data_7I4C
# 
_entry.id   7I4C 
# 
_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   7I4C         pdb_00007i4c 10.2210/pdb7i4c/pdb 
WWPDB D_1001408299 ?            ?                   
# 
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                        7I4C 
_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)phenyl]methyl}-6-oxopiperidine-3-carboxamide' 278.370   1   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                                65.409    1   ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                      78.133    2   ?         ? ? ? 
5 water       nat water                                                                     18.015    178 ?         ? ? ? 
# 
_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)phenyl]methyl}-6-oxopiperidine-3-carboxamide' A1B2Q 
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 
A1B2Q non-polymer         . '(3S)-1-{[2-(methylsulfanyl)phenyl]methyl}-6-oxopiperidine-3-carboxamide' ? 'C14 H18 N2 O2 S' 278.370 
ALA   'L-peptide linking' y ALANINE                                                                   ? 'C3 H7 N O2'      89.093  
ARG   'L-peptide linking' y ARGININE                                                                  ? 'C6 H15 N4 O2 1'  175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                ? 'C4 H8 N2 O3'     132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                           ? 'C4 H7 N O4'      133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                  ? 'C3 H7 N O2 S'    121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                      ? 'C2 H6 O S'       78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                                 ? 'C5 H10 N2 O3'    146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                           ? 'C5 H9 N O4'      147.129 
GLY   'peptide linking'   y GLYCINE                                                                   ? 'C2 H5 N O2'      75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                 ? 'C6 H10 N3 O2 1'  156.162 
HOH   non-polymer         . WATER                                                                     ? 'H2 O'            18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                ? 'C6 H13 N O2'     131.173 
LEU   'L-peptide linking' y LEUCINE                                                                   ? 'C6 H13 N O2'     131.173 
LYS   'L-peptide linking' y LYSINE                                                                    ? 'C6 H15 N2 O2 1'  147.195 
MET   'L-peptide linking' y METHIONINE                                                                ? 'C5 H11 N O2 S'   149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                             ? 'C9 H11 N O2'     165.189 
PRO   'L-peptide linking' y PROLINE                                                                   ? 'C5 H9 N O2'      115.130 
SER   'L-peptide linking' y SERINE                                                                    ? 'C3 H7 N O3'      105.093 
THR   'L-peptide linking' y THREONINE                                                                 ? 'C4 H9 N O3'      119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                ? 'C11 H12 N2 O2'   204.225 
TYR   'L-peptide linking' y TYROSINE                                                                  ? 'C9 H11 N O3'     181.189 
VAL   'L-peptide linking' y VALINE                                                                    ? 'C5 H11 N O2'     117.146 
ZN    non-polymer         . 'ZINC ION'                                                                ? 'Zn 2'            65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   7   7   SER SER A . n 
A 1 2   GLY 2   8   8   GLY GLY A . n 
A 1 3   ALA 3   9   9   ALA ALA A . n 
A 1 4   ILE 4   10  10  ILE ILE A . n 
A 1 5   TYR 5   11  11  TYR TYR A . n 
A 1 6   VAL 6   12  12  VAL VAL A . n 
A 1 7   GLY 7   13  13  GLY GLY A . n 
A 1 8   ASN 8   14  14  ASN ASN A . n 
A 1 9   TYR 9   15  15  TYR TYR A . n 
A 1 10  ARG 10  16  16  ARG ARG A . n 
A 1 11  VAL 11  17  17  VAL VAL A . n 
A 1 12  VAL 12  18  18  VAL VAL A . n 
A 1 13  ASN 13  19  19  ASN ASN A . n 
A 1 14  ARG 14  20  20  ARG ARG A . n 
A 1 15  HIS 15  21  21  HIS HIS A . n 
A 1 16  LEU 16  22  22  LEU LEU A . n 
A 1 17  ALA 17  23  23  ALA ALA A . n 
A 1 18  THR 18  24  24  THR THR A . n 
A 1 19  HIS 19  25  25  HIS HIS A . n 
A 1 20  ASN 20  26  26  ASN ASN A . n 
A 1 21  ASP 21  27  27  ASP ASP A . n 
A 1 22  TRP 22  28  28  TRP TRP A . n 
A 1 23  ALA 23  29  29  ALA ALA A . n 
A 1 24  ASN 24  30  30  ASN ASN A . n 
A 1 25  LEU 25  31  31  LEU LEU A . n 
A 1 26  VAL 26  32  32  VAL VAL A . n 
A 1 27  TRP 27  33  33  TRP TRP A . n 
A 1 28  GLU 28  34  34  GLU GLU A . n 
A 1 29  ASP 29  35  35  ASP ASP A . n 
A 1 30  SER 30  36  36  SER SER A . n 
A 1 31  SER 31  37  37  SER SER A . n 
A 1 32  ARG 32  38  38  ARG ARG A . n 
A 1 33  ASP 33  39  39  ASP ASP A . n 
A 1 34  LEU 34  40  40  LEU LEU A . n 
A 1 35  LEU 35  41  41  LEU LEU A . n 
A 1 36  VAL 36  42  42  VAL VAL A . n 
A 1 37  SER 37  43  43  SER SER A . n 
A 1 38  SER 38  44  44  SER SER A . n 
A 1 39  THR 39  45  45  THR THR A . n 
A 1 40  THR 40  46  46  THR THR A . n 
A 1 41  ALA 41  47  47  ALA ALA A . n 
A 1 42  GLN 42  48  48  GLN GLN A . n 
A 1 43  GLY 43  49  49  GLY GLY A . n 
A 1 44  CYS 44  50  50  CYS CYS A . n 
A 1 45  ASP 45  51  51  ASP ASP A . n 
A 1 46  THR 46  52  52  THR THR A . n 
A 1 47  ILE 47  53  53  ILE ILE A . n 
A 1 48  ALA 48  54  54  ALA ALA A . n 
A 1 49  ARG 49  55  55  ARG ARG A . n 
A 1 50  CYS 50  56  56  CYS CYS A . n 
A 1 51  ASP 51  57  57  ASP ASP A . n 
A 1 52  CYS 52  58  58  CYS CYS A . n 
A 1 53  GLN 53  59  59  GLN GLN A . n 
A 1 54  THR 54  60  60  THR THR A . n 
A 1 55  GLY 55  61  61  GLY GLY A . n 
A 1 56  VAL 56  62  62  VAL VAL A . n 
A 1 57  TYR 57  63  63  TYR TYR A . n 
A 1 58  TYR 58  64  64  TYR TYR A . n 
A 1 59  CYS 59  65  65  CYS CYS A . n 
A 1 60  SER 60  66  66  SER SER A . n 
A 1 61  SER 61  67  67  SER SER A . n 
A 1 62  ARG 62  68  68  ARG ARG A . n 
A 1 63  ARG 63  69  69  ARG ARG A . n 
A 1 64  LYS 64  70  70  LYS LYS A . n 
A 1 65  HIS 65  71  71  HIS HIS A . n 
A 1 66  TYR 66  72  72  TYR TYR A . n 
A 1 67  PRO 67  73  73  PRO PRO A . n 
A 1 68  VAL 68  74  74  VAL VAL A . n 
A 1 69  SER 69  75  75  SER SER A . n 
A 1 70  PHE 70  76  76  PHE PHE A . n 
A 1 71  SER 71  77  77  SER SER A . n 
A 1 72  LYS 72  78  78  LYS LYS A . n 
A 1 73  PRO 73  79  79  PRO PRO A . n 
A 1 74  SER 74  80  80  SER SER A . n 
A 1 75  LEU 75  81  81  LEU LEU A . n 
A 1 76  ILE 76  82  82  ILE ILE A . n 
A 1 77  PHE 77  83  83  PHE PHE A . n 
A 1 78  VAL 78  84  84  VAL VAL A . n 
A 1 79  GLU 79  85  85  GLU GLU A . n 
A 1 80  ALA 80  86  86  ALA ALA A . n 
A 1 81  SER 81  87  87  SER SER A . n 
A 1 82  GLU 82  88  88  GLU GLU A . n 
A 1 83  TYR 83  89  89  TYR TYR A . n 
A 1 84  TYR 84  90  90  TYR TYR A . n 
A 1 85  PRO 85  91  91  PRO PRO A . n 
A 1 86  ALA 86  92  92  ALA ALA A . n 
A 1 87  ARG 87  93  93  ARG ARG A . n 
A 1 88  TYR 88  94  94  TYR TYR A . n 
A 1 89  GLN 89  95  95  GLN GLN A . n 
A 1 90  SER 90  96  96  SER SER A . n 
A 1 91  HIS 91  97  97  HIS HIS A . n 
A 1 92  LEU 92  98  98  LEU LEU A . n 
A 1 93  MET 93  99  99  MET MET A . n 
A 1 94  LEU 94  100 100 LEU LEU A . n 
A 1 95  ALA 95  101 101 ALA ALA A . n 
A 1 96  VAL 96  102 102 VAL VAL A . n 
A 1 97  GLY 97  103 103 GLY GLY A . n 
A 1 98  HIS 98  104 104 HIS HIS A . n 
A 1 99  SER 99  105 105 SER SER A . n 
A 1 100 GLU 100 106 106 GLU GLU A . n 
A 1 101 PRO 101 107 107 PRO PRO A . n 
A 1 102 GLY 102 108 108 GLY GLY A . n 
A 1 103 ASP 103 109 109 ASP ASP A . n 
A 1 104 CYS 104 110 110 CYS CYS A . n 
A 1 105 GLY 105 111 111 GLY GLY A . n 
A 1 106 GLY 106 112 112 GLY GLY A . n 
A 1 107 ILE 107 113 113 ILE ILE A . n 
A 1 108 LEU 108 114 114 LEU LEU A . n 
A 1 109 ARG 109 115 115 ARG ARG A . n 
A 1 110 CYS 110 116 116 CYS CYS A . n 
A 1 111 GLN 111 117 117 GLN GLN A . n 
A 1 112 HIS 112 118 118 HIS HIS A . n 
A 1 113 GLY 113 119 119 GLY GLY A . n 
A 1 114 VAL 114 120 120 VAL VAL A . n 
A 1 115 VAL 115 121 121 VAL VAL A . n 
A 1 116 GLY 116 122 122 GLY GLY A . n 
A 1 117 ILE 117 123 123 ILE ILE A . n 
A 1 118 VAL 118 124 124 VAL VAL A . n 
A 1 119 SER 119 125 125 SER SER A . n 
A 1 120 THR 120 126 126 THR THR A . n 
A 1 121 GLY 121 127 127 GLY GLY A . n 
A 1 122 GLY 122 128 128 GLY GLY A . n 
A 1 123 ASN 123 129 129 ASN ASN A . n 
A 1 124 GLY 124 130 130 GLY GLY A . n 
A 1 125 LEU 125 131 131 LEU LEU A . n 
A 1 126 VAL 126 132 132 VAL VAL A . n 
A 1 127 GLY 127 133 133 GLY GLY A . n 
A 1 128 PHE 128 134 134 PHE PHE A . n 
A 1 129 ALA 129 135 135 ALA ALA A . n 
A 1 130 ASP 130 136 136 ASP ASP A . n 
A 1 131 VAL 131 137 137 VAL VAL A . n 
A 1 132 ARG 132 138 138 ARG ARG A . n 
A 1 133 ASP 133 139 139 ASP ASP A . n 
A 1 134 LEU 134 140 140 LEU LEU A . n 
A 1 135 LEU 135 141 141 LEU LEU A . n 
A 1 136 TRP 136 142 142 TRP TRP A . n 
A 1 137 LEU 137 143 143 LEU LEU A . n 
A 1 138 ASP 138 144 144 ASP ASP A . n 
A 1 139 GLU 139 145 145 GLU GLU A . n 
A 1 140 GLU 140 146 146 GLU GLU A . n 
A 1 141 ALA 141 147 ?   ?   ?   A . n 
A 1 142 MET 142 148 ?   ?   ?   A . n 
A 1 143 GLU 143 149 ?   ?   ?   A . n 
A 1 144 GLN 144 150 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1B2Q 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1B2Q 
_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 A1B2Q 1   201 201 A1B2Q LIG A . 
C 3 ZN    1   202 1   ZN    ZN  A . 
D 4 DMS   1   203 0   DMS   DMS A . 
E 4 DMS   1   204 1   DMS   DMS A . 
F 5 HOH   1   301 137 HOH   HOH A . 
F 5 HOH   2   302 217 HOH   HOH A . 
F 5 HOH   3   303 75  HOH   HOH A . 
F 5 HOH   4   304 229 HOH   HOH A . 
F 5 HOH   5   305 161 HOH   HOH A . 
F 5 HOH   6   306 152 HOH   HOH A . 
F 5 HOH   7   307 169 HOH   HOH A . 
F 5 HOH   8   308 36  HOH   HOH A . 
F 5 HOH   9   309 37  HOH   HOH A . 
F 5 HOH   10  310 133 HOH   HOH A . 
F 5 HOH   11  311 104 HOH   HOH A . 
F 5 HOH   12  312 216 HOH   HOH A . 
F 5 HOH   13  313 77  HOH   HOH A . 
F 5 HOH   14  314 30  HOH   HOH A . 
F 5 HOH   15  315 55  HOH   HOH A . 
F 5 HOH   16  316 41  HOH   HOH A . 
F 5 HOH   17  317 67  HOH   HOH A . 
F 5 HOH   18  318 43  HOH   HOH A . 
F 5 HOH   19  319 46  HOH   HOH A . 
F 5 HOH   20  320 258 HOH   HOH A . 
F 5 HOH   21  321 140 HOH   HOH A . 
F 5 HOH   22  322 108 HOH   HOH A . 
F 5 HOH   23  323 34  HOH   HOH A . 
F 5 HOH   24  324 19  HOH   HOH A . 
F 5 HOH   25  325 264 HOH   HOH A . 
F 5 HOH   26  326 4   HOH   HOH A . 
F 5 HOH   27  327 68  HOH   HOH A . 
F 5 HOH   28  328 147 HOH   HOH A . 
F 5 HOH   29  329 59  HOH   HOH A . 
F 5 HOH   30  330 167 HOH   HOH A . 
F 5 HOH   31  331 13  HOH   HOH A . 
F 5 HOH   32  332 57  HOH   HOH A . 
F 5 HOH   33  333 257 HOH   HOH A . 
F 5 HOH   34  334 211 HOH   HOH A . 
F 5 HOH   35  335 253 HOH   HOH A . 
F 5 HOH   36  336 121 HOH   HOH A . 
F 5 HOH   37  337 270 HOH   HOH A . 
F 5 HOH   38  338 268 HOH   HOH A . 
F 5 HOH   39  339 33  HOH   HOH A . 
F 5 HOH   40  340 272 HOH   HOH A . 
F 5 HOH   41  341 25  HOH   HOH A . 
F 5 HOH   42  342 248 HOH   HOH A . 
F 5 HOH   43  343 35  HOH   HOH A . 
F 5 HOH   44  344 2   HOH   HOH A . 
F 5 HOH   45  345 259 HOH   HOH A . 
F 5 HOH   46  346 254 HOH   HOH A . 
F 5 HOH   47  347 24  HOH   HOH A . 
F 5 HOH   48  348 255 HOH   HOH A . 
F 5 HOH   49  349 150 HOH   HOH A . 
F 5 HOH   50  350 146 HOH   HOH A . 
F 5 HOH   51  351 42  HOH   HOH A . 
F 5 HOH   52  352 267 HOH   HOH A . 
F 5 HOH   53  353 9   HOH   HOH A . 
F 5 HOH   54  354 28  HOH   HOH A . 
F 5 HOH   55  355 60  HOH   HOH A . 
F 5 HOH   56  356 252 HOH   HOH A . 
F 5 HOH   57  357 205 HOH   HOH A . 
F 5 HOH   58  358 111 HOH   HOH A . 
F 5 HOH   59  359 21  HOH   HOH A . 
F 5 HOH   60  360 93  HOH   HOH A . 
F 5 HOH   61  361 110 HOH   HOH A . 
F 5 HOH   62  362 26  HOH   HOH A . 
F 5 HOH   63  363 135 HOH   HOH A . 
F 5 HOH   64  364 263 HOH   HOH A . 
F 5 HOH   65  365 148 HOH   HOH A . 
F 5 HOH   66  366 29  HOH   HOH A . 
F 5 HOH   67  367 174 HOH   HOH A . 
F 5 HOH   68  368 124 HOH   HOH A . 
F 5 HOH   69  369 106 HOH   HOH A . 
F 5 HOH   70  370 62  HOH   HOH A . 
F 5 HOH   71  371 215 HOH   HOH A . 
F 5 HOH   72  372 116 HOH   HOH A . 
F 5 HOH   73  373 7   HOH   HOH A . 
F 5 HOH   74  374 50  HOH   HOH A . 
F 5 HOH   75  375 191 HOH   HOH A . 
F 5 HOH   76  376 214 HOH   HOH A . 
F 5 HOH   77  377 265 HOH   HOH A . 
F 5 HOH   78  378 105 HOH   HOH A . 
F 5 HOH   79  379 74  HOH   HOH A . 
F 5 HOH   80  380 12  HOH   HOH A . 
F 5 HOH   81  381 126 HOH   HOH A . 
F 5 HOH   82  382 82  HOH   HOH A . 
F 5 HOH   83  383 16  HOH   HOH A . 
F 5 HOH   84  384 18  HOH   HOH A . 
F 5 HOH   85  385 260 HOH   HOH A . 
F 5 HOH   86  386 84  HOH   HOH A . 
F 5 HOH   87  387 177 HOH   HOH A . 
F 5 HOH   88  388 182 HOH   HOH A . 
F 5 HOH   89  389 176 HOH   HOH A . 
F 5 HOH   90  390 15  HOH   HOH A . 
F 5 HOH   91  391 144 HOH   HOH A . 
F 5 HOH   92  392 70  HOH   HOH A . 
F 5 HOH   93  393 103 HOH   HOH A . 
F 5 HOH   94  394 95  HOH   HOH A . 
F 5 HOH   95  395 11  HOH   HOH A . 
F 5 HOH   96  396 20  HOH   HOH A . 
F 5 HOH   97  397 156 HOH   HOH A . 
F 5 HOH   98  398 168 HOH   HOH A . 
F 5 HOH   99  399 262 HOH   HOH A . 
F 5 HOH   100 400 89  HOH   HOH A . 
F 5 HOH   101 401 181 HOH   HOH A . 
F 5 HOH   102 402 27  HOH   HOH A . 
F 5 HOH   103 403 40  HOH   HOH A . 
F 5 HOH   104 404 79  HOH   HOH A . 
F 5 HOH   105 405 51  HOH   HOH A . 
F 5 HOH   106 406 131 HOH   HOH A . 
F 5 HOH   107 407 3   HOH   HOH A . 
F 5 HOH   108 408 185 HOH   HOH A . 
F 5 HOH   109 409 39  HOH   HOH A . 
F 5 HOH   110 410 38  HOH   HOH A . 
F 5 HOH   111 411 80  HOH   HOH A . 
F 5 HOH   112 412 132 HOH   HOH A . 
F 5 HOH   113 413 192 HOH   HOH A . 
F 5 HOH   114 414 58  HOH   HOH A . 
F 5 HOH   115 415 47  HOH   HOH A . 
F 5 HOH   116 416 23  HOH   HOH A . 
F 5 HOH   117 417 231 HOH   HOH A . 
F 5 HOH   118 418 85  HOH   HOH A . 
F 5 HOH   119 419 10  HOH   HOH A . 
F 5 HOH   120 420 204 HOH   HOH A . 
F 5 HOH   121 421 203 HOH   HOH A . 
F 5 HOH   122 422 8   HOH   HOH A . 
F 5 HOH   123 423 218 HOH   HOH A . 
F 5 HOH   124 424 76  HOH   HOH A . 
F 5 HOH   125 425 186 HOH   HOH A . 
F 5 HOH   126 426 91  HOH   HOH A . 
F 5 HOH   127 427 69  HOH   HOH A . 
F 5 HOH   128 428 123 HOH   HOH A . 
F 5 HOH   129 429 159 HOH   HOH A . 
F 5 HOH   130 430 100 HOH   HOH A . 
F 5 HOH   131 431 96  HOH   HOH A . 
F 5 HOH   132 432 175 HOH   HOH A . 
F 5 HOH   133 433 155 HOH   HOH A . 
F 5 HOH   134 434 233 HOH   HOH A . 
F 5 HOH   135 435 138 HOH   HOH A . 
F 5 HOH   136 436 158 HOH   HOH A . 
F 5 HOH   137 437 90  HOH   HOH A . 
F 5 HOH   138 438 261 HOH   HOH A . 
F 5 HOH   139 439 171 HOH   HOH A . 
F 5 HOH   140 440 160 HOH   HOH A . 
F 5 HOH   141 441 207 HOH   HOH A . 
F 5 HOH   142 442 98  HOH   HOH A . 
F 5 HOH   143 443 240 HOH   HOH A . 
F 5 HOH   144 444 251 HOH   HOH A . 
F 5 HOH   145 445 48  HOH   HOH A . 
F 5 HOH   146 446 246 HOH   HOH A . 
F 5 HOH   147 447 65  HOH   HOH A . 
F 5 HOH   148 448 14  HOH   HOH A . 
F 5 HOH   149 449 269 HOH   HOH A . 
F 5 HOH   150 450 134 HOH   HOH A . 
F 5 HOH   151 451 99  HOH   HOH A . 
F 5 HOH   152 452 213 HOH   HOH A . 
F 5 HOH   153 453 114 HOH   HOH A . 
F 5 HOH   154 454 127 HOH   HOH A . 
F 5 HOH   155 455 209 HOH   HOH A . 
F 5 HOH   156 456 88  HOH   HOH A . 
F 5 HOH   157 457 129 HOH   HOH A . 
F 5 HOH   158 458 221 HOH   HOH A . 
F 5 HOH   159 459 256 HOH   HOH A . 
F 5 HOH   160 460 271 HOH   HOH A . 
F 5 HOH   161 461 86  HOH   HOH A . 
F 5 HOH   162 462 266 HOH   HOH A . 
F 5 HOH   163 463 56  HOH   HOH A . 
F 5 HOH   164 464 190 HOH   HOH A . 
F 5 HOH   165 465 153 HOH   HOH A . 
F 5 HOH   166 466 118 HOH   HOH A . 
F 5 HOH   167 467 61  HOH   HOH A . 
F 5 HOH   168 468 170 HOH   HOH A . 
F 5 HOH   169 469 243 HOH   HOH A . 
F 5 HOH   170 470 202 HOH   HOH A . 
F 5 HOH   171 471 52  HOH   HOH A . 
F 5 HOH   172 472 92  HOH   HOH A . 
F 5 HOH   173 473 208 HOH   HOH A . 
F 5 HOH   174 474 226 HOH   HOH A . 
F 5 HOH   175 475 222 HOH   HOH A . 
F 5 HOH   176 476 83  HOH   HOH A . 
F 5 HOH   177 477 230 HOH   HOH A . 
F 5 HOH   178 478 244 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           7I4C 
_cell.length_a           89.270 
_cell.length_b           58.180 
_cell.length_c           32.923 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.89 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I4C 
_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          7I4C 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.69 
_exptl_crystal.density_percent_sol   54.27 
_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   2025-01-17 
_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   0.92201 
_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        0.92201 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7I4C 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             48.75 
_reflns.d_resolution_high            1.56 
_reflns.number_obs                   24222 
_reflns.percent_possible_obs         99.6 
_reflns.pdbx_Rmerge_I_obs            0.176 
_reflns.pdbx_netI_over_sigmaI        4.0 
_reflns.pdbx_redundancy              6.7 
_reflns.pdbx_Rrim_I_all              0.191 
_reflns.pdbx_Rpim_I_all              0.073 
_reflns.pdbx_CC_half                 0.991 
_reflns.pdbx_number_measured_all     162601 
_reflns.pdbx_chi_squared             0.30 
_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                  1.56 
_reflns_shell.d_res_low                   1.58 
_reflns_shell.number_measured_all         6343 
_reflns_shell.number_unique_obs           1141 
_reflns_shell.Rmerge_I_obs                2.126 
_reflns_shell.pdbx_chi_squared            0.03 
_reflns_shell.pdbx_redundancy             5.6 
_reflns_shell.percent_possible_obs        92.9 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.2 
_reflns_shell.pdbx_Rrim_I_all             2.350 
_reflns_shell.pdbx_Rpim_I_all             0.987 
_reflns_shell.pdbx_CC_half                0.191 
_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                                 7I4C 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     20597 
_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                             22.32 
_refine.ls_d_res_high                            1.557 
_refine.ls_percent_reflns_obs                    85.2 
_refine.ls_R_factor_obs                          0.2022 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2010 
_refine.ls_R_factor_R_free                       0.2259 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.040 
_refine.ls_number_reflns_R_free                  1039 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.951 
_refine.correlation_coeff_Fo_to_Fc_free          0.941 
_refine.B_iso_mean                               29.71 
_refine.aniso_B[1][1]                            -8.40450 
_refine.aniso_B[2][2]                            6.11890 
_refine.aniso_B[3][3]                            2.28550 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -2.20900 
_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             0.096 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.093 
_refine.pdbx_overall_SU_R_Blow_DPI               0.103 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.098 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7I4C 
_refine_analyze.Luzzati_coordinate_error_obs    0.24 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1083 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         28 
_refine_hist.number_atoms_solvent             178 
_refine_hist.number_atoms_total               1289 
_refine_hist.d_res_high                       1.557 
_refine_hist.d_res_low                        22.32 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
t_bond_d                  0.010 ? 2.00  1155 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               0.91  ? 2.00  1573 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  387  '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  210  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1155 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           3.41  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           15.48 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  141  '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  911  '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                       1.56 
_refine_ls_shell.d_res_low                        1.63 
_refine_ls_shell.number_reflns_R_work             397 
_refine_ls_shell.R_factor_R_work                  0.3869 
_refine_ls_shell.percent_reflns_obs               13.65 
_refine_ls_shell.R_factor_R_free                  0.3573 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            3.64 
_refine_ls_shell.number_reflns_R_free             15 
_refine_ls_shell.number_reflns_all                412 
_refine_ls_shell.R_factor_all                     0.3858 
# 
_struct.entry_id                  7I4C 
_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-0036629-001 (A71EV2A-x4694)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I4C 
_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 4 ? 
F 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              7I4C 
_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,F 
# 
_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 GLU A 100 ? CYS A 104 ? GLU A 106 CYS A 110 5 ? 5 
HELX_P HELX_P5 AA5 LEU A 134 ? GLU A 139 ? LEU A 140 GLU A 145 5 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 50  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 56  A ZN 202 1_555 ? ? ? ? ? ? ? 2.338 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.408 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.454 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 C ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.105 ? ? 
# 
_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_555 108.0 ? 
2 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 104.7 ? 
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_555 118.2 ? 
4 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 111.9 ? 
5 SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 99.3  ? 
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_555 114.7 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
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 
AA1 3 4 ? 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 ILE A 4   ? VAL A 6   ? ILE A 10  VAL A 12  
AA1 2 TYR A 9   ? ASN A 13  ? TYR A 15  ASN A 19  
AA1 3 LEU A 34  ? SER A 38  ? LEU A 40  SER A 44  
AA1 4 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
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 ILE A 4   ? N ILE A 10  O VAL A 11  ? O VAL A 17  
AA1 2 3 N ARG A 10  ? N ARG A 16  O SER A 37  ? O SER A 43  
AA1 3 4 O VAL A 36  ? O VAL A 42  N TRP A 27  ? N TRP A 33  
AA2 1 2 O LYS A 64  ? O LYS A 70  N CYS A 59  ? N CYS A 65  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N LEU A 108 ? N LEU A 114 O VAL A 115 ? O VAL A 121 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O PHE A 128 ? O PHE A 134 N MET A 93  ? N MET A 99  
AA2 6 7 O GLN A 89  ? O GLN A 95  N ILE A 76  ? N ILE A 82  
# 
_pdbx_entry_details.entry_id                   7I4C 
_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_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    SER 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     125 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -133.19 
_pdbx_validate_torsion.psi             -31.05 
# 
_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         15.7817 
_pdbx_refine_tls.origin_y         7.6575 
_pdbx_refine_tls.origin_z         13.4454 
_pdbx_refine_tls.T[1][1]          -0.1290 
_pdbx_refine_tls.T[2][2]          0.0793 
_pdbx_refine_tls.T[3][3]          -0.0017 
_pdbx_refine_tls.T[1][2]          -0.0071 
_pdbx_refine_tls.T[1][3]          -0.0252 
_pdbx_refine_tls.T[2][3]          -0.0003 
_pdbx_refine_tls.L[1][1]          0.8468 
_pdbx_refine_tls.L[2][2]          1.1491 
_pdbx_refine_tls.L[3][3]          0.4560 
_pdbx_refine_tls.L[1][2]          0.3055 
_pdbx_refine_tls.L[1][3]          -0.0224 
_pdbx_refine_tls.L[2][3]          -0.2265 
_pdbx_refine_tls.S[1][1]          -0.0540 
_pdbx_refine_tls.S[1][2]          0.0423 
_pdbx_refine_tls.S[1][3]          0.0388 
_pdbx_refine_tls.S[2][1]          -0.0023 
_pdbx_refine_tls.S[2][2]          0.0454 
_pdbx_refine_tls.S[2][3]          -0.0579 
_pdbx_refine_tls.S[3][1]          0.0295 
_pdbx_refine_tls.S[3][2]          -0.0288 
_pdbx_refine_tls.S[3][3]          0.0086 
# 
_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|* }' 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       478 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   7.12 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A ALA 147 ? A ALA 141 
2 1 Y 1 A MET 148 ? A MET 142 
3 1 Y 1 A GLU 149 ? A GLU 143 
4 1 Y 1 A GLN 150 ? A GLN 144 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1B2Q N1   N  N N 1   
A1B2Q C4   C  Y N 2   
A1B2Q C5   C  Y N 3   
A1B2Q C6   C  Y N 4   
A1B2Q C7   C  N N 5   
A1B2Q C8   C  N N 6   
A1B2Q C10  C  N N 7   
A1B2Q C13  C  N N 8   
A1B2Q O1   O  N N 9   
A1B2Q C12  C  N N 10  
A1B2Q C11  C  N N 11  
A1B2Q C9   C  N R 12  
A1B2Q O    O  N N 13  
A1B2Q N    N  N N 14  
A1B2Q C1   C  Y N 15  
A1B2Q S    S  N N 16  
A1B2Q C    C  N N 17  
A1B2Q C3   C  Y N 18  
A1B2Q C2   C  Y N 19  
A1B2Q H13  H  N N 20  
A1B2Q H12  H  N N 21  
A1B2Q H6   H  N N 22  
A1B2Q H7   H  N N 23  
A1B2Q H9   H  N N 24  
A1B2Q H8   H  N N 25  
A1B2Q H11  H  N N 26  
A1B2Q H10  H  N N 27  
A1B2Q H17  H  N N 28  
A1B2Q H16  H  N N 29  
A1B2Q H15  H  N N 30  
A1B2Q H14  H  N N 31  
A1B2Q H    H  N N 32  
A1B2Q H3   H  N N 33  
A1B2Q H2   H  N N 34  
A1B2Q H1   H  N N 35  
A1B2Q H5   H  N N 36  
A1B2Q H4   H  N N 37  
ALA   N    N  N N 38  
ALA   CA   C  N S 39  
ALA   C    C  N N 40  
ALA   O    O  N N 41  
ALA   CB   C  N N 42  
ALA   OXT  O  N N 43  
ALA   H    H  N N 44  
ALA   H2   H  N N 45  
ALA   HA   H  N N 46  
ALA   HB1  H  N N 47  
ALA   HB2  H  N N 48  
ALA   HB3  H  N N 49  
ALA   HXT  H  N N 50  
ARG   N    N  N N 51  
ARG   CA   C  N S 52  
ARG   C    C  N N 53  
ARG   O    O  N N 54  
ARG   CB   C  N N 55  
ARG   CG   C  N N 56  
ARG   CD   C  N N 57  
ARG   NE   N  N N 58  
ARG   CZ   C  N N 59  
ARG   NH1  N  N N 60  
ARG   NH2  N  N N 61  
ARG   OXT  O  N N 62  
ARG   H    H  N N 63  
ARG   H2   H  N N 64  
ARG   HA   H  N N 65  
ARG   HB2  H  N N 66  
ARG   HB3  H  N N 67  
ARG   HG2  H  N N 68  
ARG   HG3  H  N N 69  
ARG   HD2  H  N N 70  
ARG   HD3  H  N N 71  
ARG   HE   H  N N 72  
ARG   HH11 H  N N 73  
ARG   HH12 H  N N 74  
ARG   HH21 H  N N 75  
ARG   HH22 H  N N 76  
ARG   HXT  H  N N 77  
ASN   N    N  N N 78  
ASN   CA   C  N S 79  
ASN   C    C  N N 80  
ASN   O    O  N N 81  
ASN   CB   C  N N 82  
ASN   CG   C  N N 83  
ASN   OD1  O  N N 84  
ASN   ND2  N  N N 85  
ASN   OXT  O  N N 86  
ASN   H    H  N N 87  
ASN   H2   H  N N 88  
ASN   HA   H  N N 89  
ASN   HB2  H  N N 90  
ASN   HB3  H  N N 91  
ASN   HD21 H  N N 92  
ASN   HD22 H  N N 93  
ASN   HXT  H  N N 94  
ASP   N    N  N N 95  
ASP   CA   C  N S 96  
ASP   C    C  N N 97  
ASP   O    O  N N 98  
ASP   CB   C  N N 99  
ASP   CG   C  N N 100 
ASP   OD1  O  N N 101 
ASP   OD2  O  N N 102 
ASP   OXT  O  N N 103 
ASP   H    H  N N 104 
ASP   H2   H  N N 105 
ASP   HA   H  N N 106 
ASP   HB2  H  N N 107 
ASP   HB3  H  N N 108 
ASP   HD2  H  N N 109 
ASP   HXT  H  N N 110 
CYS   N    N  N N 111 
CYS   CA   C  N R 112 
CYS   C    C  N N 113 
CYS   O    O  N N 114 
CYS   CB   C  N N 115 
CYS   SG   S  N N 116 
CYS   OXT  O  N N 117 
CYS   H    H  N N 118 
CYS   H2   H  N N 119 
CYS   HA   H  N N 120 
CYS   HB2  H  N N 121 
CYS   HB3  H  N N 122 
CYS   HG   H  N N 123 
CYS   HXT  H  N N 124 
DMS   S    S  N N 125 
DMS   O    O  N N 126 
DMS   C1   C  N N 127 
DMS   C2   C  N N 128 
DMS   H11  H  N N 129 
DMS   H12  H  N N 130 
DMS   H13  H  N N 131 
DMS   H21  H  N N 132 
DMS   H22  H  N N 133 
DMS   H23  H  N N 134 
GLN   N    N  N N 135 
GLN   CA   C  N S 136 
GLN   C    C  N N 137 
GLN   O    O  N N 138 
GLN   CB   C  N N 139 
GLN   CG   C  N N 140 
GLN   CD   C  N N 141 
GLN   OE1  O  N N 142 
GLN   NE2  N  N N 143 
GLN   OXT  O  N N 144 
GLN   H    H  N N 145 
GLN   H2   H  N N 146 
GLN   HA   H  N N 147 
GLN   HB2  H  N N 148 
GLN   HB3  H  N N 149 
GLN   HG2  H  N N 150 
GLN   HG3  H  N N 151 
GLN   HE21 H  N N 152 
GLN   HE22 H  N N 153 
GLN   HXT  H  N N 154 
GLU   N    N  N N 155 
GLU   CA   C  N S 156 
GLU   C    C  N N 157 
GLU   O    O  N N 158 
GLU   CB   C  N N 159 
GLU   CG   C  N N 160 
GLU   CD   C  N N 161 
GLU   OE1  O  N N 162 
GLU   OE2  O  N N 163 
GLU   OXT  O  N N 164 
GLU   H    H  N N 165 
GLU   H2   H  N N 166 
GLU   HA   H  N N 167 
GLU   HB2  H  N N 168 
GLU   HB3  H  N N 169 
GLU   HG2  H  N N 170 
GLU   HG3  H  N N 171 
GLU   HE2  H  N N 172 
GLU   HXT  H  N N 173 
GLY   N    N  N N 174 
GLY   CA   C  N N 175 
GLY   C    C  N N 176 
GLY   O    O  N N 177 
GLY   OXT  O  N N 178 
GLY   H    H  N N 179 
GLY   H2   H  N N 180 
GLY   HA2  H  N N 181 
GLY   HA3  H  N N 182 
GLY   HXT  H  N N 183 
HIS   N    N  N N 184 
HIS   CA   C  N S 185 
HIS   C    C  N N 186 
HIS   O    O  N N 187 
HIS   CB   C  N N 188 
HIS   CG   C  Y N 189 
HIS   ND1  N  Y N 190 
HIS   CD2  C  Y N 191 
HIS   CE1  C  Y N 192 
HIS   NE2  N  Y N 193 
HIS   OXT  O  N N 194 
HIS   H    H  N N 195 
HIS   H2   H  N N 196 
HIS   HA   H  N N 197 
HIS   HB2  H  N N 198 
HIS   HB3  H  N N 199 
HIS   HD1  H  N N 200 
HIS   HD2  H  N N 201 
HIS   HE1  H  N N 202 
HIS   HE2  H  N N 203 
HIS   HXT  H  N N 204 
HOH   O    O  N N 205 
HOH   H1   H  N N 206 
HOH   H2   H  N N 207 
ILE   N    N  N N 208 
ILE   CA   C  N S 209 
ILE   C    C  N N 210 
ILE   O    O  N N 211 
ILE   CB   C  N S 212 
ILE   CG1  C  N N 213 
ILE   CG2  C  N N 214 
ILE   CD1  C  N N 215 
ILE   OXT  O  N N 216 
ILE   H    H  N N 217 
ILE   H2   H  N N 218 
ILE   HA   H  N N 219 
ILE   HB   H  N N 220 
ILE   HG12 H  N N 221 
ILE   HG13 H  N N 222 
ILE   HG21 H  N N 223 
ILE   HG22 H  N N 224 
ILE   HG23 H  N N 225 
ILE   HD11 H  N N 226 
ILE   HD12 H  N N 227 
ILE   HD13 H  N N 228 
ILE   HXT  H  N N 229 
LEU   N    N  N N 230 
LEU   CA   C  N S 231 
LEU   C    C  N N 232 
LEU   O    O  N N 233 
LEU   CB   C  N N 234 
LEU   CG   C  N N 235 
LEU   CD1  C  N N 236 
LEU   CD2  C  N N 237 
LEU   OXT  O  N N 238 
LEU   H    H  N N 239 
LEU   H2   H  N N 240 
LEU   HA   H  N N 241 
LEU   HB2  H  N N 242 
LEU   HB3  H  N N 243 
LEU   HG   H  N N 244 
LEU   HD11 H  N N 245 
LEU   HD12 H  N N 246 
LEU   HD13 H  N N 247 
LEU   HD21 H  N N 248 
LEU   HD22 H  N N 249 
LEU   HD23 H  N N 250 
LEU   HXT  H  N N 251 
LYS   N    N  N N 252 
LYS   CA   C  N S 253 
LYS   C    C  N N 254 
LYS   O    O  N N 255 
LYS   CB   C  N N 256 
LYS   CG   C  N N 257 
LYS   CD   C  N N 258 
LYS   CE   C  N N 259 
LYS   NZ   N  N N 260 
LYS   OXT  O  N N 261 
LYS   H    H  N N 262 
LYS   H2   H  N N 263 
LYS   HA   H  N N 264 
LYS   HB2  H  N N 265 
LYS   HB3  H  N N 266 
LYS   HG2  H  N N 267 
LYS   HG3  H  N N 268 
LYS   HD2  H  N N 269 
LYS   HD3  H  N N 270 
LYS   HE2  H  N N 271 
LYS   HE3  H  N N 272 
LYS   HZ1  H  N N 273 
LYS   HZ2  H  N N 274 
LYS   HZ3  H  N N 275 
LYS   HXT  H  N N 276 
MET   N    N  N N 277 
MET   CA   C  N S 278 
MET   C    C  N N 279 
MET   O    O  N N 280 
MET   CB   C  N N 281 
MET   CG   C  N N 282 
MET   SD   S  N N 283 
MET   CE   C  N N 284 
MET   OXT  O  N N 285 
MET   H    H  N N 286 
MET   H2   H  N N 287 
MET   HA   H  N N 288 
MET   HB2  H  N N 289 
MET   HB3  H  N N 290 
MET   HG2  H  N N 291 
MET   HG3  H  N N 292 
MET   HE1  H  N N 293 
MET   HE2  H  N N 294 
MET   HE3  H  N N 295 
MET   HXT  H  N N 296 
PHE   N    N  N N 297 
PHE   CA   C  N S 298 
PHE   C    C  N N 299 
PHE   O    O  N N 300 
PHE   CB   C  N N 301 
PHE   CG   C  Y N 302 
PHE   CD1  C  Y N 303 
PHE   CD2  C  Y N 304 
PHE   CE1  C  Y N 305 
PHE   CE2  C  Y N 306 
PHE   CZ   C  Y N 307 
PHE   OXT  O  N N 308 
PHE   H    H  N N 309 
PHE   H2   H  N N 310 
PHE   HA   H  N N 311 
PHE   HB2  H  N N 312 
PHE   HB3  H  N N 313 
PHE   HD1  H  N N 314 
PHE   HD2  H  N N 315 
PHE   HE1  H  N N 316 
PHE   HE2  H  N N 317 
PHE   HZ   H  N N 318 
PHE   HXT  H  N N 319 
PRO   N    N  N N 320 
PRO   CA   C  N S 321 
PRO   C    C  N N 322 
PRO   O    O  N N 323 
PRO   CB   C  N N 324 
PRO   CG   C  N N 325 
PRO   CD   C  N N 326 
PRO   OXT  O  N N 327 
PRO   H    H  N N 328 
PRO   HA   H  N N 329 
PRO   HB2  H  N N 330 
PRO   HB3  H  N N 331 
PRO   HG2  H  N N 332 
PRO   HG3  H  N N 333 
PRO   HD2  H  N N 334 
PRO   HD3  H  N N 335 
PRO   HXT  H  N N 336 
SER   N    N  N N 337 
SER   CA   C  N S 338 
SER   C    C  N N 339 
SER   O    O  N N 340 
SER   CB   C  N N 341 
SER   OG   O  N N 342 
SER   OXT  O  N N 343 
SER   H    H  N N 344 
SER   H2   H  N N 345 
SER   HA   H  N N 346 
SER   HB2  H  N N 347 
SER   HB3  H  N N 348 
SER   HG   H  N N 349 
SER   HXT  H  N N 350 
THR   N    N  N N 351 
THR   CA   C  N S 352 
THR   C    C  N N 353 
THR   O    O  N N 354 
THR   CB   C  N R 355 
THR   OG1  O  N N 356 
THR   CG2  C  N N 357 
THR   OXT  O  N N 358 
THR   H    H  N N 359 
THR   H2   H  N N 360 
THR   HA   H  N N 361 
THR   HB   H  N N 362 
THR   HG1  H  N N 363 
THR   HG21 H  N N 364 
THR   HG22 H  N N 365 
THR   HG23 H  N N 366 
THR   HXT  H  N N 367 
TRP   N    N  N N 368 
TRP   CA   C  N S 369 
TRP   C    C  N N 370 
TRP   O    O  N N 371 
TRP   CB   C  N N 372 
TRP   CG   C  Y N 373 
TRP   CD1  C  Y N 374 
TRP   CD2  C  Y N 375 
TRP   NE1  N  Y N 376 
TRP   CE2  C  Y N 377 
TRP   CE3  C  Y N 378 
TRP   CZ2  C  Y N 379 
TRP   CZ3  C  Y N 380 
TRP   CH2  C  Y N 381 
TRP   OXT  O  N N 382 
TRP   H    H  N N 383 
TRP   H2   H  N N 384 
TRP   HA   H  N N 385 
TRP   HB2  H  N N 386 
TRP   HB3  H  N N 387 
TRP   HD1  H  N N 388 
TRP   HE1  H  N N 389 
TRP   HE3  H  N N 390 
TRP   HZ2  H  N N 391 
TRP   HZ3  H  N N 392 
TRP   HH2  H  N N 393 
TRP   HXT  H  N N 394 
TYR   N    N  N N 395 
TYR   CA   C  N S 396 
TYR   C    C  N N 397 
TYR   O    O  N N 398 
TYR   CB   C  N N 399 
TYR   CG   C  Y N 400 
TYR   CD1  C  Y N 401 
TYR   CD2  C  Y N 402 
TYR   CE1  C  Y N 403 
TYR   CE2  C  Y N 404 
TYR   CZ   C  Y N 405 
TYR   OH   O  N N 406 
TYR   OXT  O  N N 407 
TYR   H    H  N N 408 
TYR   H2   H  N N 409 
TYR   HA   H  N N 410 
TYR   HB2  H  N N 411 
TYR   HB3  H  N N 412 
TYR   HD1  H  N N 413 
TYR   HD2  H  N N 414 
TYR   HE1  H  N N 415 
TYR   HE2  H  N N 416 
TYR   HH   H  N N 417 
TYR   HXT  H  N N 418 
VAL   N    N  N N 419 
VAL   CA   C  N S 420 
VAL   C    C  N N 421 
VAL   O    O  N N 422 
VAL   CB   C  N N 423 
VAL   CG1  C  N N 424 
VAL   CG2  C  N N 425 
VAL   OXT  O  N N 426 
VAL   H    H  N N 427 
VAL   H2   H  N N 428 
VAL   HA   H  N N 429 
VAL   HB   H  N N 430 
VAL   HG11 H  N N 431 
VAL   HG12 H  N N 432 
VAL   HG13 H  N N 433 
VAL   HG21 H  N N 434 
VAL   HG22 H  N N 435 
VAL   HG23 H  N N 436 
VAL   HXT  H  N N 437 
ZN    ZN   ZN N N 438 
# 
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 
A1B2Q C   S    sing N N 1   
A1B2Q S   C1   sing N N 2   
A1B2Q C1  C2   doub Y N 3   
A1B2Q C2  C3   sing Y N 4   
A1B2Q C3  C4   doub Y N 5   
A1B2Q C4  C5   sing Y N 6   
A1B2Q C5  C6   doub Y N 7   
A1B2Q C1  C6   sing Y N 8   
A1B2Q C6  C7   sing N N 9   
A1B2Q C7  N    sing N N 10  
A1B2Q N   C8   sing N N 11  
A1B2Q C8  C9   sing N N 12  
A1B2Q C10 C9   sing N N 13  
A1B2Q N1  C10  sing N N 14  
A1B2Q O   C10  doub N N 15  
A1B2Q C9  C11  sing N N 16  
A1B2Q C11 C12  sing N N 17  
A1B2Q C12 C13  sing N N 18  
A1B2Q N   C13  sing N N 19  
A1B2Q C13 O1   doub N N 20  
A1B2Q N1  H13  sing N N 21  
A1B2Q N1  H12  sing N N 22  
A1B2Q C4  H6   sing N N 23  
A1B2Q C5  H7   sing N N 24  
A1B2Q C7  H9   sing N N 25  
A1B2Q C7  H8   sing N N 26  
A1B2Q C8  H11  sing N N 27  
A1B2Q C8  H10  sing N N 28  
A1B2Q C12 H17  sing N N 29  
A1B2Q C12 H16  sing N N 30  
A1B2Q C11 H15  sing N N 31  
A1B2Q C11 H14  sing N N 32  
A1B2Q C9  H    sing N N 33  
A1B2Q C   H3   sing N N 34  
A1B2Q C   H2   sing N N 35  
A1B2Q C   H1   sing N N 36  
A1B2Q C3  H5   sing N N 37  
A1B2Q C2  H4   sing N N 38  
ALA   N   CA   sing N N 39  
ALA   N   H    sing N N 40  
ALA   N   H2   sing N N 41  
ALA   CA  C    sing N N 42  
ALA   CA  CB   sing N N 43  
ALA   CA  HA   sing N N 44  
ALA   C   O    doub N N 45  
ALA   C   OXT  sing N N 46  
ALA   CB  HB1  sing N N 47  
ALA   CB  HB2  sing N N 48  
ALA   CB  HB3  sing N N 49  
ALA   OXT HXT  sing N N 50  
ARG   N   CA   sing N N 51  
ARG   N   H    sing N N 52  
ARG   N   H2   sing N N 53  
ARG   CA  C    sing N N 54  
ARG   CA  CB   sing N N 55  
ARG   CA  HA   sing N N 56  
ARG   C   O    doub N N 57  
ARG   C   OXT  sing N N 58  
ARG   CB  CG   sing N N 59  
ARG   CB  HB2  sing N N 60  
ARG   CB  HB3  sing N N 61  
ARG   CG  CD   sing N N 62  
ARG   CG  HG2  sing N N 63  
ARG   CG  HG3  sing N N 64  
ARG   CD  NE   sing N N 65  
ARG   CD  HD2  sing N N 66  
ARG   CD  HD3  sing N N 67  
ARG   NE  CZ   sing N N 68  
ARG   NE  HE   sing N N 69  
ARG   CZ  NH1  sing N N 70  
ARG   CZ  NH2  doub N N 71  
ARG   NH1 HH11 sing N N 72  
ARG   NH1 HH12 sing N N 73  
ARG   NH2 HH21 sing N N 74  
ARG   NH2 HH22 sing N N 75  
ARG   OXT HXT  sing N N 76  
ASN   N   CA   sing N N 77  
ASN   N   H    sing N N 78  
ASN   N   H2   sing N N 79  
ASN   CA  C    sing N N 80  
ASN   CA  CB   sing N N 81  
ASN   CA  HA   sing N N 82  
ASN   C   O    doub N N 83  
ASN   C   OXT  sing N N 84  
ASN   CB  CG   sing N N 85  
ASN   CB  HB2  sing N N 86  
ASN   CB  HB3  sing N N 87  
ASN   CG  OD1  doub N N 88  
ASN   CG  ND2  sing N N 89  
ASN   ND2 HD21 sing N N 90  
ASN   ND2 HD22 sing N N 91  
ASN   OXT HXT  sing N N 92  
ASP   N   CA   sing N N 93  
ASP   N   H    sing N N 94  
ASP   N   H2   sing N N 95  
ASP   CA  C    sing N N 96  
ASP   CA  CB   sing N N 97  
ASP   CA  HA   sing N N 98  
ASP   C   O    doub N N 99  
ASP   C   OXT  sing N N 100 
ASP   CB  CG   sing N N 101 
ASP   CB  HB2  sing N N 102 
ASP   CB  HB3  sing N N 103 
ASP   CG  OD1  doub N N 104 
ASP   CG  OD2  sing N N 105 
ASP   OD2 HD2  sing N N 106 
ASP   OXT HXT  sing N N 107 
CYS   N   CA   sing N N 108 
CYS   N   H    sing N N 109 
CYS   N   H2   sing N N 110 
CYS   CA  C    sing N N 111 
CYS   CA  CB   sing N N 112 
CYS   CA  HA   sing N N 113 
CYS   C   O    doub N N 114 
CYS   C   OXT  sing N N 115 
CYS   CB  SG   sing N N 116 
CYS   CB  HB2  sing N N 117 
CYS   CB  HB3  sing N N 118 
CYS   SG  HG   sing N N 119 
CYS   OXT HXT  sing N N 120 
DMS   S   O    doub N N 121 
DMS   S   C1   sing N N 122 
DMS   S   C2   sing N N 123 
DMS   C1  H11  sing N N 124 
DMS   C1  H12  sing N N 125 
DMS   C1  H13  sing N N 126 
DMS   C2  H21  sing N N 127 
DMS   C2  H22  sing N N 128 
DMS   C2  H23  sing N N 129 
GLN   N   CA   sing N N 130 
GLN   N   H    sing N N 131 
GLN   N   H2   sing N N 132 
GLN   CA  C    sing N N 133 
GLN   CA  CB   sing N N 134 
GLN   CA  HA   sing N N 135 
GLN   C   O    doub N N 136 
GLN   C   OXT  sing N N 137 
GLN   CB  CG   sing N N 138 
GLN   CB  HB2  sing N N 139 
GLN   CB  HB3  sing N N 140 
GLN   CG  CD   sing N N 141 
GLN   CG  HG2  sing N N 142 
GLN   CG  HG3  sing N N 143 
GLN   CD  OE1  doub N N 144 
GLN   CD  NE2  sing N N 145 
GLN   NE2 HE21 sing N N 146 
GLN   NE2 HE22 sing N N 147 
GLN   OXT HXT  sing N N 148 
GLU   N   CA   sing N N 149 
GLU   N   H    sing N N 150 
GLU   N   H2   sing N N 151 
GLU   CA  C    sing N N 152 
GLU   CA  CB   sing N N 153 
GLU   CA  HA   sing N N 154 
GLU   C   O    doub N N 155 
GLU   C   OXT  sing N N 156 
GLU   CB  CG   sing N N 157 
GLU   CB  HB2  sing N N 158 
GLU   CB  HB3  sing N N 159 
GLU   CG  CD   sing N N 160 
GLU   CG  HG2  sing N N 161 
GLU   CG  HG3  sing N N 162 
GLU   CD  OE1  doub N N 163 
GLU   CD  OE2  sing N N 164 
GLU   OE2 HE2  sing N N 165 
GLU   OXT HXT  sing N N 166 
GLY   N   CA   sing N N 167 
GLY   N   H    sing N N 168 
GLY   N   H2   sing N N 169 
GLY   CA  C    sing N N 170 
GLY   CA  HA2  sing N N 171 
GLY   CA  HA3  sing N N 172 
GLY   C   O    doub N N 173 
GLY   C   OXT  sing N N 174 
GLY   OXT HXT  sing N N 175 
HIS   N   CA   sing N N 176 
HIS   N   H    sing N N 177 
HIS   N   H2   sing N N 178 
HIS   CA  C    sing N N 179 
HIS   CA  CB   sing N N 180 
HIS   CA  HA   sing N N 181 
HIS   C   O    doub N N 182 
HIS   C   OXT  sing N N 183 
HIS   CB  CG   sing N N 184 
HIS   CB  HB2  sing N N 185 
HIS   CB  HB3  sing N N 186 
HIS   CG  ND1  sing Y N 187 
HIS   CG  CD2  doub Y N 188 
HIS   ND1 CE1  doub Y N 189 
HIS   ND1 HD1  sing N N 190 
HIS   CD2 NE2  sing Y N 191 
HIS   CD2 HD2  sing N N 192 
HIS   CE1 NE2  sing Y N 193 
HIS   CE1 HE1  sing N N 194 
HIS   NE2 HE2  sing N N 195 
HIS   OXT HXT  sing N N 196 
HOH   O   H1   sing N N 197 
HOH   O   H2   sing N N 198 
ILE   N   CA   sing N N 199 
ILE   N   H    sing N N 200 
ILE   N   H2   sing N N 201 
ILE   CA  C    sing N N 202 
ILE   CA  CB   sing N N 203 
ILE   CA  HA   sing N N 204 
ILE   C   O    doub N N 205 
ILE   C   OXT  sing N N 206 
ILE   CB  CG1  sing N N 207 
ILE   CB  CG2  sing N N 208 
ILE   CB  HB   sing N N 209 
ILE   CG1 CD1  sing N N 210 
ILE   CG1 HG12 sing N N 211 
ILE   CG1 HG13 sing N N 212 
ILE   CG2 HG21 sing N N 213 
ILE   CG2 HG22 sing N N 214 
ILE   CG2 HG23 sing N N 215 
ILE   CD1 HD11 sing N N 216 
ILE   CD1 HD12 sing N N 217 
ILE   CD1 HD13 sing N N 218 
ILE   OXT HXT  sing N N 219 
LEU   N   CA   sing N N 220 
LEU   N   H    sing N N 221 
LEU   N   H2   sing N N 222 
LEU   CA  C    sing N N 223 
LEU   CA  CB   sing N N 224 
LEU   CA  HA   sing N N 225 
LEU   C   O    doub N N 226 
LEU   C   OXT  sing N N 227 
LEU   CB  CG   sing N N 228 
LEU   CB  HB2  sing N N 229 
LEU   CB  HB3  sing N N 230 
LEU   CG  CD1  sing N N 231 
LEU   CG  CD2  sing N N 232 
LEU   CG  HG   sing N N 233 
LEU   CD1 HD11 sing N N 234 
LEU   CD1 HD12 sing N N 235 
LEU   CD1 HD13 sing N N 236 
LEU   CD2 HD21 sing N N 237 
LEU   CD2 HD22 sing N N 238 
LEU   CD2 HD23 sing N N 239 
LEU   OXT HXT  sing N N 240 
LYS   N   CA   sing N N 241 
LYS   N   H    sing N N 242 
LYS   N   H2   sing N N 243 
LYS   CA  C    sing N N 244 
LYS   CA  CB   sing N N 245 
LYS   CA  HA   sing N N 246 
LYS   C   O    doub N N 247 
LYS   C   OXT  sing N N 248 
LYS   CB  CG   sing N N 249 
LYS   CB  HB2  sing N N 250 
LYS   CB  HB3  sing N N 251 
LYS   CG  CD   sing N N 252 
LYS   CG  HG2  sing N N 253 
LYS   CG  HG3  sing N N 254 
LYS   CD  CE   sing N N 255 
LYS   CD  HD2  sing N N 256 
LYS   CD  HD3  sing N N 257 
LYS   CE  NZ   sing N N 258 
LYS   CE  HE2  sing N N 259 
LYS   CE  HE3  sing N N 260 
LYS   NZ  HZ1  sing N N 261 
LYS   NZ  HZ2  sing N N 262 
LYS   NZ  HZ3  sing N N 263 
LYS   OXT HXT  sing N N 264 
MET   N   CA   sing N N 265 
MET   N   H    sing N N 266 
MET   N   H2   sing N N 267 
MET   CA  C    sing N N 268 
MET   CA  CB   sing N N 269 
MET   CA  HA   sing N N 270 
MET   C   O    doub N N 271 
MET   C   OXT  sing N N 272 
MET   CB  CG   sing N N 273 
MET   CB  HB2  sing N N 274 
MET   CB  HB3  sing N N 275 
MET   CG  SD   sing N N 276 
MET   CG  HG2  sing N N 277 
MET   CG  HG3  sing N N 278 
MET   SD  CE   sing N N 279 
MET   CE  HE1  sing N N 280 
MET   CE  HE2  sing N N 281 
MET   CE  HE3  sing N N 282 
MET   OXT HXT  sing N N 283 
PHE   N   CA   sing N N 284 
PHE   N   H    sing N N 285 
PHE   N   H2   sing N N 286 
PHE   CA  C    sing N N 287 
PHE   CA  CB   sing N N 288 
PHE   CA  HA   sing N N 289 
PHE   C   O    doub N N 290 
PHE   C   OXT  sing N N 291 
PHE   CB  CG   sing N N 292 
PHE   CB  HB2  sing N N 293 
PHE   CB  HB3  sing N N 294 
PHE   CG  CD1  doub Y N 295 
PHE   CG  CD2  sing Y N 296 
PHE   CD1 CE1  sing Y N 297 
PHE   CD1 HD1  sing N N 298 
PHE   CD2 CE2  doub Y N 299 
PHE   CD2 HD2  sing N N 300 
PHE   CE1 CZ   doub Y N 301 
PHE   CE1 HE1  sing N N 302 
PHE   CE2 CZ   sing Y N 303 
PHE   CE2 HE2  sing N N 304 
PHE   CZ  HZ   sing N N 305 
PHE   OXT HXT  sing N N 306 
PRO   N   CA   sing N N 307 
PRO   N   CD   sing N N 308 
PRO   N   H    sing N N 309 
PRO   CA  C    sing N N 310 
PRO   CA  CB   sing N N 311 
PRO   CA  HA   sing N N 312 
PRO   C   O    doub N N 313 
PRO   C   OXT  sing N N 314 
PRO   CB  CG   sing N N 315 
PRO   CB  HB2  sing N N 316 
PRO   CB  HB3  sing N N 317 
PRO   CG  CD   sing N N 318 
PRO   CG  HG2  sing N N 319 
PRO   CG  HG3  sing N N 320 
PRO   CD  HD2  sing N N 321 
PRO   CD  HD3  sing N N 322 
PRO   OXT HXT  sing N N 323 
SER   N   CA   sing N N 324 
SER   N   H    sing N N 325 
SER   N   H2   sing N N 326 
SER   CA  C    sing N N 327 
SER   CA  CB   sing N N 328 
SER   CA  HA   sing N N 329 
SER   C   O    doub N N 330 
SER   C   OXT  sing N N 331 
SER   CB  OG   sing N N 332 
SER   CB  HB2  sing N N 333 
SER   CB  HB3  sing N N 334 
SER   OG  HG   sing N N 335 
SER   OXT HXT  sing N N 336 
THR   N   CA   sing N N 337 
THR   N   H    sing N N 338 
THR   N   H2   sing N N 339 
THR   CA  C    sing N N 340 
THR   CA  CB   sing N N 341 
THR   CA  HA   sing N N 342 
THR   C   O    doub N N 343 
THR   C   OXT  sing N N 344 
THR   CB  OG1  sing N N 345 
THR   CB  CG2  sing N N 346 
THR   CB  HB   sing N N 347 
THR   OG1 HG1  sing N N 348 
THR   CG2 HG21 sing N N 349 
THR   CG2 HG22 sing N N 350 
THR   CG2 HG23 sing N N 351 
THR   OXT HXT  sing N N 352 
TRP   N   CA   sing N N 353 
TRP   N   H    sing N N 354 
TRP   N   H2   sing N N 355 
TRP   CA  C    sing N N 356 
TRP   CA  CB   sing N N 357 
TRP   CA  HA   sing N N 358 
TRP   C   O    doub N N 359 
TRP   C   OXT  sing N N 360 
TRP   CB  CG   sing N N 361 
TRP   CB  HB2  sing N N 362 
TRP   CB  HB3  sing N N 363 
TRP   CG  CD1  doub Y N 364 
TRP   CG  CD2  sing Y N 365 
TRP   CD1 NE1  sing Y N 366 
TRP   CD1 HD1  sing N N 367 
TRP   CD2 CE2  doub Y N 368 
TRP   CD2 CE3  sing Y N 369 
TRP   NE1 CE2  sing Y N 370 
TRP   NE1 HE1  sing N N 371 
TRP   CE2 CZ2  sing Y N 372 
TRP   CE3 CZ3  doub Y N 373 
TRP   CE3 HE3  sing N N 374 
TRP   CZ2 CH2  doub Y N 375 
TRP   CZ2 HZ2  sing N N 376 
TRP   CZ3 CH2  sing Y N 377 
TRP   CZ3 HZ3  sing N N 378 
TRP   CH2 HH2  sing N N 379 
TRP   OXT HXT  sing N N 380 
TYR   N   CA   sing N N 381 
TYR   N   H    sing N N 382 
TYR   N   H2   sing N N 383 
TYR   CA  C    sing N N 384 
TYR   CA  CB   sing N N 385 
TYR   CA  HA   sing N N 386 
TYR   C   O    doub N N 387 
TYR   C   OXT  sing N N 388 
TYR   CB  CG   sing N N 389 
TYR   CB  HB2  sing N N 390 
TYR   CB  HB3  sing N N 391 
TYR   CG  CD1  doub Y N 392 
TYR   CG  CD2  sing Y N 393 
TYR   CD1 CE1  sing Y N 394 
TYR   CD1 HD1  sing N N 395 
TYR   CD2 CE2  doub Y N 396 
TYR   CD2 HD2  sing N N 397 
TYR   CE1 CZ   doub Y N 398 
TYR   CE1 HE1  sing N N 399 
TYR   CE2 CZ   sing Y N 400 
TYR   CE2 HE2  sing N N 401 
TYR   CZ  OH   sing N N 402 
TYR   OH  HH   sing N N 403 
TYR   OXT HXT  sing N N 404 
VAL   N   CA   sing N N 405 
VAL   N   H    sing N N 406 
VAL   N   H2   sing N N 407 
VAL   CA  C    sing N N 408 
VAL   CA  CB   sing N N 409 
VAL   CA  HA   sing N N 410 
VAL   C   O    doub N N 411 
VAL   C   OXT  sing N N 412 
VAL   CB  CG1  sing N N 413 
VAL   CB  CG2  sing N N 414 
VAL   CB  HB   sing N N 415 
VAL   CG1 HG11 sing N N 416 
VAL   CG1 HG12 sing N N 417 
VAL   CG1 HG13 sing N N 418 
VAL   CG2 HG21 sing N N 419 
VAL   CG2 HG22 sing N N 420 
VAL   CG2 HG23 sing N N 421 
VAL   OXT HXT  sing N N 422 
# 
_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                    7I4C 
_atom_sites.fract_transf_matrix[1][1]   0.011202 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000174 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017188 
_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]   0.030378 
_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   ? 20.172 6.913   23.539 1.00 27.28  ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 21.256 7.041   22.552 1.00 28.18  ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 21.287 5.845   21.580 1.00 27.86  ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 20.636 4.814   21.828 1.00 28.52  ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 22.597 7.171   23.264 1.00 29.72  ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 22.815 5.956   23.959 1.00 32.31  ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 22.029 5.991   20.484 1.00 26.66  ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 22.150 4.945   19.476 1.00 26.19  ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 22.471 5.505   18.104 1.00 25.73  ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 22.190 6.678   17.830 1.00 25.57  ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 23.043 4.671   17.222 1.00 24.93  ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 23.404 5.111   15.869 1.00 25.17  ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 23.337 3.960   14.853 1.00 25.82  ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 23.352 2.785   15.250 1.00 26.64  ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 24.817 5.714   15.886 1.00 24.71  ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 23.297 4.298   13.539 1.00 24.69  ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 23.329 3.348   12.430 1.00 24.55  ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 24.704 3.506   11.755 1.00 25.42  ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 25.117 4.632   11.455 1.00 25.60  ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 22.190 3.628   11.399 1.00 24.50  ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 20.809 3.729   12.067 1.00 24.64  ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 22.194 2.578   10.270 1.00 24.70  ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.753 4.432   11.163 1.00 25.19  ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 25.422 2.380   11.519 1.00 25.18  ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 26.724 2.401   10.865 1.00 25.36  ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 26.623 1.658   9.530  1.00 25.43  ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 26.495 0.432   9.527  1.00 26.24  ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.815 1.778   11.772 1.00 25.52  ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 28.053 2.577   13.034 1.00 26.39  ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 28.845 3.721   13.020 1.00 27.16  ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 27.435 2.230   14.227 1.00 27.56  ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 29.038 4.482   14.167 1.00 27.52  ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 27.597 3.001   15.375 1.00 28.26  ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 28.396 4.130   15.339 1.00 28.63  ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 28.525 4.908   16.466 1.00 29.44  ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 26.584 2.398   8.408  1.00 24.89  ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 26.475 1.828   7.056  1.00 26.61  ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.576 2.423   6.157  1.00 28.26  ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.750 3.651   6.127  1.00 28.10  ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 25.059 2.027   6.454  1.00 27.43  ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.619 3.497   6.520  1.00 27.68  ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.984 1.492   5.030  1.00 27.86  ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.381 1.561   5.501  1.00 28.74  ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.507 2.001   4.677  1.00 29.04  ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.447 2.887   5.482  1.00 29.37  ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.768 2.553   6.626  1.00 29.13  ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.762 4.080   4.967  1.00 29.25  ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.576 5.027   5.732  1.00 29.49  ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.706 6.165   6.302  1.00 28.84  ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 31.156 7.308   6.381  1.00 29.12  ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.770 5.547   4.928  1.00 31.23  ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.866 4.511   4.794  1.00 36.16  ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.784 4.411   5.624  1.00 37.09  ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.778 3.703   3.754  1.00 37.07  ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.472 5.839   6.724  1.00 27.62  ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.542 6.817   7.305  1.00 27.14  ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 28.052 6.416   8.721  1.00 25.46  ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.934 5.227   9.028  1.00 24.86  ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 27.329 7.025   6.381  1.00 27.44  ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.668 7.572   5.007  1.00 28.33  ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 28.215 8.840   4.858  1.00 29.80  ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.348 6.863   3.856  1.00 29.05  ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.486 9.365   3.596  1.00 31.21  ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.598 7.382   2.591  1.00 30.31  ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 28.173 8.632   2.463  1.00 32.16  ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.422 9.141   1.204  1.00 33.53  ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.775 7.431   9.569  1.00 24.34  ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 27.229 7.298   10.935 1.00 24.24  ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.918 8.110   10.967 1.00 24.10  ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.954 9.308   10.709 1.00 24.58  ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 28.226 7.850   11.986 1.00 24.50  ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 27.646 8.045   13.411 1.00 25.03  ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 28.751 8.346   14.435 1.00 26.12  ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 28.370 9.341   15.441 1.00 27.50  ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 27.884 9.048   16.650 1.00 29.56  ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 27.676 7.783   17.002 1.00 28.26  ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 27.564 10.021  17.500 1.00 28.21  ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 24.772 7.470   11.231 1.00 23.27  ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 23.476 8.167   11.258 1.00 23.21  ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 23.016 8.270   12.721 1.00 23.36  ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 22.845 7.232   13.383 1.00 23.59  ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 22.395 7.435   10.421 1.00 23.38  ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 21.108 8.263   10.351 1.00 23.00  ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.913 7.073   9.021  1.00 23.68  ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 22.810 9.500   13.219 1.00 22.92  ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 22.370 9.712   14.607 1.00 23.54  ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 21.200 10.740  14.676 1.00 23.09  ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 20.972 11.478  13.706 1.00 23.38  ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 23.549 10.235  15.471 1.00 25.81  ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 24.703 9.242   15.517 1.00 27.21  ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 24.029 11.594  14.962 1.00 26.64  ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 20.534 10.877  15.859 1.00 21.26  ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 19.543 11.944  16.035 1.00 21.01  ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 20.333 13.281  16.002 1.00 22.44  ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 21.410 13.397  16.628 1.00 22.52  ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 18.774 11.842  17.400 1.00 20.32  ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 17.873 10.626  17.528 1.00 21.24  ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 18.328 9.545   17.896 1.00 22.56  ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 16.584 10.772  17.204 1.00 19.74  ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 19.838 14.263  15.235 1.00 22.53  ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 20.508 15.572  15.127 1.00 22.71  ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 20.776 16.216  16.507 1.00 22.65  ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 21.881 16.725  16.744 1.00 22.73  ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 19.696 16.513  14.245 1.00 23.81  ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 20.452 17.802  13.837 1.00 24.94  ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 19.442 18.766  13.253 1.00 26.21  ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 20.021 19.980  12.693 1.00 26.80  ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 20.188 21.120  13.360 1.00 28.69  ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 19.907 21.189  14.660 1.00 27.84  ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 20.638 22.199  12.737 1.00 26.26  ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 19.809 16.094  17.440 1.00 22.27  ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 19.953 16.656  18.791 1.00 22.91  ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 21.028 15.962  19.632 1.00 23.73  ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 21.461 16.549  20.607 1.00 24.78  ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 18.601 16.734  19.551 1.00 23.48  ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 18.060 15.421  20.038 1.00 24.45  ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 17.320 14.586  19.204 1.00 25.29  ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 18.074 14.884  21.287 1.00 24.97  ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 16.959 13.553  19.952 1.00 25.23  ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 17.377 13.687  21.211 1.00 25.74  ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 21.454 14.729  19.282 1.00 23.61  ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 22.489 14.032  20.051 1.00 24.81  ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 23.871 14.023  19.358 1.00 25.58  ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 24.781 13.337  19.843 1.00 25.84  ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 22.046 12.575  20.356 1.00 25.14  ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 20.683 12.418  21.082 1.00 26.50  ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 20.350 10.947  21.303 1.00 26.80  ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 20.688 13.132  22.433 1.00 26.39  ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 24.012 14.695  18.194 1.00 26.03  ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 25.271 14.685  17.442 1.00 26.85  ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 26.402 15.340  18.246 1.00 27.14  ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 26.159 16.319  18.946 1.00 26.42  ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 25.105 15.390  16.098 1.00 26.72  ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 27.621 14.781  18.160 1.00 26.94  ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 28.767 15.312  18.912 1.00 27.34  ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 29.533 16.402  18.110 1.00 28.17  ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 29.239 16.636  16.918 1.00 28.02  ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 29.730 14.140  19.283 1.00 28.46  ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 30.357 13.677  18.086 1.00 29.01  ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 29.048 12.999  20.037 1.00 28.60  ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 30.570 17.022  18.737 1.00 28.94  ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 31.426 18.002  18.080 1.00 30.88  ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 32.093 17.359  16.836 1.00 30.31  ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 32.109 17.974  15.773 1.00 30.40  ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 32.467 18.539  19.082 1.00 34.45  ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 31.955 19.698  19.892 1.00 41.50  ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 30.632 19.756  20.319 1.00 44.16  ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 32.596 20.820  20.308 1.00 43.49  ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 30.518 20.895  20.985 1.00 44.84  ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 31.668 21.576  20.993 1.00 44.87  ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 32.567 16.105  16.958 1.00 29.57  ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 33.187 15.364  15.847 1.00 30.00  ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 32.204 15.121  14.687 1.00 28.74  ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 32.600 15.233  13.525 1.00 28.95  ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 33.736 14.026  16.327 1.00 33.25  ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 34.600 13.351  15.294 1.00 40.59  ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 35.787 13.692  15.122 1.00 43.72  ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 34.032 12.384  14.575 1.00 41.79  ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 30.930 14.785  14.990 1.00 27.03  ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 29.917 14.599  13.948 1.00 25.84  ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 29.733 15.889  13.124 1.00 24.61  ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 29.637 15.819  11.903 1.00 24.37  ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 28.544 14.230  14.557 1.00 26.14  ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 28.447 12.843  15.129 1.00 28.95  ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 29.016 11.916  14.528 1.00 28.97  ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 27.785 12.681  16.182 1.00 30.42  ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 29.655 17.042  13.784 1.00 23.44  ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 29.458 18.330  13.088 1.00 24.76  ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 30.705 18.702  12.263 1.00 25.39  ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 30.582 19.264  11.170 1.00 25.49  ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 29.157 19.461  14.098 1.00 24.89  ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 27.763 19.450  14.641 1.00 25.66  ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 27.379 19.145  15.919 1.00 26.77  ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 26.558 19.729  13.912 1.00 26.01  ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 26.002 19.219  16.026 1.00 27.31  ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 25.480 19.610  14.819 1.00 27.03  ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 26.291 20.146  12.599 1.00 26.57  ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 24.154 19.860  14.442 1.00 27.81  ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.978 20.385  12.227 1.00 27.48  ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 23.926 20.224  13.136 1.00 27.93  ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 31.902 18.392  12.799 1.00 25.13  ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 33.161 18.664  12.109 1.00 25.36  ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 33.269 17.776  10.853 1.00 25.94  ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.865 18.189  9.873  1.00 26.59  ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 34.328 18.377  13.038 1.00 25.63  ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 32.705 16.549  10.895 1.00 24.76  ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 32.729 15.635  9.757  1.00 24.11  ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 31.314 15.472  9.155  1.00 22.92  ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.973 14.398  8.650  1.00 22.50  ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 33.328 14.301  10.197 1.00 25.37  ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 34.771 14.493  10.597 1.00 27.69  ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 35.650 14.596  9.744  1.00 29.51  ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 35.038 14.591  11.890 1.00 27.13  ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 30.536 16.580  9.132  1.00 21.74  ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 29.155 16.590  8.640  1.00 22.43  ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 29.072 16.267  7.149  1.00 23.83  ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.816 16.851  6.355  1.00 23.61  ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 28.528 17.991  8.882  1.00 22.67  ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 27.103 18.250  8.342  1.00 24.08  ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 26.062 17.372  9.044  1.00 25.13  ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.732 19.755  8.431  1.00 25.07  ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 28.123 15.382  6.780  1.00 23.97  ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.800 15.028  5.400  1.00 25.15  ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 26.419 15.678  5.046  1.00 26.20  ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 26.288 16.345  4.029  1.00 26.97  ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.772 13.479  5.191  1.00 25.54  ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 27.192 13.115  3.822  1.00 25.61  ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 29.168 12.866  5.365  1.00 25.21  ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 25.405 15.488  5.901  1.00 25.21  ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 24.056 16.013  5.645  1.00 24.99  ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 23.267 16.056  6.964  1.00 23.62  ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 23.440 15.168  7.807  1.00 22.90  ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 23.313 15.122  4.595  1.00 24.91  ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.827 15.344  4.471  1.00 25.83  ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 21.192 16.274  3.697  1.00 26.77  ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.797 14.652  5.196  1.00 26.19  ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.821 16.177  3.867  1.00 27.03  ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.556 15.184  4.778  1.00 26.88  ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.804 13.646  6.170  1.00 26.49  ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 18.340 14.712  5.276  1.00 27.27  ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.595 13.165  6.638  1.00 27.32  ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 18.386 13.710  6.207  1.00 27.17  ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 22.413 17.088  7.142  1.00 22.16  ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 21.568 17.187  8.332  1.00 22.69  ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 20.258 17.921  7.989  1.00 23.54  ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 20.232 18.771  7.095  1.00 23.98  ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 22.292 17.848  9.526  1.00 22.28  ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.882 19.228  9.224  1.00 26.21  ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.992 20.451  9.371  1.00 31.60  ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 22.362 21.514  8.823  1.00 34.01  ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 20.930 20.355  10.024 1.00 32.70  ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 19.192 17.623  8.729  1.00 23.21  ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.884 18.264  8.510  1.00 23.05  ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 17.211 18.354  9.865  1.00 22.08  ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 16.822 17.338  10.425 1.00 22.06  ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 17.053 17.445  7.516  1.00 25.10  ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.707 18.048  7.138  1.00 29.93  ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 15.184 18.873  7.913  1.00 30.71  ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 15.190 17.710  6.055  1.00 31.16  ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 17.080 19.576  10.402 1.00 21.29  ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 16.463 19.823  11.703 0.50 21.41  ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 16.471 19.773  11.718 0.50 21.72  ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 14.993 19.353  11.727 1.00 22.08  ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 14.507 18.872  12.763 1.00 22.39  ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 16.521 21.315  12.028 0.50 21.77  ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 16.601 21.226  12.172 0.50 23.04  ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 15.937 21.591  13.288 0.50 21.04  ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 15.761 22.076  11.410 0.50 23.75  ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 14.287 19.517  10.590 1.00 21.76  ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 12.871 19.131  10.527 1.00 22.97  ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 12.658 17.607  10.553 1.00 23.05  ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 11.538 17.172  10.767 1.00 24.25  ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 12.170 19.788  9.339  1.00 25.65  ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 12.388 19.086  8.127  1.00 29.91  ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 13.720 16.813  10.391 1.00 22.07  ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 13.673 15.342  10.457 1.00 21.74  ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 14.347 14.780  11.731 1.00 22.07  ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 14.261 13.569  11.968 1.00 21.83  ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 14.391 14.735  9.225  1.00 22.46  ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 13.637 14.921  7.915  1.00 23.64  ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 14.379 14.309  6.729  1.00 24.04  ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 14.364 12.842  6.766  1.00 24.19  ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 14.400 12.064  5.686  1.00 25.85  ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 14.459 12.604  4.469  1.00 25.05  ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 14.376 10.741  5.811  1.00 23.44  ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 15.077 15.638  12.497 1.00 21.82  ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 15.858 15.270  13.674 1.00 21.68  ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 16.927 14.233  13.271 1.00 22.01  ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 17.229 13.339  14.062 1.00 21.21  ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 14.963 14.790  14.864 1.00 22.36  ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 15.735 14.465  16.155 1.00 22.67  ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 16.611 15.270  16.544 1.00 24.04  ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 15.484 13.375  16.753 1.00 21.72  ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 17.531 14.378  12.032 1.00 22.30  ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 18.587 13.491  11.510 1.00 22.90  ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 19.908 14.200  11.168 1.00 22.89  ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 19.918 15.336  10.664 1.00 22.28  ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 18.120 12.731  10.259 1.00 23.89  ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 17.114 11.568  10.430 1.00 25.82  ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 16.889 10.877  9.099  1.00 26.39  ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 17.607 10.544  11.452 1.00 25.93  ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 21.028 13.495  11.400 1.00 22.46  ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 22.358 13.987  11.042 1.00 23.35  ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 23.205 12.784  10.591 1.00 23.96  ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 23.131 11.704  11.189 1.00 24.58  ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 23.042 14.796  12.179 1.00 23.84  ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 24.429 15.426  11.877 1.00 25.50  ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 24.638 16.710  12.650 1.00 25.67  ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 25.563 14.462  12.175 1.00 26.11  ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 23.967 12.955  9.496  1.00 23.50  ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 24.864 11.917  8.983  1.00 23.25  ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 26.274 12.504  8.961  1.00 23.34  ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 26.467 13.609  8.447  1.00 23.63  ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 24.447 11.438  7.566  1.00 24.57  ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 25.459 10.438  7.007  1.00 25.68  ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 23.025 10.850  7.563  1.00 24.21  ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 27.242 11.796  9.540  1.00 23.06  ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 28.658 12.191  9.554  1.00 24.27  ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 29.508 11.061  8.937  1.00 26.18  ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 29.050 9.907   8.865  1.00 26.77  ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 29.123 12.500  10.980 1.00 24.36  ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 29.087 11.337  11.788 1.00 25.38  ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 30.741 11.381  8.485  1.00 26.39  ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 31.613 10.384  7.853  1.00 27.85  ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 32.463 9.639   8.879  1.00 29.24  ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 32.765 10.181  9.935  1.00 30.21  ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 32.519 11.048  6.814  1.00 29.21  ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 33.236 12.126  7.402  1.00 31.39  ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 32.833 8.399   8.588  1.00 29.60  ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 33.656 7.599   9.500  1.00 31.14  ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 34.910 7.101   8.769  1.00 33.14  ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 34.931 7.026   7.539  1.00 32.84  ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 32.874 6.372   10.025 1.00 31.83  ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 32.565 5.515   8.921  1.00 32.22  ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 31.614 6.753   10.797 1.00 31.88  ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? 35.938 6.728   9.529  1.00 35.11  ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? 37.156 6.186   8.953  1.00 37.15  ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? 36.985 4.662   8.730  1.00 37.56  ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? 37.508 4.127   7.755  1.00 38.67  ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? 38.377 6.555   9.823  1.00 40.22  ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? 38.366 5.745   11.003 1.00 42.54  ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? 38.399 8.043   10.217 1.00 40.49  ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? 36.250 3.973   9.609  1.00 36.81  ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? 36.037 2.532   9.484  1.00 36.90  ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 34.684 2.180   8.853  1.00 36.67  ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 33.708 2.908   9.010  1.00 36.26  ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? 36.155 1.863   10.850 1.00 37.09  ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 34.626 1.027   8.177  1.00 36.26  ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 33.418 0.524   7.526  1.00 35.98  ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 32.406 -0.025  8.538  1.00 34.39  ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 32.787 -0.763  9.437  1.00 34.67  ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 33.794 -0.606  6.547  1.00 38.56  ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 34.227 -0.133  5.163  1.00 45.17  ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 33.094 -0.265  4.171  1.00 52.82  ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 32.535 -1.356  3.972  1.00 56.13  ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 32.729 0.843   3.522  1.00 53.02  ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 31.128 0.290   8.345  1.00 32.39  ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 30.044 -0.212  9.183  1.00 31.62  ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 29.448 -1.512  8.670  1.00 30.85  ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 29.719 -1.913  7.531  1.00 31.26  ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 28.628 -2.192  9.499  1.00 29.48  ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 28.054 -3.481  9.117  1.00 29.21  ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 26.519 -3.483  8.966  1.00 28.73  ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 25.966 -4.555  8.696  1.00 29.11  ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 28.504 -4.573  10.087 1.00 29.99  ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 30.298 -4.706  10.287 1.00 35.74  ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 25.822 -2.343  9.192  1.00 27.60  ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 24.356 -2.339  9.082  1.00 27.90  ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 23.917 -2.242  7.607  1.00 27.85  ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 24.664 -1.736  6.767  1.00 27.81  ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 23.696 -1.214  9.928  1.00 30.64  ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 23.915 -1.282  11.444 1.00 35.94  ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 23.902 -2.409  11.998 1.00 36.97  ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 24.154 -0.203  12.071 1.00 34.88  ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 22.699 -2.709  7.307  1.00 27.79  ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 22.083 -2.661  5.973  1.00 28.53  ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 20.787 -1.845  6.114  1.00 28.25  ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 19.991 -2.123  7.016  1.00 27.97  ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 21.708 -4.101  5.504  1.00 30.84  ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 22.891 -4.815  5.144  1.00 32.64  ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 20.715 -4.118  4.325  1.00 31.25  ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 20.587 -0.830  5.255  1.00 27.78  ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 19.382 -0.009  5.301  1.00 27.39  ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 18.288 -0.738  4.499  1.00 27.94  ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 18.566 -1.260  3.410  1.00 28.70  ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 19.656 1.396   4.722  1.00 27.89  ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 20.843 2.086   5.427  1.00 28.39  ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 18.399 2.273   4.763  1.00 28.56  ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 20.642 2.393   6.895  1.00 28.48  ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 17.059 -0.789  5.030  1.00 26.98  ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 15.958 -1.415  4.303  1.00 26.49  ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 15.521 -0.497  3.135  1.00 25.55  ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 15.504 0.724   3.294  1.00 24.74  ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 14.788 -1.640  5.245  1.00 26.50  ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 15.144 -1.096  1.988  1.00 24.89  ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 14.608 -0.394  0.811  1.00 25.15  ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 13.277 -1.125  0.519  1.00 25.34  ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 13.254 -2.111  -0.227 1.00 26.07  ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 15.587 -0.446  -0.375 1.00 26.18  ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 17.001 0.114   -0.051 1.00 28.82  ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 17.013 1.564   0.424  1.00 29.84  ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 18.367 1.999   0.780  1.00 30.80  ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 18.657 3.160   1.366  1.00 30.38  ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 17.693 4.024   1.658  1.00 27.18  ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 19.917 3.465   1.661  1.00 29.65  ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 12.193 -0.662  1.158  1.00 24.87  ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 10.890 -1.336  1.185  1.00 24.90  ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 9.747  -0.376  1.646  1.00 25.44  ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 10.020 0.740   2.117  1.00 25.73  ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 11.023 -2.473  2.200  1.00 25.00  ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 11.109 -1.886  3.929  1.00 27.92  ? 56  CYS   A SG  1 
ATOM   392  N  N   A ASP   A 1 51  ? 8.486  -0.847  1.613  0.50 25.04  ? 57  ASP   A N   1 
ATOM   393  N  N   B ASP   A 1 51  ? 8.492  -0.885  1.596  0.50 25.77  ? 57  ASP   A N   1 
ATOM   394  C  CA  A ASP   A 1 51  ? 7.376  -0.059  2.164  0.50 25.05  ? 57  ASP   A CA  1 
ATOM   395  C  CA  B ASP   A 1 51  ? 7.264  -0.219  2.048  0.50 26.55  ? 57  ASP   A CA  1 
ATOM   396  C  C   A ASP   A 1 51  ? 6.759  -0.727  3.430  0.50 25.41  ? 57  ASP   A C   1 
ATOM   397  C  C   B ASP   A 1 51  ? 6.679  -0.921  3.319  0.50 26.18  ? 57  ASP   A C   1 
ATOM   398  O  O   A ASP   A 1 51  ? 5.618  -0.418  3.781  0.50 25.04  ? 57  ASP   A O   1 
ATOM   399  O  O   B ASP   A 1 51  ? 5.479  -0.817  3.570  0.50 25.95  ? 57  ASP   A O   1 
ATOM   400  C  CB  A ASP   A 1 51  ? 6.300  0.234   1.107  0.50 25.80  ? 57  ASP   A CB  1 
ATOM   401  C  CB  B ASP   A 1 51  ? 6.209  -0.285  0.926  0.50 29.12  ? 57  ASP   A CB  1 
ATOM   402  C  CG  A ASP   A 1 51  ? 5.560  -0.978  0.569  0.50 27.62  ? 57  ASP   A CG  1 
ATOM   403  C  CG  B ASP   A 1 51  ? 5.212  0.857   0.917  0.50 35.71  ? 57  ASP   A CG  1 
ATOM   404  O  OD1 A ASP   A 1 51  ? 5.986  -2.109  0.852  0.50 27.80  ? 57  ASP   A OD1 1 
ATOM   405  O  OD1 B ASP   A 1 51  ? 5.193  1.636   1.891  0.50 37.48  ? 57  ASP   A OD1 1 
ATOM   406  O  OD2 A ASP   A 1 51  ? 4.566  -0.788  -0.152 0.50 30.15  ? 57  ASP   A OD2 1 
ATOM   407  O  OD2 B ASP   A 1 51  ? 4.448  0.968   -0.063 0.50 38.27  ? 57  ASP   A OD2 1 
ATOM   408  N  N   . CYS   A 1 52  ? 7.509  -1.642  4.091  1.00 25.58  ? 58  CYS   A N   1 
ATOM   409  C  CA  . CYS   A 1 52  ? 7.074  -2.367  5.312  1.00 25.21  ? 58  CYS   A CA  1 
ATOM   410  C  C   . CYS   A 1 52  ? 6.364  -1.489  6.377  1.00 24.27  ? 58  CYS   A C   1 
ATOM   411  O  O   . CYS   A 1 52  ? 6.750  -0.329  6.583  1.00 22.59  ? 58  CYS   A O   1 
ATOM   412  C  CB  . CYS   A 1 52  ? 8.250  -3.116  5.942  1.00 25.72  ? 58  CYS   A CB  1 
ATOM   413  S  SG  . CYS   A 1 52  ? 8.719  -4.657  5.094  1.00 28.88  ? 58  CYS   A SG  1 
ATOM   414  N  N   . GLN   A 1 53  ? 5.350  -2.069  7.075  1.00 23.28  ? 59  GLN   A N   1 
ATOM   415  C  CA  . GLN   A 1 53  ? 4.655  -1.394  8.173  1.00 23.17  ? 59  GLN   A CA  1 
ATOM   416  C  C   . GLN   A 1 53  ? 4.653  -2.237  9.466  1.00 22.52  ? 59  GLN   A C   1 
ATOM   417  O  O   . GLN   A 1 53  ? 3.855  -1.954  10.350 1.00 22.22  ? 59  GLN   A O   1 
ATOM   418  C  CB  . GLN   A 1 53  ? 3.221  -0.971  7.790  1.00 24.87  ? 59  GLN   A CB  1 
ATOM   419  C  CG  . GLN   A 1 53  ? 3.190  0.346   7.025  1.00 29.35  ? 59  GLN   A CG  1 
ATOM   420  C  CD  . GLN   A 1 53  ? 1.781  0.864   6.794  1.00 33.76  ? 59  GLN   A CD  1 
ATOM   421  O  OE1 . GLN   A 1 53  ? 1.241  0.771   5.682  1.00 34.78  ? 59  GLN   A OE1 1 
ATOM   422  N  NE2 . GLN   A 1 53  ? 1.164  1.437   7.833  1.00 33.09  ? 59  GLN   A NE2 1 
ATOM   423  N  N   . THR   A 1 54  ? 5.507  -3.295  9.554  1.00 22.03  ? 60  THR   A N   1 
ATOM   424  C  CA  . THR   A 1 54  ? 5.691  -4.127  10.741 1.00 22.12  ? 60  THR   A CA  1 
ATOM   425  C  C   . THR   A 1 54  ? 7.209  -4.361  10.909 1.00 20.85  ? 60  THR   A C   1 
ATOM   426  O  O   . THR   A 1 54  ? 7.946  -4.455  9.934  1.00 19.97  ? 60  THR   A O   1 
ATOM   427  C  CB  . THR   A 1 54  ? 4.938  -5.497  10.710 1.00 24.74  ? 60  THR   A CB  1 
ATOM   428  O  OG1 . THR   A 1 54  ? 5.513  -6.323  9.713  1.00 26.74  ? 60  THR   A OG1 1 
ATOM   429  C  CG2 . THR   A 1 54  ? 3.447  -5.377  10.482 1.00 25.29  ? 60  THR   A CG2 1 
ATOM   430  N  N   . GLY   A 1 55  ? 7.645  -4.417  12.158 1.00 20.18  ? 61  GLY   A N   1 
ATOM   431  C  CA  . GLY   A 1 55  ? 9.041  -4.617  12.527 1.00 20.34  ? 61  GLY   A CA  1 
ATOM   432  C  C   . GLY   A 1 55  ? 9.193  -4.767  14.036 1.00 20.72  ? 61  GLY   A C   1 
ATOM   433  O  O   . GLY   A 1 55  ? 8.216  -5.041  14.734 1.00 20.44  ? 61  GLY   A O   1 
ATOM   434  N  N   . VAL   A 1 56  ? 10.431 -4.613  14.540 1.00 20.78  ? 62  VAL   A N   1 
ATOM   435  C  CA  . VAL   A 1 56  ? 10.811 -4.710  15.945 1.00 21.38  ? 62  VAL   A CA  1 
ATOM   436  C  C   . VAL   A 1 56  ? 11.703 -3.494  16.289 1.00 21.52  ? 62  VAL   A C   1 
ATOM   437  O  O   . VAL   A 1 56  ? 12.517 -3.086  15.464 1.00 22.76  ? 62  VAL   A O   1 
ATOM   438  C  CB  . VAL   A 1 56  ? 11.582 -6.047  16.231 1.00 22.79  ? 62  VAL   A CB  1 
ATOM   439  C  CG1 . VAL   A 1 56  ? 11.942 -6.174  17.718 1.00 23.14  ? 62  VAL   A CG1 1 
ATOM   440  C  CG2 . VAL   A 1 56  ? 10.756 -7.256  15.795 1.00 24.37  ? 62  VAL   A CG2 1 
ATOM   441  N  N   . TYR   A 1 57  ? 11.551 -2.913  17.486 1.00 20.79  ? 63  TYR   A N   1 
ATOM   442  C  CA  . TYR   A 1 57  ? 12.393 -1.780  17.905 1.00 20.50  ? 63  TYR   A CA  1 
ATOM   443  C  C   . TYR   A 1 57  ? 12.970 -2.013  19.291 1.00 21.71  ? 63  TYR   A C   1 
ATOM   444  O  O   . TYR   A 1 57  ? 12.382 -2.758  20.080 1.00 21.72  ? 63  TYR   A O   1 
ATOM   445  C  CB  . TYR   A 1 57  ? 11.667 -0.404  17.816 1.00 20.41  ? 63  TYR   A CB  1 
ATOM   446  C  CG  . TYR   A 1 57  ? 10.797 -0.042  19.013 1.00 21.68  ? 63  TYR   A CG  1 
ATOM   447  C  CD1 . TYR   A 1 57  ? 9.506  -0.542  19.139 1.00 22.12  ? 63  TYR   A CD1 1 
ATOM   448  C  CD2 . TYR   A 1 57  ? 11.256 0.832   19.998 1.00 22.29  ? 63  TYR   A CD2 1 
ATOM   449  C  CE1 . TYR   A 1 57  ? 8.699  -0.199  20.221 1.00 23.61  ? 63  TYR   A CE1 1 
ATOM   450  C  CE2 . TYR   A 1 57  ? 10.452 1.194   21.074 1.00 23.67  ? 63  TYR   A CE2 1 
ATOM   451  C  CZ  . TYR   A 1 57  ? 9.170  0.672   21.186 1.00 24.20  ? 63  TYR   A CZ  1 
ATOM   452  O  OH  . TYR   A 1 57  ? 8.371  0.979   22.270 1.00 24.57  ? 63  TYR   A OH  1 
ATOM   453  N  N   . TYR   A 1 58  ? 14.115 -1.382  19.600 1.00 21.87  ? 64  TYR   A N   1 
ATOM   454  C  CA  . TYR   A 1 58  ? 14.703 -1.559  20.925 1.00 21.92  ? 64  TYR   A CA  1 
ATOM   455  C  C   . TYR   A 1 58  ? 14.289 -0.397  21.819 1.00 21.96  ? 64  TYR   A C   1 
ATOM   456  O  O   . TYR   A 1 58  ? 14.517 0.756   21.457 1.00 21.78  ? 64  TYR   A O   1 
ATOM   457  C  CB  . TYR   A 1 58  ? 16.236 -1.683  20.875 1.00 22.11  ? 64  TYR   A CB  1 
ATOM   458  C  CG  . TYR   A 1 58  ? 16.863 -1.732  22.257 1.00 23.57  ? 64  TYR   A CG  1 
ATOM   459  C  CD1 . TYR   A 1 58  ? 16.641 -2.810  23.109 1.00 24.96  ? 64  TYR   A CD1 1 
ATOM   460  C  CD2 . TYR   A 1 58  ? 17.680 -0.702  22.711 1.00 25.40  ? 64  TYR   A CD2 1 
ATOM   461  C  CE1 . TYR   A 1 58  ? 17.232 -2.874  24.371 1.00 25.66  ? 64  TYR   A CE1 1 
ATOM   462  C  CE2 . TYR   A 1 58  ? 18.261 -0.743  23.982 1.00 26.19  ? 64  TYR   A CE2 1 
ATOM   463  C  CZ  . TYR   A 1 58  ? 18.017 -1.826  24.817 1.00 26.82  ? 64  TYR   A CZ  1 
ATOM   464  O  OH  . TYR   A 1 58  ? 18.572 -1.885  26.074 1.00 28.40  ? 64  TYR   A OH  1 
ATOM   465  N  N   . CYS   A 1 59  ? 13.776 -0.712  23.024 1.00 21.74  ? 65  CYS   A N   1 
ATOM   466  C  CA  . CYS   A 1 59  ? 13.381 0.291   24.021 1.00 21.91  ? 65  CYS   A CA  1 
ATOM   467  C  C   . CYS   A 1 59  ? 14.327 0.218   25.235 1.00 22.05  ? 65  CYS   A C   1 
ATOM   468  O  O   . CYS   A 1 59  ? 14.152 -0.678  26.060 1.00 21.56  ? 65  CYS   A O   1 
ATOM   469  C  CB  . CYS   A 1 59  ? 11.922 0.079   24.436 1.00 22.41  ? 65  CYS   A CB  1 
ATOM   470  S  SG  . CYS   A 1 59  ? 11.339 1.216   25.730 1.00 24.01  ? 65  CYS   A SG  1 
ATOM   471  N  N   . SER   A 1 60  ? 15.341 1.125   25.344 1.00 21.68  ? 66  SER   A N   1 
ATOM   472  C  CA  . SER   A 1 60  ? 16.300 1.070   26.456 1.00 22.78  ? 66  SER   A CA  1 
ATOM   473  C  C   . SER   A 1 60  ? 15.687 1.297   27.858 1.00 23.11  ? 66  SER   A C   1 
ATOM   474  O  O   . SER   A 1 60  ? 16.172 0.721   28.835 1.00 23.97  ? 66  SER   A O   1 
ATOM   475  C  CB  . SER   A 1 60  ? 17.470 2.027   26.242 1.00 25.09  ? 66  SER   A CB  1 
ATOM   476  O  OG  . SER   A 1 60  ? 17.076 3.378   26.423 1.00 28.09  ? 66  SER   A OG  1 
ATOM   477  N  N   . SER   A 1 61  ? 14.611 2.096   27.957 1.00 22.15  ? 67  SER   A N   1 
ATOM   478  C  CA  . SER   A 1 61  ? 13.947 2.342   29.246 1.00 22.53  ? 67  SER   A CA  1 
ATOM   479  C  C   . SER   A 1 61  ? 13.137 1.113   29.765 1.00 22.83  ? 67  SER   A C   1 
ATOM   480  O  O   . SER   A 1 61  ? 12.635 1.136   30.891 1.00 23.16  ? 67  SER   A O   1 
ATOM   481  C  CB  . SER   A 1 61  ? 13.089 3.601   29.181 1.00 23.30  ? 67  SER   A CB  1 
ATOM   482  O  OG  . SER   A 1 61  ? 11.987 3.428   28.307 1.00 23.84  ? 67  SER   A OG  1 
ATOM   483  N  N   . ARG   A 1 62  ? 13.047 0.036   28.956 1.00 22.08  ? 68  ARG   A N   1 
ATOM   484  C  CA  . ARG   A 1 62  ? 12.422 -1.229  29.341 1.00 22.49  ? 68  ARG   A CA  1 
ATOM   485  C  C   . ARG   A 1 62  ? 13.389 -2.431  29.167 1.00 23.59  ? 68  ARG   A C   1 
ATOM   486  O  O   . ARG   A 1 62  ? 13.019 -3.576  29.498 1.00 23.16  ? 68  ARG   A O   1 
ATOM   487  C  CB  . ARG   A 1 62  ? 11.153 -1.464  28.495 1.00 22.73  ? 68  ARG   A CB  1 
ATOM   488  C  CG  . ARG   A 1 62  ? 10.002 -0.496  28.790 1.00 23.65  ? 68  ARG   A CG  1 
ATOM   489  C  CD  . ARG   A 1 62  ? 9.331  -0.782  30.146 1.00 25.91  ? 68  ARG   A CD  1 
ATOM   490  N  NE  . ARG   A 1 62  ? 8.246  0.166   30.417 1.00 27.55  ? 68  ARG   A NE  1 
ATOM   491  C  CZ  . ARG   A 1 62  ? 8.392  1.300   31.096 1.00 27.23  ? 68  ARG   A CZ  1 
ATOM   492  N  NH1 . ARG   A 1 62  ? 9.572  1.625   31.618 1.00 25.32  ? 68  ARG   A NH1 1 
ATOM   493  N  NH2 . ARG   A 1 62  ? 7.359  2.118   31.263 1.00 26.80  ? 68  ARG   A NH2 1 
ATOM   494  N  N   . ARG   A 1 63  ? 14.590 -2.198  28.575 1.00 23.88  ? 69  ARG   A N   1 
ATOM   495  C  CA  . ARG   A 1 63  ? 15.559 -3.237  28.207 1.00 25.08  ? 69  ARG   A CA  1 
ATOM   496  C  C   . ARG   A 1 63  ? 14.852 -4.337  27.377 1.00 24.95  ? 69  ARG   A C   1 
ATOM   497  O  O   . ARG   A 1 63  ? 15.043 -5.521  27.630 1.00 25.04  ? 69  ARG   A O   1 
ATOM   498  C  CB  . ARG   A 1 63  ? 16.273 -3.820  29.451 1.00 26.85  ? 69  ARG   A CB  1 
ATOM   499  C  CG  . ARG   A 1 63  ? 17.410 -2.945  29.988 1.00 30.14  ? 69  ARG   A CG  1 
ATOM   500  C  CD  . ARG   A 1 63  ? 18.117 -3.622  31.154 1.00 32.32  ? 69  ARG   A CD  1 
ATOM   501  N  NE  . ARG   A 1 63  ? 18.943 -2.694  31.927 1.00 34.39  ? 69  ARG   A NE  1 
ATOM   502  C  CZ  . ARG   A 1 63  ? 18.846 -2.512  33.245 1.00 35.62  ? 69  ARG   A CZ  1 
ATOM   503  N  NH1 . ARG   A 1 63  ? 17.939 -3.177  33.949 1.00 33.66  ? 69  ARG   A NH1 1 
ATOM   504  N  NH2 . ARG   A 1 63  ? 19.643 -1.645  33.864 1.00 35.50  ? 69  ARG   A NH2 1 
ATOM   505  N  N   . LYS   A 1 64  ? 13.959 -3.931  26.455 1.00 24.55  ? 70  LYS   A N   1 
ATOM   506  C  CA  . LYS   A 1 64  ? 13.184 -4.907  25.672 1.00 24.89  ? 70  LYS   A CA  1 
ATOM   507  C  C   . LYS   A 1 64  ? 13.085 -4.552  24.191 1.00 23.62  ? 70  LYS   A C   1 
ATOM   508  O  O   . LYS   A 1 64  ? 13.134 -3.375  23.824 1.00 24.48  ? 70  LYS   A O   1 
ATOM   509  C  CB  . LYS   A 1 64  ? 11.759 -5.065  26.246 1.00 28.74  ? 70  LYS   A CB  1 
ATOM   510  C  CG  . LYS   A 1 64  ? 11.671 -6.109  27.339 1.00 36.93  ? 70  LYS   A CG  1 
ATOM   511  C  CD  . LYS   A 1 64  ? 10.280 -6.721  27.457 1.00 44.09  ? 70  LYS   A CD  1 
ATOM   512  C  CE  . LYS   A 1 64  ? 10.187 -7.612  28.685 1.00 50.10  ? 70  LYS   A CE  1 
ATOM   513  N  NZ  . LYS   A 1 64  ? 10.441 -6.874  29.965 1.00 52.48  ? 70  LYS   A NZ  1 
ATOM   514  N  N   . HIS   A 1 65  ? 12.880 -5.568  23.356 1.00 21.95  ? 71  HIS   A N   1 
ATOM   515  C  CA  . HIS   A 1 65  ? 12.689 -5.405  21.909 1.00 21.85  ? 71  HIS   A CA  1 
ATOM   516  C  C   . HIS   A 1 65  ? 11.203 -5.718  21.627 1.00 22.33  ? 71  HIS   A C   1 
ATOM   517  O  O   . HIS   A 1 65  ? 10.741 -6.826  21.921 1.00 22.13  ? 71  HIS   A O   1 
ATOM   518  C  CB  . HIS   A 1 65  ? 13.620 -6.360  21.117 1.00 21.95  ? 71  HIS   A CB  1 
ATOM   519  C  CG  . HIS   A 1 65  ? 15.085 -6.173  21.431 1.00 23.40  ? 71  HIS   A CG  1 
ATOM   520  N  ND1 . HIS   A 1 65  ? 15.944 -5.539  20.537 1.00 24.62  ? 71  HIS   A ND1 1 
ATOM   521  C  CD2 . HIS   A 1 65  ? 15.778 -6.481  22.551 1.00 24.54  ? 71  HIS   A CD2 1 
ATOM   522  C  CE1 . HIS   A 1 65  ? 17.129 -5.527  21.122 1.00 24.92  ? 71  HIS   A CE1 1 
ATOM   523  N  NE2 . HIS   A 1 65  ? 17.075 -6.060  22.344 1.00 25.37  ? 71  HIS   A NE2 1 
ATOM   524  N  N   . TYR   A 1 66  ? 10.450 -4.726  21.149 1.00 21.71  ? 72  TYR   A N   1 
ATOM   525  C  CA  . TYR   A 1 66  ? 9.009  -4.903  20.926 1.00 21.88  ? 72  TYR   A CA  1 
ATOM   526  C  C   . TYR   A 1 66  ? 8.589  -5.048  19.450 1.00 22.36  ? 72  TYR   A C   1 
ATOM   527  O  O   . TYR   A 1 66  ? 8.927  -4.198  18.629 1.00 22.15  ? 72  TYR   A O   1 
ATOM   528  C  CB  . TYR   A 1 66  ? 8.248  -3.692  21.488 1.00 21.68  ? 72  TYR   A CB  1 
ATOM   529  C  CG  . TYR   A 1 66  ? 8.294  -3.509  22.997 1.00 22.50  ? 72  TYR   A CG  1 
ATOM   530  C  CD1 . TYR   A 1 66  ? 7.435  -4.215  23.829 1.00 23.53  ? 72  TYR   A CD1 1 
ATOM   531  C  CD2 . TYR   A 1 66  ? 9.101  -2.537  23.575 1.00 23.87  ? 72  TYR   A CD2 1 
ATOM   532  C  CE1 . TYR   A 1 66  ? 7.434  -4.017  25.210 1.00 25.10  ? 72  TYR   A CE1 1 
ATOM   533  C  CE2 . TYR   A 1 66  ? 9.084  -2.304  24.948 1.00 25.19  ? 72  TYR   A CE2 1 
ATOM   534  C  CZ  . TYR   A 1 66  ? 8.233  -3.032  25.761 1.00 26.63  ? 72  TYR   A CZ  1 
ATOM   535  O  OH  . TYR   A 1 66  ? 8.248  -2.834  27.122 1.00 29.03  ? 72  TYR   A OH  1 
ATOM   536  N  N   . PRO   A 1 67  ? 7.764  -6.058  19.124 1.00 22.52  ? 73  PRO   A N   1 
ATOM   537  C  CA  . PRO   A 1 67  ? 7.224  -6.133  17.753 1.00 22.56  ? 73  PRO   A CA  1 
ATOM   538  C  C   . PRO   A 1 67  ? 6.128  -5.059  17.602 1.00 23.19  ? 73  PRO   A C   1 
ATOM   539  O  O   . PRO   A 1 67  ? 5.323  -4.896  18.527 1.00 23.39  ? 73  PRO   A O   1 
ATOM   540  C  CB  . PRO   A 1 67  ? 6.648  -7.562  17.650 1.00 23.71  ? 73  PRO   A CB  1 
ATOM   541  C  CG  . PRO   A 1 67  ? 6.588  -8.102  19.059 1.00 24.69  ? 73  PRO   A CG  1 
ATOM   542  C  CD  . PRO   A 1 67  ? 7.231  -7.118  20.014 1.00 22.80  ? 73  PRO   A CD  1 
ATOM   543  N  N   . VAL   A 1 68  ? 6.117  -4.286  16.501 1.00 22.87  ? 74  VAL   A N   1 
ATOM   544  C  CA  . VAL   A 1 68  ? 5.106  -3.228  16.326 1.00 23.37  ? 74  VAL   A CA  1 
ATOM   545  C  C   . VAL   A 1 68  ? 4.631  -3.097  14.869 1.00 23.62  ? 74  VAL   A C   1 
ATOM   546  O  O   . VAL   A 1 68  ? 5.373  -3.429  13.932 1.00 23.39  ? 74  VAL   A O   1 
ATOM   547  C  CB  . VAL   A 1 68  ? 5.620  -1.815  16.783 1.00 24.10  ? 74  VAL   A CB  1 
ATOM   548  C  CG1 . VAL   A 1 68  ? 5.707  -1.673  18.314 1.00 24.86  ? 74  VAL   A CG1 1 
ATOM   549  C  CG2 . VAL   A 1 68  ? 6.934  -1.425  16.083 1.00 23.58  ? 74  VAL   A CG2 1 
ATOM   550  N  N   . SER   A 1 69  ? 3.414  -2.510  14.699 1.00 22.82  ? 75  SER   A N   1 
ATOM   551  C  CA  . SER   A 1 69  ? 2.848  -2.040  13.439 1.00 22.81  ? 75  SER   A CA  1 
ATOM   552  C  C   . SER   A 1 69  ? 3.142  -0.528  13.475 1.00 22.10  ? 75  SER   A C   1 
ATOM   553  O  O   . SER   A 1 69  ? 2.901  0.097   14.511 1.00 22.61  ? 75  SER   A O   1 
ATOM   554  C  CB  . SER   A 1 69  ? 1.331  -2.190  13.431 1.00 24.93  ? 75  SER   A CB  1 
ATOM   555  O  OG  . SER   A 1 69  ? 0.960  -3.544  13.269 1.00 28.80  ? 75  SER   A OG  1 
ATOM   556  N  N   . PHE   A 1 70  ? 3.585  0.073   12.370 1.00 20.43  ? 76  PHE   A N   1 
ATOM   557  C  CA  . PHE   A 1 70  ? 3.855  1.517   12.368 1.00 21.10  ? 76  PHE   A CA  1 
ATOM   558  C  C   . PHE   A 1 70  ? 3.289  2.203   11.133 1.00 22.72  ? 76  PHE   A C   1 
ATOM   559  O  O   . PHE   A 1 70  ? 3.094  1.561   10.107 1.00 22.88  ? 76  PHE   A O   1 
ATOM   560  C  CB  . PHE   A 1 70  ? 5.365  1.837   12.573 1.00 20.34  ? 76  PHE   A CB  1 
ATOM   561  C  CG  . PHE   A 1 70  ? 6.273  1.106   11.617 1.00 21.14  ? 76  PHE   A CG  1 
ATOM   562  C  CD1 . PHE   A 1 70  ? 6.715  -0.182  11.901 1.00 22.61  ? 76  PHE   A CD1 1 
ATOM   563  C  CD2 . PHE   A 1 70  ? 6.658  1.686   10.422 1.00 22.43  ? 76  PHE   A CD2 1 
ATOM   564  C  CE1 . PHE   A 1 70  ? 7.558  -0.857  11.016 1.00 23.20  ? 76  PHE   A CE1 1 
ATOM   565  C  CE2 . PHE   A 1 70  ? 7.494  1.015   9.536  1.00 23.23  ? 76  PHE   A CE2 1 
ATOM   566  C  CZ  . PHE   A 1 70  ? 7.952  -0.248  9.838  1.00 22.62  ? 76  PHE   A CZ  1 
ATOM   567  N  N   . SER   A 1 71  ? 3.039  3.510   11.222 1.00 23.06  ? 77  SER   A N   1 
ATOM   568  C  CA  . SER   A 1 71  ? 2.446  4.241   10.118 1.00 24.88  ? 77  SER   A CA  1 
ATOM   569  C  C   . SER   A 1 71  ? 3.468  4.612   9.001  1.00 26.66  ? 77  SER   A C   1 
ATOM   570  O  O   . SER   A 1 71  ? 4.673  4.435   9.178  1.00 27.57  ? 77  SER   A O   1 
ATOM   571  C  CB  . SER   A 1 71  ? 1.698  5.459   10.667 1.00 26.10  ? 77  SER   A CB  1 
ATOM   572  O  OG  . SER   A 1 71  ? 2.592  6.397   11.236 1.00 28.68  ? 77  SER   A OG  1 
ATOM   573  N  N   . LYS   A 1 72  ? 2.997  5.116   7.849  1.00 27.29  ? 78  LYS   A N   1 
ATOM   574  C  CA  . LYS   A 1 72  ? 3.901  5.531   6.759  1.00 28.96  ? 78  LYS   A CA  1 
ATOM   575  C  C   . LYS   A 1 72  ? 4.573  6.887   7.080  1.00 28.53  ? 78  LYS   A C   1 
ATOM   576  O  O   . LYS   A 1 72  ? 3.989  7.663   7.827  1.00 28.34  ? 78  LYS   A O   1 
ATOM   577  C  CB  . LYS   A 1 72  ? 3.131  5.579   5.423  1.00 32.69  ? 78  LYS   A CB  1 
ATOM   578  C  CG  . LYS   A 1 72  ? 3.253  4.266   4.641  1.00 39.28  ? 78  LYS   A CG  1 
ATOM   579  C  CD  . LYS   A 1 72  ? 1.982  3.944   3.876  1.00 46.41  ? 78  LYS   A CD  1 
ATOM   580  C  CE  . LYS   A 1 72  ? 2.152  2.756   2.957  1.00 52.59  ? 78  LYS   A CE  1 
ATOM   581  N  NZ  . LYS   A 1 72  ? 2.870  3.137   1.708  1.00 56.52  ? 78  LYS   A NZ  1 
ATOM   582  N  N   . PRO   A 1 73  ? 5.795  7.200   6.567  1.00 28.61  ? 79  PRO   A N   1 
ATOM   583  C  CA  . PRO   A 1 73  ? 6.439  8.485   6.936  1.00 27.87  ? 79  PRO   A CA  1 
ATOM   584  C  C   . PRO   A 1 73  ? 5.568  9.680   6.572  1.00 26.38  ? 79  PRO   A C   1 
ATOM   585  O  O   . PRO   A 1 73  ? 5.106  9.775   5.437  1.00 25.83  ? 79  PRO   A O   1 
ATOM   586  C  CB  . PRO   A 1 73  ? 7.754  8.467   6.153  1.00 29.19  ? 79  PRO   A CB  1 
ATOM   587  C  CG  . PRO   A 1 73  ? 8.016  7.022   5.882  1.00 30.35  ? 79  PRO   A CG  1 
ATOM   588  C  CD  . PRO   A 1 73  ? 6.653  6.413   5.666  1.00 28.65  ? 79  PRO   A CD  1 
ATOM   589  N  N   A SER   A 1 74  ? 5.321  10.569  7.543  0.50 26.06  ? 80  SER   A N   1 
ATOM   590  N  N   B SER   A 1 74  ? 5.319  10.572  7.539  0.50 26.00  ? 80  SER   A N   1 
ATOM   591  C  CA  A SER   A 1 74  ? 4.426  11.717  7.357  0.50 26.62  ? 80  SER   A CA  1 
ATOM   592  C  CA  B SER   A 1 74  ? 4.447  11.731  7.339  0.50 26.50  ? 80  SER   A CA  1 
ATOM   593  C  C   A SER   A 1 74  ? 4.912  12.992  8.097  0.50 26.69  ? 80  SER   A C   1 
ATOM   594  C  C   B SER   A 1 74  ? 4.917  12.997  8.094  0.50 26.62  ? 80  SER   A C   1 
ATOM   595  O  O   A SER   A 1 74  ? 5.871  12.941  8.880  0.50 26.75  ? 80  SER   A O   1 
ATOM   596  O  O   B SER   A 1 74  ? 5.874  12.946  8.879  0.50 26.69  ? 80  SER   A O   1 
ATOM   597  C  CB  A SER   A 1 74  ? 3.013  11.362  7.837  0.50 27.99  ? 80  SER   A CB  1 
ATOM   598  C  CB  B SER   A 1 74  ? 3.018  11.377  7.754  0.50 27.72  ? 80  SER   A CB  1 
ATOM   599  O  OG  A SER   A 1 74  ? 2.654  10.003  7.632  0.50 31.07  ? 80  SER   A OG  1 
ATOM   600  O  OG  B SER   A 1 74  ? 2.517  10.291  6.995  0.50 30.49  ? 80  SER   A OG  1 
ATOM   601  N  N   . LEU   A 1 75  ? 4.238  14.130  7.837  1.00 26.51  ? 81  LEU   A N   1 
ATOM   602  C  CA  . LEU   A 1 75  ? 4.495  15.419  8.468  1.00 27.17  ? 81  LEU   A CA  1 
ATOM   603  C  C   . LEU   A 1 75  ? 3.563  15.405  9.714  1.00 28.34  ? 81  LEU   A C   1 
ATOM   604  O  O   . LEU   A 1 75  ? 2.337  15.270  9.579  1.00 28.78  ? 81  LEU   A O   1 
ATOM   605  C  CB  . LEU   A 1 75  ? 4.095  16.526  7.476  1.00 27.40  ? 81  LEU   A CB  1 
ATOM   606  C  CG  . LEU   A 1 75  ? 4.539  17.957  7.779  1.00 29.47  ? 81  LEU   A CG  1 
ATOM   607  C  CD1 . LEU   A 1 75  ? 6.048  18.076  7.885  1.00 29.32  ? 81  LEU   A CD1 1 
ATOM   608  C  CD2 . LEU   A 1 75  ? 4.020  18.920  6.727  1.00 30.55  ? 81  LEU   A CD2 1 
ATOM   609  N  N   . ILE   A 1 76  ? 4.147  15.415  10.921 1.00 27.87  ? 82  ILE   A N   1 
ATOM   610  C  CA  . ILE   A 1 76  ? 3.388  15.293  12.175 1.00 28.18  ? 82  ILE   A CA  1 
ATOM   611  C  C   . ILE   A 1 76  ? 3.709  16.432  13.141 1.00 28.42  ? 82  ILE   A C   1 
ATOM   612  O  O   . ILE   A 1 76  ? 4.886  16.730  13.341 1.00 28.18  ? 82  ILE   A O   1 
ATOM   613  C  CB  . ILE   A 1 76  ? 3.763  13.948  12.862 1.00 29.03  ? 82  ILE   A CB  1 
ATOM   614  C  CG1 . ILE   A 1 76  ? 3.527  12.717  11.943 1.00 30.78  ? 82  ILE   A CG1 1 
ATOM   615  C  CG2 . ILE   A 1 76  ? 3.085  13.784  14.232 1.00 29.02  ? 82  ILE   A CG2 1 
ATOM   616  C  CD1 . ILE   A 1 76  ? 2.142  12.245  11.765 1.00 32.78  ? 82  ILE   A CD1 1 
ATOM   617  N  N   . PHE   A 1 77  ? 2.694  17.010  13.807 1.00 28.33  ? 83  PHE   A N   1 
ATOM   618  C  CA  . PHE   A 1 77  ? 2.947  18.034  14.822 1.00 28.44  ? 83  PHE   A CA  1 
ATOM   619  C  C   . PHE   A 1 77  ? 3.571  17.400  16.085 1.00 27.57  ? 83  PHE   A C   1 
ATOM   620  O  O   . PHE   A 1 77  ? 3.079  16.380  16.588 1.00 27.79  ? 83  PHE   A O   1 
ATOM   621  C  CB  . PHE   A 1 77  ? 1.681  18.826  15.173 1.00 29.12  ? 83  PHE   A CB  1 
ATOM   622  C  CG  . PHE   A 1 77  ? 2.000  20.084  15.948 1.00 30.77  ? 83  PHE   A CG  1 
ATOM   623  C  CD1 . PHE   A 1 77  ? 2.538  21.191  15.313 1.00 32.08  ? 83  PHE   A CD1 1 
ATOM   624  C  CD2 . PHE   A 1 77  ? 1.782  20.151  17.312 1.00 32.19  ? 83  PHE   A CD2 1 
ATOM   625  C  CE1 . PHE   A 1 77  ? 2.834  22.346  16.023 1.00 33.31  ? 83  PHE   A CE1 1 
ATOM   626  C  CE2 . PHE   A 1 77  ? 2.091  21.304  18.024 1.00 33.16  ? 83  PHE   A CE2 1 
ATOM   627  C  CZ  . PHE   A 1 77  ? 2.619  22.393  17.378 1.00 33.03  ? 83  PHE   A CZ  1 
ATOM   628  N  N   . VAL   A 1 78  ? 4.704  17.959  16.536 1.00 26.19  ? 84  VAL   A N   1 
ATOM   629  C  CA  . VAL   A 1 78  ? 5.455  17.470  17.688 1.00 25.86  ? 84  VAL   A CA  1 
ATOM   630  C  C   . VAL   A 1 78  ? 5.564  18.571  18.745 1.00 26.11  ? 84  VAL   A C   1 
ATOM   631  O  O   . VAL   A 1 78  ? 6.053  19.660  18.438 1.00 26.40  ? 84  VAL   A O   1 
ATOM   632  C  CB  . VAL   A 1 78  ? 6.855  16.949  17.260 1.00 25.74  ? 84  VAL   A CB  1 
ATOM   633  C  CG1 . VAL   A 1 78  ? 7.742  16.676  18.470 1.00 25.99  ? 84  VAL   A CG1 1 
ATOM   634  C  CG2 . VAL   A 1 78  ? 6.737  15.705  16.389 1.00 25.90  ? 84  VAL   A CG2 1 
ATOM   635  N  N   . GLU   A 1 79  ? 5.112  18.296  19.986 1.00 25.81  ? 85  GLU   A N   1 
ATOM   636  C  CA  . GLU   A 1 79  ? 5.158  19.294  21.061 1.00 26.67  ? 85  GLU   A CA  1 
ATOM   637  C  C   . GLU   A 1 79  ? 6.591  19.747  21.407 1.00 26.76  ? 85  GLU   A C   1 
ATOM   638  O  O   . GLU   A 1 79  ? 7.553  18.988  21.194 1.00 26.19  ? 85  GLU   A O   1 
ATOM   639  C  CB  . GLU   A 1 79  ? 4.477  18.756  22.351 1.00 29.15  ? 85  GLU   A CB  1 
ATOM   640  C  CG  . GLU   A 1 79  ? 2.995  18.468  22.219 1.00 34.00  ? 85  GLU   A CG  1 
ATOM   641  C  CD  . GLU   A 1 79  ? 2.119  19.677  21.942 1.00 43.85  ? 85  GLU   A CD  1 
ATOM   642  O  OE1 . GLU   A 1 79  ? 2.531  20.819  22.254 1.00 45.48  ? 85  GLU   A OE1 1 
ATOM   643  O  OE2 . GLU   A 1 79  ? 1.005  19.476  21.409 1.00 47.78  ? 85  GLU   A OE2 1 
ATOM   644  N  N   . ALA   A 1 80  ? 6.726  20.948  22.017 1.00 26.40  ? 86  ALA   A N   1 
ATOM   645  C  CA  . ALA   A 1 80  ? 8.029  21.437  22.460 1.00 27.37  ? 86  ALA   A CA  1 
ATOM   646  C  C   . ALA   A 1 80  ? 8.718  20.433  23.428 1.00 27.82  ? 86  ALA   A C   1 
ATOM   647  O  O   . ALA   A 1 80  ? 8.048  19.694  24.163 1.00 27.63  ? 86  ALA   A O   1 
ATOM   648  C  CB  . ALA   A 1 80  ? 7.878  22.799  23.135 1.00 27.71  ? 86  ALA   A CB  1 
ATOM   649  N  N   . SER   A 1 81  ? 10.051 20.380  23.365 1.00 27.74  ? 87  SER   A N   1 
ATOM   650  C  CA  . SER   A 1 81  ? 10.887 19.480  24.162 1.00 27.83  ? 87  SER   A CA  1 
ATOM   651  C  C   . SER   A 1 81  ? 12.119 20.255  24.676 1.00 28.37  ? 87  SER   A C   1 
ATOM   652  O  O   . SER   A 1 81  ? 12.255 21.452  24.400 1.00 28.69  ? 87  SER   A O   1 
ATOM   653  C  CB  . SER   A 1 81  ? 11.347 18.311  23.289 1.00 28.07  ? 87  SER   A CB  1 
ATOM   654  O  OG  . SER   A 1 81  ? 12.310 18.722  22.323 1.00 29.22  ? 87  SER   A OG  1 
ATOM   655  N  N   . GLU   A 1 82  ? 13.053 19.551  25.344 1.00 28.15  ? 88  GLU   A N   1 
ATOM   656  C  CA  . GLU   A 1 82  ? 14.304 20.142  25.787 1.00 29.37  ? 88  GLU   A CA  1 
ATOM   657  C  C   . GLU   A 1 82  ? 15.135 20.639  24.580 1.00 29.71  ? 88  GLU   A C   1 
ATOM   658  O  O   . GLU   A 1 82  ? 15.858 21.623  24.715 1.00 30.32  ? 88  GLU   A O   1 
ATOM   659  C  CB  . GLU   A 1 82  ? 15.120 19.095  26.594 1.00 33.10  ? 88  GLU   A CB  1 
ATOM   660  C  CG  . GLU   A 1 82  ? 16.445 19.637  27.119 1.00 40.70  ? 88  GLU   A CG  1 
ATOM   661  C  CD  . GLU   A 1 82  ? 17.347 18.722  27.933 1.00 48.76  ? 88  GLU   A CD  1 
ATOM   662  O  OE1 . GLU   A 1 82  ? 18.550 19.058  28.048 1.00 49.79  ? 88  GLU   A OE1 1 
ATOM   663  O  OE2 . GLU   A 1 82  ? 16.864 17.688  28.458 1.00 49.59  ? 88  GLU   A OE2 1 
ATOM   664  N  N   . TYR   A 1 83  ? 14.988 19.996  23.388 1.00 29.25  ? 89  TYR   A N   1 
ATOM   665  C  CA  . TYR   A 1 83  ? 15.817 20.283  22.215 1.00 29.62  ? 89  TYR   A CA  1 
ATOM   666  C  C   . TYR   A 1 83  ? 15.183 21.069  21.057 1.00 29.46  ? 89  TYR   A C   1 
ATOM   667  O  O   . TYR   A 1 83  ? 15.927 21.574  20.224 1.00 30.74  ? 89  TYR   A O   1 
ATOM   668  C  CB  . TYR   A 1 83  ? 16.363 18.958  21.674 1.00 30.08  ? 89  TYR   A CB  1 
ATOM   669  C  CG  . TYR   A 1 83  ? 17.235 18.234  22.681 1.00 31.82  ? 89  TYR   A CG  1 
ATOM   670  C  CD1 . TYR   A 1 83  ? 18.581 18.542  22.812 1.00 33.37  ? 89  TYR   A CD1 1 
ATOM   671  C  CD2 . TYR   A 1 83  ? 16.699 17.278  23.537 1.00 33.28  ? 89  TYR   A CD2 1 
ATOM   672  C  CE1 . TYR   A 1 83  ? 19.387 17.881  23.735 1.00 34.76  ? 89  TYR   A CE1 1 
ATOM   673  C  CE2 . TYR   A 1 83  ? 17.487 16.625  24.475 1.00 34.63  ? 89  TYR   A CE2 1 
ATOM   674  C  CZ  . TYR   A 1 83  ? 18.834 16.925  24.568 1.00 36.34  ? 89  TYR   A CZ  1 
ATOM   675  O  OH  . TYR   A 1 83  ? 19.622 16.271  25.488 1.00 39.63  ? 89  TYR   A OH  1 
ATOM   676  N  N   . TYR   A 1 84  ? 13.852 21.137  20.953 1.00 28.07  ? 90  TYR   A N   1 
ATOM   677  C  CA  . TYR   A 1 84  ? 13.203 21.871  19.854 1.00 27.27  ? 90  TYR   A CA  1 
ATOM   678  C  C   . TYR   A 1 84  ? 11.956 22.586  20.376 1.00 27.61  ? 90  TYR   A C   1 
ATOM   679  O  O   . TYR   A 1 84  ? 11.250 22.018  21.213 1.00 27.93  ? 90  TYR   A O   1 
ATOM   680  C  CB  . TYR   A 1 84  ? 12.725 20.900  18.734 1.00 26.21  ? 90  TYR   A CB  1 
ATOM   681  C  CG  . TYR   A 1 84  ? 13.796 20.098  18.030 1.00 25.83  ? 90  TYR   A CG  1 
ATOM   682  C  CD1 . TYR   A 1 84  ? 14.526 20.643  16.978 1.00 26.17  ? 90  TYR   A CD1 1 
ATOM   683  C  CD2 . TYR   A 1 84  ? 14.027 18.768  18.362 1.00 26.07  ? 90  TYR   A CD2 1 
ATOM   684  C  CE1 . TYR   A 1 84  ? 15.495 19.899  16.310 1.00 26.56  ? 90  TYR   A CE1 1 
ATOM   685  C  CE2 . TYR   A 1 84  ? 14.991 18.016  17.705 1.00 26.38  ? 90  TYR   A CE2 1 
ATOM   686  C  CZ  . TYR   A 1 84  ? 15.726 18.583  16.677 1.00 26.83  ? 90  TYR   A CZ  1 
ATOM   687  O  OH  . TYR   A 1 84  ? 16.687 17.835  16.038 1.00 26.26  ? 90  TYR   A OH  1 
ATOM   688  N  N   . PRO   A 1 85  ? 11.594 23.767  19.829 1.00 27.82  ? 91  PRO   A N   1 
ATOM   689  C  CA  . PRO   A 1 85  ? 10.270 24.344  20.166 1.00 27.29  ? 91  PRO   A CA  1 
ATOM   690  C  C   . PRO   A 1 85  ? 9.160  23.534  19.454 1.00 26.50  ? 91  PRO   A C   1 
ATOM   691  O  O   . PRO   A 1 85  ? 9.483  22.675  18.622 1.00 26.13  ? 91  PRO   A O   1 
ATOM   692  C  CB  . PRO   A 1 85  ? 10.357 25.771  19.589 1.00 28.38  ? 91  PRO   A CB  1 
ATOM   693  C  CG  . PRO   A 1 85  ? 11.239 25.620  18.384 1.00 28.88  ? 91  PRO   A CG  1 
ATOM   694  C  CD  . PRO   A 1 85  ? 12.264 24.530  18.745 1.00 27.64  ? 91  PRO   A CD  1 
ATOM   695  N  N   . ALA   A 1 86  ? 7.861  23.819  19.710 1.00 26.26  ? 92  ALA   A N   1 
ATOM   696  C  CA  . ALA   A 1 86  ? 6.769  23.094  19.025 1.00 26.27  ? 92  ALA   A CA  1 
ATOM   697  C  C   . ALA   A 1 86  ? 6.875  23.285  17.498 1.00 26.48  ? 92  ALA   A C   1 
ATOM   698  O  O   . ALA   A 1 86  ? 7.072  24.411  17.046 1.00 27.18  ? 92  ALA   A O   1 
ATOM   699  C  CB  . ALA   A 1 86  ? 5.418  23.592  19.521 1.00 26.91  ? 92  ALA   A CB  1 
ATOM   700  N  N   . ARG   A 1 87  ? 6.802  22.202  16.714 1.00 25.91  ? 93  ARG   A N   1 
ATOM   701  C  CA  . ARG   A 1 87  ? 6.945  22.319  15.249 1.00 26.27  ? 93  ARG   A CA  1 
ATOM   702  C  C   . ARG   A 1 87  ? 6.393  21.071  14.530 1.00 27.50  ? 93  ARG   A C   1 
ATOM   703  O  O   . ARG   A 1 87  ? 6.102  20.075  15.194 1.00 29.15  ? 93  ARG   A O   1 
ATOM   704  C  CB  . ARG   A 1 87  ? 8.455  22.524  14.883 1.00 25.84  ? 93  ARG   A CB  1 
ATOM   705  C  CG  . ARG   A 1 87  ? 9.273  21.211  14.804 1.00 25.96  ? 93  ARG   A CG  1 
ATOM   706  C  CD  . ARG   A 1 87  ? 10.733 21.289  15.246 1.00 26.53  ? 93  ARG   A CD  1 
ATOM   707  N  NE  . ARG   A 1 87  ? 11.564 20.167  14.757 1.00 27.20  ? 93  ARG   A NE  1 
ATOM   708  C  CZ  . ARG   A 1 87  ? 11.495 18.912  15.205 1.00 26.86  ? 93  ARG   A CZ  1 
ATOM   709  N  NH1 . ARG   A 1 87  ? 10.609 18.579  16.144 1.00 23.67  ? 93  ARG   A NH1 1 
ATOM   710  N  NH2 . ARG   A 1 87  ? 12.316 17.979  14.721 1.00 25.94  ? 93  ARG   A NH2 1 
ATOM   711  N  N   . TYR   A 1 88  ? 6.344  21.081  13.179 1.00 26.46  ? 94  TYR   A N   1 
ATOM   712  C  CA  . TYR   A 1 88  ? 6.000  19.877  12.435 1.00 26.74  ? 94  TYR   A CA  1 
ATOM   713  C  C   . TYR   A 1 88  ? 7.304  19.129  12.132 1.00 26.01  ? 94  TYR   A C   1 
ATOM   714  O  O   . TYR   A 1 88  ? 8.263  19.740  11.657 1.00 26.38  ? 94  TYR   A O   1 
ATOM   715  C  CB  . TYR   A 1 88  ? 5.319  20.228  11.110 1.00 27.10  ? 94  TYR   A CB  1 
ATOM   716  C  CG  . TYR   A 1 88  ? 3.877  20.629  11.295 1.00 27.88  ? 94  TYR   A CG  1 
ATOM   717  C  CD1 . TYR   A 1 88  ? 2.878  19.674  11.359 1.00 29.08  ? 94  TYR   A CD1 1 
ATOM   718  C  CD2 . TYR   A 1 88  ? 3.524  21.959  11.493 1.00 29.01  ? 94  TYR   A CD2 1 
ATOM   719  C  CE1 . TYR   A 1 88  ? 1.556  20.029  11.575 1.00 30.55  ? 94  TYR   A CE1 1 
ATOM   720  C  CE2 . TYR   A 1 88  ? 2.200  22.331  11.711 1.00 30.04  ? 94  TYR   A CE2 1 
ATOM   721  C  CZ  . TYR   A 1 88  ? 1.215  21.361  11.738 1.00 31.77  ? 94  TYR   A CZ  1 
ATOM   722  O  OH  . TYR   A 1 88  ? -0.098 21.703  11.959 1.00 34.05  ? 94  TYR   A OH  1 
ATOM   723  N  N   . GLN   A 1 89  ? 7.347  17.827  12.406 1.00 24.66  ? 95  GLN   A N   1 
ATOM   724  C  CA  . GLN   A 1 89  ? 8.528  17.017  12.105 1.00 24.08  ? 95  GLN   A CA  1 
ATOM   725  C  C   . GLN   A 1 89  ? 8.156  16.177  10.883 1.00 23.88  ? 95  GLN   A C   1 
ATOM   726  O  O   . GLN   A 1 89  ? 7.068  15.580  10.864 1.00 24.77  ? 95  GLN   A O   1 
ATOM   727  C  CB  . GLN   A 1 89  ? 8.955  16.115  13.298 1.00 25.17  ? 95  GLN   A CB  1 
ATOM   728  C  CG  . GLN   A 1 89  ? 10.192 15.234  12.960 1.00 27.08  ? 95  GLN   A CG  1 
ATOM   729  C  CD  . GLN   A 1 89  ? 10.925 14.637  14.153 1.00 25.15  ? 95  GLN   A CD  1 
ATOM   730  O  OE1 . GLN   A 1 89  ? 11.137 15.299  15.166 1.00 25.64  ? 95  GLN   A OE1 1 
ATOM   731  N  NE2 . GLN   A 1 89  ? 11.363 13.365  14.042 1.00 22.39  ? 95  GLN   A NE2 1 
ATOM   732  N  N   . SER   A 1 90  ? 9.001  16.195  9.837  1.00 22.66  ? 96  SER   A N   1 
ATOM   733  C  CA  . SER   A 1 90  ? 8.721  15.451  8.601  1.00 22.74  ? 96  SER   A CA  1 
ATOM   734  C  C   . SER   A 1 90  ? 9.352  14.034  8.601  1.00 23.37  ? 96  SER   A C   1 
ATOM   735  O  O   . SER   A 1 90  ? 10.263 13.755  9.401  1.00 23.40  ? 96  SER   A O   1 
ATOM   736  C  CB  . SER   A 1 90  ? 9.181  16.244  7.376  1.00 23.88  ? 96  SER   A CB  1 
ATOM   737  O  OG  . SER   A 1 90  ? 10.598 16.390  7.373  1.00 27.30  ? 96  SER   A OG  1 
ATOM   738  N  N   . HIS   A 1 91  ? 8.848  13.151  7.711  1.00 22.81  ? 97  HIS   A N   1 
ATOM   739  C  CA  . HIS   A 1 91  ? 9.330  11.771  7.545  1.00 23.21  ? 97  HIS   A CA  1 
ATOM   740  C  C   . HIS   A 1 91  ? 9.246  10.983  8.865  1.00 23.50  ? 97  HIS   A C   1 
ATOM   741  O  O   . HIS   A 1 91  ? 10.111 10.147  9.131  1.00 24.11  ? 97  HIS   A O   1 
ATOM   742  C  CB  . HIS   A 1 91  ? 10.768 11.752  6.981  1.00 23.94  ? 97  HIS   A CB  1 
ATOM   743  C  CG  . HIS   A 1 91  ? 10.913 12.471  5.669  1.00 26.43  ? 97  HIS   A CG  1 
ATOM   744  N  ND1 . HIS   A 1 91  ? 10.908 11.782  4.468  1.00 28.46  ? 97  HIS   A ND1 1 
ATOM   745  C  CD2 . HIS   A 1 91  ? 11.014 13.798  5.409  1.00 26.88  ? 97  HIS   A CD2 1 
ATOM   746  C  CE1 . HIS   A 1 91  ? 11.041 12.702  3.522  1.00 28.88  ? 97  HIS   A CE1 1 
ATOM   747  N  NE2 . HIS   A 1 91  ? 11.095 13.930  4.037  1.00 28.37  ? 97  HIS   A NE2 1 
ATOM   748  N  N   . LEU   A 1 92  ? 8.215  11.262  9.696  1.00 23.24  ? 98  LEU   A N   1 
ATOM   749  C  CA  . LEU   A 1 92  ? 8.044  10.611  11.004 1.00 23.41  ? 98  LEU   A CA  1 
ATOM   750  C  C   . LEU   A 1 92  ? 6.988  9.481   10.930 1.00 23.84  ? 98  LEU   A C   1 
ATOM   751  O  O   . LEU   A 1 92  ? 5.944  9.662   10.279 1.00 23.71  ? 98  LEU   A O   1 
ATOM   752  C  CB  . LEU   A 1 92  ? 7.616  11.666  12.041 1.00 24.12  ? 98  LEU   A CB  1 
ATOM   753  C  CG  . LEU   A 1 92  ? 7.448  11.228  13.516 1.00 25.94  ? 98  LEU   A CG  1 
ATOM   754  C  CD1 . LEU   A 1 92  ? 8.792  10.821  14.139 1.00 25.67  ? 98  LEU   A CD1 1 
ATOM   755  C  CD2 . LEU   A 1 92  ? 6.837  12.344  14.338 1.00 27.47  ? 98  LEU   A CD2 1 
ATOM   756  N  N   . MET   A 1 93  ? 7.249  8.331   11.614 1.00 22.92  ? 99  MET   A N   1 
ATOM   757  C  CA  . MET   A 1 93  ? 6.321  7.184   11.637 1.00 22.72  ? 99  MET   A CA  1 
ATOM   758  C  C   . MET   A 1 93  ? 5.923  6.880   13.104 1.00 22.71  ? 99  MET   A C   1 
ATOM   759  O  O   . MET   A 1 93  ? 6.795  6.917   13.972 1.00 22.22  ? 99  MET   A O   1 
ATOM   760  C  CB  . MET   A 1 93  ? 6.996  5.943   11.045 1.00 23.10  ? 99  MET   A CB  1 
ATOM   761  C  CG  . MET   A 1 93  ? 7.510  6.127   9.588  1.00 24.86  ? 99  MET   A CG  1 
ATOM   762  S  SD  . MET   A 1 93  ? 8.525  4.700   9.071  1.00 28.07  ? 99  MET   A SD  1 
ATOM   763  C  CE  . MET   A 1 93  ? 10.018 4.984   9.950  1.00 24.50  ? 99  MET   A CE  1 
ATOM   764  N  N   . LEU   A 1 94  ? 4.626  6.604   13.381 1.00 21.97  ? 100 LEU   A N   1 
ATOM   765  C  CA  . LEU   A 1 94  ? 4.197  6.306   14.749 1.00 21.82  ? 100 LEU   A CA  1 
ATOM   766  C  C   . LEU   A 1 94  ? 3.754  4.852   14.919 1.00 22.18  ? 100 LEU   A C   1 
ATOM   767  O  O   . LEU   A 1 94  ? 3.205  4.214   14.003 1.00 21.76  ? 100 LEU   A O   1 
ATOM   768  C  CB  . LEU   A 1 94  ? 3.023  7.211   15.186 1.00 22.21  ? 100 LEU   A CB  1 
ATOM   769  C  CG  . LEU   A 1 94  ? 3.236  8.730   15.134 1.00 23.63  ? 100 LEU   A CG  1 
ATOM   770  C  CD1 . LEU   A 1 94  ? 1.960  9.481   15.527 1.00 25.07  ? 100 LEU   A CD1 1 
ATOM   771  C  CD2 . LEU   A 1 94  ? 4.390  9.153   15.980 1.00 23.65  ? 100 LEU   A CD2 1 
ATOM   772  N  N   . ALA   A 1 95  ? 3.900  4.385   16.140 1.00 21.87  ? 101 ALA   A N   1 
ATOM   773  C  CA  . ALA   A 1 95  ? 3.448  3.078   16.597 1.00 22.35  ? 101 ALA   A CA  1 
ATOM   774  C  C   . ALA   A 1 95  ? 2.937  3.244   18.047 1.00 22.31  ? 101 ALA   A C   1 
ATOM   775  O  O   . ALA   A 1 95  ? 3.252  4.241   18.729 1.00 21.07  ? 101 ALA   A O   1 
ATOM   776  C  CB  . ALA   A 1 95  ? 4.603  2.067   16.557 1.00 22.36  ? 101 ALA   A CB  1 
ATOM   777  N  N   . VAL   A 1 96  ? 2.124  2.289   18.483 1.00 22.11  ? 102 VAL   A N   1 
ATOM   778  C  CA  . VAL   A 1 96  ? 1.628  2.236   19.851 1.00 22.80  ? 102 VAL   A CA  1 
ATOM   779  C  C   . VAL   A 1 96  ? 2.713  1.506   20.649 1.00 23.80  ? 102 VAL   A C   1 
ATOM   780  O  O   . VAL   A 1 96  ? 2.926  0.296   20.470 1.00 23.58  ? 102 VAL   A O   1 
ATOM   781  C  CB  . VAL   A 1 96  ? 0.270  1.499   19.943 1.00 23.79  ? 102 VAL   A CB  1 
ATOM   782  C  CG1 . VAL   A 1 96  ? -0.173 1.356   21.404 1.00 24.87  ? 102 VAL   A CG1 1 
ATOM   783  C  CG2 . VAL   A 1 96  ? -0.801 2.241   19.129 1.00 24.20  ? 102 VAL   A CG2 1 
ATOM   784  N  N   . GLY   A 1 97  ? 3.407  2.241   21.500 1.00 24.49  ? 103 GLY   A N   1 
ATOM   785  C  CA  . GLY   A 1 97  ? 4.466  1.658   22.313 1.00 24.93  ? 103 GLY   A CA  1 
ATOM   786  C  C   . GLY   A 1 97  ? 5.101  2.644   23.275 1.00 25.33  ? 103 GLY   A C   1 
ATOM   787  O  O   . GLY   A 1 97  ? 4.743  3.832   23.286 1.00 25.28  ? 103 GLY   A O   1 
ATOM   788  N  N   . HIS   A 1 98  ? 6.052  2.159   24.097 1.00 24.52  ? 104 HIS   A N   1 
ATOM   789  C  CA  . HIS   A 1 98  ? 6.670  3.000   25.113 1.00 24.98  ? 104 HIS   A CA  1 
ATOM   790  C  C   . HIS   A 1 98  ? 7.912  3.717   24.607 1.00 23.90  ? 104 HIS   A C   1 
ATOM   791  O  O   . HIS   A 1 98  ? 8.740  3.112   23.934 1.00 24.67  ? 104 HIS   A O   1 
ATOM   792  C  CB  . HIS   A 1 98  ? 6.954  2.204   26.416 1.00 25.56  ? 104 HIS   A CB  1 
ATOM   793  C  CG  . HIS   A 1 98  ? 7.588  3.029   27.508 1.00 28.08  ? 104 HIS   A CG  1 
ATOM   794  N  ND1 . HIS   A 1 98  ? 6.861  3.972   28.227 1.00 29.72  ? 104 HIS   A ND1 1 
ATOM   795  C  CD2 . HIS   A 1 98  ? 8.869  3.032   27.957 1.00 28.86  ? 104 HIS   A CD2 1 
ATOM   796  C  CE1 . HIS   A 1 98  ? 7.721  4.511   29.079 1.00 30.25  ? 104 HIS   A CE1 1 
ATOM   797  N  NE2 . HIS   A 1 98  ? 8.942  3.974   28.953 1.00 29.66  ? 104 HIS   A NE2 1 
ATOM   798  N  N   . SER   A 1 99  ? 8.074  4.977   24.986 1.00 22.60  ? 105 SER   A N   1 
ATOM   799  C  CA  . SER   A 1 99  ? 9.216  5.757   24.563 1.00 22.81  ? 105 SER   A CA  1 
ATOM   800  C  C   . SER   A 1 99  ? 9.442  6.935   25.514 1.00 23.02  ? 105 SER   A C   1 
ATOM   801  O  O   . SER   A 1 99  ? 8.512  7.707   25.768 1.00 22.61  ? 105 SER   A O   1 
ATOM   802  C  CB  . SER   A 1 99  ? 8.956  6.302   23.153 1.00 24.59  ? 105 SER   A CB  1 
ATOM   803  O  OG  . SER   A 1 99  ? 10.024 7.089   22.659 1.00 28.42  ? 105 SER   A OG  1 
ATOM   804  N  N   . GLU   A 1 100 ? 10.691 7.098   25.984 1.00 22.91  ? 106 GLU   A N   1 
ATOM   805  C  CA  . GLU   A 1 100 ? 11.131 8.201   26.831 1.00 24.10  ? 106 GLU   A CA  1 
ATOM   806  C  C   . GLU   A 1 100 ? 12.291 8.942   26.132 1.00 25.12  ? 106 GLU   A C   1 
ATOM   807  O  O   . GLU   A 1 100 ? 12.934 8.375   25.243 1.00 24.77  ? 106 GLU   A O   1 
ATOM   808  C  CB  . GLU   A 1 100 ? 11.535 7.687   28.236 1.00 27.08  ? 106 GLU   A CB  1 
ATOM   809  C  CG  . GLU   A 1 100 ? 10.380 7.048   28.995 1.00 32.11  ? 106 GLU   A CG  1 
ATOM   810  C  CD  . GLU   A 1 100 ? 10.755 6.395   30.318 1.00 38.28  ? 106 GLU   A CD  1 
ATOM   811  O  OE1 . GLU   A 1 100 ? 11.716 6.867   30.968 1.00 38.10  ? 106 GLU   A OE1 1 
ATOM   812  O  OE2 . GLU   A 1 100 ? 10.082 5.414   30.711 1.00 40.01  ? 106 GLU   A OE2 1 
ATOM   813  N  N   . PRO   A 1 101 ? 12.550 10.233  26.448 1.00 25.69  ? 107 PRO   A N   1 
ATOM   814  C  CA  . PRO   A 1 101 ? 13.614 10.964  25.721 1.00 25.38  ? 107 PRO   A CA  1 
ATOM   815  C  C   . PRO   A 1 101 ? 14.957 10.215  25.521 1.00 24.09  ? 107 PRO   A C   1 
ATOM   816  O  O   . PRO   A 1 101 ? 15.525 10.217  24.411 1.00 23.82  ? 107 PRO   A O   1 
ATOM   817  C  CB  . PRO   A 1 101 ? 13.777 12.250  26.538 1.00 26.47  ? 107 PRO   A CB  1 
ATOM   818  C  CG  . PRO   A 1 101 ? 12.397 12.494  27.122 1.00 27.05  ? 107 PRO   A CG  1 
ATOM   819  C  CD  . PRO   A 1 101 ? 11.848 11.106  27.422 1.00 25.88  ? 107 PRO   A CD  1 
ATOM   820  N  N   . GLY   A 1 102 ? 15.445 9.556   26.567 1.00 23.12  ? 108 GLY   A N   1 
ATOM   821  C  CA  . GLY   A 1 102 ? 16.707 8.822   26.502 1.00 23.01  ? 108 GLY   A CA  1 
ATOM   822  C  C   . GLY   A 1 102 ? 16.661 7.588   25.618 1.00 22.90  ? 108 GLY   A C   1 
ATOM   823  O  O   . GLY   A 1 102 ? 17.697 6.983   25.360 1.00 23.24  ? 108 GLY   A O   1 
ATOM   824  N  N   . ASP   A 1 103 ? 15.459 7.190   25.142 1.00 22.13  ? 109 ASP   A N   1 
ATOM   825  C  CA  . ASP   A 1 103 ? 15.303 6.074   24.213 1.00 22.25  ? 109 ASP   A CA  1 
ATOM   826  C  C   . ASP   A 1 103 ? 15.644 6.471   22.757 1.00 22.12  ? 109 ASP   A C   1 
ATOM   827  O  O   . ASP   A 1 103 ? 15.758 5.584   21.904 1.00 21.86  ? 109 ASP   A O   1 
ATOM   828  C  CB  . ASP   A 1 103 ? 13.875 5.511   24.256 1.00 23.17  ? 109 ASP   A CB  1 
ATOM   829  C  CG  . ASP   A 1 103 ? 13.572 4.768   25.542 1.00 25.64  ? 109 ASP   A CG  1 
ATOM   830  O  OD1 . ASP   A 1 103 ? 14.449 4.007   26.008 1.00 25.14  ? 109 ASP   A OD1 1 
ATOM   831  O  OD2 . ASP   A 1 103 ? 12.438 4.908   26.052 1.00 26.43  ? 109 ASP   A OD2 1 
ATOM   832  N  N   . CYS   A 1 104 ? 15.803 7.799   22.458 1.00 21.51  ? 110 CYS   A N   1 
ATOM   833  C  CA  . CYS   A 1 104 ? 16.149 8.257   21.096 1.00 21.37  ? 110 CYS   A CA  1 
ATOM   834  C  C   . CYS   A 1 104 ? 17.421 7.565   20.611 1.00 22.10  ? 110 CYS   A C   1 
ATOM   835  O  O   . CYS   A 1 104 ? 18.358 7.429   21.388 1.00 22.19  ? 110 CYS   A O   1 
ATOM   836  C  CB  . CYS   A 1 104 ? 16.286 9.776   21.036 1.00 22.33  ? 110 CYS   A CB  1 
ATOM   837  S  SG  . CYS   A 1 104 ? 14.711 10.667  21.191 1.00 25.11  ? 110 CYS   A SG  1 
ATOM   838  N  N   . GLY   A 1 105 ? 17.436 7.099   19.365 1.00 22.15  ? 111 GLY   A N   1 
ATOM   839  C  CA  . GLY   A 1 105 ? 18.582 6.361   18.848 1.00 22.29  ? 111 GLY   A CA  1 
ATOM   840  C  C   . GLY   A 1 105 ? 18.309 4.862   18.727 1.00 22.61  ? 111 GLY   A C   1 
ATOM   841  O  O   . GLY   A 1 105 ? 18.988 4.178   17.949 1.00 22.85  ? 111 GLY   A O   1 
ATOM   842  N  N   . GLY   A 1 106 ? 17.309 4.347   19.466 1.00 21.91  ? 112 GLY   A N   1 
ATOM   843  C  CA  . GLY   A 1 106 ? 16.910 2.934   19.394 1.00 21.54  ? 112 GLY   A CA  1 
ATOM   844  C  C   . GLY   A 1 106 ? 16.510 2.566   17.966 1.00 21.36  ? 112 GLY   A C   1 
ATOM   845  O  O   . GLY   A 1 106 ? 15.786 3.321   17.317 1.00 20.14  ? 112 GLY   A O   1 
ATOM   846  N  N   . ILE   A 1 107 ? 17.026 1.455   17.431 1.00 21.46  ? 113 ILE   A N   1 
ATOM   847  C  CA  . ILE   A 1 107 ? 16.758 1.079   16.046 1.00 23.00  ? 113 ILE   A CA  1 
ATOM   848  C  C   . ILE   A 1 107 ? 15.414 0.342   15.851 1.00 23.30  ? 113 ILE   A C   1 
ATOM   849  O  O   . ILE   A 1 107 ? 15.020 -0.489  16.674 1.00 23.46  ? 113 ILE   A O   1 
ATOM   850  C  CB  . ILE   A 1 107 ? 17.964 0.277   15.449 1.00 24.42  ? 113 ILE   A CB  1 
ATOM   851  C  CG1 . ILE   A 1 107 ? 19.127 1.229   15.066 1.00 25.95  ? 113 ILE   A CG1 1 
ATOM   852  C  CG2 . ILE   A 1 107 ? 17.581 -0.602  14.244 1.00 25.43  ? 113 ILE   A CG2 1 
ATOM   853  C  CD1 . ILE   A 1 107 ? 20.460 0.476   14.739 1.00 27.67  ? 113 ILE   A CD1 1 
ATOM   854  N  N   . LEU   A 1 108 ? 14.732 0.676   14.741 1.00 22.65  ? 114 LEU   A N   1 
ATOM   855  C  CA  . LEU   A 1 108 ? 13.521 0.008   14.268 1.00 22.13  ? 114 LEU   A CA  1 
ATOM   856  C  C   . LEU   A 1 108 ? 13.979 -0.784  13.019 1.00 21.98  ? 114 LEU   A C   1 
ATOM   857  O  O   . LEU   A 1 108 ? 14.542 -0.184  12.090 1.00 21.66  ? 114 LEU   A O   1 
ATOM   858  C  CB  . LEU   A 1 108 ? 12.453 1.036   13.858 1.00 21.43  ? 114 LEU   A CB  1 
ATOM   859  C  CG  . LEU   A 1 108 ? 11.270 0.464   13.059 1.00 22.93  ? 114 LEU   A CG  1 
ATOM   860  C  CD1 . LEU   A 1 108 ? 10.474 -0.603  13.883 1.00 23.83  ? 114 LEU   A CD1 1 
ATOM   861  C  CD2 . LEU   A 1 108 ? 10.385 1.596   12.516 1.00 23.98  ? 114 LEU   A CD2 1 
ATOM   862  N  N   . ARG   A 1 109 ? 13.712 -2.096  12.989 1.00 22.12  ? 115 ARG   A N   1 
ATOM   863  C  CA  . ARG   A 1 109 ? 14.136 -2.888  11.858 1.00 23.18  ? 115 ARG   A CA  1 
ATOM   864  C  C   . ARG   A 1 109 ? 13.066 -3.886  11.365 1.00 22.93  ? 115 ARG   A C   1 
ATOM   865  O  O   . ARG   A 1 109 ? 12.272 -4.391  12.147 1.00 21.99  ? 115 ARG   A O   1 
ATOM   866  C  CB  . ARG   A 1 109 ? 15.493 -3.554  12.139 1.00 26.01  ? 115 ARG   A CB  1 
ATOM   867  C  CG  . ARG   A 1 109 ? 15.495 -4.793  13.000 1.00 31.30  ? 115 ARG   A CG  1 
ATOM   868  C  CD  . ARG   A 1 109 ? 16.827 -5.558  12.837 1.00 35.16  ? 115 ARG   A CD  1 
ATOM   869  N  NE  . ARG   A 1 109 ? 17.999 -4.784  13.274 1.00 38.11  ? 115 ARG   A NE  1 
ATOM   870  C  CZ  . ARG   A 1 109 ? 19.022 -4.452  12.484 1.00 39.20  ? 115 ARG   A CZ  1 
ATOM   871  N  NH1 . ARG   A 1 109 ? 19.007 -4.770  11.195 1.00 38.23  ? 115 ARG   A NH1 1 
ATOM   872  N  NH2 . ARG   A 1 109 ? 20.044 -3.757  12.967 1.00 37.60  ? 115 ARG   A NH2 1 
ATOM   873  N  N   . CYS   A 1 110 ? 13.024 -4.108  10.044 1.00 22.80  ? 116 CYS   A N   1 
ATOM   874  C  CA  . CYS   A 1 110 ? 12.090 -5.067  9.434  1.00 23.68  ? 116 CYS   A CA  1 
ATOM   875  C  C   . CYS   A 1 110 ? 12.957 -6.255  8.827  1.00 24.82  ? 116 CYS   A C   1 
ATOM   876  O  O   . CYS   A 1 110 ? 14.175 -6.307  9.038  1.00 24.86  ? 116 CYS   A O   1 
ATOM   877  C  CB  . CYS   A 1 110 ? 11.293 -4.353  8.345  1.00 23.64  ? 116 CYS   A CB  1 
ATOM   878  S  SG  . CYS   A 1 110 ? 12.339 -3.786  6.976  1.00 26.84  ? 116 CYS   A SG  1 
ATOM   879  N  N   . GLN   A 1 111 ? 12.349 -7.152  8.044  1.00 26.14  ? 117 GLN   A N   1 
ATOM   880  C  CA  . GLN   A 1 111 ? 13.087 -8.252  7.405  1.00 27.89  ? 117 GLN   A CA  1 
ATOM   881  C  C   . GLN   A 1 111 ? 14.144 -7.782  6.402  1.00 28.50  ? 117 GLN   A C   1 
ATOM   882  O  O   . GLN   A 1 111 ? 15.050 -8.542  6.094  1.00 29.65  ? 117 GLN   A O   1 
ATOM   883  C  CB  . GLN   A 1 111 ? 12.123 -9.242  6.705  1.00 30.42  ? 117 GLN   A CB  1 
ATOM   884  C  CG  . GLN   A 1 111 ? 11.412 -8.645  5.496  1.00 34.89  ? 117 GLN   A CG  1 
ATOM   885  C  CD  . GLN   A 1 111 ? 10.486 -9.619  4.804  1.00 40.46  ? 117 GLN   A CD  1 
ATOM   886  O  OE1 . GLN   A 1 111 ? 9.252  -9.534  4.923  1.00 41.92  ? 117 GLN   A OE1 1 
ATOM   887  N  NE2 . GLN   A 1 111 ? 11.060 -10.562 4.065  1.00 40.32  ? 117 GLN   A NE2 1 
ATOM   888  N  N   . HIS   A 1 112 ? 14.050 -6.527  5.911  1.00 28.12  ? 118 HIS   A N   1 
ATOM   889  C  CA  . HIS   A 1 112 ? 14.970 -5.975  4.903  1.00 28.45  ? 118 HIS   A CA  1 
ATOM   890  C  C   . HIS   A 1 112 ? 16.154 -5.183  5.482  1.00 28.29  ? 118 HIS   A C   1 
ATOM   891  O  O   . HIS   A 1 112 ? 17.091 -4.868  4.757  1.00 29.47  ? 118 HIS   A O   1 
ATOM   892  C  CB  . HIS   A 1 112 ? 14.179 -5.106  3.909  1.00 29.08  ? 118 HIS   A CB  1 
ATOM   893  C  CG  . HIS   A 1 112 ? 13.017 -5.824  3.277  1.00 31.46  ? 118 HIS   A CG  1 
ATOM   894  N  ND1 . HIS   A 1 112 ? 11.705 -5.505  3.598  1.00 33.02  ? 118 HIS   A ND1 1 
ATOM   895  C  CD2 . HIS   A 1 112 ? 13.009 -6.841  2.381  1.00 32.55  ? 118 HIS   A CD2 1 
ATOM   896  C  CE1 . HIS   A 1 112 ? 10.948 -6.313  2.874  1.00 32.83  ? 118 HIS   A CE1 1 
ATOM   897  N  NE2 . HIS   A 1 112 ? 11.686 -7.140  2.132  1.00 33.34  ? 118 HIS   A NE2 1 
ATOM   898  N  N   . GLY   A 1 113 ? 16.083 -4.821  6.757  1.00 26.63  ? 119 GLY   A N   1 
ATOM   899  C  CA  . GLY   A 1 113 ? 17.143 -4.063  7.402  1.00 24.97  ? 119 GLY   A CA  1 
ATOM   900  C  C   . GLY   A 1 113 ? 16.626 -2.951  8.296  1.00 23.64  ? 119 GLY   A C   1 
ATOM   901  O  O   . GLY   A 1 113 ? 15.488 -3.001  8.784  1.00 22.94  ? 119 GLY   A O   1 
ATOM   902  N  N   . VAL   A 1 114 ? 17.471 -1.945  8.517  1.00 21.94  ? 120 VAL   A N   1 
ATOM   903  C  CA  . VAL   A 1 114 ? 17.149 -0.805  9.361  1.00 21.28  ? 120 VAL   A CA  1 
ATOM   904  C  C   . VAL   A 1 114 ? 16.152 0.104   8.660  1.00 20.00  ? 120 VAL   A C   1 
ATOM   905  O  O   . VAL   A 1 114 ? 16.381 0.486   7.506  1.00 19.87  ? 120 VAL   A O   1 
ATOM   906  C  CB  . VAL   A 1 114 ? 18.441 -0.039  9.717  1.00 22.71  ? 120 VAL   A CB  1 
ATOM   907  C  CG1 . VAL   A 1 114 ? 18.124 1.253   10.466 1.00 23.74  ? 120 VAL   A CG1 1 
ATOM   908  C  CG2 . VAL   A 1 114 ? 19.394 -0.923  10.520 1.00 23.92  ? 120 VAL   A CG2 1 
ATOM   909  N  N   . VAL   A 1 115 ? 15.048 0.442   9.348  1.00 19.06  ? 121 VAL   A N   1 
ATOM   910  C  CA  . VAL   A 1 115 ? 13.980 1.313   8.850  1.00 19.19  ? 121 VAL   A CA  1 
ATOM   911  C  C   . VAL   A 1 115 ? 14.135 2.763   9.355  1.00 19.93  ? 121 VAL   A C   1 
ATOM   912  O  O   . VAL   A 1 115 ? 13.874 3.718   8.612  1.00 20.51  ? 121 VAL   A O   1 
ATOM   913  C  CB  . VAL   A 1 115 ? 12.603 0.750   9.249  1.00 19.89  ? 121 VAL   A CB  1 
ATOM   914  C  CG1 . VAL   A 1 115 ? 11.457 1.668   8.807  1.00 20.41  ? 121 VAL   A CG1 1 
ATOM   915  C  CG2 . VAL   A 1 115 ? 12.411 -0.662  8.724  1.00 20.45  ? 121 VAL   A CG2 1 
ATOM   916  N  N   . GLY   A 1 116 ? 14.525 2.911   10.625 1.00 19.67  ? 122 GLY   A N   1 
ATOM   917  C  CA  . GLY   A 1 116 ? 14.684 4.224   11.242 1.00 19.94  ? 122 GLY   A CA  1 
ATOM   918  C  C   . GLY   A 1 116 ? 15.146 4.154   12.691 1.00 20.62  ? 122 GLY   A C   1 
ATOM   919  O  O   . GLY   A 1 116 ? 15.514 3.074   13.181 1.00 20.88  ? 122 GLY   A O   1 
ATOM   920  N  N   . ILE   A 1 117 ? 15.130 5.304   13.394 1.00 19.86  ? 123 ILE   A N   1 
ATOM   921  C  CA  . ILE   A 1 117 ? 15.533 5.379   14.799 1.00 20.55  ? 123 ILE   A CA  1 
ATOM   922  C  C   . ILE   A 1 117 ? 14.496 6.154   15.645 1.00 20.19  ? 123 ILE   A C   1 
ATOM   923  O  O   . ILE   A 1 117 ? 13.845 7.048   15.124 1.00 20.62  ? 123 ILE   A O   1 
ATOM   924  C  CB  . ILE   A 1 117 ? 16.950 6.002   14.973 1.00 21.94  ? 123 ILE   A CB  1 
ATOM   925  C  CG1 . ILE   A 1 117 ? 17.037 7.396   14.303 1.00 22.19  ? 123 ILE   A CG1 1 
ATOM   926  C  CG2 . ILE   A 1 117 ? 18.074 5.051   14.523 1.00 23.31  ? 123 ILE   A CG2 1 
ATOM   927  C  CD1 . ILE   A 1 117 ? 18.380 8.128   14.561 1.00 23.26  ? 123 ILE   A CD1 1 
ATOM   928  N  N   . VAL   A 1 118 ? 14.348 5.808   16.946 1.00 19.76  ? 124 VAL   A N   1 
ATOM   929  C  CA  . VAL   A 1 118 ? 13.417 6.493   17.841 1.00 20.11  ? 124 VAL   A CA  1 
ATOM   930  C  C   . VAL   A 1 118 ? 13.759 8.000   17.909 1.00 19.31  ? 124 VAL   A C   1 
ATOM   931  O  O   . VAL   A 1 118 ? 14.934 8.363   18.069 1.00 17.59  ? 124 VAL   A O   1 
ATOM   932  C  CB  . VAL   A 1 118 ? 13.444 5.846   19.242 1.00 22.16  ? 124 VAL   A CB  1 
ATOM   933  C  CG1 . VAL   A 1 118 ? 12.575 6.633   20.225 1.00 23.37  ? 124 VAL   A CG1 1 
ATOM   934  C  CG2 . VAL   A 1 118 ? 13.005 4.379   19.168 1.00 22.89  ? 124 VAL   A CG2 1 
ATOM   935  N  N   . SER   A 1 119 ? 12.745 8.858   17.739 1.00 19.80  ? 125 SER   A N   1 
ATOM   936  C  CA  . SER   A 1 119 ? 12.950 10.310  17.742 1.00 20.91  ? 125 SER   A CA  1 
ATOM   937  C  C   . SER   A 1 119 ? 11.920 11.048  18.625 1.00 22.30  ? 125 SER   A C   1 
ATOM   938  O  O   . SER   A 1 119 ? 12.227 12.130  19.162 1.00 22.04  ? 125 SER   A O   1 
ATOM   939  C  CB  . SER   A 1 119 ? 12.907 10.848  16.308 1.00 20.86  ? 125 SER   A CB  1 
ATOM   940  O  OG  . SER   A 1 119 ? 12.968 12.268  16.255 1.00 21.92  ? 125 SER   A OG  1 
ATOM   941  N  N   . THR   A 1 120 ? 10.674 10.499  18.738 1.00 23.30  ? 126 THR   A N   1 
ATOM   942  C  CA  . THR   A 1 120 ? 9.606  11.124  19.551 1.00 25.02  ? 126 THR   A CA  1 
ATOM   943  C  C   . THR   A 1 120 ? 8.872  10.114  20.484 1.00 25.88  ? 126 THR   A C   1 
ATOM   944  O  O   . THR   A 1 120 ? 9.060  8.906   20.361 1.00 25.73  ? 126 THR   A O   1 
ATOM   945  C  CB  . THR   A 1 120 ? 8.579  11.880  18.628 1.00 26.91  ? 126 THR   A CB  1 
ATOM   946  O  OG1 . THR   A 1 120 ? 7.717  10.926  18.000 1.00 28.12  ? 126 THR   A OG1 1 
ATOM   947  C  CG2 . THR   A 1 120 ? 9.228  12.786  17.605 1.00 27.20  ? 126 THR   A CG2 1 
ATOM   948  N  N   . GLY   A 1 121 ? 7.996  10.611  21.364 1.00 27.19  ? 127 GLY   A N   1 
ATOM   949  C  CA  . GLY   A 1 121 ? 7.223  9.748   22.249 1.00 28.15  ? 127 GLY   A CA  1 
ATOM   950  C  C   . GLY   A 1 121 ? 6.270  10.503  23.147 1.00 29.04  ? 127 GLY   A C   1 
ATOM   951  O  O   . GLY   A 1 121 ? 6.233  11.734  23.138 1.00 28.93  ? 127 GLY   A O   1 
ATOM   952  N  N   . GLY   A 1 122 ? 5.522  9.756   23.943 1.00 29.38  ? 128 GLY   A N   1 
ATOM   953  C  CA  . GLY   A 1 122 ? 4.543  10.309  24.867 1.00 29.94  ? 128 GLY   A CA  1 
ATOM   954  C  C   . GLY   A 1 122 ? 3.150  9.821   24.532 1.00 30.04  ? 128 GLY   A C   1 
ATOM   955  O  O   . GLY   A 1 122 ? 2.885  9.444   23.385 1.00 29.95  ? 128 GLY   A O   1 
ATOM   956  N  N   . ASN   A 1 123 ? 2.256  9.793   25.542 1.00 29.99  ? 129 ASN   A N   1 
ATOM   957  C  CA  . ASN   A 1 123 ? 0.853  9.390   25.377 1.00 30.36  ? 129 ASN   A CA  1 
ATOM   958  C  C   . ASN   A 1 123 ? 0.664  7.943   24.917 1.00 29.30  ? 129 ASN   A C   1 
ATOM   959  O  O   . ASN   A 1 123 ? -0.347 7.634   24.293 1.00 30.17  ? 129 ASN   A O   1 
ATOM   960  C  CB  . ASN   A 1 123 ? 0.115  10.339  24.416 1.00 32.70  ? 129 ASN   A CB  1 
ATOM   961  C  CG  . ASN   A 1 123 ? 0.040  11.763  24.906 1.00 37.81  ? 129 ASN   A CG  1 
ATOM   962  O  OD1 . ASN   A 1 123 ? -0.033 12.023  26.115 1.00 39.50  ? 129 ASN   A OD1 1 
ATOM   963  N  ND2 . ASN   A 1 123 ? 0.033  12.721  23.972 1.00 38.61  ? 129 ASN   A ND2 1 
ATOM   964  N  N   . GLY   A 1 124 ? 1.611  7.073   25.230 1.00 27.40  ? 130 GLY   A N   1 
ATOM   965  C  CA  . GLY   A 1 124 ? 1.527  5.674   24.803 1.00 26.19  ? 130 GLY   A CA  1 
ATOM   966  C  C   . GLY   A 1 124 ? 1.895  5.459   23.337 1.00 25.26  ? 130 GLY   A C   1 
ATOM   967  O  O   . GLY   A 1 124 ? 1.629  4.396   22.771 1.00 25.06  ? 130 GLY   A O   1 
ATOM   968  N  N   . LEU   A 1 125 ? 2.545  6.446   22.718 1.00 23.87  ? 131 LEU   A N   1 
ATOM   969  C  CA  . LEU   A 1 125 ? 2.999  6.351   21.344 1.00 23.59  ? 131 LEU   A CA  1 
ATOM   970  C  C   . LEU   A 1 125 ? 4.537  6.471   21.268 1.00 23.62  ? 131 LEU   A C   1 
ATOM   971  O  O   . LEU   A 1 125 ? 5.151  7.081   22.146 1.00 25.00  ? 131 LEU   A O   1 
ATOM   972  C  CB  . LEU   A 1 125 ? 2.344  7.464   20.518 1.00 24.02  ? 131 LEU   A CB  1 
ATOM   973  C  CG  . LEU   A 1 125 ? 0.815  7.342   20.449 1.00 26.23  ? 131 LEU   A CG  1 
ATOM   974  C  CD1 . LEU   A 1 125 ? 0.193  8.631   20.044 1.00 28.24  ? 131 LEU   A CD1 1 
ATOM   975  C  CD2 . LEU   A 1 125 ? 0.400  6.203   19.555 1.00 26.04  ? 131 LEU   A CD2 1 
ATOM   976  N  N   . VAL   A 1 126 ? 5.145  5.898   20.210 1.00 21.65  ? 132 VAL   A N   1 
ATOM   977  C  CA  . VAL   A 1 126 ? 6.579  6.001   19.929 1.00 20.66  ? 132 VAL   A CA  1 
ATOM   978  C  C   . VAL   A 1 126 ? 6.699  6.441   18.455 1.00 20.10  ? 132 VAL   A C   1 
ATOM   979  O  O   . VAL   A 1 126 ? 5.912  6.008   17.603 1.00 19.36  ? 132 VAL   A O   1 
ATOM   980  C  CB  . VAL   A 1 126 ? 7.380  4.697   20.235 1.00 20.59  ? 132 VAL   A CB  1 
ATOM   981  C  CG1 . VAL   A 1 126 ? 6.740  3.467   19.588 1.00 20.04  ? 132 VAL   A CG1 1 
ATOM   982  C  CG2 . VAL   A 1 126 ? 8.863  4.832   19.839 1.00 21.13  ? 132 VAL   A CG2 1 
ATOM   983  N  N   . GLY   A 1 127 ? 7.606  7.375   18.184 1.00 20.55  ? 133 GLY   A N   1 
ATOM   984  C  CA  . GLY   A 1 127 ? 7.801  7.866   16.826 1.00 20.21  ? 133 GLY   A CA  1 
ATOM   985  C  C   . GLY   A 1 127 ? 9.213  7.611   16.356 1.00 21.23  ? 133 GLY   A C   1 
ATOM   986  O  O   . GLY   A 1 127 ? 10.157 7.764   17.135 1.00 21.75  ? 133 GLY   A O   1 
ATOM   987  N  N   . PHE   A 1 128 ? 9.372  7.249   15.072 1.00 20.99  ? 134 PHE   A N   1 
ATOM   988  C  CA  . PHE   A 1 128 ? 10.655 6.897   14.465 1.00 20.63  ? 134 PHE   A CA  1 
ATOM   989  C  C   . PHE   A 1 128 ? 10.923 7.781   13.234 1.00 20.78  ? 134 PHE   A C   1 
ATOM   990  O  O   . PHE   A 1 128 ? 10.004 8.007   12.424 1.00 20.06  ? 134 PHE   A O   1 
ATOM   991  C  CB  . PHE   A 1 128 ? 10.616 5.413   14.003 1.00 20.35  ? 134 PHE   A CB  1 
ATOM   992  C  CG  . PHE   A 1 128 ? 10.119 4.421   15.041 1.00 20.05  ? 134 PHE   A CG  1 
ATOM   993  C  CD1 . PHE   A 1 128 ? 10.997 3.837   15.944 1.00 20.17  ? 134 PHE   A CD1 1 
ATOM   994  C  CD2 . PHE   A 1 128 ? 8.783  4.042   15.081 1.00 20.61  ? 134 PHE   A CD2 1 
ATOM   995  C  CE1 . PHE   A 1 128 ? 10.549 2.908   16.882 1.00 20.41  ? 134 PHE   A CE1 1 
ATOM   996  C  CE2 . PHE   A 1 128 ? 8.339  3.100   16.012 1.00 21.32  ? 134 PHE   A CE2 1 
ATOM   997  C  CZ  . PHE   A 1 128 ? 9.223  2.555   16.916 1.00 20.96  ? 134 PHE   A CZ  1 
ATOM   998  N  N   . ALA   A 1 129 ? 12.185 8.277   13.102 1.00 20.12  ? 135 ALA   A N   1 
ATOM   999  C  CA  . ALA   A 1 129 ? 12.623 9.066   11.955 1.00 20.69  ? 135 ALA   A CA  1 
ATOM   1000 C  C   . ALA   A 1 129 ? 12.989 8.060   10.851 1.00 21.29  ? 135 ALA   A C   1 
ATOM   1001 O  O   . ALA   A 1 129 ? 13.926 7.278   11.028 1.00 20.12  ? 135 ALA   A O   1 
ATOM   1002 C  CB  . ALA   A 1 129 ? 13.860 9.892   12.323 1.00 20.48  ? 135 ALA   A CB  1 
ATOM   1003 N  N   . ASP   A 1 130 ? 12.283 8.100   9.712  1.00 22.10  ? 136 ASP   A N   1 
ATOM   1004 C  CA  . ASP   A 1 130 ? 12.583 7.187   8.584  1.00 22.57  ? 136 ASP   A CA  1 
ATOM   1005 C  C   . ASP   A 1 130 ? 13.930 7.471   7.932  1.00 22.67  ? 136 ASP   A C   1 
ATOM   1006 O  O   . ASP   A 1 130 ? 14.319 8.646   7.835  1.00 22.71  ? 136 ASP   A O   1 
ATOM   1007 C  CB  . ASP   A 1 130 ? 11.483 7.273   7.510  1.00 23.89  ? 136 ASP   A CB  1 
ATOM   1008 C  CG  . ASP   A 1 130 ? 11.610 6.239   6.406  1.00 29.35  ? 136 ASP   A CG  1 
ATOM   1009 O  OD1 . ASP   A 1 130 ? 11.623 5.031   6.717  1.00 29.48  ? 136 ASP   A OD1 1 
ATOM   1010 O  OD2 . ASP   A 1 130 ? 11.715 6.636   5.233  1.00 33.25  ? 136 ASP   A OD2 1 
ATOM   1011 N  N   . VAL   A 1 131 ? 14.671 6.407   7.517  1.00 22.01  ? 137 VAL   A N   1 
ATOM   1012 C  CA  . VAL   A 1 131 ? 15.945 6.588   6.778  1.00 22.83  ? 137 VAL   A CA  1 
ATOM   1013 C  C   . VAL   A 1 131 ? 15.918 5.868   5.373  1.00 24.23  ? 137 VAL   A C   1 
ATOM   1014 O  O   . VAL   A 1 131 ? 16.875 5.994   4.606  1.00 24.44  ? 137 VAL   A O   1 
ATOM   1015 C  CB  . VAL   A 1 131 ? 17.217 6.195   7.590  1.00 22.34  ? 137 VAL   A CB  1 
ATOM   1016 C  CG1 . VAL   A 1 131 ? 17.299 6.964   8.906  1.00 22.17  ? 137 VAL   A CG1 1 
ATOM   1017 C  CG2 . VAL   A 1 131 ? 17.277 4.689   7.833  1.00 22.31  ? 137 VAL   A CG2 1 
ATOM   1018 N  N   . ARG   A 1 132 ? 14.830 5.102   5.057  1.00 24.42  ? 138 ARG   A N   1 
ATOM   1019 C  CA  . ARG   A 1 132 ? 14.687 4.295   3.830  1.00 24.65  ? 138 ARG   A CA  1 
ATOM   1020 C  C   . ARG   A 1 132 ? 14.723 5.079   2.502  1.00 25.57  ? 138 ARG   A C   1 
ATOM   1021 O  O   . ARG   A 1 132 ? 14.996 4.473   1.451  1.00 26.48  ? 138 ARG   A O   1 
ATOM   1022 C  CB  . ARG   A 1 132 ? 13.412 3.427   3.871  1.00 24.15  ? 138 ARG   A CB  1 
ATOM   1023 C  CG  . ARG   A 1 132 ? 13.372 2.399   5.015  1.00 23.74  ? 138 ARG   A CG  1 
ATOM   1024 C  CD  . ARG   A 1 132 ? 12.036 1.662   5.020  1.00 25.68  ? 138 ARG   A CD  1 
ATOM   1025 N  NE  . ARG   A 1 132 ? 10.942 2.510   5.504  1.00 27.66  ? 138 ARG   A NE  1 
ATOM   1026 C  CZ  . ARG   A 1 132 ? 9.684  2.098   5.659  1.00 28.59  ? 138 ARG   A CZ  1 
ATOM   1027 N  NH1 . ARG   A 1 132 ? 9.336  0.856   5.324  1.00 27.11  ? 138 ARG   A NH1 1 
ATOM   1028 N  NH2 . ARG   A 1 132 ? 8.759  2.931   6.129  1.00 26.54  ? 138 ARG   A NH2 1 
ATOM   1029 N  N   . ASP   A 1 133 ? 14.443 6.402   2.532  1.00 24.54  ? 139 ASP   A N   1 
ATOM   1030 C  CA  . ASP   A 1 133 ? 14.496 7.251   1.337  1.00 24.84  ? 139 ASP   A CA  1 
ATOM   1031 C  C   . ASP   A 1 133 ? 15.935 7.799   1.060  1.00 25.59  ? 139 ASP   A C   1 
ATOM   1032 O  O   . ASP   A 1 133 ? 16.209 8.288   -0.046 1.00 26.43  ? 139 ASP   A O   1 
ATOM   1033 C  CB  . ASP   A 1 133 ? 13.521 8.427   1.473  1.00 25.84  ? 139 ASP   A CB  1 
ATOM   1034 C  CG  . ASP   A 1 133 ? 13.878 9.399   2.590  1.00 31.42  ? 139 ASP   A CG  1 
ATOM   1035 O  OD1 . ASP   A 1 133 ? 14.246 8.927   3.707  1.00 32.20  ? 139 ASP   A OD1 1 
ATOM   1036 O  OD2 . ASP   A 1 133 ? 13.771 10.630  2.364  1.00 32.15  ? 139 ASP   A OD2 1 
ATOM   1037 N  N   . LEU   A 1 134 ? 16.846 7.711   2.048  1.00 25.15  ? 140 LEU   A N   1 
ATOM   1038 C  CA  . LEU   A 1 134 ? 18.225 8.191   1.901  1.00 25.70  ? 140 LEU   A CA  1 
ATOM   1039 C  C   . LEU   A 1 134 ? 19.051 7.143   1.113  1.00 26.07  ? 140 LEU   A C   1 
ATOM   1040 O  O   . LEU   A 1 134 ? 19.866 6.405   1.688  1.00 26.26  ? 140 LEU   A O   1 
ATOM   1041 C  CB  . LEU   A 1 134 ? 18.829 8.505   3.284  1.00 25.64  ? 140 LEU   A CB  1 
ATOM   1042 C  CG  . LEU   A 1 134 ? 18.025 9.495   4.134  1.00 26.68  ? 140 LEU   A CG  1 
ATOM   1043 C  CD1 . LEU   A 1 134 ? 18.562 9.569   5.572  1.00 27.23  ? 140 LEU   A CD1 1 
ATOM   1044 C  CD2 . LEU   A 1 134 ? 17.981 10.874  3.493  1.00 26.94  ? 140 LEU   A CD2 1 
ATOM   1045 N  N   . LEU   A 1 135 ? 18.802 7.064   -0.221 1.00 25.38  ? 141 LEU   A N   1 
ATOM   1046 C  CA  . LEU   A 1 135 ? 19.416 6.055   -1.087 1.00 25.56  ? 141 LEU   A CA  1 
ATOM   1047 C  C   . LEU   A 1 135 ? 20.927 6.166   -1.171 1.00 25.80  ? 141 LEU   A C   1 
ATOM   1048 O  O   . LEU   A 1 135 ? 21.609 5.143   -1.322 1.00 25.08  ? 141 LEU   A O   1 
ATOM   1049 C  CB  . LEU   A 1 135 ? 18.822 6.079   -2.501 1.00 25.98  ? 141 LEU   A CB  1 
ATOM   1050 C  CG  . LEU   A 1 135 ? 17.302 6.039   -2.645 1.00 28.08  ? 141 LEU   A CG  1 
ATOM   1051 C  CD1 . LEU   A 1 135 ? 16.912 5.838   -4.117 1.00 29.35  ? 141 LEU   A CD1 1 
ATOM   1052 C  CD2 . LEU   A 1 135 ? 16.669 4.939   -1.795 1.00 28.62  ? 141 LEU   A CD2 1 
ATOM   1053 N  N   . TRP   A 1 136 ? 21.450 7.404   -1.066 1.00 25.51  ? 142 TRP   A N   1 
ATOM   1054 C  CA  . TRP   A 1 136 ? 22.880 7.667   -1.143 1.00 26.89  ? 142 TRP   A CA  1 
ATOM   1055 C  C   . TRP   A 1 136 ? 23.687 6.990   -0.025 1.00 28.18  ? 142 TRP   A C   1 
ATOM   1056 O  O   . TRP   A 1 136 ? 24.897 6.840   -0.174 1.00 28.86  ? 142 TRP   A O   1 
ATOM   1057 C  CB  . TRP   A 1 136 ? 23.166 9.185   -1.224 1.00 27.11  ? 142 TRP   A CB  1 
ATOM   1058 C  CG  . TRP   A 1 136 ? 22.510 9.991   -0.150 1.00 28.06  ? 142 TRP   A CG  1 
ATOM   1059 C  CD1 . TRP   A 1 136 ? 21.298 10.621  -0.215 1.00 29.05  ? 142 TRP   A CD1 1 
ATOM   1060 C  CD2 . TRP   A 1 136 ? 23.030 10.248  1.164  1.00 28.41  ? 142 TRP   A CD2 1 
ATOM   1061 N  NE1 . TRP   A 1 136 ? 21.029 11.243  0.982  1.00 29.37  ? 142 TRP   A NE1 1 
ATOM   1062 C  CE2 . TRP   A 1 136 ? 22.096 11.064  1.832  1.00 29.18  ? 142 TRP   A CE2 1 
ATOM   1063 C  CE3 . TRP   A 1 136 ? 24.224 9.911   1.822  1.00 29.16  ? 142 TRP   A CE3 1 
ATOM   1064 C  CZ2 . TRP   A 1 136 ? 22.289 11.491  3.152  1.00 29.73  ? 142 TRP   A CZ2 1 
ATOM   1065 C  CZ3 . TRP   A 1 136 ? 24.426 10.365  3.114  1.00 29.61  ? 142 TRP   A CZ3 1 
ATOM   1066 C  CH2 . TRP   A 1 136 ? 23.450 11.112  3.777  1.00 29.57  ? 142 TRP   A CH2 1 
ATOM   1067 N  N   . LEU   A 1 137 ? 23.038 6.564   1.073  1.00 29.02  ? 143 LEU   A N   1 
ATOM   1068 C  CA  . LEU   A 1 137 ? 23.713 5.844   2.150  1.00 31.07  ? 143 LEU   A CA  1 
ATOM   1069 C  C   . LEU   A 1 137 ? 24.297 4.493   1.662  1.00 34.03  ? 143 LEU   A C   1 
ATOM   1070 O  O   . LEU   A 1 137 ? 25.241 3.996   2.269  1.00 33.60  ? 143 LEU   A O   1 
ATOM   1071 C  CB  . LEU   A 1 137 ? 22.753 5.584   3.320  1.00 30.90  ? 143 LEU   A CB  1 
ATOM   1072 C  CG  . LEU   A 1 137 ? 22.405 6.778   4.200  1.00 31.35  ? 143 LEU   A CG  1 
ATOM   1073 C  CD1 . LEU   A 1 137 ? 21.278 6.422   5.165  1.00 31.04  ? 143 LEU   A CD1 1 
ATOM   1074 C  CD2 . LEU   A 1 137 ? 23.629 7.259   4.961  1.00 32.28  ? 143 LEU   A CD2 1 
ATOM   1075 N  N   . ASP   A 1 138 ? 23.728 3.893   0.587  1.00 36.41  ? 144 ASP   A N   1 
ATOM   1076 C  CA  . ASP   A 1 138 ? 24.214 2.604   0.061  1.00 39.49  ? 144 ASP   A CA  1 
ATOM   1077 C  C   . ASP   A 1 138 ? 25.411 2.738   -0.888 1.00 43.01  ? 144 ASP   A C   1 
ATOM   1078 O  O   . ASP   A 1 138 ? 25.914 1.713   -1.344 1.00 43.13  ? 144 ASP   A O   1 
ATOM   1079 C  CB  . ASP   A 1 138 ? 23.119 1.870   -0.735 1.00 41.01  ? 144 ASP   A CB  1 
ATOM   1080 C  CG  . ASP   A 1 138 ? 21.845 1.546   0.001  1.00 45.90  ? 144 ASP   A CG  1 
ATOM   1081 O  OD1 . ASP   A 1 138 ? 21.889 1.434   1.239  1.00 47.58  ? 144 ASP   A OD1 1 
ATOM   1082 O  OD2 . ASP   A 1 138 ? 20.798 1.408   -0.661 1.00 47.78  ? 144 ASP   A OD2 1 
ATOM   1083 N  N   . GLU   A 1 139 ? 25.822 3.962   -1.253 1.00 45.74  ? 145 GLU   A N   1 
ATOM   1084 C  CA  . GLU   A 1 139 ? 26.903 4.141   -2.226 1.00 49.23  ? 145 GLU   A CA  1 
ATOM   1085 C  C   . GLU   A 1 139 ? 27.963 5.171   -1.800 1.00 52.10  ? 145 GLU   A C   1 
ATOM   1086 O  O   . GLU   A 1 139 ? 27.707 5.983   -0.911 1.00 52.52  ? 145 GLU   A O   1 
ATOM   1087 C  CB  . GLU   A 1 139 ? 26.296 4.524   -3.595 1.00 52.34  ? 145 GLU   A CB  1 
ATOM   1088 C  CG  . GLU   A 1 139 ? 25.495 5.816   -3.546 1.00 58.69  ? 145 GLU   A CG  1 
ATOM   1089 C  CD  . GLU   A 1 139 ? 24.610 6.106   -4.747 1.00 67.39  ? 145 GLU   A CD  1 
ATOM   1090 O  OE1 . GLU   A 1 139 ? 24.079 7.239   -4.826 1.00 68.35  ? 145 GLU   A OE1 1 
ATOM   1091 O  OE2 . GLU   A 1 139 ? 24.443 5.207   -5.606 1.00 70.16  ? 145 GLU   A OE2 1 
ATOM   1092 N  N   . GLU   A 1 140 ? 29.148 5.132   -2.450 1.00 53.81  ? 146 GLU   A N   1 
ATOM   1093 C  CA  . GLU   A 1 140 ? 30.296 6.037   -2.267 1.00 55.82  ? 146 GLU   A CA  1 
ATOM   1094 C  C   . GLU   A 1 140 ? 30.488 6.518   -0.819 1.00 57.20  ? 146 GLU   A C   1 
ATOM   1095 O  O   . GLU   A 1 140 ? 31.589 6.907   -0.429 1.00 57.98  ? 146 GLU   A O   1 
ATOM   1096 C  CB  . GLU   A 1 140 ? 30.223 7.221   -3.265 1.00 58.80  ? 146 GLU   A CB  1 
ATOM   1097 C  CG  . GLU   A 1 140 ? 29.669 8.539   -2.744 1.00 64.79  ? 146 GLU   A CG  1 
ATOM   1098 C  CD  . GLU   A 1 140 ? 30.743 9.519   -2.313 1.00 73.54  ? 146 GLU   A CD  1 
ATOM   1099 O  OE1 . GLU   A 1 140 ? 30.575 10.158  -1.249 1.00 75.04  ? 146 GLU   A OE1 1 
ATOM   1100 O  OE2 . GLU   A 1 140 ? 31.774 9.619   -3.020 1.00 76.53  ? 146 GLU   A OE2 1 
HETATM 1101 N  N1  . A1B2Q B 2 .   ? 12.285 14.855  17.805 1.00 24.25  ? 201 A1B2Q A N1  1 
HETATM 1102 C  C4  . A1B2Q B 2 .   ? 11.257 10.651  22.978 1.00 25.01  ? 201 A1B2Q A C4  1 
HETATM 1103 C  C5  . A1B2Q B 2 .   ? 11.436 12.016  22.815 1.00 24.89  ? 201 A1B2Q A C5  1 
HETATM 1104 C  C6  . A1B2Q B 2 .   ? 10.635 12.935  23.491 1.00 25.47  ? 201 A1B2Q A C6  1 
HETATM 1105 C  C7  . A1B2Q B 2 .   ? 10.802 14.422  23.264 1.00 25.11  ? 201 A1B2Q A C7  1 
HETATM 1106 C  C8  . A1B2Q B 2 .   ? 11.344 14.933  20.937 1.00 24.52  ? 201 A1B2Q A C8  1 
HETATM 1107 C  C10 . A1B2Q B 2 .   ? 11.900 15.830  18.622 1.00 25.29  ? 201 A1B2Q A C10 1 
HETATM 1108 C  C13 . A1B2Q B 2 .   ? 13.131 14.868  22.731 1.00 24.59  ? 201 A1B2Q A C13 1 
HETATM 1109 O  O1  . A1B2Q B 2 .   ? 13.431 14.795  23.909 1.00 24.87  ? 201 A1B2Q A O1  1 
HETATM 1110 C  C12 . A1B2Q B 2 .   ? 14.197 15.110  21.687 1.00 24.56  ? 201 A1B2Q A C12 1 
HETATM 1111 C  C11 . A1B2Q B 2 .   ? 13.730 15.089  20.229 1.00 24.48  ? 201 A1B2Q A C11 1 
HETATM 1112 C  C9  . A1B2Q B 2 .   ? 12.334 15.717  20.075 1.00 24.86  ? 201 A1B2Q A C9  1 
HETATM 1113 O  O   . A1B2Q B 2 .   ? 11.180 16.761  18.251 1.00 25.86  ? 201 A1B2Q A O   1 
HETATM 1114 N  N   . A1B2Q B 2 .   ? 11.848 14.757  22.303 1.00 24.82  ? 201 A1B2Q A N   1 
HETATM 1115 C  C1  . A1B2Q B 2 .   ? 9.651  12.442  24.361 1.00 26.06  ? 201 A1B2Q A C1  1 
HETATM 1116 S  S   . A1B2Q B 2 .   ? 8.664  13.617  25.243 1.00 27.49  ? 201 A1B2Q A S   1 
HETATM 1117 C  C   . A1B2Q B 2 .   ? 7.579  12.589  26.246 1.00 27.25  ? 201 A1B2Q A C   1 
HETATM 1118 C  C3  . A1B2Q B 2 .   ? 10.296 10.182  23.831 1.00 25.16  ? 201 A1B2Q A C3  1 
HETATM 1119 C  C2  . A1B2Q B 2 .   ? 9.489  11.068  24.527 1.00 25.59  ? 201 A1B2Q A C2  1 
HETATM 1120 ZN ZN  . ZN    C 3 .   ? 11.030 -4.006  4.912  1.00 28.31  2 202 ZN    A ZN  1 
HETATM 1121 S  S   . DMS   D 4 .   ? 15.277 21.577  7.290  1.00 90.18  ? 203 DMS   A S   1 
HETATM 1122 O  O   . DMS   D 4 .   ? 14.718 22.114  8.576  1.00 90.15  ? 203 DMS   A O   1 
HETATM 1123 C  C1  . DMS   D 4 .   ? 13.949 21.596  6.052  1.00 90.12  ? 203 DMS   A C1  1 
HETATM 1124 C  C2  . DMS   D 4 .   ? 16.284 22.881  6.529  1.00 90.26  ? 203 DMS   A C2  1 
HETATM 1125 S  S   . DMS   E 4 .   ? 21.442 -4.215  22.701 1.00 102.07 ? 204 DMS   A S   1 
HETATM 1126 O  O   . DMS   E 4 .   ? 22.572 -5.133  22.335 1.00 101.91 ? 204 DMS   A O   1 
HETATM 1127 C  C1  . DMS   E 4 .   ? 22.048 -3.076  23.977 1.00 102.12 ? 204 DMS   A C1  1 
HETATM 1128 C  C2  . DMS   E 4 .   ? 21.273 -2.960  21.402 1.00 102.10 ? 204 DMS   A C2  1 
HETATM 1129 O  O   . HOH   F 5 .   ? 13.775 8.102   30.823 1.00 42.28  ? 301 HOH   A O   1 
HETATM 1130 O  O   . HOH   F 5 .   ? 9.502  21.838  11.156 1.00 52.69  ? 302 HOH   A O   1 
HETATM 1131 O  O   . HOH   F 5 .   ? 4.327  22.518  22.961 1.00 39.48  ? 303 HOH   A O   1 
HETATM 1132 O  O   . HOH   F 5 .   ? 26.654 8.434   -1.178 1.00 51.27  ? 304 HOH   A O   1 
HETATM 1133 O  O   . HOH   F 5 .   ? 5.135  1.402   -2.534 1.00 55.30  ? 305 HOH   A O   1 
HETATM 1134 O  O   . HOH   F 5 .   ? 6.467  3.595   3.035  1.00 42.96  ? 306 HOH   A O   1 
HETATM 1135 O  O   . HOH   F 5 .   ? 8.169  -3.302  0.001  1.00 40.85  ? 307 HOH   A O   1 
HETATM 1136 O  O   . HOH   F 5 .   ? 22.366 -0.471  3.000  1.00 34.96  ? 308 HOH   A O   1 
HETATM 1137 O  O   . HOH   F 5 .   ? 1.707  -2.023  20.077 1.00 33.99  ? 309 HOH   A O   1 
HETATM 1138 O  O   . HOH   F 5 .   ? 31.536 11.298  18.060 1.00 35.17  ? 310 HOH   A O   1 
HETATM 1139 O  O   . HOH   F 5 .   ? 4.667  -4.352  21.042 1.00 26.56  ? 311 HOH   A O   1 
HETATM 1140 O  O   . HOH   F 5 .   ? 12.114 11.705  0.586  1.00 47.22  ? 312 HOH   A O   1 
HETATM 1141 O  O   . HOH   F 5 .   ? 23.992 0.220   14.950 1.00 32.03  ? 313 HOH   A O   1 
HETATM 1142 O  O   . HOH   F 5 .   ? 2.280  8.790   10.108 1.00 42.69  ? 314 HOH   A O   1 
HETATM 1143 O  O   . HOH   F 5 .   ? 10.495 18.463  20.185 1.00 29.47  ? 315 HOH   A O   1 
HETATM 1144 O  O   . HOH   F 5 .   ? -0.934 1.843   4.562  1.00 57.00  ? 316 HOH   A O   1 
HETATM 1145 O  O   . HOH   F 5 .   ? 15.697 -10.840 7.295  1.00 55.15  ? 317 HOH   A O   1 
HETATM 1146 O  O   . HOH   F 5 .   ? 5.370  6.641   24.773 1.00 32.29  ? 318 HOH   A O   1 
HETATM 1147 O  O   . HOH   F 5 .   ? 31.386 11.124  15.492 1.00 44.91  ? 319 HOH   A O   1 
HETATM 1148 O  O   . HOH   F 5 .   ? 29.831 3.355   9.305  1.00 30.99  ? 320 HOH   A O   1 
HETATM 1149 O  O   . HOH   F 5 .   ? 19.691 21.009  26.585 1.00 66.97  ? 321 HOH   A O   1 
HETATM 1150 O  O   . HOH   F 5 .   ? 1.549  9.816   4.528  1.00 57.71  ? 322 HOH   A O   1 
HETATM 1151 O  O   . HOH   F 5 .   ? 20.445 -0.027  26.622 1.00 49.97  ? 323 HOH   A O   1 
HETATM 1152 O  O   . HOH   F 5 .   ? 5.953  2.223   6.210  1.00 42.08  ? 324 HOH   A O   1 
HETATM 1153 O  O   . HOH   F 5 .   ? 15.113 15.674  28.041 1.00 41.11  ? 325 HOH   A O   1 
HETATM 1154 O  O   . HOH   F 5 .   ? 21.005 9.258   18.228 1.00 26.07  ? 326 HOH   A O   1 
HETATM 1155 O  O   . HOH   F 5 .   ? 6.807  -4.606  28.588 1.00 34.49  ? 327 HOH   A O   1 
HETATM 1156 O  O   . HOH   F 5 .   ? 12.588 17.933  5.267  1.00 50.59  ? 328 HOH   A O   1 
HETATM 1157 O  O   . HOH   F 5 .   ? 10.742 9.058   4.390  1.00 29.12  ? 329 HOH   A O   1 
HETATM 1158 O  O   . HOH   F 5 .   ? 7.124  13.865  21.674 1.00 30.61  ? 330 HOH   A O   1 
HETATM 1159 O  O   . HOH   F 5 .   ? 0.605  15.388  17.232 1.00 38.36  ? 331 HOH   A O   1 
HETATM 1160 O  O   . HOH   F 5 .   ? 17.870 -6.214  2.494  1.00 41.49  ? 332 HOH   A O   1 
HETATM 1161 O  O   . HOH   F 5 .   ? 8.016  16.401  21.994 1.00 28.42  ? 333 HOH   A O   1 
HETATM 1162 O  O   . HOH   F 5 .   ? 18.810 0.739   29.608 1.00 36.78  ? 334 HOH   A O   1 
HETATM 1163 O  O   . HOH   F 5 .   ? 8.978  19.981  18.384 1.00 26.24  ? 335 HOH   A O   1 
HETATM 1164 O  O   . HOH   F 5 .   ? 27.882 3.419   1.755  1.00 45.70  ? 336 HOH   A O   1 
HETATM 1165 O  O   . HOH   F 5 .   ? 20.088 -3.239  15.671 1.00 39.66  ? 337 HOH   A O   1 
HETATM 1166 O  O   . HOH   F 5 .   ? 13.215 21.914  12.949 1.00 35.52  ? 338 HOH   A O   1 
HETATM 1167 O  O   . HOH   F 5 .   ? 1.162  0.245   16.654 1.00 21.60  ? 339 HOH   A O   1 
HETATM 1168 O  O   . HOH   F 5 .   ? 11.469 16.561  3.269  1.00 46.09  ? 340 HOH   A O   1 
HETATM 1169 O  O   . HOH   F 5 .   ? 1.150  2.322   24.539 1.00 31.14  ? 341 HOH   A O   1 
HETATM 1170 O  O   . HOH   F 5 .   ? 26.415 -2.477  13.165 1.00 47.52  ? 342 HOH   A O   1 
HETATM 1171 O  O   . HOH   F 5 .   ? 18.931 19.984  4.962  1.00 49.10  ? 343 HOH   A O   1 
HETATM 1172 O  O   . HOH   F 5 .   ? 15.766 2.896   22.714 1.00 21.94  ? 344 HOH   A O   1 
HETATM 1173 O  O   . HOH   F 5 .   ? 6.078  20.122  26.075 1.00 37.78  ? 345 HOH   A O   1 
HETATM 1174 O  O   . HOH   F 5 .   ? 8.241  17.070  25.068 1.00 26.10  ? 346 HOH   A O   1 
HETATM 1175 O  O   . HOH   F 5 .   ? 10.413 5.444   3.081  1.00 26.52  ? 347 HOH   A O   1 
HETATM 1176 O  O   . HOH   F 5 .   ? 24.844 22.774  8.655  1.00 25.88  ? 348 HOH   A O   1 
HETATM 1177 O  O   . HOH   F 5 .   ? 11.061 23.934  24.840 1.00 33.61  ? 349 HOH   A O   1 
HETATM 1178 O  O   . HOH   F 5 .   ? 31.491 19.081  6.435  1.00 40.73  ? 350 HOH   A O   1 
HETATM 1179 O  O   . HOH   F 5 .   ? 35.157 20.635  9.494  1.00 26.56  ? 351 HOH   A O   1 
HETATM 1180 O  O   . HOH   F 5 .   ? 15.729 23.308  26.943 1.00 40.44  ? 352 HOH   A O   1 
HETATM 1181 O  O   . HOH   F 5 .   ? 13.102 2.726   0.330  1.00 23.64  ? 353 HOH   A O   1 
HETATM 1182 O  O   . HOH   F 5 .   ? 11.824 12.257  11.196 1.00 25.48  ? 354 HOH   A O   1 
HETATM 1183 O  O   . HOH   F 5 .   ? 23.783 -5.933  7.583  1.00 43.59  ? 355 HOH   A O   1 
HETATM 1184 O  O   . HOH   F 5 .   ? 12.986 16.460  26.138 1.00 27.07  ? 356 HOH   A O   1 
HETATM 1185 O  O   . HOH   F 5 .   ? 20.662 -1.011  30.452 1.00 49.49  ? 357 HOH   A O   1 
HETATM 1186 O  O   . HOH   F 5 .   ? 15.392 12.013  0.513  1.00 33.73  ? 358 HOH   A O   1 
HETATM 1187 O  O   . HOH   F 5 .   ? 17.214 12.373  23.718 1.00 26.45  ? 359 HOH   A O   1 
HETATM 1188 O  O   . HOH   F 5 .   ? 5.718  26.756  17.867 1.00 46.19  ? 360 HOH   A O   1 
HETATM 1189 O  O   . HOH   F 5 .   ? 8.615  -5.389  31.539 1.00 59.32  ? 361 HOH   A O   1 
HETATM 1190 O  O   . HOH   F 5 .   ? 31.883 2.770   11.176 1.00 39.50  ? 362 HOH   A O   1 
HETATM 1191 O  O   . HOH   F 5 .   ? 24.543 17.659  2.203  1.00 45.44  ? 363 HOH   A O   1 
HETATM 1192 O  O   . HOH   F 5 .   ? 16.325 23.979  18.750 1.00 43.76  ? 364 HOH   A O   1 
HETATM 1193 O  O   . HOH   F 5 .   ? 13.454 -6.247  30.389 1.00 61.86  ? 365 HOH   A O   1 
HETATM 1194 O  O   . HOH   F 5 .   ? 18.696 2.880   22.618 1.00 24.53  ? 366 HOH   A O   1 
HETATM 1195 O  O   . HOH   F 5 .   ? 8.298  4.360   32.753 1.00 36.15  ? 367 HOH   A O   1 
HETATM 1196 O  O   . HOH   F 5 .   ? 4.061  4.228   27.734 1.00 41.68  ? 368 HOH   A O   1 
HETATM 1197 O  O   . HOH   F 5 .   ? 4.106  -4.525  6.310  1.00 31.47  ? 369 HOH   A O   1 
HETATM 1198 O  O   . HOH   F 5 .   ? 30.940 20.755  8.756  1.00 22.72  ? 370 HOH   A O   1 
HETATM 1199 O  O   . HOH   F 5 .   ? 19.572 -4.406  26.984 1.00 56.21  ? 371 HOH   A O   1 
HETATM 1200 O  O   . HOH   F 5 .   ? 23.260 16.657  22.835 1.00 50.23  ? 372 HOH   A O   1 
HETATM 1201 O  O   . HOH   F 5 .   ? 9.045  3.397   2.578  1.00 34.31  ? 373 HOH   A O   1 
HETATM 1202 O  O   . HOH   F 5 .   ? 19.103 19.257  16.649 1.00 33.10  ? 374 HOH   A O   1 
HETATM 1203 O  O   . HOH   F 5 .   ? 25.988 12.021  22.089 1.00 39.70  ? 375 HOH   A O   1 
HETATM 1204 O  O   . HOH   F 5 .   ? 19.898 4.544   25.155 1.00 33.44  ? 376 HOH   A O   1 
HETATM 1205 O  O   . HOH   F 5 .   ? 7.212  25.942  21.553 1.00 41.32  ? 377 HOH   A O   1 
HETATM 1206 O  O   . HOH   F 5 .   ? 14.687 15.260  3.360  1.00 38.14  ? 378 HOH   A O   1 
HETATM 1207 O  O   . HOH   F 5 .   ? 27.295 9.624   20.349 1.00 54.69  ? 379 HOH   A O   1 
HETATM 1208 O  O   . HOH   F 5 .   ? 13.539 11.150  9.051  1.00 24.52  ? 380 HOH   A O   1 
HETATM 1209 O  O   . HOH   F 5 .   ? 6.298  -7.113  14.108 1.00 50.89  ? 381 HOH   A O   1 
HETATM 1210 O  O   . HOH   F 5 .   ? 14.948 9.946   29.392 1.00 33.13  ? 382 HOH   A O   1 
HETATM 1211 O  O   . HOH   F 5 .   ? 18.571 21.780  9.118  1.00 26.66  ? 383 HOH   A O   1 
HETATM 1212 O  O   . HOH   F 5 .   ? 5.073  10.473  19.106 1.00 39.90  ? 384 HOH   A O   1 
HETATM 1213 O  O   . HOH   F 5 .   ? 16.843 17.780  3.664  1.00 44.59  ? 385 HOH   A O   1 
HETATM 1214 O  O   . HOH   F 5 .   ? 20.410 9.294   25.200 1.00 27.51  ? 386 HOH   A O   1 
HETATM 1215 O  O   . HOH   F 5 .   ? 0.448  4.151   6.806  1.00 38.05  ? 387 HOH   A O   1 
HETATM 1216 O  O   . HOH   F 5 .   ? 30.267 4.827   2.187  1.00 32.86  ? 388 HOH   A O   1 
HETATM 1217 O  O   . HOH   F 5 .   ? 6.841  23.655  11.847 1.00 38.43  ? 389 HOH   A O   1 
HETATM 1218 O  O   . HOH   F 5 .   ? 16.623 -2.920  17.089 1.00 28.33  ? 390 HOH   A O   1 
HETATM 1219 O  O   . HOH   F 5 .   ? 6.643  8.956   27.681 1.00 49.16  ? 391 HOH   A O   1 
HETATM 1220 O  O   . HOH   F 5 .   ? 31.914 8.982   4.060  1.00 34.65  ? 392 HOH   A O   1 
HETATM 1221 O  O   . HOH   F 5 .   ? 27.755 -1.327  5.273  1.00 41.42  ? 393 HOH   A O   1 
HETATM 1222 O  O   . HOH   F 5 .   ? 21.309 -4.399  9.312  1.00 44.15  ? 394 HOH   A O   1 
HETATM 1223 O  O   . HOH   F 5 .   ? 6.174  -0.812  24.067 1.00 26.76  ? 395 HOH   A O   1 
HETATM 1224 O  O   . HOH   F 5 .   ? 11.147 5.156   33.476 1.00 35.81  ? 396 HOH   A O   1 
HETATM 1225 O  O   . HOH   F 5 .   ? 28.928 -1.591  12.397 1.00 42.16  ? 397 HOH   A O   1 
HETATM 1226 O  O   . HOH   F 5 .   ? -0.164 16.555  13.111 1.00 42.31  ? 398 HOH   A O   1 
HETATM 1227 O  O   . HOH   F 5 .   ? 34.389 -3.275  9.448  1.00 37.76  ? 399 HOH   A O   1 
HETATM 1228 O  O   . HOH   F 5 .   ? 24.481 2.434   18.584 1.00 36.21  ? 400 HOH   A O   1 
HETATM 1229 O  O   . HOH   F 5 .   ? 21.993 21.567  5.857  1.00 42.04  ? 401 HOH   A O   1 
HETATM 1230 O  O   . HOH   F 5 .   ? 24.173 18.457  18.293 1.00 32.17  ? 402 HOH   A O   1 
HETATM 1231 O  O   . HOH   F 5 .   ? 15.479 -3.856  0.760  1.00 30.87  ? 403 HOH   A O   1 
HETATM 1232 O  O   . HOH   F 5 .   ? 10.953 -4.437  31.630 1.00 44.52  ? 404 HOH   A O   1 
HETATM 1233 O  O   . HOH   F 5 .   ? 19.376 0.188   18.792 1.00 27.76  ? 405 HOH   A O   1 
HETATM 1234 O  O   . HOH   F 5 .   ? 31.401 -4.118  6.392  1.00 44.08  ? 406 HOH   A O   1 
HETATM 1235 O  O   . HOH   F 5 .   ? 4.812  12.598  20.639 1.00 49.77  ? 407 HOH   A O   1 
HETATM 1236 O  O   . HOH   F 5 .   ? 4.631  14.022  24.246 1.00 46.00  ? 408 HOH   A O   1 
HETATM 1237 O  O   . HOH   F 5 .   ? 37.124 -0.646  8.249  1.00 51.16  ? 409 HOH   A O   1 
HETATM 1238 O  O   . HOH   F 5 .   ? 4.806  -1.695  21.744 1.00 28.64  ? 410 HOH   A O   1 
HETATM 1239 O  O   . HOH   F 5 .   ? 1.793  -2.334  17.252 1.00 30.02  ? 411 HOH   A O   1 
HETATM 1240 O  O   . HOH   F 5 .   ? 20.887 2.923   -3.304 1.00 41.67  ? 412 HOH   A O   1 
HETATM 1241 O  O   . HOH   F 5 .   ? 35.708 5.328   12.435 1.00 63.74  ? 413 HOH   A O   1 
HETATM 1242 O  O   . HOH   F 5 .   ? 4.103  7.449   26.972 1.00 64.69  ? 414 HOH   A O   1 
HETATM 1243 O  O   . HOH   F 5 .   ? 32.323 0.200   12.309 1.00 43.76  ? 415 HOH   A O   1 
HETATM 1244 O  O   . HOH   F 5 .   ? 22.960 19.266  5.053  1.00 29.91  ? 416 HOH   A O   1 
HETATM 1245 O  O   . HOH   F 5 .   ? 8.337  21.157  8.913  1.00 46.56  ? 417 HOH   A O   1 
HETATM 1246 O  O   . HOH   F 5 .   ? 18.650 20.687  19.055 1.00 42.37  ? 418 HOH   A O   1 
HETATM 1247 O  O   . HOH   F 5 .   ? 23.247 8.808   20.083 1.00 25.58  ? 419 HOH   A O   1 
HETATM 1248 O  O   . HOH   F 5 .   ? -0.471 15.452  10.876 1.00 44.02  ? 420 HOH   A O   1 
HETATM 1249 O  O   . HOH   F 5 .   ? 3.961  15.437  20.317 1.00 38.74  ? 421 HOH   A O   1 
HETATM 1250 O  O   . HOH   F 5 .   ? 6.920  13.703  5.330  1.00 35.73  ? 422 HOH   A O   1 
HETATM 1251 O  O   . HOH   F 5 .   ? -0.071 16.373  7.940  1.00 64.63  ? 423 HOH   A O   1 
HETATM 1252 O  O   . HOH   F 5 .   ? 6.388  -3.340  -1.984 1.00 45.19  ? 424 HOH   A O   1 
HETATM 1253 O  O   . HOH   F 5 .   ? 17.120 24.468  13.627 1.00 52.26  ? 425 HOH   A O   1 
HETATM 1254 O  O   . HOH   F 5 .   ? 22.700 -2.295  14.891 1.00 45.63  ? 426 HOH   A O   1 
HETATM 1255 O  O   . HOH   F 5 .   ? 25.737 7.636   19.522 1.00 41.73  ? 427 HOH   A O   1 
HETATM 1256 O  O   . HOH   F 5 .   ? 9.216  -7.161  8.636  1.00 44.36  ? 428 HOH   A O   1 
HETATM 1257 O  O   . HOH   F 5 .   ? 17.847 9.629   -2.431 1.00 39.76  ? 429 HOH   A O   1 
HETATM 1258 O  O   . HOH   F 5 .   ? 19.002 13.667  1.418  1.00 49.50  ? 430 HOH   A O   1 
HETATM 1259 O  O   . HOH   F 5 .   ? 2.322  13.812  5.248  1.00 43.25  ? 431 HOH   A O   1 
HETATM 1260 O  O   . HOH   F 5 .   ? 7.091  -4.833  2.232  1.00 38.50  ? 432 HOH   A O   1 
HETATM 1261 O  O   . HOH   F 5 .   ? 5.449  -0.809  29.008 1.00 43.57  ? 433 HOH   A O   1 
HETATM 1262 O  O   . HOH   F 5 .   ? 20.257 7.618   27.473 1.00 38.44  ? 434 HOH   A O   1 
HETATM 1263 O  O   . HOH   F 5 .   ? 2.250  -6.107  17.689 1.00 49.35  ? 435 HOH   A O   1 
HETATM 1264 O  O   . HOH   F 5 .   ? 17.840 11.584  -0.272 1.00 42.83  ? 436 HOH   A O   1 
HETATM 1265 O  O   . HOH   F 5 .   ? 21.338 1.696   18.384 1.00 55.72  ? 437 HOH   A O   1 
HETATM 1266 O  O   . HOH   F 5 .   ? 36.105 10.716  11.159 1.00 72.96  ? 438 HOH   A O   1 
HETATM 1267 O  O   . HOH   F 5 .   ? 2.800  14.661  22.730 1.00 38.36  ? 439 HOH   A O   1 
HETATM 1268 O  O   . HOH   F 5 .   ? 38.610 1.177   5.949  1.00 77.08  ? 440 HOH   A O   1 
HETATM 1269 O  O   . HOH   F 5 .   ? 20.202 9.572   -3.732 1.00 35.05  ? 441 HOH   A O   1 
HETATM 1270 O  O   . HOH   F 5 .   ? 11.291 10.499  31.392 1.00 44.43  ? 442 HOH   A O   1 
HETATM 1271 O  O   . HOH   F 5 .   ? 20.603 15.617  0.290  1.00 48.76  ? 443 HOH   A O   1 
HETATM 1272 O  O   . HOH   F 5 .   ? 16.806 -5.853  16.616 1.00 56.78  ? 444 HOH   A O   1 
HETATM 1273 O  O   . HOH   F 5 .   ? 3.355  13.213  27.137 1.00 48.26  ? 445 HOH   A O   1 
HETATM 1274 O  O   . HOH   F 5 .   ? 17.731 12.036  28.201 1.00 46.69  ? 446 HOH   A O   1 
HETATM 1275 O  O   . HOH   F 5 .   ? 3.086  2.113   26.452 1.00 34.54  ? 447 HOH   A O   1 
HETATM 1276 O  O   . HOH   F 5 .   ? 4.371  12.699  18.252 1.00 47.73  ? 448 HOH   A O   1 
HETATM 1277 O  O   . HOH   F 5 .   ? 1.527  -1.027  23.904 1.00 45.12  ? 449 HOH   A O   1 
HETATM 1278 O  O   . HOH   F 5 .   ? 19.049 11.708  25.499 1.00 44.46  ? 450 HOH   A O   1 
HETATM 1279 O  O   . HOH   F 5 .   ? 4.643  -1.263  26.392 1.00 45.97  ? 451 HOH   A O   1 
HETATM 1280 O  O   . HOH   F 5 .   ? 3.273  -6.751  14.874 1.00 56.48  ? 452 HOH   A O   1 
HETATM 1281 O  O   . HOH   F 5 .   ? 31.478 11.306  2.783  1.00 44.37  ? 453 HOH   A O   1 
HETATM 1282 O  O   . HOH   F 5 .   ? 16.465 14.379  1.292  1.00 49.39  ? 454 HOH   A O   1 
HETATM 1283 O  O   . HOH   F 5 .   ? 4.150  -3.778  27.447 1.00 61.91  ? 455 HOH   A O   1 
HETATM 1284 O  O   . HOH   F 5 .   ? 19.768 -8.748  12.475 1.00 65.25  ? 456 HOH   A O   1 
HETATM 1285 O  O   . HOH   F 5 .   ? 15.271 -6.290  32.642 1.00 45.43  ? 457 HOH   A O   1 
HETATM 1286 O  O   . HOH   F 5 .   ? 5.973  6.107   2.061  1.00 60.11  ? 458 HOH   A O   1 
HETATM 1287 O  O   . HOH   F 5 .   ? 10.223 16.638  26.817 1.00 29.92  ? 459 HOH   A O   1 
HETATM 1288 O  O   . HOH   F 5 .   ? 32.720 4.309   13.086 1.00 41.44  ? 460 HOH   A O   1 
HETATM 1289 O  O   . HOH   F 5 .   ? 8.875  8.088   2.263  1.00 41.92  ? 461 HOH   A O   1 
HETATM 1290 O  O   . HOH   F 5 .   ? 7.094  28.154  19.841 1.00 40.49  ? 462 HOH   A O   1 
HETATM 1291 O  O   . HOH   F 5 .   ? 24.194 10.097  22.783 1.00 40.58  ? 463 HOH   A O   1 
HETATM 1292 O  O   . HOH   F 5 .   ? 4.928  25.361  13.087 1.00 61.16  ? 464 HOH   A O   1 
HETATM 1293 O  O   . HOH   F 5 .   ? 23.279 10.483  -7.875 1.00 47.67  ? 465 HOH   A O   1 
HETATM 1294 O  O   . HOH   F 5 .   ? 13.569 12.008  30.584 1.00 37.43  ? 466 HOH   A O   1 
HETATM 1295 O  O   . HOH   F 5 .   ? 19.174 -2.619  17.954 1.00 29.40  ? 467 HOH   A O   1 
HETATM 1296 O  O   . HOH   F 5 .   ? 5.812  15.886  25.701 1.00 40.22  ? 468 HOH   A O   1 
HETATM 1297 O  O   . HOH   F 5 .   ? 2.103  21.775  7.831  1.00 59.13  ? 469 HOH   A O   1 
HETATM 1298 O  O   . HOH   F 5 .   ? 0.337  12.727  17.617 1.00 37.23  ? 470 HOH   A O   1 
HETATM 1299 O  O   . HOH   F 5 .   ? 30.251 14.173  1.213  1.00 55.76  ? 471 HOH   A O   1 
HETATM 1300 O  O   . HOH   F 5 .   ? 37.819 20.851  9.694  1.00 38.81  ? 472 HOH   A O   1 
HETATM 1301 O  O   . HOH   F 5 .   ? 4.563  -6.395  22.991 1.00 41.83  ? 473 HOH   A O   1 
HETATM 1302 O  O   . HOH   F 5 .   ? 4.025  25.519  22.334 1.00 48.68  ? 474 HOH   A O   1 
HETATM 1303 O  O   . HOH   F 5 .   ? 21.594 11.792  -3.983 1.00 49.26  ? 475 HOH   A O   1 
HETATM 1304 O  O   . HOH   F 5 .   ? 30.509 -0.002  14.002 1.00 66.68  ? 476 HOH   A O   1 
HETATM 1305 O  O   . HOH   F 5 .   ? 4.123  -10.101 16.584 1.00 56.41  ? 477 HOH   A O   1 
HETATM 1306 O  O   . HOH   F 5 .   ? 1.306  20.308  4.650  1.00 54.61  ? 478 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   ? 0.2482 0.4321 0.3562 0.0002  -0.0504 -0.0031 7   SER   A N   
2    C CA  . SER   A 1   ? 0.2543 0.4417 0.3748 0.0005  -0.0512 -0.0023 7   SER   A CA  
3    C C   . SER   A 1   ? 0.2475 0.4373 0.3739 0.0011  -0.0475 -0.0006 7   SER   A C   
4    O O   . SER   A 1   ? 0.2580 0.4463 0.3794 0.0012  -0.0458 0.0004  7   SER   A O   
5    C CB  . SER   A 1   ? 0.2728 0.4592 0.3972 0.0001  -0.0579 -0.0010 7   SER   A CB  
6    O OG  . SER   A 1   ? 0.3071 0.4916 0.4290 0.0003  -0.0604 0.0018  7   SER   A OG  
7    N N   . GLY   A 2   ? 0.2277 0.4208 0.3643 0.0013  -0.0460 -0.0005 8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.2195 0.4142 0.3614 0.0017  -0.0418 0.0002  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.2102 0.4084 0.3589 0.0012  -0.0381 -0.0007 8   GLY   A C   
10   O O   . GLY   A 2   ? 0.2081 0.4077 0.3559 0.0005  -0.0381 -0.0015 8   GLY   A O   
11   N N   . ALA   A 3   ? 0.1976 0.3969 0.3528 0.0015  -0.0345 -0.0005 9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.1979 0.4003 0.3582 0.0006  -0.0302 -0.0013 9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.2062 0.4079 0.3668 0.0003  -0.0245 -0.0024 9   ALA   A C   
14   O O   . ALA   A 3   ? 0.2174 0.4164 0.3783 0.0014  -0.0243 -0.0023 9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.1873 0.3923 0.3592 0.0012  -0.0321 -0.0002 9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.1914 0.3949 0.3517 -0.0013 -0.0198 -0.0035 10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.1904 0.3926 0.3498 -0.0023 -0.0137 -0.0054 10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.1971 0.4017 0.3672 -0.0017 -0.0100 -0.0055 10  ILE   A C   
19   O O   . ILE   A 4   ? 0.1971 0.4051 0.3705 -0.0025 -0.0104 -0.0043 10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.1933 0.3956 0.3422 -0.0054 -0.0112 -0.0064 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.1980 0.3994 0.3388 -0.0059 -0.0149 -0.0057 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.1977 0.3975 0.3433 -0.0070 -0.0051 -0.0090 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.2067 0.4100 0.3404 -0.0088 -0.0144 -0.0053 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.1924 0.3953 0.3690 -0.0002 -0.0059 -0.0067 11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.1900 0.3954 0.3783 0.0006  -0.0011 -0.0070 11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.1933 0.3961 0.3768 -0.0010 0.0075  -0.0105 11  TYR   A C   
27   O O   . TYR   A 5   ? 0.2052 0.4036 0.3881 0.0000  0.0101  -0.0126 11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.1869 0.3928 0.3899 0.0041  -0.0035 -0.0052 11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.1959 0.4042 0.4028 0.0049  -0.0123 -0.0019 11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.2012 0.4142 0.4163 0.0044  -0.0142 -0.0002 11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.2136 0.4189 0.4147 0.0056  -0.0186 -0.0006 11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.2047 0.4188 0.4219 0.0045  -0.0225 0.0022  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.2219 0.4284 0.4237 0.0057  -0.0264 0.0018  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.2225 0.4332 0.4321 0.0051  -0.0286 0.0029  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.2330 0.4438 0.4419 0.0047  -0.0365 0.0046  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.1876 0.3923 0.3659 -0.0039 0.0117  -0.0112 12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.2129 0.4147 0.3836 -0.0063 0.0200  -0.0148 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.2302 0.4356 0.4078 -0.0070 0.0265  -0.0147 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.2261 0.4360 0.4056 -0.0082 0.0239  -0.0115 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.2298 0.4294 0.3829 -0.0104 0.0186  -0.0156 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.2325 0.4366 0.3826 -0.0120 0.0135  -0.0119 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.2397 0.4359 0.3829 -0.0138 0.0265  -0.0195 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.2352 0.4387 0.4182 -0.0061 0.0351  -0.0179 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.2350 0.4420 0.4262 -0.0065 0.0427  -0.0179 13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.2312 0.4450 0.4396 -0.0042 0.0381  -0.0132 13  GLY   A C   
46   O O   . GLY   A 7   ? 0.2242 0.4388 0.4439 -0.0007 0.0323  -0.0116 13  GLY   A O   
47   N N   . ASN   A 8   ? 0.2280 0.4462 0.4370 -0.0066 0.0390  -0.0107 14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.2239 0.4482 0.4485 -0.0052 0.0336  -0.0063 14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.2183 0.4430 0.4346 -0.0070 0.0241  -0.0033 14  ASN   A C   
50   O O   . ASN   A 8   ? 0.2183 0.4471 0.4412 -0.0081 0.0216  -0.0001 14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.2403 0.4696 0.4766 -0.0062 0.0412  -0.0050 14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.2973 0.5275 0.5492 -0.0029 0.0490  -0.0070 14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.3011 0.5354 0.5726 0.0004  0.0458  -0.0047 14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.3129 0.5391 0.5566 -0.0038 0.0593  -0.0115 14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.2086 0.4291 0.4118 -0.0072 0.0192  -0.0045 15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.2050 0.4255 0.4007 -0.0083 0.0111  -0.0023 15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.1844 0.4028 0.3802 -0.0056 0.0033  -0.0024 15  TYR   A C   
58   O O   . TYR   A 9   ? 0.1779 0.3934 0.3731 -0.0039 0.0043  -0.0043 15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.2154 0.4334 0.3939 -0.0118 0.0126  -0.0029 15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.2272 0.4469 0.4022 -0.0153 0.0192  -0.0021 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.2424 0.4658 0.4240 -0.0165 0.0181  0.0016  15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.2412 0.4579 0.4046 -0.0179 0.0260  -0.0049 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.2613 0.4860 0.4387 -0.0201 0.0242  0.0031  15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.2588 0.4765 0.4162 -0.0217 0.0320  -0.0038 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.2785 0.5004 0.4431 -0.0228 0.0312  0.0005  15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.2978 0.5205 0.4559 -0.0269 0.0373  0.0021  15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.1698 0.3891 0.3659 -0.0056 -0.0040 -0.0002 16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.1701 0.3871 0.3637 -0.0038 -0.0114 -0.0001 16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.1728 0.3883 0.3545 -0.0055 -0.0144 0.0002  16  ARG   A C   
70   O O   . ARG   A 10  ? 0.1779 0.3951 0.3608 -0.0069 -0.0157 0.0018  16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.1687 0.3878 0.3745 -0.0024 -0.0173 0.0018  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.1781 0.3944 0.3787 -0.0015 -0.0253 0.0020  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.1875 0.4054 0.3995 -0.0006 -0.0315 0.0037  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.2074 0.4232 0.4143 -0.0014 -0.0385 0.0037  16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.2371 0.4493 0.4366 -0.0006 -0.0438 0.0032  16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.2222 0.4327 0.4188 0.0009  -0.0433 0.0033  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.2227 0.4323 0.4167 -0.0016 -0.0491 0.0025  16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.1667 0.3793 0.3383 -0.0053 -0.0153 -0.0011 17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.1692 0.3810 0.3315 -0.0065 -0.0177 -0.0006 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.1724 0.3822 0.3331 -0.0047 -0.0233 -0.0008 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.1767 0.3844 0.3352 -0.0034 -0.0240 -0.0017 17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.1753 0.3858 0.3274 -0.0084 -0.0145 -0.0017 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.1725 0.3835 0.3180 -0.0096 -0.0171 -0.0003 17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.1791 0.3903 0.3304 -0.0105 -0.0082 -0.0024 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.1666 0.3765 0.3278 -0.0047 -0.0270 -0.0001 18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.1764 0.3836 0.3343 -0.0032 -0.0317 -0.0008 18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.1726 0.3791 0.3255 -0.0036 -0.0326 -0.0008 18  VAL   A C   
88   O O   . VAL   A 12  ? 0.1753 0.3836 0.3295 -0.0050 -0.0311 0.0006  18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.2028 0.4097 0.3680 -0.0026 -0.0361 -0.0007 18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.2177 0.4259 0.3905 -0.0018 -0.0358 0.0000  18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.2108 0.4192 0.3822 -0.0039 -0.0366 0.0003  18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.1521 0.3558 0.3000 -0.0024 -0.0352 -0.0021 19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.1500 0.3528 0.2956 -0.0022 -0.0357 -0.0024 19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.1662 0.3682 0.3182 -0.0026 -0.0380 -0.0022 19  ASN   A C   
95   O O   . ASN   A 13  ? 0.1664 0.3672 0.3219 -0.0026 -0.0410 -0.0030 19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.1447 0.3440 0.2834 -0.0008 -0.0370 -0.0045 19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.1581 0.3580 0.2909 -0.0006 -0.0347 -0.0043 19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.1757 0.3748 0.3066 -0.0005 -0.0351 -0.0043 19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.1393 0.3406 0.2702 -0.0006 -0.0324 -0.0038 19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.1662 0.3691 0.3207 -0.0032 -0.0370 -0.0007 20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.1666 0.3683 0.3278 -0.0039 -0.0390 -0.0001 20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.1677 0.3646 0.3283 -0.0030 -0.0428 -0.0032 20  ARG   A C   
103  O O   . ARG   A 14  ? 0.1672 0.3630 0.3332 -0.0040 -0.0457 -0.0035 20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.1796 0.3822 0.3429 -0.0044 -0.0378 0.0024  20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.1915 0.3932 0.3629 -0.0057 -0.0393 0.0042  20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.2071 0.4084 0.3803 -0.0056 -0.0389 0.0068  20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.2124 0.4127 0.3932 -0.0071 -0.0400 0.0095  20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.2363 0.4319 0.4221 -0.0065 -0.0425 0.0080  20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.2281 0.4191 0.4107 -0.0045 -0.0439 0.0032  20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.2034 0.3980 0.3965 -0.0081 -0.0433 0.0112  20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.1663 0.3601 0.3197 -0.0014 -0.0426 -0.0057 21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.1776 0.3657 0.3272 -0.0009 -0.0456 -0.0094 21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.1890 0.3761 0.3364 -0.0017 -0.0494 -0.0104 21  HIS   A C   
114  O O   . HIS   A 15  ? 0.2047 0.3870 0.3497 -0.0023 -0.0532 -0.0130 21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.1883 0.3734 0.3305 0.0009  -0.0432 -0.0119 21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.2029 0.3891 0.3371 0.0015  -0.0415 -0.0121 21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.2116 0.4027 0.3464 0.0017  -0.0383 -0.0095 21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.2136 0.3963 0.3390 0.0016  -0.0427 -0.0145 21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.2136 0.4039 0.3410 0.0020  -0.0375 -0.0103 21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.2238 0.4093 0.3451 0.0021  -0.0399 -0.0130 21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.1860 0.3769 0.3342 -0.0018 -0.0487 -0.0083 22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.2015 0.3917 0.3495 -0.0024 -0.0528 -0.0083 22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.2059 0.4001 0.3658 -0.0035 -0.0543 -0.0059 22  LEU   A C   
124  O O   . LEU   A 16  ? 0.2080 0.4029 0.3708 -0.0037 -0.0576 -0.0050 22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.2075 0.3985 0.3491 -0.0014 -0.0512 -0.0077 22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.2295 0.4174 0.3599 -0.0005 -0.0491 -0.0095 22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.2346 0.4234 0.3602 0.0000  -0.0477 -0.0082 22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.2326 0.4146 0.3555 -0.0009 -0.0526 -0.0126 22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.2082 0.4052 0.3755 -0.0042 -0.0516 -0.0044 23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.2133 0.4146 0.3923 -0.0053 -0.0514 -0.0019 23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.2153 0.4151 0.4008 -0.0067 -0.0576 -0.0023 23  ALA   A C   
132  O O   . ALA   A 17  ? 0.2089 0.4039 0.3909 -0.0075 -0.0610 -0.0045 23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.2093 0.4131 0.3929 -0.0064 -0.0473 0.0001  23  ALA   A CB  
134  N N   . THR   A 18  ? 0.2081 0.4118 0.4036 -0.0071 -0.0591 -0.0003 24  THR   A N   
135  C CA  . THR   A 18  ? 0.2107 0.4140 0.4142 -0.0089 -0.0660 0.0000  24  THR   A CA  
136  C C   . THR   A 18  ? 0.2161 0.4220 0.4321 -0.0110 -0.0653 0.0018  24  THR   A C   
137  O O   . THR   A 18  ? 0.2127 0.4211 0.4308 -0.0110 -0.0592 0.0033  24  THR   A O   
138  C CB  . THR   A 18  ? 0.2214 0.4281 0.4318 -0.0082 -0.0685 0.0022  24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.2224 0.4353 0.4447 -0.0076 -0.0628 0.0047  24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.2279 0.4320 0.4269 -0.0063 -0.0692 0.0013  24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.2232 0.4287 0.4476 -0.0132 -0.0719 0.0021  25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.2423 0.4506 0.4804 -0.0157 -0.0719 0.0043  25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.2286 0.4448 0.4785 -0.0151 -0.0651 0.0080  25  HIS   A C   
144  O O   . HIS   A 19  ? 0.2275 0.4457 0.4819 -0.0162 -0.0601 0.0098  25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.2855 0.4925 0.5310 -0.0184 -0.0811 0.0040  25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.3807 0.5792 0.6171 -0.0202 -0.0860 0.0002  25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.4220 0.6141 0.6417 -0.0184 -0.0842 -0.0036 25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.4049 0.6002 0.6474 -0.0237 -0.0919 -0.0007 25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.4342 0.6192 0.6503 -0.0205 -0.0886 -0.0069 25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.4300 0.6161 0.6588 -0.0239 -0.0935 -0.0054 25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.2165 0.4366 0.4704 -0.0133 -0.0645 0.0090  26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.2162 0.4429 0.4808 -0.0123 -0.0571 0.0116  26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.2036 0.4300 0.4583 -0.0114 -0.0483 0.0110  26  ASN   A C   
154  O O   . ASN   A 20  ? 0.2028 0.4331 0.4641 -0.0123 -0.0417 0.0130  26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.2547 0.4841 0.5246 -0.0100 -0.0583 0.0124  26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.3407 0.5767 0.6249 -0.0091 -0.0509 0.0147  26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.3726 0.6140 0.6744 -0.0103 -0.0515 0.0174  26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.3582 0.5941 0.6356 -0.0070 -0.0432 0.0136  26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.1888 0.4105 0.4277 -0.0100 -0.0482 0.0086  27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.1771 0.3983 0.4064 -0.0097 -0.0413 0.0082  27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.1612 0.3824 0.3914 -0.0120 -0.0394 0.0099  27  ASP   A C   
162  O O   . ASP   A 21  ? 0.1576 0.3812 0.3872 -0.0130 -0.0330 0.0116  27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.1877 0.4040 0.4015 -0.0081 -0.0428 0.0057  27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.2246 0.4406 0.4349 -0.0060 -0.0430 0.0046  27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.2218 0.4409 0.4379 -0.0053 -0.0387 0.0054  27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.2475 0.4595 0.4489 -0.0051 -0.0472 0.0028  27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.1474 0.3651 0.3782 -0.0131 -0.0450 0.0094  28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.1638 0.3805 0.3964 -0.0153 -0.0439 0.0114  28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.1655 0.3872 0.4122 -0.0177 -0.0411 0.0150  28  TRP   A C   
170  O O   . TRP   A 22  ? 0.1661 0.3891 0.4133 -0.0195 -0.0366 0.0179  28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.1680 0.3787 0.3991 -0.0158 -0.0505 0.0094  28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.1839 0.3893 0.4016 -0.0138 -0.0513 0.0065  28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.2019 0.4032 0.4121 -0.0124 -0.0555 0.0027  28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.1911 0.3955 0.4018 -0.0132 -0.0476 0.0075  28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.2134 0.4113 0.4131 -0.0106 -0.0537 0.0010  28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.2087 0.4087 0.4096 -0.0111 -0.0494 0.0040  28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.1968 0.4035 0.4090 -0.0145 -0.0434 0.0113  28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.2213 0.4197 0.4158 -0.0099 -0.0470 0.0044  28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.2114 0.4164 0.4162 -0.0136 -0.0420 0.0120  28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.2210 0.4222 0.4181 -0.0112 -0.0437 0.0086  28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.1571 0.3820 0.4157 -0.0179 -0.0438 0.0152  29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.1528 0.3835 0.4272 -0.0200 -0.0408 0.0187  29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.1587 0.3941 0.4328 -0.0194 -0.0310 0.0201  29  ALA   A C   
184  O O   . ALA   A 23  ? 0.1632 0.4023 0.4448 -0.0217 -0.0256 0.0232  29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.1508 0.3844 0.4387 -0.0200 -0.0465 0.0187  29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.1470 0.3817 0.4119 -0.0168 -0.0285 0.0176  30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.1386 0.3763 0.4011 -0.0163 -0.0193 0.0178  30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.1309 0.3647 0.3751 -0.0164 -0.0165 0.0166  30  ASN   A C   
189  O O   . ASN   A 24  ? 0.1280 0.3618 0.3652 -0.0154 -0.0114 0.0149  30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.1517 0.3916 0.4206 -0.0135 -0.0183 0.0162  30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.1726 0.4176 0.4617 -0.0138 -0.0205 0.0184  30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.1901 0.4402 0.4907 -0.0150 -0.0141 0.0206  30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.1643 0.4083 0.4582 -0.0131 -0.0298 0.0181  30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.1192 0.3498 0.3571 -0.0179 -0.0198 0.0178  31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.1339 0.3614 0.3568 -0.0181 -0.0188 0.0175  31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.1529 0.3825 0.3700 -0.0203 -0.0108 0.0193  31  LEU   A C   
197  O O   . LEU   A 25  ? 0.1471 0.3793 0.3705 -0.0229 -0.0071 0.0225  31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.1386 0.3627 0.3602 -0.0192 -0.0238 0.0192  31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.1614 0.3828 0.3706 -0.0196 -0.0235 0.0202  31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.1786 0.3978 0.3782 -0.0169 -0.0253 0.0166  31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.1741 0.3925 0.3862 -0.0207 -0.0275 0.0228  31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.1596 0.3875 0.3639 -0.0198 -0.0086 0.0174  32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.1775 0.4060 0.3721 -0.0225 -0.0021 0.0185  32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.1954 0.4214 0.3786 -0.0240 -0.0055 0.0207  32  VAL   A C   
205  O O   . VAL   A 26  ? 0.2064 0.4328 0.3857 -0.0273 -0.0035 0.0246  32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.1845 0.4125 0.3733 -0.0213 0.0029  0.0145  32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.1904 0.4174 0.3653 -0.0246 0.0085  0.0148  32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.1749 0.4059 0.3769 -0.0197 0.0071  0.0131  32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.1852 0.4087 0.3639 -0.0217 -0.0106 0.0187  33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.1858 0.4076 0.3562 -0.0226 -0.0139 0.0208  33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.1690 0.3885 0.3400 -0.0192 -0.0195 0.0184  33  TRP   A C   
212  O O   . TRP   A 27  ? 0.1599 0.3788 0.3314 -0.0169 -0.0198 0.0147  33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.1891 0.4110 0.3464 -0.0249 -0.0104 0.0207  33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.2036 0.4245 0.3532 -0.0255 -0.0145 0.0225  33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.2164 0.4377 0.3631 -0.0281 -0.0166 0.0276  33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.2098 0.4296 0.3555 -0.0233 -0.0173 0.0197  33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.2214 0.4422 0.3634 -0.0275 -0.0206 0.0282  33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.2200 0.4401 0.3612 -0.0247 -0.0207 0.0232  33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.2139 0.4327 0.3600 -0.0205 -0.0173 0.0152  33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.2260 0.4459 0.3641 -0.0233 -0.0235 0.0220  33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.2262 0.4442 0.3675 -0.0194 -0.0198 0.0140  33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.2252 0.4440 0.3630 -0.0208 -0.0227 0.0173  33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.1510 0.3688 0.3222 -0.0190 -0.0235 0.0207  34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.1585 0.3739 0.3296 -0.0160 -0.0276 0.0182  34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.1703 0.3851 0.3390 -0.0162 -0.0298 0.0213  34  GLU   A C   
226  O O   . GLU   A 28  ? 0.1751 0.3905 0.3454 -0.0185 -0.0300 0.0259  34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.1514 0.3643 0.3308 -0.0141 -0.0308 0.0161  34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.1987 0.4107 0.3863 -0.0157 -0.0321 0.0192  34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.2675 0.4763 0.4570 -0.0151 -0.0352 0.0211  34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.2961 0.5043 0.4917 -0.0169 -0.0357 0.0248  34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.2832 0.4901 0.4691 -0.0127 -0.0367 0.0190  34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.1674 0.3812 0.3333 -0.0139 -0.0316 0.0192  35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.1654 0.3792 0.3313 -0.0136 -0.0337 0.0222  35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.1533 0.3646 0.3210 -0.0099 -0.0352 0.0185  35  ASP   A C   
235  O O   . ASP   A 29  ? 0.1546 0.3664 0.3173 -0.0088 -0.0343 0.0154  35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.1929 0.4099 0.3510 -0.0159 -0.0328 0.0244  35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.2531 0.4714 0.4126 -0.0161 -0.0356 0.0286  35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.2612 0.4778 0.4277 -0.0131 -0.0375 0.0284  35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.2697 0.4906 0.4235 -0.0193 -0.0361 0.0321  35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.1422 0.3503 0.3166 -0.0083 -0.0372 0.0187  36  SER   A N   
241  C CA  A SER   A 30  ? 0.1444 0.3491 0.3199 -0.0049 -0.0378 0.0147  36  SER   A CA  
242  C CA  B SER   A 30  ? 0.1485 0.3532 0.3238 -0.0049 -0.0378 0.0146  36  SER   A CA  
243  C C   . SER   A 30  ? 0.1529 0.3600 0.3262 -0.0036 -0.0370 0.0154  36  SER   A C   
244  O O   . SER   A 30  ? 0.1581 0.3640 0.3286 -0.0014 -0.0360 0.0115  36  SER   A O   
245  C CB  A SER   A 30  ? 0.1478 0.3480 0.3314 -0.0037 -0.0395 0.0151  36  SER   A CB  
246  C CB  B SER   A 30  ? 0.1642 0.3642 0.3472 -0.0036 -0.0394 0.0143  36  SER   A CB  
247  O OG  A SER   A 30  ? 0.1398 0.3359 0.3236 -0.0006 -0.0393 0.0105  36  SER   A OG  
248  O OG  B SER   A 30  ? 0.1710 0.3718 0.3598 -0.0036 -0.0402 0.0193  36  SER   A OG  
249  N N   . SER   A 31  ? 0.1470 0.3578 0.3219 -0.0053 -0.0378 0.0207  37  SER   A N   
250  C CA  . SER   A 31  ? 0.1613 0.3752 0.3362 -0.0045 -0.0378 0.0222  37  SER   A CA  
251  C C   . SER   A 31  ? 0.1643 0.3809 0.3307 -0.0057 -0.0363 0.0201  37  SER   A C   
252  O O   . SER   A 31  ? 0.1785 0.3975 0.3452 -0.0049 -0.0360 0.0204  37  SER   A O   
253  C CB  . SER   A 31  ? 0.1926 0.4097 0.3724 -0.0062 -0.0402 0.0291  37  SER   A CB  
254  O OG  . SER   A 31  ? 0.2478 0.4682 0.4203 -0.0105 -0.0408 0.0323  37  SER   A OG  
255  N N   . ARG   A 32  ? 0.1540 0.3701 0.3143 -0.0074 -0.0351 0.0180  38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.1520 0.3694 0.3047 -0.0084 -0.0335 0.0156  38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.1580 0.3721 0.3085 -0.0062 -0.0322 0.0106  38  ARG   A C   
258  O O   . ARG   A 32  ? 0.1565 0.3710 0.3018 -0.0066 -0.0309 0.0087  38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.1625 0.3812 0.3098 -0.0121 -0.0325 0.0171  38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.1770 0.3988 0.3224 -0.0154 -0.0341 0.0220  38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.1845 0.4067 0.3223 -0.0194 -0.0322 0.0226  38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.1890 0.4107 0.3196 -0.0204 -0.0300 0.0189  38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.2127 0.4347 0.3348 -0.0244 -0.0286 0.0191  38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.2034 0.4264 0.3218 -0.0280 -0.0292 0.0230  38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.1845 0.4051 0.3012 -0.0250 -0.0265 0.0153  38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.1547 0.3654 0.3090 -0.0044 -0.0331 0.0087  39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.1547 0.3622 0.3068 -0.0030 -0.0332 0.0046  39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.1594 0.3679 0.3090 -0.0046 -0.0324 0.0042  39  ASP   A C   
269  O O   . ASP   A 33  ? 0.1509 0.3580 0.2971 -0.0037 -0.0323 0.0018  39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.1653 0.3712 0.3132 -0.0009 -0.0323 0.0019  39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.1718 0.3737 0.3158 0.0002  -0.0333 -0.0019 39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.1893 0.3882 0.3360 0.0004  -0.0353 -0.0032 39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.1618 0.3635 0.3001 0.0005  -0.0323 -0.0031 39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.1617 0.3724 0.3133 -0.0069 -0.0316 0.0068  40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.1693 0.3810 0.3199 -0.0083 -0.0295 0.0063  40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.1668 0.3788 0.3241 -0.0092 -0.0295 0.0073  40  LEU   A C   
277  O O   . LEU   A 34  ? 0.1578 0.3700 0.3188 -0.0102 -0.0304 0.0100  40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.1829 0.3969 0.3281 -0.0109 -0.0270 0.0078  40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.2094 0.4234 0.3483 -0.0109 -0.0263 0.0065  40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.2180 0.4335 0.3512 -0.0143 -0.0241 0.0075  40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.2117 0.4236 0.3500 -0.0090 -0.0258 0.0033  40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.1604 0.3725 0.3202 -0.0089 -0.0285 0.0058  41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.1688 0.3821 0.3364 -0.0099 -0.0279 0.0069  41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.1756 0.3907 0.3443 -0.0102 -0.0240 0.0060  41  LEU   A C   
285  O O   . LEU   A 35  ? 0.1845 0.3986 0.3509 -0.0086 -0.0240 0.0038  41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.1733 0.3846 0.3477 -0.0087 -0.0323 0.0059  41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.1904 0.4034 0.3752 -0.0100 -0.0324 0.0075  41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.1918 0.4020 0.3815 -0.0101 -0.0371 0.0073  41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.1955 0.4105 0.3859 -0.0094 -0.0317 0.0065  41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.1677 0.3851 0.3399 -0.0122 -0.0201 0.0077  42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.1631 0.3821 0.3380 -0.0124 -0.0151 0.0066  42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.1593 0.3809 0.3468 -0.0126 -0.0144 0.0080  42  VAL   A C   
293  O O   . VAL   A 36  ? 0.1617 0.3843 0.3520 -0.0146 -0.0144 0.0107  42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.1827 0.4020 0.3488 -0.0151 -0.0094 0.0068  42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.1954 0.4156 0.3649 -0.0151 -0.0030 0.0050  42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.1826 0.3998 0.3374 -0.0154 -0.0108 0.0057  42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.1525 0.3751 0.3486 -0.0108 -0.0143 0.0067  43  SER   A N   
298  C CA  . SER   A 37  ? 0.1618 0.3878 0.3723 -0.0109 -0.0137 0.0083  43  SER   A CA  
299  C C   . SER   A 37  ? 0.1834 0.4116 0.3997 -0.0102 -0.0067 0.0073  43  SER   A C   
300  O O   . SER   A 37  ? 0.1937 0.4198 0.4035 -0.0090 -0.0042 0.0048  43  SER   A O   
301  C CB  . SER   A 37  ? 0.1607 0.3861 0.3788 -0.0093 -0.0213 0.0082  43  SER   A CB  
302  O OG  . SER   A 37  ? 0.1744 0.3984 0.3914 -0.0068 -0.0231 0.0064  43  SER   A OG  
303  N N   . SER   A 38  ? 0.1802 0.4127 0.4097 -0.0110 -0.0031 0.0091  44  SER   A N   
304  C CA  . SER   A 38  ? 0.1954 0.4302 0.4324 -0.0100 0.0048  0.0080  44  SER   A CA  
305  C C   . SER   A 38  ? 0.2078 0.4442 0.4588 -0.0067 0.0015  0.0077  44  SER   A C   
306  O O   . SER   A 38  ? 0.2176 0.4548 0.4756 -0.0061 -0.0066 0.0093  44  SER   A O   
307  C CB  . SER   A 38  ? 0.2085 0.4476 0.4537 -0.0125 0.0114  0.0103  44  SER   A CB  
308  O OG  . SER   A 38  ? 0.2308 0.4731 0.4889 -0.0132 0.0059  0.0135  44  SER   A OG  
309  N N   . THR   A 39  ? 0.2112 0.4475 0.4660 -0.0046 0.0074  0.0057  45  THR   A N   
310  C CA  . THR   A 39  ? 0.2254 0.4631 0.4949 -0.0013 0.0044  0.0062  45  THR   A CA  
311  C C   . THR   A 39  ? 0.2436 0.4858 0.5299 -0.0001 0.0132  0.0064  45  THR   A C   
312  O O   . THR   A 39  ? 0.2411 0.4834 0.5230 -0.0016 0.0230  0.0048  45  THR   A O   
313  C CB  . THR   A 39  ? 0.2388 0.4713 0.4991 0.0010  0.0028  0.0038  45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.2472 0.4769 0.5001 0.0008  0.0124  0.0005  45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.2461 0.4744 0.4907 0.0002  -0.0050 0.0035  45  THR   A CG2 
316  N N   . THR   A 40  ? 0.2610 0.5069 0.5663 0.0026  0.0099  0.0086  46  THR   A N   
317  C CA  . THR   A 40  ? 0.2788 0.5294 0.6034 0.0044  0.0182  0.0090  46  THR   A CA  
318  C C   . THR   A 40  ? 0.2859 0.5322 0.6090 0.0076  0.0245  0.0055  46  THR   A C   
319  O O   . THR   A 40  ? 0.2976 0.5448 0.6268 0.0084  0.0358  0.0034  46  THR   A O   
320  C CB  . THR   A 40  ? 0.3075 0.5649 0.6558 0.0055  0.0113  0.0135  46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.3362 0.5916 0.6886 0.0085  0.0030  0.0145  46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.3103 0.5701 0.6579 0.0020  0.0034  0.0164  46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.2809 0.5221 0.5956 0.0093  0.0176  0.0049  47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.2841 0.5203 0.5975 0.0122  0.0225  0.0019  47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.2918 0.5207 0.5808 0.0101  0.0263  -0.0026 47  ALA   A C   
326  O O   . ALA   A 41  ? 0.2925 0.5198 0.5655 0.0073  0.0210  -0.0024 47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.2844 0.5195 0.6056 0.0152  0.0128  0.0047  47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.2886 0.5130 0.5760 0.0115  0.0350  -0.0067 48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.2947 0.5118 0.5604 0.0092  0.0388  -0.0112 48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.2794 0.4916 0.5355 0.0099  0.0301  -0.0107 48  GLN   A C   
331  O O   . GLN   A 42  ? 0.2795 0.4909 0.5467 0.0133  0.0261  -0.0089 48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.3280 0.5409 0.5962 0.0104  0.0510  -0.0162 48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.4120 0.6269 0.6775 0.0078  0.0622  -0.0187 48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.5194 0.7278 0.7597 0.0033  0.0665  -0.0233 48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 0.5667 0.7676 0.7985 0.0036  0.0694  -0.0277 48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.5252 0.7360 0.7534 -0.0010 0.0664  -0.0220 48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.2619 0.4708 0.4978 0.0066  0.0277  -0.0121 49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.2572 0.4616 0.4827 0.0067  0.0209  -0.0119 49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.2526 0.4496 0.4699 0.0065  0.0263  -0.0163 49  GLY   A C   
340  O O   . GLY   A 43  ? 0.2590 0.4539 0.4748 0.0055  0.0358  -0.0203 49  GLY   A O   
341  N N   . CYS   A 44  ? 0.2387 0.4314 0.4502 0.0070  0.0208  -0.0157 50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.2400 0.4251 0.4449 0.0067  0.0252  -0.0196 50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.2415 0.4231 0.4269 0.0027  0.0225  -0.0210 50  CYS   A C   
344  O O   . CYS   A 44  ? 0.2504 0.4255 0.4300 0.0018  0.0253  -0.0241 50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.2467 0.4287 0.4640 0.0107  0.0226  -0.0176 50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.3094 0.4959 0.5527 0.0155  0.0252  -0.0152 50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.2285 0.4144 0.4056 0.0005  0.0170  -0.0186 51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.2384 0.4220 0.3997 -0.0029 0.0143  -0.0193 51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.2422 0.4241 0.3917 -0.0072 0.0201  -0.0231 51  ASP   A C   
350  O O   . ASP   A 45  ? 0.2403 0.4245 0.3920 -0.0078 0.0252  -0.0241 51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.2729 0.4610 0.4304 -0.0033 0.0064  -0.0154 51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.3374 0.5261 0.5019 -0.0002 -0.0001 -0.0119 51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.3511 0.5356 0.5182 0.0013  -0.0006 -0.0117 51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.3216 0.5147 0.4889 0.0005  -0.0049 -0.0092 51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.2469 0.4251 0.3839 -0.0105 0.0191  -0.0248 52  THR   A N   
356  C CA  . THR   A 46  ? 0.2615 0.4376 0.3848 -0.0155 0.0228  -0.0280 52  THR   A CA  
357  C C   . THR   A 46  ? 0.2599 0.4395 0.3740 -0.0184 0.0160  -0.0249 52  THR   A C   
358  O O   . THR   A 46  ? 0.2565 0.4358 0.3706 -0.0177 0.0110  -0.0231 52  THR   A O   
359  C CB  . THR   A 46  ? 0.2956 0.4633 0.4129 -0.0174 0.0268  -0.0330 52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.3169 0.4808 0.4424 -0.0149 0.0346  -0.0366 52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.3073 0.4723 0.4076 -0.0236 0.0278  -0.0358 52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.2551 0.4381 0.3623 -0.0215 0.0161  -0.0239 53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.2512 0.4379 0.3516 -0.0240 0.0100  -0.0205 53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.2637 0.4464 0.3514 -0.0291 0.0099  -0.0230 53  ILE   A C   
365  O O   . ILE   A 47  ? 0.2773 0.4557 0.3574 -0.0322 0.0152  -0.0269 53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.2561 0.4478 0.3558 -0.0252 0.0095  -0.0176 53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.2569 0.4522 0.3697 -0.0208 0.0097  -0.0156 53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.2650 0.4605 0.3596 -0.0274 0.0031  -0.0137 53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.2547 0.4521 0.3753 -0.0171 0.0037  -0.0130 53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.2519 0.4358 0.3374 -0.0302 0.0042  -0.0208 54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.2503 0.4313 0.3250 -0.0355 0.0029  -0.0225 54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.2405 0.4245 0.3057 -0.0402 0.0013  -0.0206 54  ALA   A C   
373  O O   . ALA   A 48  ? 0.2270 0.4168 0.2960 -0.0389 -0.0016 -0.0163 54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.2489 0.4316 0.3262 -0.0352 -0.0026 -0.0199 54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.2379 0.4174 0.2905 -0.0459 0.0029  -0.0238 55  ARG   A N   
376  C CA  . ARG   A 49  ? 0.2443 0.4258 0.2855 -0.0516 0.0004  -0.0218 55  ARG   A CA  
377  C C   . ARG   A 49  ? 0.2500 0.4294 0.2833 -0.0569 -0.0044 -0.0224 55  ARG   A C   
378  O O   . ARG   A 49  ? 0.2651 0.4374 0.2880 -0.0612 -0.0015 -0.0276 55  ARG   A O   
379  C CB  . ARG   A 49  ? 0.2620 0.4393 0.2936 -0.0542 0.0075  -0.0255 55  ARG   A CB  
380  C CG  . ARG   A 49  ? 0.2913 0.4707 0.3331 -0.0490 0.0130  -0.0252 55  ARG   A CG  
381  C CD  . ARG   A 49  ? 0.2988 0.4860 0.3490 -0.0463 0.0085  -0.0186 55  ARG   A CD  
382  N NE  . ARG   A 49  ? 0.3068 0.4958 0.3677 -0.0418 0.0133  -0.0186 55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.2964 0.4910 0.3669 -0.0386 0.0103  -0.0139 55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.2543 0.4531 0.3254 -0.0391 0.0032  -0.0091 55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.2833 0.4793 0.3639 -0.0351 0.0144  -0.0141 55  ARG   A NH2 
386  N N   . CYS   A 50  ? 0.2400 0.4253 0.2794 -0.0564 -0.0113 -0.0174 56  CYS   A N   
387  C CA  . CYS   A 50  ? 0.2414 0.4263 0.2783 -0.0604 -0.0164 -0.0170 56  CYS   A CA  
388  C C   . CYS   A 50  ? 0.2428 0.4365 0.2873 -0.0600 -0.0237 -0.0100 56  CYS   A C   
389  O O   . CYS   A 50  ? 0.2421 0.4411 0.2945 -0.0558 -0.0244 -0.0062 56  CYS   A O   
390  C CB  . CYS   A 50  ? 0.2419 0.4225 0.2856 -0.0571 -0.0137 -0.0203 56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.2714 0.4580 0.3316 -0.0492 -0.0149 -0.0160 56  CYS   A SG  
392  N N   A ASP   A 51  ? 0.2374 0.4325 0.2815 -0.0640 -0.0289 -0.0086 57  ASP   A N   
393  N N   B ASP   A 51  ? 0.2469 0.4417 0.2906 -0.0641 -0.0288 -0.0088 57  ASP   A N   
394  C CA  A ASP   A 51  ? 0.2313 0.4349 0.2854 -0.0629 -0.0348 -0.0022 57  ASP   A CA  
395  C CA  B ASP   A 51  ? 0.2510 0.4541 0.3037 -0.0640 -0.0352 -0.0025 57  ASP   A CA  
396  C C   A ASP   A 51  ? 0.2321 0.4368 0.2965 -0.0600 -0.0348 -0.0021 57  ASP   A C   
397  C C   B ASP   A 51  ? 0.2427 0.4465 0.3056 -0.0610 -0.0350 -0.0026 57  ASP   A C   
398  O O   A ASP   A 51  ? 0.2228 0.4338 0.2947 -0.0606 -0.0393 0.0024  57  ASP   A O   
399  O O   B ASP   A 51  ? 0.2358 0.4452 0.3050 -0.0626 -0.0397 0.0013  57  ASP   A O   
400  C CB  A ASP   A 51  ? 0.2415 0.4487 0.2899 -0.0698 -0.0419 0.0016  57  ASP   A CB  
401  C CB  B ASP   A 51  ? 0.2857 0.4903 0.3305 -0.0719 -0.0417 -0.0003 57  ASP   A CB  
402  C CG  A ASP   A 51  ? 0.2687 0.4716 0.3093 -0.0766 -0.0444 -0.0012 57  ASP   A CG  
403  C CG  B ASP   A 51  ? 0.3632 0.5773 0.4164 -0.0721 -0.0486 0.0075  57  ASP   A CG  
404  O OD1 A ASP   A 51  ? 0.2742 0.4700 0.3120 -0.0763 -0.0399 -0.0070 57  ASP   A OD1 
405  O OD1 B ASP   A 51  ? 0.3796 0.5988 0.4456 -0.0659 -0.0478 0.0106  57  ASP   A OD1 
406  O OD2 A ASP   A 51  ? 0.3005 0.5071 0.3382 -0.0824 -0.0514 0.0025  57  ASP   A OD2 
407  O OD2 B ASP   A 51  ? 0.3970 0.6131 0.4441 -0.0785 -0.0548 0.0104  57  ASP   A OD2 
408  N N   . CYS   A 52  ? 0.2362 0.4347 0.3011 -0.0571 -0.0296 -0.0066 58  CYS   A N   
409  C CA  . CYS   A 52  ? 0.2289 0.4272 0.3018 -0.0545 -0.0289 -0.0064 58  CYS   A CA  
410  C C   . CYS   A 52  ? 0.2104 0.4167 0.2948 -0.0505 -0.0311 -0.0012 58  CYS   A C   
411  O O   . CYS   A 52  ? 0.1867 0.3969 0.2748 -0.0467 -0.0310 0.0010  58  CYS   A O   
412  C CB  . CYS   A 52  ? 0.2375 0.4289 0.3110 -0.0504 -0.0232 -0.0106 58  CYS   A CB  
413  S SG  . CYS   A 52  ? 0.2844 0.4648 0.3481 -0.0548 -0.0196 -0.0174 58  CYS   A SG  
414  N N   . GLN   A 53  ? 0.1953 0.4036 0.2855 -0.0513 -0.0324 0.0005  59  GLN   A N   
415  C CA  . GLN   A 53  ? 0.1881 0.4031 0.2889 -0.0475 -0.0329 0.0047  59  GLN   A CA  
416  C C   . GLN   A 53  ? 0.1797 0.3919 0.2841 -0.0448 -0.0295 0.0040  59  GLN   A C   
417  O O   . GLN   A 53  ? 0.1717 0.3889 0.2837 -0.0430 -0.0294 0.0071  59  GLN   A O   
418  C CB  . GLN   A 53  ? 0.2051 0.4279 0.3120 -0.0510 -0.0378 0.0094  59  GLN   A CB  
419  C CG  . GLN   A 53  ? 0.2599 0.4877 0.3676 -0.0509 -0.0411 0.0125  59  GLN   A CG  
420  C CD  . GLN   A 53  ? 0.3098 0.5463 0.4267 -0.0534 -0.0462 0.0181  59  GLN   A CD  
421  O OE1 . GLN   A 53  ? 0.3234 0.5614 0.4368 -0.0592 -0.0515 0.0198  59  GLN   A OE1 
422  N NE2 . GLN   A 53  ? 0.2953 0.5374 0.4244 -0.0490 -0.0448 0.0211  59  GLN   A NE2 
423  N N   . THR   A 54  ? 0.1780 0.3820 0.2771 -0.0448 -0.0267 0.0001  60  THR   A N   
424  C CA  . THR   A 54  ? 0.1795 0.3797 0.2811 -0.0422 -0.0238 -0.0002 60  THR   A CA  
425  C C   . THR   A 54  ? 0.1667 0.3604 0.2650 -0.0386 -0.0207 -0.0034 60  THR   A C   
426  O O   . THR   A 54  ? 0.1584 0.3485 0.2518 -0.0399 -0.0199 -0.0067 60  THR   A O   
427  C CB  . THR   A 54  ? 0.2141 0.4106 0.3155 -0.0469 -0.0242 -0.0006 60  THR   A CB  
428  O OG1 . THR   A 54  ? 0.2443 0.4332 0.3385 -0.0502 -0.0237 -0.0051 60  THR   A OG1 
429  C CG2 . THR   A 54  ? 0.2172 0.4205 0.3234 -0.0511 -0.0276 0.0028  60  THR   A CG2 
430  N N   . GLY   A 55  ? 0.1575 0.3501 0.2589 -0.0343 -0.0190 -0.0023 61  GLY   A N   
431  C CA  . GLY   A 55  ? 0.1615 0.3490 0.2623 -0.0304 -0.0169 -0.0042 61  GLY   A CA  
432  C C   . GLY   A 55  ? 0.1657 0.3525 0.2692 -0.0268 -0.0164 -0.0017 61  GLY   A C   
433  O O   . GLY   A 55  ? 0.1611 0.3496 0.2659 -0.0279 -0.0165 0.0009  61  GLY   A O   
434  N N   . VAL   A 56  ? 0.1670 0.3512 0.2714 -0.0229 -0.0158 -0.0022 62  VAL   A N   
435  C CA  . VAL   A 56  ? 0.1747 0.3575 0.2801 -0.0196 -0.0161 0.0002  62  VAL   A CA  
436  C C   . VAL   A 56  ? 0.1753 0.3607 0.2816 -0.0160 -0.0172 0.0001  62  VAL   A C   
437  O O   . VAL   A 56  ? 0.1905 0.3762 0.2982 -0.0154 -0.0169 -0.0020 62  VAL   A O   
438  C CB  . VAL   A 56  ? 0.1946 0.3699 0.3013 -0.0190 -0.0153 0.0000  62  VAL   A CB  
439  C CG1 . VAL   A 56  ? 0.1996 0.3732 0.3062 -0.0162 -0.0166 0.0034  62  VAL   A CG1 
440  C CG2 . VAL   A 56  ? 0.2162 0.3877 0.3222 -0.0230 -0.0142 -0.0005 62  VAL   A CG2 
441  N N   . TYR   A 57  ? 0.1658 0.3530 0.2711 -0.0139 -0.0182 0.0022  63  TYR   A N   
442  C CA  . TYR   A 57  ? 0.1614 0.3502 0.2672 -0.0108 -0.0197 0.0019  63  TYR   A CA  
443  C C   . TYR   A 57  ? 0.1786 0.3642 0.2822 -0.0087 -0.0214 0.0038  63  TYR   A C   
444  O O   . TYR   A 57  ? 0.1804 0.3638 0.2809 -0.0096 -0.0209 0.0060  63  TYR   A O   
445  C CB  . TYR   A 57  ? 0.1585 0.3527 0.2642 -0.0106 -0.0198 0.0018  63  TYR   A CB  
446  C CG  . TYR   A 57  ? 0.1751 0.3706 0.2780 -0.0099 -0.0191 0.0034  63  TYR   A CG  
447  C CD1 . TYR   A 57  ? 0.1801 0.3774 0.2828 -0.0120 -0.0171 0.0049  63  TYR   A CD1 
448  C CD2 . TYR   A 57  ? 0.1838 0.3787 0.2843 -0.0075 -0.0201 0.0031  63  TYR   A CD2 
449  C CE1 . TYR   A 57  ? 0.1992 0.3979 0.2998 -0.0113 -0.0153 0.0062  63  TYR   A CE1 
450  C CE2 . TYR   A 57  ? 0.2024 0.3978 0.2990 -0.0069 -0.0185 0.0038  63  TYR   A CE2 
451  C CZ  . TYR   A 57  ? 0.2084 0.4058 0.3052 -0.0087 -0.0156 0.0054  63  TYR   A CZ  
452  O OH  . TYR   A 57  ? 0.2140 0.4121 0.3073 -0.0082 -0.0128 0.0061  63  TYR   A OH  
453  N N   . TYR   A 58  ? 0.1802 0.3654 0.2853 -0.0064 -0.0236 0.0034  64  TYR   A N   
454  C CA  . TYR   A 58  ? 0.1828 0.3649 0.2851 -0.0049 -0.0264 0.0055  64  TYR   A CA  
455  C C   . TYR   A 58  ? 0.1847 0.3685 0.2814 -0.0043 -0.0272 0.0053  64  TYR   A C   
456  O O   . TYR   A 58  ? 0.1808 0.3673 0.2794 -0.0035 -0.0277 0.0033  64  TYR   A O   
457  C CB  . TYR   A 58  ? 0.1840 0.3643 0.2920 -0.0030 -0.0292 0.0057  64  TYR   A CB  
458  C CG  . TYR   A 58  ? 0.2044 0.3820 0.3092 -0.0019 -0.0335 0.0085  64  TYR   A CG  
459  C CD1 . TYR   A 58  ? 0.2247 0.3982 0.3257 -0.0025 -0.0344 0.0118  64  TYR   A CD1 
460  C CD2 . TYR   A 58  ? 0.2271 0.4058 0.3321 -0.0007 -0.0371 0.0080  64  TYR   A CD2 
461  C CE1 . TYR   A 58  ? 0.2358 0.4065 0.3326 -0.0020 -0.0391 0.0150  64  TYR   A CE1 
462  C CE2 . TYR   A 58  ? 0.2394 0.4153 0.3403 -0.0004 -0.0420 0.0106  64  TYR   A CE2 
463  C CZ  . TYR   A 58  ? 0.2504 0.4223 0.3465 -0.0011 -0.0431 0.0142  64  TYR   A CZ  
464  O OH  . TYR   A 58  ? 0.2733 0.4422 0.3637 -0.0013 -0.0485 0.0174  64  TYR   A OH  
465  N N   . CYS   A 59  ? 0.1850 0.3665 0.2745 -0.0047 -0.0272 0.0074  65  CYS   A N   
466  C CA  . CYS   A 59  ? 0.1894 0.3711 0.2718 -0.0043 -0.0271 0.0066  65  CYS   A CA  
467  C C   . CYS   A 59  ? 0.1947 0.3720 0.2710 -0.0038 -0.0315 0.0082  65  CYS   A C   
468  O O   . CYS   A 59  ? 0.1916 0.3656 0.2621 -0.0048 -0.0319 0.0113  65  CYS   A O   
469  C CB  . CYS   A 59  ? 0.1968 0.3797 0.2749 -0.0057 -0.0227 0.0075  65  CYS   A CB  
470  S SG  . CYS   A 59  ? 0.2205 0.4027 0.2889 -0.0050 -0.0207 0.0060  65  CYS   A SG  
471  N N   . SER   A 60  ? 0.1897 0.3668 0.2672 -0.0027 -0.0354 0.0066  66  SER   A N   
472  C CA  . SER   A 60  ? 0.2068 0.3799 0.2788 -0.0027 -0.0409 0.0084  66  SER   A CA  
473  C C   . SER   A 60  ? 0.2169 0.3865 0.2746 -0.0041 -0.0406 0.0088  66  SER   A C   
474  O O   . SER   A 60  ? 0.2314 0.3970 0.2822 -0.0051 -0.0446 0.0120  66  SER   A O   
475  C CB  . SER   A 60  ? 0.2340 0.4081 0.3114 -0.0018 -0.0453 0.0066  66  SER   A CB  
476  O OG  . SER   A 60  ? 0.2732 0.4477 0.3463 -0.0018 -0.0441 0.0029  66  SER   A OG  
477  N N   . SER   A 61  ? 0.2058 0.3767 0.2589 -0.0041 -0.0356 0.0058  67  SER   A N   
478  C CA  . SER   A 61  ? 0.2165 0.3839 0.2555 -0.0053 -0.0336 0.0054  67  SER   A CA  
479  C C   . SER   A 61  ? 0.2226 0.3887 0.2561 -0.0069 -0.0303 0.0094  67  SER   A C   
480  O O   . SER   A 61  ? 0.2322 0.3950 0.2528 -0.0084 -0.0283 0.0098  67  SER   A O   
481  C CB  . SER   A 61  ? 0.2261 0.3951 0.2641 -0.0044 -0.0285 0.0007  67  SER   A CB  
482  O OG  . SER   A 61  ? 0.2285 0.4026 0.2747 -0.0039 -0.0228 0.0008  67  SER   A OG  
483  N N   . ARG   A 62  ? 0.2094 0.3775 0.2520 -0.0070 -0.0298 0.0122  68  ARG   A N   
484  C CA  . ARG   A 62  ? 0.2163 0.3827 0.2556 -0.0087 -0.0276 0.0166  68  ARG   A CA  
485  C C   . ARG   A 62  ? 0.2293 0.3929 0.2739 -0.0088 -0.0327 0.0208  68  ARG   A C   
486  O O   . ARG   A 62  ? 0.2254 0.3866 0.2681 -0.0103 -0.0318 0.0250  68  ARG   A O   
487  C CB  . ARG   A 62  ? 0.2153 0.3864 0.2618 -0.0092 -0.0213 0.0158  68  ARG   A CB  
488  C CG  . ARG   A 62  ? 0.2272 0.4013 0.2702 -0.0091 -0.0154 0.0130  68  ARG   A CG  
489  C CD  . ARG   A 62  ? 0.2612 0.4321 0.2913 -0.0108 -0.0118 0.0151  68  ARG   A CD  
490  N NE  . ARG   A 62  ? 0.2815 0.4554 0.3098 -0.0103 -0.0050 0.0119  68  ARG   A NE  
491  C CZ  . ARG   A 62  ? 0.2810 0.4525 0.3011 -0.0092 -0.0041 0.0080  68  ARG   A CZ  
492  N NH1 . ARG   A 62  ? 0.2611 0.4276 0.2732 -0.0092 -0.0102 0.0071  68  ARG   A NH1 
493  N NH2 . ARG   A 62  ? 0.2744 0.4485 0.2952 -0.0083 0.0029  0.0050  68  ARG   A NH2 
494  N N   . ARG   A 63  ? 0.2301 0.3943 0.2829 -0.0071 -0.0374 0.0197  69  ARG   A N   
495  C CA  . ARG   A 63  ? 0.2430 0.4053 0.3046 -0.0064 -0.0414 0.0229  69  ARG   A CA  
496  C C   . ARG   A 63  ? 0.2390 0.4016 0.3073 -0.0070 -0.0370 0.0239  69  ARG   A C   
497  O O   . ARG   A 63  ? 0.2410 0.3997 0.3108 -0.0076 -0.0383 0.0280  69  ARG   A O   
498  C CB  . ARG   A 63  ? 0.2695 0.4267 0.3241 -0.0072 -0.0473 0.0282  69  ARG   A CB  
499  C CG  . ARG   A 63  ? 0.3120 0.4688 0.3645 -0.0066 -0.0540 0.0277  69  ARG   A CG  
500  C CD  . ARG   A 63  ? 0.3433 0.4952 0.3895 -0.0079 -0.0610 0.0338  69  ARG   A CD  
501  N NE  . ARG   A 63  ? 0.3721 0.5230 0.4117 -0.0086 -0.0677 0.0332  69  ARG   A NE  
502  C CZ  . ARG   A 63  ? 0.3948 0.5413 0.4175 -0.0113 -0.0711 0.0352  69  ARG   A CZ  
503  N NH1 . ARG   A 63  ? 0.3750 0.5182 0.3858 -0.0133 -0.0677 0.0383  69  ARG   A NH1 
504  N NH2 . ARG   A 63  ? 0.3955 0.5408 0.4125 -0.0123 -0.0777 0.0341  69  ARG   A NH2 
505  N N   . LYS   A 64  ? 0.2315 0.3982 0.3032 -0.0073 -0.0320 0.0202  70  LYS   A N   
506  C CA  . LYS   A 64  ? 0.2340 0.4009 0.3110 -0.0088 -0.0283 0.0207  70  LYS   A CA  
507  C C   . LYS   A 64  ? 0.2137 0.3845 0.2991 -0.0084 -0.0261 0.0165  70  LYS   A C   
508  O O   . LYS   A 64  ? 0.2232 0.3979 0.3092 -0.0074 -0.0259 0.0135  70  LYS   A O   
509  C CB  . LYS   A 64  ? 0.2846 0.4524 0.3549 -0.0111 -0.0239 0.0222  70  LYS   A CB  
510  C CG  . LYS   A 64  ? 0.3922 0.5549 0.4562 -0.0126 -0.0248 0.0276  70  LYS   A CG  
511  C CD  . LYS   A 64  ? 0.4830 0.6466 0.5455 -0.0154 -0.0197 0.0295  70  LYS   A CD  
512  C CE  . LYS   A 64  ? 0.5636 0.7220 0.6180 -0.0172 -0.0202 0.0353  70  LYS   A CE  
513  N NZ  . LYS   A 64  ? 0.5985 0.7555 0.6399 -0.0170 -0.0216 0.0363  70  LYS   A NZ  
514  N N   . HIS   A 65  ? 0.1913 0.3606 0.2822 -0.0097 -0.0244 0.0165  71  HIS   A N   
515  C CA  . HIS   A 65  ? 0.1871 0.3591 0.2839 -0.0103 -0.0223 0.0128  71  HIS   A CA  
516  C C   . HIS   A 65  ? 0.1928 0.3670 0.2885 -0.0134 -0.0191 0.0130  71  HIS   A C   
517  O O   . HIS   A 65  ? 0.1916 0.3623 0.2868 -0.0153 -0.0182 0.0154  71  HIS   A O   
518  C CB  . HIS   A 65  ? 0.1875 0.3554 0.2912 -0.0098 -0.0226 0.0118  71  HIS   A CB  
519  C CG  . HIS   A 65  ? 0.2051 0.3715 0.3126 -0.0067 -0.0258 0.0124  71  HIS   A CG  
520  N ND1 . HIS   A 65  ? 0.2178 0.3866 0.3309 -0.0052 -0.0257 0.0093  71  HIS   A ND1 
521  C CD2 . HIS   A 65  ? 0.2207 0.3841 0.3275 -0.0053 -0.0295 0.0163  71  HIS   A CD2 
522  C CE1 . HIS   A 65  ? 0.2208 0.3882 0.3379 -0.0028 -0.0291 0.0112  71  HIS   A CE1 
523  N NE2 . HIS   A 65  ? 0.2287 0.3930 0.3420 -0.0028 -0.0320 0.0155  71  HIS   A NE2 
524  N N   . TYR   A 66  ? 0.1831 0.3630 0.2789 -0.0139 -0.0176 0.0110  72  TYR   A N   
525  C CA  . TYR   A 66  ? 0.1839 0.3672 0.2805 -0.0168 -0.0151 0.0118  72  TYR   A CA  
526  C C   . TYR   A 66  ? 0.1877 0.3731 0.2888 -0.0193 -0.0148 0.0095  72  TYR   A C   
527  O O   . TYR   A 66  ? 0.1836 0.3718 0.2862 -0.0185 -0.0157 0.0071  72  TYR   A O   
528  C CB  . TYR   A 66  ? 0.1800 0.3688 0.2748 -0.0158 -0.0135 0.0119  72  TYR   A CB  
529  C CG  . TYR   A 66  ? 0.1934 0.3802 0.2813 -0.0145 -0.0127 0.0139  72  TYR   A CG  
530  C CD1 . TYR   A 66  ? 0.2078 0.3937 0.2927 -0.0163 -0.0100 0.0171  72  TYR   A CD1 
531  C CD2 . TYR   A 66  ? 0.2124 0.3984 0.2963 -0.0117 -0.0144 0.0125  72  TYR   A CD2 
532  C CE1 . TYR   A 66  ? 0.2312 0.4150 0.3076 -0.0156 -0.0088 0.0189  72  TYR   A CE1 
533  C CE2 . TYR   A 66  ? 0.2327 0.4164 0.3081 -0.0111 -0.0138 0.0139  72  TYR   A CE2 
534  C CZ  . TYR   A 66  ? 0.2527 0.4353 0.3238 -0.0130 -0.0107 0.0170  72  TYR   A CZ  
535  O OH  . TYR   A 66  ? 0.2876 0.4673 0.3482 -0.0128 -0.0098 0.0183  72  TYR   A OH  
536  N N   . PRO   A 67  ? 0.1896 0.3738 0.2922 -0.0229 -0.0139 0.0104  73  PRO   A N   
537  C CA  . PRO   A 67  ? 0.1885 0.3749 0.2939 -0.0262 -0.0143 0.0082  73  PRO   A CA  
538  C C   . PRO   A 67  ? 0.1928 0.3876 0.3008 -0.0268 -0.0141 0.0092  73  PRO   A C   
539  O O   . PRO   A 67  ? 0.1939 0.3917 0.3029 -0.0265 -0.0123 0.0119  73  PRO   A O   
540  C CB  . PRO   A 67  ? 0.2041 0.3861 0.3105 -0.0300 -0.0137 0.0092  73  PRO   A CB  
541  C CG  . PRO   A 67  ? 0.2179 0.3972 0.3228 -0.0289 -0.0125 0.0130  73  PRO   A CG  
542  C CD  . PRO   A 67  ? 0.1945 0.3755 0.2961 -0.0246 -0.0126 0.0138  73  PRO   A CD  
543  N N   . VAL   A 68  ? 0.1871 0.3855 0.2965 -0.0274 -0.0156 0.0073  74  VAL   A N   
544  C CA  . VAL   A 68  ? 0.1894 0.3957 0.3031 -0.0277 -0.0160 0.0089  74  VAL   A CA  
545  C C   . VAL   A 68  ? 0.1908 0.4002 0.3064 -0.0314 -0.0187 0.0082  74  VAL   A C   
546  O O   . VAL   A 68  ? 0.1907 0.3959 0.3022 -0.0329 -0.0198 0.0055  74  VAL   A O   
547  C CB  . VAL   A 68  ? 0.1976 0.4065 0.3114 -0.0232 -0.0157 0.0084  74  VAL   A CB  
548  C CG1 . VAL   A 68  ? 0.2086 0.4160 0.3200 -0.0201 -0.0132 0.0095  74  VAL   A CG1 
549  C CG2 . VAL   A 68  ? 0.1929 0.3989 0.3040 -0.0217 -0.0173 0.0057  74  VAL   A CG2 
550  N N   . SER   A 69  ? 0.1761 0.3929 0.2979 -0.0329 -0.0195 0.0108  75  SER   A N   
551  C CA  . SER   A 69  ? 0.1736 0.3951 0.2980 -0.0361 -0.0231 0.0115  75  SER   A CA  
552  C C   . SER   A 69  ? 0.1624 0.3879 0.2893 -0.0320 -0.0233 0.0121  75  SER   A C   
553  O O   . SER   A 69  ? 0.1669 0.3948 0.2976 -0.0283 -0.0208 0.0132  75  SER   A O   
554  C CB  . SER   A 69  ? 0.1954 0.4236 0.3281 -0.0393 -0.0242 0.0151  75  SER   A CB  
555  O OG  . SER   A 69  ? 0.2461 0.4709 0.3774 -0.0440 -0.0247 0.0148  75  SER   A OG  
556  N N   . PHE   A 70  ? 0.1419 0.3678 0.2665 -0.0330 -0.0261 0.0114  76  PHE   A N   
557  C CA  . PHE   A 70  ? 0.1483 0.3774 0.2760 -0.0294 -0.0265 0.0123  76  PHE   A CA  
558  C C   . PHE   A 70  ? 0.1661 0.4003 0.2968 -0.0324 -0.0308 0.0150  76  PHE   A C   
559  O O   . PHE   A 70  ? 0.1698 0.4032 0.2963 -0.0374 -0.0337 0.0149  76  PHE   A O   
560  C CB  . PHE   A 70  ? 0.1424 0.3661 0.2644 -0.0261 -0.0250 0.0093  76  PHE   A CB  
561  C CG  . PHE   A 70  ? 0.1567 0.3752 0.2713 -0.0287 -0.0255 0.0065  76  PHE   A CG  
562  C CD1 . PHE   A 70  ? 0.1787 0.3914 0.2892 -0.0296 -0.0237 0.0041  76  PHE   A CD1 
563  C CD2 . PHE   A 70  ? 0.1737 0.3929 0.2856 -0.0305 -0.0274 0.0065  76  PHE   A CD2 
564  C CE1 . PHE   A 70  ? 0.1898 0.3972 0.2943 -0.0317 -0.0231 0.0010  76  PHE   A CE1 
565  C CE2 . PHE   A 70  ? 0.1881 0.4022 0.2925 -0.0330 -0.0267 0.0034  76  PHE   A CE2 
566  C CZ  . PHE   A 70  ? 0.1834 0.3915 0.2845 -0.0334 -0.0243 0.0004  76  PHE   A CZ  
567  N N   . SER   A 71  ? 0.1666 0.4054 0.3041 -0.0295 -0.0315 0.0174  77  SER   A N   
568  C CA  . SER   A 71  ? 0.1866 0.4305 0.3282 -0.0320 -0.0361 0.0211  77  SER   A CA  
569  C C   . SER   A 71  ? 0.2130 0.4536 0.3462 -0.0336 -0.0383 0.0202  77  SER   A C   
570  O O   . SER   A 71  ? 0.2288 0.4636 0.3550 -0.0319 -0.0355 0.0165  77  SER   A O   
571  C CB  . SER   A 71  ? 0.1959 0.4459 0.3500 -0.0281 -0.0358 0.0245  77  SER   A CB  
572  O OG  . SER   A 71  ? 0.2299 0.4767 0.3832 -0.0232 -0.0332 0.0226  77  SER   A OG  
573  N N   . LYS   A 72  ? 0.2195 0.4638 0.3535 -0.0372 -0.0432 0.0239  78  LYS   A N   
574  C CA  . LYS   A 72  ? 0.2446 0.4860 0.3699 -0.0392 -0.0448 0.0236  78  LYS   A CA  
575  C C   . LYS   A 72  ? 0.2375 0.4791 0.3673 -0.0343 -0.0435 0.0246  78  LYS   A C   
576  O O   . LYS   A 72  ? 0.2302 0.4756 0.3709 -0.0305 -0.0432 0.0268  78  LYS   A O   
577  C CB  . LYS   A 72  ? 0.2915 0.5363 0.4143 -0.0454 -0.0511 0.0277  78  LYS   A CB  
578  C CG  . LYS   A 72  ? 0.3807 0.6208 0.4910 -0.0515 -0.0518 0.0243  78  LYS   A CG  
579  C CD  . LYS   A 72  ? 0.4691 0.7138 0.5806 -0.0577 -0.0583 0.0282  78  LYS   A CD  
580  C CE  . LYS   A 72  ? 0.5541 0.7929 0.6511 -0.0646 -0.0594 0.0243  78  LYS   A CE  
581  N NZ  . LYS   A 72  ? 0.6094 0.8448 0.6932 -0.0682 -0.0609 0.0241  78  LYS   A NZ  
582  N N   . PRO   A 73  ? 0.2423 0.4798 0.3648 -0.0342 -0.0422 0.0228  79  PRO   A N   
583  C CA  . PRO   A 73  ? 0.2313 0.4686 0.3591 -0.0299 -0.0411 0.0238  79  PRO   A CA  
584  C C   . PRO   A 73  ? 0.2075 0.4502 0.3447 -0.0296 -0.0453 0.0298  79  PRO   A C   
585  O O   . PRO   A 73  ? 0.2005 0.4457 0.3351 -0.0341 -0.0497 0.0339  79  PRO   A O   
586  C CB  . PRO   A 73  ? 0.2525 0.4855 0.3709 -0.0316 -0.0396 0.0218  79  PRO   A CB  
587  C CG  . PRO   A 73  ? 0.2716 0.5008 0.3806 -0.0347 -0.0376 0.0177  79  PRO   A CG  
588  C CD  . PRO   A 73  ? 0.2487 0.4812 0.3587 -0.0381 -0.0411 0.0197  79  PRO   A CD  
589  N N   A SER   A 74  ? 0.1994 0.4435 0.3472 -0.0245 -0.0439 0.0305  80  SER   A N   
590  N N   B SER   A 74  ? 0.1987 0.4428 0.3465 -0.0245 -0.0439 0.0305  80  SER   A N   
591  C CA  A SER   A 74  ? 0.2010 0.4499 0.3606 -0.0232 -0.0471 0.0361  80  SER   A CA  
592  C CA  B SER   A 74  ? 0.1995 0.4484 0.3590 -0.0232 -0.0472 0.0361  80  SER   A CA  
593  C C   A SER   A 74  ? 0.2001 0.4468 0.3671 -0.0178 -0.0448 0.0355  80  SER   A C   
594  C C   B SER   A 74  ? 0.1993 0.4460 0.3663 -0.0178 -0.0448 0.0355  80  SER   A C   
595  O O   A SER   A 74  ? 0.2039 0.4457 0.3668 -0.0151 -0.0410 0.0306  80  SER   A O   
596  O O   B SER   A 74  ? 0.2031 0.4449 0.3660 -0.0151 -0.0410 0.0306  80  SER   A O   
597  C CB  A SER   A 74  ? 0.2133 0.4678 0.3825 -0.0227 -0.0477 0.0380  80  SER   A CB  
598  C CB  B SER   A 74  ? 0.2099 0.4644 0.3788 -0.0230 -0.0480 0.0383  80  SER   A CB  
599  O OG  A SER   A 74  ? 0.2543 0.5093 0.4169 -0.0269 -0.0482 0.0365  80  SER   A OG  
600  O OG  B SER   A 74  ? 0.2463 0.5028 0.4092 -0.0286 -0.0511 0.0392  80  SER   A OG  
601  N N   . LEU   A 75  ? 0.1929 0.4429 0.3713 -0.0163 -0.0476 0.0408  81  LEU   A N   
602  C CA  . LEU   A 75  ? 0.1991 0.4468 0.3864 -0.0114 -0.0459 0.0406  81  LEU   A CA  
603  C C   . LEU   A 75  ? 0.2101 0.4596 0.4070 -0.0071 -0.0421 0.0384  81  LEU   A C   
604  O O   . LEU   A 75  ? 0.2107 0.4661 0.4166 -0.0075 -0.0436 0.0422  81  LEU   A O   
605  C CB  . LEU   A 75  ? 0.1983 0.4488 0.3939 -0.0124 -0.0510 0.0480  81  LEU   A CB  
606  C CG  . LEU   A 75  ? 0.2230 0.4699 0.4269 -0.0085 -0.0502 0.0488  81  LEU   A CG  
607  C CD1 . LEU   A 75  ? 0.2264 0.4670 0.4206 -0.0087 -0.0479 0.0446  81  LEU   A CD1 
608  C CD2 . LEU   A 75  ? 0.2327 0.4828 0.4454 -0.0099 -0.0558 0.0574  81  LEU   A CD2 
609  N N   . ILE   A 76  ? 0.2069 0.4513 0.4007 -0.0036 -0.0370 0.0323  82  ILE   A N   
610  C CA  . ILE   A 76  ? 0.2088 0.4538 0.4082 0.0001  -0.0322 0.0293  82  ILE   A CA  
611  C C   . ILE   A 76  ? 0.2121 0.4519 0.4160 0.0050  -0.0286 0.0259  82  ILE   A C   
612  O O   . ILE   A 76  ? 0.2134 0.4473 0.4101 0.0053  -0.0285 0.0226  82  ILE   A O   
613  C CB  . ILE   A 76  ? 0.2242 0.4670 0.4119 -0.0012 -0.0293 0.0245  82  ILE   A CB  
614  C CG1 . ILE   A 76  ? 0.2471 0.4934 0.4289 -0.0063 -0.0324 0.0268  82  ILE   A CG1 
615  C CG2 . ILE   A 76  ? 0.2231 0.4656 0.4138 0.0022  -0.0236 0.0213  82  ILE   A CG2 
616  C CD1 . ILE   A 76  ? 0.2675 0.5206 0.4573 -0.0079 -0.0333 0.0304  82  ILE   A CD1 
617  N N   . PHE   A 77  ? 0.2064 0.4480 0.4221 0.0087  -0.0253 0.0261  83  PHE   A N   
618  C CA  . PHE   A 77  ? 0.2088 0.4443 0.4276 0.0133  -0.0210 0.0216  83  PHE   A CA  
619  C C   . PHE   A 77  ? 0.2040 0.4338 0.4097 0.0140  -0.0164 0.0144  83  PHE   A C   
620  O O   . PHE   A 77  ? 0.2074 0.4396 0.4090 0.0132  -0.0137 0.0132  83  PHE   A O   
621  C CB  . PHE   A 77  ? 0.2108 0.4494 0.4464 0.0174  -0.0176 0.0234  83  PHE   A CB  
622  C CG  . PHE   A 77  ? 0.2328 0.4638 0.4723 0.0217  -0.0140 0.0190  83  PHE   A CG  
623  C CD1 . PHE   A 77  ? 0.2488 0.4765 0.4936 0.0222  -0.0178 0.0214  83  PHE   A CD1 
624  C CD2 . PHE   A 77  ? 0.2532 0.4798 0.4901 0.0249  -0.0067 0.0125  83  PHE   A CD2 
625  C CE1 . PHE   A 77  ? 0.2658 0.4856 0.5142 0.0259  -0.0146 0.0171  83  PHE   A CE1 
626  C CE2 . PHE   A 77  ? 0.2674 0.4859 0.5065 0.0285  -0.0033 0.0077  83  PHE   A CE2 
627  C CZ  . PHE   A 77  ? 0.2649 0.4799 0.5102 0.0290  -0.0074 0.0098  83  PHE   A CZ  
628  N N   . VAL   A 78  ? 0.1913 0.4136 0.3901 0.0148  -0.0164 0.0101  84  VAL   A N   
629  C CA  . VAL   A 78  ? 0.1935 0.4097 0.3792 0.0150  -0.0137 0.0039  84  VAL   A CA  
630  C C   . VAL   A 78  ? 0.1987 0.4078 0.3854 0.0185  -0.0100 -0.0013 84  VAL   A C   
631  O O   . VAL   A 78  ? 0.2020 0.4074 0.3936 0.0194  -0.0121 -0.0013 84  VAL   A O   
632  C CB  . VAL   A 78  ? 0.1963 0.4101 0.3715 0.0118  -0.0180 0.0034  84  VAL   A CB  
633  C CG1 . VAL   A 78  ? 0.2056 0.4127 0.3692 0.0122  -0.0165 -0.0024 84  VAL   A CG1 
634  C CG2 . VAL   A 78  ? 0.1976 0.4170 0.3695 0.0083  -0.0203 0.0070  84  VAL   A CG2 
635  N N   . GLU   A 79  ? 0.1976 0.4040 0.3791 0.0202  -0.0043 -0.0059 85  GLU   A N   
636  C CA  . GLU   A 79  ? 0.2115 0.4100 0.3917 0.0232  0.0000  -0.0118 85  GLU   A CA  
637  C C   . GLU   A 79  ? 0.2188 0.4090 0.3891 0.0219  -0.0036 -0.0159 85  GLU   A C   
638  O O   . GLU   A 79  ? 0.2144 0.4049 0.3759 0.0189  -0.0079 -0.0152 85  GLU   A O   
639  C CB  . GLU   A 79  ? 0.2459 0.4428 0.4188 0.0244  0.0072  -0.0161 85  GLU   A CB  
640  C CG  . GLU   A 79  ? 0.3008 0.5056 0.4855 0.0261  0.0121  -0.0128 85  GLU   A CG  
641  C CD  . GLU   A 79  ? 0.4191 0.6252 0.6218 0.0300  0.0150  -0.0116 85  GLU   A CD  
642  O OE1 . GLU   A 79  ? 0.4419 0.6404 0.6458 0.0322  0.0159  -0.0155 85  GLU   A OE1 
643  O OE2 . GLU   A 79  ? 0.4614 0.6760 0.6779 0.0309  0.0162  -0.0065 85  GLU   A OE2 
644  N N   . ALA   A 80  ? 0.2163 0.3987 0.3883 0.0242  -0.0014 -0.0206 86  ALA   A N   
645  C CA  . ALA   A 80  ? 0.2343 0.4084 0.3974 0.0227  -0.0050 -0.0250 86  ALA   A CA  
646  C C   . ALA   A 80  ? 0.2469 0.4180 0.3923 0.0202  -0.0056 -0.0285 86  ALA   A C   
647  O O   . ALA   A 80  ? 0.2464 0.4185 0.3850 0.0206  -0.0010 -0.0300 86  ALA   A O   
648  C CB  . ALA   A 80  ? 0.2404 0.4055 0.4068 0.0254  -0.0015 -0.0305 86  ALA   A CB  
649  N N   . SER   A 81  ? 0.2489 0.4170 0.3881 0.0176  -0.0115 -0.0291 87  SER   A N   
650  C CA  . SER   A 81  ? 0.2558 0.4214 0.3803 0.0150  -0.0140 -0.0312 87  SER   A CA  
651  C C   . SER   A 81  ? 0.2671 0.4245 0.3864 0.0133  -0.0186 -0.0354 87  SER   A C   
652  O O   . SER   A 81  ? 0.2697 0.4234 0.3968 0.0142  -0.0192 -0.0367 87  SER   A O   
653  C CB  . SER   A 81  ? 0.2561 0.4291 0.3814 0.0129  -0.0179 -0.0257 87  SER   A CB  
654  O OG  . SER   A 81  ? 0.2679 0.4422 0.4001 0.0115  -0.0230 -0.0231 87  SER   A OG  
655  N N   . GLU   A 82  ? 0.2691 0.4241 0.3765 0.0107  -0.0226 -0.0367 88  GLU   A N   
656  C CA  . GLU   A 82  ? 0.2881 0.4367 0.3913 0.0084  -0.0283 -0.0397 88  GLU   A CA  
657  C C   . GLU   A 82  ? 0.2868 0.4388 0.4030 0.0075  -0.0329 -0.0358 88  GLU   A C   
658  O O   . GLU   A 82  ? 0.2958 0.4422 0.4142 0.0064  -0.0362 -0.0382 88  GLU   A O   
659  C CB  . GLU   A 82  ? 0.3400 0.4875 0.4301 0.0056  -0.0325 -0.0399 88  GLU   A CB  
660  C CG  . GLU   A 82  ? 0.4398 0.5811 0.5257 0.0027  -0.0396 -0.0426 88  GLU   A CG  
661  C CD  . GLU   A 82  ? 0.5460 0.6861 0.6205 -0.0002 -0.0452 -0.0422 88  GLU   A CD  
662  O OE1 . GLU   A 82  ? 0.5594 0.6972 0.6353 -0.0028 -0.0522 -0.0424 88  GLU   A OE1 
663  O OE2 . GLU   A 82  ? 0.5592 0.7007 0.6244 -0.0001 -0.0430 -0.0411 88  GLU   A OE2 
664  N N   . TYR   A 83  ? 0.2754 0.4361 0.3998 0.0078  -0.0328 -0.0297 89  TYR   A N   
665  C CA  . TYR   A 83  ? 0.2754 0.4399 0.4102 0.0064  -0.0366 -0.0255 89  TYR   A CA  
666  C C   . TYR   A 83  ? 0.2681 0.4358 0.4154 0.0078  -0.0347 -0.0219 89  TYR   A C   
667  O O   . TYR   A 83  ? 0.2814 0.4503 0.4362 0.0064  -0.0376 -0.0190 89  TYR   A O   
668  C CB  . TYR   A 83  ? 0.2794 0.4505 0.4129 0.0049  -0.0384 -0.0215 89  TYR   A CB  
669  C CG  . TYR   A 83  ? 0.3055 0.4740 0.4295 0.0033  -0.0419 -0.0236 89  TYR   A CG  
670  C CD1 . TYR   A 83  ? 0.3251 0.4916 0.4511 0.0011  -0.0474 -0.0240 89  TYR   A CD1 
671  C CD2 . TYR   A 83  ? 0.3277 0.4956 0.4412 0.0037  -0.0400 -0.0248 89  TYR   A CD2 
672  C CE1 . TYR   A 83  ? 0.3460 0.5104 0.4643 -0.0005 -0.0516 -0.0251 89  TYR   A CE1 
673  C CE2 . TYR   A 83  ? 0.3488 0.5139 0.4532 0.0020  -0.0439 -0.0260 89  TYR   A CE2 
674  C CZ  . TYR   A 83  ? 0.3700 0.5335 0.4771 -0.0001 -0.0501 -0.0260 89  TYR   A CZ  
675  O OH  . TYR   A 83  ? 0.4151 0.5763 0.5144 -0.0019 -0.0549 -0.0263 89  TYR   A OH  
676  N N   . TYR   A 84  ? 0.2489 0.4185 0.3991 0.0103  -0.0300 -0.0213 90  TYR   A N   
677  C CA  . TYR   A 84  ? 0.2335 0.4063 0.3962 0.0116  -0.0291 -0.0169 90  TYR   A CA  
678  C C   . TYR   A 84  ? 0.2375 0.4073 0.4043 0.0150  -0.0243 -0.0193 90  TYR   A C   
679  O O   . TYR   A 84  ? 0.2438 0.4133 0.4041 0.0163  -0.0203 -0.0223 90  TYR   A O   
680  C CB  . TYR   A 84  ? 0.2162 0.3983 0.3815 0.0108  -0.0290 -0.0108 90  TYR   A CB  
681  C CG  . TYR   A 84  ? 0.2110 0.3968 0.3734 0.0078  -0.0322 -0.0081 90  TYR   A CG  
682  C CD1 . TYR   A 84  ? 0.2127 0.4000 0.3816 0.0060  -0.0349 -0.0044 90  TYR   A CD1 
683  C CD2 . TYR   A 84  ? 0.2161 0.4042 0.3701 0.0068  -0.0321 -0.0089 90  TYR   A CD2 
684  C CE1 . TYR   A 84  ? 0.2171 0.4079 0.3840 0.0034  -0.0366 -0.0022 90  TYR   A CE1 
685  C CE2 . TYR   A 84  ? 0.2194 0.4106 0.3722 0.0044  -0.0343 -0.0067 90  TYR   A CE2 
686  C CZ  . TYR   A 84  ? 0.2225 0.4152 0.3817 0.0028  -0.0362 -0.0035 90  TYR   A CZ  
687  O OH  . TYR   A 84  ? 0.2145 0.4103 0.3730 0.0007  -0.0372 -0.0018 90  TYR   A OH  
688  N N   . PRO   A 85  ? 0.2367 0.4049 0.4155 0.0166  -0.0240 -0.0174 91  PRO   A N   
689  C CA  . PRO   A 85  ? 0.2279 0.3949 0.4139 0.0204  -0.0188 -0.0187 91  PRO   A CA  
690  C C   . PRO   A 85  ? 0.2129 0.3898 0.4042 0.0212  -0.0171 -0.0130 91  PRO   A C   
691  O O   . PRO   A 85  ? 0.2068 0.3902 0.3957 0.0185  -0.0204 -0.0084 91  PRO   A O   
692  C CB  . PRO   A 85  ? 0.2388 0.4019 0.4378 0.0215  -0.0204 -0.0167 91  PRO   A CB  
693  C CG  . PRO   A 85  ? 0.2427 0.4104 0.4440 0.0181  -0.0260 -0.0105 91  PRO   A CG  
694  C CD  . PRO   A 85  ? 0.2311 0.3999 0.4190 0.0150  -0.0282 -0.0127 91  PRO   A CD  
695  N N   . ALA   A 86  ? 0.2067 0.3850 0.4062 0.0246  -0.0121 -0.0131 92  ALA   A N   
696  C CA  . ALA   A 86  ? 0.2013 0.3895 0.4075 0.0250  -0.0112 -0.0073 92  ALA   A CA  
697  C C   . ALA   A 86  ? 0.1989 0.3930 0.4140 0.0230  -0.0169 0.0009  92  ALA   A C   
698  O O   . ALA   A 86  ? 0.2059 0.3968 0.4301 0.0239  -0.0189 0.0029  92  ALA   A O   
699  C CB  . ALA   A 86  ? 0.2055 0.3942 0.4226 0.0293  -0.0050 -0.0083 92  ALA   A CB  
700  N N   . ARG   A 87  ? 0.1905 0.3921 0.4019 0.0201  -0.0196 0.0054  93  ARG   A N   
701  C CA  . ARG   A 87  ? 0.1917 0.3982 0.4084 0.0174  -0.0249 0.0129  93  ARG   A CA  
702  C C   . ARG   A 87  ? 0.2054 0.4204 0.4190 0.0146  -0.0265 0.0171  93  ARG   A C   
703  O O   . ARG   A 87  ? 0.2281 0.4446 0.4350 0.0146  -0.0236 0.0140  93  ARG   A O   
704  C CB  . ARG   A 87  ? 0.1899 0.3924 0.3996 0.0146  -0.0285 0.0123  93  ARG   A CB  
705  C CG  . ARG   A 87  ? 0.1951 0.3995 0.3916 0.0112  -0.0295 0.0109  93  ARG   A CG  
706  C CD  . ARG   A 87  ? 0.2068 0.4056 0.3958 0.0100  -0.0306 0.0068  93  ARG   A CD  
707  N NE  . ARG   A 87  ? 0.2170 0.4188 0.3975 0.0067  -0.0322 0.0076  93  ARG   A NE  
708  C CZ  . ARG   A 87  ? 0.2149 0.4185 0.3871 0.0062  -0.0307 0.0053  93  ARG   A CZ  
709  N NH1 . ARG   A 87  ? 0.1752 0.3784 0.3458 0.0083  -0.0277 0.0026  93  ARG   A NH1 
710  N NH2 . ARG   A 87  ? 0.2047 0.4101 0.3708 0.0035  -0.0319 0.0059  93  ARG   A NH2 
711  N N   . TYR   A 88  ? 0.1896 0.4094 0.4064 0.0117  -0.0312 0.0240  94  TYR   A N   
712  C CA  . TYR   A 88  ? 0.1927 0.4191 0.4041 0.0081  -0.0332 0.0272  94  TYR   A CA  
713  C C   . TYR   A 88  ? 0.1888 0.4130 0.3866 0.0047  -0.0344 0.0250  94  TYR   A C   
714  O O   . TYR   A 88  ? 0.1948 0.4160 0.3914 0.0035  -0.0363 0.0260  94  TYR   A O   
715  C CB  . TYR   A 88  ? 0.1926 0.4247 0.4122 0.0060  -0.0381 0.0355  94  TYR   A CB  
716  C CG  . TYR   A 88  ? 0.1960 0.4327 0.4306 0.0090  -0.0374 0.0388  94  TYR   A CG  
717  C CD1 . TYR   A 88  ? 0.2086 0.4516 0.4445 0.0081  -0.0368 0.0398  94  TYR   A CD1 
718  C CD2 . TYR   A 88  ? 0.2065 0.4409 0.4550 0.0129  -0.0368 0.0404  94  TYR   A CD2 
719  C CE1 . TYR   A 88  ? 0.2204 0.4684 0.4720 0.0110  -0.0356 0.0428  94  TYR   A CE1 
720  C CE2 . TYR   A 88  ? 0.2127 0.4514 0.4771 0.0162  -0.0354 0.0432  94  TYR   A CE2 
721  C CZ  . TYR   A 88  ? 0.2315 0.4776 0.4978 0.0152  -0.0348 0.0446  94  TYR   A CZ  
722  O OH  . TYR   A 88  ? 0.2528 0.5042 0.5366 0.0185  -0.0331 0.0477  94  TYR   A OH  
723  N N   . GLN   A 89  ? 0.1743 0.4000 0.3629 0.0031  -0.0330 0.0223  95  GLN   A N   
724  C CA  . GLN   A 89  ? 0.1712 0.3951 0.3486 0.0002  -0.0336 0.0204  95  GLN   A CA  
725  C C   . GLN   A 89  ? 0.1682 0.3972 0.3419 -0.0040 -0.0361 0.0245  95  GLN   A C   
726  O O   . GLN   A 89  ? 0.1774 0.4105 0.3531 -0.0046 -0.0362 0.0260  95  GLN   A O   
727  C CB  . GLN   A 89  ? 0.1887 0.4095 0.3580 0.0013  -0.0305 0.0144  95  GLN   A CB  
728  C CG  . GLN   A 89  ? 0.2165 0.4358 0.3766 -0.0013 -0.0312 0.0128  95  GLN   A CG  
729  C CD  . GLN   A 89  ? 0.1956 0.4107 0.3492 0.0000  -0.0294 0.0077  95  GLN   A CD  
730  O OE1 . GLN   A 89  ? 0.2029 0.4140 0.3574 0.0024  -0.0286 0.0047  95  GLN   A OE1 
731  N NE2 . GLN   A 89  ? 0.1628 0.3783 0.3096 -0.0019 -0.0290 0.0067  95  GLN   A NE2 
732  N N   . SER   A 90  ? 0.1545 0.3831 0.3233 -0.0073 -0.0381 0.0266  96  SER   A N   
733  C CA  . SER   A 90  ? 0.1563 0.3885 0.3194 -0.0119 -0.0404 0.0300  96  SER   A CA  
734  C C   . SER   A 90  ? 0.1684 0.3991 0.3204 -0.0141 -0.0382 0.0258  96  SER   A C   
735  O O   . SER   A 90  ? 0.1709 0.3979 0.3202 -0.0122 -0.0355 0.0212  96  SER   A O   
736  C CB  . SER   A 90  ? 0.1707 0.4031 0.3335 -0.0147 -0.0432 0.0349  96  SER   A CB  
737  O OG  . SER   A 90  ? 0.2168 0.4452 0.3752 -0.0149 -0.0411 0.0323  96  SER   A OG  
738  N N   . HIS   A 91  ? 0.1624 0.3957 0.3086 -0.0182 -0.0397 0.0275  97  HIS   A N   
739  C CA  . HIS   A 91  ? 0.1714 0.4028 0.3077 -0.0207 -0.0376 0.0237  97  HIS   A CA  
740  C C   . HIS   A 91  ? 0.1756 0.4052 0.3122 -0.0177 -0.0348 0.0192  97  HIS   A C   
741  O O   . HIS   A 91  ? 0.1862 0.4125 0.3172 -0.0177 -0.0323 0.0154  97  HIS   A O   
742  C CB  . HIS   A 91  ? 0.1838 0.4118 0.3138 -0.0220 -0.0356 0.0220  97  HIS   A CB  
743  C CG  . HIS   A 91  ? 0.2158 0.4450 0.3435 -0.0255 -0.0377 0.0266  97  HIS   A CG  
744  N ND1 . HIS   A 91  ? 0.2448 0.4740 0.3623 -0.0306 -0.0381 0.0273  97  HIS   A ND1 
745  C CD2 . HIS   A 91  ? 0.2192 0.4491 0.3529 -0.0247 -0.0397 0.0308  97  HIS   A CD2 
746  C CE1 . HIS   A 91  ? 0.2502 0.4804 0.3669 -0.0330 -0.0401 0.0322  97  HIS   A CE1 
747  N NE2 . HIS   A 91  ? 0.2400 0.4708 0.3670 -0.0295 -0.0414 0.0347  97  HIS   A NE2 
748  N N   . LEU   A 92  ? 0.1691 0.4010 0.3129 -0.0151 -0.0349 0.0200  98  LEU   A N   
749  C CA  . LEU   A 92  ? 0.1719 0.4022 0.3155 -0.0125 -0.0319 0.0164  98  LEU   A CA  
750  C C   . LEU   A 92  ? 0.1767 0.4098 0.3192 -0.0150 -0.0320 0.0171  98  LEU   A C   
751  O O   . LEU   A 92  ? 0.1718 0.4098 0.3191 -0.0170 -0.0347 0.0210  98  LEU   A O   
752  C CB  . LEU   A 92  ? 0.1781 0.4085 0.3298 -0.0082 -0.0306 0.0162  98  LEU   A CB  
753  C CG  . LEU   A 92  ? 0.2025 0.4306 0.3527 -0.0053 -0.0271 0.0125  98  LEU   A CG  
754  C CD1 . LEU   A 92  ? 0.2034 0.4260 0.3461 -0.0046 -0.0261 0.0085  98  LEU   A CD1 
755  C CD2 . LEU   A 92  ? 0.2192 0.4473 0.3772 -0.0016 -0.0253 0.0122  98  LEU   A CD2 
756  N N   . MET   A 93  ? 0.1678 0.3981 0.3049 -0.0150 -0.0296 0.0137  99  MET   A N   
757  C CA  . MET   A 93  ? 0.1650 0.3970 0.3011 -0.0175 -0.0294 0.0141  99  MET   A CA  
758  C C   . MET   A 93  ? 0.1645 0.3958 0.3025 -0.0145 -0.0260 0.0126  99  MET   A C   
759  O O   . MET   A 93  ? 0.1610 0.3879 0.2954 -0.0118 -0.0241 0.0097  99  MET   A O   
760  C CB  . MET   A 93  ? 0.1741 0.4023 0.3013 -0.0208 -0.0292 0.0118  99  MET   A CB  
761  C CG  . MET   A 93  ? 0.1981 0.4260 0.3205 -0.0242 -0.0314 0.0125  99  MET   A CG  
762  S SD  . MET   A 93  ? 0.2443 0.4659 0.3565 -0.0270 -0.0291 0.0082  99  MET   A SD  
763  C CE  . MET   A 93  ? 0.2001 0.4178 0.3131 -0.0222 -0.0261 0.0054  99  MET   A CE  
764  N N   . LEU   A 94  ? 0.1518 0.3874 0.2955 -0.0152 -0.0254 0.0147  100 LEU   A N   
765  C CA  . LEU   A 94  ? 0.1498 0.3848 0.2944 -0.0128 -0.0214 0.0134  100 LEU   A CA  
766  C C   . LEU   A 94  ? 0.1555 0.3901 0.2970 -0.0158 -0.0205 0.0135  100 LEU   A C   
767  O O   . LEU   A 94  ? 0.1491 0.3861 0.2916 -0.0199 -0.0231 0.0153  100 LEU   A O   
768  C CB  . LEU   A 94  ? 0.1493 0.3897 0.3048 -0.0104 -0.0196 0.0157  100 LEU   A CB  
769  C CG  . LEU   A 94  ? 0.1654 0.4059 0.3264 -0.0071 -0.0200 0.0159  100 LEU   A CG  
770  C CD1 . LEU   A 94  ? 0.1776 0.4235 0.3514 -0.0047 -0.0176 0.0182  100 LEU   A CD1 
771  C CD2 . LEU   A 94  ? 0.1701 0.4041 0.3242 -0.0041 -0.0182 0.0118  100 LEU   A CD2 
772  N N   . ALA   A 95  ? 0.1539 0.3853 0.2917 -0.0140 -0.0170 0.0118  101 ALA   A N   
773  C CA  . ALA   A 95  ? 0.1611 0.3915 0.2965 -0.0163 -0.0153 0.0123  101 ALA   A CA  
774  C C   . ALA   A 95  ? 0.1604 0.3909 0.2964 -0.0136 -0.0105 0.0123  101 ALA   A C   
775  O O   . ALA   A 95  ? 0.1454 0.3746 0.2807 -0.0100 -0.0086 0.0107  101 ALA   A O   
776  C CB  . ALA   A 95  ? 0.1666 0.3901 0.2930 -0.0174 -0.0162 0.0101  101 ALA   A CB  
777  N N   . VAL   A 96  ? 0.1571 0.3889 0.2943 -0.0157 -0.0082 0.0140  102 VAL   A N   
778  C CA  . VAL   A 96  ? 0.1663 0.3978 0.3023 -0.0140 -0.0029 0.0143  102 VAL   A CA  
779  C C   . VAL   A 96  ? 0.1856 0.4091 0.3096 -0.0136 -0.0027 0.0126  102 VAL   A C   
780  O O   . VAL   A 96  ? 0.1849 0.4055 0.3057 -0.0164 -0.0041 0.0134  102 VAL   A O   
781  C CB  . VAL   A 96  ? 0.1746 0.4115 0.3180 -0.0169 -0.0004 0.0176  102 VAL   A CB  
782  C CG1 . VAL   A 96  ? 0.1896 0.4255 0.3300 -0.0154 0.0062  0.0179  102 VAL   A CG1 
783  C CG2 . VAL   A 96  ? 0.1722 0.4178 0.3295 -0.0173 -0.0015 0.0200  102 VAL   A CG2 
784  N N   . GLY   A 97  ? 0.1977 0.4174 0.3155 -0.0104 -0.0015 0.0103  103 GLY   A N   
785  C CA  . GLY   A 97  ? 0.2091 0.4218 0.3162 -0.0100 -0.0023 0.0093  103 GLY   A CA  
786  C C   . GLY   A 97  ? 0.2177 0.4267 0.3181 -0.0069 -0.0014 0.0066  103 GLY   A C   
787  O O   . GLY   A 97  ? 0.2150 0.4264 0.3194 -0.0048 0.0003  0.0050  103 GLY   A O   
788  N N   . HIS   A 98  ? 0.2128 0.4155 0.3032 -0.0069 -0.0030 0.0063  104 HIS   A N   
789  C CA  . HIS   A 98  ? 0.2229 0.4213 0.3051 -0.0048 -0.0029 0.0038  104 HIS   A CA  
790  C C   . HIS   A 98  ? 0.2096 0.4060 0.2926 -0.0033 -0.0078 0.0015  104 HIS   A C   
791  O O   . HIS   A 98  ? 0.2190 0.4145 0.3040 -0.0041 -0.0117 0.0024  104 HIS   A O   
792  C CB  . HIS   A 98  ? 0.2361 0.4289 0.3062 -0.0059 -0.0023 0.0052  104 HIS   A CB  
793  C CG  . HIS   A 98  ? 0.2732 0.4609 0.3327 -0.0045 -0.0028 0.0024  104 HIS   A CG  
794  N ND1 . HIS   A 98  ? 0.2953 0.4829 0.3513 -0.0033 0.0025  -0.0003 104 HIS   A ND1 
795  C CD2 . HIS   A 98  ? 0.2872 0.4696 0.3395 -0.0045 -0.0083 0.0019  104 HIS   A CD2 
796  C CE1 . HIS   A 98  ? 0.3075 0.4891 0.3527 -0.0030 0.0000  -0.0028 104 HIS   A CE1 
797  N NE2 . HIS   A 98  ? 0.3018 0.4804 0.3447 -0.0038 -0.0069 -0.0012 104 HIS   A NE2 
798  N N   . SER   A 99  ? 0.1939 0.3891 0.2755 -0.0013 -0.0073 -0.0015 105 SER   A N   
799  C CA  . SER   A 99  ? 0.1966 0.3901 0.2798 -0.0002 -0.0118 -0.0035 105 SER   A CA  
800  C C   . SER   A 99  ? 0.2028 0.3921 0.2799 0.0013  -0.0112 -0.0071 105 SER   A C   
801  O O   . SER   A 99  ? 0.1965 0.3870 0.2755 0.0026  -0.0065 -0.0088 105 SER   A O   
802  C CB  . SER   A 99  ? 0.2137 0.4123 0.3083 0.0001  -0.0124 -0.0031 105 SER   A CB  
803  O OG  . SER   A 99  ? 0.2618 0.4591 0.3588 0.0010  -0.0162 -0.0046 105 SER   A OG  
804  N N   . GLU   A 100 ? 0.2050 0.3895 0.2761 0.0012  -0.0159 -0.0083 106 GLU   A N   
805  C CA  . GLU   A 100 ? 0.2239 0.4033 0.2884 0.0019  -0.0168 -0.0122 106 GLU   A CA  
806  C C   . GLU   A 100 ? 0.2348 0.4140 0.3058 0.0023  -0.0222 -0.0132 106 GLU   A C   
807  O O   . GLU   A 100 ? 0.2272 0.4093 0.3047 0.0018  -0.0253 -0.0107 106 GLU   A O   
808  C CB  . GLU   A 100 ? 0.2687 0.4421 0.3183 0.0004  -0.0183 -0.0123 106 GLU   A CB  
809  C CG  . GLU   A 100 ? 0.3347 0.5080 0.3771 -0.0003 -0.0121 -0.0112 106 GLU   A CG  
810  C CD  . GLU   A 100 ? 0.4201 0.5875 0.4467 -0.0024 -0.0138 -0.0102 106 GLU   A CD  
811  O OE1 . GLU   A 100 ? 0.4225 0.5844 0.4407 -0.0032 -0.0187 -0.0121 106 GLU   A OE1 
812  O OE2 . GLU   A 100 ? 0.4433 0.6112 0.4656 -0.0037 -0.0104 -0.0070 106 GLU   A OE2 
813  N N   . PRO   A 101 ? 0.2435 0.4193 0.3135 0.0032  -0.0228 -0.0169 107 PRO   A N   
814  C CA  . PRO   A 101 ? 0.2369 0.4129 0.3145 0.0032  -0.0276 -0.0174 107 PRO   A CA  
815  C C   . PRO   A 101 ? 0.2201 0.3964 0.2988 0.0019  -0.0337 -0.0149 107 PRO   A C   
816  O O   . PRO   A 101 ? 0.2121 0.3921 0.3007 0.0020  -0.0354 -0.0132 107 PRO   A O   
817  C CB  . PRO   A 101 ? 0.2544 0.4244 0.3269 0.0036  -0.0279 -0.0221 107 PRO   A CB  
818  C CG  . PRO   A 101 ? 0.2635 0.4324 0.3317 0.0049  -0.0207 -0.0243 107 PRO   A CG  
819  C CD  . PRO   A 101 ? 0.2497 0.4211 0.3126 0.0040  -0.0185 -0.0211 107 PRO   A CD  
820  N N   . GLY   A 102 ? 0.2123 0.3847 0.2813 0.0006  -0.0366 -0.0144 108 GLY   A N   
821  C CA  . GLY   A 102 ? 0.2101 0.3827 0.2815 -0.0004 -0.0425 -0.0117 108 GLY   A CA  
822  C C   . GLY   A 102 ? 0.2049 0.3819 0.2832 -0.0001 -0.0412 -0.0079 108 GLY   A C   
823  O O   . GLY   A 102 ? 0.2073 0.3851 0.2907 -0.0004 -0.0450 -0.0057 108 GLY   A O   
824  N N   . ASP   A 103 ? 0.1939 0.3737 0.2731 0.0003  -0.0357 -0.0073 109 ASP   A N   
825  C CA  . ASP   A 103 ? 0.1922 0.3757 0.2776 0.0001  -0.0342 -0.0046 109 ASP   A CA  
826  C C   . ASP   A 103 ? 0.1856 0.3731 0.2817 0.0004  -0.0339 -0.0047 109 ASP   A C   
827  O O   . ASP   A 103 ? 0.1801 0.3697 0.2809 0.0000  -0.0330 -0.0031 109 ASP   A O   
828  C CB  . ASP   A 103 ? 0.2044 0.3893 0.2868 -0.0003 -0.0290 -0.0037 109 ASP   A CB  
829  C CG  . ASP   A 103 ? 0.2403 0.4215 0.3123 -0.0011 -0.0286 -0.0024 109 ASP   A CG  
830  O OD1 . ASP   A 103 ? 0.2359 0.4142 0.3052 -0.0017 -0.0326 -0.0003 109 ASP   A OD1 
831  O OD2 . ASP   A 103 ? 0.2520 0.4333 0.3191 -0.0013 -0.0241 -0.0030 109 ASP   A OD2 
832  N N   . CYS   A 104 ? 0.1765 0.3647 0.2762 0.0010  -0.0344 -0.0067 110 CYS   A N   
833  C CA  . CYS   A 104 ? 0.1704 0.3622 0.2793 0.0009  -0.0341 -0.0062 110 CYS   A CA  
834  C C   . CYS   A 104 ? 0.1778 0.3703 0.2918 0.0005  -0.0364 -0.0049 110 CYS   A C   
835  O O   . CYS   A 104 ? 0.1800 0.3700 0.2931 0.0007  -0.0401 -0.0047 110 CYS   A O   
836  C CB  . CYS   A 104 ? 0.1817 0.3730 0.2936 0.0015  -0.0350 -0.0080 110 CYS   A CB  
837  S SG  . CYS   A 104 ? 0.2172 0.4089 0.3279 0.0025  -0.0310 -0.0094 110 CYS   A SG  
838  N N   . GLY   A 105 ? 0.1757 0.3712 0.2947 -0.0001 -0.0342 -0.0039 111 GLY   A N   
839  C CA  . GLY   A 105 ? 0.1754 0.3714 0.3000 -0.0002 -0.0348 -0.0030 111 GLY   A CA  
840  C C   . GLY   A 105 ? 0.1804 0.3753 0.3032 -0.0005 -0.0329 -0.0021 111 GLY   A C   
841  O O   . GLY   A 105 ? 0.1816 0.3770 0.3095 -0.0006 -0.0315 -0.0018 111 GLY   A O   
842  N N   . GLY   A 106 ? 0.1743 0.3676 0.2904 -0.0007 -0.0322 -0.0016 112 GLY   A N   
843  C CA  . GLY   A 106 ? 0.1708 0.3626 0.2851 -0.0014 -0.0304 -0.0006 112 GLY   A CA  
844  C C   . GLY   A 106 ? 0.1670 0.3608 0.2839 -0.0029 -0.0270 -0.0013 112 GLY   A C   
845  O O   . GLY   A 106 ? 0.1506 0.3474 0.2671 -0.0039 -0.0258 -0.0018 112 GLY   A O   
846  N N   . ILE   A 107 ? 0.1679 0.3598 0.2875 -0.0033 -0.0256 -0.0014 113 ILE   A N   
847  C CA  . ILE   A 107 ? 0.1869 0.3797 0.3073 -0.0052 -0.0223 -0.0028 113 ILE   A CA  
848  C C   . ILE   A 107 ? 0.1925 0.3848 0.3081 -0.0076 -0.0208 -0.0027 113 ILE   A C   
849  O O   . ILE   A 107 ? 0.1961 0.3858 0.3096 -0.0075 -0.0211 -0.0015 113 ILE   A O   
850  C CB  . ILE   A 107 ? 0.2038 0.3943 0.3298 -0.0046 -0.0205 -0.0039 113 ILE   A CB  
851  C CG1 . ILE   A 107 ? 0.2202 0.4134 0.3524 -0.0034 -0.0208 -0.0042 113 ILE   A CG1 
852  C CG2 . ILE   A 107 ? 0.2179 0.4066 0.3418 -0.0070 -0.0165 -0.0060 113 ILE   A CG2 
853  C CD1 . ILE   A 107 ? 0.2398 0.4313 0.3803 -0.0019 -0.0188 -0.0048 113 ILE   A CD1 
854  N N   . LEU   A 108 ? 0.1839 0.3787 0.2979 -0.0100 -0.0194 -0.0034 114 LEU   A N   
855  C CA  . LEU   A 108 ? 0.1784 0.3733 0.2890 -0.0130 -0.0185 -0.0034 114 LEU   A CA  
856  C C   . LEU   A 108 ? 0.1778 0.3698 0.2874 -0.0153 -0.0161 -0.0058 114 LEU   A C   
857  O O   . LEU   A 108 ? 0.1732 0.3666 0.2831 -0.0158 -0.0151 -0.0069 114 LEU   A O   
858  C CB  . LEU   A 108 ? 0.1680 0.3680 0.2781 -0.0144 -0.0195 -0.0022 114 LEU   A CB  
859  C CG  . LEU   A 108 ? 0.1875 0.3887 0.2952 -0.0184 -0.0193 -0.0018 114 LEU   A CG  
860  C CD1 . LEU   A 108 ? 0.1996 0.3990 0.3067 -0.0192 -0.0189 -0.0010 114 LEU   A CD1 
861  C CD2 . LEU   A 108 ? 0.1983 0.4053 0.3075 -0.0196 -0.0211 0.0001  114 LEU   A CD2 
862  N N   . ARG   A 109 ? 0.1816 0.3693 0.2897 -0.0168 -0.0148 -0.0068 115 ARG   A N   
863  C CA  . ARG   A 109 ? 0.1969 0.3807 0.3033 -0.0190 -0.0119 -0.0100 115 ARG   A CA  
864  C C   . ARG   A 109 ? 0.1961 0.3771 0.2980 -0.0233 -0.0116 -0.0111 115 ARG   A C   
865  O O   . ARG   A 109 ? 0.1842 0.3647 0.2865 -0.0237 -0.0129 -0.0091 115 ARG   A O   
866  C CB  . ARG   A 109 ? 0.2325 0.4118 0.3441 -0.0159 -0.0097 -0.0113 115 ARG   A CB  
867  C CG  . ARG   A 109 ? 0.3004 0.4745 0.4143 -0.0149 -0.0099 -0.0105 115 ARG   A CG  
868  C CD  . ARG   A 109 ? 0.3488 0.5180 0.4691 -0.0124 -0.0070 -0.0123 115 ARG   A CD  
869  N NE  . ARG   A 109 ? 0.3829 0.5553 0.5099 -0.0087 -0.0080 -0.0109 115 ARG   A NE  
870  C CZ  . ARG   A 109 ? 0.3949 0.5682 0.5263 -0.0077 -0.0050 -0.0130 115 ARG   A CZ  
871  N NH1 . ARG   A 109 ? 0.3846 0.5556 0.5124 -0.0102 -0.0002 -0.0169 115 ARG   A NH1 
872  N NH2 . ARG   A 109 ? 0.3711 0.5477 0.5098 -0.0047 -0.0066 -0.0112 115 ARG   A NH2 
873  N N   . CYS   A 110 ? 0.1968 0.3758 0.2936 -0.0269 -0.0098 -0.0141 116 CYS   A N   
874  C CA  . CYS   A 110 ? 0.2108 0.3864 0.3025 -0.0318 -0.0099 -0.0158 116 CYS   A CA  
875  C C   . CYS   A 110 ? 0.2287 0.3955 0.3188 -0.0324 -0.0054 -0.0207 116 CYS   A C   
876  O O   . CYS   A 110 ? 0.2283 0.3931 0.3233 -0.0285 -0.0025 -0.0218 116 CYS   A O   
877  C CB  . CYS   A 110 ? 0.2108 0.3906 0.2966 -0.0362 -0.0121 -0.0155 116 CYS   A CB  
878  S SG  . CYS   A 110 ? 0.2537 0.4324 0.3337 -0.0373 -0.0090 -0.0186 116 CYS   A SG  
879  N N   . GLN   A 111 ? 0.2491 0.4109 0.3332 -0.0373 -0.0047 -0.0238 117 GLN   A N   
880  C CA  . GLN   A 111 ? 0.2750 0.4276 0.3571 -0.0381 0.0002  -0.0293 117 GLN   A CA  
881  C C   . GLN   A 111 ? 0.2842 0.4359 0.3630 -0.0376 0.0047  -0.0329 117 GLN   A C   
882  O O   . GLN   A 111 ? 0.3004 0.4453 0.3809 -0.0363 0.0101  -0.0371 117 GLN   A O   
883  C CB  . GLN   A 111 ? 0.3116 0.4582 0.3862 -0.0445 -0.0004 -0.0325 117 GLN   A CB  
884  C CG  . GLN   A 111 ? 0.3708 0.5203 0.4347 -0.0504 -0.0027 -0.0335 117 GLN   A CG  
885  C CD  . GLN   A 111 ? 0.4459 0.5894 0.5021 -0.0574 -0.0042 -0.0368 117 GLN   A CD  
886  O OE1 . GLN   A 111 ? 0.4630 0.6108 0.5190 -0.0611 -0.0096 -0.0335 117 GLN   A OE1 
887  N NE2 . GLN   A 111 ? 0.4494 0.5827 0.4998 -0.0594 0.0007  -0.0434 117 GLN   A NE2 
888  N N   . HIS   A 112 ? 0.2783 0.4369 0.3534 -0.0386 0.0029  -0.0309 118 HIS   A N   
889  C CA  . HIS   A 112 ? 0.2838 0.4424 0.3549 -0.0388 0.0072  -0.0335 118 HIS   A CA  
890  C C   . HIS   A 112 ? 0.2770 0.4399 0.3580 -0.0330 0.0089  -0.0313 118 HIS   A C   
891  O O   . HIS   A 112 ? 0.2923 0.4549 0.3725 -0.0325 0.0136  -0.0334 118 HIS   A O   
892  C CB  . HIS   A 112 ? 0.2938 0.4566 0.3545 -0.0441 0.0040  -0.0322 118 HIS   A CB  
893  C CG  . HIS   A 112 ? 0.3285 0.4876 0.3794 -0.0507 0.0013  -0.0341 118 HIS   A CG  
894  N ND1 . HIS   A 112 ? 0.3462 0.5108 0.3977 -0.0531 -0.0055 -0.0297 118 HIS   A ND1 
895  C CD2 . HIS   A 112 ? 0.3483 0.4988 0.3897 -0.0552 0.0046  -0.0400 118 HIS   A CD2 
896  C CE1 . HIS   A 112 ? 0.3484 0.5081 0.3911 -0.0593 -0.0069 -0.0326 118 HIS   A CE1 
897  N NE2 . HIS   A 112 ? 0.3602 0.5108 0.3957 -0.0610 -0.0011 -0.0391 118 HIS   A NE2 
898  N N   . GLY   A 113 ? 0.2516 0.4188 0.3413 -0.0289 0.0050  -0.0269 119 GLY   A N   
899  C CA  . GLY   A 113 ? 0.2261 0.3974 0.3251 -0.0239 0.0053  -0.0246 119 GLY   A CA  
900  C C   . GLY   A 113 ? 0.2061 0.3842 0.3078 -0.0223 -0.0004 -0.0196 119 GLY   A C   
901  O O   . GLY   A 113 ? 0.1976 0.3771 0.2969 -0.0236 -0.0041 -0.0176 119 GLY   A O   
902  N N   . VAL   A 114 ? 0.1813 0.3636 0.2886 -0.0194 -0.0006 -0.0178 120 VAL   A N   
903  C CA  . VAL   A 114 ? 0.1702 0.3580 0.2804 -0.0176 -0.0053 -0.0139 120 VAL   A CA  
904  C C   . VAL   A 114 ? 0.1547 0.3465 0.2586 -0.0209 -0.0075 -0.0124 120 VAL   A C   
905  O O   . VAL   A 114 ? 0.1543 0.3466 0.2540 -0.0235 -0.0055 -0.0132 120 VAL   A O   
906  C CB  . VAL   A 114 ? 0.1848 0.3751 0.3032 -0.0141 -0.0049 -0.0129 120 VAL   A CB  
907  C CG1 . VAL   A 114 ? 0.1955 0.3905 0.3158 -0.0127 -0.0095 -0.0096 120 VAL   A CG1 
908  C CG2 . VAL   A 114 ? 0.1984 0.3855 0.3249 -0.0106 -0.0040 -0.0133 120 VAL   A CG2 
909  N N   . VAL   A 115 ? 0.1420 0.3366 0.2457 -0.0210 -0.0115 -0.0098 121 VAL   A N   
910  C CA  . VAL   A 115 ? 0.1432 0.3422 0.2437 -0.0236 -0.0144 -0.0073 121 VAL   A CA  
911  C C   . VAL   A 115 ? 0.1494 0.3529 0.2550 -0.0208 -0.0166 -0.0045 121 VAL   A C   
912  O O   . VAL   A 115 ? 0.1561 0.3627 0.2606 -0.0225 -0.0179 -0.0026 121 VAL   A O   
913  C CB  . VAL   A 115 ? 0.1524 0.3520 0.2514 -0.0253 -0.0167 -0.0062 121 VAL   A CB  
914  C CG1 . VAL   A 115 ? 0.1573 0.3623 0.2558 -0.0276 -0.0201 -0.0030 121 VAL   A CG1 
915  C CG2 . VAL   A 115 ? 0.1629 0.3573 0.2568 -0.0286 -0.0148 -0.0092 121 VAL   A CG2 
916  N N   . GLY   A 116 ? 0.1445 0.3476 0.2551 -0.0170 -0.0174 -0.0042 122 GLY   A N   
917  C CA  . GLY   A 116 ? 0.1455 0.3515 0.2605 -0.0144 -0.0196 -0.0023 122 GLY   A CA  
918  C C   . GLY   A 116 ? 0.1537 0.3580 0.2719 -0.0109 -0.0206 -0.0026 122 GLY   A C   
919  O O   . GLY   A 116 ? 0.1581 0.3593 0.2760 -0.0102 -0.0198 -0.0037 122 GLY   A O   
920  N N   . ILE   A 117 ? 0.1427 0.3486 0.2635 -0.0090 -0.0226 -0.0016 123 ILE   A N   
921  C CA  . ILE   A 117 ? 0.1517 0.3556 0.2735 -0.0063 -0.0242 -0.0020 123 ILE   A CA  
922  C C   . ILE   A 117 ? 0.1472 0.3521 0.2677 -0.0052 -0.0252 -0.0014 123 ILE   A C   
923  O O   . ILE   A 117 ? 0.1511 0.3587 0.2734 -0.0057 -0.0253 -0.0005 123 ILE   A O   
924  C CB  . ILE   A 117 ? 0.1679 0.3712 0.2944 -0.0048 -0.0256 -0.0024 123 ILE   A CB  
925  C CG1 . ILE   A 117 ? 0.1693 0.3751 0.2989 -0.0052 -0.0261 -0.0016 123 ILE   A CG1 
926  C CG2 . ILE   A 117 ? 0.1847 0.3867 0.3142 -0.0048 -0.0240 -0.0031 123 ILE   A CG2 
927  C CD1 . ILE   A 117 ? 0.1811 0.3864 0.3164 -0.0041 -0.0278 -0.0018 123 ILE   A CD1 
928  N N   . VAL   A 118 ? 0.1436 0.3461 0.2611 -0.0038 -0.0258 -0.0018 124 VAL   A N   
929  C CA  . VAL   A 118 ? 0.1486 0.3513 0.2642 -0.0027 -0.0255 -0.0019 124 VAL   A CA  
930  C C   . VAL   A 118 ? 0.1373 0.3402 0.2560 -0.0014 -0.0268 -0.0027 124 VAL   A C   
931  O O   . VAL   A 118 ? 0.1157 0.3167 0.2358 -0.0009 -0.0289 -0.0035 124 VAL   A O   
932  C CB  . VAL   A 118 ? 0.1777 0.3769 0.2876 -0.0019 -0.0257 -0.0023 124 VAL   A CB  
933  C CG1 . VAL   A 118 ? 0.1941 0.3928 0.3010 -0.0007 -0.0243 -0.0032 124 VAL   A CG1 
934  C CG2 . VAL   A 118 ? 0.1878 0.3865 0.2955 -0.0034 -0.0242 -0.0010 124 VAL   A CG2 
935  N N   . SER   A 119 ? 0.1420 0.3471 0.2632 -0.0010 -0.0256 -0.0023 125 SER   A N   
936  C CA  . SER   A 119 ? 0.1550 0.3595 0.2801 0.0003  -0.0266 -0.0029 125 SER   A CA  
937  C C   . SER   A 119 ? 0.1728 0.3765 0.2979 0.0022  -0.0247 -0.0041 125 SER   A C   
938  O O   . SER   A 119 ? 0.1703 0.3709 0.2962 0.0036  -0.0253 -0.0061 125 SER   A O   
939  C CB  . SER   A 119 ? 0.1511 0.3592 0.2821 -0.0010 -0.0272 -0.0006 125 SER   A CB  
940  O OG  . SER   A 119 ? 0.1632 0.3706 0.2991 0.0001  -0.0282 -0.0005 125 SER   A OG  
941  N N   . THR   A 120 ? 0.1846 0.3910 0.3096 0.0020  -0.0219 -0.0030 126 THR   A N   
942  C CA  . THR   A 120 ? 0.2061 0.4124 0.3324 0.0040  -0.0186 -0.0041 126 THR   A CA  
943  C C   . THR   A 120 ? 0.2188 0.4250 0.3394 0.0037  -0.0154 -0.0044 126 THR   A C   
944  O O   . THR   A 120 ? 0.2181 0.4246 0.3349 0.0019  -0.0161 -0.0032 126 THR   A O   
945  C CB  . THR   A 120 ? 0.2248 0.4361 0.3614 0.0044  -0.0180 -0.0014 126 THR   A CB  
946  O OG1 . THR   A 120 ? 0.2377 0.4542 0.3764 0.0024  -0.0175 0.0016  126 THR   A OG1 
947  C CG2 . THR   A 120 ? 0.2266 0.4383 0.3686 0.0041  -0.0212 0.0000  126 THR   A CG2 
948  N N   . GLY   A 121 ? 0.2357 0.4412 0.3563 0.0055  -0.0113 -0.0059 127 GLY   A N   
949  C CA  . GLY   A 121 ? 0.2495 0.4551 0.3650 0.0051  -0.0073 -0.0058 127 GLY   A CA  
950  C C   . GLY   A 121 ? 0.2606 0.4655 0.3771 0.0074  -0.0017 -0.0080 127 GLY   A C   
951  O O   . GLY   A 121 ? 0.2582 0.4617 0.3794 0.0096  -0.0009 -0.0100 127 GLY   A O   
952  N N   . GLY   A 122 ? 0.2662 0.4717 0.3783 0.0069  0.0028  -0.0076 128 GLY   A N   
953  C CA  . GLY   A 122 ? 0.2734 0.4784 0.3859 0.0089  0.0098  -0.0097 128 GLY   A CA  
954  C C   . GLY   A 122 ? 0.2686 0.4813 0.3915 0.0085  0.0139  -0.0061 128 GLY   A C   
955  O O   . GLY   A 122 ? 0.2625 0.4810 0.3945 0.0071  0.0105  -0.0023 128 GLY   A O   
956  N N   . ASN   A 123 ? 0.2686 0.4813 0.3897 0.0095  0.0214  -0.0073 129 ASN   A N   
957  C CA  . ASN   A 123 ? 0.2667 0.4873 0.3994 0.0093  0.0264  -0.0039 129 ASN   A CA  
958  C C   . ASN   A 123 ? 0.2520 0.4766 0.3846 0.0054  0.0236  0.0006  129 ASN   A C   
959  O O   . ASN   A 123 ? 0.2563 0.4885 0.4015 0.0045  0.0245  0.0044  129 ASN   A O   
960  C CB  . ASN   A 123 ? 0.2880 0.5151 0.4392 0.0115  0.0260  -0.0021 129 ASN   A CB  
961  C CG  . ASN   A 123 ? 0.3529 0.5763 0.5074 0.0156  0.0302  -0.0063 129 ASN   A CG  
962  O OD1 . ASN   A 123 ? 0.3791 0.5970 0.5246 0.0170  0.0368  -0.0107 129 ASN   A OD1 
963  N ND2 . ASN   A 123 ? 0.3582 0.5839 0.5250 0.0174  0.0267  -0.0051 129 ASN   A ND2 
964  N N   . GLY   A 124 ? 0.2343 0.4535 0.3535 0.0032  0.0202  0.0004  130 GLY   A N   
965  C CA  . GLY   A 124 ? 0.2182 0.4396 0.3371 -0.0004 0.0176  0.0043  130 GLY   A CA  
966  C C   . GLY   A 124 ? 0.2032 0.4276 0.3291 -0.0019 0.0107  0.0062  130 GLY   A C   
967  O O   . GLY   A 124 ? 0.1990 0.4259 0.3272 -0.0051 0.0087  0.0091  130 GLY   A O   
968  N N   . LEU   A 125 ? 0.1851 0.4086 0.3134 -0.0001 0.0071  0.0045  131 LEU   A N   
969  C CA  . LEU   A 125 ? 0.1793 0.4048 0.3121 -0.0018 0.0010  0.0060  131 LEU   A CA  
970  C C   . LEU   A 125 ? 0.1847 0.4040 0.3088 -0.0014 -0.0032 0.0036  131 LEU   A C   
971  O O   . LEU   A 125 ? 0.2059 0.4203 0.3236 0.0007  -0.0023 0.0006  131 LEU   A O   
972  C CB  . LEU   A 125 ? 0.1787 0.4098 0.3243 -0.0003 0.0003  0.0073  131 LEU   A CB  
973  C CG  . LEU   A 125 ? 0.2002 0.4388 0.3576 -0.0008 0.0037  0.0106  131 LEU   A CG  
974  C CD1 . LEU   A 125 ? 0.2198 0.4629 0.3903 0.0019  0.0041  0.0116  131 LEU   A CD1 
975  C CD2 . LEU   A 125 ? 0.1954 0.4382 0.3557 -0.0052 0.0002  0.0141  131 LEU   A CD2 
976  N N   . VAL   A 126 ? 0.1597 0.3791 0.2839 -0.0036 -0.0077 0.0047  132 VAL   A N   
977  C CA  . VAL   A 126 ? 0.1503 0.3653 0.2694 -0.0033 -0.0114 0.0029  132 VAL   A CA  
978  C C   . VAL   A 126 ? 0.1400 0.3583 0.2654 -0.0044 -0.0147 0.0042  132 VAL   A C   
979  O O   . VAL   A 126 ? 0.1277 0.3504 0.2577 -0.0068 -0.0153 0.0065  132 VAL   A O   
980  C CB  . VAL   A 126 ? 0.1534 0.3639 0.2649 -0.0048 -0.0127 0.0029  132 VAL   A CB  
981  C CG1 . VAL   A 126 ? 0.1451 0.3578 0.2586 -0.0080 -0.0126 0.0051  132 VAL   A CG1 
982  C CG2 . VAL   A 126 ? 0.1622 0.3692 0.2714 -0.0044 -0.0163 0.0014  132 VAL   A CG2 
983  N N   . GLY   A 127 ? 0.1462 0.3626 0.2719 -0.0030 -0.0167 0.0028  133 GLY   A N   
984  C CA  . GLY   A 127 ? 0.1395 0.3586 0.2699 -0.0042 -0.0195 0.0044  133 GLY   A CA  
985  C C   . GLY   A 127 ? 0.1549 0.3706 0.2811 -0.0050 -0.0217 0.0031  133 GLY   A C   
986  O O   . GLY   A 127 ? 0.1640 0.3757 0.2868 -0.0033 -0.0219 0.0010  133 GLY   A O   
987  N N   . PHE   A 128 ? 0.1513 0.3687 0.2778 -0.0077 -0.0232 0.0044  134 PHE   A N   
988  C CA  . PHE   A 128 ? 0.1486 0.3634 0.2720 -0.0087 -0.0241 0.0032  134 PHE   A CA  
989  C C   . PHE   A 128 ? 0.1489 0.3658 0.2749 -0.0099 -0.0256 0.0048  134 PHE   A C   
990  O O   . PHE   A 128 ? 0.1379 0.3584 0.2660 -0.0119 -0.0267 0.0073  134 PHE   A O   
991  C CB  . PHE   A 128 ? 0.1468 0.3603 0.2661 -0.0114 -0.0234 0.0028  134 PHE   A CB  
992  C CG  . PHE   A 128 ? 0.1443 0.3560 0.2613 -0.0110 -0.0220 0.0024  134 PHE   A CG  
993  C CD1 . PHE   A 128 ? 0.1483 0.3557 0.2624 -0.0094 -0.0216 0.0010  134 PHE   A CD1 
994  C CD2 . PHE   A 128 ? 0.1499 0.3646 0.2684 -0.0126 -0.0214 0.0041  134 PHE   A CD2 
995  C CE1 . PHE   A 128 ? 0.1528 0.3583 0.2642 -0.0094 -0.0204 0.0015  134 PHE   A CE1 
996  C CE2 . PHE   A 128 ? 0.1602 0.3732 0.2766 -0.0127 -0.0197 0.0042  134 PHE   A CE2 
997  C CZ  . PHE   A 128 ? 0.1587 0.3669 0.2709 -0.0111 -0.0192 0.0030  134 PHE   A CZ  
998  N N   . ALA   A 129 ? 0.1411 0.3559 0.2675 -0.0091 -0.0259 0.0038  135 ALA   A N   
999  C CA  . ALA   A 129 ? 0.1472 0.3635 0.2754 -0.0105 -0.0269 0.0054  135 ALA   A CA  
1000 C C   . ALA   A 129 ? 0.1567 0.3725 0.2798 -0.0138 -0.0257 0.0050  135 ALA   A C   
1001 O O   . ALA   A 129 ? 0.1434 0.3564 0.2647 -0.0134 -0.0239 0.0026  135 ALA   A O   
1002 C CB  . ALA   A 129 ? 0.1442 0.3584 0.2754 -0.0086 -0.0272 0.0044  135 ALA   A CB  
1003 N N   . ASP   A 130 ? 0.1669 0.3852 0.2878 -0.0172 -0.0266 0.0073  136 ASP   A N   
1004 C CA  . ASP   A 130 ? 0.1755 0.3924 0.2895 -0.0210 -0.0252 0.0062  136 ASP   A CA  
1005 C C   . ASP   A 130 ? 0.1777 0.3931 0.2907 -0.0213 -0.0230 0.0054  136 ASP   A C   
1006 O O   . ASP   A 130 ? 0.1763 0.3931 0.2934 -0.0204 -0.0239 0.0075  136 ASP   A O   
1007 C CB  . ASP   A 130 ? 0.1924 0.4122 0.3031 -0.0251 -0.0278 0.0092  136 ASP   A CB  
1008 C CG  . ASP   A 130 ? 0.2655 0.4830 0.3669 -0.0297 -0.0264 0.0074  136 ASP   A CG  
1009 O OD1 . ASP   A 130 ? 0.2690 0.4834 0.3676 -0.0301 -0.0245 0.0041  136 ASP   A OD1 
1010 O OD2 . ASP   A 130 ? 0.3164 0.5344 0.4127 -0.0332 -0.0271 0.0091  136 ASP   A OD2 
1011 N N   . VAL   A 131 ? 0.1718 0.3840 0.2804 -0.0226 -0.0196 0.0023  137 VAL   A N   
1012 C CA  . VAL   A 131 ? 0.1827 0.3938 0.2909 -0.0232 -0.0162 0.0014  137 VAL   A CA  
1013 C C   . VAL   A 131 ? 0.2044 0.4135 0.3026 -0.0280 -0.0133 -0.0001 137 VAL   A C   
1014 O O   . VAL   A 131 ? 0.2080 0.4162 0.3045 -0.0292 -0.0095 -0.0009 137 VAL   A O   
1015 C CB  . VAL   A 131 ? 0.1752 0.3842 0.2896 -0.0197 -0.0137 -0.0012 137 VAL   A CB  
1016 C CG1 . VAL   A 131 ? 0.1702 0.3804 0.2919 -0.0159 -0.0170 0.0000  137 VAL   A CG1 
1017 C CG2 . VAL   A 131 ? 0.1768 0.3822 0.2889 -0.0195 -0.0113 -0.0046 137 VAL   A CG2 
1018 N N   . ARG   A 132 ? 0.2093 0.4176 0.3010 -0.0311 -0.0149 -0.0007 138 ARG   A N   
1019 C CA  . ARG   A 132 ? 0.2170 0.4221 0.2975 -0.0361 -0.0127 -0.0029 138 ARG   A CA  
1020 C C   . ARG   A 132 ? 0.2308 0.4372 0.3037 -0.0405 -0.0129 -0.0003 138 ARG   A C   
1021 O O   . ARG   A 132 ? 0.2470 0.4499 0.3094 -0.0446 -0.0095 -0.0030 138 ARG   A O   
1022 C CB  . ARG   A 132 ? 0.2124 0.4166 0.2885 -0.0389 -0.0157 -0.0035 138 ARG   A CB  
1023 C CG  . ARG   A 132 ? 0.2064 0.4081 0.2876 -0.0357 -0.0147 -0.0062 138 ARG   A CG  
1024 C CD  . ARG   A 132 ? 0.2321 0.4336 0.3100 -0.0389 -0.0179 -0.0059 138 ARG   A CD  
1025 N NE  . ARG   A 132 ? 0.2533 0.4609 0.3368 -0.0383 -0.0229 -0.0012 138 ARG   A NE  
1026 C CZ  . ARG   A 132 ? 0.2641 0.4736 0.3484 -0.0405 -0.0262 0.0004  138 ARG   A CZ  
1027 N NH1 . ARG   A 132 ? 0.2486 0.4541 0.3272 -0.0442 -0.0257 -0.0025 138 ARG   A NH1 
1028 N NH2 . ARG   A 132 ? 0.2339 0.4493 0.3253 -0.0392 -0.0298 0.0047  138 ARG   A NH2 
1029 N N   . ASP   A 133 ? 0.2146 0.4255 0.2922 -0.0398 -0.0168 0.0049  139 ASP   A N   
1030 C CA  . ASP   A 133 ? 0.2201 0.4324 0.2913 -0.0438 -0.0176 0.0087  139 ASP   A CA  
1031 C C   . ASP   A 133 ? 0.2290 0.4407 0.3025 -0.0426 -0.0123 0.0083  139 ASP   A C   
1032 O O   . ASP   A 133 ? 0.2422 0.4538 0.3083 -0.0465 -0.0110 0.0107  139 ASP   A O   
1033 C CB  . ASP   A 133 ? 0.2293 0.4465 0.3062 -0.0436 -0.0242 0.0151  139 ASP   A CB  
1034 C CG  . ASP   A 133 ? 0.2948 0.5141 0.3851 -0.0379 -0.0249 0.0166  139 ASP   A CG  
1035 O OD1 . ASP   A 133 ? 0.3031 0.5211 0.3993 -0.0337 -0.0230 0.0129  139 ASP   A OD1 
1036 O OD2 . ASP   A 133 ? 0.3017 0.5235 0.3963 -0.0378 -0.0277 0.0216  139 ASP   A OD2 
1037 N N   . LEU   A 134 ? 0.2203 0.4316 0.3039 -0.0376 -0.0095 0.0059  140 LEU   A N   
1038 C CA  . LEU   A 134 ? 0.2254 0.4369 0.3141 -0.0362 -0.0048 0.0057  140 LEU   A CA  
1039 C C   . LEU   A 134 ? 0.2337 0.4414 0.3153 -0.0383 0.0028  0.0009  140 LEU   A C   
1040 O O   . LEU   A 134 ? 0.2345 0.4405 0.3227 -0.0350 0.0068  -0.0030 140 LEU   A O   
1041 C CB  . LEU   A 134 ? 0.2196 0.4323 0.3221 -0.0305 -0.0059 0.0052  140 LEU   A CB  
1042 C CG  . LEU   A 134 ? 0.2299 0.4452 0.3388 -0.0283 -0.0122 0.0087  140 LEU   A CG  
1043 C CD1 . LEU   A 134 ? 0.2335 0.4486 0.3528 -0.0233 -0.0133 0.0070  140 LEU   A CD1 
1044 C CD2 . LEU   A 134 ? 0.2321 0.4496 0.3420 -0.0301 -0.0143 0.0139  140 LEU   A CD2 
1045 N N   . LEU   A 135 ? 0.2301 0.4362 0.2981 -0.0439 0.0047  0.0012  141 LEU   A N   
1046 C CA  . LEU   A 135 ? 0.2372 0.4385 0.2956 -0.0467 0.0125  -0.0040 141 LEU   A CA  
1047 C C   . LEU   A 135 ? 0.2375 0.4391 0.3036 -0.0444 0.0203  -0.0056 141 LEU   A C   
1048 O O   . LEU   A 135 ? 0.2298 0.4277 0.2955 -0.0436 0.0274  -0.0111 141 LEU   A O   
1049 C CB  . LEU   A 135 ? 0.2491 0.4484 0.2894 -0.0539 0.0124  -0.0030 141 LEU   A CB  
1050 C CG  . LEU   A 135 ? 0.2783 0.4780 0.3107 -0.0574 0.0041  -0.0004 141 LEU   A CG  
1051 C CD1 . LEU   A 135 ? 0.3021 0.4985 0.3147 -0.0652 0.0047  -0.0005 141 LEU   A CD1 
1052 C CD2 . LEU   A 135 ? 0.2845 0.4822 0.3205 -0.0551 0.0020  -0.0044 141 LEU   A CD2 
1053 N N   . TRP   A 136 ? 0.2297 0.4357 0.3039 -0.0433 0.0192  -0.0007 142 TRP   A N   
1054 C CA  . TRP   A 136 ? 0.2436 0.4511 0.3272 -0.0415 0.0261  -0.0011 142 TRP   A CA  
1055 C C   . TRP   A 136 ? 0.2547 0.4624 0.3534 -0.0357 0.0279  -0.0047 142 TRP   A C   
1056 O O   . TRP   A 136 ? 0.2605 0.4690 0.3672 -0.0342 0.0348  -0.0062 142 TRP   A O   
1057 C CB  . TRP   A 136 ? 0.2428 0.4548 0.3325 -0.0420 0.0233  0.0054  142 TRP   A CB  
1058 C CG  . TRP   A 136 ? 0.2510 0.4656 0.3496 -0.0390 0.0143  0.0090  142 TRP   A CG  
1059 C CD1 . TRP   A 136 ? 0.2651 0.4803 0.3584 -0.0407 0.0071  0.0130  142 TRP   A CD1 
1060 C CD2 . TRP   A 136 ? 0.2496 0.4661 0.3640 -0.0337 0.0116  0.0087  142 TRP   A CD2 
1061 N NE1 . TRP   A 136 ? 0.2646 0.4818 0.3695 -0.0365 0.0012  0.0146  142 TRP   A NE1 
1062 C CE2 . TRP   A 136 ? 0.2581 0.4757 0.3748 -0.0325 0.0037  0.0120  142 TRP   A CE2 
1063 C CE3 . TRP   A 136 ? 0.2544 0.4718 0.3815 -0.0301 0.0151  0.0062  142 TRP   A CE3 
1064 C CZ2 . TRP   A 136 ? 0.2607 0.4794 0.3897 -0.0282 -0.0006 0.0120  142 TRP   A CZ2 
1065 C CZ3 . TRP   A 136 ? 0.2555 0.4745 0.3950 -0.0261 0.0097  0.0070  142 TRP   A CZ3 
1066 C CH2 . TRP   A 136 ? 0.2550 0.4742 0.3942 -0.0253 0.0022  0.0094  142 TRP   A CH2 
1067 N N   . LEU   A 137 ? 0.2642 0.4713 0.3671 -0.0325 0.0220  -0.0056 143 LEU   A N   
1068 C CA  . LEU   A 137 ? 0.2860 0.4928 0.4017 -0.0274 0.0228  -0.0083 143 LEU   A CA  
1069 C C   . LEU   A 137 ? 0.3256 0.5279 0.4394 -0.0273 0.0310  -0.0139 143 LEU   A C   
1070 O O   . LEU   A 137 ? 0.3158 0.5184 0.4425 -0.0233 0.0338  -0.0155 143 LEU   A O   
1071 C CB  . LEU   A 137 ? 0.2837 0.4898 0.4007 -0.0250 0.0153  -0.0080 143 LEU   A CB  
1072 C CG  . LEU   A 137 ? 0.2860 0.4958 0.4093 -0.0232 0.0080  -0.0037 143 LEU   A CG  
1073 C CD1 . LEU   A 137 ? 0.2831 0.4918 0.4044 -0.0217 0.0021  -0.0039 143 LEU   A CD1 
1074 C CD2 . LEU   A 137 ? 0.2920 0.5044 0.4300 -0.0197 0.0080  -0.0027 143 LEU   A CD2 
1075 N N   . ASP   A 138 ? 0.3625 0.5604 0.4606 -0.0318 0.0347  -0.0169 144 ASP   A N   
1076 C CA  . ASP   A 138 ? 0.4044 0.5966 0.4994 -0.0320 0.0431  -0.0232 144 ASP   A CA  
1077 C C   . ASP   A 138 ? 0.4484 0.6410 0.5448 -0.0330 0.0534  -0.0248 144 ASP   A C   
1078 O O   . ASP   A 138 ? 0.4520 0.6396 0.5470 -0.0328 0.0617  -0.0303 144 ASP   A O   
1079 C CB  . ASP   A 138 ? 0.4319 0.6182 0.5081 -0.0371 0.0430  -0.0266 144 ASP   A CB  
1080 C CG  . ASP   A 138 ? 0.4951 0.6806 0.5685 -0.0370 0.0343  -0.0256 144 ASP   A CG  
1081 O OD1 . ASP   A 138 ? 0.5115 0.6989 0.5974 -0.0323 0.0302  -0.0243 144 ASP   A OD1 
1082 O OD2 . ASP   A 138 ? 0.5245 0.7077 0.5834 -0.0421 0.0315  -0.0260 144 ASP   A OD2 
1083 N N   . GLU   A 139 ? 0.4807 0.6783 0.5790 -0.0345 0.0535  -0.0201 145 GLU   A N   
1084 C CA  . GLU   A 139 ? 0.5246 0.7228 0.6232 -0.0362 0.0639  -0.0211 145 GLU   A CA  
1085 C C   . GLU   A 139 ? 0.5525 0.7579 0.6690 -0.0334 0.0641  -0.0163 145 GLU   A C   
1086 O O   . GLU   A 139 ? 0.5538 0.7632 0.6784 -0.0315 0.0552  -0.0117 145 GLU   A O   
1087 C CB  . GLU   A 139 ? 0.5721 0.7679 0.6488 -0.0433 0.0659  -0.0205 145 GLU   A CB  
1088 C CG  . GLU   A 139 ? 0.6526 0.8524 0.7251 -0.0458 0.0563  -0.0132 145 GLU   A CG  
1089 C CD  . GLU   A 139 ? 0.7711 0.9682 0.8214 -0.0530 0.0551  -0.0116 145 GLU   A CD  
1090 O OE1 . GLU   A 139 ? 0.7826 0.9833 0.8310 -0.0550 0.0481  -0.0049 145 GLU   A OE1 
1091 O OE2 . GLU   A 139 ? 0.8133 1.0045 0.8481 -0.0567 0.0607  -0.0169 145 GLU   A OE2 
1092 N N   . GLU   A 140 ? 0.5718 0.7785 0.6943 -0.0336 0.0747  -0.0176 146 GLU   A N   
1093 C CA  . GLU   A 140 ? 0.5891 0.8026 0.7290 -0.0319 0.0769  -0.0133 146 GLU   A CA  
1094 C C   . GLU   A 140 ? 0.5988 0.8171 0.7574 -0.0271 0.0672  -0.0096 146 GLU   A C   
1095 O O   . GLU   A 140 ? 0.6008 0.8243 0.7780 -0.0247 0.0689  -0.0074 146 GLU   A O   
1096 C CB  . GLU   A 140 ? 0.6296 0.8452 0.7591 -0.0375 0.0783  -0.0085 146 GLU   A CB  
1097 C CG  . GLU   A 140 ? 0.7035 0.9229 0.8352 -0.0381 0.0673  -0.0017 146 GLU   A CG  
1098 C CD  . GLU   A 140 ? 0.8057 1.0315 0.9571 -0.0364 0.0672  0.0030  146 GLU   A CD  
1099 O OE1 . GLU   A 140 ? 0.8203 1.0486 0.9821 -0.0338 0.0577  0.0061  146 GLU   A OE1 
1100 O OE2 . GLU   A 140 ? 0.8410 1.0691 0.9976 -0.0377 0.0770  0.0032  146 GLU   A OE2 
1101 N N1  . A1B2Q B .   ? 0.1927 0.3940 0.3345 0.0048  -0.0272 -0.0042 201 A1B2Q A N1  
1102 C C4  . A1B2Q B .   ? 0.2193 0.4107 0.3203 0.0048  -0.0195 -0.0115 201 A1B2Q A C4  
1103 C C5  . A1B2Q B .   ? 0.2167 0.4065 0.3224 0.0061  -0.0201 -0.0136 201 A1B2Q A C5  
1104 C C6  . A1B2Q B .   ? 0.2251 0.4124 0.3303 0.0079  -0.0162 -0.0164 201 A1B2Q A C6  
1105 C C7  . A1B2Q B .   ? 0.2192 0.4041 0.3308 0.0094  -0.0168 -0.0185 201 A1B2Q A C7  
1106 C C8  . A1B2Q B .   ? 0.2037 0.3958 0.3320 0.0084  -0.0216 -0.0128 201 A1B2Q A C8  
1107 C C10 . A1B2Q B .   ? 0.2067 0.4043 0.3499 0.0070  -0.0259 -0.0068 201 A1B2Q A C10 
1108 C C13 . A1B2Q B .   ? 0.2133 0.3950 0.3259 0.0071  -0.0260 -0.0185 201 A1B2Q A C13 
1109 O O1  . A1B2Q B .   ? 0.2220 0.3983 0.3248 0.0067  -0.0266 -0.0217 201 A1B2Q A O1  
1110 C C12 . A1B2Q B .   ? 0.2098 0.3935 0.3297 0.0059  -0.0302 -0.0162 201 A1B2Q A C12 
1111 C C11 . A1B2Q B .   ? 0.2036 0.3937 0.3328 0.0058  -0.0292 -0.0120 201 A1B2Q A C11 
1112 C C9  . A1B2Q B .   ? 0.2061 0.3978 0.3405 0.0076  -0.0255 -0.0116 201 A1B2Q A C9  
1113 O O   . A1B2Q B .   ? 0.2110 0.4095 0.3619 0.0083  -0.0249 -0.0055 201 A1B2Q A O   
1114 N N   . A1B2Q B .   ? 0.2132 0.3992 0.3306 0.0083  -0.0217 -0.0168 201 A1B2Q A N   
1115 C C1  . A1B2Q B .   ? 0.2345 0.4216 0.3341 0.0083  -0.0112 -0.0172 201 A1B2Q A C1  
1116 S S   . A1B2Q B .   ? 0.2539 0.4374 0.3533 0.0109  -0.0048 -0.0215 201 A1B2Q A S   
1117 C C   . A1B2Q B .   ? 0.2532 0.4377 0.3446 0.0105  0.0018  -0.0212 201 A1B2Q A C   
1118 C C3  . A1B2Q B .   ? 0.2232 0.4141 0.3187 0.0050  -0.0153 -0.0119 201 A1B2Q A C3  
1119 C C2  . A1B2Q B .   ? 0.2295 0.4186 0.3241 0.0067  -0.0109 -0.0146 201 A1B2Q A C2  
# 
