data_7I64
# 
_entry.id   7I64 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   7I64         pdb_00007i64 10.2210/pdb7i64/pdb 
WWPDB D_1001408363 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-04-02 ? 
2 'Structure model' 1 1 2025-04-09 ? 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Refinement description' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            pdbx_initial_refinement_model 
# 
_pdbx_database_status.entry_id                        7I64 
_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   2025-03-12 
_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-(methylsulfanyl)pyridin-3-yl]acetyl}piperidine-3-carboxamide' 293.385   1   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                                65.409    1   ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                      78.133    1   ?         ? ? ? 
5 water       nat water                                                                     18.015    120 ?         ? ? ? 
# 
_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-(methylsulfanyl)pyridin-3-yl]acetyl}piperidine-3-carboxamide' A1B4J 
3 'ZINC ION'                                                                ZN    
4 'DIMETHYL SULFOXIDE'                                                      DMS   
5 water                                                                     HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   GLY n 
1 3   ALA n 
1 4   ILE n 
1 5   TYR n 
1 6   VAL n 
1 7   GLY n 
1 8   ASN n 
1 9   TYR n 
1 10  ARG n 
1 11  VAL n 
1 12  VAL n 
1 13  ASN n 
1 14  ARG n 
1 15  HIS n 
1 16  LEU n 
1 17  ALA n 
1 18  THR n 
1 19  HIS n 
1 20  ASN n 
1 21  ASP n 
1 22  TRP n 
1 23  ALA n 
1 24  ASN n 
1 25  LEU n 
1 26  VAL n 
1 27  TRP n 
1 28  GLU n 
1 29  ASP n 
1 30  SER n 
1 31  SER n 
1 32  ARG n 
1 33  ASP n 
1 34  LEU n 
1 35  LEU n 
1 36  VAL n 
1 37  SER n 
1 38  SER n 
1 39  THR n 
1 40  THR n 
1 41  ALA n 
1 42  GLN n 
1 43  GLY n 
1 44  CYS n 
1 45  ASP n 
1 46  THR n 
1 47  ILE n 
1 48  ALA n 
1 49  ARG n 
1 50  CYS n 
1 51  ASP n 
1 52  CYS n 
1 53  GLN n 
1 54  THR n 
1 55  GLY n 
1 56  VAL n 
1 57  TYR n 
1 58  TYR n 
1 59  CYS n 
1 60  SER n 
1 61  SER n 
1 62  ARG n 
1 63  ARG n 
1 64  LYS n 
1 65  HIS n 
1 66  TYR n 
1 67  PRO n 
1 68  VAL n 
1 69  SER n 
1 70  PHE n 
1 71  SER n 
1 72  LYS n 
1 73  PRO n 
1 74  SER n 
1 75  LEU n 
1 76  ILE n 
1 77  PHE n 
1 78  VAL n 
1 79  GLU n 
1 80  ALA n 
1 81  SER n 
1 82  GLU n 
1 83  TYR n 
1 84  TYR n 
1 85  PRO n 
1 86  ALA n 
1 87  ARG n 
1 88  TYR n 
1 89  GLN n 
1 90  SER n 
1 91  HIS n 
1 92  LEU n 
1 93  MET n 
1 94  LEU n 
1 95  ALA n 
1 96  VAL n 
1 97  GLY n 
1 98  HIS n 
1 99  SER n 
1 100 GLU n 
1 101 PRO n 
1 102 GLY n 
1 103 ASP n 
1 104 CYS n 
1 105 GLY n 
1 106 GLY n 
1 107 ILE n 
1 108 LEU n 
1 109 ARG n 
1 110 CYS n 
1 111 GLN n 
1 112 HIS n 
1 113 GLY n 
1 114 VAL n 
1 115 VAL n 
1 116 GLY n 
1 117 ILE n 
1 118 VAL n 
1 119 SER n 
1 120 THR n 
1 121 GLY n 
1 122 GLY n 
1 123 ASN n 
1 124 GLY n 
1 125 LEU n 
1 126 VAL n 
1 127 GLY n 
1 128 PHE n 
1 129 ALA n 
1 130 ASP n 
1 131 VAL n 
1 132 ARG n 
1 133 ASP n 
1 134 LEU n 
1 135 LEU n 
1 136 TRP n 
1 137 LEU n 
1 138 ASP n 
1 139 GLU n 
1 140 GLU n 
1 141 ALA n 
1 142 MET n 
1 143 GLU n 
1 144 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   144 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Coxsackievirus A16' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     31704 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1B4J non-polymer         . '(3S)-1-{[2-(methylsulfanyl)pyridin-3-yl]acetyl}piperidine-3-carboxamide' ? 'C14 H19 N3 O2 S' 293.385 
ALA   'L-peptide linking' y ALANINE                                                                   ? 'C3 H7 N O2'      89.093  
ARG   'L-peptide linking' y ARGININE                                                                  ? 'C6 H15 N4 O2 1'  175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                ? 'C4 H8 N2 O3'     132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                           ? 'C4 H7 N O4'      133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                  ? 'C3 H7 N O2 S'    121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                      ? 'C2 H6 O S'       78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                                 ? 'C5 H10 N2 O3'    146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                           ? 'C5 H9 N O4'      147.129 
GLY   'peptide linking'   y GLYCINE                                                                   ? 'C2 H5 N O2'      75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                 ? 'C6 H10 N3 O2 1'  156.162 
HOH   non-polymer         . WATER                                                                     ? 'H2 O'            18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                ? 'C6 H13 N O2'     131.173 
LEU   'L-peptide linking' y LEUCINE                                                                   ? 'C6 H13 N O2'     131.173 
LYS   'L-peptide linking' y LYSINE                                                                    ? 'C6 H15 N2 O2 1'  147.195 
MET   'L-peptide linking' y METHIONINE                                                                ? 'C5 H11 N O2 S'   149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                             ? 'C9 H11 N O2'     165.189 
PRO   'L-peptide linking' y PROLINE                                                                   ? 'C5 H9 N O2'      115.130 
SER   'L-peptide linking' y SERINE                                                                    ? 'C3 H7 N O3'      105.093 
THR   'L-peptide linking' y THREONINE                                                                 ? 'C4 H9 N O3'      119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                ? 'C11 H12 N2 O2'   204.225 
TYR   'L-peptide linking' y TYROSINE                                                                  ? 'C9 H11 N O3'     181.189 
VAL   'L-peptide linking' y VALINE                                                                    ? 'C5 H11 N O2'     117.146 
ZN    non-polymer         . 'ZINC ION'                                                                ? 'Zn 2'            65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   7   7   SER SER A . n 
A 1 2   GLY 2   8   8   GLY GLY A . n 
A 1 3   ALA 3   9   9   ALA ALA A . n 
A 1 4   ILE 4   10  10  ILE ILE A . n 
A 1 5   TYR 5   11  11  TYR TYR A . n 
A 1 6   VAL 6   12  12  VAL VAL A . n 
A 1 7   GLY 7   13  13  GLY GLY A . n 
A 1 8   ASN 8   14  14  ASN ASN A . n 
A 1 9   TYR 9   15  15  TYR TYR A . n 
A 1 10  ARG 10  16  16  ARG ARG A . n 
A 1 11  VAL 11  17  17  VAL VAL A . n 
A 1 12  VAL 12  18  18  VAL VAL A . n 
A 1 13  ASN 13  19  19  ASN ASN A . n 
A 1 14  ARG 14  20  20  ARG ARG A . n 
A 1 15  HIS 15  21  21  HIS HIS A . n 
A 1 16  LEU 16  22  22  LEU LEU A . n 
A 1 17  ALA 17  23  23  ALA ALA A . n 
A 1 18  THR 18  24  24  THR THR A . n 
A 1 19  HIS 19  25  25  HIS HIS A . n 
A 1 20  ASN 20  26  26  ASN ASN A . n 
A 1 21  ASP 21  27  27  ASP ASP A . n 
A 1 22  TRP 22  28  28  TRP TRP A . n 
A 1 23  ALA 23  29  29  ALA ALA A . n 
A 1 24  ASN 24  30  30  ASN ASN A . n 
A 1 25  LEU 25  31  31  LEU LEU A . n 
A 1 26  VAL 26  32  32  VAL VAL A . n 
A 1 27  TRP 27  33  33  TRP TRP A . n 
A 1 28  GLU 28  34  34  GLU GLU A . n 
A 1 29  ASP 29  35  35  ASP ASP A . n 
A 1 30  SER 30  36  36  SER SER A . n 
A 1 31  SER 31  37  37  SER SER A . n 
A 1 32  ARG 32  38  38  ARG ARG A . n 
A 1 33  ASP 33  39  39  ASP ASP A . n 
A 1 34  LEU 34  40  40  LEU LEU A . n 
A 1 35  LEU 35  41  41  LEU LEU A . n 
A 1 36  VAL 36  42  42  VAL VAL A . n 
A 1 37  SER 37  43  43  SER SER A . n 
A 1 38  SER 38  44  44  SER SER A . n 
A 1 39  THR 39  45  45  THR THR A . n 
A 1 40  THR 40  46  46  THR THR A . n 
A 1 41  ALA 41  47  47  ALA ALA A . n 
A 1 42  GLN 42  48  48  GLN GLN A . n 
A 1 43  GLY 43  49  49  GLY GLY A . n 
A 1 44  CYS 44  50  50  CYS CYS A . n 
A 1 45  ASP 45  51  51  ASP ASP A . n 
A 1 46  THR 46  52  52  THR THR A . n 
A 1 47  ILE 47  53  53  ILE ILE A . n 
A 1 48  ALA 48  54  54  ALA ALA A . n 
A 1 49  ARG 49  55  55  ARG ARG A . n 
A 1 50  CYS 50  56  56  CYS CYS A . n 
A 1 51  ASP 51  57  57  ASP ASP A . n 
A 1 52  CYS 52  58  58  CYS CYS A . n 
A 1 53  GLN 53  59  59  GLN GLN A . n 
A 1 54  THR 54  60  60  THR THR A . n 
A 1 55  GLY 55  61  61  GLY GLY A . n 
A 1 56  VAL 56  62  62  VAL VAL A . n 
A 1 57  TYR 57  63  63  TYR TYR A . n 
A 1 58  TYR 58  64  64  TYR TYR A . n 
A 1 59  CYS 59  65  65  CYS CYS A . n 
A 1 60  SER 60  66  66  SER SER A . n 
A 1 61  SER 61  67  67  SER SER A . n 
A 1 62  ARG 62  68  68  ARG ARG A . n 
A 1 63  ARG 63  69  69  ARG ARG A . n 
A 1 64  LYS 64  70  70  LYS LYS A . n 
A 1 65  HIS 65  71  71  HIS HIS A . n 
A 1 66  TYR 66  72  72  TYR TYR A . n 
A 1 67  PRO 67  73  73  PRO PRO A . n 
A 1 68  VAL 68  74  74  VAL VAL A . n 
A 1 69  SER 69  75  75  SER SER A . n 
A 1 70  PHE 70  76  76  PHE PHE A . n 
A 1 71  SER 71  77  77  SER SER A . n 
A 1 72  LYS 72  78  78  LYS LYS A . n 
A 1 73  PRO 73  79  79  PRO PRO A . n 
A 1 74  SER 74  80  80  SER SER A . n 
A 1 75  LEU 75  81  81  LEU LEU A . n 
A 1 76  ILE 76  82  82  ILE ILE A . n 
A 1 77  PHE 77  83  83  PHE PHE A . n 
A 1 78  VAL 78  84  84  VAL VAL A . n 
A 1 79  GLU 79  85  85  GLU GLU A . n 
A 1 80  ALA 80  86  86  ALA ALA A . n 
A 1 81  SER 81  87  87  SER SER A . n 
A 1 82  GLU 82  88  88  GLU GLU A . n 
A 1 83  TYR 83  89  89  TYR TYR A . n 
A 1 84  TYR 84  90  90  TYR TYR A . n 
A 1 85  PRO 85  91  91  PRO PRO A . n 
A 1 86  ALA 86  92  92  ALA ALA A . n 
A 1 87  ARG 87  93  93  ARG ARG A . n 
A 1 88  TYR 88  94  94  TYR TYR A . n 
A 1 89  GLN 89  95  95  GLN GLN A . n 
A 1 90  SER 90  96  96  SER SER A . n 
A 1 91  HIS 91  97  97  HIS HIS A . n 
A 1 92  LEU 92  98  98  LEU LEU A . n 
A 1 93  MET 93  99  99  MET MET A . n 
A 1 94  LEU 94  100 100 LEU LEU A . n 
A 1 95  ALA 95  101 101 ALA ALA A . n 
A 1 96  VAL 96  102 102 VAL VAL A . n 
A 1 97  GLY 97  103 103 GLY GLY A . n 
A 1 98  HIS 98  104 104 HIS HIS A . n 
A 1 99  SER 99  105 105 SER SER A . n 
A 1 100 GLU 100 106 106 GLU GLU A . n 
A 1 101 PRO 101 107 107 PRO PRO A . n 
A 1 102 GLY 102 108 108 GLY GLY A . n 
A 1 103 ASP 103 109 109 ASP ASP A . n 
A 1 104 CYS 104 110 110 CYS CYS A . n 
A 1 105 GLY 105 111 111 GLY GLY A . n 
A 1 106 GLY 106 112 112 GLY GLY A . n 
A 1 107 ILE 107 113 113 ILE ILE A . n 
A 1 108 LEU 108 114 114 LEU LEU A . n 
A 1 109 ARG 109 115 115 ARG ARG A . n 
A 1 110 CYS 110 116 116 CYS CYS A . n 
A 1 111 GLN 111 117 117 GLN GLN A . n 
A 1 112 HIS 112 118 118 HIS HIS A . n 
A 1 113 GLY 113 119 119 GLY GLY A . n 
A 1 114 VAL 114 120 120 VAL VAL A . n 
A 1 115 VAL 115 121 121 VAL VAL A . n 
A 1 116 GLY 116 122 122 GLY GLY A . n 
A 1 117 ILE 117 123 123 ILE ILE A . n 
A 1 118 VAL 118 124 124 VAL VAL A . n 
A 1 119 SER 119 125 125 SER SER A . n 
A 1 120 THR 120 126 126 THR THR A . n 
A 1 121 GLY 121 127 127 GLY GLY A . n 
A 1 122 GLY 122 128 128 GLY GLY A . n 
A 1 123 ASN 123 129 129 ASN ASN A . n 
A 1 124 GLY 124 130 130 GLY GLY A . n 
A 1 125 LEU 125 131 131 LEU LEU A . n 
A 1 126 VAL 126 132 132 VAL VAL A . n 
A 1 127 GLY 127 133 133 GLY GLY A . n 
A 1 128 PHE 128 134 134 PHE PHE A . n 
A 1 129 ALA 129 135 135 ALA ALA A . n 
A 1 130 ASP 130 136 136 ASP ASP A . n 
A 1 131 VAL 131 137 137 VAL VAL A . n 
A 1 132 ARG 132 138 138 ARG ARG A . n 
A 1 133 ASP 133 139 139 ASP ASP A . n 
A 1 134 LEU 134 140 140 LEU LEU A . n 
A 1 135 LEU 135 141 141 LEU LEU A . n 
A 1 136 TRP 136 142 142 TRP TRP A . n 
A 1 137 LEU 137 143 143 LEU LEU A . n 
A 1 138 ASP 138 144 144 ASP ASP A . n 
A 1 139 GLU 139 145 145 GLU GLU A . n 
A 1 140 GLU 140 146 ?   ?   ?   A . n 
A 1 141 ALA 141 147 ?   ?   ?   A . n 
A 1 142 MET 142 148 ?   ?   ?   A . n 
A 1 143 GLU 143 149 ?   ?   ?   A . n 
A 1 144 GLN 144 150 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1B4J 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1B4J 
_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 A1B4J 1   201 201 A1B4J LIG A . 
C 3 ZN    1   202 1   ZN    ZN  A . 
D 4 DMS   1   203 2   DMS   DMS A . 
E 5 HOH   1   301 85  HOH   HOH A . 
E 5 HOH   2   302 105 HOH   HOH A . 
E 5 HOH   3   303 37  HOH   HOH A . 
E 5 HOH   4   304 36  HOH   HOH A . 
E 5 HOH   5   305 81  HOH   HOH A . 
E 5 HOH   6   306 18  HOH   HOH A . 
E 5 HOH   7   307 89  HOH   HOH A . 
E 5 HOH   8   308 60  HOH   HOH A . 
E 5 HOH   9   309 32  HOH   HOH A . 
E 5 HOH   10  310 59  HOH   HOH A . 
E 5 HOH   11  311 29  HOH   HOH A . 
E 5 HOH   12  312 76  HOH   HOH A . 
E 5 HOH   13  313 14  HOH   HOH A . 
E 5 HOH   14  314 71  HOH   HOH A . 
E 5 HOH   15  315 98  HOH   HOH A . 
E 5 HOH   16  316 9   HOH   HOH A . 
E 5 HOH   17  317 47  HOH   HOH A . 
E 5 HOH   18  318 8   HOH   HOH A . 
E 5 HOH   19  319 7   HOH   HOH A . 
E 5 HOH   20  320 50  HOH   HOH A . 
E 5 HOH   21  321 22  HOH   HOH A . 
E 5 HOH   22  322 25  HOH   HOH A . 
E 5 HOH   23  323 42  HOH   HOH A . 
E 5 HOH   24  324 13  HOH   HOH A . 
E 5 HOH   25  325 27  HOH   HOH A . 
E 5 HOH   26  326 54  HOH   HOH A . 
E 5 HOH   27  327 35  HOH   HOH A . 
E 5 HOH   28  328 97  HOH   HOH A . 
E 5 HOH   29  329 78  HOH   HOH A . 
E 5 HOH   30  330 19  HOH   HOH A . 
E 5 HOH   31  331 75  HOH   HOH A . 
E 5 HOH   32  332 12  HOH   HOH A . 
E 5 HOH   33  333 83  HOH   HOH A . 
E 5 HOH   34  334 73  HOH   HOH A . 
E 5 HOH   35  335 93  HOH   HOH A . 
E 5 HOH   36  336 91  HOH   HOH A . 
E 5 HOH   37  337 94  HOH   HOH A . 
E 5 HOH   38  338 90  HOH   HOH A . 
E 5 HOH   39  339 48  HOH   HOH A . 
E 5 HOH   40  340 11  HOH   HOH A . 
E 5 HOH   41  341 16  HOH   HOH A . 
E 5 HOH   42  342 2   HOH   HOH A . 
E 5 HOH   43  343 86  HOH   HOH A . 
E 5 HOH   44  344 117 HOH   HOH A . 
E 5 HOH   45  345 17  HOH   HOH A . 
E 5 HOH   46  346 39  HOH   HOH A . 
E 5 HOH   47  347 68  HOH   HOH A . 
E 5 HOH   48  348 51  HOH   HOH A . 
E 5 HOH   49  349 49  HOH   HOH A . 
E 5 HOH   50  350 45  HOH   HOH A . 
E 5 HOH   51  351 77  HOH   HOH A . 
E 5 HOH   52  352 34  HOH   HOH A . 
E 5 HOH   53  353 21  HOH   HOH A . 
E 5 HOH   54  354 74  HOH   HOH A . 
E 5 HOH   55  355 58  HOH   HOH A . 
E 5 HOH   56  356 23  HOH   HOH A . 
E 5 HOH   57  357 40  HOH   HOH A . 
E 5 HOH   58  358 24  HOH   HOH A . 
E 5 HOH   59  359 10  HOH   HOH A . 
E 5 HOH   60  360 72  HOH   HOH A . 
E 5 HOH   61  361 4   HOH   HOH A . 
E 5 HOH   62  362 109 HOH   HOH A . 
E 5 HOH   63  363 79  HOH   HOH A . 
E 5 HOH   64  364 116 HOH   HOH A . 
E 5 HOH   65  365 30  HOH   HOH A . 
E 5 HOH   66  366 112 HOH   HOH A . 
E 5 HOH   67  367 55  HOH   HOH A . 
E 5 HOH   68  368 92  HOH   HOH A . 
E 5 HOH   69  369 88  HOH   HOH A . 
E 5 HOH   70  370 95  HOH   HOH A . 
E 5 HOH   71  371 80  HOH   HOH A . 
E 5 HOH   72  372 82  HOH   HOH A . 
E 5 HOH   73  373 56  HOH   HOH A . 
E 5 HOH   74  374 53  HOH   HOH A . 
E 5 HOH   75  375 103 HOH   HOH A . 
E 5 HOH   76  376 33  HOH   HOH A . 
E 5 HOH   77  377 20  HOH   HOH A . 
E 5 HOH   78  378 84  HOH   HOH A . 
E 5 HOH   79  379 111 HOH   HOH A . 
E 5 HOH   80  380 67  HOH   HOH A . 
E 5 HOH   81  381 5   HOH   HOH A . 
E 5 HOH   82  382 3   HOH   HOH A . 
E 5 HOH   83  383 96  HOH   HOH A . 
E 5 HOH   84  384 6   HOH   HOH A . 
E 5 HOH   85  385 110 HOH   HOH A . 
E 5 HOH   86  386 57  HOH   HOH A . 
E 5 HOH   87  387 43  HOH   HOH A . 
E 5 HOH   88  388 46  HOH   HOH A . 
E 5 HOH   89  389 15  HOH   HOH A . 
E 5 HOH   90  390 26  HOH   HOH A . 
E 5 HOH   91  391 115 HOH   HOH A . 
E 5 HOH   92  392 119 HOH   HOH A . 
E 5 HOH   93  393 66  HOH   HOH A . 
E 5 HOH   94  394 118 HOH   HOH A . 
E 5 HOH   95  395 113 HOH   HOH A . 
E 5 HOH   96  396 107 HOH   HOH A . 
E 5 HOH   97  397 121 HOH   HOH A . 
E 5 HOH   98  398 28  HOH   HOH A . 
E 5 HOH   99  399 87  HOH   HOH A . 
E 5 HOH   100 400 106 HOH   HOH A . 
E 5 HOH   101 401 63  HOH   HOH A . 
E 5 HOH   102 402 70  HOH   HOH A . 
E 5 HOH   103 403 41  HOH   HOH A . 
E 5 HOH   104 404 38  HOH   HOH A . 
E 5 HOH   105 405 122 HOH   HOH A . 
E 5 HOH   106 406 64  HOH   HOH A . 
E 5 HOH   107 407 108 HOH   HOH A . 
E 5 HOH   108 408 31  HOH   HOH A . 
E 5 HOH   109 409 104 HOH   HOH A . 
E 5 HOH   110 410 61  HOH   HOH A . 
E 5 HOH   111 411 52  HOH   HOH A . 
E 5 HOH   112 412 101 HOH   HOH A . 
E 5 HOH   113 413 102 HOH   HOH A . 
E 5 HOH   114 414 99  HOH   HOH A . 
E 5 HOH   115 415 100 HOH   HOH A . 
E 5 HOH   116 416 44  HOH   HOH A . 
E 5 HOH   117 417 69  HOH   HOH A . 
E 5 HOH   118 418 114 HOH   HOH A . 
E 5 HOH   119 419 120 HOH   HOH A . 
E 5 HOH   120 420 62  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           7I64 
_cell.length_a           73.513 
_cell.length_b           61.796 
_cell.length_c           32.941 
_cell.angle_alpha        90.00 
_cell.angle_beta         92.53 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I64 
_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          7I64 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.35 
_exptl_crystal.density_percent_sol   47.70 
_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   2025-01-24 
_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   0.92204 
_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        0.92204 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7I64 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             47.30 
_reflns.d_resolution_high            1.46 
_reflns.number_obs                   25399 
_reflns.percent_possible_obs         99.3 
_reflns.pdbx_Rmerge_I_obs            0.111 
_reflns.pdbx_netI_over_sigmaI        8.0 
_reflns.pdbx_redundancy              6.5 
_reflns.pdbx_Rrim_I_all              0.120 
_reflns.pdbx_Rpim_I_all              0.046 
_reflns.pdbx_CC_half                 0.992 
_reflns.pdbx_number_measured_all     165477 
_reflns.pdbx_chi_squared             0.39 
_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                  1.46 
_reflns_shell.d_res_low                   1.49 
_reflns_shell.number_measured_all         5990 
_reflns_shell.number_unique_obs           1234 
_reflns_shell.Rmerge_I_obs                2.485 
_reflns_shell.pdbx_chi_squared            0.07 
_reflns_shell.pdbx_redundancy             4.9 
_reflns_shell.percent_possible_obs        93.8 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.3 
_reflns_shell.pdbx_Rrim_I_all             2.796 
_reflns_shell.pdbx_Rpim_I_all             1.253 
_reflns_shell.pdbx_CC_half                0.267 
_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                                 7I64 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     24393 
_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                             16.45 
_refine.ls_d_res_high                            1.460 
_refine.ls_percent_reflns_obs                    95.3 
_refine.ls_R_factor_obs                          0.2072 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2063 
_refine.ls_R_factor_R_free                       0.2248 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.850 
_refine.ls_number_reflns_R_free                  1184 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.955 
_refine.correlation_coeff_Fo_to_Fc_free          0.950 
_refine.B_iso_mean                               30.18 
_refine.aniso_B[1][1]                            -5.10970 
_refine.aniso_B[2][2]                            0.64170 
_refine.aniso_B[3][3]                            4.46800 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            1.06660 
_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             0.076 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.074 
_refine.pdbx_overall_SU_R_Blow_DPI               0.079 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.076 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7I64 
_refine_analyze.Luzzati_coordinate_error_obs    0.23 
_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         25 
_refine_hist.number_atoms_solvent             120 
_refine_hist.number_atoms_total               1219 
_refine_hist.d_res_high                       1.460 
_refine_hist.d_res_low                        16.45 
# 
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                  0.011 ? 2.00  1128 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               0.95  ? 2.00  1534 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  377  'X-RAY DIFFRACTION' SINUSOIDAL   
t_incorr_chiral_ct        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_pseud_angle             ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_trig_c_planes           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_gen_planes              ?     ? 5.00  204  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1128 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           3.94  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           14.63 ? ?     ?    '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  890  'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   51 
_refine_ls_shell.d_res_high                       1.46 
_refine_ls_shell.d_res_low                        1.48 
_refine_ls_shell.number_reflns_R_work             472 
_refine_ls_shell.R_factor_R_work                  0.3493 
_refine_ls_shell.percent_reflns_obs               53.30 
_refine_ls_shell.R_factor_R_free                  0.3297 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            3.28 
_refine_ls_shell.number_reflns_R_free             16 
_refine_ls_shell.number_reflns_all                488 
_refine_ls_shell.R_factor_all                     0.3486 
# 
_struct.entry_id                  7I64 
_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-0037666-001 (A71EV2A-x4918)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I64 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    POLG_CX16G 
_struct_ref.pdbx_db_accession          Q65900 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_struct_ref.pdbx_align_begin           869 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              7I64 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 144 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q65900 
_struct_ref_seq.db_align_beg                  869 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1012 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       7 
_struct_ref_seq.pdbx_auth_seq_align_end       150 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2 AA2 THR A 18  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
HELX_P HELX_P3 AA3 SER A 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 ? ? ? ? ? ? ? 2.351 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.329 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.417 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 C ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.213 ? ? 
# 
_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_555 113.3 ? 
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_555 107.9 ? 
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_555 116.4 ? 
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_555 105.8 ? 
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_555 100.6 ? 
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_555 112.3 ? 
# 
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 VAL A 126 ? O VAL A 132 N ALA A 95  ? N ALA A 101 
AA2 6 7 O GLN A 89  ? O GLN A 95  N ILE A 76  ? N ILE A 82  
# 
_pdbx_entry_details.entry_id                   7I64 
_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     301 
_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     301 
_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              1.01 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    ASN 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     14 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -95.41 
_pdbx_validate_torsion.psi             32.35 
# 
_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         15.4041 
_pdbx_refine_tls.origin_y         6.6230 
_pdbx_refine_tls.origin_z         14.3576 
_pdbx_refine_tls.T[1][1]          -0.0413 
_pdbx_refine_tls.T[2][2]          -0.0389 
_pdbx_refine_tls.T[3][3]          0.0089 
_pdbx_refine_tls.T[1][2]          0.0006 
_pdbx_refine_tls.T[1][3]          0.0011 
_pdbx_refine_tls.T[2][3]          -0.0094 
_pdbx_refine_tls.L[1][1]          0.8890 
_pdbx_refine_tls.L[2][2]          4.7188 
_pdbx_refine_tls.L[3][3]          0.6206 
_pdbx_refine_tls.L[1][2]          1.5279 
_pdbx_refine_tls.L[1][3]          -0.5256 
_pdbx_refine_tls.L[2][3]          -1.7247 
_pdbx_refine_tls.S[1][1]          -0.0781 
_pdbx_refine_tls.S[1][2]          0.0691 
_pdbx_refine_tls.S[1][3]          0.0009 
_pdbx_refine_tls.S[2][1]          0.1930 
_pdbx_refine_tls.S[2][2]          0.0935 
_pdbx_refine_tls.S[2][3]          -0.1351 
_pdbx_refine_tls.S[3][1]          -0.0473 
_pdbx_refine_tls.S[3][2]          -0.1005 
_pdbx_refine_tls.S[3][3]          -0.0154 
# 
_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 
A1B4J N1   N  N N 1   
A1B4J C4   C  Y N 2   
A1B4J C5   C  Y N 3   
A1B4J C6   C  N N 4   
A1B4J C7   C  N N 5   
A1B4J C8   C  N N 6   
A1B4J C10  C  N N 7   
A1B4J C13  C  N N 8   
A1B4J O1   O  N N 9   
A1B4J C12  C  N N 10  
A1B4J N2   N  N N 11  
A1B4J C11  C  N S 12  
A1B4J C9   C  N N 13  
A1B4J O    O  N N 14  
A1B4J C1   C  Y N 15  
A1B4J S    S  N N 16  
A1B4J C    C  N N 17  
A1B4J C3   C  Y N 18  
A1B4J C2   C  Y N 19  
A1B4J N    N  Y N 20  
A1B4J H6   H  N N 21  
A1B4J H7   H  N N 22  
A1B4J H8   H  N N 23  
A1B4J H10  H  N N 24  
A1B4J H9   H  N N 25  
A1B4J H13  H  N N 26  
A1B4J H14  H  N N 27  
A1B4J H17  H  N N 28  
A1B4J H18  H  N N 29  
A1B4J H16  H  N N 30  
A1B4J H15  H  N N 31  
A1B4J H    H  N N 32  
A1B4J H11  H  N N 33  
A1B4J H12  H  N N 34  
A1B4J H2   H  N N 35  
A1B4J H1   H  N N 36  
A1B4J H3   H  N N 37  
A1B4J H5   H  N N 38  
A1B4J H4   H  N N 39  
ALA   N    N  N N 40  
ALA   CA   C  N S 41  
ALA   C    C  N N 42  
ALA   O    O  N N 43  
ALA   CB   C  N N 44  
ALA   OXT  O  N N 45  
ALA   H    H  N N 46  
ALA   H2   H  N N 47  
ALA   HA   H  N N 48  
ALA   HB1  H  N N 49  
ALA   HB2  H  N N 50  
ALA   HB3  H  N N 51  
ALA   HXT  H  N N 52  
ARG   N    N  N N 53  
ARG   CA   C  N S 54  
ARG   C    C  N N 55  
ARG   O    O  N N 56  
ARG   CB   C  N N 57  
ARG   CG   C  N N 58  
ARG   CD   C  N N 59  
ARG   NE   N  N N 60  
ARG   CZ   C  N N 61  
ARG   NH1  N  N N 62  
ARG   NH2  N  N N 63  
ARG   OXT  O  N N 64  
ARG   H    H  N N 65  
ARG   H2   H  N N 66  
ARG   HA   H  N N 67  
ARG   HB2  H  N N 68  
ARG   HB3  H  N N 69  
ARG   HG2  H  N N 70  
ARG   HG3  H  N N 71  
ARG   HD2  H  N N 72  
ARG   HD3  H  N N 73  
ARG   HE   H  N N 74  
ARG   HH11 H  N N 75  
ARG   HH12 H  N N 76  
ARG   HH21 H  N N 77  
ARG   HH22 H  N N 78  
ARG   HXT  H  N N 79  
ASN   N    N  N N 80  
ASN   CA   C  N S 81  
ASN   C    C  N N 82  
ASN   O    O  N N 83  
ASN   CB   C  N N 84  
ASN   CG   C  N N 85  
ASN   OD1  O  N N 86  
ASN   ND2  N  N N 87  
ASN   OXT  O  N N 88  
ASN   H    H  N N 89  
ASN   H2   H  N N 90  
ASN   HA   H  N N 91  
ASN   HB2  H  N N 92  
ASN   HB3  H  N N 93  
ASN   HD21 H  N N 94  
ASN   HD22 H  N N 95  
ASN   HXT  H  N N 96  
ASP   N    N  N N 97  
ASP   CA   C  N S 98  
ASP   C    C  N N 99  
ASP   O    O  N N 100 
ASP   CB   C  N N 101 
ASP   CG   C  N N 102 
ASP   OD1  O  N N 103 
ASP   OD2  O  N N 104 
ASP   OXT  O  N N 105 
ASP   H    H  N N 106 
ASP   H2   H  N N 107 
ASP   HA   H  N N 108 
ASP   HB2  H  N N 109 
ASP   HB3  H  N N 110 
ASP   HD2  H  N N 111 
ASP   HXT  H  N N 112 
CYS   N    N  N N 113 
CYS   CA   C  N R 114 
CYS   C    C  N N 115 
CYS   O    O  N N 116 
CYS   CB   C  N N 117 
CYS   SG   S  N N 118 
CYS   OXT  O  N N 119 
CYS   H    H  N N 120 
CYS   H2   H  N N 121 
CYS   HA   H  N N 122 
CYS   HB2  H  N N 123 
CYS   HB3  H  N N 124 
CYS   HG   H  N N 125 
CYS   HXT  H  N N 126 
DMS   S    S  N N 127 
DMS   O    O  N N 128 
DMS   C1   C  N N 129 
DMS   C2   C  N N 130 
DMS   H11  H  N N 131 
DMS   H12  H  N N 132 
DMS   H13  H  N N 133 
DMS   H21  H  N N 134 
DMS   H22  H  N N 135 
DMS   H23  H  N N 136 
GLN   N    N  N N 137 
GLN   CA   C  N S 138 
GLN   C    C  N N 139 
GLN   O    O  N N 140 
GLN   CB   C  N N 141 
GLN   CG   C  N N 142 
GLN   CD   C  N N 143 
GLN   OE1  O  N N 144 
GLN   NE2  N  N N 145 
GLN   OXT  O  N N 146 
GLN   H    H  N N 147 
GLN   H2   H  N N 148 
GLN   HA   H  N N 149 
GLN   HB2  H  N N 150 
GLN   HB3  H  N N 151 
GLN   HG2  H  N N 152 
GLN   HG3  H  N N 153 
GLN   HE21 H  N N 154 
GLN   HE22 H  N N 155 
GLN   HXT  H  N N 156 
GLU   N    N  N N 157 
GLU   CA   C  N S 158 
GLU   C    C  N N 159 
GLU   O    O  N N 160 
GLU   CB   C  N N 161 
GLU   CG   C  N N 162 
GLU   CD   C  N N 163 
GLU   OE1  O  N N 164 
GLU   OE2  O  N N 165 
GLU   OXT  O  N N 166 
GLU   H    H  N N 167 
GLU   H2   H  N N 168 
GLU   HA   H  N N 169 
GLU   HB2  H  N N 170 
GLU   HB3  H  N N 171 
GLU   HG2  H  N N 172 
GLU   HG3  H  N N 173 
GLU   HE2  H  N N 174 
GLU   HXT  H  N N 175 
GLY   N    N  N N 176 
GLY   CA   C  N N 177 
GLY   C    C  N N 178 
GLY   O    O  N N 179 
GLY   OXT  O  N N 180 
GLY   H    H  N N 181 
GLY   H2   H  N N 182 
GLY   HA2  H  N N 183 
GLY   HA3  H  N N 184 
GLY   HXT  H  N N 185 
HIS   N    N  N N 186 
HIS   CA   C  N S 187 
HIS   C    C  N N 188 
HIS   O    O  N N 189 
HIS   CB   C  N N 190 
HIS   CG   C  Y N 191 
HIS   ND1  N  Y N 192 
HIS   CD2  C  Y N 193 
HIS   CE1  C  Y N 194 
HIS   NE2  N  Y N 195 
HIS   OXT  O  N N 196 
HIS   H    H  N N 197 
HIS   H2   H  N N 198 
HIS   HA   H  N N 199 
HIS   HB2  H  N N 200 
HIS   HB3  H  N N 201 
HIS   HD1  H  N N 202 
HIS   HD2  H  N N 203 
HIS   HE1  H  N N 204 
HIS   HE2  H  N N 205 
HIS   HXT  H  N N 206 
HOH   O    O  N N 207 
HOH   H1   H  N N 208 
HOH   H2   H  N N 209 
ILE   N    N  N N 210 
ILE   CA   C  N S 211 
ILE   C    C  N N 212 
ILE   O    O  N N 213 
ILE   CB   C  N S 214 
ILE   CG1  C  N N 215 
ILE   CG2  C  N N 216 
ILE   CD1  C  N N 217 
ILE   OXT  O  N N 218 
ILE   H    H  N N 219 
ILE   H2   H  N N 220 
ILE   HA   H  N N 221 
ILE   HB   H  N N 222 
ILE   HG12 H  N N 223 
ILE   HG13 H  N N 224 
ILE   HG21 H  N N 225 
ILE   HG22 H  N N 226 
ILE   HG23 H  N N 227 
ILE   HD11 H  N N 228 
ILE   HD12 H  N N 229 
ILE   HD13 H  N N 230 
ILE   HXT  H  N N 231 
LEU   N    N  N N 232 
LEU   CA   C  N S 233 
LEU   C    C  N N 234 
LEU   O    O  N N 235 
LEU   CB   C  N N 236 
LEU   CG   C  N N 237 
LEU   CD1  C  N N 238 
LEU   CD2  C  N N 239 
LEU   OXT  O  N N 240 
LEU   H    H  N N 241 
LEU   H2   H  N N 242 
LEU   HA   H  N N 243 
LEU   HB2  H  N N 244 
LEU   HB3  H  N N 245 
LEU   HG   H  N N 246 
LEU   HD11 H  N N 247 
LEU   HD12 H  N N 248 
LEU   HD13 H  N N 249 
LEU   HD21 H  N N 250 
LEU   HD22 H  N N 251 
LEU   HD23 H  N N 252 
LEU   HXT  H  N N 253 
LYS   N    N  N N 254 
LYS   CA   C  N S 255 
LYS   C    C  N N 256 
LYS   O    O  N N 257 
LYS   CB   C  N N 258 
LYS   CG   C  N N 259 
LYS   CD   C  N N 260 
LYS   CE   C  N N 261 
LYS   NZ   N  N N 262 
LYS   OXT  O  N N 263 
LYS   H    H  N N 264 
LYS   H2   H  N N 265 
LYS   HA   H  N N 266 
LYS   HB2  H  N N 267 
LYS   HB3  H  N N 268 
LYS   HG2  H  N N 269 
LYS   HG3  H  N N 270 
LYS   HD2  H  N N 271 
LYS   HD3  H  N N 272 
LYS   HE2  H  N N 273 
LYS   HE3  H  N N 274 
LYS   HZ1  H  N N 275 
LYS   HZ2  H  N N 276 
LYS   HZ3  H  N N 277 
LYS   HXT  H  N N 278 
MET   N    N  N N 279 
MET   CA   C  N S 280 
MET   C    C  N N 281 
MET   O    O  N N 282 
MET   CB   C  N N 283 
MET   CG   C  N N 284 
MET   SD   S  N N 285 
MET   CE   C  N N 286 
MET   OXT  O  N N 287 
MET   H    H  N N 288 
MET   H2   H  N N 289 
MET   HA   H  N N 290 
MET   HB2  H  N N 291 
MET   HB3  H  N N 292 
MET   HG2  H  N N 293 
MET   HG3  H  N N 294 
MET   HE1  H  N N 295 
MET   HE2  H  N N 296 
MET   HE3  H  N N 297 
MET   HXT  H  N N 298 
PHE   N    N  N N 299 
PHE   CA   C  N S 300 
PHE   C    C  N N 301 
PHE   O    O  N N 302 
PHE   CB   C  N N 303 
PHE   CG   C  Y N 304 
PHE   CD1  C  Y N 305 
PHE   CD2  C  Y N 306 
PHE   CE1  C  Y N 307 
PHE   CE2  C  Y N 308 
PHE   CZ   C  Y N 309 
PHE   OXT  O  N N 310 
PHE   H    H  N N 311 
PHE   H2   H  N N 312 
PHE   HA   H  N N 313 
PHE   HB2  H  N N 314 
PHE   HB3  H  N N 315 
PHE   HD1  H  N N 316 
PHE   HD2  H  N N 317 
PHE   HE1  H  N N 318 
PHE   HE2  H  N N 319 
PHE   HZ   H  N N 320 
PHE   HXT  H  N N 321 
PRO   N    N  N N 322 
PRO   CA   C  N S 323 
PRO   C    C  N N 324 
PRO   O    O  N N 325 
PRO   CB   C  N N 326 
PRO   CG   C  N N 327 
PRO   CD   C  N N 328 
PRO   OXT  O  N N 329 
PRO   H    H  N N 330 
PRO   HA   H  N N 331 
PRO   HB2  H  N N 332 
PRO   HB3  H  N N 333 
PRO   HG2  H  N N 334 
PRO   HG3  H  N N 335 
PRO   HD2  H  N N 336 
PRO   HD3  H  N N 337 
PRO   HXT  H  N N 338 
SER   N    N  N N 339 
SER   CA   C  N S 340 
SER   C    C  N N 341 
SER   O    O  N N 342 
SER   CB   C  N N 343 
SER   OG   O  N N 344 
SER   OXT  O  N N 345 
SER   H    H  N N 346 
SER   H2   H  N N 347 
SER   HA   H  N N 348 
SER   HB2  H  N N 349 
SER   HB3  H  N N 350 
SER   HG   H  N N 351 
SER   HXT  H  N N 352 
THR   N    N  N N 353 
THR   CA   C  N S 354 
THR   C    C  N N 355 
THR   O    O  N N 356 
THR   CB   C  N R 357 
THR   OG1  O  N N 358 
THR   CG2  C  N N 359 
THR   OXT  O  N N 360 
THR   H    H  N N 361 
THR   H2   H  N N 362 
THR   HA   H  N N 363 
THR   HB   H  N N 364 
THR   HG1  H  N N 365 
THR   HG21 H  N N 366 
THR   HG22 H  N N 367 
THR   HG23 H  N N 368 
THR   HXT  H  N N 369 
TRP   N    N  N N 370 
TRP   CA   C  N S 371 
TRP   C    C  N N 372 
TRP   O    O  N N 373 
TRP   CB   C  N N 374 
TRP   CG   C  Y N 375 
TRP   CD1  C  Y N 376 
TRP   CD2  C  Y N 377 
TRP   NE1  N  Y N 378 
TRP   CE2  C  Y N 379 
TRP   CE3  C  Y N 380 
TRP   CZ2  C  Y N 381 
TRP   CZ3  C  Y N 382 
TRP   CH2  C  Y N 383 
TRP   OXT  O  N N 384 
TRP   H    H  N N 385 
TRP   H2   H  N N 386 
TRP   HA   H  N N 387 
TRP   HB2  H  N N 388 
TRP   HB3  H  N N 389 
TRP   HD1  H  N N 390 
TRP   HE1  H  N N 391 
TRP   HE3  H  N N 392 
TRP   HZ2  H  N N 393 
TRP   HZ3  H  N N 394 
TRP   HH2  H  N N 395 
TRP   HXT  H  N N 396 
TYR   N    N  N N 397 
TYR   CA   C  N S 398 
TYR   C    C  N N 399 
TYR   O    O  N N 400 
TYR   CB   C  N N 401 
TYR   CG   C  Y N 402 
TYR   CD1  C  Y N 403 
TYR   CD2  C  Y N 404 
TYR   CE1  C  Y N 405 
TYR   CE2  C  Y N 406 
TYR   CZ   C  Y N 407 
TYR   OH   O  N N 408 
TYR   OXT  O  N N 409 
TYR   H    H  N N 410 
TYR   H2   H  N N 411 
TYR   HA   H  N N 412 
TYR   HB2  H  N N 413 
TYR   HB3  H  N N 414 
TYR   HD1  H  N N 415 
TYR   HD2  H  N N 416 
TYR   HE1  H  N N 417 
TYR   HE2  H  N N 418 
TYR   HH   H  N N 419 
TYR   HXT  H  N N 420 
VAL   N    N  N N 421 
VAL   CA   C  N S 422 
VAL   C    C  N N 423 
VAL   O    O  N N 424 
VAL   CB   C  N N 425 
VAL   CG1  C  N N 426 
VAL   CG2  C  N N 427 
VAL   OXT  O  N N 428 
VAL   H    H  N N 429 
VAL   H2   H  N N 430 
VAL   HA   H  N N 431 
VAL   HB   H  N N 432 
VAL   HG11 H  N N 433 
VAL   HG12 H  N N 434 
VAL   HG13 H  N N 435 
VAL   HG21 H  N N 436 
VAL   HG22 H  N N 437 
VAL   HG23 H  N N 438 
VAL   HXT  H  N N 439 
ZN    ZN   ZN N N 440 
# 
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 
A1B4J C   S    sing N N 1   
A1B4J S   C1   sing N N 2   
A1B4J C1  N    doub Y N 3   
A1B4J N   C2   sing Y N 4   
A1B4J C2  C3   doub Y N 5   
A1B4J C3  C4   sing Y N 6   
A1B4J C4  C5   doub Y N 7   
A1B4J C1  C5   sing Y N 8   
A1B4J C5  C6   sing N N 9   
A1B4J C6  C7   sing N N 10  
A1B4J O   C7   doub N N 11  
A1B4J C7  N1   sing N N 12  
A1B4J N1  C8   sing N N 13  
A1B4J C8  C9   sing N N 14  
A1B4J C9  C10  sing N N 15  
A1B4J C10 C11  sing N N 16  
A1B4J C11 C12  sing N N 17  
A1B4J N2  C12  sing N N 18  
A1B4J C12 O1   doub N N 19  
A1B4J C13 C11  sing N N 20  
A1B4J N1  C13  sing N N 21  
A1B4J C4  H6   sing N N 22  
A1B4J C6  H7   sing N N 23  
A1B4J C6  H8   sing N N 24  
A1B4J C8  H10  sing N N 25  
A1B4J C8  H9   sing N N 26  
A1B4J C10 H13  sing N N 27  
A1B4J C10 H14  sing N N 28  
A1B4J C13 H17  sing N N 29  
A1B4J C13 H18  sing N N 30  
A1B4J N2  H16  sing N N 31  
A1B4J N2  H15  sing N N 32  
A1B4J C11 H    sing N N 33  
A1B4J C9  H11  sing N N 34  
A1B4J C9  H12  sing N N 35  
A1B4J C   H2   sing N N 36  
A1B4J C   H1   sing N N 37  
A1B4J C   H3   sing N N 38  
A1B4J C3  H5   sing N N 39  
A1B4J C2  H4   sing N N 40  
ALA   N   CA   sing N N 41  
ALA   N   H    sing N N 42  
ALA   N   H2   sing N N 43  
ALA   CA  C    sing N N 44  
ALA   CA  CB   sing N N 45  
ALA   CA  HA   sing N N 46  
ALA   C   O    doub N N 47  
ALA   C   OXT  sing N N 48  
ALA   CB  HB1  sing N N 49  
ALA   CB  HB2  sing N N 50  
ALA   CB  HB3  sing N N 51  
ALA   OXT HXT  sing N N 52  
ARG   N   CA   sing N N 53  
ARG   N   H    sing N N 54  
ARG   N   H2   sing N N 55  
ARG   CA  C    sing N N 56  
ARG   CA  CB   sing N N 57  
ARG   CA  HA   sing N N 58  
ARG   C   O    doub N N 59  
ARG   C   OXT  sing N N 60  
ARG   CB  CG   sing N N 61  
ARG   CB  HB2  sing N N 62  
ARG   CB  HB3  sing N N 63  
ARG   CG  CD   sing N N 64  
ARG   CG  HG2  sing N N 65  
ARG   CG  HG3  sing N N 66  
ARG   CD  NE   sing N N 67  
ARG   CD  HD2  sing N N 68  
ARG   CD  HD3  sing N N 69  
ARG   NE  CZ   sing N N 70  
ARG   NE  HE   sing N N 71  
ARG   CZ  NH1  sing N N 72  
ARG   CZ  NH2  doub N N 73  
ARG   NH1 HH11 sing N N 74  
ARG   NH1 HH12 sing N N 75  
ARG   NH2 HH21 sing N N 76  
ARG   NH2 HH22 sing N N 77  
ARG   OXT HXT  sing N N 78  
ASN   N   CA   sing N N 79  
ASN   N   H    sing N N 80  
ASN   N   H2   sing N N 81  
ASN   CA  C    sing N N 82  
ASN   CA  CB   sing N N 83  
ASN   CA  HA   sing N N 84  
ASN   C   O    doub N N 85  
ASN   C   OXT  sing N N 86  
ASN   CB  CG   sing N N 87  
ASN   CB  HB2  sing N N 88  
ASN   CB  HB3  sing N N 89  
ASN   CG  OD1  doub N N 90  
ASN   CG  ND2  sing N N 91  
ASN   ND2 HD21 sing N N 92  
ASN   ND2 HD22 sing N N 93  
ASN   OXT HXT  sing N N 94  
ASP   N   CA   sing N N 95  
ASP   N   H    sing N N 96  
ASP   N   H2   sing N N 97  
ASP   CA  C    sing N N 98  
ASP   CA  CB   sing N N 99  
ASP   CA  HA   sing N N 100 
ASP   C   O    doub N N 101 
ASP   C   OXT  sing N N 102 
ASP   CB  CG   sing N N 103 
ASP   CB  HB2  sing N N 104 
ASP   CB  HB3  sing N N 105 
ASP   CG  OD1  doub N N 106 
ASP   CG  OD2  sing N N 107 
ASP   OD2 HD2  sing N N 108 
ASP   OXT HXT  sing N N 109 
CYS   N   CA   sing N N 110 
CYS   N   H    sing N N 111 
CYS   N   H2   sing N N 112 
CYS   CA  C    sing N N 113 
CYS   CA  CB   sing N N 114 
CYS   CA  HA   sing N N 115 
CYS   C   O    doub N N 116 
CYS   C   OXT  sing N N 117 
CYS   CB  SG   sing N N 118 
CYS   CB  HB2  sing N N 119 
CYS   CB  HB3  sing N N 120 
CYS   SG  HG   sing N N 121 
CYS   OXT HXT  sing N N 122 
DMS   S   O    doub N N 123 
DMS   S   C1   sing N N 124 
DMS   S   C2   sing N N 125 
DMS   C1  H11  sing N N 126 
DMS   C1  H12  sing N N 127 
DMS   C1  H13  sing N N 128 
DMS   C2  H21  sing N N 129 
DMS   C2  H22  sing N N 130 
DMS   C2  H23  sing N N 131 
GLN   N   CA   sing N N 132 
GLN   N   H    sing N N 133 
GLN   N   H2   sing N N 134 
GLN   CA  C    sing N N 135 
GLN   CA  CB   sing N N 136 
GLN   CA  HA   sing N N 137 
GLN   C   O    doub N N 138 
GLN   C   OXT  sing N N 139 
GLN   CB  CG   sing N N 140 
GLN   CB  HB2  sing N N 141 
GLN   CB  HB3  sing N N 142 
GLN   CG  CD   sing N N 143 
GLN   CG  HG2  sing N N 144 
GLN   CG  HG3  sing N N 145 
GLN   CD  OE1  doub N N 146 
GLN   CD  NE2  sing N N 147 
GLN   NE2 HE21 sing N N 148 
GLN   NE2 HE22 sing N N 149 
GLN   OXT HXT  sing N N 150 
GLU   N   CA   sing N N 151 
GLU   N   H    sing N N 152 
GLU   N   H2   sing N N 153 
GLU   CA  C    sing N N 154 
GLU   CA  CB   sing N N 155 
GLU   CA  HA   sing N N 156 
GLU   C   O    doub N N 157 
GLU   C   OXT  sing N N 158 
GLU   CB  CG   sing N N 159 
GLU   CB  HB2  sing N N 160 
GLU   CB  HB3  sing N N 161 
GLU   CG  CD   sing N N 162 
GLU   CG  HG2  sing N N 163 
GLU   CG  HG3  sing N N 164 
GLU   CD  OE1  doub N N 165 
GLU   CD  OE2  sing N N 166 
GLU   OE2 HE2  sing N N 167 
GLU   OXT HXT  sing N N 168 
GLY   N   CA   sing N N 169 
GLY   N   H    sing N N 170 
GLY   N   H2   sing N N 171 
GLY   CA  C    sing N N 172 
GLY   CA  HA2  sing N N 173 
GLY   CA  HA3  sing N N 174 
GLY   C   O    doub N N 175 
GLY   C   OXT  sing N N 176 
GLY   OXT HXT  sing N N 177 
HIS   N   CA   sing N N 178 
HIS   N   H    sing N N 179 
HIS   N   H2   sing N N 180 
HIS   CA  C    sing N N 181 
HIS   CA  CB   sing N N 182 
HIS   CA  HA   sing N N 183 
HIS   C   O    doub N N 184 
HIS   C   OXT  sing N N 185 
HIS   CB  CG   sing N N 186 
HIS   CB  HB2  sing N N 187 
HIS   CB  HB3  sing N N 188 
HIS   CG  ND1  sing Y N 189 
HIS   CG  CD2  doub Y N 190 
HIS   ND1 CE1  doub Y N 191 
HIS   ND1 HD1  sing N N 192 
HIS   CD2 NE2  sing Y N 193 
HIS   CD2 HD2  sing N N 194 
HIS   CE1 NE2  sing Y N 195 
HIS   CE1 HE1  sing N N 196 
HIS   NE2 HE2  sing N N 197 
HIS   OXT HXT  sing N N 198 
HOH   O   H1   sing N N 199 
HOH   O   H2   sing N N 200 
ILE   N   CA   sing N N 201 
ILE   N   H    sing N N 202 
ILE   N   H2   sing N N 203 
ILE   CA  C    sing N N 204 
ILE   CA  CB   sing N N 205 
ILE   CA  HA   sing N N 206 
ILE   C   O    doub N N 207 
ILE   C   OXT  sing N N 208 
ILE   CB  CG1  sing N N 209 
ILE   CB  CG2  sing N N 210 
ILE   CB  HB   sing N N 211 
ILE   CG1 CD1  sing N N 212 
ILE   CG1 HG12 sing N N 213 
ILE   CG1 HG13 sing N N 214 
ILE   CG2 HG21 sing N N 215 
ILE   CG2 HG22 sing N N 216 
ILE   CG2 HG23 sing N N 217 
ILE   CD1 HD11 sing N N 218 
ILE   CD1 HD12 sing N N 219 
ILE   CD1 HD13 sing N N 220 
ILE   OXT HXT  sing N N 221 
LEU   N   CA   sing N N 222 
LEU   N   H    sing N N 223 
LEU   N   H2   sing N N 224 
LEU   CA  C    sing N N 225 
LEU   CA  CB   sing N N 226 
LEU   CA  HA   sing N N 227 
LEU   C   O    doub N N 228 
LEU   C   OXT  sing N N 229 
LEU   CB  CG   sing N N 230 
LEU   CB  HB2  sing N N 231 
LEU   CB  HB3  sing N N 232 
LEU   CG  CD1  sing N N 233 
LEU   CG  CD2  sing N N 234 
LEU   CG  HG   sing N N 235 
LEU   CD1 HD11 sing N N 236 
LEU   CD1 HD12 sing N N 237 
LEU   CD1 HD13 sing N N 238 
LEU   CD2 HD21 sing N N 239 
LEU   CD2 HD22 sing N N 240 
LEU   CD2 HD23 sing N N 241 
LEU   OXT HXT  sing N N 242 
LYS   N   CA   sing N N 243 
LYS   N   H    sing N N 244 
LYS   N   H2   sing N N 245 
LYS   CA  C    sing N N 246 
LYS   CA  CB   sing N N 247 
LYS   CA  HA   sing N N 248 
LYS   C   O    doub N N 249 
LYS   C   OXT  sing N N 250 
LYS   CB  CG   sing N N 251 
LYS   CB  HB2  sing N N 252 
LYS   CB  HB3  sing N N 253 
LYS   CG  CD   sing N N 254 
LYS   CG  HG2  sing N N 255 
LYS   CG  HG3  sing N N 256 
LYS   CD  CE   sing N N 257 
LYS   CD  HD2  sing N N 258 
LYS   CD  HD3  sing N N 259 
LYS   CE  NZ   sing N N 260 
LYS   CE  HE2  sing N N 261 
LYS   CE  HE3  sing N N 262 
LYS   NZ  HZ1  sing N N 263 
LYS   NZ  HZ2  sing N N 264 
LYS   NZ  HZ3  sing N N 265 
LYS   OXT HXT  sing N N 266 
MET   N   CA   sing N N 267 
MET   N   H    sing N N 268 
MET   N   H2   sing N N 269 
MET   CA  C    sing N N 270 
MET   CA  CB   sing N N 271 
MET   CA  HA   sing N N 272 
MET   C   O    doub N N 273 
MET   C   OXT  sing N N 274 
MET   CB  CG   sing N N 275 
MET   CB  HB2  sing N N 276 
MET   CB  HB3  sing N N 277 
MET   CG  SD   sing N N 278 
MET   CG  HG2  sing N N 279 
MET   CG  HG3  sing N N 280 
MET   SD  CE   sing N N 281 
MET   CE  HE1  sing N N 282 
MET   CE  HE2  sing N N 283 
MET   CE  HE3  sing N N 284 
MET   OXT HXT  sing N N 285 
PHE   N   CA   sing N N 286 
PHE   N   H    sing N N 287 
PHE   N   H2   sing N N 288 
PHE   CA  C    sing N N 289 
PHE   CA  CB   sing N N 290 
PHE   CA  HA   sing N N 291 
PHE   C   O    doub N N 292 
PHE   C   OXT  sing N N 293 
PHE   CB  CG   sing N N 294 
PHE   CB  HB2  sing N N 295 
PHE   CB  HB3  sing N N 296 
PHE   CG  CD1  doub Y N 297 
PHE   CG  CD2  sing Y N 298 
PHE   CD1 CE1  sing Y N 299 
PHE   CD1 HD1  sing N N 300 
PHE   CD2 CE2  doub Y N 301 
PHE   CD2 HD2  sing N N 302 
PHE   CE1 CZ   doub Y N 303 
PHE   CE1 HE1  sing N N 304 
PHE   CE2 CZ   sing Y N 305 
PHE   CE2 HE2  sing N N 306 
PHE   CZ  HZ   sing N N 307 
PHE   OXT HXT  sing N N 308 
PRO   N   CA   sing N N 309 
PRO   N   CD   sing N N 310 
PRO   N   H    sing N N 311 
PRO   CA  C    sing N N 312 
PRO   CA  CB   sing N N 313 
PRO   CA  HA   sing N N 314 
PRO   C   O    doub N N 315 
PRO   C   OXT  sing N N 316 
PRO   CB  CG   sing N N 317 
PRO   CB  HB2  sing N N 318 
PRO   CB  HB3  sing N N 319 
PRO   CG  CD   sing N N 320 
PRO   CG  HG2  sing N N 321 
PRO   CG  HG3  sing N N 322 
PRO   CD  HD2  sing N N 323 
PRO   CD  HD3  sing N N 324 
PRO   OXT HXT  sing N N 325 
SER   N   CA   sing N N 326 
SER   N   H    sing N N 327 
SER   N   H2   sing N N 328 
SER   CA  C    sing N N 329 
SER   CA  CB   sing N N 330 
SER   CA  HA   sing N N 331 
SER   C   O    doub N N 332 
SER   C   OXT  sing N N 333 
SER   CB  OG   sing N N 334 
SER   CB  HB2  sing N N 335 
SER   CB  HB3  sing N N 336 
SER   OG  HG   sing N N 337 
SER   OXT HXT  sing N N 338 
THR   N   CA   sing N N 339 
THR   N   H    sing N N 340 
THR   N   H2   sing N N 341 
THR   CA  C    sing N N 342 
THR   CA  CB   sing N N 343 
THR   CA  HA   sing N N 344 
THR   C   O    doub N N 345 
THR   C   OXT  sing N N 346 
THR   CB  OG1  sing N N 347 
THR   CB  CG2  sing N N 348 
THR   CB  HB   sing N N 349 
THR   OG1 HG1  sing N N 350 
THR   CG2 HG21 sing N N 351 
THR   CG2 HG22 sing N N 352 
THR   CG2 HG23 sing N N 353 
THR   OXT HXT  sing N N 354 
TRP   N   CA   sing N N 355 
TRP   N   H    sing N N 356 
TRP   N   H2   sing N N 357 
TRP   CA  C    sing N N 358 
TRP   CA  CB   sing N N 359 
TRP   CA  HA   sing N N 360 
TRP   C   O    doub N N 361 
TRP   C   OXT  sing N N 362 
TRP   CB  CG   sing N N 363 
TRP   CB  HB2  sing N N 364 
TRP   CB  HB3  sing N N 365 
TRP   CG  CD1  doub Y N 366 
TRP   CG  CD2  sing Y N 367 
TRP   CD1 NE1  sing Y N 368 
TRP   CD1 HD1  sing N N 369 
TRP   CD2 CE2  doub Y N 370 
TRP   CD2 CE3  sing Y N 371 
TRP   NE1 CE2  sing Y N 372 
TRP   NE1 HE1  sing N N 373 
TRP   CE2 CZ2  sing Y N 374 
TRP   CE3 CZ3  doub Y N 375 
TRP   CE3 HE3  sing N N 376 
TRP   CZ2 CH2  doub Y N 377 
TRP   CZ2 HZ2  sing N N 378 
TRP   CZ3 CH2  sing Y N 379 
TRP   CZ3 HZ3  sing N N 380 
TRP   CH2 HH2  sing N N 381 
TRP   OXT HXT  sing N N 382 
TYR   N   CA   sing N N 383 
TYR   N   H    sing N N 384 
TYR   N   H2   sing N N 385 
TYR   CA  C    sing N N 386 
TYR   CA  CB   sing N N 387 
TYR   CA  HA   sing N N 388 
TYR   C   O    doub N N 389 
TYR   C   OXT  sing N N 390 
TYR   CB  CG   sing N N 391 
TYR   CB  HB2  sing N N 392 
TYR   CB  HB3  sing N N 393 
TYR   CG  CD1  doub Y N 394 
TYR   CG  CD2  sing Y N 395 
TYR   CD1 CE1  sing Y N 396 
TYR   CD1 HD1  sing N N 397 
TYR   CD2 CE2  doub Y N 398 
TYR   CD2 HD2  sing N N 399 
TYR   CE1 CZ   doub Y N 400 
TYR   CE1 HE1  sing N N 401 
TYR   CE2 CZ   sing Y N 402 
TYR   CE2 HE2  sing N N 403 
TYR   CZ  OH   sing N N 404 
TYR   OH  HH   sing N N 405 
TYR   OXT HXT  sing N N 406 
VAL   N   CA   sing N N 407 
VAL   N   H    sing N N 408 
VAL   N   H2   sing N N 409 
VAL   CA  C    sing N N 410 
VAL   CA  CB   sing N N 411 
VAL   CA  HA   sing N N 412 
VAL   C   O    doub N N 413 
VAL   C   OXT  sing N N 414 
VAL   CB  CG1  sing N N 415 
VAL   CB  CG2  sing N N 416 
VAL   CB  HB   sing N N 417 
VAL   CG1 HG11 sing N N 418 
VAL   CG1 HG12 sing N N 419 
VAL   CG1 HG13 sing N N 420 
VAL   CG2 HG21 sing N N 421 
VAL   CG2 HG22 sing N N 422 
VAL   CG2 HG23 sing N N 423 
VAL   OXT HXT  sing N N 424 
# 
_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_1002344 
_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                    7I64 
_atom_sites.fract_transf_matrix[1][1]   0.013603 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000601 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016182 
_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]   0.030387 
_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   ? 19.341 6.021   24.353 1.00 32.07 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 20.473 6.197   23.440 1.00 32.14 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 20.575 5.010   22.469 1.00 30.37 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 19.896 3.994   22.659 1.00 30.00 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 21.768 6.358   24.243 1.00 35.44 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 21.930 5.210   25.055 1.00 38.82 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 21.404 5.155   21.432 1.00 28.46 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 21.610 4.104   20.441 1.00 27.34 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 21.864 4.661   19.049 1.00 26.76 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 21.413 5.764   18.721 1.00 26.01 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 22.588 3.913   18.223 1.00 25.94 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 22.910 4.349   16.863 1.00 25.88 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 22.897 3.164   15.858 1.00 25.44 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 22.933 2.021   16.293 1.00 25.50 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 24.297 4.978   16.859 1.00 26.81 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 22.880 3.459   14.535 1.00 24.68 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.992 2.482   13.448 1.00 25.02 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 24.362 2.694   12.801 1.00 26.26 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.736 3.831   12.493 1.00 25.56 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.885 2.712   12.394 1.00 24.86 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 20.494 2.674   13.014 1.00 24.39 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 22.016 1.700   11.237 1.00 25.68 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.439 3.231   12.057 1.00 23.89 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 25.135 1.612   12.637 1.00 27.78 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 26.464 1.681   12.039 1.00 29.47 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 26.448 0.910   10.712 1.00 31.37 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 26.295 -0.316  10.725 1.00 31.96 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.497 1.049   12.997 1.00 29.40 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.665 1.836   14.275 1.00 29.37 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 28.468 2.972   14.316 1.00 30.43 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 26.946 1.510   15.411 1.00 29.77 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 28.594 3.726   15.478 1.00 31.35 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 27.056 2.259   16.577 1.00 30.46 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 27.887 3.363   16.608 1.00 31.79 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 27.974 4.113   17.751 1.00 33.32 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 26.580 1.623   9.581  1.00 31.69 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 26.559 1.042   8.237  1.00 32.15 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.652 1.668   7.373  1.00 33.26 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.676 2.887   7.169  1.00 33.42 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 25.158 1.139   7.572  1.00 33.41 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.578 2.556   7.661  1.00 33.42 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 25.201 0.651   6.130  1.00 34.96 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.600 0.845   6.902  1.00 33.23 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.716 1.357   6.115  1.00 34.98 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.536 2.331   6.943  1.00 36.02 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.713 2.094   8.144  1.00 36.96 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.891 3.481   6.382  1.00 35.72 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.622 4.503   7.137  1.00 35.99 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.651 5.563   7.730  1.00 34.10 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 31.040 6.722   7.901  1.00 33.59 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.656 5.173   6.251  1.00 39.80 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.754 4.227   5.822  1.00 47.94 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.386 3.544   6.641  1.00 50.18 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 34.023 4.178   4.523  1.00 50.51 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.420 5.151   8.091  1.00 32.29 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.425 6.081   8.649  1.00 31.25 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.897 5.645   10.024 1.00 29.95 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.800 4.447   10.328 1.00 29.92 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 27.207 6.224   7.699  1.00 31.01 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.535 6.790   6.339  1.00 32.33 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 28.115 8.047   6.208  1.00 33.14 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.206 6.100   5.177  1.00 33.44 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.428 8.572   4.959  1.00 34.78 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.485 6.629   3.920  1.00 34.95 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 28.108 7.862   3.815  1.00 36.38 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.405 8.402   2.582  1.00 38.69 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.492 6.645   10.828 1.00 28.05 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.850 6.452   12.122 1.00 26.43 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.551 7.281   12.083 1.00 24.61 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.611 8.484   11.899 1.00 24.06 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.780 6.936   13.250 1.00 27.32 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 27.107 7.168   14.611 1.00 28.92 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 28.149 7.403   15.714 1.00 31.42 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 27.733 8.441   16.662 1.00 33.11 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 27.234 8.196   17.873 1.00 35.06 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 27.111 6.943   18.310 1.00 33.21 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 26.858 9.201   18.660 1.00 34.54 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 24.391 6.637   12.246 1.00 23.37 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 23.081 7.325   12.264 1.00 22.54 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.594 7.452   13.705 1.00 22.42 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 22.448 6.424   14.378 1.00 23.25 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 22.019 6.541   11.469 1.00 22.44 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.740 7.401   11.299 1.00 22.78 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.570 6.085   10.109 1.00 22.03 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 22.300 8.679   14.177 1.00 21.13 ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 21.815 8.857   15.550 1.00 20.81 ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 20.611 9.818   15.563 1.00 19.63 ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 20.402 10.573  14.596 1.00 20.09 ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 22.927 9.496   16.441 1.00 23.53 ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 24.025 8.502   16.750 1.00 26.05 ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 23.467 10.776  15.791 1.00 23.89 ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 19.849 9.871   16.689 1.00 18.59 ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 18.806 10.936  16.820 1.00 18.61 ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 19.562 12.291  16.802 1.00 20.11 ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 20.588 12.427  17.491 1.00 21.61 ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 18.074 10.827  18.182 1.00 19.81 ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 17.258 9.567   18.286 1.00 21.61 ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.763 8.519   18.725 1.00 22.46 ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 15.994 9.637   17.901 1.00 19.98 ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 19.107 13.253  15.995 1.00 19.55 ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 19.801 14.563  15.935 1.00 18.71 ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 19.834 15.235  17.312 1.00 20.49 ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 20.848 15.849  17.654 1.00 22.75 ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 19.098 15.497  14.944 1.00 18.63 ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.897 16.788  14.622 1.00 19.54 ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 18.958 17.654  13.774 1.00 21.22 ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.551 18.895  13.247 1.00 21.44 ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.633 20.032  13.930 1.00 23.59 ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 19.213 20.091  15.193 1.00 22.12 ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 20.103 21.132  13.347 1.00 25.08 ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 18.768 15.065  18.144 1.00 20.83 ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 18.754 15.737  19.466 1.00 23.02 ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 19.746 15.139  20.496 1.00 25.21 ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 20.010 15.767  21.537 1.00 27.33 ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 17.333 15.848  20.068 1.00 24.14 ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 16.747 14.556  20.560 1.00 24.93 ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 16.084 13.682  19.695 1.00 25.67 ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 16.706 14.040  21.823 1.00 26.14 ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 15.678 12.658  20.454 1.00 27.18 ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 16.038 12.817  21.743 1.00 26.68 ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 20.320 13.968  20.175 1.00 24.12 ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 21.297 13.313  21.031 1.00 24.93 ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 22.721 13.327  20.424 1.00 25.83 ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 23.604 12.655  20.966 1.00 26.71 ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 20.849 11.859  21.341 1.00 25.56 ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 19.495 11.730  22.069 1.00 27.90 ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 19.122 10.253  22.296 1.00 28.44 ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 19.512 12.479  23.416 1.00 28.95 ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 22.931 13.989  19.253 1.00 25.39 ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 24.235 13.992  18.607 1.00 26.41 ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 25.299 14.613  19.510 1.00 28.27 ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 24.998 15.553  20.247 1.00 29.52 ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 24.173 14.771  17.296 1.00 25.75 ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 26.525 14.081  19.464 1.00 29.00 ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 27.646 14.586  20.292 1.00 30.89 ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 28.484 15.673  19.556 1.00 31.79 ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 28.268 15.913  18.378 1.00 30.87 ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 28.557 13.384  20.639 1.00 33.05 ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 29.194 12.943  19.430 1.00 34.80 ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 27.799 12.256  21.294 1.00 32.69 ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 29.504 16.283  20.228 1.00 33.31 ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 30.388 17.235  19.560 1.00 34.61 ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 31.127 16.547  18.395 1.00 33.64 ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 31.282 17.133  17.333 1.00 34.62 ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 31.437 17.795  20.551 1.00 38.73 ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 30.860 18.628  21.652 1.00 46.51 ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 30.204 19.814  21.388 1.00 50.01 ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 30.954 18.469  22.996 1.00 49.40 ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 29.884 20.319  22.571 1.00 51.24 ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 30.312 19.543  23.569 1.00 51.19 ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 31.589 15.304  18.608 1.00 33.02 ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 32.283 14.541  17.571 1.00 33.45 ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 31.375 14.247  16.360 1.00 31.69 ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 31.816 14.367  15.214 1.00 31.71 ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 32.885 13.275  18.184 1.00 36.63 ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 33.986 13.665  19.123 1.00 43.69 ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.861 14.479  18.775 1.00 45.82 ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 33.967 13.137  20.339 1.00 46.51 ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 30.087 13.988  16.602 1.00 30.06 ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 29.124 13.784  15.508 1.00 28.92 ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 29.033 15.058  14.642 1.00 27.94 ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 29.125 14.976  13.422 1.00 28.32 ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 27.734 13.462  16.071 1.00 29.04 ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 27.570 12.030  16.545 1.00 31.46 ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 28.120 11.114  15.882 1.00 31.30 ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 26.880 11.823  17.567 1.00 31.73 ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 28.923 16.240  15.276 1.00 27.04 ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.809 17.500  14.533 1.00 26.68 ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 30.145 17.876  13.834 1.00 28.05 ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 30.127 18.528  12.792 1.00 28.23 ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 28.331 18.633  15.480 1.00 25.95 ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 26.840 18.658  15.681 1.00 24.23 ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 26.143 18.213  16.773 1.00 24.86 ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 25.876 19.231  14.787 1.00 22.57 ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 24.788 18.439  16.588 1.00 24.41 ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 24.597 19.033  15.362 1.00 23.38 ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 25.960 19.797  13.508 1.00 22.63 ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 23.423 19.501  14.751 1.00 22.82 ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.793 20.250  12.889 1.00 22.72 ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 23.538 20.068  13.497 1.00 22.56 ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 31.297 17.495  14.425 1.00 28.84 ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.602 17.801  13.819 1.00 31.61 ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.890 16.898  12.587 1.00 33.29 ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.782 17.214  11.798 1.00 34.47 ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 33.731 17.637  14.852 1.00 32.43 ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 32.173 15.760  12.450 1.00 31.96 ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 32.319 14.850  11.311 1.00 31.49 ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.949 14.678  10.612 1.00 29.60 ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.608 13.594  10.167 1.00 28.90 ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.874 13.520  11.763 1.00 33.82 ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 34.269 13.626  12.363 1.00 39.37 ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 35.269 13.837  11.656 1.00 42.31 ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 34.361 13.506  13.679 1.00 39.16 ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 30.160 15.765  10.558 1.00 28.57 ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.827 15.783  9.978  1.00 26.88 ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.836 15.436  8.492  1.00 27.92 ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.607 16.034  7.732  1.00 29.20 ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 28.238 17.189  10.149 1.00 26.13 ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.826 17.377  9.605  1.00 26.25 ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.829 16.547  10.428 1.00 26.50 ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.437 18.863  9.568  1.00 25.07 ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.906 14.534  8.063  1.00 25.87 ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.674 14.160  6.670  1.00 25.86 ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 26.316 14.783  6.222  1.00 25.56 ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 26.218 15.419  5.170  1.00 27.32 ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.631 12.614  6.515  1.00 26.96 ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 27.147 12.226  5.120  1.00 27.94 ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 29.008 12.007  6.803  1.00 27.34 ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 25.288 14.627  7.052  1.00 24.05 ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 23.951 15.125  6.748  1.00 23.23 ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 23.117 15.195  8.046  1.00 22.28 ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 23.286 14.379  8.938  1.00 22.89 ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 23.278 14.146  5.752  1.00 23.28 ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.804 14.359  5.524  1.00 24.06 ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 21.215 15.268  4.686  1.00 25.63 ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.735 13.617  6.131  1.00 23.65 ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.836 15.126  4.733  1.00 25.54 ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.521 14.126  5.618  1.00 24.32 ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.688 12.582  7.083  1.00 23.71 ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 18.279 13.585  5.967  1.00 24.08 ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.450 12.081  7.458  1.00 24.26 ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 18.271 12.558  6.879  1.00 23.74 ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 22.228 16.181  8.136  1.00 20.60 ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 21.325 16.302  9.270  1.00 21.33 ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 20.004 16.899  8.797  1.00 21.87 ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 19.983 17.679  7.836  1.00 22.03 ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 21.918 17.058  10.456 1.00 22.70 ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.491 18.436  10.147 1.00 23.69 ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.488 19.566  10.012 1.00 26.95 ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 21.779 20.515  9.244  1.00 30.13 ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 20.425 19.525  10.676 1.00 24.29 ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 18.911 16.516  9.463  1.00 20.99 ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.584 17.015  9.137  1.00 20.29 ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.755 17.169  10.427 1.00 20.20 ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 16.295 16.182  10.994 1.00 21.29 ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.907 16.126  8.087  1.00 21.30 ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.631 16.686  7.498  1.00 26.90 ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 14.943 17.445  8.195  1.00 28.19 ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 15.314 16.345  6.328  1.00 27.99 ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.561 18.433  10.884 1.00 19.24 ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 15.802 18.736  12.085 0.50 20.07 ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 15.810 18.670  12.109 0.50 20.00 ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 14.363 18.190  11.972 1.00 20.54 ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 13.798 17.707  12.946 1.00 21.73 ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 15.755 20.252  12.277 0.50 21.91 ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 15.842 20.147  12.502 0.50 21.71 ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 15.664 20.632  13.635 0.50 25.14 ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 15.175 20.938  11.534 0.50 24.89 ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 13.758 18.326  10.773 1.00 20.15 ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 12.373 17.885  10.581 1.00 20.62 ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 12.224 16.374  10.740 1.00 20.24 ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 11.103 15.915  10.958 1.00 21.88 ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 11.826 18.336  9.229  1.00 23.86 ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 12.292 17.518  8.162  1.00 27.89 ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 13.340 15.606  10.632 1.00 18.35 ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 13.283 14.130  10.782 1.00 18.16 ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 13.898 13.641  12.105 1.00 18.94 ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 13.853 12.437  12.376 1.00 19.60 ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 14.020 13.425  9.605  1.00 18.77 ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 13.354 13.659  8.260  1.00 19.59 ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 14.131 13.003  7.104  1.00 19.86 ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 14.132 11.532  7.222  1.00 20.17 ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 14.282 10.702  6.185  1.00 21.90 ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 14.429 11.186  4.949  1.00 21.67 ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 14.265 9.378   6.375  1.00 21.60 ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 14.550 14.548  12.880 1.00 18.96 ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 15.271 14.180  14.114 1.00 18.10 ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 16.404 13.210  13.799 1.00 17.78 ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 16.712 12.376  14.641 1.00 17.74 ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 14.354 13.628  15.230 1.00 17.58 ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 15.080 13.370  16.544 1.00 20.29 ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 15.933 14.225  16.941 1.00 20.28 ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 14.838 12.302  17.160 1.00 21.33 ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 17.052 13.335  12.596 1.00 18.09 ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 18.194 12.488  12.222 1.00 17.60 ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 19.495 13.289  12.003 1.00 18.78 ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 19.479 14.400  11.490 1.00 19.67 ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.931 11.691  10.928 1.00 17.66 ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 16.891 10.538  11.033 1.00 18.49 ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 16.745 9.842   9.677  1.00 19.10 ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 17.298 9.493   12.130 1.00 18.55 ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 20.619 12.641  12.288 1.00 18.99 ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 21.943 13.186  12.005 1.00 19.85 ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 22.841 11.990  11.673 1.00 19.87 ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 22.743 10.941  12.326 1.00 21.04 ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 22.517 14.014  13.170 1.00 20.26 ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 23.914 14.648  12.931 1.00 22.21 ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 24.065 15.951  13.693 1.00 22.55 ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 25.085 13.711  13.408 1.00 23.82 ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 23.632 12.102  10.598 1.00 20.05 ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 24.579 11.066  10.165 1.00 20.75 ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 25.990 11.683  10.203 1.00 22.28 ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 26.211 12.797  9.695  1.00 22.40 ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 24.249 10.498  8.747  1.00 22.36 ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 25.296 9.472   8.286  1.00 23.60 ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 22.848 9.885   8.724  1.00 22.20 ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 26.915 10.966  10.847 1.00 22.64 ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 28.306 11.401  10.921 1.00 25.12 ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 29.195 10.297  10.336 1.00 27.38 ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 28.761 9.146   10.193 1.00 26.56 ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 28.714 11.706  12.363 1.00 26.15 ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 28.553 10.580  13.214 1.00 28.30 ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 30.450 10.652  10.003 1.00 29.59 ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 31.373 9.672   9.445  1.00 32.82 ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 32.182 8.956   10.538 1.00 36.32 ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 32.400 9.508   11.618 1.00 36.98 ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 32.318 10.352  8.465  1.00 34.38 ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 33.001 11.384  9.157  1.00 37.91 ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 32.638 7.723   10.247 1.00 37.83 ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 33.409 6.899   11.178 1.00 41.11 ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 34.647 6.357   10.453 1.00 45.64 ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 34.618 6.151   9.236  1.00 46.14 ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 32.582 5.675   11.640 1.00 41.62 ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 32.330 4.841   10.515 1.00 43.43 ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 31.254 6.043   12.275 1.00 40.81 ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? 35.684 6.026   11.211 1.00 48.49 ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? 36.904 5.443   10.656 1.00 51.45 ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? 36.720 3.927   10.447 1.00 53.34 ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? 37.235 3.369   9.476  1.00 54.95 ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? 38.102 5.764   11.575 1.00 53.92 ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? 37.751 5.442   12.928 1.00 56.09 ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? 38.524 7.219   11.498 1.00 54.60 ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? 36.013 3.255   11.368 1.00 52.85 ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? 35.776 1.810   11.276 1.00 53.09 ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 34.550 1.488   10.412 1.00 52.82 ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 33.656 2.326   10.258 1.00 52.91 ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? 35.602 1.228   12.667 1.00 53.37 ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 34.510 0.276   9.847  1.00 52.68 ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 33.423 -0.181  8.980  1.00 52.79 ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 32.251 -0.789  9.750  1.00 51.15 ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 32.442 -1.743  10.495 1.00 51.62 ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 33.951 -1.235  7.995  1.00 56.09 ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 33.099 -1.377  6.739  1.00 61.74 ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 33.677 -0.534  5.629  1.00 67.15 ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 34.836 -0.702  5.242  1.00 68.76 ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 32.892 0.397   5.091  1.00 67.78 ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 31.044 -0.295  9.481  1.00 48.71 ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 29.800 -0.776  10.070 1.00 46.95 ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 29.172 -1.921  9.291  1.00 44.51 ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 29.224 -1.946  8.058  1.00 44.52 ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 28.520 -2.838  9.995  1.00 41.96 ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 27.942 -4.017  9.362  1.00 40.95 ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 26.448 -4.175  9.512  1.00 38.53 ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 25.964 -5.288  9.260  1.00 38.73 ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 28.655 -5.270  9.849  1.00 43.86 ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 30.402 -5.313  9.430  1.00 52.93 ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 25.707 -3.118  9.922  1.00 35.76 ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 24.251 -3.247  10.021 1.00 35.30 ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 23.676 -3.255  8.601  1.00 34.86 ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 24.183 -2.572  7.707  1.00 35.37 ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 23.598 -2.099  10.847 1.00 36.83 ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 23.876 -2.106  12.342 1.00 41.23 ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 24.038 -3.196  12.909 1.00 42.27 ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 23.903 -1.010  12.951 1.00 42.18 ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 22.620 -4.006  8.401  1.00 34.22 ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 21.965 -4.097  7.104  1.00 34.13 ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 20.741 -3.201  7.130  1.00 31.93 ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 19.903 -3.390  8.008  1.00 32.03 ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 21.522 -5.550  6.860  1.00 36.76 ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 22.702 -6.338  6.621  1.00 38.70 ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 20.595 -5.672  5.657  1.00 36.92 ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 20.597 -2.284  6.162  1.00 29.40 ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 19.410 -1.445  6.117  1.00 27.11 ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 18.352 -2.146  5.264  1.00 26.89 ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 18.661 -2.634  4.150  1.00 28.09 ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 19.742 -0.042  5.562  1.00 27.04 ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 20.956 0.587   6.288  1.00 27.74 ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 18.505 0.881   5.626  1.00 27.09 ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 20.725 0.930   7.783  1.00 28.40 ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 17.124 -2.202  5.766  1.00 24.51 ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 16.006 -2.784  5.034  1.00 25.10 ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 15.600 -1.852  3.878  1.00 25.84 ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 15.583 -0.638  4.062  1.00 25.44 ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 14.813 -2.958  5.967  1.00 23.88 ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 15.232 -2.429  2.714  1.00 27.19 ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 14.727 -1.674  1.574  1.00 28.12 ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 13.378 -2.334  1.237  1.00 30.00 ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 13.350 -3.320  0.484  1.00 31.07 ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 15.721 -1.769  0.403  1.00 28.81 ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 17.127 -1.293  0.765  1.00 29.22 ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 17.205 0.206   1.181  1.00 31.42 ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 18.588 0.599   1.474  1.00 30.40 ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 18.936 1.720   2.099  1.00 30.94 ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 18.009 2.579   2.504  1.00 28.33 ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 20.215 1.983   2.340  1.00 29.42 ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 12.279 -1.868  1.881  1.00 30.50 ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 10.976 -2.551  1.786  1.00 30.89 ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 9.833  -1.621  2.234  1.00 31.65 ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 10.084 -0.500  2.681  1.00 31.49 ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 11.039 -3.754  2.720  1.00 30.12 ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 11.211 -3.270  4.471  1.00 28.41 ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 8.586  -2.146  2.240  1.00 31.30 ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 7.464  -1.392  2.786  1.00 32.25 ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 6.805  -2.148  3.951  1.00 31.25 ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 5.623  -1.949  4.198  1.00 31.64 ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 6.436  -0.947  1.720  1.00 36.13 ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 5.603  -2.055  1.141  1.00 43.62 ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 5.991  -3.237  1.297  1.00 45.09 ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 4.547  -1.750  0.538  1.00 48.67 ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 7.563  -3.015  4.672  1.00 29.76 ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 7.077  -3.739  5.881  1.00 27.34 ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 6.367  -2.788  6.851  1.00 25.60 ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 6.818  -1.649  7.070  1.00 25.79 ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 8.242  -4.422  6.603  1.00 27.47 ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 8.785  -5.992  5.880  1.00 28.28 ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 5.319  -3.267  7.471  1.00 24.14 ? 59  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 53  ? 4.600  -2.565  8.520  1.00 24.08 ? 59  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 53  ? 4.541  -3.411  9.814  1.00 22.36 ? 59  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 53  ? 3.684  -3.171  10.668 1.00 22.41 ? 59  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 53  ? 3.195  -2.133  8.062  1.00 27.46 ? 59  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 53  ? 3.188  -0.854  7.215  1.00 31.37 ? 59  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 53  ? 1.765  -0.412  6.949  1.00 36.21 ? 59  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 53  ? 1.254  -0.531  5.832  1.00 37.67 ? 59  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 53  ? 1.078  0.063   7.990  1.00 36.08 ? 59  GLN   A NE2 1 
ATOM   415  N  N   . THR   A 1 54  ? 5.422  -4.446  9.951  1.00 21.42 ? 60  THR   A N   1 
ATOM   416  C  CA  . THR   A 1 54  ? 5.552  -5.280  11.157 1.00 21.05 ? 60  THR   A CA  1 
ATOM   417  C  C   . THR   A 1 54  ? 7.062  -5.428  11.420 1.00 19.42 ? 60  THR   A C   1 
ATOM   418  O  O   . THR   A 1 54  ? 7.865  -5.509  10.484 1.00 19.42 ? 60  THR   A O   1 
ATOM   419  C  CB  . THR   A 1 54  ? 4.877  -6.680  11.061 1.00 25.18 ? 60  THR   A CB  1 
ATOM   420  O  OG1 . THR   A 1 54  ? 5.575  -7.499  10.111 1.00 27.64 ? 60  THR   A OG1 1 
ATOM   421  C  CG2 . THR   A 1 54  ? 3.396  -6.615  10.732 1.00 27.12 ? 60  THR   A CG2 1 
ATOM   422  N  N   . GLY   A 1 55  ? 7.430  -5.430  12.689 1.00 18.35 ? 61  GLY   A N   1 
ATOM   423  C  CA  . GLY   A 1 55  ? 8.841  -5.530  13.098 1.00 17.34 ? 61  GLY   A CA  1 
ATOM   424  C  C   . GLY   A 1 55  ? 8.996  -5.713  14.604 1.00 17.79 ? 61  GLY   A C   1 
ATOM   425  O  O   . GLY   A 1 55  ? 8.014  -5.950  15.297 1.00 18.41 ? 61  GLY   A O   1 
ATOM   426  N  N   . VAL   A 1 56  ? 10.237 -5.600  15.107 1.00 17.17 ? 62  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 56  ? 10.564 -5.741  16.511 1.00 17.90 ? 62  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 56  ? 11.430 -4.546  16.927 1.00 18.17 ? 62  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 56  ? 12.420 -4.270  16.243 1.00 17.50 ? 62  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 56  ? 11.307 -7.074  16.737 1.00 19.62 ? 62  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 56  ? 11.797 -7.200  18.199 1.00 21.35 ? 62  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 56  ? 10.385 -8.240  16.365 1.00 20.05 ? 62  VAL   A CG2 1 
ATOM   433  N  N   . TYR   A 1 57  ? 11.094 -3.877  18.042 1.00 17.81 ? 63  TYR   A N   1 
ATOM   434  C  CA  . TYR   A 1 57  ? 11.959 -2.778  18.522 1.00 18.21 ? 63  TYR   A CA  1 
ATOM   435  C  C   . TYR   A 1 57  ? 12.555 -3.069  19.898 1.00 19.16 ? 63  TYR   A C   1 
ATOM   436  O  O   . TYR   A 1 57  ? 11.956 -3.794  20.687 1.00 19.17 ? 63  TYR   A O   1 
ATOM   437  C  CB  . TYR   A 1 57  ? 11.250 -1.387  18.508 1.00 17.98 ? 63  TYR   A CB  1 
ATOM   438  C  CG  . TYR   A 1 57  ? 10.298 -1.126  19.671 1.00 18.94 ? 63  TYR   A CG  1 
ATOM   439  C  CD1 . TYR   A 1 57  ? 9.018  -1.673  19.686 1.00 19.88 ? 63  TYR   A CD1 1 
ATOM   440  C  CD2 . TYR   A 1 57  ? 10.633 -0.243  20.690 1.00 19.28 ? 63  TYR   A CD2 1 
ATOM   441  C  CE1 . TYR   A 1 57  ? 8.115  -1.384  20.710 1.00 20.49 ? 63  TYR   A CE1 1 
ATOM   442  C  CE2 . TYR   A 1 57  ? 9.747  0.035   21.742 1.00 19.87 ? 63  TYR   A CE2 1 
ATOM   443  C  CZ  . TYR   A 1 57  ? 8.484  -0.534  21.745 1.00 20.62 ? 63  TYR   A CZ  1 
ATOM   444  O  OH  . TYR   A 1 57  ? 7.578  -0.289  22.758 1.00 22.25 ? 63  TYR   A OH  1 
ATOM   445  N  N   . TYR   A 1 58  ? 13.731 -2.475  20.193 1.00 19.60 ? 64  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 58  ? 14.363 -2.619  21.492 1.00 21.17 ? 64  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 58  ? 13.934 -1.456  22.395 1.00 21.18 ? 64  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 58  ? 14.103 -0.270  22.043 1.00 19.80 ? 64  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 58  ? 15.905 -2.667  21.413 1.00 22.09 ? 64  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 58  ? 16.516 -2.832  22.787 1.00 23.97 ? 64  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 58  ? 16.260 -3.965  23.548 1.00 25.58 ? 64  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 58  ? 17.290 -1.827  23.352 1.00 25.55 ? 64  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 58  ? 16.795 -4.120  24.824 1.00 26.81 ? 64  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 58  ? 17.809 -1.953  24.638 1.00 27.26 ? 64  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 58  ? 17.556 -3.101  25.373 1.00 28.73 ? 64  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 58  ? 18.065 -3.228  26.644 1.00 31.71 ? 64  TYR   A OH  1 
ATOM   457  N  N   . CYS   A 1 59  ? 13.386 -1.808  23.576 1.00 21.03 ? 65  CYS   A N   1 
ATOM   458  C  CA  . CYS   A 1 59  ? 12.943 -0.812  24.574 1.00 22.65 ? 65  CYS   A CA  1 
ATOM   459  C  C   . CYS   A 1 59  ? 13.874 -0.853  25.816 1.00 23.94 ? 65  CYS   A C   1 
ATOM   460  O  O   . CYS   A 1 59  ? 13.703 -1.713  26.684 1.00 24.03 ? 65  CYS   A O   1 
ATOM   461  C  CB  . CYS   A 1 59  ? 11.485 -1.080  24.948 1.00 24.61 ? 65  CYS   A CB  1 
ATOM   462  S  SG  . CYS   A 1 59  ? 10.847 -0.035  26.290 1.00 26.38 ? 65  CYS   A SG  1 
ATOM   463  N  N   . SER   A 1 60  ? 14.840 0.122   25.922 1.00 24.16 ? 66  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 60  ? 15.790 0.117   27.017 1.00 26.20 ? 66  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 60  ? 15.140 0.283   28.400 1.00 26.46 ? 66  SER   A C   1 
ATOM   466  O  O   . SER   A 1 60  ? 15.610 -0.331  29.380 1.00 28.24 ? 66  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 60  ? 16.892 1.147   26.797 1.00 30.22 ? 66  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 60  ? 16.381 2.464   26.889 1.00 35.83 ? 66  SER   A OG  1 
ATOM   469  N  N   . SER   A 1 61  ? 14.019 1.039   28.480 1.00 25.32 ? 67  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 61  ? 13.304 1.237   29.771 1.00 25.95 ? 67  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 61  ? 12.616 -0.021  30.326 1.00 27.17 ? 67  SER   A C   1 
ATOM   472  O  O   . SER   A 1 61  ? 12.090 0.010   31.456 1.00 29.24 ? 67  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 61  ? 12.286 2.370   29.674 1.00 26.41 ? 67  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 61  ? 11.217 2.058   28.794 1.00 28.24 ? 67  SER   A OG  1 
ATOM   475  N  N   . ARG   A 1 62  ? 12.645 -1.122  29.562 1.00 25.69 ? 68  ARG   A N   1 
ATOM   476  C  CA  . ARG   A 1 62  ? 12.123 -2.418  29.998 1.00 25.26 ? 68  ARG   A CA  1 
ATOM   477  C  C   . ARG   A 1 62  ? 13.146 -3.564  29.793 1.00 26.89 ? 68  ARG   A C   1 
ATOM   478  O  O   . ARG   A 1 62  ? 12.847 -4.729  30.130 1.00 27.51 ? 68  ARG   A O   1 
ATOM   479  C  CB  . ARG   A 1 62  ? 10.829 -2.770  29.243 1.00 26.28 ? 68  ARG   A CB  1 
ATOM   480  C  CG  . ARG   A 1 62  ? 9.646  -1.854  29.555 1.00 28.59 ? 68  ARG   A CG  1 
ATOM   481  C  CD  . ARG   A 1 62  ? 8.989  -2.169  30.885 1.00 29.09 ? 68  ARG   A CD  1 
ATOM   482  N  NE  . ARG   A 1 62  ? 7.804  -1.334  31.125 1.00 32.22 ? 68  ARG   A NE  1 
ATOM   483  C  CZ  . ARG   A 1 62  ? 7.831  -0.136  31.702 1.00 34.18 ? 68  ARG   A CZ  1 
ATOM   484  N  NH1 . ARG   A 1 62  ? 8.985  0.389   32.108 1.00 33.61 ? 68  ARG   A NH1 1 
ATOM   485  N  NH2 . ARG   A 1 62  ? 6.705  0.550   31.878 1.00 34.02 ? 68  ARG   A NH2 1 
ATOM   486  N  N   . ARG   A 1 63  ? 14.334 -3.261  29.189 1.00 27.16 ? 69  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 63  ? 15.368 -4.245  28.815 1.00 27.85 ? 69  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 63  ? 14.708 -5.408  28.025 1.00 27.66 ? 69  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 63  ? 14.957 -6.585  28.307 1.00 28.12 ? 69  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 63  ? 16.127 -4.752  30.052 1.00 30.00 ? 69  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 63  ? 17.132 -3.735  30.596 1.00 34.22 ? 69  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 63  ? 17.894 -4.381  31.760 1.00 40.91 ? 69  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 63  ? 18.478 -3.398  32.667 1.00 47.37 ? 69  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 63  ? 18.377 -3.443  33.995 1.00 51.07 ? 69  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 63  ? 17.701 -4.426  34.586 1.00 51.57 ? 69  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 63  ? 18.911 -2.481  34.740 1.00 51.06 ? 69  ARG   A NH2 1 
ATOM   497  N  N   . LYS   A 1 64  ? 13.794 -5.041  27.091 1.00 25.53 ? 70  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 64  ? 13.032 -6.051  26.344 1.00 25.34 ? 70  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 64  ? 12.832 -5.628  24.891 1.00 23.58 ? 70  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 64  ? 12.784 -4.430  24.603 1.00 23.11 ? 70  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 64  ? 11.607 -6.157  26.915 1.00 28.38 ? 70  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 64  ? 11.421 -7.182  28.021 1.00 36.50 ? 70  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 64  ? 9.979  -7.141  28.511 1.00 43.35 ? 70  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 64  ? 9.640  -8.300  29.423 1.00 50.29 ? 70  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 64  ? 10.414 -8.258  30.692 1.00 54.40 ? 70  LYS   A NZ  1 
ATOM   506  N  N   . HIS   A 1 65  ? 12.641 -6.625  23.996 1.00 22.79 ? 71  HIS   A N   1 
ATOM   507  C  CA  . HIS   A 1 65  ? 12.276 -6.344  22.613 1.00 21.79 ? 71  HIS   A CA  1 
ATOM   508  C  C   . HIS   A 1 65  ? 10.759 -6.612  22.496 1.00 22.37 ? 71  HIS   A C   1 
ATOM   509  O  O   . HIS   A 1 65  ? 10.224 -7.564  23.110 1.00 23.44 ? 71  HIS   A O   1 
ATOM   510  C  CB  . HIS   A 1 65  ? 13.032 -7.261  21.614 1.00 21.71 ? 71  HIS   A CB  1 
ATOM   511  C  CG  . HIS   A 1 65  ? 14.524 -7.064  21.599 1.00 22.54 ? 71  HIS   A CG  1 
ATOM   512  N  ND1 . HIS   A 1 65  ? 15.154 -6.307  20.604 1.00 25.17 ? 71  HIS   A ND1 1 
ATOM   513  C  CD2 . HIS   A 1 65  ? 15.471 -7.577  22.410 1.00 22.84 ? 71  HIS   A CD2 1 
ATOM   514  C  CE1 . HIS   A 1 65  ? 16.453 -6.377  20.866 1.00 24.70 ? 71  HIS   A CE1 1 
ATOM   515  N  NE2 . HIS   A 1 65  ? 16.690 -7.085  21.961 1.00 25.14 ? 71  HIS   A NE2 1 
ATOM   516  N  N   . TYR   A 1 66  ? 10.057 -5.773  21.737 1.00 20.21 ? 72  TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 66  ? 8.612  -5.953  21.527 1.00 20.63 ? 72  TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 66  ? 8.240  -6.041  20.045 1.00 20.29 ? 72  TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 66  ? 8.677  -5.213  19.245 1.00 19.61 ? 72  TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 66  ? 7.831  -4.746  22.098 1.00 21.65 ? 72  TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 66  ? 7.876  -4.630  23.604 1.00 23.48 ? 72  TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 66  ? 7.112  -5.466  24.410 1.00 25.77 ? 72  TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 66  ? 8.655  -3.660  24.227 1.00 25.56 ? 72  TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 66  ? 7.143  -5.362  25.804 1.00 26.95 ? 72  TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 66  ? 8.695  -3.547  25.620 1.00 27.51 ? 72  TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 66  ? 7.944  -4.407  26.403 1.00 28.40 ? 72  TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 66  ? 7.943  -4.273  27.781 1.00 30.64 ? 72  TYR   A OH  1 
ATOM   528  N  N   . PRO   A 1 67  ? 7.388  -7.016  19.668 1.00 19.88 ? 73  PRO   A N   1 
ATOM   529  C  CA  . PRO   A 1 67  ? 6.877  -7.061  18.278 1.00 19.85 ? 73  PRO   A CA  1 
ATOM   530  C  C   . PRO   A 1 67  ? 5.757  -6.003  18.108 1.00 21.34 ? 73  PRO   A C   1 
ATOM   531  O  O   . PRO   A 1 67  ? 4.898  -5.883  19.006 1.00 22.83 ? 73  PRO   A O   1 
ATOM   532  C  CB  . PRO   A 1 67  ? 6.266  -8.465  18.173 1.00 20.68 ? 73  PRO   A CB  1 
ATOM   533  C  CG  . PRO   A 1 67  ? 5.871  -8.808  19.600 1.00 21.24 ? 73  PRO   A CG  1 
ATOM   534  C  CD  . PRO   A 1 67  ? 6.803  -8.073  20.528 1.00 20.43 ? 73  PRO   A CD  1 
ATOM   535  N  N   . VAL   A 1 68  ? 5.743  -5.263  16.996 1.00 20.04 ? 74  VAL   A N   1 
ATOM   536  C  CA  . VAL   A 1 68  ? 4.733  -4.221  16.760 1.00 20.93 ? 74  VAL   A CA  1 
ATOM   537  C  C   . VAL   A 1 68  ? 4.289  -4.151  15.290 1.00 20.57 ? 74  VAL   A C   1 
ATOM   538  O  O   . VAL   A 1 68  ? 5.043  -4.510  14.366 1.00 20.48 ? 74  VAL   A O   1 
ATOM   539  C  CB  . VAL   A 1 68  ? 5.283  -2.791  17.125 1.00 21.97 ? 74  VAL   A CB  1 
ATOM   540  C  CG1 . VAL   A 1 68  ? 5.328  -2.548  18.628 1.00 23.48 ? 74  VAL   A CG1 1 
ATOM   541  C  CG2 . VAL   A 1 68  ? 6.642  -2.537  16.480 1.00 21.58 ? 74  VAL   A CG2 1 
ATOM   542  N  N   . SER   A 1 69  ? 3.071  -3.622  15.081 1.00 20.17 ? 75  SER   A N   1 
ATOM   543  C  CA  . SER   A 1 69  ? 2.565  -3.189  13.784 1.00 21.45 ? 75  SER   A CA  1 
ATOM   544  C  C   . SER   A 1 69  ? 2.794  -1.657  13.764 1.00 21.17 ? 75  SER   A C   1 
ATOM   545  O  O   . SER   A 1 69  ? 2.590  -1.016  14.802 1.00 22.31 ? 75  SER   A O   1 
ATOM   546  C  CB  . SER   A 1 69  ? 1.070  -3.457  13.649 1.00 24.71 ? 75  SER   A CB  1 
ATOM   547  O  OG  . SER   A 1 69  ? 0.834  -4.850  13.601 1.00 30.41 ? 75  SER   A OG  1 
ATOM   548  N  N   . PHE   A 1 70  ? 3.288  -1.098  12.662 1.00 19.24 ? 76  PHE   A N   1 
ATOM   549  C  CA  . PHE   A 1 70  ? 3.573  0.344   12.607 1.00 20.20 ? 76  PHE   A CA  1 
ATOM   550  C  C   . PHE   A 1 70  ? 3.054  1.006   11.354 1.00 22.78 ? 76  PHE   A C   1 
ATOM   551  O  O   . PHE   A 1 70  ? 2.890  0.346   10.316 1.00 24.28 ? 76  PHE   A O   1 
ATOM   552  C  CB  . PHE   A 1 70  ? 5.077  0.646   12.816 1.00 19.60 ? 76  PHE   A CB  1 
ATOM   553  C  CG  . PHE   A 1 70  ? 6.066  -0.090  11.926 1.00 18.51 ? 76  PHE   A CG  1 
ATOM   554  C  CD1 . PHE   A 1 70  ? 6.546  -1.345  12.278 1.00 18.34 ? 76  PHE   A CD1 1 
ATOM   555  C  CD2 . PHE   A 1 70  ? 6.519  0.475   10.746 1.00 19.13 ? 76  PHE   A CD2 1 
ATOM   556  C  CE1 . PHE   A 1 70  ? 7.501  -1.996  11.478 1.00 18.99 ? 76  PHE   A CE1 1 
ATOM   557  C  CE2 . PHE   A 1 70  ? 7.456  -0.180  9.938  1.00 19.44 ? 76  PHE   A CE2 1 
ATOM   558  C  CZ  . PHE   A 1 70  ? 7.932  -1.422  10.302 1.00 19.20 ? 76  PHE   A CZ  1 
ATOM   559  N  N   . SER   A 1 71  ? 2.761  2.335   11.440 1.00 22.68 ? 77  SER   A N   1 
ATOM   560  C  CA  . SER   A 1 71  ? 2.209  3.032   10.282 1.00 23.54 ? 77  SER   A CA  1 
ATOM   561  C  C   . SER   A 1 71  ? 3.265  3.329   9.179  1.00 23.94 ? 77  SER   A C   1 
ATOM   562  O  O   . SER   A 1 71  ? 4.454  3.187   9.429  1.00 23.80 ? 77  SER   A O   1 
ATOM   563  C  CB  . SER   A 1 71  ? 1.530  4.322   10.737 1.00 26.45 ? 77  SER   A CB  1 
ATOM   564  O  OG  . SER   A 1 71  ? 2.507  5.218   11.242 1.00 27.24 ? 77  SER   A OG  1 
ATOM   565  N  N   . LYS   A 1 72  ? 2.842  3.725   7.945  1.00 25.25 ? 78  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 72  ? 3.813  4.110   6.893  1.00 26.88 ? 78  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 72  ? 4.468  5.479   7.260  1.00 27.24 ? 78  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 72  ? 3.845  6.267   7.958  1.00 27.98 ? 78  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 72  ? 3.134  4.167   5.497  1.00 31.84 ? 78  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 72  ? 2.855  2.755   4.945  1.00 37.07 ? 78  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 72  ? 2.472  2.702   3.462  1.00 43.33 ? 78  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 72  ? 2.250  1.246   3.097  1.00 48.63 ? 78  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 72  ? 2.159  1.017   1.629  1.00 51.69 ? 78  LYS   A NZ  1 
ATOM   574  N  N   . PRO   A 1 73  ? 5.696  5.785   6.789  1.00 26.46 ? 79  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 73  ? 6.331  7.068   7.174  1.00 27.02 ? 79  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 73  ? 5.478  8.265   6.766  1.00 27.47 ? 79  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 73  ? 5.000  8.328   5.621  1.00 27.04 ? 79  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 73  ? 7.664  7.078   6.411  1.00 28.51 ? 79  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 73  ? 7.898  5.689   5.945  1.00 29.36 ? 79  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 73  ? 6.569  4.966   5.928  1.00 26.62 ? 79  PRO   A CD  1 
ATOM   581  N  N   . SER   A 1 74  ? 5.248  9.193   7.702  1.00 27.53 ? 80  SER   A N   1 
ATOM   582  C  CA  . SER   A 1 74  ? 4.388  10.345  7.413  1.00 28.83 ? 80  SER   A CA  1 
ATOM   583  C  C   . SER   A 1 74  ? 4.725  11.575  8.294  1.00 28.61 ? 80  SER   A C   1 
ATOM   584  O  O   . SER   A 1 74  ? 5.629  11.507  9.137  1.00 28.01 ? 80  SER   A O   1 
ATOM   585  C  CB  . SER   A 1 74  ? 2.917  9.932   7.521  1.00 32.88 ? 80  SER   A CB  1 
ATOM   586  O  OG  . SER   A 1 74  ? 2.538  9.633   8.853  1.00 37.41 ? 80  SER   A OG  1 
ATOM   587  N  N   . LEU   A 1 75  ? 4.057  12.732  8.022  1.00 28.48 ? 81  LEU   A N   1 
ATOM   588  C  CA  . LEU   A 1 75  ? 4.221  13.971  8.775  1.00 29.56 ? 81  LEU   A CA  1 
ATOM   589  C  C   . LEU   A 1 75  ? 3.284  13.865  9.965  1.00 31.23 ? 81  LEU   A C   1 
ATOM   590  O  O   . LEU   A 1 75  ? 2.055  13.797  9.765  1.00 33.04 ? 81  LEU   A O   1 
ATOM   591  C  CB  . LEU   A 1 75  ? 3.699  15.167  7.943  1.00 30.31 ? 81  LEU   A CB  1 
ATOM   592  C  CG  . LEU   A 1 75  ? 4.655  15.919  7.091  1.00 32.60 ? 81  LEU   A CG  1 
ATOM   593  C  CD1 . LEU   A 1 75  ? 3.907  17.030  6.356  1.00 33.64 ? 81  LEU   A CD1 1 
ATOM   594  C  CD2 . LEU   A 1 75  ? 5.768  16.534  7.910  1.00 33.57 ? 81  LEU   A CD2 1 
ATOM   595  N  N   . ILE   A 1 76  ? 3.825  13.890  11.180 1.00 30.06 ? 82  ILE   A N   1 
ATOM   596  C  CA  . ILE   A 1 76  ? 3.032  13.761  12.382 1.00 32.00 ? 82  ILE   A CA  1 
ATOM   597  C  C   . ILE   A 1 76  ? 3.372  14.893  13.354 1.00 34.09 ? 82  ILE   A C   1 
ATOM   598  O  O   . ILE   A 1 76  ? 4.557  15.202  13.574 1.00 33.17 ? 82  ILE   A O   1 
ATOM   599  C  CB  . ILE   A 1 76  ? 3.288  12.353  13.022 1.00 33.06 ? 82  ILE   A CB  1 
ATOM   600  C  CG1 . ILE   A 1 76  ? 2.749  11.229  12.102 1.00 34.37 ? 82  ILE   A CG1 1 
ATOM   601  C  CG2 . ILE   A 1 76  ? 2.666  12.253  14.415 1.00 33.69 ? 82  ILE   A CG2 1 
ATOM   602  C  CD1 . ILE   A 1 76  ? 3.233  9.957   12.395 1.00 36.69 ? 82  ILE   A CD1 1 
ATOM   603  N  N   . PHE   A 1 77  ? 2.327  15.513  13.940 1.00 35.56 ? 83  PHE   A N   1 
ATOM   604  C  CA  . PHE   A 1 77  ? 2.511  16.568  14.930 1.00 38.04 ? 83  PHE   A CA  1 
ATOM   605  C  C   . PHE   A 1 77  ? 3.173  16.040  16.218 1.00 37.43 ? 83  PHE   A C   1 
ATOM   606  O  O   . PHE   A 1 77  ? 2.799  14.989  16.735 1.00 37.85 ? 83  PHE   A O   1 
ATOM   607  C  CB  . PHE   A 1 77  ? 1.173  17.272  15.248 1.00 40.07 ? 83  PHE   A CB  1 
ATOM   608  C  CG  . PHE   A 1 77  ? 1.361  18.600  15.942 1.00 42.79 ? 83  PHE   A CG  1 
ATOM   609  C  CD1 . PHE   A 1 77  ? 1.755  19.717  15.236 1.00 45.07 ? 83  PHE   A CD1 1 
ATOM   610  C  CD2 . PHE   A 1 77  ? 1.159  18.722  17.307 1.00 44.52 ? 83  PHE   A CD2 1 
ATOM   611  C  CE1 . PHE   A 1 77  ? 1.913  20.947  15.874 1.00 46.42 ? 83  PHE   A CE1 1 
ATOM   612  C  CE2 . PHE   A 1 77  ? 1.343  19.944  17.949 1.00 45.64 ? 83  PHE   A CE2 1 
ATOM   613  C  CZ  . PHE   A 1 77  ? 1.709  21.047  17.231 1.00 46.07 ? 83  PHE   A CZ  1 
ATOM   614  N  N   . VAL   A 1 78  ? 4.217  16.741  16.679 1.00 36.51 ? 84  VAL   A N   1 
ATOM   615  C  CA  . VAL   A 1 78  ? 5.007  16.402  17.855 1.00 36.71 ? 84  VAL   A CA  1 
ATOM   616  C  C   . VAL   A 1 78  ? 5.079  17.601  18.792 1.00 38.64 ? 84  VAL   A C   1 
ATOM   617  O  O   . VAL   A 1 78  ? 5.521  18.690  18.391 1.00 38.64 ? 84  VAL   A O   1 
ATOM   618  C  CB  . VAL   A 1 78  ? 6.439  15.932  17.463 1.00 35.88 ? 84  VAL   A CB  1 
ATOM   619  C  CG1 . VAL   A 1 78  ? 7.300  15.680  18.697 1.00 35.94 ? 84  VAL   A CG1 1 
ATOM   620  C  CG2 . VAL   A 1 78  ? 6.397  14.706  16.564 1.00 35.50 ? 84  VAL   A CG2 1 
ATOM   621  N  N   . GLU   A 1 79  ? 4.674  17.389  20.054 1.00 39.40 ? 85  GLU   A N   1 
ATOM   622  C  CA  . GLU   A 1 79  ? 4.671  18.429  21.087 1.00 40.01 ? 85  GLU   A CA  1 
ATOM   623  C  C   . GLU   A 1 79  ? 6.042  19.011  21.375 1.00 39.01 ? 85  GLU   A C   1 
ATOM   624  O  O   . GLU   A 1 79  ? 7.047  18.320  21.230 1.00 38.85 ? 85  GLU   A O   1 
ATOM   625  C  CB  . GLU   A 1 79  ? 4.128  17.845  22.395 1.00 44.13 ? 85  GLU   A CB  1 
ATOM   626  C  CG  . GLU   A 1 79  ? 2.699  17.375  22.279 1.00 54.18 ? 85  GLU   A CG  1 
ATOM   627  C  CD  . GLU   A 1 79  ? 1.747  18.487  21.897 1.00 66.82 ? 85  GLU   A CD  1 
ATOM   628  O  OE1 . GLU   A 1 79  ? 1.848  19.591  22.484 1.00 69.02 ? 85  GLU   A OE1 1 
ATOM   629  O  OE2 . GLU   A 1 79  ? 0.913  18.262  20.990 1.00 71.25 ? 85  GLU   A OE2 1 
ATOM   630  N  N   . ALA   A 1 80  ? 6.081  20.262  21.860 1.00 38.23 ? 86  ALA   A N   1 
ATOM   631  C  CA  . ALA   A 1 80  ? 7.341  20.906  22.215 1.00 38.69 ? 86  ALA   A CA  1 
ATOM   632  C  C   . ALA   A 1 80  ? 8.100  20.132  23.292 1.00 39.36 ? 86  ALA   A C   1 
ATOM   633  O  O   . ALA   A 1 80  ? 7.490  19.458  24.129 1.00 40.54 ? 86  ALA   A O   1 
ATOM   634  C  CB  . ALA   A 1 80  ? 7.083  22.339  22.698 1.00 39.12 ? 86  ALA   A CB  1 
ATOM   635  N  N   . SER   A 1 81  ? 9.425  20.242  23.263 1.00 38.37 ? 87  SER   A N   1 
ATOM   636  C  CA  . SER   A 1 81  ? 10.352 19.642  24.219 1.00 38.44 ? 87  SER   A CA  1 
ATOM   637  C  C   . SER   A 1 81  ? 11.528 20.639  24.404 1.00 39.80 ? 87  SER   A C   1 
ATOM   638  O  O   . SER   A 1 81  ? 11.533 21.719  23.802 1.00 40.43 ? 87  SER   A O   1 
ATOM   639  C  CB  . SER   A 1 81  ? 10.851 18.285  23.685 1.00 38.33 ? 87  SER   A CB  1 
ATOM   640  O  OG  . SER   A 1 81  ? 11.773 18.432  22.615 1.00 38.20 ? 87  SER   A OG  1 
ATOM   641  N  N   . GLU   A 1 82  ? 12.523 20.296  25.229 1.00 40.33 ? 88  GLU   A N   1 
ATOM   642  C  CA  . GLU   A 1 82  ? 13.714 21.132  25.398 1.00 40.56 ? 88  GLU   A CA  1 
ATOM   643  C  C   . GLU   A 1 82  ? 14.609 21.161  24.141 1.00 39.00 ? 88  GLU   A C   1 
ATOM   644  O  O   . GLU   A 1 82  ? 15.491 22.016  24.033 1.00 39.77 ? 88  GLU   A O   1 
ATOM   645  C  CB  . GLU   A 1 82  ? 14.524 20.675  26.627 1.00 46.07 ? 88  GLU   A CB  1 
ATOM   646  C  CG  . GLU   A 1 82  ? 14.694 19.163  26.722 1.00 54.06 ? 88  GLU   A CG  1 
ATOM   647  C  CD  . GLU   A 1 82  ? 15.802 18.691  27.643 1.00 63.78 ? 88  GLU   A CD  1 
ATOM   648  O  OE1 . GLU   A 1 82  ? 16.571 19.546  28.143 1.00 65.57 ? 88  GLU   A OE1 1 
ATOM   649  O  OE2 . GLU   A 1 82  ? 15.908 17.461  27.858 1.00 66.59 ? 88  GLU   A OE2 1 
ATOM   650  N  N   . TYR   A 1 83  ? 14.379 20.234  23.177 1.00 36.26 ? 89  TYR   A N   1 
ATOM   651  C  CA  . TYR   A 1 83  ? 15.156 20.130  21.940 1.00 34.17 ? 89  TYR   A CA  1 
ATOM   652  C  C   . TYR   A 1 83  ? 14.464 20.768  20.723 1.00 32.41 ? 89  TYR   A C   1 
ATOM   653  O  O   . TYR   A 1 83  ? 15.155 21.203  19.806 1.00 32.85 ? 89  TYR   A O   1 
ATOM   654  C  CB  . TYR   A 1 83  ? 15.481 18.654  21.641 1.00 33.20 ? 89  TYR   A CB  1 
ATOM   655  C  CG  . TYR   A 1 83  ? 15.953 17.862  22.846 1.00 33.40 ? 89  TYR   A CG  1 
ATOM   656  C  CD1 . TYR   A 1 83  ? 17.286 17.868  23.228 1.00 34.66 ? 89  TYR   A CD1 1 
ATOM   657  C  CD2 . TYR   A 1 83  ? 15.071 17.087  23.581 1.00 34.23 ? 89  TYR   A CD2 1 
ATOM   658  C  CE1 . TYR   A 1 83  ? 17.735 17.095  24.293 1.00 36.17 ? 89  TYR   A CE1 1 
ATOM   659  C  CE2 . TYR   A 1 83  ? 15.504 16.318  24.656 1.00 36.12 ? 89  TYR   A CE2 1 
ATOM   660  C  CZ  . TYR   A 1 83  ? 16.834 16.351  25.032 1.00 37.81 ? 89  TYR   A CZ  1 
ATOM   661  O  OH  . TYR   A 1 83  ? 17.259 15.600  26.112 1.00 40.86 ? 89  TYR   A OH  1 
ATOM   662  N  N   . TYR   A 1 84  ? 13.116 20.815  20.694 1.00 30.64 ? 90  TYR   A N   1 
ATOM   663  C  CA  . TYR   A 1 84  ? 12.409 21.391  19.537 1.00 29.39 ? 90  TYR   A CA  1 
ATOM   664  C  C   . TYR   A 1 84  ? 11.146 22.123  19.966 1.00 31.48 ? 90  TYR   A C   1 
ATOM   665  O  O   . TYR   A 1 84  ? 10.469 21.678  20.889 1.00 32.42 ? 90  TYR   A O   1 
ATOM   666  C  CB  . TYR   A 1 84  ? 11.936 20.269  18.572 1.00 26.94 ? 90  TYR   A CB  1 
ATOM   667  C  CG  . TYR   A 1 84  ? 13.011 19.371  17.998 1.00 24.23 ? 90  TYR   A CG  1 
ATOM   668  C  CD1 . TYR   A 1 84  ? 13.175 18.067  18.455 1.00 23.45 ? 90  TYR   A CD1 1 
ATOM   669  C  CD2 . TYR   A 1 84  ? 13.806 19.791  16.941 1.00 23.57 ? 90  TYR   A CD2 1 
ATOM   670  C  CE1 . TYR   A 1 84  ? 14.143 17.226  17.913 1.00 22.05 ? 90  TYR   A CE1 1 
ATOM   671  C  CE2 . TYR   A 1 84  ? 14.785 18.960  16.397 1.00 23.35 ? 90  TYR   A CE2 1 
ATOM   672  C  CZ  . TYR   A 1 84  ? 14.919 17.657  16.855 1.00 22.83 ? 90  TYR   A CZ  1 
ATOM   673  O  OH  . TYR   A 1 84  ? 15.902 16.818  16.352 1.00 22.08 ? 90  TYR   A OH  1 
ATOM   674  N  N   . PRO   A 1 85  ? 10.725 23.159  19.216 1.00 32.07 ? 91  PRO   A N   1 
ATOM   675  C  CA  . PRO   A 1 85  ? 9.382  23.720  19.471 1.00 33.22 ? 91  PRO   A CA  1 
ATOM   676  C  C   . PRO   A 1 85  ? 8.320  22.715  18.946 1.00 34.33 ? 91  PRO   A C   1 
ATOM   677  O  O   . PRO   A 1 85  ? 8.669  21.706  18.290 1.00 34.79 ? 91  PRO   A O   1 
ATOM   678  C  CB  . PRO   A 1 85  ? 9.381  25.013  18.643 1.00 34.19 ? 91  PRO   A CB  1 
ATOM   679  C  CG  . PRO   A 1 85  ? 10.307 24.702  17.478 1.00 34.12 ? 91  PRO   A CG  1 
ATOM   680  C  CD  . PRO   A 1 85  ? 11.374 23.761  18.030 1.00 32.17 ? 91  PRO   A CD  1 
ATOM   681  N  N   . ALA   A 1 86  ? 7.024  22.975  19.201 1.00 35.00 ? 92  ALA   A N   1 
ATOM   682  C  CA  . ALA   A 1 86  ? 5.930  22.129  18.685 1.00 35.74 ? 92  ALA   A CA  1 
ATOM   683  C  C   . ALA   A 1 86  ? 5.991  22.187  17.130 1.00 35.02 ? 92  ALA   A C   1 
ATOM   684  O  O   . ALA   A 1 86  ? 6.183  23.275  16.570 1.00 35.62 ? 92  ALA   A O   1 
ATOM   685  C  CB  . ALA   A 1 86  ? 4.598  22.668  19.182 1.00 36.43 ? 92  ALA   A CB  1 
ATOM   686  N  N   . ARG   A 1 87  ? 5.968  21.020  16.450 1.00 33.12 ? 93  ARG   A N   1 
ATOM   687  C  CA  . ARG   A 1 87  ? 6.169  21.011  14.994 1.00 31.28 ? 93  ARG   A CA  1 
ATOM   688  C  C   . ARG   A 1 87  ? 5.683  19.716  14.340 1.00 31.02 ? 93  ARG   A C   1 
ATOM   689  O  O   . ARG   A 1 87  ? 5.378  18.765  15.058 1.00 31.66 ? 93  ARG   A O   1 
ATOM   690  C  CB  . ARG   A 1 87  ? 7.684  21.173  14.733 1.00 30.34 ? 93  ARG   A CB  1 
ATOM   691  C  CG  . ARG   A 1 87  ? 8.488  19.850  14.959 1.00 28.85 ? 93  ARG   A CG  1 
ATOM   692  C  CD  . ARG   A 1 87  ? 9.932  20.054  15.334 1.00 28.97 ? 93  ARG   A CD  1 
ATOM   693  N  NE  . ARG   A 1 87  ? 10.825 18.976  14.882 1.00 28.23 ? 93  ARG   A NE  1 
ATOM   694  C  CZ  . ARG   A 1 87  ? 10.896 17.771  15.441 1.00 27.44 ? 93  ARG   A CZ  1 
ATOM   695  N  NH1 . ARG   A 1 87  ? 11.781 16.879  15.000 1.00 23.23 ? 93  ARG   A NH1 1 
ATOM   696  N  NH2 . ARG   A 1 87  ? 10.123 17.467  16.484 1.00 26.73 ? 93  ARG   A NH2 1 
ATOM   697  N  N   . TYR   A 1 88  ? 5.694  19.642  12.985 1.00 30.07 ? 94  TYR   A N   1 
ATOM   698  C  CA  . TYR   A 1 88  ? 5.432  18.357  12.332 1.00 30.21 ? 94  TYR   A CA  1 
ATOM   699  C  C   . TYR   A 1 88  ? 6.795  17.705  12.095 1.00 27.39 ? 94  TYR   A C   1 
ATOM   700  O  O   . TYR   A 1 88  ? 7.720  18.350  11.583 1.00 26.25 ? 94  TYR   A O   1 
ATOM   701  C  CB  . TYR   A 1 88  ? 4.752  18.510  10.973 1.00 32.09 ? 94  TYR   A CB  1 
ATOM   702  C  CG  . TYR   A 1 88  ? 3.308  18.933  11.071 1.00 35.93 ? 94  TYR   A CG  1 
ATOM   703  C  CD1 . TYR   A 1 88  ? 2.299  17.997  11.229 1.00 38.08 ? 94  TYR   A CD1 1 
ATOM   704  C  CD2 . TYR   A 1 88  ? 2.950  20.269  10.972 1.00 38.00 ? 94  TYR   A CD2 1 
ATOM   705  C  CE1 . TYR   A 1 88  ? 0.963  18.380  11.296 1.00 40.56 ? 94  TYR   A CE1 1 
ATOM   706  C  CE2 . TYR   A 1 88  ? 1.621  20.667  11.034 1.00 39.81 ? 94  TYR   A CE2 1 
ATOM   707  C  CZ  . TYR   A 1 88  ? 0.631  19.722  11.214 1.00 41.98 ? 94  TYR   A CZ  1 
ATOM   708  O  OH  . TYR   A 1 88  ? -0.683 20.132  11.267 1.00 45.82 ? 94  TYR   A OH  1 
ATOM   709  N  N   . GLN   A 1 89  ? 6.916  16.427  12.465 1.00 24.79 ? 95  GLN   A N   1 
ATOM   710  C  CA  . GLN   A 1 89  ? 8.129  15.661  12.193 1.00 23.08 ? 95  GLN   A CA  1 
ATOM   711  C  C   . GLN   A 1 89  ? 7.814  14.747  10.999 1.00 22.93 ? 95  GLN   A C   1 
ATOM   712  O  O   . GLN   A 1 89  ? 6.764  14.079  10.972 1.00 23.82 ? 95  GLN   A O   1 
ATOM   713  C  CB  . GLN   A 1 89  ? 8.576  14.852  13.430 1.00 23.13 ? 95  GLN   A CB  1 
ATOM   714  C  CG  . GLN   A 1 89  ? 9.768  13.883  13.116 1.00 22.31 ? 95  GLN   A CG  1 
ATOM   715  C  CD  . GLN   A 1 89  ? 10.465 13.400  14.380 1.00 23.48 ? 95  GLN   A CD  1 
ATOM   716  O  OE1 . GLN   A 1 89  ? 10.592 14.148  15.371 1.00 23.27 ? 95  GLN   A OE1 1 
ATOM   717  N  NE2 . GLN   A 1 89  ? 10.982 12.148  14.360 1.00 20.62 ? 95  GLN   A NE2 1 
ATOM   718  N  N   . SER   A 1 90  ? 8.648  14.795  9.958  1.00 21.14 ? 96  SER   A N   1 
ATOM   719  C  CA  . SER   A 1 90  ? 8.412  14.010  8.751  1.00 20.87 ? 96  SER   A CA  1 
ATOM   720  C  C   . SER   A 1 90  ? 9.103  12.633  8.829  1.00 20.79 ? 96  SER   A C   1 
ATOM   721  O  O   . SER   A 1 90  ? 9.998  12.423  9.671  1.00 20.45 ? 96  SER   A O   1 
ATOM   722  C  CB  . SER   A 1 90  ? 8.944  14.767  7.532  1.00 22.33 ? 96  SER   A CB  1 
ATOM   723  O  OG  . SER   A 1 90  ? 10.349 14.948  7.666  1.00 23.52 ? 96  SER   A OG  1 
ATOM   724  N  N   . HIS   A 1 91  ? 8.652  11.699  7.952  1.00 20.95 ? 97  HIS   A N   1 
ATOM   725  C  CA  . HIS   A 1 91  ? 9.214  10.358  7.841  1.00 21.17 ? 97  HIS   A CA  1 
ATOM   726  C  C   . HIS   A 1 91  ? 9.078  9.574   9.181  1.00 21.32 ? 97  HIS   A C   1 
ATOM   727  O  O   . HIS   A 1 91  ? 9.936  8.741   9.504  1.00 21.11 ? 97  HIS   A O   1 
ATOM   728  C  CB  . HIS   A 1 91  ? 10.686 10.457  7.383  1.00 22.03 ? 97  HIS   A CB  1 
ATOM   729  C  CG  . HIS   A 1 91  ? 10.845 11.063  6.009  1.00 23.59 ? 97  HIS   A CG  1 
ATOM   730  N  ND1 . HIS   A 1 91  ? 10.843 10.274  4.857  1.00 26.48 ? 97  HIS   A ND1 1 
ATOM   731  C  CD2 . HIS   A 1 91  ? 10.947 12.361  5.640  1.00 25.15 ? 97  HIS   A CD2 1 
ATOM   732  C  CE1 . HIS   A 1 91  ? 10.947 11.114  3.832  1.00 25.95 ? 97  HIS   A CE1 1 
ATOM   733  N  NE2 . HIS   A 1 91  ? 11.006 12.377  4.244  1.00 25.36 ? 97  HIS   A NE2 1 
ATOM   734  N  N   . LEU   A 1 92  ? 8.008  9.861   9.951  1.00 20.45 ? 98  LEU   A N   1 
ATOM   735  C  CA  . LEU   A 1 92  ? 7.776  9.221   11.264 1.00 20.40 ? 98  LEU   A CA  1 
ATOM   736  C  C   . LEU   A 1 92  ? 6.716  8.100   11.187 1.00 20.64 ? 98  LEU   A C   1 
ATOM   737  O  O   . LEU   A 1 92  ? 5.696  8.270   10.522 1.00 21.26 ? 98  LEU   A O   1 
ATOM   738  C  CB  . LEU   A 1 92  ? 7.329  10.307  12.288 1.00 20.25 ? 98  LEU   A CB  1 
ATOM   739  C  CG  . LEU   A 1 92  ? 7.210  9.907   13.769 1.00 21.62 ? 98  LEU   A CG  1 
ATOM   740  C  CD1 . LEU   A 1 92  ? 8.563  9.504   14.337 1.00 21.20 ? 98  LEU   A CD1 1 
ATOM   741  C  CD2 . LEU   A 1 92  ? 6.564  11.060  14.605 1.00 24.23 ? 98  LEU   A CD2 1 
ATOM   742  N  N   . MET   A 1 93  ? 6.940  6.985   11.907 1.00 19.53 ? 99  MET   A N   1 
ATOM   743  C  CA  . MET   A 1 93  ? 6.002  5.838   11.898 1.00 19.82 ? 99  MET   A CA  1 
ATOM   744  C  C   . MET   A 1 93  ? 5.566  5.568   13.334 1.00 21.47 ? 99  MET   A C   1 
ATOM   745  O  O   . MET   A 1 93  ? 6.436  5.525   14.203 1.00 22.98 ? 99  MET   A O   1 
ATOM   746  C  CB  . MET   A 1 93  ? 6.745  4.601   11.364 1.00 19.75 ? 99  MET   A CB  1 
ATOM   747  C  CG  . MET   A 1 93  ? 7.328  4.837   9.937  1.00 22.90 ? 99  MET   A CG  1 
ATOM   748  S  SD  . MET   A 1 93  ? 8.382  3.487   9.412  1.00 25.02 ? 99  MET   A SD  1 
ATOM   749  C  CE  . MET   A 1 93  ? 9.840  3.726   10.378 1.00 23.65 ? 99  MET   A CE  1 
ATOM   750  N  N   . LEU   A 1 94  ? 4.258  5.369   13.601 1.00 20.52 ? 100 LEU   A N   1 
ATOM   751  C  CA  . LEU   A 1 94  ? 3.808  5.130   14.972 1.00 21.03 ? 100 LEU   A CA  1 
ATOM   752  C  C   . LEU   A 1 94  ? 3.373  3.682   15.180 1.00 21.54 ? 100 LEU   A C   1 
ATOM   753  O  O   . LEU   A 1 94  ? 2.832  3.056   14.262 1.00 22.24 ? 100 LEU   A O   1 
ATOM   754  C  CB  . LEU   A 1 94  ? 2.601  6.019   15.330 1.00 22.78 ? 100 LEU   A CB  1 
ATOM   755  C  CG  . LEU   A 1 94  ? 2.826  7.538   15.304 1.00 26.27 ? 100 LEU   A CG  1 
ATOM   756  C  CD1 . LEU   A 1 94  ? 1.567  8.287   15.793 1.00 28.30 ? 100 LEU   A CD1 1 
ATOM   757  C  CD2 . LEU   A 1 94  ? 3.995  7.950   16.138 1.00 27.67 ? 100 LEU   A CD2 1 
ATOM   758  N  N   . ALA   A 1 95  ? 3.490  3.227   16.427 1.00 20.78 ? 101 ALA   A N   1 
ATOM   759  C  CA  . ALA   A 1 95  ? 3.027  1.907   16.863 1.00 20.91 ? 101 ALA   A CA  1 
ATOM   760  C  C   . ALA   A 1 95  ? 2.474  2.013   18.299 1.00 22.03 ? 101 ALA   A C   1 
ATOM   761  O  O   . ALA   A 1 95  ? 2.832  2.932   19.041 1.00 22.90 ? 101 ALA   A O   1 
ATOM   762  C  CB  . ALA   A 1 95  ? 4.191  0.939   16.863 1.00 21.14 ? 101 ALA   A CB  1 
ATOM   763  N  N   . VAL   A 1 96  ? 1.594  1.093   18.674 1.00 21.68 ? 102 VAL   A N   1 
ATOM   764  C  CA  . VAL   A 1 96  ? 1.090  1.019   20.039 1.00 22.92 ? 102 VAL   A CA  1 
ATOM   765  C  C   . VAL   A 1 96  ? 2.181  0.285   20.846 1.00 24.57 ? 102 VAL   A C   1 
ATOM   766  O  O   . VAL   A 1 96  ? 2.516  -0.876  20.552 1.00 24.80 ? 102 VAL   A O   1 
ATOM   767  C  CB  . VAL   A 1 96  ? -0.253 0.246   20.078 1.00 24.70 ? 102 VAL   A CB  1 
ATOM   768  C  CG1 . VAL   A 1 96  ? -0.679 -0.021  21.517 1.00 27.03 ? 102 VAL   A CG1 1 
ATOM   769  C  CG2 . VAL   A 1 96  ? -1.349 1.024   19.331 1.00 25.08 ? 102 VAL   A CG2 1 
ATOM   770  N  N   . GLY   A 1 97  ? 2.764  0.969   21.825 1.00 24.73 ? 103 GLY   A N   1 
ATOM   771  C  CA  . GLY   A 1 97  ? 3.840  0.367   22.608 1.00 25.40 ? 103 GLY   A CA  1 
ATOM   772  C  C   . GLY   A 1 97  ? 4.428  1.338   23.605 1.00 26.04 ? 103 GLY   A C   1 
ATOM   773  O  O   . GLY   A 1 97  ? 4.191  2.553   23.531 1.00 27.16 ? 103 GLY   A O   1 
ATOM   774  N  N   . HIS   A 1 98  ? 5.180  0.797   24.559 1.00 24.64 ? 104 HIS   A N   1 
ATOM   775  C  CA  . HIS   A 1 98  ? 5.785  1.595   25.591 1.00 24.93 ? 104 HIS   A CA  1 
ATOM   776  C  C   . HIS   A 1 98  ? 7.080  2.268   25.148 1.00 23.46 ? 104 HIS   A C   1 
ATOM   777  O  O   . HIS   A 1 98  ? 7.905  1.665   24.457 1.00 22.78 ? 104 HIS   A O   1 
ATOM   778  C  CB  . HIS   A 1 98  ? 6.068  0.702   26.829 1.00 26.35 ? 104 HIS   A CB  1 
ATOM   779  C  CG  . HIS   A 1 98  ? 6.733  1.456   27.933 1.00 29.90 ? 104 HIS   A CG  1 
ATOM   780  N  ND1 . HIS   A 1 98  ? 6.055  2.435   28.645 1.00 32.57 ? 104 HIS   A ND1 1 
ATOM   781  C  CD2 . HIS   A 1 98  ? 8.021  1.421   28.352 1.00 31.65 ? 104 HIS   A CD2 1 
ATOM   782  C  CE1 . HIS   A 1 98  ? 6.940  2.935   29.501 1.00 33.54 ? 104 HIS   A CE1 1 
ATOM   783  N  NE2 . HIS   A 1 98  ? 8.129  2.335   29.374 1.00 33.61 ? 104 HIS   A NE2 1 
ATOM   784  N  N   . SER   A 1 99  ? 7.309  3.472   25.667 1.00 23.38 ? 105 SER   A N   1 
ATOM   785  C  CA  . SER   A 1 99  ? 8.551  4.204   25.495 1.00 24.17 ? 105 SER   A CA  1 
ATOM   786  C  C   . SER   A 1 99  ? 8.691  5.310   26.567 1.00 25.92 ? 105 SER   A C   1 
ATOM   787  O  O   . SER   A 1 99  ? 7.699  5.779   27.110 1.00 26.99 ? 105 SER   A O   1 
ATOM   788  C  CB  . SER   A 1 99  ? 8.681  4.790   24.090 1.00 25.29 ? 105 SER   A CB  1 
ATOM   789  O  OG  . SER   A 1 99  ? 7.897  5.961   23.924 1.00 26.53 ? 105 SER   A OG  1 
ATOM   790  N  N   . GLU   A 1 100 ? 9.932  5.701   26.858 1.00 26.18 ? 106 GLU   A N   1 
ATOM   791  C  CA  . GLU   A 1 100 ? 10.313 6.804   27.737 1.00 27.84 ? 106 GLU   A CA  1 
ATOM   792  C  C   . GLU   A 1 100 ? 11.429 7.604   27.014 1.00 28.90 ? 106 GLU   A C   1 
ATOM   793  O  O   . GLU   A 1 100 ? 12.042 7.074   26.081 1.00 29.49 ? 106 GLU   A O   1 
ATOM   794  C  CB  . GLU   A 1 100 ? 10.721 6.296   29.136 1.00 30.60 ? 106 GLU   A CB  1 
ATOM   795  C  CG  . GLU   A 1 100 ? 9.550  5.655   29.858 1.00 35.76 ? 106 GLU   A CG  1 
ATOM   796  C  CD  . GLU   A 1 100 ? 9.884  4.856   31.105 1.00 40.15 ? 106 GLU   A CD  1 
ATOM   797  O  OE1 . GLU   A 1 100 ? 10.785 5.288   31.856 1.00 42.16 ? 106 GLU   A OE1 1 
ATOM   798  O  OE2 . GLU   A 1 100 ? 9.243  3.808   31.338 1.00 38.20 ? 106 GLU   A OE2 1 
ATOM   799  N  N   . PRO   A 1 101 ? 11.709 8.880   27.374 1.00 29.68 ? 107 PRO   A N   1 
ATOM   800  C  CA  . PRO   A 1 101 ? 12.674 9.671   26.563 1.00 29.34 ? 107 PRO   A CA  1 
ATOM   801  C  C   . PRO   A 1 101 ? 14.041 9.015   26.286 1.00 28.69 ? 107 PRO   A C   1 
ATOM   802  O  O   . PRO   A 1 101 ? 14.560 9.078   25.137 1.00 28.82 ? 107 PRO   A O   1 
ATOM   803  C  CB  . PRO   A 1 101 ? 12.801 10.974  27.340 1.00 30.59 ? 107 PRO   A CB  1 
ATOM   804  C  CG  . PRO   A 1 101 ? 11.459 11.137  28.012 1.00 31.76 ? 107 PRO   A CG  1 
ATOM   805  C  CD  . PRO   A 1 101 ? 11.041 9.709   28.396 1.00 30.05 ? 107 PRO   A CD  1 
ATOM   806  N  N   . GLY   A 1 102 ? 14.592 8.346   27.294 1.00 28.35 ? 108 GLY   A N   1 
ATOM   807  C  CA  . GLY   A 1 102 ? 15.853 7.620   27.180 1.00 28.10 ? 108 GLY   A CA  1 
ATOM   808  C  C   . GLY   A 1 102 ? 15.821 6.425   26.234 1.00 26.87 ? 108 GLY   A C   1 
ATOM   809  O  O   . GLY   A 1 102 ? 16.860 5.822   25.936 1.00 27.56 ? 108 GLY   A O   1 
ATOM   810  N  N   . ASP   A 1 103 ? 14.622 6.040   25.767 1.00 24.79 ? 109 ASP   A N   1 
ATOM   811  C  CA  . ASP   A 1 103 ? 14.480 4.962   24.794 1.00 23.28 ? 109 ASP   A CA  1 
ATOM   812  C  C   . ASP   A 1 103 ? 14.850 5.390   23.373 1.00 21.86 ? 109 ASP   A C   1 
ATOM   813  O  O   . ASP   A 1 103 ? 15.000 4.524   22.492 1.00 21.78 ? 109 ASP   A O   1 
ATOM   814  C  CB  . ASP   A 1 103 ? 13.067 4.371   24.780 1.00 24.26 ? 109 ASP   A CB  1 
ATOM   815  C  CG  . ASP   A 1 103 ? 12.798 3.526   26.007 1.00 25.30 ? 109 ASP   A CG  1 
ATOM   816  O  OD1 . ASP   A 1 103 ? 13.742 2.886   26.499 1.00 25.67 ? 109 ASP   A OD1 1 
ATOM   817  O  OD2 . ASP   A 1 103 ? 11.648 3.523   26.483 1.00 25.57 ? 109 ASP   A OD2 1 
ATOM   818  N  N   . CYS   A 1 104 ? 14.978 6.708   23.112 1.00 22.03 ? 110 CYS   A N   1 
ATOM   819  C  CA  . CYS   A 1 104 ? 15.376 7.172   21.766 1.00 21.58 ? 110 CYS   A CA  1 
ATOM   820  C  C   . CYS   A 1 104 ? 16.686 6.507   21.326 1.00 22.01 ? 110 CYS   A C   1 
ATOM   821  O  O   . CYS   A 1 104 ? 17.613 6.370   22.146 1.00 22.52 ? 110 CYS   A O   1 
ATOM   822  C  CB  . CYS   A 1 104 ? 15.473 8.695   21.730 1.00 21.74 ? 110 CYS   A CB  1 
ATOM   823  S  SG  . CYS   A 1 104 ? 13.863 9.540   21.770 1.00 24.13 ? 110 CYS   A SG  1 
ATOM   824  N  N   . GLY   A 1 105 ? 16.731 6.040   20.080 1.00 20.89 ? 111 GLY   A N   1 
ATOM   825  C  CA  . GLY   A 1 105 ? 17.930 5.383   19.585 1.00 21.22 ? 111 GLY   A CA  1 
ATOM   826  C  C   . GLY   A 1 105 ? 17.819 3.864   19.532 1.00 22.13 ? 111 GLY   A C   1 
ATOM   827  O  O   . GLY   A 1 105 ? 18.619 3.210   18.853 1.00 22.35 ? 111 GLY   A O   1 
ATOM   828  N  N   . GLY   A 1 106 ? 16.822 3.280   20.218 1.00 21.02 ? 112 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 106 ? 16.573 1.838   20.097 1.00 20.07 ? 112 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 106 ? 16.193 1.498   18.650 1.00 19.70 ? 112 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 106 ? 15.436 2.235   18.006 1.00 19.24 ? 112 GLY   A O   1 
ATOM   832  N  N   . ILE   A 1 107 ? 16.725 0.395   18.130 1.00 19.53 ? 113 ILE   A N   1 
ATOM   833  C  CA  . ILE   A 1 107 ? 16.456 0.006   16.751 1.00 19.42 ? 113 ILE   A CA  1 
ATOM   834  C  C   . ILE   A 1 107 ? 15.131 -0.730  16.573 1.00 18.54 ? 113 ILE   A C   1 
ATOM   835  O  O   . ILE   A 1 107 ? 14.755 -1.591  17.411 1.00 18.73 ? 113 ILE   A O   1 
ATOM   836  C  CB  . ILE   A 1 107 ? 17.685 -0.824  16.242 1.00 21.83 ? 113 ILE   A CB  1 
ATOM   837  C  CG1 . ILE   A 1 107 ? 18.904 0.102   15.899 1.00 22.85 ? 113 ILE   A CG1 1 
ATOM   838  C  CG2 . ILE   A 1 107 ? 17.354 -1.784  15.115 1.00 23.19 ? 113 ILE   A CG2 1 
ATOM   839  C  CD1 . ILE   A 1 107 ? 20.214 -0.682  15.592 1.00 24.86 ? 113 ILE   A CD1 1 
ATOM   840  N  N   . LEU   A 1 108 ? 14.461 -0.430  15.423 1.00 17.27 ? 114 LEU   A N   1 
ATOM   841  C  CA  . LEU   A 1 108 ? 13.281 -1.166  14.933 1.00 17.40 ? 114 LEU   A CA  1 
ATOM   842  C  C   . LEU   A 1 108 ? 13.802 -1.975  13.731 1.00 18.51 ? 114 LEU   A C   1 
ATOM   843  O  O   . LEU   A 1 108 ? 14.440 -1.422  12.805 1.00 18.20 ? 114 LEU   A O   1 
ATOM   844  C  CB  . LEU   A 1 108 ? 12.201 -0.184  14.449 1.00 17.72 ? 114 LEU   A CB  1 
ATOM   845  C  CG  . LEU   A 1 108 ? 11.028 -0.824  13.683 1.00 18.09 ? 114 LEU   A CG  1 
ATOM   846  C  CD1 . LEU   A 1 108 ? 10.224 -1.772  14.585 1.00 18.95 ? 114 LEU   A CD1 1 
ATOM   847  C  CD2 . LEU   A 1 108 ? 10.058 0.293   13.199 1.00 18.88 ? 114 LEU   A CD2 1 
ATOM   848  N  N   . ARG   A 1 109 ? 13.529 -3.306  13.744 1.00 18.14 ? 115 ARG   A N   1 
ATOM   849  C  CA  . ARG   A 1 109 ? 14.010 -4.188  12.678 1.00 18.40 ? 115 ARG   A CA  1 
ATOM   850  C  C   . ARG   A 1 109 ? 12.863 -5.027  12.145 1.00 19.87 ? 115 ARG   A C   1 
ATOM   851  O  O   . ARG   A 1 109 ? 12.040 -5.480  12.921 1.00 19.87 ? 115 ARG   A O   1 
ATOM   852  C  CB  . ARG   A 1 109 ? 14.998 -5.238  13.266 1.00 21.24 ? 115 ARG   A CB  1 
ATOM   853  C  CG  . ARG   A 1 109 ? 16.373 -4.743  13.626 1.00 28.20 ? 115 ARG   A CG  1 
ATOM   854  C  CD  . ARG   A 1 109 ? 17.223 -5.933  14.079 1.00 31.94 ? 115 ARG   A CD  1 
ATOM   855  N  NE  . ARG   A 1 109 ? 17.677 -6.642  12.889 1.00 36.45 ? 115 ARG   A NE  1 
ATOM   856  C  CZ  . ARG   A 1 109 ? 18.844 -6.419  12.286 1.00 37.75 ? 115 ARG   A CZ  1 
ATOM   857  N  NH1 . ARG   A 1 109 ? 19.143 -7.045  11.161 1.00 39.63 ? 115 ARG   A NH1 1 
ATOM   858  N  NH2 . ARG   A 1 109 ? 19.747 -5.625  12.845 1.00 37.59 ? 115 ARG   A NH2 1 
ATOM   859  N  N   . CYS   A 1 110 ? 12.901 -5.327  10.851 1.00 20.34 ? 116 CYS   A N   1 
ATOM   860  C  CA  . CYS   A 1 110 ? 11.970 -6.281  10.207 1.00 22.69 ? 116 CYS   A CA  1 
ATOM   861  C  C   . CYS   A 1 110 ? 12.823 -7.481  9.656  1.00 24.82 ? 116 CYS   A C   1 
ATOM   862  O  O   . CYS   A 1 110 ? 14.044 -7.524  9.870  1.00 24.95 ? 116 CYS   A O   1 
ATOM   863  C  CB  . CYS   A 1 110 ? 11.203 -5.578  9.094  1.00 23.68 ? 116 CYS   A CB  1 
ATOM   864  S  SG  . CYS   A 1 110 ? 12.264 -5.083  7.706  1.00 24.62 ? 116 CYS   A SG  1 
ATOM   865  N  N   . GLN   A 1 111 ? 12.197 -8.465  8.969  1.00 27.27 ? 117 GLN   A N   1 
ATOM   866  C  CA  . GLN   A 1 111 ? 12.958 -9.582  8.392  1.00 29.82 ? 117 GLN   A CA  1 
ATOM   867  C  C   . GLN   A 1 111 ? 14.079 -9.128  7.389  1.00 31.28 ? 117 GLN   A C   1 
ATOM   868  O  O   . GLN   A 1 111 ? 15.047 -9.871  7.161  1.00 33.30 ? 117 GLN   A O   1 
ATOM   869  C  CB  . GLN   A 1 111 ? 11.991 -10.563 7.694  1.00 33.80 ? 117 GLN   A CB  1 
ATOM   870  C  CG  . GLN   A 1 111 ? 11.188 -9.901  6.562  1.00 38.62 ? 117 GLN   A CG  1 
ATOM   871  C  CD  . GLN   A 1 111 ? 10.248 -10.870 5.874  1.00 45.78 ? 117 GLN   A CD  1 
ATOM   872  O  OE1 . GLN   A 1 111 ? 9.042  -10.597 5.725  1.00 48.07 ? 117 GLN   A OE1 1 
ATOM   873  N  NE2 . GLN   A 1 111 ? 10.786 -12.010 5.420  1.00 45.03 ? 117 GLN   A NE2 1 
ATOM   874  N  N   . HIS   A 1 112 ? 13.966 -7.915  6.815  1.00 29.73 ? 118 HIS   A N   1 
ATOM   875  C  CA  . HIS   A 1 112 ? 14.957 -7.445  5.821  1.00 28.87 ? 118 HIS   A CA  1 
ATOM   876  C  C   . HIS   A 1 112 ? 16.143 -6.670  6.431  1.00 28.10 ? 118 HIS   A C   1 
ATOM   877  O  O   . HIS   A 1 112 ? 17.148 -6.439  5.754  1.00 29.35 ? 118 HIS   A O   1 
ATOM   878  C  CB  . HIS   A 1 112 ? 14.277 -6.618  4.703  1.00 29.52 ? 118 HIS   A CB  1 
ATOM   879  C  CG  . HIS   A 1 112 ? 13.083 -7.297  4.082  1.00 31.96 ? 118 HIS   A CG  1 
ATOM   880  N  ND1 . HIS   A 1 112 ? 11.794 -6.860  4.327  1.00 33.18 ? 118 HIS   A ND1 1 
ATOM   881  C  CD2 . HIS   A 1 112 ? 13.024 -8.369  3.255  1.00 34.34 ? 118 HIS   A CD2 1 
ATOM   882  C  CE1 . HIS   A 1 112 ? 10.990 -7.683  3.685  1.00 35.22 ? 118 HIS   A CE1 1 
ATOM   883  N  NE2 . HIS   A 1 112 ? 11.681 -8.606  3.007  1.00 36.25 ? 118 HIS   A NE2 1 
ATOM   884  N  N   . GLY   A 1 113 ? 16.020 -6.253  7.696  1.00 25.27 ? 119 GLY   A N   1 
ATOM   885  C  CA  . GLY   A 1 113 ? 17.080 -5.485  8.339  1.00 24.06 ? 119 GLY   A CA  1 
ATOM   886  C  C   . GLY   A 1 113 ? 16.583 -4.293  9.147  1.00 21.19 ? 119 GLY   A C   1 
ATOM   887  O  O   . GLY   A 1 113 ? 15.454 -4.281  9.619  1.00 21.24 ? 119 GLY   A O   1 
ATOM   888  N  N   . VAL   A 1 114 ? 17.457 -3.329  9.378  1.00 20.70 ? 120 VAL   A N   1 
ATOM   889  C  CA  . VAL   A 1 114 ? 17.153 -2.128  10.127 1.00 20.68 ? 120 VAL   A CA  1 
ATOM   890  C  C   . VAL   A 1 114 ? 16.162 -1.204  9.401  1.00 20.19 ? 120 VAL   A C   1 
ATOM   891  O  O   . VAL   A 1 114 ? 16.421 -0.809  8.255  1.00 20.88 ? 120 VAL   A O   1 
ATOM   892  C  CB  . VAL   A 1 114 ? 18.436 -1.359  10.533 1.00 21.86 ? 120 VAL   A CB  1 
ATOM   893  C  CG1 . VAL   A 1 114 ? 18.058 -0.041  11.230 1.00 22.75 ? 120 VAL   A CG1 1 
ATOM   894  C  CG2 . VAL   A 1 114 ? 19.314 -2.228  11.457 1.00 22.48 ? 120 VAL   A CG2 1 
ATOM   895  N  N   . VAL   A 1 115 ? 15.048 -0.865  10.076 1.00 18.77 ? 121 VAL   A N   1 
ATOM   896  C  CA  . VAL   A 1 115 ? 13.991 0.013   9.542  1.00 18.69 ? 121 VAL   A CA  1 
ATOM   897  C  C   . VAL   A 1 115 ? 14.145 1.472   10.000 1.00 18.75 ? 121 VAL   A C   1 
ATOM   898  O  O   . VAL   A 1 115 ? 13.950 2.417   9.222  1.00 19.13 ? 121 VAL   A O   1 
ATOM   899  C  CB  . VAL   A 1 115 ? 12.593 -0.526  9.954  1.00 19.91 ? 121 VAL   A CB  1 
ATOM   900  C  CG1 . VAL   A 1 115 ? 11.475 0.432   9.548  1.00 20.06 ? 121 VAL   A CG1 1 
ATOM   901  C  CG2 . VAL   A 1 115 ? 12.347 -1.915  9.392  1.00 22.18 ? 121 VAL   A CG2 1 
ATOM   902  N  N   . GLY   A 1 116 ? 14.413 1.651   11.299 1.00 17.76 ? 122 GLY   A N   1 
ATOM   903  C  CA  . GLY   A 1 116 ? 14.581 3.006   11.832 1.00 18.78 ? 122 GLY   A CA  1 
ATOM   904  C  C   . GLY   A 1 116 ? 14.979 2.989   13.294 1.00 18.54 ? 122 GLY   A C   1 
ATOM   905  O  O   . GLY   A 1 116 ? 15.395 1.945   13.818 1.00 17.70 ? 122 GLY   A O   1 
ATOM   906  N  N   . ILE   A 1 117 ? 14.894 4.156   13.943 1.00 18.34 ? 123 ILE   A N   1 
ATOM   907  C  CA  . ILE   A 1 117 ? 15.251 4.232   15.367 1.00 18.13 ? 123 ILE   A CA  1 
ATOM   908  C  C   . ILE   A 1 117 ? 14.151 4.940   16.156 1.00 17.42 ? 123 ILE   A C   1 
ATOM   909  O  O   . ILE   A 1 117 ? 13.477 5.820   15.628 1.00 16.75 ? 123 ILE   A O   1 
ATOM   910  C  CB  . ILE   A 1 117 ? 16.598 4.990   15.559 1.00 19.72 ? 123 ILE   A CB  1 
ATOM   911  C  CG1 . ILE   A 1 117 ? 16.613 6.320   14.780 1.00 21.70 ? 123 ILE   A CG1 1 
ATOM   912  C  CG2 . ILE   A 1 117 ? 17.822 4.119   15.262 1.00 21.66 ? 123 ILE   A CG2 1 
ATOM   913  C  CD1 . ILE   A 1 117 ? 17.850 7.189   15.267 1.00 23.92 ? 123 ILE   A CD1 1 
ATOM   914  N  N   . VAL   A 1 118 ? 13.935 4.551   17.427 1.00 17.49 ? 124 VAL   A N   1 
ATOM   915  C  CA  . VAL   A 1 118 ? 12.951 5.259   18.263 1.00 17.12 ? 124 VAL   A CA  1 
ATOM   916  C  C   . VAL   A 1 118 ? 13.264 6.768   18.334 1.00 17.19 ? 124 VAL   A C   1 
ATOM   917  O  O   . VAL   A 1 118 ? 14.417 7.162   18.554 1.00 17.55 ? 124 VAL   A O   1 
ATOM   918  C  CB  . VAL   A 1 118 ? 12.935 4.671   19.679 1.00 18.06 ? 124 VAL   A CB  1 
ATOM   919  C  CG1 . VAL   A 1 118 ? 12.028 5.480   20.601 1.00 20.43 ? 124 VAL   A CG1 1 
ATOM   920  C  CG2 . VAL   A 1 118 ? 12.508 3.194   19.662 1.00 18.38 ? 124 VAL   A CG2 1 
ATOM   921  N  N   . SER   A 1 119 ? 12.234 7.593   18.151 1.00 17.61 ? 125 SER   A N   1 
ATOM   922  C  CA  . SER   A 1 119 ? 12.449 9.050   18.143 1.00 18.55 ? 125 SER   A CA  1 
ATOM   923  C  C   . SER   A 1 119 ? 11.421 9.852   18.940 1.00 20.11 ? 125 SER   A C   1 
ATOM   924  O  O   . SER   A 1 119 ? 11.749 10.955  19.396 1.00 21.21 ? 125 SER   A O   1 
ATOM   925  C  CB  . SER   A 1 119 ? 12.529 9.551   16.700 1.00 20.48 ? 125 SER   A CB  1 
ATOM   926  O  OG  . SER   A 1 119 ? 12.524 10.969  16.578 1.00 21.14 ? 125 SER   A OG  1 
ATOM   927  N  N   . THR   A 1 120 ? 10.176 9.343   19.072 1.00 20.85 ? 126 THR   A N   1 
ATOM   928  C  CA  . THR   A 1 120 ? 9.144  10.065  19.863 1.00 22.53 ? 126 THR   A CA  1 
ATOM   929  C  C   . THR   A 1 120 ? 8.293  9.081   20.695 1.00 23.66 ? 126 THR   A C   1 
ATOM   930  O  O   . THR   A 1 120 ? 8.361  7.854   20.496 1.00 23.01 ? 126 THR   A O   1 
ATOM   931  C  CB  . THR   A 1 120 ? 8.177  10.861  18.930 1.00 23.98 ? 126 THR   A CB  1 
ATOM   932  O  OG1 . THR   A 1 120 ? 7.314  9.941   18.255 1.00 26.00 ? 126 THR   A OG1 1 
ATOM   933  C  CG2 . THR   A 1 120 ? 8.879  11.797  17.943 1.00 24.09 ? 126 THR   A CG2 1 
ATOM   934  N  N   . GLY   A 1 121 ? 7.449  9.618   21.588 1.00 24.55 ? 127 GLY   A N   1 
ATOM   935  C  CA  . GLY   A 1 121 ? 6.520  8.774   22.304 1.00 26.54 ? 127 GLY   A CA  1 
ATOM   936  C  C   . GLY   A 1 121 ? 5.569  9.548   23.183 1.00 29.15 ? 127 GLY   A C   1 
ATOM   937  O  O   . GLY   A 1 121 ? 5.745  10.741  23.401 1.00 30.73 ? 127 GLY   A O   1 
ATOM   938  N  N   . GLY   A 1 122 ? 4.593  8.843   23.704 1.00 31.15 ? 128 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 122 ? 3.618  9.458   24.609 1.00 33.72 ? 128 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 122 ? 2.266  8.792   24.473 1.00 35.52 ? 128 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 122 ? 1.942  8.284   23.398 1.00 35.07 ? 128 GLY   A O   1 
ATOM   942  N  N   . ASN   A 1 123 ? 1.502  8.726   25.561 1.00 36.82 ? 129 ASN   A N   1 
ATOM   943  C  CA  . ASN   A 1 123 ? 0.153  8.156   25.546 1.00 38.20 ? 129 ASN   A CA  1 
ATOM   944  C  C   . ASN   A 1 123 ? 0.051  6.708   25.072 1.00 38.02 ? 129 ASN   A C   1 
ATOM   945  O  O   . ASN   A 1 123 ? -1.002 6.308   24.576 1.00 39.76 ? 129 ASN   A O   1 
ATOM   946  C  CB  . ASN   A 1 123 ? -0.762 9.044   24.700 1.00 40.88 ? 129 ASN   A CB  1 
ATOM   947  C  CG  . ASN   A 1 123 ? -0.937 10.428  25.273 1.00 46.40 ? 129 ASN   A CG  1 
ATOM   948  O  OD1 . ASN   A 1 123 ? -1.162 10.587  26.476 1.00 48.87 ? 129 ASN   A OD1 1 
ATOM   949  N  ND2 . ASN   A 1 123 ? -0.877 11.448  24.421 1.00 46.29 ? 129 ASN   A ND2 1 
ATOM   950  N  N   . GLY   A 1 124 ? 1.101  5.920   25.274 1.00 35.56 ? 130 GLY   A N   1 
ATOM   951  C  CA  . GLY   A 1 124 ? 1.097  4.539   24.840 1.00 34.60 ? 130 GLY   A CA  1 
ATOM   952  C  C   . GLY   A 1 124 ? 1.393  4.339   23.365 1.00 32.94 ? 130 GLY   A C   1 
ATOM   953  O  O   . GLY   A 1 124 ? 1.195  3.233   22.855 1.00 33.90 ? 130 GLY   A O   1 
ATOM   954  N  N   . LEU   A 1 125 ? 1.916  5.374   22.689 1.00 31.04 ? 131 LEU   A N   1 
ATOM   955  C  CA  . LEU   A 1 125 ? 2.306  5.291   21.284 1.00 29.60 ? 131 LEU   A CA  1 
ATOM   956  C  C   . LEU   A 1 125 ? 3.797  5.578   21.195 1.00 28.70 ? 131 LEU   A C   1 
ATOM   957  O  O   . LEU   A 1 125 ? 4.267  6.525   21.821 1.00 30.80 ? 131 LEU   A O   1 
ATOM   958  C  CB  . LEU   A 1 125 ? 1.546  6.330   20.445 1.00 30.50 ? 131 LEU   A CB  1 
ATOM   959  C  CG  . LEU   A 1 125 ? 0.032  6.138   20.379 1.00 33.40 ? 131 LEU   A CG  1 
ATOM   960  C  CD1 . LEU   A 1 125 ? -0.662 7.425   20.035 1.00 34.97 ? 131 LEU   A CD1 1 
ATOM   961  C  CD2 . LEU   A 1 125 ? -0.333 5.030   19.370 1.00 33.90 ? 131 LEU   A CD2 1 
ATOM   962  N  N   . VAL   A 1 126 ? 4.545  4.804   20.391 1.00 24.54 ? 132 VAL   A N   1 
ATOM   963  C  CA  . VAL   A 1 126 ? 5.953  5.034   20.214 1.00 22.14 ? 132 VAL   A CA  1 
ATOM   964  C  C   . VAL   A 1 126 ? 6.167  5.378   18.725 1.00 21.47 ? 132 VAL   A C   1 
ATOM   965  O  O   . VAL   A 1 126 ? 5.533  4.760   17.864 1.00 21.56 ? 132 VAL   A O   1 
ATOM   966  C  CB  . VAL   A 1 126 ? 6.768  3.780   20.632 1.00 22.35 ? 132 VAL   A CB  1 
ATOM   967  C  CG1 . VAL   A 1 126 ? 6.262  2.511   19.943 1.00 23.18 ? 132 VAL   A CG1 1 
ATOM   968  C  CG2 . VAL   A 1 126 ? 8.273  3.983   20.418 1.00 22.17 ? 132 VAL   A CG2 1 
ATOM   969  N  N   . GLY   A 1 127 ? 7.024  6.368   18.457 1.00 19.95 ? 133 GLY   A N   1 
ATOM   970  C  CA  . GLY   A 1 127 ? 7.334  6.792   17.094 1.00 19.01 ? 133 GLY   A CA  1 
ATOM   971  C  C   . GLY   A 1 127 ? 8.766  6.482   16.688 1.00 20.12 ? 133 GLY   A C   1 
ATOM   972  O  O   . GLY   A 1 127 ? 9.685  6.610   17.505 1.00 20.97 ? 133 GLY   A O   1 
ATOM   973  N  N   . PHE   A 1 128 ? 8.962  6.029   15.421 1.00 19.14 ? 134 PHE   A N   1 
ATOM   974  C  CA  . PHE   A 1 128 ? 10.268 5.630   14.862 1.00 18.81 ? 134 PHE   A CA  1 
ATOM   975  C  C   . PHE   A 1 128 ? 10.586 6.497   13.627 1.00 18.69 ? 134 PHE   A C   1 
ATOM   976  O  O   . PHE   A 1 128 ? 9.748  6.667   12.745 1.00 19.53 ? 134 PHE   A O   1 
ATOM   977  C  CB  . PHE   A 1 128 ? 10.243 4.146   14.397 1.00 18.81 ? 134 PHE   A CB  1 
ATOM   978  C  CG  . PHE   A 1 128 ? 9.712  3.199   15.469 1.00 18.80 ? 134 PHE   A CG  1 
ATOM   979  C  CD1 . PHE   A 1 128 ? 10.559 2.660   16.422 1.00 19.13 ? 134 PHE   A CD1 1 
ATOM   980  C  CD2 . PHE   A 1 128 ? 8.388  2.769   15.451 1.00 19.86 ? 134 PHE   A CD2 1 
ATOM   981  C  CE1 . PHE   A 1 128 ? 10.076 1.786   17.402 1.00 19.05 ? 134 PHE   A CE1 1 
ATOM   982  C  CE2 . PHE   A 1 128 ? 7.918  1.858   16.403 1.00 19.92 ? 134 PHE   A CE2 1 
ATOM   983  C  CZ  . PHE   A 1 128 ? 8.773  1.362   17.366 1.00 19.01 ? 134 PHE   A CZ  1 
ATOM   984  N  N   . ALA   A 1 129 ? 11.817 7.026   13.585 1.00 17.75 ? 135 ALA   A N   1 
ATOM   985  C  CA  . ALA   A 1 129 ? 12.321 7.781   12.462 1.00 17.30 ? 135 ALA   A CA  1 
ATOM   986  C  C   . ALA   A 1 129 ? 12.797 6.744   11.441 1.00 18.27 ? 135 ALA   A C   1 
ATOM   987  O  O   . ALA   A 1 129 ? 13.714 5.938   11.723 1.00 17.20 ? 135 ALA   A O   1 
ATOM   988  C  CB  . ALA   A 1 129 ? 13.492 8.656   12.902 1.00 17.17 ? 135 ALA   A CB  1 
ATOM   989  N  N   . ASP   A 1 130 ? 12.162 6.751   10.254 1.00 18.06 ? 136 ASP   A N   1 
ATOM   990  C  CA  . ASP   A 1 130 ? 12.469 5.822   9.157  1.00 19.47 ? 136 ASP   A CA  1 
ATOM   991  C  C   . ASP   A 1 130 ? 13.806 6.152   8.554  1.00 19.63 ? 136 ASP   A C   1 
ATOM   992  O  O   . ASP   A 1 130 ? 14.130 7.345   8.419  1.00 19.76 ? 136 ASP   A O   1 
ATOM   993  C  CB  . ASP   A 1 130 ? 11.412 5.960   8.038  1.00 21.77 ? 136 ASP   A CB  1 
ATOM   994  C  CG  . ASP   A 1 130 ? 11.538 4.924   6.913  1.00 25.53 ? 136 ASP   A CG  1 
ATOM   995  O  OD1 . ASP   A 1 130 ? 11.705 3.740   7.221  1.00 24.23 ? 136 ASP   A OD1 1 
ATOM   996  O  OD2 . ASP   A 1 130 ? 11.546 5.328   5.721  1.00 29.39 ? 136 ASP   A OD2 1 
ATOM   997  N  N   . VAL   A 1 131 ? 14.584 5.099   8.142  1.00 18.60 ? 137 VAL   A N   1 
ATOM   998  C  CA  . VAL   A 1 131 ? 15.852 5.342   7.445  1.00 19.10 ? 137 VAL   A CA  1 
ATOM   999  C  C   . VAL   A 1 131 ? 15.895 4.530   6.100  1.00 20.82 ? 137 VAL   A C   1 
ATOM   1000 O  O   . VAL   A 1 131 ? 16.916 4.561   5.413  1.00 22.41 ? 137 VAL   A O   1 
ATOM   1001 C  CB  . VAL   A 1 131 ? 17.094 5.008   8.335  1.00 19.19 ? 137 VAL   A CB  1 
ATOM   1002 C  CG1 . VAL   A 1 131 ? 17.114 5.832   9.644  1.00 19.55 ? 137 VAL   A CG1 1 
ATOM   1003 C  CG2 . VAL   A 1 131 ? 17.145 3.507   8.645  1.00 18.81 ? 137 VAL   A CG2 1 
ATOM   1004 N  N   . ARG   A 1 132 ? 14.812 3.792   5.741  1.00 20.08 ? 138 ARG   A N   1 
ATOM   1005 C  CA  . ARG   A 1 132 ? 14.814 2.924   4.562  1.00 20.78 ? 138 ARG   A CA  1 
ATOM   1006 C  C   . ARG   A 1 132 ? 14.926 3.695   3.230  1.00 23.71 ? 138 ARG   A C   1 
ATOM   1007 O  O   . ARG   A 1 132 ? 15.394 3.131   2.237  1.00 25.02 ? 138 ARG   A O   1 
ATOM   1008 C  CB  . ARG   A 1 132 ? 13.553 2.044   4.532  1.00 21.92 ? 138 ARG   A CB  1 
ATOM   1009 C  CG  . ARG   A 1 132 ? 13.445 1.152   5.771  1.00 22.61 ? 138 ARG   A CG  1 
ATOM   1010 C  CD  . ARG   A 1 132 ? 12.131 0.390   5.722  1.00 21.65 ? 138 ARG   A CD  1 
ATOM   1011 N  NE  . ARG   A 1 132 ? 11.006 1.247   6.118  1.00 22.49 ? 138 ARG   A NE  1 
ATOM   1012 C  CZ  . ARG   A 1 132 ? 9.757  0.824   6.252  1.00 24.72 ? 138 ARG   A CZ  1 
ATOM   1013 N  NH1 . ARG   A 1 132 ? 9.434  -0.426  5.934  1.00 23.33 ? 138 ARG   A NH1 1 
ATOM   1014 N  NH2 . ARG   A 1 132 ? 8.818  1.645   6.705  1.00 26.38 ? 138 ARG   A NH2 1 
ATOM   1015 N  N   . ASP   A 1 133 ? 14.515 4.971   3.218  1.00 24.18 ? 139 ASP   A N   1 
ATOM   1016 C  CA  . ASP   A 1 133 ? 14.604 5.774   2.004  1.00 24.70 ? 139 ASP   A CA  1 
ATOM   1017 C  C   . ASP   A 1 133 ? 16.020 6.340   1.742  1.00 25.61 ? 139 ASP   A C   1 
ATOM   1018 O  O   . ASP   A 1 133 ? 16.293 6.862   0.622  1.00 26.11 ? 139 ASP   A O   1 
ATOM   1019 C  CB  . ASP   A 1 133 ? 13.566 6.910   2.039  1.00 27.17 ? 139 ASP   A CB  1 
ATOM   1020 C  CG  . ASP   A 1 133 ? 13.878 7.950   3.111  1.00 28.81 ? 139 ASP   A CG  1 
ATOM   1021 O  OD1 . ASP   A 1 133 ? 14.212 7.543   4.255  1.00 25.94 ? 139 ASP   A OD1 1 
ATOM   1022 O  OD2 . ASP   A 1 133 ? 13.829 9.169   2.796  1.00 28.44 ? 139 ASP   A OD2 1 
ATOM   1023 N  N   . LEU   A 1 134 ? 16.926 6.276   2.744  1.00 24.82 ? 140 LEU   A N   1 
ATOM   1024 C  CA  . LEU   A 1 134 ? 18.275 6.864   2.621  1.00 24.77 ? 140 LEU   A CA  1 
ATOM   1025 C  C   . LEU   A 1 134 ? 19.171 5.900   1.890  1.00 26.06 ? 140 LEU   A C   1 
ATOM   1026 O  O   . LEU   A 1 134 ? 19.992 5.205   2.499  1.00 26.83 ? 140 LEU   A O   1 
ATOM   1027 C  CB  . LEU   A 1 134 ? 18.862 7.217   3.999  1.00 24.11 ? 140 LEU   A CB  1 
ATOM   1028 C  CG  . LEU   A 1 134 ? 17.998 8.159   4.851  1.00 23.96 ? 140 LEU   A CG  1 
ATOM   1029 C  CD1 . LEU   A 1 134 ? 18.614 8.343   6.232  1.00 22.78 ? 140 LEU   A CD1 1 
ATOM   1030 C  CD2 . LEU   A 1 134 ? 17.748 9.533   4.129  1.00 24.75 ? 140 LEU   A CD2 1 
ATOM   1031 N  N   . LEU   A 1 135 ? 18.968 5.806   0.570  1.00 26.81 ? 141 LEU   A N   1 
ATOM   1032 C  CA  . LEU   A 1 135 ? 19.675 4.815   -0.219 1.00 28.65 ? 141 LEU   A CA  1 
ATOM   1033 C  C   . LEU   A 1 135 ? 21.188 4.993   -0.213 1.00 29.38 ? 141 LEU   A C   1 
ATOM   1034 O  O   . LEU   A 1 135 ? 21.916 4.002   -0.343 1.00 30.56 ? 141 LEU   A O   1 
ATOM   1035 C  CB  . LEU   A 1 135 ? 19.120 4.770   -1.646 1.00 29.44 ? 141 LEU   A CB  1 
ATOM   1036 C  CG  . LEU   A 1 135 ? 17.602 4.675   -1.809 1.00 30.91 ? 141 LEU   A CG  1 
ATOM   1037 C  CD1 . LEU   A 1 135 ? 17.234 4.572   -3.299 1.00 32.06 ? 141 LEU   A CD1 1 
ATOM   1038 C  CD2 . LEU   A 1 135 ? 17.008 3.478   -1.058 1.00 31.07 ? 141 LEU   A CD2 1 
ATOM   1039 N  N   . TRP   A 1 136 ? 21.669 6.232   -0.006 1.00 29.38 ? 142 TRP   A N   1 
ATOM   1040 C  CA  . TRP   A 1 136 ? 23.096 6.515   -0.001 1.00 30.13 ? 142 TRP   A CA  1 
ATOM   1041 C  C   . TRP   A 1 136 ? 23.862 5.907   1.181  1.00 31.76 ? 142 TRP   A C   1 
ATOM   1042 O  O   . TRP   A 1 136 ? 25.087 5.805   1.121  1.00 32.03 ? 142 TRP   A O   1 
ATOM   1043 C  CB  . TRP   A 1 136 ? 23.332 8.017   -0.092 1.00 29.80 ? 142 TRP   A CB  1 
ATOM   1044 C  CG  . TRP   A 1 136 ? 22.591 8.807   0.944  1.00 29.09 ? 142 TRP   A CG  1 
ATOM   1045 C  CD1 . TRP   A 1 136 ? 21.361 9.385   0.822  1.00 29.12 ? 142 TRP   A CD1 1 
ATOM   1046 C  CD2 . TRP   A 1 136 ? 23.071 9.144   2.251  1.00 28.48 ? 142 TRP   A CD2 1 
ATOM   1047 N  NE1 . TRP   A 1 136 ? 21.049 10.073  1.976  1.00 29.04 ? 142 TRP   A NE1 1 
ATOM   1048 C  CE2 . TRP   A 1 136 ? 22.096 9.960   2.859  1.00 28.88 ? 142 TRP   A CE2 1 
ATOM   1049 C  CE3 . TRP   A 1 136 ? 24.269 8.897   2.937  1.00 28.93 ? 142 TRP   A CE3 1 
ATOM   1050 C  CZ2 . TRP   A 1 136 ? 22.250 10.469  4.147  1.00 28.91 ? 142 TRP   A CZ2 1 
ATOM   1051 C  CZ3 . TRP   A 1 136 ? 24.422 9.412   4.211  1.00 29.56 ? 142 TRP   A CZ3 1 
ATOM   1052 C  CH2 . TRP   A 1 136 ? 23.426 10.204  4.795  1.00 29.09 ? 142 TRP   A CH2 1 
ATOM   1053 N  N   . LEU   A 1 137 ? 23.158 5.455   2.242  1.00 32.04 ? 143 LEU   A N   1 
ATOM   1054 C  CA  . LEU   A 1 137 ? 23.826 4.843   3.394  1.00 32.62 ? 143 LEU   A CA  1 
ATOM   1055 C  C   . LEU   A 1 137 ? 24.681 3.630   3.000  1.00 36.91 ? 143 LEU   A C   1 
ATOM   1056 O  O   . LEU   A 1 137 ? 25.654 3.322   3.691  1.00 36.51 ? 143 LEU   A O   1 
ATOM   1057 C  CB  . LEU   A 1 137 ? 22.789 4.419   4.450  1.00 31.07 ? 143 LEU   A CB  1 
ATOM   1058 C  CG  . LEU   A 1 137 ? 22.108 5.551   5.202  1.00 30.04 ? 143 LEU   A CG  1 
ATOM   1059 C  CD1 . LEU   A 1 137 ? 21.053 4.984   6.195  1.00 29.42 ? 143 LEU   A CD1 1 
ATOM   1060 C  CD2 . LEU   A 1 137 ? 23.143 6.393   5.977  1.00 30.25 ? 143 LEU   A CD2 1 
ATOM   1061 N  N   . ASP   A 1 138 ? 24.312 2.945   1.889  1.00 40.37 ? 144 ASP   A N   1 
ATOM   1062 C  CA  . ASP   A 1 138 ? 25.017 1.769   1.378  1.00 44.91 ? 144 ASP   A CA  1 
ATOM   1063 C  C   . ASP   A 1 138 ? 26.203 2.071   0.481  1.00 49.84 ? 144 ASP   A C   1 
ATOM   1064 O  O   . ASP   A 1 138 ? 27.034 1.188   0.297  1.00 51.55 ? 144 ASP   A O   1 
ATOM   1065 C  CB  . ASP   A 1 138 ? 24.038 0.877   0.625  1.00 47.17 ? 144 ASP   A CB  1 
ATOM   1066 C  CG  . ASP   A 1 138 ? 23.080 0.212   1.565  1.00 52.23 ? 144 ASP   A CG  1 
ATOM   1067 O  OD1 . ASP   A 1 138 ? 23.530 -0.255  2.631  1.00 54.06 ? 144 ASP   A OD1 1 
ATOM   1068 O  OD2 . ASP   A 1 138 ? 21.878 0.168   1.247  1.00 54.26 ? 144 ASP   A OD2 1 
ATOM   1069 N  N   . GLU   A 1 139 ? 26.283 3.273   -0.118 1.00 52.06 ? 145 GLU   A N   1 
ATOM   1070 C  CA  . GLU   A 1 139 ? 27.410 3.604   -1.004 1.00 54.72 ? 145 GLU   A CA  1 
ATOM   1071 C  C   . GLU   A 1 139 ? 28.215 4.813   -0.527 1.00 56.35 ? 145 GLU   A C   1 
ATOM   1072 O  O   . GLU   A 1 139 ? 28.976 5.403   -1.316 1.00 57.46 ? 145 GLU   A O   1 
ATOM   1073 C  CB  . GLU   A 1 139 ? 26.926 3.833   -2.442 1.00 58.00 ? 145 GLU   A CB  1 
ATOM   1074 C  CG  . GLU   A 1 139 ? 25.824 4.876   -2.548 1.00 63.51 ? 145 GLU   A CG  1 
ATOM   1075 C  CD  . GLU   A 1 139 ? 24.523 4.378   -3.152 1.00 70.67 ? 145 GLU   A CD  1 
ATOM   1076 O  OE1 . GLU   A 1 139 ? 23.642 5.222   -3.439 1.00 72.02 ? 145 GLU   A OE1 1 
ATOM   1077 O  OE2 . GLU   A 1 139 ? 24.384 3.148   -3.344 1.00 73.17 ? 145 GLU   A OE2 1 
HETATM 1078 N  N1  . A1B4J B 2 .   ? 10.391 13.653  22.626 1.00 27.33 ? 201 A1B4J A N1  1 
HETATM 1079 C  C4  . A1B4J B 2 .   ? 8.114  11.100  25.903 1.00 29.14 ? 201 A1B4J A C4  1 
HETATM 1080 C  C5  . A1B4J B 2 .   ? 9.116  10.979  24.939 1.00 28.38 ? 201 A1B4J A C5  1 
HETATM 1081 C  C6  . A1B4J B 2 .   ? 9.928  12.191  24.535 1.00 29.09 ? 201 A1B4J A C6  1 
HETATM 1082 C  C7  . A1B4J B 2 .   ? 9.605  12.671  23.129 1.00 28.34 ? 201 A1B4J A C7  1 
HETATM 1083 C  C8  . A1B4J B 2 .   ? 11.477 14.312  23.372 1.00 27.24 ? 201 A1B4J A C8  1 
HETATM 1084 C  C10 . A1B4J B 2 .   ? 12.681 14.676  21.193 1.00 27.20 ? 201 A1B4J A C10 1 
HETATM 1085 C  C13 . A1B4J B 2 .   ? 10.215 14.159  21.259 1.00 26.88 ? 201 A1B4J A C13 1 
HETATM 1086 O  O1  . A1B4J B 2 .   ? 10.938 15.659  18.791 1.00 26.11 ? 201 A1B4J A O1  1 
HETATM 1087 C  C12 . A1B4J B 2 .   ? 11.388 14.527  19.025 1.00 26.21 ? 201 A1B4J A C12 1 
HETATM 1088 N  N2  . A1B4J B 2 .   ? 11.760 13.689  18.064 1.00 24.83 ? 201 A1B4J A N2  1 
HETATM 1089 C  C11 . A1B4J B 2 .   ? 11.511 14.008  20.450 1.00 26.47 ? 201 A1B4J A C11 1 
HETATM 1090 C  C9  . A1B4J B 2 .   ? 12.804 14.177  22.638 1.00 27.34 ? 201 A1B4J A C9  1 
HETATM 1091 O  O   . A1B4J B 2 .   ? 8.684  12.184  22.487 1.00 27.78 ? 201 A1B4J A O   1 
HETATM 1092 C  C1  . A1B4J B 2 .   ? 9.332  9.673   24.444 1.00 27.32 ? 201 A1B4J A C1  1 
HETATM 1093 S  S   . A1B4J B 2 .   ? 10.629 9.530   23.261 1.00 26.64 ? 201 A1B4J A S   1 
HETATM 1094 C  C   . A1B4J B 2 .   ? 10.739 7.749   23.031 1.00 26.62 ? 201 A1B4J A C   1 
HETATM 1095 C  C3  . A1B4J B 2 .   ? 7.388  9.989   26.305 1.00 28.47 ? 201 A1B4J A C3  1 
HETATM 1096 C  C2  . A1B4J B 2 .   ? 7.692  8.768   25.752 1.00 28.15 ? 201 A1B4J A C2  1 
HETATM 1097 N  N   . A1B4J B 2 .   ? 8.663  8.586   24.842 1.00 26.72 ? 201 A1B4J A N   1 
HETATM 1098 ZN ZN  . ZN    C 3 .   ? 10.993 -5.286  5.660  1.00 27.26 2 202 ZN    A ZN  1 
HETATM 1099 S  S   . DMS   D 4 .   ? 14.418 20.131  7.323  1.00 88.42 ? 203 DMS   A S   1 
HETATM 1100 O  O   . DMS   D 4 .   ? 14.584 20.666  8.721  1.00 88.14 ? 203 DMS   A O   1 
HETATM 1101 C  C1  . DMS   D 4 .   ? 13.004 20.978  6.558  1.00 88.41 ? 203 DMS   A C1  1 
HETATM 1102 C  C2  . DMS   D 4 .   ? 15.692 20.903  6.283  1.00 88.45 ? 203 DMS   A C2  1 
HETATM 1103 O  O   . HOH   E 5 .   ? 36.070 15.074  16.957 1.00 40.57 ? 301 HOH   A O   1 
HETATM 1104 O  O   . HOH   E 5 .   ? 12.976 6.147   31.435 1.00 37.87 ? 302 HOH   A O   1 
HETATM 1105 O  O   . HOH   E 5 .   ? 20.438 22.041  7.959  1.00 33.86 ? 303 HOH   A O   1 
HETATM 1106 O  O   . HOH   E 5 .   ? 8.089  -4.579  0.740  1.00 32.33 ? 304 HOH   A O   1 
HETATM 1107 O  O   . HOH   E 5 .   ? 23.797 -0.564  15.483 1.00 40.89 ? 305 HOH   A O   1 
HETATM 1108 O  O   . HOH   E 5 .   ? 10.706 7.544   4.715  1.00 31.71 ? 306 HOH   A O   1 
HETATM 1109 O  O   . HOH   E 5 .   ? 27.719 15.668  3.091  1.00 54.07 ? 307 HOH   A O   1 
HETATM 1110 O  O   . HOH   E 5 .   ? 11.096 -5.555  31.853 1.00 37.80 ? 308 HOH   A O   1 
HETATM 1111 O  O   . HOH   E 5 .   ? 4.026  -5.483  21.418 1.00 34.14 ? 309 HOH   A O   1 
HETATM 1112 O  O   . HOH   E 5 .   ? 22.859 -2.159  4.288  1.00 37.70 ? 310 HOH   A O   1 
HETATM 1113 O  O   . HOH   E 5 .   ? 23.916 21.413  8.021  1.00 31.77 ? 311 HOH   A O   1 
HETATM 1114 O  O   . HOH   E 5 .   ? 29.736 2.671   10.526 1.00 34.86 ? 312 HOH   A O   1 
HETATM 1115 O  O   . HOH   E 5 .   ? 18.177 20.648  9.863  1.00 30.52 ? 313 HOH   A O   1 
HETATM 1116 O  O   . HOH   E 5 .   ? 14.925 10.687  0.906  1.00 41.11 ? 314 HOH   A O   1 
HETATM 1117 O  O   . HOH   E 5 .   ? 17.984 -7.589  3.503  1.00 39.32 ? 315 HOH   A O   1 
HETATM 1118 O  O   . HOH   E 5 .   ? 20.417 8.270   19.083 1.00 21.39 ? 316 HOH   A O   1 
HETATM 1119 O  O   . HOH   E 5 .   ? 8.572  19.021  18.478 1.00 31.24 ? 317 HOH   A O   1 
HETATM 1120 O  O   . HOH   E 5 .   ? 0.688  -0.909  16.717 1.00 25.38 ? 318 HOH   A O   1 
HETATM 1121 O  O   . HOH   E 5 .   ? 11.866 1.467   33.738 1.00 27.92 ? 319 HOH   A O   1 
HETATM 1122 O  O   . HOH   E 5 .   ? 19.222 19.179  27.664 1.00 52.19 ? 320 HOH   A O   1 
HETATM 1123 O  O   . HOH   E 5 .   ? 8.973  1.957   3.063  1.00 32.28 ? 321 HOH   A O   1 
HETATM 1124 O  O   . HOH   E 5 .   ? 10.374 4.152   3.555  1.00 24.85 ? 322 HOH   A O   1 
HETATM 1125 O  O   . HOH   E 5 .   ? 31.177 19.977  10.728 1.00 40.79 ? 323 HOH   A O   1 
HETATM 1126 O  O   . HOH   E 5 .   ? 11.212 16.562  5.626  1.00 52.32 ? 324 HOH   A O   1 
HETATM 1127 O  O   . HOH   E 5 .   ? 10.071 17.730  20.369 1.00 30.57 ? 325 HOH   A O   1 
HETATM 1128 O  O   . HOH   E 5 .   ? 0.356  1.210   24.516 1.00 38.36 ? 326 HOH   A O   1 
HETATM 1129 O  O   . HOH   E 5 .   ? 30.375 10.480  19.762 1.00 36.91 ? 327 HOH   A O   1 
HETATM 1130 O  O   . HOH   E 5 .   ? 35.233 19.548  11.941 1.00 54.72 ? 328 HOH   A O   1 
HETATM 1131 O  O   . HOH   E 5 .   ? 15.729 13.311  26.371 1.00 35.23 ? 329 HOH   A O   1 
HETATM 1132 O  O   . HOH   E 5 .   ? 14.912 -4.966  17.225 1.00 32.29 ? 330 HOH   A O   1 
HETATM 1133 O  O   . HOH   E 5 .   ? 5.221  5.350   24.280 1.00 32.26 ? 331 HOH   A O   1 
HETATM 1134 O  O   . HOH   E 5 .   ? 15.283 1.837   23.401 1.00 23.97 ? 332 HOH   A O   1 
HETATM 1135 O  O   . HOH   E 5 .   ? 18.490 18.752  5.755  1.00 38.62 ? 333 HOH   A O   1 
HETATM 1136 O  O   . HOH   E 5 .   ? 18.276 -0.152  30.155 1.00 47.65 ? 334 HOH   A O   1 
HETATM 1137 O  O   . HOH   E 5 .   ? 2.491  9.871   21.177 1.00 47.45 ? 335 HOH   A O   1 
HETATM 1138 O  O   . HOH   E 5 .   ? 19.581 -1.025  27.426 1.00 36.42 ? 336 HOH   A O   1 
HETATM 1139 O  O   . HOH   E 5 .   ? 5.296  12.880  25.142 1.00 43.73 ? 337 HOH   A O   1 
HETATM 1140 O  O   . HOH   E 5 .   ? -0.016 14.814  8.167  1.00 48.90 ? 338 HOH   A O   1 
HETATM 1141 O  O   . HOH   E 5 .   ? 6.793  -6.283  29.368 1.00 37.56 ? 339 HOH   A O   1 
HETATM 1142 O  O   . HOH   E 5 .   ? 6.472  7.352   29.087 1.00 36.73 ? 340 HOH   A O   1 
HETATM 1143 O  O   . HOH   E 5 .   ? 11.534 10.936  11.496 1.00 20.56 ? 341 HOH   A O   1 
HETATM 1144 O  O   . HOH   E 5 .   ? 13.354 9.828   9.500  1.00 19.37 ? 342 HOH   A O   1 
HETATM 1145 O  O   . HOH   E 5 .   ? 1.050  -3.252  20.175 1.00 36.27 ? 343 HOH   A O   1 
HETATM 1146 O  O   . HOH   E 5 .   ? 16.684 -8.303  10.548 1.00 46.42 ? 344 HOH   A O   1 
HETATM 1147 O  O   . HOH   E 5 .   ? 15.556 11.605  24.315 1.00 28.56 ? 345 HOH   A O   1 
HETATM 1148 O  O   . HOH   E 5 .   ? 8.730  -7.987  9.392  1.00 42.10 ? 346 HOH   A O   1 
HETATM 1149 O  O   . HOH   E 5 .   ? 3.391  12.639  18.222 1.00 47.41 ? 347 HOH   A O   1 
HETATM 1150 O  O   . HOH   E 5 .   ? 23.352 17.776  19.588 1.00 35.47 ? 348 HOH   A O   1 
HETATM 1151 O  O   . HOH   E 5 .   ? 19.023 12.083  1.847  1.00 36.18 ? 349 HOH   A O   1 
HETATM 1152 O  O   . HOH   E 5 .   ? 31.358 19.971  17.002 1.00 32.61 ? 350 HOH   A O   1 
HETATM 1153 O  O   . HOH   E 5 .   ? 21.910 18.498  17.811 1.00 40.06 ? 351 HOH   A O   1 
HETATM 1154 O  O   . HOH   E 5 .   ? 18.212 1.775   23.320 1.00 25.32 ? 352 HOH   A O   1 
HETATM 1155 O  O   . HOH   E 5 .   ? 4.151  -5.752  6.638  1.00 38.75 ? 353 HOH   A O   1 
HETATM 1156 O  O   . HOH   E 5 .   ? 14.129 8.561   30.121 1.00 38.11 ? 354 HOH   A O   1 
HETATM 1157 O  O   . HOH   E 5 .   ? 0.238  3.681   6.732  1.00 52.96 ? 355 HOH   A O   1 
HETATM 1158 O  O   . HOH   E 5 .   ? 18.258 18.281  17.213 1.00 22.01 ? 356 HOH   A O   1 
HETATM 1159 O  O   . HOH   E 5 .   ? 7.151  3.032   33.301 1.00 33.00 ? 357 HOH   A O   1 
HETATM 1160 O  O   . HOH   E 5 .   ? 10.316 3.585   34.152 1.00 34.56 ? 358 HOH   A O   1 
HETATM 1161 O  O   . HOH   E 5 .   ? 5.962  1.155   6.730  1.00 38.11 ? 359 HOH   A O   1 
HETATM 1162 O  O   . HOH   E 5 .   ? 6.885  12.222  5.708  1.00 28.81 ? 360 HOH   A O   1 
HETATM 1163 O  O   . HOH   E 5 .   ? 5.432  -2.099  24.497 1.00 27.53 ? 361 HOH   A O   1 
HETATM 1164 O  O   . HOH   E 5 .   ? 19.536 8.490   25.881 1.00 38.59 ? 362 HOH   A O   1 
HETATM 1165 O  O   . HOH   E 5 .   ? 28.730 -2.766  12.902 1.00 42.01 ? 363 HOH   A O   1 
HETATM 1166 O  O   . HOH   E 5 .   ? 18.912 3.760   26.209 1.00 41.75 ? 364 HOH   A O   1 
HETATM 1167 O  O   . HOH   E 5 .   ? 14.782 13.777  3.593  1.00 32.71 ? 365 HOH   A O   1 
HETATM 1168 O  O   . HOH   E 5 .   ? 18.819 -1.136  19.596 1.00 27.49 ? 366 HOH   A O   1 
HETATM 1169 O  O   . HOH   E 5 .   ? 9.611  20.595  11.062 1.00 39.95 ? 367 HOH   A O   1 
HETATM 1170 O  O   . HOH   E 5 .   ? 30.472 10.193  17.466 1.00 41.28 ? 368 HOH   A O   1 
HETATM 1171 O  O   . HOH   E 5 .   ? -0.574 -6.607  11.637 1.00 70.05 ? 369 HOH   A O   1 
HETATM 1172 O  O   . HOH   E 5 .   ? 26.385 3.275   20.141 1.00 50.35 ? 370 HOH   A O   1 
HETATM 1173 O  O   . HOH   E 5 .   ? 3.258  3.321   27.942 1.00 42.40 ? 371 HOH   A O   1 
HETATM 1174 O  O   . HOH   E 5 .   ? 24.125 1.689   19.579 1.00 37.82 ? 372 HOH   A O   1 
HETATM 1175 O  O   . HOH   E 5 .   ? 2.028  12.665  5.764  1.00 45.25 ? 373 HOH   A O   1 
HETATM 1176 O  O   . HOH   E 5 .   ? 30.464 4.383   3.509  1.00 60.77 ? 374 HOH   A O   1 
HETATM 1177 O  O   . HOH   E 5 .   ? 3.922  6.272   26.380 1.00 41.64 ? 375 HOH   A O   1 
HETATM 1178 O  O   . HOH   E 5 .   ? 16.439 23.262  14.981 1.00 51.37 ? 376 HOH   A O   1 
HETATM 1179 O  O   . HOH   E 5 .   ? 1.494  -3.328  17.681 1.00 31.76 ? 377 HOH   A O   1 
HETATM 1180 O  O   . HOH   E 5 .   ? 4.188  -3.029  21.937 1.00 40.92 ? 378 HOH   A O   1 
HETATM 1181 O  O   . HOH   E 5 .   ? 5.961  13.346  21.703 1.00 48.49 ? 379 HOH   A O   1 
HETATM 1182 O  O   . HOH   E 5 .   ? 19.926 23.249  15.563 1.00 31.99 ? 380 HOH   A O   1 
HETATM 1183 O  O   . HOH   E 5 .   ? 22.723 18.487  6.164  1.00 31.31 ? 381 HOH   A O   1 
HETATM 1184 O  O   . HOH   E 5 .   ? 15.913 -5.344  1.944  1.00 32.34 ? 382 HOH   A O   1 
HETATM 1185 O  O   . HOH   E 5 .   ? 31.676 18.010  8.927  1.00 51.34 ? 383 HOH   A O   1 
HETATM 1186 O  O   . HOH   E 5 .   ? 12.234 20.732  12.749 1.00 33.02 ? 384 HOH   A O   1 
HETATM 1187 O  O   . HOH   E 5 .   ? 6.162  22.289  11.342 1.00 36.67 ? 385 HOH   A O   1 
HETATM 1188 O  O   . HOH   E 5 .   ? 4.321  10.378  19.145 1.00 53.78 ? 386 HOH   A O   1 
HETATM 1189 O  O   . HOH   E 5 .   ? -1.625 -5.119  15.624 1.00 51.43 ? 387 HOH   A O   1 
HETATM 1190 O  O   . HOH   E 5 .   ? 7.509  25.188  14.362 1.00 62.42 ? 388 HOH   A O   1 
HETATM 1191 O  O   . HOH   E 5 .   ? 22.409 8.191   21.139 1.00 29.34 ? 389 HOH   A O   1 
HETATM 1192 O  O   . HOH   E 5 .   ? 12.237 -8.684  13.116 1.00 35.80 ? 390 HOH   A O   1 
HETATM 1193 O  O   . HOH   E 5 .   ? 28.962 15.960  23.385 1.00 40.89 ? 391 HOH   A O   1 
HETATM 1194 O  O   . HOH   E 5 .   ? 7.101  10.396  4.269  1.00 45.86 ? 392 HOH   A O   1 
HETATM 1195 O  O   . HOH   E 5 .   ? 7.181  -5.874  2.808  1.00 37.51 ? 393 HOH   A O   1 
HETATM 1196 O  O   . HOH   E 5 .   ? 26.716 -2.436  14.749 1.00 42.38 ? 394 HOH   A O   1 
HETATM 1197 O  O   . HOH   E 5 .   ? 32.892 13.988  7.027  1.00 53.11 ? 395 HOH   A O   1 
HETATM 1198 O  O   . HOH   E 5 .   ? 19.282 6.613   28.176 1.00 42.72 ? 396 HOH   A O   1 
HETATM 1199 O  O   . HOH   E 5 .   ? -0.051 15.506  22.738 1.00 54.86 ? 397 HOH   A O   1 
HETATM 1200 O  O   . HOH   E 5 .   ? 4.949  -1.978  29.339 1.00 48.91 ? 398 HOH   A O   1 
HETATM 1201 O  O   . HOH   E 5 .   ? 31.379 1.798   12.771 1.00 46.27 ? 399 HOH   A O   1 
HETATM 1202 O  O   . HOH   E 5 .   ? 20.139 8.189   -2.387 1.00 38.25 ? 400 HOH   A O   1 
HETATM 1203 O  O   . HOH   E 5 .   ? 2.671  14.587  20.182 1.00 44.95 ? 401 HOH   A O   1 
HETATM 1204 O  O   . HOH   E 5 .   ? 28.709 21.476  18.737 1.00 47.10 ? 402 HOH   A O   1 
HETATM 1205 O  O   . HOH   E 5 .   ? 37.088 6.324   6.805  1.00 58.91 ? 403 HOH   A O   1 
HETATM 1206 O  O   . HOH   E 5 .   ? 11.482 17.471  26.965 1.00 43.67 ? 404 HOH   A O   1 
HETATM 1207 O  O   . HOH   E 5 .   ? 16.998 -4.179  18.077 1.00 38.65 ? 405 HOH   A O   1 
HETATM 1208 O  O   . HOH   E 5 .   ? 24.551 6.529   20.701 1.00 52.15 ? 406 HOH   A O   1 
HETATM 1209 O  O   . HOH   E 5 .   ? 17.754 10.428  26.207 1.00 43.65 ? 407 HOH   A O   1 
HETATM 1210 O  O   . HOH   E 5 .   ? 21.304 21.397  17.929 1.00 38.81 ? 408 HOH   A O   1 
HETATM 1211 O  O   . HOH   E 5 .   ? 4.371  8.284   28.128 1.00 52.88 ? 409 HOH   A O   1 
HETATM 1212 O  O   . HOH   E 5 .   ? 2.047  1.086   26.948 1.00 41.65 ? 410 HOH   A O   1 
HETATM 1213 O  O   . HOH   E 5 .   ? 11.897 22.829  14.470 1.00 35.81 ? 411 HOH   A O   1 
HETATM 1214 O  O   . HOH   E 5 .   ? 8.941  22.067  26.859 1.00 43.01 ? 412 HOH   A O   1 
HETATM 1215 O  O   . HOH   E 5 .   ? 2.350  13.577  22.944 1.00 50.84 ? 413 HOH   A O   1 
HETATM 1216 O  O   . HOH   E 5 .   ? 33.271 21.312  12.310 1.00 41.34 ? 414 HOH   A O   1 
HETATM 1217 O  O   . HOH   E 5 .   ? 33.048 21.241  14.907 1.00 43.00 ? 415 HOH   A O   1 
HETATM 1218 O  O   . HOH   E 5 .   ? 8.948  6.487   2.658  1.00 45.46 ? 416 HOH   A O   1 
HETATM 1219 O  O   . HOH   E 5 .   ? 9.595  -9.206  12.666 1.00 39.38 ? 417 HOH   A O   1 
HETATM 1220 O  O   . HOH   E 5 .   ? 5.491  -9.060  23.533 1.00 39.70 ? 418 HOH   A O   1 
HETATM 1221 O  O   . HOH   E 5 .   ? 9.850  14.522  27.315 1.00 57.93 ? 419 HOH   A O   1 
HETATM 1222 O  O   . HOH   E 5 .   ? 10.026 24.478  13.530 1.00 38.83 ? 420 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   ? 0.5085 0.3119 0.3982 -0.0396 -0.0931 0.0107  7   SER   A N   
2    C CA  . SER   A 1   ? 0.4845 0.3142 0.4226 -0.0387 -0.1037 0.0166  7   SER   A CA  
3    C C   . SER   A 1   ? 0.4327 0.3005 0.4208 -0.0312 -0.0952 0.0171  7   SER   A C   
4    O O   . SER   A 1   ? 0.4279 0.2999 0.4120 -0.0288 -0.0871 0.0145  7   SER   A O   
5    C CB  . SER   A 1   ? 0.5346 0.3413 0.4707 -0.0534 -0.1341 0.0295  7   SER   A CB  
6    O OG  . SER   A 1   ? 0.5819 0.3784 0.5145 -0.0611 -0.1467 0.0368  7   SER   A OG  
7    N N   . GLY   A 2   ? 0.3858 0.2774 0.4181 -0.0281 -0.0950 0.0202  8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.3475 0.2678 0.4234 -0.0224 -0.0835 0.0201  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.3245 0.2654 0.4268 -0.0165 -0.0701 0.0164  8   GLY   A C   
10   O O   . GLY   A 2   ? 0.3216 0.2613 0.4055 -0.0139 -0.0651 0.0111  8   GLY   A O   
11   N N   . ALA   A 3   ? 0.2945 0.2517 0.4394 -0.0147 -0.0626 0.0196  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.2817 0.2530 0.4484 -0.0108 -0.0474 0.0162  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.2649 0.2478 0.4540 -0.0084 -0.0269 0.0124  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.2623 0.2446 0.4618 -0.0094 -0.0272 0.0152  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.2828 0.2524 0.4835 -0.0134 -0.0587 0.0270  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.2518 0.2412 0.4449 -0.0068 -0.0091 0.0065  10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.2507 0.2422 0.4577 -0.0071 0.0132  0.0022  10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.2530 0.2433 0.5017 -0.0065 0.0228  0.0085  10  ILE   A C   
19   O O   . ILE   A 4   ? 0.2430 0.2342 0.4938 -0.0060 0.0195  0.0099  10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.2601 0.2526 0.4320 -0.0091 0.0259  -0.0083 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.2642 0.2596 0.4029 -0.0089 0.0169  -0.0116 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.2716 0.2571 0.4469 -0.0129 0.0494  -0.0135 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.2659 0.2644 0.3773 -0.0119 0.0227  -0.0168 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.2606 0.2482 0.5466 -0.0062 0.0356  0.0135  11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.2666 0.2516 0.6015 -0.0047 0.0496  0.0216  11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.2957 0.2688 0.6275 -0.0059 0.0848  0.0126  11  TYR   A C   
27   O O   . TYR   A 5   ? 0.3033 0.2710 0.6399 -0.0066 0.0967  0.0107  11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.2463 0.2344 0.6366 -0.0040 0.0373  0.0388  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.2453 0.2367 0.6337 -0.0067 0.0014  0.0493  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.2518 0.2442 0.6604 -0.0075 -0.0107 0.0584  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.2612 0.2504 0.6195 -0.0097 -0.0194 0.0490  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.2683 0.2570 0.6658 -0.0127 -0.0441 0.0673  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.2765 0.2598 0.6209 -0.0148 -0.0505 0.0573  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.2880 0.2697 0.6504 -0.0170 -0.0634 0.0663  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.3189 0.2881 0.6589 -0.0245 -0.0941 0.0738  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.3067 0.2719 0.6255 -0.0076 0.1015  0.0066  12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.3247 0.2694 0.6274 -0.0120 0.1359  -0.0029 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.3329 0.2675 0.6635 -0.0110 0.1567  0.0008  12  VAL   A C   
39   O O   . VAL   A 6   ? 0.3364 0.2768 0.6567 -0.0110 0.1465  0.0010  12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.3658 0.3034 0.6002 -0.0199 0.1357  -0.0168 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.3701 0.3204 0.5791 -0.0201 0.1137  -0.0174 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.4041 0.3123 0.6120 -0.0286 0.1693  -0.0261 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.3243 0.2432 0.6952 -0.0095 0.1875  0.0049  13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.3388 0.2460 0.7441 -0.0075 0.2120  0.0102  13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.3270 0.2575 0.7840 -0.0011 0.1855  0.0266  13  GLY   A C   
46   O O   . GLY   A 7   ? 0.3221 0.2705 0.8117 0.0020  0.1588  0.0384  13  GLY   A O   
47   N N   . ASN   A 8   ? 0.3242 0.2538 0.7793 -0.0012 0.1876  0.0270  14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.3065 0.2561 0.8047 0.0031  0.1601  0.0424  14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.2948 0.2589 0.7420 0.0008  0.1238  0.0362  14  ASN   A C   
50   O O   . ASN   A 8   ? 0.2820 0.2544 0.7399 0.0019  0.1076  0.0425  14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.3463 0.2868 0.8792 0.0052  0.1837  0.0483  14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.4328 0.3588 1.0300 0.0091  0.2208  0.0585  14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.4369 0.3735 1.0962 0.0129  0.2125  0.0750  14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.4785 0.3772 1.0634 0.0074  0.2636  0.0500  14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.2881 0.2542 0.6845 -0.0021 0.1121  0.0254  15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.2865 0.2633 0.6375 -0.0035 0.0834  0.0200  15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.2695 0.2550 0.6137 -0.0031 0.0567  0.0233  15  TYR   A C   
58   O O   . TYR   A 9   ? 0.2668 0.2502 0.6199 -0.0032 0.0621  0.0239  15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.3066 0.2758 0.5960 -0.0087 0.0942  0.0044  15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.3309 0.2869 0.6106 -0.0122 0.1172  -0.0001 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.3342 0.2959 0.6291 -0.0099 0.1103  0.0052  15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.3627 0.2968 0.6110 -0.0195 0.1449  -0.0099 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.3631 0.3109 0.6476 -0.0136 0.1320  0.0014  15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.3939 0.3096 0.6245 -0.0251 0.1663  -0.0142 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.4027 0.3263 0.6532 -0.0216 0.1603  -0.0084 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.4446 0.3488 0.6768 -0.0274 0.1819  -0.0123 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.2503 0.2421 0.5732 -0.0034 0.0299  0.0246  16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.2363 0.2296 0.5383 -0.0045 0.0061  0.0258  16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.2309 0.2250 0.4791 -0.0048 0.0007  0.0148  16  ARG   A C   
70   O O   . ARG   A 10  ? 0.2263 0.2211 0.4666 -0.0045 -0.0049 0.0147  16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.2385 0.2306 0.5691 -0.0065 -0.0207 0.0410  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.2736 0.2583 0.5671 -0.0102 -0.0470 0.0413  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.2988 0.2757 0.6192 -0.0165 -0.0753 0.0588  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.3402 0.3019 0.6159 -0.0219 -0.0979 0.0577  16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.3823 0.3275 0.6225 -0.0279 -0.1153 0.0583  16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.3561 0.3019 0.6040 -0.0292 -0.1158 0.0613  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.3977 0.3224 0.5921 -0.0334 -0.1305 0.0560  16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.2258 0.2200 0.4421 -0.0053 0.0031  0.0071  17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.2288 0.2246 0.4031 -0.0052 -0.0009 -0.0001 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.2353 0.2253 0.3912 -0.0047 -0.0190 0.0021  17  VAL   A C   
81   O O   . VAL   A 11  ? 0.2466 0.2339 0.4028 -0.0054 -0.0219 0.0033  17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.2342 0.2321 0.3863 -0.0075 0.0136  -0.0079 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.2475 0.2495 0.3683 -0.0078 0.0098  -0.0112 17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.2270 0.2205 0.3895 -0.0111 0.0345  -0.0108 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.2273 0.2119 0.3637 -0.0041 -0.0291 0.0022  18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.2368 0.2069 0.3468 -0.0051 -0.0422 0.0032  18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.2330 0.2003 0.3126 -0.0023 -0.0371 -0.0020 18  VAL   A C   
88   O O   . VAL   A 12  ? 0.2342 0.2115 0.3176 -0.0005 -0.0297 -0.0039 18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.2743 0.2293 0.3906 -0.0097 -0.0620 0.0117  18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.2944 0.2502 0.4451 -0.0134 -0.0711 0.0213  18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.2744 0.2327 0.4007 -0.0088 -0.0626 0.0128  18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.2351 0.1860 0.2853 -0.0024 -0.0401 -0.0031 19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.2453 0.1892 0.2725 0.0010  -0.0327 -0.0060 19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.2675 0.2026 0.2941 -0.0004 -0.0402 -0.0042 19  ASN   A C   
95   O O   . ASN   A 13  ? 0.2925 0.2119 0.3168 -0.0059 -0.0553 -0.0004 19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.2802 0.1987 0.2737 0.0003  -0.0317 -0.0071 19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.3002 0.2266 0.2942 0.0021  -0.0241 -0.0083 19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.3109 0.2347 0.3077 -0.0015 -0.0319 -0.0069 19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.2762 0.2123 0.2707 0.0070  -0.0100 -0.0090 19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.2556 0.2008 0.2866 0.0032  -0.0320 -0.0053 20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.2475 0.1849 0.2786 0.0022  -0.0385 -0.0038 20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.2931 0.1957 0.2897 -0.0014 -0.0453 -0.0041 20  ARG   A C   
103  O O   . ARG   A 14  ? 0.3274 0.2159 0.3212 -0.0067 -0.0595 -0.0010 20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.2390 0.1909 0.2778 0.0065  -0.0277 -0.0042 20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.2494 0.1986 0.2945 0.0057  -0.0336 -0.0026 20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.2644 0.2266 0.3153 0.0098  -0.0226 -0.0017 20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.2637 0.2277 0.3232 0.0097  -0.0260 0.0000  20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.3026 0.2465 0.3472 0.0104  -0.0278 -0.0002 20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.3029 0.2189 0.3187 0.0100  -0.0256 -0.0026 20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.3165 0.2648 0.3716 0.0106  -0.0303 0.0016  20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.3128 0.1973 0.2811 0.0001  -0.0353 -0.0070 21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.3695 0.2109 0.2943 -0.0053 -0.0378 -0.0085 21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.4122 0.2286 0.3172 -0.0166 -0.0591 -0.0053 21  HIS   A C   
114  O O   . HIS   A 15  ? 0.4664 0.2416 0.3302 -0.0255 -0.0670 -0.0052 21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.3983 0.2212 0.2977 -0.0005 -0.0159 -0.0121 21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.4108 0.2331 0.3034 -0.0002 -0.0113 -0.0127 21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.3970 0.2556 0.3227 0.0062  -0.0037 -0.0113 21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.4509 0.2380 0.3045 -0.0069 -0.0134 -0.0142 21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.4251 0.2724 0.3351 0.0048  -0.0011 -0.0122 21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.4473 0.2523 0.3142 -0.0029 -0.0065 -0.0139 21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.3811 0.2201 0.3153 -0.0177 -0.0687 -0.0013 22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.3992 0.2207 0.3273 -0.0286 -0.0911 0.0055  22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.3895 0.2299 0.3618 -0.0318 -0.1086 0.0146  22  LEU   A C   
124  O O   . LEU   A 16  ? 0.3992 0.2329 0.3828 -0.0404 -0.1281 0.0240  22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.4043 0.2324 0.3344 -0.0278 -0.0876 0.0052  22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.4548 0.2614 0.3439 -0.0253 -0.0702 -0.0017 22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.4561 0.2726 0.3520 -0.0244 -0.0681 -0.0012 22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.5058 0.2584 0.3358 -0.0362 -0.0764 -0.0023 22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.3655 0.2310 0.3682 -0.0249 -0.1004 0.0134  23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.3574 0.2403 0.4058 -0.0265 -0.1115 0.0222  23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.3927 0.2487 0.4329 -0.0389 -0.1385 0.0327  23  ALA   A C   
132  O O   . ALA   A 17  ? 0.4339 0.2587 0.4292 -0.0445 -0.1438 0.0297  23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.3338 0.2402 0.4043 -0.0185 -0.0970 0.0182  23  ALA   A CB  
134  N N   . THR   A 18  ? 0.3844 0.2494 0.4682 -0.0440 -0.1551 0.0462  24  THR   A N   
135  C CA  . THR   A 18  ? 0.4161 0.2570 0.5007 -0.0584 -0.1863 0.0610  24  THR   A CA  
136  C C   . THR   A 18  ? 0.4133 0.2650 0.5296 -0.0570 -0.1900 0.0664  24  THR   A C   
137  O O   . THR   A 18  ? 0.3848 0.2634 0.5247 -0.0450 -0.1678 0.0591  24  THR   A O   
138  C CB  . THR   A 18  ? 0.4270 0.2746 0.5543 -0.0650 -0.2038 0.0773  24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.4141 0.2984 0.6097 -0.0549 -0.1892 0.0818  24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.4339 0.2734 0.5349 -0.0661 -0.2001 0.0727  24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.4389 0.2689 0.5579 -0.0709 -0.2200 0.0812  25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.4394 0.2807 0.5950 -0.0701 -0.2250 0.0887  25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.3877 0.2689 0.6214 -0.0598 -0.2110 0.0962  25  HIS   A C   
144  O O   . HIS   A 19  ? 0.3853 0.2862 0.6439 -0.0507 -0.1942 0.0923  25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.5034 0.3138 0.6545 -0.0895 -0.2643 0.1073  25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.6457 0.4073 0.7141 -0.1024 -0.2769 0.1001  25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.7063 0.4575 0.7365 -0.0969 -0.2608 0.0854  25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.7138 0.4307 0.7327 -0.1222 -0.3043 0.1075  25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.7633 0.4625 0.7212 -0.1122 -0.2747 0.0828  25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.7752 0.4501 0.7195 -0.1286 -0.3014 0.0953  25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.3646 0.2545 0.6356 -0.0619 -0.2163 0.1074  26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.3352 0.2566 0.6792 -0.0525 -0.1982 0.1146  26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.3086 0.2508 0.6445 -0.0374 -0.1592 0.0946  26  ASN   A C   
154  O O   . ASN   A 20  ? 0.2898 0.2503 0.6648 -0.0297 -0.1388 0.0946  26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.3622 0.2844 0.7451 -0.0588 -0.2123 0.1315  26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.4501 0.3547 0.8552 -0.0754 -0.2528 0.1563  26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.4633 0.3723 0.9052 -0.0772 -0.2612 0.1680  26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.5015 0.3833 0.8823 -0.0895 -0.2808 0.1659  26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.3082 0.2442 0.5896 -0.0347 -0.1494 0.0783  27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.2926 0.2453 0.5608 -0.0236 -0.1178 0.0614  27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.2803 0.2387 0.5424 -0.0192 -0.1081 0.0552  27  ASP   A C   
162  O O   . ASP   A 21  ? 0.2724 0.2469 0.5567 -0.0130 -0.0862 0.0513  27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.3157 0.2588 0.5287 -0.0228 -0.1136 0.0484  27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.3443 0.2881 0.5630 -0.0240 -0.1135 0.0504  27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.3223 0.2818 0.5853 -0.0207 -0.1016 0.0548  27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.3672 0.2934 0.5450 -0.0283 -0.1229 0.0472  27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.2850 0.2264 0.5158 -0.0239 -0.1243 0.0551  28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.2809 0.2271 0.5057 -0.0200 -0.1164 0.0499  28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.2764 0.2339 0.5555 -0.0199 -0.1181 0.0618  28  TRP   A C   
170  O O   . TRP   A 22  ? 0.2722 0.2412 0.5592 -0.0146 -0.1027 0.0571  28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.2967 0.2170 0.4723 -0.0254 -0.1312 0.0465  28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.2930 0.2067 0.4211 -0.0212 -0.1171 0.0328  28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.3213 0.2133 0.4101 -0.0251 -0.1215 0.0293  28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.2708 0.1979 0.3887 -0.0130 -0.0968 0.0230  28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.3247 0.2177 0.3849 -0.0183 -0.1024 0.0181  28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.2975 0.2135 0.3774 -0.0112 -0.0885 0.0151  28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.2574 0.2051 0.3973 -0.0077 -0.0844 0.0216  28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.2908 0.2165 0.3596 -0.0044 -0.0707 0.0082  28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.2614 0.2174 0.3843 -0.0024 -0.0689 0.0140  28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.2729 0.2198 0.3645 -0.0007 -0.0628 0.0085  28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.2749 0.2280 0.5931 -0.0267 -0.1375 0.0788  29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.2861 0.2499 0.6652 -0.0263 -0.1382 0.0933  29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.2859 0.2696 0.7093 -0.0174 -0.1063 0.0921  29  ALA   A C   
184  O O   . ALA   A 23  ? 0.2827 0.2750 0.7521 -0.0145 -0.0956 0.1002  29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.2883 0.2412 0.7026 -0.0377 -0.1709 0.1159  29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.2728 0.2600 0.6816 -0.0140 -0.0901 0.0828  30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.2538 0.2515 0.6912 -0.0077 -0.0575 0.0792  30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.2474 0.2464 0.6307 -0.0042 -0.0369 0.0588  30  ASN   A C   
189  O O   . ASN   A 24  ? 0.2386 0.2389 0.6205 -0.0024 -0.0177 0.0529  30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.2693 0.2680 0.7478 -0.0088 -0.0579 0.0905  30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.3180 0.3169 0.8608 -0.0135 -0.0793 0.1153  30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.3347 0.3398 0.9331 -0.0105 -0.0661 0.1262  30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.3205 0.3105 0.8568 -0.0224 -0.1133 0.1261  30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.2492 0.2466 0.5897 -0.0042 -0.0427 0.0497  31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.2426 0.2420 0.5367 -0.0025 -0.0291 0.0347  31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.2529 0.2557 0.5520 -0.0014 -0.0005 0.0289  31  LEU   A C   
197  O O   . LEU   A 25  ? 0.2615 0.2647 0.5832 -0.0008 0.0089  0.0327  31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.2443 0.2415 0.5071 -0.0025 -0.0401 0.0307  31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.2580 0.2589 0.4805 -0.0013 -0.0296 0.0194  31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.2710 0.2682 0.4675 -0.0014 -0.0334 0.0148  31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.2493 0.2492 0.4541 -0.0005 -0.0364 0.0181  31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.2365 0.2382 0.5083 -0.0026 0.0133  0.0196  32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.2425 0.2392 0.5010 -0.0055 0.0388  0.0126  32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.2535 0.2526 0.4650 -0.0089 0.0353  0.0048  32  VAL   A C   
205  O O   . VAL   A 26  ? 0.2812 0.2773 0.4794 -0.0126 0.0444  0.0026  32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.2577 0.2474 0.5192 -0.0071 0.0552  0.0096  32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.2849 0.2617 0.5149 -0.0139 0.0796  0.0006  32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.2446 0.2323 0.5620 -0.0038 0.0622  0.0200  32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.2400 0.2438 0.4298 -0.0080 0.0216  0.0025  33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.2397 0.2475 0.3957 -0.0105 0.0178  -0.0013 33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.2303 0.2414 0.3750 -0.0065 0.0025  -0.0010 33  TRP   A C   
212  O O   . TRP   A 27  ? 0.2371 0.2452 0.3876 -0.0046 -0.0017 -0.0006 33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.2497 0.2518 0.3829 -0.0182 0.0319  -0.0061 33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.2674 0.2745 0.3720 -0.0227 0.0250  -0.0063 33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.2915 0.3007 0.3815 -0.0282 0.0224  -0.0037 33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.2649 0.2759 0.3576 -0.0225 0.0195  -0.0068 33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.2938 0.3090 0.3678 -0.0317 0.0146  -0.0008 33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.2773 0.2937 0.3529 -0.0279 0.0137  -0.0031 33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.2642 0.2748 0.3618 -0.0186 0.0182  -0.0087 33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.2757 0.2972 0.3420 -0.0293 0.0084  -0.0006 33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.2745 0.2893 0.3579 -0.0195 0.0136  -0.0081 33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.2707 0.2911 0.3402 -0.0247 0.0095  -0.0039 33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.2129 0.2278 0.3422 -0.0055 -0.0039 -0.0004 34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.2271 0.2401 0.3430 -0.0018 -0.0121 -0.0003 34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.2359 0.2558 0.3391 -0.0026 -0.0102 0.0015  34  GLU   A C   
226  O O   . GLU   A 28  ? 0.2355 0.2607 0.3409 -0.0055 -0.0086 0.0039  34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.2475 0.2498 0.3652 0.0017  -0.0237 0.0015  34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.2577 0.2594 0.3829 0.0024  -0.0276 0.0040  34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.3026 0.3060 0.4153 0.0044  -0.0260 0.0045  34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.3383 0.3471 0.4593 0.0039  -0.0253 0.0066  34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.2756 0.2742 0.3733 0.0068  -0.0241 0.0038  34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.2281 0.2479 0.3215 -0.0006 -0.0104 0.0020  35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.2175 0.2449 0.3086 -0.0010 -0.0087 0.0073  35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.2209 0.2402 0.3066 0.0057  -0.0070 0.0082  35  ASP   A C   
235  O O   . ASP   A 29  ? 0.2375 0.2543 0.3172 0.0064  -0.0049 0.0068  35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.2287 0.2646 0.3162 -0.0093 -0.0067 0.0100  35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.2947 0.3404 0.3869 -0.0130 -0.0093 0.0200  35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.3073 0.3544 0.4093 -0.0061 -0.0084 0.0249  35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.3094 0.3586 0.3953 -0.0241 -0.0120 0.0242  35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.2108 0.2231 0.2970 0.0104  -0.0056 0.0105  36  SER   A N   
241  C CA  A SER   A 30  ? 0.2297 0.2264 0.3066 0.0162  0.0014  0.0108  36  SER   A CA  
242  C CA  B SER   A 30  ? 0.2290 0.2255 0.3054 0.0161  0.0013  0.0106  36  SER   A CA  
243  C C   . SER   A 30  ? 0.2288 0.2356 0.3159 0.0173  0.0090  0.0177  36  SER   A C   
244  O O   . SER   A 30  ? 0.2509 0.2457 0.3289 0.0208  0.0163  0.0165  36  SER   A O   
245  C CB  A SER   A 30  ? 0.2558 0.2429 0.3340 0.0199  0.0051  0.0130  36  SER   A CB  
246  C CB  B SER   A 30  ? 0.2560 0.2391 0.3299 0.0201  0.0049  0.0117  36  SER   A CB  
247  O OG  A SER   A 30  ? 0.3137 0.2715 0.3699 0.0235  0.0117  0.0091  36  SER   A OG  
248  O OG  B SER   A 30  ? 0.2832 0.2833 0.3790 0.0204  0.0077  0.0201  36  SER   A OG  
249  N N   . SER   A 31  ? 0.2107 0.2380 0.3169 0.0130  0.0064  0.0265  37  SER   A N   
250  C CA  . SER   A 31  ? 0.2074 0.2459 0.3300 0.0121  0.0099  0.0371  37  SER   A CA  
251  C C   . SER   A 31  ? 0.2054 0.2453 0.3185 0.0088  0.0083  0.0336  37  SER   A C   
252  O O   . SER   A 31  ? 0.2205 0.2653 0.3456 0.0098  0.0126  0.0415  37  SER   A O   
253  C CB  . SER   A 31  ? 0.2355 0.2929 0.3783 0.0043  0.0021  0.0499  37  SER   A CB  
254  O OG  . SER   A 31  ? 0.2885 0.3522 0.4190 -0.0071 -0.0080 0.0475  37  SER   A OG  
255  N N   . ARG   A 32  ? 0.1884 0.2243 0.2845 0.0052  0.0031  0.0233  38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.1887 0.2248 0.2765 0.0021  0.0025  0.0194  38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.2090 0.2286 0.2822 0.0077  0.0051  0.0107  38  ARG   A C   
258  O O   . ARG   A 32  ? 0.2193 0.2382 0.2871 0.0062  0.0050  0.0078  38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.1970 0.2378 0.2784 -0.0076 -0.0026 0.0158  38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.2027 0.2536 0.2880 -0.0179 -0.0077 0.0250  38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.2134 0.2589 0.2823 -0.0293 -0.0085 0.0198  38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.2228 0.2629 0.2807 -0.0328 -0.0053 0.0146  38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.2536 0.2851 0.2933 -0.0455 -0.0039 0.0125  38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.2571 0.2825 0.2837 -0.0571 -0.0059 0.0152  38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.2548 0.2801 0.2857 -0.0479 0.0004  0.0076  38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.2171 0.2213 0.2820 0.0122  0.0052  0.0070  39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.2192 0.2029 0.2656 0.0136  0.0027  0.0006  39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.2122 0.2007 0.2625 0.0091  -0.0055 -0.0031 39  ASP   A C   
269  O O   . ASP   A 33  ? 0.2182 0.1963 0.2596 0.0085  -0.0086 -0.0055 39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.2217 0.1916 0.2546 0.0169  0.0108  0.0007  39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.2740 0.2165 0.2805 0.0154  0.0060  -0.0046 39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.2836 0.2092 0.2777 0.0135  -0.0007 -0.0065 39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.2920 0.2290 0.2895 0.0146  0.0068  -0.0059 39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.2072 0.2087 0.2713 0.0056  -0.0075 -0.0029 40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.1973 0.2006 0.2708 0.0021  -0.0100 -0.0055 40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.2093 0.2096 0.2946 0.0016  -0.0150 -0.0049 40  LEU   A C   
277  O O   . LEU   A 34  ? 0.2190 0.2223 0.3060 0.0021  -0.0149 -0.0035 40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.1929 0.2076 0.2706 -0.0035 -0.0031 -0.0061 40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.2049 0.2227 0.2749 -0.0053 0.0001  -0.0060 40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.2124 0.2342 0.2789 -0.0142 0.0055  -0.0066 40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.2083 0.2184 0.2781 -0.0028 -0.0016 -0.0087 40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.2090 0.2050 0.3076 0.0003  -0.0191 -0.0044 41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.2132 0.2082 0.3327 -0.0005 -0.0232 -0.0013 41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.2045 0.2018 0.3485 -0.0023 -0.0178 0.0002  41  LEU   A C   
285  O O   . LEU   A 35  ? 0.2203 0.2147 0.3645 -0.0027 -0.0198 0.0005  41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.2248 0.2050 0.3399 -0.0007 -0.0389 0.0026  41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.2408 0.2204 0.3826 -0.0023 -0.0464 0.0087  41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.2554 0.2200 0.3814 -0.0037 -0.0598 0.0109  41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.2523 0.2290 0.4237 -0.0053 -0.0549 0.0165  41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.1986 0.1999 0.3631 -0.0034 -0.0077 0.0011  42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.1983 0.1985 0.3917 -0.0045 0.0036  0.0034  42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.2057 0.2049 0.4361 -0.0034 -0.0008 0.0122  42  VAL   A C   
293  O O   . VAL   A 36  ? 0.2066 0.2072 0.4371 -0.0032 -0.0009 0.0126  42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.2228 0.2213 0.4055 -0.0083 0.0260  -0.0031 42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.2307 0.2221 0.4440 -0.0090 0.0438  -0.0011 42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.2314 0.2312 0.3810 -0.0111 0.0265  -0.0089 42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.1995 0.1966 0.4643 -0.0034 -0.0063 0.0209  43  SER   A N   
298  C CA  . SER   A 37  ? 0.2156 0.2127 0.5260 -0.0032 -0.0121 0.0333  43  SER   A CA  
299  C C   . SER   A 37  ? 0.2291 0.2262 0.5850 -0.0020 0.0086  0.0388  43  SER   A C   
300  O O   . SER   A 37  ? 0.2218 0.2168 0.5706 -0.0021 0.0216  0.0336  43  SER   A O   
301  C CB  . SER   A 37  ? 0.2284 0.2201 0.5453 -0.0066 -0.0425 0.0441  43  SER   A CB  
302  O OG  . SER   A 37  ? 0.2564 0.2448 0.5742 -0.0086 -0.0501 0.0471  43  SER   A OG  
303  N N   . SER   A 38  ? 0.2404 0.2383 0.6458 -0.0009 0.0131  0.0504  44  SER   A N   
304  C CA  . SER   A 38  ? 0.2650 0.2602 0.7217 0.0012  0.0373  0.0577  44  SER   A CA  
305  C C   . SER   A 38  ? 0.2911 0.2897 0.7993 0.0003  0.0194  0.0758  44  SER   A C   
306  O O   . SER   A 38  ? 0.2975 0.2983 0.8094 -0.0037 -0.0140 0.0862  44  SER   A O   
307  C CB  . SER   A 38  ? 0.2743 0.2672 0.7646 0.0033  0.0561  0.0628  44  SER   A CB  
308  O OG  . SER   A 38  ? 0.3081 0.3079 0.8246 0.0024  0.0286  0.0763  44  SER   A OG  
309  N N   . THR   A 39  ? 0.2981 0.2941 0.8452 0.0024  0.0415  0.0805  45  THR   A N   
310  C CA  . THR   A 39  ? 0.3195 0.3194 0.9232 0.0012  0.0270  0.0999  45  THR   A CA  
311  C C   . THR   A 39  ? 0.3515 0.3496 1.0331 0.0057  0.0570  0.1138  45  THR   A C   
312  O O   . THR   A 39  ? 0.3635 0.3513 1.0384 0.0093  0.0964  0.1025  45  THR   A O   
313  C CB  . THR   A 39  ? 0.3355 0.3334 0.9126 0.0003  0.0277  0.0920  45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.3634 0.3528 0.9339 0.0038  0.0682  0.0795  45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.3504 0.3477 0.8524 -0.0029 0.0062  0.0775  45  THR   A CG2 
316  N N   . THR   A 40  ? 0.3611 0.3659 1.1153 0.0042  0.0400  0.1392  46  THR   A N   
317  C CA  . THR   A 40  ? 0.3695 0.3734 1.2118 0.0092  0.0688  0.1570  46  THR   A CA  
318  C C   . THR   A 40  ? 0.3914 0.3882 1.2469 0.0124  0.0976  0.1531  46  THR   A C   
319  O O   . THR   A 40  ? 0.4033 0.3887 1.2957 0.0180  0.1422  0.1531  46  THR   A O   
320  C CB  . THR   A 40  ? 0.3704 0.3856 1.2929 0.0048  0.0344  0.1902  46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.4025 0.4213 1.3074 -0.0037 -0.0087 0.1980  46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.3776 0.3962 1.3005 0.0025  0.0164  0.1957  46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.3941 0.3946 1.2196 0.0084  0.0740  0.1502  47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.3959 0.3903 1.2311 0.0108  0.0974  0.1466  47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.4247 0.4052 1.1770 0.0117  0.1255  0.1157  47  ALA   A C   
326  O O   . ALA   A 41  ? 0.4495 0.4299 1.1311 0.0092  0.1141  0.0987  47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.3941 0.3978 1.2360 0.0051  0.0582  0.1591  47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.4240 0.3911 1.1866 0.0143  0.1617  0.1100  48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.4566 0.4057 1.1437 0.0124  0.1887  0.0834  48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.4510 0.4065 1.0859 0.0089  0.1652  0.0734  48  GLN   A C   
331  O O   . GLN   A 42  ? 0.4433 0.4043 1.1135 0.0096  0.1577  0.0841  48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.4963 0.4207 1.2141 0.0151  0.2416  0.0816  48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.6043 0.4998 1.2419 0.0099  0.2750  0.0553  48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.6786 0.5565 1.3161 0.0098  0.3033  0.0526  48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 0.6800 0.5473 1.3853 0.0150  0.3342  0.0657  48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.7122 0.5860 1.2771 0.0039  0.2942  0.0370  48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.4477 0.4009 1.0023 0.0050  0.1574  0.0538  49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.4418 0.3995 0.9425 0.0018  0.1391  0.0430  49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.4279 0.3667 0.8964 -0.0010 0.1700  0.0284  49  GLY   A C   
340  O O   . GLY   A 43  ? 0.4420 0.3590 0.8905 -0.0037 0.2031  0.0182  49  GLY   A O   
341  N N   . CYS   A 44  ? 0.3982 0.3419 0.8543 -0.0019 0.1586  0.0267  50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.4010 0.3260 0.8289 -0.0054 0.1854  0.0144  50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.3923 0.3197 0.7518 -0.0107 0.1698  0.0007  50  CYS   A C   
344  O O   . CYS   A 44  ? 0.4052 0.3198 0.7467 -0.0141 0.1851  -0.0065 50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.4184 0.3425 0.9057 -0.0016 0.1965  0.0262  50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.5056 0.4219 1.0838 0.0044  0.2259  0.0442  50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.3641 0.3062 0.6885 -0.0114 0.1413  -0.0018 51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.3767 0.3212 0.6435 -0.0160 0.1289  -0.0124 51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.3942 0.3174 0.6131 -0.0249 0.1511  -0.0255 51  ASP   A C   
350  O O   . ASP   A 45  ? 0.4054 0.3171 0.6216 -0.0272 0.1657  -0.0274 51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.3969 0.3596 0.6428 -0.0140 0.0967  -0.0104 51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.4396 0.4157 0.7114 -0.0095 0.0707  0.0008  51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.4459 0.4219 0.7384 -0.0088 0.0708  0.0054  51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.4509 0.4342 0.7177 -0.0082 0.0498  0.0051  51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.4016 0.3176 0.5811 -0.0315 0.1522  -0.0334 52  THR   A N   
356  C CA  . THR   A 46  ? 0.4262 0.3177 0.5529 -0.0440 0.1678  -0.0440 52  THR   A CA  
357  C C   . THR   A 46  ? 0.4066 0.3119 0.4945 -0.0482 0.1424  -0.0451 52  THR   A C   
358  O O   . THR   A 46  ? 0.4030 0.3261 0.4878 -0.0452 0.1223  -0.0426 52  THR   A O   
359  C CB  . THR   A 46  ? 0.4721 0.3447 0.5799 -0.0509 0.1828  -0.0501 52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.4906 0.3446 0.6352 -0.0477 0.2134  -0.0491 52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.5050 0.3505 0.5475 -0.0679 0.1900  -0.0596 52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.3875 0.2828 0.4468 -0.0557 0.1449  -0.0479 53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.3644 0.2726 0.3930 -0.0604 0.1217  -0.0464 53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.3847 0.2727 0.3644 -0.0768 0.1238  -0.0508 53  ILE   A C   
365  O O   . ILE   A 47  ? 0.4209 0.2749 0.3714 -0.0894 0.1457  -0.0573 53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.3641 0.2738 0.3895 -0.0609 0.1190  -0.0447 53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.3519 0.2761 0.4260 -0.0470 0.1186  -0.0396 53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.3665 0.2927 0.3702 -0.0641 0.0944  -0.0404 53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.3429 0.2945 0.4417 -0.0355 0.0938  -0.0330 53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.3523 0.2572 0.3217 -0.0779 0.1022  -0.0466 54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.3793 0.2684 0.3062 -0.0948 0.0974  -0.0470 54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.4047 0.2806 0.2963 -0.1098 0.0911  -0.0446 54  ALA   A C   
373  O O   . ALA   A 48  ? 0.3882 0.2834 0.2950 -0.1032 0.0793  -0.0392 54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.3520 0.2668 0.2885 -0.0902 0.0754  -0.0399 54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.4501 0.2908 0.2921 -0.1314 0.0976  -0.0477 55  ARG   A N   
376  C CA  . ARG   A 49  ? 0.4813 0.3045 0.2825 -0.1504 0.0876  -0.0433 55  ARG   A CA  
377  C C   . ARG   A 49  ? 0.5193 0.3334 0.2873 -0.1691 0.0685  -0.0363 55  ARG   A C   
378  O O   . ARG   A 49  ? 0.5608 0.3355 0.2843 -0.1872 0.0800  -0.0424 55  ARG   A O   
379  C CB  . ARG   A 49  ? 0.5174 0.2953 0.2820 -0.1628 0.1157  -0.0532 55  ARG   A CB  
380  C CG  . ARG   A 49  ? 0.5059 0.2923 0.3120 -0.1438 0.1370  -0.0583 55  ARG   A CG  
381  C CD  . ARG   A 49  ? 0.5116 0.3327 0.3497 -0.1313 0.1193  -0.0508 55  ARG   A CD  
382  N NE  . ARG   A 49  ? 0.4842 0.3100 0.3611 -0.1157 0.1384  -0.0542 55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.4685 0.3242 0.3826 -0.1012 0.1267  -0.0489 55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.4256 0.3080 0.3429 -0.0990 0.0996  -0.0412 55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.4364 0.2942 0.3873 -0.0891 0.1426  -0.0502 55  ARG   A NH2 
386  N N   . CYS   A 50  ? 0.5055 0.3548 0.2988 -0.1641 0.0412  -0.0232 56  CYS   A N   
387  C CA  . CYS   A 50  ? 0.5160 0.3642 0.2937 -0.1785 0.0215  -0.0134 56  CYS   A CA  
388  C C   . CYS   A 50  ? 0.5027 0.3873 0.3126 -0.1742 -0.0063 0.0048  56  CYS   A C   
389  O O   . CYS   A 50  ? 0.4821 0.3909 0.3235 -0.1591 -0.0080 0.0075  56  CYS   A O   
390  C CB  . CYS   A 50  ? 0.4971 0.3530 0.2942 -0.1665 0.0312  -0.0197 56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.4367 0.3418 0.3010 -0.1337 0.0292  -0.0178 56  CYS   A SG  
392  N N   . ASP   A 51  ? 0.4971 0.3865 0.3056 -0.1856 -0.0262 0.0177  57  ASP   A N   
393  C CA  . ASP   A 51  ? 0.4834 0.4083 0.3338 -0.1791 -0.0481 0.0368  57  ASP   A CA  
394  C C   . ASP   A 51  ? 0.4515 0.3996 0.3362 -0.1652 -0.0492 0.0402  57  ASP   A C   
395  O O   . ASP   A 51  ? 0.4408 0.4087 0.3527 -0.1669 -0.0672 0.0585  57  ASP   A O   
396  C CB  . ASP   A 51  ? 0.5415 0.4574 0.3738 -0.2051 -0.0755 0.0570  57  ASP   A CB  
397  C CG  . ASP   A 51  ? 0.6546 0.5477 0.4551 -0.2299 -0.0906 0.0651  57  ASP   A CG  
398  O OD1 . ASP   A 51  ? 0.6869 0.5615 0.4650 -0.2302 -0.0756 0.0508  57  ASP   A OD1 
399  O OD2 . ASP   A 51  ? 0.7186 0.6121 0.5187 -0.2500 -0.1189 0.0873  57  ASP   A OD2 
400  N N   . CYS   A 52  ? 0.4329 0.3782 0.3196 -0.1517 -0.0296 0.0243  58  CYS   A N   
401  C CA  . CYS   A 52  ? 0.3853 0.3509 0.3026 -0.1370 -0.0282 0.0257  58  CYS   A CA  
402  C C   . CYS   A 52  ? 0.3367 0.3355 0.3003 -0.1202 -0.0356 0.0383  58  CYS   A C   
403  O O   . CYS   A 52  ? 0.3311 0.3397 0.3090 -0.1094 -0.0320 0.0372  58  CYS   A O   
404  C CB  . CYS   A 52  ? 0.3876 0.3486 0.3077 -0.1220 -0.0064 0.0079  58  CYS   A CB  
405  S SG  . CYS   A 52  ? 0.4238 0.3478 0.3029 -0.1373 0.0079  -0.0051 58  CYS   A SG  
406  N N   . GLN   A 53  ? 0.3058 0.3190 0.2924 -0.1174 -0.0427 0.0493  59  GLN   A N   
407  C CA  . GLN   A 53  ? 0.2818 0.3209 0.3122 -0.1004 -0.0430 0.0604  59  GLN   A CA  
408  C C   . GLN   A 53  ? 0.2530 0.2988 0.2976 -0.0851 -0.0315 0.0544  59  GLN   A C   
409  O O   . GLN   A 53  ? 0.2379 0.2991 0.3143 -0.0745 -0.0303 0.0652  59  GLN   A O   
410  C CB  . GLN   A 53  ? 0.3123 0.3637 0.3676 -0.1114 -0.0620 0.0854  59  GLN   A CB  
411  C CG  . GLN   A 53  ? 0.3606 0.4135 0.4179 -0.1192 -0.0723 0.0948  59  GLN   A CG  
412  C CD  . GLN   A 53  ? 0.4037 0.4727 0.4993 -0.1278 -0.0912 0.1234  59  GLN   A CD  
413  O OE1 . GLN   A 53  ? 0.4300 0.4898 0.5116 -0.1519 -0.1133 0.1376  59  GLN   A OE1 
414  N NE2 . GLN   A 53  ? 0.3785 0.4690 0.5235 -0.1094 -0.0826 0.1340  59  GLN   A NE2 
415  N N   . THR   A 54  ? 0.2534 0.2853 0.2753 -0.0846 -0.0217 0.0382  60  THR   A N   
416  C CA  . THR   A 54  ? 0.2441 0.2797 0.2758 -0.0714 -0.0116 0.0316  60  THR   A CA  
417  C C   . THR   A 54  ? 0.2315 0.2562 0.2503 -0.0640 0.0010  0.0142  60  THR   A C   
418  O O   . THR   A 54  ? 0.2434 0.2531 0.2414 -0.0732 0.0043  0.0064  60  THR   A O   
419  C CB  . THR   A 54  ? 0.2999 0.3312 0.3258 -0.0807 -0.0158 0.0347  60  THR   A CB  
420  O OG1 . THR   A 54  ? 0.3497 0.3586 0.3419 -0.0950 -0.0134 0.0240  60  THR   A OG1 
421  C CG2 . THR   A 54  ? 0.3150 0.3568 0.3586 -0.0903 -0.0311 0.0551  60  THR   A CG2 
422  N N   . GLY   A 55  ? 0.2117 0.2417 0.2437 -0.0487 0.0081  0.0100  61  GLY   A N   
423  C CA  . GLY   A 55  ? 0.2028 0.2247 0.2315 -0.0417 0.0165  -0.0020 61  GLY   A CA  
424  C C   . GLY   A 55  ? 0.2040 0.2287 0.2433 -0.0287 0.0193  -0.0031 61  GLY   A C   
425  O O   . GLY   A 55  ? 0.2080 0.2381 0.2534 -0.0250 0.0185  0.0032  61  GLY   A O   
426  N N   . VAL   A 56  ? 0.1976 0.2160 0.2388 -0.0231 0.0222  -0.0098 62  VAL   A N   
427  C CA  . VAL   A 56  ? 0.2069 0.2217 0.2515 -0.0144 0.0215  -0.0101 62  VAL   A CA  
428  C C   . VAL   A 56  ? 0.2120 0.2219 0.2564 -0.0096 0.0186  -0.0112 62  VAL   A C   
429  O O   . VAL   A 56  ? 0.2022 0.2107 0.2519 -0.0120 0.0191  -0.0145 62  VAL   A O   
430  C CB  . VAL   A 56  ? 0.2284 0.2383 0.2787 -0.0159 0.0237  -0.0141 62  VAL   A CB  
431  C CG1 . VAL   A 56  ? 0.2520 0.2552 0.3041 -0.0097 0.0189  -0.0125 62  VAL   A CG1 
432  C CG2 . VAL   A 56  ? 0.2339 0.2465 0.2813 -0.0213 0.0263  -0.0131 62  VAL   A CG2 
433  N N   . TYR   A 57  ? 0.2121 0.2157 0.2489 -0.0036 0.0171  -0.0083 63  TYR   A N   
434  C CA  . TYR   A 57  ? 0.2222 0.2160 0.2536 -0.0010 0.0127  -0.0093 63  TYR   A CA  
435  C C   . TYR   A 57  ? 0.2433 0.2204 0.2644 -0.0001 0.0065  -0.0087 63  TYR   A C   
436  O O   . TYR   A 57  ? 0.2483 0.2194 0.2606 0.0007  0.0084  -0.0073 63  TYR   A O   
437  C CB  . TYR   A 57  ? 0.2219 0.2146 0.2467 0.0024  0.0162  -0.0065 63  TYR   A CB  
438  C CG  . TYR   A 57  ? 0.2429 0.2227 0.2540 0.0073  0.0229  -0.0032 63  TYR   A CG  
439  C CD1 . TYR   A 57  ? 0.2501 0.2370 0.2683 0.0090  0.0307  0.0017  63  TYR   A CD1 
440  C CD2 . TYR   A 57  ? 0.2617 0.2188 0.2519 0.0094  0.0233  -0.0043 63  TYR   A CD2 
441  C CE1 . TYR   A 57  ? 0.2657 0.2383 0.2744 0.0142  0.0419  0.0055  63  TYR   A CE1 
442  C CE2 . TYR   A 57  ? 0.2818 0.2194 0.2538 0.0131  0.0348  -0.0021 63  TYR   A CE2 
443  C CZ  . TYR   A 57  ? 0.2848 0.2306 0.2682 0.0164  0.0459  0.0028  63  TYR   A CZ  
444  O OH  . TYR   A 57  ? 0.3173 0.2418 0.2863 0.0208  0.0620  0.0056  63  TYR   A OH  
445  N N   . TYR   A 58  ? 0.2519 0.2196 0.2731 -0.0016 -0.0025 -0.0084 64  TYR   A N   
446  C CA  . TYR   A 58  ? 0.2829 0.2306 0.2908 -0.0045 -0.0135 -0.0053 64  TYR   A CA  
447  C C   . TYR   A 58  ? 0.3018 0.2264 0.2767 -0.0040 -0.0131 -0.0052 64  TYR   A C   
448  O O   . TYR   A 58  ? 0.2858 0.2087 0.2579 -0.0029 -0.0125 -0.0062 64  TYR   A O   
449  C CB  . TYR   A 58  ? 0.2877 0.2348 0.3168 -0.0087 -0.0264 -0.0014 64  TYR   A CB  
450  C CG  . TYR   A 58  ? 0.3240 0.2482 0.3384 -0.0149 -0.0429 0.0052  64  TYR   A CG  
451  C CD1 . TYR   A 58  ? 0.3483 0.2663 0.3573 -0.0173 -0.0457 0.0079  64  TYR   A CD1 
452  C CD2 . TYR   A 58  ? 0.3546 0.2601 0.3561 -0.0203 -0.0571 0.0096  64  TYR   A CD2 
453  C CE1 . TYR   A 58  ? 0.3784 0.2715 0.3688 -0.0259 -0.0634 0.0154  64  TYR   A CE1 
454  C CE2 . TYR   A 58  ? 0.3923 0.2708 0.3727 -0.0298 -0.0758 0.0172  64  TYR   A CE2 
455  C CZ  . TYR   A 58  ? 0.4154 0.2871 0.3892 -0.0331 -0.0792 0.0204  64  TYR   A CZ  
456  O OH  . TYR   A 58  ? 0.4716 0.3131 0.4202 -0.0452 -0.1001 0.0294  64  TYR   A OH  
457  N N   . CYS   A 59  ? 0.3162 0.2192 0.2638 -0.0055 -0.0116 -0.0041 65  CYS   A N   
458  C CA  . CYS   A 59  ? 0.3608 0.2313 0.2685 -0.0065 -0.0065 -0.0047 65  CYS   A CA  
459  C C   . CYS   A 59  ? 0.3990 0.2353 0.2754 -0.0173 -0.0243 -0.0013 65  CYS   A C   
460  O O   . CYS   A 59  ? 0.4111 0.2319 0.2700 -0.0217 -0.0271 0.0009  65  CYS   A O   
461  C CB  . CYS   A 59  ? 0.3913 0.2565 0.2874 -0.0010 0.0131  -0.0054 65  CYS   A CB  
462  S SG  . CYS   A 59  ? 0.4478 0.2636 0.2910 -0.0023 0.0279  -0.0067 65  CYS   A SG  
463  N N   . SER   A 60  ? 0.4095 0.2318 0.2769 -0.0232 -0.0379 0.0005  66  SER   A N   
464  C CA  . SER   A 60  ? 0.4556 0.2448 0.2951 -0.0368 -0.0602 0.0069  66  SER   A CA  
465  C C   . SER   A 60  ? 0.4963 0.2364 0.2728 -0.0442 -0.0547 0.0054  66  SER   A C   
466  O O   . SER   A 60  ? 0.5357 0.2497 0.2876 -0.0565 -0.0720 0.0116  66  SER   A O   
467  C CB  . SER   A 60  ? 0.5064 0.2906 0.3511 -0.0423 -0.0765 0.0105  66  SER   A CB  
468  O OG  . SER   A 60  ? 0.5951 0.3587 0.4078 -0.0404 -0.0641 0.0045  66  SER   A OG  
469  N N   . SER   A 61  ? 0.4949 0.2205 0.2467 -0.0372 -0.0290 -0.0017 67  SER   A N   
470  C CA  . SER   A 61  ? 0.5414 0.2141 0.2304 -0.0434 -0.0157 -0.0042 67  SER   A CA  
471  C C   . SER   A 61  ? 0.5598 0.2298 0.2426 -0.0428 -0.0079 -0.0033 67  SER   A C   
472  O O   . SER   A 61  ? 0.6205 0.2424 0.2481 -0.0495 0.0035  -0.0049 67  SER   A O   
473  C CB  . SER   A 61  ? 0.5573 0.2154 0.2308 -0.0346 0.0144  -0.0105 67  SER   A CB  
474  O OG  . SER   A 61  ? 0.5517 0.2504 0.2710 -0.0191 0.0357  -0.0113 67  SER   A OG  
475  N N   . ARG   A 62  ? 0.5083 0.2248 0.2430 -0.0359 -0.0131 -0.0008 68  ARG   A N   
476  C CA  . ARG   A 62  ? 0.5017 0.2209 0.2372 -0.0356 -0.0094 0.0010  68  ARG   A CA  
477  C C   . ARG   A 62  ? 0.5030 0.2465 0.2723 -0.0410 -0.0351 0.0077  68  ARG   A C   
478  O O   . ARG   A 62  ? 0.5079 0.2557 0.2817 -0.0414 -0.0350 0.0100  68  ARG   A O   
479  C CB  . ARG   A 62  ? 0.4926 0.2442 0.2618 -0.0207 0.0161  -0.0020 68  ARG   A CB  
480  C CG  . ARG   A 62  ? 0.5374 0.2656 0.2833 -0.0142 0.0456  -0.0052 68  ARG   A CG  
481  C CD  . ARG   A 62  ? 0.5760 0.2574 0.2718 -0.0189 0.0609  -0.0055 68  ARG   A CD  
482  N NE  . ARG   A 62  ? 0.6276 0.2867 0.3098 -0.0109 0.0953  -0.0073 68  ARG   A NE  
483  C CZ  . ARG   A 62  ? 0.6824 0.2962 0.3202 -0.0150 0.1078  -0.0109 68  ARG   A CZ  
484  N NH1 . ARG   A 62  ? 0.6976 0.2830 0.2965 -0.0286 0.0852  -0.0128 68  ARG   A NH1 
485  N NH2 . ARG   A 62  ? 0.6879 0.2828 0.3220 -0.0062 0.1435  -0.0113 68  ARG   A NH2 
486  N N   . ARG   A 63  ? 0.4908 0.2516 0.2896 -0.0441 -0.0548 0.0117  69  ARG   A N   
487  C CA  . ARG   A 63  ? 0.4757 0.2627 0.3198 -0.0471 -0.0746 0.0196  69  ARG   A CA  
488  C C   . ARG   A 63  ? 0.4477 0.2720 0.3311 -0.0362 -0.0597 0.0162  69  ARG   A C   
489  O O   . ARG   A 63  ? 0.4467 0.2765 0.3451 -0.0394 -0.0678 0.0214  69  ARG   A O   
490  C CB  . ARG   A 63  ? 0.5222 0.2768 0.3410 -0.0635 -0.1003 0.0305  69  ARG   A CB  
491  C CG  . ARG   A 63  ? 0.5946 0.3179 0.3877 -0.0776 -0.1237 0.0376  69  ARG   A CG  
492  C CD  . ARG   A 63  ? 0.6963 0.3890 0.4690 -0.0966 -0.1539 0.0520  69  ARG   A CD  
493  N NE  . ARG   A 63  ? 0.8126 0.4558 0.5315 -0.1151 -0.1755 0.0581  69  ARG   A NE  
494  C CZ  . ARG   A 63  ? 0.9007 0.4887 0.5511 -0.1336 -0.1881 0.0626  69  ARG   A CZ  
495  N NH1 . ARG   A 63  ? 0.9170 0.4949 0.5475 -0.1344 -0.1802 0.0615  69  ARG   A NH1 
496  N NH2 . ARG   A 63  ? 0.9352 0.4737 0.5313 -0.1524 -0.2079 0.0677  69  ARG   A NH2 
497  N N   . LYS   A 64  ? 0.4094 0.2553 0.3054 -0.0249 -0.0385 0.0084  70  LYS   A N   
498  C CA  . LYS   A 64  ? 0.3873 0.2630 0.3124 -0.0171 -0.0252 0.0057  70  LYS   A CA  
499  C C   . LYS   A 64  ? 0.3450 0.2506 0.3005 -0.0100 -0.0153 0.0013  70  LYS   A C   
500  O O   . LYS   A 64  ? 0.3427 0.2449 0.2904 -0.0081 -0.0119 -0.0008 70  LYS   A O   
501  C CB  . LYS   A 64  ? 0.4385 0.3018 0.3378 -0.0129 -0.0072 0.0033  70  LYS   A CB  
502  C CG  . LYS   A 64  ? 0.5547 0.3988 0.4335 -0.0179 -0.0105 0.0066  70  LYS   A CG  
503  C CD  . LYS   A 64  ? 0.6532 0.4841 0.5098 -0.0125 0.0119  0.0046  70  LYS   A CD  
504  C CE  . LYS   A 64  ? 0.7506 0.5680 0.5923 -0.0160 0.0120  0.0074  70  LYS   A CE  
505  N NZ  . LYS   A 64  ? 0.8312 0.6071 0.6285 -0.0289 -0.0038 0.0109  70  LYS   A NZ  
506  N N   . HIS   A 65  ? 0.3163 0.2477 0.3019 -0.0073 -0.0101 0.0000  71  HIS   A N   
507  C CA  . HIS   A 65  ? 0.2895 0.2435 0.2949 -0.0036 -0.0007 -0.0036 71  HIS   A CA  
508  C C   . HIS   A 65  ? 0.2960 0.2569 0.2969 0.0002  0.0120  -0.0036 71  HIS   A C   
509  O O   . HIS   A 65  ? 0.3122 0.2697 0.3089 0.0003  0.0144  -0.0020 71  HIS   A O   
510  C CB  . HIS   A 65  ? 0.2727 0.2436 0.3087 -0.0057 -0.0014 -0.0048 71  HIS   A CB  
511  C CG  . HIS   A 65  ? 0.2786 0.2461 0.3319 -0.0085 -0.0113 -0.0020 71  HIS   A CG  
512  N ND1 . HIS   A 65  ? 0.3048 0.2795 0.3721 -0.0082 -0.0089 -0.0040 71  HIS   A ND1 
513  C CD2 . HIS   A 65  ? 0.2819 0.2405 0.3455 -0.0123 -0.0238 0.0046  71  HIS   A CD2 
514  C CE1 . HIS   A 65  ? 0.2932 0.2638 0.3816 -0.0108 -0.0185 0.0017  71  HIS   A CE1 
515  N NE2 . HIS   A 65  ? 0.3022 0.2632 0.3899 -0.0138 -0.0294 0.0079  71  HIS   A NE2 
516  N N   . TYR   A 66  ? 0.2641 0.2345 0.2692 0.0028  0.0192  -0.0035 72  TYR   A N   
517  C CA  . TYR   A 66  ? 0.2646 0.2440 0.2754 0.0055  0.0293  0.0005  72  TYR   A CA  
518  C C   . TYR   A 66  ? 0.2467 0.2474 0.2769 0.0020  0.0287  0.0018  72  TYR   A C   
519  O O   . TYR   A 66  ? 0.2354 0.2407 0.2689 0.0004  0.0261  0.0004  72  TYR   A O   
520  C CB  . TYR   A 66  ? 0.2852 0.2523 0.2851 0.0108  0.0396  0.0040  72  TYR   A CB  
521  C CG  . TYR   A 66  ? 0.3285 0.2654 0.2985 0.0122  0.0444  0.0032  72  TYR   A CG  
522  C CD1 . TYR   A 66  ? 0.3628 0.2908 0.3256 0.0136  0.0526  0.0058  72  TYR   A CD1 
523  C CD2 . TYR   A 66  ? 0.3711 0.2842 0.3158 0.0104  0.0408  0.0002  72  TYR   A CD2 
524  C CE1 . TYR   A 66  ? 0.4013 0.2945 0.3283 0.0126  0.0581  0.0048  72  TYR   A CE1 
525  C CE2 . TYR   A 66  ? 0.4205 0.2973 0.3273 0.0081  0.0443  -0.0005 72  TYR   A CE2 
526  C CZ  . TYR   A 66  ? 0.4391 0.3048 0.3352 0.0088  0.0535  0.0015  72  TYR   A CZ  
527  O OH  . TYR   A 66  ? 0.4966 0.3199 0.3476 0.0046  0.0587  0.0006  72  TYR   A OH  
528  N N   . PRO   A 67  ? 0.2348 0.2458 0.2748 -0.0007 0.0303  0.0053  73  PRO   A N   
529  C CA  . PRO   A 67  ? 0.2260 0.2511 0.2772 -0.0077 0.0273  0.0087  73  PRO   A CA  
530  C C   . PRO   A 67  ? 0.2387 0.2707 0.3015 -0.0054 0.0301  0.0190  73  PRO   A C   
531  O O   . PRO   A 67  ? 0.2566 0.2855 0.3253 0.0013  0.0384  0.0254  73  PRO   A O   
532  C CB  . PRO   A 67  ? 0.2335 0.2631 0.2891 -0.0122 0.0267  0.0109  73  PRO   A CB  
533  C CG  . PRO   A 67  ? 0.2437 0.2662 0.2973 -0.0043 0.0328  0.0128  73  PRO   A CG  
534  C CD  . PRO   A 67  ? 0.2434 0.2508 0.2821 0.0012  0.0339  0.0076  73  PRO   A CD  
535  N N   . VAL   A 68  ? 0.2180 0.2574 0.2859 -0.0109 0.0248  0.0219  74  VAL   A N   
536  C CA  . VAL   A 68  ? 0.2206 0.2681 0.3065 -0.0094 0.0260  0.0342  74  VAL   A CA  
537  C C   . VAL   A 68  ? 0.2098 0.2681 0.3036 -0.0224 0.0140  0.0423  74  VAL   A C   
538  O O   . VAL   A 68  ? 0.2159 0.2699 0.2923 -0.0321 0.0075  0.0348  74  VAL   A O   
539  C CB  . VAL   A 68  ? 0.2378 0.2780 0.3190 -0.0020 0.0312  0.0310  74  VAL   A CB  
540  C CG1 . VAL   A 68  ? 0.2662 0.2894 0.3366 0.0085  0.0436  0.0277  74  VAL   A CG1 
541  C CG2 . VAL   A 68  ? 0.2391 0.2758 0.3049 -0.0063 0.0246  0.0202  74  VAL   A CG2 
542  N N   . SER   A 69  ? 0.1922 0.2614 0.3126 -0.0233 0.0120  0.0592  75  SER   A N   
543  C CA  . SER   A 69  ? 0.2022 0.2801 0.3327 -0.0365 -0.0023 0.0715  75  SER   A CA  
544  C C   . SER   A 69  ? 0.1951 0.2747 0.3345 -0.0300 0.0017  0.0736  75  SER   A C   
545  O O   . SER   A 69  ? 0.2061 0.2835 0.3581 -0.0160 0.0161  0.0746  75  SER   A O   
546  C CB  . SER   A 69  ? 0.2279 0.3185 0.3925 -0.0414 -0.0088 0.0933  75  SER   A CB  
547  O OG  . SER   A 69  ? 0.3039 0.3923 0.4594 -0.0488 -0.0140 0.0920  75  SER   A OG  
548  N N   . PHE   A 70  ? 0.1747 0.2538 0.3025 -0.0400 -0.0087 0.0725  76  PHE   A N   
549  C CA  . PHE   A 70  ? 0.1837 0.2645 0.3193 -0.0340 -0.0054 0.0738  76  PHE   A CA  
550  C C   . PHE   A 70  ? 0.2096 0.2986 0.3574 -0.0476 -0.0209 0.0891  76  PHE   A C   
551  O O   . PHE   A 70  ? 0.2343 0.3205 0.3678 -0.0653 -0.0362 0.0932  76  PHE   A O   
552  C CB  . PHE   A 70  ? 0.1896 0.2583 0.2968 -0.0286 0.0008  0.0541  76  PHE   A CB  
553  C CG  . PHE   A 70  ? 0.1885 0.2481 0.2668 -0.0399 -0.0051 0.0422  76  PHE   A CG  
554  C CD1 . PHE   A 70  ? 0.1936 0.2455 0.2575 -0.0400 -0.0011 0.0319  76  PHE   A CD1 
555  C CD2 . PHE   A 70  ? 0.2014 0.2577 0.2676 -0.0505 -0.0121 0.0418  76  PHE   A CD2 
556  C CE1 . PHE   A 70  ? 0.2137 0.2537 0.2543 -0.0493 -0.0011 0.0210  76  PHE   A CE1 
557  C CE2 . PHE   A 70  ? 0.2195 0.2615 0.2575 -0.0606 -0.0117 0.0303  76  PHE   A CE2 
558  C CZ  . PHE   A 70  ? 0.2230 0.2565 0.2499 -0.0597 -0.0049 0.0201  76  PHE   A CZ  
559  N N   . SER   A 71  ? 0.1977 0.2937 0.3702 -0.0408 -0.0174 0.0986  77  SER   A N   
560  C CA  . SER   A 71  ? 0.2001 0.3049 0.3892 -0.0543 -0.0342 0.1164  77  SER   A CA  
561  C C   . SER   A 71  ? 0.2209 0.3155 0.3730 -0.0665 -0.0439 0.1054  77  SER   A C   
562  O O   . SER   A 71  ? 0.2328 0.3160 0.3556 -0.0607 -0.0342 0.0849  77  SER   A O   
563  C CB  . SER   A 71  ? 0.2190 0.3344 0.4516 -0.0427 -0.0253 0.1314  77  SER   A CB  
564  O OG  . SER   A 71  ? 0.2374 0.3439 0.4538 -0.0304 -0.0115 0.1155  77  SER   A OG  
565  N N   . LYS   A 72  ? 0.2365 0.3329 0.3902 -0.0847 -0.0632 0.1206  78  LYS   A N   
566  C CA  . LYS   A 72  ? 0.2741 0.3568 0.3906 -0.0965 -0.0694 0.1108  78  LYS   A CA  
567  C C   . LYS   A 72  ? 0.2733 0.3608 0.4010 -0.0816 -0.0582 0.1049  78  LYS   A C   
568  O O   . LYS   A 72  ? 0.2654 0.3662 0.4317 -0.0688 -0.0519 0.1156  78  LYS   A O   
569  C CB  . LYS   A 72  ? 0.3408 0.4190 0.4499 -0.1230 -0.0950 0.1301  78  LYS   A CB  
570  C CG  . LYS   A 72  ? 0.4230 0.4851 0.5004 -0.1424 -0.1061 0.1300  78  LYS   A CG  
571  C CD  . LYS   A 72  ? 0.5181 0.5625 0.5659 -0.1740 -0.1322 0.1444  78  LYS   A CD  
572  C CE  . LYS   A 72  ? 0.6041 0.6276 0.6161 -0.1916 -0.1394 0.1414  78  LYS   A CE  
573  N NZ  . LYS   A 72  ? 0.6707 0.6624 0.6309 -0.2259 -0.1612 0.1486  78  LYS   A NZ  
574  N N   . PRO   A 73  ? 0.2784 0.3531 0.3740 -0.0834 -0.0542 0.0889  79  PRO   A N   
575  C CA  . PRO   A 73  ? 0.2805 0.3593 0.3868 -0.0697 -0.0449 0.0836  79  PRO   A CA  
576  C C   . PRO   A 73  ? 0.2709 0.3629 0.4099 -0.0724 -0.0545 0.1044  79  PRO   A C   
577  O O   . PRO   A 73  ? 0.2667 0.3584 0.4022 -0.0916 -0.0729 0.1186  79  PRO   A O   
578  C CB  . PRO   A 73  ? 0.3173 0.3799 0.3862 -0.0765 -0.0428 0.0676  79  PRO   A CB  
579  C CG  . PRO   A 73  ? 0.3437 0.3908 0.3811 -0.0888 -0.0434 0.0596  79  PRO   A CG  
580  C CD  . PRO   A 73  ? 0.3026 0.3563 0.3525 -0.0975 -0.0552 0.0751  79  PRO   A CD  
581  N N   . SER   A 74  ? 0.2583 0.3592 0.4286 -0.0549 -0.0421 0.1076  80  SER   A N   
582  C CA  . SER   A 74  ? 0.2569 0.3710 0.4674 -0.0554 -0.0477 0.1291  80  SER   A CA  
583  C C   . SER   A 74  ? 0.2491 0.3625 0.4755 -0.0364 -0.0294 0.1236  80  SER   A C   
584  O O   . SER   A 74  ? 0.2534 0.3547 0.4560 -0.0248 -0.0153 0.1036  80  SER   A O   
585  C CB  . SER   A 74  ? 0.2900 0.4172 0.5420 -0.0590 -0.0541 0.1528  80  SER   A CB  
586  O OG  . SER   A 74  ? 0.3413 0.4685 0.6116 -0.0414 -0.0336 0.1494  80  SER   A OG  
587  N N   . LEU   A 75  ? 0.2309 0.3551 0.4959 -0.0355 -0.0313 0.1423  81  LEU   A N   
588  C CA  . LEU   A 75  ? 0.2402 0.3609 0.5222 -0.0192 -0.0131 0.1398  81  LEU   A CA  
589  C C   . LEU   A 75  ? 0.2513 0.3703 0.5650 -0.0052 0.0076  0.1471  81  LEU   A C   
590  O O   . LEU   A 75  ? 0.2541 0.3871 0.6144 -0.0082 0.0042  0.1711  81  LEU   A O   
591  C CB  . LEU   A 75  ? 0.2331 0.3669 0.5518 -0.0249 -0.0229 0.1610  81  LEU   A CB  
592  C CG  . LEU   A 75  ? 0.2710 0.4021 0.5656 -0.0319 -0.0331 0.1537  81  LEU   A CG  
593  C CD1 . LEU   A 75  ? 0.2646 0.4102 0.6034 -0.0378 -0.0434 0.1791  81  LEU   A CD1 
594  C CD2 . LEU   A 75  ? 0.2965 0.4128 0.5663 -0.0171 -0.0152 0.1313  81  LEU   A CD2 
595  N N   . ILE   A 76  ? 0.2507 0.3504 0.5409 0.0089  0.0287  0.1287  82  ILE   A N   
596  C CA  . ILE   A 76  ? 0.2724 0.3619 0.5815 0.0217  0.0525  0.1325  82  ILE   A CA  
597  C C   . ILE   A 76  ? 0.3096 0.3756 0.6099 0.0353  0.0770  0.1233  82  ILE   A C   
598  O O   . ILE   A 76  ? 0.3171 0.3679 0.5754 0.0361  0.0754  0.1041  82  ILE   A O   
599  C CB  . ILE   A 76  ? 0.2998 0.3801 0.5763 0.0216  0.0537  0.1184  82  ILE   A CB  
600  C CG1 . ILE   A 76  ? 0.3058 0.4060 0.5939 0.0077  0.0322  0.1299  82  ILE   A CG1 
601  C CG2 . ILE   A 76  ? 0.3121 0.3734 0.5947 0.0350  0.0817  0.1178  82  ILE   A CG2 
602  C CD1 . ILE   A 76  ? 0.3490 0.4425 0.6026 0.0049  0.0288  0.1150  82  ILE   A CD1 
603  N N   . PHE   A 77  ? 0.3167 0.3769 0.6577 0.0453  0.1006  0.1382  83  PHE   A N   
604  C CA  . PHE   A 77  ? 0.3620 0.3920 0.6913 0.0574  0.1288  0.1300  83  PHE   A CA  
605  C C   . PHE   A 77  ? 0.3856 0.3802 0.6564 0.0620  0.1432  0.1069  83  PHE   A C   
606  O O   . PHE   A 77  ? 0.3943 0.3850 0.6586 0.0626  0.1478  0.1056  83  PHE   A O   
607  C CB  . PHE   A 77  ? 0.3680 0.3964 0.7581 0.0671  0.1557  0.1527  83  PHE   A CB  
608  C CG  . PHE   A 77  ? 0.4154 0.4129 0.7974 0.0772  0.1838  0.1468  83  PHE   A CG  
609  C CD1 . PHE   A 77  ? 0.4374 0.4440 0.8310 0.0753  0.1747  0.1501  83  PHE   A CD1 
610  C CD2 . PHE   A 77  ? 0.4597 0.4146 0.8172 0.0873  0.2199  0.1372  83  PHE   A CD2 
611  C CE1 . PHE   A 77  ? 0.4676 0.4433 0.8529 0.0841  0.2013  0.1447  83  PHE   A CE1 
612  C CE2 . PHE   A 77  ? 0.4910 0.4101 0.8332 0.0946  0.2472  0.1307  83  PHE   A CE2 
613  C CZ  . PHE   A 77  ? 0.4874 0.4180 0.8452 0.0933  0.2377  0.1346  83  PHE   A CZ  
614  N N   . VAL   A 78  ? 0.3973 0.3660 0.6238 0.0633  0.1464  0.0895  84  VAL   A N   
615  C CA  . VAL   A 78  ? 0.4326 0.3638 0.5986 0.0639  0.1541  0.0690  84  VAL   A CA  
616  C C   . VAL   A 78  ? 0.4788 0.3674 0.6218 0.0701  0.1808  0.0631  84  VAL   A C   
617  O O   . VAL   A 78  ? 0.4781 0.3664 0.6237 0.0701  0.1776  0.0625  84  VAL   A O   
618  C CB  . VAL   A 78  ? 0.4323 0.3706 0.5602 0.0549  0.1250  0.0536  84  VAL   A CB  
619  C CG1 . VAL   A 78  ? 0.4660 0.3645 0.5351 0.0534  0.1289  0.0361  84  VAL   A CG1 
620  C CG2 . VAL   A 78  ? 0.4108 0.3835 0.5546 0.0478  0.1030  0.0576  84  VAL   A CG2 
621  N N   . GLU   A 79  ? 0.5112 0.3594 0.6264 0.0744  0.2077  0.0578  85  GLU   A N   
622  C CA  . GLU   A 79  ? 0.5479 0.3428 0.6293 0.0784  0.2382  0.0508  85  GLU   A CA  
623  C C   . GLU   A 79  ? 0.5636 0.3319 0.5867 0.0706  0.2230  0.0337  85  GLU   A C   
624  O O   . GLU   A 79  ? 0.5671 0.3460 0.5628 0.0623  0.1935  0.0243  85  GLU   A O   
625  C CB  . GLU   A 79  ? 0.6259 0.3769 0.6738 0.0806  0.2668  0.0459  85  GLU   A CB  
626  C CG  . GLU   A 79  ? 0.7265 0.4970 0.8349 0.0895  0.2881  0.0644  85  GLU   A CG  
627  C CD  . GLU   A 79  ? 0.8637 0.6408 1.0342 0.0992  0.3137  0.0826  85  GLU   A CD  
628  O OE1 . GLU   A 79  ? 0.9140 0.6480 1.0603 0.1023  0.3401  0.0768  85  GLU   A OE1 
629  O OE2 . GLU   A 79  ? 0.8797 0.7039 1.1235 0.1023  0.3060  0.1038  85  GLU   A OE2 
630  N N   . ALA   A 80  ? 0.5731 0.3027 0.5768 0.0729  0.2447  0.0304  86  ALA   A N   
631  C CA  . ALA   A 80  ? 0.6082 0.3068 0.5549 0.0641  0.2306  0.0157  86  ALA   A CA  
632  C C   . ALA   A 80  ? 0.6537 0.3125 0.5293 0.0535  0.2209  0.0014  86  ALA   A C   
633  O O   . ALA   A 80  ? 0.6842 0.3166 0.5395 0.0542  0.2400  0.0002  86  ALA   A O   
634  C CB  . ALA   A 80  ? 0.6330 0.2875 0.5659 0.0678  0.2614  0.0148  86  ALA   A CB  
635  N N   . SER   A 81  ? 0.6543 0.3084 0.4951 0.0431  0.1908  -0.0076 87  SER   A N   
636  C CA  . SER   A 81  ? 0.6892 0.3061 0.4651 0.0299  0.1737  -0.0183 87  SER   A CA  
637  C C   . SER   A 81  ? 0.7290 0.3175 0.4657 0.0196  0.1567  -0.0249 87  SER   A C   
638  O O   . SER   A 81  ? 0.7256 0.3244 0.4860 0.0244  0.1614  -0.0224 87  SER   A O   
639  C CB  . SER   A 81  ? 0.6653 0.3279 0.4633 0.0271  0.1431  -0.0167 87  SER   A CB  
640  O OG  . SER   A 81  ? 0.6396 0.3442 0.4676 0.0255  0.1143  -0.0150 87  SER   A OG  
641  N N   . GLU   A 82  ? 0.7669 0.3195 0.4459 0.0046  0.1351  -0.0318 88  GLU   A N   
642  C CA  . GLU   A 82  ? 0.7896 0.3171 0.4344 -0.0075 0.1129  -0.0355 88  GLU   A CA  
643  C C   . GLU   A 82  ? 0.7315 0.3198 0.4304 -0.0050 0.0821  -0.0305 88  GLU   A C   
644  O O   . GLU   A 82  ? 0.7486 0.3265 0.4361 -0.0117 0.0665  -0.0313 88  GLU   A O   
645  C CB  . GLU   A 82  ? 0.9020 0.3746 0.4738 -0.0270 0.0937  -0.0403 88  GLU   A CB  
646  C CG  . GLU   A 82  ? 0.9914 0.4887 0.5738 -0.0295 0.0753  -0.0375 88  GLU   A CG  
647  C CD  . GLU   A 82  ? 1.1452 0.6045 0.6736 -0.0503 0.0431  -0.0375 88  GLU   A CD  
648  O OE1 . GLU   A 82  ? 1.1975 0.6133 0.6805 -0.0648 0.0292  -0.0387 88  GLU   A OE1 
649  O OE2 . GLU   A 82  ? 1.1747 0.6475 0.7079 -0.0533 0.0300  -0.0347 88  GLU   A OE2 
650  N N   . TYR   A 83  ? 0.6580 0.3062 0.4135 0.0036  0.0748  -0.0251 89  TYR   A N   
651  C CA  . TYR   A 83  ? 0.5975 0.2993 0.4014 0.0056  0.0507  -0.0208 89  TYR   A CA  
652  C C   . TYR   A 83  ? 0.5439 0.2865 0.4009 0.0176  0.0634  -0.0152 89  TYR   A C   
653  O O   . TYR   A 83  ? 0.5314 0.3021 0.4148 0.0175  0.0481  -0.0130 89  TYR   A O   
654  C CB  . TYR   A 83  ? 0.5674 0.3019 0.3920 0.0042  0.0332  -0.0188 89  TYR   A CB  
655  C CG  . TYR   A 83  ? 0.5976 0.2952 0.3761 -0.0072 0.0217  -0.0215 89  TYR   A CG  
656  C CD1 . TYR   A 83  ? 0.6255 0.3070 0.3843 -0.0201 -0.0069 -0.0203 89  TYR   A CD1 
657  C CD2 . TYR   A 83  ? 0.6210 0.3006 0.3791 -0.0060 0.0378  -0.0232 89  TYR   A CD2 
658  C CE1 . TYR   A 83  ? 0.6683 0.3175 0.3884 -0.0326 -0.0217 -0.0198 89  TYR   A CE1 
659  C CE2 . TYR   A 83  ? 0.6705 0.3162 0.3855 -0.0178 0.0255  -0.0248 89  TYR   A CE2 
660  C CZ  . TYR   A 83  ? 0.7045 0.3335 0.3985 -0.0319 -0.0052 -0.0227 89  TYR   A CZ  
661  O OH  . TYR   A 83  ? 0.7689 0.3628 0.4207 -0.0458 -0.0207 -0.0216 89  TYR   A OH  
662  N N   . TYR   A 84  ? 0.5142 0.2601 0.3899 0.0270  0.0904  -0.0112 90  TYR   A N   
663  C CA  . TYR   A 84  ? 0.4672 0.2522 0.3974 0.0362  0.0989  -0.0021 90  TYR   A CA  
664  C C   . TYR   A 84  ? 0.4985 0.2613 0.4363 0.0445  0.1332  0.0027  90  TYR   A C   
665  O O   . TYR   A 84  ? 0.5272 0.2607 0.4438 0.0460  0.1533  0.0011  90  TYR   A O   
666  C CB  . TYR   A 84  ? 0.4051 0.2397 0.3789 0.0391  0.0904  0.0051  90  TYR   A CB  
667  C CG  . TYR   A 84  ? 0.3617 0.2215 0.3375 0.0325  0.0629  0.0017  90  TYR   A CG  
668  C CD1 . TYR   A 84  ? 0.3570 0.2152 0.3187 0.0290  0.0558  -0.0017 90  TYR   A CD1 
669  C CD2 . TYR   A 84  ? 0.3380 0.2235 0.3340 0.0303  0.0466  0.0031  90  TYR   A CD2 
670  C CE1 . TYR   A 84  ? 0.3296 0.2096 0.2987 0.0238  0.0344  -0.0036 90  TYR   A CE1 
671  C CE2 . TYR   A 84  ? 0.3270 0.2321 0.3281 0.0249  0.0268  0.0006  90  TYR   A CE2 
672  C CZ  . TYR   A 84  ? 0.3245 0.2280 0.3150 0.0221  0.0217  -0.0023 90  TYR   A CZ  
673  O OH  . TYR   A 84  ? 0.3064 0.2267 0.3060 0.0174  0.0056  -0.0038 90  TYR   A OH  
674  N N   . PRO   A 85  ? 0.4874 0.2676 0.4634 0.0507  0.1419  0.0109  91  PRO   A N   
675  C CA  . PRO   A 85  ? 0.4974 0.2653 0.4995 0.0603  0.1765  0.0201  91  PRO   A CA  
676  C C   . PRO   A 85  ? 0.4822 0.2888 0.5335 0.0654  0.1790  0.0329  91  PRO   A C   
677  O O   . PRO   A 85  ? 0.4729 0.3147 0.5341 0.0608  0.1535  0.0332  91  PRO   A O   
678  C CB  . PRO   A 85  ? 0.4927 0.2771 0.5295 0.0639  0.1773  0.0276  91  PRO   A CB  
679  C CG  . PRO   A 85  ? 0.4717 0.3009 0.5240 0.0580  0.1410  0.0278  91  PRO   A CG  
680  C CD  . PRO   A 85  ? 0.4673 0.2828 0.4720 0.0494  0.1212  0.0145  91  PRO   A CD  
681  N N   . ALA   A 86  ? 0.4818 0.2814 0.5666 0.0743  0.2100  0.0447  92  ALA   A N   
682  C CA  . ALA   A 86  ? 0.4608 0.2972 0.5999 0.0784  0.2118  0.0607  92  ALA   A CA  
683  C C   . ALA   A 86  ? 0.4163 0.3089 0.6053 0.0748  0.1827  0.0734  92  ALA   A C   
684  O O   . ALA   A 86  ? 0.4157 0.3153 0.6225 0.0756  0.1803  0.0780  92  ALA   A O   
685  C CB  . ALA   A 86  ? 0.4634 0.2812 0.6396 0.0890  0.2520  0.0743  92  ALA   A CB  
686  N N   . ARG   A 87  ? 0.3766 0.3037 0.5782 0.0690  0.1592  0.0770  93  ARG   A N   
687  C CA  . ARG   A 87  ? 0.3288 0.2990 0.5607 0.0619  0.1307  0.0864  93  ARG   A CA  
688  C C   . ARG   A 87  ? 0.3086 0.3094 0.5604 0.0555  0.1136  0.0950  93  ARG   A C   
689  O O   . ARG   A 87  ? 0.3246 0.3151 0.5633 0.0573  0.1216  0.0910  93  ARG   A O   
690  C CB  . ARG   A 87  ? 0.3324 0.2988 0.5216 0.0554  0.1100  0.0693  93  ARG   A CB  
691  C CG  . ARG   A 87  ? 0.3265 0.2917 0.4778 0.0493  0.0943  0.0554  93  ARG   A CG  
692  C CD  . ARG   A 87  ? 0.3494 0.2949 0.4565 0.0457  0.0839  0.0386  93  ARG   A CD  
693  N NE  . ARG   A 87  ? 0.3396 0.3001 0.4327 0.0384  0.0624  0.0314  93  ARG   A NE  
694  C CZ  . ARG   A 87  ? 0.3376 0.2922 0.4129 0.0367  0.0605  0.0258  93  ARG   A CZ  
695  N NH1 . ARG   A 87  ? 0.2831 0.2498 0.3498 0.0305  0.0434  0.0198  93  ARG   A NH1 
696  N NH2 . ARG   A 87  ? 0.3389 0.2724 0.4045 0.0412  0.0779  0.0260  93  ARG   A NH2 
697  N N   . TYR   A 88  ? 0.2776 0.3117 0.5532 0.0462  0.0889  0.1056  94  TYR   A N   
698  C CA  . TYR   A 88  ? 0.2706 0.3266 0.5505 0.0367  0.0701  0.1106  94  TYR   A CA  
699  C C   . TYR   A 88  ? 0.2524 0.3048 0.4836 0.0298  0.0535  0.0904  94  TYR   A C   
700  O O   . TYR   A 88  ? 0.2427 0.2952 0.4593 0.0266  0.0443  0.0836  94  TYR   A O   
701  C CB  . TYR   A 88  ? 0.2704 0.3567 0.5922 0.0262  0.0506  0.1328  94  TYR   A CB  
702  C CG  . TYR   A 88  ? 0.2951 0.3913 0.6787 0.0310  0.0627  0.1587  94  TYR   A CG  
703  C CD1 . TYR   A 88  ? 0.3104 0.4157 0.7209 0.0297  0.0637  0.1721  94  TYR   A CD1 
704  C CD2 . TYR   A 88  ? 0.3087 0.4060 0.7292 0.0367  0.0731  0.1716  94  TYR   A CD2 
705  C CE1 . TYR   A 88  ? 0.3160 0.4319 0.7930 0.0342  0.0752  0.1993  94  TYR   A CE1 
706  C CE2 . TYR   A 88  ? 0.3059 0.4133 0.7932 0.0414  0.0857  0.1986  94  TYR   A CE2 
707  C CZ  . TYR   A 88  ? 0.3202 0.4370 0.8376 0.0405  0.0872  0.2130  94  TYR   A CZ  
708  O OH  . TYR   A 88  ? 0.3402 0.4681 0.9328 0.0454  0.1003  0.2428  94  TYR   A OH  
709  N N   . GLN   A 89  ? 0.2275 0.2767 0.4377 0.0277  0.0509  0.0823  95  GLN   A N   
710  C CA  . GLN   A 89  ? 0.2187 0.2662 0.3922 0.0210  0.0368  0.0663  95  GLN   A CA  
711  C C   . GLN   A 89  ? 0.2070 0.2754 0.3888 0.0084  0.0194  0.0743  95  GLN   A C   
712  O O   . GLN   A 89  ? 0.2085 0.2860 0.4105 0.0061  0.0190  0.0861  95  GLN   A O   
713  C CB  . GLN   A 89  ? 0.2367 0.2630 0.3792 0.0260  0.0450  0.0520  95  GLN   A CB  
714  C CG  . GLN   A 89  ? 0.2350 0.2624 0.3504 0.0190  0.0308  0.0390  95  GLN   A CG  
715  C CD  . GLN   A 89  ? 0.2675 0.2715 0.3530 0.0229  0.0355  0.0262  95  GLN   A CD  
716  O OE1 . GLN   A 89  ? 0.2777 0.2582 0.3483 0.0285  0.0454  0.0224  95  GLN   A OE1 
717  N NE2 . GLN   A 89  ? 0.2343 0.2410 0.3080 0.0185  0.0277  0.0198  95  GLN   A NE2 
718  N N   . SER   A 90  ? 0.1875 0.2610 0.3546 -0.0011 0.0056  0.0698  96  SER   A N   
719  C CA  . SER   A 90  ? 0.1815 0.2658 0.3456 -0.0163 -0.0099 0.0763  96  SER   A CA  
720  C C   . SER   A 90  ? 0.1931 0.2694 0.3273 -0.0203 -0.0110 0.0620  96  SER   A C   
721  O O   . SER   A 90  ? 0.1981 0.2629 0.3158 -0.0121 -0.0031 0.0475  96  SER   A O   
722  C CB  . SER   A 90  ? 0.2009 0.2885 0.3592 -0.0263 -0.0209 0.0787  96  SER   A CB  
723  O OG  . SER   A 90  ? 0.2279 0.3044 0.3615 -0.0225 -0.0165 0.0613  96  SER   A OG  
724  N N   . HIS   A 91  ? 0.1960 0.2762 0.3240 -0.0343 -0.0217 0.0680  97  HIS   A N   
725  C CA  . HIS   A 91  ? 0.2108 0.2819 0.3118 -0.0400 -0.0217 0.0562  97  HIS   A CA  
726  C C   . HIS   A 91  ? 0.2127 0.2810 0.3163 -0.0283 -0.0116 0.0497  97  HIS   A C   
727  O O   . HIS   A 91  ? 0.2195 0.2786 0.3041 -0.0268 -0.0075 0.0363  97  HIS   A O   
728  C CB  . HIS   A 91  ? 0.2335 0.2933 0.3104 -0.0419 -0.0186 0.0414  97  HIS   A CB  
729  C CG  . HIS   A 91  ? 0.2573 0.3148 0.3241 -0.0556 -0.0268 0.0467  97  HIS   A CG  
730  N ND1 . HIS   A 91  ? 0.3068 0.3525 0.3467 -0.0738 -0.0326 0.0470  97  HIS   A ND1 
731  C CD2 . HIS   A 91  ? 0.2721 0.3343 0.3490 -0.0547 -0.0300 0.0523  97  HIS   A CD2 
732  C CE1 . HIS   A 91  ? 0.3039 0.3462 0.3359 -0.0843 -0.0396 0.0529  97  HIS   A CE1 
733  N NE2 . HIS   A 91  ? 0.2843 0.3386 0.3406 -0.0729 -0.0389 0.0567  97  HIS   A NE2 
734  N N   . LEU   A 92  ? 0.1914 0.2658 0.3199 -0.0202 -0.0063 0.0602  98  LEU   A N   
735  C CA  . LEU   A 92  ? 0.1931 0.2608 0.3212 -0.0097 0.0051  0.0552  98  LEU   A CA  
736  C C   . LEU   A 92  ? 0.1899 0.2652 0.3291 -0.0151 0.0016  0.0647  98  LEU   A C   
737  O O   . LEU   A 92  ? 0.1855 0.2731 0.3491 -0.0224 -0.0065 0.0822  98  LEU   A O   
738  C CB  . LEU   A 92  ? 0.1878 0.2495 0.3322 0.0036  0.0194  0.0593  98  LEU   A CB  
739  C CG  . LEU   A 92  ? 0.2141 0.2590 0.3482 0.0140  0.0346  0.0525  98  LEU   A CG  
740  C CD1 . LEU   A 92  ? 0.2255 0.2547 0.3252 0.0149  0.0325  0.0349  98  LEU   A CD1 
741  C CD2 . LEU   A 92  ? 0.2463 0.2792 0.3951 0.0248  0.0529  0.0588  98  LEU   A CD2 
742  N N   . MET   A 93  ? 0.1833 0.2513 0.3075 -0.0121 0.0064  0.0552  99  MET   A N   
743  C CA  . MET   A 93  ? 0.1820 0.2561 0.3151 -0.0171 0.0033  0.0631  99  MET   A CA  
744  C C   . MET   A 93  ? 0.2032 0.2702 0.3425 -0.0041 0.0186  0.0616  99  MET   A C   
745  O O   . MET   A 93  ? 0.2346 0.2869 0.3516 0.0030  0.0260  0.0476  99  MET   A O   
746  C CB  . MET   A 93  ? 0.1922 0.2606 0.2975 -0.0269 -0.0034 0.0517  99  MET   A CB  
747  C CG  . MET   A 93  ? 0.2383 0.3045 0.3272 -0.0410 -0.0140 0.0503  99  MET   A CG  
748  S SD  . MET   A 93  ? 0.2815 0.3327 0.3366 -0.0502 -0.0128 0.0346  99  MET   A SD  
749  C CE  . MET   A 93  ? 0.2681 0.3119 0.3187 -0.0358 -0.0012 0.0186  99  MET   A CE  
750  N N   . LEU   A 94  ? 0.1788 0.2535 0.3473 -0.0022 0.0231  0.0770  100 LEU   A N   
751  C CA  . LEU   A 94  ? 0.1881 0.2512 0.3596 0.0098  0.0415  0.0756  100 LEU   A CA  
752  C C   . LEU   A 94  ? 0.1940 0.2602 0.3640 0.0064  0.0388  0.0763  100 LEU   A C   
753  O O   . LEU   A 94  ? 0.1937 0.2744 0.3770 -0.0048 0.0245  0.0865  100 LEU   A O   
754  C CB  . LEU   A 94  ? 0.1960 0.2618 0.4079 0.0177  0.0562  0.0934  100 LEU   A CB  
755  C CG  . LEU   A 94  ? 0.2396 0.3000 0.4586 0.0233  0.0640  0.0948  100 LEU   A CG  
756  C CD1 . LEU   A 94  ? 0.2507 0.3101 0.5146 0.0327  0.0848  0.1133  100 LEU   A CD1 
757  C CD2 . LEU   A 94  ? 0.2797 0.3152 0.4562 0.0293  0.0724  0.0746  100 LEU   A CD2 
758  N N   . ALA   A 95  ? 0.1952 0.2452 0.3493 0.0151  0.0528  0.0676  101 ALA   A N   
759  C CA  . ALA   A 95  ? 0.1968 0.2474 0.3504 0.0142  0.0540  0.0683  101 ALA   A CA  
760  C C   . ALA   A 95  ? 0.2174 0.2489 0.3707 0.0261  0.0773  0.0690  101 ALA   A C   
761  O O   . ALA   A 95  ? 0.2407 0.2515 0.3778 0.0332  0.0908  0.0629  101 ALA   A O   
762  C CB  . ALA   A 95  ? 0.2130 0.2575 0.3326 0.0094  0.0446  0.0517  101 ALA   A CB  
763  N N   . VAL   A 96  ? 0.2067 0.2417 0.3754 0.0272  0.0828  0.0768  102 VAL   A N   
764  C CA  . VAL   A 96  ? 0.2319 0.2443 0.3947 0.0372  0.1070  0.0765  102 VAL   A CA  
765  C C   . VAL   A 96  ? 0.2760 0.2679 0.3896 0.0360  0.1039  0.0576  102 VAL   A C   
766  O O   . VAL   A 96  ? 0.2777 0.2803 0.3845 0.0298  0.0895  0.0531  102 VAL   A O   
767  C CB  . VAL   A 96  ? 0.2369 0.2626 0.4391 0.0382  0.1132  0.0936  102 VAL   A CB  
768  C CG1 . VAL   A 96  ? 0.2800 0.2781 0.4690 0.0477  0.1400  0.0911  102 VAL   A CG1 
769  C CG2 . VAL   A 96  ? 0.2161 0.2618 0.4752 0.0385  0.1145  0.1168  102 VAL   A CG2 
770  N N   . GLY   A 97  ? 0.2997 0.2607 0.3791 0.0403  0.1159  0.0477  103 GLY   A N   
771  C CA  . GLY   A 97  ? 0.3302 0.2702 0.3648 0.0369  0.1088  0.0331  103 GLY   A CA  
772  C C   . GLY   A 97  ? 0.3644 0.2660 0.3589 0.0384  0.1192  0.0249  103 GLY   A C   
773  O O   . GLY   A 97  ? 0.3796 0.2729 0.3795 0.0424  0.1308  0.0278  103 GLY   A O   
774  N N   . HIS   A 98  ? 0.3692 0.2447 0.3222 0.0339  0.1143  0.0158  104 HIS   A N   
775  C CA  . HIS   A 98  ? 0.4034 0.2353 0.3086 0.0313  0.1202  0.0085  104 HIS   A CA  
776  C C   . HIS   A 98  ? 0.3874 0.2218 0.2821 0.0258  0.0997  0.0025  104 HIS   A C   
777  O O   . HIS   A 98  ? 0.3655 0.2254 0.2745 0.0216  0.0779  0.0006  104 HIS   A O   
778  C CB  . HIS   A 98  ? 0.4464 0.2459 0.3088 0.0254  0.1192  0.0037  104 HIS   A CB  
779  C CG  . HIS   A 98  ? 0.5284 0.2757 0.3319 0.0181  0.1213  -0.0028 104 HIS   A CG  
780  N ND1 . HIS   A 98  ? 0.5848 0.2913 0.3615 0.0211  0.1499  -0.0032 104 HIS   A ND1 
781  C CD2 . HIS   A 98  ? 0.5681 0.2970 0.3373 0.0070  0.0975  -0.0078 104 HIS   A CD2 
782  C CE1 . HIS   A 98  ? 0.6318 0.2925 0.3501 0.0101  0.1420  -0.0099 104 HIS   A CE1 
783  N NE2 . HIS   A 98  ? 0.6298 0.3036 0.3435 0.0009  0.1085  -0.0116 104 HIS   A NE2 
784  N N   . SER   A 99  ? 0.4069 0.2089 0.2726 0.0250  0.1084  -0.0006 105 SER   A N   
785  C CA  . SER   A 99  ? 0.4246 0.2200 0.2738 0.0189  0.0900  -0.0057 105 SER   A CA  
786  C C   . SER   A 99  ? 0.4820 0.2233 0.2796 0.0149  0.1024  -0.0100 105 SER   A C   
787  O O   . SER   A 99  ? 0.5080 0.2234 0.2941 0.0201  0.1308  -0.0086 105 SER   A O   
788  C CB  . SER   A 99  ? 0.4112 0.2464 0.3034 0.0229  0.0827  -0.0028 105 SER   A CB  
789  O OG  . SER   A 99  ? 0.4252 0.2549 0.3280 0.0294  0.1023  0.0010  105 SER   A OG  
790  N N   . GLU   A 100 ? 0.5016 0.2238 0.2692 0.0050  0.0815  -0.0141 106 GLU   A N   
791  C CA  . GLU   A 100 ? 0.5582 0.2274 0.2721 -0.0026 0.0861  -0.0183 106 GLU   A CA  
792  C C   . GLU   A 100 ? 0.5615 0.2472 0.2892 -0.0059 0.0639  -0.0187 106 GLU   A C   
793  O O   . GLU   A 100 ? 0.5406 0.2703 0.3097 -0.0046 0.0443  -0.0163 106 GLU   A O   
794  C CB  . GLU   A 100 ? 0.6320 0.2484 0.2823 -0.0167 0.0789  -0.0208 106 GLU   A CB  
795  C CG  . GLU   A 100 ? 0.7098 0.3052 0.3439 -0.0127 0.1060  -0.0208 106 GLU   A CG  
796  C CD  . GLU   A 100 ? 0.7992 0.3500 0.3762 -0.0269 0.0967  -0.0219 106 GLU   A CD  
797  O OE1 . GLU   A 100 ? 0.8580 0.3638 0.3801 -0.0430 0.0793  -0.0236 106 GLU   A OE1 
798  O OE2 . GLU   A 100 ? 0.7687 0.3280 0.3548 -0.0233 0.1052  -0.0199 106 GLU   A OE2 
799  N N   . PRO   A 101 ? 0.5942 0.2444 0.2890 -0.0102 0.0684  -0.0217 107 PRO   A N   
800  C CA  . PRO   A 101 ? 0.5758 0.2471 0.2918 -0.0115 0.0493  -0.0211 107 PRO   A CA  
801  C C   . PRO   A 101 ? 0.5556 0.2478 0.2867 -0.0200 0.0143  -0.0179 107 PRO   A C   
802  O O   . PRO   A 101 ? 0.5271 0.2625 0.3053 -0.0153 0.0033  -0.0157 107 PRO   A O   
803  C CB  . PRO   A 101 ? 0.6274 0.2439 0.2910 -0.0184 0.0584  -0.0251 107 PRO   A CB  
804  C CG  . PRO   A 101 ? 0.6611 0.2445 0.3011 -0.0124 0.0960  -0.0274 107 PRO   A CG  
805  C CD  . PRO   A 101 ? 0.6363 0.2272 0.2782 -0.0123 0.0962  -0.0257 107 PRO   A CD  
806  N N   . GLY   A 102 ? 0.5735 0.2351 0.2684 -0.0327 -0.0018 -0.0164 108 GLY   A N   
807  C CA  . GLY   A 102 ? 0.5583 0.2367 0.2728 -0.0413 -0.0341 -0.0100 108 GLY   A CA  
808  C C   . GLY   A 102 ? 0.5054 0.2375 0.2779 -0.0324 -0.0362 -0.0076 108 GLY   A C   
809  O O   . GLY   A 102 ? 0.4979 0.2497 0.2995 -0.0369 -0.0580 -0.0017 108 GLY   A O   
810  N N   . ASP   A 103 ? 0.4656 0.2197 0.2565 -0.0206 -0.0129 -0.0109 109 ASP   A N   
811  C CA  . ASP   A 103 ? 0.4148 0.2153 0.2546 -0.0135 -0.0131 -0.0094 109 ASP   A CA  
812  C C   . ASP   A 103 ? 0.3693 0.2082 0.2529 -0.0077 -0.0150 -0.0092 109 ASP   A C   
813  O O   . ASP   A 103 ? 0.3455 0.2172 0.2650 -0.0049 -0.0174 -0.0083 109 ASP   A O   
814  C CB  . ASP   A 103 ? 0.4227 0.2319 0.2672 -0.0053 0.0090  -0.0108 109 ASP   A CB  
815  C CG  . ASP   A 103 ? 0.4572 0.2367 0.2675 -0.0108 0.0100  -0.0105 109 ASP   A CG  
816  O OD1 . ASP   A 103 ? 0.4677 0.2382 0.2694 -0.0202 -0.0110 -0.0076 109 ASP   A OD1 
817  O OD2 . ASP   A 103 ? 0.4711 0.2351 0.2653 -0.0062 0.0320  -0.0117 109 ASP   A OD2 
818  N N   . CYS   A 104 ? 0.3754 0.2077 0.2538 -0.0066 -0.0124 -0.0105 110 CYS   A N   
819  C CA  . CYS   A 104 ? 0.3462 0.2116 0.2623 -0.0024 -0.0146 -0.0100 110 CYS   A CA  
820  C C   . CYS   A 104 ? 0.3372 0.2189 0.2801 -0.0070 -0.0326 -0.0068 110 CYS   A C   
821  O O   . CYS   A 104 ? 0.3543 0.2159 0.2853 -0.0152 -0.0497 -0.0028 110 CYS   A O   
822  C CB  . CYS   A 104 ? 0.3572 0.2083 0.2607 -0.0018 -0.0118 -0.0111 110 CYS   A CB  
823  S SG  . CYS   A 104 ? 0.3928 0.2364 0.2876 0.0070  0.0159  -0.0123 110 CYS   A SG  
824  N N   . GLY   A 105 ? 0.3003 0.2147 0.2788 -0.0030 -0.0282 -0.0072 111 GLY   A N   
825  C CA  . GLY   A 105 ? 0.2899 0.2178 0.2985 -0.0061 -0.0384 -0.0040 111 GLY   A CA  
826  C C   . GLY   A 105 ? 0.2932 0.2318 0.3160 -0.0063 -0.0361 -0.0036 111 GLY   A C   
827  O O   . GLY   A 105 ? 0.2810 0.2336 0.3347 -0.0071 -0.0368 -0.0016 111 GLY   A O   
828  N N   . GLY   A 106 ? 0.2886 0.2194 0.2908 -0.0052 -0.0306 -0.0052 112 GLY   A N   
829  C CA  . GLY   A 106 ? 0.2684 0.2106 0.2837 -0.0050 -0.0269 -0.0053 112 GLY   A CA  
830  C C   . GLY   A 106 ? 0.2483 0.2150 0.2850 -0.0023 -0.0148 -0.0087 112 GLY   A C   
831  O O   . GLY   A 106 ? 0.2416 0.2155 0.2738 0.0001  -0.0072 -0.0104 112 GLY   A O   
832  N N   . ILE   A 107 ? 0.2358 0.2120 0.2944 -0.0041 -0.0130 -0.0086 113 ILE   A N   
833  C CA  . ILE   A 107 ? 0.2258 0.2163 0.2956 -0.0049 -0.0011 -0.0123 113 ILE   A CA  
834  C C   . ILE   A 107 ? 0.2165 0.2127 0.2751 -0.0052 0.0058  -0.0140 113 ILE   A C   
835  O O   . ILE   A 107 ? 0.2217 0.2142 0.2757 -0.0045 0.0043  -0.0129 113 ILE   A O   
836  C CB  . ILE   A 107 ? 0.2465 0.2385 0.3443 -0.0072 0.0022  -0.0115 113 ILE   A CB  
837  C CG1 . ILE   A 107 ? 0.2537 0.2443 0.3700 -0.0072 -0.0008 -0.0086 113 ILE   A CG1 
838  C CG2 . ILE   A 107 ? 0.2615 0.2578 0.3617 -0.0105 0.0168  -0.0162 113 ILE   A CG2 
839  C CD1 . ILE   A 107 ? 0.2669 0.2571 0.4208 -0.0083 0.0043  -0.0044 113 ILE   A CD1 
840  N N   . LEU   A 108 ? 0.1987 0.2034 0.2541 -0.0079 0.0119  -0.0152 114 LEU   A N   
841  C CA  . LEU   A 108 ? 0.2003 0.2111 0.2495 -0.0116 0.0161  -0.0144 114 LEU   A CA  
842  C C   . LEU   A 108 ? 0.2144 0.2231 0.2658 -0.0193 0.0231  -0.0186 114 LEU   A C   
843  O O   . LEU   A 108 ? 0.2112 0.2170 0.2631 -0.0228 0.0268  -0.0207 114 LEU   A O   
844  C CB  . LEU   A 108 ? 0.2037 0.2215 0.2481 -0.0123 0.0152  -0.0096 114 LEU   A CB  
845  C CG  . LEU   A 108 ? 0.2069 0.2314 0.2488 -0.0196 0.0155  -0.0052 114 LEU   A CG  
846  C CD1 . LEU   A 108 ? 0.2169 0.2426 0.2605 -0.0165 0.0165  -0.0026 114 LEU   A CD1 
847  C CD2 . LEU   A 108 ? 0.2127 0.2455 0.2589 -0.0211 0.0119  0.0036  114 LEU   A CD2 
848  N N   . ARG   A 109 ? 0.2108 0.2173 0.2611 -0.0224 0.0269  -0.0201 115 ARG   A N   
849  C CA  . ARG   A 109 ? 0.2181 0.2152 0.2656 -0.0306 0.0375  -0.0250 115 ARG   A CA  
850  C C   . ARG   A 109 ? 0.2430 0.2384 0.2736 -0.0394 0.0377  -0.0243 115 ARG   A C   
851  O O   . ARG   A 109 ? 0.2399 0.2426 0.2726 -0.0362 0.0323  -0.0206 115 ARG   A O   
852  C CB  . ARG   A 109 ? 0.2494 0.2414 0.3162 -0.0269 0.0434  -0.0269 115 ARG   A CB  
853  C CG  . ARG   A 109 ? 0.3300 0.3207 0.4207 -0.0215 0.0434  -0.0253 115 ARG   A CG  
854  C CD  . ARG   A 109 ? 0.3705 0.3567 0.4865 -0.0198 0.0490  -0.0238 115 ARG   A CD  
855  N NE  . ARG   A 109 ? 0.4310 0.4044 0.5495 -0.0256 0.0693  -0.0290 115 ARG   A NE  
856  C CZ  . ARG   A 109 ? 0.4432 0.4085 0.5828 -0.0255 0.0823  -0.0289 115 ARG   A CZ  
857  N NH1 . ARG   A 109 ? 0.4751 0.4219 0.6089 -0.0319 0.1053  -0.0348 115 ARG   A NH1 
858  N NH2 . ARG   A 109 ? 0.4297 0.4019 0.5965 -0.0196 0.0735  -0.0221 115 ARG   A NH2 
859  N N   . CYS   A 110 ? 0.2595 0.2412 0.2720 -0.0515 0.0449  -0.0278 116 CYS   A N   
860  C CA  . CYS   A 110 ? 0.2994 0.2721 0.2905 -0.0641 0.0444  -0.0272 116 CYS   A CA  
861  C C   . CYS   A 110 ? 0.3367 0.2866 0.3197 -0.0703 0.0625  -0.0361 116 CYS   A C   
862  O O   . CYS   A 110 ? 0.3333 0.2791 0.3356 -0.0630 0.0745  -0.0403 116 CYS   A O   
863  C CB  . CYS   A 110 ? 0.3213 0.2892 0.2894 -0.0776 0.0360  -0.0221 116 CYS   A CB  
864  S SG  . CYS   A 110 ? 0.3493 0.2921 0.2942 -0.0883 0.0490  -0.0295 116 CYS   A SG  
865  N N   . GLN   A 111 ? 0.3821 0.3151 0.3390 -0.0841 0.0652  -0.0378 117 GLN   A N   
866  C CA  . GLN   A 111 ? 0.4274 0.3327 0.3728 -0.0909 0.0864  -0.0468 117 GLN   A CA  
867  C C   . GLN   A 111 ? 0.4575 0.3387 0.3921 -0.0958 0.1058  -0.0536 117 GLN   A C   
868  O O   . GLN   A 111 ? 0.4876 0.3486 0.4290 -0.0952 0.1294  -0.0603 117 GLN   A O   
869  C CB  . GLN   A 111 ? 0.4966 0.3819 0.4055 -0.1087 0.0842  -0.0472 117 GLN   A CB  
870  C CG  . GLN   A 111 ? 0.5752 0.4471 0.4451 -0.1276 0.0716  -0.0426 117 GLN   A CG  
871  C CD  . GLN   A 111 ? 0.6866 0.5349 0.5178 -0.1485 0.0654  -0.0409 117 GLN   A CD  
872  O OE1 . GLN   A 111 ? 0.7149 0.5732 0.5383 -0.1582 0.0419  -0.0289 117 GLN   A OE1 
873  N NE2 . GLN   A 111 ? 0.6961 0.5107 0.5039 -0.1569 0.0867  -0.0514 117 GLN   A NE2 
874  N N   . HIS   A 112 ? 0.4417 0.3245 0.3632 -0.1000 0.0979  -0.0510 118 HIS   A N   
875  C CA  . HIS   A 112 ? 0.4437 0.3016 0.3517 -0.1056 0.1169  -0.0570 118 HIS   A CA  
876  C C   . HIS   A 112 ? 0.4136 0.2887 0.3655 -0.0883 0.1228  -0.0561 118 HIS   A C   
877  O O   . HIS   A 112 ? 0.4357 0.2913 0.3882 -0.0898 0.1430  -0.0605 118 HIS   A O   
878  C CB  . HIS   A 112 ? 0.4708 0.3148 0.3360 -0.1230 0.1063  -0.0544 118 HIS   A CB  
879  C CG  . HIS   A 112 ? 0.5219 0.3480 0.3443 -0.1434 0.0947  -0.0516 118 HIS   A CG  
880  N ND1 . HIS   A 112 ? 0.5291 0.3784 0.3532 -0.1468 0.0661  -0.0394 118 HIS   A ND1 
881  C CD2 . HIS   A 112 ? 0.5800 0.3655 0.3592 -0.1617 0.1084  -0.0583 118 HIS   A CD2 
882  C CE1 . HIS   A 112 ? 0.5754 0.4014 0.3616 -0.1670 0.0597  -0.0374 118 HIS   A CE1 
883  N NE2 . HIS   A 112 ? 0.6131 0.3980 0.3661 -0.1776 0.0841  -0.0494 118 HIS   A NE2 
884  N N   . GLY   A 113 ? 0.3553 0.2633 0.3416 -0.0732 0.1054  -0.0497 119 GLY   A N   
885  C CA  . GLY   A 113 ? 0.3224 0.2448 0.3469 -0.0595 0.1055  -0.0468 119 GLY   A CA  
886  C C   . GLY   A 113 ? 0.2744 0.2227 0.3078 -0.0513 0.0825  -0.0402 119 GLY   A C   
887  O O   . GLY   A 113 ? 0.2743 0.2348 0.2979 -0.0513 0.0678  -0.0366 119 GLY   A O   
888  N N   . VAL   A 114 ? 0.2589 0.2139 0.3138 -0.0438 0.0812  -0.0379 120 VAL   A N   
889  C CA  . VAL   A 114 ? 0.2503 0.2237 0.3116 -0.0364 0.0630  -0.0326 120 VAL   A CA  
890  C C   . VAL   A 114 ? 0.2520 0.2280 0.2871 -0.0432 0.0552  -0.0312 120 VAL   A C   
891  O O   . VAL   A 114 ? 0.2699 0.2335 0.2899 -0.0515 0.0631  -0.0336 120 VAL   A O   
892  C CB  . VAL   A 114 ? 0.2543 0.2311 0.3453 -0.0284 0.0625  -0.0297 120 VAL   A CB  
893  C CG1 . VAL   A 114 ? 0.2620 0.2517 0.3508 -0.0229 0.0449  -0.0254 120 VAL   A CG1 
894  C CG2 . VAL   A 114 ? 0.2509 0.2284 0.3748 -0.0224 0.0635  -0.0261 120 VAL   A CG2 
895  N N   . VAL   A 115 ? 0.2305 0.2205 0.2622 -0.0401 0.0409  -0.0260 121 VAL   A N   
896  C CA  . VAL   A 115 ? 0.2322 0.2283 0.2498 -0.0455 0.0316  -0.0205 121 VAL   A CA  
897  C C   . VAL   A 115 ? 0.2255 0.2320 0.2550 -0.0370 0.0247  -0.0169 121 VAL   A C   
898  O O   . VAL   A 115 ? 0.2322 0.2396 0.2550 -0.0418 0.0217  -0.0139 121 VAL   A O   
899  C CB  . VAL   A 115 ? 0.2460 0.2504 0.2600 -0.0472 0.0233  -0.0145 121 VAL   A CB  
900  C CG1 . VAL   A 115 ? 0.2454 0.2592 0.2575 -0.0515 0.0125  -0.0044 121 VAL   A CG1 
901  C CG2 . VAL   A 115 ? 0.2841 0.2763 0.2822 -0.0579 0.0283  -0.0175 121 VAL   A CG2 
902  N N   . GLY   A 116 ? 0.2065 0.2182 0.2501 -0.0258 0.0212  -0.0165 122 GLY   A N   
903  C CA  . GLY   A 116 ? 0.2162 0.2318 0.2658 -0.0188 0.0156  -0.0138 122 GLY   A CA  
904  C C   . GLY   A 116 ? 0.2123 0.2242 0.2677 -0.0103 0.0115  -0.0140 122 GLY   A C   
905  O O   . GLY   A 116 ? 0.2015 0.2094 0.2615 -0.0098 0.0122  -0.0157 122 GLY   A O   
906  N N   . ILE   A 117 ? 0.2114 0.2212 0.2643 -0.0052 0.0070  -0.0117 123 ILE   A N   
907  C CA  . ILE   A 117 ? 0.2144 0.2123 0.2621 -0.0006 0.0017  -0.0115 123 ILE   A CA  
908  C C   . ILE   A 117 ? 0.2122 0.2037 0.2461 0.0038  0.0041  -0.0088 123 ILE   A C   
909  O O   . ILE   A 117 ? 0.2007 0.1985 0.2372 0.0049  0.0078  -0.0059 123 ILE   A O   
910  C CB  . ILE   A 117 ? 0.2348 0.2253 0.2892 -0.0004 -0.0055 -0.0114 123 ILE   A CB  
911  C CG1 . ILE   A 117 ? 0.2578 0.2530 0.3136 0.0000  -0.0042 -0.0110 123 ILE   A CG1 
912  C CG2 . ILE   A 117 ? 0.2519 0.2438 0.3272 -0.0031 -0.0064 -0.0114 123 ILE   A CG2 
913  C CD1 . ILE   A 117 ? 0.2879 0.2728 0.3482 0.0004  -0.0135 -0.0096 123 ILE   A CD1 
914  N N   . VAL   A 118 ? 0.2227 0.1994 0.2423 0.0057  0.0037  -0.0089 124 VAL   A N   
915  C CA  . VAL   A 118 ? 0.2279 0.1909 0.2317 0.0100  0.0115  -0.0068 124 VAL   A CA  
916  C C   . VAL   A 118 ? 0.2348 0.1872 0.2314 0.0116  0.0115  -0.0069 124 VAL   A C   
917  O O   . VAL   A 118 ? 0.2446 0.1871 0.2352 0.0086  0.0013  -0.0089 124 VAL   A O   
918  C CB  . VAL   A 118 ? 0.2552 0.1949 0.2359 0.0096  0.0112  -0.0080 124 VAL   A CB  
919  C CG1 . VAL   A 118 ? 0.3005 0.2167 0.2589 0.0134  0.0242  -0.0070 124 VAL   A CG1 
920  C CG2 . VAL   A 118 ? 0.2530 0.2035 0.2418 0.0088  0.0124  -0.0075 124 VAL   A CG2 
921  N N   . SER   A 119 ? 0.2380 0.1924 0.2389 0.0158  0.0226  -0.0031 125 SER   A N   
922  C CA  . SER   A 119 ? 0.2546 0.1993 0.2508 0.0177  0.0246  -0.0029 125 SER   A CA  
923  C C   . SER   A 119 ? 0.2848 0.2091 0.2700 0.0231  0.0418  -0.0001 125 SER   A C   
924  O O   . SER   A 119 ? 0.3118 0.2143 0.2798 0.0236  0.0448  -0.0022 125 SER   A O   
925  C CB  . SER   A 119 ? 0.2621 0.2325 0.2835 0.0166  0.0208  0.0003  125 SER   A CB  
926  O OG  . SER   A 119 ? 0.2719 0.2370 0.2943 0.0191  0.0241  0.0021  125 SER   A OG  
927  N N   . THR   A 120 ? 0.2886 0.2182 0.2856 0.0270  0.0547  0.0054  126 THR   A N   
928  C CA  . THR   A 120 ? 0.3190 0.2262 0.3109 0.0333  0.0771  0.0094  126 THR   A CA  
929  C C   . THR   A 120 ? 0.3393 0.2353 0.3246 0.0355  0.0896  0.0111  126 THR   A C   
930  O O   . THR   A 120 ? 0.3237 0.2360 0.3147 0.0325  0.0795  0.0107  126 THR   A O   
931  C CB  . THR   A 120 ? 0.3160 0.2461 0.3490 0.0380  0.0856  0.0211  126 THR   A CB  
932  O OG1 . THR   A 120 ? 0.3215 0.2800 0.3864 0.0372  0.0828  0.0304  126 THR   A OG1 
933  C CG2 . THR   A 120 ? 0.3090 0.2539 0.3526 0.0355  0.0733  0.0210  126 THR   A CG2 
934  N N   . GLY   A 121 ? 0.3635 0.2308 0.3386 0.0410  0.1143  0.0136  127 GLY   A N   
935  C CA  . GLY   A 121 ? 0.3924 0.2496 0.3665 0.0440  0.1302  0.0170  127 GLY   A CA  
936  C C   . GLY   A 121 ? 0.4395 0.2617 0.4065 0.0509  0.1635  0.0207  127 GLY   A C   
937  O O   . GLY   A 121 ? 0.4720 0.2706 0.4248 0.0522  0.1743  0.0184  127 GLY   A O   
938  N N   . GLY   A 122 ? 0.4638 0.2801 0.4398 0.0550  0.1814  0.0263  128 GLY   A N   
939  C CA  . GLY   A 122 ? 0.5107 0.2889 0.4815 0.0622  0.2196  0.0305  128 GLY   A CA  
940  C C   . GLY   A 122 ? 0.5097 0.3088 0.5311 0.0696  0.2361  0.0455  128 GLY   A C   
941  O O   . GLY   A 122 ? 0.4711 0.3189 0.5424 0.0694  0.2175  0.0561  128 GLY   A O   
942  N N   . ASN   A 123 ? 0.5444 0.3042 0.5503 0.0744  0.2701  0.0467  129 ASN   A N   
943  C CA  . ASN   A 123 ? 0.5390 0.3148 0.5977 0.0824  0.2903  0.0631  129 ASN   A CA  
944  C C   . ASN   A 123 ? 0.5167 0.3318 0.5962 0.0786  0.2650  0.0670  129 ASN   A C   
945  O O   . ASN   A 123 ? 0.5084 0.3542 0.6483 0.0832  0.2694  0.0847  129 ASN   A O   
946  C CB  . ASN   A 123 ? 0.5387 0.3428 0.6715 0.0906  0.3020  0.0831  129 ASN   A CB  
947  C CG  . ASN   A 123 ? 0.6267 0.3882 0.7481 0.0968  0.3370  0.0821  129 ASN   A CG  
948  O OD1 . ASN   A 123 ? 0.6906 0.3965 0.7699 0.0993  0.3720  0.0749  129 ASN   A OD1 
949  N ND2 . ASN   A 123 ? 0.6060 0.3895 0.7632 0.0986  0.3301  0.0897  129 ASN   A ND2 
950  N N   . GLY   A 124 ? 0.5027 0.3141 0.5345 0.0697  0.2400  0.0520  130 GLY   A N   
951  C CA  . GLY   A 124 ? 0.4743 0.3190 0.5215 0.0656  0.2173  0.0540  130 GLY   A CA  
952  C C   . GLY   A 124 ? 0.4237 0.3193 0.5086 0.0609  0.1854  0.0592  130 GLY   A C   
953  O O   . GLY   A 124 ? 0.4201 0.3436 0.5243 0.0571  0.1693  0.0633  130 GLY   A O   
954  N N   . LEU   A 125 ? 0.3954 0.2990 0.4848 0.0597  0.1763  0.0580  131 LEU   A N   
955  C CA  . LEU   A 125 ? 0.3553 0.2992 0.4703 0.0533  0.1476  0.0614  131 LEU   A CA  
956  C C   . LEU   A 125 ? 0.3605 0.2956 0.4343 0.0476  0.1298  0.0451  131 LEU   A C   
957  O O   . LEU   A 125 ? 0.4063 0.3122 0.4517 0.0496  0.1397  0.0380  131 LEU   A O   
958  C CB  . LEU   A 125 ? 0.3433 0.3071 0.5085 0.0563  0.1521  0.0780  131 LEU   A CB  
959  C CG  . LEU   A 125 ? 0.3566 0.3343 0.5781 0.0613  0.1671  0.0998  131 LEU   A CG  
960  C CD1 . LEU   A 125 ? 0.3599 0.3424 0.6266 0.0669  0.1812  0.1160  131 LEU   A CD1 
961  C CD2 . LEU   A 125 ? 0.3412 0.3557 0.5911 0.0521  0.1410  0.1101  131 LEU   A CD2 
962  N N   . VAL   A 126 ? 0.3009 0.2589 0.3727 0.0399  0.1047  0.0402  132 VAL   A N   
963  C CA  . VAL   A 126 ? 0.2815 0.2346 0.3253 0.0349  0.0886  0.0278  132 VAL   A CA  
964  C C   . VAL   A 126 ? 0.2543 0.2375 0.3238 0.0301  0.0730  0.0323  132 VAL   A C   
965  O O   . VAL   A 126 ? 0.2389 0.2461 0.3343 0.0260  0.0658  0.0410  132 VAL   A O   
966  C CB  . VAL   A 126 ? 0.2941 0.2422 0.3131 0.0298  0.0765  0.0183  132 VAL   A CB  
967  C CG1 . VAL   A 126 ? 0.2882 0.2623 0.3301 0.0265  0.0689  0.0233  132 VAL   A CG1 
968  C CG2 . VAL   A 126 ? 0.2991 0.2439 0.2992 0.0246  0.0596  0.0088  132 VAL   A CG2 
969  N N   . GLY   A 127 ? 0.2401 0.2186 0.2994 0.0293  0.0678  0.0270  133 GLY   A N   
970  C CA  . GLY   A 127 ? 0.2147 0.2161 0.2917 0.0240  0.0544  0.0301  133 GLY   A CA  
971  C C   . GLY   A 127 ? 0.2347 0.2366 0.2930 0.0182  0.0398  0.0189  133 GLY   A C   
972  O O   . GLY   A 127 ? 0.2598 0.2423 0.2945 0.0195  0.0388  0.0102  133 GLY   A O   
973  N N   . PHE   A 128 ? 0.2125 0.2337 0.2812 0.0105  0.0286  0.0203  134 PHE   A N   
974  C CA  . PHE   A 128 ? 0.2119 0.2335 0.2694 0.0049  0.0193  0.0111  134 PHE   A CA  
975  C C   . PHE   A 128 ? 0.2048 0.2358 0.2693 -0.0001 0.0139  0.0133  134 PHE   A C   
976  O O   . PHE   A 128 ? 0.2074 0.2504 0.2843 -0.0055 0.0109  0.0225  134 PHE   A O   
977  C CB  . PHE   A 128 ? 0.2100 0.2382 0.2666 -0.0017 0.0156  0.0093  134 PHE   A CB  
978  C CG  . PHE   A 128 ? 0.2130 0.2353 0.2660 0.0023  0.0204  0.0093  134 PHE   A CG  
979  C CD1 . PHE   A 128 ? 0.2262 0.2352 0.2656 0.0047  0.0199  0.0018  134 PHE   A CD1 
980  C CD2 . PHE   A 128 ? 0.2195 0.2500 0.2850 0.0019  0.0236  0.0184  134 PHE   A CD2 
981  C CE1 . PHE   A 128 ? 0.2296 0.2313 0.2628 0.0073  0.0239  0.0021  134 PHE   A CE1 
982  C CE2 . PHE   A 128 ? 0.2234 0.2479 0.2856 0.0054  0.0291  0.0183  134 PHE   A CE2 
983  C CZ  . PHE   A 128 ? 0.2230 0.2326 0.2667 0.0080  0.0295  0.0093  134 PHE   A CZ  
984  N N   . ALA   A 129 ? 0.1977 0.2220 0.2548 0.0005  0.0113  0.0063  135 ALA   A N   
985  C CA  . ALA   A 129 ? 0.1889 0.2190 0.2496 -0.0043 0.0074  0.0068  135 ALA   A CA  
986  C C   . ALA   A 129 ? 0.2022 0.2344 0.2577 -0.0137 0.0057  0.0030  135 ALA   A C   
987  O O   . ALA   A 129 ? 0.1919 0.2174 0.2441 -0.0132 0.0077  -0.0041 135 ALA   A O   
988  C CB  . ALA   A 129 ? 0.1917 0.2122 0.2486 0.0001  0.0061  0.0013  135 ALA   A CB  
989  N N   . ASP   A 130 ? 0.1979 0.2362 0.2521 -0.0235 0.0024  0.0089  136 ASP   A N   
990  C CA  . ASP   A 130 ? 0.2227 0.2548 0.2623 -0.0357 0.0030  0.0054  136 ASP   A CA  
991  C C   . ASP   A 130 ? 0.2296 0.2527 0.2637 -0.0375 0.0083  -0.0020 136 ASP   A C   
992  O O   . ASP   A 130 ? 0.2283 0.2543 0.2683 -0.0344 0.0063  -0.0003 136 ASP   A O   
993  C CB  . ASP   A 130 ? 0.2528 0.2881 0.2864 -0.0493 -0.0054 0.0160  136 ASP   A CB  
994  C CG  . ASP   A 130 ? 0.3141 0.3345 0.3215 -0.0657 -0.0049 0.0128  136 ASP   A CG  
995  O OD1 . ASP   A 130 ? 0.3019 0.3158 0.3030 -0.0657 0.0009  0.0064  136 ASP   A OD1 
996  O OD2 . ASP   A 130 ? 0.3717 0.3832 0.3618 -0.0793 -0.0091 0.0160  136 ASP   A OD2 
997  N N   . VAL   A 131 ? 0.2235 0.2345 0.2486 -0.0425 0.0170  -0.0096 137 VAL   A N   
998  C CA  . VAL   A 131 ? 0.2340 0.2338 0.2578 -0.0447 0.0265  -0.0153 137 VAL   A CA  
999  C C   . VAL   A 131 ? 0.2714 0.2513 0.2683 -0.0604 0.0363  -0.0190 137 VAL   A C   
1000 O O   . VAL   A 131 ? 0.2978 0.2627 0.2908 -0.0636 0.0497  -0.0242 137 VAL   A O   
1001 C CB  . VAL   A 131 ? 0.2283 0.2268 0.2741 -0.0343 0.0324  -0.0199 137 VAL   A CB  
1002 C CG1 . VAL   A 131 ? 0.2244 0.2332 0.2853 -0.0228 0.0215  -0.0165 137 VAL   A CG1 
1003 C CG2 . VAL   A 131 ? 0.2252 0.2177 0.2717 -0.0352 0.0392  -0.0234 137 VAL   A CG2 
1004 N N   . ARG   A 132 ? 0.2700 0.2459 0.2472 -0.0712 0.0310  -0.0159 138 ARG   A N   
1005 C CA  . ARG   A 132 ? 0.2991 0.2486 0.2420 -0.0887 0.0399  -0.0199 138 ARG   A CA  
1006 C C   . ARG   A 132 ? 0.3512 0.2834 0.2663 -0.1034 0.0404  -0.0183 138 ARG   A C   
1007 O O   . ARG   A 132 ? 0.3890 0.2899 0.2717 -0.1171 0.0551  -0.0248 138 ARG   A O   
1008 C CB  . ARG   A 132 ? 0.3187 0.2676 0.2464 -0.0987 0.0292  -0.0145 138 ARG   A CB  
1009 C CG  . ARG   A 132 ? 0.3156 0.2776 0.2659 -0.0858 0.0308  -0.0167 138 ARG   A CG  
1010 C CD  . ARG   A 132 ? 0.3069 0.2702 0.2457 -0.0956 0.0193  -0.0096 138 ARG   A CD  
1011 N NE  . ARG   A 132 ? 0.3035 0.2897 0.2611 -0.0921 0.0020  0.0038  138 ARG   A NE  
1012 C CZ  . ARG   A 132 ? 0.3278 0.3220 0.2896 -0.0976 -0.0101 0.0145  138 ARG   A CZ  
1013 N NH1 . ARG   A 132 ? 0.3214 0.3018 0.2633 -0.1090 -0.0100 0.0129  138 ARG   A NH1 
1014 N NH2 . ARG   A 132 ? 0.3330 0.3480 0.3213 -0.0917 -0.0212 0.0279  138 ARG   A NH2 
1015 N N   . ASP   A 133 ? 0.3480 0.2969 0.2739 -0.1011 0.0262  -0.0097 139 ASP   A N   
1016 C CA  . ASP   A 133 ? 0.3680 0.3017 0.2689 -0.1153 0.0243  -0.0067 139 ASP   A CA  
1017 C C   . ASP   A 133 ? 0.3808 0.3050 0.2874 -0.1088 0.0421  -0.0151 139 ASP   A C   
1018 O O   . ASP   A 133 ? 0.4027 0.3068 0.2823 -0.1218 0.0462  -0.0150 139 ASP   A O   
1019 C CB  . ASP   A 133 ? 0.3873 0.3429 0.3022 -0.1162 0.0022  0.0080  139 ASP   A CB  
1020 C CG  . ASP   A 133 ? 0.3856 0.3678 0.3414 -0.0946 0.0011  0.0089  139 ASP   A CG  
1021 O OD1 . ASP   A 133 ? 0.3387 0.3309 0.3160 -0.0792 0.0071  0.0032  139 ASP   A OD1 
1022 O OD2 . ASP   A 133 ? 0.3760 0.3656 0.3391 -0.0946 -0.0058 0.0152  139 ASP   A OD2 
1023 N N   . LEU   A 134 ? 0.3547 0.2917 0.2965 -0.0901 0.0514  -0.0206 140 LEU   A N   
1024 C CA  . LEU   A 134 ? 0.3501 0.2825 0.3086 -0.0826 0.0656  -0.0251 140 LEU   A CA  
1025 C C   . LEU   A 134 ? 0.3820 0.2832 0.3251 -0.0898 0.0919  -0.0337 140 LEU   A C   
1026 O O   . LEU   A 134 ? 0.3824 0.2840 0.3530 -0.0796 0.1050  -0.0374 140 LEU   A O   
1027 C CB  . LEU   A 134 ? 0.3191 0.2752 0.3219 -0.0628 0.0609  -0.0242 140 LEU   A CB  
1028 C CG  . LEU   A 134 ? 0.3047 0.2853 0.3202 -0.0549 0.0401  -0.0170 140 LEU   A CG  
1029 C CD1 . LEU   A 134 ? 0.2751 0.2684 0.3220 -0.0392 0.0362  -0.0171 140 LEU   A CD1 
1030 C CD2 . LEU   A 134 ? 0.3159 0.2999 0.3244 -0.0595 0.0326  -0.0115 140 LEU   A CD2 
1031 N N   . LEU   A 135 ? 0.4170 0.2874 0.3141 -0.1090 0.1001  -0.0357 141 LEU   A N   
1032 C CA  . LEU   A 135 ? 0.4619 0.2929 0.3338 -0.1187 0.1294  -0.0448 141 LEU   A CA  
1033 C C   . LEU   A 135 ? 0.4623 0.2866 0.3674 -0.1073 0.1554  -0.0487 141 LEU   A C   
1034 O O   . LEU   A 135 ? 0.4830 0.2848 0.3933 -0.1067 0.1824  -0.0547 141 LEU   A O   
1035 C CB  . LEU   A 135 ? 0.5071 0.2989 0.3127 -0.1451 0.1318  -0.0458 141 LEU   A CB  
1036 C CG  . LEU   A 135 ? 0.5343 0.3309 0.3092 -0.1603 0.1026  -0.0375 141 LEU   A CG  
1037 C CD1 . LEU   A 135 ? 0.5887 0.3374 0.2922 -0.1906 0.1048  -0.0376 141 LEU   A CD1 
1038 C CD2 . LEU   A 135 ? 0.5306 0.3361 0.3138 -0.1569 0.0979  -0.0385 141 LEU   A CD2 
1039 N N   . TRP   A 136 ? 0.4462 0.2906 0.3795 -0.0975 0.1476  -0.0440 142 TRP   A N   
1040 C CA  . TRP   A 136 ? 0.4443 0.2849 0.4154 -0.0870 0.1692  -0.0445 142 TRP   A CA  
1041 C C   . TRP   A 136 ? 0.4394 0.2991 0.4684 -0.0698 0.1724  -0.0420 142 TRP   A C   
1042 O O   . TRP   A 136 ? 0.4334 0.2850 0.4986 -0.0630 0.1942  -0.0407 142 TRP   A O   
1043 C CB  . TRP   A 136 ? 0.4306 0.2875 0.4144 -0.0827 0.1568  -0.0392 142 TRP   A CB  
1044 C CG  . TRP   A 136 ? 0.4024 0.2976 0.4054 -0.0731 0.1236  -0.0325 142 TRP   A CG  
1045 C CD1 . TRP   A 136 ? 0.4078 0.3136 0.3850 -0.0801 0.1011  -0.0286 142 TRP   A CD1 
1046 C CD2 . TRP   A 136 ? 0.3688 0.2922 0.4210 -0.0558 0.1112  -0.0279 142 TRP   A CD2 
1047 N NE1 . TRP   A 136 ? 0.3860 0.3236 0.3937 -0.0666 0.0798  -0.0231 142 TRP   A NE1 
1048 C CE2 . TRP   A 136 ? 0.3675 0.3139 0.4160 -0.0527 0.0849  -0.0234 142 TRP   A CE2 
1049 C CE3 . TRP   A 136 ? 0.3570 0.2856 0.4566 -0.0441 0.1194  -0.0254 142 TRP   A CE3 
1050 C CZ2 . TRP   A 136 ? 0.3498 0.3185 0.4302 -0.0394 0.0687  -0.0191 142 TRP   A CZ2 
1051 C CZ3 . TRP   A 136 ? 0.3458 0.2991 0.4782 -0.0325 0.0980  -0.0193 142 TRP   A CZ3 
1052 C CH2 . TRP   A 136 ? 0.3390 0.3093 0.4569 -0.0306 0.0741  -0.0174 142 TRP   A CH2 
1053 N N   . LEU   A 137 ? 0.4317 0.3146 0.4710 -0.0637 0.1515  -0.0399 143 LEU   A N   
1054 C CA  . LEU   A 137 ? 0.4171 0.3158 0.5066 -0.0501 0.1508  -0.0360 143 LEU   A CA  
1055 C C   . LEU   A 137 ? 0.4749 0.3482 0.5793 -0.0512 0.1833  -0.0391 143 LEU   A C   
1056 O O   . LEU   A 137 ? 0.4488 0.3313 0.6073 -0.0404 0.1885  -0.0325 143 LEU   A O   
1057 C CB  . LEU   A 137 ? 0.3920 0.3113 0.4772 -0.0467 0.1267  -0.0347 143 LEU   A CB  
1058 C CG  . LEU   A 137 ? 0.3702 0.3151 0.4559 -0.0413 0.0981  -0.0298 143 LEU   A CG  
1059 C CD1 . LEU   A 137 ? 0.3599 0.3188 0.4392 -0.0386 0.0810  -0.0288 143 LEU   A CD1 
1060 C CD2 . LEU   A 137 ? 0.3541 0.3130 0.4823 -0.0299 0.0902  -0.0232 143 LEU   A CD2 
1061 N N   . ASP   A 138 ? 0.5464 0.3850 0.6025 -0.0657 0.2049  -0.0478 144 ASP   A N   
1062 C CA  . ASP   A 138 ? 0.6134 0.4191 0.6739 -0.0689 0.2416  -0.0525 144 ASP   A CA  
1063 C C   . ASP   A 138 ? 0.6806 0.4587 0.7543 -0.0696 0.2764  -0.0529 144 ASP   A C   
1064 O O   . ASP   A 138 ? 0.7012 0.4570 0.8005 -0.0671 0.3097  -0.0535 144 ASP   A O   
1065 C CB  . ASP   A 138 ? 0.6745 0.4487 0.6692 -0.0865 0.2492  -0.0620 144 ASP   A CB  
1066 C CG  . ASP   A 138 ? 0.7304 0.5283 0.7257 -0.0837 0.2242  -0.0606 144 ASP   A CG  
1067 O OD1 . ASP   A 138 ? 0.7289 0.5493 0.7758 -0.0696 0.2204  -0.0555 144 ASP   A OD1 
1068 O OD2 . ASP   A 138 ? 0.7740 0.5677 0.7200 -0.0964 0.2073  -0.0630 144 ASP   A OD2 
1069 N N   . GLU   A 139 ? 0.7148 0.4914 0.7719 -0.0733 0.2722  -0.0523 145 GLU   A N   
1070 C CA  . GLU   A 139 ? 0.7540 0.5023 0.8229 -0.0742 0.3074  -0.0525 145 GLU   A CA  
1071 C C   . GLU   A 139 ? 0.7457 0.5249 0.8704 -0.0606 0.2944  -0.0418 145 GLU   A C   
1072 O O   . GLU   A 139 ? 0.7649 0.5248 0.8936 -0.0622 0.3173  -0.0412 145 GLU   A O   
1073 C CB  . GLU   A 139 ? 0.8373 0.5407 0.8259 -0.0952 0.3232  -0.0623 145 GLU   A CB  
1074 C CG  . GLU   A 139 ? 0.9144 0.6369 0.8618 -0.1035 0.2848  -0.0611 145 GLU   A CG  
1075 C CD  . GLU   A 139 ? 1.0382 0.7371 0.9099 -0.1246 0.2736  -0.0672 145 GLU   A CD  
1076 O OE1 . GLU   A 139 ? 1.0634 0.7718 0.9014 -0.1342 0.2457  -0.0640 145 GLU   A OE1 
1077 O OE2 . GLU   A 139 ? 1.0872 0.7575 0.9353 -0.1323 0.2920  -0.0737 145 GLU   A OE2 
1078 N N1  . A1B4J B .   ? 0.4638 0.2378 0.3368 0.0291  0.1039  -0.0077 201 A1B4J A N1  
1079 C C4  . A1B4J B .   ? 0.5432 0.2276 0.3364 0.0291  0.1590  -0.0104 201 A1B4J A C4  
1080 C C5  . A1B4J B .   ? 0.5126 0.2365 0.3292 0.0257  0.1271  -0.0107 201 A1B4J A C5  
1081 C C6  . A1B4J B .   ? 0.5240 0.2449 0.3363 0.0231  0.1170  -0.0131 201 A1B4J A C6  
1082 C C7  . A1B4J B .   ? 0.4784 0.2485 0.3499 0.0313  0.1155  -0.0060 201 A1B4J A C7  
1083 C C8  . A1B4J B .   ? 0.4925 0.2263 0.3164 0.0197  0.0932  -0.0151 201 A1B4J A C8  
1084 C C10 . A1B4J B .   ? 0.4456 0.2526 0.3352 0.0208  0.0597  -0.0108 201 A1B4J A C10 
1085 C C13 . A1B4J B .   ? 0.4267 0.2443 0.3502 0.0344  0.0994  -0.0009 201 A1B4J A C13 
1086 O O1  . A1B4J B .   ? 0.3752 0.2547 0.3623 0.0358  0.0772  0.0068  201 A1B4J A O1  
1087 C C12 . A1B4J B .   ? 0.3798 0.2616 0.3545 0.0315  0.0658  0.0025  201 A1B4J A C12 
1088 N N2  . A1B4J B .   ? 0.3441 0.2589 0.3405 0.0284  0.0501  0.0037  201 A1B4J A N2  
1089 C C11 . A1B4J B .   ? 0.4107 0.2531 0.3418 0.0284  0.0707  -0.0038 201 A1B4J A C11 
1090 C C9  . A1B4J B .   ? 0.4798 0.2410 0.3180 0.0138  0.0616  -0.0157 201 A1B4J A C9  
1091 O O   . A1B4J B .   ? 0.4460 0.2490 0.3604 0.0380  0.1227  0.0020  201 A1B4J A O   
1092 C C1  . A1B4J B .   ? 0.4786 0.2396 0.3197 0.0245  0.1080  -0.0088 201 A1B4J A C1  
1093 S S   . A1B4J B .   ? 0.4473 0.2496 0.3154 0.0202  0.0749  -0.0096 201 A1B4J A S   
1094 C C   . A1B4J B .   ? 0.4317 0.2622 0.3175 0.0180  0.0608  -0.0085 201 A1B4J A C   
1095 C C3  . A1B4J B .   ? 0.5327 0.2189 0.3301 0.0314  0.1687  -0.0077 201 A1B4J A C3  
1096 C C2  . A1B4J B .   ? 0.5067 0.2335 0.3293 0.0298  0.1450  -0.0060 201 A1B4J A C2  
1097 N N   . A1B4J B .   ? 0.4700 0.2323 0.3129 0.0261  0.1157  -0.0069 201 A1B4J A N   
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