data_7I4J
# 
_entry.id   7I4J 
# 
_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   7I4J         pdb_00007i4j 10.2210/pdb7i4j/pdb 
WWPDB D_1001408306 ?            ?                   
# 
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                        7I4J 
_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-{[3-(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    198 ?         ? ? ? 
# 
_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-{[3-(methylsulfanyl)phenyl]methyl}-6-oxopiperidine-3-carboxamide' A1B2X 
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 
A1B2X non-polymer         . '(3S)-1-{[3-(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        A1B2X 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1B2X 
_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 A1B2X 1   201 201 A1B2X 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   301 276 HOH   HOH A . 
F 5 HOH   2   302 49  HOH   HOH A . 
F 5 HOH   3   303 245 HOH   HOH A . 
F 5 HOH   4   304 137 HOH   HOH A . 
F 5 HOH   5   305 217 HOH   HOH A . 
F 5 HOH   6   306 46  HOH   HOH A . 
F 5 HOH   7   307 152 HOH   HOH A . 
F 5 HOH   8   308 43  HOH   HOH A . 
F 5 HOH   9   309 30  HOH   HOH A . 
F 5 HOH   10  310 135 HOH   HOH A . 
F 5 HOH   11  311 260 HOH   HOH A . 
F 5 HOH   12  312 68  HOH   HOH A . 
F 5 HOH   13  313 173 HOH   HOH A . 
F 5 HOH   14  314 34  HOH   HOH A . 
F 5 HOH   15  315 183 HOH   HOH A . 
F 5 HOH   16  316 252 HOH   HOH A . 
F 5 HOH   17  317 263 HOH   HOH A . 
F 5 HOH   18  318 167 HOH   HOH A . 
F 5 HOH   19  319 77  HOH   HOH A . 
F 5 HOH   20  320 59  HOH   HOH A . 
F 5 HOH   21  321 33  HOH   HOH A . 
F 5 HOH   22  322 258 HOH   HOH A . 
F 5 HOH   23  323 55  HOH   HOH A . 
F 5 HOH   24  324 104 HOH   HOH A . 
F 5 HOH   25  325 108 HOH   HOH A . 
F 5 HOH   26  326 214 HOH   HOH A . 
F 5 HOH   27  327 169 HOH   HOH A . 
F 5 HOH   28  328 119 HOH   HOH A . 
F 5 HOH   29  329 107 HOH   HOH A . 
F 5 HOH   30  330 41  HOH   HOH A . 
F 5 HOH   31  331 70  HOH   HOH A . 
F 5 HOH   32  332 26  HOH   HOH A . 
F 5 HOH   33  333 146 HOH   HOH A . 
F 5 HOH   34  334 133 HOH   HOH A . 
F 5 HOH   35  335 24  HOH   HOH A . 
F 5 HOH   36  336 216 HOH   HOH A . 
F 5 HOH   37  337 4   HOH   HOH A . 
F 5 HOH   38  338 268 HOH   HOH A . 
F 5 HOH   39  339 47  HOH   HOH A . 
F 5 HOH   40  340 42  HOH   HOH A . 
F 5 HOH   41  341 161 HOH   HOH A . 
F 5 HOH   42  342 178 HOH   HOH A . 
F 5 HOH   43  343 67  HOH   HOH A . 
F 5 HOH   44  344 37  HOH   HOH A . 
F 5 HOH   45  345 251 HOH   HOH A . 
F 5 HOH   46  346 191 HOH   HOH A . 
F 5 HOH   47  347 25  HOH   HOH A . 
F 5 HOH   48  348 15  HOH   HOH A . 
F 5 HOH   49  349 111 HOH   HOH A . 
F 5 HOH   50  350 9   HOH   HOH A . 
F 5 HOH   51  351 275 HOH   HOH A . 
F 5 HOH   52  352 7   HOH   HOH A . 
F 5 HOH   53  353 121 HOH   HOH A . 
F 5 HOH   54  354 94  HOH   HOH A . 
F 5 HOH   55  355 20  HOH   HOH A . 
F 5 HOH   56  356 85  HOH   HOH A . 
F 5 HOH   57  357 21  HOH   HOH A . 
F 5 HOH   58  358 105 HOH   HOH A . 
F 5 HOH   59  359 50  HOH   HOH A . 
F 5 HOH   60  360 254 HOH   HOH A . 
F 5 HOH   61  361 211 HOH   HOH A . 
F 5 HOH   62  362 124 HOH   HOH A . 
F 5 HOH   63  363 157 HOH   HOH A . 
F 5 HOH   64  364 156 HOH   HOH A . 
F 5 HOH   65  365 103 HOH   HOH A . 
F 5 HOH   66  366 264 HOH   HOH A . 
F 5 HOH   67  367 257 HOH   HOH A . 
F 5 HOH   68  368 60  HOH   HOH A . 
F 5 HOH   69  369 2   HOH   HOH A . 
F 5 HOH   70  370 253 HOH   HOH A . 
F 5 HOH   71  371 205 HOH   HOH A . 
F 5 HOH   72  372 180 HOH   HOH A . 
F 5 HOH   73  373 28  HOH   HOH A . 
F 5 HOH   74  374 181 HOH   HOH A . 
F 5 HOH   75  375 18  HOH   HOH A . 
F 5 HOH   76  376 106 HOH   HOH A . 
F 5 HOH   77  377 36  HOH   HOH A . 
F 5 HOH   78  378 144 HOH   HOH A . 
F 5 HOH   79  379 256 HOH   HOH A . 
F 5 HOH   80  380 16  HOH   HOH A . 
F 5 HOH   81  381 182 HOH   HOH A . 
F 5 HOH   82  382 174 HOH   HOH A . 
F 5 HOH   83  383 74  HOH   HOH A . 
F 5 HOH   84  384 29  HOH   HOH A . 
F 5 HOH   85  385 52  HOH   HOH A . 
F 5 HOH   86  386 57  HOH   HOH A . 
F 5 HOH   87  387 147 HOH   HOH A . 
F 5 HOH   88  388 19  HOH   HOH A . 
F 5 HOH   89  389 126 HOH   HOH A . 
F 5 HOH   90  390 102 HOH   HOH A . 
F 5 HOH   91  391 219 HOH   HOH A . 
F 5 HOH   92  392 231 HOH   HOH A . 
F 5 HOH   93  393 170 HOH   HOH A . 
F 5 HOH   94  394 110 HOH   HOH A . 
F 5 HOH   95  395 27  HOH   HOH A . 
F 5 HOH   96  396 62  HOH   HOH A . 
F 5 HOH   97  397 11  HOH   HOH A . 
F 5 HOH   98  398 84  HOH   HOH A . 
F 5 HOH   99  399 79  HOH   HOH A . 
F 5 HOH   100 400 177 HOH   HOH A . 
F 5 HOH   101 401 113 HOH   HOH A . 
F 5 HOH   102 402 82  HOH   HOH A . 
F 5 HOH   103 403 12  HOH   HOH A . 
F 5 HOH   104 404 131 HOH   HOH A . 
F 5 HOH   105 405 51  HOH   HOH A . 
F 5 HOH   106 406 274 HOH   HOH A . 
F 5 HOH   107 407 203 HOH   HOH A . 
F 5 HOH   108 408 248 HOH   HOH A . 
F 5 HOH   109 409 39  HOH   HOH A . 
F 5 HOH   110 410 132 HOH   HOH A . 
F 5 HOH   111 411 148 HOH   HOH A . 
F 5 HOH   112 412 123 HOH   HOH A . 
F 5 HOH   113 413 8   HOH   HOH A . 
F 5 HOH   114 414 262 HOH   HOH A . 
F 5 HOH   115 415 40  HOH   HOH A . 
F 5 HOH   116 416 64  HOH   HOH A . 
F 5 HOH   117 417 35  HOH   HOH A . 
F 5 HOH   118 418 17  HOH   HOH A . 
F 5 HOH   119 419 10  HOH   HOH A . 
F 5 HOH   120 420 89  HOH   HOH A . 
F 5 HOH   121 421 13  HOH   HOH A . 
F 5 HOH   122 422 192 HOH   HOH A . 
F 5 HOH   123 423 80  HOH   HOH A . 
F 5 HOH   124 424 176 HOH   HOH A . 
F 5 HOH   125 425 98  HOH   HOH A . 
F 5 HOH   126 426 96  HOH   HOH A . 
F 5 HOH   127 427 255 HOH   HOH A . 
F 5 HOH   128 428 38  HOH   HOH A . 
F 5 HOH   129 429 91  HOH   HOH A . 
F 5 HOH   130 430 220 HOH   HOH A . 
F 5 HOH   131 431 23  HOH   HOH A . 
F 5 HOH   132 432 168 HOH   HOH A . 
F 5 HOH   133 433 141 HOH   HOH A . 
F 5 HOH   134 434 100 HOH   HOH A . 
F 5 HOH   135 435 5   HOH   HOH A . 
F 5 HOH   136 436 95  HOH   HOH A . 
F 5 HOH   137 437 186 HOH   HOH A . 
F 5 HOH   138 438 90  HOH   HOH A . 
F 5 HOH   139 439 61  HOH   HOH A . 
F 5 HOH   140 440 120 HOH   HOH A . 
F 5 HOH   141 441 76  HOH   HOH A . 
F 5 HOH   142 442 53  HOH   HOH A . 
F 5 HOH   143 443 138 HOH   HOH A . 
F 5 HOH   144 444 128 HOH   HOH A . 
F 5 HOH   145 445 212 HOH   HOH A . 
F 5 HOH   146 446 233 HOH   HOH A . 
F 5 HOH   147 447 159 HOH   HOH A . 
F 5 HOH   148 448 201 HOH   HOH A . 
F 5 HOH   149 449 83  HOH   HOH A . 
F 5 HOH   150 450 69  HOH   HOH A . 
F 5 HOH   151 451 155 HOH   HOH A . 
F 5 HOH   152 452 72  HOH   HOH A . 
F 5 HOH   153 453 269 HOH   HOH A . 
F 5 HOH   154 454 158 HOH   HOH A . 
F 5 HOH   155 455 162 HOH   HOH A . 
F 5 HOH   156 456 175 HOH   HOH A . 
F 5 HOH   157 457 87  HOH   HOH A . 
F 5 HOH   158 458 151 HOH   HOH A . 
F 5 HOH   159 459 71  HOH   HOH A . 
F 5 HOH   160 460 213 HOH   HOH A . 
F 5 HOH   161 461 48  HOH   HOH A . 
F 5 HOH   162 462 221 HOH   HOH A . 
F 5 HOH   163 463 207 HOH   HOH A . 
F 5 HOH   164 464 246 HOH   HOH A . 
F 5 HOH   165 465 240 HOH   HOH A . 
F 5 HOH   166 466 267 HOH   HOH A . 
F 5 HOH   167 467 65  HOH   HOH A . 
F 5 HOH   168 468 134 HOH   HOH A . 
F 5 HOH   169 469 99  HOH   HOH A . 
F 5 HOH   170 470 171 HOH   HOH A . 
F 5 HOH   171 471 189 HOH   HOH A . 
F 5 HOH   172 472 127 HOH   HOH A . 
F 5 HOH   173 473 229 HOH   HOH A . 
F 5 HOH   174 474 270 HOH   HOH A . 
F 5 HOH   175 475 164 HOH   HOH A . 
F 5 HOH   176 476 272 HOH   HOH A . 
F 5 HOH   177 477 265 HOH   HOH A . 
F 5 HOH   178 478 86  HOH   HOH A . 
F 5 HOH   179 479 129 HOH   HOH A . 
F 5 HOH   180 480 266 HOH   HOH A . 
F 5 HOH   181 481 150 HOH   HOH A . 
F 5 HOH   182 482 56  HOH   HOH A . 
F 5 HOH   183 483 209 HOH   HOH A . 
F 5 HOH   184 484 73  HOH   HOH A . 
F 5 HOH   185 485 273 HOH   HOH A . 
F 5 HOH   186 486 243 HOH   HOH A . 
F 5 HOH   187 487 202 HOH   HOH A . 
F 5 HOH   188 488 122 HOH   HOH A . 
F 5 HOH   189 489 241 HOH   HOH A . 
F 5 HOH   190 490 179 HOH   HOH A . 
F 5 HOH   191 491 271 HOH   HOH A . 
F 5 HOH   192 492 153 HOH   HOH A . 
F 5 HOH   193 493 118 HOH   HOH A . 
F 5 HOH   194 494 92  HOH   HOH A . 
F 5 HOH   195 495 230 HOH   HOH A . 
F 5 HOH   196 496 222 HOH   HOH A . 
F 5 HOH   197 497 208 HOH   HOH A . 
F 5 HOH   198 498 117 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           7I4J 
_cell.length_a           88.368 
_cell.length_b           57.469 
_cell.length_c           32.688 
_cell.angle_alpha        90.00 
_cell.angle_beta         91.09 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I4J 
_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          7I4J 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.61 
_exptl_crystal.density_percent_sol   52.89 
_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                     7I4J 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             48.17 
_reflns.d_resolution_high            1.44 
_reflns.number_obs                   29070 
_reflns.percent_possible_obs         98.7 
_reflns.pdbx_Rmerge_I_obs            0.131 
_reflns.pdbx_netI_over_sigmaI        5.8 
_reflns.pdbx_redundancy              6.4 
_reflns.pdbx_Rrim_I_all              0.143 
_reflns.pdbx_Rpim_I_all              0.055 
_reflns.pdbx_CC_half                 0.996 
_reflns.pdbx_number_measured_all     187195 
_reflns.pdbx_chi_squared             0.31 
_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                  1.44 
_reflns_shell.d_res_low                   1.47 
_reflns_shell.number_measured_all         6630 
_reflns_shell.number_unique_obs           1372 
_reflns_shell.Rmerge_I_obs                3.300 
_reflns_shell.pdbx_chi_squared            0.02 
_reflns_shell.pdbx_redundancy             4.8 
_reflns_shell.percent_possible_obs        91.3 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.1 
_reflns_shell.pdbx_Rrim_I_all             3.700 
_reflns_shell.pdbx_Rpim_I_all             1.644 
_reflns_shell.pdbx_CC_half                0.261 
_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                                 7I4J 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     23731 
_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                             22.09 
_refine.ls_d_res_high                            1.445 
_refine.ls_percent_reflns_obs                    80.8 
_refine.ls_R_factor_obs                          0.2148 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2123 
_refine.ls_R_factor_R_free                       0.2624 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.070 
_refine.ls_number_reflns_R_free                  1202 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.961 
_refine.correlation_coeff_Fo_to_Fc_free          0.939 
_refine.B_iso_mean                               30.77 
_refine.aniso_B[1][1]                            -4.21020 
_refine.aniso_B[2][2]                            0.42280 
_refine.aniso_B[3][3]                            3.78740 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -0.48340 
_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             0.088 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.096 
_refine.pdbx_overall_SU_R_Blow_DPI               0.095 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.101 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7I4J 
_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             196 
_refine_hist.number_atoms_total               1307 
_refine_hist.d_res_high                       1.445 
_refine_hist.d_res_low                        22.09 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
t_bond_d                  0.011 ? 2.00  1155 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               0.98  ? 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           3.86  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           16.15 ? ?     ?    '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  1141 '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                       1.45 
_refine_ls_shell.d_res_low                        1.50 
_refine_ls_shell.number_reflns_R_work             453 
_refine_ls_shell.R_factor_R_work                  0.3761 
_refine_ls_shell.percent_reflns_obs               14.92 
_refine_ls_shell.R_factor_R_free                  0.3605 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            4.63 
_refine_ls_shell.number_reflns_R_free             22 
_refine_ls_shell.number_reflns_all                475 
_refine_ls_shell.R_factor_all                     0.3754 
# 
_struct.entry_id                  7I4J 
_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-0036648-001 (A71EV2A-x4710)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I4J 
_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              7I4J 
_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 ? ? ? ? ? ? ? 2.384 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.379 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.268 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 C ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.243 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 52  ? A CYS 58  ? 1_555 111.0 ? 
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_555 109.8 ? 
3 SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 113.0 ? 
4 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 110.9 ? 
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 97.0  ? 
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_555 114.6 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA1 2 LEU A 34  ? CYS A 44  ? LEU A 40  CYS A 50  
AA1 3 ILE A 4   ? ASN A 13  ? ILE A 10  ASN A 19  
AA2 1 LYS A 64  ? SER A 69  ? LYS A 70  SER A 75  
AA2 2 THR A 54  ? CYS A 59  ? THR A 60  CYS A 65  
AA2 3 ILE A 107 ? CYS A 110 ? ILE A 113 CYS A 116 
AA2 4 GLY A 113 ? GLY A 122 ? GLY A 119 GLY A 128 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 26  ? N VAL A 32  O VAL A 36  ? O VAL A 42  
AA1 2 3 N LEU A 35  ? N LEU A 41  O VAL A 12  ? O VAL A 18  
AA2 1 2 O LYS A 64  ? O LYS A 70  N CYS A 59  ? N CYS A 65  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N LEU A 108 ? N LEU A 114 O VAL A 115 ? O VAL A 121 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O ASP A 130 ? O ASP A 136 N HIS A 91  ? N HIS A 97  
AA2 6 7 O GLN A 89  ? O GLN A 95  N ILE A 76  ? N ILE A 82  
# 
_pdbx_entry_details.entry_id                   7I4J 
_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 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   A HOH 364 ? ? O A HOH 491 ? ? 2.17 
2 1 OE2 A GLU 88  ? ? O A HOH 301 ? ? 2.19 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 CYS A 116 ? ? -116.64 -169.28 
2 1 SER A 125 ? ? -138.65 -31.03  
# 
_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         15.6122 
_pdbx_refine_tls.origin_y         7.4569 
_pdbx_refine_tls.origin_z         13.3952 
_pdbx_refine_tls.T[1][1]          -0.0876 
_pdbx_refine_tls.T[2][2]          -0.0552 
_pdbx_refine_tls.T[3][3]          0.0945 
_pdbx_refine_tls.T[1][2]          -0.0074 
_pdbx_refine_tls.T[1][3]          0.0010 
_pdbx_refine_tls.T[2][3]          0.0070 
_pdbx_refine_tls.L[1][1]          0.8713 
_pdbx_refine_tls.L[2][2]          2.2414 
_pdbx_refine_tls.L[3][3]          0.2420 
_pdbx_refine_tls.L[1][2]          0.3606 
_pdbx_refine_tls.L[1][3]          -0.2951 
_pdbx_refine_tls.L[2][3]          -0.3104 
_pdbx_refine_tls.S[1][1]          -0.0497 
_pdbx_refine_tls.S[1][2]          0.0203 
_pdbx_refine_tls.S[1][3]          0.1072 
_pdbx_refine_tls.S[2][1]          -0.0241 
_pdbx_refine_tls.S[2][2]          0.0239 
_pdbx_refine_tls.S[2][3]          -0.1525 
_pdbx_refine_tls.S[3][1]          0.0039 
_pdbx_refine_tls.S[3][2]          -0.0743 
_pdbx_refine_tls.S[3][3]          0.0258 
# 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   '{ A|* }' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A 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 
A1B2X N1   N  N N 1   
A1B2X C4   C  Y N 2   
A1B2X C5   C  Y N 3   
A1B2X C6   C  N N 4   
A1B2X C7   C  N N 5   
A1B2X C8   C  N R 6   
A1B2X C10  C  N N 7   
A1B2X C13  C  Y N 8   
A1B2X O1   O  N N 9   
A1B2X C12  C  N N 10  
A1B2X C11  C  N N 11  
A1B2X C9   C  N N 12  
A1B2X O    O  N N 13  
A1B2X N    N  N N 14  
A1B2X C3   C  Y N 15  
A1B2X C2   C  Y N 16  
A1B2X C1   C  Y N 17  
A1B2X S    S  N N 18  
A1B2X C    C  N N 19  
A1B2X H12  H  N N 20  
A1B2X H11  H  N N 21  
A1B2X H6   H  N N 22  
A1B2X H8   H  N N 23  
A1B2X H7   H  N N 24  
A1B2X H10  H  N N 25  
A1B2X H9   H  N N 26  
A1B2X H    H  N N 27  
A1B2X H14  H  N N 28  
A1B2X H13  H  N N 29  
A1B2X H17  H  N N 30  
A1B2X H16  H  N N 31  
A1B2X H15  H  N N 32  
A1B2X H5   H  N N 33  
A1B2X H4   H  N N 34  
A1B2X H2   H  N N 35  
A1B2X H1   H  N N 36  
A1B2X H3   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 
A1B2X C   S    sing N N 1   
A1B2X S   C1   sing N N 2   
A1B2X C1  C2   sing Y N 3   
A1B2X C2  C3   doub Y N 4   
A1B2X C3  C4   sing Y N 5   
A1B2X C4  C5   doub Y N 6   
A1B2X C5  C6   sing N N 7   
A1B2X C6  N    sing N N 8   
A1B2X N   C7   sing N N 9   
A1B2X C7  C8   sing N N 10  
A1B2X C9  C8   sing N N 11  
A1B2X N1  C9   sing N N 12  
A1B2X O   C9   doub N N 13  
A1B2X C8  C10  sing N N 14  
A1B2X C10 C11  sing N N 15  
A1B2X C11 C12  sing N N 16  
A1B2X N   C12  sing N N 17  
A1B2X C12 O1   doub N N 18  
A1B2X C13 C5   sing Y N 19  
A1B2X C1  C13  doub Y N 20  
A1B2X N1  H12  sing N N 21  
A1B2X N1  H11  sing N N 22  
A1B2X C4  H6   sing N N 23  
A1B2X C6  H8   sing N N 24  
A1B2X C6  H7   sing N N 25  
A1B2X C7  H10  sing N N 26  
A1B2X C7  H9   sing N N 27  
A1B2X C8  H    sing N N 28  
A1B2X C10 H14  sing N N 29  
A1B2X C10 H13  sing N N 30  
A1B2X C13 H17  sing N N 31  
A1B2X C11 H16  sing N N 32  
A1B2X C11 H15  sing N N 33  
A1B2X C3  H5   sing N N 34  
A1B2X C2  H4   sing N N 35  
A1B2X C   H2   sing N N 36  
A1B2X C   H1   sing N N 37  
A1B2X C   H3   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                    7I4J 
_atom_sites.fract_transf_matrix[1][1]   0.011316 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000215 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017401 
_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]   0.030598 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER   A 1 1   ? 19.826 6.794   23.430 1.00 28.52 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 21.002 6.847   22.536 1.00 29.94 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 21.013 5.728   21.479 1.00 29.77 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 20.262 4.750   21.616 1.00 30.43 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 22.289 6.837   23.357 1.00 32.92 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 22.635 5.517   23.742 1.00 36.45 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 21.839 5.875   20.438 1.00 28.69 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 21.941 4.854   19.402 1.00 28.54 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 22.246 5.382   18.016 1.00 27.81 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 21.889 6.512   17.698 1.00 27.57 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 22.903 4.575   17.174 1.00 27.22 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 23.216 4.975   15.796 1.00 27.62 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 23.171 3.802   14.801 1.00 27.30 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 23.287 2.641   15.207 1.00 28.27 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 24.600 5.638   15.747 1.00 27.65 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 23.023 4.119   13.497 1.00 25.55 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 23.091 3.190   12.383 1.00 23.82 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 24.478 3.373   11.693 1.00 24.51 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.910 4.493   11.389 1.00 24.52 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.942 3.467   11.379 1.00 23.37 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 20.560 3.574   12.067 1.00 22.43 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.918 2.439   10.254 1.00 24.56 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.514 4.202   11.149 1.00 22.97 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 25.186 2.259   11.474 1.00 25.21 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 26.476 2.282   10.813 1.00 25.83 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 26.351 1.544   9.499  1.00 26.49 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 26.215 0.314   9.478  1.00 27.85 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.548 1.650   11.704 1.00 26.74 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.785 2.439   12.970 1.00 27.87 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 28.564 3.594   12.959 1.00 29.06 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 27.184 2.074   14.163 1.00 29.97 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 28.748 4.349   14.107 1.00 30.56 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 27.362 2.822   15.319 1.00 30.94 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 28.133 3.970   15.283 1.00 32.00 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 28.255 4.749   16.410 1.00 34.21 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 26.263 2.278   8.428  1.00 26.67 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 26.142 1.727   7.089  1.00 27.73 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.281 2.284   6.230  1.00 29.79 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.483 3.511   6.175  1.00 29.92 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.755 2.008   6.474  1.00 28.14 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.356 3.491   6.619  1.00 27.50 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.712 1.565   5.017  1.00 29.33 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.086 1.400   5.612  1.00 30.69 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.241 1.824   4.816  1.00 30.92 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.168 2.742   5.598  1.00 31.38 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.477 2.458   6.757  1.00 32.06 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.492 3.903   5.038  1.00 31.27 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.296 4.877   5.756  1.00 31.15 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.420 6.017   6.299  1.00 30.50 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.867 7.161   6.334  1.00 30.27 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.451 5.392   4.912  1.00 34.20 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.540 4.365   4.759  1.00 42.09 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.370 4.142   5.665  1.00 44.57 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.539 3.696   3.616  1.00 43.49 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.197 5.697   6.759  1.00 29.62 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.276 6.705   7.318  1.00 29.08 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.787 6.310   8.723  1.00 28.19 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.640 5.126   9.044  1.00 27.64 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 27.040 6.879   6.407  1.00 28.97 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.357 7.393   5.023  1.00 29.85 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 27.997 8.616   4.844  1.00 30.99 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 26.939 6.704   3.891  1.00 30.95 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.272 9.106   3.576  1.00 31.97 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.204 7.188   2.614  1.00 32.38 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 27.854 8.404   2.465  1.00 33.58 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.120 8.927   1.228  1.00 36.39 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.514 7.307   9.537  1.00 26.56 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.945 7.129   10.867 1.00 25.74 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.689 7.945   10.908 1.00 24.81 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.758 9.164   10.728 1.00 24.39 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.939 7.535   11.966 1.00 26.31 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 27.343 7.801   13.347 1.00 27.61 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 28.454 7.981   14.381 1.00 30.50 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 28.138 9.027   15.362 1.00 31.60 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 27.648 8.793   16.578 1.00 32.81 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 27.372 7.544   16.964 1.00 31.93 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 27.361 9.807   17.393 1.00 28.60 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 24.530 7.309   11.180 1.00 24.33 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 23.252 8.024   11.245 1.00 24.76 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.820 8.137   12.683 1.00 24.25 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 22.605 7.105   13.312 1.00 24.29 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 22.152 7.295   10.463 1.00 25.06 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.856 8.103   10.466 1.00 24.25 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.621 6.965   9.041  1.00 26.15 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 22.629 9.379   13.191 1.00 22.54 ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 22.214 9.569   14.568 1.00 23.19 ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 21.012 10.548  14.650 1.00 22.82 ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 20.728 11.272  13.673 1.00 22.87 ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 23.390 10.072  15.451 1.00 25.22 ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 24.494 9.036   15.531 1.00 27.78 ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 23.956 11.417  14.919 1.00 25.42 ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 20.338 10.638  15.829 1.00 21.53 ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 19.324 11.693  16.011 1.00 21.39 ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 20.088 13.039  15.963 1.00 23.73 ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 21.119 13.201  16.655 1.00 24.36 ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 18.637 11.617  17.366 1.00 20.58 ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 17.716 10.390  17.492 1.00 22.65 ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 18.134 9.312   17.887 1.00 23.74 ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 16.461 10.523  17.116 1.00 21.86 ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 19.605 13.992  15.171 1.00 23.90 ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 20.281 15.308  15.067 1.00 24.38 ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 20.532 15.935  16.442 1.00 24.45 ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 21.658 16.347  16.709 1.00 26.13 ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 19.500 16.257  14.174 1.00 24.66 ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 20.272 17.563  13.830 1.00 26.24 ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 19.323 18.456  13.085 1.00 26.86 ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.921 19.696  12.580 1.00 27.43 ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.963 20.841  13.264 1.00 29.22 ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 19.611 20.873  14.545 1.00 27.87 ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 20.416 21.952  12.687 1.00 26.45 ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 19.540 15.850  17.365 1.00 22.78 ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 19.718 16.395  18.708 1.00 22.77 ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 20.749 15.691  19.559 1.00 23.94 ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 21.131 16.269  20.567 1.00 25.09 ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 18.401 16.514  19.480 1.00 23.21 ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 17.813 15.202  19.890 1.00 24.32 ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 17.136 14.404  18.980 1.00 24.06 ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 17.776 14.615  21.115 1.00 24.86 ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 16.708 13.355  19.669 1.00 24.71 ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 17.057 13.443  20.968 1.00 24.80 ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 21.202 14.468  19.205 1.00 25.21 ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 22.220 13.744  19.968 1.00 26.27 ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 23.596 13.727  19.258 1.00 29.08 ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 24.514 13.037  19.721 1.00 30.08 ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 21.740 12.292  20.267 1.00 25.75 ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 20.431 12.214  21.087 1.00 25.84 ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 20.018 10.749  21.279 1.00 25.24 ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 20.599 12.906  22.478 1.00 25.45 ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 23.740 14.460  18.119 1.00 29.73 ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 25.010 14.459  17.399 1.00 30.04 ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 26.132 15.044  18.256 1.00 29.44 ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 25.884 15.949  19.049 1.00 29.15 ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 24.887 15.208  16.079 1.00 30.32 ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 27.351 14.518  18.108 1.00 29.19 ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 28.511 14.994  18.882 1.00 30.67 ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 29.302 16.088  18.082 1.00 31.65 ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 29.017 16.312  16.896 1.00 31.25 ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 29.455 13.809  19.220 1.00 33.08 ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 30.144 13.441  18.022 1.00 35.31 ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 28.721 12.599  19.791 1.00 32.74 ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 30.363 16.658  18.701 1.00 32.98 ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 31.271 17.633  18.086 1.00 35.61 ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 31.892 16.996  16.812 1.00 35.60 ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 31.946 17.660  15.771 1.00 36.70 ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 32.339 18.016  19.139 1.00 39.38 ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 33.648 18.518  18.615 1.00 46.52 ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 34.059 19.824  18.840 1.00 50.20 ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 34.653 17.847  17.996 1.00 48.52 ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 35.264 19.917  18.291 1.00 50.77 ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 35.654 18.752  17.761 1.00 49.87 ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 32.351 15.731  16.912 1.00 34.71 ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 32.935 14.976  15.799 1.00 34.93 ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 31.915 14.763  14.655 1.00 33.57 ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 32.304 14.812  13.489 1.00 33.77 ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 33.463 13.606  16.271 1.00 38.93 ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 34.371 12.946  15.260 1.00 46.31 ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 35.454 13.470  14.931 1.00 49.24 ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 33.950 11.792  14.731 1.00 47.92 ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 30.630 14.484  14.982 1.00 31.13 ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 29.605 14.310  13.950 1.00 29.70 ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 29.416 15.618  13.165 1.00 29.12 ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 29.235 15.565  11.949 1.00 29.62 ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 28.242 13.948  14.562 1.00 28.64 ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 28.133 12.559  15.116 1.00 31.98 ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 28.755 11.636  14.535 1.00 33.26 ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 27.390 12.379  16.122 1.00 33.35 ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 29.359 16.768  13.853 1.00 28.69 ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 29.206 18.063  13.174 1.00 29.53 ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 30.453 18.413  12.345 1.00 29.88 ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 30.316 18.867  11.213 1.00 29.93 ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 28.921 19.199  14.173 1.00 29.58 ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 27.514 19.188  14.685 1.00 30.45 ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 27.096 18.818  15.931 1.00 31.51 ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 26.333 19.478  13.927 1.00 30.69 ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 25.719 18.889  16.003 1.00 32.32 ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 25.225 19.274  14.778 1.00 31.87 ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 26.103 19.903  12.609 1.00 31.33 ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 23.920 19.578  14.382 1.00 32.38 ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.807 20.170  12.210 1.00 32.44 ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 23.725 19.957  13.075 1.00 32.60 ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 31.652 18.156  12.891 1.00 30.36 ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.925 18.386  12.169 1.00 30.46 ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.998 17.479  10.916 1.00 31.69 ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.593 17.866  9.911  1.00 33.02 ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 34.109 18.083  13.085 1.00 30.03 ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 32.397 16.263  10.973 1.00 30.82 ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 32.448 15.347  9.832  1.00 30.99 ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 31.073 15.181  9.178  1.00 29.69 ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.733 14.079  8.722  1.00 28.83 ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.990 14.000  10.290 1.00 33.16 ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 34.426 14.157  10.679 1.00 36.38 ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 35.282 14.341  9.819  1.00 38.13 ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 34.709 14.136  11.984 1.00 36.40 ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 30.309 16.297  9.115  1.00 27.71 ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.933 16.308  8.635  1.00 27.96 ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.808 15.972  7.160  1.00 28.92 ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.553 16.510  6.333  1.00 28.60 ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 28.271 17.677  8.915  1.00 27.31 ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.852 17.898  8.408  1.00 26.81 ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.860 17.009  9.147  1.00 26.71 ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.449 19.379  8.530  1.00 27.73 ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.849 15.097  6.831  1.00 27.81 ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.542 14.742  5.448  1.00 28.21 ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 26.193 15.394  5.086  1.00 29.35 ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 26.068 16.062  4.062  1.00 31.44 ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.494 13.188  5.235  1.00 27.97 ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 26.966 12.860  3.839  1.00 27.74 ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 28.872 12.582  5.442  1.00 27.93 ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 25.187 15.224  5.951  1.00 28.45 ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 23.860 15.750  5.698  1.00 28.33 ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 23.063 15.788  7.002  1.00 26.18 ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 23.182 14.888  7.816  1.00 25.38 ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 23.138 14.888  4.630  1.00 28.77 ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.660 15.141  4.507  1.00 29.03 ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 21.046 16.084  3.734  1.00 30.22 ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.618 14.451  5.212  1.00 28.35 ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.677 16.036  3.926  1.00 30.64 ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.389 15.029  4.821  1.00 29.35 ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.603 13.398  6.135  1.00 28.28 ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 18.161 14.555  5.289  1.00 28.76 ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.382 12.968  6.642  1.00 27.86 ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 18.184 13.519  6.190  1.00 27.65 ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 22.253 16.843  7.211  1.00 24.42 ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 21.416 16.932  8.398  1.00 24.96 ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 20.111 17.647  8.049  1.00 24.62 ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 20.078 18.493  7.137  1.00 25.02 ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 22.147 17.592  9.581  1.00 25.83 ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.724 18.983  9.249  1.00 27.41 ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.806 20.194  9.349  1.00 30.08 ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 22.198 21.280  8.859  1.00 27.93 ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 20.704 20.069  9.930  1.00 29.98 ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 19.039 17.332  8.791  1.00 24.44 ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.743 17.958  8.537  1.00 24.73 ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 17.016 18.070  9.867  1.00 23.70 ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 16.572 17.072  10.417 1.00 24.65 ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.972 17.205  7.444  1.00 26.67 ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.626 17.767  7.058  1.00 32.32 ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 15.053 18.515  7.852  1.00 34.10 ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 15.158 17.474  5.928  1.00 33.84 ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.922 19.304  10.395 1.00 22.27 ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 16.285 19.584  11.668 0.50 21.66 ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 16.296 19.517  11.695 0.50 22.41 ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 14.822 19.102  11.667 1.00 21.89 ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 14.318 18.656  12.696 1.00 22.35 ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 16.311 21.096  11.918 0.50 21.42 ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 16.412 20.983  12.132 0.50 24.66 ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 15.919 21.387  13.243 0.50 19.58 ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 15.526 21.792  11.380 0.50 26.57 ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 14.123 19.236  10.492 1.00 20.45 ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 12.727 18.830  10.438 1.00 21.60 ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 12.552 17.319  10.512 1.00 21.94 ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 11.477 16.877  10.858 1.00 23.32 ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 11.995 19.398  9.223  1.00 26.57 ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 12.401 18.776  8.018  1.00 31.54 ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 13.605 16.549  10.255 1.00 21.60 ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 13.580 15.097  10.352 1.00 20.80 ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 14.221 14.562  11.659 1.00 21.36 ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 14.154 13.339  11.902 1.00 21.27 ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 14.337 14.510  9.150  1.00 22.01 ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 13.562 14.686  7.848  1.00 22.85 ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 14.312 14.114  6.658  1.00 23.95 ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 14.336 12.642  6.694  1.00 23.31 ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 14.324 11.865  5.615  1.00 24.14 ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 14.280 12.404  4.399  1.00 23.43 ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 14.280 10.536  5.743  1.00 23.40 ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 14.909 15.445  12.434 1.00 21.22 ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 15.704 15.098  13.623 1.00 21.12 ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 16.791 14.069  13.195 1.00 21.84 ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 17.086 13.151  13.962 1.00 21.50 ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 14.831 14.545  14.765 1.00 22.32 ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 15.600 14.255  16.076 1.00 23.68 ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 16.517 15.017  16.402 1.00 22.86 ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 15.311 13.210  16.733 1.00 22.45 ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 17.396 14.213  11.965 1.00 21.74 ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 18.448 13.297  11.520 1.00 21.22 ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 19.762 14.039  11.197 1.00 22.04 ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 19.758 15.189  10.755 1.00 21.72 ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 18.039 12.524  10.262 1.00 22.04 ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 16.976 11.379  10.421 1.00 24.04 ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 16.755 10.666  9.093  1.00 24.32 ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 17.383 10.378  11.501 1.00 23.32 ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 20.878 13.317  11.381 1.00 22.04 ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 22.197 13.790  11.035 1.00 23.16 ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 23.003 12.586  10.594 1.00 24.21 ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 22.871 11.485  11.173 1.00 25.19 ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 22.892 14.508  12.208 1.00 24.28 ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 24.283 15.105  11.905 1.00 26.04 ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 24.450 16.451  12.596 1.00 26.08 ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 25.416 14.133  12.299 1.00 27.67 ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 23.797 12.756  9.535  1.00 24.28 ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 24.665 11.690  9.029  1.00 25.62 ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 26.076 12.287  8.981  1.00 26.29 ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 26.264 13.439  8.562  1.00 25.44 ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 24.232 11.177  7.625  1.00 26.54 ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 25.228 10.160  7.074  1.00 27.57 ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 22.817 10.603  7.659  1.00 26.26 ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 27.030 11.536  9.511  1.00 27.44 ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 28.421 11.926  9.480  1.00 28.83 ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 29.266 10.805  8.876  1.00 30.26 ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 28.819 9.668   8.755  1.00 29.82 ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 28.918 12.335  10.866 1.00 29.61 ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 28.755 11.275  11.782 1.00 29.74 ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 30.478 11.148  8.424  1.00 30.69 ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 31.379 10.159  7.826  1.00 31.95 ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 32.149 9.413   8.912  1.00 33.32 ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 32.423 9.965   9.977  1.00 34.93 ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 32.378 10.852  6.892  1.00 34.36 ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 32.996 11.919  7.588  1.00 36.85 ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 32.519 8.178   8.641  1.00 33.38 ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 33.297 7.368   9.583  1.00 34.50 ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 34.562 6.876   8.882  1.00 37.16 ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 34.561 6.765   7.650  1.00 37.28 ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 32.499 6.103   9.996  1.00 34.08 ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 32.328 5.265   8.846  1.00 33.72 ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 31.178 6.437   10.643 1.00 33.87 ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? 35.588 6.480   9.656  1.00 38.72 ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? 36.802 5.927   9.048  1.00 41.54 ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? 36.654 4.418   8.818  1.00 41.55 ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? 37.211 3.883   7.863  1.00 42.10 ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? 38.070 6.300   9.867  1.00 45.70 ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? 38.169 5.441   11.012 1.00 48.96 ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? 38.081 7.774   10.303 1.00 45.94 ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? 35.927 3.723   9.702  1.00 40.99 ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? 35.728 2.277   9.590  1.00 40.81 ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 34.375 1.945   8.960  1.00 40.71 ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 33.400 2.687   9.135  1.00 40.61 ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? 35.828 1.622   10.959 1.00 40.82 ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 34.307 0.825   8.246  1.00 40.17 ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 33.068 0.407   7.611  1.00 40.05 ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 32.054 -0.183  8.598  1.00 37.23 ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 32.418 -0.960  9.474  1.00 36.77 ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 33.332 -0.573  6.455  1.00 44.05 ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 32.950 0.033   5.106  1.00 51.74 ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 32.608 -1.047  4.119  1.00 59.56 ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 33.474 -1.539  3.392  1.00 62.72 ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 31.340 -1.448  4.076  1.00 60.67 ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 30.797 0.221   8.446  1.00 35.03 ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 29.679 -0.277  9.239  1.00 33.95 ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 29.092 -1.559  8.687  1.00 33.00 ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 29.341 -1.915  7.531  1.00 33.43 ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 28.284 -2.251  9.494  1.00 32.05 ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 27.715 -3.541  9.101  1.00 32.01 ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 26.193 -3.555  8.979  1.00 31.19 ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 25.632 -4.639  8.745  1.00 31.22 ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 28.188 -4.649  10.049 1.00 32.84 ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 29.989 -4.800  10.184 1.00 37.37 ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 25.505 -2.408  9.232  1.00 29.28 ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 24.046 -2.410  9.169  1.00 28.74 ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 23.619 -2.341  7.677  1.00 28.95 ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 24.381 -1.885  6.814  1.00 29.43 ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 23.451 -1.230  9.991  1.00 30.32 ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 23.719 -1.331  11.503 1.00 34.46 ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 23.734 -2.466  12.029 1.00 34.76 ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 23.929 -0.271  12.155 1.00 31.04 ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 22.430 -2.840  7.387  1.00 29.08 ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 21.826 -2.805  6.049  1.00 30.02 ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 20.551 -1.965  6.182  1.00 29.13 ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 19.755 -2.224  7.083  1.00 28.69 ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 21.476 -4.239  5.561  1.00 32.41 ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 22.678 -4.901  5.159  1.00 34.58 ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 20.488 -4.245  4.378  1.00 32.48 ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 20.361 -0.984  5.301  1.00 27.95 ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 19.161 -0.158  5.336  1.00 26.83 ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 18.087 -0.888  4.541  1.00 26.28 ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 18.360 -1.363  3.435  1.00 27.45 ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 19.408 1.247   4.760  1.00 27.58 ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 20.633 1.904   5.442  1.00 28.95 ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 18.136 2.152   4.908  1.00 27.72 ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 20.438 2.120   6.992  1.00 29.77 ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 16.864 -0.943  5.070  1.00 23.64 ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 15.762 -1.544  4.350  1.00 23.12 ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 15.392 -0.656  3.149  1.00 22.89 ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 15.430 0.574   3.252  1.00 23.42 ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 14.566 -1.700  5.293  1.00 23.01 ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 15.008 -1.255  2.029  1.00 23.86 ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 14.508 -0.544  0.849  1.00 24.87 ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 13.162 -1.238  0.541  1.00 26.22 ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 13.104 -2.250  -0.164 1.00 27.65 ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 15.505 -0.636  -0.308 1.00 26.11 ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 16.885 -0.073  0.058  1.00 27.86 ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 16.894 1.413   0.421  1.00 30.14 ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 18.250 1.858   0.765  1.00 33.31 ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 18.544 3.023   1.348  1.00 33.53 ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 17.580 3.878   1.664  1.00 30.31 ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 19.801 3.333   1.626  1.00 32.60 ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 12.093 -0.742  1.170  1.00 26.17 ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 10.788 -1.396  1.168  1.00 26.36 ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 9.675  -0.418  1.636  1.00 27.29 ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 9.960  0.729   1.991  1.00 27.70 ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 10.892 -2.542  2.161  1.00 24.72 ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 11.062 -1.976  3.878  1.00 26.25 ? 56  CYS   A SG  1 
ATOM   392  N  N   A ASP   A 1 51  ? 8.422  -0.896  1.709  0.50 27.33 ? 57  ASP   A N   1 
ATOM   393  N  N   B ASP   A 1 51  ? 8.422  -0.942  1.693  0.50 28.13 ? 57  ASP   A N   1 
ATOM   394  C  CA  A ASP   A 1 51  ? 7.338  -0.090  2.270  0.50 27.91 ? 57  ASP   A CA  1 
ATOM   395  C  CA  B ASP   A 1 51  ? 7.184  -0.298  2.146  0.50 29.55 ? 57  ASP   A CA  1 
ATOM   396  C  C   A ASP   A 1 51  ? 6.708  -0.790  3.488  0.50 28.33 ? 57  ASP   A C   1 
ATOM   397  C  C   B ASP   A 1 51  ? 6.597  -1.081  3.352  0.50 29.16 ? 57  ASP   A C   1 
ATOM   398  O  O   A ASP   A 1 51  ? 5.574  -0.470  3.826  0.50 27.95 ? 57  ASP   A O   1 
ATOM   399  O  O   B ASP   A 1 51  ? 5.384  -1.110  3.530  0.50 28.92 ? 57  ASP   A O   1 
ATOM   400  C  CB  A ASP   A 1 51  ? 6.276  0.286   1.216  0.50 29.56 ? 57  ASP   A CB  1 
ATOM   401  C  CB  B ASP   A 1 51  ? 6.156  -0.339  1.005  0.50 33.15 ? 57  ASP   A CB  1 
ATOM   402  C  CG  A ASP   A 1 51  ? 5.485  -0.873  0.638  0.50 33.55 ? 57  ASP   A CG  1 
ATOM   403  C  CG  B ASP   A 1 51  ? 5.130  0.769   1.020  0.50 41.40 ? 57  ASP   A CG  1 
ATOM   404  O  OD1 A ASP   A 1 51  ? 5.775  -2.024  0.997  0.50 33.49 ? 57  ASP   A OD1 1 
ATOM   405  O  OD1 B ASP   A 1 51  ? 5.380  1.801   1.676  0.50 43.46 ? 57  ASP   A OD1 1 
ATOM   406  O  OD2 A ASP   A 1 51  ? 4.602  -0.623  -0.213 0.50 36.77 ? 57  ASP   A OD2 1 
ATOM   407  O  OD2 B ASP   A 1 51  ? 4.096  0.627   0.331  0.50 44.77 ? 57  ASP   A OD2 1 
ATOM   408  N  N   . CYS   A 1 52  ? 7.445  -1.734  4.154  1.00 28.36 ? 58  CYS   A N   1 
ATOM   409  C  CA  . CYS   A 1 52  ? 7.007  -2.495  5.338  1.00 27.36 ? 58  CYS   A CA  1 
ATOM   410  C  C   . CYS   A 1 52  ? 6.328  -1.575  6.362  1.00 25.76 ? 58  CYS   A C   1 
ATOM   411  O  O   . CYS   A 1 52  ? 6.727  -0.416  6.527  1.00 23.54 ? 58  CYS   A O   1 
ATOM   412  C  CB  . CYS   A 1 52  ? 8.197  -3.195  5.983  1.00 27.05 ? 58  CYS   A CB  1 
ATOM   413  S  SG  . CYS   A 1 52  ? 8.659  -4.774  5.223  1.00 26.82 ? 58  CYS   A SG  1 
ATOM   414  N  N   . GLN   A 1 53  ? 5.295  -2.103  7.023  1.00 25.05 ? 59  GLN   A N   1 
ATOM   415  C  CA  . GLN   A 1 53  ? 4.614  -1.388  8.093  1.00 25.12 ? 59  GLN   A CA  1 
ATOM   416  C  C   . GLN   A 1 53  ? 4.606  -2.208  9.409  1.00 24.66 ? 59  GLN   A C   1 
ATOM   417  O  O   . GLN   A 1 53  ? 3.810  -1.915  10.284 1.00 24.43 ? 59  GLN   A O   1 
ATOM   418  C  CB  . GLN   A 1 53  ? 3.195  -0.975  7.676  1.00 26.16 ? 59  GLN   A CB  1 
ATOM   419  C  CG  . GLN   A 1 53  ? 3.163  0.361   6.974  1.00 27.91 ? 59  GLN   A CG  1 
ATOM   420  C  CD  . GLN   A 1 53  ? 1.730  0.832   6.786  1.00 30.79 ? 59  GLN   A CD  1 
ATOM   421  O  OE1 . GLN   A 1 53  ? 1.119  0.635   5.719  1.00 31.45 ? 59  GLN   A OE1 1 
ATOM   422  N  NE2 . GLN   A 1 53  ? 1.162  1.453   7.816  1.00 27.60 ? 59  GLN   A NE2 1 
ATOM   423  N  N   . THR   A 1 54  ? 5.428  -3.307  9.492  1.00 23.51 ? 60  THR   A N   1 
ATOM   424  C  CA  . THR   A 1 54  ? 5.582  -4.143  10.677 1.00 22.42 ? 60  THR   A CA  1 
ATOM   425  C  C   . THR   A 1 54  ? 7.079  -4.384  10.850 1.00 19.98 ? 60  THR   A C   1 
ATOM   426  O  O   . THR   A 1 54  ? 7.823  -4.491  9.883  1.00 19.95 ? 60  THR   A O   1 
ATOM   427  C  CB  . THR   A 1 54  ? 4.778  -5.485  10.602 1.00 25.55 ? 60  THR   A CB  1 
ATOM   428  O  OG1 . THR   A 1 54  ? 5.328  -6.266  9.541  1.00 27.74 ? 60  THR   A OG1 1 
ATOM   429  C  CG2 . THR   A 1 54  ? 3.293  -5.263  10.343 1.00 25.67 ? 60  THR   A CG2 1 
ATOM   430  N  N   . GLY   A 1 55  ? 7.512  -4.462  12.103 1.00 18.18 ? 61  GLY   A N   1 
ATOM   431  C  CA  . GLY   A 1 55  ? 8.923  -4.604  12.421 1.00 16.37 ? 61  GLY   A CA  1 
ATOM   432  C  C   . GLY   A 1 55  ? 9.071  -4.713  13.938 1.00 16.51 ? 61  GLY   A C   1 
ATOM   433  O  O   . GLY   A 1 55  ? 8.105  -4.970  14.638 1.00 19.35 ? 61  GLY   A O   1 
ATOM   434  N  N   . VAL   A 1 56  ? 10.277 -4.606  14.432 1.00 16.75 ? 62  VAL   A N   1 
ATOM   435  C  CA  . VAL   A 1 56  ? 10.612 -4.703  15.874 1.00 17.62 ? 62  VAL   A CA  1 
ATOM   436  C  C   . VAL   A 1 56  ? 11.516 -3.516  16.221 1.00 20.11 ? 62  VAL   A C   1 
ATOM   437  O  O   . VAL   A 1 56  ? 12.392 -3.180  15.429 1.00 22.41 ? 62  VAL   A O   1 
ATOM   438  C  CB  . VAL   A 1 56  ? 11.356 -6.061  16.148 1.00 19.54 ? 62  VAL   A CB  1 
ATOM   439  C  CG1 . VAL   A 1 56  ? 11.710 -6.229  17.648 1.00 19.99 ? 62  VAL   A CG1 1 
ATOM   440  C  CG2 . VAL   A 1 56  ? 10.477 -7.208  15.724 1.00 21.02 ? 62  VAL   A CG2 1 
ATOM   441  N  N   . TYR   A 1 57  ? 11.307 -2.856  17.390 1.00 19.44 ? 63  TYR   A N   1 
ATOM   442  C  CA  . TYR   A 1 57  ? 12.198 -1.769  17.784 1.00 18.40 ? 63  TYR   A CA  1 
ATOM   443  C  C   . TYR   A 1 57  ? 12.756 -2.054  19.180 1.00 18.80 ? 63  TYR   A C   1 
ATOM   444  O  O   . TYR   A 1 57  ? 12.116 -2.768  19.918 1.00 19.22 ? 63  TYR   A O   1 
ATOM   445  C  CB  . TYR   A 1 57  ? 11.492 -0.391  17.729 1.00 18.95 ? 63  TYR   A CB  1 
ATOM   446  C  CG  . TYR   A 1 57  ? 10.603 -0.071  18.914 1.00 20.75 ? 63  TYR   A CG  1 
ATOM   447  C  CD1 . TYR   A 1 57  ? 9.335  -0.627  19.030 1.00 21.56 ? 63  TYR   A CD1 1 
ATOM   448  C  CD2 . TYR   A 1 57  ? 11.026 0.794   19.912 1.00 21.86 ? 63  TYR   A CD2 1 
ATOM   449  C  CE1 . TYR   A 1 57  ? 8.486  -0.279  20.080 1.00 22.82 ? 63  TYR   A CE1 1 
ATOM   450  C  CE2 . TYR   A 1 57  ? 10.193 1.138   20.977 1.00 22.96 ? 63  TYR   A CE2 1 
ATOM   451  C  CZ  . TYR   A 1 57  ? 8.929  0.570   21.079 1.00 23.26 ? 63  TYR   A CZ  1 
ATOM   452  O  OH  . TYR   A 1 57  ? 8.081  0.858   22.123 1.00 23.13 ? 63  TYR   A OH  1 
ATOM   453  N  N   . TYR   A 1 58  ? 13.887 -1.481  19.519 1.00 19.28 ? 64  TYR   A N   1 
ATOM   454  C  CA  . TYR   A 1 58  ? 14.489 -1.644  20.847 1.00 19.91 ? 64  TYR   A CA  1 
ATOM   455  C  C   . TYR   A 1 58  ? 14.063 -0.451  21.678 1.00 20.67 ? 64  TYR   A C   1 
ATOM   456  O  O   . TYR   A 1 58  ? 14.366 0.684   21.270 1.00 19.99 ? 64  TYR   A O   1 
ATOM   457  C  CB  . TYR   A 1 58  ? 16.018 -1.578  20.767 1.00 19.74 ? 64  TYR   A CB  1 
ATOM   458  C  CG  . TYR   A 1 58  ? 16.634 -1.720  22.142 1.00 21.27 ? 64  TYR   A CG  1 
ATOM   459  C  CD1 . TYR   A 1 58  ? 16.310 -2.796  22.962 1.00 22.33 ? 64  TYR   A CD1 1 
ATOM   460  C  CD2 . TYR   A 1 58  ? 17.519 -0.771  22.630 1.00 23.00 ? 64  TYR   A CD2 1 
ATOM   461  C  CE1 . TYR   A 1 58  ? 16.858 -2.927  24.241 1.00 22.87 ? 64  TYR   A CE1 1 
ATOM   462  C  CE2 . TYR   A 1 58  ? 18.086 -0.899  23.902 1.00 23.98 ? 64  TYR   A CE2 1 
ATOM   463  C  CZ  . TYR   A 1 58  ? 17.730 -1.965  24.709 1.00 24.59 ? 64  TYR   A CZ  1 
ATOM   464  O  OH  . TYR   A 1 58  ? 18.267 -2.094  25.978 1.00 27.07 ? 64  TYR   A OH  1 
ATOM   465  N  N   . CYS   A 1 59  ? 13.576 -0.707  22.918 1.00 21.41 ? 65  CYS   A N   1 
ATOM   466  C  CA  . CYS   A 1 59  ? 13.165 0.307   23.843 1.00 21.90 ? 65  CYS   A CA  1 
ATOM   467  C  C   . CYS   A 1 59  ? 14.097 0.209   25.099 1.00 22.01 ? 65  CYS   A C   1 
ATOM   468  O  O   . CYS   A 1 59  ? 13.922 -0.680  25.886 1.00 21.97 ? 65  CYS   A O   1 
ATOM   469  C  CB  . CYS   A 1 59  ? 11.693 0.093   24.201 1.00 23.62 ? 65  CYS   A CB  1 
ATOM   470  S  SG  . CYS   A 1 59  ? 11.101 1.092   25.596 1.00 24.78 ? 65  CYS   A SG  1 
ATOM   471  N  N   . SER   A 1 60  ? 15.104 1.076   25.215 1.00 21.19 ? 66  SER   A N   1 
ATOM   472  C  CA  . SER   A 1 60  ? 16.081 1.004   26.299 1.00 22.31 ? 66  SER   A CA  1 
ATOM   473  C  C   . SER   A 1 60  ? 15.477 1.197   27.677 1.00 22.84 ? 66  SER   A C   1 
ATOM   474  O  O   . SER   A 1 60  ? 15.992 0.637   28.636 1.00 23.51 ? 66  SER   A O   1 
ATOM   475  C  CB  . SER   A 1 60  ? 17.231 1.995   26.078 1.00 25.01 ? 66  SER   A CB  1 
ATOM   476  O  OG  . SER   A 1 60  ? 16.762 3.326   26.086 1.00 28.93 ? 66  SER   A OG  1 
ATOM   477  N  N   . SER   A 1 61  ? 14.391 1.999   27.797 1.00 22.64 ? 67  SER   A N   1 
ATOM   478  C  CA  . SER   A 1 61  ? 13.722 2.206   29.093 1.00 22.31 ? 67  SER   A CA  1 
ATOM   479  C  C   . SER   A 1 61  ? 12.960 0.963   29.594 1.00 23.00 ? 67  SER   A C   1 
ATOM   480  O  O   . SER   A 1 61  ? 12.500 0.956   30.743 1.00 23.53 ? 67  SER   A O   1 
ATOM   481  C  CB  . SER   A 1 61  ? 12.781 3.408   29.053 1.00 22.29 ? 67  SER   A CB  1 
ATOM   482  O  OG  . SER   A 1 61  ? 11.702 3.194   28.160 1.00 23.12 ? 67  SER   A OG  1 
ATOM   483  N  N   . ARG   A 1 62  ? 12.882 -0.089  28.786 1.00 22.27 ? 68  ARG   A N   1 
ATOM   484  C  CA  . ARG   A 1 62  ? 12.285 -1.346  29.221 1.00 21.98 ? 68  ARG   A CA  1 
ATOM   485  C  C   . ARG   A 1 62  ? 13.234 -2.529  28.990 1.00 22.60 ? 68  ARG   A C   1 
ATOM   486  O  O   . ARG   A 1 62  ? 12.827 -3.684  29.233 1.00 22.52 ? 68  ARG   A O   1 
ATOM   487  C  CB  . ARG   A 1 62  ? 10.993 -1.613  28.433 1.00 23.73 ? 68  ARG   A CB  1 
ATOM   488  C  CG  . ARG   A 1 62  ? 9.835  -0.658  28.719 1.00 24.82 ? 68  ARG   A CG  1 
ATOM   489  C  CD  . ARG   A 1 62  ? 9.160  -0.987  30.044 1.00 27.19 ? 68  ARG   A CD  1 
ATOM   490  N  NE  . ARG   A 1 62  ? 8.081  -0.043  30.323 1.00 29.21 ? 68  ARG   A NE  1 
ATOM   491  C  CZ  . ARG   A 1 62  ? 8.258  1.140   30.901 1.00 30.96 ? 68  ARG   A CZ  1 
ATOM   492  N  NH1 . ARG   A 1 62  ? 9.452  1.483   31.380 1.00 30.30 ? 68  ARG   A NH1 1 
ATOM   493  N  NH2 . ARG   A 1 62  ? 7.227  1.963   31.070 1.00 31.32 ? 68  ARG   A NH2 1 
ATOM   494  N  N   . ARG   A 1 63  ? 14.441 -2.288  28.380 1.00 22.67 ? 69  ARG   A N   1 
ATOM   495  C  CA  . ARG   A 1 63  ? 15.387 -3.343  27.977 1.00 23.12 ? 69  ARG   A CA  1 
ATOM   496  C  C   . ARG   A 1 63  ? 14.642 -4.437  27.202 1.00 23.06 ? 69  ARG   A C   1 
ATOM   497  O  O   . ARG   A 1 63  ? 14.765 -5.633  27.505 1.00 23.64 ? 69  ARG   A O   1 
ATOM   498  C  CB  . ARG   A 1 63  ? 16.111 -3.924  29.199 1.00 24.43 ? 69  ARG   A CB  1 
ATOM   499  C  CG  . ARG   A 1 63  ? 17.147 -3.002  29.784 1.00 26.69 ? 69  ARG   A CG  1 
ATOM   500  C  CD  . ARG   A 1 63  ? 17.694 -3.611  31.067 1.00 30.78 ? 69  ARG   A CD  1 
ATOM   501  N  NE  . ARG   A 1 63  ? 18.527 -2.661  31.795 1.00 33.60 ? 69  ARG   A NE  1 
ATOM   502  C  CZ  . ARG   A 1 63  ? 18.590 -2.571  33.121 1.00 35.50 ? 69  ARG   A CZ  1 
ATOM   503  N  NH1 . ARG   A 1 63  ? 17.834 -3.353  33.882 1.00 35.38 ? 69  ARG   A NH1 1 
ATOM   504  N  NH2 . ARG   A 1 63  ? 19.355 -1.645  33.696 1.00 34.79 ? 69  ARG   A NH2 1 
ATOM   505  N  N   . LYS   A 1 64  ? 13.844 -4.005  26.189 1.00 21.96 ? 70  LYS   A N   1 
ATOM   506  C  CA  . LYS   A 1 64  ? 12.985 -4.948  25.493 1.00 21.93 ? 70  LYS   A CA  1 
ATOM   507  C  C   . LYS   A 1 64  ? 12.839 -4.547  24.049 1.00 21.24 ? 70  LYS   A C   1 
ATOM   508  O  O   . LYS   A 1 64  ? 12.912 -3.359  23.718 1.00 21.92 ? 70  LYS   A O   1 
ATOM   509  C  CB  . LYS   A 1 64  ? 11.579 -4.945  26.141 1.00 25.94 ? 70  LYS   A CB  1 
ATOM   510  C  CG  . LYS   A 1 64  ? 11.396 -6.044  27.176 1.00 35.80 ? 70  LYS   A CG  1 
ATOM   511  C  CD  . LYS   A 1 64  ? 9.988  -6.605  27.178 1.00 43.59 ? 70  LYS   A CD  1 
ATOM   512  C  CE  . LYS   A 1 64  ? 9.809  -7.533  28.358 1.00 50.66 ? 70  LYS   A CE  1 
ATOM   513  N  NZ  . LYS   A 1 64  ? 10.338 -6.938  29.626 1.00 53.75 ? 70  LYS   A NZ  1 
ATOM   514  N  N   . HIS   A 1 65  ? 12.655 -5.532  23.208 1.00 20.11 ? 71  HIS   A N   1 
ATOM   515  C  CA  . HIS   A 1 65  ? 12.489 -5.352  21.753 1.00 20.40 ? 71  HIS   A CA  1 
ATOM   516  C  C   . HIS   A 1 65  ? 11.020 -5.678  21.488 1.00 21.27 ? 71  HIS   A C   1 
ATOM   517  O  O   . HIS   A 1 65  ? 10.563 -6.809  21.787 1.00 21.41 ? 71  HIS   A O   1 
ATOM   518  C  CB  . HIS   A 1 65  ? 13.419 -6.345  20.988 1.00 21.13 ? 71  HIS   A CB  1 
ATOM   519  C  CG  . HIS   A 1 65  ? 14.877 -6.172  21.317 1.00 21.41 ? 71  HIS   A CG  1 
ATOM   520  N  ND1 . HIS   A 1 65  ? 15.759 -5.558  20.432 1.00 22.65 ? 71  HIS   A ND1 1 
ATOM   521  C  CD2 . HIS   A 1 65  ? 15.536 -6.437  22.477 1.00 21.89 ? 71  HIS   A CD2 1 
ATOM   522  C  CE1 . HIS   A 1 65  ? 16.931 -5.530  21.051 1.00 23.17 ? 71  HIS   A CE1 1 
ATOM   523  N  NE2 . HIS   A 1 65  ? 16.841 -6.020  22.296 1.00 22.72 ? 71  HIS   A NE2 1 
ATOM   524  N  N   . TYR   A 1 66  ? 10.252 -4.682  21.039 1.00 19.98 ? 72  TYR   A N   1 
ATOM   525  C  CA  . TYR   A 1 66  ? 8.839  -4.856  20.844 1.00 20.05 ? 72  TYR   A CA  1 
ATOM   526  C  C   . TYR   A 1 66  ? 8.416  -5.000  19.367 1.00 20.68 ? 72  TYR   A C   1 
ATOM   527  O  O   . TYR   A 1 66  ? 8.766  -4.167  18.541 1.00 20.47 ? 72  TYR   A O   1 
ATOM   528  C  CB  . TYR   A 1 66  ? 8.088  -3.637  21.427 1.00 20.22 ? 72  TYR   A CB  1 
ATOM   529  C  CG  . TYR   A 1 66  ? 8.159  -3.530  22.937 1.00 21.64 ? 72  TYR   A CG  1 
ATOM   530  C  CD1 . TYR   A 1 66  ? 7.336  -4.302  23.748 1.00 23.32 ? 72  TYR   A CD1 1 
ATOM   531  C  CD2 . TYR   A 1 66  ? 8.966  -2.586  23.546 1.00 23.10 ? 72  TYR   A CD2 1 
ATOM   532  C  CE1 . TYR   A 1 66  ? 7.351  -4.160  25.137 1.00 25.01 ? 72  TYR   A CE1 1 
ATOM   533  C  CE2 . TYR   A 1 66  ? 8.982  -2.427  24.928 1.00 24.13 ? 72  TYR   A CE2 1 
ATOM   534  C  CZ  . TYR   A 1 66  ? 8.135  -3.181  25.716 1.00 26.12 ? 72  TYR   A CZ  1 
ATOM   535  O  OH  . TYR   A 1 66  ? 8.202  -3.052  27.086 1.00 28.60 ? 72  TYR   A OH  1 
ATOM   536  N  N   . PRO   A 1 67  ? 7.613  -6.019  19.043 1.00 21.30 ? 73  PRO   A N   1 
ATOM   537  C  CA  . PRO   A 1 67  ? 7.070  -6.106  17.663 1.00 21.43 ? 73  PRO   A CA  1 
ATOM   538  C  C   . PRO   A 1 67  ? 5.967  -5.032  17.537 1.00 22.34 ? 73  PRO   A C   1 
ATOM   539  O  O   . PRO   A 1 67  ? 5.137  -4.925  18.448 1.00 22.69 ? 73  PRO   A O   1 
ATOM   540  C  CB  . PRO   A 1 67  ? 6.450  -7.528  17.589 1.00 22.98 ? 73  PRO   A CB  1 
ATOM   541  C  CG  . PRO   A 1 67  ? 6.427  -8.031  18.947 1.00 23.97 ? 73  PRO   A CG  1 
ATOM   542  C  CD  . PRO   A 1 67  ? 7.135  -7.128  19.907 1.00 21.89 ? 73  PRO   A CD  1 
ATOM   543  N  N   . VAL   A 1 68  ? 5.956  -4.231  16.453 1.00 21.38 ? 74  VAL   A N   1 
ATOM   544  C  CA  . VAL   A 1 68  ? 4.970  -3.171  16.290 1.00 21.90 ? 74  VAL   A CA  1 
ATOM   545  C  C   . VAL   A 1 68  ? 4.480  -3.085  14.817 1.00 21.28 ? 74  VAL   A C   1 
ATOM   546  O  O   . VAL   A 1 68  ? 5.176  -3.516  13.892 1.00 20.63 ? 74  VAL   A O   1 
ATOM   547  C  CB  . VAL   A 1 68  ? 5.581  -1.804  16.708 1.00 23.80 ? 74  VAL   A CB  1 
ATOM   548  C  CG1 . VAL   A 1 68  ? 5.733  -1.685  18.244 1.00 25.44 ? 74  VAL   A CG1 1 
ATOM   549  C  CG2 . VAL   A 1 68  ? 6.910  -1.541  15.983 1.00 23.35 ? 74  VAL   A CG2 1 
ATOM   550  N  N   . SER   A 1 69  ? 3.318  -2.459  14.630 1.00 20.67 ? 75  SER   A N   1 
ATOM   551  C  CA  . SER   A 1 69  ? 2.785  -2.048  13.328 1.00 21.54 ? 75  SER   A CA  1 
ATOM   552  C  C   . SER   A 1 69  ? 3.033  -0.517  13.367 1.00 21.07 ? 75  SER   A C   1 
ATOM   553  O  O   . SER   A 1 69  ? 2.766  0.116   14.390 1.00 20.96 ? 75  SER   A O   1 
ATOM   554  C  CB  . SER   A 1 69  ? 1.281  -2.275  13.234 1.00 23.28 ? 75  SER   A CB  1 
ATOM   555  O  OG  . SER   A 1 69  ? 0.970  -3.656  13.172 1.00 28.98 ? 75  SER   A OG  1 
ATOM   556  N  N   . PHE   A 1 70  ? 3.515  0.063   12.285 1.00 19.79 ? 76  PHE   A N   1 
ATOM   557  C  CA  . PHE   A 1 70  ? 3.768  1.511   12.266 1.00 19.98 ? 76  PHE   A CA  1 
ATOM   558  C  C   . PHE   A 1 70  ? 3.194  2.165   11.035 1.00 21.54 ? 76  PHE   A C   1 
ATOM   559  O  O   . PHE   A 1 70  ? 2.964  1.514   10.025 1.00 22.39 ? 76  PHE   A O   1 
ATOM   560  C  CB  . PHE   A 1 70  ? 5.256  1.838   12.480 1.00 20.65 ? 76  PHE   A CB  1 
ATOM   561  C  CG  . PHE   A 1 70  ? 6.192  1.113   11.549 1.00 20.53 ? 76  PHE   A CG  1 
ATOM   562  C  CD1 . PHE   A 1 70  ? 6.618  -0.181  11.831 1.00 21.41 ? 76  PHE   A CD1 1 
ATOM   563  C  CD2 . PHE   A 1 70  ? 6.549  1.670   10.329 1.00 21.69 ? 76  PHE   A CD2 1 
ATOM   564  C  CE1 . PHE   A 1 70  ? 7.486  -0.846  10.959 1.00 22.60 ? 76  PHE   A CE1 1 
ATOM   565  C  CE2 . PHE   A 1 70  ? 7.426  1.006   9.466  1.00 22.48 ? 76  PHE   A CE2 1 
ATOM   566  C  CZ  . PHE   A 1 70  ? 7.843  -0.272  9.755  1.00 21.61 ? 76  PHE   A CZ  1 
ATOM   567  N  N   . SER   A 1 71  ? 2.922  3.482   11.130 1.00 22.14 ? 77  SER   A N   1 
ATOM   568  C  CA  . SER   A 1 71  ? 2.336  4.196   10.007 1.00 23.33 ? 77  SER   A CA  1 
ATOM   569  C  C   . SER   A 1 71  ? 3.455  4.540   8.974  1.00 24.69 ? 77  SER   A C   1 
ATOM   570  O  O   . SER   A 1 71  ? 4.636  4.500   9.306  1.00 25.27 ? 77  SER   A O   1 
ATOM   571  C  CB  . SER   A 1 71  ? 1.652  5.467   10.530 1.00 24.20 ? 77  SER   A CB  1 
ATOM   572  O  OG  . SER   A 1 71  ? 2.605  6.363   11.082 1.00 25.70 ? 77  SER   A OG  1 
ATOM   573  N  N   . LYS   A 1 72  ? 3.075  4.884   7.726  1.00 24.70 ? 78  LYS   A N   1 
ATOM   574  C  CA  . LYS   A 1 72  ? 4.016  5.290   6.694  1.00 25.48 ? 78  LYS   A CA  1 
ATOM   575  C  C   . LYS   A 1 72  ? 4.620  6.675   6.996  1.00 25.38 ? 78  LYS   A C   1 
ATOM   576  O  O   . LYS   A 1 72  ? 3.964  7.512   7.599  1.00 25.70 ? 78  LYS   A O   1 
ATOM   577  C  CB  . LYS   A 1 72  ? 3.294  5.296   5.311  1.00 29.00 ? 78  LYS   A CB  1 
ATOM   578  C  CG  . LYS   A 1 72  ? 3.024  3.852   4.825  1.00 34.58 ? 78  LYS   A CG  1 
ATOM   579  C  CD  . LYS   A 1 72  ? 2.553  3.745   3.370  1.00 40.19 ? 78  LYS   A CD  1 
ATOM   580  C  CE  . LYS   A 1 72  ? 2.393  2.278   3.020  1.00 45.22 ? 78  LYS   A CE  1 
ATOM   581  N  NZ  . LYS   A 1 72  ? 1.875  2.056   1.635  1.00 48.22 ? 78  LYS   A NZ  1 
ATOM   582  N  N   . PRO   A 1 73  ? 5.855  6.955   6.545  1.00 25.41 ? 79  PRO   A N   1 
ATOM   583  C  CA  . PRO   A 1 73  ? 6.479  8.271   6.863  1.00 25.63 ? 79  PRO   A CA  1 
ATOM   584  C  C   . PRO   A 1 73  ? 5.615  9.477   6.473  1.00 25.97 ? 79  PRO   A C   1 
ATOM   585  O  O   . PRO   A 1 73  ? 5.149  9.575   5.323  1.00 25.99 ? 79  PRO   A O   1 
ATOM   586  C  CB  . PRO   A 1 73  ? 7.825  8.219   6.137  1.00 27.32 ? 79  PRO   A CB  1 
ATOM   587  C  CG  . PRO   A 1 73  ? 8.105  6.782   5.894  1.00 28.22 ? 79  PRO   A CG  1 
ATOM   588  C  CD  . PRO   A 1 73  ? 6.775  6.064   5.818  1.00 25.62 ? 79  PRO   A CD  1 
ATOM   589  N  N   A SER   A 1 74  ? 5.372  10.381  7.423  0.50 25.83 ? 80  SER   A N   1 
ATOM   590  N  N   B SER   A 1 74  ? 5.362  10.377  7.429  0.50 25.85 ? 80  SER   A N   1 
ATOM   591  C  CA  A SER   A 1 74  ? 4.484  11.533  7.190  0.50 26.67 ? 80  SER   A CA  1 
ATOM   592  C  CA  B SER   A 1 74  ? 4.477  11.533  7.207  0.50 26.70 ? 80  SER   A CA  1 
ATOM   593  C  C   A SER   A 1 74  ? 4.966  12.815  7.901  0.50 27.19 ? 80  SER   A C   1 
ATOM   594  C  C   B SER   A 1 74  ? 4.905  12.795  7.978  0.50 27.29 ? 80  SER   A C   1 
ATOM   595  O  O   A SER   A 1 74  ? 5.931  12.783  8.670  0.50 27.80 ? 80  SER   A O   1 
ATOM   596  O  O   B SER   A 1 74  ? 5.749  12.725  8.880  0.50 27.96 ? 80  SER   A O   1 
ATOM   597  C  CB  A SER   A 1 74  ? 3.061  11.201  7.666  0.50 28.13 ? 80  SER   A CB  1 
ATOM   598  C  CB  B SER   A 1 74  ? 3.041  11.168  7.597  0.50 28.11 ? 80  SER   A CB  1 
ATOM   599  O  OG  A SER   A 1 74  ? 2.665  9.856   7.448  0.50 31.42 ? 80  SER   A OG  1 
ATOM   600  O  OG  B SER   A 1 74  ? 2.538  10.084  6.835  0.50 31.29 ? 80  SER   A OG  1 
ATOM   601  N  N   . LEU   A 1 75  ? 4.278  13.939  7.658  1.00 26.95 ? 81  LEU   A N   1 
ATOM   602  C  CA  . LEU   A 1 75  ? 4.546  15.221  8.308  1.00 27.86 ? 81  LEU   A CA  1 
ATOM   603  C  C   . LEU   A 1 75  ? 3.557  15.231  9.498  1.00 29.43 ? 81  LEU   A C   1 
ATOM   604  O  O   . LEU   A 1 75  ? 2.344  15.146  9.285  1.00 30.47 ? 81  LEU   A O   1 
ATOM   605  C  CB  . LEU   A 1 75  ? 4.201  16.325  7.300  1.00 27.71 ? 81  LEU   A CB  1 
ATOM   606  C  CG  . LEU   A 1 75  ? 4.633  17.763  7.642  1.00 29.83 ? 81  LEU   A CG  1 
ATOM   607  C  CD1 . LEU   A 1 75  ? 6.114  17.862  7.920  1.00 29.87 ? 81  LEU   A CD1 1 
ATOM   608  C  CD2 . LEU   A 1 75  ? 4.254  18.719  6.524  1.00 30.75 ? 81  LEU   A CD2 1 
ATOM   609  N  N   . ILE   A 1 76  ? 4.072  15.207  10.740 1.00 28.94 ? 82  ILE   A N   1 
ATOM   610  C  CA  . ILE   A 1 76  ? 3.279  15.055  11.956 1.00 30.35 ? 82  ILE   A CA  1 
ATOM   611  C  C   . ILE   A 1 76  ? 3.618  16.158  12.941 1.00 30.48 ? 82  ILE   A C   1 
ATOM   612  O  O   . ILE   A 1 76  ? 4.798  16.433  13.141 1.00 29.61 ? 82  ILE   A O   1 
ATOM   613  C  CB  . ILE   A 1 76  ? 3.642  13.661  12.590 1.00 31.76 ? 82  ILE   A CB  1 
ATOM   614  C  CG1 . ILE   A 1 76  ? 3.323  12.484  11.628 1.00 34.14 ? 82  ILE   A CG1 1 
ATOM   615  C  CG2 . ILE   A 1 76  ? 3.042  13.442  14.002 1.00 31.87 ? 82  ILE   A CG2 1 
ATOM   616  C  CD1 . ILE   A 1 76  ? 1.916  11.942  11.606 1.00 36.55 ? 82  ILE   A CD1 1 
ATOM   617  N  N   . PHE   A 1 77  ? 2.599  16.734  13.621 1.00 30.35 ? 83  PHE   A N   1 
ATOM   618  C  CA  . PHE   A 1 77  ? 2.853  17.757  14.630 1.00 30.25 ? 83  PHE   A CA  1 
ATOM   619  C  C   . PHE   A 1 77  ? 3.445  17.090  15.880 1.00 29.29 ? 83  PHE   A C   1 
ATOM   620  O  O   . PHE   A 1 77  ? 2.921  16.075  16.359 1.00 29.81 ? 83  PHE   A O   1 
ATOM   621  C  CB  . PHE   A 1 77  ? 1.565  18.519  14.994 1.00 31.26 ? 83  PHE   A CB  1 
ATOM   622  C  CG  . PHE   A 1 77  ? 1.877  19.764  15.786 1.00 33.07 ? 83  PHE   A CG  1 
ATOM   623  C  CD1 . PHE   A 1 77  ? 2.521  20.841  15.190 1.00 34.09 ? 83  PHE   A CD1 1 
ATOM   624  C  CD2 . PHE   A 1 77  ? 1.597  19.831  17.137 1.00 34.56 ? 83  PHE   A CD2 1 
ATOM   625  C  CE1 . PHE   A 1 77  ? 2.849  21.969  15.925 1.00 35.15 ? 83  PHE   A CE1 1 
ATOM   626  C  CE2 . PHE   A 1 77  ? 1.908  20.973  17.867 1.00 35.55 ? 83  PHE   A CE2 1 
ATOM   627  C  CZ  . PHE   A 1 77  ? 2.543  22.024  17.263 1.00 35.27 ? 83  PHE   A CZ  1 
ATOM   628  N  N   . VAL   A 1 78  ? 4.524  17.662  16.404 1.00 27.77 ? 84  VAL   A N   1 
ATOM   629  C  CA  . VAL   A 1 78  ? 5.255  17.121  17.547 1.00 27.90 ? 84  VAL   A CA  1 
ATOM   630  C  C   . VAL   A 1 78  ? 5.377  18.194  18.605 1.00 29.12 ? 84  VAL   A C   1 
ATOM   631  O  O   . VAL   A 1 78  ? 5.889  19.285  18.331 1.00 28.77 ? 84  VAL   A O   1 
ATOM   632  C  CB  . VAL   A 1 78  ? 6.673  16.613  17.119 1.00 27.21 ? 84  VAL   A CB  1 
ATOM   633  C  CG1 . VAL   A 1 78  ? 7.478  16.142  18.332 1.00 27.80 ? 84  VAL   A CG1 1 
ATOM   634  C  CG2 . VAL   A 1 78  ? 6.583  15.514  16.078 1.00 26.04 ? 84  VAL   A CG2 1 
ATOM   635  N  N   . GLU   A 1 79  ? 4.895  17.891  19.807 1.00 29.96 ? 85  GLU   A N   1 
ATOM   636  C  CA  . GLU   A 1 79  ? 4.907  18.822  20.928 1.00 31.03 ? 85  GLU   A CA  1 
ATOM   637  C  C   . GLU   A 1 79  ? 6.310  19.301  21.284 1.00 31.40 ? 85  GLU   A C   1 
ATOM   638  O  O   . GLU   A 1 79  ? 7.295  18.643  20.960 1.00 30.84 ? 85  GLU   A O   1 
ATOM   639  C  CB  . GLU   A 1 79  ? 4.225  18.193  22.160 1.00 33.96 ? 85  GLU   A CB  1 
ATOM   640  C  CG  . GLU   A 1 79  ? 2.743  17.950  21.964 1.00 39.98 ? 85  GLU   A CG  1 
ATOM   641  C  CD  . GLU   A 1 79  ? 1.972  19.238  21.744 1.00 47.77 ? 85  GLU   A CD  1 
ATOM   642  O  OE1 . GLU   A 1 79  ? 2.143  20.177  22.553 1.00 48.10 ? 85  GLU   A OE1 1 
ATOM   643  O  OE2 . GLU   A 1 79  ? 1.213  19.317  20.749 1.00 50.48 ? 85  GLU   A OE2 1 
ATOM   644  N  N   . ALA   A 1 80  ? 6.403  20.450  21.969 1.00 31.54 ? 86  ALA   A N   1 
ATOM   645  C  CA  . ALA   A 1 80  ? 7.702  20.982  22.384 1.00 32.12 ? 86  ALA   A CA  1 
ATOM   646  C  C   . ALA   A 1 80  ? 8.431  19.984  23.311 1.00 32.16 ? 86  ALA   A C   1 
ATOM   647  O  O   . ALA   A 1 80  ? 7.793  19.243  24.066 1.00 31.79 ? 86  ALA   A O   1 
ATOM   648  C  CB  . ALA   A 1 80  ? 7.525  22.323  23.100 1.00 31.82 ? 86  ALA   A CB  1 
ATOM   649  N  N   . SER   A 1 81  ? 9.758  19.948  23.202 1.00 31.79 ? 87  SER   A N   1 
ATOM   650  C  CA  . SER   A 1 81  ? 10.626 19.093  24.002 1.00 31.83 ? 87  SER   A CA  1 
ATOM   651  C  C   . SER   A 1 81  ? 11.860 19.895  24.501 1.00 32.92 ? 87  SER   A C   1 
ATOM   652  O  O   . SER   A 1 81  ? 11.968 21.110  24.254 1.00 33.17 ? 87  SER   A O   1 
ATOM   653  C  CB  . SER   A 1 81  ? 11.075 17.901  23.156 1.00 30.82 ? 87  SER   A CB  1 
ATOM   654  O  OG  . SER   A 1 81  ? 12.009 18.290  22.160 1.00 30.93 ? 87  SER   A OG  1 
ATOM   655  N  N   . GLU   A 1 82  ? 12.801 19.207  25.181 1.00 33.67 ? 88  GLU   A N   1 
ATOM   656  C  CA  . GLU   A 1 82  ? 14.053 19.800  25.640 1.00 34.40 ? 88  GLU   A CA  1 
ATOM   657  C  C   . GLU   A 1 82  ? 14.933 20.264  24.447 1.00 33.88 ? 88  GLU   A C   1 
ATOM   658  O  O   . GLU   A 1 82  ? 15.720 21.188  24.609 1.00 34.27 ? 88  GLU   A O   1 
ATOM   659  C  CB  . GLU   A 1 82  ? 14.849 18.767  26.466 1.00 38.25 ? 88  GLU   A CB  1 
ATOM   660  C  CG  . GLU   A 1 82  ? 16.123 19.337  27.066 1.00 46.32 ? 88  GLU   A CG  1 
ATOM   661  C  CD  . GLU   A 1 82  ? 17.090 18.363  27.707 1.00 54.45 ? 88  GLU   A CD  1 
ATOM   662  O  OE1 . GLU   A 1 82  ? 16.660 17.246  28.082 1.00 54.56 ? 88  GLU   A OE1 1 
ATOM   663  O  OE2 . GLU   A 1 82  ? 18.285 18.725  27.834 1.00 57.22 ? 88  GLU   A OE2 1 
ATOM   664  N  N   . TYR   A 1 83  ? 14.742 19.687  23.242 1.00 33.14 ? 89  TYR   A N   1 
ATOM   665  C  CA  . TYR   A 1 83  ? 15.609 19.959  22.091 1.00 33.47 ? 89  TYR   A CA  1 
ATOM   666  C  C   . TYR   A 1 83  ? 14.986 20.715  20.910 1.00 32.19 ? 89  TYR   A C   1 
ATOM   667  O  O   . TYR   A 1 83  ? 15.731 21.213  20.060 1.00 32.32 ? 89  TYR   A O   1 
ATOM   668  C  CB  . TYR   A 1 83  ? 16.194 18.623  21.583 1.00 34.76 ? 89  TYR   A CB  1 
ATOM   669  C  CG  . TYR   A 1 83  ? 17.065 17.923  22.606 1.00 37.73 ? 89  TYR   A CG  1 
ATOM   670  C  CD1 . TYR   A 1 83  ? 18.408 18.247  22.745 1.00 39.47 ? 89  TYR   A CD1 1 
ATOM   671  C  CD2 . TYR   A 1 83  ? 16.543 16.938  23.434 1.00 40.24 ? 89  TYR   A CD2 1 
ATOM   672  C  CE1 . TYR   A 1 83  ? 19.212 17.609  23.685 1.00 41.18 ? 89  TYR   A CE1 1 
ATOM   673  C  CE2 . TYR   A 1 83  ? 17.344 16.268  24.356 1.00 42.11 ? 89  TYR   A CE2 1 
ATOM   674  C  CZ  . TYR   A 1 83  ? 18.679 16.607  24.480 1.00 43.49 ? 89  TYR   A CZ  1 
ATOM   675  O  OH  . TYR   A 1 83  ? 19.464 15.928  25.393 1.00 46.52 ? 89  TYR   A OH  1 
ATOM   676  N  N   . TYR   A 1 84  ? 13.654 20.728  20.792 1.00 29.94 ? 90  TYR   A N   1 
ATOM   677  C  CA  . TYR   A 1 84  ? 12.995 21.470  19.718 1.00 28.31 ? 90  TYR   A CA  1 
ATOM   678  C  C   . TYR   A 1 84  ? 11.756 22.162  20.278 1.00 29.33 ? 90  TYR   A C   1 
ATOM   679  O  O   . TYR   A 1 84  ? 11.081 21.611  21.156 1.00 29.29 ? 90  TYR   A O   1 
ATOM   680  C  CB  . TYR   A 1 84  ? 12.532 20.541  18.569 1.00 26.69 ? 90  TYR   A CB  1 
ATOM   681  C  CG  . TYR   A 1 84  ? 13.606 19.759  17.859 1.00 25.22 ? 90  TYR   A CG  1 
ATOM   682  C  CD1 . TYR   A 1 84  ? 14.360 20.332  16.838 1.00 24.94 ? 90  TYR   A CD1 1 
ATOM   683  C  CD2 . TYR   A 1 84  ? 13.844 18.425  18.173 1.00 25.40 ? 90  TYR   A CD2 1 
ATOM   684  C  CE1 . TYR   A 1 84  ? 15.357 19.613  16.189 1.00 24.25 ? 90  TYR   A CE1 1 
ATOM   685  C  CE2 . TYR   A 1 84  ? 14.839 17.704  17.542 1.00 24.98 ? 90  TYR   A CE2 1 
ATOM   686  C  CZ  . TYR   A 1 84  ? 15.575 18.286  16.528 1.00 24.62 ? 90  TYR   A CZ  1 
ATOM   687  O  OH  . TYR   A 1 84  ? 16.558 17.539  15.914 1.00 23.70 ? 90  TYR   A OH  1 
ATOM   688  N  N   . PRO   A 1 85  ? 11.380 23.335  19.729 1.00 30.33 ? 91  PRO   A N   1 
ATOM   689  C  CA  . PRO   A 1 85  ? 10.058 23.906  20.080 1.00 30.60 ? 91  PRO   A CA  1 
ATOM   690  C  C   . PRO   A 1 85  ? 8.952  23.074  19.374 1.00 29.93 ? 91  PRO   A C   1 
ATOM   691  O  O   . PRO   A 1 85  ? 9.274  22.152  18.578 1.00 30.12 ? 91  PRO   A O   1 
ATOM   692  C  CB  . PRO   A 1 85  ? 10.125 25.328  19.482 1.00 31.40 ? 91  PRO   A CB  1 
ATOM   693  C  CG  . PRO   A 1 85  ? 10.992 25.176  18.290 1.00 31.69 ? 91  PRO   A CG  1 
ATOM   694  C  CD  . PRO   A 1 85  ? 12.013 24.077  18.619 1.00 30.26 ? 91  PRO   A CD  1 
ATOM   695  N  N   . ALA   A 1 86  ? 7.662  23.371  19.628 1.00 29.00 ? 92  ALA   A N   1 
ATOM   696  C  CA  . ALA   A 1 86  ? 6.573  22.634  18.957 1.00 29.91 ? 92  ALA   A CA  1 
ATOM   697  C  C   . ALA   A 1 86  ? 6.651  22.875  17.460 1.00 29.42 ? 92  ALA   A C   1 
ATOM   698  O  O   . ALA   A 1 86  ? 6.873  24.004  17.054 1.00 29.78 ? 92  ALA   A O   1 
ATOM   699  C  CB  . ALA   A 1 86  ? 5.211  23.071  19.491 1.00 31.06 ? 92  ALA   A CB  1 
ATOM   700  N  N   . ARG   A 1 87  ? 6.633  21.814  16.653 1.00 29.05 ? 93  ARG   A N   1 
ATOM   701  C  CA  . ARG   A 1 87  ? 6.772  21.965  15.197 1.00 28.93 ? 93  ARG   A CA  1 
ATOM   702  C  C   . ARG   A 1 87  ? 6.257  20.720  14.467 1.00 30.02 ? 93  ARG   A C   1 
ATOM   703  O  O   . ARG   A 1 87  ? 6.013  19.697  15.097 1.00 32.03 ? 93  ARG   A O   1 
ATOM   704  C  CB  . ARG   A 1 87  ? 8.276  22.215  14.841 1.00 28.37 ? 93  ARG   A CB  1 
ATOM   705  C  CG  . ARG   A 1 87  ? 9.143  20.932  14.662 1.00 26.82 ? 93  ARG   A CG  1 
ATOM   706  C  CD  . ARG   A 1 87  ? 10.560 21.003  15.223 1.00 27.01 ? 93  ARG   A CD  1 
ATOM   707  N  NE  . ARG   A 1 87  ? 11.449 19.927  14.740 1.00 27.36 ? 93  ARG   A NE  1 
ATOM   708  C  CZ  . ARG   A 1 87  ? 11.382 18.659  15.142 1.00 28.54 ? 93  ARG   A CZ  1 
ATOM   709  N  NH1 . ARG   A 1 87  ? 10.440 18.277  16.006 1.00 25.00 ? 93  ARG   A NH1 1 
ATOM   710  N  NH2 . ARG   A 1 87  ? 12.250 17.756  14.675 1.00 27.30 ? 93  ARG   A NH2 1 
ATOM   711  N  N   . TYR   A 1 88  ? 6.173  20.787  13.138 1.00 28.79 ? 94  TYR   A N   1 
ATOM   712  C  CA  . TYR   A 1 88  ? 5.910  19.646  12.306 1.00 28.41 ? 94  TYR   A CA  1 
ATOM   713  C  C   . TYR   A 1 88  ? 7.226  18.905  12.014 1.00 26.98 ? 94  TYR   A C   1 
ATOM   714  O  O   . TYR   A 1 88  ? 8.203  19.511  11.536 1.00 27.69 ? 94  TYR   A O   1 
ATOM   715  C  CB  . TYR   A 1 88  ? 5.283  20.083  10.990 1.00 28.87 ? 94  TYR   A CB  1 
ATOM   716  C  CG  . TYR   A 1 88  ? 3.827  20.413  11.167 1.00 29.67 ? 94  TYR   A CG  1 
ATOM   717  C  CD1 . TYR   A 1 88  ? 2.875  19.408  11.236 1.00 30.63 ? 94  TYR   A CD1 1 
ATOM   718  C  CD2 . TYR   A 1 88  ? 3.411  21.726  11.361 1.00 31.21 ? 94  TYR   A CD2 1 
ATOM   719  C  CE1 . TYR   A 1 88  ? 1.534  19.698  11.444 1.00 32.66 ? 94  TYR   A CE1 1 
ATOM   720  C  CE2 . TYR   A 1 88  ? 2.067  22.037  11.544 1.00 32.44 ? 94  TYR   A CE2 1 
ATOM   721  C  CZ  . TYR   A 1 88  ? 1.132  21.014  11.599 1.00 33.29 ? 94  TYR   A CZ  1 
ATOM   722  O  OH  . TYR   A 1 88  ? -0.189 21.302  11.776 1.00 35.17 ? 94  TYR   A OH  1 
ATOM   723  N  N   . GLN   A 1 89  ? 7.255  17.594  12.307 1.00 24.86 ? 95  GLN   A N   1 
ATOM   724  C  CA  . GLN   A 1 89  ? 8.429  16.773  12.006 1.00 24.81 ? 95  GLN   A CA  1 
ATOM   725  C  C   . GLN   A 1 89  ? 8.059  15.952  10.773 1.00 24.20 ? 95  GLN   A C   1 
ATOM   726  O  O   . GLN   A 1 89  ? 6.984  15.336  10.757 1.00 24.43 ? 95  GLN   A O   1 
ATOM   727  C  CB  . GLN   A 1 89  ? 8.835  15.842  13.188 1.00 24.74 ? 95  GLN   A CB  1 
ATOM   728  C  CG  . GLN   A 1 89  ? 10.071 14.974  12.863 1.00 26.34 ? 95  GLN   A CG  1 
ATOM   729  C  CD  . GLN   A 1 89  ? 10.804 14.388  14.066 1.00 26.49 ? 95  GLN   A CD  1 
ATOM   730  O  OE1 . GLN   A 1 89  ? 10.989 15.047  15.094 1.00 27.49 ? 95  GLN   A OE1 1 
ATOM   731  N  NE2 . GLN   A 1 89  ? 11.259 13.119  13.950 1.00 25.29 ? 95  GLN   A NE2 1 
ATOM   732  N  N   . SER   A 1 90  ? 8.936  15.958  9.749  1.00 23.25 ? 96  SER   A N   1 
ATOM   733  C  CA  . SER   A 1 90  ? 8.699  15.235  8.495  1.00 23.45 ? 96  SER   A CA  1 
ATOM   734  C  C   . SER   A 1 90  ? 9.326  13.816  8.481  1.00 22.24 ? 96  SER   A C   1 
ATOM   735  O  O   . SER   A 1 90  ? 10.183 13.494  9.339  1.00 21.98 ? 96  SER   A O   1 
ATOM   736  C  CB  . SER   A 1 90  ? 9.181  16.052  7.304  1.00 24.43 ? 96  SER   A CB  1 
ATOM   737  O  OG  . SER   A 1 90  ? 10.601 16.108  7.312  1.00 25.62 ? 96  SER   A OG  1 
ATOM   738  N  N   . HIS   A 1 91  ? 8.851  12.963  7.557  1.00 20.30 ? 97  HIS   A N   1 
ATOM   739  C  CA  . HIS   A 1 91  ? 9.355  11.567  7.415  1.00 20.76 ? 97  HIS   A CA  1 
ATOM   740  C  C   . HIS   A 1 91  ? 9.241  10.759  8.750  1.00 22.06 ? 97  HIS   A C   1 
ATOM   741  O  O   . HIS   A 1 91  ? 10.114 9.955   9.053  1.00 22.44 ? 97  HIS   A O   1 
ATOM   742  C  CB  . HIS   A 1 91  ? 10.819 11.551  6.872  1.00 20.98 ? 97  HIS   A CB  1 
ATOM   743  C  CG  . HIS   A 1 91  ? 10.965 12.230  5.533  1.00 24.30 ? 97  HIS   A CG  1 
ATOM   744  N  ND1 . HIS   A 1 91  ? 10.866 11.516  4.357  1.00 27.08 ? 97  HIS   A ND1 1 
ATOM   745  C  CD2 . HIS   A 1 91  ? 11.053 13.550  5.233  1.00 24.60 ? 97  HIS   A CD2 1 
ATOM   746  C  CE1 . HIS   A 1 91  ? 10.972 12.402  3.381  1.00 27.54 ? 97  HIS   A CE1 1 
ATOM   747  N  NE2 . HIS   A 1 91  ? 11.046 13.645  3.856  1.00 26.34 ? 97  HIS   A NE2 1 
ATOM   748  N  N   . LEU   A 1 92  ? 8.152  10.987  9.539  1.00 22.01 ? 98  LEU   A N   1 
ATOM   749  C  CA  . LEU   A 1 92  ? 7.963  10.351  10.860 1.00 22.95 ? 98  LEU   A CA  1 
ATOM   750  C  C   . LEU   A 1 92  ? 6.874  9.248   10.784 1.00 23.65 ? 98  LEU   A C   1 
ATOM   751  O  O   . LEU   A 1 92  ? 5.862  9.406   10.073 1.00 24.39 ? 98  LEU   A O   1 
ATOM   752  C  CB  . LEU   A 1 92  ? 7.544  11.412  11.881 1.00 23.09 ? 98  LEU   A CB  1 
ATOM   753  C  CG  . LEU   A 1 92  ? 7.425  11.019  13.362 1.00 24.08 ? 98  LEU   A CG  1 
ATOM   754  C  CD1 . LEU   A 1 92  ? 8.789  10.682  13.940 1.00 22.80 ? 98  LEU   A CD1 1 
ATOM   755  C  CD2 . LEU   A 1 92  ? 6.774  12.174  14.185 1.00 25.74 ? 98  LEU   A CD2 1 
ATOM   756  N  N   . MET   A 1 93  ? 7.114  8.137   11.476 1.00 22.36 ? 99  MET   A N   1 
ATOM   757  C  CA  . MET   A 1 93  ? 6.202  6.991   11.513 1.00 20.71 ? 99  MET   A CA  1 
ATOM   758  C  C   . MET   A 1 93  ? 5.822  6.760   12.971 1.00 21.87 ? 99  MET   A C   1 
ATOM   759  O  O   . MET   A 1 93  ? 6.715  6.830   13.828 1.00 22.04 ? 99  MET   A O   1 
ATOM   760  C  CB  . MET   A 1 93  ? 6.956  5.756   10.987 1.00 20.88 ? 99  MET   A CB  1 
ATOM   761  C  CG  . MET   A 1 93  ? 7.462  5.938   9.515  1.00 22.57 ? 99  MET   A CG  1 
ATOM   762  S  SD  . MET   A 1 93  ? 8.579  4.617   9.008  1.00 25.83 ? 99  MET   A SD  1 
ATOM   763  C  CE  . MET   A 1 93  ? 9.863  4.762   10.215 1.00 23.38 ? 99  MET   A CE  1 
ATOM   764  N  N   . LEU   A 1 94  ? 4.526  6.475   13.269 1.00 20.98 ? 100 LEU   A N   1 
ATOM   765  C  CA  . LEU   A 1 94  ? 4.139  6.250   14.656 1.00 20.56 ? 100 LEU   A CA  1 
ATOM   766  C  C   . LEU   A 1 94  ? 3.701  4.797   14.842 1.00 20.96 ? 100 LEU   A C   1 
ATOM   767  O  O   . LEU   A 1 94  ? 3.137  4.175   13.935 1.00 21.23 ? 100 LEU   A O   1 
ATOM   768  C  CB  . LEU   A 1 94  ? 2.938  7.142   15.062 1.00 21.69 ? 100 LEU   A CB  1 
ATOM   769  C  CG  . LEU   A 1 94  ? 3.123  8.648   14.974 1.00 24.61 ? 100 LEU   A CG  1 
ATOM   770  C  CD1 . LEU   A 1 94  ? 1.818  9.401   15.415 1.00 24.76 ? 100 LEU   A CD1 1 
ATOM   771  C  CD2 . LEU   A 1 94  ? 4.304  9.098   15.825 1.00 26.17 ? 100 LEU   A CD2 1 
ATOM   772  N  N   . ALA   A 1 95  ? 3.916  4.307   16.032 1.00 20.47 ? 101 ALA   A N   1 
ATOM   773  C  CA  . ALA   A 1 95  ? 3.422  3.004   16.500 1.00 21.23 ? 101 ALA   A CA  1 
ATOM   774  C  C   . ALA   A 1 95  ? 2.875  3.172   17.921 1.00 21.92 ? 101 ALA   A C   1 
ATOM   775  O  O   . ALA   A 1 95  ? 3.177  4.169   18.598 1.00 22.97 ? 101 ALA   A O   1 
ATOM   776  C  CB  . ALA   A 1 95  ? 4.547  1.960   16.491 1.00 20.11 ? 101 ALA   A CB  1 
ATOM   777  N  N   . VAL   A 1 96  ? 2.031  2.218   18.350 1.00 20.60 ? 102 VAL   A N   1 
ATOM   778  C  CA  . VAL   A 1 96  ? 1.584  2.209   19.706 1.00 21.93 ? 102 VAL   A CA  1 
ATOM   779  C  C   . VAL   A 1 96  ? 2.673  1.469   20.438 1.00 23.14 ? 102 VAL   A C   1 
ATOM   780  O  O   . VAL   A 1 96  ? 2.967  0.288   20.132 1.00 23.71 ? 102 VAL   A O   1 
ATOM   781  C  CB  . VAL   A 1 96  ? 0.204  1.519   19.865 1.00 22.60 ? 102 VAL   A CB  1 
ATOM   782  C  CG1 . VAL   A 1 96  ? -0.191 1.440   21.337 1.00 23.91 ? 102 VAL   A CG1 1 
ATOM   783  C  CG2 . VAL   A 1 96  ? -0.860 2.269   19.058 1.00 23.11 ? 102 VAL   A CG2 1 
ATOM   784  N  N   . GLY   A 1 97  ? 3.241  2.124   21.423 1.00 24.03 ? 103 GLY   A N   1 
ATOM   785  C  CA  . GLY   A 1 97  ? 4.278  1.508   22.229 1.00 24.93 ? 103 GLY   A CA  1 
ATOM   786  C  C   . GLY   A 1 97  ? 4.963  2.450   23.183 1.00 24.83 ? 103 GLY   A C   1 
ATOM   787  O  O   . GLY   A 1 97  ? 4.734  3.666   23.136 1.00 25.54 ? 103 GLY   A O   1 
ATOM   788  N  N   . HIS   A 1 98  ? 5.831  1.895   24.051 1.00 24.41 ? 104 HIS   A N   1 
ATOM   789  C  CA  . HIS   A 1 98  ? 6.511  2.739   25.029 1.00 25.43 ? 104 HIS   A CA  1 
ATOM   790  C  C   . HIS   A 1 98  ? 7.762  3.461   24.499 1.00 25.34 ? 104 HIS   A C   1 
ATOM   791  O  O   . HIS   A 1 98  ? 8.561  2.913   23.752 1.00 24.84 ? 104 HIS   A O   1 
ATOM   792  C  CB  . HIS   A 1 98  ? 6.841  1.971   26.315 1.00 25.71 ? 104 HIS   A CB  1 
ATOM   793  C  CG  . HIS   A 1 98  ? 7.430  2.825   27.394 1.00 28.83 ? 104 HIS   A CG  1 
ATOM   794  N  ND1 . HIS   A 1 98  ? 6.670  3.784   28.067 1.00 31.41 ? 104 HIS   A ND1 1 
ATOM   795  C  CD2 . HIS   A 1 98  ? 8.682  2.831   27.906 1.00 30.34 ? 104 HIS   A CD2 1 
ATOM   796  C  CE1 . HIS   A 1 98  ? 7.493  4.346   28.946 1.00 31.10 ? 104 HIS   A CE1 1 
ATOM   797  N  NE2 . HIS   A 1 98  ? 8.716  3.810   28.882 1.00 30.36 ? 104 HIS   A NE2 1 
ATOM   798  N  N   . SER   A 1 99  ? 7.917  4.705   24.886 1.00 25.78 ? 105 SER   A N   1 
ATOM   799  C  CA  . SER   A 1 99  ? 9.101  5.497   24.578 1.00 27.55 ? 105 SER   A CA  1 
ATOM   800  C  C   . SER   A 1 99  ? 9.268  6.612   25.581 1.00 27.90 ? 105 SER   A C   1 
ATOM   801  O  O   . SER   A 1 99  ? 8.280  7.149   26.081 1.00 29.39 ? 105 SER   A O   1 
ATOM   802  C  CB  . SER   A 1 99  ? 9.073  6.085   23.175 1.00 30.29 ? 105 SER   A CB  1 
ATOM   803  O  OG  . SER   A 1 99  ? 7.893  6.838   23.000 1.00 33.90 ? 105 SER   A OG  1 
ATOM   804  N  N   . GLU   A 1 100 ? 10.514 6.913   25.907 1.00 26.34 ? 106 GLU   A N   1 
ATOM   805  C  CA  . GLU   A 1 100 ? 10.936 8.010   26.776 1.00 26.73 ? 106 GLU   A CA  1 
ATOM   806  C  C   . GLU   A 1 100 ? 12.078 8.738   26.039 1.00 26.80 ? 106 GLU   A C   1 
ATOM   807  O  O   . GLU   A 1 100 ? 12.685 8.150   25.143 1.00 26.50 ? 106 GLU   A O   1 
ATOM   808  C  CB  . GLU   A 1 100 ? 11.367 7.460   28.169 1.00 28.18 ? 106 GLU   A CB  1 
ATOM   809  C  CG  . GLU   A 1 100 ? 10.237 6.739   28.878 1.00 29.56 ? 106 GLU   A CG  1 
ATOM   810  C  CD  . GLU   A 1 100 ? 10.576 6.185   30.262 1.00 36.40 ? 106 GLU   A CD  1 
ATOM   811  O  OE1 . GLU   A 1 100 ? 11.330 6.856   31.001 1.00 36.24 ? 106 GLU   A OE1 1 
ATOM   812  O  OE2 . GLU   A 1 100 ? 10.085 5.087   30.614 1.00 36.75 ? 106 GLU   A OE2 1 
ATOM   813  N  N   . PRO   A 1 101 ? 12.339 10.039  26.304 1.00 27.05 ? 107 PRO   A N   1 
ATOM   814  C  CA  . PRO   A 1 101 ? 13.375 10.754  25.525 1.00 26.77 ? 107 PRO   A CA  1 
ATOM   815  C  C   . PRO   A 1 101 ? 14.717 10.013  25.306 1.00 26.17 ? 107 PRO   A C   1 
ATOM   816  O  O   . PRO   A 1 101 ? 15.249 9.996   24.169 1.00 26.03 ? 107 PRO   A O   1 
ATOM   817  C  CB  . PRO   A 1 101 ? 13.554 12.073  26.286 1.00 27.69 ? 107 PRO   A CB  1 
ATOM   818  C  CG  . PRO   A 1 101 ? 12.193 12.312  26.938 1.00 27.69 ? 107 PRO   A CG  1 
ATOM   819  C  CD  . PRO   A 1 101 ? 11.669 10.922  27.286 1.00 26.83 ? 107 PRO   A CD  1 
ATOM   820  N  N   . GLY   A 1 102 ? 15.261 9.411   26.378 1.00 25.01 ? 108 GLY   A N   1 
ATOM   821  C  CA  . GLY   A 1 102 ? 16.508 8.652   26.309 1.00 25.27 ? 108 GLY   A CA  1 
ATOM   822  C  C   . GLY   A 1 102 ? 16.454 7.417   25.419 1.00 25.50 ? 108 GLY   A C   1 
ATOM   823  O  O   . GLY   A 1 102 ? 17.483 6.800   25.156 1.00 26.36 ? 108 GLY   A O   1 
ATOM   824  N  N   . ASP   A 1 103 ? 15.248 7.014   24.967 1.00 24.62 ? 109 ASP   A N   1 
ATOM   825  C  CA  . ASP   A 1 103 ? 15.061 5.913   24.027 1.00 24.21 ? 109 ASP   A CA  1 
ATOM   826  C  C   . ASP   A 1 103 ? 15.369 6.322   22.586 1.00 22.88 ? 109 ASP   A C   1 
ATOM   827  O  O   . ASP   A 1 103 ? 15.517 5.434   21.731 1.00 22.77 ? 109 ASP   A O   1 
ATOM   828  C  CB  . ASP   A 1 103 ? 13.633 5.347   24.066 1.00 24.74 ? 109 ASP   A CB  1 
ATOM   829  C  CG  . ASP   A 1 103 ? 13.332 4.579   25.340 1.00 25.99 ? 109 ASP   A CG  1 
ATOM   830  O  OD1 . ASP   A 1 103 ? 14.233 3.904   25.839 1.00 25.56 ? 109 ASP   A OD1 1 
ATOM   831  O  OD2 . ASP   A 1 103 ? 12.171 4.636   25.809 1.00 26.01 ? 109 ASP   A OD2 1 
ATOM   832  N  N   . CYS   A 1 104 ? 15.549 7.645   22.290 1.00 21.42 ? 110 CYS   A N   1 
ATOM   833  C  CA  . CYS   A 1 104 ? 15.896 8.060   20.925 1.00 20.07 ? 110 CYS   A CA  1 
ATOM   834  C  C   . CYS   A 1 104 ? 17.168 7.367   20.485 1.00 19.98 ? 110 CYS   A C   1 
ATOM   835  O  O   . CYS   A 1 104 ? 18.049 7.156   21.312 1.00 20.13 ? 110 CYS   A O   1 
ATOM   836  C  CB  . CYS   A 1 104 ? 16.043 9.578   20.856 1.00 21.20 ? 110 CYS   A CB  1 
ATOM   837  S  SG  . CYS   A 1 104 ? 14.473 10.428  21.055 1.00 24.79 ? 110 CYS   A SG  1 
ATOM   838  N  N   . GLY   A 1 105 ? 17.218 6.950   19.235 1.00 18.73 ? 111 GLY   A N   1 
ATOM   839  C  CA  . GLY   A 1 105 ? 18.373 6.222   18.741 1.00 20.15 ? 111 GLY   A CA  1 
ATOM   840  C  C   . GLY   A 1 105 ? 18.119 4.725   18.686 1.00 21.00 ? 111 GLY   A C   1 
ATOM   841  O  O   . GLY   A 1 105 ? 18.854 4.006   17.987 1.00 22.57 ? 111 GLY   A O   1 
ATOM   842  N  N   . GLY   A 1 106 ? 17.075 4.239   19.392 1.00 19.84 ? 112 GLY   A N   1 
ATOM   843  C  CA  . GLY   A 1 106 ? 16.732 2.820   19.354 1.00 18.66 ? 112 GLY   A CA  1 
ATOM   844  C  C   . GLY   A 1 106 ? 16.315 2.427   17.937 1.00 20.15 ? 112 GLY   A C   1 
ATOM   845  O  O   . GLY   A 1 106 ? 15.564 3.164   17.314 1.00 19.74 ? 112 GLY   A O   1 
ATOM   846  N  N   . ILE   A 1 107 ? 16.838 1.294   17.395 1.00 19.88 ? 113 ILE   A N   1 
ATOM   847  C  CA  . ILE   A 1 107 ? 16.545 0.966   15.995 1.00 20.75 ? 113 ILE   A CA  1 
ATOM   848  C  C   . ILE   A 1 107 ? 15.196 0.282   15.827 1.00 21.27 ? 113 ILE   A C   1 
ATOM   849  O  O   . ILE   A 1 107 ? 14.812 -0.525  16.664 1.00 20.84 ? 113 ILE   A O   1 
ATOM   850  C  CB  . ILE   A 1 107 ? 17.738 0.133   15.392 1.00 22.72 ? 113 ILE   A CB  1 
ATOM   851  C  CG1 . ILE   A 1 107 ? 18.925 1.097   15.046 1.00 24.40 ? 113 ILE   A CG1 1 
ATOM   852  C  CG2 . ILE   A 1 107 ? 17.321 -0.666  14.129 1.00 24.00 ? 113 ILE   A CG2 1 
ATOM   853  C  CD1 . ILE   A 1 107 ? 20.311 0.430   14.756 1.00 25.88 ? 113 ILE   A CD1 1 
ATOM   854  N  N   . LEU   A 1 108 ? 14.533 0.564   14.688 1.00 21.31 ? 114 LEU   A N   1 
ATOM   855  C  CA  . LEU   A 1 108 ? 13.334 -0.109  14.229 1.00 21.30 ? 114 LEU   A CA  1 
ATOM   856  C  C   . LEU   A 1 108 ? 13.803 -0.891  12.998 1.00 21.69 ? 114 LEU   A C   1 
ATOM   857  O  O   . LEU   A 1 108 ? 14.344 -0.303  12.094 1.00 21.15 ? 114 LEU   A O   1 
ATOM   858  C  CB  . LEU   A 1 108 ? 12.261 0.899   13.788 1.00 21.82 ? 114 LEU   A CB  1 
ATOM   859  C  CG  . LEU   A 1 108 ? 11.081 0.306   12.996 1.00 23.47 ? 114 LEU   A CG  1 
ATOM   860  C  CD1 . LEU   A 1 108 ? 10.199 -0.583  13.915 1.00 23.23 ? 114 LEU   A CD1 1 
ATOM   861  C  CD2 . LEU   A 1 108 ? 10.219 1.451   12.405 1.00 24.74 ? 114 LEU   A CD2 1 
ATOM   862  N  N   . ARG   A 1 109 ? 13.551 -2.203  12.966 1.00 22.45 ? 115 ARG   A N   1 
ATOM   863  C  CA  . ARG   A 1 109 ? 13.983 -3.031  11.844 1.00 24.38 ? 115 ARG   A CA  1 
ATOM   864  C  C   . ARG   A 1 109 ? 12.892 -3.945  11.328 1.00 23.78 ? 115 ARG   A C   1 
ATOM   865  O  O   . ARG   A 1 109 ? 12.064 -4.376  12.102 1.00 22.57 ? 115 ARG   A O   1 
ATOM   866  C  CB  . ARG   A 1 109 ? 15.228 -3.856  12.203 1.00 28.33 ? 115 ARG   A CB  1 
ATOM   867  C  CG  . ARG   A 1 109 ? 15.247 -4.389  13.617 1.00 36.99 ? 115 ARG   A CG  1 
ATOM   868  C  CD  . ARG   A 1 109 ? 16.440 -5.303  13.777 1.00 45.38 ? 115 ARG   A CD  1 
ATOM   869  N  NE  . ARG   A 1 109 ? 17.207 -5.034  15.000 1.00 51.36 ? 115 ARG   A NE  1 
ATOM   870  C  CZ  . ARG   A 1 109 ? 17.146 -5.786  16.098 1.00 54.80 ? 115 ARG   A CZ  1 
ATOM   871  N  NH1 . ARG   A 1 109 ? 16.269 -6.782  16.183 1.00 54.54 ? 115 ARG   A NH1 1 
ATOM   872  N  NH2 . ARG   A 1 109 ? 17.900 -5.494  17.152 1.00 54.81 ? 115 ARG   A NH2 1 
ATOM   873  N  N   . CYS   A 1 110 ? 12.867 -4.187  10.002 1.00 24.04 ? 116 CYS   A N   1 
ATOM   874  C  CA  . CYS   A 1 110 ? 11.907 -5.143  9.458  1.00 25.48 ? 116 CYS   A CA  1 
ATOM   875  C  C   . CYS   A 1 110 ? 12.772 -6.322  8.831  1.00 26.25 ? 116 CYS   A C   1 
ATOM   876  O  O   . CYS   A 1 110 ? 14.006 -6.290  8.907  1.00 26.32 ? 116 CYS   A O   1 
ATOM   877  C  CB  . CYS   A 1 110 ? 11.072 -4.451  8.392  1.00 25.44 ? 116 CYS   A CB  1 
ATOM   878  S  SG  . CYS   A 1 110 ? 12.043 -4.005  6.947  1.00 21.23 ? 116 CYS   A SG  1 
ATOM   879  N  N   . GLN   A 1 111 ? 12.151 -7.224  8.075  1.00 28.51 ? 117 GLN   A N   1 
ATOM   880  C  CA  . GLN   A 1 111 ? 12.879 -8.318  7.402  1.00 29.85 ? 117 GLN   A CA  1 
ATOM   881  C  C   . GLN   A 1 111 ? 13.921 -7.824  6.398  1.00 31.14 ? 117 GLN   A C   1 
ATOM   882  O  O   . GLN   A 1 111 ? 14.818 -8.585  6.034  1.00 32.59 ? 117 GLN   A O   1 
ATOM   883  C  CB  . GLN   A 1 111 ? 11.887 -9.261  6.705  1.00 31.88 ? 117 GLN   A CB  1 
ATOM   884  C  CG  . GLN   A 1 111 ? 11.096 -8.599  5.575  1.00 34.94 ? 117 GLN   A CG  1 
ATOM   885  C  CD  . GLN   A 1 111 ? 10.121 -9.551  4.920  1.00 39.91 ? 117 GLN   A CD  1 
ATOM   886  O  OE1 . GLN   A 1 111 ? 8.905  -9.498  5.155  1.00 40.84 ? 117 GLN   A OE1 1 
ATOM   887  N  NE2 . GLN   A 1 111 ? 10.638 -10.454 4.093  1.00 39.75 ? 117 GLN   A NE2 1 
ATOM   888  N  N   . HIS   A 1 112 ? 13.828 -6.550  5.942  1.00 30.23 ? 118 HIS   A N   1 
ATOM   889  C  CA  . HIS   A 1 112 ? 14.754 -6.025  4.944  1.00 30.49 ? 118 HIS   A CA  1 
ATOM   890  C  C   . HIS   A 1 112 ? 15.935 -5.233  5.501  1.00 30.67 ? 118 HIS   A C   1 
ATOM   891  O  O   . HIS   A 1 112 ? 16.831 -4.860  4.750  1.00 32.13 ? 118 HIS   A O   1 
ATOM   892  C  CB  . HIS   A 1 112 ? 14.000 -5.178  3.902  1.00 31.08 ? 118 HIS   A CB  1 
ATOM   893  C  CG  . HIS   A 1 112 ? 12.879 -5.917  3.221  1.00 33.12 ? 118 HIS   A CG  1 
ATOM   894  N  ND1 . HIS   A 1 112 ? 11.564 -5.745  3.607  1.00 35.24 ? 118 HIS   A ND1 1 
ATOM   895  C  CD2 . HIS   A 1 112 ? 12.913 -6.772  2.172  1.00 34.01 ? 118 HIS   A CD2 1 
ATOM   896  C  CE1 . HIS   A 1 112 ? 10.843 -6.499  2.794  1.00 35.29 ? 118 HIS   A CE1 1 
ATOM   897  N  NE2 . HIS   A 1 112 ? 11.617 -7.152  1.927  1.00 35.32 ? 118 HIS   A NE2 1 
ATOM   898  N  N   . GLY   A 1 113 ? 15.923 -4.944  6.794  1.00 28.41 ? 119 GLY   A N   1 
ATOM   899  C  CA  . GLY   A 1 113 ? 16.999 -4.196  7.410  1.00 26.99 ? 119 GLY   A CA  1 
ATOM   900  C  C   . GLY   A 1 113 ? 16.474 -3.089  8.294  1.00 25.69 ? 119 GLY   A C   1 
ATOM   901  O  O   . GLY   A 1 113 ? 15.367 -3.188  8.827  1.00 24.12 ? 119 GLY   A O   1 
ATOM   902  N  N   . VAL   A 1 114 ? 17.308 -2.069  8.498  1.00 25.03 ? 120 VAL   A N   1 
ATOM   903  C  CA  . VAL   A 1 114 ? 16.978 -0.921  9.330  1.00 24.64 ? 120 VAL   A CA  1 
ATOM   904  C  C   . VAL   A 1 114 ? 16.001 -0.031  8.632  1.00 23.20 ? 120 VAL   A C   1 
ATOM   905  O  O   . VAL   A 1 114 ? 16.232 0.371   7.489  1.00 23.63 ? 120 VAL   A O   1 
ATOM   906  C  CB  . VAL   A 1 114 ? 18.237 -0.127  9.742  1.00 25.62 ? 120 VAL   A CB  1 
ATOM   907  C  CG1 . VAL   A 1 114 ? 17.844 1.100   10.578 1.00 25.96 ? 120 VAL   A CG1 1 
ATOM   908  C  CG2 . VAL   A 1 114 ? 19.192 -1.037  10.520 1.00 26.50 ? 120 VAL   A CG2 1 
ATOM   909  N  N   . VAL   A 1 115 ? 14.915 0.301   9.324  1.00 21.79 ? 121 VAL   A N   1 
ATOM   910  C  CA  . VAL   A 1 115 ? 13.863 1.171   8.794  1.00 20.71 ? 121 VAL   A CA  1 
ATOM   911  C  C   . VAL   A 1 115 ? 14.040 2.619   9.291  1.00 20.42 ? 121 VAL   A C   1 
ATOM   912  O  O   . VAL   A 1 115 ? 13.797 3.571   8.561  1.00 20.77 ? 121 VAL   A O   1 
ATOM   913  C  CB  . VAL   A 1 115 ? 12.506 0.602   9.285  1.00 21.01 ? 121 VAL   A CB  1 
ATOM   914  C  CG1 . VAL   A 1 115 ? 11.339 1.532   8.973  1.00 20.86 ? 121 VAL   A CG1 1 
ATOM   915  C  CG2 . VAL   A 1 115 ? 12.276 -0.805  8.777  1.00 20.98 ? 121 VAL   A CG2 1 
ATOM   916  N  N   . GLY   A 1 116 ? 14.401 2.777   10.576 1.00 19.39 ? 122 GLY   A N   1 
ATOM   917  C  CA  . GLY   A 1 116 ? 14.551 4.107   11.153 1.00 20.13 ? 122 GLY   A CA  1 
ATOM   918  C  C   . GLY   A 1 116 ? 14.980 4.029   12.603 1.00 20.47 ? 122 GLY   A C   1 
ATOM   919  O  O   . GLY   A 1 116 ? 15.363 2.954   13.066 1.00 20.66 ? 122 GLY   A O   1 
ATOM   920  N  N   . ILE   A 1 117 ? 14.958 5.153   13.301 1.00 19.94 ? 123 ILE   A N   1 
ATOM   921  C  CA  . ILE   A 1 117 ? 15.366 5.173   14.734 1.00 20.07 ? 123 ILE   A CA  1 
ATOM   922  C  C   . ILE   A 1 117 ? 14.313 5.927   15.578 1.00 20.71 ? 123 ILE   A C   1 
ATOM   923  O  O   . ILE   A 1 117 ? 13.716 6.864   15.083 1.00 20.54 ? 123 ILE   A O   1 
ATOM   924  C  CB  . ILE   A 1 117 ? 16.767 5.805   14.925 1.00 21.21 ? 123 ILE   A CB  1 
ATOM   925  C  CG1 . ILE   A 1 117 ? 16.860 7.195   14.251 1.00 22.77 ? 123 ILE   A CG1 1 
ATOM   926  C  CG2 . ILE   A 1 117 ? 17.915 4.847   14.469 1.00 22.49 ? 123 ILE   A CG2 1 
ATOM   927  C  CD1 . ILE   A 1 117 ? 18.239 7.907   14.504 1.00 23.94 ? 123 ILE   A CD1 1 
ATOM   928  N  N   . VAL   A 1 118 ? 14.182 5.614   16.901 1.00 20.83 ? 124 VAL   A N   1 
ATOM   929  C  CA  . VAL   A 1 118 ? 13.244 6.318   17.769 1.00 20.10 ? 124 VAL   A CA  1 
ATOM   930  C  C   . VAL   A 1 118 ? 13.607 7.816   17.781 1.00 19.75 ? 124 VAL   A C   1 
ATOM   931  O  O   . VAL   A 1 118 ? 14.791 8.167   17.846 1.00 19.56 ? 124 VAL   A O   1 
ATOM   932  C  CB  . VAL   A 1 118 ? 13.311 5.762   19.206 1.00 20.85 ? 124 VAL   A CB  1 
ATOM   933  C  CG1 . VAL   A 1 118 ? 12.393 6.566   20.115 1.00 21.75 ? 124 VAL   A CG1 1 
ATOM   934  C  CG2 . VAL   A 1 118 ? 12.887 4.275   19.234 1.00 21.35 ? 124 VAL   A CG2 1 
ATOM   935  N  N   . SER   A 1 119 ? 12.599 8.657   17.686 1.00 18.56 ? 125 SER   A N   1 
ATOM   936  C  CA  . SER   A 1 119 ? 12.851 10.121  17.642 1.00 19.18 ? 125 SER   A CA  1 
ATOM   937  C  C   . SER   A 1 119 ? 11.824 10.875  18.502 1.00 21.89 ? 125 SER   A C   1 
ATOM   938  O  O   . SER   A 1 119 ? 12.127 11.964  19.029 1.00 22.68 ? 125 SER   A O   1 
ATOM   939  C  CB  . SER   A 1 119 ? 12.770 10.620  16.197 1.00 21.10 ? 125 SER   A CB  1 
ATOM   940  O  OG  . SER   A 1 119 ? 12.892 12.045  16.105 1.00 23.98 ? 125 SER   A OG  1 
ATOM   941  N  N   . THR   A 1 120 ? 10.582 10.331  18.608 1.00 22.43 ? 126 THR   A N   1 
ATOM   942  C  CA  . THR   A 1 120 ? 9.516  11.015  19.373 1.00 24.05 ? 126 THR   A CA  1 
ATOM   943  C  C   . THR   A 1 120 ? 8.738  10.031  20.282 1.00 24.81 ? 126 THR   A C   1 
ATOM   944  O  O   . THR   A 1 120 ? 8.920  8.807   20.197 1.00 24.41 ? 126 THR   A O   1 
ATOM   945  C  CB  . THR   A 1 120 ? 8.528  11.777  18.395 1.00 25.28 ? 126 THR   A CB  1 
ATOM   946  O  OG1 . THR   A 1 120 ? 7.622  10.819  17.844 1.00 25.33 ? 126 THR   A OG1 1 
ATOM   947  C  CG2 . THR   A 1 120 ? 9.227  12.615  17.308 1.00 25.82 ? 126 THR   A CG2 1 
ATOM   948  N  N   . GLY   A 1 121 ? 7.798  10.551  21.072 1.00 26.93 ? 127 GLY   A N   1 
ATOM   949  C  CA  . GLY   A 1 121 ? 6.955  9.709   21.902 1.00 28.98 ? 127 GLY   A CA  1 
ATOM   950  C  C   . GLY   A 1 121 ? 6.051  10.496  22.814 1.00 30.20 ? 127 GLY   A C   1 
ATOM   951  O  O   . GLY   A 1 121 ? 6.109  11.722  22.861 1.00 29.96 ? 127 GLY   A O   1 
ATOM   952  N  N   . GLY   A 1 122 ? 5.224  9.774   23.538 1.00 32.08 ? 128 GLY   A N   1 
ATOM   953  C  CA  . GLY   A 1 122 ? 4.292  10.349  24.492 1.00 34.19 ? 128 GLY   A CA  1 
ATOM   954  C  C   . GLY   A 1 122 ? 2.905  9.798   24.271 1.00 35.74 ? 128 GLY   A C   1 
ATOM   955  O  O   . GLY   A 1 122 ? 2.544  9.441   23.141 1.00 35.26 ? 128 GLY   A O   1 
ATOM   956  N  N   . ASN   A 1 123 ? 2.107  9.752   25.345 1.00 36.93 ? 129 ASN   A N   1 
ATOM   957  C  CA  . ASN   A 1 123 ? 0.719  9.304   25.262 1.00 37.45 ? 129 ASN   A CA  1 
ATOM   958  C  C   . ASN   A 1 123 ? 0.594  7.852   24.795 1.00 36.98 ? 129 ASN   A C   1 
ATOM   959  O  O   . ASN   A 1 123 ? -0.420 7.497   24.188 1.00 38.48 ? 129 ASN   A O   1 
ATOM   960  C  CB  . ASN   A 1 123 ? -0.084 10.221  24.313 1.00 39.15 ? 129 ASN   A CB  1 
ATOM   961  C  CG  . ASN   A 1 123 ? -0.233 11.648  24.792 1.00 43.90 ? 129 ASN   A CG  1 
ATOM   962  O  OD1 . ASN   A 1 123 ? -0.169 11.931  25.998 1.00 46.64 ? 129 ASN   A OD1 1 
ATOM   963  N  ND2 . ASN   A 1 123 ? -0.489 12.567  23.865 1.00 43.53 ? 129 ASN   A ND2 1 
ATOM   964  N  N   . GLY   A 1 124 ? 1.593  7.021   25.073 1.00 34.56 ? 130 GLY   A N   1 
ATOM   965  C  CA  . GLY   A 1 124 ? 1.556  5.624   24.648 1.00 32.20 ? 130 GLY   A CA  1 
ATOM   966  C  C   . GLY   A 1 124 ? 1.928  5.398   23.185 1.00 30.12 ? 130 GLY   A C   1 
ATOM   967  O  O   . GLY   A 1 124 ? 1.711  4.314   22.637 1.00 29.34 ? 130 GLY   A O   1 
ATOM   968  N  N   . LEU   A 1 125 ? 2.515  6.413   22.552 1.00 28.95 ? 131 LEU   A N   1 
ATOM   969  C  CA  . LEU   A 1 125 ? 2.949  6.298   21.189 1.00 28.30 ? 131 LEU   A CA  1 
ATOM   970  C  C   . LEU   A 1 125 ? 4.496  6.408   21.156 1.00 27.50 ? 131 LEU   A C   1 
ATOM   971  O  O   . LEU   A 1 125 ? 5.130  6.816   22.146 1.00 28.79 ? 131 LEU   A O   1 
ATOM   972  C  CB  . LEU   A 1 125 ? 2.271  7.372   20.332 1.00 28.96 ? 131 LEU   A CB  1 
ATOM   973  C  CG  . LEU   A 1 125 ? 0.728  7.284   20.321 1.00 31.82 ? 131 LEU   A CG  1 
ATOM   974  C  CD1 . LEU   A 1 125 ? 0.086  8.662   20.054 1.00 34.30 ? 131 LEU   A CD1 1 
ATOM   975  C  CD2 . LEU   A 1 125 ? 0.248  6.231   19.365 1.00 31.92 ? 131 LEU   A CD2 1 
ATOM   976  N  N   . VAL   A 1 126 ? 5.085  5.910   20.078 1.00 24.18 ? 132 VAL   A N   1 
ATOM   977  C  CA  . VAL   A 1 126 ? 6.511  6.028   19.805 1.00 20.75 ? 132 VAL   A CA  1 
ATOM   978  C  C   . VAL   A 1 126 ? 6.615  6.387   18.323 1.00 21.27 ? 132 VAL   A C   1 
ATOM   979  O  O   . VAL   A 1 126 ? 5.875  5.858   17.492 1.00 21.03 ? 132 VAL   A O   1 
ATOM   980  C  CB  . VAL   A 1 126 ? 7.317  4.755   20.169 1.00 20.58 ? 132 VAL   A CB  1 
ATOM   981  C  CG1 . VAL   A 1 126 ? 6.643  3.467   19.700 1.00 19.97 ? 132 VAL   A CG1 1 
ATOM   982  C  CG2 . VAL   A 1 126 ? 8.763  4.846   19.690 1.00 19.72 ? 132 VAL   A CG2 1 
ATOM   983  N  N   . GLY   A 1 127 ? 7.482  7.347   18.014 1.00 21.36 ? 133 GLY   A N   1 
ATOM   984  C  CA  . GLY   A 1 127 ? 7.667  7.778   16.653 1.00 22.18 ? 133 GLY   A CA  1 
ATOM   985  C  C   . GLY   A 1 127 ? 9.102  7.520   16.254 1.00 21.98 ? 133 GLY   A C   1 
ATOM   986  O  O   . GLY   A 1 127 ? 10.025 7.653   17.070 1.00 22.37 ? 133 GLY   A O   1 
ATOM   987  N  N   . PHE   A 1 128 ? 9.270  7.142   15.012 1.00 20.57 ? 134 PHE   A N   1 
ATOM   988  C  CA  . PHE   A 1 128 ? 10.552 6.776   14.425 1.00 20.45 ? 134 PHE   A CA  1 
ATOM   989  C  C   . PHE   A 1 128 ? 10.829 7.647   13.218 1.00 21.22 ? 134 PHE   A C   1 
ATOM   990  O  O   . PHE   A 1 128 ? 9.950  7.807   12.346 1.00 21.24 ? 134 PHE   A O   1 
ATOM   991  C  CB  . PHE   A 1 128 ? 10.481 5.306   13.929 1.00 20.05 ? 134 PHE   A CB  1 
ATOM   992  C  CG  . PHE   A 1 128 ? 9.969  4.313   14.945 1.00 20.31 ? 134 PHE   A CG  1 
ATOM   993  C  CD1 . PHE   A 1 128 ? 10.833 3.728   15.872 1.00 20.84 ? 134 PHE   A CD1 1 
ATOM   994  C  CD2 . PHE   A 1 128 ? 8.627  3.952   14.975 1.00 20.61 ? 134 PHE   A CD2 1 
ATOM   995  C  CE1 . PHE   A 1 128 ? 10.353 2.826   16.827 1.00 21.38 ? 134 PHE   A CE1 1 
ATOM   996  C  CE2 . PHE   A 1 128 ? 8.153  3.028   15.922 1.00 21.78 ? 134 PHE   A CE2 1 
ATOM   997  C  CZ  . PHE   A 1 128 ? 9.020  2.470   16.836 1.00 21.16 ? 134 PHE   A CZ  1 
ATOM   998  N  N   . ALA   A 1 129 ? 12.098 8.122   13.089 1.00 21.48 ? 135 ALA   A N   1 
ATOM   999  C  CA  . ALA   A 1 129 ? 12.494 8.885   11.923 1.00 22.10 ? 135 ALA   A CA  1 
ATOM   1000 C  C   . ALA   A 1 129 ? 12.846 7.868   10.824 1.00 20.79 ? 135 ALA   A C   1 
ATOM   1001 O  O   . ALA   A 1 129 ? 13.752 7.080   11.021 1.00 18.83 ? 135 ALA   A O   1 
ATOM   1002 C  CB  . ALA   A 1 129 ? 13.723 9.742   12.253 1.00 22.48 ? 135 ALA   A CB  1 
ATOM   1003 N  N   . ASP   A 1 130 ? 12.153 7.900   9.651  1.00 21.30 ? 136 ASP   A N   1 
ATOM   1004 C  CA  . ASP   A 1 130 ? 12.488 6.983   8.563  1.00 21.19 ? 136 ASP   A CA  1 
ATOM   1005 C  C   . ASP   A 1 130 ? 13.883 7.260   7.928  1.00 22.09 ? 136 ASP   A C   1 
ATOM   1006 O  O   . ASP   A 1 130 ? 14.280 8.438   7.782  1.00 21.66 ? 136 ASP   A O   1 
ATOM   1007 C  CB  . ASP   A 1 130 ? 11.433 7.135   7.438  1.00 22.17 ? 136 ASP   A CB  1 
ATOM   1008 C  CG  . ASP   A 1 130 ? 11.564 6.103   6.329  1.00 26.82 ? 136 ASP   A CG  1 
ATOM   1009 O  OD1 . ASP   A 1 130 ? 11.612 4.906   6.636  1.00 27.84 ? 136 ASP   A OD1 1 
ATOM   1010 O  OD2 . ASP   A 1 130 ? 11.619 6.497   5.157  1.00 30.05 ? 136 ASP   A OD2 1 
ATOM   1011 N  N   . VAL   A 1 131 ? 14.598 6.208   7.492  1.00 21.35 ? 137 VAL   A N   1 
ATOM   1012 C  CA  . VAL   A 1 131 ? 15.878 6.406   6.743  1.00 22.48 ? 137 VAL   A CA  1 
ATOM   1013 C  C   . VAL   A 1 131 ? 15.828 5.673   5.361  1.00 24.14 ? 137 VAL   A C   1 
ATOM   1014 O  O   . VAL   A 1 131 ? 16.799 5.740   4.629  1.00 25.06 ? 137 VAL   A O   1 
ATOM   1015 C  CB  . VAL   A 1 131 ? 17.135 5.937   7.531  1.00 22.58 ? 137 VAL   A CB  1 
ATOM   1016 C  CG1 . VAL   A 1 131 ? 17.240 6.700   8.853  1.00 22.82 ? 137 VAL   A CG1 1 
ATOM   1017 C  CG2 . VAL   A 1 131 ? 17.061 4.437   7.792  1.00 22.72 ? 137 VAL   A CG2 1 
ATOM   1018 N  N   . ARG   A 1 132 ? 14.764 4.864   5.075  1.00 24.27 ? 138 ARG   A N   1 
ATOM   1019 C  CA  . ARG   A 1 132 ? 14.635 4.092   3.836  1.00 24.66 ? 138 ARG   A CA  1 
ATOM   1020 C  C   . ARG   A 1 132 ? 14.620 4.914   2.543  1.00 26.06 ? 138 ARG   A C   1 
ATOM   1021 O  O   . ARG   A 1 132 ? 14.862 4.353   1.465  1.00 27.64 ? 138 ARG   A O   1 
ATOM   1022 C  CB  . ARG   A 1 132 ? 13.389 3.177   3.872  1.00 24.27 ? 138 ARG   A CB  1 
ATOM   1023 C  CG  . ARG   A 1 132 ? 13.331 2.199   5.029  1.00 24.47 ? 138 ARG   A CG  1 
ATOM   1024 C  CD  . ARG   A 1 132 ? 11.971 1.485   5.018  1.00 23.43 ? 138 ARG   A CD  1 
ATOM   1025 N  NE  . ARG   A 1 132 ? 10.880 2.394   5.434  1.00 22.59 ? 138 ARG   A NE  1 
ATOM   1026 C  CZ  . ARG   A 1 132 ? 9.647  1.985   5.726  1.00 24.31 ? 138 ARG   A CZ  1 
ATOM   1027 N  NH1 . ARG   A 1 132 ? 9.297  0.710   5.542  1.00 25.08 ? 138 ARG   A NH1 1 
ATOM   1028 N  NH2 . ARG   A 1 132 ? 8.744  2.848   6.162  1.00 22.42 ? 138 ARG   A NH2 1 
ATOM   1029 N  N   . ASP   A 1 133 ? 14.339 6.225   2.619  1.00 25.27 ? 139 ASP   A N   1 
ATOM   1030 C  CA  . ASP   A 1 133 ? 14.367 7.058   1.403  1.00 25.44 ? 139 ASP   A CA  1 
ATOM   1031 C  C   . ASP   A 1 133 ? 15.799 7.562   1.095  1.00 25.58 ? 139 ASP   A C   1 
ATOM   1032 O  O   . ASP   A 1 133 ? 16.072 7.978   -0.027 1.00 27.13 ? 139 ASP   A O   1 
ATOM   1033 C  CB  . ASP   A 1 133 ? 13.401 8.246   1.518  1.00 25.69 ? 139 ASP   A CB  1 
ATOM   1034 C  CG  . ASP   A 1 133 ? 13.755 9.200   2.628  1.00 28.72 ? 139 ASP   A CG  1 
ATOM   1035 O  OD1 . ASP   A 1 133 ? 14.055 8.724   3.756  1.00 28.02 ? 139 ASP   A OD1 1 
ATOM   1036 O  OD2 . ASP   A 1 133 ? 13.733 10.433  2.381  1.00 30.65 ? 139 ASP   A OD2 1 
ATOM   1037 N  N   . LEU   A 1 134 ? 16.720 7.514   2.072  1.00 24.20 ? 140 LEU   A N   1 
ATOM   1038 C  CA  . LEU   A 1 134 ? 18.102 7.993   1.907  1.00 24.33 ? 140 LEU   A CA  1 
ATOM   1039 C  C   . LEU   A 1 134 ? 18.931 6.927   1.148  1.00 24.90 ? 140 LEU   A C   1 
ATOM   1040 O  O   . LEU   A 1 134 ? 19.768 6.224   1.720  1.00 24.39 ? 140 LEU   A O   1 
ATOM   1041 C  CB  . LEU   A 1 134 ? 18.685 8.300   3.320  1.00 23.88 ? 140 LEU   A CB  1 
ATOM   1042 C  CG  . LEU   A 1 134 ? 17.870 9.326   4.126  1.00 25.63 ? 140 LEU   A CG  1 
ATOM   1043 C  CD1 . LEU   A 1 134 ? 18.421 9.483   5.573  1.00 25.05 ? 140 LEU   A CD1 1 
ATOM   1044 C  CD2 . LEU   A 1 134 ? 17.773 10.654  3.398  1.00 27.18 ? 140 LEU   A CD2 1 
ATOM   1045 N  N   . LEU   A 1 135 ? 18.665 6.808   -0.177 1.00 25.32 ? 141 LEU   A N   1 
ATOM   1046 C  CA  . LEU   A 1 135 ? 19.264 5.814   -1.012 1.00 26.29 ? 141 LEU   A CA  1 
ATOM   1047 C  C   . LEU   A 1 135 ? 20.778 5.937   -1.092 1.00 27.19 ? 141 LEU   A C   1 
ATOM   1048 O  O   . LEU   A 1 135 ? 21.463 4.916   -1.227 1.00 27.06 ? 141 LEU   A O   1 
ATOM   1049 C  CB  . LEU   A 1 135 ? 18.659 5.861   -2.433 1.00 27.82 ? 141 LEU   A CB  1 
ATOM   1050 C  CG  . LEU   A 1 135 ? 17.151 5.857   -2.545 1.00 30.39 ? 141 LEU   A CG  1 
ATOM   1051 C  CD1 . LEU   A 1 135 ? 16.739 5.808   -4.009 1.00 32.35 ? 141 LEU   A CD1 1 
ATOM   1052 C  CD2 . LEU   A 1 135 ? 16.509 4.682   -1.792 1.00 30.83 ? 141 LEU   A CD2 1 
ATOM   1053 N  N   . TRP   A 1 136 ? 21.299 7.180   -1.018 1.00 27.40 ? 142 TRP   A N   1 
ATOM   1054 C  CA  . TRP   A 1 136 ? 22.729 7.437   -1.078 1.00 28.62 ? 142 TRP   A CA  1 
ATOM   1055 C  C   . TRP   A 1 136 ? 23.484 6.777   0.079  1.00 30.67 ? 142 TRP   A C   1 
ATOM   1056 O  O   . TRP   A 1 136 ? 24.687 6.587   -0.050 1.00 31.84 ? 142 TRP   A O   1 
ATOM   1057 C  CB  . TRP   A 1 136 ? 23.012 8.950   -1.139 1.00 28.16 ? 142 TRP   A CB  1 
ATOM   1058 C  CG  . TRP   A 1 136 ? 22.352 9.729   -0.042 1.00 27.55 ? 142 TRP   A CG  1 
ATOM   1059 C  CD1 . TRP   A 1 136 ? 21.152 10.378  -0.103 1.00 27.65 ? 142 TRP   A CD1 1 
ATOM   1060 C  CD2 . TRP   A 1 136 ? 22.876 9.971   1.278  1.00 27.23 ? 142 TRP   A CD2 1 
ATOM   1061 N  NE1 . TRP   A 1 136 ? 20.898 11.006  1.091  1.00 27.88 ? 142 TRP   A NE1 1 
ATOM   1062 C  CE2 . TRP   A 1 136 ? 21.957 10.800  1.945  1.00 27.41 ? 142 TRP   A CE2 1 
ATOM   1063 C  CE3 . TRP   A 1 136 ? 24.071 9.620   1.933  1.00 27.62 ? 142 TRP   A CE3 1 
ATOM   1064 C  CZ2 . TRP   A 1 136 ? 22.136 11.193  3.278  1.00 27.56 ? 142 TRP   A CZ2 1 
ATOM   1065 C  CZ3 . TRP   A 1 136 ? 24.276 10.067  3.228  1.00 27.78 ? 142 TRP   A CZ3 1 
ATOM   1066 C  CH2 . TRP   A 1 136 ? 23.317 10.845  3.885  1.00 27.75 ? 142 TRP   A CH2 1 
ATOM   1067 N  N   . LEU   A 1 137 ? 22.801 6.391   1.190  1.00 31.39 ? 143 LEU   A N   1 
ATOM   1068 C  CA  . LEU   A 1 137 ? 23.462 5.669   2.280  1.00 32.53 ? 143 LEU   A CA  1 
ATOM   1069 C  C   . LEU   A 1 137 ? 24.083 4.323   1.789  1.00 35.59 ? 143 LEU   A C   1 
ATOM   1070 O  O   . LEU   A 1 137 ? 24.998 3.811   2.432  1.00 35.08 ? 143 LEU   A O   1 
ATOM   1071 C  CB  . LEU   A 1 137 ? 22.472 5.363   3.420  1.00 31.79 ? 143 LEU   A CB  1 
ATOM   1072 C  CG  . LEU   A 1 137 ? 22.038 6.536   4.283  1.00 31.68 ? 143 LEU   A CG  1 
ATOM   1073 C  CD1 . LEU   A 1 137 ? 20.904 6.129   5.210  1.00 30.03 ? 143 LEU   A CD1 1 
ATOM   1074 C  CD2 . LEU   A 1 137 ? 23.211 7.085   5.089  1.00 32.39 ? 143 LEU   A CD2 1 
ATOM   1075 N  N   . ASP   A 1 138 ? 23.576 3.766   0.660  1.00 38.20 ? 144 ASP   A N   1 
ATOM   1076 C  CA  . ASP   A 1 138 ? 24.014 2.473   0.102  1.00 41.28 ? 144 ASP   A CA  1 
ATOM   1077 C  C   . ASP   A 1 138 ? 25.247 2.574   -0.779 1.00 45.70 ? 144 ASP   A C   1 
ATOM   1078 O  O   . ASP   A 1 138 ? 25.772 1.532   -1.158 1.00 46.42 ? 144 ASP   A O   1 
ATOM   1079 C  CB  . ASP   A 1 138 ? 22.908 1.834   -0.754 1.00 41.14 ? 144 ASP   A CB  1 
ATOM   1080 C  CG  . ASP   A 1 138 ? 21.649 1.444   -0.017 1.00 43.88 ? 144 ASP   A CG  1 
ATOM   1081 O  OD1 . ASP   A 1 138 ? 21.668 1.451   1.233  1.00 44.33 ? 144 ASP   A OD1 1 
ATOM   1082 O  OD2 . ASP   A 1 138 ? 20.635 1.134   -0.691 1.00 44.93 ? 144 ASP   A OD2 1 
ATOM   1083 N  N   . GLU   A 1 139 ? 25.690 3.790   -1.149 1.00 48.72 ? 145 GLU   A N   1 
ATOM   1084 C  CA  . GLU   A 1 139 ? 26.826 3.924   -2.054 1.00 52.54 ? 145 GLU   A CA  1 
ATOM   1085 C  C   . GLU   A 1 139 ? 27.801 5.058   -1.704 1.00 55.82 ? 145 GLU   A C   1 
ATOM   1086 O  O   . GLU   A 1 139 ? 27.426 6.011   -1.018 1.00 56.39 ? 145 GLU   A O   1 
ATOM   1087 C  CB  . GLU   A 1 139 ? 26.306 4.079   -3.496 1.00 55.57 ? 145 GLU   A CB  1 
ATOM   1088 C  CG  . GLU   A 1 139 ? 25.394 5.282   -3.693 1.00 60.86 ? 145 GLU   A CG  1 
ATOM   1089 C  CD  . GLU   A 1 139 ? 24.190 5.001   -4.573 1.00 68.26 ? 145 GLU   A CD  1 
ATOM   1090 O  OE1 . GLU   A 1 139 ? 23.902 5.818   -5.480 1.00 68.83 ? 145 GLU   A OE1 1 
ATOM   1091 O  OE2 . GLU   A 1 139 ? 23.534 3.956   -4.352 1.00 71.01 ? 145 GLU   A OE2 1 
ATOM   1092 N  N   . GLU   A 1 140 ? 29.048 4.958   -2.210 1.00 57.88 ? 146 GLU   A N   1 
ATOM   1093 C  CA  . GLU   A 1 140 ? 30.120 5.958   -2.046 1.00 60.06 ? 146 GLU   A CA  1 
ATOM   1094 C  C   . GLU   A 1 140 ? 30.235 6.478   -0.595 1.00 61.48 ? 146 GLU   A C   1 
ATOM   1095 O  O   . GLU   A 1 140 ? 31.163 7.212   -0.241 1.00 62.07 ? 146 GLU   A O   1 
ATOM   1096 C  CB  . GLU   A 1 140 ? 29.966 7.102   -3.085 1.00 62.55 ? 146 GLU   A CB  1 
ATOM   1097 C  CG  . GLU   A 1 140 ? 29.334 8.404   -2.611 1.00 68.30 ? 146 GLU   A CG  1 
ATOM   1098 C  CD  . GLU   A 1 140 ? 30.332 9.469   -2.189 1.00 76.59 ? 146 GLU   A CD  1 
ATOM   1099 O  OE1 . GLU   A 1 140 ? 29.929 10.406  -1.461 1.00 78.12 ? 146 GLU   A OE1 1 
ATOM   1100 O  OE2 . GLU   A 1 140 ? 31.520 9.357   -2.572 1.00 79.30 ? 146 GLU   A OE2 1 
HETATM 1101 N  N1  . A1B2X B 2 .   ? 12.346 14.638  17.596 1.00 24.02 ? 201 A1B2X A N1  1 
HETATM 1102 C  C4  . A1B2X B 2 .   ? 11.113 11.756  22.652 1.00 28.41 ? 201 A1B2X A C4  1 
HETATM 1103 C  C5  . A1B2X B 2 .   ? 10.356 12.715  23.313 1.00 28.65 ? 201 A1B2X A C5  1 
HETATM 1104 C  C6  . A1B2X B 2 .   ? 10.626 14.192  23.123 1.00 28.58 ? 201 A1B2X A C6  1 
HETATM 1105 C  C7  . A1B2X B 2 .   ? 11.191 14.634  20.769 1.00 27.90 ? 201 A1B2X A C7  1 
HETATM 1106 C  C8  . A1B2X B 2 .   ? 12.202 15.383  19.899 1.00 27.60 ? 201 A1B2X A C8  1 
HETATM 1107 C  C10 . A1B2X B 2 .   ? 13.567 14.708  20.074 1.00 26.98 ? 201 A1B2X A C10 1 
HETATM 1108 C  C13 . A1B2X B 2 .   ? 9.367  12.289  24.193 1.00 29.19 ? 201 A1B2X A C13 1 
HETATM 1109 O  O1  . A1B2X B 2 .   ? 13.288 14.432  23.736 1.00 28.50 ? 201 A1B2X A O1  1 
HETATM 1110 C  C12 . A1B2X B 2 .   ? 12.972 14.565  22.565 1.00 27.63 ? 201 A1B2X A C12 1 
HETATM 1111 C  C11 . A1B2X B 2 .   ? 14.030 14.841  21.529 1.00 27.31 ? 201 A1B2X A C11 1 
HETATM 1112 C  C9  . A1B2X B 2 .   ? 11.791 15.497  18.439 1.00 26.58 ? 201 A1B2X A C9  1 
HETATM 1113 O  O   . A1B2X B 2 .   ? 11.001 16.371  18.076 1.00 27.29 ? 201 A1B2X A O   1 
HETATM 1114 N  N   . A1B2X B 2 .   ? 11.681 14.482  22.145 1.00 28.16 ? 201 A1B2X A N   1 
HETATM 1115 C  C3  . A1B2X B 2 .   ? 10.887 10.405  22.864 1.00 28.48 ? 201 A1B2X A C3  1 
HETATM 1116 C  C2  . A1B2X B 2 .   ? 9.918  9.991   23.757 1.00 29.15 ? 201 A1B2X A C2  1 
HETATM 1117 C  C1  . A1B2X B 2 .   ? 9.156  10.932  24.433 1.00 30.24 ? 201 A1B2X A C1  1 
HETATM 1118 S  S   . A1B2X B 2 .   ? 7.972  10.431  25.644 1.00 31.59 ? 201 A1B2X A S   1 
HETATM 1119 C  C   . A1B2X B 2 .   ? 7.228  11.979  26.174 1.00 30.68 ? 201 A1B2X A C   1 
HETATM 1120 ZN ZN  . ZN    C 3 .   ? 10.924 -4.088  4.976  1.00 24.84 2 202 ZN    A ZN  1 
HETATM 1121 S  S   . DMS   D 4 .   ? 14.997 21.340  7.332  1.00 85.22 ? 203 DMS   A S   1 
HETATM 1122 O  O   . DMS   D 4 .   ? 14.527 21.967  8.615  1.00 85.08 ? 203 DMS   A O   1 
HETATM 1123 C  C1  . DMS   D 4 .   ? 13.651 21.375  6.113  1.00 85.12 ? 203 DMS   A C1  1 
HETATM 1124 C  C2  . DMS   D 4 .   ? 16.065 22.533  6.466  1.00 85.29 ? 203 DMS   A C2  1 
HETATM 1125 S  S   . DMS   E 4 .   ? 19.889 -3.514  21.691 1.00 83.14 ? 204 DMS   A S   1 
HETATM 1126 O  O   . DMS   E 4 .   ? 20.579 -4.119  22.879 1.00 83.11 ? 204 DMS   A O   1 
HETATM 1127 C  C1  . DMS   E 4 .   ? 20.761 -1.960  21.311 1.00 83.23 ? 204 DMS   A C1  1 
HETATM 1128 C  C2  . DMS   E 4 .   ? 20.394 -4.421  20.191 1.00 83.01 ? 204 DMS   A C2  1 
HETATM 1129 O  O   . HOH   F 5 .   ? 19.086 20.388  26.647 1.00 30.00 ? 301 HOH   A O   1 
HETATM 1130 O  O   . HOH   F 5 .   ? 22.522 -5.312  22.676 1.00 45.90 ? 302 HOH   A O   1 
HETATM 1131 O  O   . HOH   F 5 .   ? 31.459 7.348   2.125  1.00 53.30 ? 303 HOH   A O   1 
HETATM 1132 O  O   . HOH   F 5 .   ? 13.601 7.615   30.635 1.00 35.78 ? 304 HOH   A O   1 
HETATM 1133 O  O   . HOH   F 5 .   ? 9.697  21.458  11.237 1.00 42.38 ? 305 HOH   A O   1 
HETATM 1134 O  O   . HOH   F 5 .   ? 31.455 10.346  12.242 1.00 52.15 ? 306 HOH   A O   1 
HETATM 1135 O  O   . HOH   F 5 .   ? 6.572  3.203   3.415  1.00 37.13 ? 307 HOH   A O   1 
HETATM 1136 O  O   . HOH   F 5 .   ? 5.424  6.620   24.667 1.00 31.73 ? 308 HOH   A O   1 
HETATM 1137 O  O   . HOH   F 5 .   ? 3.050  8.591   9.928  1.00 39.45 ? 309 HOH   A O   1 
HETATM 1138 O  O   . HOH   F 5 .   ? 24.541 17.312  2.415  1.00 45.82 ? 310 HOH   A O   1 
HETATM 1139 O  O   . HOH   F 5 .   ? 16.380 17.154  3.657  1.00 37.74 ? 311 HOH   A O   1 
HETATM 1140 O  O   . HOH   F 5 .   ? 7.018  -4.867  28.527 1.00 30.95 ? 312 HOH   A O   1 
HETATM 1141 O  O   . HOH   F 5 .   ? 4.073  21.904  22.909 1.00 35.21 ? 313 HOH   A O   1 
HETATM 1142 O  O   . HOH   F 5 .   ? 19.983 -0.210  26.676 1.00 37.21 ? 314 HOH   A O   1 
HETATM 1143 O  O   . HOH   F 5 .   ? 5.948  19.934  25.831 1.00 40.80 ? 315 HOH   A O   1 
HETATM 1144 O  O   . HOH   F 5 .   ? 8.837  19.570  18.200 1.00 21.96 ? 316 HOH   A O   1 
HETATM 1145 O  O   . HOH   F 5 .   ? 14.992 -5.035  17.953 1.00 36.43 ? 317 HOH   A O   1 
HETATM 1146 O  O   . HOH   F 5 .   ? 6.617  13.674  21.143 1.00 30.39 ? 318 HOH   A O   1 
HETATM 1147 O  O   . HOH   F 5 .   ? 23.808 0.074   14.785 1.00 29.55 ? 319 HOH   A O   1 
HETATM 1148 O  O   . HOH   F 5 .   ? 10.661 8.869   4.264  1.00 29.05 ? 320 HOH   A O   1 
HETATM 1149 O  O   . HOH   F 5 .   ? 1.118  0.172   16.476 1.00 22.42 ? 321 HOH   A O   1 
HETATM 1150 O  O   . HOH   F 5 .   ? 10.839 23.485  24.684 1.00 35.53 ? 322 HOH   A O   1 
HETATM 1151 O  O   . HOH   F 5 .   ? 10.250 18.167  20.161 1.00 25.91 ? 323 HOH   A O   1 
HETATM 1152 O  O   . HOH   F 5 .   ? 4.638  -4.442  21.026 1.00 32.63 ? 324 HOH   A O   1 
HETATM 1153 O  O   . HOH   F 5 .   ? 1.838  9.605   4.301  1.00 56.32 ? 325 HOH   A O   1 
HETATM 1154 O  O   . HOH   F 5 .   ? 19.091 4.873   26.076 1.00 39.58 ? 326 HOH   A O   1 
HETATM 1155 O  O   . HOH   F 5 .   ? 7.958  -3.362  0.223  1.00 34.94 ? 327 HOH   A O   1 
HETATM 1156 O  O   . HOH   F 5 .   ? 22.162 -4.621  11.802 1.00 34.55 ? 328 HOH   A O   1 
HETATM 1157 O  O   . HOH   F 5 .   ? 27.111 3.994   18.712 1.00 44.40 ? 329 HOH   A O   1 
HETATM 1158 O  O   . HOH   F 5 .   ? -1.010 1.708   4.493  1.00 48.71 ? 330 HOH   A O   1 
HETATM 1159 O  O   . HOH   F 5 .   ? 31.563 8.695   4.243  1.00 33.28 ? 331 HOH   A O   1 
HETATM 1160 O  O   . HOH   F 5 .   ? 29.465 3.151   9.180  1.00 30.22 ? 332 HOH   A O   1 
HETATM 1161 O  O   . HOH   F 5 .   ? 31.186 18.643  6.525  1.00 37.13 ? 333 HOH   A O   1 
HETATM 1162 O  O   . HOH   F 5 .   ? 31.069 10.909  15.713 1.00 54.17 ? 334 HOH   A O   1 
HETATM 1163 O  O   . HOH   F 5 .   ? 10.440 5.397   2.995  1.00 26.52 ? 335 HOH   A O   1 
HETATM 1164 O  O   . HOH   F 5 .   ? 12.098 11.318  0.417  1.00 51.99 ? 336 HOH   A O   1 
HETATM 1165 O  O   . HOH   F 5 .   ? 20.879 8.972   18.191 1.00 24.92 ? 337 HOH   A O   1 
HETATM 1166 O  O   . HOH   F 5 .   ? 14.692 15.417  27.765 1.00 40.45 ? 338 HOH   A O   1 
HETATM 1167 O  O   . HOH   F 5 .   ? 31.529 2.738   11.098 1.00 40.66 ? 339 HOH   A O   1 
HETATM 1168 O  O   . HOH   F 5 .   ? 8.846  -8.401  23.156 1.00 23.13 ? 340 HOH   A O   1 
HETATM 1169 O  O   . HOH   F 5 .   ? 5.125  1.186   -2.169 1.00 51.97 ? 341 HOH   A O   1 
HETATM 1170 O  O   . HOH   F 5 .   ? 31.395 11.031  17.997 1.00 39.18 ? 342 HOH   A O   1 
HETATM 1171 O  O   . HOH   F 5 .   ? 15.646 -10.851 7.285  1.00 47.74 ? 343 HOH   A O   1 
HETATM 1172 O  O   . HOH   F 5 .   ? 1.745  -2.110  19.737 1.00 33.90 ? 344 HOH   A O   1 
HETATM 1173 O  O   . HOH   F 5 .   ? 24.646 22.441  8.603  1.00 26.19 ? 345 HOH   A O   1 
HETATM 1174 O  O   . HOH   F 5 .   ? 25.617 11.975  21.977 1.00 47.29 ? 346 HOH   A O   1 
HETATM 1175 O  O   . HOH   F 5 .   ? 1.099  2.261   24.344 1.00 33.68 ? 347 HOH   A O   1 
HETATM 1176 O  O   . HOH   F 5 .   ? 16.163 -2.883  17.066 1.00 28.93 ? 348 HOH   A O   1 
HETATM 1177 O  O   . HOH   F 5 .   ? 15.134 11.720  0.394  1.00 35.04 ? 349 HOH   A O   1 
HETATM 1178 O  O   . HOH   F 5 .   ? 13.043 2.597   0.358  1.00 24.96 ? 350 HOH   A O   1 
HETATM 1179 O  O   . HOH   F 5 .   ? 15.405 23.003  26.668 1.00 30.00 ? 351 HOH   A O   1 
HETATM 1180 O  O   . HOH   F 5 .   ? 9.062  3.304   2.438  1.00 34.52 ? 352 HOH   A O   1 
HETATM 1181 O  O   . HOH   F 5 .   ? 27.645 3.324   1.805  1.00 50.69 ? 353 HOH   A O   1 
HETATM 1182 O  O   . HOH   F 5 .   ? 28.208 11.583  0.469  1.00 62.30 ? 354 HOH   A O   1 
HETATM 1183 O  O   . HOH   F 5 .   ? 11.074 5.012   33.195 1.00 28.28 ? 355 HOH   A O   1 
HETATM 1184 O  O   . HOH   F 5 .   ? 18.083 20.279  18.938 1.00 41.39 ? 356 HOH   A O   1 
HETATM 1185 O  O   . HOH   F 5 .   ? 16.842 12.175  23.525 1.00 28.37 ? 357 HOH   A O   1 
HETATM 1186 O  O   . HOH   F 5 .   ? 14.681 14.876  3.197  1.00 34.60 ? 358 HOH   A O   1 
HETATM 1187 O  O   . HOH   F 5 .   ? 18.821 19.032  16.525 1.00 25.18 ? 359 HOH   A O   1 
HETATM 1188 O  O   . HOH   F 5 .   ? 7.770  16.112  22.009 1.00 32.47 ? 360 HOH   A O   1 
HETATM 1189 O  O   . HOH   F 5 .   ? 18.622 0.739   29.545 1.00 37.84 ? 361 HOH   A O   1 
HETATM 1190 O  O   . HOH   F 5 .   ? 3.973  4.109   27.445 1.00 42.82 ? 362 HOH   A O   1 
HETATM 1191 O  O   . HOH   F 5 .   ? 25.762 15.858  21.834 1.00 50.93 ? 363 HOH   A O   1 
HETATM 1192 O  O   . HOH   F 5 .   ? 28.385 -1.924  12.265 1.00 37.54 ? 364 HOH   A O   1 
HETATM 1193 O  O   . HOH   F 5 .   ? 27.574 -1.494  5.404  1.00 41.55 ? 365 HOH   A O   1 
HETATM 1194 O  O   . HOH   F 5 .   ? 5.346  26.256  17.704 1.00 47.40 ? 366 HOH   A O   1 
HETATM 1195 O  O   . HOH   F 5 .   ? 12.781 16.152  25.886 1.00 33.84 ? 367 HOH   A O   1 
HETATM 1196 O  O   . HOH   F 5 .   ? 23.505 -6.145  7.714  1.00 59.06 ? 368 HOH   A O   1 
HETATM 1197 O  O   . HOH   F 5 .   ? 15.613 2.756   22.705 1.00 21.65 ? 369 HOH   A O   1 
HETATM 1198 O  O   . HOH   F 5 .   ? 34.024 -3.272  9.375  1.00 36.17 ? 370 HOH   A O   1 
HETATM 1199 O  O   . HOH   F 5 .   ? 21.030 -1.113  -2.350 1.00 48.01 ? 371 HOH   A O   1 
HETATM 1200 O  O   . HOH   F 5 .   ? 8.451  25.635  15.372 1.00 41.08 ? 372 HOH   A O   1 
HETATM 1201 O  O   . HOH   F 5 .   ? 11.745 12.024  11.231 1.00 22.57 ? 373 HOH   A O   1 
HETATM 1202 O  O   . HOH   F 5 .   ? 21.988 21.423  6.038  1.00 44.19 ? 374 HOH   A O   1 
HETATM 1203 O  O   . HOH   F 5 .   ? 4.971  10.623  18.822 1.00 42.81 ? 375 HOH   A O   1 
HETATM 1204 O  O   . HOH   F 5 .   ? 3.994  -4.514  6.302  1.00 35.89 ? 376 HOH   A O   1 
HETATM 1205 O  O   . HOH   F 5 .   ? 22.135 -0.683  3.041  1.00 36.02 ? 377 HOH   A O   1 
HETATM 1206 O  O   . HOH   F 5 .   ? 6.930  8.333   28.280 1.00 38.58 ? 378 HOH   A O   1 
HETATM 1207 O  O   . HOH   F 5 .   ? 16.018 23.605  18.551 1.00 34.20 ? 379 HOH   A O   1 
HETATM 1208 O  O   . HOH   F 5 .   ? 18.391 21.414  8.959  1.00 24.90 ? 380 HOH   A O   1 
HETATM 1209 O  O   . HOH   F 5 .   ? 29.910 4.597   2.337  1.00 36.06 ? 381 HOH   A O   1 
HETATM 1210 O  O   . HOH   F 5 .   ? 7.937  4.230   32.643 1.00 38.85 ? 382 HOH   A O   1 
HETATM 1211 O  O   . HOH   F 5 .   ? 27.331 9.594   20.241 1.00 48.02 ? 383 HOH   A O   1 
HETATM 1212 O  O   . HOH   F 5 .   ? 18.501 2.645   22.415 1.00 22.96 ? 384 HOH   A O   1 
HETATM 1213 O  O   . HOH   F 5 .   ? 27.745 16.278  1.751  1.00 41.30 ? 385 HOH   A O   1 
HETATM 1214 O  O   . HOH   F 5 .   ? 17.626 -6.338  2.427  1.00 46.58 ? 386 HOH   A O   1 
HETATM 1215 O  O   . HOH   F 5 .   ? 11.480 16.433  3.335  1.00 43.06 ? 387 HOH   A O   1 
HETATM 1216 O  O   . HOH   F 5 .   ? 5.887  2.320   6.252  1.00 35.51 ? 388 HOH   A O   1 
HETATM 1217 O  O   . HOH   F 5 .   ? 6.072  -6.917  14.051 1.00 45.63 ? 389 HOH   A O   1 
HETATM 1218 O  O   . HOH   F 5 .   ? 30.428 16.403  21.565 1.00 40.70 ? 390 HOH   A O   1 
HETATM 1219 O  O   . HOH   F 5 .   ? 4.764  7.885   3.019  1.00 58.08 ? 391 HOH   A O   1 
HETATM 1220 O  O   . HOH   F 5 .   ? 8.468  20.776  8.955  1.00 46.49 ? 392 HOH   A O   1 
HETATM 1221 O  O   . HOH   F 5 .   ? 7.959  16.454  24.818 1.00 35.33 ? 393 HOH   A O   1 
HETATM 1222 O  O   . HOH   F 5 .   ? 8.420  -5.230  30.960 1.00 56.39 ? 394 HOH   A O   1 
HETATM 1223 O  O   . HOH   F 5 .   ? 23.788 18.139  18.024 1.00 30.68 ? 395 HOH   A O   1 
HETATM 1224 O  O   . HOH   F 5 .   ? 12.998 -8.313  23.935 1.00 24.48 ? 396 HOH   A O   1 
HETATM 1225 O  O   . HOH   F 5 .   ? 5.951  -0.989  23.818 1.00 25.58 ? 397 HOH   A O   1 
HETATM 1226 O  O   . HOH   F 5 .   ? 20.113 9.150   25.120 1.00 32.83 ? 398 HOH   A O   1 
HETATM 1227 O  O   . HOH   F 5 .   ? 11.367 -4.276  -1.344 1.00 47.58 ? 399 HOH   A O   1 
HETATM 1228 O  O   . HOH   F 5 .   ? 0.395  4.173   6.810  1.00 37.61 ? 400 HOH   A O   1 
HETATM 1229 O  O   . HOH   F 5 .   ? 13.004 21.630  12.844 1.00 32.20 ? 401 HOH   A O   1 
HETATM 1230 O  O   . HOH   F 5 .   ? 14.876 9.698   29.260 1.00 33.14 ? 402 HOH   A O   1 
HETATM 1231 O  O   . HOH   F 5 .   ? 13.401 10.975  8.941  1.00 19.84 ? 403 HOH   A O   1 
HETATM 1232 O  O   . HOH   F 5 .   ? 30.930 -4.114  6.439  1.00 39.42 ? 404 HOH   A O   1 
HETATM 1233 O  O   . HOH   F 5 .   ? 19.097 0.048   18.780 1.00 31.15 ? 405 HOH   A O   1 
HETATM 1234 O  O   . HOH   F 5 .   ? 15.999 14.238  24.826 1.00 30.00 ? 406 HOH   A O   1 
HETATM 1235 O  O   . HOH   F 5 .   ? 4.187  15.116  20.436 1.00 29.85 ? 407 HOH   A O   1 
HETATM 1236 O  O   . HOH   F 5 .   ? 26.021 -2.379  13.864 1.00 64.71 ? 408 HOH   A O   1 
HETATM 1237 O  O   . HOH   F 5 .   ? 36.887 -0.545  7.908  1.00 45.42 ? 409 HOH   A O   1 
HETATM 1238 O  O   . HOH   F 5 .   ? 20.625 2.958   -3.255 1.00 42.76 ? 410 HOH   A O   1 
HETATM 1239 O  O   . HOH   F 5 .   ? 13.483 -6.506  30.008 1.00 46.06 ? 411 HOH   A O   1 
HETATM 1240 O  O   . HOH   F 5 .   ? 8.675  -7.008  8.612  1.00 39.57 ? 412 HOH   A O   1 
HETATM 1241 O  O   . HOH   F 5 .   ? 6.940  13.449  5.366  1.00 28.96 ? 413 HOH   A O   1 
HETATM 1242 O  O   . HOH   F 5 .   ? 22.415 -2.375  14.690 1.00 33.69 ? 414 HOH   A O   1 
HETATM 1243 O  O   . HOH   F 5 .   ? 15.211 -4.038  0.968  1.00 35.43 ? 415 HOH   A O   1 
HETATM 1244 O  O   . HOH   F 5 .   ? 6.886  25.413  21.676 1.00 34.44 ? 416 HOH   A O   1 
HETATM 1245 O  O   . HOH   F 5 .   ? 18.715 19.724  4.766  1.00 49.99 ? 417 HOH   A O   1 
HETATM 1246 O  O   . HOH   F 5 .   ? 33.012 14.442  19.546 1.00 56.15 ? 418 HOH   A O   1 
HETATM 1247 O  O   . HOH   F 5 .   ? 22.949 8.659   20.079 1.00 26.83 ? 419 HOH   A O   1 
HETATM 1248 O  O   . HOH   F 5 .   ? 24.451 2.408   18.616 1.00 37.68 ? 420 HOH   A O   1 
HETATM 1249 O  O   . HOH   F 5 .   ? 0.159  15.399  17.411 1.00 43.20 ? 421 HOH   A O   1 
HETATM 1250 O  O   . HOH   F 5 .   ? 35.134 7.137   12.582 1.00 55.93 ? 422 HOH   A O   1 
HETATM 1251 O  O   . HOH   F 5 .   ? 1.687  -2.348  17.190 1.00 30.92 ? 423 HOH   A O   1 
HETATM 1252 O  O   . HOH   F 5 .   ? 6.850  23.442  11.825 1.00 35.49 ? 424 HOH   A O   1 
HETATM 1253 O  O   . HOH   F 5 .   ? 10.533 9.781   31.230 1.00 45.49 ? 425 HOH   A O   1 
HETATM 1254 O  O   . HOH   F 5 .   ? 2.352  13.797  5.305  1.00 41.91 ? 426 HOH   A O   1 
HETATM 1255 O  O   . HOH   F 5 .   ? 32.850 14.526  6.015  1.00 54.48 ? 427 HOH   A O   1 
HETATM 1256 O  O   . HOH   F 5 .   ? 4.748  -1.695  21.612 1.00 29.64 ? 428 HOH   A O   1 
HETATM 1257 O  O   . HOH   F 5 .   ? 19.745 -3.353  15.346 1.00 36.09 ? 429 HOH   A O   1 
HETATM 1258 O  O   . HOH   F 5 .   ? 31.735 2.022   1.787  1.00 52.19 ? 430 HOH   A O   1 
HETATM 1259 O  O   . HOH   F 5 .   ? 22.844 19.066  5.159  1.00 28.05 ? 431 HOH   A O   1 
HETATM 1260 O  O   . HOH   F 5 .   ? -0.262 15.897  12.795 1.00 48.25 ? 432 HOH   A O   1 
HETATM 1261 O  O   . HOH   F 5 .   ? 24.004 3.386   21.944 1.00 61.54 ? 433 HOH   A O   1 
HETATM 1262 O  O   . HOH   F 5 .   ? 18.822 13.318  1.360  1.00 42.69 ? 434 HOH   A O   1 
HETATM 1263 O  O   . HOH   F 5 .   ? 35.411 4.632   12.645 1.00 56.56 ? 435 HOH   A O   1 
HETATM 1264 O  O   . HOH   F 5 .   ? 20.987 -4.755  9.416  1.00 35.87 ? 436 HOH   A O   1 
HETATM 1265 O  O   . HOH   F 5 .   ? 18.503 22.854  16.734 1.00 51.61 ? 437 HOH   A O   1 
HETATM 1266 O  O   . HOH   F 5 .   ? 21.075 1.755   17.961 1.00 45.57 ? 438 HOH   A O   1 
HETATM 1267 O  O   . HOH   F 5 .   ? 18.792 -2.515  17.876 1.00 33.44 ? 439 HOH   A O   1 
HETATM 1268 O  O   . HOH   F 5 .   ? 31.160 6.008   16.830 1.00 50.93 ? 440 HOH   A O   1 
HETATM 1269 O  O   . HOH   F 5 .   ? 6.569  -3.290  -1.846 1.00 41.22 ? 441 HOH   A O   1 
HETATM 1270 O  O   . HOH   F 5 .   ? 3.335  11.248  20.580 1.00 51.10 ? 442 HOH   A O   1 
HETATM 1271 O  O   . HOH   F 5 .   ? 2.181  -6.142  17.963 1.00 55.18 ? 443 HOH   A O   1 
HETATM 1272 O  O   . HOH   F 5 .   ? 7.376  11.545  4.039  1.00 52.24 ? 444 HOH   A O   1 
HETATM 1273 O  O   . HOH   F 5 .   ? 19.444 -4.143  12.794 1.00 40.31 ? 445 HOH   A O   1 
HETATM 1274 O  O   . HOH   F 5 .   ? 19.962 7.373   27.205 1.00 36.81 ? 446 HOH   A O   1 
HETATM 1275 O  O   . HOH   F 5 .   ? 17.939 9.422   -2.294 1.00 40.05 ? 447 HOH   A O   1 
HETATM 1276 O  O   . HOH   F 5 .   ? 4.417  -4.654  2.420  1.00 54.34 ? 448 HOH   A O   1 
HETATM 1277 O  O   . HOH   F 5 .   ? 31.675 0.207   12.454 1.00 49.04 ? 449 HOH   A O   1 
HETATM 1278 O  O   . HOH   F 5 .   ? 25.404 7.471   19.654 1.00 44.69 ? 450 HOH   A O   1 
HETATM 1279 O  O   . HOH   F 5 .   ? 5.297  -1.011  28.759 1.00 42.06 ? 451 HOH   A O   1 
HETATM 1280 O  O   . HOH   F 5 .   ? 2.718  -3.127  3.879  1.00 63.84 ? 452 HOH   A O   1 
HETATM 1281 O  O   . HOH   F 5 .   ? 2.894  6.482   28.125 1.00 49.59 ? 453 HOH   A O   1 
HETATM 1282 O  O   . HOH   F 5 .   ? 17.775 11.338  -0.216 1.00 40.07 ? 454 HOH   A O   1 
HETATM 1283 O  O   . HOH   F 5 .   ? 22.597 -2.879  33.967 1.00 52.21 ? 455 HOH   A O   1 
HETATM 1284 O  O   . HOH   F 5 .   ? 7.180  -4.870  2.446  1.00 31.73 ? 456 HOH   A O   1 
HETATM 1285 O  O   . HOH   F 5 .   ? 39.186 1.002   7.741  1.00 64.32 ? 457 HOH   A O   1 
HETATM 1286 O  O   . HOH   F 5 .   ? 19.318 -6.577  33.737 1.00 48.26 ? 458 HOH   A O   1 
HETATM 1287 O  O   . HOH   F 5 .   ? 34.938 17.737  6.616  1.00 57.76 ? 459 HOH   A O   1 
HETATM 1288 O  O   . HOH   F 5 .   ? 2.909  -6.404  14.380 1.00 47.61 ? 460 HOH   A O   1 
HETATM 1289 O  O   . HOH   F 5 .   ? 4.442  9.636   28.058 1.00 45.28 ? 461 HOH   A O   1 
HETATM 1290 O  O   . HOH   F 5 .   ? 6.007  5.359   1.948  1.00 57.18 ? 462 HOH   A O   1 
HETATM 1291 O  O   . HOH   F 5 .   ? 19.978 9.410   -3.620 1.00 32.80 ? 463 HOH   A O   1 
HETATM 1292 O  O   . HOH   F 5 .   ? 17.453 11.879  28.033 1.00 50.28 ? 464 HOH   A O   1 
HETATM 1293 O  O   . HOH   F 5 .   ? 20.423 15.131  0.423  1.00 51.94 ? 465 HOH   A O   1 
HETATM 1294 O  O   . HOH   F 5 .   ? 12.996 14.359  0.767  1.00 49.59 ? 466 HOH   A O   1 
HETATM 1295 O  O   . HOH   F 5 .   ? 2.830  1.972   26.478 1.00 37.27 ? 467 HOH   A O   1 
HETATM 1296 O  O   . HOH   F 5 .   ? 18.625 11.671  25.364 1.00 43.82 ? 468 HOH   A O   1 
HETATM 1297 O  O   . HOH   F 5 .   ? 4.651  -1.459  26.381 1.00 40.81 ? 469 HOH   A O   1 
HETATM 1298 O  O   . HOH   F 5 .   ? 3.100  14.321  22.746 1.00 50.56 ? 470 HOH   A O   1 
HETATM 1299 O  O   . HOH   F 5 .   ? 7.484  -7.568  1.970  1.00 56.13 ? 471 HOH   A O   1 
HETATM 1300 O  O   . HOH   F 5 .   ? 16.320 14.156  1.426  1.00 46.43 ? 472 HOH   A O   1 
HETATM 1301 O  O   . HOH   F 5 .   ? 25.999 11.236  -1.371 1.00 65.30 ? 473 HOH   A O   1 
HETATM 1302 O  O   . HOH   F 5 .   ? 12.941 23.678  14.916 1.00 35.06 ? 474 HOH   A O   1 
HETATM 1303 O  O   . HOH   F 5 .   ? 22.123 12.753  25.834 1.00 56.47 ? 475 HOH   A O   1 
HETATM 1304 O  O   . HOH   F 5 .   ? 1.382  -1.309  23.688 1.00 42.07 ? 476 HOH   A O   1 
HETATM 1305 O  O   . HOH   F 5 .   ? 6.647  27.462  19.969 1.00 62.31 ? 477 HOH   A O   1 
HETATM 1306 O  O   . HOH   F 5 .   ? 8.976  8.168   2.206  1.00 41.90 ? 478 HOH   A O   1 
HETATM 1307 O  O   . HOH   F 5 .   ? 15.053 -6.360  32.402 1.00 45.44 ? 479 HOH   A O   1 
HETATM 1308 O  O   . HOH   F 5 .   ? 8.974  10.365  29.061 1.00 46.08 ? 480 HOH   A O   1 
HETATM 1309 O  O   . HOH   F 5 .   ? 9.071  23.015  26.956 1.00 56.95 ? 481 HOH   A O   1 
HETATM 1310 O  O   . HOH   F 5 .   ? 23.787 9.709   22.537 1.00 40.22 ? 482 HOH   A O   1 
HETATM 1311 O  O   . HOH   F 5 .   ? 3.887  -4.084  26.980 1.00 53.32 ? 483 HOH   A O   1 
HETATM 1312 O  O   . HOH   F 5 .   ? 32.633 4.022   13.309 1.00 45.03 ? 484 HOH   A O   1 
HETATM 1313 O  O   . HOH   F 5 .   ? 14.976 24.209  16.583 1.00 37.90 ? 485 HOH   A O   1 
HETATM 1314 O  O   . HOH   F 5 .   ? 1.846  21.268  7.764  1.00 60.55 ? 486 HOH   A O   1 
HETATM 1315 O  O   . HOH   F 5 .   ? 0.270  12.650  17.587 1.00 40.61 ? 487 HOH   A O   1 
HETATM 1316 O  O   . HOH   F 5 .   ? 31.871 6.512   14.314 1.00 42.31 ? 488 HOH   A O   1 
HETATM 1317 O  O   . HOH   F 5 .   ? 24.573 13.663  0.506  1.00 43.44 ? 489 HOH   A O   1 
HETATM 1318 O  O   . HOH   F 5 .   ? 10.025 15.778  26.602 1.00 37.57 ? 490 HOH   A O   1 
HETATM 1319 O  O   . HOH   F 5 .   ? 29.854 -1.445  13.792 1.00 44.91 ? 491 HOH   A O   1 
HETATM 1320 O  O   . HOH   F 5 .   ? 22.633 10.245  24.912 1.00 42.76 ? 492 HOH   A O   1 
HETATM 1321 O  O   . HOH   F 5 .   ? 14.401 11.867  -2.201 1.00 41.41 ? 493 HOH   A O   1 
HETATM 1322 O  O   . HOH   F 5 .   ? 37.446 20.640  9.297  1.00 43.91 ? 494 HOH   A O   1 
HETATM 1323 O  O   . HOH   F 5 .   ? 40.229 18.994  16.260 1.00 48.59 ? 495 HOH   A O   1 
HETATM 1324 O  O   . HOH   F 5 .   ? 21.555 11.637  -3.821 1.00 44.58 ? 496 HOH   A O   1 
HETATM 1325 O  O   . HOH   F 5 .   ? 4.261  -6.239  23.267 1.00 49.18 ? 497 HOH   A O   1 
HETATM 1326 O  O   . HOH   F 5 .   ? 10.822 25.188  14.037 1.00 40.22 ? 498 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   ? 0.3124 0.3031 0.4681 -0.0093 -0.0524 -0.0035 7   SER   A N   
2    C CA  . SER   A 1   ? 0.3201 0.3167 0.5008 -0.0092 -0.0542 -0.0002 7   SER   A CA  
3    C C   . SER   A 1   ? 0.3117 0.3160 0.5032 -0.0083 -0.0462 0.0036  7   SER   A C   
4    O O   . SER   A 1   ? 0.3236 0.3286 0.5039 -0.0082 -0.0421 0.0041  7   SER   A O   
5    C CB  . SER   A 1   ? 0.3571 0.3483 0.5456 -0.0113 -0.0676 0.0019  7   SER   A CB  
6    O OG  . SER   A 1   ? 0.4018 0.3925 0.5905 -0.0120 -0.0712 0.0064  7   SER   A OG  
7    N N   . GLY   A 2   ? 0.2896 0.2985 0.5020 -0.0079 -0.0430 0.0058  8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.2832 0.2967 0.5045 -0.0076 -0.0344 0.0086  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.2684 0.2852 0.5028 -0.0071 -0.0261 0.0092  8   GLY   A C   
10   O O   . GLY   A 2   ? 0.2662 0.2834 0.4982 -0.0065 -0.0248 0.0071  8   GLY   A O   
11   N N   . ALA   A 3   ? 0.2563 0.2742 0.5040 -0.0074 -0.0195 0.0120  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.2580 0.2764 0.5149 -0.0075 -0.0097 0.0126  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.2544 0.2721 0.5109 -0.0085 0.0012  0.0137  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.2662 0.2837 0.5241 -0.0090 0.0009  0.0149  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.2508 0.2679 0.5320 -0.0071 -0.0121 0.0148  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.2337 0.2498 0.4875 -0.0093 0.0110  0.0135  10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.2136 0.2260 0.4653 -0.0112 0.0228  0.0138  10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.2166 0.2245 0.4902 -0.0111 0.0307  0.0162  10  ILE   A C   
19   O O   . ILE   A 4   ? 0.2144 0.2215 0.4957 -0.0104 0.0310  0.0170  10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.2155 0.2268 0.4457 -0.0128 0.0277  0.0121  10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.2072 0.2238 0.4211 -0.0124 0.0200  0.0102  10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.2350 0.2402 0.4578 -0.0158 0.0392  0.0116  10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.2191 0.2358 0.4178 -0.0137 0.0219  0.0099  10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.2225 0.2271 0.5081 -0.0119 0.0378  0.0175  11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.2244 0.2239 0.5331 -0.0118 0.0476  0.0200  11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.2392 0.2301 0.5370 -0.0144 0.0639  0.0185  11  TYR   A C   
27   O O   . TYR   A 5   ? 0.2581 0.2468 0.5532 -0.0157 0.0685  0.0176  11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.2258 0.2275 0.5626 -0.0105 0.0426  0.0234  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.2351 0.2428 0.5811 -0.0088 0.0257  0.0248  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.2442 0.2522 0.6078 -0.0080 0.0228  0.0262  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.2642 0.2757 0.5987 -0.0086 0.0129  0.0244  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.2600 0.2718 0.6292 -0.0074 0.0068  0.0266  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.2745 0.2888 0.6123 -0.0079 -0.0024 0.0250  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.2824 0.2967 0.6370 -0.0075 -0.0058 0.0258  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.3099 0.3253 0.6647 -0.0075 -0.0212 0.0254  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.2469 0.2319 0.5344 -0.0157 0.0721  0.0179  12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.2693 0.2431 0.5412 -0.0191 0.0877  0.0161  12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.2932 0.2582 0.5807 -0.0191 0.1011  0.0182  12  VAL   A C   
39   O O   . VAL   A 6   ? 0.2925 0.2592 0.5850 -0.0177 0.0979  0.0201  12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.2863 0.2587 0.5240 -0.0217 0.0852  0.0137  12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.2777 0.2554 0.5117 -0.0200 0.0761  0.0153  12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.3127 0.2707 0.5311 -0.0262 0.1006  0.0121  12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.3042 0.2595 0.6024 -0.0205 0.1168  0.0182  13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.3044 0.2499 0.6205 -0.0205 0.1323  0.0203  13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.2960 0.2501 0.6463 -0.0167 0.1241  0.0244  13  GLY   A C   
46   O O   . GLY   A 7   ? 0.2939 0.2582 0.6658 -0.0144 0.1118  0.0261  13  GLY   A O   
47   N N   . ASN   A 8   ? 0.2951 0.2455 0.6475 -0.0164 0.1285  0.0260  14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.2806 0.2389 0.6643 -0.0134 0.1197  0.0294  14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.2747 0.2417 0.6426 -0.0123 0.1031  0.0287  14  ASN   A C   
50   O O   . ASN   A 8   ? 0.2667 0.2350 0.6483 -0.0110 0.1008  0.0306  14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.3148 0.2637 0.7211 -0.0132 0.1365  0.0323  14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.4068 0.3500 0.8426 -0.0132 0.1504  0.0339  14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.4230 0.3745 0.8960 -0.0109 0.1426  0.0371  14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.4349 0.3631 0.8543 -0.0159 0.1710  0.0320  14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.2704 0.2430 0.6120 -0.0129 0.0921  0.0258  15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.2659 0.2461 0.5930 -0.0118 0.0775  0.0249  15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.2511 0.2416 0.5783 -0.0105 0.0610  0.0234  15  TYR   A C   
58   O O   . TYR   A 9   ? 0.2448 0.2360 0.5694 -0.0112 0.0607  0.0225  15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.2778 0.2536 0.5692 -0.0140 0.0808  0.0234  15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.2956 0.2594 0.5793 -0.0158 0.0956  0.0252  15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.3052 0.2679 0.6043 -0.0142 0.0974  0.0280  15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.3218 0.2744 0.5798 -0.0196 0.1072  0.0241  15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.3246 0.2751 0.6148 -0.0159 0.1117  0.0303  15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.3482 0.2874 0.5945 -0.0218 0.1209  0.0260  15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.3586 0.2968 0.6206 -0.0198 0.1232  0.0294  15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.4030 0.3271 0.6527 -0.0219 0.1372  0.0319  15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.2280 0.2247 0.5565 -0.0090 0.0481  0.0229  16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.2170 0.2211 0.5401 -0.0081 0.0330  0.0211  16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.2121 0.2186 0.5119 -0.0078 0.0278  0.0189  16  ARG   A C   
70   O O   . ARG   A 10  ? 0.2056 0.2119 0.5091 -0.0070 0.0267  0.0194  16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.2144 0.2218 0.5634 -0.0069 0.0219  0.0225  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.2327 0.2447 0.5717 -0.0065 0.0057  0.0202  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.2606 0.2738 0.6244 -0.0064 -0.0061 0.0220  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.2768 0.2907 0.6333 -0.0065 -0.0192 0.0193  16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.2969 0.3110 0.6389 -0.0071 -0.0312 0.0173  16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.2884 0.3031 0.6218 -0.0074 -0.0324 0.0183  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.2468 0.2593 0.5804 -0.0075 -0.0410 0.0140  16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.2124 0.2215 0.4907 -0.0084 0.0245  0.0168  17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.2233 0.2352 0.4825 -0.0081 0.0199  0.0151  17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.2161 0.2325 0.4728 -0.0068 0.0081  0.0129  17  VAL   A C   
81   O O   . VAL   A 11  ? 0.2179 0.2355 0.4697 -0.0073 0.0053  0.0120  17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.2347 0.2457 0.4720 -0.0100 0.0250  0.0146  17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.2280 0.2425 0.4507 -0.0095 0.0202  0.0140  17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.2518 0.2551 0.4867 -0.0123 0.0376  0.0162  17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.1936 0.2111 0.4518 -0.0055 0.0020  0.0117  18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.2032 0.2221 0.4558 -0.0048 -0.0080 0.0088  18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.2022 0.2224 0.4424 -0.0038 -0.0090 0.0069  18  VAL   A C   
88   O O   . VAL   A 12  ? 0.2026 0.2231 0.4431 -0.0034 -0.0040 0.0086  18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.2239 0.2407 0.4935 -0.0048 -0.0162 0.0086  18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.2515 0.2677 0.5363 -0.0056 -0.0166 0.0113  18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.2221 0.2377 0.5059 -0.0042 -0.0145 0.0093  18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.1894 0.2092 0.4194 -0.0034 -0.0152 0.0037  19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.1899 0.2100 0.4130 -0.0021 -0.0153 0.0018  19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.2158 0.2333 0.4524 -0.0015 -0.0172 0.0014  19  ASN   A C   
95   O O   . ASN   A 13  ? 0.2219 0.2362 0.4676 -0.0023 -0.0232 0.0001  19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.1847 0.2021 0.3952 -0.0020 -0.0198 -0.0022 19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.2143 0.2341 0.4120 -0.0024 -0.0172 -0.0019 19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.2293 0.2482 0.4244 -0.0034 -0.0193 -0.0014 19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.2053 0.2283 0.3970 -0.0016 -0.0129 -0.0017 19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.2167 0.2355 0.4558 -0.0004 -0.0129 0.0030  20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.2190 0.2353 0.4720 0.0003  -0.0137 0.0029  20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.2213 0.2328 0.4749 0.0000  -0.0211 -0.0022 20  ARG   A C   
103  O O   . ARG   A 14  ? 0.2391 0.2477 0.5059 -0.0009 -0.0254 -0.0029 20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.2218 0.2397 0.4753 0.0018  -0.0086 0.0057  20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.2374 0.2526 0.5070 0.0025  -0.0077 0.0068  20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.2452 0.2618 0.5136 0.0041  -0.0037 0.0100  20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.2484 0.2624 0.5314 0.0050  -0.0014 0.0123  20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.2691 0.2803 0.5609 0.0060  -0.0037 0.0091  20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.2545 0.2637 0.5407 0.0058  -0.0084 0.0028  20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.2301 0.2391 0.5356 0.0069  -0.0007 0.0119  20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.2057 0.2154 0.4443 0.0002  -0.0228 -0.0060 21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.2098 0.2119 0.4434 -0.0008 -0.0292 -0.0115 21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.2263 0.2244 0.4590 -0.0033 -0.0380 -0.0127 21  HIS   A C   
114  O O   . HIS   A 15  ? 0.2445 0.2349 0.4741 -0.0050 -0.0451 -0.0170 21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.2220 0.2208 0.4389 -0.0001 -0.0265 -0.0154 21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.2407 0.2406 0.4427 -0.0006 -0.0260 -0.0152 21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.2349 0.2428 0.4366 0.0004  -0.0206 -0.0110 21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.2551 0.2481 0.4414 -0.0023 -0.0303 -0.0186 21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.2481 0.2545 0.4363 -0.0004 -0.0211 -0.0121 21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.2556 0.2529 0.4336 -0.0019 -0.0265 -0.0164 21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.2401 0.2424 0.4754 -0.0038 -0.0383 -0.0090 22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.2536 0.2528 0.4917 -0.0060 -0.0475 -0.0086 22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.2798 0.2820 0.5432 -0.0064 -0.0486 -0.0045 22  LEU   A C   
124  O O   . LEU   A 16  ? 0.2900 0.2912 0.5616 -0.0080 -0.0558 -0.0027 22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.2511 0.2518 0.4754 -0.0062 -0.0468 -0.0072 22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.2616 0.2582 0.4621 -0.0060 -0.0451 -0.0110 22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.2569 0.2554 0.4467 -0.0062 -0.0436 -0.0090 22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.2643 0.2497 0.4528 -0.0081 -0.0536 -0.0161 22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.2824 0.2878 0.5593 -0.0050 -0.0409 -0.0025 23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.2776 0.2847 0.5792 -0.0052 -0.0393 0.0014  23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.2661 0.2691 0.5836 -0.0072 -0.0507 0.0001  23  ALA   A C   
132  O O   . ALA   A 17  ? 0.2664 0.2645 0.5766 -0.0082 -0.0571 -0.0045 23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.2779 0.2870 0.5872 -0.0036 -0.0285 0.0039  23  ALA   A CB  
134  N N   . THR   A 18  ? 0.2550 0.2593 0.5949 -0.0082 -0.0534 0.0039  24  THR   A N   
135  C CA  . THR   A 18  ? 0.2683 0.2693 0.6277 -0.0106 -0.0660 0.0036  24  THR   A CA  
136  C C   . THR   A 18  ? 0.2716 0.2733 0.6577 -0.0101 -0.0609 0.0052  24  THR   A C   
137  O O   . THR   A 18  ? 0.2651 0.2692 0.6532 -0.0078 -0.0472 0.0073  24  THR   A O   
138  C CB  . THR   A 18  ? 0.2933 0.2959 0.6677 -0.0119 -0.0727 0.0081  24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.3120 0.3189 0.7106 -0.0103 -0.0610 0.0132  24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.2970 0.2994 0.6476 -0.0120 -0.0749 0.0080  24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.2823 0.2812 0.6897 -0.0125 -0.0723 0.0049  25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.3056 0.3048 0.7427 -0.0125 -0.0689 0.0066  25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.2967 0.3003 0.7555 -0.0105 -0.0547 0.0131  25  HIS   A C   
144  O O   . HIS   A 19  ? 0.3077 0.3114 0.7755 -0.0088 -0.0421 0.0148  25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.3480 0.3436 0.8045 -0.0164 -0.0868 0.0056  25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.4242 0.4216 0.9218 -0.0169 -0.0857 0.0096  25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.4675 0.4611 0.9789 -0.0187 -0.0910 0.0067  25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.4377 0.4393 0.9665 -0.0162 -0.0805 0.0162  25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.4605 0.4570 1.0115 -0.0189 -0.0883 0.0118  25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.4436 0.4448 1.0065 -0.0173 -0.0813 0.0177  25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.2822 0.2882 0.7485 -0.0108 -0.0562 0.0167  26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.2778 0.2861 0.7631 -0.0092 -0.0417 0.0222  26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.2688 0.2769 0.7298 -0.0069 -0.0246 0.0220  26  ASN   A C   
154  O O   . ASN   A 20  ? 0.2678 0.2745 0.7409 -0.0059 -0.0097 0.0253  26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.3245 0.3349 0.8197 -0.0100 -0.0473 0.0256  26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.4081 0.4194 0.9322 -0.0088 -0.0330 0.0313  26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.4338 0.4447 0.9924 -0.0090 -0.0304 0.0344  26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.4327 0.4442 0.9439 -0.0077 -0.0224 0.0325  26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.2490 0.2576 0.6761 -0.0065 -0.0267 0.0185  27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.2385 0.2471 0.6428 -0.0050 -0.0134 0.0186  27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.2315 0.2380 0.6370 -0.0040 -0.0060 0.0188  27  ASP   A C   
162  O O   . ASP   A 21  ? 0.2401 0.2446 0.6408 -0.0033 0.0076  0.0216  27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.2354 0.2453 0.6075 -0.0049 -0.0186 0.0149  27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.2798 0.2912 0.6440 -0.0056 -0.0225 0.0151  27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.2919 0.3035 0.6685 -0.0057 -0.0154 0.0186  27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.3035 0.3149 0.6487 -0.0061 -0.0316 0.0119  27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.2253 0.2310 0.6336 -0.0042 -0.0148 0.0158  28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.2355 0.2392 0.6473 -0.0031 -0.0084 0.0164  28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.2307 0.2322 0.6724 -0.0031 0.0004  0.0209  28  TRP   A C   
170  O O   . TRP   A 22  ? 0.2329 0.2316 0.6728 -0.0020 0.0130  0.0241  28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.2372 0.2394 0.6471 -0.0037 -0.0194 0.0116  28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.2579 0.2606 0.6383 -0.0030 -0.0225 0.0077  28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.2767 0.2784 0.6423 -0.0043 -0.0333 0.0030  28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.2666 0.2703 0.6292 -0.0010 -0.0141 0.0088  28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.2948 0.2970 0.6363 -0.0030 -0.0307 0.0008  28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.2886 0.2928 0.6293 -0.0010 -0.0197 0.0046  28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.2746 0.2781 0.6376 0.0004  -0.0028 0.0136  28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.3001 0.3057 0.6245 0.0008  -0.0147 0.0049  28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.2946 0.2992 0.6388 0.0018  0.0005  0.0143  28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.3018 0.3083 0.6285 0.0021  -0.0054 0.0102  28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.2274 0.2295 0.6966 -0.0045 -0.0060 0.0217  29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.2181 0.2182 0.7211 -0.0045 0.0030  0.0263  29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.2358 0.2333 0.7351 -0.0036 0.0210  0.0306  29  ALA   A C   
184  O O   . ALA   A 23  ? 0.2491 0.2421 0.7634 -0.0031 0.0350  0.0343  29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.2016 0.2038 0.7357 -0.0064 -0.0093 0.0269  29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.2312 0.2302 0.7096 -0.0037 0.0213  0.0298  30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.2369 0.2316 0.7091 -0.0036 0.0381  0.0328  30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.2340 0.2269 0.6672 -0.0034 0.0436  0.0315  30  ASN   A C   
189  O O   . ASN   A 24  ? 0.2289 0.2199 0.6467 -0.0041 0.0504  0.0317  30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.2597 0.2566 0.7438 -0.0042 0.0357  0.0335  30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.2857 0.2837 0.8127 -0.0046 0.0323  0.0365  30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.3018 0.2953 0.8518 -0.0043 0.0465  0.0400  30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.2804 0.2836 0.8189 -0.0055 0.0133  0.0352  30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.2134 0.2066 0.6329 -0.0027 0.0405  0.0305  31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.2279 0.2206 0.6139 -0.0025 0.0422  0.0299  31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.2474 0.2324 0.6191 -0.0035 0.0582  0.0336  31  LEU   A C   
197  O O   . LEU   A 25  ? 0.2415 0.2198 0.6256 -0.0035 0.0694  0.0371  31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.2206 0.2151 0.6019 -0.0013 0.0356  0.0289  31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.2239 0.2185 0.5764 -0.0009 0.0365  0.0295  31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.2273 0.2271 0.5605 -0.0012 0.0283  0.0258  31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.2343 0.2293 0.5901 0.0006  0.0329  0.0298  31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.2426 0.2271 0.5868 -0.0046 0.0593  0.0326  32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.2577 0.2331 0.5809 -0.0065 0.0725  0.0354  32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.2805 0.2568 0.5780 -0.0066 0.0676  0.0366  32  VAL   A C   
205  O O   . VAL   A 26  ? 0.3126 0.2816 0.6005 -0.0073 0.0749  0.0407  32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.2594 0.2322 0.5712 -0.0086 0.0777  0.0337  32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.2697 0.2316 0.5527 -0.0115 0.0893  0.0356  32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.2499 0.2208 0.5904 -0.0084 0.0845  0.0339  32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.2694 0.2542 0.5572 -0.0059 0.0553  0.0335  33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.2739 0.2608 0.5418 -0.0058 0.0501  0.0349  33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.2432 0.2399 0.5115 -0.0041 0.0372  0.0307  33  TRP   A C   
212  O O   . TRP   A 27  ? 0.2312 0.2316 0.5016 -0.0043 0.0332  0.0270  33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.2906 0.2717 0.5310 -0.0090 0.0553  0.0367  33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.2988 0.2839 0.5204 -0.0093 0.0472  0.0381  33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.3178 0.3000 0.5303 -0.0095 0.0466  0.0432  33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.2904 0.2834 0.5033 -0.0094 0.0384  0.0349  33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.3249 0.3134 0.5257 -0.0096 0.0373  0.0436  33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.3065 0.3015 0.5073 -0.0096 0.0329  0.0383  33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.2871 0.2852 0.5021 -0.0093 0.0350  0.0300  33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.2994 0.3015 0.4918 -0.0099 0.0249  0.0368  33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.2831 0.2877 0.4877 -0.0095 0.0274  0.0283  33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.2833 0.2898 0.4774 -0.0098 0.0230  0.0315  33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.2204 0.2203 0.4871 -0.0024 0.0316  0.0316  34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.2252 0.2323 0.4907 -0.0009 0.0217  0.0275  34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.2236 0.2328 0.4790 -0.0001 0.0191  0.0304  34  GLU   A C   
226  O O   . GLU   A 28  ? 0.2298 0.2354 0.4856 0.0001  0.0228  0.0355  34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.2294 0.2380 0.5140 0.0006  0.0163  0.0236  34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.2452 0.2506 0.5456 0.0019  0.0189  0.0259  34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.2789 0.2856 0.5784 0.0037  0.0162  0.0268  34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.2489 0.2525 0.5599 0.0046  0.0197  0.0299  34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.2797 0.2904 0.5690 0.0044  0.0112  0.0245  34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.2220 0.2367 0.4701 0.0005  0.0130  0.0276  35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.2263 0.2441 0.4692 0.0015  0.0103  0.0307  35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.2107 0.2332 0.4566 0.0033  0.0050  0.0257  35  ASP   A C   
235  O O   . ASP   A 29  ? 0.2246 0.2498 0.4622 0.0025  0.0029  0.0226  35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.2569 0.2741 0.4823 -0.0012 0.0110  0.0351  35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.3284 0.3490 0.5505 -0.0007 0.0067  0.0398  35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.3459 0.3708 0.5789 0.0021  0.0037  0.0384  35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.3531 0.3711 0.5617 -0.0034 0.0064  0.0451  35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.1888 0.2110 0.4465 0.0056  0.0039  0.0246  36  SER   A N   
241  C CA  A SER   A 30  ? 0.1799 0.2035 0.4397 0.0072  0.0008  0.0193  36  SER   A CA  
242  C CA  B SER   A 30  ? 0.1895 0.2132 0.4488 0.0071  0.0008  0.0191  36  SER   A CA  
243  C C   . SER   A 30  ? 0.1838 0.2124 0.4356 0.0075  -0.0002 0.0207  36  SER   A C   
244  O O   . SER   A 30  ? 0.1908 0.2202 0.4383 0.0078  -0.0013 0.0159  36  SER   A O   
245  C CB  A SER   A 30  ? 0.1731 0.1943 0.4467 0.0094  0.0016  0.0190  36  SER   A CB  
246  C CB  B SER   A 30  ? 0.2145 0.2353 0.4874 0.0092  0.0011  0.0177  36  SER   A CB  
247  O OG  A SER   A 30  ? 0.1500 0.1695 0.4243 0.0104  0.0000  0.0124  36  SER   A OG  
248  O OG  B SER   A 30  ? 0.2363 0.2592 0.5141 0.0108  0.0027  0.0236  36  SER   A OG  
249  N N   . SER   A 31  ? 0.1653 0.1964 0.4153 0.0071  0.0000  0.0279  37  SER   A N   
250  C CA  . SER   A 31  ? 0.1794 0.2157 0.4258 0.0070  -0.0021 0.0301  37  SER   A CA  
251  C C   . SER   A 31  ? 0.1875 0.2257 0.4204 0.0045  -0.0032 0.0279  37  SER   A C   
252  O O   . SER   A 31  ? 0.2039 0.2463 0.4357 0.0046  -0.0045 0.0275  37  SER   A O   
253  C CB  . SER   A 31  ? 0.2409 0.2790 0.4897 0.0068  -0.0040 0.0389  37  SER   A CB  
254  O OG  . SER   A 31  ? 0.3091 0.3445 0.5448 0.0035  -0.0045 0.0433  37  SER   A OG  
255  N N   . ARG   A 32  ? 0.1868 0.2218 0.4121 0.0025  -0.0017 0.0263  38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.1802 0.2161 0.3940 0.0001  -0.0019 0.0240  38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.1877 0.2223 0.4018 0.0008  -0.0019 0.0173  38  ARG   A C   
258  O O   . ARG   A 32  ? 0.1890 0.2244 0.3949 -0.0008 -0.0019 0.0154  38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.1999 0.2315 0.4049 -0.0029 0.0008  0.0269  38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.2132 0.2444 0.4105 -0.0050 -0.0007 0.0335  38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.2340 0.2577 0.4183 -0.0086 0.0035  0.0357  38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.2298 0.2527 0.4031 -0.0115 0.0048  0.0322  38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.2478 0.2647 0.4048 -0.0159 0.0070  0.0339  38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.2442 0.2547 0.3913 -0.0182 0.0076  0.0394  38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.2412 0.2577 0.3901 -0.0183 0.0084  0.0303  38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.1839 0.2155 0.4070 0.0026  -0.0023 0.0143  39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.1837 0.2122 0.4067 0.0026  -0.0043 0.0088  39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.1936 0.2208 0.4153 0.0006  -0.0035 0.0095  39  ASP   A C   
269  O O   . ASP   A 33  ? 0.1910 0.2175 0.4085 -0.0002 -0.0055 0.0067  39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.2014 0.2305 0.4161 0.0029  -0.0055 0.0048  39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.2216 0.2454 0.4327 0.0024  -0.0089 -0.0004 39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.2102 0.2299 0.4285 0.0025  -0.0114 -0.0022 39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.2094 0.2329 0.4105 0.0016  -0.0096 -0.0023 39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.1916 0.2174 0.4169 -0.0004 0.0003  0.0136  40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.1856 0.2089 0.4119 -0.0022 0.0034  0.0143  40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.1923 0.2116 0.4336 -0.0018 0.0059  0.0156  40  LEU   A C   
277  O O   . LEU   A 34  ? 0.1867 0.2048 0.4338 -0.0007 0.0072  0.0178  40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.2002 0.2226 0.4147 -0.0045 0.0083  0.0176  40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.2288 0.2545 0.4300 -0.0060 0.0067  0.0163  40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.2375 0.2601 0.4265 -0.0093 0.0111  0.0191  40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.2191 0.2455 0.4215 -0.0059 0.0049  0.0126  40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.1902 0.2076 0.4396 -0.0027 0.0070  0.0148  41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.1998 0.2135 0.4667 -0.0026 0.0103  0.0165  41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.2128 0.2241 0.4831 -0.0043 0.0161  0.0176  41  LEU   A C   
285  O O   . LEU   A 35  ? 0.2262 0.2394 0.4917 -0.0049 0.0134  0.0158  41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.2087 0.2227 0.4910 -0.0017 0.0025  0.0136  41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.2245 0.2353 0.5297 -0.0017 0.0051  0.0155  41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.2217 0.2318 0.5373 -0.0008 -0.0012 0.0134  41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.2404 0.2508 0.5600 -0.0028 0.0036  0.0157  41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.2127 0.2189 0.4910 -0.0049 0.0255  0.0208  42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.2290 0.2310 0.5134 -0.0064 0.0338  0.0218  42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.2294 0.2286 0.5410 -0.0057 0.0373  0.0237  42  VAL   A C   
293  O O   . VAL   A 36  ? 0.2173 0.2144 0.5350 -0.0049 0.0396  0.0255  42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.2492 0.2446 0.5145 -0.0088 0.0449  0.0238  42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.2619 0.2506 0.5351 -0.0104 0.0562  0.0244  42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.2527 0.2513 0.4938 -0.0100 0.0402  0.0222  42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.2375 0.2374 0.5676 -0.0058 0.0364  0.0236  43  SER   A N   
298  C CA  . SER   A 37  ? 0.2457 0.2434 0.6062 -0.0054 0.0396  0.0258  43  SER   A CA  
299  C C   . SER   A 37  ? 0.2615 0.2544 0.6338 -0.0064 0.0515  0.0279  43  SER   A C   
300  O O   . SER   A 37  ? 0.2609 0.2531 0.6188 -0.0074 0.0544  0.0268  43  SER   A O   
301  C CB  . SER   A 37  ? 0.2477 0.2507 0.6266 -0.0046 0.0245  0.0244  43  SER   A CB  
302  O OG  . SER   A 37  ? 0.2496 0.2561 0.6243 -0.0051 0.0162  0.0229  43  SER   A OG  
303  N N   . SER   A 38  ? 0.2593 0.2481 0.6587 -0.0061 0.0601  0.0308  44  SER   A N   
304  C CA  . SER   A 38  ? 0.2719 0.2549 0.6872 -0.0069 0.0738  0.0329  44  SER   A CA  
305  C C   . SER   A 38  ? 0.2783 0.2672 0.7206 -0.0063 0.0643  0.0338  44  SER   A C   
306  O O   . SER   A 38  ? 0.2915 0.2869 0.7487 -0.0056 0.0488  0.0338  44  SER   A O   
307  C CB  . SER   A 38  ? 0.2981 0.2733 0.7340 -0.0068 0.0886  0.0363  44  SER   A CB  
308  O OG  . SER   A 38  ? 0.3191 0.2997 0.7812 -0.0054 0.0784  0.0374  44  SER   A OG  
309  N N   . THR   A 39  ? 0.2779 0.2636 0.7266 -0.0069 0.0732  0.0347  45  THR   A N   
310  C CA  . THR   A 39  ? 0.2812 0.2720 0.7578 -0.0063 0.0649  0.0369  45  THR   A CA  
311  C C   . THR   A 39  ? 0.3057 0.2903 0.8159 -0.0062 0.0815  0.0407  45  THR   A C   
312  O O   . THR   A 39  ? 0.3138 0.2885 0.8141 -0.0071 0.1012  0.0403  45  THR   A O   
313  C CB  . THR   A 39  ? 0.2824 0.2751 0.7375 -0.0069 0.0610  0.0349  45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.2848 0.2689 0.7274 -0.0082 0.0800  0.0340  45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.2891 0.2869 0.7111 -0.0071 0.0475  0.0312  45  THR   A CG2 
316  N N   . THR   A 40  ? 0.3112 0.3005 0.8593 -0.0055 0.0739  0.0446  46  THR   A N   
317  C CA  . THR   A 40  ? 0.3364 0.3202 0.9217 -0.0051 0.0904  0.0488  46  THR   A CA  
318  C C   . THR   A 40  ? 0.3397 0.3197 0.9193 -0.0055 0.1002  0.0485  46  THR   A C   
319  O O   . THR   A 40  ? 0.3457 0.3163 0.9375 -0.0058 0.1217  0.0495  46  THR   A O   
320  C CB  . THR   A 40  ? 0.3703 0.3607 1.0055 -0.0042 0.0784  0.0542  46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.4058 0.4033 1.0513 -0.0042 0.0613  0.0565  46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.3713 0.3659 1.0083 -0.0044 0.0648  0.0534  46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.3365 0.3227 0.8984 -0.0057 0.0855  0.0472  47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.3369 0.3201 0.8935 -0.0061 0.0932  0.0470  47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.3536 0.3317 0.8613 -0.0078 0.1001  0.0409  47  ALA   A C   
326  O O   . ALA   A 41  ? 0.3613 0.3428 0.8388 -0.0083 0.0902  0.0377  47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.3297 0.3220 0.8993 -0.0053 0.0731  0.0502  47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.3517 0.3216 0.8530 -0.0091 0.1166  0.0395  48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.3669 0.3312 0.8237 -0.0115 0.1226  0.0339  48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.3350 0.3079 0.7716 -0.0115 0.1058  0.0323  48  GLN   A C   
331  O O   . GLN   A 42  ? 0.3209 0.2990 0.7772 -0.0102 0.0981  0.0353  48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.4233 0.3733 0.8772 -0.0137 0.1469  0.0319  48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.5350 0.4721 0.9589 -0.0165 0.1622  0.0283  48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.6465 0.5691 1.0475 -0.0202 0.1807  0.0240  48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 0.6851 0.5952 1.1027 -0.0210 0.2014  0.0243  48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.6730 0.5960 1.0363 -0.0227 0.1740  0.0196  48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.3194 0.2934 0.7182 -0.0128 0.1004  0.0281  49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.3111 0.2917 0.6872 -0.0131 0.0873  0.0261  49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.3071 0.2813 0.6653 -0.0155 0.0979  0.0229  49  GLY   A C   
340  O O   . GLY   A 43  ? 0.3178 0.2806 0.6717 -0.0178 0.1159  0.0211  49  GLY   A O   
341  N N   . CYS   A 44  ? 0.2973 0.2774 0.6431 -0.0155 0.0876  0.0220  50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.3034 0.2782 0.6345 -0.0179 0.0962  0.0191  50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.3046 0.2810 0.5994 -0.0201 0.0909  0.0147  50  CYS   A C   
344  O O   . CYS   A 44  ? 0.3104 0.2830 0.5928 -0.0225 0.0961  0.0121  50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.3052 0.2838 0.6587 -0.0162 0.0919  0.0227  50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.3468 0.3238 0.7493 -0.0138 0.0979  0.0290  50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.2833 0.2657 0.5636 -0.0194 0.0799  0.0142  51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.2855 0.2703 0.5361 -0.0213 0.0744  0.0109  51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.2990 0.2737 0.5274 -0.0254 0.0860  0.0077  51  ASP   A C   
350  O O   . ASP   A 45  ? 0.3061 0.2727 0.5392 -0.0262 0.0963  0.0083  51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.3042 0.2983 0.5494 -0.0189 0.0595  0.0117  51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.3494 0.3510 0.6087 -0.0159 0.0470  0.0142  51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.3517 0.3538 0.6151 -0.0159 0.0466  0.0150  51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.3027 0.3087 0.5680 -0.0138 0.0375  0.0155  51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.3088 0.2827 0.5133 -0.0285 0.0844  0.0046  52  THR   A N   
356  C CA  . THR   A 46  ? 0.3327 0.2967 0.5114 -0.0334 0.0917  0.0017  52  THR   A CA  
357  C C   . THR   A 46  ? 0.3246 0.2962 0.4859 -0.0336 0.0789  0.0019  52  THR   A C   
358  O O   . THR   A 46  ? 0.3160 0.2969 0.4770 -0.0322 0.0691  0.0016  52  THR   A O   
359  C CB  . THR   A 46  ? 0.3696 0.3254 0.5365 -0.0378 0.1000  -0.0022 52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.3954 0.3410 0.5773 -0.0382 0.1152  -0.0026 52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.3843 0.3310 0.5189 -0.0439 0.1018  -0.0056 52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.3156 0.2826 0.4636 -0.0352 0.0796  0.0027  53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.3038 0.2776 0.4381 -0.0353 0.0680  0.0037  53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.3068 0.2751 0.4168 -0.0411 0.0679  0.0011  53  ILE   A C   
365  O O   . ILE   A 47  ? 0.3311 0.2856 0.4262 -0.0459 0.0779  -0.0008 53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.3147 0.2862 0.4469 -0.0345 0.0678  0.0067  53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.3221 0.2973 0.4804 -0.0296 0.0692  0.0089  53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.3169 0.2968 0.4397 -0.0340 0.0551  0.0086  53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.3227 0.3114 0.4970 -0.0250 0.0570  0.0093  53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.2717 0.2494 0.3772 -0.0410 0.0569  0.0010  54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.2732 0.2470 0.3581 -0.0468 0.0543  -0.0009 54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.2792 0.2457 0.3449 -0.0504 0.0522  0.0013  54  ALA   A C   
373  O O   . ALA   A 48  ? 0.2825 0.2537 0.3537 -0.0472 0.0475  0.0051  54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.2658 0.2526 0.3559 -0.0451 0.0432  -0.0006 54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.3034 0.2576 0.3456 -0.0575 0.0550  -0.0008 55  ARG   A N   
376  C CA  . ARG   A 49  ? 0.3266 0.2723 0.3459 -0.0622 0.0510  0.0018  55  ARG   A CA  
377  C C   . ARG   A 49  ? 0.3486 0.2948 0.3530 -0.0681 0.0412  0.0003  55  ARG   A C   
378  O O   . ARG   A 49  ? 0.3768 0.3105 0.3631 -0.0746 0.0462  -0.0040 55  ARG   A O   
379  C CB  . ARG   A 49  ? 0.3548 0.2806 0.3566 -0.0663 0.0651  0.0004  55  ARG   A CB  
380  C CG  . ARG   A 49  ? 0.3702 0.2961 0.3923 -0.0604 0.0756  0.0018  55  ARG   A CG  
381  C CD  . ARG   A 49  ? 0.3916 0.3274 0.4262 -0.0552 0.0680  0.0074  55  ARG   A CD  
382  N NE  . ARG   A 49  ? 0.4249 0.3603 0.4805 -0.0503 0.0778  0.0083  55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.4185 0.3632 0.4922 -0.0449 0.0731  0.0120  55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.3743 0.3293 0.4479 -0.0432 0.0600  0.0151  55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.4005 0.3440 0.4942 -0.0412 0.0817  0.0126  55  ARG   A NH2 
386  N N   . CYS   A 50  ? 0.3394 0.3005 0.3547 -0.0656 0.0278  0.0035  56  CYS   A N   
387  C CA  . CYS   A 50  ? 0.3417 0.3074 0.3525 -0.0698 0.0178  0.0027  56  CYS   A CA  
388  C C   . CYS   A 50  ? 0.3442 0.3247 0.3680 -0.0667 0.0039  0.0082  56  CYS   A C   
389  O O   . CYS   A 50  ? 0.3437 0.3300 0.3787 -0.0612 0.0028  0.0121  56  CYS   A O   
390  C CB  . CYS   A 50  ? 0.3142 0.2858 0.3395 -0.0676 0.0228  -0.0018 56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.3172 0.3067 0.3734 -0.0574 0.0211  0.0003  56  CYS   A SG  
392  N N   A ASP   A 51  ? 0.3422 0.3288 0.3675 -0.0699 -0.0060 0.0085  57  ASP   A N   
393  N N   B ASP   A 51  ? 0.3526 0.3389 0.3774 -0.0701 -0.0058 0.0083  57  ASP   A N   
394  C CA  A ASP   A 51  ? 0.3389 0.3400 0.3818 -0.0665 -0.0173 0.0135  57  ASP   A CA  
395  C CA  B ASP   A 51  ? 0.3608 0.3609 0.4012 -0.0680 -0.0183 0.0131  57  ASP   A CA  
396  C C   A ASP   A 51  ? 0.3335 0.3467 0.3964 -0.0633 -0.0176 0.0112  57  ASP   A C   
397  C C   B ASP   A 51  ? 0.3453 0.3572 0.4053 -0.0650 -0.0179 0.0104  57  ASP   A C   
398  O O   A ASP   A 51  ? 0.3207 0.3443 0.3971 -0.0624 -0.0264 0.0145  57  ASP   A O   
399  O O   B ASP   A 51  ? 0.3362 0.3565 0.4062 -0.0661 -0.0270 0.0128  57  ASP   A O   
400  C CB  A ASP   A 51  ? 0.3644 0.3630 0.3956 -0.0728 -0.0308 0.0184  57  ASP   A CB  
401  C CB  B ASP   A 51  ? 0.4134 0.4084 0.4379 -0.0761 -0.0306 0.0161  57  ASP   A CB  
402  C CG  A ASP   A 51  ? 0.4209 0.4144 0.4396 -0.0811 -0.0366 0.0157  57  ASP   A CG  
403  C CG  B ASP   A 51  ? 0.5099 0.5154 0.5478 -0.0744 -0.0437 0.0238  57  ASP   A CG  
404  O OD1 A ASP   A 51  ? 0.4212 0.4121 0.4393 -0.0821 -0.0287 0.0095  57  ASP   A OD1 
405  O OD1 B ASP   A 51  ? 0.5278 0.5414 0.5822 -0.0671 -0.0418 0.0268  57  ASP   A OD1 
406  O OD2 A ASP   A 51  ? 0.4657 0.4566 0.4748 -0.0870 -0.0495 0.0200  57  ASP   A OD2 
407  O OD2 B ASP   A 51  ? 0.5547 0.5596 0.5868 -0.0806 -0.0562 0.0269  57  ASP   A OD2 
408  N N   . CYS   A 52  ? 0.3333 0.3449 0.3993 -0.0614 -0.0074 0.0060  58  CYS   A N   
409  C CA  . CYS   A 52  ? 0.3123 0.3329 0.3944 -0.0584 -0.0058 0.0039  58  CYS   A CA  
410  C C   . CYS   A 52  ? 0.2810 0.3147 0.3830 -0.0523 -0.0105 0.0076  58  CYS   A C   
411  O O   . CYS   A 52  ? 0.2507 0.2864 0.3571 -0.0480 -0.0108 0.0103  58  CYS   A O   
412  C CB  . CYS   A 52  ? 0.3087 0.3256 0.3933 -0.0554 0.0055  0.0000  58  CYS   A CB  
413  S SG  . CYS   A 52  ? 0.3155 0.3190 0.3847 -0.0622 0.0136  -0.0057 58  CYS   A SG  
414  N N   . GLN   A 53  ? 0.2655 0.3069 0.3795 -0.0521 -0.0131 0.0074  59  GLN   A N   
415  C CA  . GLN   A 53  ? 0.2565 0.3085 0.3894 -0.0464 -0.0147 0.0100  59  GLN   A CA  
416  C C   . GLN   A 53  ? 0.2467 0.3018 0.3885 -0.0430 -0.0076 0.0071  59  GLN   A C   
417  O O   . GLN   A 53  ? 0.2368 0.2989 0.3926 -0.0396 -0.0077 0.0086  59  GLN   A O   
418  C CB  . GLN   A 53  ? 0.2640 0.3228 0.4070 -0.0488 -0.0245 0.0144  59  GLN   A CB  
419  C CG  . GLN   A 53  ? 0.2863 0.3454 0.4285 -0.0484 -0.0312 0.0195  59  GLN   A CG  
420  C CD  . GLN   A 53  ? 0.3146 0.3821 0.4732 -0.0496 -0.0411 0.0249  59  GLN   A CD  
421  O OE1 . GLN   A 53  ? 0.3256 0.3912 0.4781 -0.0561 -0.0510 0.0277  59  GLN   A OE1 
422  N NE2 . GLN   A 53  ? 0.2642 0.3404 0.4442 -0.0438 -0.0386 0.0267  59  GLN   A NE2 
423  N N   . THR   A 54  ? 0.2371 0.2858 0.3705 -0.0443 -0.0012 0.0033  60  THR   A N   
424  C CA  . THR   A 54  ? 0.2209 0.2707 0.3602 -0.0414 0.0053  0.0013  60  THR   A CA  
425  C C   . THR   A 54  ? 0.1944 0.2375 0.3273 -0.0395 0.0113  -0.0005 60  THR   A C   
426  O O   . THR   A 54  ? 0.1995 0.2358 0.3228 -0.0425 0.0128  -0.0017 60  THR   A O   
427  C CB  . THR   A 54  ? 0.2599 0.3098 0.4010 -0.0458 0.0060  -0.0005 60  THR   A CB  
428  O OG1 . THR   A 54  ? 0.2949 0.3364 0.4229 -0.0514 0.0074  -0.0034 60  THR   A OG1 
429  C CG2 . THR   A 54  ? 0.2557 0.3127 0.4068 -0.0483 -0.0010 0.0019  60  THR   A CG2 
430  N N   . GLY   A 55  ? 0.1694 0.2136 0.3078 -0.0347 0.0149  -0.0005 61  GLY   A N   
431  C CA  . GLY   A 55  ? 0.1488 0.1878 0.2855 -0.0325 0.0190  -0.0011 61  GLY   A CA  
432  C C   . GLY   A 55  ? 0.1483 0.1888 0.2900 -0.0279 0.0203  -0.0003 61  GLY   A C   
433  O O   . GLY   A 55  ? 0.1824 0.2260 0.3268 -0.0272 0.0207  0.0000  61  GLY   A O   
434  N N   . VAL   A 56  ? 0.1523 0.1893 0.2949 -0.0253 0.0213  0.0002  62  VAL   A N   
435  C CA  . VAL   A 56  ? 0.1632 0.1990 0.3071 -0.0216 0.0210  0.0014  62  VAL   A CA  
436  C C   . VAL   A 56  ? 0.1947 0.2294 0.3399 -0.0186 0.0173  0.0022  62  VAL   A C   
437  O O   . VAL   A 56  ? 0.2235 0.2566 0.3714 -0.0192 0.0173  0.0022  62  VAL   A O   
438  C CB  . VAL   A 56  ? 0.1884 0.2199 0.3343 -0.0223 0.0246  0.0020  62  VAL   A CB  
439  C CG1 . VAL   A 56  ? 0.1952 0.2241 0.3402 -0.0191 0.0228  0.0043  62  VAL   A CG1 
440  C CG2 . VAL   A 56  ? 0.2071 0.2392 0.3524 -0.0257 0.0286  0.0007  62  VAL   A CG2 
441  N N   . TYR   A 57  ? 0.1872 0.2214 0.3299 -0.0156 0.0147  0.0025  63  TYR   A N   
442  C CA  . TYR   A 57  ? 0.1745 0.2065 0.3182 -0.0133 0.0105  0.0028  63  TYR   A CA  
443  C C   . TYR   A 57  ? 0.1828 0.2094 0.3221 -0.0117 0.0077  0.0038  63  TYR   A C   
444  O O   . TYR   A 57  ? 0.1907 0.2155 0.3241 -0.0117 0.0099  0.0042  63  TYR   A O   
445  C CB  . TYR   A 57  ? 0.1807 0.2154 0.3240 -0.0120 0.0090  0.0017  63  TYR   A CB  
446  C CG  . TYR   A 57  ? 0.2060 0.2389 0.3437 -0.0102 0.0100  0.0008  63  TYR   A CG  
447  C CD1 . TYR   A 57  ? 0.2155 0.2508 0.3527 -0.0109 0.0142  0.0007  63  TYR   A CD1 
448  C CD2 . TYR   A 57  ? 0.2235 0.2511 0.3562 -0.0082 0.0072  -0.0002 63  TYR   A CD2 
449  C CE1 . TYR   A 57  ? 0.2338 0.2663 0.3668 -0.0092 0.0174  -0.0002 63  TYR   A CE1 
450  C CE2 . TYR   A 57  ? 0.2413 0.2648 0.3664 -0.0069 0.0100  -0.0017 63  TYR   A CE2 
451  C CZ  . TYR   A 57  ? 0.2442 0.2699 0.3696 -0.0072 0.0160  -0.0016 63  TYR   A CZ  
452  O OH  . TYR   A 57  ? 0.2465 0.2669 0.3653 -0.0059 0.0211  -0.0030 63  TYR   A OH  
453  N N   . TYR   A 58  ? 0.1890 0.2125 0.3311 -0.0106 0.0027  0.0046  64  TYR   A N   
454  C CA  . TYR   A 58  ? 0.2009 0.2180 0.3374 -0.0097 -0.0026 0.0061  64  TYR   A CA  
455  C C   . TYR   A 58  ? 0.2151 0.2285 0.3418 -0.0085 -0.0052 0.0037  64  TYR   A C   
456  O O   . TYR   A 58  ? 0.2044 0.2193 0.3360 -0.0079 -0.0074 0.0023  64  TYR   A O   
457  C CB  . TYR   A 58  ? 0.1957 0.2112 0.3432 -0.0096 -0.0082 0.0084  64  TYR   A CB  
458  C CG  . TYR   A 58  ? 0.2196 0.2279 0.3608 -0.0093 -0.0162 0.0106  64  TYR   A CG  
459  C CD1 . TYR   A 58  ? 0.2373 0.2415 0.3695 -0.0097 -0.0159 0.0129  64  TYR   A CD1 
460  C CD2 . TYR   A 58  ? 0.2420 0.2467 0.3851 -0.0091 -0.0247 0.0107  64  TYR   A CD2 
461  C CE1 . TYR   A 58  ? 0.2499 0.2458 0.3731 -0.0100 -0.0243 0.0158  64  TYR   A CE1 
462  C CE2 . TYR   A 58  ? 0.2598 0.2564 0.3948 -0.0098 -0.0341 0.0131  64  TYR   A CE2 
463  C CZ  . TYR   A 58  ? 0.2729 0.2648 0.3965 -0.0102 -0.0340 0.0157  64  TYR   A CZ  
464  O OH  . TYR   A 58  ? 0.3114 0.2937 0.4236 -0.0113 -0.0442 0.0187  64  TYR   A OH  
465  N N   . CYS   A 59  ? 0.2315 0.2381 0.3439 -0.0083 -0.0053 0.0036  65  CYS   A N   
466  C CA  . CYS   A 59  ? 0.2442 0.2439 0.3439 -0.0076 -0.0062 0.0008  65  CYS   A CA  
467  C C   . CYS   A 59  ? 0.2533 0.2421 0.3408 -0.0084 -0.0148 0.0023  65  CYS   A C   
468  O O   . CYS   A 59  ? 0.2586 0.2414 0.3349 -0.0091 -0.0144 0.0044  65  CYS   A O   
469  C CB  . CYS   A 59  ? 0.2690 0.2678 0.3606 -0.0071 0.0026  -0.0006 65  CYS   A CB  
470  S SG  . CYS   A 59  ? 0.2945 0.2804 0.3665 -0.0066 0.0050  -0.0043 65  CYS   A SG  
471  N N   . SER   A 60  ? 0.2428 0.2290 0.3335 -0.0088 -0.0231 0.0017  66  SER   A N   
472  C CA  . SER   A 60  ? 0.2634 0.2397 0.3447 -0.0103 -0.0339 0.0037  66  SER   A CA  
473  C C   . SER   A 60  ? 0.2839 0.2461 0.3380 -0.0114 -0.0339 0.0015  66  SER   A C   
474  O O   . SER   A 60  ? 0.2998 0.2526 0.3409 -0.0132 -0.0414 0.0046  66  SER   A O   
475  C CB  . SER   A 60  ? 0.2936 0.2703 0.3865 -0.0108 -0.0430 0.0031  66  SER   A CB  
476  O OG  . SER   A 60  ? 0.3455 0.3202 0.4336 -0.0104 -0.0406 -0.0021 66  SER   A OG  
477  N N   . SER   A 61  ? 0.2851 0.2449 0.3302 -0.0106 -0.0253 -0.0034 67  SER   A N   
478  C CA  . SER   A 61  ? 0.2952 0.2395 0.3130 -0.0118 -0.0219 -0.0062 67  SER   A CA  
479  C C   . SER   A 61  ? 0.3090 0.2496 0.3153 -0.0118 -0.0147 -0.0034 67  SER   A C   
480  O O   . SER   A 61  ? 0.3292 0.2547 0.3103 -0.0131 -0.0115 -0.0048 67  SER   A O   
481  C CB  . SER   A 61  ? 0.2965 0.2388 0.3117 -0.0106 -0.0129 -0.0121 67  SER   A CB  
482  O OG  . SER   A 61  ? 0.2979 0.2521 0.3283 -0.0083 -0.0018 -0.0120 67  SER   A OG  
483  N N   . ARG   A 62  ? 0.2902 0.2426 0.3132 -0.0107 -0.0121 0.0005  68  ARG   A N   
484  C CA  . ARG   A 62  ? 0.2903 0.2396 0.3052 -0.0109 -0.0061 0.0038  68  ARG   A CA  
485  C C   . ARG   A 62  ? 0.2934 0.2470 0.3184 -0.0115 -0.0134 0.0099  68  ARG   A C   
486  O O   . ARG   A 62  ? 0.2938 0.2461 0.3156 -0.0115 -0.0087 0.0133  68  ARG   A O   
487  C CB  . ARG   A 62  ? 0.3048 0.2643 0.3323 -0.0093 0.0068  0.0023  68  ARG   A CB  
488  C CG  . ARG   A 62  ? 0.3222 0.2776 0.3432 -0.0083 0.0167  -0.0025 68  ARG   A CG  
489  C CD  . ARG   A 62  ? 0.3657 0.3053 0.3622 -0.0091 0.0243  -0.0028 68  ARG   A CD  
490  N NE  . ARG   A 62  ? 0.3942 0.3288 0.3868 -0.0081 0.0355  -0.0076 68  ARG   A NE  
491  C CZ  . ARG   A 62  ? 0.4245 0.3483 0.4037 -0.0086 0.0346  -0.0121 68  ARG   A CZ  
492  N NH1 . ARG   A 62  ? 0.4235 0.3389 0.3888 -0.0106 0.0220  -0.0123 68  ARG   A NH1 
493  N NH2 . ARG   A 62  ? 0.4301 0.3500 0.4098 -0.0074 0.0465  -0.0163 68  ARG   A NH2 
494  N N   . ARG   A 63  ? 0.2866 0.2465 0.3282 -0.0116 -0.0231 0.0114  69  ARG   A N   
495  C CA  . ARG   A 63  ? 0.2851 0.2503 0.3429 -0.0118 -0.0285 0.0171  69  ARG   A CA  
496  C C   . ARG   A 63  ? 0.2779 0.2517 0.3464 -0.0109 -0.0178 0.0181  69  ARG   A C   
497  O O   . ARG   A 63  ? 0.2859 0.2576 0.3545 -0.0113 -0.0175 0.0227  69  ARG   A O   
498  C CB  . ARG   A 63  ? 0.3104 0.2637 0.3541 -0.0134 -0.0388 0.0226  69  ARG   A CB  
499  C CG  . ARG   A 63  ? 0.3431 0.2892 0.3818 -0.0151 -0.0529 0.0226  69  ARG   A CG  
500  C CD  . ARG   A 63  ? 0.4056 0.3379 0.4260 -0.0174 -0.0640 0.0285  69  ARG   A CD  
501  N NE  . ARG   A 63  ? 0.4481 0.3706 0.4579 -0.0201 -0.0785 0.0279  69  ARG   A NE  
502  C CZ  . ARG   A 63  ? 0.4882 0.3929 0.4675 -0.0232 -0.0870 0.0291  69  ARG   A CZ  
503  N NH1 . ARG   A 63  ? 0.4981 0.3926 0.4537 -0.0237 -0.0810 0.0313  69  ARG   A NH1 
504  N NH2 . ARG   A 63  ? 0.4853 0.3809 0.4556 -0.0262 -0.1010 0.0277  69  ARG   A NH2 
505  N N   . LYS   A 64  ? 0.2578 0.2408 0.3356 -0.0101 -0.0095 0.0139  70  LYS   A N   
506  C CA  . LYS   A 64  ? 0.2526 0.2424 0.3383 -0.0101 0.0000  0.0139  70  LYS   A CA  
507  C C   . LYS   A 64  ? 0.2347 0.2355 0.3367 -0.0101 0.0032  0.0112  70  LYS   A C   
508  O O   . LYS   A 64  ? 0.2420 0.2448 0.3458 -0.0095 0.0012  0.0084  70  LYS   A O   
509  C CB  . LYS   A 64  ? 0.3094 0.2949 0.3812 -0.0099 0.0086  0.0120  70  LYS   A CB  
510  C CG  . LYS   A 64  ? 0.4416 0.4182 0.5005 -0.0103 0.0105  0.0158  70  LYS   A CG  
511  C CD  . LYS   A 64  ? 0.5399 0.5180 0.5983 -0.0103 0.0224  0.0149  70  LYS   A CD  
512  C CE  . LYS   A 64  ? 0.6387 0.6053 0.6808 -0.0107 0.0250  0.0189  70  LYS   A CE  
513  N NZ  . LYS   A 64  ? 0.6908 0.6425 0.7089 -0.0110 0.0188  0.0198  70  LYS   A NZ  
514  N N   . HIS   A 65  ? 0.2151 0.2215 0.3275 -0.0111 0.0081  0.0120  71  HIS   A N   
515  C CA  . HIS   A 65  ? 0.2118 0.2267 0.3365 -0.0120 0.0113  0.0096  71  HIS   A CA  
516  C C   . HIS   A 65  ? 0.2222 0.2406 0.3453 -0.0129 0.0183  0.0077  71  HIS   A C   
517  O O   . HIS   A 65  ? 0.2247 0.2419 0.3468 -0.0138 0.0226  0.0091  71  HIS   A O   
518  C CB  . HIS   A 65  ? 0.2166 0.2328 0.3535 -0.0133 0.0122  0.0116  71  HIS   A CB  
519  C CG  . HIS   A 65  ? 0.2190 0.2320 0.3624 -0.0123 0.0054  0.0145  71  HIS   A CG  
520  N ND1 . HIS   A 65  ? 0.2301 0.2456 0.3849 -0.0124 0.0041  0.0138  71  HIS   A ND1 
521  C CD2 . HIS   A 65  ? 0.2284 0.2353 0.3681 -0.0115 -0.0010 0.0184  71  HIS   A CD2 
522  C CE1 . HIS   A 65  ? 0.2356 0.2477 0.3969 -0.0115 -0.0028 0.0173  71  HIS   A CE1 
523  N NE2 . HIS   A 65  ? 0.2348 0.2416 0.3868 -0.0111 -0.0072 0.0203  71  HIS   A NE2 
524  N N   . TYR   A 66  ? 0.2041 0.2267 0.3282 -0.0127 0.0193  0.0052  72  TYR   A N   
525  C CA  . TYR   A 66  ? 0.2031 0.2296 0.3291 -0.0135 0.0247  0.0041  72  TYR   A CA  
526  C C   . TYR   A 66  ? 0.2054 0.2394 0.3410 -0.0162 0.0251  0.0030  72  TYR   A C   
527  O O   . TYR   A 66  ? 0.2009 0.2375 0.3394 -0.0164 0.0218  0.0023  72  TYR   A O   
528  C CB  . TYR   A 66  ? 0.2067 0.2323 0.3292 -0.0115 0.0257  0.0026  72  TYR   A CB  
529  C CG  . TYR   A 66  ? 0.2327 0.2484 0.3413 -0.0098 0.0271  0.0029  72  TYR   A CG  
530  C CD1 . TYR   A 66  ? 0.2573 0.2686 0.3601 -0.0098 0.0338  0.0038  72  TYR   A CD1 
531  C CD2 . TYR   A 66  ? 0.2561 0.2656 0.3561 -0.0085 0.0220  0.0020  72  TYR   A CD2 
532  C CE1 . TYR   A 66  ? 0.2882 0.2878 0.3742 -0.0087 0.0359  0.0040  72  TYR   A CE1 
533  C CE2 . TYR   A 66  ? 0.2785 0.2766 0.3618 -0.0078 0.0228  0.0018  72  TYR   A CE2 
534  C CZ  . TYR   A 66  ? 0.3084 0.3009 0.3833 -0.0079 0.0302  0.0027  72  TYR   A CZ  
535  O OH  . TYR   A 66  ? 0.3513 0.3298 0.4054 -0.0078 0.0313  0.0026  72  TYR   A OH  
536  N N   . PRO   A 67  ? 0.2112 0.2475 0.3507 -0.0185 0.0290  0.0030  73  PRO   A N   
537  C CA  . PRO   A 67  ? 0.2089 0.2507 0.3546 -0.0220 0.0280  0.0018  73  PRO   A CA  
538  C C   . PRO   A 67  ? 0.2170 0.2640 0.3678 -0.0213 0.0266  0.0018  73  PRO   A C   
539  O O   . PRO   A 67  ? 0.2209 0.2678 0.3736 -0.0194 0.0303  0.0023  73  PRO   A O   
540  C CB  . PRO   A 67  ? 0.2275 0.2694 0.3763 -0.0248 0.0323  0.0016  73  PRO   A CB  
541  C CG  . PRO   A 67  ? 0.2426 0.2801 0.3879 -0.0223 0.0363  0.0032  73  PRO   A CG  
542  C CD  . PRO   A 67  ? 0.2204 0.2535 0.3579 -0.0186 0.0340  0.0042  73  PRO   A CD  
543  N N   . VAL   A 68  ? 0.2028 0.2534 0.3562 -0.0226 0.0221  0.0017  74  VAL   A N   
544  C CA  . VAL   A 68  ? 0.2052 0.2609 0.3661 -0.0218 0.0199  0.0028  74  VAL   A CA  
545  C C   . VAL   A 68  ? 0.1945 0.2546 0.3592 -0.0260 0.0145  0.0036  74  VAL   A C   
546  O O   . VAL   A 68  ? 0.1897 0.2468 0.3472 -0.0292 0.0127  0.0027  74  VAL   A O   
547  C CB  . VAL   A 68  ? 0.2307 0.2845 0.3892 -0.0180 0.0184  0.0028  74  VAL   A CB  
548  C CG1 . VAL   A 68  ? 0.2550 0.3034 0.4083 -0.0144 0.0228  0.0020  74  VAL   A CG1 
549  C CG2 . VAL   A 68  ? 0.2277 0.2789 0.3806 -0.0186 0.0150  0.0025  74  VAL   A CG2 
550  N N   . SER   A 69  ? 0.1813 0.2472 0.3570 -0.0261 0.0120  0.0057  75  SER   A N   
551  C CA  . SER   A 69  ? 0.1896 0.2594 0.3692 -0.0298 0.0044  0.0078  75  SER   A CA  
552  C C   . SER   A 69  ? 0.1825 0.2534 0.3648 -0.0261 0.0023  0.0097  75  SER   A C   
553  O O   . SER   A 69  ? 0.1785 0.2502 0.3676 -0.0217 0.0065  0.0098  75  SER   A O   
554  C CB  . SER   A 69  ? 0.2043 0.2807 0.3996 -0.0319 0.0021  0.0101  75  SER   A CB  
555  O OG  . SER   A 69  ? 0.2770 0.3525 0.4715 -0.0356 0.0039  0.0083  75  SER   A OG  
556  N N   . PHE   A 70  ? 0.1686 0.2382 0.3450 -0.0280 -0.0032 0.0111  76  PHE   A N   
557  C CA  . PHE   A 70  ? 0.1696 0.2400 0.3495 -0.0246 -0.0050 0.0132  76  PHE   A CA  
558  C C   . PHE   A 70  ? 0.1871 0.2605 0.3706 -0.0275 -0.0133 0.0177  76  PHE   A C   
559  O O   . PHE   A 70  ? 0.2005 0.2728 0.3773 -0.0329 -0.0183 0.0185  76  PHE   A O   
560  C CB  . PHE   A 70  ? 0.1837 0.2480 0.3530 -0.0223 -0.0021 0.0109  76  PHE   A CB  
561  C CG  . PHE   A 70  ? 0.1883 0.2470 0.3447 -0.0261 -0.0023 0.0097  76  PHE   A CG  
562  C CD1 . PHE   A 70  ? 0.2025 0.2578 0.3531 -0.0277 0.0019  0.0068  76  PHE   A CD1 
563  C CD2 . PHE   A 70  ? 0.2060 0.2620 0.3560 -0.0286 -0.0060 0.0118  76  PHE   A CD2 
564  C CE1 . PHE   A 70  ? 0.2232 0.2722 0.3633 -0.0312 0.0035  0.0053  76  PHE   A CE1 
565  C CE2 . PHE   A 70  ? 0.2229 0.2715 0.3598 -0.0323 -0.0039 0.0102  76  PHE   A CE2 
566  C CZ  . PHE   A 70  ? 0.2143 0.2596 0.3471 -0.0337 0.0011  0.0067  76  PHE   A CZ  
567  N N   . SER   A 71  ? 0.1903 0.2667 0.3842 -0.0241 -0.0150 0.0208  77  SER   A N   
568  C CA  . SER   A 71  ? 0.2028 0.2821 0.4016 -0.0266 -0.0239 0.0265  77  SER   A CA  
569  C C   . SER   A 71  ? 0.2282 0.3004 0.4095 -0.0287 -0.0264 0.0271  77  SER   A C   
570  O O   . SER   A 71  ? 0.2405 0.3074 0.4123 -0.0268 -0.0204 0.0234  77  SER   A O   
571  C CB  . SER   A 71  ? 0.2054 0.2900 0.4241 -0.0218 -0.0235 0.0300  77  SER   A CB  
572  O OG  . SER   A 71  ? 0.2269 0.3076 0.4420 -0.0174 -0.0183 0.0278  77  SER   A OG  
573  N N   . LYS   A 72  ? 0.2299 0.3013 0.4073 -0.0328 -0.0352 0.0322  78  LYS   A N   
574  C CA  . LYS   A 72  ? 0.2482 0.3115 0.4083 -0.0350 -0.0366 0.0335  78  LYS   A CA  
575  C C   . LYS   A 72  ? 0.2446 0.3080 0.4116 -0.0296 -0.0338 0.0354  78  LYS   A C   
576  O O   . LYS   A 72  ? 0.2405 0.3104 0.4257 -0.0255 -0.0346 0.0378  78  LYS   A O   
577  C CB  . LYS   A 72  ? 0.2963 0.3574 0.4484 -0.0415 -0.0480 0.0392  78  LYS   A CB  
578  C CG  . LYS   A 72  ? 0.3728 0.4298 0.5114 -0.0483 -0.0502 0.0359  78  LYS   A CG  
579  C CD  . LYS   A 72  ? 0.4514 0.5019 0.5739 -0.0563 -0.0616 0.0403  78  LYS   A CD  
580  C CE  . LYS   A 72  ? 0.5215 0.5665 0.6300 -0.0630 -0.0619 0.0353  78  LYS   A CE  
581  N NZ  . LYS   A 72  ? 0.5686 0.6053 0.6583 -0.0721 -0.0740 0.0387  78  LYS   A NZ  
582  N N   . PRO   A 73  ? 0.2521 0.3075 0.4057 -0.0296 -0.0299 0.0343  79  PRO   A N   
583  C CA  . PRO   A 73  ? 0.2524 0.3076 0.4140 -0.0246 -0.0271 0.0357  79  PRO   A CA  
584  C C   . PRO   A 73  ? 0.2509 0.3106 0.4251 -0.0234 -0.0339 0.0429  79  PRO   A C   
585  O O   . PRO   A 73  ? 0.2543 0.3119 0.4212 -0.0277 -0.0417 0.0486  79  PRO   A O   
586  C CB  . PRO   A 73  ? 0.2824 0.3277 0.4277 -0.0265 -0.0226 0.0345  79  PRO   A CB  
587  C CG  . PRO   A 73  ? 0.3002 0.3407 0.4314 -0.0307 -0.0196 0.0302  79  PRO   A CG  
588  C CD  . PRO   A 73  ? 0.2649 0.3106 0.3979 -0.0340 -0.0262 0.0312  79  PRO   A CD  
589  N N   A SER   A 74  ? 0.2412 0.3062 0.4338 -0.0179 -0.0313 0.0428  80  SER   A N   
590  N N   B SER   A 74  ? 0.2414 0.3065 0.4341 -0.0179 -0.0313 0.0428  80  SER   A N   
591  C CA  A SER   A 74  ? 0.2446 0.3145 0.4541 -0.0160 -0.0367 0.0497  80  SER   A CA  
592  C CA  B SER   A 74  ? 0.2449 0.3149 0.4547 -0.0159 -0.0366 0.0497  80  SER   A CA  
593  C C   A SER   A 74  ? 0.2472 0.3168 0.4690 -0.0102 -0.0311 0.0489  80  SER   A C   
594  C C   B SER   A 74  ? 0.2481 0.3181 0.4709 -0.0101 -0.0309 0.0487  80  SER   A C   
595  O O   A SER   A 74  ? 0.2575 0.3236 0.4750 -0.0079 -0.0241 0.0426  80  SER   A O   
596  O O   B SER   A 74  ? 0.2585 0.3256 0.4783 -0.0075 -0.0237 0.0421  80  SER   A O   
597  C CB  A SER   A 74  ? 0.2544 0.3329 0.4815 -0.0158 -0.0397 0.0513  80  SER   A CB  
598  C CB  B SER   A 74  ? 0.2544 0.3328 0.4809 -0.0161 -0.0402 0.0516  80  SER   A CB  
599  O OG  A SER   A 74  ? 0.2988 0.3779 0.5171 -0.0204 -0.0425 0.0494  80  SER   A OG  
600  O OG  B SER   A 74  ? 0.2979 0.3764 0.5145 -0.0221 -0.0471 0.0530  80  SER   A OG  
601  N N   . LEU   A 75  ? 0.2374 0.3106 0.4758 -0.0081 -0.0348 0.0554  81  LEU   A N   
602  C CA  . LEU   A 75  ? 0.2443 0.3171 0.4970 -0.0029 -0.0296 0.0549  81  LEU   A CA  
603  C C   . LEU   A 75  ? 0.2562 0.3344 0.5276 0.0004  -0.0251 0.0520  81  LEU   A C   
604  O O   . LEU   A 75  ? 0.2623 0.3469 0.5484 -0.0003 -0.0295 0.0571  81  LEU   A O   
605  C CB  . LEU   A 75  ? 0.2393 0.3127 0.5009 -0.0028 -0.0361 0.0645  81  LEU   A CB  
606  C CG  . LEU   A 75  ? 0.2625 0.3338 0.5373 0.0019  -0.0313 0.0653  81  LEU   A CG  
607  C CD1 . LEU   A 75  ? 0.2698 0.3337 0.5313 0.0026  -0.0248 0.0589  81  LEU   A CD1 
608  C CD2 . LEU   A 75  ? 0.2715 0.3430 0.5538 0.0014  -0.0386 0.0763  81  LEU   A CD2 
609  N N   . ILE   A 76  ? 0.2518 0.3266 0.5213 0.0032  -0.0163 0.0438  82  ILE   A N   
610  C CA  . ILE   A 76  ? 0.2653 0.3418 0.5461 0.0058  -0.0096 0.0396  82  ILE   A CA  
611  C C   . ILE   A 76  ? 0.2664 0.3376 0.5541 0.0100  -0.0018 0.0351  82  ILE   A C   
612  O O   . ILE   A 76  ? 0.2613 0.3264 0.5374 0.0103  -0.0004 0.0310  82  ILE   A O   
613  C CB  . ILE   A 76  ? 0.2896 0.3638 0.5532 0.0037  -0.0067 0.0329  82  ILE   A CB  
614  C CG1 . ILE   A 76  ? 0.3211 0.3993 0.5768 -0.0010 -0.0137 0.0362  82  ILE   A CG1 
615  C CG2 . ILE   A 76  ? 0.2898 0.3624 0.5589 0.0062  0.0022  0.0274  82  ILE   A CG2 
616  C CD1 . ILE   A 76  ? 0.3446 0.4298 0.6144 -0.0022 -0.0159 0.0396  82  ILE   A CD1 
617  N N   . PHE   A 77  ? 0.2578 0.3304 0.5649 0.0130  0.0041  0.0354  83  PHE   A N   
618  C CA  . PHE   A 77  ? 0.2574 0.3227 0.5694 0.0165  0.0129  0.0300  83  PHE   A CA  
619  C C   . PHE   A 77  ? 0.2544 0.3115 0.5470 0.0161  0.0193  0.0202  83  PHE   A C   
620  O O   . PHE   A 77  ? 0.2624 0.3203 0.5501 0.0151  0.0219  0.0182  83  PHE   A O   
621  C CB  . PHE   A 77  ? 0.2605 0.3281 0.5992 0.0198  0.0192  0.0329  83  PHE   A CB  
622  C CG  . PHE   A 77  ? 0.2845 0.3433 0.6286 0.0230  0.0279  0.0280  83  PHE   A CG  
623  C CD1 . PHE   A 77  ? 0.2963 0.3539 0.6451 0.0240  0.0244  0.0309  83  PHE   A CD1 
624  C CD2 . PHE   A 77  ? 0.3071 0.3571 0.6489 0.0245  0.0399  0.0200  83  PHE   A CD2 
625  C CE1 . PHE   A 77  ? 0.3111 0.3599 0.6645 0.0265  0.0323  0.0257  83  PHE   A CE1 
626  C CE2 . PHE   A 77  ? 0.3223 0.3622 0.6664 0.0268  0.0479  0.0146  83  PHE   A CE2 
627  C CZ  . PHE   A 77  ? 0.3166 0.3563 0.6671 0.0277  0.0438  0.0172  83  PHE   A CZ  
628  N N   . VAL   A 78  ? 0.2416 0.2902 0.5234 0.0167  0.0211  0.0146  84  VAL   A N   
629  C CA  . VAL   A 78  ? 0.2529 0.2925 0.5146 0.0157  0.0245  0.0061  84  VAL   A CA  
630  C C   . VAL   A 78  ? 0.2718 0.3006 0.5340 0.0176  0.0320  -0.0002 84  VAL   A C   
631  O O   . VAL   A 78  ? 0.2658 0.2924 0.5350 0.0187  0.0308  0.0001  84  VAL   A O   
632  C CB  . VAL   A 78  ? 0.2497 0.2885 0.4955 0.0132  0.0170  0.0052  84  VAL   A CB  
633  C CG1 . VAL   A 78  ? 0.2667 0.2958 0.4937 0.0121  0.0186  -0.0026 84  VAL   A CG1 
634  C CG2 . VAL   A 78  ? 0.2333 0.2803 0.4758 0.0108  0.0111  0.0104  84  VAL   A CG2 
635  N N   . GLU   A 79  ? 0.2880 0.3086 0.5419 0.0178  0.0403  -0.0061 85  GLU   A N   
636  C CA  . GLU   A 79  ? 0.3072 0.3144 0.5574 0.0189  0.0490  -0.0133 85  GLU   A CA  
637  C C   . GLU   A 79  ? 0.3200 0.3182 0.5550 0.0173  0.0438  -0.0187 85  GLU   A C   
638  O O   . GLU   A 79  ? 0.3155 0.3166 0.5396 0.0152  0.0349  -0.0179 85  GLU   A O   
639  C CB  . GLU   A 79  ? 0.3516 0.3493 0.5893 0.0186  0.0591  -0.0187 85  GLU   A CB  
640  C CG  . GLU   A 79  ? 0.4187 0.4236 0.6768 0.0206  0.0668  -0.0139 85  GLU   A CG  
641  C CD  . GLU   A 79  ? 0.5082 0.5139 0.7930 0.0238  0.0737  -0.0115 85  GLU   A CD  
642  O OE1 . GLU   A 79  ? 0.5182 0.5106 0.7988 0.0245  0.0819  -0.0180 85  GLU   A OE1 
643  O OE2 . GLU   A 79  ? 0.5296 0.5487 0.8397 0.0253  0.0704  -0.0029 85  GLU   A OE2 
644  N N   . ALA   A 80  ? 0.3252 0.3121 0.5610 0.0180  0.0498  -0.0242 86  ALA   A N   
645  C CA  . ALA   A 80  ? 0.3399 0.3174 0.5629 0.0159  0.0443  -0.0298 86  ALA   A CA  
646  C C   . ALA   A 80  ? 0.3527 0.3215 0.5478 0.0125  0.0399  -0.0352 86  ALA   A C   
647  O O   . ALA   A 80  ? 0.3541 0.3176 0.5362 0.0119  0.0457  -0.0376 86  ALA   A O   
648  C CB  . ALA   A 80  ? 0.3394 0.3038 0.5660 0.0168  0.0528  -0.0361 86  ALA   A CB  
649  N N   . SER   A 81  ? 0.3506 0.3185 0.5387 0.0102  0.0295  -0.0361 87  SER   A N   
650  C CA  . SER   A 81  ? 0.3613 0.3216 0.5264 0.0068  0.0226  -0.0399 87  SER   A CA  
651  C C   . SER   A 81  ? 0.3807 0.3305 0.5396 0.0042  0.0154  -0.0452 87  SER   A C   
652  O O   . SER   A 81  ? 0.3801 0.3282 0.5521 0.0051  0.0173  -0.0465 87  SER   A O   
653  C CB  . SER   A 81  ? 0.3433 0.3166 0.5109 0.0064  0.0151  -0.0334 87  SER   A CB  
654  O OG  . SER   A 81  ? 0.3375 0.3184 0.5193 0.0065  0.0081  -0.0296 87  SER   A OG  
655  N N   . GLU   A 82  ? 0.3985 0.3416 0.5392 0.0006  0.0063  -0.0476 88  GLU   A N   
656  C CA  . GLU   A 82  ? 0.4123 0.3464 0.5484 -0.0026 -0.0034 -0.0518 88  GLU   A CA  
657  C C   . GLU   A 82  ? 0.3934 0.3396 0.5544 -0.0014 -0.0094 -0.0467 88  GLU   A C   
658  O O   . GLU   A 82  ? 0.3986 0.3388 0.5648 -0.0031 -0.0141 -0.0500 88  GLU   A O   
659  C CB  . GLU   A 82  ? 0.4703 0.3975 0.5854 -0.0065 -0.0137 -0.0530 88  GLU   A CB  
660  C CG  . GLU   A 82  ? 0.5776 0.4945 0.6880 -0.0106 -0.0258 -0.0571 88  GLU   A CG  
661  C CD  . GLU   A 82  ? 0.6871 0.5990 0.7825 -0.0145 -0.0390 -0.0562 88  GLU   A CD  
662  O OE1 . GLU   A 82  ? 0.6938 0.6051 0.7740 -0.0146 -0.0376 -0.0543 88  GLU   A OE1 
663  O OE2 . GLU   A 82  ? 0.7216 0.6302 0.8224 -0.0176 -0.0512 -0.0571 88  GLU   A OE2 
664  N N   . TYR   A 83  ? 0.3739 0.3357 0.5496 0.0012  -0.0082 -0.0390 89  TYR   A N   
665  C CA  . TYR   A 83  ? 0.3682 0.3397 0.5638 0.0019  -0.0126 -0.0337 89  TYR   A CA  
666  C C   . TYR   A 83  ? 0.3426 0.3231 0.5573 0.0053  -0.0060 -0.0286 89  TYR   A C   
667  O O   . TYR   A 83  ? 0.3377 0.3228 0.5676 0.0057  -0.0084 -0.0250 89  TYR   A O   
668  C CB  . TYR   A 83  ? 0.3819 0.3617 0.5769 0.0011  -0.0179 -0.0286 89  TYR   A CB  
669  C CG  . TYR   A 83  ? 0.4268 0.3989 0.6079 -0.0023 -0.0268 -0.0318 89  TYR   A CG  
670  C CD1 . TYR   A 83  ? 0.4473 0.4162 0.6362 -0.0046 -0.0361 -0.0324 89  TYR   A CD1 
671  C CD2 . TYR   A 83  ? 0.4667 0.4343 0.6280 -0.0033 -0.0265 -0.0333 89  TYR   A CD2 
672  C CE1 . TYR   A 83  ? 0.4751 0.4369 0.6528 -0.0080 -0.0463 -0.0342 89  TYR   A CE1 
673  C CE2 . TYR   A 83  ? 0.4973 0.4573 0.6453 -0.0066 -0.0359 -0.0350 89  TYR   A CE2 
674  C CZ  . TYR   A 83  ? 0.5130 0.4702 0.6694 -0.0090 -0.0465 -0.0352 89  TYR   A CZ  
675  O OH  . TYR   A 83  ? 0.5576 0.5075 0.7023 -0.0125 -0.0575 -0.0357 89  TYR   A OH  
676  N N   . TYR   A 84  ? 0.3130 0.2964 0.5284 0.0076  0.0019  -0.0272 90  TYR   A N   
677  C CA  . TYR   A 84  ? 0.2833 0.2748 0.5174 0.0106  0.0067  -0.0214 90  TYR   A CA  
678  C C   . TYR   A 84  ? 0.2969 0.2836 0.5338 0.0126  0.0157  -0.0241 90  TYR   A C   
679  O O   . TYR   A 84  ? 0.3025 0.2840 0.5264 0.0122  0.0199  -0.0280 90  TYR   A O   
680  C CB  . TYR   A 84  ? 0.2575 0.2615 0.4952 0.0115  0.0062  -0.0133 90  TYR   A CB  
681  C CG  . TYR   A 84  ? 0.2379 0.2465 0.4739 0.0097  0.0001  -0.0100 90  TYR   A CG  
682  C CD1 . TYR   A 84  ? 0.2293 0.2408 0.4774 0.0099  -0.0014 -0.0056 90  TYR   A CD1 
683  C CD2 . TYR   A 84  ? 0.2441 0.2535 0.4672 0.0078  -0.0027 -0.0109 90  TYR   A CD2 
684  C CE1 . TYR   A 84  ? 0.2199 0.2342 0.4674 0.0083  -0.0048 -0.0027 90  TYR   A CE1 
685  C CE2 . TYR   A 84  ? 0.2376 0.2504 0.4612 0.0063  -0.0068 -0.0080 90  TYR   A CE2 
686  C CZ  . TYR   A 84  ? 0.2281 0.2432 0.4640 0.0066  -0.0072 -0.0040 90  TYR   A CZ  
687  O OH  . TYR   A 84  ? 0.2154 0.2325 0.4525 0.0051  -0.0092 -0.0014 90  TYR   A OH  
688  N N   . PRO   A 85  ? 0.3029 0.2913 0.5582 0.0151  0.0198  -0.0213 91  PRO   A N   
689  C CA  . PRO   A 85  ? 0.3044 0.2904 0.5680 0.0176  0.0296  -0.0220 91  PRO   A CA  
690  C C   . PRO   A 85  ? 0.2898 0.2878 0.5598 0.0192  0.0309  -0.0145 91  PRO   A C   
691  O O   . PRO   A 85  ? 0.2905 0.2974 0.5566 0.0181  0.0242  -0.0094 91  PRO   A O   
692  C CB  . PRO   A 85  ? 0.3074 0.2938 0.5920 0.0198  0.0317  -0.0191 91  PRO   A CB  
693  C CG  . PRO   A 85  ? 0.3062 0.3015 0.5965 0.0193  0.0236  -0.0122 91  PRO   A CG  
694  C CD  . PRO   A 85  ? 0.2948 0.2888 0.5664 0.0160  0.0165  -0.0155 91  PRO   A CD  
695  N N   . ALA   A 86  ? 0.2743 0.2723 0.5552 0.0215  0.0395  -0.0137 92  ALA   A N   
696  C CA  . ALA   A 86  ? 0.2788 0.2884 0.5692 0.0227  0.0397  -0.0062 92  ALA   A CA  
697  C C   . ALA   A 86  ? 0.2638 0.2851 0.5690 0.0234  0.0323  0.0039  92  ALA   A C   
698  O O   . ALA   A 86  ? 0.2641 0.2845 0.5827 0.0249  0.0325  0.0064  92  ALA   A O   
699  C CB  . ALA   A 86  ? 0.2892 0.2965 0.5944 0.0253  0.0508  -0.0066 92  ALA   A CB  
700  N N   . ARG   A 87  ? 0.2581 0.2883 0.5575 0.0217  0.0255  0.0093  93  ARG   A N   
701  C CA  . ARG   A 87  ? 0.2510 0.2895 0.5585 0.0214  0.0182  0.0187  93  ARG   A CA  
702  C C   . ARG   A 87  ? 0.2639 0.3110 0.5658 0.0192  0.0127  0.0239  93  ARG   A C   
703  O O   . ARG   A 87  ? 0.2929 0.3396 0.5843 0.0180  0.0143  0.0198  93  ARG   A O   
704  C CB  . ARG   A 87  ? 0.2484 0.2830 0.5466 0.0199  0.0140  0.0173  93  ARG   A CB  
705  C CG  . ARG   A 87  ? 0.2349 0.2703 0.5140 0.0168  0.0092  0.0156  93  ARG   A CG  
706  C CD  . ARG   A 87  ? 0.2427 0.2708 0.5126 0.0155  0.0082  0.0092  93  ARG   A CD  
707  N NE  . ARG   A 87  ? 0.2506 0.2804 0.5086 0.0129  0.0038  0.0100  93  ARG   A NE  
708  C CZ  . ARG   A 87  ? 0.2694 0.3002 0.5148 0.0112  0.0028  0.0075  93  ARG   A CZ  
709  N NH1 . ARG   A 87  ? 0.2260 0.2563 0.4677 0.0117  0.0058  0.0043  93  ARG   A NH1 
710  N NH2 . ARG   A 87  ? 0.2561 0.2878 0.4933 0.0090  -0.0002 0.0083  93  ARG   A NH2 
711  N N   . TYR   A 88  ? 0.2448 0.2979 0.5512 0.0183  0.0060  0.0328  94  TYR   A N   
712  C CA  . TYR   A 88  ? 0.2412 0.3000 0.5383 0.0151  -0.0004 0.0372  94  TYR   A CA  
713  C C   . TYR   A 88  ? 0.2311 0.2863 0.5076 0.0123  -0.0027 0.0341  94  TYR   A C   
714  O O   . TYR   A 88  ? 0.2420 0.2935 0.5166 0.0123  -0.0034 0.0351  94  TYR   A O   
715  C CB  . TYR   A 88  ? 0.2415 0.3060 0.5494 0.0145  -0.0072 0.0482  94  TYR   A CB  
716  C CG  . TYR   A 88  ? 0.2422 0.3125 0.5725 0.0166  -0.0067 0.0528  94  TYR   A CG  
717  C CD1 . TYR   A 88  ? 0.2519 0.3279 0.5839 0.0149  -0.0087 0.0537  94  TYR   A CD1 
718  C CD2 . TYR   A 88  ? 0.2546 0.3244 0.6068 0.0203  -0.0029 0.0556  94  TYR   A CD2 
719  C CE1 . TYR   A 88  ? 0.2675 0.3492 0.6242 0.0168  -0.0075 0.0581  94  TYR   A CE1 
720  C CE2 . TYR   A 88  ? 0.2601 0.3353 0.6371 0.0225  -0.0013 0.0602  94  TYR   A CE2 
721  C CZ  . TYR   A 88  ? 0.2679 0.3493 0.6478 0.0207  -0.0035 0.0615  94  TYR   A CZ  
722  O OH  . TYR   A 88  ? 0.2805 0.3675 0.6884 0.0228  -0.0016 0.0664  94  TYR   A OH  
723  N N   . GLN   A 89  ? 0.2084 0.2645 0.4716 0.0100  -0.0031 0.0305  95  GLN   A N   
724  C CA  . GLN   A 89  ? 0.2145 0.2673 0.4609 0.0074  -0.0047 0.0281  95  GLN   A CA  
725  C C   . GLN   A 89  ? 0.2079 0.2645 0.4469 0.0038  -0.0098 0.0339  95  GLN   A C   
726  O O   . GLN   A 89  ? 0.2085 0.2700 0.4498 0.0028  -0.0118 0.0356  95  GLN   A O   
727  C CB  . GLN   A 89  ? 0.2181 0.2679 0.4540 0.0070  -0.0018 0.0202  95  GLN   A CB  
728  C CG  . GLN   A 89  ? 0.2437 0.2906 0.4665 0.0044  -0.0033 0.0185  95  GLN   A CG  
729  C CD  . GLN   A 89  ? 0.2498 0.2921 0.4648 0.0044  -0.0018 0.0116  95  GLN   A CD  
730  O OE1 . GLN   A 89  ? 0.2632 0.3010 0.4804 0.0062  -0.0002 0.0073  95  GLN   A OE1 
731  N NE2 . GLN   A 89  ? 0.2379 0.2802 0.4428 0.0021  -0.0026 0.0107  95  GLN   A NE2 
732  N N   . SER   A 90  ? 0.2002 0.2531 0.4301 0.0017  -0.0115 0.0368  96  SER   A N   
733  C CA  . SER   A 90  ? 0.2067 0.2597 0.4248 -0.0025 -0.0159 0.0419  96  SER   A CA  
734  C C   . SER   A 90  ? 0.1976 0.2478 0.3997 -0.0057 -0.0140 0.0372  96  SER   A C   
735  O O   . SER   A 90  ? 0.1954 0.2433 0.3963 -0.0044 -0.0098 0.0312  96  SER   A O   
736  C CB  . SER   A 90  ? 0.2215 0.2700 0.4366 -0.0035 -0.0174 0.0483  96  SER   A CB  
737  O OG  . SER   A 90  ? 0.2407 0.2827 0.4502 -0.0033 -0.0121 0.0449  96  SER   A OG  
738  N N   . HIS   A 91  ? 0.1769 0.2269 0.3674 -0.0101 -0.0178 0.0402  97  HIS   A N   
739  C CA  . HIS   A 91  ? 0.1890 0.2354 0.3645 -0.0135 -0.0154 0.0361  97  HIS   A CA  
740  C C   . HIS   A 91  ? 0.2028 0.2529 0.3825 -0.0117 -0.0126 0.0297  97  HIS   A C   
741  O O   . HIS   A 91  ? 0.2111 0.2577 0.3840 -0.0124 -0.0087 0.0254  97  HIS   A O   
742  C CB  . HIS   A 91  ? 0.1977 0.2355 0.3638 -0.0146 -0.0100 0.0349  97  HIS   A CB  
743  C CG  . HIS   A 91  ? 0.2445 0.2762 0.4025 -0.0169 -0.0112 0.0412  97  HIS   A CG  
744  N ND1 . HIS   A 91  ? 0.2883 0.3133 0.4272 -0.0224 -0.0123 0.0435  97  HIS   A ND1 
745  C CD2 . HIS   A 91  ? 0.2459 0.2769 0.4118 -0.0146 -0.0121 0.0460  97  HIS   A CD2 
746  C CE1 . HIS   A 91  ? 0.2979 0.3173 0.4313 -0.0234 -0.0136 0.0497  97  HIS   A CE1 
747  N NE2 . HIS   A 91  ? 0.2756 0.2991 0.4261 -0.0187 -0.0138 0.0518  97  HIS   A NE2 
748  N N   . LEU   A 92  ? 0.1962 0.2526 0.3876 -0.0095 -0.0140 0.0296  98  LEU   A N   
749  C CA  . LEU   A 92  ? 0.2067 0.2648 0.4006 -0.0077 -0.0105 0.0241  98  LEU   A CA  
750  C C   . LEU   A 92  ? 0.2145 0.2769 0.4072 -0.0104 -0.0124 0.0246  98  LEU   A C   
751  O O   . LEU   A 92  ? 0.2206 0.2872 0.4190 -0.0121 -0.0175 0.0295  98  LEU   A O   
752  C CB  . LEU   A 92  ? 0.2035 0.2631 0.4106 -0.0033 -0.0081 0.0229  98  LEU   A CB  
753  C CG  . LEU   A 92  ? 0.2167 0.2748 0.4235 -0.0013 -0.0034 0.0171  98  LEU   A CG  
754  C CD1 . LEU   A 92  ? 0.2059 0.2580 0.4026 -0.0012 -0.0018 0.0124  98  LEU   A CD1 
755  C CD2 . LEU   A 92  ? 0.2335 0.2914 0.4530 0.0024  0.0001  0.0163  98  LEU   A CD2 
756  N N   . MET   A 93  ? 0.2007 0.2618 0.3869 -0.0110 -0.0091 0.0200  99  MET   A N   
757  C CA  . MET   A 93  ? 0.1789 0.2434 0.3644 -0.0135 -0.0097 0.0197  99  MET   A CA  
758  C C   . MET   A 93  ? 0.1916 0.2568 0.3823 -0.0105 -0.0045 0.0160  99  MET   A C   
759  O O   . MET   A 93  ? 0.1972 0.2577 0.3826 -0.0083 -0.0010 0.0123  99  MET   A O   
760  C CB  . MET   A 93  ? 0.1874 0.2475 0.3585 -0.0173 -0.0089 0.0175  99  MET   A CB  
761  C CG  . MET   A 93  ? 0.2135 0.2693 0.3747 -0.0210 -0.0120 0.0205  99  MET   A CG  
762  S SD  . MET   A 93  ? 0.2628 0.3106 0.4081 -0.0248 -0.0074 0.0169  99  MET   A SD  
763  C CE  . MET   A 93  ? 0.2307 0.2765 0.3811 -0.0201 -0.0017 0.0132  99  MET   A CE  
764  N N   . LEU   A 94  ? 0.1754 0.2456 0.3762 -0.0105 -0.0039 0.0173  100 LEU   A N   
765  C CA  . LEU   A 94  ? 0.1696 0.2384 0.3733 -0.0078 0.0029  0.0138  100 LEU   A CA  
766  C C   . LEU   A 94  ? 0.1755 0.2452 0.3756 -0.0104 0.0046  0.0126  100 LEU   A C   
767  O O   . LEU   A 94  ? 0.1766 0.2506 0.3794 -0.0141 0.0001  0.0152  100 LEU   A O   
768  C CB  . LEU   A 94  ? 0.1767 0.2490 0.3984 -0.0051 0.0056  0.0160  100 LEU   A CB  
769  C CG  . LEU   A 94  ? 0.2114 0.2829 0.4409 -0.0022 0.0052  0.0174  100 LEU   A CG  
770  C CD1 . LEU   A 94  ? 0.2050 0.2799 0.4558 0.0006  0.0096  0.0197  100 LEU   A CD1 
771  C CD2 . LEU   A 94  ? 0.2379 0.3011 0.4552 0.0000  0.0089  0.0123  100 LEU   A CD2 
772  N N   . ALA   A 95  ? 0.1730 0.2380 0.3668 -0.0087 0.0108  0.0090  101 ALA   A N   
773  C CA  . ALA   A 95  ? 0.1833 0.2483 0.3751 -0.0103 0.0145  0.0079  101 ALA   A CA  
774  C C   . ALA   A 95  ? 0.1930 0.2537 0.3864 -0.0071 0.0230  0.0058  101 ALA   A C   
775  O O   . ALA   A 95  ? 0.2087 0.2645 0.3996 -0.0042 0.0256  0.0040  101 ALA   A O   
776  C CB  . ALA   A 95  ? 0.1755 0.2360 0.3526 -0.0121 0.0138  0.0057  101 ALA   A CB  
777  N N   . VAL   A 96  ? 0.1746 0.2362 0.3719 -0.0080 0.0278  0.0059  102 VAL   A N   
778  C CA  . VAL   A 96  ? 0.1945 0.2495 0.3894 -0.0055 0.0375  0.0039  102 VAL   A CA  
779  C C   . VAL   A 96  ? 0.2195 0.2660 0.3936 -0.0057 0.0382  0.0013  102 VAL   A C   
780  O O   . VAL   A 96  ? 0.2277 0.2757 0.3976 -0.0082 0.0361  0.0019  102 VAL   A O   
781  C CB  . VAL   A 96  ? 0.1965 0.2556 0.4064 -0.0063 0.0435  0.0057  102 VAL   A CB  
782  C CG1 . VAL   A 96  ? 0.2184 0.2678 0.4223 -0.0038 0.0558  0.0034  102 VAL   A CG1 
783  C CG2 . VAL   A 96  ? 0.1917 0.2602 0.4261 -0.0063 0.0406  0.0095  102 VAL   A CG2 
784  N N   . GLY   A 97  ? 0.2379 0.2752 0.3997 -0.0035 0.0409  -0.0013 103 GLY   A N   
785  C CA  . GLY   A 97  ? 0.2588 0.2872 0.4012 -0.0039 0.0399  -0.0030 103 GLY   A CA  
786  C C   . GLY   A 97  ? 0.2658 0.2834 0.3943 -0.0022 0.0400  -0.0060 103 GLY   A C   
787  O O   . GLY   A 97  ? 0.2729 0.2902 0.4072 -0.0007 0.0412  -0.0073 103 GLY   A O   
788  N N   . HIS   A 98  ? 0.2696 0.2778 0.3800 -0.0029 0.0381  -0.0068 104 HIS   A N   
789  C CA  . HIS   A 98  ? 0.2919 0.2881 0.3863 -0.0023 0.0366  -0.0098 104 HIS   A CA  
790  C C   . HIS   A 98  ? 0.2894 0.2876 0.3859 -0.0025 0.0265  -0.0102 104 HIS   A C   
791  O O   . HIS   A 98  ? 0.2790 0.2835 0.3812 -0.0035 0.0199  -0.0079 104 HIS   A O   
792  C CB  . HIS   A 98  ? 0.3073 0.2901 0.3794 -0.0033 0.0379  -0.0101 104 HIS   A CB  
793  C CG  . HIS   A 98  ? 0.3584 0.3264 0.4106 -0.0037 0.0358  -0.0136 104 HIS   A CG  
794  N ND1 . HIS   A 98  ? 0.3963 0.3550 0.4421 -0.0028 0.0448  -0.0175 104 HIS   A ND1 
795  C CD2 . HIS   A 98  ? 0.3848 0.3451 0.4230 -0.0052 0.0257  -0.0136 104 HIS   A CD2 
796  C CE1 . HIS   A 98  ? 0.4039 0.3486 0.4291 -0.0042 0.0397  -0.0205 104 HIS   A CE1 
797  N NE2 . HIS   A 98  ? 0.3958 0.3415 0.4165 -0.0057 0.0272  -0.0180 104 HIS   A NE2 
798  N N   . SER   A 99  ? 0.2981 0.2903 0.3912 -0.0016 0.0264  -0.0134 105 SER   A N   
799  C CA  . SER   A 99  ? 0.3199 0.3121 0.4148 -0.0019 0.0175  -0.0142 105 SER   A CA  
800  C C   . SER   A 99  ? 0.3329 0.3121 0.4151 -0.0018 0.0182  -0.0188 105 SER   A C   
801  O O   . SER   A 99  ? 0.3544 0.3282 0.4339 -0.0007 0.0274  -0.0214 105 SER   A O   
802  C CB  . SER   A 99  ? 0.3438 0.3483 0.4587 -0.0010 0.0155  -0.0122 105 SER   A CB  
803  O OG  . SER   A 99  ? 0.3855 0.3926 0.5099 0.0007  0.0225  -0.0128 105 SER   A OG  
804  N N   . GLU   A 100 ? 0.3174 0.2909 0.3924 -0.0031 0.0088  -0.0198 106 GLU   A N   
805  C CA  . GLU   A 100 ? 0.3309 0.2914 0.3934 -0.0040 0.0065  -0.0245 106 GLU   A CA  
806  C C   . GLU   A 100 ? 0.3252 0.2915 0.4017 -0.0042 -0.0030 -0.0239 106 GLU   A C   
807  O O   . GLU   A 100 ? 0.3135 0.2903 0.4032 -0.0041 -0.0078 -0.0198 106 GLU   A O   
808  C CB  . GLU   A 100 ? 0.3638 0.3080 0.3990 -0.0068 0.0027  -0.0260 106 GLU   A CB  
809  C CG  . GLU   A 100 ? 0.3882 0.3256 0.4092 -0.0066 0.0138  -0.0262 106 GLU   A CG  
810  C CD  . GLU   A 100 ? 0.4911 0.4104 0.4817 -0.0095 0.0108  -0.0270 106 GLU   A CD  
811  O OE1 . GLU   A 100 ? 0.4990 0.4051 0.4731 -0.0120 0.0032  -0.0303 106 GLU   A OE1 
812  O OE2 . GLU   A 100 ? 0.4990 0.4163 0.4812 -0.0096 0.0157  -0.0241 106 GLU   A OE2 
813  N N   . PRO   A 101 ? 0.3308 0.2905 0.4066 -0.0044 -0.0042 -0.0281 107 PRO   A N   
814  C CA  . PRO   A 101 ? 0.3197 0.2856 0.4119 -0.0044 -0.0120 -0.0271 107 PRO   A CA  
815  C C   . PRO   A 101 ? 0.3094 0.2787 0.4063 -0.0060 -0.0230 -0.0234 107 PRO   A C   
816  O O   . PRO   A 101 ? 0.2976 0.2778 0.4137 -0.0051 -0.0248 -0.0199 107 PRO   A O   
817  C CB  . PRO   A 101 ? 0.3382 0.2915 0.4223 -0.0054 -0.0128 -0.0330 107 PRO   A CB  
818  C CG  . PRO   A 101 ? 0.3447 0.2901 0.4172 -0.0044 -0.0004 -0.0367 107 PRO   A CG  
819  C CD  . PRO   A 101 ? 0.3376 0.2832 0.3988 -0.0047 0.0028  -0.0340 107 PRO   A CD  
820  N N   . GLY   A 102 ? 0.3039 0.2628 0.3836 -0.0085 -0.0300 -0.0238 108 GLY   A N   
821  C CA  . GLY   A 102 ? 0.3042 0.2656 0.3903 -0.0101 -0.0407 -0.0195 108 GLY   A CA  
822  C C   . GLY   A 102 ? 0.2991 0.2724 0.3975 -0.0088 -0.0376 -0.0142 108 GLY   A C   
823  O O   . GLY   A 102 ? 0.3052 0.2821 0.4144 -0.0095 -0.0444 -0.0103 108 GLY   A O   
824  N N   . ASP   A 103 ? 0.2862 0.2653 0.3840 -0.0070 -0.0271 -0.0139 109 ASP   A N   
825  C CA  . ASP   A 103 ? 0.2739 0.2635 0.3824 -0.0062 -0.0232 -0.0098 109 ASP   A CA  
826  C C   . ASP   A 103 ? 0.2468 0.2471 0.3755 -0.0052 -0.0216 -0.0081 109 ASP   A C   
827  O O   . ASP   A 103 ? 0.2402 0.2474 0.3775 -0.0054 -0.0195 -0.0049 109 ASP   A O   
828  C CB  . ASP   A 103 ? 0.2823 0.2738 0.3838 -0.0054 -0.0135 -0.0101 109 ASP   A CB  
829  C CG  . ASP   A 103 ? 0.3081 0.2894 0.3898 -0.0064 -0.0130 -0.0104 109 ASP   A CG  
830  O OD1 . ASP   A 103 ? 0.3058 0.2827 0.3825 -0.0079 -0.0205 -0.0080 109 ASP   A OD1 
831  O OD2 . ASP   A 103 ? 0.3129 0.2903 0.3850 -0.0058 -0.0047 -0.0125 109 ASP   A OD2 
832  N N   . CYS   A 104 ? 0.2260 0.2263 0.3616 -0.0045 -0.0224 -0.0101 110 CYS   A N   
833  C CA  . CYS   A 104 ? 0.2004 0.2090 0.3532 -0.0038 -0.0207 -0.0078 110 CYS   A CA  
834  C C   . CYS   A 104 ? 0.1950 0.2055 0.3585 -0.0048 -0.0247 -0.0046 110 CYS   A C   
835  O O   . CYS   A 104 ? 0.1991 0.2043 0.3615 -0.0059 -0.0320 -0.0045 110 CYS   A O   
836  C CB  . CYS   A 104 ? 0.2134 0.2200 0.3721 -0.0030 -0.0216 -0.0101 110 CYS   A CB  
837  S SG  . CYS   A 104 ? 0.2611 0.2669 0.4140 -0.0012 -0.0142 -0.0129 110 CYS   A SG  
838  N N   . GLY   A 105 ? 0.1740 0.1910 0.3468 -0.0048 -0.0198 -0.0019 111 GLY   A N   
839  C CA  . GLY   A 105 ? 0.1876 0.2058 0.3721 -0.0056 -0.0208 0.0011  111 GLY   A CA  
840  C C   . GLY   A 105 ? 0.1994 0.2189 0.3795 -0.0065 -0.0178 0.0027  111 GLY   A C   
841  O O   . GLY   A 105 ? 0.2154 0.2363 0.4058 -0.0072 -0.0151 0.0051  111 GLY   A O   
842  N N   . GLY   A 106 ? 0.1898 0.2083 0.3558 -0.0065 -0.0168 0.0014  112 GLY   A N   
843  C CA  . GLY   A 106 ? 0.1757 0.1954 0.3379 -0.0074 -0.0134 0.0029  112 GLY   A CA  
844  C C   . GLY   A 106 ? 0.1915 0.2163 0.3578 -0.0083 -0.0062 0.0035  112 GLY   A C   
845  O O   . GLY   A 106 ? 0.1859 0.2136 0.3505 -0.0081 -0.0039 0.0026  112 GLY   A O   
846  N N   . ILE   A 107 ? 0.1862 0.2112 0.3580 -0.0096 -0.0029 0.0053  113 ILE   A N   
847  C CA  . ILE   A 107 ? 0.1963 0.2234 0.3689 -0.0114 0.0039  0.0052  113 ILE   A CA  
848  C C   . ILE   A 107 ? 0.2053 0.2349 0.3679 -0.0128 0.0069  0.0042  113 ILE   A C   
849  O O   . ILE   A 107 ? 0.2014 0.2305 0.3599 -0.0127 0.0065  0.0041  113 ILE   A O   
850  C CB  . ILE   A 107 ? 0.2185 0.2428 0.4020 -0.0126 0.0080  0.0069  113 ILE   A CB  
851  C CG1 . ILE   A 107 ? 0.2359 0.2587 0.4324 -0.0116 0.0071  0.0081  113 ILE   A CG1 
852  C CG2 . ILE   A 107 ? 0.2366 0.2599 0.4153 -0.0155 0.0162  0.0060  113 ILE   A CG2 
853  C CD1 . ILE   A 107 ? 0.2501 0.2697 0.4634 -0.0120 0.0107  0.0104  113 ILE   A CD1 
854  N N   . LEU   A 108 ? 0.2061 0.2378 0.3656 -0.0146 0.0097  0.0038  114 LEU   A N   
855  C CA  . LEU   A 108 ? 0.2074 0.2415 0.3602 -0.0169 0.0119  0.0031  114 LEU   A CA  
856  C C   . LEU   A 108 ? 0.2142 0.2446 0.3655 -0.0204 0.0170  0.0029  114 LEU   A C   
857  O O   . LEU   A 108 ? 0.2081 0.2359 0.3596 -0.0212 0.0186  0.0034  114 LEU   A O   
858  C CB  . LEU   A 108 ? 0.2134 0.2515 0.3640 -0.0169 0.0096  0.0034  114 LEU   A CB  
859  C CG  . LEU   A 108 ? 0.2351 0.2756 0.3810 -0.0203 0.0102  0.0035  114 LEU   A CG  
860  C CD1 . LEU   A 108 ? 0.2312 0.2741 0.3771 -0.0201 0.0111  0.0026  114 LEU   A CD1 
861  C CD2 . LEU   A 108 ? 0.2496 0.2938 0.3966 -0.0204 0.0065  0.0054  114 LEU   A CD2 
862  N N   . ARG   A 109 ? 0.2251 0.2541 0.3738 -0.0226 0.0204  0.0019  115 ARG   A N   
863  C CA  . ARG   A 109 ? 0.2524 0.2758 0.3982 -0.0263 0.0266  0.0008  115 ARG   A CA  
864  C C   . ARG   A 109 ? 0.2476 0.2709 0.3850 -0.0304 0.0279  -0.0010 115 ARG   A C   
865  O O   . ARG   A 109 ? 0.2305 0.2581 0.3689 -0.0297 0.0257  -0.0010 115 ARG   A O   
866  C CB  . ARG   A 109 ? 0.3007 0.3198 0.4560 -0.0254 0.0312  0.0013  115 ARG   A CB  
867  C CG  . ARG   A 109 ? 0.4076 0.4294 0.5685 -0.0226 0.0279  0.0027  115 ARG   A CG  
868  C CD  . ARG   A 109 ? 0.5116 0.5290 0.6837 -0.0222 0.0321  0.0041  115 ARG   A CD  
869  N NE  . ARG   A 109 ? 0.5838 0.6023 0.7653 -0.0187 0.0258  0.0072  115 ARG   A NE  
870  C CZ  . ARG   A 109 ? 0.6269 0.6455 0.8095 -0.0175 0.0228  0.0093  115 ARG   A CZ  
871  N NH1 . ARG   A 109 ? 0.6258 0.6445 0.8019 -0.0190 0.0261  0.0084  115 ARG   A NH1 
872  N NH2 . ARG   A 109 ? 0.6252 0.6433 0.8142 -0.0150 0.0157  0.0125  115 ARG   A NH2 
873  N N   . CYS   A 110 ? 0.2560 0.2733 0.3842 -0.0351 0.0314  -0.0025 116 CYS   A N   
874  C CA  . CYS   A 110 ? 0.2775 0.2933 0.3972 -0.0400 0.0319  -0.0047 116 CYS   A CA  
875  C C   . CYS   A 110 ? 0.2916 0.2972 0.4085 -0.0434 0.0415  -0.0075 116 CYS   A C   
876  O O   . CYS   A 110 ? 0.2915 0.2930 0.4157 -0.0412 0.0472  -0.0069 116 CYS   A O   
877  C CB  . CYS   A 110 ? 0.2809 0.2961 0.3894 -0.0438 0.0268  -0.0043 116 CYS   A CB  
878  S SG  . CYS   A 110 ? 0.2360 0.2392 0.3317 -0.0472 0.0321  -0.0047 116 CYS   A SG  
879  N N   . GLN   A 111 ? 0.3254 0.3258 0.4319 -0.0491 0.0436  -0.0105 117 GLN   A N   
880  C CA  . GLN   A 111 ? 0.3477 0.3365 0.4500 -0.0529 0.0541  -0.0139 117 GLN   A CA  
881  C C   . GLN   A 111 ? 0.3699 0.3481 0.4653 -0.0543 0.0613  -0.0145 117 GLN   A C   
882  O O   . GLN   A 111 ? 0.3909 0.3593 0.4880 -0.0558 0.0723  -0.0167 117 GLN   A O   
883  C CB  . GLN   A 111 ? 0.3793 0.3632 0.4687 -0.0598 0.0538  -0.0178 117 GLN   A CB  
884  C CG  . GLN   A 111 ? 0.4253 0.4058 0.4965 -0.0652 0.0470  -0.0182 117 GLN   A CG  
885  C CD  . GLN   A 111 ? 0.4940 0.4692 0.5530 -0.0728 0.0448  -0.0221 117 GLN   A CD  
886  O OE1 . GLN   A 111 ? 0.5021 0.4858 0.5638 -0.0741 0.0351  -0.0208 117 GLN   A OE1 
887  N NE2 . GLN   A 111 ? 0.5012 0.4616 0.5477 -0.0783 0.0543  -0.0269 117 GLN   A NE2 
888  N N   . HIS   A 112 ? 0.3603 0.3396 0.4489 -0.0538 0.0562  -0.0123 118 HIS   A N   
889  C CA  . HIS   A 112 ? 0.3698 0.3381 0.4505 -0.0554 0.0637  -0.0124 118 HIS   A CA  
890  C C   . HIS   A 112 ? 0.3651 0.3366 0.4634 -0.0493 0.0665  -0.0092 118 HIS   A C   
891  O O   . HIS   A 112 ? 0.3876 0.3497 0.4834 -0.0501 0.0747  -0.0091 118 HIS   A O   
892  C CB  . HIS   A 112 ? 0.3854 0.3498 0.4456 -0.0597 0.0574  -0.0115 118 HIS   A CB  
893  C CG  . HIS   A 112 ? 0.4189 0.3786 0.4610 -0.0669 0.0531  -0.0144 118 HIS   A CG  
894  N ND1 . HIS   A 112 ? 0.4414 0.4122 0.4855 -0.0672 0.0405  -0.0127 118 HIS   A ND1 
895  C CD2 . HIS   A 112 ? 0.4419 0.3862 0.4642 -0.0743 0.0599  -0.0190 118 HIS   A CD2 
896  C CE1 . HIS   A 112 ? 0.4502 0.4131 0.4774 -0.0747 0.0385  -0.0158 118 HIS   A CE1 
897  N NE2 . HIS   A 112 ? 0.4612 0.4076 0.4733 -0.0795 0.0499  -0.0200 118 HIS   A NE2 
898  N N   . GLY   A 113 ? 0.3269 0.3105 0.4422 -0.0436 0.0596  -0.0066 119 GLY   A N   
899  C CA  . GLY   A 113 ? 0.3021 0.2890 0.4346 -0.0383 0.0600  -0.0037 119 GLY   A CA  
900  C C   . GLY   A 113 ? 0.2802 0.2783 0.4176 -0.0342 0.0486  -0.0010 119 GLY   A C   
901  O O   . GLY   A 113 ? 0.2594 0.2643 0.3928 -0.0340 0.0416  -0.0013 119 GLY   A O   
902  N N   . VAL   A 114 ? 0.2680 0.2672 0.4157 -0.0308 0.0478  0.0013  120 VAL   A N   
903  C CA  . VAL   A 114 ? 0.2586 0.2663 0.4115 -0.0269 0.0384  0.0032  120 VAL   A CA  
904  C C   . VAL   A 114 ? 0.2440 0.2530 0.3843 -0.0285 0.0342  0.0039  120 VAL   A C   
905  O O   . VAL   A 114 ? 0.2545 0.2567 0.3866 -0.0311 0.0383  0.0045  120 VAL   A O   
906  C CB  . VAL   A 114 ? 0.2655 0.2733 0.4348 -0.0233 0.0384  0.0053  120 VAL   A CB  
907  C CG1 . VAL   A 114 ? 0.2664 0.2813 0.4387 -0.0200 0.0290  0.0064  120 VAL   A CG1 
908  C CG2 . VAL   A 114 ? 0.2716 0.2788 0.4564 -0.0218 0.0404  0.0058  120 VAL   A CG2 
909  N N   . VAL   A 115 ? 0.2239 0.2409 0.3633 -0.0270 0.0264  0.0042  121 VAL   A N   
910  C CA  . VAL   A 115 ? 0.2118 0.2316 0.3436 -0.0281 0.0210  0.0058  121 VAL   A CA  
911  C C   . VAL   A 115 ? 0.2038 0.2278 0.3445 -0.0239 0.0168  0.0079  121 VAL   A C   
912  O O   . VAL   A 115 ? 0.2096 0.2328 0.3469 -0.0244 0.0150  0.0103  121 VAL   A O   
913  C CB  . VAL   A 115 ? 0.2143 0.2403 0.3438 -0.0289 0.0163  0.0051  121 VAL   A CB  
914  C CG1 . VAL   A 115 ? 0.2112 0.2423 0.3392 -0.0292 0.0095  0.0076  121 VAL   A CG1 
915  C CG2 . VAL   A 115 ? 0.2180 0.2397 0.3392 -0.0335 0.0200  0.0027  121 VAL   A CG2 
916  N N   . GLY   A 116 ? 0.1859 0.2137 0.3370 -0.0200 0.0147  0.0071  122 GLY   A N   
917  C CA  . GLY   A 116 ? 0.1919 0.2224 0.3507 -0.0164 0.0108  0.0080  122 GLY   A CA  
918  C C   . GLY   A 116 ? 0.1933 0.2252 0.3592 -0.0134 0.0082  0.0064  122 GLY   A C   
919  O O   . GLY   A 116 ? 0.1960 0.2265 0.3624 -0.0139 0.0095  0.0055  122 GLY   A O   
920  N N   . ILE   A 117 ? 0.1846 0.2179 0.3551 -0.0107 0.0043  0.0062  123 ILE   A N   
921  C CA  . ILE   A 117 ? 0.1857 0.2179 0.3590 -0.0086 0.0007  0.0044  123 ILE   A CA  
922  C C   . ILE   A 117 ? 0.1944 0.2283 0.3640 -0.0068 -0.0017 0.0029  123 ILE   A C   
923  O O   . ILE   A 117 ? 0.1910 0.2270 0.3626 -0.0061 -0.0015 0.0037  123 ILE   A O   
924  C CB  . ILE   A 117 ? 0.1977 0.2267 0.3816 -0.0076 -0.0015 0.0048  123 ILE   A CB  
925  C CG1 . ILE   A 117 ? 0.2156 0.2448 0.4047 -0.0067 -0.0011 0.0057  123 ILE   A CG1 
926  C CG2 . ILE   A 117 ? 0.2123 0.2388 0.4034 -0.0089 0.0018  0.0062  123 ILE   A CG2 
927  C CD1 . ILE   A 117 ? 0.2271 0.2532 0.4294 -0.0058 -0.0035 0.0059  123 ILE   A CD1 
928  N N   . VAL   A 118 ? 0.1985 0.2299 0.3631 -0.0059 -0.0037 0.0009  124 VAL   A N   
929  C CA  . VAL   A 118 ? 0.1911 0.2214 0.3512 -0.0043 -0.0037 -0.0012 124 VAL   A CA  
930  C C   . VAL   A 118 ? 0.1853 0.2138 0.3513 -0.0028 -0.0057 -0.0021 124 VAL   A C   
931  O O   . VAL   A 118 ? 0.1823 0.2080 0.3531 -0.0029 -0.0092 -0.0022 124 VAL   A O   
932  C CB  . VAL   A 118 ? 0.2058 0.2302 0.3561 -0.0041 -0.0053 -0.0033 124 VAL   A CB  
933  C CG1 . VAL   A 118 ? 0.2205 0.2411 0.3646 -0.0027 -0.0031 -0.0061 124 VAL   A CG1 
934  C CG2 . VAL   A 118 ? 0.2132 0.2392 0.3587 -0.0054 -0.0026 -0.0020 124 VAL   A CG2 
935  N N   . SER   A 119 ? 0.1689 0.1994 0.3369 -0.0015 -0.0034 -0.0023 125 SER   A N   
936  C CA  . SER   A 119 ? 0.1750 0.2037 0.3500 0.0000  -0.0044 -0.0030 125 SER   A CA  
937  C C   . SER   A 119 ? 0.2109 0.2367 0.3841 0.0017  -0.0013 -0.0057 125 SER   A C   
938  O O   . SER   A 119 ? 0.2221 0.2426 0.3970 0.0027  -0.0019 -0.0084 125 SER   A O   
939  C CB  . SER   A 119 ? 0.1945 0.2285 0.3785 -0.0001 -0.0037 0.0011  125 SER   A CB  
940  O OG  . SER   A 119 ? 0.2288 0.2614 0.4210 0.0015  -0.0039 0.0012  125 SER   A OG  
941  N N   . THR   A 120 ? 0.2174 0.2462 0.3888 0.0019  0.0029  -0.0051 126 THR   A N   
942  C CA  . THR   A 120 ? 0.2384 0.2642 0.4110 0.0037  0.0082  -0.0073 126 THR   A CA  
943  C C   . THR   A 120 ? 0.2523 0.2750 0.4152 0.0033  0.0129  -0.0091 126 THR   A C   
944  O O   . THR   A 120 ? 0.2487 0.2733 0.4056 0.0017  0.0114  -0.0079 126 THR   A O   
945  C CB  . THR   A 120 ? 0.2462 0.2796 0.4349 0.0051  0.0101  -0.0032 126 THR   A CB  
946  O OG1 . THR   A 120 ? 0.2434 0.2839 0.4350 0.0040  0.0108  0.0002  126 THR   A OG1 
947  C CG2 . THR   A 120 ? 0.2491 0.2856 0.4464 0.0052  0.0059  0.0000  126 THR   A CG2 
948  N N   . GLY   A 121 ? 0.2807 0.2987 0.4438 0.0048  0.0199  -0.0115 127 GLY   A N   
949  C CA  . GLY   A 121 ? 0.3105 0.3248 0.4658 0.0046  0.0264  -0.0127 127 GLY   A CA  
950  C C   . GLY   A 121 ? 0.3286 0.3348 0.4840 0.0063  0.0361  -0.0161 127 GLY   A C   
951  O O   . GLY   A 121 ? 0.3248 0.3277 0.4859 0.0077  0.0375  -0.0179 127 GLY   A O   
952  N N   . GLY   A 122 ? 0.3557 0.3579 0.5053 0.0062  0.0438  -0.0169 128 GLY   A N   
953  C CA  . GLY   A 122 ? 0.3861 0.3785 0.5346 0.0077  0.0560  -0.0204 128 GLY   A CA  
954  C C   . GLY   A 122 ? 0.3979 0.3974 0.5628 0.0087  0.0641  -0.0169 128 GLY   A C   
955  O O   . GLY   A 122 ? 0.3810 0.3949 0.5639 0.0086  0.0588  -0.0116 128 GLY   A O   
956  N N   . ASN   A 123 ? 0.4186 0.4071 0.5773 0.0094  0.0771  -0.0200 129 ASN   A N   
957  C CA  . ASN   A 123 ? 0.4170 0.4112 0.5948 0.0105  0.0867  -0.0168 129 ASN   A CA  
958  C C   . ASN   A 123 ? 0.4075 0.4111 0.5864 0.0087  0.0817  -0.0128 129 ASN   A C   
959  O O   . ASN   A 123 ? 0.4152 0.4297 0.6171 0.0090  0.0837  -0.0085 129 ASN   A O   
960  C CB  . ASN   A 123 ? 0.4236 0.4298 0.6341 0.0127  0.0868  -0.0126 129 ASN   A CB  
961  C CG  . ASN   A 123 ? 0.4854 0.4823 0.7005 0.0150  0.0949  -0.0162 129 ASN   A CG  
962  O OD1 . ASN   A 123 ? 0.5321 0.5117 0.7282 0.0150  0.1054  -0.0225 129 ASN   A OD1 
963  N ND2 . ASN   A 123 ? 0.4689 0.4760 0.7089 0.0167  0.0909  -0.0122 129 ASN   A ND2 
964  N N   . GLY   A 124 ? 0.3858 0.3851 0.5421 0.0066  0.0752  -0.0141 130 GLY   A N   
965  C CA  . GLY   A 124 ? 0.3531 0.3601 0.5101 0.0047  0.0711  -0.0107 130 GLY   A CA  
966  C C   . GLY   A 124 ? 0.3174 0.3394 0.4877 0.0034  0.0589  -0.0067 130 GLY   A C   
967  O O   . GLY   A 124 ? 0.3035 0.3329 0.4785 0.0016  0.0560  -0.0039 130 GLY   A O   
968  N N   . LEU   A 125 ? 0.3000 0.3252 0.4749 0.0041  0.0521  -0.0066 131 LEU   A N   
969  C CA  . LEU   A 125 ? 0.2852 0.3216 0.4687 0.0026  0.0416  -0.0030 131 LEU   A CA  
970  C C   . LEU   A 125 ? 0.2817 0.3137 0.4495 0.0019  0.0341  -0.0049 131 LEU   A C   
971  O O   . LEU   A 125 ? 0.3064 0.3276 0.4599 0.0026  0.0356  -0.0088 131 LEU   A O   
972  C CB  . LEU   A 125 ? 0.2836 0.3280 0.4887 0.0039  0.0401  0.0003  131 LEU   A CB  
973  C CG  . LEU   A 125 ? 0.3110 0.3609 0.5372 0.0047  0.0465  0.0032  131 LEU   A CG  
974  C CD1 . LEU   A 125 ? 0.3345 0.3873 0.5815 0.0072  0.0485  0.0055  131 LEU   A CD1 
975  C CD2 . LEU   A 125 ? 0.3060 0.3661 0.5408 0.0017  0.0405  0.0074  131 LEU   A CD2 
976  N N   . VAL   A 126 ? 0.2367 0.2756 0.4063 -0.0001 0.0264  -0.0024 132 VAL   A N   
977  C CA  . VAL   A 126 ? 0.1968 0.2334 0.3580 -0.0008 0.0198  -0.0031 132 VAL   A CA  
978  C C   . VAL   A 126 ? 0.1971 0.2420 0.3690 -0.0018 0.0144  0.0004  132 VAL   A C   
979  O O   . VAL   A 126 ? 0.1894 0.2412 0.3685 -0.0035 0.0134  0.0034  132 VAL   A O   
980  C CB  . VAL   A 126 ? 0.2000 0.2331 0.3487 -0.0025 0.0179  -0.0037 132 VAL   A CB  
981  C CG1 . VAL   A 126 ? 0.1894 0.2280 0.3412 -0.0045 0.0196  -0.0017 132 VAL   A CG1 
982  C CG2 . VAL   A 126 ? 0.1902 0.2226 0.3364 -0.0033 0.0114  -0.0035 132 VAL   A CG2 
983  N N   . GLY   A 127 ? 0.1985 0.2418 0.3711 -0.0010 0.0109  0.0002  133 GLY   A N   
984  C CA  . GLY   A 127 ? 0.2046 0.2534 0.3846 -0.0020 0.0066  0.0038  133 GLY   A CA  
985  C C   . GLY   A 127 ? 0.2052 0.2512 0.3787 -0.0032 0.0033  0.0034  133 GLY   A C   
986  O O   . GLY   A 127 ? 0.2138 0.2540 0.3822 -0.0023 0.0028  0.0006  133 GLY   A O   
987  N N   . PHE   A 128 ? 0.1862 0.2353 0.3600 -0.0056 0.0012  0.0063  134 PHE   A N   
988  C CA  . PHE   A 128 ? 0.1871 0.2332 0.3567 -0.0071 0.0002  0.0064  134 PHE   A CA  
989  C C   . PHE   A 128 ? 0.1956 0.2422 0.3686 -0.0077 -0.0013 0.0096  134 PHE   A C   
990  O O   . PHE   A 128 ? 0.1943 0.2443 0.3684 -0.0092 -0.0029 0.0128  134 PHE   A O   
991  C CB  . PHE   A 128 ? 0.1840 0.2306 0.3473 -0.0103 0.0014  0.0066  134 PHE   A CB  
992  C CG  . PHE   A 128 ? 0.1882 0.2350 0.3484 -0.0102 0.0033  0.0045  134 PHE   A CG  
993  C CD1 . PHE   A 128 ? 0.1979 0.2401 0.3540 -0.0094 0.0039  0.0026  134 PHE   A CD1 
994  C CD2 . PHE   A 128 ? 0.1899 0.2408 0.3522 -0.0109 0.0042  0.0052  134 PHE   A CD2 
995  C CE1 . PHE   A 128 ? 0.2066 0.2477 0.3582 -0.0093 0.0060  0.0014  134 PHE   A CE1 
996  C CE2 . PHE   A 128 ? 0.2060 0.2561 0.3655 -0.0108 0.0073  0.0036  134 PHE   A CE2 
997  C CZ  . PHE   A 128 ? 0.2021 0.2469 0.3550 -0.0099 0.0084  0.0018  134 PHE   A CZ  
998  N N   . ALA   A 129 ? 0.1996 0.2422 0.3743 -0.0071 -0.0010 0.0092  135 ALA   A N   
999  C CA  . ALA   A 129 ? 0.2072 0.2485 0.3839 -0.0078 -0.0010 0.0125  135 ALA   A CA  
1000 C C   . ALA   A 129 ? 0.1945 0.2330 0.3624 -0.0116 0.0013  0.0137  135 ALA   A C   
1001 O O   . ALA   A 129 ? 0.1711 0.2064 0.3380 -0.0122 0.0041  0.0117  135 ALA   A O   
1002 C CB  . ALA   A 129 ? 0.2109 0.2485 0.3948 -0.0058 -0.0006 0.0115  135 ALA   A CB  
1003 N N   . ASP   A 130 ? 0.2032 0.2417 0.3646 -0.0144 0.0001  0.0172  136 ASP   A N   
1004 C CA  . ASP   A 130 ? 0.2075 0.2405 0.3570 -0.0187 0.0030  0.0176  136 ASP   A CA  
1005 C C   . ASP   A 130 ? 0.2218 0.2471 0.3706 -0.0191 0.0087  0.0181  136 ASP   A C   
1006 O O   . ASP   A 130 ? 0.2144 0.2389 0.3697 -0.0170 0.0086  0.0204  136 ASP   A O   
1007 C CB  . ASP   A 130 ? 0.2230 0.2559 0.3636 -0.0223 -0.0014 0.0216  136 ASP   A CB  
1008 C CG  . ASP   A 130 ? 0.2900 0.3153 0.4138 -0.0279 0.0011  0.0213  136 ASP   A CG  
1009 O OD1 . ASP   A 130 ? 0.3042 0.3289 0.4249 -0.0295 0.0037  0.0176  136 ASP   A OD1 
1010 O OD2 . ASP   A 130 ? 0.3369 0.3556 0.4494 -0.0310 0.0006  0.0246  136 ASP   A OD2 
1011 N N   . VAL   A 131 ? 0.2165 0.2356 0.3589 -0.0218 0.0147  0.0162  137 VAL   A N   
1012 C CA  . VAL   A 131 ? 0.2338 0.2442 0.3763 -0.0226 0.0223  0.0171  137 VAL   A CA  
1013 C C   . VAL   A 131 ? 0.2645 0.2647 0.3880 -0.0282 0.0279  0.0174  137 VAL   A C   
1014 O O   . VAL   A 131 ? 0.2801 0.2711 0.4011 -0.0295 0.0363  0.0180  137 VAL   A O   
1015 C CB  . VAL   A 131 ? 0.2305 0.2403 0.3872 -0.0204 0.0267  0.0146  137 VAL   A CB  
1016 C CG1 . VAL   A 131 ? 0.2262 0.2432 0.3976 -0.0159 0.0203  0.0139  137 VAL   A CG1 
1017 C CG2 . VAL   A 131 ? 0.2338 0.2429 0.3866 -0.0223 0.0291  0.0117  137 VAL   A CG2 
1018 N N   . ARG   A 132 ? 0.2702 0.2711 0.3807 -0.0319 0.0242  0.0165  138 ARG   A N   
1019 C CA  . ARG   A 132 ? 0.2860 0.2758 0.3754 -0.0382 0.0284  0.0159  138 ARG   A CA  
1020 C C   . ARG   A 132 ? 0.3121 0.2924 0.3857 -0.0413 0.0289  0.0201  138 ARG   A C   
1021 O O   . ARG   A 132 ? 0.3433 0.3101 0.3968 -0.0468 0.0351  0.0192  138 ARG   A O   
1022 C CB  . ARG   A 132 ? 0.2826 0.2762 0.3634 -0.0417 0.0218  0.0143  138 ARG   A CB  
1023 C CG  . ARG   A 132 ? 0.2788 0.2795 0.3714 -0.0394 0.0224  0.0105  138 ARG   A CG  
1024 C CD  . ARG   A 132 ? 0.2663 0.2712 0.3525 -0.0428 0.0155  0.0098  138 ARG   A CD  
1025 N NE  . ARG   A 132 ? 0.2495 0.2648 0.3441 -0.0404 0.0056  0.0133  138 ARG   A NE  
1026 C CZ  . ARG   A 132 ? 0.2680 0.2902 0.3654 -0.0417 -0.0009 0.0135  138 ARG   A CZ  
1027 N NH1 . ARG   A 132 ? 0.2811 0.3006 0.3713 -0.0460 0.0002  0.0104  138 ARG   A NH1 
1028 N NH2 . ARG   A 132 ? 0.2373 0.2686 0.3461 -0.0389 -0.0079 0.0169  138 ARG   A NH2 
1029 N N   . ASP   A 133 ? 0.2980 0.2835 0.3787 -0.0383 0.0229  0.0247  139 ASP   A N   
1030 C CA  . ASP   A 133 ? 0.3084 0.2842 0.3741 -0.0411 0.0232  0.0297  139 ASP   A CA  
1031 C C   . ASP   A 133 ? 0.3116 0.2785 0.3817 -0.0393 0.0351  0.0301  139 ASP   A C   
1032 O O   . ASP   A 133 ? 0.3410 0.2954 0.3946 -0.0425 0.0397  0.0335  139 ASP   A O   
1033 C CB  . ASP   A 133 ? 0.3064 0.2909 0.3790 -0.0388 0.0119  0.0354  139 ASP   A CB  
1034 C CG  . ASP   A 133 ? 0.3329 0.3276 0.4308 -0.0318 0.0115  0.0355  139 ASP   A CG  
1035 O OD1 . ASP   A 133 ? 0.3170 0.3186 0.4289 -0.0286 0.0131  0.0307  139 ASP   A OD1 
1036 O OD2 . ASP   A 133 ? 0.3555 0.3505 0.4585 -0.0297 0.0092  0.0404  139 ASP   A OD2 
1037 N N   . LEU   A 134 ? 0.2850 0.2574 0.3770 -0.0346 0.0400  0.0271  140 LEU   A N   
1038 C CA  . LEU   A 134 ? 0.2853 0.2511 0.3881 -0.0326 0.0507  0.0277  140 LEU   A CA  
1039 C C   . LEU   A 134 ? 0.3010 0.2526 0.3927 -0.0367 0.0644  0.0248  140 LEU   A C   
1040 O O   . LEU   A 134 ? 0.2890 0.2417 0.3960 -0.0350 0.0708  0.0215  140 LEU   A O   
1041 C CB  . LEU   A 134 ? 0.2661 0.2435 0.3976 -0.0267 0.0480  0.0258  140 LEU   A CB  
1042 C CG  . LEU   A 134 ? 0.2810 0.2703 0.4224 -0.0229 0.0364  0.0275  140 LEU   A CG  
1043 C CD1 . LEU   A 134 ? 0.2631 0.2612 0.4276 -0.0183 0.0334  0.0245  140 LEU   A CD1 
1044 C CD2 . LEU   A 134 ? 0.3026 0.2885 0.4415 -0.0225 0.0358  0.0328  140 LEU   A CD2 
1045 N N   . LEU   A 135 ? 0.3204 0.2575 0.3842 -0.0424 0.0688  0.0264  141 LEU   A N   
1046 C CA  . LEU   A 135 ? 0.3433 0.2643 0.3911 -0.0473 0.0824  0.0232  141 LEU   A CA  
1047 C C   . LEU   A 135 ? 0.3518 0.2652 0.4162 -0.0450 0.0982  0.0229  141 LEU   A C   
1048 O O   . LEU   A 135 ? 0.3524 0.2576 0.4183 -0.0467 0.1102  0.0190  141 LEU   A O   
1049 C CB  . LEU   A 135 ? 0.3805 0.2851 0.3914 -0.0544 0.0830  0.0255  141 LEU   A CB  
1050 C CG  . LEU   A 135 ? 0.4164 0.3270 0.4113 -0.0575 0.0663  0.0273  141 LEU   A CG  
1051 C CD1 . LEU   A 135 ? 0.4605 0.3517 0.4170 -0.0657 0.0671  0.0295  141 LEU   A CD1 
1052 C CD2 . LEU   A 135 ? 0.4169 0.3373 0.4173 -0.0581 0.0604  0.0221  141 LEU   A CD2 
1053 N N   . TRP   A 136 ? 0.3488 0.2646 0.4278 -0.0412 0.0987  0.0272  142 TRP   A N   
1054 C CA  . TRP   A 136 ? 0.3595 0.2692 0.4588 -0.0388 0.1129  0.0277  142 TRP   A CA  
1055 C C   . TRP   A 136 ? 0.3715 0.2915 0.5024 -0.0348 0.1138  0.0244  142 TRP   A C   
1056 O O   . TRP   A 136 ? 0.3827 0.2960 0.5309 -0.0340 0.1272  0.0241  142 TRP   A O   
1057 C CB  . TRP   A 136 ? 0.3493 0.2612 0.4596 -0.0355 0.1110  0.0331  142 TRP   A CB  
1058 C CG  . TRP   A 136 ? 0.3299 0.2604 0.4565 -0.0309 0.0941  0.0342  142 TRP   A CG  
1059 C CD1 . TRP   A 136 ? 0.3336 0.2698 0.4472 -0.0312 0.0814  0.0372  142 TRP   A CD1 
1060 C CD2 . TRP   A 136 ? 0.3104 0.2547 0.4694 -0.0256 0.0886  0.0326  142 TRP   A CD2 
1061 N NE1 . TRP   A 136 ? 0.3239 0.2758 0.4598 -0.0262 0.0703  0.0369  142 TRP   A NE1 
1062 C CE2 . TRP   A 136 ? 0.3078 0.2642 0.4696 -0.0230 0.0741  0.0339  142 TRP   A CE2 
1063 C CE3 . TRP   A 136 ? 0.3054 0.2519 0.4920 -0.0231 0.0944  0.0305  142 TRP   A CE3 
1064 C CZ2 . TRP   A 136 ? 0.2971 0.2664 0.4835 -0.0185 0.0656  0.0321  142 TRP   A CZ2 
1065 C CZ3 . TRP   A 136 ? 0.2946 0.2546 0.5064 -0.0188 0.0840  0.0297  142 TRP   A CZ3 
1066 C CH2 . TRP   A 136 ? 0.2915 0.2617 0.5011 -0.0167 0.0701  0.0300  142 TRP   A CH2 
1067 N N   . LEU   A 137 ? 0.3728 0.3080 0.5117 -0.0326 0.1001  0.0222  143 LEU   A N   
1068 C CA  . LEU   A 137 ? 0.3757 0.3193 0.5409 -0.0295 0.0996  0.0196  143 LEU   A CA  
1069 C C   . LEU   A 137 ? 0.4191 0.3512 0.5821 -0.0326 0.1141  0.0166  143 LEU   A C   
1070 O O   . LEU   A 137 ? 0.4029 0.3382 0.5920 -0.0301 0.1180  0.0160  143 LEU   A O   
1071 C CB  . LEU   A 137 ? 0.3611 0.3194 0.5273 -0.0277 0.0840  0.0178  143 LEU   A CB  
1072 C CG  . LEU   A 137 ? 0.3523 0.3228 0.5287 -0.0238 0.0708  0.0197  143 LEU   A CG  
1073 C CD1 . LEU   A 137 ? 0.3294 0.3108 0.5008 -0.0230 0.0584  0.0177  143 LEU   A CD1 
1074 C CD2 . LEU   A 137 ? 0.3498 0.3247 0.5563 -0.0197 0.0706  0.0206  143 LEU   A CD2 
1075 N N   . ASP   A 138 ? 0.4670 0.3853 0.5990 -0.0383 0.1215  0.0148  144 ASP   A N   
1076 C CA  . ASP   A 138 ? 0.5126 0.4178 0.6379 -0.0421 0.1362  0.0110  144 ASP   A CA  
1077 C C   . ASP   A 138 ? 0.5724 0.4609 0.7030 -0.0432 0.1567  0.0117  144 ASP   A C   
1078 O O   . ASP   A 138 ? 0.5853 0.4624 0.7159 -0.0457 0.1711  0.0085  144 ASP   A O   
1079 C CB  . ASP   A 138 ? 0.5270 0.4222 0.6139 -0.0487 0.1351  0.0080  144 ASP   A CB  
1080 C CG  . ASP   A 138 ? 0.5589 0.4681 0.6403 -0.0487 0.1180  0.0066  144 ASP   A CG  
1081 O OD1 . ASP   A 138 ? 0.5510 0.4765 0.6569 -0.0435 0.1088  0.0071  144 ASP   A OD1 
1082 O OD2 . ASP   A 138 ? 0.5840 0.4871 0.6360 -0.0541 0.1136  0.0051  144 ASP   A OD2 
1083 N N   . GLU   A 139 ? 0.6102 0.4958 0.7450 -0.0416 0.1594  0.0159  145 GLU   A N   
1084 C CA  . GLU   A 139 ? 0.6632 0.5312 0.8020 -0.0429 0.1806  0.0170  145 GLU   A CA  
1085 C C   . GLU   A 139 ? 0.6919 0.5657 0.8633 -0.0378 0.1824  0.0216  145 GLU   A C   
1086 O O   . GLU   A 139 ? 0.6910 0.5795 0.8719 -0.0343 0.1666  0.0243  145 GLU   A O   
1087 C CB  . GLU   A 139 ? 0.7233 0.5704 0.8176 -0.0495 0.1890  0.0168  145 GLU   A CB  
1088 C CG  . GLU   A 139 ? 0.7948 0.6469 0.8706 -0.0496 0.1742  0.0213  145 GLU   A CG  
1089 C CD  . GLU   A 139 ? 0.9072 0.7488 0.9376 -0.0564 0.1683  0.0202  145 GLU   A CD  
1090 O OE1 . GLU   A 139 ? 0.9266 0.7569 0.9318 -0.0593 0.1686  0.0243  145 GLU   A OE1 
1091 O OE2 . GLU   A 139 ? 0.9446 0.7888 0.9648 -0.0590 0.1627  0.0157  145 GLU   A OE2 
1092 N N   . GLU   A 140 ? 0.7163 0.5775 0.9052 -0.0377 0.2027  0.0225  146 GLU   A N   
1093 C CA  . GLU   A 140 ? 0.7320 0.5957 0.9543 -0.0337 0.2079  0.0270  146 GLU   A CA  
1094 C C   . GLU   A 140 ? 0.7305 0.6176 0.9879 -0.0280 0.1883  0.0287  146 GLU   A C   
1095 O O   . GLU   A 140 ? 0.7252 0.6169 1.0161 -0.0246 0.1897  0.0320  146 GLU   A O   
1096 C CB  . GLU   A 140 ? 0.7757 0.6267 0.9741 -0.0357 0.2140  0.0306  146 GLU   A CB  
1097 C CG  . GLU   A 140 ? 0.8437 0.7087 1.0428 -0.0328 0.1953  0.0343  146 GLU   A CG  
1098 C CD  . GLU   A 140 ? 0.9338 0.8051 1.1712 -0.0282 0.1968  0.0383  146 GLU   A CD  
1099 O OE1 . GLU   A 140 ? 0.9449 0.8309 1.1922 -0.0250 0.1799  0.0402  146 GLU   A OE1 
1100 O OE2 . GLU   A 140 ? 0.9643 0.8254 1.2233 -0.0279 0.2154  0.0395  146 GLU   A OE2 
1101 N N1  . A1B2X B .   ? 0.2295 0.2532 0.4301 0.0055  -0.0015 -0.0048 201 A1B2X A N1  
1102 C C4  . A1B2X B .   ? 0.3154 0.3105 0.4535 0.0021  0.0051  -0.0204 201 A1B2X A C4  
1103 C C5  . A1B2X B .   ? 0.3216 0.3093 0.4576 0.0033  0.0119  -0.0243 201 A1B2X A C5  
1104 C C6  . A1B2X B .   ? 0.3182 0.3036 0.4641 0.0043  0.0117  -0.0263 201 A1B2X A C6  
1105 C C7  . A1B2X B .   ? 0.2932 0.2981 0.4688 0.0058  0.0058  -0.0173 201 A1B2X A C7  
1106 C C8  . A1B2X B .   ? 0.2844 0.2924 0.4718 0.0058  0.0008  -0.0151 201 A1B2X A C8  
1107 C C10 . A1B2X B .   ? 0.2793 0.2851 0.4608 0.0036  -0.0064 -0.0156 201 A1B2X A C10 
1108 C C13 . A1B2X B .   ? 0.3343 0.3154 0.4592 0.0034  0.0200  -0.0266 201 A1B2X A C13 
1109 O O1  . A1B2X B .   ? 0.3242 0.2991 0.4595 0.0000  -0.0065 -0.0298 201 A1B2X A O1  
1110 C C12 . A1B2X B .   ? 0.3038 0.2901 0.4559 0.0020  -0.0039 -0.0253 201 A1B2X A C12 
1111 C C11 . A1B2X B .   ? 0.2924 0.2858 0.4596 0.0019  -0.0097 -0.0217 201 A1B2X A C11 
1112 C C9  . A1B2X B .   ? 0.2634 0.2820 0.4646 0.0069  0.0017  -0.0085 201 A1B2X A C9  
1113 O O   . A1B2X B .   ? 0.2681 0.2890 0.4800 0.0088  0.0052  -0.0065 201 A1B2X A O   
1114 N N   . A1B2X B .   ? 0.3065 0.2989 0.4644 0.0040  0.0041  -0.0232 201 A1B2X A N   
1115 C C3  . A1B2X B .   ? 0.3186 0.3151 0.4483 0.0012  0.0056  -0.0188 201 A1B2X A C3  
1116 C C2  . A1B2X B .   ? 0.3329 0.3232 0.4514 0.0013  0.0128  -0.0208 201 A1B2X A C2  
1117 C C1  . A1B2X B .   ? 0.3504 0.3327 0.4661 0.0024  0.0204  -0.0247 201 A1B2X A C1  
1118 S S   . A1B2X B .   ? 0.3761 0.3476 0.4765 0.0024  0.0321  -0.0275 201 A1B2X A S   
1119 C C   . A1B2X B .   ? 0.3669 0.3286 0.4704 0.0041  0.0424  -0.0326 201 A1B2X A C   
# 
