data_7HUQ
# 
_entry.id   7HUQ 
# 
_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   7HUQ         pdb_00007huq 10.2210/pdb7huq/pdb 
WWPDB D_1001407955 ?            ?                   
# 
_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                        7HUQ 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-10 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frank.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lithgo, R.M.'        1  ? 
'Fairhead, M.'        2  ? 
'Koekemoer, L.'       3  ? 
'Balcomb, B.H.'       4  ? 
'Capkin, E.'          5  ? 
'Chandran, A.V.'      6  ? 
'Golding, M.'         7  ? 
'Godoy, A.S.'         8  ? 
'Aschenbrenner, J.C.' 9  ? 
'Marples, P.G.'       10 ? 
'Ni, X.'              11 ? 
'Thompson, W.'        12 ? 
'Tomlinson, C.W.E.'   13 ? 
'Wild, C.'            14 ? 
'Winokan, M.'         15 ? 
'Xavier, M.-A.E.'     16 ? 
'Kenton, N.'          17 ? 
'Tucker, J.'          18 ? 
'DiPoto, M.'          19 ? 
'Lee, A.'             20 ? 
'Fearon, D.'          21 ? 
'von Delft, F.'       22 ? 
# 
_citation.id                        primary 
_citation.title                     
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Lithgo, R.M.'        ? 1  
primary 'Fairhead, M.'        ? 2  
primary 'Koekemoer, L.'       ? 3  
primary 'Balcomb, B.H.'       ? 4  
primary 'Capkin, E.'          ? 5  
primary 'Chandran, A.V.'      ? 6  
primary 'Golding, M.'         ? 7  
primary 'Godoy, A.S.'         ? 8  
primary 'Aschenbrenner, J.C.' ? 9  
primary 'Marples, P.G.'       ? 10 
primary 'Ni, X.'              ? 11 
primary 'Thompson, W.'        ? 12 
primary 'Tomlinson, C.W.E.'   ? 13 
primary 'Wild, C.'            ? 14 
primary 'Winokan, M.'         ? 15 
primary 'Xavier, M.-A.E.'     ? 16 
primary 'Kenton, N.'          ? 17 
primary 'Tucker, J.'          ? 18 
primary 'DiPoto, M.'          ? 19 
primary 'Lee, A.'             ? 20 
primary 'Fearon, D.'          ? 21 
primary 'von Delft, F.'       ? 22 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Protease 2A'                                                   15892.732 1   3.4.22.29 ? ? ? 
2 non-polymer syn '(3S)-1-[(2-methylpyridin-4-yl)acetyl]piperidine-3-carboxamide' 261.320   1   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                      65.409    1   ?         ? ? ? 
4 water       nat water                                                           18.015    147 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'P2A,Picornain 2A,Protein 2A' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '(3S)-1-[(2-methylpyridin-4-yl)acetyl]piperidine-3-carboxamide' A1BSN 
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 
A1BSN non-polymer         . '(3S)-1-[(2-methylpyridin-4-yl)acetyl]piperidine-3-carboxamide' ? 'C14 H19 N3 O2'  261.320 
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 ?   ?   ?   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        A1BSN 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BSN 
_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 A1BSN 1   201 201 A1BSN LIG A . 
C 3 ZN    1   202 1   ZN    ZN  A . 
D 4 HOH   1   301 116 HOH   HOH A . 
D 4 HOH   2   302 95  HOH   HOH A . 
D 4 HOH   3   303 142 HOH   HOH A . 
D 4 HOH   4   304 134 HOH   HOH A . 
D 4 HOH   5   305 83  HOH   HOH A . 
D 4 HOH   6   306 38  HOH   HOH A . 
D 4 HOH   7   307 91  HOH   HOH A . 
D 4 HOH   8   308 127 HOH   HOH A . 
D 4 HOH   9   309 26  HOH   HOH A . 
D 4 HOH   10  310 55  HOH   HOH A . 
D 4 HOH   11  311 141 HOH   HOH A . 
D 4 HOH   12  312 105 HOH   HOH A . 
D 4 HOH   13  313 113 HOH   HOH A . 
D 4 HOH   14  314 15  HOH   HOH A . 
D 4 HOH   15  315 11  HOH   HOH A . 
D 4 HOH   16  316 1   HOH   HOH A . 
D 4 HOH   17  317 97  HOH   HOH A . 
D 4 HOH   18  318 24  HOH   HOH A . 
D 4 HOH   19  319 9   HOH   HOH A . 
D 4 HOH   20  320 27  HOH   HOH A . 
D 4 HOH   21  321 93  HOH   HOH A . 
D 4 HOH   22  322 4   HOH   HOH A . 
D 4 HOH   23  323 56  HOH   HOH A . 
D 4 HOH   24  324 52  HOH   HOH A . 
D 4 HOH   25  325 87  HOH   HOH A . 
D 4 HOH   26  326 82  HOH   HOH A . 
D 4 HOH   27  327 40  HOH   HOH A . 
D 4 HOH   28  328 66  HOH   HOH A . 
D 4 HOH   29  329 139 HOH   HOH A . 
D 4 HOH   30  330 53  HOH   HOH A . 
D 4 HOH   31  331 103 HOH   HOH A . 
D 4 HOH   32  332 31  HOH   HOH A . 
D 4 HOH   33  333 3   HOH   HOH A . 
D 4 HOH   34  334 81  HOH   HOH A . 
D 4 HOH   35  335 62  HOH   HOH A . 
D 4 HOH   36  336 140 HOH   HOH A . 
D 4 HOH   37  337 16  HOH   HOH A . 
D 4 HOH   38  338 12  HOH   HOH A . 
D 4 HOH   39  339 45  HOH   HOH A . 
D 4 HOH   40  340 67  HOH   HOH A . 
D 4 HOH   41  341 147 HOH   HOH A . 
D 4 HOH   42  342 135 HOH   HOH A . 
D 4 HOH   43  343 68  HOH   HOH A . 
D 4 HOH   44  344 92  HOH   HOH A . 
D 4 HOH   45  345 108 HOH   HOH A . 
D 4 HOH   46  346 29  HOH   HOH A . 
D 4 HOH   47  347 25  HOH   HOH A . 
D 4 HOH   48  348 63  HOH   HOH A . 
D 4 HOH   49  349 42  HOH   HOH A . 
D 4 HOH   50  350 77  HOH   HOH A . 
D 4 HOH   51  351 17  HOH   HOH A . 
D 4 HOH   52  352 28  HOH   HOH A . 
D 4 HOH   53  353 138 HOH   HOH A . 
D 4 HOH   54  354 61  HOH   HOH A . 
D 4 HOH   55  355 37  HOH   HOH A . 
D 4 HOH   56  356 41  HOH   HOH A . 
D 4 HOH   57  357 85  HOH   HOH A . 
D 4 HOH   58  358 58  HOH   HOH A . 
D 4 HOH   59  359 101 HOH   HOH A . 
D 4 HOH   60  360 78  HOH   HOH A . 
D 4 HOH   61  361 115 HOH   HOH A . 
D 4 HOH   62  362 75  HOH   HOH A . 
D 4 HOH   63  363 44  HOH   HOH A . 
D 4 HOH   64  364 5   HOH   HOH A . 
D 4 HOH   65  365 100 HOH   HOH A . 
D 4 HOH   66  366 107 HOH   HOH A . 
D 4 HOH   67  367 64  HOH   HOH A . 
D 4 HOH   68  368 14  HOH   HOH A . 
D 4 HOH   69  369 144 HOH   HOH A . 
D 4 HOH   70  370 96  HOH   HOH A . 
D 4 HOH   71  371 13  HOH   HOH A . 
D 4 HOH   72  372 79  HOH   HOH A . 
D 4 HOH   73  373 60  HOH   HOH A . 
D 4 HOH   74  374 86  HOH   HOH A . 
D 4 HOH   75  375 8   HOH   HOH A . 
D 4 HOH   76  376 70  HOH   HOH A . 
D 4 HOH   77  377 146 HOH   HOH A . 
D 4 HOH   78  378 151 HOH   HOH A . 
D 4 HOH   79  379 50  HOH   HOH A . 
D 4 HOH   80  380 136 HOH   HOH A . 
D 4 HOH   81  381 10  HOH   HOH A . 
D 4 HOH   82  382 18  HOH   HOH A . 
D 4 HOH   83  383 143 HOH   HOH A . 
D 4 HOH   84  384 71  HOH   HOH A . 
D 4 HOH   85  385 43  HOH   HOH A . 
D 4 HOH   86  386 137 HOH   HOH A . 
D 4 HOH   87  387 89  HOH   HOH A . 
D 4 HOH   88  388 112 HOH   HOH A . 
D 4 HOH   89  389 35  HOH   HOH A . 
D 4 HOH   90  390 34  HOH   HOH A . 
D 4 HOH   91  391 111 HOH   HOH A . 
D 4 HOH   92  392 39  HOH   HOH A . 
D 4 HOH   93  393 109 HOH   HOH A . 
D 4 HOH   94  394 19  HOH   HOH A . 
D 4 HOH   95  395 149 HOH   HOH A . 
D 4 HOH   96  396 65  HOH   HOH A . 
D 4 HOH   97  397 33  HOH   HOH A . 
D 4 HOH   98  398 84  HOH   HOH A . 
D 4 HOH   99  399 74  HOH   HOH A . 
D 4 HOH   100 400 22  HOH   HOH A . 
D 4 HOH   101 401 54  HOH   HOH A . 
D 4 HOH   102 402 125 HOH   HOH A . 
D 4 HOH   103 403 69  HOH   HOH A . 
D 4 HOH   104 404 133 HOH   HOH A . 
D 4 HOH   105 405 99  HOH   HOH A . 
D 4 HOH   106 406 76  HOH   HOH A . 
D 4 HOH   107 407 57  HOH   HOH A . 
D 4 HOH   108 408 104 HOH   HOH A . 
D 4 HOH   109 409 80  HOH   HOH A . 
D 4 HOH   110 410 6   HOH   HOH A . 
D 4 HOH   111 411 72  HOH   HOH A . 
D 4 HOH   112 412 94  HOH   HOH A . 
D 4 HOH   113 413 48  HOH   HOH A . 
D 4 HOH   114 414 59  HOH   HOH A . 
D 4 HOH   115 415 110 HOH   HOH A . 
D 4 HOH   116 416 32  HOH   HOH A . 
D 4 HOH   117 417 73  HOH   HOH A . 
D 4 HOH   118 418 30  HOH   HOH A . 
D 4 HOH   119 419 121 HOH   HOH A . 
D 4 HOH   120 420 123 HOH   HOH A . 
D 4 HOH   121 421 117 HOH   HOH A . 
D 4 HOH   122 422 131 HOH   HOH A . 
D 4 HOH   123 423 90  HOH   HOH A . 
D 4 HOH   124 424 88  HOH   HOH A . 
D 4 HOH   125 425 7   HOH   HOH A . 
D 4 HOH   126 426 23  HOH   HOH A . 
D 4 HOH   127 427 132 HOH   HOH A . 
D 4 HOH   128 428 148 HOH   HOH A . 
D 4 HOH   129 429 51  HOH   HOH A . 
D 4 HOH   130 430 20  HOH   HOH A . 
D 4 HOH   131 431 114 HOH   HOH A . 
D 4 HOH   132 432 129 HOH   HOH A . 
D 4 HOH   133 433 21  HOH   HOH A . 
D 4 HOH   134 434 120 HOH   HOH A . 
D 4 HOH   135 435 122 HOH   HOH A . 
D 4 HOH   136 436 152 HOH   HOH A . 
D 4 HOH   137 437 119 HOH   HOH A . 
D 4 HOH   138 438 124 HOH   HOH A . 
D 4 HOH   139 439 128 HOH   HOH A . 
D 4 HOH   140 440 2   HOH   HOH A . 
D 4 HOH   141 441 106 HOH   HOH A . 
D 4 HOH   142 442 98  HOH   HOH A . 
D 4 HOH   143 443 102 HOH   HOH A . 
D 4 HOH   144 444 145 HOH   HOH A . 
D 4 HOH   145 445 126 HOH   HOH A . 
D 4 HOH   146 446 130 HOH   HOH A . 
D 4 HOH   147 447 118 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           7HUQ 
_cell.length_a           73.469 
_cell.length_b           61.750 
_cell.length_c           32.809 
_cell.angle_alpha        90.00 
_cell.angle_beta         92.78 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HUQ 
_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          7HUQ 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.34 
_exptl_crystal.density_percent_sol   47.41 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2024-10-08 
_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   0.92209 
_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        0.92209 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HUQ 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             36.69 
_reflns.d_resolution_high            1.59 
_reflns.number_obs                   14776 
_reflns.percent_possible_obs         74.5 
_reflns.pdbx_Rmerge_I_obs            0.050 
_reflns.pdbx_netI_over_sigmaI        16.2 
_reflns.pdbx_redundancy              4.7 
_reflns.pdbx_Rrim_I_all              0.055 
_reflns.pdbx_Rpim_I_all              0.022 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     69453 
_reflns.pdbx_chi_squared             0.81 
_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                  1.59 
_reflns_shell.d_res_low                   1.67 
_reflns_shell.number_measured_all         793 
_reflns_shell.number_unique_obs           636 
_reflns_shell.Rmerge_I_obs                0.334 
_reflns_shell.pdbx_chi_squared            0.26 
_reflns_shell.pdbx_redundancy             1.2 
_reflns_shell.percent_possible_obs        22.0 
_reflns_shell.pdbx_netI_over_sigmaI_obs   1.2 
_reflns_shell.pdbx_Rrim_I_all             0.460 
_reflns_shell.pdbx_Rpim_I_all             0.315 
_reflns_shell.pdbx_CC_half                0.745 
_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                                 7HUQ 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     14748 
_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                             32.77 
_refine.ls_d_res_high                            1.588 
_refine.ls_percent_reflns_obs                    74.4 
_refine.ls_R_factor_obs                          0.1829 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1802 
_refine.ls_R_factor_R_free                       0.2426 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.540 
_refine.ls_number_reflns_R_free                  670 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.954 
_refine.correlation_coeff_Fo_to_Fc_free          0.918 
_refine.B_iso_mean                               21.86 
_refine.aniso_B[1][1]                            -1.67200 
_refine.aniso_B[2][2]                            -1.31030 
_refine.aniso_B[3][3]                            2.98230 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -0.49990 
_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             0.112 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.123 
_refine.pdbx_overall_SU_R_Blow_DPI               0.120 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.127 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HUQ 
_refine_analyze.Luzzati_coordinate_error_obs    0.21 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1074 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         20 
_refine_hist.number_atoms_solvent             147 
_refine_hist.number_atoms_total               1241 
_refine_hist.d_res_high                       1.588 
_refine_hist.d_res_low                        32.77 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
t_bond_d                  0.010 ? 2.00  1124 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               0.95  ? 2.00  1530 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  376  'X-RAY DIFFRACTION' SINUSOIDAL   
t_incorr_chiral_ct        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_pseud_angle             ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_trig_c_planes           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_gen_planes              ?     ? 5.00  203  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1124 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           3.96  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           14.37 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  138  'X-RAY DIFFRACTION' SEMIHARMONIC 
t_sum_occupancies         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_distance        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_angle           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_torsion         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_ideal_dist_contact      ?     ? 4.00  969  'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   34 
_refine_ls_shell.d_res_high                       1.59 
_refine_ls_shell.d_res_low                        1.65 
_refine_ls_shell.number_reflns_R_work             431 
_refine_ls_shell.R_factor_R_work                  0.2467 
_refine_ls_shell.percent_reflns_obs               19.75 
_refine_ls_shell.R_factor_R_free                  0.2590 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            3.58 
_refine_ls_shell.number_reflns_R_free             16 
_refine_ls_shell.number_reflns_all                447 
_refine_ls_shell.R_factor_all                     0.2471 
# 
_struct.entry_id                  7HUQ 
_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-0031813-001 (A71EV2A-x3194)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HUQ 
_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              7HUQ 
_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 GLU A 100 ? CYS A 104 ? GLU A 106 CYS A 110 5 ? 5 
HELX_P HELX_P6 AA6 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 ? ? ? ? ? ? ? 2.261 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.393 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.406 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 C ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.165 ? ? 
# 
_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_555 111.2 ? 
2 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 107.3 ? 
3 SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 116.0 ? 
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_555 111.0 ? 
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_555 111.1 ? 
# 
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 GLY A 43  ? N GLY A 49  O GLY A 7   ? O GLY A 13  
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                   7HUQ 
_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_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     302 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     302 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   2_656 
_pdbx_validate_symm_contact.dist              1.13 
# 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         15.3479 
_pdbx_refine_tls.origin_y         7.1091 
_pdbx_refine_tls.origin_z         14.2932 
_pdbx_refine_tls.T[1][1]          -0.0291 
_pdbx_refine_tls.T[2][2]          -0.0471 
_pdbx_refine_tls.T[3][3]          -0.0148 
_pdbx_refine_tls.T[1][2]          -0.0016 
_pdbx_refine_tls.T[1][3]          -0.0142 
_pdbx_refine_tls.T[2][3]          -0.0067 
_pdbx_refine_tls.L[1][1]          1.2249 
_pdbx_refine_tls.L[2][2]          2.0635 
_pdbx_refine_tls.L[3][3]          0.8419 
_pdbx_refine_tls.L[1][2]          1.1935 
_pdbx_refine_tls.L[1][3]          -0.2793 
_pdbx_refine_tls.L[2][3]          -0.6394 
_pdbx_refine_tls.S[1][1]          -0.0865 
_pdbx_refine_tls.S[1][2]          0.0306 
_pdbx_refine_tls.S[1][3]          0.0627 
_pdbx_refine_tls.S[2][1]          0.0283 
_pdbx_refine_tls.S[2][2]          0.0699 
_pdbx_refine_tls.S[2][3]          -0.0567 
_pdbx_refine_tls.S[3][1]          0.0090 
_pdbx_refine_tls.S[3][2]          -0.0454 
_pdbx_refine_tls.S[3][3]          0.0166 
# 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   '{ A|* }' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A GLU 146 ? A GLU 140 
2 1 Y 1 A ALA 147 ? A ALA 141 
3 1 Y 1 A MET 148 ? A MET 142 
4 1 Y 1 A GLU 149 ? A GLU 143 
5 1 Y 1 A GLN 150 ? A GLN 144 
# 
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 
A1BSN N1   N  N N 1   
A1BSN C4   C  N N 2   
A1BSN C5   C  N N 3   
A1BSN C6   C  N N 4   
A1BSN C7   C  N N 5   
A1BSN C8   C  N N 6   
A1BSN C10  C  N N 7   
A1BSN C13  C  Y N 8   
A1BSN O1   O  N N 9   
A1BSN C9   C  N S 10  
A1BSN C11  C  N N 11  
A1BSN N    N  N N 12  
A1BSN O    O  N N 13  
A1BSN C3   C  Y N 14  
A1BSN C2   C  Y N 15  
A1BSN C12  C  Y N 16  
A1BSN N2   N  Y N 17  
A1BSN C1   C  Y N 18  
A1BSN C    C  N N 19  
A1BSN H14  H  N N 20  
A1BSN H13  H  N N 21  
A1BSN H6   H  N N 22  
A1BSN H5   H  N N 23  
A1BSN H8   H  N N 24  
A1BSN H7   H  N N 25  
A1BSN H9   H  N N 26  
A1BSN H10  H  N N 27  
A1BSN H11  H  N N 28  
A1BSN H12  H  N N 29  
A1BSN H18  H  N N 30  
A1BSN H    H  N N 31  
A1BSN H15  H  N N 32  
A1BSN H16  H  N N 33  
A1BSN H4   H  N N 34  
A1BSN H17  H  N N 35  
A1BSN H2   H  N N 36  
A1BSN H1   H  N N 37  
A1BSN H3   H  N N 38  
ALA   N    N  N N 39  
ALA   CA   C  N S 40  
ALA   C    C  N N 41  
ALA   O    O  N N 42  
ALA   CB   C  N N 43  
ALA   OXT  O  N N 44  
ALA   H    H  N N 45  
ALA   H2   H  N N 46  
ALA   HA   H  N N 47  
ALA   HB1  H  N N 48  
ALA   HB2  H  N N 49  
ALA   HB3  H  N N 50  
ALA   HXT  H  N N 51  
ARG   N    N  N N 52  
ARG   CA   C  N S 53  
ARG   C    C  N N 54  
ARG   O    O  N N 55  
ARG   CB   C  N N 56  
ARG   CG   C  N N 57  
ARG   CD   C  N N 58  
ARG   NE   N  N N 59  
ARG   CZ   C  N N 60  
ARG   NH1  N  N N 61  
ARG   NH2  N  N N 62  
ARG   OXT  O  N N 63  
ARG   H    H  N N 64  
ARG   H2   H  N N 65  
ARG   HA   H  N N 66  
ARG   HB2  H  N N 67  
ARG   HB3  H  N N 68  
ARG   HG2  H  N N 69  
ARG   HG3  H  N N 70  
ARG   HD2  H  N N 71  
ARG   HD3  H  N N 72  
ARG   HE   H  N N 73  
ARG   HH11 H  N N 74  
ARG   HH12 H  N N 75  
ARG   HH21 H  N N 76  
ARG   HH22 H  N N 77  
ARG   HXT  H  N N 78  
ASN   N    N  N N 79  
ASN   CA   C  N S 80  
ASN   C    C  N N 81  
ASN   O    O  N N 82  
ASN   CB   C  N N 83  
ASN   CG   C  N N 84  
ASN   OD1  O  N N 85  
ASN   ND2  N  N N 86  
ASN   OXT  O  N N 87  
ASN   H    H  N N 88  
ASN   H2   H  N N 89  
ASN   HA   H  N N 90  
ASN   HB2  H  N N 91  
ASN   HB3  H  N N 92  
ASN   HD21 H  N N 93  
ASN   HD22 H  N N 94  
ASN   HXT  H  N N 95  
ASP   N    N  N N 96  
ASP   CA   C  N S 97  
ASP   C    C  N N 98  
ASP   O    O  N N 99  
ASP   CB   C  N N 100 
ASP   CG   C  N N 101 
ASP   OD1  O  N N 102 
ASP   OD2  O  N N 103 
ASP   OXT  O  N N 104 
ASP   H    H  N N 105 
ASP   H2   H  N N 106 
ASP   HA   H  N N 107 
ASP   HB2  H  N N 108 
ASP   HB3  H  N N 109 
ASP   HD2  H  N N 110 
ASP   HXT  H  N N 111 
CYS   N    N  N N 112 
CYS   CA   C  N R 113 
CYS   C    C  N N 114 
CYS   O    O  N N 115 
CYS   CB   C  N N 116 
CYS   SG   S  N N 117 
CYS   OXT  O  N N 118 
CYS   H    H  N N 119 
CYS   H2   H  N N 120 
CYS   HA   H  N N 121 
CYS   HB2  H  N N 122 
CYS   HB3  H  N N 123 
CYS   HG   H  N N 124 
CYS   HXT  H  N N 125 
GLN   N    N  N N 126 
GLN   CA   C  N S 127 
GLN   C    C  N N 128 
GLN   O    O  N N 129 
GLN   CB   C  N N 130 
GLN   CG   C  N N 131 
GLN   CD   C  N N 132 
GLN   OE1  O  N N 133 
GLN   NE2  N  N N 134 
GLN   OXT  O  N N 135 
GLN   H    H  N N 136 
GLN   H2   H  N N 137 
GLN   HA   H  N N 138 
GLN   HB2  H  N N 139 
GLN   HB3  H  N N 140 
GLN   HG2  H  N N 141 
GLN   HG3  H  N N 142 
GLN   HE21 H  N N 143 
GLN   HE22 H  N N 144 
GLN   HXT  H  N N 145 
GLU   N    N  N N 146 
GLU   CA   C  N S 147 
GLU   C    C  N N 148 
GLU   O    O  N N 149 
GLU   CB   C  N N 150 
GLU   CG   C  N N 151 
GLU   CD   C  N N 152 
GLU   OE1  O  N N 153 
GLU   OE2  O  N N 154 
GLU   OXT  O  N N 155 
GLU   H    H  N N 156 
GLU   H2   H  N N 157 
GLU   HA   H  N N 158 
GLU   HB2  H  N N 159 
GLU   HB3  H  N N 160 
GLU   HG2  H  N N 161 
GLU   HG3  H  N N 162 
GLU   HE2  H  N N 163 
GLU   HXT  H  N N 164 
GLY   N    N  N N 165 
GLY   CA   C  N N 166 
GLY   C    C  N N 167 
GLY   O    O  N N 168 
GLY   OXT  O  N N 169 
GLY   H    H  N N 170 
GLY   H2   H  N N 171 
GLY   HA2  H  N N 172 
GLY   HA3  H  N N 173 
GLY   HXT  H  N N 174 
HIS   N    N  N N 175 
HIS   CA   C  N S 176 
HIS   C    C  N N 177 
HIS   O    O  N N 178 
HIS   CB   C  N N 179 
HIS   CG   C  Y N 180 
HIS   ND1  N  Y N 181 
HIS   CD2  C  Y N 182 
HIS   CE1  C  Y N 183 
HIS   NE2  N  Y N 184 
HIS   OXT  O  N N 185 
HIS   H    H  N N 186 
HIS   H2   H  N N 187 
HIS   HA   H  N N 188 
HIS   HB2  H  N N 189 
HIS   HB3  H  N N 190 
HIS   HD1  H  N N 191 
HIS   HD2  H  N N 192 
HIS   HE1  H  N N 193 
HIS   HE2  H  N N 194 
HIS   HXT  H  N N 195 
HOH   O    O  N N 196 
HOH   H1   H  N N 197 
HOH   H2   H  N N 198 
ILE   N    N  N N 199 
ILE   CA   C  N S 200 
ILE   C    C  N N 201 
ILE   O    O  N N 202 
ILE   CB   C  N S 203 
ILE   CG1  C  N N 204 
ILE   CG2  C  N N 205 
ILE   CD1  C  N N 206 
ILE   OXT  O  N N 207 
ILE   H    H  N N 208 
ILE   H2   H  N N 209 
ILE   HA   H  N N 210 
ILE   HB   H  N N 211 
ILE   HG12 H  N N 212 
ILE   HG13 H  N N 213 
ILE   HG21 H  N N 214 
ILE   HG22 H  N N 215 
ILE   HG23 H  N N 216 
ILE   HD11 H  N N 217 
ILE   HD12 H  N N 218 
ILE   HD13 H  N N 219 
ILE   HXT  H  N N 220 
LEU   N    N  N N 221 
LEU   CA   C  N S 222 
LEU   C    C  N N 223 
LEU   O    O  N N 224 
LEU   CB   C  N N 225 
LEU   CG   C  N N 226 
LEU   CD1  C  N N 227 
LEU   CD2  C  N N 228 
LEU   OXT  O  N N 229 
LEU   H    H  N N 230 
LEU   H2   H  N N 231 
LEU   HA   H  N N 232 
LEU   HB2  H  N N 233 
LEU   HB3  H  N N 234 
LEU   HG   H  N N 235 
LEU   HD11 H  N N 236 
LEU   HD12 H  N N 237 
LEU   HD13 H  N N 238 
LEU   HD21 H  N N 239 
LEU   HD22 H  N N 240 
LEU   HD23 H  N N 241 
LEU   HXT  H  N N 242 
LYS   N    N  N N 243 
LYS   CA   C  N S 244 
LYS   C    C  N N 245 
LYS   O    O  N N 246 
LYS   CB   C  N N 247 
LYS   CG   C  N N 248 
LYS   CD   C  N N 249 
LYS   CE   C  N N 250 
LYS   NZ   N  N N 251 
LYS   OXT  O  N N 252 
LYS   H    H  N N 253 
LYS   H2   H  N N 254 
LYS   HA   H  N N 255 
LYS   HB2  H  N N 256 
LYS   HB3  H  N N 257 
LYS   HG2  H  N N 258 
LYS   HG3  H  N N 259 
LYS   HD2  H  N N 260 
LYS   HD3  H  N N 261 
LYS   HE2  H  N N 262 
LYS   HE3  H  N N 263 
LYS   HZ1  H  N N 264 
LYS   HZ2  H  N N 265 
LYS   HZ3  H  N N 266 
LYS   HXT  H  N N 267 
MET   N    N  N N 268 
MET   CA   C  N S 269 
MET   C    C  N N 270 
MET   O    O  N N 271 
MET   CB   C  N N 272 
MET   CG   C  N N 273 
MET   SD   S  N N 274 
MET   CE   C  N N 275 
MET   OXT  O  N N 276 
MET   H    H  N N 277 
MET   H2   H  N N 278 
MET   HA   H  N N 279 
MET   HB2  H  N N 280 
MET   HB3  H  N N 281 
MET   HG2  H  N N 282 
MET   HG3  H  N N 283 
MET   HE1  H  N N 284 
MET   HE2  H  N N 285 
MET   HE3  H  N N 286 
MET   HXT  H  N N 287 
PHE   N    N  N N 288 
PHE   CA   C  N S 289 
PHE   C    C  N N 290 
PHE   O    O  N N 291 
PHE   CB   C  N N 292 
PHE   CG   C  Y N 293 
PHE   CD1  C  Y N 294 
PHE   CD2  C  Y N 295 
PHE   CE1  C  Y N 296 
PHE   CE2  C  Y N 297 
PHE   CZ   C  Y N 298 
PHE   OXT  O  N N 299 
PHE   H    H  N N 300 
PHE   H2   H  N N 301 
PHE   HA   H  N N 302 
PHE   HB2  H  N N 303 
PHE   HB3  H  N N 304 
PHE   HD1  H  N N 305 
PHE   HD2  H  N N 306 
PHE   HE1  H  N N 307 
PHE   HE2  H  N N 308 
PHE   HZ   H  N N 309 
PHE   HXT  H  N N 310 
PRO   N    N  N N 311 
PRO   CA   C  N S 312 
PRO   C    C  N N 313 
PRO   O    O  N N 314 
PRO   CB   C  N N 315 
PRO   CG   C  N N 316 
PRO   CD   C  N N 317 
PRO   OXT  O  N N 318 
PRO   H    H  N N 319 
PRO   HA   H  N N 320 
PRO   HB2  H  N N 321 
PRO   HB3  H  N N 322 
PRO   HG2  H  N N 323 
PRO   HG3  H  N N 324 
PRO   HD2  H  N N 325 
PRO   HD3  H  N N 326 
PRO   HXT  H  N N 327 
SER   N    N  N N 328 
SER   CA   C  N S 329 
SER   C    C  N N 330 
SER   O    O  N N 331 
SER   CB   C  N N 332 
SER   OG   O  N N 333 
SER   OXT  O  N N 334 
SER   H    H  N N 335 
SER   H2   H  N N 336 
SER   HA   H  N N 337 
SER   HB2  H  N N 338 
SER   HB3  H  N N 339 
SER   HG   H  N N 340 
SER   HXT  H  N N 341 
THR   N    N  N N 342 
THR   CA   C  N S 343 
THR   C    C  N N 344 
THR   O    O  N N 345 
THR   CB   C  N R 346 
THR   OG1  O  N N 347 
THR   CG2  C  N N 348 
THR   OXT  O  N N 349 
THR   H    H  N N 350 
THR   H2   H  N N 351 
THR   HA   H  N N 352 
THR   HB   H  N N 353 
THR   HG1  H  N N 354 
THR   HG21 H  N N 355 
THR   HG22 H  N N 356 
THR   HG23 H  N N 357 
THR   HXT  H  N N 358 
TRP   N    N  N N 359 
TRP   CA   C  N S 360 
TRP   C    C  N N 361 
TRP   O    O  N N 362 
TRP   CB   C  N N 363 
TRP   CG   C  Y N 364 
TRP   CD1  C  Y N 365 
TRP   CD2  C  Y N 366 
TRP   NE1  N  Y N 367 
TRP   CE2  C  Y N 368 
TRP   CE3  C  Y N 369 
TRP   CZ2  C  Y N 370 
TRP   CZ3  C  Y N 371 
TRP   CH2  C  Y N 372 
TRP   OXT  O  N N 373 
TRP   H    H  N N 374 
TRP   H2   H  N N 375 
TRP   HA   H  N N 376 
TRP   HB2  H  N N 377 
TRP   HB3  H  N N 378 
TRP   HD1  H  N N 379 
TRP   HE1  H  N N 380 
TRP   HE3  H  N N 381 
TRP   HZ2  H  N N 382 
TRP   HZ3  H  N N 383 
TRP   HH2  H  N N 384 
TRP   HXT  H  N N 385 
TYR   N    N  N N 386 
TYR   CA   C  N S 387 
TYR   C    C  N N 388 
TYR   O    O  N N 389 
TYR   CB   C  N N 390 
TYR   CG   C  Y N 391 
TYR   CD1  C  Y N 392 
TYR   CD2  C  Y N 393 
TYR   CE1  C  Y N 394 
TYR   CE2  C  Y N 395 
TYR   CZ   C  Y N 396 
TYR   OH   O  N N 397 
TYR   OXT  O  N N 398 
TYR   H    H  N N 399 
TYR   H2   H  N N 400 
TYR   HA   H  N N 401 
TYR   HB2  H  N N 402 
TYR   HB3  H  N N 403 
TYR   HD1  H  N N 404 
TYR   HD2  H  N N 405 
TYR   HE1  H  N N 406 
TYR   HE2  H  N N 407 
TYR   HH   H  N N 408 
TYR   HXT  H  N N 409 
VAL   N    N  N N 410 
VAL   CA   C  N S 411 
VAL   C    C  N N 412 
VAL   O    O  N N 413 
VAL   CB   C  N N 414 
VAL   CG1  C  N N 415 
VAL   CG2  C  N N 416 
VAL   OXT  O  N N 417 
VAL   H    H  N N 418 
VAL   H2   H  N N 419 
VAL   HA   H  N N 420 
VAL   HB   H  N N 421 
VAL   HG11 H  N N 422 
VAL   HG12 H  N N 423 
VAL   HG13 H  N N 424 
VAL   HG21 H  N N 425 
VAL   HG22 H  N N 426 
VAL   HG23 H  N N 427 
VAL   HXT  H  N N 428 
ZN    ZN   ZN N N 429 
# 
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 
A1BSN C   C1   sing N N 1   
A1BSN C1  C2   doub Y N 2   
A1BSN C2  C3   sing Y N 3   
A1BSN C3  C4   sing N N 4   
A1BSN C4  C5   sing N N 5   
A1BSN O   C5   doub N N 6   
A1BSN C5  N    sing N N 7   
A1BSN N   C6   sing N N 8   
A1BSN C6  C7   sing N N 9   
A1BSN C7  C8   sing N N 10  
A1BSN C8  C9   sing N N 11  
A1BSN C9  C10  sing N N 12  
A1BSN N1  C10  sing N N 13  
A1BSN C10 O1   doub N N 14  
A1BSN C11 C9   sing N N 15  
A1BSN N   C11  sing N N 16  
A1BSN C12 C3   doub Y N 17  
A1BSN C13 C12  sing Y N 18  
A1BSN N2  C13  doub Y N 19  
A1BSN C1  N2   sing Y N 20  
A1BSN N1  H14  sing N N 21  
A1BSN N1  H13  sing N N 22  
A1BSN C4  H6   sing N N 23  
A1BSN C4  H5   sing N N 24  
A1BSN C6  H8   sing N N 25  
A1BSN C6  H7   sing N N 26  
A1BSN C7  H9   sing N N 27  
A1BSN C7  H10  sing N N 28  
A1BSN C8  H11  sing N N 29  
A1BSN C8  H12  sing N N 30  
A1BSN C13 H18  sing N N 31  
A1BSN C9  H    sing N N 32  
A1BSN C11 H15  sing N N 33  
A1BSN C11 H16  sing N N 34  
A1BSN C2  H4   sing N N 35  
A1BSN C12 H17  sing N N 36  
A1BSN C   H2   sing N N 37  
A1BSN C   H1   sing N N 38  
A1BSN C   H3   sing N N 39  
ALA   N   CA   sing N N 40  
ALA   N   H    sing N N 41  
ALA   N   H2   sing N N 42  
ALA   CA  C    sing N N 43  
ALA   CA  CB   sing N N 44  
ALA   CA  HA   sing N N 45  
ALA   C   O    doub N N 46  
ALA   C   OXT  sing N N 47  
ALA   CB  HB1  sing N N 48  
ALA   CB  HB2  sing N N 49  
ALA   CB  HB3  sing N N 50  
ALA   OXT HXT  sing N N 51  
ARG   N   CA   sing N N 52  
ARG   N   H    sing N N 53  
ARG   N   H2   sing N N 54  
ARG   CA  C    sing N N 55  
ARG   CA  CB   sing N N 56  
ARG   CA  HA   sing N N 57  
ARG   C   O    doub N N 58  
ARG   C   OXT  sing N N 59  
ARG   CB  CG   sing N N 60  
ARG   CB  HB2  sing N N 61  
ARG   CB  HB3  sing N N 62  
ARG   CG  CD   sing N N 63  
ARG   CG  HG2  sing N N 64  
ARG   CG  HG3  sing N N 65  
ARG   CD  NE   sing N N 66  
ARG   CD  HD2  sing N N 67  
ARG   CD  HD3  sing N N 68  
ARG   NE  CZ   sing N N 69  
ARG   NE  HE   sing N N 70  
ARG   CZ  NH1  sing N N 71  
ARG   CZ  NH2  doub N N 72  
ARG   NH1 HH11 sing N N 73  
ARG   NH1 HH12 sing N N 74  
ARG   NH2 HH21 sing N N 75  
ARG   NH2 HH22 sing N N 76  
ARG   OXT HXT  sing N N 77  
ASN   N   CA   sing N N 78  
ASN   N   H    sing N N 79  
ASN   N   H2   sing N N 80  
ASN   CA  C    sing N N 81  
ASN   CA  CB   sing N N 82  
ASN   CA  HA   sing N N 83  
ASN   C   O    doub N N 84  
ASN   C   OXT  sing N N 85  
ASN   CB  CG   sing N N 86  
ASN   CB  HB2  sing N N 87  
ASN   CB  HB3  sing N N 88  
ASN   CG  OD1  doub N N 89  
ASN   CG  ND2  sing N N 90  
ASN   ND2 HD21 sing N N 91  
ASN   ND2 HD22 sing N N 92  
ASN   OXT HXT  sing N N 93  
ASP   N   CA   sing N N 94  
ASP   N   H    sing N N 95  
ASP   N   H2   sing N N 96  
ASP   CA  C    sing N N 97  
ASP   CA  CB   sing N N 98  
ASP   CA  HA   sing N N 99  
ASP   C   O    doub N N 100 
ASP   C   OXT  sing N N 101 
ASP   CB  CG   sing N N 102 
ASP   CB  HB2  sing N N 103 
ASP   CB  HB3  sing N N 104 
ASP   CG  OD1  doub N N 105 
ASP   CG  OD2  sing N N 106 
ASP   OD2 HD2  sing N N 107 
ASP   OXT HXT  sing N N 108 
CYS   N   CA   sing N N 109 
CYS   N   H    sing N N 110 
CYS   N   H2   sing N N 111 
CYS   CA  C    sing N N 112 
CYS   CA  CB   sing N N 113 
CYS   CA  HA   sing N N 114 
CYS   C   O    doub N N 115 
CYS   C   OXT  sing N N 116 
CYS   CB  SG   sing N N 117 
CYS   CB  HB2  sing N N 118 
CYS   CB  HB3  sing N N 119 
CYS   SG  HG   sing N N 120 
CYS   OXT HXT  sing N N 121 
GLN   N   CA   sing N N 122 
GLN   N   H    sing N N 123 
GLN   N   H2   sing N N 124 
GLN   CA  C    sing N N 125 
GLN   CA  CB   sing N N 126 
GLN   CA  HA   sing N N 127 
GLN   C   O    doub N N 128 
GLN   C   OXT  sing N N 129 
GLN   CB  CG   sing N N 130 
GLN   CB  HB2  sing N N 131 
GLN   CB  HB3  sing N N 132 
GLN   CG  CD   sing N N 133 
GLN   CG  HG2  sing N N 134 
GLN   CG  HG3  sing N N 135 
GLN   CD  OE1  doub N N 136 
GLN   CD  NE2  sing N N 137 
GLN   NE2 HE21 sing N N 138 
GLN   NE2 HE22 sing N N 139 
GLN   OXT HXT  sing N N 140 
GLU   N   CA   sing N N 141 
GLU   N   H    sing N N 142 
GLU   N   H2   sing N N 143 
GLU   CA  C    sing N N 144 
GLU   CA  CB   sing N N 145 
GLU   CA  HA   sing N N 146 
GLU   C   O    doub N N 147 
GLU   C   OXT  sing N N 148 
GLU   CB  CG   sing N N 149 
GLU   CB  HB2  sing N N 150 
GLU   CB  HB3  sing N N 151 
GLU   CG  CD   sing N N 152 
GLU   CG  HG2  sing N N 153 
GLU   CG  HG3  sing N N 154 
GLU   CD  OE1  doub N N 155 
GLU   CD  OE2  sing N N 156 
GLU   OE2 HE2  sing N N 157 
GLU   OXT HXT  sing N N 158 
GLY   N   CA   sing N N 159 
GLY   N   H    sing N N 160 
GLY   N   H2   sing N N 161 
GLY   CA  C    sing N N 162 
GLY   CA  HA2  sing N N 163 
GLY   CA  HA3  sing N N 164 
GLY   C   O    doub N N 165 
GLY   C   OXT  sing N N 166 
GLY   OXT HXT  sing N N 167 
HIS   N   CA   sing N N 168 
HIS   N   H    sing N N 169 
HIS   N   H2   sing N N 170 
HIS   CA  C    sing N N 171 
HIS   CA  CB   sing N N 172 
HIS   CA  HA   sing N N 173 
HIS   C   O    doub N N 174 
HIS   C   OXT  sing N N 175 
HIS   CB  CG   sing N N 176 
HIS   CB  HB2  sing N N 177 
HIS   CB  HB3  sing N N 178 
HIS   CG  ND1  sing Y N 179 
HIS   CG  CD2  doub Y N 180 
HIS   ND1 CE1  doub Y N 181 
HIS   ND1 HD1  sing N N 182 
HIS   CD2 NE2  sing Y N 183 
HIS   CD2 HD2  sing N N 184 
HIS   CE1 NE2  sing Y N 185 
HIS   CE1 HE1  sing N N 186 
HIS   NE2 HE2  sing N N 187 
HIS   OXT HXT  sing N N 188 
HOH   O   H1   sing N N 189 
HOH   O   H2   sing N N 190 
ILE   N   CA   sing N N 191 
ILE   N   H    sing N N 192 
ILE   N   H2   sing N N 193 
ILE   CA  C    sing N N 194 
ILE   CA  CB   sing N N 195 
ILE   CA  HA   sing N N 196 
ILE   C   O    doub N N 197 
ILE   C   OXT  sing N N 198 
ILE   CB  CG1  sing N N 199 
ILE   CB  CG2  sing N N 200 
ILE   CB  HB   sing N N 201 
ILE   CG1 CD1  sing N N 202 
ILE   CG1 HG12 sing N N 203 
ILE   CG1 HG13 sing N N 204 
ILE   CG2 HG21 sing N N 205 
ILE   CG2 HG22 sing N N 206 
ILE   CG2 HG23 sing N N 207 
ILE   CD1 HD11 sing N N 208 
ILE   CD1 HD12 sing N N 209 
ILE   CD1 HD13 sing N N 210 
ILE   OXT HXT  sing N N 211 
LEU   N   CA   sing N N 212 
LEU   N   H    sing N N 213 
LEU   N   H2   sing N N 214 
LEU   CA  C    sing N N 215 
LEU   CA  CB   sing N N 216 
LEU   CA  HA   sing N N 217 
LEU   C   O    doub N N 218 
LEU   C   OXT  sing N N 219 
LEU   CB  CG   sing N N 220 
LEU   CB  HB2  sing N N 221 
LEU   CB  HB3  sing N N 222 
LEU   CG  CD1  sing N N 223 
LEU   CG  CD2  sing N N 224 
LEU   CG  HG   sing N N 225 
LEU   CD1 HD11 sing N N 226 
LEU   CD1 HD12 sing N N 227 
LEU   CD1 HD13 sing N N 228 
LEU   CD2 HD21 sing N N 229 
LEU   CD2 HD22 sing N N 230 
LEU   CD2 HD23 sing N N 231 
LEU   OXT HXT  sing N N 232 
LYS   N   CA   sing N N 233 
LYS   N   H    sing N N 234 
LYS   N   H2   sing N N 235 
LYS   CA  C    sing N N 236 
LYS   CA  CB   sing N N 237 
LYS   CA  HA   sing N N 238 
LYS   C   O    doub N N 239 
LYS   C   OXT  sing N N 240 
LYS   CB  CG   sing N N 241 
LYS   CB  HB2  sing N N 242 
LYS   CB  HB3  sing N N 243 
LYS   CG  CD   sing N N 244 
LYS   CG  HG2  sing N N 245 
LYS   CG  HG3  sing N N 246 
LYS   CD  CE   sing N N 247 
LYS   CD  HD2  sing N N 248 
LYS   CD  HD3  sing N N 249 
LYS   CE  NZ   sing N N 250 
LYS   CE  HE2  sing N N 251 
LYS   CE  HE3  sing N N 252 
LYS   NZ  HZ1  sing N N 253 
LYS   NZ  HZ2  sing N N 254 
LYS   NZ  HZ3  sing N N 255 
LYS   OXT HXT  sing N N 256 
MET   N   CA   sing N N 257 
MET   N   H    sing N N 258 
MET   N   H2   sing N N 259 
MET   CA  C    sing N N 260 
MET   CA  CB   sing N N 261 
MET   CA  HA   sing N N 262 
MET   C   O    doub N N 263 
MET   C   OXT  sing N N 264 
MET   CB  CG   sing N N 265 
MET   CB  HB2  sing N N 266 
MET   CB  HB3  sing N N 267 
MET   CG  SD   sing N N 268 
MET   CG  HG2  sing N N 269 
MET   CG  HG3  sing N N 270 
MET   SD  CE   sing N N 271 
MET   CE  HE1  sing N N 272 
MET   CE  HE2  sing N N 273 
MET   CE  HE3  sing N N 274 
MET   OXT HXT  sing N N 275 
PHE   N   CA   sing N N 276 
PHE   N   H    sing N N 277 
PHE   N   H2   sing N N 278 
PHE   CA  C    sing N N 279 
PHE   CA  CB   sing N N 280 
PHE   CA  HA   sing N N 281 
PHE   C   O    doub N N 282 
PHE   C   OXT  sing N N 283 
PHE   CB  CG   sing N N 284 
PHE   CB  HB2  sing N N 285 
PHE   CB  HB3  sing N N 286 
PHE   CG  CD1  doub Y N 287 
PHE   CG  CD2  sing Y N 288 
PHE   CD1 CE1  sing Y N 289 
PHE   CD1 HD1  sing N N 290 
PHE   CD2 CE2  doub Y N 291 
PHE   CD2 HD2  sing N N 292 
PHE   CE1 CZ   doub Y N 293 
PHE   CE1 HE1  sing N N 294 
PHE   CE2 CZ   sing Y N 295 
PHE   CE2 HE2  sing N N 296 
PHE   CZ  HZ   sing N N 297 
PHE   OXT HXT  sing N N 298 
PRO   N   CA   sing N N 299 
PRO   N   CD   sing N N 300 
PRO   N   H    sing N N 301 
PRO   CA  C    sing N N 302 
PRO   CA  CB   sing N N 303 
PRO   CA  HA   sing N N 304 
PRO   C   O    doub N N 305 
PRO   C   OXT  sing N N 306 
PRO   CB  CG   sing N N 307 
PRO   CB  HB2  sing N N 308 
PRO   CB  HB3  sing N N 309 
PRO   CG  CD   sing N N 310 
PRO   CG  HG2  sing N N 311 
PRO   CG  HG3  sing N N 312 
PRO   CD  HD2  sing N N 313 
PRO   CD  HD3  sing N N 314 
PRO   OXT HXT  sing N N 315 
SER   N   CA   sing N N 316 
SER   N   H    sing N N 317 
SER   N   H2   sing N N 318 
SER   CA  C    sing N N 319 
SER   CA  CB   sing N N 320 
SER   CA  HA   sing N N 321 
SER   C   O    doub N N 322 
SER   C   OXT  sing N N 323 
SER   CB  OG   sing N N 324 
SER   CB  HB2  sing N N 325 
SER   CB  HB3  sing N N 326 
SER   OG  HG   sing N N 327 
SER   OXT HXT  sing N N 328 
THR   N   CA   sing N N 329 
THR   N   H    sing N N 330 
THR   N   H2   sing N N 331 
THR   CA  C    sing N N 332 
THR   CA  CB   sing N N 333 
THR   CA  HA   sing N N 334 
THR   C   O    doub N N 335 
THR   C   OXT  sing N N 336 
THR   CB  OG1  sing N N 337 
THR   CB  CG2  sing N N 338 
THR   CB  HB   sing N N 339 
THR   OG1 HG1  sing N N 340 
THR   CG2 HG21 sing N N 341 
THR   CG2 HG22 sing N N 342 
THR   CG2 HG23 sing N N 343 
THR   OXT HXT  sing N N 344 
TRP   N   CA   sing N N 345 
TRP   N   H    sing N N 346 
TRP   N   H2   sing N N 347 
TRP   CA  C    sing N N 348 
TRP   CA  CB   sing N N 349 
TRP   CA  HA   sing N N 350 
TRP   C   O    doub N N 351 
TRP   C   OXT  sing N N 352 
TRP   CB  CG   sing N N 353 
TRP   CB  HB2  sing N N 354 
TRP   CB  HB3  sing N N 355 
TRP   CG  CD1  doub Y N 356 
TRP   CG  CD2  sing Y N 357 
TRP   CD1 NE1  sing Y N 358 
TRP   CD1 HD1  sing N N 359 
TRP   CD2 CE2  doub Y N 360 
TRP   CD2 CE3  sing Y N 361 
TRP   NE1 CE2  sing Y N 362 
TRP   NE1 HE1  sing N N 363 
TRP   CE2 CZ2  sing Y N 364 
TRP   CE3 CZ3  doub Y N 365 
TRP   CE3 HE3  sing N N 366 
TRP   CZ2 CH2  doub Y N 367 
TRP   CZ2 HZ2  sing N N 368 
TRP   CZ3 CH2  sing Y N 369 
TRP   CZ3 HZ3  sing N N 370 
TRP   CH2 HH2  sing N N 371 
TRP   OXT HXT  sing N N 372 
TYR   N   CA   sing N N 373 
TYR   N   H    sing N N 374 
TYR   N   H2   sing N N 375 
TYR   CA  C    sing N N 376 
TYR   CA  CB   sing N N 377 
TYR   CA  HA   sing N N 378 
TYR   C   O    doub N N 379 
TYR   C   OXT  sing N N 380 
TYR   CB  CG   sing N N 381 
TYR   CB  HB2  sing N N 382 
TYR   CB  HB3  sing N N 383 
TYR   CG  CD1  doub Y N 384 
TYR   CG  CD2  sing Y N 385 
TYR   CD1 CE1  sing Y N 386 
TYR   CD1 HD1  sing N N 387 
TYR   CD2 CE2  doub Y N 388 
TYR   CD2 HD2  sing N N 389 
TYR   CE1 CZ   doub Y N 390 
TYR   CE1 HE1  sing N N 391 
TYR   CE2 CZ   sing Y N 392 
TYR   CE2 HE2  sing N N 393 
TYR   CZ  OH   sing N N 394 
TYR   OH  HH   sing N N 395 
TYR   OXT HXT  sing N N 396 
VAL   N   CA   sing N N 397 
VAL   N   H    sing N N 398 
VAL   N   H2   sing N N 399 
VAL   CA  C    sing N N 400 
VAL   CA  CB   sing N N 401 
VAL   CA  HA   sing N N 402 
VAL   C   O    doub N N 403 
VAL   C   OXT  sing N N 404 
VAL   CB  CG1  sing N N 405 
VAL   CB  CG2  sing N N 406 
VAL   CB  HB   sing N N 407 
VAL   CG1 HG11 sing N N 408 
VAL   CG1 HG12 sing N N 409 
VAL   CG1 HG13 sing N N 410 
VAL   CG2 HG21 sing N N 411 
VAL   CG2 HG22 sing N N 412 
VAL   CG2 HG23 sing N N 413 
VAL   OXT HXT  sing N N 414 
# 
_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                    7HUQ 
_atom_sites.fract_transf_matrix[1][1]   0.013611 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000661 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016194 
_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]   0.030515 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER   A 1 1   ? 19.236 6.486   24.315 1.00 21.53 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 20.408 6.664   23.453 1.00 22.54 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 20.491 5.503   22.451 1.00 21.87 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 19.801 4.493   22.625 1.00 22.31 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 21.682 6.720   24.303 1.00 25.14 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 21.828 5.488   24.992 1.00 28.36 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 21.322 5.654   21.422 1.00 20.67 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 21.521 4.615   20.422 1.00 20.01 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 21.790 5.186   19.045 1.00 19.89 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 21.376 6.310   18.739 1.00 20.10 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 22.445 4.404   18.194 1.00 18.43 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 22.758 4.851   16.841 1.00 17.70 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 22.766 3.653   15.855 1.00 16.70 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 22.780 2.504   16.299 1.00 15.71 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 24.135 5.506   16.857 1.00 18.17 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 22.773 3.940   14.531 1.00 16.11 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.926 2.961   13.447 1.00 15.46 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 24.314 3.181   12.819 1.00 16.40 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.690 4.312   12.528 1.00 16.84 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.862 3.195   12.357 1.00 15.24 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 20.462 3.210   12.940 1.00 13.92 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 22.017 2.118   11.241 1.00 15.38 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.388 3.812   11.913 1.00 13.62 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 25.082 2.109   12.626 1.00 17.69 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 26.417 2.198   12.069 1.00 18.87 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 26.401 1.424   10.762 1.00 20.42 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 26.228 0.208   10.780 1.00 21.42 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.438 1.606   13.059 1.00 18.73 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.557 2.416   14.329 1.00 18.82 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 28.361 3.551   14.382 1.00 19.45 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 26.806 2.104   15.447 1.00 19.40 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 28.473 4.302   15.547 1.00 19.56 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 26.907 2.849   16.616 1.00 19.84 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 27.709 3.971   16.646 1.00 20.44 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 27.791 4.705   17.792 1.00 21.44 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 26.522 2.122   9.640  1.00 20.17 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 26.493 1.521   8.315  1.00 21.00 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.587 2.161   7.486  1.00 22.44 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.644 3.385   7.375  1.00 23.00 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 25.093 1.659   7.645  1.00 22.37 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.547 3.080   7.771  1.00 21.82 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 25.146 1.222   6.176  1.00 24.09 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.507 1.343   6.965  1.00 22.57 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.646 1.850   6.211  1.00 23.54 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.470 2.844   7.020  1.00 24.42 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.801 2.571   8.178  1.00 25.09 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.718 4.036   6.473  1.00 24.51 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.440 5.069   7.225  1.00 25.15 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.500 6.130   7.790  1.00 24.13 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.906 7.282   7.961  1.00 24.55 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.557 5.687   6.419  1.00 27.49 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.676 4.723   6.145  1.00 33.63 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.385 4.261   7.053  1.00 36.15 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.864 4.410   4.882  1.00 35.10 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.265 5.726   8.147  1.00 22.16 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.292 6.655   8.688  1.00 21.11 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.765 6.211   10.047 1.00 19.75 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.635 5.016   10.310 1.00 19.54 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 27.084 6.784   7.728  1.00 21.25 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.434 7.312   6.356  1.00 22.48 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 27.977 8.582   6.194  1.00 24.13 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.196 6.558   5.220  1.00 23.26 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.282 9.083   4.927  1.00 25.19 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.502 7.042   3.951  1.00 24.28 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 28.032 8.309   3.805  1.00 25.73 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.315 8.791   2.542  1.00 26.89 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.368 7.191   10.867 1.00 17.89 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.730 6.991   12.164 1.00 16.19 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.436 7.806   12.123 1.00 16.46 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.476 9.015   11.907 1.00 16.52 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.660 7.460   13.310 1.00 16.54 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.950 7.709   14.667 1.00 19.64 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.962 8.010   15.791 1.00 21.84 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 27.511 9.056   16.720 1.00 22.88 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 26.982 8.816   17.920 1.00 22.22 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 26.812 7.564   18.340 1.00 20.70 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 26.610 9.824   18.703 1.00 18.77 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 24.294 7.150   12.315 1.00 15.89 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.977 7.826   12.281 1.00 15.45 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.483 7.942   13.708 1.00 14.68 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 22.352 6.924   14.383 1.00 14.41 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.977 7.006   11.438 1.00 16.28 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.636 7.762   11.305 1.00 16.74 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.572 6.668   10.066 1.00 16.39 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 22.192 9.150   14.178 1.00 13.71 ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 21.728 9.330   15.560 1.00 14.06 ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 20.518 10.279  15.546 1.00 13.71 ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 20.312 11.013  14.563 1.00 14.04 ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 22.846 9.943   16.461 1.00 15.69 ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 23.974 8.963   16.701 1.00 18.32 ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 23.373 11.245  15.858 1.00 15.12 ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 19.792 10.378  16.679 1.00 12.74 ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 18.754 11.411  16.811 1.00 13.16 ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 19.500 12.756  16.816 1.00 13.79 ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 20.509 12.899  17.534 1.00 14.06 ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 18.000 11.273  18.150 1.00 14.05 ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 17.132 10.035  18.241 1.00 15.35 ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.584 8.980   18.709 1.00 17.78 ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 15.869 10.122  17.792 1.00 13.54 ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 19.039 13.725  16.008 1.00 12.86 ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 19.701 15.033  15.935 1.00 13.00 ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 19.732 15.711  17.309 1.00 14.01 ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 20.742 16.345  17.647 1.00 14.35 ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 18.995 15.938  14.902 1.00 12.42 ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.766 17.230  14.523 1.00 11.75 ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 18.787 18.133  13.750 1.00 13.79 ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.394 19.356  13.200 1.00 16.10 ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.478 20.515  13.850 1.00 17.52 ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 19.069 20.611  15.106 1.00 15.92 ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 19.970 21.587  13.244 1.00 17.56 ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 18.642 15.562  18.122 1.00 13.42 ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 18.626 16.223  19.437 1.00 14.91 ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 19.630 15.610  20.444 1.00 16.40 ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 19.944 16.251  21.454 1.00 17.99 ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 17.201 16.328  20.034 1.00 15.78 ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 16.613 15.034  20.512 1.00 16.84 ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 15.971 14.178  19.639 1.00 17.55 ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 16.538 14.523  21.772 1.00 17.60 ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 15.563 13.144  20.377 1.00 18.47 ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 15.882 13.306  21.675 1.00 17.75 ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 20.202 14.443  20.115 1.00 15.80 ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 21.192 13.787  20.949 1.00 16.37 ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 22.611 13.815  20.349 1.00 16.85 ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 23.523 13.197  20.916 1.00 17.16 ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 20.744 12.335  21.201 1.00 16.92 ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 19.425 12.179  21.975 1.00 18.33 ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 19.138 10.709  22.253 1.00 18.68 ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 19.437 12.953  23.287 1.00 18.12 ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 22.807 14.494  19.198 1.00 16.56 ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 24.113 14.518  18.554 1.00 17.46 ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 25.188 15.126  19.469 1.00 17.35 ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 24.913 16.083  20.176 1.00 17.75 ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 24.039 15.305  17.245 1.00 17.93 ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 26.401 14.577  19.446 1.00 17.77 ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 27.515 15.077  20.269 1.00 18.27 ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 28.329 16.175  19.529 1.00 19.04 ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 28.107 16.423  18.347 1.00 18.83 ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 28.438 13.877  20.624 1.00 19.87 ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 29.113 13.468  19.431 1.00 21.23 ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 27.677 12.705  21.242 1.00 20.10 ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 29.329 16.788  20.208 1.00 20.20 ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 30.239 17.724  19.571 1.00 22.54 ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 31.005 17.042  18.424 1.00 22.11 ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 31.191 17.649  17.362 1.00 22.51 ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 31.234 18.257  20.611 1.00 25.95 ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 30.613 19.246  21.530 1.00 34.01 ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 30.654 20.598  21.256 1.00 38.24 ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 29.907 19.051  22.666 1.00 36.98 ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 29.988 21.184  22.241 1.00 39.23 ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 29.527 20.292  23.116 1.00 39.00 ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 31.438 15.784  18.623 1.00 20.90 ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 32.156 15.045  17.579 1.00 21.17 ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 31.252 14.770  16.377 1.00 19.67 ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 31.727 14.785  15.242 1.00 19.80 ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 32.700 13.708  18.100 1.00 24.60 ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 33.514 12.954  17.053 1.00 32.53 ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.632 13.369  16.686 1.00 34.45 ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 32.949 11.863  16.501 1.00 33.81 ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 29.948 14.524  16.609 1.00 17.42 ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 29.014 14.307  15.492 1.00 16.25 ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 28.938 15.567  14.633 1.00 16.81 ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 29.075 15.492  13.415 1.00 16.93 ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 27.617 13.982  16.027 1.00 16.60 ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 27.474 12.572  16.541 1.00 19.22 ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 28.070 11.671  15.946 1.00 19.41 ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 26.760 12.379  17.548 1.00 20.60 ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 28.793 16.744  15.277 1.00 16.66 ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.703 18.003  14.527 1.00 17.08 ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 30.044 18.379  13.830 1.00 18.65 ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 30.035 18.992  12.757 1.00 19.06 ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 28.220 19.130  15.457 1.00 17.30 ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 26.731 19.180  15.622 1.00 17.07 ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 26.005 18.750  16.695 1.00 18.15 ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 25.790 19.729  14.687 1.00 16.17 ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 24.654 18.983  16.473 1.00 18.27 ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 24.500 19.574  15.244 1.00 17.38 ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 25.909 20.287  13.407 1.00 16.41 ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 23.342 20.021  14.590 1.00 17.25 ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.764 20.715  12.749 1.00 16.90 ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 23.498 20.584  13.338 1.00 16.98 ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 31.188 18.003  14.437 1.00 18.67 ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.504 18.280  13.848 1.00 19.83 ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.773 17.398  12.604 1.00 20.92 ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.661 17.709  11.809 1.00 22.02 ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 33.605 18.050  14.885 1.00 20.48 ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 32.071 16.263  12.484 1.00 19.44 ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 32.200 15.346  11.351 1.00 19.46 ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.831 15.173  10.661 1.00 19.06 ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.507 14.091  10.182 1.00 18.17 ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.713 14.005  11.839 1.00 19.71 ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 34.108 14.100  12.407 1.00 23.66 ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 35.109 14.106  11.671 1.00 27.14 ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 34.206 14.201  13.713 1.00 23.10 ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 30.059 16.269  10.574 1.00 18.73 ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.727 16.286  9.980  1.00 18.20 ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.738 15.936  8.494  1.00 19.64 ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.506 16.536  7.739  1.00 21.14 ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 28.134 17.697  10.131 1.00 17.22 ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.744 17.932  9.516  1.00 16.81 ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.685 17.062  10.202 1.00 17.24 ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.361 19.396  9.582  1.00 15.80 ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.816 15.047  8.071  1.00 18.36 ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.590 14.659  6.683  1.00 18.63 ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 26.239 15.278  6.238  1.00 18.98 ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 26.133 15.922  5.186  1.00 19.87 ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.566 13.108  6.586  1.00 19.69 ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 27.066 12.647  5.216  1.00 20.14 ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 28.942 12.522  6.909  1.00 20.01 ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 25.202 15.104  7.069  1.00 17.98 ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 23.874 15.585  6.752  1.00 16.64 ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 23.036 15.668  8.025  1.00 15.27 ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 23.140 14.802  8.879  1.00 14.62 ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 23.221 14.607  5.737  1.00 16.94 ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.753 14.818  5.474  1.00 17.45 ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 21.189 15.742  4.636  1.00 19.18 ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.664 14.075  6.044  1.00 17.43 ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.812 15.612  4.648  1.00 19.80 ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.469 14.588  5.498  1.00 18.44 ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.584 13.017  6.968  1.00 17.46 ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 18.215 14.066  5.830  1.00 18.81 ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.347 12.505  7.289  1.00 18.10 ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 18.179 13.035  6.736  1.00 18.21 ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 22.182 16.679  8.132  1.00 14.91 ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 21.251 16.770  9.253  1.00 14.37 ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 19.923 17.358  8.774  1.00 14.91 ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 19.911 18.192  7.860  1.00 14.30 ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 21.848 17.514  10.473 1.00 14.54 ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.413 18.907  10.181 1.00 17.75 ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.376 20.001  10.019 1.00 19.66 ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 21.600 20.932  9.213  1.00 21.02 ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 20.331 19.925  10.695 1.00 19.28 ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 18.810 16.917  9.382  1.00 14.34 ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.486 17.436  9.069  1.00 14.56 ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.684 17.580  10.370 1.00 14.53 ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 16.278 16.591  10.967 1.00 15.43 ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.789 16.573  8.015  1.00 15.41 ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.517 17.164  7.453  1.00 20.83 ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 14.911 18.008  8.127  1.00 23.39 ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 15.121 16.768  6.333  1.00 22.06 ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.484 18.827  10.814 1.00 13.77 ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 15.744 19.152  12.025 0.50 14.52 ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 15.762 19.076  12.053 0.50 14.42 ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 14.290 18.644  11.905 1.00 14.93 ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 13.702 18.163  12.872 1.00 15.46 ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 15.748 20.670  12.219 0.50 16.07 ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 15.875 20.545  12.455 0.50 15.86 ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 15.243 21.044  13.487 0.50 19.12 ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 15.093 21.328  11.577 0.50 17.59 ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 13.689 18.782  10.690 1.00 15.19 ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 12.302 18.339  10.498 1.00 16.26 ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 12.173 16.807  10.667 1.00 15.17 ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 11.086 16.341  10.951 1.00 15.37 ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 11.753 18.790  9.145  1.00 19.20 ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 12.163 17.939  8.085  1.00 23.03 ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 13.261 16.047  10.515 1.00 13.90 ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 13.209 14.577  10.678 1.00 14.47 ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 13.833 14.088  12.018 1.00 14.07 ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 13.788 12.896  12.309 1.00 14.54 ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 13.961 13.888  9.513  1.00 14.61 ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 13.341 14.101  8.154  1.00 15.89 ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 14.137 13.443  7.034  1.00 15.91 ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 14.088 11.975  7.161  1.00 13.79 ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 14.210 11.128  6.145  1.00 16.00 ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 14.423 11.583  4.910  1.00 16.49 ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 14.151 9.812   6.358  1.00 14.80 ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 14.469 14.986  12.791 1.00 13.64 ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 15.207 14.667  14.025 1.00 12.88 ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 16.321 13.686  13.708 1.00 13.07 ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 16.617 12.816  14.527 1.00 13.23 ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 14.300 14.141  15.183 1.00 13.30 ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 15.037 13.858  16.497 1.00 15.02 ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 15.893 14.677  16.885 1.00 13.74 ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 14.793 12.782  17.104 1.00 15.03 ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 16.996 13.849  12.548 1.00 12.80 ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 18.102 12.968  12.191 1.00 12.55 ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 19.391 13.764  11.950 1.00 12.80 ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 19.359 14.885  11.441 1.00 13.20 ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.783 12.180  10.894 1.00 12.49 ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 16.785 11.008  11.010 1.00 13.42 ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 16.679 10.279  9.671  1.00 13.01 ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 17.206 9.998   12.154 1.00 14.67 ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 20.523 13.153  12.295 1.00 12.11 ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 21.856 13.692  12.005 1.00 13.18 ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 22.722 12.479  11.641 1.00 13.55 ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 22.625 11.416  12.274 1.00 14.30 ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 22.486 14.458  13.209 1.00 12.92 ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 23.868 15.133  12.918 1.00 15.08 ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 23.993 16.461  13.612 1.00 14.91 ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 25.048 14.233  13.313 1.00 16.65 ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 23.559 12.624  10.607 1.00 13.79 ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 24.473 11.581  10.174 1.00 14.10 ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 25.888 12.192  10.215 1.00 14.82 ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 26.111 13.299  9.711  1.00 14.71 ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 24.114 11.036  8.757  1.00 15.21 ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 25.168 10.043  8.257  1.00 16.35 ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 22.714 10.399  8.754  1.00 15.51 ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 26.802 11.508  10.905 1.00 14.44 ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 28.199 11.921  10.986 1.00 15.43 ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 29.067 10.828  10.352 1.00 17.45 ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 28.620 9.675   10.206 1.00 17.35 ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 28.612 12.178  12.441 1.00 16.01 ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 28.485 11.034  13.278 1.00 16.32 ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 30.324 11.170  10.018 1.00 18.32 ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 31.251 10.216  9.441  1.00 20.53 ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 32.046 9.503   10.535 1.00 23.90 ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 32.244 10.049  11.627 1.00 25.17 ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 32.198 10.922  8.474  1.00 21.33 ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 32.967 11.894  9.167  1.00 24.10 ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 32.500 8.279   10.253 1.00 25.06 ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 33.246 7.480   11.215 1.00 27.23 ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 34.532 6.970   10.550 1.00 30.40 ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 34.591 6.823   9.320  1.00 30.99 ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 32.413 6.253   11.669 1.00 28.67 ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 32.240 5.370   10.564 1.00 29.72 ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 31.051 6.619   12.238 1.00 28.38 ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? 35.536 6.652   11.359 1.00 32.11 ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? 36.779 6.081   10.839 1.00 34.16 ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? 36.590 4.546   10.700 1.00 36.44 ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? 37.055 3.946   9.724  1.00 37.68 ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? 37.959 6.464   11.755 1.00 34.79 ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? 37.640 6.089   13.096 1.00 35.69 ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? 38.254 7.958   11.732 1.00 35.57 ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? 35.911 3.910   11.669 1.00 36.49 ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? 35.690 2.459   11.623 1.00 37.20 ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 34.508 2.106   10.728 1.00 37.83 ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 33.549 2.876   10.646 1.00 38.39 ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? 35.448 1.928   13.026 1.00 37.46 ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 34.543 0.932   10.092 1.00 37.71 ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 33.442 0.497   9.226  1.00 38.26 ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 32.283 -0.096  10.039 1.00 37.35 ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 32.514 -0.926  10.912 1.00 38.11 ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 33.948 -0.538  8.201  1.00 41.81 ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 33.243 -0.459  6.846  1.00 47.88 ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 33.746 0.695   6.003  1.00 54.40 ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 34.875 1.176   6.168  1.00 57.18 ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 32.925 1.162   5.064  1.00 54.99 ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 31.055 0.302   9.705  1.00 35.57 ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 29.814 -0.161  10.314 1.00 34.45 ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 29.214 -1.333  9.560  1.00 33.25 ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 29.350 -1.431  8.337  1.00 33.73 ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 28.528 -2.214  10.275 1.00 31.69 ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 28.009 -3.437  9.680  1.00 31.10 ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 26.529 -3.639  9.793  1.00 28.84 ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 26.084 -4.763  9.534  1.00 28.30 ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 28.750 -4.636  10.249 1.00 34.08 ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 30.492 -4.662  9.824  1.00 44.32 ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 25.760 -2.588  10.143 1.00 26.86 ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 24.306 -2.711  10.214 1.00 26.22 ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 23.760 -2.709  8.777  1.00 25.03 ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 24.344 -2.096  7.883  1.00 25.46 ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 23.672 -1.552  11.022 1.00 28.09 ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 23.830 -1.639  12.535 1.00 32.70 ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 23.726 -2.749  13.074 1.00 32.84 ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 24.030 -0.573  13.185 1.00 33.45 ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 22.654 -3.387  8.560  1.00 23.26 ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 22.033 -3.470  7.236  1.00 23.27 ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 20.794 -2.585  7.243  1.00 21.76 ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 19.995 -2.715  8.156  1.00 21.48 ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 21.643 -4.939  6.984  1.00 25.83 ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 22.839 -5.657  6.679  1.00 28.39 ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 20.648 -5.099  5.849  1.00 26.21 ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 20.618 -1.709  6.241  1.00 20.15 ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 19.421 -0.875  6.174  1.00 18.90 ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 18.355 -1.602  5.339  1.00 19.21 ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 18.672 -2.136  4.275  1.00 19.87 ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 19.752 0.531   5.590  1.00 18.85 ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 20.982 1.165   6.313  1.00 19.00 ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 18.527 1.465   5.661  1.00 19.72 ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 20.733 1.454   7.819  1.00 19.37 ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 17.109 -1.648  5.822  1.00 17.58 ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 16.017 -2.274  5.055  1.00 17.18 ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 15.628 -1.379  3.868  1.00 17.26 ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 15.579 -0.180  4.010  1.00 16.49 ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 14.790 -2.466  5.952  1.00 16.06 ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 15.345 -1.970  2.705  1.00 17.55 ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 14.845 -1.227  1.544  1.00 18.20 ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 13.515 -1.945  1.201  1.00 19.45 ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 13.502 -2.943  0.453  1.00 19.85 ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 15.841 -1.302  0.388  1.00 19.37 ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 17.227 -0.772  0.737  1.00 21.61 ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 17.275 0.730   1.132  1.00 24.02 ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 18.642 1.117   1.485  1.00 24.23 ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 18.975 2.235   2.127  1.00 24.80 ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 18.040 3.099   2.498  1.00 22.97 ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 20.238 2.479   2.430  1.00 22.37 ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 12.417 -1.463  1.797  1.00 19.42 ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 11.113 -2.155  1.760  1.00 19.92 ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 9.990  -1.199  2.191  1.00 20.88 ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 10.267 -0.061  2.591  1.00 20.18 ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 11.175 -3.348  2.722  1.00 19.56 ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 11.283 -2.887  4.487  1.00 20.17 ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 8.724  -1.709  2.204  1.00 22.11 ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 7.603  -0.947  2.724  1.00 23.52 ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 6.924  -1.690  3.867  1.00 23.01 ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 5.739  -1.478  4.079  1.00 23.18 ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 6.584  -0.520  1.640  1.00 27.60 ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 5.805  -1.638  0.980  1.00 35.79 ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 6.143  -2.824  1.212  1.00 36.69 ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 4.846  -1.331  0.228  1.00 39.96 ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 7.677  -2.517  4.657  1.00 21.62 ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 7.123  -3.242  5.822  1.00 20.25 ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 6.393  -2.297  6.750  1.00 19.49 ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 6.813  -1.151  6.927  1.00 19.61 ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 8.236  -3.953  6.595  1.00 19.91 ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 8.808  -5.494  5.838  1.00 21.26 ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 5.329  -2.773  7.336  1.00 17.81 ? 59  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 53  ? 4.601  -2.060  8.363  1.00 17.24 ? 59  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 53  ? 4.567  -2.870  9.674  1.00 15.54 ? 59  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 53  ? 3.725  -2.608  10.528 1.00 16.03 ? 59  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 53  ? 3.200  -1.644  7.897  1.00 19.07 ? 59  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 53  ? 3.181  -0.345  7.058  1.00 21.69 ? 59  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 53  ? 1.734  0.076   6.855  1.00 24.26 ? 59  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 53  ? 1.154  -0.115  5.777  1.00 22.43 ? 59  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 53  ? 1.090  0.603   7.913  1.00 23.51 ? 59  GLN   A NE2 1 
ATOM   415  N  N   . THR   A 1 54  ? 5.433  -3.890  9.823  1.00 14.11 ? 60  THR   A N   1 
ATOM   416  C  CA  . THR   A 1 54  ? 5.542  -4.662  11.073 1.00 14.97 ? 60  THR   A CA  1 
ATOM   417  C  C   . THR   A 1 54  ? 7.042  -4.846  11.347 1.00 13.93 ? 60  THR   A C   1 
ATOM   418  O  O   . THR   A 1 54  ? 7.861  -4.957  10.426 1.00 13.71 ? 60  THR   A O   1 
ATOM   419  C  CB  . THR   A 1 54  ? 4.843  -6.052  11.031 1.00 18.96 ? 60  THR   A CB  1 
ATOM   420  O  OG1 . THR   A 1 54  ? 5.497  -6.888  10.066 1.00 21.45 ? 60  THR   A OG1 1 
ATOM   421  C  CG2 . THR   A 1 54  ? 3.345  -5.972  10.701 1.00 20.17 ? 60  THR   A CG2 1 
ATOM   422  N  N   . GLY   A 1 55  ? 7.379  -4.893  12.606 1.00 13.39 ? 61  GLY   A N   1 
ATOM   423  C  CA  . GLY   A 1 55  ? 8.764  -5.061  13.027 1.00 13.49 ? 61  GLY   A CA  1 
ATOM   424  C  C   . GLY   A 1 55  ? 8.891  -5.203  14.524 1.00 13.46 ? 61  GLY   A C   1 
ATOM   425  O  O   . GLY   A 1 55  ? 7.899  -5.421  15.213 1.00 13.06 ? 61  GLY   A O   1 
ATOM   426  N  N   . VAL   A 1 56  ? 10.130 -5.067  15.023 1.00 12.88 ? 62  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 56  ? 10.480 -5.212  16.441 1.00 12.68 ? 62  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 56  ? 11.357 -4.045  16.840 1.00 12.16 ? 62  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 56  ? 12.339 -3.763  16.148 1.00 10.89 ? 62  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 56  ? 11.226 -6.552  16.626 1.00 14.09 ? 62  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 56  ? 11.757 -6.703  18.066 1.00 14.79 ? 62  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 56  ? 10.327 -7.738  16.252 1.00 14.71 ? 62  VAL   A CG2 1 
ATOM   433  N  N   . TYR   A 1 57  ? 11.064 -3.403  17.988 1.00 11.93 ? 63  TYR   A N   1 
ATOM   434  C  CA  . TYR   A 1 57  ? 11.915 -2.295  18.465 1.00 11.60 ? 63  TYR   A CA  1 
ATOM   435  C  C   . TYR   A 1 57  ? 12.522 -2.566  19.840 1.00 12.52 ? 63  TYR   A C   1 
ATOM   436  O  O   . TYR   A 1 57  ? 11.933 -3.299  20.650 1.00 12.35 ? 63  TYR   A O   1 
ATOM   437  C  CB  . TYR   A 1 57  ? 11.187 -0.916  18.435 1.00 10.58 ? 63  TYR   A CB  1 
ATOM   438  C  CG  . TYR   A 1 57  ? 10.210 -0.678  19.579 1.00 10.87 ? 63  TYR   A CG  1 
ATOM   439  C  CD1 . TYR   A 1 57  ? 8.923  -1.211  19.549 1.00 11.78 ? 63  TYR   A CD1 1 
ATOM   440  C  CD2 . TYR   A 1 57  ? 10.539 0.161   20.640 1.00 11.49 ? 63  TYR   A CD2 1 
ATOM   441  C  CE1 . TYR   A 1 57  ? 8.012  -0.960  20.580 1.00 12.98 ? 63  TYR   A CE1 1 
ATOM   442  C  CE2 . TYR   A 1 57  ? 9.620  0.461   21.643 1.00 12.03 ? 63  TYR   A CE2 1 
ATOM   443  C  CZ  . TYR   A 1 57  ? 8.373  -0.135  21.636 1.00 12.91 ? 63  TYR   A CZ  1 
ATOM   444  O  OH  . TYR   A 1 57  ? 7.492  0.128   22.664 1.00 14.55 ? 63  TYR   A OH  1 
ATOM   445  N  N   . TYR   A 1 58  ? 13.716 -2.004  20.087 1.00 11.79 ? 64  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 58  ? 14.326 -2.148  21.397 1.00 12.46 ? 64  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 58  ? 13.888 -1.005  22.293 1.00 12.32 ? 64  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 58  ? 14.014 0.168   21.926 1.00 11.25 ? 64  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 58  ? 15.857 -2.296  21.346 1.00 12.84 ? 64  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 58  ? 16.426 -2.431  22.742 1.00 13.95 ? 64  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 58  ? 16.216 -3.580  23.489 1.00 15.01 ? 64  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 58  ? 17.186 -1.413  23.306 1.00 15.90 ? 64  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 58  ? 16.718 -3.704  24.787 1.00 17.03 ? 64  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 58  ? 17.679 -1.516  24.599 1.00 17.31 ? 64  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 58  ? 17.444 -2.663  25.338 1.00 19.08 ? 64  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 58  ? 17.957 -2.760  26.613 1.00 21.80 ? 64  TYR   A OH  1 
ATOM   457  N  N   . CYS   A 1 59  ? 13.337 -1.353  23.465 1.00 12.76 ? 65  CYS   A N   1 
ATOM   458  C  CA  . CYS   A 1 59  ? 12.881 -0.366  24.464 1.00 13.58 ? 65  CYS   A CA  1 
ATOM   459  C  C   . CYS   A 1 59  ? 13.827 -0.415  25.711 1.00 14.00 ? 65  CYS   A C   1 
ATOM   460  O  O   . CYS   A 1 59  ? 13.675 -1.309  26.565 1.00 14.23 ? 65  CYS   A O   1 
ATOM   461  C  CB  . CYS   A 1 59  ? 11.426 -0.651  24.846 1.00 15.58 ? 65  CYS   A CB  1 
ATOM   462  S  SG  . CYS   A 1 59  ? 10.792 0.374   26.205 1.00 18.04 ? 65  CYS   A SG  1 
ATOM   463  N  N   . SER   A 1 60  ? 14.798 0.539   25.830 1.00 13.92 ? 66  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 60  ? 15.729 0.480   26.979 1.00 14.82 ? 66  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 60  ? 15.053 0.624   28.344 1.00 15.18 ? 66  SER   A C   1 
ATOM   466  O  O   . SER   A 1 60  ? 15.505 -0.016  29.308 1.00 16.36 ? 66  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 60  ? 16.880 1.482   26.874 1.00 18.00 ? 66  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 60  ? 16.427 2.819   26.855 1.00 24.10 ? 66  SER   A OG  1 
ATOM   469  N  N   . SER   A 1 61  ? 13.981 1.451   28.433 1.00 15.22 ? 67  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 61  ? 13.247 1.657   29.699 1.00 15.81 ? 67  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 61  ? 12.561 0.380   30.234 1.00 16.97 ? 67  SER   A C   1 
ATOM   472  O  O   . SER   A 1 61  ? 12.052 0.394   31.372 1.00 18.36 ? 67  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 61  ? 12.236 2.797   29.597 1.00 15.87 ? 67  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 61  ? 11.163 2.469   28.719 1.00 16.47 ? 67  SER   A OG  1 
ATOM   475  N  N   . ARG   A 1 62  ? 12.569 -0.713  29.453 1.00 16.31 ? 68  ARG   A N   1 
ATOM   476  C  CA  . ARG   A 1 62  ? 12.036 -2.008  29.888 1.00 16.56 ? 68  ARG   A CA  1 
ATOM   477  C  C   . ARG   A 1 62  ? 13.050 -3.153  29.670 1.00 17.24 ? 68  ARG   A C   1 
ATOM   478  O  O   . ARG   A 1 62  ? 12.721 -4.297  29.982 1.00 17.52 ? 68  ARG   A O   1 
ATOM   479  C  CB  . ARG   A 1 62  ? 10.761 -2.342  29.115 1.00 18.12 ? 68  ARG   A CB  1 
ATOM   480  C  CG  . ARG   A 1 62  ? 9.605  -1.385  29.378 1.00 20.36 ? 68  ARG   A CG  1 
ATOM   481  C  CD  . ARG   A 1 62  ? 8.889  -1.751  30.665 1.00 21.81 ? 68  ARG   A CD  1 
ATOM   482  N  NE  . ARG   A 1 62  ? 7.723  -0.900  30.884 1.00 23.65 ? 68  ARG   A NE  1 
ATOM   483  C  CZ  . ARG   A 1 62  ? 7.746  0.261   31.529 1.00 25.41 ? 68  ARG   A CZ  1 
ATOM   484  N  NH1 . ARG   A 1 62  ? 8.889  0.730   32.033 1.00 23.59 ? 68  ARG   A NH1 1 
ATOM   485  N  NH2 . ARG   A 1 62  ? 6.629  0.970   31.670 1.00 24.32 ? 68  ARG   A NH2 1 
ATOM   486  N  N   . ARG   A 1 63  ? 14.250 -2.875  29.087 1.00 17.40 ? 69  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 63  ? 15.263 -3.881  28.702 1.00 18.99 ? 69  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 63  ? 14.574 -5.012  27.889 1.00 18.98 ? 69  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 63  ? 14.743 -6.201  28.175 1.00 19.60 ? 69  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 63  ? 16.014 -4.424  29.936 1.00 20.99 ? 69  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 63  ? 16.921 -3.369  30.610 1.00 25.78 ? 69  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 63  ? 17.695 -3.986  31.783 1.00 30.51 ? 69  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 63  ? 18.349 -3.006  32.667 1.00 35.42 ? 69  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 63  ? 18.245 -3.014  33.999 1.00 38.79 ? 69  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 63  ? 17.486 -3.921  34.609 1.00 38.64 ? 69  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 63  ? 18.852 -2.078  34.728 1.00 38.86 ? 69  ARG   A NH2 1 
ATOM   497  N  N   . LYS   A 1 64  ? 13.688 -4.608  26.966 1.00 17.60 ? 70  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 64  ? 12.905 -5.593  26.203 1.00 17.71 ? 70  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 64  ? 12.710 -5.174  24.756 1.00 16.42 ? 70  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 64  ? 12.733 -3.982  24.441 1.00 15.48 ? 70  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 64  ? 11.501 -5.750  26.827 1.00 20.28 ? 70  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 64  ? 11.405 -6.761  27.979 1.00 26.86 ? 70  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 64  ? 9.978  -6.823  28.477 1.00 32.61 ? 70  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 64  ? 9.727  -8.002  29.391 1.00 38.73 ? 70  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 64  ? 10.038 -7.692  30.817 1.00 43.03 ? 70  LYS   A NZ  1 
ATOM   506  N  N   . HIS   A 1 65  ? 12.503 -6.169  23.877 1.00 15.01 ? 71  HIS   A N   1 
ATOM   507  C  CA  . HIS   A 1 65  ? 12.172 -5.902  22.484 1.00 14.22 ? 71  HIS   A CA  1 
ATOM   508  C  C   . HIS   A 1 65  ? 10.670 -6.167  22.349 1.00 15.71 ? 71  HIS   A C   1 
ATOM   509  O  O   . HIS   A 1 65  ? 10.154 -7.156  22.897 1.00 17.54 ? 71  HIS   A O   1 
ATOM   510  C  CB  . HIS   A 1 65  ? 12.930 -6.845  21.544 1.00 15.28 ? 71  HIS   A CB  1 
ATOM   511  C  CG  . HIS   A 1 65  ? 14.417 -6.687  21.561 1.00 16.74 ? 71  HIS   A CG  1 
ATOM   512  N  ND1 . HIS   A 1 65  ? 15.070 -5.939  20.601 1.00 18.84 ? 71  HIS   A ND1 1 
ATOM   513  C  CD2 . HIS   A 1 65  ? 15.332 -7.190  22.414 1.00 16.93 ? 71  HIS   A CD2 1 
ATOM   514  C  CE1 . HIS   A 1 65  ? 16.360 -6.046  20.879 1.00 17.41 ? 71  HIS   A CE1 1 
ATOM   515  N  NE2 . HIS   A 1 65  ? 16.561 -6.742  21.985 1.00 18.78 ? 71  HIS   A NE2 1 
ATOM   516  N  N   . TYR   A 1 66  ? 9.965  -5.325  21.602 1.00 14.42 ? 72  TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 66  ? 8.524  -5.479  21.422 1.00 14.25 ? 72  TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 66  ? 8.163  -5.555  19.934 1.00 14.35 ? 72  TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 66  ? 8.607  -4.705  19.159 1.00 13.89 ? 72  TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 66  ? 7.785  -4.246  22.011 1.00 14.80 ? 72  TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 66  ? 7.830  -4.150  23.517 1.00 16.86 ? 72  TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 66  ? 7.045  -4.980  24.312 1.00 19.21 ? 72  TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 66  ? 8.609  -3.192  24.150 1.00 18.54 ? 72  TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 66  ? 7.094  -4.906  25.706 1.00 20.46 ? 72  TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 66  ? 8.646  -3.094  25.541 1.00 20.09 ? 72  TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 66  ? 7.879  -3.948  26.312 1.00 21.66 ? 72  TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 66  ? 7.916  -3.863  27.689 1.00 24.45 ? 72  TYR   A OH  1 
ATOM   528  N  N   . PRO   A 1 67  ? 7.294  -6.509  19.548 1.00 14.03 ? 73  PRO   A N   1 
ATOM   529  C  CA  . PRO   A 1 67  ? 6.799  -6.544  18.151 1.00 14.36 ? 73  PRO   A CA  1 
ATOM   530  C  C   . PRO   A 1 67  ? 5.661  -5.491  17.977 1.00 15.54 ? 73  PRO   A C   1 
ATOM   531  O  O   . PRO   A 1 67  ? 4.813  -5.350  18.873 1.00 17.21 ? 73  PRO   A O   1 
ATOM   532  C  CB  . PRO   A 1 67  ? 6.270  -7.978  18.013 1.00 14.71 ? 73  PRO   A CB  1 
ATOM   533  C  CG  . PRO   A 1 67  ? 5.765  -8.307  19.408 1.00 14.58 ? 73  PRO   A CG  1 
ATOM   534  C  CD  . PRO   A 1 67  ? 6.703  -7.581  20.382 1.00 13.46 ? 73  PRO   A CD  1 
ATOM   535  N  N   . VAL   A 1 68  ? 5.661  -4.731  16.884 1.00 14.72 ? 74  VAL   A N   1 
ATOM   536  C  CA  . VAL   A 1 68  ? 4.661  -3.684  16.643 1.00 15.11 ? 74  VAL   A CA  1 
ATOM   537  C  C   . VAL   A 1 68  ? 4.231  -3.613  15.191 1.00 13.91 ? 74  VAL   A C   1 
ATOM   538  O  O   . VAL   A 1 68  ? 5.001  -3.943  14.283 1.00 13.55 ? 74  VAL   A O   1 
ATOM   539  C  CB  . VAL   A 1 68  ? 5.234  -2.270  16.992 1.00 15.99 ? 74  VAL   A CB  1 
ATOM   540  C  CG1 . VAL   A 1 68  ? 5.218  -2.002  18.502 1.00 16.62 ? 74  VAL   A CG1 1 
ATOM   541  C  CG2 . VAL   A 1 68  ? 6.635  -2.053  16.393 1.00 16.26 ? 74  VAL   A CG2 1 
ATOM   542  N  N   . SER   A 1 69  ? 3.004  -3.092  14.967 1.00 14.04 ? 75  SER   A N   1 
ATOM   543  C  CA  . SER   A 1 69  ? 2.534  -2.683  13.630 1.00 14.19 ? 75  SER   A CA  1 
ATOM   544  C  C   . SER   A 1 69  ? 2.731  -1.161  13.633 1.00 12.66 ? 75  SER   A C   1 
ATOM   545  O  O   . SER   A 1 69  ? 2.482  -0.542  14.673 1.00 13.54 ? 75  SER   A O   1 
ATOM   546  C  CB  . SER   A 1 69  ? 1.043  -2.962  13.462 1.00 17.61 ? 75  SER   A CB  1 
ATOM   547  O  OG  . SER   A 1 69  ? 0.831  -4.358  13.489 1.00 24.48 ? 75  SER   A OG  1 
ATOM   548  N  N   . PHE   A 1 70  ? 3.263  -0.571  12.557 1.00 11.45 ? 76  PHE   A N   1 
ATOM   549  C  CA  . PHE   A 1 70  ? 3.526  0.862   12.518 1.00 12.49 ? 76  PHE   A CA  1 
ATOM   550  C  C   . PHE   A 1 70  ? 3.011  1.509   11.231 1.00 14.60 ? 76  PHE   A C   1 
ATOM   551  O  O   . PHE   A 1 70  ? 2.969  0.862   10.175 1.00 15.32 ? 76  PHE   A O   1 
ATOM   552  C  CB  . PHE   A 1 70  ? 5.046  1.160   12.734 1.00 12.10 ? 76  PHE   A CB  1 
ATOM   553  C  CG  . PHE   A 1 70  ? 6.026  0.435   11.816 1.00 12.18 ? 76  PHE   A CG  1 
ATOM   554  C  CD1 . PHE   A 1 70  ? 6.534  -0.818  12.156 1.00 12.60 ? 76  PHE   A CD1 1 
ATOM   555  C  CD2 . PHE   A 1 70  ? 6.443  1.013   10.622 1.00 13.17 ? 76  PHE   A CD2 1 
ATOM   556  C  CE1 . PHE   A 1 70  ? 7.474  -1.458  11.333 1.00 13.64 ? 76  PHE   A CE1 1 
ATOM   557  C  CE2 . PHE   A 1 70  ? 7.370  0.377   9.798  1.00 14.17 ? 76  PHE   A CE2 1 
ATOM   558  C  CZ  . PHE   A 1 70  ? 7.855  -0.879  10.138 1.00 13.83 ? 76  PHE   A CZ  1 
ATOM   559  N  N   . SER   A 1 71  ? 2.626  2.805   11.313 1.00 14.54 ? 77  SER   A N   1 
ATOM   560  C  CA  . SER   A 1 71  ? 2.122  3.492   10.138 1.00 14.75 ? 77  SER   A CA  1 
ATOM   561  C  C   . SER   A 1 71  ? 3.266  3.830   9.140  1.00 15.02 ? 77  SER   A C   1 
ATOM   562  O  O   . SER   A 1 71  ? 4.435  3.854   9.514  1.00 14.67 ? 77  SER   A O   1 
ATOM   563  C  CB  . SER   A 1 71  ? 1.386  4.754   10.568 1.00 16.92 ? 77  SER   A CB  1 
ATOM   564  O  OG  . SER   A 1 71  ? 2.267  5.630   11.248 1.00 19.57 ? 77  SER   A OG  1 
ATOM   565  N  N   . LYS   A 1 72  ? 2.922  4.093   7.861  1.00 15.08 ? 78  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 72  ? 3.931  4.479   6.853  1.00 15.81 ? 78  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 72  ? 4.500  5.878   7.210  1.00 17.20 ? 78  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 72  ? 3.805  6.650   7.861  1.00 18.27 ? 78  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 72  ? 3.292  4.503   5.442  1.00 17.60 ? 78  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 72  ? 2.941  3.085   4.940  1.00 20.72 ? 78  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 72  ? 2.331  3.072   3.552  1.00 26.58 ? 78  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 72  ? 2.360  1.656   3.018  1.00 32.29 ? 78  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 72  ? 1.920  1.579   1.604  1.00 35.42 ? 78  LYS   A NZ  1 
ATOM   574  N  N   . PRO   A 1 73  ? 5.748  6.200   6.813  1.00 17.10 ? 79  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 73  ? 6.334  7.506   7.188  1.00 17.92 ? 79  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 73  ? 5.484  8.687   6.720  1.00 18.68 ? 79  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 73  ? 5.008  8.719   5.571  1.00 18.32 ? 79  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 73  ? 7.698  7.530   6.480  1.00 19.10 ? 79  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 73  ? 7.944  6.165   5.987  1.00 19.63 ? 79  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 73  ? 6.699  5.351   6.071  1.00 17.54 ? 79  PRO   A CD  1 
ATOM   581  N  N   . SER   A 1 74  ? 5.263  9.644   7.628  1.00 18.68 ? 80  SER   A N   1 
ATOM   582  C  CA  . SER   A 1 74  ? 4.396  10.771  7.312  1.00 20.10 ? 80  SER   A CA  1 
ATOM   583  C  C   . SER   A 1 74  ? 4.700  11.980  8.213  1.00 20.13 ? 80  SER   A C   1 
ATOM   584  O  O   . SER   A 1 74  ? 5.591  11.916  9.058  1.00 19.81 ? 80  SER   A O   1 
ATOM   585  C  CB  . SER   A 1 74  ? 2.921  10.351  7.400  1.00 23.07 ? 80  SER   A CB  1 
ATOM   586  O  OG  . SER   A 1 74  ? 2.522  10.144  8.742  1.00 27.09 ? 80  SER   A OG  1 
ATOM   587  N  N   . LEU   A 1 75  ? 4.022  13.101  7.954  1.00 19.55 ? 81  LEU   A N   1 
ATOM   588  C  CA  . LEU   A 1 75  ? 4.194  14.346  8.700  1.00 20.58 ? 81  LEU   A CA  1 
ATOM   589  C  C   . LEU   A 1 75  ? 3.253  14.284  9.888  1.00 21.03 ? 81  LEU   A C   1 
ATOM   590  O  O   . LEU   A 1 75  ? 2.033  14.267  9.693  1.00 21.04 ? 81  LEU   A O   1 
ATOM   591  C  CB  . LEU   A 1 75  ? 3.696  15.504  7.825  1.00 21.64 ? 81  LEU   A CB  1 
ATOM   592  C  CG  . LEU   A 1 75  ? 4.678  16.316  7.068  1.00 25.64 ? 81  LEU   A CG  1 
ATOM   593  C  CD1 . LEU   A 1 75  ? 3.934  17.398  6.278  1.00 26.69 ? 81  LEU   A CD1 1 
ATOM   594  C  CD2 . LEU   A 1 75  ? 5.703  16.940  7.995  1.00 27.03 ? 81  LEU   A CD2 1 
ATOM   595  N  N   . ILE   A 1 76  ? 3.800  14.306  11.104 1.00 20.39 ? 82  ILE   A N   1 
ATOM   596  C  CA  . ILE   A 1 76  ? 3.033  14.206  12.329 1.00 21.59 ? 82  ILE   A CA  1 
ATOM   597  C  C   . ILE   A 1 76  ? 3.354  15.359  13.276 1.00 22.63 ? 82  ILE   A C   1 
ATOM   598  O  O   . ILE   A 1 76  ? 4.528  15.689  13.471 1.00 21.91 ? 82  ILE   A O   1 
ATOM   599  C  CB  . ILE   A 1 76  ? 3.389  12.839  12.971 1.00 23.10 ? 82  ILE   A CB  1 
ATOM   600  C  CG1 . ILE   A 1 76  ? 2.880  11.689  12.083 1.00 24.43 ? 82  ILE   A CG1 1 
ATOM   601  C  CG2 . ILE   A 1 76  ? 2.921  12.726  14.434 1.00 23.41 ? 82  ILE   A CG2 1 
ATOM   602  C  CD1 . ILE   A 1 76  ? 3.352  10.408  12.451 1.00 27.61 ? 82  ILE   A CD1 1 
ATOM   603  N  N   . PHE   A 1 77  ? 2.316  15.974  13.866 1.00 23.47 ? 83  PHE   A N   1 
ATOM   604  C  CA  . PHE   A 1 77  ? 2.518  17.051  14.830 1.00 25.62 ? 83  PHE   A CA  1 
ATOM   605  C  C   . PHE   A 1 77  ? 3.183  16.516  16.122 1.00 25.06 ? 83  PHE   A C   1 
ATOM   606  O  O   . PHE   A 1 77  ? 2.770  15.502  16.686 1.00 24.98 ? 83  PHE   A O   1 
ATOM   607  C  CB  . PHE   A 1 77  ? 1.189  17.770  15.153 1.00 27.72 ? 83  PHE   A CB  1 
ATOM   608  C  CG  . PHE   A 1 77  ? 1.351  19.011  16.005 1.00 30.62 ? 83  PHE   A CG  1 
ATOM   609  C  CD1 . PHE   A 1 77  ? 1.791  20.194  15.453 1.00 32.77 ? 83  PHE   A CD1 1 
ATOM   610  C  CD2 . PHE   A 1 77  ? 1.043  18.990  17.354 1.00 32.51 ? 83  PHE   A CD2 1 
ATOM   611  C  CE1 . PHE   A 1 77  ? 1.907  21.346  16.231 1.00 33.84 ? 83  PHE   A CE1 1 
ATOM   612  C  CE2 . PHE   A 1 77  ? 1.176  20.136  18.131 1.00 33.56 ? 83  PHE   A CE2 1 
ATOM   613  C  CZ  . PHE   A 1 77  ? 1.617  21.300  17.568 1.00 33.54 ? 83  PHE   A CZ  1 
ATOM   614  N  N   . VAL   A 1 78  ? 4.222  17.207  16.571 1.00 24.03 ? 84  VAL   A N   1 
ATOM   615  C  CA  . VAL   A 1 78  ? 4.961  16.837  17.760 1.00 23.59 ? 84  VAL   A CA  1 
ATOM   616  C  C   . VAL   A 1 78  ? 5.031  18.036  18.682 1.00 25.46 ? 84  VAL   A C   1 
ATOM   617  O  O   . VAL   A 1 78  ? 5.481  19.113  18.260 1.00 26.25 ? 84  VAL   A O   1 
ATOM   618  C  CB  . VAL   A 1 78  ? 6.391  16.339  17.381 1.00 22.36 ? 84  VAL   A CB  1 
ATOM   619  C  CG1 . VAL   A 1 78  ? 7.262  16.149  18.625 1.00 22.36 ? 84  VAL   A CG1 1 
ATOM   620  C  CG2 . VAL   A 1 78  ? 6.325  15.060  16.558 1.00 21.54 ? 84  VAL   A CG2 1 
ATOM   621  N  N   . GLU   A 1 79  ? 4.588  17.857  19.942 1.00 26.20 ? 85  GLU   A N   1 
ATOM   622  C  CA  . GLU   A 1 79  ? 4.603  18.917  20.968 1.00 26.98 ? 85  GLU   A CA  1 
ATOM   623  C  C   . GLU   A 1 79  ? 5.986  19.515  21.191 1.00 27.06 ? 85  GLU   A C   1 
ATOM   624  O  O   . GLU   A 1 79  ? 6.998  18.829  21.035 1.00 26.92 ? 85  GLU   A O   1 
ATOM   625  C  CB  . GLU   A 1 79  ? 4.131  18.353  22.319 1.00 29.82 ? 85  GLU   A CB  1 
ATOM   626  C  CG  . GLU   A 1 79  ? 2.676  17.953  22.362 1.00 36.40 ? 85  GLU   A CG  1 
ATOM   627  C  CD  . GLU   A 1 79  ? 1.716  19.064  22.000 1.00 46.98 ? 85  GLU   A CD  1 
ATOM   628  O  OE1 . GLU   A 1 79  ? 1.877  20.194  22.518 1.00 48.94 ? 85  GLU   A OE1 1 
ATOM   629  O  OE2 . GLU   A 1 79  ? 0.796  18.803  21.190 1.00 50.37 ? 85  GLU   A OE2 1 
ATOM   630  N  N   . ALA   A 1 80  ? 6.032  20.799  21.614 1.00 27.10 ? 86  ALA   A N   1 
ATOM   631  C  CA  . ALA   A 1 80  ? 7.301  21.456  21.933 1.00 27.38 ? 86  ALA   A CA  1 
ATOM   632  C  C   . ALA   A 1 80  ? 8.024  20.727  23.062 1.00 28.24 ? 86  ALA   A C   1 
ATOM   633  O  O   . ALA   A 1 80  ? 7.389  20.104  23.916 1.00 28.65 ? 86  ALA   A O   1 
ATOM   634  C  CB  . ALA   A 1 80  ? 7.059  22.908  22.354 1.00 27.29 ? 86  ALA   A CB  1 
ATOM   635  N  N   . SER   A 1 81  ? 9.352  20.776  23.026 1.00 28.41 ? 87  SER   A N   1 
ATOM   636  C  CA  . SER   A 1 81  ? 10.265 20.212  24.015 1.00 29.02 ? 87  SER   A CA  1 
ATOM   637  C  C   . SER   A 1 81  ? 11.425 21.213  24.180 1.00 30.66 ? 87  SER   A C   1 
ATOM   638  O  O   . SER   A 1 81  ? 11.420 22.272  23.537 1.00 31.29 ? 87  SER   A O   1 
ATOM   639  C  CB  . SER   A 1 81  ? 10.782 18.849  23.529 1.00 28.75 ? 87  SER   A CB  1 
ATOM   640  O  OG  . SER   A 1 81  ? 11.555 18.986  22.346 1.00 29.09 ? 87  SER   A OG  1 
ATOM   641  N  N   . GLU   A 1 82  ? 12.441 20.898  25.010 1.00 31.27 ? 88  GLU   A N   1 
ATOM   642  C  CA  . GLU   A 1 82  ? 13.615 21.772  25.131 1.00 31.86 ? 88  GLU   A CA  1 
ATOM   643  C  C   . GLU   A 1 82  ? 14.494 21.777  23.870 1.00 30.42 ? 88  GLU   A C   1 
ATOM   644  O  O   . GLU   A 1 82  ? 15.377 22.621  23.740 1.00 30.87 ? 88  GLU   A O   1 
ATOM   645  C  CB  . GLU   A 1 82  ? 14.480 21.405  26.351 1.00 37.79 ? 88  GLU   A CB  1 
ATOM   646  C  CG  . GLU   A 1 82  ? 13.691 21.078  27.608 1.00 46.78 ? 88  GLU   A CG  1 
ATOM   647  C  CD  . GLU   A 1 82  ? 13.537 19.589  27.854 1.00 58.14 ? 88  GLU   A CD  1 
ATOM   648  O  OE1 . GLU   A 1 82  ? 13.660 18.805  26.882 1.00 59.49 ? 88  GLU   A OE1 1 
ATOM   649  O  OE2 . GLU   A 1 82  ? 13.286 19.206  29.022 1.00 62.06 ? 88  GLU   A OE2 1 
ATOM   650  N  N   . TYR   A 1 83  ? 14.282 20.825  22.951 1.00 28.69 ? 89  TYR   A N   1 
ATOM   651  C  CA  . TYR   A 1 83  ? 15.088 20.726  21.741 1.00 26.92 ? 89  TYR   A CA  1 
ATOM   652  C  C   . TYR   A 1 83  ? 14.414 21.391  20.533 1.00 25.49 ? 89  TYR   A C   1 
ATOM   653  O  O   . TYR   A 1 83  ? 15.106 21.846  19.620 1.00 26.06 ? 89  TYR   A O   1 
ATOM   654  C  CB  . TYR   A 1 83  ? 15.404 19.245  21.442 1.00 26.16 ? 89  TYR   A CB  1 
ATOM   655  C  CG  . TYR   A 1 83  ? 15.866 18.439  22.649 1.00 26.57 ? 89  TYR   A CG  1 
ATOM   656  C  CD1 . TYR   A 1 83  ? 17.196 18.453  23.059 1.00 27.91 ? 89  TYR   A CD1 1 
ATOM   657  C  CD2 . TYR   A 1 83  ? 14.977 17.654  23.363 1.00 27.23 ? 89  TYR   A CD2 1 
ATOM   658  C  CE1 . TYR   A 1 83  ? 17.624 17.690  24.150 1.00 29.07 ? 89  TYR   A CE1 1 
ATOM   659  C  CE2 . TYR   A 1 83  ? 15.390 16.888  24.446 1.00 28.74 ? 89  TYR   A CE2 1 
ATOM   660  C  CZ  . TYR   A 1 83  ? 16.713 16.909  24.841 1.00 30.72 ? 89  TYR   A CZ  1 
ATOM   661  O  OH  . TYR   A 1 83  ? 17.088 16.121  25.919 1.00 34.06 ? 89  TYR   A OH  1 
ATOM   662  N  N   . TYR   A 1 84  ? 13.072 21.419  20.505 1.00 23.89 ? 90  TYR   A N   1 
ATOM   663  C  CA  . TYR   A 1 84  ? 12.358 21.982  19.367 1.00 23.50 ? 90  TYR   A CA  1 
ATOM   664  C  C   . TYR   A 1 84  ? 11.073 22.664  19.814 1.00 25.05 ? 90  TYR   A C   1 
ATOM   665  O  O   . TYR   A 1 84  ? 10.392 22.175  20.717 1.00 25.00 ? 90  TYR   A O   1 
ATOM   666  C  CB  . TYR   A 1 84  ? 11.928 20.872  18.356 1.00 22.06 ? 90  TYR   A CB  1 
ATOM   667  C  CG  . TYR   A 1 84  ? 13.000 19.931  17.842 1.00 20.19 ? 90  TYR   A CG  1 
ATOM   668  C  CD1 . TYR   A 1 84  ? 13.039 18.603  18.249 1.00 20.05 ? 90  TYR   A CD1 1 
ATOM   669  C  CD2 . TYR   A 1 84  ? 13.899 20.334  16.866 1.00 19.21 ? 90  TYR   A CD2 1 
ATOM   670  C  CE1 . TYR   A 1 84  ? 14.003 17.723  17.769 1.00 19.01 ? 90  TYR   A CE1 1 
ATOM   671  C  CE2 . TYR   A 1 84  ? 14.852 19.456  16.355 1.00 19.06 ? 90  TYR   A CE2 1 
ATOM   672  C  CZ  . TYR   A 1 84  ? 14.882 18.137  16.789 1.00 18.96 ? 90  TYR   A CZ  1 
ATOM   673  O  OH  . TYR   A 1 84  ? 15.849 17.268  16.321 1.00 17.31 ? 90  TYR   A OH  1 
ATOM   674  N  N   . PRO   A 1 85  ? 10.647 23.717  19.095 1.00 26.17 ? 91  PRO   A N   1 
ATOM   675  C  CA  . PRO   A 1 85  ? 9.285  24.241  19.332 1.00 26.95 ? 91  PRO   A CA  1 
ATOM   676  C  C   . PRO   A 1 85  ? 8.254  23.253  18.727 1.00 27.87 ? 91  PRO   A C   1 
ATOM   677  O  O   . PRO   A 1 85  ? 8.629  22.272  18.058 1.00 28.33 ? 91  PRO   A O   1 
ATOM   678  C  CB  . PRO   A 1 85  ? 9.291  25.577  18.582 1.00 27.97 ? 91  PRO   A CB  1 
ATOM   679  C  CG  . PRO   A 1 85  ? 10.272 25.358  17.447 1.00 28.07 ? 91  PRO   A CG  1 
ATOM   680  C  CD  . PRO   A 1 85  ? 11.306 24.361  17.935 1.00 25.93 ? 91  PRO   A CD  1 
ATOM   681  N  N   . ALA   A 1 86  ? 6.951  23.491  18.944 1.00 27.50 ? 92  ALA   A N   1 
ATOM   682  C  CA  . ALA   A 1 86  ? 5.910  22.626  18.382 1.00 27.38 ? 92  ALA   A CA  1 
ATOM   683  C  C   . ALA   A 1 86  ? 5.989  22.674  16.831 1.00 26.33 ? 92  ALA   A C   1 
ATOM   684  O  O   . ALA   A 1 86  ? 6.098  23.763  16.265 1.00 25.55 ? 92  ALA   A O   1 
ATOM   685  C  CB  . ALA   A 1 86  ? 4.537  23.105  18.853 1.00 28.11 ? 92  ALA   A CB  1 
ATOM   686  N  N   . ARG   A 1 87  ? 6.101  21.511  16.173 1.00 25.07 ? 93  ARG   A N   1 
ATOM   687  C  CA  . ARG   A 1 87  ? 6.188  21.489  14.714 1.00 24.15 ? 93  ARG   A CA  1 
ATOM   688  C  C   . ARG   A 1 87  ? 5.719  20.149  14.141 1.00 22.97 ? 93  ARG   A C   1 
ATOM   689  O  O   . ARG   A 1 87  ? 5.328  19.256  14.892 1.00 22.85 ? 93  ARG   A O   1 
ATOM   690  C  CB  . ARG   A 1 87  ? 7.585  21.955  14.123 1.00 25.39 ? 93  ARG   A CB  1 
ATOM   691  C  CG  . ARG   A 1 87  ? 8.979  21.570  14.702 1.00 28.67 ? 93  ARG   A CG  1 
ATOM   692  C  CD  . ARG   A 1 87  ? 9.161  20.153  15.180 1.00 25.48 ? 93  ARG   A CD  1 
ATOM   693  N  NE  . ARG   A 1 87  ? 10.395 19.398  14.803 1.00 23.50 ? 93  ARG   A NE  1 
ATOM   694  C  CZ  . ARG   A 1 87  ? 10.725 18.237  15.388 1.00 21.73 ? 93  ARG   A CZ  1 
ATOM   695  N  NH1 . ARG   A 1 87  ? 11.762 17.521  14.944 1.00 17.84 ? 93  ARG   A NH1 1 
ATOM   696  N  NH2 . ARG   A 1 87  ? 10.031 17.790  16.427 1.00 21.47 ? 93  ARG   A NH2 1 
ATOM   697  N  N   . TYR   A 1 88  ? 5.709  20.028  12.811 1.00 22.28 ? 94  TYR   A N   1 
ATOM   698  C  CA  . TYR   A 1 88  ? 5.456  18.745  12.178 1.00 21.89 ? 94  TYR   A CA  1 
ATOM   699  C  C   . TYR   A 1 88  ? 6.793  18.085  11.937 1.00 19.43 ? 94  TYR   A C   1 
ATOM   700  O  O   . TYR   A 1 88  ? 7.689  18.703  11.367 1.00 19.23 ? 94  TYR   A O   1 
ATOM   701  C  CB  . TYR   A 1 88  ? 4.764  18.916  10.832 1.00 23.70 ? 94  TYR   A CB  1 
ATOM   702  C  CG  . TYR   A 1 88  ? 3.344  19.383  10.986 1.00 26.19 ? 94  TYR   A CG  1 
ATOM   703  C  CD1 . TYR   A 1 88  ? 2.316  18.478  11.204 1.00 28.17 ? 94  TYR   A CD1 1 
ATOM   704  C  CD2 . TYR   A 1 88  ? 3.041  20.735  11.042 1.00 28.08 ? 94  TYR   A CD2 1 
ATOM   705  C  CE1 . TYR   A 1 88  ? 1.004  18.904  11.369 1.00 30.35 ? 94  TYR   A CE1 1 
ATOM   706  C  CE2 . TYR   A 1 88  ? 1.732  21.176  11.197 1.00 29.94 ? 94  TYR   A CE2 1 
ATOM   707  C  CZ  . TYR   A 1 88  ? 0.716  20.257  11.378 1.00 32.05 ? 94  TYR   A CZ  1 
ATOM   708  O  OH  . TYR   A 1 88  ? -0.581 20.699  11.526 1.00 35.76 ? 94  TYR   A OH  1 
ATOM   709  N  N   . GLN   A 1 89  ? 6.955  16.845  12.404 1.00 17.46 ? 95  GLN   A N   1 
ATOM   710  C  CA  . GLN   A 1 89  ? 8.161  16.076  12.149 1.00 15.84 ? 95  GLN   A CA  1 
ATOM   711  C  C   . GLN   A 1 89  ? 7.839  15.177  10.945 1.00 15.64 ? 95  GLN   A C   1 
ATOM   712  O  O   . GLN   A 1 89  ? 6.801  14.501  10.936 1.00 15.63 ? 95  GLN   A O   1 
ATOM   713  C  CB  . GLN   A 1 89  ? 8.560  15.231  13.375 1.00 16.52 ? 95  GLN   A CB  1 
ATOM   714  C  CG  . GLN   A 1 89  ? 9.718  14.249  13.087 1.00 16.57 ? 95  GLN   A CG  1 
ATOM   715  C  CD  . GLN   A 1 89  ? 10.467 13.820  14.330 1.00 15.81 ? 95  GLN   A CD  1 
ATOM   716  O  OE1 . GLN   A 1 89  ? 10.644 14.579  15.287 1.00 15.63 ? 95  GLN   A OE1 1 
ATOM   717  N  NE2 . GLN   A 1 89  ? 10.934 12.579  14.337 1.00 13.53 ? 95  GLN   A NE2 1 
ATOM   718  N  N   . SER   A 1 90  ? 8.672  15.222  9.912  1.00 14.91 ? 96  SER   A N   1 
ATOM   719  C  CA  . SER   A 1 90  ? 8.444  14.431  8.715  1.00 15.12 ? 96  SER   A CA  1 
ATOM   720  C  C   . SER   A 1 90  ? 9.123  13.061  8.831  1.00 15.23 ? 96  SER   A C   1 
ATOM   721  O  O   . SER   A 1 90  ? 9.965  12.833  9.733  1.00 14.54 ? 96  SER   A O   1 
ATOM   722  C  CB  . SER   A 1 90  ? 8.957  15.181  7.491  1.00 17.01 ? 96  SER   A CB  1 
ATOM   723  O  OG  . SER   A 1 90  ? 10.339 15.465  7.644  1.00 19.19 ? 96  SER   A OG  1 
ATOM   724  N  N   . HIS   A 1 91  ? 8.670  12.127  7.962  1.00 15.34 ? 97  HIS   A N   1 
ATOM   725  C  CA  . HIS   A 1 91  ? 9.196  10.777  7.827  1.00 15.57 ? 97  HIS   A CA  1 
ATOM   726  C  C   . HIS   A 1 91  ? 9.076  9.988   9.136  1.00 15.25 ? 97  HIS   A C   1 
ATOM   727  O  O   . HIS   A 1 91  ? 9.945  9.172   9.450  1.00 15.38 ? 97  HIS   A O   1 
ATOM   728  C  CB  . HIS   A 1 91  ? 10.661 10.854  7.352  1.00 16.04 ? 97  HIS   A CB  1 
ATOM   729  C  CG  . HIS   A 1 91  ? 10.817 11.509  6.013  1.00 18.13 ? 97  HIS   A CG  1 
ATOM   730  N  ND1 . HIS   A 1 91  ? 10.809 10.767  4.850  1.00 19.72 ? 97  HIS   A ND1 1 
ATOM   731  C  CD2 . HIS   A 1 91  ? 10.912 12.818  5.690  1.00 18.32 ? 97  HIS   A CD2 1 
ATOM   732  C  CE1 . HIS   A 1 91  ? 10.896 11.639  3.858  1.00 19.81 ? 97  HIS   A CE1 1 
ATOM   733  N  NE2 . HIS   A 1 91  ? 10.958 12.884  4.310  1.00 18.69 ? 97  HIS   A NE2 1 
ATOM   734  N  N   . LEU   A 1 92  ? 8.013  10.245  9.905  1.00 14.50 ? 98  LEU   A N   1 
ATOM   735  C  CA  . LEU   A 1 92  ? 7.783  9.626   11.210 1.00 14.21 ? 98  LEU   A CA  1 
ATOM   736  C  C   . LEU   A 1 92  ? 6.726  8.511   11.114 1.00 13.60 ? 98  LEU   A C   1 
ATOM   737  O  O   . LEU   A 1 92  ? 5.692  8.677   10.429 1.00 13.70 ? 98  LEU   A O   1 
ATOM   738  C  CB  . LEU   A 1 92  ? 7.295  10.721  12.183 1.00 13.89 ? 98  LEU   A CB  1 
ATOM   739  C  CG  . LEU   A 1 92  ? 7.217  10.358  13.672 1.00 14.83 ? 98  LEU   A CG  1 
ATOM   740  C  CD1 . LEU   A 1 92  ? 8.550  9.974   14.201 1.00 15.06 ? 98  LEU   A CD1 1 
ATOM   741  C  CD2 . LEU   A 1 92  ? 6.606  11.533  14.507 1.00 16.34 ? 98  LEU   A CD2 1 
ATOM   742  N  N   . MET   A 1 93  ? 6.992  7.371   11.786 1.00 12.96 ? 99  MET   A N   1 
ATOM   743  C  CA  . MET   A 1 93  ? 6.075  6.222   11.780 1.00 13.37 ? 99  MET   A CA  1 
ATOM   744  C  C   . MET   A 1 93  ? 5.595  5.980   13.225 1.00 14.35 ? 99  MET   A C   1 
ATOM   745  O  O   . MET   A 1 93  ? 6.429  5.974   14.119 1.00 14.68 ? 99  MET   A O   1 
ATOM   746  C  CB  . MET   A 1 93  ? 6.833  4.981   11.270 1.00 12.98 ? 99  MET   A CB  1 
ATOM   747  C  CG  . MET   A 1 93  ? 7.428  5.200   9.842  1.00 13.44 ? 99  MET   A CG  1 
ATOM   748  S  SD  . MET   A 1 93  ? 8.553  3.868   9.403  1.00 17.77 ? 99  MET   A SD  1 
ATOM   749  C  CE  . MET   A 1 93  ? 9.948  4.220   10.459 1.00 17.59 ? 99  MET   A CE  1 
ATOM   750  N  N   . LEU   A 1 94  ? 4.298  5.773   13.457 1.00 13.96 ? 100 LEU   A N   1 
ATOM   751  C  CA  . LEU   A 1 94  ? 3.802  5.562   14.835 1.00 13.75 ? 100 LEU   A CA  1 
ATOM   752  C  C   . LEU   A 1 94  ? 3.348  4.144   15.058 1.00 13.69 ? 100 LEU   A C   1 
ATOM   753  O  O   . LEU   A 1 94  ? 2.758  3.543   14.153 1.00 13.56 ? 100 LEU   A O   1 
ATOM   754  C  CB  . LEU   A 1 94  ? 2.586  6.454   15.172 1.00 15.17 ? 100 LEU   A CB  1 
ATOM   755  C  CG  . LEU   A 1 94  ? 2.830  7.987   15.192 1.00 18.64 ? 100 LEU   A CG  1 
ATOM   756  C  CD1 . LEU   A 1 94  ? 1.592  8.704   15.695 1.00 21.05 ? 100 LEU   A CD1 1 
ATOM   757  C  CD2 . LEU   A 1 94  ? 3.941  8.341   16.146 1.00 19.39 ? 100 LEU   A CD2 1 
ATOM   758  N  N   . ALA   A 1 95  ? 3.495  3.679   16.298 1.00 12.73 ? 101 ALA   A N   1 
ATOM   759  C  CA  . ALA   A 1 95  ? 3.001  2.374   16.732 1.00 13.17 ? 101 ALA   A CA  1 
ATOM   760  C  C   . ALA   A 1 95  ? 2.432  2.508   18.151 1.00 13.54 ? 101 ALA   A C   1 
ATOM   761  O  O   . ALA   A 1 95  ? 2.847  3.382   18.913 1.00 14.18 ? 101 ALA   A O   1 
ATOM   762  C  CB  . ALA   A 1 95  ? 4.141  1.362   16.744 1.00 14.13 ? 101 ALA   A CB  1 
ATOM   763  N  N   . VAL   A 1 96  ? 1.511  1.622   18.511 1.00 13.53 ? 102 VAL   A N   1 
ATOM   764  C  CA  . VAL   A 1 96  ? 0.996  1.549   19.874 1.00 13.59 ? 102 VAL   A CA  1 
ATOM   765  C  C   . VAL   A 1 96  ? 2.042  0.793   20.704 1.00 14.03 ? 102 VAL   A C   1 
ATOM   766  O  O   . VAL   A 1 96  ? 2.374  -0.362  20.384 1.00 14.72 ? 102 VAL   A O   1 
ATOM   767  C  CB  . VAL   A 1 96  ? -0.376 0.825   19.911 1.00 14.12 ? 102 VAL   A CB  1 
ATOM   768  C  CG1 . VAL   A 1 96  ? -0.874 0.691   21.348 1.00 14.02 ? 102 VAL   A CG1 1 
ATOM   769  C  CG2 . VAL   A 1 96  ? -1.412 1.574   19.050 1.00 14.80 ? 102 VAL   A CG2 1 
ATOM   770  N  N   . GLY   A 1 97  ? 2.604  1.458   21.706 1.00 14.30 ? 103 GLY   A N   1 
ATOM   771  C  CA  . GLY   A 1 97  ? 3.609  0.818   22.544 1.00 15.37 ? 103 GLY   A CA  1 
ATOM   772  C  C   . GLY   A 1 97  ? 4.203  1.729   23.590 1.00 16.60 ? 103 GLY   A C   1 
ATOM   773  O  O   . GLY   A 1 97  ? 3.923  2.926   23.594 1.00 18.34 ? 103 GLY   A O   1 
ATOM   774  N  N   . HIS   A 1 98  ? 5.044  1.178   24.478 1.00 14.71 ? 104 HIS   A N   1 
ATOM   775  C  CA  . HIS   A 1 98  ? 5.675  1.967   25.517 1.00 14.77 ? 104 HIS   A CA  1 
ATOM   776  C  C   . HIS   A 1 98  ? 6.996  2.604   25.076 1.00 14.51 ? 104 HIS   A C   1 
ATOM   777  O  O   . HIS   A 1 98  ? 7.817  1.955   24.419 1.00 13.79 ? 104 HIS   A O   1 
ATOM   778  C  CB  . HIS   A 1 98  ? 5.943  1.084   26.756 1.00 15.08 ? 104 HIS   A CB  1 
ATOM   779  C  CG  . HIS   A 1 98  ? 6.615  1.850   27.853 1.00 18.06 ? 104 HIS   A CG  1 
ATOM   780  N  ND1 . HIS   A 1 98  ? 5.960  2.885   28.513 1.00 19.88 ? 104 HIS   A ND1 1 
ATOM   781  C  CD2 . HIS   A 1 98  ? 7.908  1.825   28.258 1.00 19.14 ? 104 HIS   A CD2 1 
ATOM   782  C  CE1 . HIS   A 1 98  ? 6.846  3.393   29.352 1.00 20.61 ? 104 HIS   A CE1 1 
ATOM   783  N  NE2 . HIS   A 1 98  ? 8.033  2.790   29.233 1.00 20.96 ? 104 HIS   A NE2 1 
ATOM   784  N  N   . SER   A 1 99  ? 7.232  3.821   25.558 1.00 15.16 ? 105 SER   A N   1 
ATOM   785  C  CA  . SER   A 1 99  ? 8.471  4.533   25.384 1.00 15.27 ? 105 SER   A CA  1 
ATOM   786  C  C   . SER   A 1 99  ? 8.565  5.692   26.374 1.00 16.39 ? 105 SER   A C   1 
ATOM   787  O  O   . SER   A 1 99  ? 7.552  6.246   26.814 1.00 16.45 ? 105 SER   A O   1 
ATOM   788  C  CB  . SER   A 1 99  ? 8.647  5.005   23.940 1.00 16.36 ? 105 SER   A CB  1 
ATOM   789  O  OG  . SER   A 1 99  ? 7.876  6.158   23.648 1.00 17.45 ? 105 SER   A OG  1 
ATOM   790  N  N   . GLU   A 1 100 ? 9.805  6.037   26.720 1.00 16.42 ? 106 GLU   A N   1 
ATOM   791  C  CA  . GLU   A 1 100 ? 10.199 7.143   27.582 1.00 17.00 ? 106 GLU   A CA  1 
ATOM   792  C  C   . GLU   A 1 100 ? 11.296 7.941   26.866 1.00 17.16 ? 106 GLU   A C   1 
ATOM   793  O  O   . GLU   A 1 100 ? 11.907 7.410   25.941 1.00 17.65 ? 106 GLU   A O   1 
ATOM   794  C  CB  . GLU   A 1 100 ? 10.678 6.581   28.922 1.00 19.63 ? 106 GLU   A CB  1 
ATOM   795  C  CG  . GLU   A 1 100 ? 9.503  6.042   29.718 1.00 25.45 ? 106 GLU   A CG  1 
ATOM   796  C  CD  . GLU   A 1 100 ? 9.846  5.381   31.035 1.00 27.97 ? 106 GLU   A CD  1 
ATOM   797  O  OE1 . GLU   A 1 100 ? 10.586 5.993   31.833 1.00 28.68 ? 106 GLU   A OE1 1 
ATOM   798  O  OE2 . GLU   A 1 100 ? 9.383  4.245   31.268 1.00 29.07 ? 106 GLU   A OE2 1 
ATOM   799  N  N   . PRO   A 1 101 ? 11.547 9.222   27.210 1.00 17.49 ? 107 PRO   A N   1 
ATOM   800  C  CA  . PRO   A 1 101 ? 12.504 10.026  26.398 1.00 17.13 ? 107 PRO   A CA  1 
ATOM   801  C  C   . PRO   A 1 101 ? 13.873 9.388   26.159 1.00 16.67 ? 107 PRO   A C   1 
ATOM   802  O  O   . PRO   A 1 101 ? 14.432 9.473   25.044 1.00 17.14 ? 107 PRO   A O   1 
ATOM   803  C  CB  . PRO   A 1 101 ? 12.606 11.344  27.176 1.00 18.16 ? 107 PRO   A CB  1 
ATOM   804  C  CG  . PRO   A 1 101 ? 11.274 11.468  27.839 1.00 18.99 ? 107 PRO   A CG  1 
ATOM   805  C  CD  . PRO   A 1 101 ? 10.867 10.051  28.228 1.00 17.25 ? 107 PRO   A CD  1 
ATOM   806  N  N   . GLY   A 1 102 ? 14.370 8.683   27.172 1.00 15.45 ? 108 GLY   A N   1 
ATOM   807  C  CA  . GLY   A 1 102 ? 15.655 7.982   27.113 1.00 15.68 ? 108 GLY   A CA  1 
ATOM   808  C  C   . GLY   A 1 102 ? 15.686 6.796   26.166 1.00 15.84 ? 108 GLY   A C   1 
ATOM   809  O  O   . GLY   A 1 102 ? 16.755 6.258   25.874 1.00 16.43 ? 108 GLY   A O   1 
ATOM   810  N  N   . ASP   A 1 103 ? 14.517 6.367   25.677 1.00 14.71 ? 109 ASP   A N   1 
ATOM   811  C  CA  . ASP   A 1 103 ? 14.441 5.291   24.690 1.00 13.79 ? 109 ASP   A CA  1 
ATOM   812  C  C   . ASP   A 1 103 ? 14.835 5.725   23.304 1.00 12.55 ? 109 ASP   A C   1 
ATOM   813  O  O   . ASP   A 1 103 ? 15.041 4.859   22.438 1.00 12.18 ? 109 ASP   A O   1 
ATOM   814  C  CB  . ASP   A 1 103 ? 13.052 4.640   24.638 1.00 15.20 ? 109 ASP   A CB  1 
ATOM   815  C  CG  . ASP   A 1 103 ? 12.785 3.862   25.908 1.00 15.56 ? 109 ASP   A CG  1 
ATOM   816  O  OD1 . ASP   A 1 103 ? 13.726 3.245   26.423 1.00 15.15 ? 109 ASP   A OD1 1 
ATOM   817  O  OD2 . ASP   A 1 103 ? 11.653 3.937   26.420 1.00 15.64 ? 109 ASP   A OD2 1 
ATOM   818  N  N   . CYS   A 1 104 ? 14.947 7.048   23.044 1.00 12.68 ? 110 CYS   A N   1 
ATOM   819  C  CA  . CYS   A 1 104 ? 15.358 7.552   21.710 1.00 12.63 ? 110 CYS   A CA  1 
ATOM   820  C  C   . CYS   A 1 104 ? 16.663 6.900   21.285 1.00 13.48 ? 110 CYS   A C   1 
ATOM   821  O  O   . CYS   A 1 104 ? 17.541 6.727   22.135 1.00 14.59 ? 110 CYS   A O   1 
ATOM   822  C  CB  . CYS   A 1 104 ? 15.484 9.073   21.690 1.00 13.12 ? 110 CYS   A CB  1 
ATOM   823  S  SG  . CYS   A 1 104 ? 13.901 9.957   21.725 1.00 16.99 ? 110 CYS   A SG  1 
ATOM   824  N  N   . GLY   A 1 105 ? 16.779 6.509   20.024 1.00 12.71 ? 111 GLY   A N   1 
ATOM   825  C  CA  . GLY   A 1 105 ? 17.978 5.836   19.534 1.00 13.84 ? 111 GLY   A CA  1 
ATOM   826  C  C   . GLY   A 1 105 ? 17.815 4.323   19.446 1.00 15.25 ? 111 GLY   A C   1 
ATOM   827  O  O   . GLY   A 1 105 ? 18.604 3.636   18.782 1.00 15.39 ? 111 GLY   A O   1 
ATOM   828  N  N   . GLY   A 1 106 ? 16.784 3.783   20.100 1.00 14.47 ? 112 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 106 ? 16.491 2.351   20.014 1.00 14.03 ? 112 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 106 ? 16.122 1.976   18.589 1.00 14.06 ? 112 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 106 ? 15.401 2.712   17.930 1.00 13.34 ? 112 GLY   A O   1 
ATOM   832  N  N   . ILE   A 1 107 ? 16.637 0.850   18.101 1.00 13.58 ? 113 ILE   A N   1 
ATOM   833  C  CA  . ILE   A 1 107 ? 16.412 0.460   16.716 1.00 13.98 ? 113 ILE   A CA  1 
ATOM   834  C  C   . ILE   A 1 107 ? 15.071 -0.247  16.499 1.00 12.70 ? 113 ILE   A C   1 
ATOM   835  O  O   . ILE   A 1 107 ? 14.689 -1.114  17.284 1.00 12.77 ? 113 ILE   A O   1 
ATOM   836  C  CB  . ILE   A 1 107 ? 17.645 -0.387  16.253 1.00 16.51 ? 113 ILE   A CB  1 
ATOM   837  C  CG1 . ILE   A 1 107 ? 18.836 0.537   15.869 1.00 17.92 ? 113 ILE   A CG1 1 
ATOM   838  C  CG2 . ILE   A 1 107 ? 17.329 -1.353  15.133 1.00 18.15 ? 113 ILE   A CG2 1 
ATOM   839  C  CD1 . ILE   A 1 107 ? 20.145 -0.216  15.503 1.00 18.89 ? 113 ILE   A CD1 1 
ATOM   840  N  N   . LEU   A 1 108 ? 14.404 0.076   15.375 1.00 12.45 ? 114 LEU   A N   1 
ATOM   841  C  CA  . LEU   A 1 108 ? 13.241 -0.652  14.899 1.00 13.11 ? 114 LEU   A CA  1 
ATOM   842  C  C   . LEU   A 1 108 ? 13.752 -1.488  13.709 1.00 13.68 ? 114 LEU   A C   1 
ATOM   843  O  O   . LEU   A 1 108 ? 14.391 -0.937  12.801 1.00 12.90 ? 114 LEU   A O   1 
ATOM   844  C  CB  . LEU   A 1 108 ? 12.136 0.321   14.449 1.00 13.41 ? 114 LEU   A CB  1 
ATOM   845  C  CG  . LEU   A 1 108 ? 10.967 -0.285  13.659 1.00 13.85 ? 114 LEU   A CG  1 
ATOM   846  C  CD1 . LEU   A 1 108 ? 10.108 -1.235  14.558 1.00 14.04 ? 114 LEU   A CD1 1 
ATOM   847  C  CD2 . LEU   A 1 108 ? 10.080 0.821   13.103 1.00 13.84 ? 114 LEU   A CD2 1 
ATOM   848  N  N   . ARG   A 1 109 ? 13.470 -2.804  13.703 1.00 14.01 ? 115 ARG   A N   1 
ATOM   849  C  CA  . ARG   A 1 109 ? 13.948 -3.687  12.633 1.00 15.66 ? 115 ARG   A CA  1 
ATOM   850  C  C   . ARG   A 1 109 ? 12.824 -4.546  12.070 1.00 16.47 ? 115 ARG   A C   1 
ATOM   851  O  O   . ARG   A 1 109 ? 11.957 -4.984  12.819 1.00 15.79 ? 115 ARG   A O   1 
ATOM   852  C  CB  . ARG   A 1 109 ? 14.937 -4.718  13.204 1.00 18.47 ? 115 ARG   A CB  1 
ATOM   853  C  CG  . ARG   A 1 109 ? 16.221 -4.194  13.759 1.00 25.39 ? 115 ARG   A CG  1 
ATOM   854  C  CD  . ARG   A 1 109 ? 17.076 -5.384  14.204 1.00 29.24 ? 115 ARG   A CD  1 
ATOM   855  N  NE  . ARG   A 1 109 ? 17.613 -6.033  13.016 1.00 32.75 ? 115 ARG   A NE  1 
ATOM   856  C  CZ  . ARG   A 1 109 ? 18.786 -5.738  12.466 1.00 33.97 ? 115 ARG   A CZ  1 
ATOM   857  N  NH1 . ARG   A 1 109 ? 19.619 -4.897  13.070 1.00 33.12 ? 115 ARG   A NH1 1 
ATOM   858  N  NH2 . ARG   A 1 109 ? 19.160 -6.325  11.340 1.00 34.60 ? 115 ARG   A NH2 1 
ATOM   859  N  N   . CYS   A 1 110 ? 12.896 -4.852  10.778 1.00 16.06 ? 116 CYS   A N   1 
ATOM   860  C  CA  . CYS   A 1 110 ? 11.992 -5.831  10.143 1.00 17.87 ? 116 CYS   A CA  1 
ATOM   861  C  C   . CYS   A 1 110 ? 12.881 -6.983  9.630  1.00 19.57 ? 116 CYS   A C   1 
ATOM   862  O  O   . CYS   A 1 110 ? 14.098 -6.981  9.851  1.00 19.39 ? 116 CYS   A O   1 
ATOM   863  C  CB  . CYS   A 1 110 ? 11.235 -5.174  8.992  1.00 18.31 ? 116 CYS   A CB  1 
ATOM   864  S  SG  . CYS   A 1 110 ? 12.326 -4.588  7.673  1.00 17.48 ? 116 CYS   A SG  1 
ATOM   865  N  N   . GLN   A 1 111 ? 12.296 -7.948  8.910  1.00 21.94 ? 117 GLN   A N   1 
ATOM   866  C  CA  . GLN   A 1 111 ? 13.050 -9.061  8.338  1.00 24.56 ? 117 GLN   A CA  1 
ATOM   867  C  C   . GLN   A 1 111 ? 14.171 -8.612  7.368  1.00 24.64 ? 117 GLN   A C   1 
ATOM   868  O  O   . GLN   A 1 111 ? 15.162 -9.337  7.193  1.00 26.25 ? 117 GLN   A O   1 
ATOM   869  C  CB  . GLN   A 1 111 ? 12.079 -10.008 7.608  1.00 28.83 ? 117 GLN   A CB  1 
ATOM   870  C  CG  . GLN   A 1 111 ? 11.247 -9.317  6.525  1.00 33.34 ? 117 GLN   A CG  1 
ATOM   871  C  CD  . GLN   A 1 111 ? 10.321 -10.265 5.794  1.00 39.60 ? 117 GLN   A CD  1 
ATOM   872  O  OE1 . GLN   A 1 111 ? 9.112  -10.004 5.653  1.00 40.84 ? 117 GLN   A OE1 1 
ATOM   873  N  NE2 . GLN   A 1 111 ? 10.870 -11.375 5.301  1.00 40.11 ? 117 GLN   A NE2 1 
ATOM   874  N  N   . HIS   A 1 112 ? 14.037 -7.418  6.765  1.00 22.74 ? 118 HIS   A N   1 
ATOM   875  C  CA  . HIS   A 1 112 ? 15.025 -6.920  5.791  1.00 22.41 ? 118 HIS   A CA  1 
ATOM   876  C  C   . HIS   A 1 112 ? 16.197 -6.106  6.397  1.00 21.72 ? 118 HIS   A C   1 
ATOM   877  O  O   . HIS   A 1 112 ? 17.160 -5.781  5.684  1.00 22.65 ? 118 HIS   A O   1 
ATOM   878  C  CB  . HIS   A 1 112 ? 14.335 -6.083  4.703  1.00 22.80 ? 118 HIS   A CB  1 
ATOM   879  C  CG  . HIS   A 1 112 ? 13.162 -6.756  4.048  1.00 26.93 ? 118 HIS   A CG  1 
ATOM   880  N  ND1 . HIS   A 1 112 ? 11.863 -6.489  4.449  1.00 28.90 ? 118 HIS   A ND1 1 
ATOM   881  C  CD2 . HIS   A 1 112 ? 13.126 -7.626  3.011  1.00 28.50 ? 118 HIS   A CD2 1 
ATOM   882  C  CE1 . HIS   A 1 112 ? 11.083 -7.206  3.661  1.00 29.68 ? 118 HIS   A CE1 1 
ATOM   883  N  NE2 . HIS   A 1 112 ? 11.797 -7.928  2.795  1.00 30.11 ? 118 HIS   A NE2 1 
ATOM   884  N  N   . GLY   A 1 113 ? 16.088 -5.743  7.667  1.00 19.42 ? 119 GLY   A N   1 
ATOM   885  C  CA  . GLY   A 1 113 ? 17.125 -4.957  8.325  1.00 17.71 ? 119 GLY   A CA  1 
ATOM   886  C  C   . GLY   A 1 113 ? 16.593 -3.784  9.131  1.00 14.90 ? 119 GLY   A C   1 
ATOM   887  O  O   . GLY   A 1 113 ? 15.461 -3.806  9.601  1.00 15.00 ? 119 GLY   A O   1 
ATOM   888  N  N   . VAL   A 1 114 ? 17.441 -2.770  9.347  1.00 14.19 ? 120 VAL   A N   1 
ATOM   889  C  CA  . VAL   A 1 114 ? 17.105 -1.594  10.133 1.00 14.22 ? 120 VAL   A CA  1 
ATOM   890  C  C   . VAL   A 1 114 ? 16.086 -0.717  9.428  1.00 13.71 ? 120 VAL   A C   1 
ATOM   891  O  O   . VAL   A 1 114 ? 16.311 -0.316  8.284  1.00 14.71 ? 120 VAL   A O   1 
ATOM   892  C  CB  . VAL   A 1 114 ? 18.381 -0.796  10.494 1.00 15.03 ? 120 VAL   A CB  1 
ATOM   893  C  CG1 . VAL   A 1 114 ? 18.020 0.510   11.210 1.00 15.38 ? 120 VAL   A CG1 1 
ATOM   894  C  CG2 . VAL   A 1 114 ? 19.323 -1.639  11.350 1.00 14.77 ? 120 VAL   A CG2 1 
ATOM   895  N  N   . VAL   A 1 115 ? 14.993 -0.368  10.114 1.00 13.19 ? 121 VAL   A N   1 
ATOM   896  C  CA  . VAL   A 1 115 ? 13.933 0.467   9.532  1.00 13.72 ? 121 VAL   A CA  1 
ATOM   897  C  C   . VAL   A 1 115 ? 14.096 1.933   9.965  1.00 14.46 ? 121 VAL   A C   1 
ATOM   898  O  O   . VAL   A 1 115 ? 13.909 2.868   9.166  1.00 14.18 ? 121 VAL   A O   1 
ATOM   899  C  CB  . VAL   A 1 115 ? 12.544 -0.108  9.966  1.00 13.44 ? 121 VAL   A CB  1 
ATOM   900  C  CG1 . VAL   A 1 115 ? 11.397 0.811   9.591  1.00 13.99 ? 121 VAL   A CG1 1 
ATOM   901  C  CG2 . VAL   A 1 115 ? 12.334 -1.490  9.380  1.00 13.84 ? 121 VAL   A CG2 1 
ATOM   902  N  N   . GLY   A 1 116 ? 14.375 2.122   11.251 1.00 14.20 ? 122 GLY   A N   1 
ATOM   903  C  CA  . GLY   A 1 116 ? 14.510 3.470   11.800 1.00 13.82 ? 122 GLY   A CA  1 
ATOM   904  C  C   . GLY   A 1 116 ? 14.905 3.474   13.268 1.00 12.65 ? 122 GLY   A C   1 
ATOM   905  O  O   . GLY   A 1 116 ? 15.268 2.433   13.803 1.00 12.19 ? 122 GLY   A O   1 
ATOM   906  N  N   . ILE   A 1 117 ? 14.821 4.621   13.927 1.00 12.10 ? 123 ILE   A N   1 
ATOM   907  C  CA  . ILE   A 1 117 ? 15.177 4.730   15.340 1.00 12.25 ? 123 ILE   A CA  1 
ATOM   908  C  C   . ILE   A 1 117 ? 14.087 5.441   16.115 1.00 12.09 ? 123 ILE   A C   1 
ATOM   909  O  O   . ILE   A 1 117 ? 13.423 6.326   15.583 1.00 12.43 ? 123 ILE   A O   1 
ATOM   910  C  CB  . ILE   A 1 117 ? 16.541 5.451   15.549 1.00 13.02 ? 123 ILE   A CB  1 
ATOM   911  C  CG1 . ILE   A 1 117 ? 16.578 6.792   14.813 1.00 14.48 ? 123 ILE   A CG1 1 
ATOM   912  C  CG2 . ILE   A 1 117 ? 17.735 4.562   15.161 1.00 14.05 ? 123 ILE   A CG2 1 
ATOM   913  C  CD1 . ILE   A 1 117 ? 17.847 7.666   15.229 1.00 16.57 ? 123 ILE   A CD1 1 
ATOM   914  N  N   . VAL   A 1 118 ? 13.896 5.074   17.384 1.00 10.82 ? 124 VAL   A N   1 
ATOM   915  C  CA  . VAL   A 1 118 ? 12.919 5.741   18.250 1.00 9.88  ? 124 VAL   A CA  1 
ATOM   916  C  C   . VAL   A 1 118 ? 13.227 7.255   18.314 1.00 10.36 ? 124 VAL   A C   1 
ATOM   917  O  O   . VAL   A 1 118 ? 14.392 7.647   18.513 1.00 10.53 ? 124 VAL   A O   1 
ATOM   918  C  CB  . VAL   A 1 118 ? 12.957 5.139   19.666 1.00 10.07 ? 124 VAL   A CB  1 
ATOM   919  C  CG1 . VAL   A 1 118 ? 12.065 5.932   20.597 1.00 9.42  ? 124 VAL   A CG1 1 
ATOM   920  C  CG2 . VAL   A 1 118 ? 12.537 3.659   19.650 1.00 11.36 ? 124 VAL   A CG2 1 
ATOM   921  N  N   . SER   A 1 119 ? 12.199 8.091   18.120 1.00 10.81 ? 125 SER   A N   1 
ATOM   922  C  CA  . SER   A 1 119 ? 12.422 9.537   18.120 1.00 11.40 ? 125 SER   A CA  1 
ATOM   923  C  C   . SER   A 1 119 ? 11.388 10.320  18.916 1.00 13.24 ? 125 SER   A C   1 
ATOM   924  O  O   . SER   A 1 119 ? 11.708 11.418  19.404 1.00 14.43 ? 125 SER   A O   1 
ATOM   925  C  CB  . SER   A 1 119 ? 12.483 10.040  16.677 1.00 12.50 ? 125 SER   A CB  1 
ATOM   926  O  OG  . SER   A 1 119 ? 12.445 11.456  16.571 1.00 14.37 ? 125 SER   A OG  1 
ATOM   927  N  N   . THR   A 1 120 ? 10.153 9.797   19.041 1.00 13.45 ? 126 THR   A N   1 
ATOM   928  C  CA  . THR   A 1 120 ? 9.094  10.533  19.784 1.00 14.00 ? 126 THR   A CA  1 
ATOM   929  C  C   . THR   A 1 120 ? 8.236  9.567   20.601 1.00 15.49 ? 126 THR   A C   1 
ATOM   930  O  O   . THR   A 1 120 ? 8.273  8.352   20.370 1.00 15.15 ? 126 THR   A O   1 
ATOM   931  C  CB  . THR   A 1 120 ? 8.158  11.318  18.818 1.00 15.30 ? 126 THR   A CB  1 
ATOM   932  O  OG1 . THR   A 1 120 ? 7.343  10.389  18.096 1.00 17.04 ? 126 THR   A OG1 1 
ATOM   933  C  CG2 . THR   A 1 120 ? 8.899  12.202  17.831 1.00 15.38 ? 126 THR   A CG2 1 
ATOM   934  N  N   . GLY   A 1 121 ? 7.449  10.101  21.524 1.00 16.85 ? 127 GLY   A N   1 
ATOM   935  C  CA  . GLY   A 1 121 ? 6.524  9.278   22.276 1.00 19.22 ? 127 GLY   A CA  1 
ATOM   936  C  C   . GLY   A 1 121 ? 5.557  10.052  23.127 1.00 22.47 ? 127 GLY   A C   1 
ATOM   937  O  O   . GLY   A 1 121 ? 5.626  11.283  23.225 1.00 22.88 ? 127 GLY   A O   1 
ATOM   938  N  N   . GLY   A 1 122 ? 4.687  9.306   23.769 1.00 24.81 ? 128 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 122 ? 3.682  9.866   24.667 1.00 27.59 ? 128 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 122 ? 2.298  9.329   24.372 1.00 29.05 ? 128 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 122 ? 2.015  8.929   23.238 1.00 29.44 ? 128 GLY   A O   1 
ATOM   942  N  N   . ASN   A 1 123 ? 1.430  9.308   25.381 1.00 29.38 ? 129 ASN   A N   1 
ATOM   943  C  CA  . ASN   A 1 123 ? 0.047  8.860   25.195 1.00 30.13 ? 129 ASN   A CA  1 
ATOM   944  C  C   . ASN   A 1 123 ? -0.048 7.412   24.673 1.00 28.54 ? 129 ASN   A C   1 
ATOM   945  O  O   . ASN   A 1 123 ? -0.989 7.085   23.961 1.00 29.29 ? 129 ASN   A O   1 
ATOM   946  C  CB  . ASN   A 1 123 ? -0.701 9.802   24.238 1.00 32.47 ? 129 ASN   A CB  1 
ATOM   947  C  CG  . ASN   A 1 123 ? -0.982 11.171  24.813 1.00 38.17 ? 129 ASN   A CG  1 
ATOM   948  O  OD1 . ASN   A 1 123 ? -0.947 11.380  26.042 1.00 40.12 ? 129 ASN   A OD1 1 
ATOM   949  N  ND2 . ASN   A 1 123 ? -1.295 12.122  23.930 1.00 37.99 ? 129 ASN   A ND2 1 
ATOM   950  N  N   . GLY   A 1 124 ? 0.943  6.591   24.986 1.00 26.34 ? 130 GLY   A N   1 
ATOM   951  C  CA  . GLY   A 1 124 ? 0.949  5.205   24.553 1.00 24.33 ? 130 GLY   A CA  1 
ATOM   952  C  C   . GLY   A 1 124 ? 1.265  4.985   23.092 1.00 21.50 ? 130 GLY   A C   1 
ATOM   953  O  O   . GLY   A 1 124 ? 1.031  3.891   22.586 1.00 20.71 ? 130 GLY   A O   1 
ATOM   954  N  N   . LEU   A 1 125 ? 1.860  5.987   22.414 1.00 19.67 ? 131 LEU   A N   1 
ATOM   955  C  CA  . LEU   A 1 125 ? 2.286  5.837   21.032 1.00 18.82 ? 131 LEU   A CA  1 
ATOM   956  C  C   . LEU   A 1 125 ? 3.785  6.106   20.955 1.00 17.64 ? 131 LEU   A C   1 
ATOM   957  O  O   . LEU   A 1 125 ? 4.234  7.098   21.498 1.00 18.56 ? 131 LEU   A O   1 
ATOM   958  C  CB  . LEU   A 1 125 ? 1.562  6.852   20.141 1.00 20.27 ? 131 LEU   A CB  1 
ATOM   959  C  CG  . LEU   A 1 125 ? 0.047  6.650   20.083 1.00 23.43 ? 131 LEU   A CG  1 
ATOM   960  C  CD1 . LEU   A 1 125 ? -0.636 7.895   19.611 1.00 25.13 ? 131 LEU   A CD1 1 
ATOM   961  C  CD2 . LEU   A 1 125 ? -0.311 5.419   19.239 1.00 23.90 ? 131 LEU   A CD2 1 
ATOM   962  N  N   . VAL   A 1 126 ? 4.530  5.272   20.236 1.00 15.41 ? 132 VAL   A N   1 
ATOM   963  C  CA  . VAL   A 1 126 ? 5.954  5.449   20.023 1.00 14.75 ? 132 VAL   A CA  1 
ATOM   964  C  C   . VAL   A 1 126 ? 6.161  5.823   18.542 1.00 13.96 ? 132 VAL   A C   1 
ATOM   965  O  O   . VAL   A 1 126 ? 5.547  5.222   17.659 1.00 13.78 ? 132 VAL   A O   1 
ATOM   966  C  CB  . VAL   A 1 126 ? 6.755  4.184   20.457 1.00 15.12 ? 132 VAL   A CB  1 
ATOM   967  C  CG1 . VAL   A 1 126 ? 6.226  2.912   19.823 1.00 16.73 ? 132 VAL   A CG1 1 
ATOM   968  C  CG2 . VAL   A 1 126 ? 8.273  4.344   20.218 1.00 14.75 ? 132 VAL   A CG2 1 
ATOM   969  N  N   . GLY   A 1 127 ? 6.947  6.869   18.295 1.00 12.79 ? 133 GLY   A N   1 
ATOM   970  C  CA  . GLY   A 1 127 ? 7.255  7.303   16.944 1.00 12.05 ? 133 GLY   A CA  1 
ATOM   971  C  C   . GLY   A 1 127 ? 8.683  6.983   16.562 1.00 12.82 ? 133 GLY   A C   1 
ATOM   972  O  O   . GLY   A 1 127 ? 9.599  7.191   17.366 1.00 12.79 ? 133 GLY   A O   1 
ATOM   973  N  N   . PHE   A 1 128 ? 8.892  6.511   15.321 1.00 12.42 ? 134 PHE   A N   1 
ATOM   974  C  CA  . PHE   A 1 128 ? 10.229 6.135   14.827 1.00 12.67 ? 134 PHE   A CA  1 
ATOM   975  C  C   . PHE   A 1 128 ? 10.587 6.978   13.603 1.00 12.66 ? 134 PHE   A C   1 
ATOM   976  O  O   . PHE   A 1 128 ? 9.765  7.141   12.697 1.00 12.06 ? 134 PHE   A O   1 
ATOM   977  C  CB  . PHE   A 1 128 ? 10.267 4.647   14.403 1.00 12.46 ? 134 PHE   A CB  1 
ATOM   978  C  CG  . PHE   A 1 128 ? 9.699  3.699   15.443 1.00 12.99 ? 134 PHE   A CG  1 
ATOM   979  C  CD1 . PHE   A 1 128 ? 10.518 3.129   16.408 1.00 13.45 ? 134 PHE   A CD1 1 
ATOM   980  C  CD2 . PHE   A 1 128 ? 8.363  3.338   15.418 1.00 12.92 ? 134 PHE   A CD2 1 
ATOM   981  C  CE1 . PHE   A 1 128 ? 10.009 2.230   17.333 1.00 13.25 ? 134 PHE   A CE1 1 
ATOM   982  C  CE2 . PHE   A 1 128 ? 7.851  2.425   16.345 1.00 12.99 ? 134 PHE   A CE2 1 
ATOM   983  C  CZ  . PHE   A 1 128 ? 8.677  1.899   17.316 1.00 12.62 ? 134 PHE   A CZ  1 
ATOM   984  N  N   . ALA   A 1 129 ? 11.814 7.500   13.572 1.00 12.72 ? 135 ALA   A N   1 
ATOM   985  C  CA  . ALA   A 1 129 ? 12.297 8.239   12.417 1.00 12.02 ? 135 ALA   A CA  1 
ATOM   986  C  C   . ALA   A 1 129 ? 12.758 7.221   11.363 1.00 12.44 ? 135 ALA   A C   1 
ATOM   987  O  O   . ALA   A 1 129 ? 13.704 6.466   11.598 1.00 11.83 ? 135 ALA   A O   1 
ATOM   988  C  CB  . ALA   A 1 129 ? 13.462 9.151   12.818 1.00 11.71 ? 135 ALA   A CB  1 
ATOM   989  N  N   . ASP   A 1 130 ? 12.110 7.212   10.187 1.00 11.97 ? 136 ASP   A N   1 
ATOM   990  C  CA  . ASP   A 1 130 ? 12.477 6.294   9.119  1.00 12.63 ? 136 ASP   A CA  1 
ATOM   991  C  C   . ASP   A 1 130 ? 13.834 6.599   8.528  1.00 13.20 ? 136 ASP   A C   1 
ATOM   992  O  O   . ASP   A 1 130 ? 14.194 7.776   8.394  1.00 14.48 ? 136 ASP   A O   1 
ATOM   993  C  CB  . ASP   A 1 130 ? 11.429 6.389   7.996  1.00 14.07 ? 136 ASP   A CB  1 
ATOM   994  C  CG  . ASP   A 1 130 ? 11.604 5.370   6.874  1.00 16.62 ? 136 ASP   A CG  1 
ATOM   995  O  OD1 . ASP   A 1 130 ? 11.777 4.174   7.181  1.00 15.68 ? 136 ASP   A OD1 1 
ATOM   996  O  OD2 . ASP   A 1 130 ? 11.562 5.776   5.688  1.00 18.62 ? 136 ASP   A OD2 1 
ATOM   997  N  N   . VAL   A 1 131 ? 14.586 5.549   8.134  1.00 11.40 ? 137 VAL   A N   1 
ATOM   998  C  CA  . VAL   A 1 131 ? 15.860 5.758   7.423  1.00 11.71 ? 137 VAL   A CA  1 
ATOM   999  C  C   . VAL   A 1 131 ? 15.869 5.010   6.048  1.00 13.58 ? 137 VAL   A C   1 
ATOM   1000 O  O   . VAL   A 1 131 ? 16.848 5.099   5.320  1.00 14.93 ? 137 VAL   A O   1 
ATOM   1001 C  CB  . VAL   A 1 131 ? 17.097 5.376   8.281  1.00 11.79 ? 137 VAL   A CB  1 
ATOM   1002 C  CG1 . VAL   A 1 131 ? 17.156 6.224   9.573  1.00 12.84 ? 137 VAL   A CG1 1 
ATOM   1003 C  CG2 . VAL   A 1 131 ? 17.092 3.876   8.616  1.00 11.28 ? 137 VAL   A CG2 1 
ATOM   1004 N  N   . ARG   A 1 132 ? 14.825 4.237   5.722  1.00 13.59 ? 138 ARG   A N   1 
ATOM   1005 C  CA  . ARG   A 1 132 ? 14.801 3.393   4.520  1.00 14.25 ? 138 ARG   A CA  1 
ATOM   1006 C  C   . ARG   A 1 132 ? 14.901 4.152   3.199  1.00 16.03 ? 138 ARG   A C   1 
ATOM   1007 O  O   . ARG   A 1 132 ? 15.366 3.591   2.193  1.00 16.77 ? 138 ARG   A O   1 
ATOM   1008 C  CB  . ARG   A 1 132 ? 13.567 2.485   4.523  1.00 14.54 ? 138 ARG   A CB  1 
ATOM   1009 C  CG  . ARG   A 1 132 ? 13.528 1.532   5.727  1.00 15.01 ? 138 ARG   A CG  1 
ATOM   1010 C  CD  . ARG   A 1 132 ? 12.203 0.786   5.674  1.00 13.11 ? 138 ARG   A CD  1 
ATOM   1011 N  NE  . ARG   A 1 132 ? 11.094 1.666   6.064  1.00 14.90 ? 138 ARG   A NE  1 
ATOM   1012 C  CZ  . ARG   A 1 132 ? 9.838  1.253   6.217  1.00 17.26 ? 138 ARG   A CZ  1 
ATOM   1013 N  NH1 . ARG   A 1 132 ? 9.499  0.004   5.915  1.00 17.76 ? 138 ARG   A NH1 1 
ATOM   1014 N  NH2 . ARG   A 1 132 ? 8.907  2.090   6.644  1.00 14.87 ? 138 ARG   A NH2 1 
ATOM   1015 N  N   . ASP   A 1 133 ? 14.490 5.422   3.188  1.00 15.75 ? 139 ASP   A N   1 
ATOM   1016 C  CA  . ASP   A 1 133 ? 14.566 6.226   1.975  1.00 15.89 ? 139 ASP   A CA  1 
ATOM   1017 C  C   . ASP   A 1 133 ? 15.987 6.791   1.734  1.00 17.13 ? 139 ASP   A C   1 
ATOM   1018 O  O   . ASP   A 1 133 ? 16.273 7.285   0.633  1.00 18.35 ? 139 ASP   A O   1 
ATOM   1019 C  CB  . ASP   A 1 133 ? 13.531 7.359   2.056  1.00 17.46 ? 139 ASP   A CB  1 
ATOM   1020 C  CG  . ASP   A 1 133 ? 13.850 8.370   3.146  1.00 21.63 ? 139 ASP   A CG  1 
ATOM   1021 O  OD1 . ASP   A 1 133 ? 14.141 7.944   4.277  1.00 21.10 ? 139 ASP   A OD1 1 
ATOM   1022 O  OD2 . ASP   A 1 133 ? 13.812 9.591   2.859  1.00 22.55 ? 139 ASP   A OD2 1 
ATOM   1023 N  N   . LEU   A 1 134 ? 16.891 6.732   2.743  1.00 16.63 ? 140 LEU   A N   1 
ATOM   1024 C  CA  . LEU   A 1 134 ? 18.236 7.327   2.590  1.00 16.51 ? 140 LEU   A CA  1 
ATOM   1025 C  C   . LEU   A 1 134 ? 19.145 6.364   1.882  1.00 17.21 ? 140 LEU   A C   1 
ATOM   1026 O  O   . LEU   A 1 134 ? 19.981 5.698   2.512  1.00 17.58 ? 140 LEU   A O   1 
ATOM   1027 C  CB  . LEU   A 1 134 ? 18.804 7.749   3.948  1.00 16.32 ? 140 LEU   A CB  1 
ATOM   1028 C  CG  . LEU   A 1 134 ? 17.895 8.665   4.774  1.00 17.76 ? 140 LEU   A CG  1 
ATOM   1029 C  CD1 . LEU   A 1 134 ? 18.409 8.814   6.217  1.00 18.24 ? 140 LEU   A CD1 1 
ATOM   1030 C  CD2 . LEU   A 1 134 ? 17.701 10.005  4.078  1.00 18.09 ? 140 LEU   A CD2 1 
ATOM   1031 N  N   . LEU   A 1 135 ? 18.965 6.243   0.553  1.00 17.72 ? 141 LEU   A N   1 
ATOM   1032 C  CA  . LEU   A 1 135 ? 19.686 5.238   -0.240 1.00 19.03 ? 141 LEU   A CA  1 
ATOM   1033 C  C   . LEU   A 1 135 ? 21.210 5.448   -0.227 1.00 20.74 ? 141 LEU   A C   1 
ATOM   1034 O  O   . LEU   A 1 135 ? 21.973 4.475   -0.339 1.00 21.75 ? 141 LEU   A O   1 
ATOM   1035 C  CB  . LEU   A 1 135 ? 19.146 5.163   -1.689 1.00 19.94 ? 141 LEU   A CB  1 
ATOM   1036 C  CG  . LEU   A 1 135 ? 17.636 5.083   -1.861 1.00 21.03 ? 141 LEU   A CG  1 
ATOM   1037 C  CD1 . LEU   A 1 135 ? 17.251 4.961   -3.352 1.00 21.86 ? 141 LEU   A CD1 1 
ATOM   1038 C  CD2 . LEU   A 1 135 ? 17.026 3.916   -1.058 1.00 21.38 ? 141 LEU   A CD2 1 
ATOM   1039 N  N   . TRP   A 1 136 ? 21.649 6.709   -0.034 1.00 20.69 ? 142 TRP   A N   1 
ATOM   1040 C  CA  . TRP   A 1 136 ? 23.063 7.068   -0.005 1.00 21.50 ? 142 TRP   A CA  1 
ATOM   1041 C  C   . TRP   A 1 136 ? 23.824 6.490   1.200  1.00 22.75 ? 142 TRP   A C   1 
ATOM   1042 O  O   . TRP   A 1 136 ? 25.058 6.472   1.179  1.00 22.72 ? 142 TRP   A O   1 
ATOM   1043 C  CB  . TRP   A 1 136 ? 23.240 8.596   -0.094 1.00 21.46 ? 142 TRP   A CB  1 
ATOM   1044 C  CG  . TRP   A 1 136 ? 22.501 9.358   0.970  1.00 21.15 ? 142 TRP   A CG  1 
ATOM   1045 C  CD1 . TRP   A 1 136 ? 21.253 9.898   0.876  1.00 21.87 ? 142 TRP   A CD1 1 
ATOM   1046 C  CD2 . TRP   A 1 136 ? 22.986 9.687   2.279  1.00 21.10 ? 142 TRP   A CD2 1 
ATOM   1047 N  NE1 . TRP   A 1 136 ? 20.938 10.565  2.042  1.00 22.05 ? 142 TRP   A NE1 1 
ATOM   1048 C  CE2 . TRP   A 1 136 ? 21.992 10.462  2.913  1.00 21.86 ? 142 TRP   A CE2 1 
ATOM   1049 C  CE3 . TRP   A 1 136 ? 24.196 9.460   2.953  1.00 21.58 ? 142 TRP   A CE3 1 
ATOM   1050 C  CZ2 . TRP   A 1 136 ? 22.145 10.953  4.209  1.00 22.47 ? 142 TRP   A CZ2 1 
ATOM   1051 C  CZ3 . TRP   A 1 136 ? 24.352 9.968   4.231  1.00 22.70 ? 142 TRP   A CZ3 1 
ATOM   1052 C  CH2 . TRP   A 1 136 ? 23.335 10.709  4.842  1.00 22.50 ? 142 TRP   A CH2 1 
ATOM   1053 N  N   . LEU   A 1 137 ? 23.110 6.006   2.246  1.00 22.75 ? 143 LEU   A N   1 
ATOM   1054 C  CA  . LEU   A 1 137 ? 23.769 5.410   3.416  1.00 24.71 ? 143 LEU   A CA  1 
ATOM   1055 C  C   . LEU   A 1 137 ? 24.589 4.169   3.063  1.00 29.38 ? 143 LEU   A C   1 
ATOM   1056 O  O   . LEU   A 1 137 ? 25.525 3.842   3.798  1.00 29.36 ? 143 LEU   A O   1 
ATOM   1057 C  CB  . LEU   A 1 137 ? 22.742 5.021   4.486  1.00 23.66 ? 143 LEU   A CB  1 
ATOM   1058 C  CG  . LEU   A 1 137 ? 22.063 6.157   5.233  1.00 22.52 ? 143 LEU   A CG  1 
ATOM   1059 C  CD1 . LEU   A 1 137 ? 21.013 5.591   6.204  1.00 22.19 ? 143 LEU   A CD1 1 
ATOM   1060 C  CD2 . LEU   A 1 137 ? 23.089 6.988   6.023  1.00 22.90 ? 143 LEU   A CD2 1 
ATOM   1061 N  N   . ASP   A 1 138 ? 24.238 3.485   1.938  1.00 32.93 ? 144 ASP   A N   1 
ATOM   1062 C  CA  . ASP   A 1 138 ? 24.877 2.266   1.434  1.00 36.99 ? 144 ASP   A CA  1 
ATOM   1063 C  C   . ASP   A 1 138 ? 25.924 2.468   0.385  1.00 40.94 ? 144 ASP   A C   1 
ATOM   1064 O  O   . ASP   A 1 138 ? 26.595 1.496   0.064  1.00 42.45 ? 144 ASP   A O   1 
ATOM   1065 C  CB  . ASP   A 1 138 ? 23.833 1.372   0.777  1.00 39.66 ? 144 ASP   A CB  1 
ATOM   1066 C  CG  . ASP   A 1 138 ? 22.941 0.695   1.757  1.00 45.52 ? 144 ASP   A CG  1 
ATOM   1067 O  OD1 . ASP   A 1 138 ? 23.426 0.353   2.859  1.00 47.44 ? 144 ASP   A OD1 1 
ATOM   1068 O  OD2 . ASP   A 1 138 ? 21.753 0.519   1.439  1.00 47.83 ? 144 ASP   A OD2 1 
ATOM   1069 N  N   . GLU   A 1 139 ? 25.993 3.642   -0.256 1.00 42.99 ? 145 GLU   A N   1 
ATOM   1070 C  CA  . GLU   A 1 139 ? 26.954 3.859   -1.339 1.00 45.57 ? 145 GLU   A CA  1 
ATOM   1071 C  C   . GLU   A 1 139 ? 28.151 4.712   -0.924 1.00 46.97 ? 145 GLU   A C   1 
ATOM   1072 O  O   . GLU   A 1 139 ? 28.870 5.231   -1.788 1.00 47.75 ? 145 GLU   A O   1 
ATOM   1073 C  CB  . GLU   A 1 139 ? 26.256 4.477   -2.565 1.00 49.21 ? 145 GLU   A CB  1 
ATOM   1074 C  CG  . GLU   A 1 139 ? 25.644 5.842   -2.296 1.00 54.77 ? 145 GLU   A CG  1 
ATOM   1075 C  CD  . GLU   A 1 139 ? 24.593 6.259   -3.304 1.00 61.75 ? 145 GLU   A CD  1 
ATOM   1076 O  OE1 . GLU   A 1 139 ? 24.421 7.481   -3.521 1.00 63.52 ? 145 GLU   A OE1 1 
ATOM   1077 O  OE2 . GLU   A 1 139 ? 23.940 5.359   -3.879 1.00 63.85 ? 145 GLU   A OE2 1 
HETATM 1078 N  N1  . A1BSN B 2 .   ? 11.748 14.172  17.946 1.00 16.21 ? 201 A1BSN A N1  1 
HETATM 1079 C  C4  . A1BSN B 2 .   ? 9.598  12.855  24.311 1.00 19.93 ? 201 A1BSN A C4  1 
HETATM 1080 C  C5  . A1BSN B 2 .   ? 9.410  13.311  22.875 1.00 18.93 ? 201 A1BSN A C5  1 
HETATM 1081 C  C6  . A1BSN B 2 .   ? 11.269 14.970  23.215 1.00 18.44 ? 201 A1BSN A C6  1 
HETATM 1082 C  C7  . A1BSN B 2 .   ? 12.639 14.792  22.559 1.00 18.14 ? 201 A1BSN A C7  1 
HETATM 1083 C  C8  . A1BSN B 2 .   ? 12.598 15.227  21.091 1.00 17.76 ? 201 A1BSN A C8  1 
HETATM 1084 C  C10 . A1BSN B 2 .   ? 11.368 15.021  18.887 1.00 17.52 ? 201 A1BSN A C10 1 
HETATM 1085 C  C13 . A1BSN B 2 .   ? 8.287  9.446   25.313 1.00 19.26 ? 201 A1BSN A C13 1 
HETATM 1086 O  O1  . A1BSN B 2 .   ? 10.949 16.155  18.634 1.00 17.75 ? 201 A1BSN A O1  1 
HETATM 1087 C  C9  . A1BSN B 2 .   ? 11.466 14.521  20.320 1.00 17.25 ? 201 A1BSN A C9  1 
HETATM 1088 C  C11 . A1BSN B 2 .   ? 10.142 14.776  21.046 1.00 17.75 ? 201 A1BSN A C11 1 
HETATM 1089 N  N   . A1BSN B 2 .   ? 10.224 14.294  22.429 1.00 18.33 ? 201 A1BSN A N   1 
HETATM 1090 O  O   . A1BSN B 2 .   ? 8.561  12.790  22.157 1.00 17.83 ? 201 A1BSN A O   1 
HETATM 1091 C  C3  . A1BSN B 2 .   ? 9.405  11.358  24.435 1.00 19.25 ? 201 A1BSN A C3  1 
HETATM 1092 C  C2  . A1BSN B 2 .   ? 10.116 10.484  23.622 1.00 18.98 ? 201 A1BSN A C2  1 
HETATM 1093 C  C12 . A1BSN B 2 .   ? 8.479  10.814  25.304 1.00 19.10 ? 201 A1BSN A C12 1 
HETATM 1094 N  N2  . A1BSN B 2 .   ? 8.979  8.598   24.536 1.00 18.72 ? 201 A1BSN A N2  1 
HETATM 1095 C  C1  . A1BSN B 2 .   ? 9.887  9.118   23.690 1.00 18.61 ? 201 A1BSN A C1  1 
HETATM 1096 C  C   . A1BSN B 2 .   ? 10.627 8.161   22.809 1.00 19.09 ? 201 A1BSN A C   1 
HETATM 1097 ZN ZN  . ZN    C 3 .   ? 11.098 -4.836  5.619  1.00 20.98 2 202 ZN    A ZN  1 
HETATM 1098 O  O   . HOH   D 4 .   ? 20.348 22.389  7.694  1.00 32.15 ? 301 HOH   A O   1 
HETATM 1099 O  O   . HOH   D 4 .   ? 35.739 15.542  16.912 1.00 40.99 ? 302 HOH   A O   1 
HETATM 1100 O  O   . HOH   D 4 .   ? 13.120 16.582  4.869  1.00 41.73 ? 303 HOH   A O   1 
HETATM 1101 O  O   . HOH   D 4 .   ? 22.819 -1.596  4.335  1.00 29.95 ? 304 HOH   A O   1 
HETATM 1102 O  O   . HOH   D 4 .   ? 12.968 6.672   31.253 1.00 33.59 ? 305 HOH   A O   1 
HETATM 1103 O  O   . HOH   D 4 .   ? 4.029  -5.034  21.295 1.00 20.90 ? 306 HOH   A O   1 
HETATM 1104 O  O   . HOH   D 4 .   ? 8.243  -4.249  0.763  1.00 31.99 ? 307 HOH   A O   1 
HETATM 1105 O  O   . HOH   D 4 .   ? 23.633 21.912  7.947  1.00 27.12 ? 308 HOH   A O   1 
HETATM 1106 O  O   . HOH   D 4 .   ? 10.581 4.699   3.548  1.00 17.73 ? 309 HOH   A O   1 
HETATM 1107 O  O   . HOH   D 4 .   ? 7.510  16.589  22.286 1.00 36.93 ? 310 HOH   A O   1 
HETATM 1108 O  O   . HOH   D 4 .   ? 30.868 9.814   13.841 1.00 35.67 ? 311 HOH   A O   1 
HETATM 1109 O  O   . HOH   D 4 .   ? 5.584  -7.003  7.451  1.00 49.89 ? 312 HOH   A O   1 
HETATM 1110 O  O   . HOH   D 4 .   ? 31.031 20.328  10.706 1.00 29.55 ? 313 HOH   A O   1 
HETATM 1111 O  O   . HOH   D 4 .   ? 3.051  7.929   10.091 1.00 28.95 ? 314 HOH   A O   1 
HETATM 1112 O  O   . HOH   D 4 .   ? 10.627 8.089   4.796  1.00 23.93 ? 315 HOH   A O   1 
HETATM 1113 O  O   . HOH   D 4 .   ? 20.311 8.702   19.159 1.00 15.77 ? 316 HOH   A O   1 
HETATM 1114 O  O   . HOH   D 4 .   ? 27.193 7.806   0.343  1.00 36.91 ? 317 HOH   A O   1 
HETATM 1115 O  O   . HOH   D 4 .   ? 9.138  2.323   2.977  1.00 22.82 ? 318 HOH   A O   1 
HETATM 1116 O  O   . HOH   D 4 .   ? 23.658 -0.103  15.790 1.00 34.51 ? 319 HOH   A O   1 
HETATM 1117 O  O   . HOH   D 4 .   ? 11.774 1.778   33.646 1.00 20.43 ? 320 HOH   A O   1 
HETATM 1118 O  O   . HOH   D 4 .   ? 27.749 15.869  3.050  1.00 34.30 ? 321 HOH   A O   1 
HETATM 1119 O  O   . HOH   D 4 .   ? 0.606  -0.357  16.582 1.00 13.14 ? 322 HOH   A O   1 
HETATM 1120 O  O   . HOH   D 4 .   ? 10.936 -5.193  31.776 1.00 34.38 ? 323 HOH   A O   1 
HETATM 1121 O  O   . HOH   D 4 .   ? 10.126 18.249  20.191 1.00 20.94 ? 324 HOH   A O   1 
HETATM 1122 O  O   . HOH   D 4 .   ? 6.563  -5.599  29.243 1.00 33.47 ? 325 HOH   A O   1 
HETATM 1123 O  O   . HOH   D 4 .   ? 19.463 -4.706  27.711 1.00 47.75 ? 326 HOH   A O   1 
HETATM 1124 O  O   . HOH   D 4 .   ? 5.198  6.027   24.078 1.00 23.51 ? 327 HOH   A O   1 
HETATM 1125 O  O   . HOH   D 4 .   ? 18.108 0.246   30.036 1.00 29.59 ? 328 HOH   A O   1 
HETATM 1126 O  O   . HOH   D 4 .   ? 3.619  22.294  22.356 1.00 34.93 ? 329 HOH   A O   1 
HETATM 1127 O  O   . HOH   D 4 .   ? 8.321  19.560  18.261 1.00 20.96 ? 330 HOH   A O   1 
HETATM 1128 O  O   . HOH   D 4 .   ? 8.089  -8.292  24.296 1.00 40.51 ? 331 HOH   A O   1 
HETATM 1129 O  O   . HOH   D 4 .   ? 30.328 11.014  19.607 1.00 26.25 ? 332 HOH   A O   1 
HETATM 1130 O  O   . HOH   D 4 .   ? 15.257 2.184   23.327 1.00 15.28 ? 333 HOH   A O   1 
HETATM 1131 O  O   . HOH   D 4 .   ? 6.212  7.910   28.558 1.00 39.34 ? 334 HOH   A O   1 
HETATM 1132 O  O   . HOH   D 4 .   ? 29.640 3.157   10.691 1.00 20.05 ? 335 HOH   A O   1 
HETATM 1133 O  O   . HOH   D 4 .   ? 32.612 21.469  19.497 1.00 46.34 ? 336 HOH   A O   1 
HETATM 1134 O  O   . HOH   D 4 .   ? 17.999 21.034  9.665  1.00 19.71 ? 337 HOH   A O   1 
HETATM 1135 O  O   . HOH   D 4 .   ? 11.543 11.432  11.567 1.00 14.13 ? 338 HOH   A O   1 
HETATM 1136 O  O   . HOH   D 4 .   ? 0.096  2.021   24.421 1.00 24.24 ? 339 HOH   A O   1 
HETATM 1137 O  O   . HOH   D 4 .   ? 0.076  15.774  8.407  1.00 45.09 ? 340 HOH   A O   1 
HETATM 1138 O  O   . HOH   D 4 .   ? 11.213 17.480  26.704 1.00 44.11 ? 341 HOH   A O   1 
HETATM 1139 O  O   . HOH   D 4 .   ? 17.559 20.722  18.909 1.00 34.78 ? 342 HOH   A O   1 
HETATM 1140 O  O   . HOH   D 4 .   ? 15.247 11.085  0.983  1.00 28.56 ? 343 HOH   A O   1 
HETATM 1141 O  O   . HOH   D 4 .   ? 19.485 -0.559  27.423 1.00 29.43 ? 344 HOH   A O   1 
HETATM 1142 O  O   . HOH   D 4 .   ? 0.226  14.570  17.394 1.00 28.35 ? 345 HOH   A O   1 
HETATM 1143 O  O   . HOH   D 4 .   ? 6.207  1.522   6.136  1.00 18.83 ? 346 HOH   A O   1 
HETATM 1144 O  O   . HOH   D 4 .   ? 7.226  3.341   33.048 1.00 21.32 ? 347 HOH   A O   1 
HETATM 1145 O  O   . HOH   D 4 .   ? 21.688 18.995  17.708 1.00 31.41 ? 348 HOH   A O   1 
HETATM 1146 O  O   . HOH   D 4 .   ? 19.384 8.857   25.839 1.00 25.24 ? 349 HOH   A O   1 
HETATM 1147 O  O   . HOH   D 4 .   ? 18.593 19.001  5.485  1.00 32.82 ? 350 HOH   A O   1 
HETATM 1148 O  O   . HOH   D 4 .   ? 4.149  -5.214  6.509  1.00 26.49 ? 351 HOH   A O   1 
HETATM 1149 O  O   . HOH   D 4 .   ? 10.291 4.017   33.949 1.00 26.95 ? 352 HOH   A O   1 
HETATM 1150 O  O   . HOH   D 4 .   ? 5.290  13.499  24.970 1.00 42.01 ? 353 HOH   A O   1 
HETATM 1151 O  O   . HOH   D 4 .   ? 31.174 20.473  17.042 1.00 22.69 ? 354 HOH   A O   1 
HETATM 1152 O  O   . HOH   D 4 .   ? 0.798  -2.698  20.009 1.00 29.21 ? 355 HOH   A O   1 
HETATM 1153 O  O   . HOH   D 4 .   ? 15.534 11.979  24.251 1.00 20.57 ? 356 HOH   A O   1 
HETATM 1154 O  O   . HOH   D 4 .   ? 30.323 4.605   3.701  1.00 33.68 ? 357 HOH   A O   1 
HETATM 1155 O  O   . HOH   D 4 .   ? 13.880 8.834   29.983 1.00 21.39 ? 358 HOH   A O   1 
HETATM 1156 O  O   . HOH   D 4 .   ? 10.678 17.162  5.370  1.00 51.35 ? 359 HOH   A O   1 
HETATM 1157 O  O   . HOH   D 4 .   ? -0.382 12.320  21.225 1.00 47.69 ? 360 HOH   A O   1 
HETATM 1158 O  O   . HOH   D 4 .   ? 23.807 12.691  23.719 1.00 52.06 ? 361 HOH   A O   1 
HETATM 1159 O  O   . HOH   D 4 .   ? 0.239  4.033   6.853  1.00 25.19 ? 362 HOH   A O   1 
HETATM 1160 O  O   . HOH   D 4 .   ? -0.621 -4.845  15.915 0.50 23.32 ? 363 HOH   A O   1 
HETATM 1161 O  O   . HOH   D 4 .   ? 13.370 10.312  9.455  1.00 12.89 ? 364 HOH   A O   1 
HETATM 1162 O  O   . HOH   D 4 .   ? 5.300  -1.735  29.592 1.00 46.92 ? 365 HOH   A O   1 
HETATM 1163 O  O   . HOH   D 4 .   ? 18.890 4.069   26.034 1.00 35.24 ? 366 HOH   A O   1 
HETATM 1164 O  O   . HOH   D 4 .   ? 14.669 14.202  3.733  1.00 28.66 ? 367 HOH   A O   1 
HETATM 1165 O  O   . HOH   D 4 .   ? 3.221  3.562   27.921 1.00 35.01 ? 368 HOH   A O   1 
HETATM 1166 O  O   . HOH   D 4 .   ? 31.717 15.218  6.432  1.00 45.11 ? 369 HOH   A O   1 
HETATM 1167 O  O   . HOH   D 4 .   ? 26.178 3.763   20.003 1.00 35.53 ? 370 HOH   A O   1 
HETATM 1168 O  O   . HOH   D 4 .   ? 5.464  -1.672  24.190 1.00 20.24 ? 371 HOH   A O   1 
HETATM 1169 O  O   . HOH   D 4 .   ? 14.860 -4.530  17.348 1.00 24.97 ? 372 HOH   A O   1 
HETATM 1170 O  O   . HOH   D 4 .   ? 14.618 20.876  8.414  1.00 38.02 ? 373 HOH   A O   1 
HETATM 1171 O  O   . HOH   D 4 .   ? 15.362 13.815  26.237 1.00 31.87 ? 374 HOH   A O   1 
HETATM 1172 O  O   . HOH   D 4 .   ? 8.272  -7.283  8.747  1.00 38.72 ? 375 HOH   A O   1 
HETATM 1173 O  O   . HOH   D 4 .   ? 28.796 -2.135  13.166 1.00 40.91 ? 376 HOH   A O   1 
HETATM 1174 O  O   . HOH   D 4 .   ? 6.088  14.314  22.048 1.00 41.87 ? 377 HOH   A O   1 
HETATM 1175 O  O   . HOH   D 4 .   ? 18.667 -0.640  19.562 1.00 23.10 ? 378 HOH   A O   1 
HETATM 1176 O  O   . HOH   D 4 .   ? 18.981 12.720  2.100  1.00 42.18 ? 379 HOH   A O   1 
HETATM 1177 O  O   . HOH   D 4 .   ? -0.392 15.132  13.206 1.00 34.50 ? 380 HOH   A O   1 
HETATM 1178 O  O   . HOH   D 4 .   ? 18.157 2.180   23.291 1.00 17.28 ? 381 HOH   A O   1 
HETATM 1179 O  O   . HOH   D 4 .   ? 18.203 18.751  17.206 1.00 15.03 ? 382 HOH   A O   1 
HETATM 1180 O  O   . HOH   D 4 .   ? 4.959  6.949   3.232  1.00 42.67 ? 383 HOH   A O   1 
HETATM 1181 O  O   . HOH   D 4 .   ? 35.255 20.168  11.968 1.00 29.46 ? 384 HOH   A O   1 
HETATM 1182 O  O   . HOH   D 4 .   ? 23.198 18.383  19.518 1.00 29.20 ? 385 HOH   A O   1 
HETATM 1183 O  O   . HOH   D 4 .   ? 35.413 10.601  10.173 1.00 36.67 ? 386 HOH   A O   1 
HETATM 1184 O  O   . HOH   D 4 .   ? 3.964  15.031  20.637 1.00 32.23 ? 387 HOH   A O   1 
HETATM 1185 O  O   . HOH   D 4 .   ? 2.157  13.014  5.632  1.00 29.95 ? 388 HOH   A O   1 
HETATM 1186 O  O   . HOH   D 4 .   ? 0.816  -2.880  9.889  1.00 30.71 ? 389 HOH   A O   1 
HETATM 1187 O  O   . HOH   D 4 .   ? 6.882  12.608  5.611  1.00 22.69 ? 390 HOH   A O   1 
HETATM 1188 O  O   . HOH   D 4 .   ? 17.097 16.943  4.088  1.00 39.43 ? 391 HOH   A O   1 
HETATM 1189 O  O   . HOH   D 4 .   ? 3.768  -2.530  21.914 1.00 31.21 ? 392 HOH   A O   1 
HETATM 1190 O  O   . HOH   D 4 .   ? 11.444 10.059  1.057  1.00 37.62 ? 393 HOH   A O   1 
HETATM 1191 O  O   . HOH   D 4 .   ? 1.238  -2.999  17.406 1.00 24.34 ? 394 HOH   A O   1 
HETATM 1192 O  O   . HOH   D 4 .   ? -0.200 16.111  22.127 1.00 50.47 ? 395 HOH   A O   1 
HETATM 1193 O  O   . HOH   D 4 .   ? 20.926 19.108  21.495 1.00 34.87 ? 396 HOH   A O   1 
HETATM 1194 O  O   . HOH   D 4 .   ? 24.041 2.244   19.599 1.00 26.96 ? 397 HOH   A O   1 
HETATM 1195 O  O   . HOH   D 4 .   ? 31.893 14.534  21.349 1.00 24.71 ? 398 HOH   A O   1 
HETATM 1196 O  O   . HOH   D 4 .   ? 31.731 9.008   5.606  1.00 32.20 ? 399 HOH   A O   1 
HETATM 1197 O  O   . HOH   D 4 .   ? 22.639 18.875  6.084  1.00 25.97 ? 400 HOH   A O   1 
HETATM 1198 O  O   . HOH   D 4 .   ? 12.249 21.101  12.706 1.00 28.22 ? 401 HOH   A O   1 
HETATM 1199 O  O   . HOH   D 4 .   ? 23.583 16.025  22.946 1.00 46.10 ? 402 HOH   A O   1 
HETATM 1200 O  O   . HOH   D 4 .   ? 24.542 7.183   20.390 1.00 37.74 ? 403 HOH   A O   1 
HETATM 1201 O  O   . HOH   D 4 .   ? 6.694  17.224  24.793 1.00 62.81 ? 404 HOH   A O   1 
HETATM 1202 O  O   . HOH   D 4 .   ? 8.110  -5.496  31.836 1.00 39.45 ? 405 HOH   A O   1 
HETATM 1203 O  O   . HOH   D 4 .   ? 31.328 2.454   12.767 1.00 25.87 ? 406 HOH   A O   1 
HETATM 1204 O  O   . HOH   D 4 .   ? 12.337 -8.057  13.141 1.00 25.78 ? 407 HOH   A O   1 
HETATM 1205 O  O   . HOH   D 4 .   ? 9.742  21.044  11.252 1.00 36.60 ? 408 HOH   A O   1 
HETATM 1206 O  O   . HOH   D 4 .   ? 15.990 -4.912  1.896  1.00 28.90 ? 409 HOH   A O   1 
HETATM 1207 O  O   . HOH   D 4 .   ? 19.813 23.660  15.575 1.00 25.10 ? 410 HOH   A O   1 
HETATM 1208 O  O   . HOH   D 4 .   ? 26.518 -1.884  14.551 1.00 29.51 ? 411 HOH   A O   1 
HETATM 1209 O  O   . HOH   D 4 .   ? 18.107 8.736   -1.458 1.00 29.31 ? 412 HOH   A O   1 
HETATM 1210 O  O   . HOH   D 4 .   ? 4.524  11.129  19.272 1.00 36.93 ? 413 HOH   A O   1 
HETATM 1211 O  O   . HOH   D 4 .   ? 6.358  22.602  11.034 1.00 34.65 ? 414 HOH   A O   1 
HETATM 1212 O  O   . HOH   D 4 .   ? 17.837 -7.867  24.699 1.00 48.39 ? 415 HOH   A O   1 
HETATM 1213 O  O   . HOH   D 4 .   ? 22.209 8.730   21.205 1.00 20.12 ? 416 HOH   A O   1 
HETATM 1214 O  O   . HOH   D 4 .   ? 7.236  10.677  4.315  1.00 37.42 ? 417 HOH   A O   1 
HETATM 1215 O  O   . HOH   D 4 .   ? 28.699 16.411  23.389 1.00 36.95 ? 418 HOH   A O   1 
HETATM 1216 O  O   . HOH   D 4 .   ? 18.033 10.641  0.423  1.00 32.49 ? 419 HOH   A O   1 
HETATM 1217 O  O   . HOH   D 4 .   ? 7.351  -5.531  2.876  1.00 28.66 ? 420 HOH   A O   1 
HETATM 1218 O  O   . HOH   D 4 .   ? 20.166 8.693   -2.472 1.00 30.01 ? 421 HOH   A O   1 
HETATM 1219 O  O   . HOH   D 4 .   ? 16.350 11.352  28.569 1.00 34.92 ? 422 HOH   A O   1 
HETATM 1220 O  O   . HOH   D 4 .   ? 28.088 19.265  5.782  1.00 56.72 ? 423 HOH   A O   1 
HETATM 1221 O  O   . HOH   D 4 .   ? 17.166 -3.682  18.052 1.00 36.24 ? 424 HOH   A O   1 
HETATM 1222 O  O   . HOH   D 4 .   ? 21.162 21.879  17.839 1.00 29.50 ? 425 HOH   A O   1 
HETATM 1223 O  O   . HOH   D 4 .   ? 8.755  22.375  26.488 1.00 39.24 ? 426 HOH   A O   1 
HETATM 1224 O  O   . HOH   D 4 .   ? 17.695 10.952  26.091 1.00 30.45 ? 427 HOH   A O   1 
HETATM 1225 O  O   . HOH   D 4 .   ? 8.865  17.341  26.075 1.00 51.11 ? 428 HOH   A O   1 
HETATM 1226 O  O   . HOH   D 4 .   ? 8.597  19.582  7.745  1.00 62.73 ? 429 HOH   A O   1 
HETATM 1227 O  O   . HOH   D 4 .   ? 1.877  1.418   26.633 1.00 28.55 ? 430 HOH   A O   1 
HETATM 1228 O  O   . HOH   D 4 .   ? 4.434  -2.467  26.660 1.00 32.08 ? 431 HOH   A O   1 
HETATM 1229 O  O   . HOH   D 4 .   ? 6.524  2.462   3.588  1.00 25.82 ? 432 HOH   A O   1 
HETATM 1230 O  O   . HOH   D 4 .   ? 0.915  -2.179  23.646 1.00 29.71 ? 433 HOH   A O   1 
HETATM 1231 O  O   . HOH   D 4 .   ? 32.857 21.645  15.091 1.00 31.37 ? 434 HOH   A O   1 
HETATM 1232 O  O   . HOH   D 4 .   ? 1.740  14.281  22.278 1.00 37.71 ? 435 HOH   A O   1 
HETATM 1233 O  O   . HOH   D 4 .   ? 5.089  4.713   32.599 1.00 39.28 ? 436 HOH   A O   1 
HETATM 1234 O  O   . HOH   D 4 .   ? 33.223 21.836  12.400 1.00 33.18 ? 437 HOH   A O   1 
HETATM 1235 O  O   . HOH   D 4 .   ? 30.282 1.212   17.668 1.00 40.94 ? 438 HOH   A O   1 
HETATM 1236 O  O   . HOH   D 4 .   ? 8.779  6.794   2.563  1.00 33.74 ? 439 HOH   A O   1 
HETATM 1237 O  O   . HOH   D 4 .   ? 21.008 -4.089  23.792 1.00 67.28 ? 440 HOH   A O   1 
HETATM 1238 O  O   . HOH   D 4 .   ? 30.973 0.588   14.811 1.00 50.87 ? 441 HOH   A O   1 
HETATM 1239 O  O   . HOH   D 4 .   ? 12.871 10.902  31.214 1.00 33.08 ? 442 HOH   A O   1 
HETATM 1240 O  O   . HOH   D 4 .   ? 32.125 3.986   14.888 1.00 25.49 ? 443 HOH   A O   1 
HETATM 1241 O  O   . HOH   D 4 .   ? 6.210  4.656   2.494  1.00 32.71 ? 444 HOH   A O   1 
HETATM 1242 O  O   . HOH   D 4 .   ? 4.045  -6.615  23.319 1.00 32.43 ? 445 HOH   A O   1 
HETATM 1243 O  O   . HOH   D 4 .   ? 9.954  14.917  27.132 1.00 42.59 ? 446 HOH   A O   1 
HETATM 1244 O  O   . HOH   D 4 .   ? 5.607  -8.592  23.489 1.00 30.92 ? 447 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   ? 0.3049 0.2471 0.2660 -0.0171 -0.0512 -0.0020 7   SER   A N   
2    C CA  . SER   A 1   ? 0.3087 0.2583 0.2894 -0.0147 -0.0551 0.0018  7   SER   A CA  
3    C C   . SER   A 1   ? 0.2915 0.2495 0.2901 -0.0089 -0.0513 0.0047  7   SER   A C   
4    O O   . SER   A 1   ? 0.2985 0.2559 0.2934 -0.0078 -0.0484 0.0051  7   SER   A O   
5    C CB  . SER   A 1   ? 0.3419 0.2901 0.3234 -0.0214 -0.0673 0.0087  7   SER   A CB  
6    O OG  . SER   A 1   ? 0.3825 0.3311 0.3640 -0.0236 -0.0727 0.0154  7   SER   A OG  
7    N N   . GLY   A 2   ? 0.2681 0.2325 0.2847 -0.0060 -0.0503 0.0062  8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.2526 0.2224 0.2851 -0.0017 -0.0447 0.0077  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.2464 0.2205 0.2889 0.0006  -0.0385 0.0048  8   GLY   A C   
10   O O   . GLY   A 2   ? 0.2518 0.2249 0.2870 0.0000  -0.0374 0.0010  8   GLY   A O   
11   N N   . ALA   A 3   ? 0.2212 0.1991 0.2800 0.0029  -0.0336 0.0064  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.2084 0.1893 0.2746 0.0035  -0.0266 0.0035  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.1933 0.1738 0.2673 0.0050  -0.0165 0.0019  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.1799 0.1584 0.2585 0.0066  -0.0159 0.0043  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.2079 0.1931 0.2895 0.0027  -0.0309 0.0074  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.1858 0.1667 0.2597 0.0034  -0.0084 -0.0019 10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.1768 0.1549 0.2557 0.0027  0.0032  -0.0049 10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.1813 0.1625 0.2793 0.0030  0.0084  -0.0039 10  ILE   A C   
19   O O   . ILE   A 4   ? 0.1856 0.1704 0.2840 0.0012  0.0058  -0.0036 10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.1809 0.1563 0.2419 -0.0020 0.0084  -0.0097 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.1697 0.1442 0.2152 -0.0022 0.0030  -0.0098 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.1845 0.1539 0.2458 -0.0050 0.0214  -0.0138 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.1706 0.1453 0.2015 -0.0075 0.0044  -0.0117 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.1923 0.1719 0.3079 0.0053  0.0164  -0.0030 11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.1985 0.1816 0.3367 0.0062  0.0234  -0.0017 11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.2214 0.1968 0.3575 0.0035  0.0408  -0.0087 11  TYR   A C   
27   O O   . TYR   A 5   ? 0.2352 0.2041 0.3746 0.0052  0.0477  -0.0102 11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.1860 0.1738 0.3519 0.0114  0.0183  0.0066  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.1855 0.1794 0.3502 0.0113  0.0008  0.0135  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.1885 0.1891 0.3613 0.0095  -0.0051 0.0166  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.1979 0.1893 0.3498 0.0115  -0.0092 0.0161  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.1903 0.1940 0.3587 0.0076  -0.0207 0.0222  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.2044 0.1986 0.3510 0.0095  -0.0239 0.0214  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.2079 0.2076 0.3613 0.0072  -0.0296 0.0239  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.2232 0.2233 0.3680 0.0035  -0.0436 0.0283  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.2213 0.1958 0.3491 -0.0019 0.0479  -0.0132 12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.2377 0.2029 0.3575 -0.0075 0.0650  -0.0207 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.2509 0.2190 0.3827 -0.0101 0.0738  -0.0218 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.2578 0.2319 0.3840 -0.0127 0.0661  -0.0197 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.2683 0.2271 0.3547 -0.0155 0.0641  -0.0255 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.2631 0.2290 0.3371 -0.0177 0.0508  -0.0223 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.2979 0.2460 0.3713 -0.0246 0.0811  -0.0333 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.2477 0.2114 0.3985 -0.0090 0.0905  -0.0247 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.2539 0.2206 0.4201 -0.0112 0.1013  -0.0257 13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.2527 0.2341 0.4409 -0.0064 0.0877  -0.0166 13  GLY   A C   
46   O O   . GLY   A 7   ? 0.2522 0.2404 0.4608 0.0010  0.0771  -0.0091 13  GLY   A O   
47   N N   . ASN   A 8   ? 0.2550 0.2405 0.4359 -0.0117 0.0857  -0.0167 14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.2531 0.2512 0.4513 -0.0088 0.0719  -0.0086 14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.2476 0.2472 0.4220 -0.0107 0.0537  -0.0065 14  ASN   A C   
50   O O   . ASN   A 8   ? 0.2498 0.2558 0.4271 -0.0123 0.0450  -0.0026 14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.2761 0.2788 0.4895 -0.0123 0.0817  -0.0086 14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.3424 0.3461 0.5893 -0.0084 0.0990  -0.0086 14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.3608 0.3726 0.6400 -0.0007 0.0940  -0.0006 14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.3660 0.3610 0.6064 -0.0142 0.1198  -0.0169 14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.2316 0.2254 0.3850 -0.0101 0.0482  -0.0086 15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.2248 0.2192 0.3580 -0.0112 0.0334  -0.0071 15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.2073 0.2024 0.3405 -0.0057 0.0222  -0.0037 15  TYR   A C   
58   O O   . TYR   A 9   ? 0.2040 0.1961 0.3423 -0.0025 0.0266  -0.0042 15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.2386 0.2257 0.3432 -0.0178 0.0370  -0.0123 15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.2572 0.2421 0.3548 -0.0259 0.0465  -0.0152 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.2751 0.2651 0.3765 -0.0282 0.0414  -0.0121 15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.2743 0.2507 0.3590 -0.0327 0.0606  -0.0212 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.2921 0.2796 0.3853 -0.0369 0.0499  -0.0142 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.2918 0.2647 0.3662 -0.0422 0.0695  -0.0239 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.3066 0.2856 0.3854 -0.0442 0.0639  -0.0200 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.3266 0.3016 0.3935 -0.0548 0.0726  -0.0222 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.1860 0.1832 0.3105 -0.0055 0.0087  -0.0009 16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.1670 0.1632 0.2851 -0.0023 -0.0019 0.0014  16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.1795 0.1719 0.2742 -0.0045 -0.0064 -0.0015 16  ARG   A C   
70   O O   . ARG   A 10  ? 0.1814 0.1744 0.2719 -0.0069 -0.0102 -0.0013 16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.1650 0.1663 0.2973 -0.0011 -0.0133 0.0080  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.2102 0.2082 0.3279 -0.0010 -0.0254 0.0095  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.2326 0.2346 0.3626 -0.0023 -0.0371 0.0168  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.2537 0.2507 0.3652 -0.0059 -0.0473 0.0161  16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.2512 0.2433 0.3496 -0.0071 -0.0545 0.0171  16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.2308 0.2231 0.3328 -0.0049 -0.0542 0.0198  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.2158 0.2012 0.2963 -0.0112 -0.0613 0.0151  16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.1779 0.1664 0.2596 -0.0036 -0.0058 -0.0037 17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.1791 0.1651 0.2429 -0.0051 -0.0092 -0.0054 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.1715 0.1560 0.2304 -0.0022 -0.0173 -0.0042 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.1683 0.1516 0.2277 -0.0002 -0.0176 -0.0035 17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.1942 0.1774 0.2470 -0.0076 -0.0024 -0.0082 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.2045 0.1874 0.2442 -0.0093 -0.0065 -0.0079 17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.1953 0.1773 0.2502 -0.0122 0.0077  -0.0104 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.1617 0.1446 0.2146 -0.0026 -0.0231 -0.0041 18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.1700 0.1491 0.2150 -0.0014 -0.0291 -0.0042 18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.1702 0.1458 0.2049 -0.0012 -0.0287 -0.0065 18  VAL   A C   
88   O O   . VAL   A 12  ? 0.1733 0.1504 0.2097 -0.0023 -0.0269 -0.0063 18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.1895 0.1676 0.2391 -0.0031 -0.0366 -0.0018 18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.2166 0.1991 0.2804 -0.0028 -0.0385 0.0026  18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.1809 0.1594 0.2341 -0.0052 -0.0378 -0.0018 18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.1626 0.1334 0.1880 -0.0003 -0.0304 -0.0082 19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.1711 0.1377 0.1910 0.0006  -0.0289 -0.0103 19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.1797 0.1426 0.2018 -0.0012 -0.0322 -0.0105 19  ASN   A C   
95   O O   . ASN   A 13  ? 0.1845 0.1446 0.2053 -0.0037 -0.0371 -0.0103 19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.1882 0.1484 0.1972 0.0010  -0.0281 -0.0130 19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.2046 0.1680 0.2108 0.0024  -0.0248 -0.0127 19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.2359 0.1998 0.2400 0.0015  -0.0268 -0.0115 19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.1804 0.1461 0.1880 0.0043  -0.0202 -0.0128 19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.1665 0.1294 0.1926 -0.0006 -0.0306 -0.0099 20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.1690 0.1275 0.1975 -0.0025 -0.0334 -0.0098 20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.1886 0.1360 0.2076 -0.0036 -0.0348 -0.0138 20  ARG   A C   
103  O O   . ARG   A 14  ? 0.1948 0.1380 0.2124 -0.0073 -0.0394 -0.0140 20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.1593 0.1187 0.1940 -0.0016 -0.0316 -0.0074 20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.1506 0.1063 0.1895 -0.0041 -0.0347 -0.0062 20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.1745 0.1295 0.2199 -0.0028 -0.0333 -0.0028 20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.2033 0.1549 0.2536 -0.0054 -0.0362 -0.0004 20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.2250 0.1658 0.2750 -0.0049 -0.0365 -0.0027 20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.2100 0.1415 0.2534 -0.0027 -0.0334 -0.0084 20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.2247 0.1627 0.2799 -0.0076 -0.0392 0.0002  20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.1856 0.1274 0.1969 -0.0016 -0.0304 -0.0172 21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.2133 0.1417 0.2116 -0.0044 -0.0297 -0.0223 21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.2367 0.1625 0.2240 -0.0101 -0.0362 -0.0223 21  HIS   A C   
114  O O   . HIS   A 15  ? 0.2653 0.1791 0.2392 -0.0155 -0.0380 -0.0259 21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.2280 0.1500 0.2217 -0.0013 -0.0210 -0.0265 21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.2418 0.1681 0.2299 -0.0005 -0.0189 -0.0265 21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.2436 0.1816 0.2417 0.0033  -0.0175 -0.0226 21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.2593 0.1782 0.2312 -0.0042 -0.0180 -0.0300 21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.2580 0.1962 0.2476 0.0027  -0.0158 -0.0237 21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.2579 0.1849 0.2316 -0.0018 -0.0162 -0.0278 21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.2234 0.1598 0.2171 -0.0097 -0.0402 -0.0178 22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.2321 0.1686 0.2213 -0.0147 -0.0478 -0.0150 22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.2307 0.1752 0.2344 -0.0165 -0.0545 -0.0095 22  LEU   A C   
124  O O   . LEU   A 16  ? 0.2328 0.1801 0.2389 -0.0201 -0.0617 -0.0049 22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.2377 0.1792 0.2260 -0.0126 -0.0466 -0.0131 22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.2628 0.1970 0.2365 -0.0121 -0.0404 -0.0179 22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.2660 0.2050 0.2386 -0.0113 -0.0406 -0.0151 22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.2717 0.1913 0.2257 -0.0189 -0.0414 -0.0222 22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.2220 0.1706 0.2367 -0.0143 -0.0520 -0.0091 23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.2256 0.1824 0.2554 -0.0159 -0.0561 -0.0043 23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.2268 0.1791 0.2535 -0.0230 -0.0655 -0.0021 23  ALA   A C   
132  O O   . ALA   A 17  ? 0.2405 0.1811 0.2526 -0.0270 -0.0670 -0.0060 23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.2280 0.1876 0.2657 -0.0142 -0.0517 -0.0047 23  ALA   A CB  
134  N N   . THR   A 18  ? 0.2242 0.1854 0.2656 -0.0251 -0.0714 0.0045  24  THR   A N   
135  C CA  . THR   A 18  ? 0.2311 0.1905 0.2725 -0.0331 -0.0824 0.0089  24  THR   A CA  
136  C C   . THR   A 18  ? 0.2367 0.1984 0.2884 -0.0355 -0.0836 0.0101  24  THR   A C   
137  O O   . THR   A 18  ? 0.2300 0.1958 0.2899 -0.0309 -0.0759 0.0083  24  THR   A O   
138  C CB  . THR   A 18  ? 0.2424 0.2122 0.3001 -0.0340 -0.0890 0.0178  24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.2469 0.2294 0.3302 -0.0290 -0.0837 0.0212  24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.2487 0.2167 0.2982 -0.0315 -0.0878 0.0176  24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.2521 0.2117 0.3035 -0.0440 -0.0940 0.0142  25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.2766 0.2399 0.3399 -0.0472 -0.0961 0.0167  25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.2561 0.2361 0.3479 -0.0421 -0.0916 0.0222  25  HIS   A C   
144  O O   . HIS   A 19  ? 0.2575 0.2405 0.3573 -0.0408 -0.0859 0.0211  25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.3224 0.2821 0.3817 -0.0585 -0.1098 0.0218  25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.4408 0.3808 0.4704 -0.0654 -0.1118 0.0147  25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.4999 0.4302 0.5227 -0.0688 -0.1105 0.0104  25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.4910 0.4181 0.4962 -0.0693 -0.1133 0.0105  25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.5280 0.4392 0.5235 -0.0744 -0.1104 0.0033  25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.5300 0.4386 0.5132 -0.0753 -0.1117 0.0028  25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.2324 0.2222 0.3395 -0.0397 -0.0930 0.0281  26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.2218 0.2256 0.3569 -0.0348 -0.0860 0.0323  26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.2044 0.2075 0.3356 -0.0280 -0.0718 0.0253  26  ASN   A C   
154  O O   . ASN   A 20  ? 0.1989 0.2087 0.3446 -0.0266 -0.0637 0.0256  26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.2562 0.2687 0.4097 -0.0329 -0.0894 0.0400  26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.3418 0.3673 0.5271 -0.0277 -0.0799 0.0439  26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.3559 0.3903 0.5628 -0.0303 -0.0811 0.0494  26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.3568 0.3828 0.5450 -0.0207 -0.0686 0.0404  26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.1854 0.1801 0.2964 -0.0249 -0.0685 0.0193  27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.1726 0.1665 0.2785 -0.0201 -0.0571 0.0139  27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.1819 0.1730 0.2836 -0.0225 -0.0547 0.0116  27  ASP   A C   
162  O O   . ASP   A 21  ? 0.1797 0.1753 0.2884 -0.0220 -0.0468 0.0112  27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.1862 0.1720 0.2725 -0.0174 -0.0559 0.0091  27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.2174 0.2059 0.3069 -0.0144 -0.0553 0.0108  27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.2117 0.2077 0.3182 -0.0121 -0.0504 0.0135  27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.2420 0.2240 0.3168 -0.0147 -0.0591 0.0093  27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.1869 0.1694 0.2769 -0.0261 -0.0614 0.0103  28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.1945 0.1731 0.2814 -0.0284 -0.0600 0.0090  28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.2059 0.1927 0.3100 -0.0324 -0.0604 0.0136  28  TRP   A C   
170  O O   . TRP   A 22  ? 0.2104 0.1978 0.3158 -0.0337 -0.0558 0.0134  28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.2070 0.1722 0.2780 -0.0311 -0.0656 0.0058  28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.2116 0.1684 0.2685 -0.0268 -0.0609 0.0007  28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.2316 0.1818 0.2762 -0.0254 -0.0614 -0.0026 28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.2015 0.1560 0.2569 -0.0240 -0.0554 -0.0005 28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.2372 0.1819 0.2749 -0.0210 -0.0552 -0.0062 28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.2225 0.1702 0.2678 -0.0200 -0.0523 -0.0043 28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.2010 0.1591 0.2633 -0.0251 -0.0530 0.0023  28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.2216 0.1669 0.2668 -0.0166 -0.0477 -0.0045 28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.2093 0.1642 0.2687 -0.0227 -0.0496 0.0024  28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.2144 0.1636 0.2670 -0.0181 -0.0473 -0.0005 28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.1991 0.1928 0.3173 -0.0349 -0.0662 0.0186  29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.2038 0.2071 0.3425 -0.0386 -0.0661 0.0239  29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.2094 0.2222 0.3634 -0.0351 -0.0534 0.0241  29  ALA   A C   
184  O O   . ALA   A 23  ? 0.2162 0.2357 0.3848 -0.0380 -0.0491 0.0267  29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.2053 0.2147 0.3581 -0.0424 -0.0767 0.0309  29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.1916 0.2044 0.3424 -0.0298 -0.0469 0.0212  30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.1868 0.2049 0.3475 -0.0275 -0.0334 0.0197  30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.1913 0.2021 0.3307 -0.0261 -0.0269 0.0137  30  ASN   A C   
189  O O   . ASN   A 24  ? 0.1798 0.1911 0.3194 -0.0236 -0.0179 0.0112  30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.1817 0.2063 0.3609 -0.0233 -0.0315 0.0229  30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.2198 0.2541 0.4251 -0.0252 -0.0382 0.0311  30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.2540 0.2964 0.4809 -0.0264 -0.0309 0.0338  30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.2135 0.2470 0.4170 -0.0265 -0.0522 0.0356  30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.1952 0.1988 0.3177 -0.0282 -0.0314 0.0121  31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.1963 0.1940 0.3011 -0.0276 -0.0280 0.0087  31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.2144 0.2141 0.3177 -0.0314 -0.0172 0.0076  31  LEU   A C   
197  O O   . LEU   A 25  ? 0.2308 0.2327 0.3396 -0.0363 -0.0143 0.0093  31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.1900 0.1805 0.2839 -0.0295 -0.0349 0.0090  31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.1911 0.1766 0.2712 -0.0292 -0.0332 0.0080  31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.1995 0.1831 0.2725 -0.0240 -0.0330 0.0053  31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.1821 0.1606 0.2576 -0.0307 -0.0391 0.0096  31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.2023 0.1997 0.2953 -0.0305 -0.0116 0.0048  32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.2091 0.2053 0.2936 -0.0362 -0.0018 0.0031  32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.2210 0.2123 0.2877 -0.0391 -0.0068 0.0045  32  VAL   A C   
205  O O   . VAL   A 26  ? 0.2355 0.2252 0.2944 -0.0464 -0.0058 0.0067  32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.2218 0.2180 0.3082 -0.0341 0.0077  -0.0006 32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.2343 0.2259 0.3050 -0.0418 0.0175  -0.0034 32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.2164 0.2182 0.3258 -0.0311 0.0133  -0.0003 32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.2107 0.2000 0.2726 -0.0338 -0.0125 0.0042  33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.1985 0.1848 0.2490 -0.0354 -0.0171 0.0066  33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.1815 0.1659 0.2327 -0.0279 -0.0231 0.0060  33  TRP   A C   
212  O O   . TRP   A 27  ? 0.1722 0.1574 0.2258 -0.0233 -0.0219 0.0030  33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.2064 0.1922 0.2451 -0.0409 -0.0109 0.0058  33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.2163 0.2010 0.2457 -0.0427 -0.0163 0.0097  33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.2401 0.2242 0.2645 -0.0490 -0.0214 0.0160  33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.2168 0.2019 0.2434 -0.0386 -0.0177 0.0089  33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.2489 0.2338 0.2697 -0.0487 -0.0262 0.0198  33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.2312 0.2168 0.2528 -0.0424 -0.0234 0.0151  33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.2165 0.2018 0.2451 -0.0324 -0.0149 0.0045  33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.2358 0.2231 0.2558 -0.0401 -0.0257 0.0166  33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.2258 0.2117 0.2501 -0.0305 -0.0169 0.0053  33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.2279 0.2151 0.2487 -0.0342 -0.0219 0.0111  33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.1786 0.1600 0.2280 -0.0271 -0.0287 0.0090  34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.1727 0.1512 0.2222 -0.0207 -0.0317 0.0077  34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.1801 0.1578 0.2288 -0.0212 -0.0344 0.0126  34  GLU   A C   
226  O O   . GLU   A 28  ? 0.1719 0.1495 0.2218 -0.0259 -0.0369 0.0177  34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.1752 0.1487 0.2285 -0.0172 -0.0352 0.0052  34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.2159 0.1856 0.2730 -0.0201 -0.0387 0.0077  34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.2414 0.2058 0.2998 -0.0190 -0.0410 0.0109  34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.2580 0.2213 0.3195 -0.0229 -0.0433 0.0153  34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.2377 0.1991 0.2956 -0.0141 -0.0402 0.0095  34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.1729 0.1507 0.2211 -0.0168 -0.0340 0.0119  35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.1739 0.1525 0.2266 -0.0162 -0.0365 0.0176  35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.1734 0.1482 0.2305 -0.0085 -0.0349 0.0145  35  ASP   A C   
235  O O   . ASP   A 29  ? 0.1856 0.1620 0.2387 -0.0060 -0.0321 0.0112  35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.1846 0.1693 0.2318 -0.0220 -0.0367 0.0220  35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.2498 0.2375 0.3043 -0.0237 -0.0417 0.0311  35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.2789 0.2643 0.3454 -0.0173 -0.0426 0.0327  35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.2659 0.2578 0.3143 -0.0320 -0.0444 0.0369  35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.1635 0.1318 0.2282 -0.0052 -0.0357 0.0152  36  SER   A N   
241  C CA  A SER   A 30  ? 0.1738 0.1357 0.2422 0.0012  -0.0318 0.0113  36  SER   A CA  
242  C CA  B SER   A 30  ? 0.1726 0.1347 0.2404 0.0012  -0.0317 0.0110  36  SER   A CA  
243  C C   . SER   A 30  ? 0.1745 0.1426 0.2502 0.0038  -0.0300 0.0155  36  SER   A C   
244  O O   . SER   A 30  ? 0.1823 0.1487 0.2564 0.0078  -0.0252 0.0111  36  SER   A O   
245  C CB  A SER   A 30  ? 0.1938 0.1463 0.2707 0.0031  -0.0319 0.0122  36  SER   A CB  
246  C CB  B SER   A 30  ? 0.1922 0.1437 0.2665 0.0033  -0.0313 0.0103  36  SER   A CB  
247  O OG  A SER   A 30  ? 0.2354 0.1781 0.3129 0.0083  -0.0258 0.0061  36  SER   A OG  
248  O OG  B SER   A 30  ? 0.2086 0.1625 0.2972 0.0036  -0.0336 0.0191  36  SER   A OG  
249  N N   . SER   A 31  ? 0.1726 0.1482 0.2564 0.0002  -0.0345 0.0251  37  SER   A N   
250  C CA  . SER   A 31  ? 0.1805 0.1637 0.2737 0.0014  -0.0346 0.0311  37  SER   A CA  
251  C C   . SER   A 31  ? 0.1690 0.1574 0.2500 -0.0004 -0.0326 0.0273  37  SER   A C   
252  O O   . SER   A 31  ? 0.1679 0.1609 0.2552 0.0018  -0.0307 0.0294  37  SER   A O   
253  C CB  . SER   A 31  ? 0.2122 0.2023 0.3150 -0.0043 -0.0421 0.0438  37  SER   A CB  
254  O OG  . SER   A 31  ? 0.2638 0.2593 0.3521 -0.0137 -0.0462 0.0460  37  SER   A OG  
255  N N   . ARG   A 32  ? 0.1582 0.1456 0.2243 -0.0042 -0.0324 0.0220  38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.1679 0.1584 0.2235 -0.0058 -0.0299 0.0184  38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.1670 0.1518 0.2157 -0.0010 -0.0255 0.0094  38  ARG   A C   
258  O O   . ARG   A 32  ? 0.1748 0.1612 0.2165 -0.0014 -0.0234 0.0067  38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.1724 0.1653 0.2174 -0.0139 -0.0312 0.0191  38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.1868 0.1846 0.2322 -0.0220 -0.0362 0.0281  38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.1922 0.1892 0.2231 -0.0316 -0.0352 0.0270  38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.1688 0.1655 0.1896 -0.0331 -0.0304 0.0219  38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.2017 0.1971 0.2089 -0.0428 -0.0283 0.0216  38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.2107 0.2054 0.2106 -0.0529 -0.0307 0.0261  38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.1898 0.1832 0.1892 -0.0434 -0.0232 0.0165  38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.1637 0.1412 0.2134 0.0021  -0.0250 0.0056  39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.1589 0.1302 0.2003 0.0040  -0.0232 -0.0014 39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.1622 0.1365 0.1978 0.0008  -0.0246 -0.0026 39  ASP   A C   
269  O O   . ASP   A 33  ? 0.1667 0.1396 0.1965 0.0017  -0.0237 -0.0058 39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.1662 0.1351 0.2040 0.0075  -0.0188 -0.0048 39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.1943 0.1556 0.2207 0.0074  -0.0183 -0.0108 39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.1812 0.1357 0.2050 0.0061  -0.0204 -0.0131 39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.1964 0.1586 0.2161 0.0074  -0.0168 -0.0124 39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.1570 0.1345 0.1947 -0.0032 -0.0262 0.0002  40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.1539 0.1336 0.1895 -0.0058 -0.0251 -0.0013 40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.1561 0.1345 0.1959 -0.0078 -0.0271 -0.0011 40  LEU   A C   
277  O O   . LEU   A 34  ? 0.1606 0.1378 0.2031 -0.0094 -0.0292 0.0014  40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.1528 0.1368 0.1851 -0.0108 -0.0225 0.0010  40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.1656 0.1514 0.1929 -0.0106 -0.0202 0.0006  40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.1619 0.1494 0.1829 -0.0179 -0.0174 0.0020  40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.1826 0.1662 0.2086 -0.0066 -0.0183 -0.0035 40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.1463 0.1255 0.1885 -0.0079 -0.0266 -0.0028 41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.1572 0.1375 0.2063 -0.0103 -0.0278 -0.0019 41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.1585 0.1430 0.2133 -0.0111 -0.0231 -0.0024 41  LEU   A C   
285  O O   . LEU   A 35  ? 0.1679 0.1525 0.2228 -0.0085 -0.0220 -0.0034 41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.1549 0.1308 0.2053 -0.0093 -0.0336 -0.0026 41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.1786 0.1564 0.2378 -0.0127 -0.0360 -0.0007 41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.1799 0.1507 0.2360 -0.0139 -0.0416 -0.0011 41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.1935 0.1763 0.2627 -0.0127 -0.0366 0.0007  41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.1588 0.1459 0.2192 -0.0149 -0.0192 -0.0015 42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.1588 0.1489 0.2279 -0.0156 -0.0120 -0.0024 42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.1620 0.1556 0.2454 -0.0167 -0.0133 -0.0002 42  VAL   A C   
293  O O   . VAL   A 36  ? 0.1611 0.1546 0.2434 -0.0202 -0.0152 0.0011  42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.1760 0.1649 0.2372 -0.0209 -0.0030 -0.0042 42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.1866 0.1764 0.2583 -0.0218 0.0075  -0.0063 42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.1849 0.1712 0.2331 -0.0208 -0.0031 -0.0053 42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.1511 0.1483 0.2491 -0.0138 -0.0137 0.0014  43  SER   A N   
298  C CA  . SER   A 37  ? 0.1560 0.1585 0.2719 -0.0150 -0.0151 0.0049  43  SER   A CA  
299  C C   . SER   A 37  ? 0.1742 0.1810 0.3077 -0.0142 -0.0039 0.0049  43  SER   A C   
300  O O   . SER   A 37  ? 0.1746 0.1789 0.3059 -0.0120 0.0028  0.0024  43  SER   A O   
301  C CB  . SER   A 37  ? 0.1612 0.1647 0.2825 -0.0135 -0.0270 0.0088  43  SER   A CB  
302  O OG  . SER   A 37  ? 0.1639 0.1677 0.2886 -0.0099 -0.0286 0.0101  43  SER   A OG  
303  N N   . SER   A 38  ? 0.1770 0.1899 0.3294 -0.0160 -0.0012 0.0079  44  SER   A N   
304  C CA  . SER   A 38  ? 0.1965 0.2134 0.3701 -0.0148 0.0113  0.0081  44  SER   A CA  
305  C C   . SER   A 38  ? 0.2287 0.2520 0.4273 -0.0097 0.0058  0.0146  44  SER   A C   
306  O O   . SER   A 38  ? 0.2432 0.2694 0.4439 -0.0098 -0.0088 0.0200  44  SER   A O   
307  C CB  . SER   A 38  ? 0.2019 0.2228 0.3857 -0.0196 0.0186  0.0085  44  SER   A CB  
308  O OG  . SER   A 38  ? 0.2309 0.2582 0.4267 -0.0205 0.0069  0.0147  44  SER   A OG  
309  N N   . THR   A 39  ? 0.2368 0.2613 0.4541 -0.0062 0.0172  0.0145  45  THR   A N   
310  C CA  . THR   A 39  ? 0.2529 0.2838 0.4977 -0.0012 0.0121  0.0224  45  THR   A CA  
311  C C   . THR   A 39  ? 0.2791 0.3168 0.5590 0.0006  0.0260  0.0251  45  THR   A C   
312  O O   . THR   A 39  ? 0.2889 0.3224 0.5661 -0.0015 0.0433  0.0179  45  THR   A O   
313  C CB  . THR   A 39  ? 0.2759 0.3003 0.5130 0.0030  0.0133  0.0207  45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.2915 0.3094 0.5283 0.0037  0.0321  0.0135  45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.2857 0.3031 0.4895 0.0015  0.0030  0.0172  45  THR   A CG2 
316  N N   . THR   A 40  ? 0.2865 0.3341 0.5995 0.0039  0.0190  0.0356  46  THR   A N   
317  C CA  . THR   A 40  ? 0.2964 0.3517 0.6499 0.0070  0.0326  0.0397  46  THR   A CA  
318  C C   . THR   A 40  ? 0.3233 0.3723 0.6889 0.0132  0.0459  0.0374  46  THR   A C   
319  O O   . THR   A 40  ? 0.3344 0.3807 0.7165 0.0149  0.0671  0.0325  46  THR   A O   
320  C CB  . THR   A 40  ? 0.2881 0.3582 0.6754 0.0070  0.0178  0.0540  46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.3003 0.3709 0.6850 0.0082  -0.0005 0.0619  46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.3000 0.3748 0.6768 -0.0001 0.0078  0.0552  46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.3281 0.3735 0.6850 0.0161  0.0345  0.0406  47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.3357 0.3742 0.7035 0.0218  0.0456  0.0391  47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.3607 0.3841 0.6925 0.0195  0.0590  0.0249  47  ALA   A C   
326  O O   . ALA   A 41  ? 0.3814 0.4004 0.6769 0.0145  0.0518  0.0193  47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.3370 0.3775 0.7087 0.0245  0.0273  0.0491  47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.3587 0.3734 0.7009 0.0226  0.0780  0.0196  48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.3824 0.3816 0.6897 0.0185  0.0905  0.0066  48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.3801 0.3732 0.6659 0.0199  0.0791  0.0070  48  GLN   A C   
331  O O   . GLN   A 42  ? 0.3821 0.3770 0.6889 0.0257  0.0737  0.0147  48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.4250 0.4145 0.7492 0.0197  0.1172  -0.0006 48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.5188 0.4941 0.8065 0.0106  0.1333  -0.0149 48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.6017 0.5816 0.8838 0.0040  0.1379  -0.0175 48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 0.6223 0.6144 0.9359 0.0071  0.1373  -0.0107 48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.6254 0.5961 0.8680 -0.0060 0.1422  -0.0266 48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.3732 0.3592 0.6190 0.0141  0.0762  -0.0007 49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.3691 0.3491 0.5907 0.0140  0.0673  -0.0017 49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.3626 0.3283 0.5725 0.0122  0.0834  -0.0103 49  GLY   A C   
340  O O   . GLY   A 43  ? 0.3735 0.3314 0.5766 0.0072  0.1005  -0.0188 49  GLY   A O   
341  N N   . CYS   A 44  ? 0.3460 0.3070 0.5510 0.0149  0.0782  -0.0085 50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.3464 0.2928 0.5424 0.0132  0.0929  -0.0159 50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.3313 0.2713 0.4932 0.0085  0.0865  -0.0197 50  CYS   A C   
344  O O   . CYS   A 44  ? 0.3304 0.2584 0.4865 0.0073  0.0960  -0.0242 50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.3735 0.3177 0.6038 0.0211  0.0981  -0.0101 50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.4860 0.4357 0.7621 0.0264  0.1121  -0.0066 50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.3109 0.2581 0.4517 0.0056  0.0716  -0.0181 51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.3141 0.2570 0.4252 0.0011  0.0659  -0.0209 51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.3100 0.2436 0.3974 -0.0086 0.0778  -0.0300 51  ASP   A C   
350  O O   . ASP   A 45  ? 0.3153 0.2492 0.4029 -0.0125 0.0852  -0.0332 51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.3384 0.2913 0.4377 0.0014  0.0483  -0.0163 51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.3908 0.3498 0.5020 0.0075  0.0350  -0.0082 51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.3920 0.3465 0.5094 0.0102  0.0357  -0.0059 51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.3973 0.3643 0.5093 0.0085  0.0235  -0.0040 51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.2974 0.2228 0.3637 -0.0137 0.0792  -0.0336 52  THR   A N   
356  C CA  . THR   A 46  ? 0.3094 0.2250 0.3497 -0.0253 0.0886  -0.0412 52  THR   A CA  
357  C C   . THR   A 46  ? 0.2955 0.2180 0.3135 -0.0305 0.0747  -0.0384 52  THR   A C   
358  O O   . THR   A 46  ? 0.2911 0.2181 0.3070 -0.0270 0.0642  -0.0344 52  THR   A O   
359  C CB  . THR   A 46  ? 0.3493 0.2498 0.3823 -0.0286 0.0996  -0.0464 52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.3775 0.2695 0.4317 -0.0251 0.1163  -0.0501 52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.3686 0.2588 0.3683 -0.0429 0.1044  -0.0527 52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.2799 0.2032 0.2825 -0.0392 0.0751  -0.0401 53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.2676 0.1976 0.2529 -0.0441 0.0622  -0.0361 53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.2831 0.2035 0.2433 -0.0563 0.0656  -0.0393 53  ILE   A C   
365  O O   . ILE   A 47  ? 0.2997 0.2077 0.2475 -0.0657 0.0785  -0.0457 53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.2653 0.2019 0.2489 -0.0474 0.0582  -0.0339 53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.2565 0.2008 0.2648 -0.0371 0.0566  -0.0314 53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.2773 0.2221 0.2497 -0.0504 0.0440  -0.0279 53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.2539 0.2073 0.2746 -0.0267 0.0436  -0.0258 53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.2635 0.1887 0.2158 -0.0569 0.0549  -0.0350 54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.2687 0.1866 0.1977 -0.0697 0.0556  -0.0362 54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.2751 0.1943 0.1864 -0.0826 0.0518  -0.0340 54  ALA   A C   
373  O O   . ALA   A 48  ? 0.2593 0.1896 0.1778 -0.0793 0.0425  -0.0283 54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.2516 0.1772 0.1813 -0.0664 0.0444  -0.0307 54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.2910 0.1976 0.1782 -0.0982 0.0588  -0.0382 55  ARG   A N   
376  C CA  . ARG   A 49  ? 0.3060 0.2128 0.1727 -0.1136 0.0533  -0.0344 55  ARG   A CA  
377  C C   . ARG   A 49  ? 0.3298 0.2328 0.1765 -0.1261 0.0477  -0.0318 55  ARG   A C   
378  O O   . ARG   A 49  ? 0.3476 0.2340 0.1727 -0.1388 0.0580  -0.0388 55  ARG   A O   
379  C CB  . ARG   A 49  ? 0.3303 0.2233 0.1826 -0.1240 0.0680  -0.0422 55  ARG   A CB  
380  C CG  . ARG   A 49  ? 0.3499 0.2464 0.2247 -0.1117 0.0755  -0.0450 55  ARG   A CG  
381  C CD  . ARG   A 49  ? 0.3699 0.2832 0.2595 -0.1043 0.0616  -0.0363 55  ARG   A CD  
382  N NE  . ARG   A 49  ? 0.3646 0.2805 0.2754 -0.0937 0.0689  -0.0392 55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.3615 0.2901 0.2906 -0.0838 0.0595  -0.0335 55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.3346 0.2737 0.2643 -0.0822 0.0439  -0.0253 55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.3236 0.2543 0.2719 -0.0756 0.0661  -0.0358 55  ARG   A NH2 
386  N N   . CYS   A 50  ? 0.3217 0.2394 0.1769 -0.1225 0.0323  -0.0220 56  CYS   A N   
387  C CA  . CYS   A 50  ? 0.3318 0.2496 0.1756 -0.1313 0.0254  -0.0179 56  CYS   A CA  
388  C C   . CYS   A 50  ? 0.3331 0.2700 0.1904 -0.1280 0.0084  -0.0051 56  CYS   A C   
389  O O   . CYS   A 50  ? 0.3147 0.2625 0.1895 -0.1179 0.0032  -0.0008 56  CYS   A O   
390  C CB  . CYS   A 50  ? 0.3263 0.2387 0.1782 -0.1217 0.0325  -0.0237 56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.3179 0.2460 0.2027 -0.0984 0.0266  -0.0199 56  CYS   A SG  
392  N N   . ASP   A 51  ? 0.3491 0.2898 0.2010 -0.1355 0.0006  0.0008  57  ASP   A N   
393  C CA  . ASP   A 51  ? 0.3549 0.3140 0.2246 -0.1308 -0.0135 0.0130  57  ASP   A CA  
394  C C   . ASP   A 51  ? 0.3430 0.3068 0.2245 -0.1218 -0.0136 0.0130  57  ASP   A C   
395  O O   . ASP   A 51  ? 0.3379 0.3141 0.2287 -0.1234 -0.0235 0.0227  57  ASP   A O   
396  C CB  . ASP   A 51  ? 0.4084 0.3732 0.2671 -0.1487 -0.0263 0.0248  57  ASP   A CB  
397  C CG  . ASP   A 51  ? 0.5227 0.4792 0.3580 -0.1669 -0.0279 0.0254  57  ASP   A CG  
398  O OD1 . ASP   A 51  ? 0.5423 0.4853 0.3665 -0.1668 -0.0167 0.0149  57  ASP   A OD1 
399  O OD2 . ASP   A 51  ? 0.5754 0.5387 0.4043 -0.1819 -0.0408 0.0373  57  ASP   A OD2 
400  N N   . CYS   A 52  ? 0.3274 0.2824 0.2116 -0.1117 -0.0028 0.0032  58  CYS   A N   
401  C CA  . CYS   A 52  ? 0.3055 0.2640 0.1998 -0.1032 -0.0025 0.0032  58  CYS   A CA  
402  C C   . CYS   A 52  ? 0.2827 0.2587 0.1993 -0.0925 -0.0110 0.0114  58  CYS   A C   
403  O O   . CYS   A 52  ? 0.2780 0.2604 0.2067 -0.0849 -0.0132 0.0132  58  CYS   A O   
404  C CB  . CYS   A 52  ? 0.3032 0.2514 0.2018 -0.0921 0.0084  -0.0063 58  CYS   A CB  
405  S SG  . CYS   A 52  ? 0.3349 0.2606 0.2122 -0.1027 0.0215  -0.0165 58  CYS   A SG  
406  N N   . GLN   A 53  ? 0.2574 0.2399 0.1793 -0.0924 -0.0144 0.0158  59  GLN   A N   
407  C CA  . GLN   A 53  ? 0.2382 0.2353 0.1817 -0.0818 -0.0189 0.0219  59  GLN   A CA  
408  C C   . GLN   A 53  ? 0.2160 0.2108 0.1636 -0.0728 -0.0134 0.0174  59  GLN   A C   
409  O O   . GLN   A 53  ? 0.2142 0.2194 0.1756 -0.0672 -0.0155 0.0220  59  GLN   A O   
410  C CB  . GLN   A 53  ? 0.2540 0.2649 0.2057 -0.0899 -0.0288 0.0340  59  GLN   A CB  
411  C CG  . GLN   A 53  ? 0.2825 0.3007 0.2410 -0.0931 -0.0363 0.0415  59  GLN   A CG  
412  C CD  . GLN   A 53  ? 0.3042 0.3385 0.2789 -0.0984 -0.0466 0.0556  59  GLN   A CD  
413  O OE1 . GLN   A 53  ? 0.2837 0.3198 0.2489 -0.1142 -0.0549 0.0635  59  GLN   A OE1 
414  N NE2 . GLN   A 53  ? 0.2826 0.3285 0.2822 -0.0862 -0.0457 0.0593  59  GLN   A NE2 
415  N N   . THR   A 54  ? 0.2062 0.1872 0.1427 -0.0721 -0.0061 0.0092  60  THR   A N   
416  C CA  . THR   A 54  ? 0.2170 0.1946 0.1571 -0.0640 -0.0018 0.0059  60  THR   A CA  
417  C C   . THR   A 54  ? 0.2076 0.1744 0.1472 -0.0568 0.0045  -0.0014 60  THR   A C   
418  O O   . THR   A 54  ? 0.2103 0.1684 0.1424 -0.0611 0.0085  -0.0056 60  THR   A O   
419  C CB  . THR   A 54  ? 0.2732 0.2447 0.2026 -0.0723 -0.0003 0.0058  60  THR   A CB  
420  O OG1 . THR   A 54  ? 0.3152 0.2712 0.2285 -0.0808 0.0052  -0.0002 60  THR   A OG1 
421  C CG2 . THR   A 54  ? 0.2840 0.2671 0.2152 -0.0811 -0.0073 0.0143  60  THR   A CG2 
422  N N   . GLY   A 55  ? 0.1979 0.1652 0.1455 -0.0469 0.0055  -0.0023 61  GLY   A N   
423  C CA  . GLY   A 55  ? 0.2006 0.1599 0.1519 -0.0398 0.0095  -0.0068 61  GLY   A CA  
424  C C   . GLY   A 55  ? 0.1977 0.1583 0.1554 -0.0316 0.0082  -0.0057 61  GLY   A C   
425  O O   . GLY   A 55  ? 0.1915 0.1566 0.1481 -0.0321 0.0064  -0.0028 61  GLY   A O   
426  N N   . VAL   A 56  ? 0.1895 0.1462 0.1537 -0.0251 0.0089  -0.0073 62  VAL   A N   
427  C CA  . VAL   A 56  ? 0.1859 0.1419 0.1541 -0.0190 0.0064  -0.0055 62  VAL   A CA  
428  C C   . VAL   A 56  ? 0.1758 0.1353 0.1509 -0.0135 0.0033  -0.0055 62  VAL   A C   
429  O O   . VAL   A 56  ? 0.1585 0.1161 0.1392 -0.0125 0.0048  -0.0073 62  VAL   A O   
430  C CB  . VAL   A 56  ? 0.2066 0.1519 0.1767 -0.0185 0.0094  -0.0058 62  VAL   A CB  
431  C CG1 . VAL   A 56  ? 0.2143 0.1587 0.1889 -0.0136 0.0048  -0.0021 62  VAL   A CG1 
432  C CG2 . VAL   A 56  ? 0.2192 0.1591 0.1808 -0.0249 0.0129  -0.0063 62  VAL   A CG2 
433  N N   . TYR   A 57  ? 0.1720 0.1353 0.1461 -0.0106 -0.0004 -0.0039 63  TYR   A N   
434  C CA  . TYR   A 57  ? 0.1658 0.1305 0.1443 -0.0067 -0.0038 -0.0041 63  TYR   A CA  
435  C C   . TYR   A 57  ? 0.1796 0.1400 0.1562 -0.0052 -0.0079 -0.0018 63  TYR   A C   
436  O O   . TYR   A 57  ? 0.1805 0.1386 0.1502 -0.0070 -0.0082 0.0000  63  TYR   A O   
437  C CB  . TYR   A 57  ? 0.1510 0.1221 0.1291 -0.0059 -0.0041 -0.0050 63  TYR   A CB  
438  C CG  . TYR   A 57  ? 0.1560 0.1284 0.1285 -0.0058 -0.0035 -0.0047 63  TYR   A CG  
439  C CD1 . TYR   A 57  ? 0.1671 0.1429 0.1374 -0.0083 -0.0005 -0.0034 63  TYR   A CD1 
440  C CD2 . TYR   A 57  ? 0.1660 0.1356 0.1348 -0.0041 -0.0049 -0.0059 63  TYR   A CD2 
441  C CE1 . TYR   A 57  ? 0.1831 0.1602 0.1498 -0.0082 0.0022  -0.0035 63  TYR   A CE1 
442  C CE2 . TYR   A 57  ? 0.1753 0.1443 0.1375 -0.0048 -0.0017 -0.0069 63  TYR   A CE2 
443  C CZ  . TYR   A 57  ? 0.1852 0.1581 0.1471 -0.0064 0.0025  -0.0057 63  TYR   A CZ  
444  O OH  . TYR   A 57  ? 0.2082 0.1803 0.1645 -0.0073 0.0075  -0.0070 63  TYR   A OH  
445  N N   . TYR   A 58  ? 0.1687 0.1283 0.1512 -0.0030 -0.0119 -0.0009 64  TYR   A N   
446  C CA  . TYR   A 58  ? 0.1792 0.1351 0.1590 -0.0035 -0.0180 0.0028  64  TYR   A CA  
447  C C   . TYR   A 58  ? 0.1811 0.1371 0.1498 -0.0049 -0.0198 0.0009  64  TYR   A C   
448  O O   . TYR   A 58  ? 0.1661 0.1245 0.1369 -0.0035 -0.0192 -0.0019 64  TYR   A O   
449  C CB  . TYR   A 58  ? 0.1799 0.1348 0.1732 -0.0016 -0.0225 0.0066  64  TYR   A CB  
450  C CG  . TYR   A 58  ? 0.1963 0.1479 0.1859 -0.0042 -0.0313 0.0124  64  TYR   A CG  
451  C CD1 . TYR   A 58  ? 0.2124 0.1597 0.1983 -0.0064 -0.0338 0.0172  64  TYR   A CD1 
452  C CD2 . TYR   A 58  ? 0.2211 0.1732 0.2097 -0.0057 -0.0378 0.0138  64  TYR   A CD2 
453  C CE1 . TYR   A 58  ? 0.2410 0.1848 0.2211 -0.0107 -0.0433 0.0239  64  TYR   A CE1 
454  C CE2 . TYR   A 58  ? 0.2425 0.1908 0.2243 -0.0105 -0.0473 0.0199  64  TYR   A CE2 
455  C CZ  . TYR   A 58  ? 0.2678 0.2121 0.2450 -0.0133 -0.0503 0.0253  64  TYR   A CZ  
456  O OH  . TYR   A 58  ? 0.3064 0.2467 0.2753 -0.0199 -0.0611 0.0327  64  TYR   A OH  
457  N N   . CYS   A 59  ? 0.1923 0.1442 0.1482 -0.0083 -0.0209 0.0022  65  CYS   A N   
458  C CA  . CYS   A 59  ? 0.2083 0.1572 0.1505 -0.0111 -0.0203 -0.0007 65  CYS   A CA  
459  C C   . CYS   A 59  ? 0.2192 0.1611 0.1516 -0.0163 -0.0290 0.0034  65  CYS   A C   
460  O O   . CYS   A 59  ? 0.2266 0.1642 0.1498 -0.0206 -0.0318 0.0073  65  CYS   A O   
461  C CB  . CYS   A 59  ? 0.2365 0.1856 0.1697 -0.0128 -0.0133 -0.0028 65  CYS   A CB  
462  S SG  . CYS   A 59  ? 0.2762 0.2182 0.1909 -0.0172 -0.0088 -0.0075 65  CYS   A SG  
463  N N   . SER   A 60  ? 0.2182 0.1587 0.1520 -0.0170 -0.0342 0.0034  66  SER   A N   
464  C CA  . SER   A 60  ? 0.2347 0.1692 0.1593 -0.0238 -0.0444 0.0089  66  SER   A CA  
465  C C   . SER   A 60  ? 0.2511 0.1762 0.1496 -0.0321 -0.0436 0.0071  66  SER   A C   
466  O O   . SER   A 60  ? 0.2710 0.1911 0.1596 -0.0393 -0.0522 0.0138  66  SER   A O   
467  C CB  . SER   A 60  ? 0.2729 0.2077 0.2032 -0.0246 -0.0509 0.0097  66  SER   A CB  
468  O OG  . SER   A 60  ? 0.3542 0.2859 0.2755 -0.0248 -0.0452 0.0019  66  SER   A OG  
469  N N   . SER   A 61  ? 0.2559 0.1783 0.1441 -0.0318 -0.0331 -0.0014 67  SER   A N   
470  C CA  . SER   A 61  ? 0.2754 0.1874 0.1381 -0.0400 -0.0285 -0.0051 67  SER   A CA  
471  C C   . SER   A 61  ? 0.2929 0.2041 0.1477 -0.0432 -0.0274 -0.0014 67  SER   A C   
472  O O   . SER   A 61  ? 0.3214 0.2232 0.1528 -0.0518 -0.0242 -0.0034 67  SER   A O   
473  C CB  . SER   A 61  ? 0.2781 0.1877 0.1373 -0.0374 -0.0151 -0.0148 67  SER   A CB  
474  O OG  . SER   A 61  ? 0.2772 0.1964 0.1520 -0.0297 -0.0064 -0.0163 67  SER   A OG  
475  N N   . ARG   A 62  ? 0.2760 0.1954 0.1482 -0.0377 -0.0295 0.0037  68  ARG   A N   
476  C CA  . ARG   A 62  ? 0.2814 0.1997 0.1481 -0.0408 -0.0297 0.0083  68  ARG   A CA  
477  C C   . ARG   A 62  ? 0.2848 0.2051 0.1651 -0.0398 -0.0407 0.0182  68  ARG   A C   
478  O O   . ARG   A 62  ? 0.2898 0.2083 0.1676 -0.0421 -0.0419 0.0231  68  ARG   A O   
479  C CB  . ARG   A 62  ? 0.2960 0.2212 0.1715 -0.0352 -0.0187 0.0042  68  ARG   A CB  
480  C CG  . ARG   A 62  ? 0.3273 0.2517 0.1946 -0.0355 -0.0065 -0.0038 68  ARG   A CG  
481  C CD  . ARG   A 62  ? 0.3558 0.2722 0.2008 -0.0441 -0.0021 -0.0044 68  ARG   A CD  
482  N NE  . ARG   A 62  ? 0.3805 0.2963 0.2216 -0.0436 0.0123  -0.0123 68  ARG   A NE  
483  C CZ  . ARG   A 62  ? 0.4101 0.3171 0.2384 -0.0470 0.0181  -0.0189 68  ARG   A CZ  
484  N NH1 . ARG   A 62  ? 0.3943 0.2925 0.2096 -0.0523 0.0092  -0.0183 68  ARG   A NH1 
485  N NH2 . ARG   A 62  ? 0.3960 0.3026 0.2255 -0.0453 0.0331  -0.0259 68  ARG   A NH2 
486  N N   . ARG   A 63  ? 0.2801 0.2039 0.1771 -0.0359 -0.0476 0.0213  69  ARG   A N   
487  C CA  . ARG   A 63  ? 0.2926 0.2192 0.2097 -0.0330 -0.0554 0.0303  69  ARG   A CA  
488  C C   . ARG   A 63  ? 0.2880 0.2172 0.2158 -0.0277 -0.0481 0.0296  69  ARG   A C   
489  O O   . ARG   A 63  ? 0.2955 0.2218 0.2276 -0.0291 -0.0521 0.0368  69  ARG   A O   
490  C CB  . ARG   A 63  ? 0.3225 0.2433 0.2318 -0.0416 -0.0687 0.0413  69  ARG   A CB  
491  C CG  . ARG   A 63  ? 0.3869 0.3050 0.2878 -0.0481 -0.0781 0.0434  69  ARG   A CG  
492  C CD  . ARG   A 63  ? 0.4507 0.3638 0.3447 -0.0583 -0.0936 0.0567  69  ARG   A CD  
493  N NE  . ARG   A 63  ? 0.5204 0.4283 0.3970 -0.0689 -0.1033 0.0587  69  ARG   A NE  
494  C CZ  . ARG   A 63  ? 0.5763 0.4741 0.4237 -0.0832 -0.1110 0.0629  69  ARG   A CZ  
495  N NH1 . ARG   A 63  ? 0.5808 0.4734 0.4138 -0.0879 -0.1094 0.0655  69  ARG   A NH1 
496  N NH2 . ARG   A 63  ? 0.5850 0.4767 0.4147 -0.0941 -0.1195 0.0640  69  ARG   A NH2 
497  N N   . LYS   A 64  ? 0.2684 0.2021 0.1981 -0.0232 -0.0378 0.0213  70  LYS   A N   
498  C CA  . LYS   A 64  ? 0.2673 0.2025 0.2029 -0.0205 -0.0310 0.0201  70  LYS   A CA  
499  C C   . LYS   A 64  ? 0.2450 0.1863 0.1926 -0.0150 -0.0240 0.0142  70  LYS   A C   
500  O O   . LYS   A 64  ? 0.2317 0.1768 0.1798 -0.0132 -0.0225 0.0099  70  LYS   A O   
501  C CB  . LYS   A 64  ? 0.3058 0.2400 0.2246 -0.0249 -0.0255 0.0175  70  LYS   A CB  
502  C CG  . LYS   A 64  ? 0.3955 0.3228 0.3023 -0.0313 -0.0303 0.0241  70  LYS   A CG  
503  C CD  . LYS   A 64  ? 0.4733 0.4005 0.3650 -0.0354 -0.0226 0.0206  70  LYS   A CD  
504  C CE  . LYS   A 64  ? 0.5567 0.4775 0.4374 -0.0420 -0.0260 0.0271  70  LYS   A CE  
505  N NZ  . LYS   A 64  ? 0.6205 0.5339 0.4807 -0.0506 -0.0318 0.0304  70  LYS   A NZ  
506  N N   . HIS   A 65  ? 0.2244 0.1654 0.1804 -0.0134 -0.0199 0.0143  71  HIS   A N   
507  C CA  . HIS   A 65  ? 0.2108 0.1560 0.1735 -0.0109 -0.0134 0.0091  71  HIS   A CA  
508  C C   . HIS   A 65  ? 0.2318 0.1796 0.1857 -0.0140 -0.0083 0.0069  71  HIS   A C   
509  O O   . HIS   A 65  ? 0.2581 0.2022 0.2060 -0.0170 -0.0082 0.0096  71  HIS   A O   
510  C CB  . HIS   A 65  ? 0.2213 0.1624 0.1970 -0.0090 -0.0109 0.0098  71  HIS   A CB  
511  C CG  . HIS   A 65  ? 0.2353 0.1754 0.2253 -0.0055 -0.0147 0.0129  71  HIS   A CG  
512  N ND1 . HIS   A 65  ? 0.2577 0.2011 0.2569 -0.0028 -0.0119 0.0094  71  HIS   A ND1 
513  C CD2 . HIS   A 65  ? 0.2361 0.1729 0.2341 -0.0049 -0.0213 0.0200  71  HIS   A CD2 
514  C CE1 . HIS   A 65  ? 0.2351 0.1775 0.2490 -0.0002 -0.0160 0.0142  71  HIS   A CE1 
515  N NE2 . HIS   A 65  ? 0.2533 0.1924 0.2676 -0.0013 -0.0225 0.0212  71  HIS   A NE2 
516  N N   . TYR   A 66  ? 0.2129 0.1673 0.1676 -0.0135 -0.0046 0.0032  72  TYR   A N   
517  C CA  . TYR   A 66  ? 0.2106 0.1698 0.1611 -0.0166 -0.0006 0.0027  72  TYR   A CA  
518  C C   . TYR   A 66  ? 0.2089 0.1716 0.1645 -0.0183 0.0019  0.0013  72  TYR   A C   
519  O O   . TYR   A 66  ? 0.2003 0.1659 0.1614 -0.0165 0.0016  -0.0005 72  TYR   A O   
520  C CB  . TYR   A 66  ? 0.2162 0.1813 0.1647 -0.0156 0.0014  0.0011  72  TYR   A CB  
521  C CG  . TYR   A 66  ? 0.2474 0.2078 0.1853 -0.0168 0.0007  0.0015  72  TYR   A CG  
522  C CD1 . TYR   A 66  ? 0.2808 0.2391 0.2100 -0.0209 0.0028  0.0034  72  TYR   A CD1 
523  C CD2 . TYR   A 66  ? 0.2710 0.2280 0.2053 -0.0155 -0.0018 -0.0001 72  TYR   A CD2 
524  C CE1 . TYR   A 66  ? 0.3031 0.2555 0.2188 -0.0240 0.0025  0.0038  72  TYR   A CE1 
525  C CE2 . TYR   A 66  ? 0.2974 0.2481 0.2177 -0.0191 -0.0025 0.0001  72  TYR   A CE2 
526  C CZ  . TYR   A 66  ? 0.3216 0.2697 0.2318 -0.0236 -0.0001 0.0020  72  TYR   A CZ  
527  O OH  . TYR   A 66  ? 0.3652 0.3057 0.2580 -0.0292 -0.0006 0.0022  72  TYR   A OH  
528  N N   . PRO   A 67  ? 0.2061 0.1686 0.1584 -0.0232 0.0040  0.0024  73  PRO   A N   
529  C CA  . PRO   A 67  ? 0.2090 0.1744 0.1624 -0.0277 0.0054  0.0017  73  PRO   A CA  
530  C C   . PRO   A 67  ? 0.2181 0.1959 0.1764 -0.0284 0.0049  0.0038  73  PRO   A C   
531  O O   . PRO   A 67  ? 0.2374 0.2201 0.1966 -0.0276 0.0061  0.0056  73  PRO   A O   
532  C CB  . PRO   A 67  ? 0.2176 0.1770 0.1644 -0.0336 0.0072  0.0027  73  PRO   A CB  
533  C CG  . PRO   A 67  ? 0.2166 0.1768 0.1606 -0.0325 0.0068  0.0053  73  PRO   A CG  
534  C CD  . PRO   A 67  ? 0.2023 0.1611 0.1480 -0.0262 0.0046  0.0048  73  PRO   A CD  
535  N N   . VAL   A 68  ? 0.2047 0.1872 0.1674 -0.0298 0.0035  0.0040  74  VAL   A N   
536  C CA  . VAL   A 68  ? 0.2027 0.1970 0.1744 -0.0300 0.0021  0.0077  74  VAL   A CA  
537  C C   . VAL   A 68  ? 0.1858 0.1844 0.1581 -0.0375 -0.0010 0.0108  74  VAL   A C   
538  O O   . VAL   A 68  ? 0.1864 0.1775 0.1510 -0.0414 -0.0011 0.0081  74  VAL   A O   
539  C CB  . VAL   A 68  ? 0.2107 0.2073 0.1897 -0.0228 0.0019  0.0061  74  VAL   A CB  
540  C CG1 . VAL   A 68  ? 0.2195 0.2143 0.1977 -0.0175 0.0049  0.0042  74  VAL   A CG1 
541  C CG2 . VAL   A 68  ? 0.2172 0.2070 0.1934 -0.0214 0.0006  0.0027  74  VAL   A CG2 
542  N N   . SER   A 69  ? 0.1801 0.1907 0.1626 -0.0400 -0.0034 0.0171  75  SER   A N   
543  C CA  . SER   A 69  ? 0.1789 0.1959 0.1644 -0.0477 -0.0089 0.0227  75  SER   A CA  
544  C C   . SER   A 69  ? 0.1528 0.1761 0.1519 -0.0409 -0.0102 0.0245  75  SER   A C   
545  O O   . SER   A 69  ? 0.1593 0.1863 0.1690 -0.0327 -0.0067 0.0239  75  SER   A O   
546  C CB  . SER   A 69  ? 0.2157 0.2440 0.2093 -0.0543 -0.0121 0.0309  75  SER   A CB  
547  O OG  . SER   A 69  ? 0.3094 0.3310 0.2898 -0.0612 -0.0109 0.0292  75  SER   A OG  
548  N N   . PHE   A 70  ? 0.1386 0.1609 0.1356 -0.0444 -0.0141 0.0255  76  PHE   A N   
549  C CA  . PHE   A 70  ? 0.1461 0.1729 0.1556 -0.0383 -0.0156 0.0273  76  PHE   A CA  
550  C C   . PHE   A 70  ? 0.1683 0.2027 0.1837 -0.0463 -0.0233 0.0362  76  PHE   A C   
551  O O   . PHE   A 70  ? 0.1827 0.2145 0.1850 -0.0578 -0.0272 0.0382  76  PHE   A O   
552  C CB  . PHE   A 70  ? 0.1472 0.1636 0.1489 -0.0327 -0.0125 0.0192  76  PHE   A CB  
553  C CG  . PHE   A 70  ? 0.1568 0.1634 0.1426 -0.0392 -0.0120 0.0150  76  PHE   A CG  
554  C CD1 . PHE   A 70  ? 0.1688 0.1660 0.1438 -0.0398 -0.0074 0.0093  76  PHE   A CD1 
555  C CD2 . PHE   A 70  ? 0.1707 0.1766 0.1532 -0.0450 -0.0151 0.0167  76  PHE   A CD2 
556  C CE1 . PHE   A 70  ? 0.1894 0.1762 0.1527 -0.0449 -0.0043 0.0046  76  PHE   A CE1 
557  C CE2 . PHE   A 70  ? 0.1916 0.1873 0.1595 -0.0511 -0.0119 0.0116  76  PHE   A CE2 
558  C CZ  . PHE   A 70  ? 0.1935 0.1794 0.1525 -0.0510 -0.0058 0.0053  76  PHE   A CZ  
559  N N   . SER   A 71  ? 0.1582 0.2011 0.1930 -0.0409 -0.0255 0.0419  77  SER   A N   
560  C CA  . SER   A 71  ? 0.1554 0.2065 0.1986 -0.0484 -0.0343 0.0526  77  SER   A CA  
561  C C   . SER   A 71  ? 0.1666 0.2092 0.1948 -0.0536 -0.0371 0.0498  77  SER   A C   
562  O O   . SER   A 71  ? 0.1685 0.2014 0.1876 -0.0479 -0.0314 0.0403  77  SER   A O   
563  C CB  . SER   A 71  ? 0.1699 0.2315 0.2415 -0.0402 -0.0348 0.0599  77  SER   A CB  
564  O OG  . SER   A 71  ? 0.2051 0.2597 0.2790 -0.0296 -0.0291 0.0525  77  SER   A OG  
565  N N   . LYS   A 72  ? 0.1668 0.2136 0.1926 -0.0654 -0.0460 0.0590  78  LYS   A N   
566  C CA  . LYS   A 72  ? 0.1836 0.2225 0.1945 -0.0718 -0.0480 0.0570  78  LYS   A CA  
567  C C   . LYS   A 72  ? 0.1958 0.2358 0.2220 -0.0610 -0.0472 0.0569  78  LYS   A C   
568  O O   . LYS   A 72  ? 0.1988 0.2473 0.2482 -0.0525 -0.0479 0.0622  78  LYS   A O   
569  C CB  . LYS   A 72  ? 0.2073 0.2505 0.2110 -0.0890 -0.0591 0.0686  78  LYS   A CB  
570  C CG  . LYS   A 72  ? 0.2560 0.2937 0.2376 -0.1027 -0.0592 0.0668  78  LYS   A CG  
571  C CD  . LYS   A 72  ? 0.3334 0.3736 0.3032 -0.1225 -0.0709 0.0782  78  LYS   A CD  
572  C CE  . LYS   A 72  ? 0.4197 0.4477 0.3596 -0.1369 -0.0677 0.0717  78  LYS   A CE  
573  N NZ  . LYS   A 72  ? 0.4662 0.4927 0.3868 -0.1595 -0.0784 0.0811  78  LYS   A NZ  
574  N N   . PRO   A 73  ? 0.2014 0.2325 0.2157 -0.0614 -0.0447 0.0507  79  PRO   A N   
575  C CA  . PRO   A 73  ? 0.2074 0.2384 0.2349 -0.0518 -0.0440 0.0501  79  PRO   A CA  
576  C C   . PRO   A 73  ? 0.2072 0.2479 0.2547 -0.0529 -0.0527 0.0635  79  PRO   A C   
577  O O   . PRO   A 73  ? 0.2024 0.2474 0.2462 -0.0655 -0.0617 0.0736  79  PRO   A O   
578  C CB  . PRO   A 73  ? 0.2315 0.2527 0.2415 -0.0565 -0.0416 0.0438  79  PRO   A CB  
579  C CG  . PRO   A 73  ? 0.2477 0.2619 0.2363 -0.0658 -0.0378 0.0383  79  PRO   A CG  
580  C CD  . PRO   A 73  ? 0.2192 0.2389 0.2083 -0.0704 -0.0408 0.0431  79  PRO   A CD  
581  N N   . SER   A 74  ? 0.1989 0.2426 0.2681 -0.0406 -0.0501 0.0640  80  SER   A N   
582  C CA  . SER   A 74  ? 0.2056 0.2583 0.2997 -0.0396 -0.0569 0.0772  80  SER   A CA  
583  C C   . SER   A 74  ? 0.2014 0.2505 0.3129 -0.0262 -0.0511 0.0735  80  SER   A C   
584  O O   . SER   A 74  ? 0.2039 0.2437 0.3053 -0.0194 -0.0431 0.0612  80  SER   A O   
585  C CB  . SER   A 74  ? 0.2334 0.2984 0.3445 -0.0415 -0.0603 0.0871  80  SER   A CB  
586  O OG  . SER   A 74  ? 0.2806 0.3460 0.4027 -0.0300 -0.0504 0.0805  80  SER   A OG  
587  N N   . LEU   A 75  ? 0.1836 0.2390 0.3204 -0.0239 -0.0558 0.0850  81  LEU   A N   
588  C CA  . LEU   A 75  ? 0.1922 0.2426 0.3471 -0.0123 -0.0499 0.0825  81  LEU   A CA  
589  C C   . LEU   A 75  ? 0.1907 0.2439 0.3644 -0.0024 -0.0405 0.0802  81  LEU   A C   
590  O O   . LEU   A 75  ? 0.1793 0.2443 0.3759 -0.0030 -0.0436 0.0918  81  LEU   A O   
591  C CB  . LEU   A 75  ? 0.1960 0.2524 0.3740 -0.0147 -0.0593 0.0981  81  LEU   A CB  
592  C CG  . LEU   A 75  ? 0.2518 0.3016 0.4210 -0.0189 -0.0647 0.0994  81  LEU   A CG  
593  C CD1 . LEU   A 75  ? 0.2533 0.3108 0.4500 -0.0212 -0.0748 0.1176  81  LEU   A CD1 
594  C CD2 . LEU   A 75  ? 0.2755 0.3123 0.4393 -0.0093 -0.0550 0.0858  81  LEU   A CD2 
595  N N   . ILE   A 76  ? 0.1889 0.2316 0.3543 0.0060  -0.0292 0.0664  82  ILE   A N   
596  C CA  . ILE   A 76  ? 0.2001 0.2425 0.3775 0.0142  -0.0180 0.0617  82  ILE   A CA  
597  C C   . ILE   A 76  ? 0.2148 0.2450 0.3999 0.0236  -0.0078 0.0540  82  ILE   A C   
598  O O   . ILE   A 76  ? 0.2155 0.2343 0.3827 0.0237  -0.0073 0.0454  82  ILE   A O   
599  C CB  . ILE   A 76  ? 0.2290 0.2680 0.3807 0.0120  -0.0139 0.0512  82  ILE   A CB  
600  C CG1 . ILE   A 76  ? 0.2442 0.2939 0.3900 0.0024  -0.0223 0.0587  82  ILE   A CG1 
601  C CG2 . ILE   A 76  ? 0.2335 0.2676 0.3883 0.0195  -0.0007 0.0428  82  ILE   A CG2 
602  C CD1 . ILE   A 76  ? 0.2941 0.3394 0.4156 -0.0008 -0.0199 0.0500  82  ILE   A CD1 
603  N N   . PHE   A 77  ? 0.2157 0.2479 0.4281 0.0310  0.0010  0.0570  83  PHE   A N   
604  C CA  . PHE   A 77  ? 0.2456 0.2636 0.4644 0.0392  0.0132  0.0484  83  PHE   A CA  
605  C C   . PHE   A 77  ? 0.2527 0.2571 0.4424 0.0400  0.0231  0.0317  83  PHE   A C   
606  O O   . PHE   A 77  ? 0.2534 0.2612 0.4345 0.0388  0.0273  0.0282  83  PHE   A O   
607  C CB  . PHE   A 77  ? 0.2579 0.2804 0.5150 0.0470  0.0228  0.0553  83  PHE   A CB  
608  C CG  . PHE   A 77  ? 0.2974 0.3030 0.5631 0.0549  0.0365  0.0468  83  PHE   A CG  
609  C CD1 . PHE   A 77  ? 0.3229 0.3224 0.5996 0.0566  0.0323  0.0511  83  PHE   A CD1 
610  C CD2 . PHE   A 77  ? 0.3265 0.3210 0.5878 0.0595  0.0543  0.0344  83  PHE   A CD2 
611  C CE1 . PHE   A 77  ? 0.3397 0.3218 0.6244 0.0633  0.0458  0.0430  83  PHE   A CE1 
612  C CE2 . PHE   A 77  ? 0.3441 0.3203 0.6107 0.0653  0.0683  0.0256  83  PHE   A CE2 
613  C CZ  . PHE   A 77  ? 0.3421 0.3119 0.6204 0.0673  0.0641  0.0297  83  PHE   A CZ  
614  N N   . VAL   A 78  ? 0.2498 0.2390 0.4243 0.0408  0.0257  0.0224  84  VAL   A N   
615  C CA  . VAL   A 78  ? 0.2582 0.2336 0.4045 0.0396  0.0326  0.0083  84  VAL   A CA  
616  C C   . VAL   A 78  ? 0.2867 0.2449 0.4357 0.0441  0.0449  -0.0001 84  VAL   A C   
617  O O   . VAL   A 78  ? 0.2963 0.2483 0.4529 0.0454  0.0424  0.0016  84  VAL   A O   
618  C CB  . VAL   A 78  ? 0.2521 0.2253 0.3721 0.0334  0.0216  0.0051  84  VAL   A CB  
619  C CG1 . VAL   A 78  ? 0.2659 0.2245 0.3592 0.0315  0.0267  -0.0075 84  VAL   A CG1 
620  C CG2 . VAL   A 78  ? 0.2390 0.2260 0.3536 0.0285  0.0124  0.0113  84  VAL   A CG2 
621  N N   . GLU   A 79  ? 0.3019 0.2507 0.4429 0.0454  0.0588  -0.0095 85  GLU   A N   
622  C CA  . GLU   A 79  ? 0.3193 0.2480 0.4578 0.0479  0.0735  -0.0199 85  GLU   A CA  
623  C C   . GLU   A 79  ? 0.3336 0.2467 0.4479 0.0434  0.0687  -0.0274 85  GLU   A C   
624  O O   . GLU   A 79  ? 0.3383 0.2541 0.4304 0.0376  0.0570  -0.0281 85  GLU   A O   
625  C CB  . GLU   A 79  ? 0.3636 0.2834 0.4858 0.0462  0.0878  -0.0302 85  GLU   A CB  
626  C CG  . GLU   A 79  ? 0.4344 0.3662 0.5823 0.0511  0.0974  -0.0248 85  GLU   A CG  
627  C CD  . GLU   A 79  ? 0.5544 0.4880 0.7428 0.0596  0.1068  -0.0186 85  GLU   A CD  
628  O OE1 . GLU   A 79  ? 0.5849 0.4999 0.7748 0.0621  0.1184  -0.0263 85  GLU   A OE1 
629  O OE2 . GLU   A 79  ? 0.5804 0.5335 0.7998 0.0633  0.1023  -0.0053 85  GLU   A OE2 
630  N N   . ALA   A 80  ? 0.3381 0.2340 0.4575 0.0458  0.0786  -0.0331 86  ALA   A N   
631  C CA  . ALA   A 80  ? 0.3550 0.2343 0.4510 0.0404  0.0749  -0.0407 86  ALA   A CA  
632  C C   . ALA   A 80  ? 0.3819 0.2510 0.4402 0.0320  0.0751  -0.0511 86  ALA   A C   
633  O O   . ALA   A 80  ? 0.3908 0.2574 0.4403 0.0309  0.0848  -0.0562 86  ALA   A O   
634  C CB  . ALA   A 80  ? 0.3570 0.2165 0.4635 0.0438  0.0886  -0.0467 86  ALA   A CB  
635  N N   . SER   A 81  ? 0.3925 0.2568 0.4301 0.0255  0.0636  -0.0530 87  SER   A N   
636  C CA  . SER   A 81  ? 0.4150 0.2696 0.4181 0.0160  0.0600  -0.0604 87  SER   A CA  
637  C C   . SER   A 81  ? 0.4455 0.2848 0.4348 0.0103  0.0554  -0.0648 87  SER   A C   
638  O O   . SER   A 81  ? 0.4486 0.2849 0.4554 0.0144  0.0563  -0.0626 87  SER   A O   
639  C CB  . SER   A 81  ? 0.4073 0.2801 0.4051 0.0139  0.0458  -0.0534 87  SER   A CB  
640  O OG  . SER   A 81  ? 0.4043 0.2880 0.4131 0.0150  0.0330  -0.0458 87  SER   A OG  
641  N N   . GLU   A 82  ? 0.4663 0.2964 0.4256 0.0002  0.0491  -0.0698 88  GLU   A N   
642  C CA  . GLU   A 82  ? 0.4822 0.2998 0.4287 -0.0067 0.0423  -0.0725 88  GLU   A CA  
643  C C   . GLU   A 82  ? 0.4533 0.2871 0.4155 -0.0044 0.0273  -0.0627 88  GLU   A C   
644  O O   . GLU   A 82  ? 0.4629 0.2888 0.4213 -0.0086 0.0220  -0.0634 88  GLU   A O   
645  C CB  . GLU   A 82  ? 0.5732 0.3780 0.4845 -0.0198 0.0376  -0.0784 88  GLU   A CB  
646  C CG  . GLU   A 82  ? 0.6988 0.4896 0.5890 -0.0245 0.0508  -0.0872 88  GLU   A CG  
647  C CD  . GLU   A 82  ? 0.8402 0.6450 0.7238 -0.0257 0.0453  -0.0827 88  GLU   A CD  
648  O OE1 . GLU   A 82  ? 0.8436 0.6703 0.7464 -0.0192 0.0353  -0.0731 88  GLU   A OE1 
649  O OE2 . GLU   A 82  ? 0.9026 0.6950 0.7605 -0.0339 0.0515  -0.0890 88  GLU   A OE2 
650  N N   . TYR   A 83  ? 0.4190 0.2743 0.3968 0.0009  0.0209  -0.0541 89  TYR   A N   
651  C CA  . TYR   A 83  ? 0.3875 0.2573 0.3779 0.0020  0.0086  -0.0456 89  TYR   A CA  
652  C C   . TYR   A 83  ? 0.3581 0.2355 0.3750 0.0094  0.0104  -0.0391 89  TYR   A C   
653  O O   . TYR   A 83  ? 0.3609 0.2433 0.3859 0.0088  0.0026  -0.0339 89  TYR   A O   
654  C CB  . TYR   A 83  ? 0.3730 0.2595 0.3615 0.0013  0.0005  -0.0404 89  TYR   A CB  
655  C CG  . TYR   A 83  ? 0.3877 0.2685 0.3533 -0.0055 -0.0017 -0.0445 89  TYR   A CG  
656  C CD1 . TYR   A 83  ? 0.4104 0.2873 0.3629 -0.0133 -0.0114 -0.0443 89  TYR   A CD1 
657  C CD2 . TYR   A 83  ? 0.3990 0.2789 0.3569 -0.0049 0.0051  -0.0472 89  TYR   A CD2 
658  C CE1 . TYR   A 83  ? 0.4332 0.3056 0.3658 -0.0207 -0.0155 -0.0458 89  TYR   A CE1 
659  C CE2 . TYR   A 83  ? 0.4270 0.3017 0.3632 -0.0122 0.0020  -0.0496 89  TYR   A CE2 
660  C CZ  . TYR   A 83  ? 0.4576 0.3285 0.3812 -0.0203 -0.0089 -0.0484 89  TYR   A CZ  
661  O OH  . TYR   A 83  ? 0.5083 0.3746 0.4113 -0.0284 -0.0136 -0.0487 89  TYR   A OH  
662  N N   . TYR   A 84  ? 0.3323 0.2116 0.3637 0.0159  0.0200  -0.0383 90  TYR   A N   
663  C CA  . TYR   A 84  ? 0.3154 0.2034 0.3741 0.0222  0.0199  -0.0297 90  TYR   A CA  
664  C C   . TYR   A 84  ? 0.3324 0.2122 0.4072 0.0284  0.0340  -0.0319 90  TYR   A C   
665  O O   . TYR   A 84  ? 0.3352 0.2110 0.4036 0.0292  0.0438  -0.0376 90  TYR   A O   
666  C CB  . TYR   A 84  ? 0.2864 0.1959 0.3559 0.0239  0.0130  -0.0203 90  TYR   A CB  
667  C CG  . TYR   A 84  ? 0.2636 0.1829 0.3207 0.0188  0.0020  -0.0179 90  TYR   A CG  
668  C CD1 . TYR   A 84  ? 0.2637 0.1891 0.3088 0.0170  0.0010  -0.0197 90  TYR   A CD1 
669  C CD2 . TYR   A 84  ? 0.2488 0.1721 0.3090 0.0160  -0.0066 -0.0131 90  TYR   A CD2 
670  C CE1 . TYR   A 84  ? 0.2504 0.1841 0.2879 0.0131  -0.0074 -0.0175 90  TYR   A CE1 
671  C CE2 . TYR   A 84  ? 0.2466 0.1789 0.2986 0.0118  -0.0142 -0.0112 90  TYR   A CE2 
672  C CZ  . TYR   A 84  ? 0.2469 0.1844 0.2889 0.0108  -0.0143 -0.0133 90  TYR   A CZ  
673  O OH  . TYR   A 84  ? 0.2254 0.1703 0.2620 0.0073  -0.0201 -0.0117 90  TYR   A OH  
674  N N   . PRO   A 85  ? 0.3387 0.2177 0.4378 0.0332  0.0353  -0.0257 91  PRO   A N   
675  C CA  . PRO   A 85  ? 0.3416 0.2171 0.4651 0.0408  0.0487  -0.0247 91  PRO   A CA  
676  C C   . PRO   A 85  ? 0.3402 0.2373 0.4815 0.0444  0.0460  -0.0149 91  PRO   A C   
677  O O   . PRO   A 85  ? 0.3436 0.2558 0.4769 0.0407  0.0340  -0.0095 91  PRO   A O   
678  C CB  . PRO   A 85  ? 0.3486 0.2193 0.4948 0.0441  0.0471  -0.0181 91  PRO   A CB  
679  C CG  . PRO   A 85  ? 0.3477 0.2307 0.4883 0.0390  0.0296  -0.0100 91  PRO   A CG  
680  C CD  . PRO   A 85  ? 0.3309 0.2148 0.4396 0.0320  0.0240  -0.0173 91  PRO   A CD  
681  N N   . ALA   A 86  ? 0.3267 0.2251 0.4931 0.0513  0.0577  -0.0124 92  ALA   A N   
682  C CA  . ALA   A 86  ? 0.3119 0.2310 0.4976 0.0540  0.0548  -0.0020 92  ALA   A CA  
683  C C   . ALA   A 86  ? 0.2875 0.2233 0.4895 0.0525  0.0381  0.0136  92  ALA   A C   
684  O O   . ALA   A 86  ? 0.2735 0.2053 0.4921 0.0544  0.0354  0.0195  92  ALA   A O   
685  C CB  . ALA   A 86  ? 0.3117 0.2288 0.5275 0.0620  0.0708  -0.0008 92  ALA   A CB  
686  N N   . ARG   A 87  ? 0.2695 0.2213 0.4617 0.0474  0.0269  0.0191  93  ARG   A N   
687  C CA  . ARG   A 87  ? 0.2500 0.2157 0.4519 0.0435  0.0119  0.0329  93  ARG   A CA  
688  C C   . ARG   A 87  ? 0.2306 0.2135 0.4288 0.0389  0.0045  0.0394  93  ARG   A C   
689  O O   . ARG   A 87  ? 0.2312 0.2157 0.4212 0.0397  0.0109  0.0335  93  ARG   A O   
690  C CB  . ARG   A 87  ? 0.2736 0.2331 0.4582 0.0380  0.0025  0.0316  93  ARG   A CB  
691  C CG  . ARG   A 87  ? 0.3292 0.2790 0.4811 0.0335  0.0020  0.0191  93  ARG   A CG  
692  C CD  . ARG   A 87  ? 0.2940 0.2486 0.4254 0.0307  0.0023  0.0131  93  ARG   A CD  
693  N NE  . ARG   A 87  ? 0.2754 0.2327 0.3849 0.0242  -0.0059 0.0106  93  ARG   A NE  
694  C CZ  . ARG   A 87  ? 0.2585 0.2169 0.3502 0.0222  -0.0049 0.0045  93  ARG   A CZ  
695  N NH1 . ARG   A 87  ? 0.2127 0.1747 0.2903 0.0172  -0.0114 0.0038  93  ARG   A NH1 
696  N NH2 . ARG   A 87  ? 0.2571 0.2126 0.3462 0.0250  0.0032  -0.0007 93  ARG   A NH2 
697  N N   . TYR   A 88  ? 0.2161 0.2109 0.4196 0.0331  -0.0088 0.0518  94  TYR   A N   
698  C CA  . TYR   A 88  ? 0.2100 0.2181 0.4037 0.0262  -0.0164 0.0567  94  TYR   A CA  
699  C C   . TYR   A 88  ? 0.1908 0.1946 0.3529 0.0197  -0.0210 0.0489  94  TYR   A C   
700  O O   . TYR   A 88  ? 0.1917 0.1910 0.3478 0.0166  -0.0261 0.0496  94  TYR   A O   
701  C CB  . TYR   A 88  ? 0.2222 0.2439 0.4344 0.0207  -0.0285 0.0743  94  TYR   A CB  
702  C CG  . TYR   A 88  ? 0.2388 0.2686 0.4875 0.0267  -0.0253 0.0848  94  TYR   A CG  
703  C CD1 . TYR   A 88  ? 0.2573 0.2984 0.5145 0.0266  -0.0234 0.0883  94  TYR   A CD1 
704  C CD2 . TYR   A 88  ? 0.2550 0.2801 0.5317 0.0335  -0.0223 0.0904  94  TYR   A CD2 
705  C CE1 . TYR   A 88  ? 0.2694 0.3194 0.5644 0.0326  -0.0196 0.0987  94  TYR   A CE1 
706  C CE2 . TYR   A 88  ? 0.2631 0.2960 0.5785 0.0401  -0.0180 0.1009  94  TYR   A CE2 
707  C CZ  . TYR   A 88  ? 0.2822 0.3281 0.6075 0.0398  -0.0164 0.1050  94  TYR   A CZ  
708  O OH  . TYR   A 88  ? 0.3119 0.3671 0.6797 0.0464  -0.0117 0.1164  94  TYR   A OH  
709  N N   . GLN   A 89  ? 0.1716 0.1766 0.3152 0.0178  -0.0184 0.0417  95  GLN   A N   
710  C CA  . GLN   A 89  ? 0.1605 0.1628 0.2785 0.0120  -0.0220 0.0354  95  GLN   A CA  
711  C C   . GLN   A 89  ? 0.1560 0.1690 0.2695 0.0033  -0.0300 0.0436  95  GLN   A C   
712  O O   . GLN   A 89  ? 0.1508 0.1720 0.2709 0.0024  -0.0301 0.0482  95  GLN   A O   
713  C CB  . GLN   A 89  ? 0.1768 0.1727 0.2780 0.0145  -0.0149 0.0237  95  GLN   A CB  
714  C CG  . GLN   A 89  ? 0.1850 0.1799 0.2647 0.0091  -0.0184 0.0189  95  GLN   A CG  
715  C CD  . GLN   A 89  ? 0.1831 0.1693 0.2484 0.0115  -0.0135 0.0086  95  GLN   A CD  
716  O OE1 . GLN   A 89  ? 0.1838 0.1610 0.2490 0.0152  -0.0091 0.0034  95  GLN   A OE1 
717  N NE2 . GLN   A 89  ? 0.1579 0.1458 0.2103 0.0084  -0.0145 0.0060  95  GLN   A NE2 
718  N N   . SER   A 90  ? 0.1505 0.1631 0.2530 -0.0039 -0.0364 0.0458  96  SER   A N   
719  C CA  . SER   A 90  ? 0.1537 0.1734 0.2474 -0.0145 -0.0431 0.0525  96  SER   A CA  
720  C C   . SER   A 90  ? 0.1635 0.1802 0.2351 -0.0180 -0.0394 0.0434  96  SER   A C   
721  O O   . SER   A 90  ? 0.1595 0.1693 0.2235 -0.0126 -0.0335 0.0332  96  SER   A O   
722  C CB  . SER   A 90  ? 0.1784 0.1978 0.2700 -0.0222 -0.0506 0.0596  96  SER   A CB  
723  O OG  . SER   A 90  ? 0.2128 0.2236 0.2928 -0.0210 -0.0472 0.0509  96  SER   A OG  
724  N N   . HIS   A 91  ? 0.1663 0.1878 0.2287 -0.0274 -0.0431 0.0478  97  HIS   A N   
725  C CA  . HIS   A 91  ? 0.1771 0.1949 0.2195 -0.0324 -0.0395 0.0406  97  HIS   A CA  
726  C C   . HIS   A 91  ? 0.1738 0.1897 0.2158 -0.0244 -0.0327 0.0328  97  HIS   A C   
727  O O   . HIS   A 91  ? 0.1816 0.1916 0.2113 -0.0239 -0.0280 0.0246  97  HIS   A O   
728  C CB  . HIS   A 91  ? 0.1900 0.2003 0.2193 -0.0354 -0.0371 0.0345  97  HIS   A CB  
729  C CG  . HIS   A 91  ? 0.2175 0.2285 0.2428 -0.0454 -0.0430 0.0418  97  HIS   A CG  
730  N ND1 . HIS   A 91  ? 0.2440 0.2536 0.2518 -0.0587 -0.0443 0.0436  97  HIS   A ND1 
731  C CD2 . HIS   A 91  ? 0.2162 0.2282 0.2518 -0.0449 -0.0480 0.0481  97  HIS   A CD2 
732  C CE1 . HIS   A 91  ? 0.2452 0.2555 0.2518 -0.0666 -0.0505 0.0513  97  HIS   A CE1 
733  N NE2 . HIS   A 91  ? 0.2246 0.2368 0.2488 -0.0584 -0.0533 0.0547  97  HIS   A NE2 
734  N N   . LEU   A 92  ? 0.1577 0.1786 0.2146 -0.0184 -0.0318 0.0359  98  LEU   A N   
735  C CA  . LEU   A 92  ? 0.1550 0.1737 0.2112 -0.0117 -0.0252 0.0292  98  LEU   A CA  
736  C C   . LEU   A 92  ? 0.1456 0.1706 0.2006 -0.0161 -0.0257 0.0327  98  LEU   A C   
737  O O   . LEU   A 92  ? 0.1403 0.1742 0.2061 -0.0207 -0.0310 0.0426  98  LEU   A O   
738  C CB  . LEU   A 92  ? 0.1455 0.1638 0.2186 -0.0026 -0.0213 0.0291  98  LEU   A CB  
739  C CG  . LEU   A 92  ? 0.1603 0.1733 0.2298 0.0038  -0.0133 0.0210  98  LEU   A CG  
740  C CD1 . LEU   A 92  ? 0.1720 0.1759 0.2244 0.0042  -0.0119 0.0122  98  LEU   A CD1 
741  C CD2 . LEU   A 92  ? 0.1747 0.1854 0.2607 0.0113  -0.0074 0.0207  98  LEU   A CD2 
742  N N   . MET   A 93  ? 0.1430 0.1636 0.1857 -0.0153 -0.0211 0.0256  99  MET   A N   
743  C CA  . MET   A 93  ? 0.1478 0.1728 0.1873 -0.0198 -0.0210 0.0279  99  MET   A CA  
744  C C   . MET   A 93  ? 0.1590 0.1834 0.2029 -0.0123 -0.0145 0.0239  99  MET   A C   
745  O O   . MET   A 93  ? 0.1682 0.1846 0.2049 -0.0073 -0.0104 0.0163  99  MET   A O   
746  C CB  . MET   A 93  ? 0.1518 0.1698 0.1716 -0.0264 -0.0202 0.0229  99  MET   A CB  
747  C CG  . MET   A 93  ? 0.1611 0.1770 0.1724 -0.0352 -0.0242 0.0251  99  MET   A CG  
748  S SD  . MET   A 93  ? 0.2267 0.2310 0.2173 -0.0408 -0.0187 0.0165  99  MET   A SD  
749  C CE  . MET   A 93  ? 0.2251 0.2234 0.2196 -0.0296 -0.0139 0.0087  99  MET   A CE  
750  N N   . LEU   A 94  ? 0.1475 0.1802 0.2028 -0.0126 -0.0137 0.0292  100 LEU   A N   
751  C CA  . LEU   A 94  ? 0.1442 0.1757 0.2025 -0.0065 -0.0059 0.0251  100 LEU   A CA  
752  C C   . LEU   A 94  ? 0.1464 0.1787 0.1949 -0.0111 -0.0050 0.0245  100 LEU   A C   
753  O O   . LEU   A 94  ? 0.1425 0.1812 0.1914 -0.0187 -0.0100 0.0308  100 LEU   A O   
754  C CB  . LEU   A 94  ? 0.1513 0.1913 0.2338 -0.0019 -0.0023 0.0310  100 LEU   A CB  
755  C CG  . LEU   A 94  ? 0.1913 0.2291 0.2878 0.0043  -0.0009 0.0315  100 LEU   A CG  
756  C CD1 . LEU   A 94  ? 0.2108 0.2555 0.3336 0.0098  0.0058  0.0363  100 LEU   A CD1 
757  C CD2 . LEU   A 94  ? 0.2101 0.2344 0.2922 0.0090  0.0044  0.0205  100 LEU   A CD2 
758  N N   . ALA   A 95  ? 0.1390 0.1653 0.1796 -0.0074 0.0013  0.0181  101 ALA   A N   
759  C CA  . ALA   A 95  ? 0.1472 0.1735 0.1796 -0.0109 0.0032  0.0177  101 ALA   A CA  
760  C C   . ALA   A 95  ? 0.1514 0.1765 0.1865 -0.0062 0.0117  0.0146  101 ALA   A C   
761  O O   . ALA   A 95  ? 0.1616 0.1807 0.1965 -0.0009 0.0162  0.0098  101 ALA   A O   
762  C CB  . ALA   A 95  ? 0.1693 0.1853 0.1823 -0.0134 0.0016  0.0122  101 ALA   A CB  
763  N N   . VAL   A 96  ? 0.1497 0.1792 0.1852 -0.0092 0.0144  0.0169  102 VAL   A N   
764  C CA  . VAL   A 96  ? 0.1518 0.1788 0.1859 -0.0066 0.0235  0.0134  102 VAL   A CA  
765  C C   . VAL   A 96  ? 0.1696 0.1834 0.1802 -0.0076 0.0233  0.0067  102 VAL   A C   
766  O O   . VAL   A 96  ? 0.1826 0.1940 0.1828 -0.0120 0.0186  0.0075  102 VAL   A O   
767  C CB  . VAL   A 96  ? 0.1517 0.1891 0.1957 -0.0103 0.0261  0.0192  102 VAL   A CB  
768  C CG1 . VAL   A 96  ? 0.1530 0.1866 0.1932 -0.0086 0.0371  0.0149  102 VAL   A CG1 
769  C CG2 . VAL   A 96  ? 0.1463 0.1985 0.2176 -0.0099 0.0243  0.0284  102 VAL   A CG2 
770  N N   . GLY   A 97  ? 0.1785 0.1833 0.1813 -0.0043 0.0277  0.0008  103 GLY   A N   
771  C CA  . GLY   A 97  ? 0.2029 0.1961 0.1850 -0.0063 0.0257  -0.0035 103 GLY   A CA  
772  C C   . GLY   A 97  ? 0.2251 0.2081 0.1976 -0.0046 0.0295  -0.0093 103 GLY   A C   
773  O O   . GLY   A 97  ? 0.2437 0.2274 0.2258 -0.0010 0.0346  -0.0113 103 GLY   A O   
774  N N   . HIS   A 98  ? 0.2108 0.1837 0.1645 -0.0079 0.0265  -0.0116 104 HIS   A N   
775  C CA  . HIS   A 98  ? 0.2198 0.1815 0.1600 -0.0090 0.0285  -0.0167 104 HIS   A CA  
776  C C   . HIS   A 98  ? 0.2175 0.1758 0.1581 -0.0073 0.0207  -0.0174 104 HIS   A C   
777  O O   . HIS   A 98  ? 0.2069 0.1673 0.1498 -0.0072 0.0124  -0.0141 104 HIS   A O   
778  C CB  . HIS   A 98  ? 0.2340 0.1864 0.1525 -0.0156 0.0273  -0.0170 104 HIS   A CB  
779  C CG  . HIS   A 98  ? 0.2821 0.2215 0.1825 -0.0196 0.0280  -0.0217 104 HIS   A CG  
780  N ND1 . HIS   A 98  ? 0.3086 0.2420 0.2046 -0.0202 0.0398  -0.0281 104 HIS   A ND1 
781  C CD2 . HIS   A 98  ? 0.3025 0.2342 0.1907 -0.0233 0.0183  -0.0207 104 HIS   A CD2 
782  C CE1 . HIS   A 98  ? 0.3287 0.2491 0.2053 -0.0256 0.0369  -0.0316 104 HIS   A CE1 
783  N NE2 . HIS   A 98  ? 0.3349 0.2549 0.2068 -0.0279 0.0231  -0.0265 104 HIS   A NE2 
784  N N   . SER   A 99  ? 0.2294 0.1806 0.1661 -0.0068 0.0243  -0.0221 105 SER   A N   
785  C CA  . SER   A 99  ? 0.2330 0.1794 0.1677 -0.0064 0.0175  -0.0232 105 SER   A CA  
786  C C   . SER   A 99  ? 0.2554 0.1896 0.1779 -0.0089 0.0233  -0.0296 105 SER   A C   
787  O O   . SER   A 99  ? 0.2568 0.1881 0.1802 -0.0081 0.0350  -0.0338 105 SER   A O   
788  C CB  . SER   A 99  ? 0.2373 0.1929 0.1914 -0.0011 0.0142  -0.0205 105 SER   A CB  
789  O OG  . SER   A 99  ? 0.2463 0.2039 0.2127 0.0028  0.0213  -0.0223 105 SER   A OG  
790  N N   . GLU   A 100 ? 0.2619 0.1884 0.1735 -0.0125 0.0155  -0.0303 106 GLU   A N   
791  C CA  . GLU   A 100 ? 0.2788 0.1916 0.1755 -0.0170 0.0183  -0.0363 106 GLU   A CA  
792  C C   . GLU   A 100 ? 0.2777 0.1914 0.1830 -0.0148 0.0104  -0.0352 106 GLU   A C   
793  O O   . GLU   A 100 ? 0.2761 0.1999 0.1944 -0.0116 0.0021  -0.0296 106 GLU   A O   
794  C CB  . GLU   A 100 ? 0.3249 0.2263 0.1946 -0.0273 0.0142  -0.0366 106 GLU   A CB  
795  C CG  . GLU   A 100 ? 0.4035 0.3015 0.2622 -0.0304 0.0249  -0.0392 106 GLU   A CG  
796  C CD  . GLU   A 100 ? 0.4486 0.3354 0.2787 -0.0421 0.0208  -0.0384 106 GLU   A CD  
797  O OE1 . GLU   A 100 ? 0.4689 0.3423 0.2784 -0.0506 0.0172  -0.0412 106 GLU   A OE1 
798  O OE2 . GLU   A 100 ? 0.4622 0.3529 0.2894 -0.0437 0.0204  -0.0345 106 GLU   A OE2 
799  N N   . PRO   A 101 ? 0.2874 0.1905 0.1866 -0.0166 0.0138  -0.0407 107 PRO   A N   
800  C CA  . PRO   A 101 ? 0.2785 0.1839 0.1887 -0.0141 0.0067  -0.0392 107 PRO   A CA  
801  C C   . PRO   A 101 ? 0.2707 0.1811 0.1815 -0.0168 -0.0074 -0.0328 107 PRO   A C   
802  O O   . PRO   A 101 ? 0.2679 0.1877 0.1959 -0.0122 -0.0124 -0.0291 107 PRO   A O   
803  C CB  . PRO   A 101 ? 0.3016 0.1905 0.1980 -0.0186 0.0126  -0.0467 107 PRO   A CB  
804  C CG  . PRO   A 101 ? 0.3162 0.1983 0.2072 -0.0182 0.0278  -0.0528 107 PRO   A CG  
805  C CD  . PRO   A 101 ? 0.2944 0.1825 0.1786 -0.0205 0.0263  -0.0492 107 PRO   A CD  
806  N N   . GLY   A 102 ? 0.2630 0.1677 0.1564 -0.0245 -0.0135 -0.0309 108 GLY   A N   
807  C CA  . GLY   A 102 ? 0.2632 0.1728 0.1599 -0.0274 -0.0270 -0.0233 108 GLY   A CA  
808  C C   . GLY   A 102 ? 0.2544 0.1775 0.1699 -0.0211 -0.0294 -0.0173 108 GLY   A C   
809  O O   . GLY   A 102 ? 0.2569 0.1852 0.1821 -0.0212 -0.0384 -0.0111 108 GLY   A O   
810  N N   . ASP   A 103 ? 0.2365 0.1647 0.1578 -0.0160 -0.0210 -0.0190 109 ASP   A N   
811  C CA  . ASP   A 103 ? 0.2161 0.1551 0.1529 -0.0111 -0.0218 -0.0146 109 ASP   A CA  
812  C C   . ASP   A 103 ? 0.1918 0.1386 0.1464 -0.0059 -0.0220 -0.0139 109 ASP   A C   
813  O O   . ASP   A 103 ? 0.1813 0.1348 0.1469 -0.0034 -0.0229 -0.0107 109 ASP   A O   
814  C CB  . ASP   A 103 ? 0.2332 0.1751 0.1691 -0.0092 -0.0138 -0.0158 109 ASP   A CB  
815  C CG  . ASP   A 103 ? 0.2457 0.1810 0.1645 -0.0151 -0.0144 -0.0149 109 ASP   A CG  
816  O OD1 . ASP   A 103 ? 0.2430 0.1756 0.1570 -0.0191 -0.0231 -0.0102 109 ASP   A OD1 
817  O OD2 . ASP   A 103 ? 0.2503 0.1830 0.1611 -0.0161 -0.0060 -0.0185 109 ASP   A OD2 
818  N N   . CYS   A 104 ? 0.1935 0.1382 0.1503 -0.0049 -0.0206 -0.0170 110 CYS   A N   
819  C CA  . CYS   A 104 ? 0.1853 0.1369 0.1576 -0.0013 -0.0212 -0.0158 110 CYS   A CA  
820  C C   . CYS   A 104 ? 0.1920 0.1475 0.1725 -0.0018 -0.0277 -0.0115 110 CYS   A C   
821  O O   . CYS   A 104 ? 0.2089 0.1607 0.1849 -0.0054 -0.0341 -0.0092 110 CYS   A O   
822  C CB  . CYS   A 104 ? 0.1931 0.1398 0.1654 -0.0012 -0.0202 -0.0190 110 CYS   A CB  
823  S SG  . CYS   A 104 ? 0.2426 0.1868 0.2161 0.0020  -0.0101 -0.0230 110 CYS   A SG  
824  N N   . GLY   A 105 ? 0.1760 0.1385 0.1685 0.0008  -0.0258 -0.0099 111 GLY   A N   
825  C CA  . GLY   A 105 ? 0.1855 0.1515 0.1890 0.0009  -0.0287 -0.0065 111 GLY   A CA  
826  C C   . GLY   A 105 ? 0.2022 0.1694 0.2080 0.0015  -0.0268 -0.0044 111 GLY   A C   
827  O O   . GLY   A 105 ? 0.1993 0.1688 0.2166 0.0025  -0.0257 -0.0024 111 GLY   A O   
828  N N   . GLY   A 106 ? 0.1965 0.1612 0.1919 0.0008  -0.0251 -0.0051 112 GLY   A N   
829  C CA  . GLY   A 106 ? 0.1906 0.1554 0.1870 0.0010  -0.0229 -0.0033 112 GLY   A CA  
830  C C   . GLY   A 106 ? 0.1880 0.1561 0.1900 0.0017  -0.0167 -0.0050 112 GLY   A C   
831  O O   . GLY   A 106 ? 0.1786 0.1496 0.1787 0.0014  -0.0142 -0.0070 112 GLY   A O   
832  N N   . ILE   A 107 ? 0.1800 0.1470 0.1891 0.0019  -0.0142 -0.0037 113 ILE   A N   
833  C CA  . ILE   A 107 ? 0.1842 0.1517 0.1952 0.0005  -0.0075 -0.0061 113 ILE   A CA  
834  C C   . ILE   A 107 ? 0.1715 0.1382 0.1728 -0.0022 -0.0044 -0.0071 113 ILE   A C   
835  O O   . ILE   A 107 ? 0.1745 0.1386 0.1721 -0.0022 -0.0051 -0.0057 113 ILE   A O   
836  C CB  . ILE   A 107 ? 0.2130 0.1775 0.2369 0.0016  -0.0039 -0.0054 113 ILE   A CB  
837  C CG1 . ILE   A 107 ? 0.2261 0.1937 0.2612 0.0028  -0.0047 -0.0050 113 ILE   A CG1 
838  C CG2 . ILE   A 107 ? 0.2361 0.1960 0.2576 -0.0014 0.0049  -0.0085 113 ILE   A CG2 
839  C CD1 . ILE   A 107 ? 0.2329 0.1987 0.2860 0.0048  -0.0001 -0.0035 113 ILE   A CD1 
840  N N   . LEU   A 108 ? 0.1688 0.1379 0.1663 -0.0057 -0.0014 -0.0087 114 LEU   A N   
841  C CA  . LEU   A 108 ? 0.1799 0.1488 0.1695 -0.0101 0.0012  -0.0088 114 LEU   A CA  
842  C C   . LEU   A 108 ? 0.1896 0.1525 0.1779 -0.0145 0.0074  -0.0114 114 LEU   A C   
843  O O   . LEU   A 108 ? 0.1791 0.1418 0.1693 -0.0163 0.0097  -0.0129 114 LEU   A O   
844  C CB  . LEU   A 108 ? 0.1822 0.1580 0.1694 -0.0125 -0.0010 -0.0072 114 LEU   A CB  
845  C CG  . LEU   A 108 ? 0.1894 0.1668 0.1699 -0.0193 0.0002  -0.0056 114 LEU   A CG  
846  C CD1 . LEU   A 108 ? 0.1930 0.1700 0.1702 -0.0191 0.0006  -0.0046 114 LEU   A CD1 
847  C CD2 . LEU   A 108 ? 0.1856 0.1712 0.1691 -0.0215 -0.0035 -0.0018 114 LEU   A CD2 
848  N N   . ARG   A 109 ? 0.1972 0.1538 0.1812 -0.0170 0.0113  -0.0123 115 ARG   A N   
849  C CA  . ARG   A 109 ? 0.2221 0.1697 0.2034 -0.0218 0.0195  -0.0161 115 ARG   A CA  
850  C C   . ARG   A 109 ? 0.2383 0.1816 0.2059 -0.0299 0.0219  -0.0171 115 ARG   A C   
851  O O   . ARG   A 109 ? 0.2298 0.1753 0.1948 -0.0295 0.0185  -0.0145 115 ARG   A O   
852  C CB  . ARG   A 109 ? 0.2565 0.1967 0.2486 -0.0169 0.0236  -0.0165 115 ARG   A CB  
853  C CG  . ARG   A 109 ? 0.3378 0.2810 0.3461 -0.0099 0.0214  -0.0144 115 ARG   A CG  
854  C CD  . ARG   A 109 ? 0.3844 0.3202 0.4063 -0.0060 0.0254  -0.0129 115 ARG   A CD  
855  N NE  . ARG   A 109 ? 0.4311 0.3577 0.4558 -0.0089 0.0379  -0.0182 115 ARG   A NE  
856  C CZ  . ARG   A 109 ? 0.4421 0.3682 0.4805 -0.0068 0.0440  -0.0197 115 ARG   A CZ  
857  N NH1 . ARG   A 109 ? 0.4236 0.3585 0.4765 -0.0014 0.0371  -0.0151 115 ARG   A NH1 
858  N NH2 . ARG   A 109 ? 0.4537 0.3696 0.4914 -0.0109 0.0576  -0.0259 115 ARG   A NH2 
859  N N   . CYS   A 110 ? 0.2387 0.1748 0.1967 -0.0383 0.0283  -0.0209 116 CYS   A N   
860  C CA  . CYS   A 110 ? 0.2691 0.1979 0.2118 -0.0484 0.0314  -0.0225 116 CYS   A CA  
861  C C   . CYS   A 110 ? 0.2966 0.2092 0.2379 -0.0505 0.0437  -0.0290 116 CYS   A C   
862  O O   . CYS   A 110 ? 0.2905 0.2002 0.2460 -0.0432 0.0489  -0.0308 116 CYS   A O   
863  C CB  . CYS   A 110 ? 0.2780 0.2104 0.2072 -0.0594 0.0281  -0.0210 116 CYS   A CB  
864  S SG  . CYS   A 110 ? 0.2713 0.1974 0.1952 -0.0649 0.0352  -0.0258 116 CYS   A SG  
865  N N   . GLN   A 111 ? 0.3358 0.2371 0.2608 -0.0611 0.0492  -0.0324 117 GLN   A N   
866  C CA  . GLN   A 111 ? 0.3761 0.2590 0.2982 -0.0643 0.0633  -0.0398 117 GLN   A CA  
867  C C   . GLN   A 111 ? 0.3787 0.2557 0.3019 -0.0662 0.0734  -0.0454 117 GLN   A C   
868  O O   . GLN   A 111 ? 0.4003 0.2647 0.3324 -0.0633 0.0865  -0.0509 117 GLN   A O   
869  C CB  . GLN   A 111 ? 0.4417 0.3127 0.3409 -0.0785 0.0667  -0.0429 117 GLN   A CB  
870  C CG  . GLN   A 111 ? 0.5046 0.3795 0.3828 -0.0927 0.0611  -0.0416 117 GLN   A CG  
871  C CD  . GLN   A 111 ? 0.5961 0.4586 0.4501 -0.1089 0.0633  -0.0440 117 GLN   A CD  
872  O OE1 . GLN   A 111 ? 0.6119 0.4837 0.4561 -0.1173 0.0521  -0.0376 117 GLN   A OE1 
873  N NE2 . GLN   A 111 ? 0.6128 0.4537 0.4576 -0.1141 0.0781  -0.0530 117 GLN   A NE2 
874  N N   . HIS   A 112 ? 0.3538 0.2398 0.2703 -0.0706 0.0678  -0.0435 118 HIS   A N   
875  C CA  . HIS   A 112 ? 0.3519 0.2326 0.2667 -0.0741 0.0771  -0.0485 118 HIS   A CA  
876  C C   . HIS   A 112 ? 0.3317 0.2221 0.2716 -0.0609 0.0761  -0.0462 118 HIS   A C   
877  O O   . HIS   A 112 ? 0.3439 0.2301 0.2868 -0.0624 0.0854  -0.0503 118 HIS   A O   
878  C CB  . HIS   A 112 ? 0.3633 0.2469 0.2562 -0.0879 0.0716  -0.0470 118 HIS   A CB  
879  C CG  . HIS   A 112 ? 0.4266 0.3024 0.2941 -0.1033 0.0700  -0.0474 118 HIS   A CG  
880  N ND1 . HIS   A 112 ? 0.4484 0.3365 0.3133 -0.1052 0.0553  -0.0391 118 HIS   A ND1 
881  C CD2 . HIS   A 112 ? 0.4607 0.3174 0.3047 -0.1182 0.0813  -0.0549 118 HIS   A CD2 
882  C CE1 . HIS   A 112 ? 0.4695 0.3474 0.3107 -0.1211 0.0565  -0.0407 118 HIS   A CE1 
883  N NE2 . HIS   A 112 ? 0.4867 0.3444 0.3128 -0.1299 0.0720  -0.0506 118 HIS   A NE2 
884  N N   . GLY   A 113 ? 0.2929 0.1959 0.2489 -0.0496 0.0650  -0.0397 119 GLY   A N   
885  C CA  . GLY   A 113 ? 0.2610 0.1733 0.2387 -0.0387 0.0619  -0.0366 119 GLY   A CA  
886  C C   . GLY   A 113 ? 0.2193 0.1467 0.2000 -0.0339 0.0471  -0.0299 119 GLY   A C   
887  O O   . GLY   A 113 ? 0.2217 0.1535 0.1946 -0.0350 0.0393  -0.0267 119 GLY   A O   
888  N N   . VAL   A 114 ? 0.2036 0.1385 0.1971 -0.0283 0.0440  -0.0279 120 VAL   A N   
889  C CA  . VAL   A 114 ? 0.1988 0.1455 0.1959 -0.0236 0.0319  -0.0227 120 VAL   A CA  
890  C C   . VAL   A 114 ? 0.1955 0.1468 0.1785 -0.0306 0.0267  -0.0212 120 VAL   A C   
891  O O   . VAL   A 114 ? 0.2114 0.1604 0.1871 -0.0377 0.0305  -0.0230 120 VAL   A O   
892  C CB  . VAL   A 114 ? 0.2018 0.1533 0.2158 -0.0172 0.0304  -0.0212 120 VAL   A CB  
893  C CG1 . VAL   A 114 ? 0.2029 0.1639 0.2175 -0.0139 0.0191  -0.0171 120 VAL   A CG1 
894  C CG2 . VAL   A 114 ? 0.1934 0.1426 0.2252 -0.0101 0.0324  -0.0197 120 VAL   A CG2 
895  N N   . VAL   A 115 ? 0.1875 0.1456 0.1681 -0.0290 0.0182  -0.0171 121 VAL   A N   
896  C CA  . VAL   A 115 ? 0.1948 0.1590 0.1674 -0.0347 0.0123  -0.0135 121 VAL   A CA  
897  C C   . VAL   A 115 ? 0.1984 0.1706 0.1804 -0.0291 0.0057  -0.0102 121 VAL   A C   
898  O O   . VAL   A 115 ? 0.1944 0.1699 0.1743 -0.0336 0.0028  -0.0076 121 VAL   A O   
899  C CB  . VAL   A 115 ? 0.1921 0.1590 0.1595 -0.0366 0.0086  -0.0107 121 VAL   A CB  
900  C CG1 . VAL   A 115 ? 0.1965 0.1723 0.1628 -0.0406 0.0013  -0.0046 121 VAL   A CG1 
901  C CG2 . VAL   A 115 ? 0.2043 0.1618 0.1599 -0.0442 0.0149  -0.0140 121 VAL   A CG2 
902  N N   . GLY   A 116 ? 0.1913 0.1657 0.1825 -0.0205 0.0030  -0.0100 122 GLY   A N   
903  C CA  . GLY   A 116 ? 0.1825 0.1619 0.1808 -0.0157 -0.0023 -0.0079 122 GLY   A CA  
904  C C   . GLY   A 116 ? 0.1661 0.1448 0.1698 -0.0086 -0.0046 -0.0084 122 GLY   A C   
905  O O   . GLY   A 116 ? 0.1613 0.1364 0.1655 -0.0070 -0.0027 -0.0095 122 GLY   A O   
906  N N   . ILE   A 117 ? 0.1573 0.1382 0.1642 -0.0052 -0.0087 -0.0075 123 ILE   A N   
907  C CA  . ILE   A 117 ? 0.1597 0.1383 0.1673 -0.0009 -0.0113 -0.0081 123 ILE   A CA  
908  C C   . ILE   A 117 ? 0.1585 0.1379 0.1632 0.0008  -0.0123 -0.0080 123 ILE   A C   
909  O O   . ILE   A 117 ? 0.1606 0.1432 0.1686 0.0006  -0.0122 -0.0067 123 ILE   A O   
910  C CB  . ILE   A 117 ? 0.1679 0.1453 0.1817 0.0005  -0.0142 -0.0083 123 ILE   A CB  
911  C CG1 . ILE   A 117 ? 0.1848 0.1642 0.2014 -0.0003 -0.0152 -0.0080 123 ILE   A CG1 
912  C CG2 . ILE   A 117 ? 0.1788 0.1552 0.1997 0.0002  -0.0121 -0.0080 123 ILE   A CG2 
913  C CD1 . ILE   A 117 ? 0.2100 0.1878 0.2319 0.0006  -0.0189 -0.0080 123 ILE   A CD1 
914  N N   . VAL   A 118 ? 0.1452 0.1212 0.1446 0.0022  -0.0126 -0.0090 124 VAL   A N   
915  C CA  . VAL   A 118 ? 0.1349 0.1097 0.1308 0.0035  -0.0109 -0.0101 124 VAL   A CA  
916  C C   . VAL   A 118 ? 0.1406 0.1131 0.1398 0.0050  -0.0118 -0.0115 124 VAL   A C   
917  O O   . VAL   A 118 ? 0.1442 0.1132 0.1427 0.0044  -0.0154 -0.0122 124 VAL   A O   
918  C CB  . VAL   A 118 ? 0.1425 0.1116 0.1284 0.0028  -0.0112 -0.0114 124 VAL   A CB  
919  C CG1 . VAL   A 118 ? 0.1373 0.1028 0.1179 0.0034  -0.0071 -0.0142 124 VAL   A CG1 
920  C CG2 . VAL   A 118 ? 0.1592 0.1299 0.1425 0.0014  -0.0101 -0.0097 124 VAL   A CG2 
921  N N   . SER   A 119 ? 0.1439 0.1184 0.1486 0.0066  -0.0086 -0.0110 125 SER   A N   
922  C CA  . SER   A 119 ? 0.1510 0.1220 0.1602 0.0082  -0.0087 -0.0122 125 SER   A CA  
923  C C   . SER   A 119 ? 0.1750 0.1418 0.1860 0.0107  -0.0024 -0.0144 125 SER   A C   
924  O O   . SER   A 119 ? 0.1932 0.1521 0.2030 0.0115  -0.0009 -0.0177 125 SER   A O   
925  C CB  . SER   A 119 ? 0.1595 0.1366 0.1790 0.0076  -0.0113 -0.0079 125 SER   A CB  
926  O OG  . SER   A 119 ? 0.1816 0.1559 0.2083 0.0094  -0.0111 -0.0076 125 SER   A OG  
927  N N   . THR   A 120 ? 0.1749 0.1464 0.1897 0.0118  0.0023  -0.0129 126 THR   A N   
928  C CA  . THR   A 120 ? 0.1812 0.1491 0.2015 0.0147  0.0109  -0.0151 126 THR   A CA  
929  C C   . THR   A 120 ? 0.2018 0.1705 0.2161 0.0139  0.0164  -0.0164 126 THR   A C   
930  O O   . THR   A 120 ? 0.1974 0.1713 0.2067 0.0114  0.0126  -0.0141 126 THR   A O   
931  C CB  . THR   A 120 ? 0.1877 0.1637 0.2301 0.0180  0.0121  -0.0090 126 THR   A CB  
932  O OG1 . THR   A 120 ? 0.2033 0.1912 0.2529 0.0165  0.0098  -0.0027 126 THR   A OG1 
933  C CG2 . THR   A 120 ? 0.1863 0.1628 0.2353 0.0179  0.0058  -0.0060 126 THR   A CG2 
934  N N   . GLY   A 121 ? 0.2208 0.1835 0.2359 0.0156  0.0263  -0.0204 127 GLY   A N   
935  C CA  . GLY   A 121 ? 0.2517 0.2157 0.2627 0.0145  0.0330  -0.0213 127 GLY   A CA  
936  C C   . GLY   A 121 ? 0.2931 0.2510 0.3098 0.0170  0.0467  -0.0257 127 GLY   A C   
937  O O   . GLY   A 121 ? 0.2986 0.2491 0.3216 0.0197  0.0517  -0.0288 127 GLY   A O   
938  N N   . GLY   A 122 ? 0.3230 0.2828 0.3368 0.0156  0.0537  -0.0263 128 GLY   A N   
939  C CA  . GLY   A 122 ? 0.3586 0.3123 0.3773 0.0173  0.0697  -0.0312 128 GLY   A CA  
940  C C   . GLY   A 122 ? 0.3652 0.3332 0.4053 0.0198  0.0751  -0.0250 128 GLY   A C   
941  O O   . GLY   A 122 ? 0.3596 0.3426 0.4163 0.0211  0.0662  -0.0159 128 GLY   A O   
942  N N   . ASN   A 123 ? 0.3714 0.3346 0.4104 0.0193  0.0900  -0.0296 129 ASN   A N   
943  C CA  . ASN   A 123 ? 0.3683 0.3457 0.4307 0.0217  0.0967  -0.0234 129 ASN   A CA  
944  C C   . ASN   A 123 ? 0.3455 0.3355 0.4033 0.0174  0.0851  -0.0163 129 ASN   A C   
945  O O   . ASN   A 123 ? 0.3420 0.3478 0.4231 0.0189  0.0834  -0.0075 129 ASN   A O   
946  C CB  . ASN   A 123 ? 0.3813 0.3704 0.4821 0.0291  0.0980  -0.0154 129 ASN   A CB  
947  C CG  . ASN   A 123 ? 0.4531 0.4307 0.5664 0.0344  0.1139  -0.0216 129 ASN   A CG  
948  O OD1 . ASN   A 123 ? 0.4895 0.4507 0.5841 0.0320  0.1282  -0.0327 129 ASN   A OD1 
949  N ND2 . ASN   A 123 ? 0.4378 0.4228 0.5828 0.0408  0.1121  -0.0143 129 ASN   A ND2 
950  N N   . GLY   A 124 ? 0.3296 0.3122 0.3588 0.0119  0.0766  -0.0194 130 GLY   A N   
951  C CA  . GLY   A 124 ? 0.3034 0.2944 0.3266 0.0078  0.0669  -0.0139 130 GLY   A CA  
952  C C   . GLY   A 124 ? 0.2603 0.2620 0.2948 0.0084  0.0535  -0.0063 130 GLY   A C   
953  O O   . GLY   A 124 ? 0.2481 0.2573 0.2815 0.0048  0.0473  -0.0014 130 GLY   A O   
954  N N   . LEU   A 125 ? 0.2347 0.2354 0.2771 0.0118  0.0491  -0.0059 131 LEU   A N   
955  C CA  . LEU   A 125 ? 0.2193 0.2279 0.2680 0.0108  0.0369  0.0004  131 LEU   A CA  
956  C C   . LEU   A 125 ? 0.2130 0.2116 0.2457 0.0104  0.0305  -0.0042 131 LEU   A C   
957  O O   . LEU   A 125 ? 0.2286 0.2182 0.2586 0.0130  0.0344  -0.0093 131 LEU   A O   
958  C CB  . LEU   A 125 ? 0.2250 0.2436 0.3015 0.0145  0.0366  0.0076  131 LEU   A CB  
959  C CG  . LEU   A 125 ? 0.2531 0.2847 0.3523 0.0149  0.0418  0.0147  131 LEU   A CG  
960  C CD1 . LEU   A 125 ? 0.2622 0.3009 0.3919 0.0201  0.0443  0.0212  131 LEU   A CD1 
961  C CD2 . LEU   A 125 ? 0.2563 0.2984 0.3535 0.0082  0.0324  0.0220  131 LEU   A CD2 
962  N N   . VAL   A 126 ? 0.1872 0.1870 0.2112 0.0070  0.0214  -0.0023 132 VAL   A N   
963  C CA  . VAL   A 126 ? 0.1848 0.1775 0.1982 0.0066  0.0153  -0.0053 132 VAL   A CA  
964  C C   . VAL   A 126 ? 0.1689 0.1685 0.1930 0.0060  0.0088  -0.0002 132 VAL   A C   
965  O O   . VAL   A 126 ? 0.1621 0.1698 0.1916 0.0027  0.0058  0.0052  132 VAL   A O   
966  C CB  . VAL   A 126 ? 0.1971 0.1842 0.1933 0.0032  0.0117  -0.0073 132 VAL   A CB  
967  C CG1 . VAL   A 126 ? 0.2153 0.2086 0.2119 -0.0004 0.0097  -0.0032 132 VAL   A CG1 
968  C CG2 . VAL   A 126 ? 0.1964 0.1777 0.1863 0.0031  0.0056  -0.0091 132 VAL   A CG2 
969  N N   . GLY   A 127 ? 0.1546 0.1503 0.1810 0.0081  0.0068  -0.0017 133 GLY   A N   
970  C CA  . GLY   A 127 ? 0.1411 0.1417 0.1750 0.0065  0.0008  0.0029  133 GLY   A CA  
971  C C   . GLY   A 127 ? 0.1563 0.1518 0.1790 0.0043  -0.0037 0.0001  133 GLY   A C   
972  O O   . GLY   A 127 ? 0.1610 0.1488 0.1762 0.0061  -0.0033 -0.0047 133 GLY   A O   
973  N N   . PHE   A 128 ? 0.1501 0.1495 0.1722 -0.0003 -0.0078 0.0035  134 PHE   A N   
974  C CA  . PHE   A 128 ? 0.1575 0.1524 0.1717 -0.0025 -0.0098 0.0008  134 PHE   A CA  
975  C C   . PHE   A 128 ? 0.1550 0.1522 0.1737 -0.0053 -0.0131 0.0039  134 PHE   A C   
976  O O   . PHE   A 128 ? 0.1441 0.1471 0.1671 -0.0094 -0.0155 0.0096  134 PHE   A O   
977  C CB  . PHE   A 128 ? 0.1578 0.1520 0.1637 -0.0071 -0.0091 0.0004  134 PHE   A CB  
978  C CG  . PHE   A 128 ? 0.1664 0.1592 0.1679 -0.0059 -0.0066 -0.0009 134 PHE   A CG  
979  C CD1 . PHE   A 128 ? 0.1763 0.1627 0.1720 -0.0036 -0.0058 -0.0043 134 PHE   A CD1 
980  C CD2 . PHE   A 128 ? 0.1629 0.1614 0.1669 -0.0079 -0.0056 0.0025  134 PHE   A CD2 
981  C CE1 . PHE   A 128 ? 0.1762 0.1608 0.1665 -0.0036 -0.0041 -0.0047 134 PHE   A CE1 
982  C CE2 . PHE   A 128 ? 0.1658 0.1629 0.1650 -0.0076 -0.0029 0.0015  134 PHE   A CE2 
983  C CZ  . PHE   A 128 ? 0.1662 0.1557 0.1575 -0.0055 -0.0021 -0.0023 134 PHE   A CZ  
984  N N   . ALA   A 129 ? 0.1576 0.1504 0.1753 -0.0041 -0.0139 0.0011  135 ALA   A N   
985  C CA  . ALA   A 129 ? 0.1475 0.1416 0.1676 -0.0076 -0.0165 0.0038  135 ALA   A CA  
986  C C   . ALA   A 129 ? 0.1560 0.1492 0.1675 -0.0144 -0.0151 0.0032  135 ALA   A C   
987  O O   . ALA   A 129 ? 0.1510 0.1398 0.1588 -0.0136 -0.0119 -0.0012 135 ALA   A O   
988  C CB  . ALA   A 129 ? 0.1443 0.1340 0.1668 -0.0044 -0.0173 0.0009  135 ALA   A CB  
989  N N   . ASP   A 130 ? 0.1499 0.1463 0.1585 -0.0218 -0.0172 0.0079  136 ASP   A N   
990  C CA  . ASP   A 130 ? 0.1633 0.1563 0.1601 -0.0304 -0.0144 0.0064  136 ASP   A CA  
991  C C   . ASP   A 130 ? 0.1729 0.1614 0.1675 -0.0322 -0.0114 0.0032  136 ASP   A C   
992  O O   . ASP   A 130 ? 0.1865 0.1767 0.1871 -0.0308 -0.0146 0.0054  136 ASP   A O   
993  C CB  . ASP   A 130 ? 0.1818 0.1789 0.1738 -0.0403 -0.0191 0.0135  136 ASP   A CB  
994  C CG  . ASP   A 130 ? 0.2219 0.2131 0.1966 -0.0520 -0.0157 0.0114  136 ASP   A CG  
995  O OD1 . ASP   A 130 ? 0.2138 0.1996 0.1822 -0.0517 -0.0099 0.0059  136 ASP   A OD1 
996  O OD2 . ASP   A 130 ? 0.2500 0.2407 0.2166 -0.0623 -0.0186 0.0154  136 ASP   A OD2 
997  N N   . VAL   A 131 ? 0.1546 0.1369 0.1418 -0.0356 -0.0044 -0.0020 137 VAL   A N   
998  C CA  . VAL   A 131 ? 0.1602 0.1384 0.1465 -0.0384 0.0006  -0.0050 137 VAL   A CA  
999  C C   . VAL   A 131 ? 0.1914 0.1630 0.1616 -0.0508 0.0070  -0.0072 137 VAL   A C   
1000 O O   . VAL   A 131 ? 0.2109 0.1780 0.1784 -0.0549 0.0135  -0.0103 137 VAL   A O   
1001 C CB  . VAL   A 131 ? 0.1583 0.1343 0.1554 -0.0303 0.0052  -0.0096 137 VAL   A CB  
1002 C CG1 . VAL   A 131 ? 0.1665 0.1469 0.1745 -0.0213 -0.0016 -0.0076 137 VAL   A CG1 
1003 C CG2 . VAL   A 131 ? 0.1542 0.1251 0.1493 -0.0293 0.0112  -0.0132 137 VAL   A CG2 
1004 N N   . ARG   A 132 ? 0.1959 0.1658 0.1547 -0.0574 0.0062  -0.0060 138 ARG   A N   
1005 C CA  . ARG   A 132 ? 0.2137 0.1744 0.1534 -0.0707 0.0130  -0.0092 138 ARG   A CA  
1006 C C   . ARG   A 132 ? 0.2410 0.2001 0.1680 -0.0831 0.0116  -0.0063 138 ARG   A C   
1007 O O   . ARG   A 132 ? 0.2594 0.2080 0.1698 -0.0942 0.0208  -0.0114 138 ARG   A O   
1008 C CB  . ARG   A 132 ? 0.2210 0.1808 0.1508 -0.0762 0.0104  -0.0075 138 ARG   A CB  
1009 C CG  . ARG   A 132 ? 0.2241 0.1831 0.1630 -0.0660 0.0134  -0.0110 138 ARG   A CG  
1010 C CD  . ARG   A 132 ? 0.2031 0.1625 0.1324 -0.0727 0.0095  -0.0080 138 ARG   A CD  
1011 N NE  . ARG   A 132 ? 0.2186 0.1908 0.1569 -0.0702 -0.0019 0.0009  138 ARG   A NE  
1012 C CZ  . ARG   A 132 ? 0.2472 0.2243 0.1842 -0.0738 -0.0071 0.0058  138 ARG   A CZ  
1013 N NH1 . ARG   A 132 ? 0.2607 0.2301 0.1838 -0.0818 -0.0032 0.0028  138 ARG   A NH1 
1014 N NH2 . ARG   A 132 ? 0.2085 0.1976 0.1588 -0.0699 -0.0156 0.0139  138 ARG   A NH2 
1015 N N   . ASP   A 133 ? 0.2320 0.2000 0.1663 -0.0820 0.0010  0.0018  139 ASP   A N   
1016 C CA  . ASP   A 133 ? 0.2379 0.2048 0.1610 -0.0942 -0.0022 0.0065  139 ASP   A CA  
1017 C C   . ASP   A 133 ? 0.2534 0.2170 0.1804 -0.0921 0.0050  0.0019  139 ASP   A C   
1018 O O   . ASP   A 133 ? 0.2743 0.2344 0.1885 -0.1038 0.0056  0.0039  139 ASP   A O   
1019 C CB  . ASP   A 133 ? 0.2509 0.2286 0.1838 -0.0935 -0.0167 0.0184  139 ASP   A CB  
1020 C CG  . ASP   A 133 ? 0.2939 0.2783 0.2497 -0.0780 -0.0198 0.0194  139 ASP   A CG  
1021 O OD1 . ASP   A 133 ? 0.2837 0.2684 0.2495 -0.0663 -0.0156 0.0137  139 ASP   A OD1 
1022 O OD2 . ASP   A 133 ? 0.3019 0.2904 0.2646 -0.0786 -0.0267 0.0263  139 ASP   A OD2 
1023 N N   . LEU   A 134 ? 0.2408 0.2059 0.1851 -0.0784 0.0100  -0.0033 140 LEU   A N   
1024 C CA  . LEU   A 134 ? 0.2371 0.2011 0.1890 -0.0761 0.0157  -0.0063 140 LEU   A CA  
1025 C C   . LEU   A 134 ? 0.2524 0.2063 0.1954 -0.0824 0.0311  -0.0146 140 LEU   A C   
1026 O O   . LEU   A 134 ? 0.2531 0.2053 0.2094 -0.0737 0.0395  -0.0202 140 LEU   A O   
1027 C CB  . LEU   A 134 ? 0.2253 0.1954 0.1995 -0.0608 0.0128  -0.0067 140 LEU   A CB  
1028 C CG  . LEU   A 134 ? 0.2381 0.2157 0.2210 -0.0539 0.0004  -0.0002 140 LEU   A CG  
1029 C CD1 . LEU   A 134 ? 0.2377 0.2182 0.2371 -0.0409 -0.0011 -0.0023 140 LEU   A CD1 
1030 C CD2 . LEU   A 134 ? 0.2418 0.2221 0.2235 -0.0593 -0.0068 0.0066  140 LEU   A CD2 
1031 N N   . LEU   A 135 ? 0.2690 0.2152 0.1892 -0.0984 0.0354  -0.0152 141 LEU   A N   
1032 C CA  . LEU   A 135 ? 0.2941 0.2273 0.2016 -0.1068 0.0527  -0.0246 141 LEU   A CA  
1033 C C   . LEU   A 135 ? 0.3108 0.2433 0.2341 -0.1012 0.0646  -0.0296 141 LEU   A C   
1034 O O   . LEU   A 135 ? 0.3251 0.2492 0.2520 -0.1003 0.0806  -0.0379 141 LEU   A O   
1035 C CB  . LEU   A 135 ? 0.3198 0.2431 0.1948 -0.1279 0.0544  -0.0241 141 LEU   A CB  
1036 C CG  . LEU   A 135 ? 0.3377 0.2634 0.1979 -0.1362 0.0406  -0.0165 141 LEU   A CG  
1037 C CD1 . LEU   A 135 ? 0.3636 0.2779 0.1890 -0.1600 0.0423  -0.0157 141 LEU   A CD1 
1038 C CD2 . LEU   A 135 ? 0.3411 0.2656 0.2057 -0.1292 0.0416  -0.0198 141 LEU   A CD2 
1039 N N   . TRP   A 136 ? 0.3031 0.2446 0.2386 -0.0969 0.0569  -0.0242 142 TRP   A N   
1040 C CA  . TRP   A 136 ? 0.3070 0.2502 0.2595 -0.0923 0.0658  -0.0270 142 TRP   A CA  
1041 C C   . TRP   A 136 ? 0.3120 0.2599 0.2927 -0.0766 0.0694  -0.0295 142 TRP   A C   
1042 O O   . TRP   A 136 ? 0.3057 0.2544 0.3032 -0.0732 0.0794  -0.0323 142 TRP   A O   
1043 C CB  . TRP   A 136 ? 0.3025 0.2536 0.2594 -0.0928 0.0549  -0.0197 142 TRP   A CB  
1044 C CG  . TRP   A 136 ? 0.2915 0.2522 0.2599 -0.0826 0.0377  -0.0125 142 TRP   A CG  
1045 C CD1 . TRP   A 136 ? 0.3031 0.2663 0.2617 -0.0862 0.0248  -0.0055 142 TRP   A CD1 
1046 C CD2 . TRP   A 136 ? 0.2804 0.2487 0.2726 -0.0682 0.0324  -0.0114 142 TRP   A CD2 
1047 N NE1 . TRP   A 136 ? 0.2972 0.2681 0.2724 -0.0740 0.0138  -0.0013 142 TRP   A NE1 
1048 C CE2 . TRP   A 136 ? 0.2880 0.2613 0.2814 -0.0638 0.0180  -0.0052 142 TRP   A CE2 
1049 C CE3 . TRP   A 136 ? 0.2785 0.2497 0.2917 -0.0596 0.0382  -0.0143 142 TRP   A CE3 
1050 C CZ2 . TRP   A 136 ? 0.2882 0.2670 0.2985 -0.0520 0.0106  -0.0036 142 TRP   A CZ2 
1051 C CZ3 . TRP   A 136 ? 0.2849 0.2629 0.3149 -0.0487 0.0283  -0.0112 142 TRP   A CZ3 
1052 C CH2 . TRP   A 136 ? 0.2827 0.2633 0.3090 -0.0455 0.0153  -0.0067 142 TRP   A CH2 
1053 N N   . LEU   A 137 ? 0.3088 0.2600 0.2955 -0.0676 0.0612  -0.0278 143 LEU   A N   
1054 C CA  . LEU   A 137 ? 0.3242 0.2792 0.3355 -0.0544 0.0627  -0.0287 143 LEU   A CA  
1055 C C   . LEU   A 137 ? 0.3838 0.3303 0.4025 -0.0546 0.0808  -0.0357 143 LEU   A C   
1056 O O   . LEU   A 137 ? 0.3734 0.3241 0.4181 -0.0449 0.0839  -0.0351 143 LEU   A O   
1057 C CB  . LEU   A 137 ? 0.3099 0.2678 0.3211 -0.0475 0.0520  -0.0260 143 LEU   A CB  
1058 C CG  . LEU   A 137 ? 0.2923 0.2587 0.3046 -0.0431 0.0358  -0.0196 143 LEU   A CG  
1059 C CD1 . LEU   A 137 ? 0.2884 0.2559 0.2989 -0.0377 0.0288  -0.0182 143 LEU   A CD1 
1060 C CD2 . LEU   A 137 ? 0.2880 0.2614 0.3206 -0.0353 0.0311  -0.0168 143 LEU   A CD2 
1061 N N   . ASP   A 138 ? 0.4403 0.3743 0.4366 -0.0664 0.0928  -0.0419 144 ASP   A N   
1062 C CA  . ASP   A 138 ? 0.4949 0.4167 0.4938 -0.0688 0.1131  -0.0503 144 ASP   A CA  
1063 C C   . ASP   A 138 ? 0.5468 0.4627 0.5459 -0.0762 0.1300  -0.0554 144 ASP   A C   
1064 O O   . ASP   A 138 ? 0.5666 0.4725 0.5737 -0.0762 0.1490  -0.0626 144 ASP   A O   
1065 C CB  . ASP   A 138 ? 0.5430 0.4512 0.5126 -0.0799 0.1178  -0.0553 144 ASP   A CB  
1066 C CG  . ASP   A 138 ? 0.6158 0.5261 0.5878 -0.0727 0.1080  -0.0527 144 ASP   A CG  
1067 O OD1 . ASP   A 138 ? 0.6292 0.5456 0.6276 -0.0590 0.1059  -0.0504 144 ASP   A OD1 
1068 O OD2 . ASP   A 138 ? 0.6543 0.5608 0.6022 -0.0813 0.1016  -0.0521 144 ASP   A OD2 
1069 N N   . GLU   A 139 ? 0.5752 0.4951 0.5631 -0.0840 0.1251  -0.0525 145 GLU   A N   
1070 C CA  . GLU   A 139 ? 0.6112 0.5246 0.5957 -0.0932 0.1422  -0.0577 145 GLU   A CA  
1071 C C   . GLU   A 139 ? 0.6145 0.5408 0.6294 -0.0846 0.1411  -0.0532 145 GLU   A C   
1072 O O   . GLU   A 139 ? 0.6262 0.5503 0.6379 -0.0926 0.1515  -0.0554 145 GLU   A O   
1073 C CB  . GLU   A 139 ? 0.6724 0.5784 0.6188 -0.1120 0.1398  -0.0577 145 GLU   A CB  
1074 C CG  . GLU   A 139 ? 0.7397 0.6583 0.6828 -0.1115 0.1172  -0.0471 145 GLU   A CG  
1075 C CD  . GLU   A 139 ? 0.8423 0.7548 0.7493 -0.1290 0.1094  -0.0439 145 GLU   A CD  
1076 O OE1 . GLU   A 139 ? 0.8635 0.7831 0.7670 -0.1327 0.0968  -0.0360 145 GLU   A OE1 
1077 O OE2 . GLU   A 139 ? 0.8811 0.7812 0.7637 -0.1398 0.1154  -0.0487 145 GLU   A OE2 
1078 N N1  . A1BSN B .   ? 0.2078 0.1651 0.2431 0.0154  -0.0019 -0.0133 201 A1BSN A N1  
1079 C C4  . A1BSN B .   ? 0.2907 0.2052 0.2612 0.0077  0.0347  -0.0424 201 A1BSN A C4  
1080 C C5  . A1BSN B .   ? 0.2655 0.1922 0.2615 0.0139  0.0309  -0.0356 201 A1BSN A C5  
1081 C C6  . A1BSN B .   ? 0.2709 0.1781 0.2516 0.0088  0.0247  -0.0419 201 A1BSN A C6  
1082 C C7  . A1BSN B .   ? 0.2660 0.1785 0.2449 0.0061  0.0113  -0.0378 201 A1BSN A C7  
1083 C C8  . A1BSN B .   ? 0.2502 0.1737 0.2507 0.0108  0.0075  -0.0313 201 A1BSN A C8  
1084 C C10 . A1BSN B .   ? 0.2282 0.1749 0.2626 0.0175  0.0051  -0.0183 201 A1BSN A C10 
1085 C C13 . A1BSN B .   ? 0.2835 0.2119 0.2364 0.0023  0.0361  -0.0377 201 A1BSN A C13 
1086 O O1  . A1BSN B .   ? 0.2278 0.1713 0.2752 0.0205  0.0084  -0.0170 201 A1BSN A O1  
1087 C C9  . A1BSN B .   ? 0.2341 0.1713 0.2499 0.0151  0.0096  -0.0255 201 A1BSN A C9  
1088 C C11 . A1BSN B .   ? 0.2404 0.1732 0.2609 0.0182  0.0215  -0.0286 201 A1BSN A C11 
1089 N N   . A1BSN B .   ? 0.2584 0.1808 0.2574 0.0140  0.0263  -0.0357 201 A1BSN A N   
1090 O O   . A1BSN B .   ? 0.2420 0.1816 0.2538 0.0173  0.0312  -0.0298 201 A1BSN A O   
1091 C C3  . A1BSN B .   ? 0.2814 0.2044 0.2458 0.0057  0.0310  -0.0390 201 A1BSN A C3  
1092 C C2  . A1BSN B .   ? 0.2733 0.2068 0.2409 0.0054  0.0196  -0.0329 201 A1BSN A C2  
1093 C C12 . A1BSN B .   ? 0.2828 0.2031 0.2396 0.0040  0.0401  -0.0418 201 A1BSN A C12 
1094 N N2  . A1BSN B .   ? 0.2726 0.2101 0.2287 0.0022  0.0247  -0.0319 201 A1BSN A N2  
1095 C C1  . A1BSN B .   ? 0.2679 0.2078 0.2314 0.0039  0.0171  -0.0298 201 A1BSN A C1  
1096 C C   . A1BSN B .   ? 0.2695 0.2184 0.2373 0.0037  0.0074  -0.0243 201 A1BSN A C   
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