ? 0.2915 0.2155 0.2973 0.0134  0.0424  -0.0130 90  TYR   A CD2 
676  C CE1 . TYR   A 84  ? 0.2956 0.2087 0.3077 0.0058  0.0487  -0.0127 90  TYR   A CE1 
677  C CE2 . TYR   A 84  ? 0.2820 0.2087 0.2870 0.0093  0.0394  -0.0154 90  TYR   A CE2 
678  C CZ  . TYR   A 84  ? 0.2890 0.2111 0.2982 0.0054  0.0430  -0.0154 90  TYR   A CZ  
679  O OH  . TYR   A 84  ? 0.2945 0.2188 0.3060 0.0008  0.0424  -0.0194 90  TYR   A OH  
680  N N   . PRO   A 85  ? 0.3713 0.2709 0.4068 0.0273  0.0635  -0.0104 91  PRO   A N   
681  C CA  . PRO   A 85  ? 0.3811 0.2804 0.4283 0.0328  0.0674  -0.0070 91  PRO   A CA  
682  C C   . PRO   A 85  ? 0.3871 0.2964 0.4389 0.0349  0.0621  0.0015  91  PRO   A C   
683  O O   . PRO   A 85  ? 0.3906 0.3048 0.4339 0.0319  0.0556  0.0055  91  PRO   A O   
684  C CB  . PRO   A 85  ? 0.3958 0.2844 0.4515 0.0345  0.0695  -0.0033 91  PRO   A CB  
685  C CG  . PRO   A 85  ? 0.4121 0.2974 0.4582 0.0300  0.0652  0.0011  91  PRO   A CG  
686  C CD  . PRO   A 85  ? 0.3868 0.2786 0.4232 0.0249  0.0635  -0.0067 91  PRO   A CD  
687  N N   . ALA   A 86  ? 0.3904 0.3029 0.4580 0.0398  0.0649  0.0035  92  ALA   A N   
688  C CA  . ALA   A 86  ? 0.3956 0.3181 0.4739 0.0422  0.0591  0.0103  92  ALA   A CA  
689  C C   . ALA   A 86  ? 0.3957 0.3151 0.4710 0.0425  0.0485  0.0200  92  ALA   A C   
690  O O   . ALA   A 86  ? 0.3960 0.3041 0.4726 0.0445  0.0480  0.0234  92  ALA   A O   
691  C CB  . ALA   A 86  ? 0.3946 0.3197 0.4973 0.0479  0.0645  0.0096  92  ALA   A CB  
692  N N   . ARG   A 87  ? 0.3798 0.3059 0.4461 0.0395  0.0410  0.0239  93  ARG   A N   
693  C CA  . ARG   A 87  ? 0.3740 0.2934 0.4302 0.0386  0.0316  0.0323  93  ARG   A CA  
694  C C   . ARG   A 87  ? 0.3778 0.3069 0.4306 0.0368  0.0227  0.0360  93  ARG   A C   
695  O O   . ARG   A 87  ? 0.3715 0.3125 0.4302 0.0357  0.0251  0.0318  93  ARG   A O   
696  C CB  . ARG   A 87  ? 0.4012 0.3100 0.4381 0.0329  0.0356  0.0301  93  ARG   A CB  
697  C CG  . ARG   A 87  ? 0.4273 0.3431 0.4512 0.0267  0.0353  0.0262  93  ARG   A CG  
698  C CD  . ARG   A 87  ? 0.4221 0.3355 0.4408 0.0226  0.0422  0.0172  93  ARG   A CD  
699  N NE  . ARG   A 87  ? 0.3952 0.3102 0.4026 0.0168  0.0407  0.0154  93  ARG   A NE  
700  C CZ  . ARG   A 87  ? 0.3984 0.3234 0.4034 0.0151  0.0383  0.0120  93  ARG   A CZ  
701  N NH1 . ARG   A 87  ? 0.3616 0.2944 0.3717 0.0181  0.0379  0.0104  93  ARG   A NH1 
702  N NH2 . ARG   A 87  ? 0.3358 0.2614 0.3335 0.0100  0.0375  0.0097  93  ARG   A NH2 
703  N N   . TYR   A 88  ? 0.3873 0.3087 0.4279 0.0360  0.0130  0.0437  94  TYR   A N   
704  C CA  . TYR   A 88  ? 0.3972 0.3258 0.4310 0.0332  0.0047  0.0460  94  TYR   A CA  
705  C C   . TYR   A 88  ? 0.3683 0.2926 0.3799 0.0258  0.0092  0.0432  94  TYR   A C   
706  O O   . TYR   A 88  ? 0.3864 0.2960 0.3826 0.0232  0.0121  0.0450  94  TYR   A O   
707  C CB  . TYR   A 88  ? 0.4337 0.3539 0.4621 0.0358  -0.0094 0.0551  94  TYR   A CB  
708  C CG  . TYR   A 88  ? 0.4677 0.3946 0.5236 0.0437  -0.0176 0.0576  94  TYR   A CG  
709  C CD1 . TYR   A 88  ? 0.4797 0.4237 0.5559 0.0448  -0.0228 0.0553  94  TYR   A CD1 
710  C CD2 . TYR   A 88  ? 0.4987 0.4141 0.5626 0.0500  -0.0206 0.0623  94  TYR   A CD2 
711  C CE1 . TYR   A 88  ? 0.4934 0.4446 0.6007 0.0519  -0.0306 0.0565  94  TYR   A CE1 
712  C CE2 . TYR   A 88  ? 0.5097 0.4317 0.6037 0.0579  -0.0292 0.0640  94  TYR   A CE2 
713  C CZ  . TYR   A 88  ? 0.5141 0.4549 0.6314 0.0588  -0.0341 0.0606  94  TYR   A CZ  
714  O OH  . TYR   A 88  ? 0.5400 0.4883 0.6928 0.0666  -0.0424 0.0611  94  TYR   A OH  
715  N N   . GLN   A 89  ? 0.3277 0.2637 0.3391 0.0224  0.0108  0.0384  95  GLN   A N   
716  C CA  . GLN   A 89  ? 0.3251 0.2582 0.3196 0.0158  0.0141  0.0350  95  GLN   A CA  
717  C C   . GLN   A 89  ? 0.3201 0.2521 0.3028 0.0129  0.0056  0.0397  95  GLN   A C   
718  O O   . GLN   A 89  ? 0.3089 0.2509 0.3011 0.0148  -0.0013 0.0412  95  GLN   A O   
719  C CB  . GLN   A 89  ? 0.3327 0.2761 0.3318 0.0141  0.0195  0.0272  95  GLN   A CB  
720  C CG  . GLN   A 89  ? 0.3449 0.2870 0.3321 0.0081  0.0214  0.0231  95  GLN   A CG  
721  C CD  . GLN   A 89  ? 0.3296 0.2770 0.3202 0.0077  0.0252  0.0153  95  GLN   A CD  
722  O OE1 . GLN   A 89  ? 0.3139 0.2596 0.3093 0.0103  0.0289  0.0115  95  GLN   A OE1 
723  N NE2 . GLN   A 89  ? 0.3205 0.2722 0.3068 0.0044  0.0237  0.0124  95  GLN   A NE2 
724  N N   . SER   A 90  ? 0.3211 0.2397 0.2834 0.0080  0.0067  0.0414  96  SER   A N   
725  C CA  . SER   A 90  ? 0.3268 0.2408 0.2729 0.0046  -0.0010 0.0452  96  SER   A CA  
726  C C   . SER   A 90  ? 0.3052 0.2275 0.2480 -0.0011 0.0026  0.0390  96  SER   A C   
727  O O   . SER   A 90  ? 0.2973 0.2249 0.2468 -0.0028 0.0110  0.0323  96  SER   A O   
728  C CB  . SER   A 90  ? 0.3593 0.2500 0.2800 0.0016  -0.0002 0.0504  96  SER   A CB  
729  O OG  . SER   A 90  ? 0.3780 0.2623 0.2936 -0.0036 0.0136  0.0448  96  SER   A OG  
730  N N   . HIS   A 91  ? 0.2995 0.2213 0.2315 -0.0039 -0.0049 0.0410  97  HIS   A N   
731  C CA  . HIS   A 91  ? 0.3000 0.2275 0.2278 -0.0095 -0.0023 0.0356  97  HIS   A CA  
732  C C   . HIS   A 91  ? 0.2839 0.2293 0.2326 -0.0076 0.0000  0.0305  97  HIS   A C   
733  O O   . HIS   A 91  ? 0.2917 0.2404 0.2403 -0.0112 0.0054  0.0247  97  HIS   A O   
734  C CB  . HIS   A 91  ? 0.3149 0.2303 0.2281 -0.0159 0.0088  0.0313  97  HIS   A CB  
735  C CG  . HIS   A 91  ? 0.3632 0.2564 0.2497 -0.0193 0.0089  0.0365  97  HIS   A CG  
736  N ND1 . HIS   A 91  ? 0.4086 0.2915 0.2726 -0.0250 0.0070  0.0369  97  HIS   A ND1 
737  C CD2 . HIS   A 91  ? 0.3971 0.2744 0.2737 -0.0178 0.0112  0.0415  97  HIS   A CD2 
738  C CE1 . HIS   A 91  ? 0.4362 0.2954 0.2741 -0.0271 0.0084  0.0423  97  HIS   A CE1 
739  N NE2 . HIS   A 91  ? 0.4348 0.2897 0.2798 -0.0228 0.0109  0.0456  97  HIS   A NE2 
740  N N   . LEU   A 92  ? 0.2509 0.2056 0.2167 -0.0020 -0.0035 0.0324  98  LEU   A N   
741  C CA  . LEU   A 92  ? 0.2494 0.2164 0.2307 -0.0003 0.0002  0.0284  98  LEU   A CA  
742  C C   . LEU   A 92  ? 0.2404 0.2172 0.2303 -0.0009 -0.0056 0.0290  98  LEU   A C   
743  O O   . LEU   A 92  ? 0.2561 0.2339 0.2502 0.0005  -0.0147 0.0329  98  LEU   A O   
744  C CB  . LEU   A 92  ? 0.2536 0.2222 0.2481 0.0054  0.0037  0.0288  98  LEU   A CB  
745  C CG  . LEU   A 92  ? 0.2704 0.2458 0.2738 0.0068  0.0103  0.0242  98  LEU   A CG  
746  C CD1 . LEU   A 92  ? 0.2900 0.2614 0.2832 0.0042  0.0149  0.0189  98  LEU   A CD1 
747  C CD2 . LEU   A 92  ? 0.2754 0.2504 0.2905 0.0119  0.0147  0.0241  98  LEU   A CD2 
748  N N   . MET   A 93  ? 0.2336 0.2167 0.2269 -0.0029 -0.0012 0.0248  99  MET   A N   
749  C CA  . MET   A 93  ? 0.2194 0.2113 0.2223 -0.0045 -0.0039 0.0242  99  MET   A CA  
750  C C   . MET   A 93  ? 0.2366 0.2335 0.2514 -0.0024 0.0037  0.0221  99  MET   A C   
751  O O   . MET   A 93  ? 0.2490 0.2412 0.2564 -0.0018 0.0100  0.0196  99  MET   A O   
752  C CB  . MET   A 93  ? 0.2263 0.2162 0.2176 -0.0100 -0.0040 0.0212  99  MET   A CB  
753  C CG  . MET   A 93  ? 0.2363 0.2174 0.2109 -0.0134 -0.0089 0.0225  99  MET   A CG  
754  S SD  . MET   A 93  ? 0.2906 0.2685 0.2537 -0.0201 -0.0060 0.0174  99  MET   A SD  
755  C CE  . MET   A 93  ? 0.2728 0.2481 0.2367 -0.0192 0.0032  0.0129  99  MET   A CE  
756  N N   . LEU   A 94  ? 0.2370 0.2420 0.2703 -0.0012 0.0034  0.0226  100 LEU   A N   
757  C CA  . LEU   A 94  ? 0.2210 0.2277 0.2633 -0.0002 0.0137  0.0203  100 LEU   A CA  
758  C C   . LEU   A 94  ? 0.2253 0.2354 0.2716 -0.0043 0.0165  0.0184  100 LEU   A C   
759  O O   . LEU   A 94  ? 0.2265 0.2430 0.2806 -0.0071 0.0093  0.0185  100 LEU   A O   
760  C CB  . LEU   A 94  ? 0.2283 0.2404 0.2934 0.0038  0.0166  0.0206  100 LEU   A CB  
761  C CG  . LEU   A 94  ? 0.2720 0.2798 0.3365 0.0085  0.0154  0.0224  100 LEU   A CG  
762  C CD1 . LEU   A 94  ? 0.2772 0.2907 0.3685 0.0126  0.0201  0.0215  100 LEU   A CD1 
763  C CD2 . LEU   A 94  ? 0.3070 0.3045 0.3517 0.0088  0.0227  0.0204  100 LEU   A CD2 
764  N N   . ALA   A 95  ? 0.2171 0.2211 0.2569 -0.0048 0.0268  0.0167  101 ALA   A N   
765  C CA  . ALA   A 95  ? 0.2125 0.2158 0.2547 -0.0086 0.0330  0.0153  101 ALA   A CA  
766  C C   . ALA   A 95  ? 0.2335 0.2303 0.2778 -0.0077 0.0473  0.0140  101 ALA   A C   
767  O O   . ALA   A 95  ? 0.2373 0.2274 0.2732 -0.0044 0.0515  0.0138  101 ALA   A O   
768  C CB  . ALA   A 95  ? 0.2303 0.2249 0.2514 -0.0107 0.0314  0.0149  101 ALA   A CB  
769  N N   . VAL   A 96  ? 0.2372 0.2343 0.2914 -0.0114 0.0557  0.0128  102 VAL   A N   
770  C CA  . VAL   A 96  ? 0.2580 0.2444 0.3091 -0.0125 0.0725  0.0113  102 VAL   A CA  
771  C C   . VAL   A 96  ? 0.2979 0.2661 0.3157 -0.0135 0.0742  0.0128  102 VAL   A C   
772  O O   . VAL   A 96  ? 0.3099 0.2768 0.3230 -0.0165 0.0704  0.0137  102 VAL   A O   
773  C CB  . VAL   A 96  ? 0.2788 0.2731 0.3583 -0.0168 0.0816  0.0087  102 VAL   A CB  
774  C CG1 . VAL   A 96  ? 0.3017 0.2802 0.3730 -0.0194 0.1026  0.0071  102 VAL   A CG1 
775  C CG2 . VAL   A 96  ? 0.2562 0.2690 0.3721 -0.0146 0.0761  0.0067  102 VAL   A CG2 
776  N N   . GLY   A 97  ? 0.3232 0.2772 0.3181 -0.0105 0.0775  0.0129  103 GLY   A N   
777  C CA  . GLY   A 97  ? 0.3546 0.2896 0.3170 -0.0100 0.0754  0.0142  103 GLY   A CA  
778  C C   . GLY   A 97  ? 0.3776 0.2976 0.3173 -0.0065 0.0780  0.0130  103 GLY   A C   
779  O O   . GLY   A 97  ? 0.3852 0.3116 0.3356 -0.0042 0.0803  0.0112  103 GLY   A O   
780  N N   . HIS   A 98  ? 0.3870 0.2849 0.2944 -0.0058 0.0775  0.0139  104 HIS   A N   
781  C CA  . HIS   A 98  ? 0.3901 0.2713 0.2724 -0.0026 0.0781  0.0120  104 HIS   A CA  
782  C C   . HIS   A 98  ? 0.3716 0.2602 0.2553 0.0015  0.0624  0.0101  104 HIS   A C   
783  O O   . HIS   A 98  ? 0.3741 0.2674 0.2597 0.0023  0.0500  0.0105  104 HIS   A O   
784  C CB  . HIS   A 98  ? 0.4278 0.2787 0.2707 -0.0028 0.0810  0.0136  104 HIS   A CB  
785  C CG  . HIS   A 98  ? 0.4563 0.2877 0.2698 0.0003  0.0796  0.0109  104 HIS   A CG  
786  N ND1 . HIS   A 98  ? 0.4741 0.2995 0.2845 -0.0006 0.0944  0.0079  104 HIS   A ND1 
787  C CD2 . HIS   A 98  ? 0.4786 0.2975 0.2692 0.0045  0.0640  0.0095  104 HIS   A CD2 
788  C CE1 . HIS   A 98  ? 0.4926 0.3010 0.2751 0.0026  0.0875  0.0050  104 HIS   A CE1 
789  N NE2 . HIS   A 98  ? 0.4990 0.3021 0.2680 0.0058  0.0687  0.0059  104 HIS   A NE2 
790  N N   . SER   A 99  ? 0.3573 0.2450 0.2399 0.0038  0.0642  0.0070  105 SER   A N   
791  C CA  . SER   A 99  ? 0.3527 0.2423 0.2329 0.0073  0.0518  0.0039  105 SER   A CA  
792  C C   . SER   A 99  ? 0.4051 0.2816 0.2701 0.0091  0.0576  0.0001  105 SER   A C   
793  O O   . SER   A 99  ? 0.4112 0.2846 0.2785 0.0078  0.0724  -0.0003 105 SER   A O   
794  C CB  . SER   A 99  ? 0.3456 0.2582 0.2550 0.0075  0.0453  0.0040  105 SER   A CB  
795  O OG  . SER   A 99  ? 0.3573 0.2797 0.2853 0.0075  0.0538  0.0043  105 SER   A OG  
796  N N   . GLU   A 100 ? 0.4177 0.2858 0.2683 0.0120  0.0460  -0.0038 106 GLU   A N   
797  C CA  . GLU   A 100 ? 0.4438 0.2979 0.2774 0.0138  0.0484  -0.0088 106 GLU   A CA  
798  C C   . GLU   A 100 ? 0.4523 0.3141 0.2960 0.0163  0.0344  -0.0135 106 GLU   A C   
799  O O   . GLU   A 100 ? 0.4527 0.3218 0.3047 0.0169  0.0222  -0.0134 106 GLU   A O   
800  C CB  . GLU   A 100 ? 0.4812 0.3060 0.2732 0.0145  0.0453  -0.0097 106 GLU   A CB  
801  C CG  . GLU   A 100 ? 0.5862 0.3915 0.3549 0.0115  0.0625  -0.0074 106 GLU   A CG  
802  C CD  . GLU   A 100 ? 0.5998 0.3739 0.3238 0.0127  0.0541  -0.0069 106 GLU   A CD  
803  O OE1 . GLU   A 100 ? 0.5908 0.3472 0.2891 0.0151  0.0466  -0.0119 106 GLU   A OE1 
804  O OE2 . GLU   A 100 ? 0.5922 0.3592 0.3070 0.0116  0.0533  -0.0016 106 GLU   A OE2 
805  N N   . PRO   A 101 ? 0.4661 0.3234 0.3074 0.0177  0.0361  -0.0189 107 PRO   A N   
806  C CA  . PRO   A 101 ? 0.4664 0.3274 0.3150 0.0196  0.0227  -0.0247 107 PRO   A CA  
807  C C   . PRO   A 101 ? 0.4605 0.3093 0.2911 0.0214  0.0062  -0.0273 107 PRO   A C   
808  O O   . PRO   A 101 ? 0.4949 0.3207 0.2921 0.0224  0.0040  -0.0280 107 PRO   A O   
809  C CB  . PRO   A 101 ? 0.4954 0.3455 0.3341 0.0204  0.0285  -0.0306 107 PRO   A CB  
810  C CG  . PRO   A 101 ? 0.5010 0.3522 0.3437 0.0189  0.0472  -0.0269 107 PRO   A CG  
811  C CD  . PRO   A 101 ? 0.4794 0.3263 0.3111 0.0172  0.0510  -0.0210 107 PRO   A CD  
812  N N   . GLY   A 102 ? 0.4208 0.2834 0.2730 0.0218  -0.0048 -0.0287 108 GLY   A N   
813  C CA  . GLY   A 102 ? 0.4043 0.2605 0.2510 0.0240  -0.0217 -0.0316 108 GLY   A CA  
814  C C   . GLY   A 102 ? 0.3869 0.2557 0.2503 0.0228  -0.0234 -0.0269 108 GLY   A C   
815  O O   . GLY   A 102 ? 0.3863 0.2568 0.2590 0.0245  -0.0366 -0.0303 108 GLY   A O   
816  N N   . ASP   A 103 ? 0.3585 0.2370 0.2291 0.0198  -0.0102 -0.0199 109 ASP   A N   
817  C CA  . ASP   A 103 ? 0.3370 0.2265 0.2211 0.0179  -0.0098 -0.0155 109 ASP   A CA  
818  C C   . ASP   A 103 ? 0.3084 0.2182 0.2228 0.0155  -0.0093 -0.0171 109 ASP   A C   
819  O O   . ASP   A 103 ? 0.2932 0.2114 0.2188 0.0135  -0.0098 -0.0151 109 ASP   A O   
820  C CB  . ASP   A 103 ? 0.3536 0.2426 0.2312 0.0153  0.0033  -0.0084 109 ASP   A CB  
821  C CG  . ASP   A 103 ? 0.3775 0.2439 0.2240 0.0163  0.0042  -0.0058 109 ASP   A CG  
822  O OD1 . ASP   A 103 ? 0.3738 0.2274 0.2064 0.0190  -0.0084 -0.0074 109 ASP   A OD1 
823  O OD2 . ASP   A 103 ? 0.3844 0.2447 0.2210 0.0143  0.0179  -0.0025 109 ASP   A OD2 
824  N N   . CYS   A 104 ? 0.2993 0.2148 0.2250 0.0153  -0.0074 -0.0210 110 CYS   A N   
825  C CA  . CYS   A 104 ? 0.2935 0.2235 0.2428 0.0124  -0.0053 -0.0221 110 CYS   A CA  
826  C C   . CYS   A 104 ? 0.3008 0.2339 0.2626 0.0120  -0.0137 -0.0271 110 CYS   A C   
827  O O   . CYS   A 104 ? 0.3212 0.2465 0.2799 0.0150  -0.0244 -0.0328 110 CYS   A O   
828  C CB  . CYS   A 104 ? 0.3031 0.2347 0.2608 0.0123  -0.0020 -0.0257 110 CYS   A CB  
829  S SG  . CYS   A 104 ? 0.3219 0.2543 0.2756 0.0125  0.0097  -0.0195 110 CYS   A SG  
830  N N   . GLY   A 105 ? 0.2683 0.2114 0.2443 0.0083  -0.0093 -0.0260 111 GLY   A N   
831  C CA  . GLY   A 105 ? 0.2618 0.2083 0.2535 0.0072  -0.0145 -0.0319 111 GLY   A CA  
832  C C   . GLY   A 105 ? 0.2806 0.2264 0.2686 0.0072  -0.0173 -0.0289 111 GLY   A C   
833  O O   . GLY   A 105 ? 0.2834 0.2332 0.2868 0.0056  -0.0189 -0.0333 111 GLY   A O   
834  N N   . GLY   A 106 ? 0.2878 0.2271 0.2567 0.0088  -0.0168 -0.0222 112 GLY   A N   
835  C CA  . GLY   A 106 ? 0.2760 0.2133 0.2409 0.0082  -0.0179 -0.0188 112 GLY   A CA  
836  C C   . GLY   A 106 ? 0.2630 0.2114 0.2391 0.0030  -0.0104 -0.0170 112 GLY   A C   
837  O O   . GLY   A 106 ? 0.2602 0.2147 0.2368 0.0003  -0.0033 -0.0138 112 GLY   A O   
838  N N   . ILE   A 107 ? 0.2564 0.2063 0.2419 0.0016  -0.0126 -0.0197 113 ILE   A N   
839  C CA  . ILE   A 107 ? 0.2576 0.2153 0.2505 -0.0039 -0.0055 -0.0192 113 ILE   A CA  
840  C C   . ILE   A 107 ? 0.2330 0.1917 0.2156 -0.0061 -0.0016 -0.0121 113 ILE   A C   
841  O O   . ILE   A 107 ? 0.2552 0.2073 0.2294 -0.0042 -0.0038 -0.0090 113 ILE   A O   
842  C CB  . ILE   A 107 ? 0.2958 0.2544 0.3049 -0.0050 -0.0076 -0.0263 113 ILE   A CB  
843  C CG1 . ILE   A 107 ? 0.3284 0.2909 0.3544 -0.0065 -0.0052 -0.0343 113 ILE   A CG1 
844  C CG2 . ILE   A 107 ? 0.3047 0.2666 0.3147 -0.0104 -0.0016 -0.0252 113 ILE   A CG2 
845  C CD1 . ILE   A 107 ? 0.3620 0.3248 0.4096 -0.0058 -0.0089 -0.0433 113 ILE   A CD1 
846  N N   . LEU   A 108 ? 0.2113 0.1768 0.1949 -0.0104 0.0040  -0.0100 114 LEU   A N   
847  C CA  . LEU   A 108 ? 0.1993 0.1681 0.1795 -0.0136 0.0065  -0.0055 114 LEU   A CA  
848  C C   . LEU   A 108 ? 0.2088 0.1793 0.1944 -0.0185 0.0080  -0.0096 114 LEU   A C   
849  O O   . LEU   A 108 ? 0.2200 0.1911 0.2081 -0.0213 0.0108  -0.0133 114 LEU   A O   
850  C CB  . LEU   A 108 ? 0.1922 0.1660 0.1704 -0.0146 0.0088  -0.0011 114 LEU   A CB  
851  C CG  . LEU   A 108 ? 0.2003 0.1791 0.1793 -0.0183 0.0091  0.0019  114 LEU   A CG  
852  C CD1 . LEU   A 108 ? 0.2080 0.1860 0.1880 -0.0174 0.0105  0.0044  114 LEU   A CD1 
853  C CD2 . LEU   A 108 ? 0.2152 0.1983 0.1944 -0.0185 0.0082  0.0056  114 LEU   A CD2 
854  N N   . ARG   A 109 ? 0.2051 0.1742 0.1914 -0.0200 0.0075  -0.0095 115 ARG   A N   
855  C CA  . ARG   A 109 ? 0.2202 0.1897 0.2115 -0.0248 0.0098  -0.0145 115 ARG   A CA  
856  C C   . ARG   A 109 ? 0.2320 0.2038 0.2201 -0.0292 0.0107  -0.0123 115 ARG   A C   
857  O O   . ARG   A 109 ? 0.2331 0.2049 0.2200 -0.0278 0.0098  -0.0080 115 ARG   A O   
858  C CB  . ARG   A 109 ? 0.2595 0.2239 0.2599 -0.0221 0.0073  -0.0194 115 ARG   A CB  
859  C CG  . ARG   A 109 ? 0.3494 0.3079 0.3462 -0.0194 0.0040  -0.0155 115 ARG   A CG  
860  C CD  . ARG   A 109 ? 0.4354 0.3865 0.4404 -0.0154 -0.0012 -0.0195 115 ARG   A CD  
861  N NE  . ARG   A 109 ? 0.4948 0.4408 0.4974 -0.0089 -0.0082 -0.0192 115 ARG   A NE  
862  C CZ  . ARG   A 109 ? 0.5299 0.4731 0.5452 -0.0049 -0.0150 -0.0253 115 ARG   A CZ  
863  N NH1 . ARG   A 109 ? 0.5458 0.4910 0.5792 -0.0065 -0.0140 -0.0322 115 ARG   A NH1 
864  N NH2 . ARG   A 109 ? 0.5178 0.4558 0.5292 0.0007  -0.0231 -0.0253 115 ARG   A NH2 
865  N N   . CYS   A 110 ? 0.2456 0.2177 0.2322 -0.0350 0.0133  -0.0161 116 CYS   A N   
866  C CA  . CYS   A 110 ? 0.2593 0.2329 0.2439 -0.0398 0.0128  -0.0159 116 CYS   A CA  
867  C C   . CYS   A 110 ? 0.2787 0.2477 0.2678 -0.0434 0.0165  -0.0232 116 CYS   A C   
868  O O   . CYS   A 110 ? 0.2896 0.2555 0.2864 -0.0412 0.0187  -0.0275 116 CYS   A O   
869  C CB  . CYS   A 110 ? 0.2905 0.2659 0.2651 -0.0435 0.0109  -0.0144 116 CYS   A CB  
870  S SG  . CYS   A 110 ? 0.3015 0.2687 0.2640 -0.0484 0.0161  -0.0198 116 CYS   A SG  
871  N N   . GLN   A 111 ? 0.3009 0.2694 0.2874 -0.0490 0.0171  -0.0254 117 GLN   A N   
872  C CA  . GLN   A 111 ? 0.3246 0.2878 0.3153 -0.0530 0.0220  -0.0333 117 GLN   A CA  
873  C C   . GLN   A 111 ? 0.3489 0.3073 0.3360 -0.0562 0.0286  -0.0398 117 GLN   A C   
874  O O   . GLN   A 111 ? 0.3825 0.3366 0.3787 -0.0582 0.0346  -0.0474 117 GLN   A O   
875  C CB  . GLN   A 111 ? 0.3662 0.3290 0.3528 -0.0594 0.0214  -0.0354 117 GLN   A CB  
876  C CG  . GLN   A 111 ? 0.4149 0.3777 0.3855 -0.0641 0.0183  -0.0348 117 GLN   A CG  
877  C CD  . GLN   A 111 ? 0.4976 0.4607 0.4660 -0.0698 0.0149  -0.0374 117 GLN   A CD  
878  O OE1 . GLN   A 111 ? 0.5069 0.4762 0.4764 -0.0698 0.0075  -0.0334 117 GLN   A OE1 
879  N NE2 . GLN   A 111 ? 0.5214 0.4779 0.4893 -0.0749 0.0203  -0.0452 117 GLN   A NE2 
880  N N   . HIS   A 112 ? 0.3391 0.2966 0.3137 -0.0572 0.0289  -0.0374 118 HIS   A N   
881  C CA  . HIS   A 112 ? 0.3445 0.2942 0.3120 -0.0616 0.0376  -0.0432 118 HIS   A CA  
882  C C   . HIS   A 112 ? 0.3473 0.2982 0.3288 -0.0573 0.0415  -0.0454 118 HIS   A C   
883  O O   . HIS   A 112 ? 0.3641 0.3085 0.3458 -0.0613 0.0515  -0.0521 118 HIS   A O   
884  C CB  . HIS   A 112 ? 0.3559 0.2993 0.2981 -0.0658 0.0362  -0.0395 118 HIS   A CB  
885  C CG  . HIS   A 112 ? 0.3546 0.2968 0.2841 -0.0700 0.0298  -0.0385 118 HIS   A CG  
886  N ND1 . HIS   A 112 ? 0.3600 0.3101 0.2902 -0.0668 0.0188  -0.0313 118 HIS   A ND1 
887  C CD2 . HIS   A 112 ? 0.3743 0.3081 0.2924 -0.0773 0.0333  -0.0450 118 HIS   A CD2 
888  C CE1 . HIS   A 112 ? 0.3740 0.3216 0.2952 -0.0720 0.0143  -0.0335 118 HIS   A CE1 
889  N NE2 . HIS   A 112 ? 0.3862 0.3234 0.2980 -0.0785 0.0224  -0.0417 118 HIS   A NE2 
890  N N   . GLY   A 113 ? 0.3207 0.2785 0.3126 -0.0498 0.0342  -0.0404 119 GLY   A N   
891  C CA  . GLY   A 113 ? 0.3057 0.2648 0.3115 -0.0454 0.0352  -0.0431 119 GLY   A CA  
892  C C   . GLY   A 113 ? 0.2919 0.2547 0.2927 -0.0400 0.0287  -0.0354 119 GLY   A C   
893  O O   . GLY   A 113 ? 0.2923 0.2582 0.2853 -0.0378 0.0227  -0.0282 119 GLY   A O   
894  N N   . VAL   A 114 ? 0.2732 0.2355 0.2804 -0.0384 0.0312  -0.0379 120 VAL   A N   
895  C CA  . VAL   A 114 ? 0.2705 0.2353 0.2744 -0.0334 0.0262  -0.0322 120 VAL   A CA  
896  C C   . VAL   A 114 ? 0.2812 0.2439 0.2665 -0.0362 0.0276  -0.0257 120 VAL   A C   
897  O O   . VAL   A 114 ? 0.2954 0.2514 0.2722 -0.0415 0.0348  -0.0279 120 VAL   A O   
898  C CB  . VAL   A 114 ? 0.2755 0.2400 0.2946 -0.0314 0.0284  -0.0384 120 VAL   A CB  
899  C CG1 . VAL   A 114 ? 0.2821 0.2477 0.2955 -0.0271 0.0243  -0.0330 120 VAL   A CG1 
900  C CG2 . VAL   A 114 ? 0.2796 0.2459 0.3193 -0.0271 0.0230  -0.0448 120 VAL   A CG2 
901  N N   . VAL   A 115 ? 0.2632 0.2299 0.2426 -0.0323 0.0211  -0.0180 121 VAL   A N   
902  C CA  . VAL   A 115 ? 0.2662 0.2319 0.2324 -0.0332 0.0194  -0.0116 121 VAL   A CA  
903  C C   . VAL   A 115 ? 0.2681 0.2326 0.2351 -0.0296 0.0201  -0.0094 121 VAL   A C   
904  O O   . VAL   A 115 ? 0.2789 0.2376 0.2358 -0.0314 0.0221  -0.0067 121 VAL   A O   
905  C CB  . VAL   A 115 ? 0.2582 0.2301 0.2244 -0.0313 0.0131  -0.0061 121 VAL   A CB  
906  C CG1 . VAL   A 115 ? 0.2560 0.2286 0.2150 -0.0305 0.0089  0.0002  121 VAL   A CG1 
907  C CG2 . VAL   A 115 ? 0.2670 0.2395 0.2332 -0.0354 0.0126  -0.0088 121 VAL   A CG2 
908  N N   . GLY   A 116 ? 0.2359 0.2039 0.2129 -0.0244 0.0179  -0.0103 122 GLY   A N   
909  C CA  . GLY   A 116 ? 0.2309 0.1978 0.2092 -0.0208 0.0181  -0.0090 122 GLY   A CA  
910  C C   . GLY   A 116 ? 0.2288 0.1971 0.2147 -0.0156 0.0144  -0.0114 122 GLY   A C   
911  O O   . GLY   A 116 ? 0.2400 0.2086 0.2304 -0.0146 0.0114  -0.0144 122 GLY   A O   
912  N N   . ILE   A 117 ? 0.2265 0.1936 0.2123 -0.0122 0.0141  -0.0103 123 ILE   A N   
913  C CA  . ILE   A 117 ? 0.2249 0.1902 0.2127 -0.0073 0.0096  -0.0128 123 ILE   A CA  
914  C C   . ILE   A 117 ? 0.2418 0.2063 0.2223 -0.0039 0.0099  -0.0077 123 ILE   A C   
915  O O   . ILE   A 117 ? 0.2490 0.2148 0.2289 -0.0044 0.0132  -0.0039 123 ILE   A O   
916  C CB  . ILE   A 117 ? 0.2448 0.2078 0.2433 -0.0065 0.0087  -0.0207 123 ILE   A CB  
917  C CG1 . ILE   A 117 ? 0.2720 0.2338 0.2723 -0.0089 0.0152  -0.0207 123 ILE   A CG1 
918  C CG2 . ILE   A 117 ? 0.2619 0.2258 0.2736 -0.0082 0.0069  -0.0282 123 ILE   A CG2 
919  C CD1 . ILE   A 117 ? 0.2875 0.2474 0.3014 -0.0089 0.0158  -0.0291 123 ILE   A CD1 
920  N N   . VAL   A 118 ? 0.2189 0.1789 0.1928 -0.0003 0.0070  -0.0076 124 VAL   A N   
921  C CA  . VAL   A 118 ? 0.2172 0.1745 0.1843 0.0025  0.0100  -0.0043 124 VAL   A CA  
922  C C   . VAL   A 118 ? 0.2200 0.1763 0.1909 0.0037  0.0118  -0.0064 124 VAL   A C   
923  O O   . VAL   A 118 ? 0.2399 0.1932 0.2142 0.0043  0.0085  -0.0125 124 VAL   A O   
924  C CB  . VAL   A 118 ? 0.2454 0.1925 0.1989 0.0055  0.0079  -0.0049 124 VAL   A CB  
925  C CG1 . VAL   A 118 ? 0.2591 0.2014 0.2051 0.0076  0.0140  -0.0030 124 VAL   A CG1 
926  C CG2 . VAL   A 118 ? 0.2554 0.2010 0.2044 0.0041  0.0076  -0.0020 124 VAL   A CG2 
927  N N   . SER   A 119 ? 0.2121 0.1703 0.1845 0.0045  0.0164  -0.0023 125 SER   A N   
928  C CA  . SER   A 119 ? 0.2147 0.1706 0.1910 0.0058  0.0189  -0.0037 125 SER   A CA  
929  C C   . SER   A 119 ? 0.2507 0.2039 0.2251 0.0091  0.0234  -0.0020 125 SER   A C   
930  O O   . SER   A 119 ? 0.2705 0.2186 0.2448 0.0109  0.0251  -0.0053 125 SER   A O   
931  C CB  . SER   A 119 ? 0.2296 0.1884 0.2118 0.0033  0.0204  -0.0003 125 SER   A CB  
932  O OG  . SER   A 119 ? 0.2679 0.2224 0.2534 0.0044  0.0234  -0.0009 125 SER   A OG  
933  N N   . THR   A 120 ? 0.2554 0.2116 0.2305 0.0095  0.0266  0.0022  126 THR   A N   
934  C CA  . THR   A 120 ? 0.2587 0.2126 0.2362 0.0122  0.0335  0.0029  126 THR   A CA  
935  C C   . THR   A 120 ? 0.2716 0.2238 0.2440 0.0115  0.0386  0.0039  126 THR   A C   
936  O O   . THR   A 120 ? 0.2677 0.2208 0.2351 0.0093  0.0354  0.0049  126 THR   A O   
937  C CB  . THR   A 120 ? 0.2672 0.2289 0.2616 0.0132  0.0343  0.0077  126 THR   A CB  
938  O OG1 . THR   A 120 ? 0.2769 0.2467 0.2786 0.0116  0.0323  0.0116  126 THR   A OG1 
939  C CG2 . THR   A 120 ? 0.2630 0.2241 0.2597 0.0129  0.0302  0.0089  126 THR   A CG2 
940  N N   . GLY   A 121 ? 0.2912 0.2402 0.2663 0.0130  0.0477  0.0034  127 GLY   A N   
941  C CA  . GLY   A 121 ? 0.3284 0.2749 0.3016 0.0114  0.0558  0.0042  127 GLY   A CA  
942  C C   . GLY   A 121 ? 0.3627 0.3091 0.3486 0.0128  0.0678  0.0031  127 GLY   A C   
943  O O   . GLY   A 121 ? 0.3779 0.3271 0.3757 0.0155  0.0684  0.0022  127 GLY   A O   
944  N N   . GLY   A 122 ? 0.3667 0.3097 0.3528 0.0106  0.0783  0.0028  128 GLY   A N   
945  C CA  . GLY   A 122 ? 0.3801 0.3223 0.3812 0.0110  0.0929  0.0002  128 GLY   A CA  
946  C C   . GLY   A 122 ? 0.4229 0.3530 0.4115 0.0072  0.1070  -0.0012 128 GLY   A C   
947  O O   . GLY   A 122 ? 0.4526 0.3703 0.4137 0.0051  0.1044  0.0000  128 GLY   A O   
948  N N   . ASN   A 123 ? 0.4227 0.3549 0.4324 0.0061  0.1226  -0.0039 129 ASN   A N   
949  C CA  . ASN   A 123 ? 0.4380 0.3568 0.4367 0.0013  0.1395  -0.0056 129 ASN   A CA  
950  C C   . ASN   A 123 ? 0.4205 0.3497 0.4315 -0.0020 0.1349  -0.0021 129 ASN   A C   
951  O O   . ASN   A 123 ? 0.4163 0.3628 0.4648 -0.0029 0.1371  -0.0029 129 ASN   A O   
952  C CB  . ASN   A 123 ? 0.4479 0.3658 0.4690 0.0004  0.1601  -0.0110 129 ASN   A CB  
953  C CG  . ASN   A 123 ? 0.5124 0.4075 0.5108 -0.0052 0.1823  -0.0139 129 ASN   A CG  
954  O OD1 . ASN   A 123 ? 0.5588 0.4380 0.5240 -0.0083 0.1813  -0.0107 129 ASN   A OD1 
955  N ND2 . ASN   A 123 ? 0.4957 0.3868 0.5110 -0.0067 0.2034  -0.0200 129 ASN   A ND2 
956  N N   . GLY   A 124 ? 0.3914 0.3090 0.3718 -0.0037 0.1282  0.0010  130 GLY   A N   
957  C CA  . GLY   A 124 ? 0.3779 0.3027 0.3663 -0.0071 0.1239  0.0039  130 GLY   A CA  
958  C C   . GLY   A 124 ? 0.3346 0.2804 0.3419 -0.0050 0.1044  0.0065  130 GLY   A C   
959  O O   . GLY   A 124 ? 0.3344 0.2902 0.3559 -0.0078 0.1004  0.0079  130 GLY   A O   
960  N N   . LEU   A 125 ? 0.3162 0.2667 0.3216 -0.0007 0.0932  0.0068  131 LEU   A N   
961  C CA  . LEU   A 125 ? 0.3019 0.2676 0.3190 0.0009  0.0763  0.0093  131 LEU   A CA  
962  C C   . LEU   A 125 ? 0.3109 0.2691 0.3033 0.0025  0.0656  0.0099  131 LEU   A C   
963  O O   . LEU   A 125 ? 0.3311 0.2754 0.3026 0.0042  0.0683  0.0079  131 LEU   A O   
964  C CB  . LEU   A 125 ? 0.2998 0.2782 0.3429 0.0044  0.0732  0.0091  131 LEU   A CB  
965  C CG  . LEU   A 125 ? 0.2973 0.2874 0.3753 0.0039  0.0799  0.0076  131 LEU   A CG  
966  C CD1 . LEU   A 125 ? 0.3088 0.3055 0.4081 0.0089  0.0784  0.0069  131 LEU   A CD1 
967  C CD2 . LEU   A 125 ? 0.2867 0.2901 0.3814 0.0014  0.0698  0.0093  131 LEU   A CD2 
968  N N   . VAL   A 126 ? 0.2784 0.2452 0.2740 0.0017  0.0535  0.0118  132 VAL   A N   
969  C CA  . VAL   A 126 ? 0.2781 0.2408 0.2586 0.0028  0.0441  0.0112  132 VAL   A CA  
970  C C   . VAL   A 126 ? 0.2627 0.2376 0.2567 0.0026  0.0351  0.0128  132 VAL   A C   
971  O O   . VAL   A 126 ? 0.2686 0.2527 0.2759 0.0006  0.0327  0.0147  132 VAL   A O   
972  C CB  . VAL   A 126 ? 0.2928 0.2473 0.2570 0.0009  0.0410  0.0110  132 VAL   A CB  
973  C CG1 . VAL   A 126 ? 0.3121 0.2747 0.2873 -0.0028 0.0405  0.0129  132 VAL   A CG1 
974  C CG2 . VAL   A 126 ? 0.2868 0.2385 0.2420 0.0022  0.0313  0.0088  132 VAL   A CG2 
975  N N   . GLY   A 127 ? 0.2406 0.2138 0.2309 0.0045  0.0309  0.0119  133 GLY   A N   
976  C CA  . GLY   A 127 ? 0.2485 0.2276 0.2451 0.0038  0.0242  0.0139  133 GLY   A CA  
977  C C   . GLY   A 127 ? 0.2435 0.2189 0.2299 0.0018  0.0199  0.0115  133 GLY   A C   
978  O O   . GLY   A 127 ? 0.2453 0.2141 0.2239 0.0030  0.0204  0.0078  133 GLY   A O   
979  N N   . PHE   A 128 ? 0.2250 0.2038 0.2121 -0.0013 0.0155  0.0129  134 PHE   A N   
980  C CA  . PHE   A 128 ? 0.2240 0.1996 0.2047 -0.0042 0.0137  0.0096  134 PHE   A CA  
981  C C   . PHE   A 128 ? 0.2317 0.2043 0.2101 -0.0059 0.0131  0.0108  134 PHE   A C   
982  O O   . PHE   A 128 ? 0.2256 0.1993 0.2036 -0.0065 0.0101  0.0152  134 PHE   A O   
983  C CB  . PHE   A 128 ? 0.2144 0.1929 0.1942 -0.0079 0.0117  0.0092  134 PHE   A CB  
984  C CG  . PHE   A 128 ? 0.2117 0.1905 0.1920 -0.0070 0.0132  0.0092  134 PHE   A CG  
985  C CD1 . PHE   A 128 ? 0.2076 0.1800 0.1818 -0.0056 0.0132  0.0060  134 PHE   A CD1 
986  C CD2 . PHE   A 128 ? 0.2076 0.1916 0.1947 -0.0076 0.0144  0.0121  134 PHE   A CD2 
987  C CE1 . PHE   A 128 ? 0.2136 0.1815 0.1829 -0.0049 0.0151  0.0070  134 PHE   A CE1 
988  C CE2 . PHE   A 128 ? 0.2167 0.1980 0.2027 -0.0076 0.0186  0.0121  134 PHE   A CE2 
989  C CZ  . PHE   A 128 ? 0.2085 0.1804 0.1831 -0.0064 0.0192  0.0101  134 PHE   A CZ  
990  N N   . ALA   A 129 ? 0.2230 0.1905 0.1996 -0.0068 0.0156  0.0066  135 ALA   A N   
991  C CA  . ALA   A 129 ? 0.2364 0.1974 0.2081 -0.0097 0.0179  0.0072  135 ALA   A CA  
992  C C   . ALA   A 129 ? 0.2483 0.2074 0.2134 -0.0153 0.0183  0.0057  135 ALA   A C   
993  O O   . ALA   A 129 ? 0.2501 0.2105 0.2197 -0.0172 0.0202  -0.0002 135 ALA   A O   
994  C CB  . ALA   A 129 ? 0.2339 0.1902 0.2100 -0.0095 0.0223  0.0016  135 ALA   A CB  
995  N N   . ASP   A 130 ? 0.2510 0.2061 0.2055 -0.0177 0.0159  0.0105  136 ASP   A N   
996  C CA  . ASP   A 130 ? 0.2608 0.2116 0.2052 -0.0238 0.0171  0.0084  136 ASP   A CA  
997  C C   . ASP   A 130 ? 0.2821 0.2226 0.2216 -0.0286 0.0268  0.0030  136 ASP   A C   
998  O O   . ASP   A 130 ? 0.2993 0.2321 0.2364 -0.0283 0.0311  0.0039  136 ASP   A O   
999  C CB  . ASP   A 130 ? 0.3034 0.2483 0.2330 -0.0250 0.0105  0.0148  136 ASP   A CB  
1000 C CG  . ASP   A 130 ? 0.3728 0.3125 0.2889 -0.0312 0.0101  0.0127  136 ASP   A CG  
1001 O OD1 . ASP   A 130 ? 0.3727 0.3207 0.2972 -0.0324 0.0098  0.0088  136 ASP   A OD1 
1002 O OD2 . ASP   A 130 ? 0.4174 0.3424 0.3124 -0.0350 0.0104  0.0149  136 ASP   A OD2 
1003 N N   . VAL   A 131 ? 0.2778 0.2175 0.2180 -0.0334 0.0313  -0.0032 137 VAL   A N   
1004 C CA  . VAL   A 131 ? 0.3009 0.2308 0.2396 -0.0392 0.0429  -0.0098 137 VAL   A CA  
1005 C C   . VAL   A 131 ? 0.3178 0.2372 0.2379 -0.0465 0.0474  -0.0111 137 VAL   A C   
1006 O O   . VAL   A 131 ? 0.3340 0.2422 0.2494 -0.0526 0.0596  -0.0168 137 VAL   A O   
1007 C CB  . VAL   A 131 ? 0.2974 0.2348 0.2604 -0.0382 0.0468  -0.0193 137 VAL   A CB  
1008 C CG1 . VAL   A 131 ? 0.2853 0.2298 0.2616 -0.0315 0.0413  -0.0186 137 VAL   A CG1 
1009 C CG2 . VAL   A 131 ? 0.3006 0.2456 0.2725 -0.0384 0.0435  -0.0235 137 VAL   A CG2 
1010 N N   . ARG   A 132 ? 0.3177 0.2395 0.2269 -0.0463 0.0384  -0.0066 138 ARG   A N   
1011 C CA  . ARG   A 132 ? 0.3275 0.2390 0.2174 -0.0532 0.0409  -0.0086 138 ARG   A CA  
1012 C C   . ARG   A 132 ? 0.3692 0.2578 0.2276 -0.0588 0.0463  -0.0056 138 ARG   A C   
1013 O O   . ARG   A 132 ? 0.3933 0.2689 0.2334 -0.0661 0.0533  -0.0098 138 ARG   A O   
1014 C CB  . ARG   A 132 ? 0.3237 0.2433 0.2116 -0.0518 0.0287  -0.0053 138 ARG   A CB  
1015 C CG  . ARG   A 132 ? 0.3092 0.2463 0.2226 -0.0476 0.0254  -0.0080 138 ARG   A CG  
1016 C CD  . ARG   A 132 ? 0.3080 0.2520 0.2205 -0.0468 0.0146  -0.0045 138 ARG   A CD  
1017 N NE  . ARG   A 132 ? 0.2991 0.2481 0.2140 -0.0414 0.0055  0.0032  138 ARG   A NE  
1018 C CZ  . ARG   A 132 ? 0.2924 0.2498 0.2138 -0.0397 -0.0039 0.0061  138 ARG   A CZ  
1019 N NH1 . ARG   A 132 ? 0.2928 0.2532 0.2156 -0.0434 -0.0060 0.0026  138 ARG   A NH1 
1020 N NH2 . ARG   A 132 ? 0.2858 0.2487 0.2153 -0.0344 -0.0105 0.0117  138 ARG   A NH2 
1021 N N   . ASP   A 133 ? 0.3908 0.2722 0.2404 -0.0556 0.0434  0.0016  139 ASP   A N   
1022 C CA  . ASP   A 133 ? 0.4194 0.2748 0.2360 -0.0606 0.0490  0.0055  139 ASP   A CA  
1023 C C   . ASP   A 133 ? 0.4367 0.2800 0.2550 -0.0663 0.0692  -0.0012 139 ASP   A C   
1024 O O   . ASP   A 133 ? 0.4710 0.2890 0.2595 -0.0721 0.0782  0.0009  139 ASP   A O   
1025 C CB  . ASP   A 133 ? 0.4425 0.2926 0.2495 -0.0544 0.0373  0.0164  139 ASP   A CB  
1026 C CG  . ASP   A 133 ? 0.4733 0.3337 0.3054 -0.0486 0.0402  0.0169  139 ASP   A CG  
1027 O OD1 . ASP   A 133 ? 0.4574 0.3376 0.3185 -0.0457 0.0414  0.0112  139 ASP   A OD1 
1028 O OD2 . ASP   A 133 ? 0.4916 0.3382 0.3122 -0.0470 0.0410  0.0229  139 ASP   A OD2 
1029 N N   . LEU   A 134 ? 0.4040 0.2638 0.2566 -0.0646 0.0758  -0.0091 140 LEU   A N   
1030 C CA  . LEU   A 134 ? 0.4137 0.2651 0.2762 -0.0696 0.0940  -0.0169 140 LEU   A CA  
1031 C C   . LEU   A 134 ? 0.4367 0.2817 0.2989 -0.0780 0.1081  -0.0273 140 LEU   A C   
1032 O O   . LEU   A 134 ? 0.4127 0.2723 0.3075 -0.0778 0.1128  -0.0373 140 LEU   A O   
1033 C CB  . LEU   A 134 ? 0.3853 0.2576 0.2864 -0.0631 0.0908  -0.0213 140 LEU   A CB  
1034 C CG  . LEU   A 134 ? 0.3902 0.2681 0.2928 -0.0550 0.0789  -0.0124 140 LEU   A CG  
1035 C CD1 . LEU   A 134 ? 0.3732 0.2684 0.3094 -0.0496 0.0765  -0.0183 140 LEU   A CD1 
1036 C CD2 . LEU   A 134 ? 0.4102 0.2667 0.2897 -0.0573 0.0848  -0.0058 140 LEU   A CD2 
1037 N N   . LEU   A 135 ? 0.4673 0.2890 0.2910 -0.0853 0.1139  -0.0248 141 LEU   A N   
1038 C CA  . LEU   A 135 ? 0.4888 0.3010 0.3058 -0.0941 0.1281  -0.0345 141 LEU   A CA  
1039 C C   . LEU   A 135 ? 0.5049 0.3139 0.3459 -0.1001 0.1506  -0.0468 141 LEU   A C   
1040 O O   . LEU   A 135 ? 0.5130 0.3269 0.3721 -0.1042 0.1604  -0.0580 141 LEU   A O   
1041 C CB  . LEU   A 135 ? 0.5242 0.3068 0.2886 -0.1013 0.1303  -0.0296 141 LEU   A CB  
1042 C CG  . LEU   A 135 ? 0.5605 0.3433 0.3005 -0.0956 0.1064  -0.0175 141 LEU   A CG  
1043 C CD1 . LEU   A 135 ? 0.6004 0.3532 0.2889 -0.1033 0.1071  -0.0152 141 LEU   A CD1 
1044 C CD2 . LEU   A 135 ? 0.5460 0.3582 0.3147 -0.0890 0.0902  -0.0186 141 LEU   A CD2 
1045 N N   . TRP   A 136 ? 0.5153 0.3162 0.3594 -0.1007 0.1591  -0.0455 142 TRP   A N   
1046 C CA  . TRP   A 136 ? 0.5197 0.3175 0.3906 -0.1068 0.1811  -0.0579 142 TRP   A CA  
1047 C C   . TRP   A 136 ? 0.5052 0.3328 0.4315 -0.1015 0.1768  -0.0690 142 TRP   A C   
1048 O O   . TRP   A 136 ? 0.5166 0.3444 0.4716 -0.1069 0.1941  -0.0821 142 TRP   A O   
1049 C CB  . TRP   A 136 ? 0.5180 0.3006 0.3805 -0.1081 0.1894  -0.0534 142 TRP   A CB  
1050 C CG  . TRP   A 136 ? 0.5029 0.3019 0.3777 -0.0973 0.1697  -0.0445 142 TRP   A CG  
1051 C CD1 . TRP   A 136 ? 0.5221 0.3148 0.3676 -0.0917 0.1540  -0.0301 142 TRP   A CD1 
1052 C CD2 . TRP   A 136 ? 0.4718 0.2942 0.3915 -0.0911 0.1645  -0.0505 142 TRP   A CD2 
1053 N NE1 . TRP   A 136 ? 0.5122 0.3229 0.3822 -0.0829 0.1416  -0.0270 142 TRP   A NE1 
1054 C CE2 . TRP   A 136 ? 0.4810 0.3091 0.3939 -0.0825 0.1476  -0.0393 142 TRP   A CE2 
1055 C CE3 . TRP   A 136 ? 0.4529 0.2911 0.4187 -0.0918 0.1715  -0.0649 142 TRP   A CE3 
1056 C CZ2 . TRP   A 136 ? 0.4589 0.3066 0.4049 -0.0753 0.1385  -0.0419 142 TRP   A CZ2 
1057 C CZ3 . TRP   A 136 ? 0.4353 0.2926 0.4336 -0.0842 0.1602  -0.0672 142 TRP   A CZ3 
1058 C CH2 . TRP   A 136 ? 0.4392 0.3004 0.4253 -0.0763 0.1443  -0.0558 142 TRP   A CH2 
1059 N N   . LEU   A 137 ? 0.4869 0.3378 0.4285 -0.0912 0.1541  -0.0642 143 LEU   A N   
1060 C CA  . LEU   A 137 ? 0.4663 0.3414 0.4547 -0.0856 0.1475  -0.0736 143 LEU   A CA  
1061 C C   . LEU   A 137 ? 0.4854 0.3625 0.4909 -0.0904 0.1573  -0.0854 143 LEU   A C   
1062 O O   . LEU   A 137 ? 0.4630 0.3552 0.5107 -0.0875 0.1564  -0.0960 143 LEU   A O   
1063 C CB  . LEU   A 137 ? 0.4439 0.3376 0.4358 -0.0748 0.1231  -0.0650 143 LEU   A CB  
1064 C CG  . LEU   A 137 ? 0.4384 0.3362 0.4289 -0.0683 0.1129  -0.0570 143 LEU   A CG  
1065 C CD1 . LEU   A 137 ? 0.4442 0.3563 0.4319 -0.0592 0.0922  -0.0484 143 LEU   A CD1 
1066 C CD2 . LEU   A 137 ? 0.4276 0.3330 0.4538 -0.0668 0.1167  -0.0665 143 LEU   A CD2 
1067 N N   . ASP   A 138 ? 0.5249 0.3863 0.4976 -0.0972 0.1648  -0.0838 144 ASP   A N   
1068 C CA  . ASP   A 138 ? 0.5577 0.4172 0.5400 -0.1028 0.1759  -0.0948 144 ASP   A CA  
1069 C C   . ASP   A 138 ? 0.6036 0.4447 0.5895 -0.1144 0.2050  -0.1070 144 ASP   A C   
1070 O O   . ASP   A 138 ? 0.6074 0.4437 0.5995 -0.1203 0.2179  -0.1172 144 ASP   A O   
1071 C CB  . ASP   A 138 ? 0.5927 0.4420 0.5344 -0.1053 0.1698  -0.0877 144 ASP   A CB  
1072 C CG  . ASP   A 138 ? 0.6595 0.5250 0.5970 -0.0958 0.1444  -0.0768 144 ASP   A CG  
1073 O OD1 . ASP   A 138 ? 0.6428 0.5285 0.6113 -0.0871 0.1317  -0.0762 144 ASP   A OD1 
1074 O OD2 . ASP   A 138 ? 0.7148 0.5713 0.6173 -0.0975 0.1372  -0.0694 144 ASP   A OD2 
1075 N N   . GLU   A 139 ? 0.6395 0.4681 0.6203 -0.1182 0.2173  -0.1064 145 GLU   A N   
1076 C CA  . GLU   A 139 ? 0.6855 0.4936 0.6682 -0.1303 0.2481  -0.1182 145 GLU   A CA  
1077 C C   . GLU   A 139 ? 0.7120 0.5238 0.7293 -0.1311 0.2585  -0.1248 145 GLU   A C   
1078 O O   . GLU   A 139 ? 0.7215 0.5420 0.7413 -0.1239 0.2435  -0.1164 145 GLU   A O   
1079 C CB  . GLU   A 139 ? 0.7522 0.5247 0.6706 -0.1400 0.2614  -0.1106 145 GLU   A CB  
1080 C CG  . GLU   A 139 ? 0.8422 0.6033 0.7210 -0.1362 0.2482  -0.0935 145 GLU   A CG  
1081 C CD  . GLU   A 139 ? 0.9861 0.7224 0.8015 -0.1393 0.2422  -0.0820 145 GLU   A CD  
1082 O OE1 . GLU   A 139 ? 1.0454 0.7470 0.8172 -0.1484 0.2591  -0.0791 145 GLU   A OE1 
1083 O OE2 . GLU   A 139 ? 1.0132 0.7631 0.8219 -0.1328 0.2203  -0.0759 145 GLU   A OE2 
1084 N N   . GLU   A 140 ? 0.7242 0.5291 0.7702 -0.1404 0.2856  -0.1412 146 GLU   A N   
1085 C CA  . GLU   A 140 ? 0.7337 0.5396 0.8185 -0.1442 0.3019  -0.1519 146 GLU   A CA  
1086 C C   . GLU   A 140 ? 0.7286 0.5615 0.8516 -0.1325 0.2782  -0.1501 146 GLU   A C   
1087 O O   . GLU   A 140 ? 0.7275 0.5628 0.8820 -0.1345 0.2872  -0.1578 146 GLU   A O   
1088 C CB  . GLU   A 140 ? 0.7977 0.5680 0.8383 -0.1555 0.3264  -0.1471 146 GLU   A CB  
1089 C CG  . GLU   A 140 ? 0.8818 0.6446 0.8877 -0.1502 0.3114  -0.1297 146 GLU   A CG  
1090 C CD  . GLU   A 140 ? 0.9674 0.7237 0.9942 -0.1540 0.3261  -0.1341 146 GLU   A CD  
1091 O OE1 . GLU   A 140 ? 0.9768 0.7344 0.9908 -0.1475 0.3110  -0.1223 146 GLU   A OE1 
1092 O OE2 . GLU   A 140 ? 0.9929 0.7433 1.0519 -0.1636 0.3534  -0.1502 146 GLU   A OE2 
1093 N N1  . A1BRI B .   ? 0.3746 0.3017 0.3376 0.0187  0.0445  -0.0119 201 A1BRI A N1  
1094 C C4  . A1BRI B .   ? 0.3805 0.2966 0.3310 0.0191  0.0413  -0.0196 201 A1BRI A C4  
1095 C C5  . A1BRI B .   ? 0.3802 0.3075 0.3399 0.0184  0.0501  -0.0090 201 A1BRI A C5  
1096 C C6  . A1BRI B .   ? 0.4384 0.3472 0.3705 0.0173  0.0639  -0.0111 201 A1BRI A C6  
1097 C C7  . A1BRI B .   ? 0.4492 0.3516 0.3819 0.0174  0.0784  -0.0127 201 A1BRI A C7  
1098 C C8  . A1BRI B .   ? 0.4564 0.3524 0.3809 0.0151  0.0884  -0.0114 201 A1BRI A C8  
1099 C C10 . A1BRI B .   ? 0.4548 0.3571 0.3690 0.0134  0.0674  -0.0062 201 A1BRI A C10 
1100 C C13 . A1BRI B .   ? 0.4323 0.3514 0.3554 0.0139  0.0278  -0.0084 201 A1BRI A C13 
1101 F F2  . A1BRI B .   ? 0.4411 0.3508 0.3547 0.0158  0.0234  -0.0143 201 A1BRI A F2  
1102 F F   . A1BRI B .   ? 0.4178 0.3498 0.3604 0.0131  0.0274  -0.0069 201 A1BRI A F   
1103 F F1  . A1BRI B .   ? 0.4280 0.3463 0.3463 0.0130  0.0211  -0.0076 201 A1BRI A F1  
1104 C C12 . A1BRI B .   ? 0.4469 0.3615 0.3652 0.0137  0.0396  -0.0058 201 A1BRI A C12 
1105 O O2  . A1BRI B .   ? 0.4471 0.3625 0.3736 0.0152  0.0460  -0.0078 201 A1BRI A O2  
1106 C C11 . A1BRI B .   ? 0.4454 0.3544 0.3689 0.0153  0.0586  -0.0081 201 A1BRI A C11 
1107 C C9  . A1BRI B .   ? 0.4573 0.3528 0.3719 0.0129  0.0829  -0.0079 201 A1BRI A C9  
1108 N N2  . A1BRI B .   ? 0.4156 0.3291 0.3558 0.0185  0.0556  -0.0129 201 A1BRI A N2  
1109 O O1  . A1BRI B .   ? 0.3631 0.3006 0.3360 0.0177  0.0506  -0.0037 201 A1BRI A O1  
1110 C C3  . A1BRI B .   ? 0.3803 0.3000 0.3363 0.0176  0.0318  -0.0225 201 A1BRI A C3  
1111 C C2  . A1BRI B .   ? 0.3727 0.3012 0.3468 0.0164  0.0335  -0.0182 201 A1BRI A C2  
1112 C C14 . A1BRI B .   ? 0.3639 0.2998 0.3443 0.0186  0.0427  -0.0078 201 A1BRI A C14 
1113 C C1  . A1BRI B .   ? 0.3648 0.3020 0.3446 0.0160  0.0353  -0.0097 201 A1BRI A C1  
1114 C C   . A1BRI B .   ? 0.3454 0.2869 0.3362 0.0149  0.0349  -0.0050 201 A1BRI A C   
1115 O O   . A1BRI B .   ? 0.3509 0.2903 0.3492 0.0169  0.0385  -0.0027 201 A1BRI A O   
1116 N N   . A1BRI B .   ? 0.3281 0.2733 0.3183 0.0117  0.0309  -0.0035 201 A1BRI A N   
# 
