data_7HW5
# 
_entry.id   7HW5 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   7HW5         pdb_00007hw5 10.2210/pdb7hw5/pdb 
WWPDB D_1001408005 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-02-26 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.entry_id                        7HW5 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-10 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frank.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lithgo, R.M.'        1  ? 
'Fairhead, M.'        2  ? 
'Koekemoer, L.'       3  ? 
'Balcomb, B.H.'       4  ? 
'Capkin, E.'          5  ? 
'Chandran, A.V.'      6  ? 
'Golding, M.'         7  ? 
'Godoy, A.S.'         8  ? 
'Aschenbrenner, J.C.' 9  ? 
'Marples, P.G.'       10 ? 
'Ni, X.'              11 ? 
'Thompson, W.'        12 ? 
'Tomlinson, C.W.E.'   13 ? 
'Wild, C.'            14 ? 
'Winokan, M.'         15 ? 
'Xavier, M.-A.E.'     16 ? 
'Kenton, N.'          17 ? 
'Tucker, J.'          18 ? 
'DiPoto, M.'          19 ? 
'Lee, A.'             20 ? 
'Fearon, D.'          21 ? 
'von Delft, F.'       22 ? 
# 
_citation.id                        primary 
_citation.title                     
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Lithgo, R.M.'        ? 1  
primary 'Fairhead, M.'        ? 2  
primary 'Koekemoer, L.'       ? 3  
primary 'Balcomb, B.H.'       ? 4  
primary 'Capkin, E.'          ? 5  
primary 'Chandran, A.V.'      ? 6  
primary 'Golding, M.'         ? 7  
primary 'Godoy, A.S.'         ? 8  
primary 'Aschenbrenner, J.C.' ? 9  
primary 'Marples, P.G.'       ? 10 
primary 'Ni, X.'              ? 11 
primary 'Thompson, W.'        ? 12 
primary 'Tomlinson, C.W.E.'   ? 13 
primary 'Wild, C.'            ? 14 
primary 'Winokan, M.'         ? 15 
primary 'Xavier, M.-A.E.'     ? 16 
primary 'Kenton, N.'          ? 17 
primary 'Tucker, J.'          ? 18 
primary 'DiPoto, M.'          ? 19 
primary 'Lee, A.'             ? 20 
primary 'Fearon, D.'          ? 21 
primary 'von Delft, F.'       ? 22 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Protease 2A'                                             15892.732 1   3.4.22.29 ? ? ? 
2 non-polymer syn '4-methyl-N~1~-(2-methylphenyl)benzene-1,3-dicarboxamide' 268.310   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    117 ?         ? ? ? 
# 
_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 '4-methyl-N~1~-(2-methylphenyl)benzene-1,3-dicarboxamide' A1BTF 
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 
A1BTF non-polymer         . '4-methyl-N~1~-(2-methylphenyl)benzene-1,3-dicarboxamide' ? 'C16 H16 N2 O2'  268.310 
ALA   'L-peptide linking' y ALANINE                                                   ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                  ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                           ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                  ? 'C3 H7 N O2 S'   121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                      ? 'C2 H6 O S'      78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                 ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                           ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                   ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                 ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                     ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                   ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                    ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                             ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                   ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                    ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                 ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                                  ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                    ? 'C5 H11 N O2'    117.146 
ZN    non-polymer         . 'ZINC ION'                                                ? 'Zn 2'           65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   7   7   SER SER A . n 
A 1 2   GLY 2   8   8   GLY GLY A . n 
A 1 3   ALA 3   9   9   ALA ALA A . n 
A 1 4   ILE 4   10  10  ILE ILE A . n 
A 1 5   TYR 5   11  11  TYR TYR A . n 
A 1 6   VAL 6   12  12  VAL VAL A . n 
A 1 7   GLY 7   13  13  GLY GLY A . n 
A 1 8   ASN 8   14  14  ASN ASN A . n 
A 1 9   TYR 9   15  15  TYR TYR A . n 
A 1 10  ARG 10  16  16  ARG ARG A . n 
A 1 11  VAL 11  17  17  VAL VAL A . n 
A 1 12  VAL 12  18  18  VAL VAL A . n 
A 1 13  ASN 13  19  19  ASN ASN A . n 
A 1 14  ARG 14  20  20  ARG ARG A . n 
A 1 15  HIS 15  21  21  HIS HIS A . n 
A 1 16  LEU 16  22  22  LEU LEU A . n 
A 1 17  ALA 17  23  23  ALA ALA A . n 
A 1 18  THR 18  24  24  THR THR A . n 
A 1 19  HIS 19  25  25  HIS HIS A . n 
A 1 20  ASN 20  26  26  ASN ASN A . n 
A 1 21  ASP 21  27  27  ASP ASP A . n 
A 1 22  TRP 22  28  28  TRP TRP A . n 
A 1 23  ALA 23  29  29  ALA ALA A . n 
A 1 24  ASN 24  30  30  ASN ASN A . n 
A 1 25  LEU 25  31  31  LEU LEU A . n 
A 1 26  VAL 26  32  32  VAL VAL A . n 
A 1 27  TRP 27  33  33  TRP TRP A . n 
A 1 28  GLU 28  34  34  GLU GLU A . n 
A 1 29  ASP 29  35  35  ASP ASP A . n 
A 1 30  SER 30  36  36  SER SER A . n 
A 1 31  SER 31  37  37  SER SER A . n 
A 1 32  ARG 32  38  38  ARG ARG A . n 
A 1 33  ASP 33  39  39  ASP ASP A . n 
A 1 34  LEU 34  40  40  LEU LEU A . n 
A 1 35  LEU 35  41  41  LEU LEU A . n 
A 1 36  VAL 36  42  42  VAL VAL A . n 
A 1 37  SER 37  43  43  SER SER A . n 
A 1 38  SER 38  44  44  SER SER A . n 
A 1 39  THR 39  45  45  THR THR A . n 
A 1 40  THR 40  46  46  THR THR A . n 
A 1 41  ALA 41  47  47  ALA ALA A . n 
A 1 42  GLN 42  48  48  GLN GLN A . n 
A 1 43  GLY 43  49  49  GLY GLY A . n 
A 1 44  CYS 44  50  50  CYS CYS A . n 
A 1 45  ASP 45  51  51  ASP ASP A . n 
A 1 46  THR 46  52  52  THR THR A . n 
A 1 47  ILE 47  53  53  ILE ILE A . n 
A 1 48  ALA 48  54  54  ALA ALA A . n 
A 1 49  ARG 49  55  55  ARG ARG A . n 
A 1 50  CYS 50  56  56  CYS CYS A . n 
A 1 51  ASP 51  57  57  ASP ASP A . n 
A 1 52  CYS 52  58  58  CYS CYS A . n 
A 1 53  GLN 53  59  59  GLN GLN A . n 
A 1 54  THR 54  60  60  THR THR A . n 
A 1 55  GLY 55  61  61  GLY GLY A . n 
A 1 56  VAL 56  62  62  VAL VAL A . n 
A 1 57  TYR 57  63  63  TYR TYR A . n 
A 1 58  TYR 58  64  64  TYR TYR A . n 
A 1 59  CYS 59  65  65  CYS CYS A . n 
A 1 60  SER 60  66  66  SER SER A . n 
A 1 61  SER 61  67  67  SER SER A . n 
A 1 62  ARG 62  68  68  ARG ARG A . n 
A 1 63  ARG 63  69  69  ARG ARG A . n 
A 1 64  LYS 64  70  70  LYS LYS A . n 
A 1 65  HIS 65  71  71  HIS HIS A . n 
A 1 66  TYR 66  72  72  TYR TYR A . n 
A 1 67  PRO 67  73  73  PRO PRO A . n 
A 1 68  VAL 68  74  74  VAL VAL A . n 
A 1 69  SER 69  75  75  SER SER A . n 
A 1 70  PHE 70  76  76  PHE PHE A . n 
A 1 71  SER 71  77  77  SER SER A . n 
A 1 72  LYS 72  78  78  LYS LYS A . n 
A 1 73  PRO 73  79  79  PRO PRO A . n 
A 1 74  SER 74  80  80  SER SER A . n 
A 1 75  LEU 75  81  81  LEU LEU A . n 
A 1 76  ILE 76  82  82  ILE ILE A . n 
A 1 77  PHE 77  83  83  PHE PHE A . n 
A 1 78  VAL 78  84  84  VAL VAL A . n 
A 1 79  GLU 79  85  85  GLU GLU A . n 
A 1 80  ALA 80  86  86  ALA ALA A . n 
A 1 81  SER 81  87  87  SER SER A . n 
A 1 82  GLU 82  88  88  GLU GLU A . n 
A 1 83  TYR 83  89  89  TYR TYR A . n 
A 1 84  TYR 84  90  90  TYR TYR A . n 
A 1 85  PRO 85  91  91  PRO PRO A . n 
A 1 86  ALA 86  92  92  ALA ALA A . n 
A 1 87  ARG 87  93  93  ARG ARG A . n 
A 1 88  TYR 88  94  94  TYR TYR A . n 
A 1 89  GLN 89  95  95  GLN GLN A . n 
A 1 90  SER 90  96  96  SER SER A . n 
A 1 91  HIS 91  97  97  HIS HIS A . n 
A 1 92  LEU 92  98  98  LEU LEU A . n 
A 1 93  MET 93  99  99  MET MET A . n 
A 1 94  LEU 94  100 100 LEU LEU A . n 
A 1 95  ALA 95  101 101 ALA ALA A . n 
A 1 96  VAL 96  102 102 VAL VAL A . n 
A 1 97  GLY 97  103 103 GLY GLY A . n 
A 1 98  HIS 98  104 104 HIS HIS A . n 
A 1 99  SER 99  105 105 SER SER A . n 
A 1 100 GLU 100 106 106 GLU GLU A . n 
A 1 101 PRO 101 107 107 PRO PRO A . n 
A 1 102 GLY 102 108 108 GLY GLY A . n 
A 1 103 ASP 103 109 109 ASP ASP A . n 
A 1 104 CYS 104 110 110 CYS CYS A . n 
A 1 105 GLY 105 111 111 GLY GLY A . n 
A 1 106 GLY 106 112 112 GLY GLY A . n 
A 1 107 ILE 107 113 113 ILE ILE A . n 
A 1 108 LEU 108 114 114 LEU LEU A . n 
A 1 109 ARG 109 115 115 ARG ARG A . n 
A 1 110 CYS 110 116 116 CYS CYS A . n 
A 1 111 GLN 111 117 117 GLN GLN A . n 
A 1 112 HIS 112 118 118 HIS HIS A . n 
A 1 113 GLY 113 119 119 GLY GLY A . n 
A 1 114 VAL 114 120 120 VAL VAL A . n 
A 1 115 VAL 115 121 121 VAL VAL A . n 
A 1 116 GLY 116 122 122 GLY GLY A . n 
A 1 117 ILE 117 123 123 ILE ILE A . n 
A 1 118 VAL 118 124 124 VAL VAL A . n 
A 1 119 SER 119 125 125 SER SER A . n 
A 1 120 THR 120 126 126 THR THR A . n 
A 1 121 GLY 121 127 127 GLY GLY A . n 
A 1 122 GLY 122 128 128 GLY GLY A . n 
A 1 123 ASN 123 129 129 ASN ASN A . n 
A 1 124 GLY 124 130 130 GLY GLY A . n 
A 1 125 LEU 125 131 131 LEU LEU A . n 
A 1 126 VAL 126 132 132 VAL VAL A . n 
A 1 127 GLY 127 133 133 GLY GLY A . n 
A 1 128 PHE 128 134 134 PHE PHE A . n 
A 1 129 ALA 129 135 135 ALA ALA A . n 
A 1 130 ASP 130 136 136 ASP ASP A . n 
A 1 131 VAL 131 137 137 VAL VAL A . n 
A 1 132 ARG 132 138 138 ARG ARG A . n 
A 1 133 ASP 133 139 139 ASP ASP A . n 
A 1 134 LEU 134 140 140 LEU LEU A . n 
A 1 135 LEU 135 141 141 LEU LEU A . n 
A 1 136 TRP 136 142 142 TRP TRP A . n 
A 1 137 LEU 137 143 143 LEU LEU A . n 
A 1 138 ASP 138 144 144 ASP ASP A . n 
A 1 139 GLU 139 145 145 GLU GLU A . n 
A 1 140 GLU 140 146 ?   ?   ?   A . n 
A 1 141 ALA 141 147 ?   ?   ?   A . n 
A 1 142 MET 142 148 ?   ?   ?   A . n 
A 1 143 GLU 143 149 ?   ?   ?   A . n 
A 1 144 GLN 144 150 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BTF 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BTF 
_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 A1BTF 1   201 201 A1BTF LIG A . 
C 3 ZN    1   202 1   ZN    ZN  A . 
D 4 DMS   1   203 6   DMS   DMS A . 
E 4 DMS   1   204 7   DMS   DMS A . 
F 5 HOH   1   301 90  HOH   HOH A . 
F 5 HOH   2   302 116 HOH   HOH A . 
F 5 HOH   3   303 23  HOH   HOH A . 
F 5 HOH   4   304 54  HOH   HOH A . 
F 5 HOH   5   305 15  HOH   HOH A . 
F 5 HOH   6   306 62  HOH   HOH A . 
F 5 HOH   7   307 11  HOH   HOH A . 
F 5 HOH   8   308 65  HOH   HOH A . 
F 5 HOH   9   309 53  HOH   HOH A . 
F 5 HOH   10  310 83  HOH   HOH A . 
F 5 HOH   11  311 82  HOH   HOH A . 
F 5 HOH   12  312 67  HOH   HOH A . 
F 5 HOH   13  313 66  HOH   HOH A . 
F 5 HOH   14  314 102 HOH   HOH A . 
F 5 HOH   15  315 1   HOH   HOH A . 
F 5 HOH   16  316 41  HOH   HOH A . 
F 5 HOH   17  317 4   HOH   HOH A . 
F 5 HOH   18  318 101 HOH   HOH A . 
F 5 HOH   19  319 38  HOH   HOH A . 
F 5 HOH   20  320 98  HOH   HOH A . 
F 5 HOH   21  321 79  HOH   HOH A . 
F 5 HOH   22  322 60  HOH   HOH A . 
F 5 HOH   23  323 77  HOH   HOH A . 
F 5 HOH   24  324 80  HOH   HOH A . 
F 5 HOH   25  325 111 HOH   HOH A . 
F 5 HOH   26  326 45  HOH   HOH A . 
F 5 HOH   27  327 37  HOH   HOH A . 
F 5 HOH   28  328 69  HOH   HOH A . 
F 5 HOH   29  329 115 HOH   HOH A . 
F 5 HOH   30  330 36  HOH   HOH A . 
F 5 HOH   31  331 12  HOH   HOH A . 
F 5 HOH   32  332 104 HOH   HOH A . 
F 5 HOH   33  333 92  HOH   HOH A . 
F 5 HOH   34  334 119 HOH   HOH A . 
F 5 HOH   35  335 26  HOH   HOH A . 
F 5 HOH   36  336 14  HOH   HOH A . 
F 5 HOH   37  337 56  HOH   HOH A . 
F 5 HOH   38  338 48  HOH   HOH A . 
F 5 HOH   39  339 78  HOH   HOH A . 
F 5 HOH   40  340 118 HOH   HOH A . 
F 5 HOH   41  341 24  HOH   HOH A . 
F 5 HOH   42  342 3   HOH   HOH A . 
F 5 HOH   43  343 42  HOH   HOH A . 
F 5 HOH   44  344 29  HOH   HOH A . 
F 5 HOH   45  345 31  HOH   HOH A . 
F 5 HOH   46  346 43  HOH   HOH A . 
F 5 HOH   47  347 105 HOH   HOH A . 
F 5 HOH   48  348 68  HOH   HOH A . 
F 5 HOH   49  349 40  HOH   HOH A . 
F 5 HOH   50  350 96  HOH   HOH A . 
F 5 HOH   51  351 9   HOH   HOH A . 
F 5 HOH   52  352 28  HOH   HOH A . 
F 5 HOH   53  353 27  HOH   HOH A . 
F 5 HOH   54  354 18  HOH   HOH A . 
F 5 HOH   55  355 55  HOH   HOH A . 
F 5 HOH   56  356 63  HOH   HOH A . 
F 5 HOH   57  357 95  HOH   HOH A . 
F 5 HOH   58  358 5   HOH   HOH A . 
F 5 HOH   59  359 16  HOH   HOH A . 
F 5 HOH   60  360 70  HOH   HOH A . 
F 5 HOH   61  361 84  HOH   HOH A . 
F 5 HOH   62  362 71  HOH   HOH A . 
F 5 HOH   63  363 17  HOH   HOH A . 
F 5 HOH   64  364 10  HOH   HOH A . 
F 5 HOH   65  365 59  HOH   HOH A . 
F 5 HOH   66  366 8   HOH   HOH A . 
F 5 HOH   67  367 50  HOH   HOH A . 
F 5 HOH   68  368 13  HOH   HOH A . 
F 5 HOH   69  369 58  HOH   HOH A . 
F 5 HOH   70  370 85  HOH   HOH A . 
F 5 HOH   71  371 110 HOH   HOH A . 
F 5 HOH   72  372 64  HOH   HOH A . 
F 5 HOH   73  373 25  HOH   HOH A . 
F 5 HOH   74  374 97  HOH   HOH A . 
F 5 HOH   75  375 61  HOH   HOH A . 
F 5 HOH   76  376 44  HOH   HOH A . 
F 5 HOH   77  377 34  HOH   HOH A . 
F 5 HOH   78  378 76  HOH   HOH A . 
F 5 HOH   79  379 113 HOH   HOH A . 
F 5 HOH   80  380 57  HOH   HOH A . 
F 5 HOH   81  381 87  HOH   HOH A . 
F 5 HOH   82  382 103 HOH   HOH A . 
F 5 HOH   83  383 6   HOH   HOH A . 
F 5 HOH   84  384 19  HOH   HOH A . 
F 5 HOH   85  385 39  HOH   HOH A . 
F 5 HOH   86  386 33  HOH   HOH A . 
F 5 HOH   87  387 73  HOH   HOH A . 
F 5 HOH   88  388 72  HOH   HOH A . 
F 5 HOH   89  389 106 HOH   HOH A . 
F 5 HOH   90  390 91  HOH   HOH A . 
F 5 HOH   91  391 100 HOH   HOH A . 
F 5 HOH   92  392 35  HOH   HOH A . 
F 5 HOH   93  393 30  HOH   HOH A . 
F 5 HOH   94  394 32  HOH   HOH A . 
F 5 HOH   95  395 74  HOH   HOH A . 
F 5 HOH   96  396 22  HOH   HOH A . 
F 5 HOH   97  397 88  HOH   HOH A . 
F 5 HOH   98  398 120 HOH   HOH A . 
F 5 HOH   99  399 117 HOH   HOH A . 
F 5 HOH   100 400 107 HOH   HOH A . 
F 5 HOH   101 401 108 HOH   HOH A . 
F 5 HOH   102 402 7   HOH   HOH A . 
F 5 HOH   103 403 99  HOH   HOH A . 
F 5 HOH   104 404 51  HOH   HOH A . 
F 5 HOH   105 405 94  HOH   HOH A . 
F 5 HOH   106 406 20  HOH   HOH A . 
F 5 HOH   107 407 21  HOH   HOH A . 
F 5 HOH   108 408 86  HOH   HOH A . 
F 5 HOH   109 409 93  HOH   HOH A . 
F 5 HOH   110 410 75  HOH   HOH A . 
F 5 HOH   111 411 109 HOH   HOH A . 
F 5 HOH   112 412 89  HOH   HOH A . 
F 5 HOH   113 413 81  HOH   HOH A . 
F 5 HOH   114 414 114 HOH   HOH A . 
F 5 HOH   115 415 2   HOH   HOH A . 
F 5 HOH   116 416 121 HOH   HOH A . 
F 5 HOH   117 417 112 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           7HW5 
_cell.length_a           73.158 
_cell.length_b           60.843 
_cell.length_c           32.639 
_cell.angle_alpha        90.00 
_cell.angle_beta         92.78 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HW5 
_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          7HW5 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.28 
_exptl_crystal.density_percent_sol   46.12 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2024-11-16 
_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   0.92202 
_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        0.92202 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HW5 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             46.76 
_reflns.d_resolution_high            1.41 
_reflns.number_obs                   27625 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.061 
_reflns.pdbx_netI_over_sigmaI        12.4 
_reflns.pdbx_redundancy              6.3 
_reflns.pdbx_Rrim_I_all              0.067 
_reflns.pdbx_Rpim_I_all              0.026 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     175256 
_reflns.pdbx_chi_squared             0.86 
_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                  1.41 
_reflns_shell.d_res_low                   1.49 
_reflns_shell.number_measured_all         18527 
_reflns_shell.number_unique_obs           4018 
_reflns_shell.Rmerge_I_obs                1.039 
_reflns_shell.pdbx_chi_squared            0.69 
_reflns_shell.pdbx_redundancy             4.6 
_reflns_shell.percent_possible_obs        100.0 
_reflns_shell.pdbx_netI_over_sigmaI_obs   1.2 
_reflns_shell.pdbx_Rrim_I_all             1.181 
_reflns_shell.pdbx_Rpim_I_all             0.544 
_reflns_shell.pdbx_CC_half                0.477 
_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                                 7HW5 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     27592 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             16.86 
_refine.ls_d_res_high                            1.409 
_refine.ls_percent_reflns_obs                    99.9 
_refine.ls_R_factor_obs                          0.1870 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1858 
_refine.ls_R_factor_R_free                       0.2120 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.640 
_refine.ls_number_reflns_R_free                  1281 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.963 
_refine.correlation_coeff_Fo_to_Fc_free          0.951 
_refine.B_iso_mean                               25.54 
_refine.aniso_B[1][1]                            -2.28300 
_refine.aniso_B[2][2]                            0.42960 
_refine.aniso_B[3][3]                            1.85340 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -0.79240 
_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             0.061 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.063 
_refine.pdbx_overall_SU_R_Blow_DPI               0.063 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.064 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HW5 
_refine_analyze.Luzzati_coordinate_error_obs    0.18 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1074 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         29 
_refine_hist.number_atoms_solvent             117 
_refine_hist.number_atoms_total               1220 
_refine_hist.d_res_high                       1.409 
_refine_hist.d_res_low                        16.86 
# 
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                  0.012 ? 2.00  1141 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               0.99  ? 2.00  1553 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  373  '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  214  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1141 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           4.40  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           13.96 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  138  'X-RAY DIFFRACTION' SEMIHARMONIC 
t_sum_occupancies         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_distance        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_angle           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_torsion         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_ideal_dist_contact      ?     ? 4.00  973  '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                       1.41 
_refine_ls_shell.d_res_low                        1.42 
_refine_ls_shell.number_reflns_R_work             524 
_refine_ls_shell.R_factor_R_work                  0.3020 
_refine_ls_shell.percent_reflns_obs               98.10 
_refine_ls_shell.R_factor_R_free                  0.3715 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            5.07 
_refine_ls_shell.number_reflns_R_free             28 
_refine_ls_shell.number_reflns_all                552 
_refine_ls_shell.R_factor_all                     0.3053 
# 
_struct.entry_id                  7HW5 
_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-0032759-001 (A71EV2A-x3867)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HW5 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN, HYDROLASE
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
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              7HW5 
_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 GLU A 100 ? CYS A 104 ? GLU A 106 CYS A 110 5 ? 5 
HELX_P HELX_P4 AA4 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 ? ? ? ? ? ? ? 2.319 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.289 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.321 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 C ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.098 ? ? 
# 
_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_555 109.4 ? 
2 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 106.8 ? 
3 SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 117.3 ? 
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_555 109.4 ? 
5 SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 100.5 ? 
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_555 113.2 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA1 2 LEU A 34  ? CYS A 44  ? LEU A 40  CYS A 50  
AA1 3 ILE A 4   ? ASN A 13  ? ILE A 10  ASN A 19  
AA2 1 LYS A 64  ? SER A 69  ? LYS A 70  SER A 75  
AA2 2 THR A 54  ? CYS A 59  ? THR A 60  CYS A 65  
AA2 3 ILE A 107 ? CYS A 110 ? ILE A 113 CYS A 116 
AA2 4 GLY A 113 ? GLY A 122 ? GLY A 119 GLY A 128 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N TRP A 27  ? N TRP A 33  O VAL A 36  ? O VAL A 42  
AA1 2 3 N GLY A 43  ? N GLY A 49  O GLY A 7   ? O GLY A 13  
AA2 1 2 O LYS A 64  ? O LYS A 70  N CYS A 59  ? N CYS A 65  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N LEU A 108 ? N LEU A 114 O VAL A 115 ? O VAL A 121 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O PHE A 128 ? O PHE A 134 N MET A 93  ? N MET A 99  
AA2 6 7 O ARG A 87  ? O ARG A 93  N VAL A 78  ? N VAL A 84  
# 
_pdbx_entry_details.entry_id                   7HW5 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    302 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    330 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.91 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    SER 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     125 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -134.14 
_pdbx_validate_torsion.psi             -31.28 
# 
_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         15.3081 
_pdbx_refine_tls.origin_y         7.0088 
_pdbx_refine_tls.origin_z         14.4160 
_pdbx_refine_tls.T[1][1]          -0.0395 
_pdbx_refine_tls.T[2][2]          -0.0275 
_pdbx_refine_tls.T[3][3]          0.0081 
_pdbx_refine_tls.T[1][2]          -0.0056 
_pdbx_refine_tls.T[1][3]          -0.0016 
_pdbx_refine_tls.T[2][3]          -0.0033 
_pdbx_refine_tls.L[1][1]          1.2160 
_pdbx_refine_tls.L[2][2]          1.6183 
_pdbx_refine_tls.L[3][3]          0.5392 
_pdbx_refine_tls.L[1][2]          0.8102 
_pdbx_refine_tls.L[1][3]          -0.1293 
_pdbx_refine_tls.L[2][3]          -0.1683 
_pdbx_refine_tls.S[1][1]          -0.0362 
_pdbx_refine_tls.S[1][2]          0.0280 
_pdbx_refine_tls.S[1][3]          0.1343 
_pdbx_refine_tls.S[2][1]          0.0094 
_pdbx_refine_tls.S[2][2]          0.0643 
_pdbx_refine_tls.S[2][3]          -0.0393 
_pdbx_refine_tls.S[3][1]          0.0321 
_pdbx_refine_tls.S[3][2]          -0.0288 
_pdbx_refine_tls.S[3][3]          -0.0281 
# 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   '{ A|* }' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A GLU 146 ? A GLU 140 
2 1 Y 1 A ALA 147 ? A ALA 141 
3 1 Y 1 A MET 148 ? A MET 142 
4 1 Y 1 A GLU 149 ? A GLU 143 
5 1 Y 1 A GLN 150 ? A GLN 144 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1BTF N1   N  N N 1   
A1BTF C4   C  Y N 2   
A1BTF C5   C  Y N 3   
A1BTF C6   C  Y N 4   
A1BTF C7   C  N N 5   
A1BTF C8   C  Y N 6   
A1BTF C10  C  Y N 7   
A1BTF C13  C  Y N 8   
A1BTF C15  C  Y N 9   
A1BTF O1   O  N N 10  
A1BTF C14  C  N N 11  
A1BTF C11  C  Y N 12  
A1BTF C12  C  N N 13  
A1BTF C9   C  Y N 14  
A1BTF O    O  N N 15  
A1BTF N    N  N N 16  
A1BTF C1   C  Y N 17  
A1BTF C    C  N N 18  
A1BTF C3   C  Y N 19  
A1BTF C2   C  Y N 20  
A1BTF H14  H  N N 21  
A1BTF H13  H  N N 22  
A1BTF H5   H  N N 23  
A1BTF H6   H  N N 24  
A1BTF H9   H  N N 25  
A1BTF H15  H  N N 26  
A1BTF H12  H  N N 27  
A1BTF H11  H  N N 28  
A1BTF H10  H  N N 29  
A1BTF H8   H  N N 30  
A1BTF H7   H  N N 31  
A1BTF H1   H  N N 32  
A1BTF H2   H  N N 33  
A1BTF H    H  N N 34  
A1BTF H4   H  N N 35  
A1BTF H3   H  N N 36  
ALA   N    N  N N 37  
ALA   CA   C  N S 38  
ALA   C    C  N N 39  
ALA   O    O  N N 40  
ALA   CB   C  N N 41  
ALA   OXT  O  N N 42  
ALA   H    H  N N 43  
ALA   H2   H  N N 44  
ALA   HA   H  N N 45  
ALA   HB1  H  N N 46  
ALA   HB2  H  N N 47  
ALA   HB3  H  N N 48  
ALA   HXT  H  N N 49  
ARG   N    N  N N 50  
ARG   CA   C  N S 51  
ARG   C    C  N N 52  
ARG   O    O  N N 53  
ARG   CB   C  N N 54  
ARG   CG   C  N N 55  
ARG   CD   C  N N 56  
ARG   NE   N  N N 57  
ARG   CZ   C  N N 58  
ARG   NH1  N  N N 59  
ARG   NH2  N  N N 60  
ARG   OXT  O  N N 61  
ARG   H    H  N N 62  
ARG   H2   H  N N 63  
ARG   HA   H  N N 64  
ARG   HB2  H  N N 65  
ARG   HB3  H  N N 66  
ARG   HG2  H  N N 67  
ARG   HG3  H  N N 68  
ARG   HD2  H  N N 69  
ARG   HD3  H  N N 70  
ARG   HE   H  N N 71  
ARG   HH11 H  N N 72  
ARG   HH12 H  N N 73  
ARG   HH21 H  N N 74  
ARG   HH22 H  N N 75  
ARG   HXT  H  N N 76  
ASN   N    N  N N 77  
ASN   CA   C  N S 78  
ASN   C    C  N N 79  
ASN   O    O  N N 80  
ASN   CB   C  N N 81  
ASN   CG   C  N N 82  
ASN   OD1  O  N N 83  
ASN   ND2  N  N N 84  
ASN   OXT  O  N N 85  
ASN   H    H  N N 86  
ASN   H2   H  N N 87  
ASN   HA   H  N N 88  
ASN   HB2  H  N N 89  
ASN   HB3  H  N N 90  
ASN   HD21 H  N N 91  
ASN   HD22 H  N N 92  
ASN   HXT  H  N N 93  
ASP   N    N  N N 94  
ASP   CA   C  N S 95  
ASP   C    C  N N 96  
ASP   O    O  N N 97  
ASP   CB   C  N N 98  
ASP   CG   C  N N 99  
ASP   OD1  O  N N 100 
ASP   OD2  O  N N 101 
ASP   OXT  O  N N 102 
ASP   H    H  N N 103 
ASP   H2   H  N N 104 
ASP   HA   H  N N 105 
ASP   HB2  H  N N 106 
ASP   HB3  H  N N 107 
ASP   HD2  H  N N 108 
ASP   HXT  H  N N 109 
CYS   N    N  N N 110 
CYS   CA   C  N R 111 
CYS   C    C  N N 112 
CYS   O    O  N N 113 
CYS   CB   C  N N 114 
CYS   SG   S  N N 115 
CYS   OXT  O  N N 116 
CYS   H    H  N N 117 
CYS   H2   H  N N 118 
CYS   HA   H  N N 119 
CYS   HB2  H  N N 120 
CYS   HB3  H  N N 121 
CYS   HG   H  N N 122 
CYS   HXT  H  N N 123 
DMS   S    S  N N 124 
DMS   O    O  N N 125 
DMS   C1   C  N N 126 
DMS   C2   C  N N 127 
DMS   H11  H  N N 128 
DMS   H12  H  N N 129 
DMS   H13  H  N N 130 
DMS   H21  H  N N 131 
DMS   H22  H  N N 132 
DMS   H23  H  N N 133 
GLN   N    N  N N 134 
GLN   CA   C  N S 135 
GLN   C    C  N N 136 
GLN   O    O  N N 137 
GLN   CB   C  N N 138 
GLN   CG   C  N N 139 
GLN   CD   C  N N 140 
GLN   OE1  O  N N 141 
GLN   NE2  N  N N 142 
GLN   OXT  O  N N 143 
GLN   H    H  N N 144 
GLN   H2   H  N N 145 
GLN   HA   H  N N 146 
GLN   HB2  H  N N 147 
GLN   HB3  H  N N 148 
GLN   HG2  H  N N 149 
GLN   HG3  H  N N 150 
GLN   HE21 H  N N 151 
GLN   HE22 H  N N 152 
GLN   HXT  H  N N 153 
GLU   N    N  N N 154 
GLU   CA   C  N S 155 
GLU   C    C  N N 156 
GLU   O    O  N N 157 
GLU   CB   C  N N 158 
GLU   CG   C  N N 159 
GLU   CD   C  N N 160 
GLU   OE1  O  N N 161 
GLU   OE2  O  N N 162 
GLU   OXT  O  N N 163 
GLU   H    H  N N 164 
GLU   H2   H  N N 165 
GLU   HA   H  N N 166 
GLU   HB2  H  N N 167 
GLU   HB3  H  N N 168 
GLU   HG2  H  N N 169 
GLU   HG3  H  N N 170 
GLU   HE2  H  N N 171 
GLU   HXT  H  N N 172 
GLY   N    N  N N 173 
GLY   CA   C  N N 174 
GLY   C    C  N N 175 
GLY   O    O  N N 176 
GLY   OXT  O  N N 177 
GLY   H    H  N N 178 
GLY   H2   H  N N 179 
GLY   HA2  H  N N 180 
GLY   HA3  H  N N 181 
GLY   HXT  H  N N 182 
HIS   N    N  N N 183 
HIS   CA   C  N S 184 
HIS   C    C  N N 185 
HIS   O    O  N N 186 
HIS   CB   C  N N 187 
HIS   CG   C  Y N 188 
HIS   ND1  N  Y N 189 
HIS   CD2  C  Y N 190 
HIS   CE1  C  Y N 191 
HIS   NE2  N  Y N 192 
HIS   OXT  O  N N 193 
HIS   H    H  N N 194 
HIS   H2   H  N N 195 
HIS   HA   H  N N 196 
HIS   HB2  H  N N 197 
HIS   HB3  H  N N 198 
HIS   HD1  H  N N 199 
HIS   HD2  H  N N 200 
HIS   HE1  H  N N 201 
HIS   HE2  H  N N 202 
HIS   HXT  H  N N 203 
HOH   O    O  N N 204 
HOH   H1   H  N N 205 
HOH   H2   H  N N 206 
ILE   N    N  N N 207 
ILE   CA   C  N S 208 
ILE   C    C  N N 209 
ILE   O    O  N N 210 
ILE   CB   C  N S 211 
ILE   CG1  C  N N 212 
ILE   CG2  C  N N 213 
ILE   CD1  C  N N 214 
ILE   OXT  O  N N 215 
ILE   H    H  N N 216 
ILE   H2   H  N N 217 
ILE   HA   H  N N 218 
ILE   HB   H  N N 219 
ILE   HG12 H  N N 220 
ILE   HG13 H  N N 221 
ILE   HG21 H  N N 222 
ILE   HG22 H  N N 223 
ILE   HG23 H  N N 224 
ILE   HD11 H  N N 225 
ILE   HD12 H  N N 226 
ILE   HD13 H  N N 227 
ILE   HXT  H  N N 228 
LEU   N    N  N N 229 
LEU   CA   C  N S 230 
LEU   C    C  N N 231 
LEU   O    O  N N 232 
LEU   CB   C  N N 233 
LEU   CG   C  N N 234 
LEU   CD1  C  N N 235 
LEU   CD2  C  N N 236 
LEU   OXT  O  N N 237 
LEU   H    H  N N 238 
LEU   H2   H  N N 239 
LEU   HA   H  N N 240 
LEU   HB2  H  N N 241 
LEU   HB3  H  N N 242 
LEU   HG   H  N N 243 
LEU   HD11 H  N N 244 
LEU   HD12 H  N N 245 
LEU   HD13 H  N N 246 
LEU   HD21 H  N N 247 
LEU   HD22 H  N N 248 
LEU   HD23 H  N N 249 
LEU   HXT  H  N N 250 
LYS   N    N  N N 251 
LYS   CA   C  N S 252 
LYS   C    C  N N 253 
LYS   O    O  N N 254 
LYS   CB   C  N N 255 
LYS   CG   C  N N 256 
LYS   CD   C  N N 257 
LYS   CE   C  N N 258 
LYS   NZ   N  N N 259 
LYS   OXT  O  N N 260 
LYS   H    H  N N 261 
LYS   H2   H  N N 262 
LYS   HA   H  N N 263 
LYS   HB2  H  N N 264 
LYS   HB3  H  N N 265 
LYS   HG2  H  N N 266 
LYS   HG3  H  N N 267 
LYS   HD2  H  N N 268 
LYS   HD3  H  N N 269 
LYS   HE2  H  N N 270 
LYS   HE3  H  N N 271 
LYS   HZ1  H  N N 272 
LYS   HZ2  H  N N 273 
LYS   HZ3  H  N N 274 
LYS   HXT  H  N N 275 
MET   N    N  N N 276 
MET   CA   C  N S 277 
MET   C    C  N N 278 
MET   O    O  N N 279 
MET   CB   C  N N 280 
MET   CG   C  N N 281 
MET   SD   S  N N 282 
MET   CE   C  N N 283 
MET   OXT  O  N N 284 
MET   H    H  N N 285 
MET   H2   H  N N 286 
MET   HA   H  N N 287 
MET   HB2  H  N N 288 
MET   HB3  H  N N 289 
MET   HG2  H  N N 290 
MET   HG3  H  N N 291 
MET   HE1  H  N N 292 
MET   HE2  H  N N 293 
MET   HE3  H  N N 294 
MET   HXT  H  N N 295 
PHE   N    N  N N 296 
PHE   CA   C  N S 297 
PHE   C    C  N N 298 
PHE   O    O  N N 299 
PHE   CB   C  N N 300 
PHE   CG   C  Y N 301 
PHE   CD1  C  Y N 302 
PHE   CD2  C  Y N 303 
PHE   CE1  C  Y N 304 
PHE   CE2  C  Y N 305 
PHE   CZ   C  Y N 306 
PHE   OXT  O  N N 307 
PHE   H    H  N N 308 
PHE   H2   H  N N 309 
PHE   HA   H  N N 310 
PHE   HB2  H  N N 311 
PHE   HB3  H  N N 312 
PHE   HD1  H  N N 313 
PHE   HD2  H  N N 314 
PHE   HE1  H  N N 315 
PHE   HE2  H  N N 316 
PHE   HZ   H  N N 317 
PHE   HXT  H  N N 318 
PRO   N    N  N N 319 
PRO   CA   C  N S 320 
PRO   C    C  N N 321 
PRO   O    O  N N 322 
PRO   CB   C  N N 323 
PRO   CG   C  N N 324 
PRO   CD   C  N N 325 
PRO   OXT  O  N N 326 
PRO   H    H  N N 327 
PRO   HA   H  N N 328 
PRO   HB2  H  N N 329 
PRO   HB3  H  N N 330 
PRO   HG2  H  N N 331 
PRO   HG3  H  N N 332 
PRO   HD2  H  N N 333 
PRO   HD3  H  N N 334 
PRO   HXT  H  N N 335 
SER   N    N  N N 336 
SER   CA   C  N S 337 
SER   C    C  N N 338 
SER   O    O  N N 339 
SER   CB   C  N N 340 
SER   OG   O  N N 341 
SER   OXT  O  N N 342 
SER   H    H  N N 343 
SER   H2   H  N N 344 
SER   HA   H  N N 345 
SER   HB2  H  N N 346 
SER   HB3  H  N N 347 
SER   HG   H  N N 348 
SER   HXT  H  N N 349 
THR   N    N  N N 350 
THR   CA   C  N S 351 
THR   C    C  N N 352 
THR   O    O  N N 353 
THR   CB   C  N R 354 
THR   OG1  O  N N 355 
THR   CG2  C  N N 356 
THR   OXT  O  N N 357 
THR   H    H  N N 358 
THR   H2   H  N N 359 
THR   HA   H  N N 360 
THR   HB   H  N N 361 
THR   HG1  H  N N 362 
THR   HG21 H  N N 363 
THR   HG22 H  N N 364 
THR   HG23 H  N N 365 
THR   HXT  H  N N 366 
TRP   N    N  N N 367 
TRP   CA   C  N S 368 
TRP   C    C  N N 369 
TRP   O    O  N N 370 
TRP   CB   C  N N 371 
TRP   CG   C  Y N 372 
TRP   CD1  C  Y N 373 
TRP   CD2  C  Y N 374 
TRP   NE1  N  Y N 375 
TRP   CE2  C  Y N 376 
TRP   CE3  C  Y N 377 
TRP   CZ2  C  Y N 378 
TRP   CZ3  C  Y N 379 
TRP   CH2  C  Y N 380 
TRP   OXT  O  N N 381 
TRP   H    H  N N 382 
TRP   H2   H  N N 383 
TRP   HA   H  N N 384 
TRP   HB2  H  N N 385 
TRP   HB3  H  N N 386 
TRP   HD1  H  N N 387 
TRP   HE1  H  N N 388 
TRP   HE3  H  N N 389 
TRP   HZ2  H  N N 390 
TRP   HZ3  H  N N 391 
TRP   HH2  H  N N 392 
TRP   HXT  H  N N 393 
TYR   N    N  N N 394 
TYR   CA   C  N S 395 
TYR   C    C  N N 396 
TYR   O    O  N N 397 
TYR   CB   C  N N 398 
TYR   CG   C  Y N 399 
TYR   CD1  C  Y N 400 
TYR   CD2  C  Y N 401 
TYR   CE1  C  Y N 402 
TYR   CE2  C  Y N 403 
TYR   CZ   C  Y N 404 
TYR   OH   O  N N 405 
TYR   OXT  O  N N 406 
TYR   H    H  N N 407 
TYR   H2   H  N N 408 
TYR   HA   H  N N 409 
TYR   HB2  H  N N 410 
TYR   HB3  H  N N 411 
TYR   HD1  H  N N 412 
TYR   HD2  H  N N 413 
TYR   HE1  H  N N 414 
TYR   HE2  H  N N 415 
TYR   HH   H  N N 416 
TYR   HXT  H  N N 417 
VAL   N    N  N N 418 
VAL   CA   C  N S 419 
VAL   C    C  N N 420 
VAL   O    O  N N 421 
VAL   CB   C  N N 422 
VAL   CG1  C  N N 423 
VAL   CG2  C  N N 424 
VAL   OXT  O  N N 425 
VAL   H    H  N N 426 
VAL   H2   H  N N 427 
VAL   HA   H  N N 428 
VAL   HB   H  N N 429 
VAL   HG11 H  N N 430 
VAL   HG12 H  N N 431 
VAL   HG13 H  N N 432 
VAL   HG21 H  N N 433 
VAL   HG22 H  N N 434 
VAL   HG23 H  N N 435 
VAL   HXT  H  N N 436 
ZN    ZN   ZN N N 437 
# 
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 
A1BTF C   C1   sing N N 1   
A1BTF C1  C2   doub Y N 2   
A1BTF C2  C3   sing Y N 3   
A1BTF C3  C4   doub Y N 4   
A1BTF C4  C5   sing Y N 5   
A1BTF C5  C6   doub Y N 6   
A1BTF C1  C6   sing Y N 7   
A1BTF C6  N    sing N N 8   
A1BTF N   C7   sing N N 9   
A1BTF O   C7   doub N N 10  
A1BTF C7  C8   sing N N 11  
A1BTF C8  C9   doub Y N 12  
A1BTF C9  C10  sing Y N 13  
A1BTF C10 C11  doub Y N 14  
A1BTF C12 C11  sing N N 15  
A1BTF C11 C13  sing Y N 16  
A1BTF C13 C14  sing N N 17  
A1BTF N1  C14  sing N N 18  
A1BTF C14 O1   doub N N 19  
A1BTF C15 C13  doub Y N 20  
A1BTF C8  C15  sing Y N 21  
A1BTF N1  H14  sing N N 22  
A1BTF N1  H13  sing N N 23  
A1BTF C4  H5   sing N N 24  
A1BTF C5  H6   sing N N 25  
A1BTF C10 H9   sing N N 26  
A1BTF C15 H15  sing N N 27  
A1BTF C12 H12  sing N N 28  
A1BTF C12 H11  sing N N 29  
A1BTF C12 H10  sing N N 30  
A1BTF C9  H8   sing N N 31  
A1BTF N   H7   sing N N 32  
A1BTF C   H1   sing N N 33  
A1BTF C   H2   sing N N 34  
A1BTF C   H    sing N N 35  
A1BTF C3  H4   sing N N 36  
A1BTF C2  H3   sing N N 37  
ALA   N   CA   sing N N 38  
ALA   N   H    sing N N 39  
ALA   N   H2   sing N N 40  
ALA   CA  C    sing N N 41  
ALA   CA  CB   sing N N 42  
ALA   CA  HA   sing N N 43  
ALA   C   O    doub N N 44  
ALA   C   OXT  sing N N 45  
ALA   CB  HB1  sing N N 46  
ALA   CB  HB2  sing N N 47  
ALA   CB  HB3  sing N N 48  
ALA   OXT HXT  sing N N 49  
ARG   N   CA   sing N N 50  
ARG   N   H    sing N N 51  
ARG   N   H2   sing N N 52  
ARG   CA  C    sing N N 53  
ARG   CA  CB   sing N N 54  
ARG   CA  HA   sing N N 55  
ARG   C   O    doub N N 56  
ARG   C   OXT  sing N N 57  
ARG   CB  CG   sing N N 58  
ARG   CB  HB2  sing N N 59  
ARG   CB  HB3  sing N N 60  
ARG   CG  CD   sing N N 61  
ARG   CG  HG2  sing N N 62  
ARG   CG  HG3  sing N N 63  
ARG   CD  NE   sing N N 64  
ARG   CD  HD2  sing N N 65  
ARG   CD  HD3  sing N N 66  
ARG   NE  CZ   sing N N 67  
ARG   NE  HE   sing N N 68  
ARG   CZ  NH1  sing N N 69  
ARG   CZ  NH2  doub N N 70  
ARG   NH1 HH11 sing N N 71  
ARG   NH1 HH12 sing N N 72  
ARG   NH2 HH21 sing N N 73  
ARG   NH2 HH22 sing N N 74  
ARG   OXT HXT  sing N N 75  
ASN   N   CA   sing N N 76  
ASN   N   H    sing N N 77  
ASN   N   H2   sing N N 78  
ASN   CA  C    sing N N 79  
ASN   CA  CB   sing N N 80  
ASN   CA  HA   sing N N 81  
ASN   C   O    doub N N 82  
ASN   C   OXT  sing N N 83  
ASN   CB  CG   sing N N 84  
ASN   CB  HB2  sing N N 85  
ASN   CB  HB3  sing N N 86  
ASN   CG  OD1  doub N N 87  
ASN   CG  ND2  sing N N 88  
ASN   ND2 HD21 sing N N 89  
ASN   ND2 HD22 sing N N 90  
ASN   OXT HXT  sing N N 91  
ASP   N   CA   sing N N 92  
ASP   N   H    sing N N 93  
ASP   N   H2   sing N N 94  
ASP   CA  C    sing N N 95  
ASP   CA  CB   sing N N 96  
ASP   CA  HA   sing N N 97  
ASP   C   O    doub N N 98  
ASP   C   OXT  sing N N 99  
ASP   CB  CG   sing N N 100 
ASP   CB  HB2  sing N N 101 
ASP   CB  HB3  sing N N 102 
ASP   CG  OD1  doub N N 103 
ASP   CG  OD2  sing N N 104 
ASP   OD2 HD2  sing N N 105 
ASP   OXT HXT  sing N N 106 
CYS   N   CA   sing N N 107 
CYS   N   H    sing N N 108 
CYS   N   H2   sing N N 109 
CYS   CA  C    sing N N 110 
CYS   CA  CB   sing N N 111 
CYS   CA  HA   sing N N 112 
CYS   C   O    doub N N 113 
CYS   C   OXT  sing N N 114 
CYS   CB  SG   sing N N 115 
CYS   CB  HB2  sing N N 116 
CYS   CB  HB3  sing N N 117 
CYS   SG  HG   sing N N 118 
CYS   OXT HXT  sing N N 119 
DMS   S   O    doub N N 120 
DMS   S   C1   sing N N 121 
DMS   S   C2   sing N N 122 
DMS   C1  H11  sing N N 123 
DMS   C1  H12  sing N N 124 
DMS   C1  H13  sing N N 125 
DMS   C2  H21  sing N N 126 
DMS   C2  H22  sing N N 127 
DMS   C2  H23  sing N N 128 
GLN   N   CA   sing N N 129 
GLN   N   H    sing N N 130 
GLN   N   H2   sing N N 131 
GLN   CA  C    sing N N 132 
GLN   CA  CB   sing N N 133 
GLN   CA  HA   sing N N 134 
GLN   C   O    doub N N 135 
GLN   C   OXT  sing N N 136 
GLN   CB  CG   sing N N 137 
GLN   CB  HB2  sing N N 138 
GLN   CB  HB3  sing N N 139 
GLN   CG  CD   sing N N 140 
GLN   CG  HG2  sing N N 141 
GLN   CG  HG3  sing N N 142 
GLN   CD  OE1  doub N N 143 
GLN   CD  NE2  sing N N 144 
GLN   NE2 HE21 sing N N 145 
GLN   NE2 HE22 sing N N 146 
GLN   OXT HXT  sing N N 147 
GLU   N   CA   sing N N 148 
GLU   N   H    sing N N 149 
GLU   N   H2   sing N N 150 
GLU   CA  C    sing N N 151 
GLU   CA  CB   sing N N 152 
GLU   CA  HA   sing N N 153 
GLU   C   O    doub N N 154 
GLU   C   OXT  sing N N 155 
GLU   CB  CG   sing N N 156 
GLU   CB  HB2  sing N N 157 
GLU   CB  HB3  sing N N 158 
GLU   CG  CD   sing N N 159 
GLU   CG  HG2  sing N N 160 
GLU   CG  HG3  sing N N 161 
GLU   CD  OE1  doub N N 162 
GLU   CD  OE2  sing N N 163 
GLU   OE2 HE2  sing N N 164 
GLU   OXT HXT  sing N N 165 
GLY   N   CA   sing N N 166 
GLY   N   H    sing N N 167 
GLY   N   H2   sing N N 168 
GLY   CA  C    sing N N 169 
GLY   CA  HA2  sing N N 170 
GLY   CA  HA3  sing N N 171 
GLY   C   O    doub N N 172 
GLY   C   OXT  sing N N 173 
GLY   OXT HXT  sing N N 174 
HIS   N   CA   sing N N 175 
HIS   N   H    sing N N 176 
HIS   N   H2   sing N N 177 
HIS   CA  C    sing N N 178 
HIS   CA  CB   sing N N 179 
HIS   CA  HA   sing N N 180 
HIS   C   O    doub N N 181 
HIS   C   OXT  sing N N 182 
HIS   CB  CG   sing N N 183 
HIS   CB  HB2  sing N N 184 
HIS   CB  HB3  sing N N 185 
HIS   CG  ND1  sing Y N 186 
HIS   CG  CD2  doub Y N 187 
HIS   ND1 CE1  doub Y N 188 
HIS   ND1 HD1  sing N N 189 
HIS   CD2 NE2  sing Y N 190 
HIS   CD2 HD2  sing N N 191 
HIS   CE1 NE2  sing Y N 192 
HIS   CE1 HE1  sing N N 193 
HIS   NE2 HE2  sing N N 194 
HIS   OXT HXT  sing N N 195 
HOH   O   H1   sing N N 196 
HOH   O   H2   sing N N 197 
ILE   N   CA   sing N N 198 
ILE   N   H    sing N N 199 
ILE   N   H2   sing N N 200 
ILE   CA  C    sing N N 201 
ILE   CA  CB   sing N N 202 
ILE   CA  HA   sing N N 203 
ILE   C   O    doub N N 204 
ILE   C   OXT  sing N N 205 
ILE   CB  CG1  sing N N 206 
ILE   CB  CG2  sing N N 207 
ILE   CB  HB   sing N N 208 
ILE   CG1 CD1  sing N N 209 
ILE   CG1 HG12 sing N N 210 
ILE   CG1 HG13 sing N N 211 
ILE   CG2 HG21 sing N N 212 
ILE   CG2 HG22 sing N N 213 
ILE   CG2 HG23 sing N N 214 
ILE   CD1 HD11 sing N N 215 
ILE   CD1 HD12 sing N N 216 
ILE   CD1 HD13 sing N N 217 
ILE   OXT HXT  sing N N 218 
LEU   N   CA   sing N N 219 
LEU   N   H    sing N N 220 
LEU   N   H2   sing N N 221 
LEU   CA  C    sing N N 222 
LEU   CA  CB   sing N N 223 
LEU   CA  HA   sing N N 224 
LEU   C   O    doub N N 225 
LEU   C   OXT  sing N N 226 
LEU   CB  CG   sing N N 227 
LEU   CB  HB2  sing N N 228 
LEU   CB  HB3  sing N N 229 
LEU   CG  CD1  sing N N 230 
LEU   CG  CD2  sing N N 231 
LEU   CG  HG   sing N N 232 
LEU   CD1 HD11 sing N N 233 
LEU   CD1 HD12 sing N N 234 
LEU   CD1 HD13 sing N N 235 
LEU   CD2 HD21 sing N N 236 
LEU   CD2 HD22 sing N N 237 
LEU   CD2 HD23 sing N N 238 
LEU   OXT HXT  sing N N 239 
LYS   N   CA   sing N N 240 
LYS   N   H    sing N N 241 
LYS   N   H2   sing N N 242 
LYS   CA  C    sing N N 243 
LYS   CA  CB   sing N N 244 
LYS   CA  HA   sing N N 245 
LYS   C   O    doub N N 246 
LYS   C   OXT  sing N N 247 
LYS   CB  CG   sing N N 248 
LYS   CB  HB2  sing N N 249 
LYS   CB  HB3  sing N N 250 
LYS   CG  CD   sing N N 251 
LYS   CG  HG2  sing N N 252 
LYS   CG  HG3  sing N N 253 
LYS   CD  CE   sing N N 254 
LYS   CD  HD2  sing N N 255 
LYS   CD  HD3  sing N N 256 
LYS   CE  NZ   sing N N 257 
LYS   CE  HE2  sing N N 258 
LYS   CE  HE3  sing N N 259 
LYS   NZ  HZ1  sing N N 260 
LYS   NZ  HZ2  sing N N 261 
LYS   NZ  HZ3  sing N N 262 
LYS   OXT HXT  sing N N 263 
MET   N   CA   sing N N 264 
MET   N   H    sing N N 265 
MET   N   H2   sing N N 266 
MET   CA  C    sing N N 267 
MET   CA  CB   sing N N 268 
MET   CA  HA   sing N N 269 
MET   C   O    doub N N 270 
MET   C   OXT  sing N N 271 
MET   CB  CG   sing N N 272 
MET   CB  HB2  sing N N 273 
MET   CB  HB3  sing N N 274 
MET   CG  SD   sing N N 275 
MET   CG  HG2  sing N N 276 
MET   CG  HG3  sing N N 277 
MET   SD  CE   sing N N 278 
MET   CE  HE1  sing N N 279 
MET   CE  HE2  sing N N 280 
MET   CE  HE3  sing N N 281 
MET   OXT HXT  sing N N 282 
PHE   N   CA   sing N N 283 
PHE   N   H    sing N N 284 
PHE   N   H2   sing N N 285 
PHE   CA  C    sing N N 286 
PHE   CA  CB   sing N N 287 
PHE   CA  HA   sing N N 288 
PHE   C   O    doub N N 289 
PHE   C   OXT  sing N N 290 
PHE   CB  CG   sing N N 291 
PHE   CB  HB2  sing N N 292 
PHE   CB  HB3  sing N N 293 
PHE   CG  CD1  doub Y N 294 
PHE   CG  CD2  sing Y N 295 
PHE   CD1 CE1  sing Y N 296 
PHE   CD1 HD1  sing N N 297 
PHE   CD2 CE2  doub Y N 298 
PHE   CD2 HD2  sing N N 299 
PHE   CE1 CZ   doub Y N 300 
PHE   CE1 HE1  sing N N 301 
PHE   CE2 CZ   sing Y N 302 
PHE   CE2 HE2  sing N N 303 
PHE   CZ  HZ   sing N N 304 
PHE   OXT HXT  sing N N 305 
PRO   N   CA   sing N N 306 
PRO   N   CD   sing N N 307 
PRO   N   H    sing N N 308 
PRO   CA  C    sing N N 309 
PRO   CA  CB   sing N N 310 
PRO   CA  HA   sing N N 311 
PRO   C   O    doub N N 312 
PRO   C   OXT  sing N N 313 
PRO   CB  CG   sing N N 314 
PRO   CB  HB2  sing N N 315 
PRO   CB  HB3  sing N N 316 
PRO   CG  CD   sing N N 317 
PRO   CG  HG2  sing N N 318 
PRO   CG  HG3  sing N N 319 
PRO   CD  HD2  sing N N 320 
PRO   CD  HD3  sing N N 321 
PRO   OXT HXT  sing N N 322 
SER   N   CA   sing N N 323 
SER   N   H    sing N N 324 
SER   N   H2   sing N N 325 
SER   CA  C    sing N N 326 
SER   CA  CB   sing N N 327 
SER   CA  HA   sing N N 328 
SER   C   O    doub N N 329 
SER   C   OXT  sing N N 330 
SER   CB  OG   sing N N 331 
SER   CB  HB2  sing N N 332 
SER   CB  HB3  sing N N 333 
SER   OG  HG   sing N N 334 
SER   OXT HXT  sing N N 335 
THR   N   CA   sing N N 336 
THR   N   H    sing N N 337 
THR   N   H2   sing N N 338 
THR   CA  C    sing N N 339 
THR   CA  CB   sing N N 340 
THR   CA  HA   sing N N 341 
THR   C   O    doub N N 342 
THR   C   OXT  sing N N 343 
THR   CB  OG1  sing N N 344 
THR   CB  CG2  sing N N 345 
THR   CB  HB   sing N N 346 
THR   OG1 HG1  sing N N 347 
THR   CG2 HG21 sing N N 348 
THR   CG2 HG22 sing N N 349 
THR   CG2 HG23 sing N N 350 
THR   OXT HXT  sing N N 351 
TRP   N   CA   sing N N 352 
TRP   N   H    sing N N 353 
TRP   N   H2   sing N N 354 
TRP   CA  C    sing N N 355 
TRP   CA  CB   sing N N 356 
TRP   CA  HA   sing N N 357 
TRP   C   O    doub N N 358 
TRP   C   OXT  sing N N 359 
TRP   CB  CG   sing N N 360 
TRP   CB  HB2  sing N N 361 
TRP   CB  HB3  sing N N 362 
TRP   CG  CD1  doub Y N 363 
TRP   CG  CD2  sing Y N 364 
TRP   CD1 NE1  sing Y N 365 
TRP   CD1 HD1  sing N N 366 
TRP   CD2 CE2  doub Y N 367 
TRP   CD2 CE3  sing Y N 368 
TRP   NE1 CE2  sing Y N 369 
TRP   NE1 HE1  sing N N 370 
TRP   CE2 CZ2  sing Y N 371 
TRP   CE3 CZ3  doub Y N 372 
TRP   CE3 HE3  sing N N 373 
TRP   CZ2 CH2  doub Y N 374 
TRP   CZ2 HZ2  sing N N 375 
TRP   CZ3 CH2  sing Y N 376 
TRP   CZ3 HZ3  sing N N 377 
TRP   CH2 HH2  sing N N 378 
TRP   OXT HXT  sing N N 379 
TYR   N   CA   sing N N 380 
TYR   N   H    sing N N 381 
TYR   N   H2   sing N N 382 
TYR   CA  C    sing N N 383 
TYR   CA  CB   sing N N 384 
TYR   CA  HA   sing N N 385 
TYR   C   O    doub N N 386 
TYR   C   OXT  sing N N 387 
TYR   CB  CG   sing N N 388 
TYR   CB  HB2  sing N N 389 
TYR   CB  HB3  sing N N 390 
TYR   CG  CD1  doub Y N 391 
TYR   CG  CD2  sing Y N 392 
TYR   CD1 CE1  sing Y N 393 
TYR   CD1 HD1  sing N N 394 
TYR   CD2 CE2  doub Y N 395 
TYR   CD2 HD2  sing N N 396 
TYR   CE1 CZ   doub Y N 397 
TYR   CE1 HE1  sing N N 398 
TYR   CE2 CZ   sing Y N 399 
TYR   CE2 HE2  sing N N 400 
TYR   CZ  OH   sing N N 401 
TYR   OH  HH   sing N N 402 
TYR   OXT HXT  sing N N 403 
VAL   N   CA   sing N N 404 
VAL   N   H    sing N N 405 
VAL   N   H2   sing N N 406 
VAL   CA  C    sing N N 407 
VAL   CA  CB   sing N N 408 
VAL   CA  HA   sing N N 409 
VAL   C   O    doub N N 410 
VAL   C   OXT  sing N N 411 
VAL   CB  CG1  sing N N 412 
VAL   CB  CG2  sing N N 413 
VAL   CB  HB   sing N N 414 
VAL   CG1 HG11 sing N N 415 
VAL   CG1 HG12 sing N N 416 
VAL   CG1 HG13 sing N N 417 
VAL   CG2 HG21 sing N N 418 
VAL   CG2 HG22 sing N N 419 
VAL   CG2 HG23 sing N N 420 
VAL   OXT HXT  sing N N 421 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171399 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002329 
_pdbx_deposit_group.group_description   
'Crystollographic structure of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitor' 
_pdbx_deposit_group.group_title         
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8POA 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    7HW5 
_atom_sites.fract_transf_matrix[1][1]   0.013669 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000664 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016436 
_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]   0.030674 
_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   ? 19.327 6.340   24.201 1.00 25.12 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 20.497 6.394   23.322 1.00 25.30 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 20.504 5.255   22.296 1.00 24.95 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 19.715 4.303   22.419 1.00 27.22 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 21.793 6.408   24.136 1.00 28.64 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 21.886 5.261   24.966 1.00 32.58 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 21.344 5.391   21.268 1.00 22.38 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 21.467 4.377   20.238 1.00 20.02 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 21.832 4.949   18.888 1.00 19.03 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 21.509 6.099   18.587 1.00 20.26 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 22.516 4.141   18.078 1.00 18.71 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 22.898 4.570   16.744 1.00 18.81 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 22.867 3.398   15.758 1.00 18.05 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 22.885 2.229   16.175 1.00 19.50 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 24.327 5.130   16.784 1.00 20.58 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 22.812 3.723   14.464 1.00 17.07 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.941 2.775   13.353 1.00 17.62 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 24.317 2.929   12.719 1.00 18.96 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.720 4.059   12.399 1.00 19.06 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.879 3.009   12.249 1.00 18.09 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 20.466 3.015   12.846 1.00 18.29 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.996 1.915   11.151 1.00 20.00 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.416 3.664   11.867 1.00 19.70 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 25.044 1.808   12.497 1.00 20.76 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 26.349 1.870   11.890 1.00 21.81 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 26.317 1.149   10.556 1.00 23.12 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 26.208 -0.076  10.541 1.00 24.49 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.409 1.251   12.825 1.00 22.21 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.582 2.043   14.105 1.00 23.28 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 28.417 3.146   14.154 1.00 24.10 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 26.827 1.754   15.230 1.00 24.47 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 28.551 3.899   15.325 1.00 24.70 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 26.957 2.492   16.399 1.00 25.04 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 27.803 3.574   16.436 1.00 26.02 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 27.903 4.304   17.598 1.00 28.39 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 26.401 1.893   9.441  1.00 22.60 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 26.355 1.315   8.104  1.00 23.78 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.456 1.924   7.272  1.00 25.77 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.593 3.147   7.188  1.00 25.77 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.942 1.489   7.470  1.00 26.14 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.485 2.945   7.537  1.00 25.98 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.922 0.971   6.031  1.00 28.96 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.341 1.073   6.737  1.00 26.79 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.486 1.558   5.965  1.00 27.23 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.329 2.508   6.798  1.00 27.21 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.594 2.211   7.961  1.00 29.07 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.658 3.678   6.267  1.00 26.60 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.396 4.673   7.044  1.00 27.24 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.459 5.782   7.560  1.00 25.86 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.864 6.925   7.643  1.00 25.48 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.539 5.253   6.247  1.00 30.92 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.622 4.241   6.018  1.00 38.20 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.454 3.974   6.894  1.00 40.94 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.588 3.607   4.866  1.00 40.10 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.247 5.409   7.955  1.00 23.67 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.277 6.361   8.489  1.00 22.44 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.748 5.915   9.848  1.00 21.04 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.606 4.703   10.120 1.00 21.44 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 27.065 6.501   7.543  1.00 23.04 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.397 7.048   6.176  1.00 24.87 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 28.044 8.270   6.034  1.00 26.57 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.047 6.354   5.022  1.00 26.69 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.355 8.779   4.781  1.00 27.96 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.331 6.868   3.758  1.00 28.12 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 27.985 8.083   3.646  1.00 29.41 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.277 8.620   2.412  1.00 33.26 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.374 6.909   10.670 1.00 19.68 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.737 6.700   11.963 1.00 19.16 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.462 7.519   11.932 1.00 18.29 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.522 8.723   11.676 1.00 18.72 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.667 7.153   13.109 1.00 20.88 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 27.019 7.341   14.483 1.00 23.14 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 28.047 7.611   15.586 1.00 24.10 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 27.604 8.609   16.550 1.00 23.88 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 27.173 8.346   17.780 1.00 25.81 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 27.096 7.087   18.213 1.00 26.65 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 26.819 9.338   18.592 1.00 25.94 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 24.300 6.866   12.128 1.00 17.64 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 23.003 7.565   12.143 1.00 17.20 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.538 7.680   13.591 1.00 16.86 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 22.402 6.645   14.279 1.00 17.52 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.940 6.796   11.332 1.00 18.34 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.644 7.629   11.209 1.00 19.00 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.497 6.415   9.950  1.00 19.60 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 22.241 8.912   14.035 1.00 16.17 ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 21.788 9.140   15.402 1.00 16.72 ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 20.561 10.091  15.410 1.00 16.38 ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 20.291 10.806  14.426 1.00 17.63 ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 22.911 9.745   16.279 1.00 18.45 ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 24.019 8.719   16.505 1.00 21.53 ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 23.473 11.040  15.660 1.00 19.40 ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 19.864 10.177  16.544 1.00 15.04 ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 18.821 11.225  16.701 1.00 15.99 ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 19.585 12.560  16.683 1.00 15.88 ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 20.591 12.714  17.380 1.00 16.35 ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 18.135 11.093  18.058 1.00 16.58 ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 17.269 9.861   18.173 1.00 16.71 ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.746 8.776   18.588 1.00 17.30 ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 15.980 10.006  17.791 1.00 17.59 ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 19.098 13.524  15.901 1.00 15.67 ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 19.787 14.839  15.810 1.00 16.33 ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 19.897 15.490  17.197 1.00 16.97 ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 20.961 16.049  17.498 1.00 17.94 ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 18.990 15.751  14.886 1.00 17.19 ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.720 17.027  14.497 1.00 17.49 ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 18.769 17.854  13.640 1.00 18.70 ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.390 19.092  13.136 1.00 18.96 ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.450 20.222  13.831 1.00 21.45 ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 19.049 20.254  15.093 1.00 22.78 ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 19.968 21.330  13.281 1.00 21.62 ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 18.852 15.360  18.058 1.00 17.38 ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 18.953 15.983  19.402 1.00 18.24 ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 19.919 15.301  20.367 1.00 20.30 ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 20.228 15.893  21.418 1.00 22.89 ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 17.578 16.130  20.050 1.00 19.47 ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 16.922 14.856  20.490 1.00 20.42 ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 16.209 14.045  19.601 1.00 20.74 ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 16.840 14.323  21.733 1.00 21.46 ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 15.674 13.082  20.351 1.00 21.40 ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 16.067 13.180  21.627 1.00 21.99 ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 20.413 14.104  20.017 1.00 19.11 ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 21.385 13.402  20.844 1.00 19.79 ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 22.789 13.414  20.231 1.00 20.90 ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 23.718 12.843  20.813 1.00 22.58 ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 20.925 11.949  21.123 1.00 19.82 ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 19.564 11.866  21.830 1.00 22.22 ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 19.122 10.424  22.038 1.00 22.84 ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 19.624 12.540  23.214 1.00 23.85 ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 22.964 14.048  19.031 1.00 19.63 ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 24.278 14.091  18.417 1.00 21.13 ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 25.336 14.745  19.313 1.00 21.58 ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 25.037 15.713  19.998 1.00 21.61 ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 24.181 14.818  17.103 1.00 21.59 ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 26.539 14.190  19.328 1.00 21.78 ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 27.632 14.701  20.164 1.00 22.51 ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 28.463 15.762  19.395 1.00 23.52 ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 28.275 15.958  18.202 1.00 23.39 ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 28.534 13.504  20.549 1.00 23.60 ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 29.226 13.086  19.375 1.00 24.35 ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 27.760 12.339  21.165 1.00 24.73 ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 29.459 16.396  20.066 1.00 24.71 ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 30.371 17.317  19.375 1.00 25.25 ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 31.111 16.606  18.244 1.00 24.69 ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 31.289 17.179  17.171 1.00 25.28 ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 31.414 17.923  20.344 1.00 28.49 ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 30.817 18.771  21.415 1.00 38.29 ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 30.363 20.053  21.151 1.00 42.25 ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 30.650 18.508  22.733 1.00 41.69 ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 29.919 20.522  22.308 1.00 43.74 ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 30.048 19.618  23.285 1.00 43.75 ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 31.504 15.341  18.459 1.00 23.39 ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 32.221 14.601  17.408 1.00 23.99 ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 31.300 14.367  16.221 1.00 22.31 ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 31.728 14.472  15.069 1.00 22.87 ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 32.748 13.282  17.953 1.00 27.43 ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 33.540 12.468  16.937 1.00 36.79 ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.634 12.866  16.511 1.00 40.46 ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 33.018 11.300  16.538 1.00 39.53 ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 29.985 14.067  16.474 1.00 20.97 ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 29.065 13.910  15.349 1.00 20.76 ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 28.984 15.203  14.522 1.00 21.13 ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 29.014 15.150  13.285 1.00 22.13 ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 27.637 13.567  15.840 1.00 19.93 ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 27.498 12.154  16.346 1.00 22.96 ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 28.023 11.245  15.698 1.00 24.08 ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 26.851 11.962  17.384 1.00 22.57 ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 28.822 16.364  15.201 1.00 22.04 ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.713 17.651  14.505 1.00 21.73 ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 30.046 18.036  13.799 1.00 23.05 ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 30.007 18.594  12.709 1.00 23.42 ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 28.272 18.766  15.481 1.00 20.88 ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 26.783 18.799  15.695 1.00 20.79 ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 26.105 18.365  16.789 1.00 21.71 ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 25.804 19.296  14.779 1.00 20.22 ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 24.739 18.554  16.610 1.00 21.01 ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 24.532 19.113  15.376 1.00 21.05 ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 25.870 19.853  13.497 1.00 21.29 ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 23.343 19.511  14.746 1.00 20.74 ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.690 20.271  12.886 1.00 21.21 ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 23.450 20.081  13.500 1.00 21.02 ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 31.192 17.649  14.374 1.00 23.79 ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.496 17.923  13.746 1.00 25.61 ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.762 17.055  12.511 1.00 25.97 ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.677 17.347  11.739 1.00 27.31 ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 33.611 17.710  14.759 1.00 26.48 ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 32.035 15.919  12.385 1.00 23.41 ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 32.181 14.997  11.234 1.00 23.36 ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.827 14.889  10.498 1.00 22.80 ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.470 13.814  10.004 1.00 22.40 ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.619 13.610  11.731 1.00 24.10 ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 34.033 13.632  12.295 1.00 28.15 ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 35.021 13.637  11.553 1.00 29.59 ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 34.155 13.717  13.612 1.00 30.38 ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 30.060 15.984  10.477 1.00 22.72 ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.751 16.003  9.861  1.00 22.06 ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.760 15.650  8.383  1.00 23.85 ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.572 16.203  7.626  1.00 25.59 ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 28.156 17.413  10.041 1.00 21.94 ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.770 17.637  9.458  1.00 22.43 ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.726 16.790  10.215 1.00 23.12 ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.425 19.141  9.490  1.00 23.47 ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.854 14.721  7.960  1.00 23.17 ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.607 14.389  6.559  1.00 23.69 ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 26.240 15.024  6.116  1.00 24.47 ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 26.148 15.694  5.074  1.00 26.28 ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.579 12.863  6.398  1.00 24.93 ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 27.077 12.467  5.013  1.00 25.76 ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 28.959 12.269  6.681  1.00 25.38 ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 25.206 14.864  6.954  1.00 22.87 ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 23.864 15.311  6.630  1.00 21.64 ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 23.027 15.407  7.913  1.00 20.65 ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 23.196 14.619  8.831  1.00 20.97 ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 23.229 14.267  5.671  1.00 22.54 ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.768 14.451  5.332  1.00 23.72 ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 21.244 15.241  4.346  1.00 26.11 ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.655 13.856  6.006  1.00 22.72 ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.867 15.129  4.337  1.00 26.71 ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.483 14.291  5.359  1.00 24.02 ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.537 12.962  7.075  1.00 22.28 ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 18.212 13.864  5.754  1.00 23.85 ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.279 12.537  7.451  1.00 23.16 ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 18.140 12.992  6.795  1.00 23.60 ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 22.159 16.394  7.990  1.00 19.19 ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 21.212 16.503  9.094  1.00 19.69 ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 19.915 17.127  8.602  1.00 18.96 ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 19.901 17.945  7.665  1.00 20.20 ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 21.759 17.268  10.299 1.00 20.59 ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.283 18.666  10.016 1.00 20.57 ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.276 19.794  9.970  1.00 22.80 ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 21.562 20.828  9.327  1.00 26.52 ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 20.201 19.655  10.577 1.00 22.56 ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 18.791 16.722  9.228  1.00 17.97 ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.501 17.313  8.876  1.00 18.27 ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.732 17.576  10.172 1.00 18.79 ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 16.314 16.618  10.842 1.00 18.74 ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.701 16.395  7.921  1.00 20.07 ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.439 17.030  7.360  1.00 25.36 ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 14.896 17.945  8.005  1.00 28.92 ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 14.999 16.619  6.249  1.00 25.17 ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.613 18.864  10.558 1.00 19.61 ? 36  SER   A N   1 
ATOM   241  C  CA  . SER   A 1 30  ? 15.916 19.262  11.780 1.00 20.97 ? 36  SER   A CA  1 
ATOM   242  C  C   . SER   A 1 30  ? 14.431 18.858  11.779 1.00 23.20 ? 36  SER   A C   1 
ATOM   243  O  O   . SER   A 1 30  ? 13.911 18.527  12.848 1.00 26.08 ? 36  SER   A O   1 
ATOM   244  C  CB  . SER   A 1 30  ? 16.070 20.770  11.992 1.00 23.59 ? 36  SER   A CB  1 
ATOM   245  O  OG  . SER   A 1 30  ? 15.590 21.527  10.885 1.00 26.48 ? 36  SER   A OG  1 
ATOM   246  N  N   . SER   A 1 31  ? 13.803 18.745  10.608 1.00 20.61 ? 37  SER   A N   1 
ATOM   247  C  CA  . SER   A 1 31  ? 12.406 18.322  10.568 1.00 20.08 ? 37  SER   A CA  1 
ATOM   248  C  C   . SER   A 1 31  ? 12.252 16.829  10.784 1.00 19.29 ? 37  SER   A C   1 
ATOM   249  O  O   . SER   A 1 31  ? 11.145 16.409  11.121 1.00 20.83 ? 37  SER   A O   1 
ATOM   250  C  CB  . SER   A 1 31  ? 11.738 18.757  9.265  1.00 24.53 ? 37  SER   A CB  1 
ATOM   251  O  OG  . SER   A 1 31  ? 12.187 17.967  8.175  1.00 31.23 ? 37  SER   A OG  1 
ATOM   252  N  N   . ARG   A 1 32  ? 13.330 16.043  10.679 1.00 18.28 ? 38  ARG   A N   1 
ATOM   253  C  CA  . ARG   A 1 32  ? 13.233 14.578  10.839 1.00 17.97 ? 38  ARG   A CA  1 
ATOM   254  C  C   . ARG   A 1 32  ? 13.849 14.075  12.145 1.00 17.49 ? 38  ARG   A C   1 
ATOM   255  O  O   . ARG   A 1 32  ? 13.785 12.872  12.386 1.00 17.25 ? 38  ARG   A O   1 
ATOM   256  C  CB  . ARG   A 1 32  ? 13.998 13.883  9.663  1.00 19.56 ? 38  ARG   A CB  1 
ATOM   257  C  CG  . ARG   A 1 32  ? 13.341 14.111  8.309  1.00 20.13 ? 38  ARG   A CG  1 
ATOM   258  C  CD  . ARG   A 1 32  ? 14.181 13.472  7.210  1.00 20.05 ? 38  ARG   A CD  1 
ATOM   259  N  NE  . ARG   A 1 32  ? 14.118 12.001  7.259  1.00 19.49 ? 38  ARG   A NE  1 
ATOM   260  C  CZ  . ARG   A 1 32  ? 14.232 11.209  6.204  1.00 19.62 ? 38  ARG   A CZ  1 
ATOM   261  N  NH1 . ARG   A 1 32  ? 14.408 11.727  4.987  1.00 21.17 ? 38  ARG   A NH1 1 
ATOM   262  N  NH2 . ARG   A 1 32  ? 14.169 9.882   6.348  1.00 19.74 ? 38  ARG   A NH2 1 
ATOM   263  N  N   . ASP   A 1 33  ? 14.551 14.923  12.912 1.00 18.29 ? 39  ASP   A N   1 
ATOM   264  C  CA  . ASP   A 1 33  ? 15.281 14.472  14.108 1.00 16.82 ? 39  ASP   A CA  1 
ATOM   265  C  C   . ASP   A 1 33  ? 16.382 13.466  13.759 1.00 16.74 ? 39  ASP   A C   1 
ATOM   266  O  O   . ASP   A 1 33  ? 16.695 12.583  14.564 1.00 16.95 ? 39  ASP   A O   1 
ATOM   267  C  CB  . ASP   A 1 33  ? 14.370 13.911  15.230 1.00 16.60 ? 39  ASP   A CB  1 
ATOM   268  C  CG  . ASP   A 1 33  ? 15.117 13.623  16.520 1.00 17.91 ? 39  ASP   A CG  1 
ATOM   269  O  OD1 . ASP   A 1 33  ? 16.006 14.418  16.884 1.00 19.61 ? 39  ASP   A OD1 1 
ATOM   270  O  OD2 . ASP   A 1 33  ? 14.797 12.595  17.188 1.00 17.49 ? 39  ASP   A OD2 1 
ATOM   271  N  N   . LEU   A 1 34  ? 16.995 13.625  12.552 1.00 16.48 ? 40  LEU   A N   1 
ATOM   272  C  CA  . LEU   A 1 34  ? 18.106 12.749  12.139 1.00 15.78 ? 40  LEU   A CA  1 
ATOM   273  C  C   . LEU   A 1 34  ? 19.390 13.531  11.871 1.00 16.07 ? 40  LEU   A C   1 
ATOM   274  O  O   . LEU   A 1 34  ? 19.363 14.634  11.310 1.00 17.11 ? 40  LEU   A O   1 
ATOM   275  C  CB  . LEU   A 1 34  ? 17.789 11.984  10.845 1.00 16.45 ? 40  LEU   A CB  1 
ATOM   276  C  CG  . LEU   A 1 34  ? 16.765 10.869  10.962 1.00 18.32 ? 40  LEU   A CG  1 
ATOM   277  C  CD1 . LEU   A 1 34  ? 16.641 10.153  9.593  1.00 19.20 ? 40  LEU   A CD1 1 
ATOM   278  C  CD2 . LEU   A 1 34  ? 17.148 9.848   12.055 1.00 17.49 ? 40  LEU   A CD2 1 
ATOM   279  N  N   . LEU   A 1 35  ? 20.508 12.873  12.166 1.00 16.05 ? 41  LEU   A N   1 
ATOM   280  C  CA  . LEU   A 1 35  ? 21.844 13.391  11.850 1.00 16.92 ? 41  LEU   A CA  1 
ATOM   281  C  C   . LEU   A 1 35  ? 22.724 12.197  11.479 1.00 17.64 ? 41  LEU   A C   1 
ATOM   282  O  O   . LEU   A 1 35  ? 22.631 11.163  12.127 1.00 17.37 ? 41  LEU   A O   1 
ATOM   283  C  CB  . LEU   A 1 35  ? 22.440 14.192  13.028 1.00 16.87 ? 41  LEU   A CB  1 
ATOM   284  C  CG  . LEU   A 1 35  ? 23.853 14.810  12.764 1.00 18.31 ? 41  LEU   A CG  1 
ATOM   285  C  CD1 . LEU   A 1 35  ? 24.027 16.132  13.525 1.00 18.53 ? 41  LEU   A CD1 1 
ATOM   286  C  CD2 . LEU   A 1 35  ? 24.989 13.900  13.224 1.00 19.14 ? 41  LEU   A CD2 1 
ATOM   287  N  N   . VAL   A 1 36  ? 23.546 12.331  10.410 1.00 17.19 ? 42  VAL   A N   1 
ATOM   288  C  CA  . VAL   A 1 36  ? 24.477 11.285  10.005 1.00 17.31 ? 42  VAL   A CA  1 
ATOM   289  C  C   . VAL   A 1 36  ? 25.891 11.888  10.044 1.00 18.58 ? 42  VAL   A C   1 
ATOM   290  O  O   . VAL   A 1 36  ? 26.124 12.998  9.530  1.00 19.63 ? 42  VAL   A O   1 
ATOM   291  C  CB  . VAL   A 1 36  ? 24.157 10.779  8.590  1.00 18.18 ? 42  VAL   A CB  1 
ATOM   292  C  CG1 . VAL   A 1 36  ? 25.209 9.773   8.099  1.00 19.04 ? 42  VAL   A CG1 1 
ATOM   293  C  CG2 . VAL   A 1 36  ? 22.755 10.170  8.535  1.00 18.53 ? 42  VAL   A CG2 1 
ATOM   294  N  N   . SER   A 1 37  ? 26.796 11.201  10.715 1.00 18.22 ? 43  SER   A N   1 
ATOM   295  C  CA  . SER   A 1 37  ? 28.213 11.618  10.794 1.00 19.33 ? 43  SER   A CA  1 
ATOM   296  C  C   . SER   A 1 37  ? 29.103 10.553  10.157 1.00 20.83 ? 43  SER   A C   1 
ATOM   297  O  O   . SER   A 1 37  ? 28.669 9.422   9.951  1.00 20.74 ? 43  SER   A O   1 
ATOM   298  C  CB  . SER   A 1 37  ? 28.640 11.870  12.243 1.00 20.32 ? 43  SER   A CB  1 
ATOM   299  O  OG  . SER   A 1 37  ? 28.469 10.721  13.074 1.00 21.56 ? 43  SER   A OG  1 
ATOM   300  N  N   . SER   A 1 38  ? 30.368 10.905  9.823  1.00 21.80 ? 44  SER   A N   1 
ATOM   301  C  CA  . SER   A 1 38  ? 31.282 9.928   9.216  1.00 24.50 ? 44  SER   A CA  1 
ATOM   302  C  C   . SER   A 1 38  ? 32.103 9.192   10.280 1.00 26.48 ? 44  SER   A C   1 
ATOM   303  O  O   . SER   A 1 38  ? 32.372 9.735   11.355 1.00 26.93 ? 44  SER   A O   1 
ATOM   304  C  CB  . SER   A 1 38  ? 32.211 10.609  8.216  1.00 27.73 ? 44  SER   A CB  1 
ATOM   305  O  OG  . SER   A 1 38  ? 32.877 11.678  8.865  1.00 30.64 ? 44  SER   A OG  1 
ATOM   306  N  N   . THR   A 1 39  ? 32.476 7.941   10.006 1.00 28.41 ? 45  THR   A N   1 
ATOM   307  C  CA  . THR   A 1 39  ? 33.242 7.133   10.960 1.00 31.17 ? 45  THR   A CA  1 
ATOM   308  C  C   . THR   A 1 39  ? 34.537 6.625   10.293 1.00 34.86 ? 45  THR   A C   1 
ATOM   309  O  O   . THR   A 1 39  ? 34.552 6.413   9.074  1.00 35.19 ? 45  THR   A O   1 
ATOM   310  C  CB  . THR   A 1 39  ? 32.414 5.889   11.395 1.00 32.43 ? 45  THR   A CB  1 
ATOM   311  O  OG1 . THR   A 1 39  ? 32.187 5.072   10.253 1.00 34.12 ? 45  THR   A OG1 1 
ATOM   312  C  CG2 . THR   A 1 39  ? 31.067 6.262   11.998 1.00 31.60 ? 45  THR   A CG2 1 
ATOM   313  N  N   . THR   A 1 40  ? 35.577 6.368   11.086 1.00 37.74 ? 46  THR   A N   1 
ATOM   314  C  CA  . THR   A 1 40  ? 36.799 5.782   10.528 1.00 40.79 ? 46  THR   A CA  1 
ATOM   315  C  C   . THR   A 1 40  ? 36.626 4.278   10.416 1.00 43.11 ? 46  THR   A C   1 
ATOM   316  O  O   . THR   A 1 40  ? 37.020 3.690   9.406  1.00 44.93 ? 46  THR   A O   1 
ATOM   317  C  CB  . THR   A 1 40  ? 38.052 6.167   11.321 1.00 42.91 ? 46  THR   A CB  1 
ATOM   318  O  OG1 . THR   A 1 40  ? 37.812 5.987   12.720 1.00 44.15 ? 46  THR   A OG1 1 
ATOM   319  C  CG2 . THR   A 1 40  ? 38.517 7.587   11.023 1.00 44.09 ? 46  THR   A CG2 1 
ATOM   320  N  N   . ALA   A 1 41  ? 36.045 3.643   11.446 1.00 42.92 ? 47  ALA   A N   1 
ATOM   321  C  CA  . ALA   A 1 41  ? 35.835 2.197   11.430 1.00 43.25 ? 47  ALA   A CA  1 
ATOM   322  C  C   . ALA   A 1 41  ? 34.622 1.837   10.580 1.00 43.02 ? 47  ALA   A C   1 
ATOM   323  O  O   . ALA   A 1 41  ? 33.643 2.586   10.531 1.00 42.79 ? 47  ALA   A O   1 
ATOM   324  C  CB  . ALA   A 1 41  ? 35.654 1.677   12.850 1.00 43.37 ? 47  ALA   A CB  1 
ATOM   325  N  N   . GLN   A 1 42  ? 34.686 0.698   9.902  1.00 42.65 ? 48  GLN   A N   1 
ATOM   326  C  CA  . GLN   A 1 42  ? 33.594 0.260   9.046  1.00 42.57 ? 48  GLN   A CA  1 
ATOM   327  C  C   . GLN   A 1 42  ? 32.481 -0.448  9.827  1.00 40.71 ? 48  GLN   A C   1 
ATOM   328  O  O   . GLN   A 1 42  ? 32.748 -1.352  10.620 1.00 41.61 ? 48  GLN   A O   1 
ATOM   329  C  CB  . GLN   A 1 42  ? 34.140 -0.654  7.939  1.00 45.59 ? 48  GLN   A CB  1 
ATOM   330  C  CG  . GLN   A 1 42  ? 33.082 -1.069  6.919  1.00 51.70 ? 48  GLN   A CG  1 
ATOM   331  C  CD  . GLN   A 1 42  ? 33.559 -0.948  5.488  1.00 58.71 ? 48  GLN   A CD  1 
ATOM   332  O  OE1 . GLN   A 1 42  ? 34.646 -0.427  5.196  1.00 60.66 ? 48  GLN   A OE1 1 
ATOM   333  N  NE2 . GLN   A 1 42  ? 32.744 -1.427  4.559  1.00 59.77 ? 48  GLN   A NE2 1 
ATOM   334  N  N   . GLY   A 1 43  ? 31.248 -0.002  9.609  1.00 37.82 ? 49  GLY   A N   1 
ATOM   335  C  CA  . GLY   A 1 43  ? 30.048 -0.601  10.181 1.00 36.31 ? 49  GLY   A CA  1 
ATOM   336  C  C   . GLY   A 1 43  ? 29.513 -1.682  9.263  1.00 34.77 ? 49  GLY   A C   1 
ATOM   337  O  O   . GLY   A 1 43  ? 29.875 -1.727  8.075  1.00 35.62 ? 49  GLY   A O   1 
ATOM   338  N  N   . CYS   A 1 44  ? 28.682 -2.584  9.798  1.00 31.95 ? 50  CYS   A N   1 
ATOM   339  C  CA  . CYS   A 1 44  ? 28.178 -3.660  8.951  1.00 31.43 ? 50  CYS   A CA  1 
ATOM   340  C  C   . CYS   A 1 44  ? 26.693 -3.921  9.182  1.00 29.42 ? 50  CYS   A C   1 
ATOM   341  O  O   . CYS   A 1 44  ? 26.239 -5.009  8.833  1.00 31.79 ? 50  CYS   A O   1 
ATOM   342  C  CB  . CYS   A 1 44  ? 29.032 -4.930  9.031  1.00 33.38 ? 50  CYS   A CB  1 
ATOM   343  S  SG  . CYS   A 1 44  ? 29.475 -5.421  10.717 1.00 40.77 ? 50  CYS   A SG  1 
ATOM   344  N  N   . ASP   A 1 45  ? 25.923 -2.907  9.711  1.00 27.03 ? 51  ASP   A N   1 
ATOM   345  C  CA  . ASP   A 1 45  ? 24.445 -2.990  9.843  1.00 26.58 ? 51  ASP   A CA  1 
ATOM   346  C  C   . ASP   A 1 45  ? 23.891 -2.912  8.361  1.00 26.16 ? 51  ASP   A C   1 
ATOM   347  O  O   . ASP   A 1 45  ? 24.607 -2.494  7.431  1.00 28.74 ? 51  ASP   A O   1 
ATOM   348  C  CB  . ASP   A 1 45  ? 23.793 -1.866  10.768 1.00 29.22 ? 51  ASP   A CB  1 
ATOM   349  C  CG  . ASP   A 1 45  ? 23.989 -1.892  12.325 1.00 34.79 ? 51  ASP   A CG  1 
ATOM   350  O  OD1 . ASP   A 1 45  ? 24.278 -2.957  12.860 1.00 38.04 ? 51  ASP   A OD1 1 
ATOM   351  O  OD2 . ASP   A 1 45  ? 23.842 -0.786  13.019 1.00 30.16 ? 51  ASP   A OD2 1 
ATOM   352  N  N   . THR   A 1 46  ? 22.658 -3.354  8.143  1.00 21.84 ? 52  THR   A N   1 
ATOM   353  C  CA  . THR   A 1 46  ? 22.022 -3.282  6.812  1.00 21.07 ? 52  THR   A CA  1 
ATOM   354  C  C   . THR   A 1 46  ? 20.714 -2.466  6.939  1.00 19.61 ? 52  THR   A C   1 
ATOM   355  O  O   . THR   A 1 46  ? 19.886 -2.753  7.808  1.00 20.52 ? 52  THR   A O   1 
ATOM   356  C  CB  . THR   A 1 46  ? 21.659 -4.686  6.338  1.00 23.96 ? 52  THR   A CB  1 
ATOM   357  O  OG1 . THR   A 1 46  ? 22.898 -5.378  6.055  1.00 25.78 ? 52  THR   A OG1 1 
ATOM   358  C  CG2 . THR   A 1 46  ? 20.802 -4.673  5.032  1.00 24.40 ? 52  THR   A CG2 1 
ATOM   359  N  N   . ILE   A 1 47  ? 20.510 -1.492  6.033  1.00 19.57 ? 53  ILE   A N   1 
ATOM   360  C  CA  . ILE   A 1 47  ? 19.280 -0.701  6.060  1.00 18.36 ? 53  ILE   A CA  1 
ATOM   361  C  C   . ILE   A 1 47  ? 18.210 -1.435  5.228  1.00 18.11 ? 53  ILE   A C   1 
ATOM   362  O  O   . ILE   A 1 47  ? 18.508 -1.894  4.105  1.00 18.97 ? 53  ILE   A O   1 
ATOM   363  C  CB  . ILE   A 1 47  ? 19.523 0.684   5.458  1.00 19.58 ? 53  ILE   A CB  1 
ATOM   364  C  CG1 . ILE   A 1 47  ? 20.740 1.400   6.100  1.00 21.28 ? 53  ILE   A CG1 1 
ATOM   365  C  CG2 . ILE   A 1 47  ? 18.262 1.544   5.550  1.00 19.68 ? 53  ILE   A CG2 1 
ATOM   366  C  CD1 . ILE   A 1 47  ? 20.489 1.665   7.630  1.00 22.16 ? 53  ILE   A CD1 1 
ATOM   367  N  N   . ALA   A 1 48  ? 16.975 -1.536  5.751  1.00 17.87 ? 54  ALA   A N   1 
ATOM   368  C  CA  . ALA   A 1 48  ? 15.877 -2.176  5.017  1.00 17.95 ? 54  ALA   A CA  1 
ATOM   369  C  C   . ALA   A 1 48  ? 15.467 -1.340  3.803  1.00 18.35 ? 54  ALA   A C   1 
ATOM   370  O  O   . ALA   A 1 48  ? 15.466 -0.109  3.879  1.00 18.28 ? 54  ALA   A O   1 
ATOM   371  C  CB  . ALA   A 1 48  ? 14.649 -2.303  5.954  1.00 18.13 ? 54  ALA   A CB  1 
ATOM   372  N  N   . ARG   A 1 49  ? 15.131 -2.015  2.658  1.00 18.82 ? 55  ARG   A N   1 
ATOM   373  C  CA  . ARG   A 1 49  ? 14.693 -1.306  1.430  1.00 19.82 ? 55  ARG   A CA  1 
ATOM   374  C  C   . ARG   A 1 49  ? 13.397 -2.023  1.105  1.00 21.07 ? 55  ARG   A C   1 
ATOM   375  O  O   . ARG   A 1 49  ? 13.385 -3.030  0.392  1.00 23.21 ? 55  ARG   A O   1 
ATOM   376  C  CB  . ARG   A 1 49  ? 15.740 -1.395  0.303  1.00 21.70 ? 55  ARG   A CB  1 
ATOM   377  C  CG  . ARG   A 1 49  ? 17.119 -0.831  0.736  1.00 22.38 ? 55  ARG   A CG  1 
ATOM   378  C  CD  . ARG   A 1 49  ? 17.150 0.674   1.114  1.00 25.34 ? 55  ARG   A CD  1 
ATOM   379  N  NE  . ARG   A 1 49  ? 18.529 1.108   1.429  1.00 23.07 ? 55  ARG   A NE  1 
ATOM   380  C  CZ  . ARG   A 1 49  ? 18.835 2.274   2.007  1.00 23.84 ? 55  ARG   A CZ  1 
ATOM   381  N  NH1 . ARG   A 1 49  ? 17.882 3.141   2.317  1.00 23.85 ? 55  ARG   A NH1 1 
ATOM   382  N  NH2 . ARG   A 1 49  ? 20.093 2.562   2.313  1.00 24.38 ? 55  ARG   A NH2 1 
ATOM   383  N  N   . CYS   A 1 50  ? 12.311 -1.471  1.635  1.00 20.34 ? 56  CYS   A N   1 
ATOM   384  C  CA  . CYS   A 1 50  ? 11.012 -2.154  1.635  1.00 20.84 ? 56  CYS   A CA  1 
ATOM   385  C  C   . CYS   A 1 50  ? 9.885  -1.211  2.052  1.00 20.81 ? 56  CYS   A C   1 
ATOM   386  O  O   . CYS   A 1 50  ? 10.138 -0.080  2.487  1.00 20.65 ? 56  CYS   A O   1 
ATOM   387  C  CB  . CYS   A 1 50  ? 11.077 -3.340  2.611  1.00 21.47 ? 56  CYS   A CB  1 
ATOM   388  S  SG  . CYS   A 1 50  ? 11.188 -2.839  4.377  1.00 19.96 ? 56  CYS   A SG  1 
ATOM   389  N  N   . ASP   A 1 51  ? 8.615  -1.746  2.043  1.00 22.49 ? 57  ASP   A N   1 
ATOM   390  C  CA  . ASP   A 1 51  ? 7.476  -0.985  2.534  1.00 23.61 ? 57  ASP   A CA  1 
ATOM   391  C  C   . ASP   A 1 51  ? 6.820  -1.733  3.711  1.00 23.75 ? 57  ASP   A C   1 
ATOM   392  O  O   . ASP   A 1 51  ? 5.631  -1.575  3.917  1.00 24.58 ? 57  ASP   A O   1 
ATOM   393  C  CB  . ASP   A 1 51  ? 6.424  -0.735  1.419  1.00 27.60 ? 57  ASP   A CB  1 
ATOM   394  C  CG  . ASP   A 1 51  ? 5.883  -1.983  0.778  1.00 34.34 ? 57  ASP   A CG  1 
ATOM   395  O  OD1 . ASP   A 1 51  ? 6.277  -3.097  1.202  1.00 35.01 ? 57  ASP   A OD1 1 
ATOM   396  O  OD2 . ASP   A 1 51  ? 5.061  -1.858  -0.162 1.00 39.60 ? 57  ASP   A OD2 1 
ATOM   397  N  N   . CYS   A 1 52  ? 7.589  -2.490  4.524  1.00 21.20 ? 58  CYS   A N   1 
ATOM   398  C  CA  . CYS   A 1 52  ? 7.030  -3.182  5.709  1.00 19.97 ? 58  CYS   A CA  1 
ATOM   399  C  C   . CYS   A 1 52  ? 6.334  -2.192  6.634  1.00 20.46 ? 58  CYS   A C   1 
ATOM   400  O  O   . CYS   A 1 52  ? 6.788  -1.039  6.772  1.00 20.43 ? 58  CYS   A O   1 
ATOM   401  C  CB  . CYS   A 1 52  ? 8.127  -3.912  6.493  1.00 21.47 ? 58  CYS   A CB  1 
ATOM   402  S  SG  . CYS   A 1 52  ? 8.778  -5.407  5.696  1.00 22.60 ? 58  CYS   A SG  1 
ATOM   403  N  N   . GLN   A 1 53  ? 5.237  -2.644  7.249  1.00 18.67 ? 59  GLN   A N   1 
ATOM   404  C  CA  . GLN   A 1 53  ? 4.546  -1.890  8.298  1.00 18.70 ? 59  GLN   A CA  1 
ATOM   405  C  C   . GLN   A 1 53  ? 4.471  -2.720  9.578  1.00 17.56 ? 59  GLN   A C   1 
ATOM   406  O  O   . GLN   A 1 53  ? 3.644  -2.437  10.442 1.00 17.73 ? 59  GLN   A O   1 
ATOM   407  C  CB  . GLN   A 1 53  ? 3.132  -1.446  7.868  1.00 20.41 ? 59  GLN   A CB  1 
ATOM   408  C  CG  . GLN   A 1 53  ? 3.149  -0.238  6.913  1.00 25.32 ? 59  GLN   A CG  1 
ATOM   409  C  CD  . GLN   A 1 53  ? 1.740  0.279   6.670  1.00 27.48 ? 59  GLN   A CD  1 
ATOM   410  O  OE1 . GLN   A 1 53  ? 1.193  0.133   5.569  1.00 29.86 ? 59  GLN   A OE1 1 
ATOM   411  N  NE2 . GLN   A 1 53  ? 1.089  0.849   7.689  1.00 24.68 ? 59  GLN   A NE2 1 
ATOM   412  N  N   . THR   A 1 54  ? 5.290  -3.812  9.699  1.00 16.99 ? 60  THR   A N   1 
ATOM   413  C  CA  . THR   A 1 54  ? 5.420  -4.558  10.937 1.00 16.90 ? 60  THR   A CA  1 
ATOM   414  C  C   . THR   A 1 54  ? 6.916  -4.768  11.161 1.00 16.85 ? 60  THR   A C   1 
ATOM   415  O  O   . THR   A 1 54  ? 7.709  -4.863  10.220 1.00 18.48 ? 60  THR   A O   1 
ATOM   416  C  CB  . THR   A 1 54  ? 4.697  -5.920  10.922 1.00 20.26 ? 60  THR   A CB  1 
ATOM   417  O  OG1 . THR   A 1 54  ? 5.266  -6.754  9.911  1.00 25.13 ? 60  THR   A OG1 1 
ATOM   418  C  CG2 . THR   A 1 54  ? 3.185  -5.800  10.685 1.00 20.85 ? 60  THR   A CG2 1 
ATOM   419  N  N   . GLY   A 1 55  ? 7.278  -4.837  12.427 1.00 16.40 ? 61  GLY   A N   1 
ATOM   420  C  CA  . GLY   A 1 55  ? 8.670  -5.013  12.814 1.00 16.32 ? 61  GLY   A CA  1 
ATOM   421  C  C   . GLY   A 1 55  ? 8.780  -5.166  14.320 1.00 15.29 ? 61  GLY   A C   1 
ATOM   422  O  O   . GLY   A 1 55  ? 7.777  -5.377  14.998 1.00 16.12 ? 61  GLY   A O   1 
ATOM   423  N  N   . VAL   A 1 56  ? 10.013 -5.102  14.816 1.00 14.42 ? 62  VAL   A N   1 
ATOM   424  C  CA  . VAL   A 1 56  ? 10.313 -5.232  16.248 1.00 14.89 ? 62  VAL   A CA  1 
ATOM   425  C  C   . VAL   A 1 56  ? 11.247 -4.083  16.639 1.00 14.65 ? 62  VAL   A C   1 
ATOM   426  O  O   . VAL   A 1 56  ? 12.222 -3.812  15.941 1.00 15.12 ? 62  VAL   A O   1 
ATOM   427  C  CB  . VAL   A 1 56  ? 11.029 -6.592  16.467 1.00 16.31 ? 62  VAL   A CB  1 
ATOM   428  C  CG1 . VAL   A 1 56  ? 11.487 -6.727  17.932 1.00 17.50 ? 62  VAL   A CG1 1 
ATOM   429  C  CG2 . VAL   A 1 56  ? 10.074 -7.759  16.094 1.00 17.27 ? 62  VAL   A CG2 1 
ATOM   430  N  N   . TYR   A 1 57  ? 10.968 -3.444  17.782 1.00 13.98 ? 63  TYR   A N   1 
ATOM   431  C  CA  . TYR   A 1 57  ? 11.855 -2.376  18.268 1.00 13.39 ? 63  TYR   A CA  1 
ATOM   432  C  C   . TYR   A 1 57  ? 12.364 -2.660  19.657 1.00 14.90 ? 63  TYR   A C   1 
ATOM   433  O  O   . TYR   A 1 57  ? 11.746 -3.408  20.432 1.00 15.22 ? 63  TYR   A O   1 
ATOM   434  C  CB  . TYR   A 1 57  ? 11.217 -0.961  18.228 1.00 13.13 ? 63  TYR   A CB  1 
ATOM   435  C  CG  . TYR   A 1 57  ? 10.250 -0.636  19.365 1.00 14.02 ? 63  TYR   A CG  1 
ATOM   436  C  CD1 . TYR   A 1 57  ? 8.962  -1.161  19.379 1.00 15.37 ? 63  TYR   A CD1 1 
ATOM   437  C  CD2 . TYR   A 1 57  ? 10.617 0.214   20.401 1.00 14.97 ? 63  TYR   A CD2 1 
ATOM   438  C  CE1 . TYR   A 1 57  ? 8.048  -0.822  20.371 1.00 16.77 ? 63  TYR   A CE1 1 
ATOM   439  C  CE2 . TYR   A 1 57  ? 9.713  0.548   21.423 1.00 15.61 ? 63  TYR   A CE2 1 
ATOM   440  C  CZ  . TYR   A 1 57  ? 8.435  0.001   21.419 1.00 16.54 ? 63  TYR   A CZ  1 
ATOM   441  O  OH  . TYR   A 1 57  ? 7.528  0.337   22.423 1.00 19.32 ? 63  TYR   A OH  1 
ATOM   442  N  N   . TYR   A 1 58  ? 13.544 -2.099  19.945 1.00 14.51 ? 64  TYR   A N   1 
ATOM   443  C  CA  . TYR   A 1 58  ? 14.140 -2.240  21.261 1.00 15.16 ? 64  TYR   A CA  1 
ATOM   444  C  C   . TYR   A 1 58  ? 13.700 -1.061  22.133 1.00 15.82 ? 64  TYR   A C   1 
ATOM   445  O  O   . TYR   A 1 58  ? 13.924 0.099   21.768 1.00 15.39 ? 64  TYR   A O   1 
ATOM   446  C  CB  . TYR   A 1 58  ? 15.698 -2.346  21.208 1.00 15.66 ? 64  TYR   A CB  1 
ATOM   447  C  CG  . TYR   A 1 58  ? 16.260 -2.476  22.601 1.00 17.17 ? 64  TYR   A CG  1 
ATOM   448  C  CD1 . TYR   A 1 58  ? 16.025 -3.611  23.365 1.00 17.72 ? 64  TYR   A CD1 1 
ATOM   449  C  CD2 . TYR   A 1 58  ? 17.053 -1.479  23.146 1.00 18.16 ? 64  TYR   A CD2 1 
ATOM   450  C  CE1 . TYR   A 1 58  ? 16.505 -3.722  24.669 1.00 19.17 ? 64  TYR   A CE1 1 
ATOM   451  C  CE2 . TYR   A 1 58  ? 17.555 -1.582  24.444 1.00 19.00 ? 64  TYR   A CE2 1 
ATOM   452  C  CZ  . TYR   A 1 58  ? 17.270 -2.702  25.205 1.00 20.53 ? 64  TYR   A CZ  1 
ATOM   453  O  OH  . TYR   A 1 58  ? 17.766 -2.834  26.493 1.00 23.89 ? 64  TYR   A OH  1 
ATOM   454  N  N   . CYS   A 1 59  ? 13.204 -1.377  23.347 1.00 15.58 ? 65  CYS   A N   1 
ATOM   455  C  CA  . CYS   A 1 59  ? 12.733 -0.409  24.323 1.00 16.02 ? 65  CYS   A CA  1 
ATOM   456  C  C   . CYS   A 1 59  ? 13.653 -0.480  25.560 1.00 17.61 ? 65  CYS   A C   1 
ATOM   457  O  O   . CYS   A 1 59  ? 13.486 -1.373  26.394 1.00 18.38 ? 65  CYS   A O   1 
ATOM   458  C  CB  . CYS   A 1 59  ? 11.287 -0.714  24.687 1.00 16.81 ? 65  CYS   A CB  1 
ATOM   459  S  SG  . CYS   A 1 59  ? 10.619 0.413   25.950 1.00 19.90 ? 65  CYS   A SG  1 
ATOM   460  N  N   A SER   A 1 60  ? 14.590 0.470   25.700 0.50 17.72 ? 66  SER   A N   1 
ATOM   461  N  N   B SER   A 1 60  ? 14.597 0.464   25.682 0.50 17.49 ? 66  SER   A N   1 
ATOM   462  C  CA  A SER   A 1 60  ? 15.549 0.430   26.803 0.50 18.60 ? 66  SER   A CA  1 
ATOM   463  C  CA  B SER   A 1 60  ? 15.541 0.422   26.788 0.50 18.09 ? 66  SER   A CA  1 
ATOM   464  C  C   A SER   A 1 60  ? 14.935 0.639   28.208 0.50 18.92 ? 66  SER   A C   1 
ATOM   465  C  C   B SER   A 1 60  ? 14.857 0.492   28.157 0.50 18.22 ? 66  SER   A C   1 
ATOM   466  O  O   A SER   A 1 60  ? 15.483 0.170   29.221 0.50 18.98 ? 66  SER   A O   1 
ATOM   467  O  O   B SER   A 1 60  ? 15.242 -0.258  29.080 0.50 17.75 ? 66  SER   A O   1 
ATOM   468  C  CB  A SER   A 1 60  ? 16.671 1.426   26.553 0.50 20.37 ? 66  SER   A CB  1 
ATOM   469  C  CB  B SER   A 1 60  ? 16.573 1.536   26.655 0.50 19.70 ? 66  SER   A CB  1 
ATOM   470  O  OG  A SER   A 1 60  ? 16.193 2.743   26.754 0.50 21.98 ? 66  SER   A OG  1 
ATOM   471  O  OG  B SER   A 1 60  ? 17.649 1.346   27.562 0.50 21.07 ? 66  SER   A OG  1 
ATOM   472  N  N   . SER   A 1 61  ? 13.800 1.334   28.273 1.00 18.18 ? 67  SER   A N   1 
ATOM   473  C  CA  . SER   A 1 61  ? 13.099 1.521   29.549 1.00 18.41 ? 67  SER   A CA  1 
ATOM   474  C  C   . SER   A 1 61  ? 12.357 0.276   30.034 1.00 19.47 ? 67  SER   A C   1 
ATOM   475  O  O   . SER   A 1 61  ? 11.854 0.279   31.160 1.00 20.60 ? 67  SER   A O   1 
ATOM   476  C  CB  . SER   A 1 61  ? 12.167 2.724   29.509 1.00 19.04 ? 67  SER   A CB  1 
ATOM   477  O  OG  . SER   A 1 61  ? 11.103 2.536   28.594 1.00 20.10 ? 67  SER   A OG  1 
ATOM   478  N  N   . ARG   A 1 62  ? 12.280 -0.778  29.211 1.00 18.34 ? 68  ARG   A N   1 
ATOM   479  C  CA  . ARG   A 1 62  ? 11.732 -2.055  29.636 1.00 18.75 ? 68  ARG   A CA  1 
ATOM   480  C  C   . ARG   A 1 62  ? 12.740 -3.192  29.449 1.00 20.00 ? 68  ARG   A C   1 
ATOM   481  O  O   . ARG   A 1 62  ? 12.410 -4.349  29.736 1.00 21.34 ? 68  ARG   A O   1 
ATOM   482  C  CB  . ARG   A 1 62  ? 10.441 -2.381  28.875 1.00 20.02 ? 68  ARG   A CB  1 
ATOM   483  C  CG  . ARG   A 1 62  ? 9.362  -1.346  29.131 1.00 21.61 ? 68  ARG   A CG  1 
ATOM   484  C  CD  . ARG   A 1 62  ? 8.704  -1.613  30.475 1.00 23.74 ? 68  ARG   A CD  1 
ATOM   485  N  NE  . ARG   A 1 62  ? 7.584  -0.694  30.719 1.00 26.07 ? 68  ARG   A NE  1 
ATOM   486  C  CZ  . ARG   A 1 62  ? 7.695  0.472   31.338 1.00 27.16 ? 68  ARG   A CZ  1 
ATOM   487  N  NH1 . ARG   A 1 62  ? 8.888  0.912   31.742 1.00 26.09 ? 68  ARG   A NH1 1 
ATOM   488  N  NH2 . ARG   A 1 62  ? 6.620  1.227   31.540 1.00 28.97 ? 68  ARG   A NH2 1 
ATOM   489  N  N   . ARG   A 1 63  ? 13.968 -2.920  28.951 1.00 20.17 ? 69  ARG   A N   1 
ATOM   490  C  CA  . ARG   A 1 63  ? 14.981 -3.947  28.576 1.00 21.12 ? 69  ARG   A CA  1 
ATOM   491  C  C   . ARG   A 1 63  ? 14.329 -5.055  27.750 1.00 21.94 ? 69  ARG   A C   1 
ATOM   492  O  O   . ARG   A 1 63  ? 14.537 -6.256  28.002 1.00 23.53 ? 69  ARG   A O   1 
ATOM   493  C  CB  . ARG   A 1 63  ? 15.739 -4.510  29.806 1.00 23.26 ? 69  ARG   A CB  1 
ATOM   494  C  CG  . ARG   A 1 63  ? 16.460 -3.418  30.575 1.00 28.18 ? 69  ARG   A CG  1 
ATOM   495  C  CD  . ARG   A 1 63  ? 17.642 -2.871  29.809 1.00 32.72 ? 69  ARG   A CD  1 
ATOM   496  N  NE  . ARG   A 1 63  ? 18.671 -2.287  30.678 1.00 36.46 ? 69  ARG   A NE  1 
ATOM   497  C  CZ  . ARG   A 1 63  ? 18.841 -0.982  30.867 1.00 37.14 ? 69  ARG   A CZ  1 
ATOM   498  N  NH1 . ARG   A 1 63  ? 18.036 -0.102  30.272 1.00 33.57 ? 69  ARG   A NH1 1 
ATOM   499  N  NH2 . ARG   A 1 63  ? 19.809 -0.543  31.656 1.00 39.81 ? 69  ARG   A NH2 1 
ATOM   500  N  N   . LYS   A 1 64  ? 13.479 -4.642  26.801 1.00 20.01 ? 70  LYS   A N   1 
ATOM   501  C  CA  . LYS   A 1 64  ? 12.727 -5.622  26.011 1.00 20.27 ? 70  LYS   A CA  1 
ATOM   502  C  C   . LYS   A 1 64  ? 12.534 -5.182  24.579 1.00 17.95 ? 70  LYS   A C   1 
ATOM   503  O  O   . LYS   A 1 64  ? 12.541 -3.998  24.292 1.00 17.21 ? 70  LYS   A O   1 
ATOM   504  C  CB  . LYS   A 1 64  ? 11.312 -5.791  26.612 1.00 25.51 ? 70  LYS   A CB  1 
ATOM   505  C  CG  . LYS   A 1 64  ? 11.222 -6.742  27.818 1.00 33.27 ? 70  LYS   A CG  1 
ATOM   506  C  CD  . LYS   A 1 64  ? 9.802  -6.732  28.366 1.00 40.47 ? 70  LYS   A CD  1 
ATOM   507  C  CE  . LYS   A 1 64  ? 9.677  -7.618  29.587 1.00 46.83 ? 70  LYS   A CE  1 
ATOM   508  N  NZ  . LYS   A 1 64  ? 10.777 -7.350  30.561 1.00 50.60 ? 70  LYS   A NZ  1 
ATOM   509  N  N   . HIS   A 1 65  ? 12.331 -6.138  23.695 1.00 17.08 ? 71  HIS   A N   1 
ATOM   510  C  CA  . HIS   A 1 65  ? 11.947 -5.889  22.326 1.00 16.54 ? 71  HIS   A CA  1 
ATOM   511  C  C   . HIS   A 1 65  ? 10.449 -6.160  22.190 1.00 17.61 ? 71  HIS   A C   1 
ATOM   512  O  O   . HIS   A 1 65  ? 9.905  -7.125  22.775 1.00 19.78 ? 71  HIS   A O   1 
ATOM   513  C  CB  . HIS   A 1 65  ? 12.696 -6.824  21.359 1.00 17.06 ? 71  HIS   A CB  1 
ATOM   514  C  CG  . HIS   A 1 65  ? 14.183 -6.663  21.374 1.00 17.54 ? 71  HIS   A CG  1 
ATOM   515  N  ND1 . HIS   A 1 65  ? 14.877 -5.886  20.429 1.00 19.98 ? 71  HIS   A ND1 1 
ATOM   516  C  CD2 . HIS   A 1 65  ? 15.071 -7.229  22.213 1.00 18.35 ? 71  HIS   A CD2 1 
ATOM   517  C  CE1 . HIS   A 1 65  ? 16.162 -5.987  20.753 1.00 18.41 ? 71  HIS   A CE1 1 
ATOM   518  N  NE2 . HIS   A 1 65  ? 16.334 -6.747  21.831 1.00 21.45 ? 71  HIS   A NE2 1 
ATOM   519  N  N   . TYR   A 1 66  ? 9.762  -5.289  21.427 1.00 16.02 ? 72  TYR   A N   1 
ATOM   520  C  CA  . TYR   A 1 66  ? 8.331  -5.433  21.218 1.00 16.04 ? 72  TYR   A CA  1 
ATOM   521  C  C   . TYR   A 1 66  ? 7.999  -5.496  19.718 1.00 15.58 ? 72  TYR   A C   1 
ATOM   522  O  O   . TYR   A 1 66  ? 8.470  -4.684  18.928 1.00 16.26 ? 72  TYR   A O   1 
ATOM   523  C  CB  . TYR   A 1 66  ? 7.586  -4.196  21.742 1.00 16.97 ? 72  TYR   A CB  1 
ATOM   524  C  CG  . TYR   A 1 66  ? 7.605  -4.063  23.247 1.00 18.73 ? 72  TYR   A CG  1 
ATOM   525  C  CD1 . TYR   A 1 66  ? 6.777  -4.847  24.042 1.00 20.14 ? 72  TYR   A CD1 1 
ATOM   526  C  CD2 . TYR   A 1 66  ? 8.350  -3.070  23.867 1.00 20.00 ? 72  TYR   A CD2 1 
ATOM   527  C  CE1 . TYR   A 1 66  ? 6.766  -4.712  25.432 1.00 21.22 ? 72  TYR   A CE1 1 
ATOM   528  C  CE2 . TYR   A 1 66  ? 8.358  -2.931  25.258 1.00 21.29 ? 72  TYR   A CE2 1 
ATOM   529  C  CZ  . TYR   A 1 66  ? 7.552  -3.749  26.031 1.00 22.50 ? 72  TYR   A CZ  1 
ATOM   530  O  OH  . TYR   A 1 66  ? 7.487  -3.573  27.402 1.00 24.36 ? 72  TYR   A OH  1 
ATOM   531  N  N   . PRO   A 1 67  ? 7.153  -6.462  19.323 1.00 15.80 ? 73  PRO   A N   1 
ATOM   532  C  CA  . PRO   A 1 67  ? 6.664  -6.491  17.928 1.00 16.11 ? 73  PRO   A CA  1 
ATOM   533  C  C   . PRO   A 1 67  ? 5.545  -5.420  17.763 1.00 17.43 ? 73  PRO   A C   1 
ATOM   534  O  O   . PRO   A 1 67  ? 4.637  -5.337  18.634 1.00 19.54 ? 73  PRO   A O   1 
ATOM   535  C  CB  . PRO   A 1 67  ? 6.060  -7.916  17.790 1.00 16.80 ? 73  PRO   A CB  1 
ATOM   536  C  CG  . PRO   A 1 67  ? 5.571  -8.231  19.199 1.00 17.49 ? 73  PRO   A CG  1 
ATOM   537  C  CD  . PRO   A 1 67  ? 6.529  -7.510  20.158 1.00 16.22 ? 73  PRO   A CD  1 
ATOM   538  N  N   . VAL   A 1 68  ? 5.579  -4.663  16.667 1.00 16.35 ? 74  VAL   A N   1 
ATOM   539  C  CA  . VAL   A 1 68  ? 4.581  -3.615  16.472 1.00 16.68 ? 74  VAL   A CA  1 
ATOM   540  C  C   . VAL   A 1 68  ? 4.153  -3.525  15.015 1.00 16.14 ? 74  VAL   A C   1 
ATOM   541  O  O   . VAL   A 1 68  ? 4.917  -3.841  14.088 1.00 16.89 ? 74  VAL   A O   1 
ATOM   542  C  CB  . VAL   A 1 68  ? 5.178  -2.237  16.858 1.00 19.10 ? 74  VAL   A CB  1 
ATOM   543  C  CG1 . VAL   A 1 68  ? 5.233  -2.073  18.389 1.00 21.16 ? 74  VAL   A CG1 1 
ATOM   544  C  CG2 . VAL   A 1 68  ? 6.542  -1.981  16.212 1.00 19.69 ? 74  VAL   A CG2 1 
ATOM   545  N  N   . SER   A 1 69  ? 2.932  -2.971  14.799 1.00 15.71 ? 75  SER   A N   1 
ATOM   546  C  CA  . SER   A 1 69  ? 2.460  -2.482  13.504 1.00 16.18 ? 75  SER   A CA  1 
ATOM   547  C  C   . SER   A 1 69  ? 2.653  -0.955  13.544 1.00 15.76 ? 75  SER   A C   1 
ATOM   548  O  O   . SER   A 1 69  ? 2.439  -0.309  14.588 1.00 18.17 ? 75  SER   A O   1 
ATOM   549  C  CB  . SER   A 1 69  ? 0.971  -2.761  13.325 1.00 18.89 ? 75  SER   A CB  1 
ATOM   550  O  OG  . SER   A 1 69  ? 0.733  -4.161  13.249 1.00 26.59 ? 75  SER   A OG  1 
ATOM   551  N  N   . PHE   A 1 70  ? 3.183  -0.386  12.459 1.00 15.04 ? 76  PHE   A N   1 
ATOM   552  C  CA  . PHE   A 1 70  ? 3.447  1.051   12.426 1.00 16.08 ? 76  PHE   A CA  1 
ATOM   553  C  C   . PHE   A 1 70  ? 2.946  1.685   11.144 1.00 17.15 ? 76  PHE   A C   1 
ATOM   554  O  O   . PHE   A 1 70  ? 2.848  1.027   10.109 1.00 17.53 ? 76  PHE   A O   1 
ATOM   555  C  CB  . PHE   A 1 70  ? 4.951  1.329   12.657 1.00 15.68 ? 76  PHE   A CB  1 
ATOM   556  C  CG  . PHE   A 1 70  ? 5.906  0.554   11.752 1.00 15.57 ? 76  PHE   A CG  1 
ATOM   557  C  CD1 . PHE   A 1 70  ? 6.394  -0.685  12.130 1.00 16.18 ? 76  PHE   A CD1 1 
ATOM   558  C  CD2 . PHE   A 1 70  ? 6.341  1.101   10.543 1.00 17.25 ? 76  PHE   A CD2 1 
ATOM   559  C  CE1 . PHE   A 1 70  ? 7.293  -1.384  11.305 1.00 17.34 ? 76  PHE   A CE1 1 
ATOM   560  C  CE2 . PHE   A 1 70  ? 7.274  0.426   9.751  1.00 17.25 ? 76  PHE   A CE2 1 
ATOM   561  C  CZ  . PHE   A 1 70  ? 7.722  -0.826  10.127 1.00 17.12 ? 76  PHE   A CZ  1 
ATOM   562  N  N   . SER   A 1 71  ? 2.654  2.995   11.218 1.00 16.89 ? 77  SER   A N   1 
ATOM   563  C  CA  . SER   A 1 71  ? 2.139  3.705   10.049 1.00 18.43 ? 77  SER   A CA  1 
ATOM   564  C  C   . SER   A 1 71  ? 3.259  4.000   9.024  1.00 18.70 ? 77  SER   A C   1 
ATOM   565  O  O   . SER   A 1 71  ? 4.441  3.959   9.363  1.00 19.41 ? 77  SER   A O   1 
ATOM   566  C  CB  . SER   A 1 71  ? 1.458  5.002   10.483 1.00 18.90 ? 77  SER   A CB  1 
ATOM   567  O  OG  . SER   A 1 71  ? 2.374  5.867   11.146 1.00 21.55 ? 77  SER   A OG  1 
ATOM   568  N  N   . LYS   A 1 72  ? 2.900  4.291   7.754  1.00 19.16 ? 78  LYS   A N   1 
ATOM   569  C  CA  . LYS   A 1 72  ? 3.919  4.664   6.758  1.00 20.04 ? 78  LYS   A CA  1 
ATOM   570  C  C   . LYS   A 1 72  ? 4.491  6.035   7.119  1.00 21.08 ? 78  LYS   A C   1 
ATOM   571  O  O   . LYS   A 1 72  ? 3.812  6.859   7.750  1.00 22.41 ? 78  LYS   A O   1 
ATOM   572  C  CB  . LYS   A 1 72  ? 3.292  4.701   5.343  1.00 22.99 ? 78  LYS   A CB  1 
ATOM   573  C  CG  . LYS   A 1 72  ? 2.943  3.299   4.844  1.00 26.56 ? 78  LYS   A CG  1 
ATOM   574  C  CD  . LYS   A 1 72  ? 2.345  3.330   3.440  1.00 31.98 ? 78  LYS   A CD  1 
ATOM   575  C  CE  . LYS   A 1 72  ? 2.111  1.918   2.951  1.00 37.53 ? 78  LYS   A CE  1 
ATOM   576  N  NZ  . LYS   A 1 72  ? 1.813  1.877   1.486  1.00 41.16 ? 78  LYS   A NZ  1 
ATOM   577  N  N   . PRO   A 1 73  ? 5.729  6.319   6.700  1.00 20.15 ? 79  PRO   A N   1 
ATOM   578  C  CA  . PRO   A 1 73  ? 6.343  7.617   7.046  1.00 20.61 ? 79  PRO   A CA  1 
ATOM   579  C  C   . PRO   A 1 73  ? 5.483  8.804   6.624  1.00 21.71 ? 79  PRO   A C   1 
ATOM   580  O  O   . PRO   A 1 73  ? 5.027  8.845   5.469  1.00 22.26 ? 79  PRO   A O   1 
ATOM   581  C  CB  . PRO   A 1 73  ? 7.681  7.606   6.290  1.00 22.00 ? 79  PRO   A CB  1 
ATOM   582  C  CG  . PRO   A 1 73  ? 8.006  6.148   6.095  1.00 23.30 ? 79  PRO   A CG  1 
ATOM   583  C  CD  . PRO   A 1 73  ? 6.644  5.455   5.935  1.00 20.94 ? 79  PRO   A CD  1 
ATOM   584  N  N   . SER   A 1 74  ? 5.250  9.746   7.551  1.00 20.31 ? 80  SER   A N   1 
ATOM   585  C  CA  . SER   A 1 74  ? 4.380  10.875  7.251  1.00 22.54 ? 80  SER   A CA  1 
ATOM   586  C  C   . SER   A 1 74  ? 4.717  12.120  8.086  1.00 22.65 ? 80  SER   A C   1 
ATOM   587  O  O   . SER   A 1 74  ? 5.652  12.098  8.903  1.00 21.03 ? 80  SER   A O   1 
ATOM   588  C  CB  . SER   A 1 74  ? 2.908  10.478  7.378  1.00 28.03 ? 80  SER   A CB  1 
ATOM   589  O  OG  . SER   A 1 74  ? 2.532  10.368  8.733  1.00 34.95 ? 80  SER   A OG  1 
ATOM   590  N  N   . LEU   A 1 75  ? 4.005  13.246  7.796  1.00 22.67 ? 81  LEU   A N   1 
ATOM   591  C  CA  . LEU   A 1 75  ? 4.220  14.540  8.450  1.00 24.33 ? 81  LEU   A CA  1 
ATOM   592  C  C   . LEU   A 1 75  ? 3.248  14.625  9.602  1.00 26.31 ? 81  LEU   A C   1 
ATOM   593  O  O   . LEU   A 1 75  ? 2.009  14.636  9.385  1.00 27.64 ? 81  LEU   A O   1 
ATOM   594  C  CB  . LEU   A 1 75  ? 3.983  15.682  7.417  1.00 24.95 ? 81  LEU   A CB  1 
ATOM   595  C  CG  . LEU   A 1 75  ? 4.395  17.076  7.878  1.00 26.26 ? 81  LEU   A CG  1 
ATOM   596  C  CD1 . LEU   A 1 75  ? 5.869  17.170  8.124  1.00 25.80 ? 81  LEU   A CD1 1 
ATOM   597  C  CD2 . LEU   A 1 75  ? 4.015  18.133  6.853  1.00 28.04 ? 81  LEU   A CD2 1 
ATOM   598  N  N   . ILE   A 1 76  ? 3.781  14.504  10.838 1.00 26.17 ? 82  ILE   A N   1 
ATOM   599  C  CA  . ILE   A 1 76  ? 2.946  14.401  12.031 1.00 26.95 ? 82  ILE   A CA  1 
ATOM   600  C  C   . ILE   A 1 76  ? 3.209  15.545  12.993 1.00 28.09 ? 82  ILE   A C   1 
ATOM   601  O  O   . ILE   A 1 76  ? 4.372  15.871  13.238 1.00 26.79 ? 82  ILE   A O   1 
ATOM   602  C  CB  . ILE   A 1 76  ? 3.285  13.023  12.689 1.00 28.29 ? 82  ILE   A CB  1 
ATOM   603  C  CG1 . ILE   A 1 76  ? 2.939  11.873  11.737 1.00 30.10 ? 82  ILE   A CG1 1 
ATOM   604  C  CG2 . ILE   A 1 76  ? 2.666  12.853  14.101 1.00 29.67 ? 82  ILE   A CG2 1 
ATOM   605  C  CD1 . ILE   A 1 76  ? 3.310  10.580  12.192 1.00 32.63 ? 82  ILE   A CD1 1 
ATOM   606  N  N   . PHE   A 1 77  ? 2.137  16.110  13.606 1.00 29.04 ? 83  PHE   A N   1 
ATOM   607  C  CA  . PHE   A 1 77  ? 2.335  17.169  14.588 1.00 31.19 ? 83  PHE   A CA  1 
ATOM   608  C  C   . PHE   A 1 77  ? 2.783  16.525  15.884 1.00 32.20 ? 83  PHE   A C   1 
ATOM   609  O  O   . PHE   A 1 77  ? 2.137  15.608  16.364 1.00 35.19 ? 83  PHE   A O   1 
ATOM   610  C  CB  . PHE   A 1 77  ? 1.045  17.999  14.838 1.00 33.05 ? 83  PHE   A CB  1 
ATOM   611  C  CG  . PHE   A 1 77  ? 1.332  19.208  15.708 1.00 35.36 ? 83  PHE   A CG  1 
ATOM   612  C  CD1 . PHE   A 1 77  ? 2.027  20.293  15.206 1.00 37.23 ? 83  PHE   A CD1 1 
ATOM   613  C  CD2 . PHE   A 1 77  ? 0.987  19.216  17.046 1.00 37.05 ? 83  PHE   A CD2 1 
ATOM   614  C  CE1 . PHE   A 1 77  ? 2.345  21.380  16.021 1.00 38.58 ? 83  PHE   A CE1 1 
ATOM   615  C  CE2 . PHE   A 1 77  ? 1.269  20.321  17.849 1.00 38.12 ? 83  PHE   A CE2 1 
ATOM   616  C  CZ  . PHE   A 1 77  ? 1.946  21.390  17.334 1.00 38.47 ? 83  PHE   A CZ  1 
ATOM   617  N  N   . VAL   A 1 78  ? 3.922  16.965  16.434 1.00 30.48 ? 84  VAL   A N   1 
ATOM   618  C  CA  . VAL   A 1 78  ? 4.423  16.427  17.689 1.00 30.31 ? 84  VAL   A CA  1 
ATOM   619  C  C   . VAL   A 1 78  ? 4.517  17.547  18.746 1.00 29.98 ? 84  VAL   A C   1 
ATOM   620  O  O   . VAL   A 1 78  ? 4.933  18.669  18.449 1.00 31.29 ? 84  VAL   A O   1 
ATOM   621  C  CB  . VAL   A 1 78  ? 5.762  15.638  17.513 1.00 31.22 ? 84  VAL   A CB  1 
ATOM   622  C  CG1 . VAL   A 1 78  ? 5.578  14.424  16.599 1.00 31.51 ? 84  VAL   A CG1 1 
ATOM   623  C  CG2 . VAL   A 1 78  ? 6.845  16.528  16.964 1.00 31.73 ? 84  VAL   A CG2 1 
ATOM   624  N  N   . GLU   A 1 79  ? 4.186  17.225  19.977 1.00 29.78 ? 85  GLU   A N   1 
ATOM   625  C  CA  . GLU   A 1 79  ? 4.191  18.205  21.077 1.00 30.42 ? 85  GLU   A CA  1 
ATOM   626  C  C   . GLU   A 1 79  ? 5.607  18.667  21.439 1.00 30.32 ? 85  GLU   A C   1 
ATOM   627  O  O   . GLU   A 1 79  ? 6.581  18.026  21.035 1.00 29.37 ? 85  GLU   A O   1 
ATOM   628  C  CB  . GLU   A 1 79  ? 3.493  17.586  22.313 1.00 33.90 ? 85  GLU   A CB  1 
ATOM   629  C  CG  . GLU   A 1 79  ? 1.996  17.409  22.134 1.00 40.89 ? 85  GLU   A CG  1 
ATOM   630  C  CD  . GLU   A 1 79  ? 1.281  18.734  21.984 1.00 51.97 ? 85  GLU   A CD  1 
ATOM   631  O  OE1 . GLU   A 1 79  ? 0.528  18.891  20.997 1.00 54.61 ? 85  GLU   A OE1 1 
ATOM   632  O  OE2 . GLU   A 1 79  ? 1.502  19.628  22.833 1.00 55.14 ? 85  GLU   A OE2 1 
ATOM   633  N  N   . ALA   A 1 80  ? 5.718  19.773  22.204 1.00 30.89 ? 86  ALA   A N   1 
ATOM   634  C  CA  . ALA   A 1 80  ? 6.987  20.292  22.673 1.00 31.48 ? 86  ALA   A CA  1 
ATOM   635  C  C   . ALA   A 1 80  ? 7.651  19.272  23.589 1.00 32.38 ? 86  ALA   A C   1 
ATOM   636  O  O   . ALA   A 1 80  ? 6.972  18.477  24.261 1.00 32.60 ? 86  ALA   A O   1 
ATOM   637  C  CB  . ALA   A 1 80  ? 6.752  21.578  23.459 1.00 31.64 ? 86  ALA   A CB  1 
ATOM   638  N  N   . SER   A 1 81  ? 8.985  19.299  23.610 1.00 31.96 ? 87  SER   A N   1 
ATOM   639  C  CA  . SER   A 1 81  ? 9.804  18.492  24.502 1.00 32.59 ? 87  SER   A CA  1 
ATOM   640  C  C   . SER   A 1 81  ? 10.537 19.460  25.476 1.00 33.97 ? 87  SER   A C   1 
ATOM   641  O  O   . SER   A 1 81  ? 10.256 20.670  25.468 1.00 34.48 ? 87  SER   A O   1 
ATOM   642  C  CB  . SER   A 1 81  ? 10.768 17.616  23.707 1.00 31.69 ? 87  SER   A CB  1 
ATOM   643  O  OG  . SER   A 1 81  ? 11.683 18.415  22.970 1.00 31.65 ? 87  SER   A OG  1 
ATOM   644  N  N   . GLU   A 1 82  ? 11.406 18.950  26.354 1.00 35.21 ? 88  GLU   A N   1 
ATOM   645  C  CA  . GLU   A 1 82  ? 12.065 19.791  27.365 1.00 36.78 ? 88  GLU   A CA  1 
ATOM   646  C  C   . GLU   A 1 82  ? 12.801 21.018  26.821 1.00 37.13 ? 88  GLU   A C   1 
ATOM   647  O  O   . GLU   A 1 82  ? 12.694 22.111  27.385 1.00 36.29 ? 88  GLU   A O   1 
ATOM   648  C  CB  . GLU   A 1 82  ? 13.021 18.947  28.223 1.00 40.88 ? 88  GLU   A CB  1 
ATOM   649  C  CG  . GLU   A 1 82  ? 13.533 19.699  29.439 1.00 47.97 ? 88  GLU   A CG  1 
ATOM   650  C  CD  . GLU   A 1 82  ? 14.336 18.871  30.422 1.00 58.22 ? 88  GLU   A CD  1 
ATOM   651  O  OE1 . GLU   A 1 82  ? 14.401 17.632  30.251 1.00 59.94 ? 88  GLU   A OE1 1 
ATOM   652  O  OE2 . GLU   A 1 82  ? 14.901 19.466  31.370 1.00 62.42 ? 88  GLU   A OE2 1 
ATOM   653  N  N   . TYR   A 1 83  ? 13.555 20.842  25.733 1.00 37.81 ? 89  TYR   A N   1 
ATOM   654  C  CA  . TYR   A 1 83  ? 14.370 21.919  25.177 1.00 38.65 ? 89  TYR   A CA  1 
ATOM   655  C  C   . TYR   A 1 83  ? 14.051 22.297  23.744 1.00 38.56 ? 89  TYR   A C   1 
ATOM   656  O  O   . TYR   A 1 83  ? 14.848 23.006  23.132 1.00 39.37 ? 89  TYR   A O   1 
ATOM   657  C  CB  . TYR   A 1 83  ? 15.842 21.494  25.238 1.00 39.84 ? 89  TYR   A CB  1 
ATOM   658  C  CG  . TYR   A 1 83  ? 16.299 21.203  26.647 1.00 42.29 ? 89  TYR   A CG  1 
ATOM   659  C  CD1 . TYR   A 1 83  ? 16.377 22.214  27.592 1.00 43.96 ? 89  TYR   A CD1 1 
ATOM   660  C  CD2 . TYR   A 1 83  ? 16.652 19.917  27.034 1.00 44.18 ? 89  TYR   A CD2 1 
ATOM   661  C  CE1 . TYR   A 1 83  ? 16.790 21.956  28.890 1.00 45.62 ? 89  TYR   A CE1 1 
ATOM   662  C  CE2 . TYR   A 1 83  ? 17.052 19.643  28.337 1.00 45.59 ? 89  TYR   A CE2 1 
ATOM   663  C  CZ  . TYR   A 1 83  ? 17.128 20.668  29.260 1.00 47.08 ? 89  TYR   A CZ  1 
ATOM   664  O  OH  . TYR   A 1 83  ? 17.531 20.430  30.553 1.00 50.11 ? 89  TYR   A OH  1 
ATOM   665  N  N   . TYR   A 1 84  ? 12.908 21.863  23.207 1.00 37.73 ? 90  TYR   A N   1 
ATOM   666  C  CA  . TYR   A 1 84  ? 12.539 22.092  21.803 1.00 37.62 ? 90  TYR   A CA  1 
ATOM   667  C  C   . TYR   A 1 84  ? 11.049 22.335  21.656 1.00 35.27 ? 90  TYR   A C   1 
ATOM   668  O  O   . TYR   A 1 84  ? 10.261 21.714  22.366 1.00 36.42 ? 90  TYR   A O   1 
ATOM   669  C  CB  . TYR   A 1 84  ? 12.923 20.862  20.951 1.00 38.89 ? 90  TYR   A CB  1 
ATOM   670  C  CG  . TYR   A 1 84  ? 14.146 21.069  20.091 1.00 42.64 ? 90  TYR   A CG  1 
ATOM   671  C  CD1 . TYR   A 1 84  ? 15.303 20.342  20.310 1.00 45.09 ? 90  TYR   A CD1 1 
ATOM   672  C  CD2 . TYR   A 1 84  ? 14.153 22.011  19.073 1.00 44.81 ? 90  TYR   A CD2 1 
ATOM   673  C  CE1 . TYR   A 1 84  ? 16.434 20.531  19.523 1.00 47.06 ? 90  TYR   A CE1 1 
ATOM   674  C  CE2 . TYR   A 1 84  ? 15.269 22.203  18.273 1.00 46.54 ? 90  TYR   A CE2 1 
ATOM   675  C  CZ  . TYR   A 1 84  ? 16.412 21.466  18.506 1.00 48.37 ? 90  TYR   A CZ  1 
ATOM   676  O  OH  . TYR   A 1 84  ? 17.517 21.656  17.715 1.00 51.69 ? 90  TYR   A OH  1 
ATOM   677  N  N   . PRO   A 1 85  ? 10.625 23.205  20.725 1.00 32.39 ? 91  PRO   A N   1 
ATOM   678  C  CA  . PRO   A 1 85  ? 9.187  23.486  20.590 1.00 31.24 ? 91  PRO   A CA  1 
ATOM   679  C  C   . PRO   A 1 85  ? 8.402  22.413  19.846 1.00 32.30 ? 91  PRO   A C   1 
ATOM   680  O  O   . PRO   A 1 85  ? 8.973  21.501  19.230 1.00 33.28 ? 91  PRO   A O   1 
ATOM   681  C  CB  . PRO   A 1 85  ? 9.172  24.788  19.774 1.00 31.42 ? 91  PRO   A CB  1 
ATOM   682  C  CG  . PRO   A 1 85  ? 10.415 24.690  18.914 1.00 32.38 ? 91  PRO   A CG  1 
ATOM   683  C  CD  . PRO   A 1 85  ? 11.437 24.055  19.821 1.00 31.46 ? 91  PRO   A CD  1 
ATOM   684  N  N   . ALA   A 1 86  ? 7.071  22.537  19.907 1.00 31.88 ? 92  ALA   A N   1 
ATOM   685  C  CA  . ALA   A 1 86  ? 6.154  21.681  19.179 1.00 32.66 ? 92  ALA   A CA  1 
ATOM   686  C  C   . ALA   A 1 86  ? 6.297  22.034  17.707 1.00 33.09 ? 92  ALA   A C   1 
ATOM   687  O  O   . ALA   A 1 86  ? 6.400  23.213  17.359 1.00 34.93 ? 92  ALA   A O   1 
ATOM   688  C  CB  . ALA   A 1 86  ? 4.739  21.952  19.629 1.00 32.37 ? 92  ALA   A CB  1 
ATOM   689  N  N   . ARG   A 1 87  ? 6.261  21.024  16.838 1.00 31.32 ? 93  ARG   A N   1 
ATOM   690  C  CA  . ARG   A 1 87  ? 6.398  21.268  15.409 1.00 30.22 ? 93  ARG   A CA  1 
ATOM   691  C  C   . ARG   A 1 87  ? 5.898  20.075  14.626 1.00 28.70 ? 93  ARG   A C   1 
ATOM   692  O  O   . ARG   A 1 87  ? 5.536  19.054  15.225 1.00 28.92 ? 93  ARG   A O   1 
ATOM   693  C  CB  . ARG   A 1 87  ? 7.873  21.632  15.044 1.00 31.25 ? 93  ARG   A CB  1 
ATOM   694  C  CG  . ARG   A 1 87  ? 9.000  20.661  15.529 1.00 34.46 ? 93  ARG   A CG  1 
ATOM   695  C  CD  . ARG   A 1 87  ? 9.672  19.920  14.342 1.00 39.87 ? 93  ARG   A CD  1 
ATOM   696  N  NE  . ARG   A 1 87  ? 10.897 19.141  14.637 1.00 40.12 ? 93  ARG   A NE  1 
ATOM   697  C  CZ  . ARG   A 1 87  ? 10.943 18.108  15.473 1.00 41.16 ? 93  ARG   A CZ  1 
ATOM   698  N  NH1 . ARG   A 1 87  ? 12.083 17.458  15.675 1.00 39.29 ? 93  ARG   A NH1 1 
ATOM   699  N  NH2 . ARG   A 1 87  ? 9.862  17.744  16.148 1.00 41.33 ? 93  ARG   A NH2 1 
ATOM   700  N  N   . TYR   A 1 88  ? 5.878  20.182  13.294 1.00 28.11 ? 94  TYR   A N   1 
ATOM   701  C  CA  . TYR   A 1 88  ? 5.551  19.028  12.457 1.00 27.85 ? 94  TYR   A CA  1 
ATOM   702  C  C   . TYR   A 1 88  ? 6.858  18.312  12.192 1.00 25.51 ? 94  TYR   A C   1 
ATOM   703  O  O   . TYR   A 1 88  ? 7.810  18.935  11.708 1.00 26.71 ? 94  TYR   A O   1 
ATOM   704  C  CB  . TYR   A 1 88  ? 4.982  19.480  11.115 1.00 29.64 ? 94  TYR   A CB  1 
ATOM   705  C  CG  . TYR   A 1 88  ? 3.528  19.873  11.210 1.00 32.18 ? 94  TYR   A CG  1 
ATOM   706  C  CD1 . TYR   A 1 88  ? 2.524  18.920  11.127 1.00 34.11 ? 94  TYR   A CD1 1 
ATOM   707  C  CD2 . TYR   A 1 88  ? 3.160  21.186  11.464 1.00 34.22 ? 94  TYR   A CD2 1 
ATOM   708  C  CE1 . TYR   A 1 88  ? 1.183  19.274  11.237 1.00 36.20 ? 94  TYR   A CE1 1 
ATOM   709  C  CE2 . TYR   A 1 88  ? 1.822  21.555  11.564 1.00 35.86 ? 94  TYR   A CE2 1 
ATOM   710  C  CZ  . TYR   A 1 88  ? 0.836  20.594  11.456 1.00 37.40 ? 94  TYR   A CZ  1 
ATOM   711  O  OH  . TYR   A 1 88  ? -0.494 20.955  11.584 1.00 40.97 ? 94  TYR   A OH  1 
ATOM   712  N  N   . GLN   A 1 89  ? 6.910  17.016  12.498 1.00 22.38 ? 95  GLN   A N   1 
ATOM   713  C  CA  . GLN   A 1 89  ? 8.092  16.194  12.229 1.00 21.56 ? 95  GLN   A CA  1 
ATOM   714  C  C   . GLN   A 1 89  ? 7.773  15.360  10.999 1.00 20.09 ? 95  GLN   A C   1 
ATOM   715  O  O   . GLN   A 1 89  ? 6.690  14.740  10.912 1.00 21.05 ? 95  GLN   A O   1 
ATOM   716  C  CB  . GLN   A 1 89  ? 8.437  15.305  13.433 1.00 21.23 ? 95  GLN   A CB  1 
ATOM   717  C  CG  . GLN   A 1 89  ? 9.680  14.419  13.200 1.00 20.88 ? 95  GLN   A CG  1 
ATOM   718  C  CD  . GLN   A 1 89  ? 10.281 13.845  14.482 1.00 20.54 ? 95  GLN   A CD  1 
ATOM   719  O  OE1 . GLN   A 1 89  ? 10.257 14.455  15.541 1.00 23.09 ? 95  GLN   A OE1 1 
ATOM   720  N  NE2 . GLN   A 1 89  ? 10.882 12.639  14.392 1.00 18.21 ? 95  GLN   A NE2 1 
ATOM   721  N  N   . SER   A 1 90  ? 8.702  15.335  10.032 1.00 19.08 ? 96  SER   A N   1 
ATOM   722  C  CA  . SER   A 1 90  ? 8.471  14.589  8.797  1.00 18.29 ? 96  SER   A CA  1 
ATOM   723  C  C   . SER   A 1 90  ? 9.115  13.180  8.864  1.00 18.52 ? 96  SER   A C   1 
ATOM   724  O  O   . SER   A 1 90  ? 9.971  12.890  9.733  1.00 19.14 ? 96  SER   A O   1 
ATOM   725  C  CB  . SER   A 1 90  ? 9.045  15.374  7.606  1.00 20.06 ? 96  SER   A CB  1 
ATOM   726  O  OG  . SER   A 1 90  ? 10.445 15.531  7.738  1.00 21.80 ? 96  SER   A OG  1 
ATOM   727  N  N   . HIS   A 1 91  ? 8.683  12.320  7.933  1.00 18.14 ? 97  HIS   A N   1 
ATOM   728  C  CA  . HIS   A 1 91  ? 9.188  10.937  7.780  1.00 18.11 ? 97  HIS   A CA  1 
ATOM   729  C  C   . HIS   A 1 91  ? 9.083  10.164  9.115  1.00 18.27 ? 97  HIS   A C   1 
ATOM   730  O  O   . HIS   A 1 91  ? 9.938  9.332   9.420  1.00 17.46 ? 97  HIS   A O   1 
ATOM   731  C  CB  . HIS   A 1 91  ? 10.661 10.985  7.296  1.00 18.01 ? 97  HIS   A CB  1 
ATOM   732  C  CG  . HIS   A 1 91  ? 10.825 11.634  5.951  1.00 20.97 ? 97  HIS   A CG  1 
ATOM   733  N  ND1 . HIS   A 1 91  ? 10.861 10.877  4.782  1.00 23.36 ? 97  HIS   A ND1 1 
ATOM   734  C  CD2 . HIS   A 1 91  ? 10.962 12.945  5.630  1.00 21.56 ? 97  HIS   A CD2 1 
ATOM   735  C  CE1 . HIS   A 1 91  ? 11.053 11.751  3.792  1.00 23.21 ? 97  HIS   A CE1 1 
ATOM   736  N  NE2 . HIS   A 1 91  ? 11.073 13.006  4.238  1.00 22.72 ? 97  HIS   A NE2 1 
ATOM   737  N  N   . LEU   A 1 92  ? 7.991  10.399  9.840  1.00 17.50 ? 98  LEU   A N   1 
ATOM   738  C  CA  . LEU   A 1 92  ? 7.766  9.779   11.140 1.00 17.21 ? 98  LEU   A CA  1 
ATOM   739  C  C   . LEU   A 1 92  ? 6.738  8.650   10.991 1.00 17.24 ? 98  LEU   A C   1 
ATOM   740  O  O   . LEU   A 1 92  ? 5.715  8.807   10.305 1.00 17.87 ? 98  LEU   A O   1 
ATOM   741  C  CB  . LEU   A 1 92  ? 7.266  10.835  12.141 1.00 18.29 ? 98  LEU   A CB  1 
ATOM   742  C  CG  . LEU   A 1 92  ? 7.126  10.373  13.629 1.00 19.59 ? 98  LEU   A CG  1 
ATOM   743  C  CD1 . LEU   A 1 92  ? 8.477  10.003  14.212 1.00 20.79 ? 98  LEU   A CD1 1 
ATOM   744  C  CD2 . LEU   A 1 92  ? 6.549  11.520  14.466 1.00 20.10 ? 98  LEU   A CD2 1 
ATOM   745  N  N   . MET   A 1 93  ? 6.964  7.535   11.718 1.00 16.73 ? 99  MET   A N   1 
ATOM   746  C  CA  . MET   A 1 93  ? 6.048  6.369   11.729 1.00 16.27 ? 99  MET   A CA  1 
ATOM   747  C  C   . MET   A 1 93  ? 5.568  6.142   13.144 1.00 16.73 ? 99  MET   A C   1 
ATOM   748  O  O   . MET   A 1 93  ? 6.397  6.157   14.058 1.00 17.19 ? 99  MET   A O   1 
ATOM   749  C  CB  . MET   A 1 93  ? 6.815  5.119   11.231 1.00 16.43 ? 99  MET   A CB  1 
ATOM   750  C  CG  . MET   A 1 93  ? 7.382  5.327   9.806  1.00 19.07 ? 99  MET   A CG  1 
ATOM   751  S  SD  . MET   A 1 93  ? 8.419  3.978   9.281  1.00 20.85 ? 99  MET   A SD  1 
ATOM   752  C  CE  . MET   A 1 93  ? 9.851  4.183   10.368 1.00 22.47 ? 99  MET   A CE  1 
ATOM   753  N  N   . LEU   A 1 94  ? 4.255  5.966   13.371 1.00 16.79 ? 100 LEU   A N   1 
ATOM   754  C  CA  . LEU   A 1 94  ? 3.773  5.781   14.757 1.00 16.60 ? 100 LEU   A CA  1 
ATOM   755  C  C   . LEU   A 1 94  ? 3.293  4.354   14.972 1.00 15.95 ? 100 LEU   A C   1 
ATOM   756  O  O   . LEU   A 1 94  ? 2.756  3.717   14.060 1.00 16.82 ? 100 LEU   A O   1 
ATOM   757  C  CB  . LEU   A 1 94  ? 2.543  6.715   15.075 1.00 18.85 ? 100 LEU   A CB  1 
ATOM   758  C  CG  . LEU   A 1 94  ? 2.803  8.203   15.090 1.00 22.94 ? 100 LEU   A CG  1 
ATOM   759  C  CD1 . LEU   A 1 94  ? 1.538  8.946   15.540 1.00 25.13 ? 100 LEU   A CD1 1 
ATOM   760  C  CD2 . LEU   A 1 94  ? 3.980  8.575   16.000 1.00 24.96 ? 100 LEU   A CD2 1 
ATOM   761  N  N   . ALA   A 1 95  ? 3.447  3.885   16.195 1.00 14.96 ? 101 ALA   A N   1 
ATOM   762  C  CA  . ALA   A 1 95  ? 2.899  2.594   16.610 1.00 15.40 ? 101 ALA   A CA  1 
ATOM   763  C  C   . ALA   A 1 95  ? 2.346  2.741   18.036 1.00 15.90 ? 101 ALA   A C   1 
ATOM   764  O  O   . ALA   A 1 95  ? 2.726  3.676   18.768 1.00 17.24 ? 101 ALA   A O   1 
ATOM   765  C  CB  . ALA   A 1 95  ? 4.016  1.518   16.652 1.00 16.37 ? 101 ALA   A CB  1 
ATOM   766  N  N   . VAL   A 1 96  ? 1.458  1.856   18.427 1.00 15.98 ? 102 VAL   A N   1 
ATOM   767  C  CA  . VAL   A 1 96  ? 0.992  1.792   19.805 1.00 15.67 ? 102 VAL   A CA  1 
ATOM   768  C  C   . VAL   A 1 96  ? 2.058  1.043   20.614 1.00 17.18 ? 102 VAL   A C   1 
ATOM   769  O  O   . VAL   A 1 96  ? 2.363  -0.138  20.351 1.00 19.09 ? 102 VAL   A O   1 
ATOM   770  C  CB  . VAL   A 1 96  ? -0.384 1.091   19.892 1.00 16.93 ? 102 VAL   A CB  1 
ATOM   771  C  CG1 . VAL   A 1 96  ? -0.824 0.946   21.348 1.00 17.84 ? 102 VAL   A CG1 1 
ATOM   772  C  CG2 . VAL   A 1 96  ? -1.413 1.862   19.064 1.00 18.14 ? 102 VAL   A CG2 1 
ATOM   773  N  N   . GLY   A 1 97  ? 2.658  1.753   21.560 1.00 18.47 ? 103 GLY   A N   1 
ATOM   774  C  CA  . GLY   A 1 97  ? 3.711  1.128   22.358 1.00 19.86 ? 103 GLY   A CA  1 
ATOM   775  C  C   . GLY   A 1 97  ? 4.349  2.081   23.324 1.00 21.07 ? 103 GLY   A C   1 
ATOM   776  O  O   . GLY   A 1 97  ? 4.087  3.275   23.293 1.00 22.13 ? 103 GLY   A O   1 
ATOM   777  N  N   . HIS   A 1 98  ? 5.231  1.532   24.179 1.00 20.93 ? 104 HIS   A N   1 
ATOM   778  C  CA  . HIS   A 1 98  ? 5.854  2.346   25.205 1.00 20.46 ? 104 HIS   A CA  1 
ATOM   779  C  C   . HIS   A 1 98  ? 7.126  3.014   24.750 1.00 19.50 ? 104 HIS   A C   1 
ATOM   780  O  O   . HIS   A 1 98  ? 7.943  2.393   24.063 1.00 18.84 ? 104 HIS   A O   1 
ATOM   781  C  CB  . HIS   A 1 98  ? 6.182  1.449   26.419 1.00 20.09 ? 104 HIS   A CB  1 
ATOM   782  C  CG  . HIS   A 1 98  ? 6.736  2.213   27.566 1.00 21.21 ? 104 HIS   A CG  1 
ATOM   783  N  ND1 . HIS   A 1 98  ? 5.953  3.117   28.250 1.00 23.77 ? 104 HIS   A ND1 1 
ATOM   784  C  CD2 . HIS   A 1 98  ? 7.992  2.232   28.082 1.00 21.59 ? 104 HIS   A CD2 1 
ATOM   785  C  CE1 . HIS   A 1 98  ? 6.738  3.642   29.182 1.00 24.39 ? 104 HIS   A CE1 1 
ATOM   786  N  NE2 . HIS   A 1 98  ? 7.986  3.168   29.094 1.00 22.82 ? 104 HIS   A NE2 1 
ATOM   787  N  N   A SER   A 1 99  ? 7.316  4.298   25.111 0.50 19.99 ? 105 SER   A N   1 
ATOM   788  N  N   B SER   A 1 99  ? 7.319  4.238   25.171 0.50 19.37 ? 105 SER   A N   1 
ATOM   789  C  CA  A SER   A 1 99  ? 8.505  5.072   24.769 0.50 21.28 ? 105 SER   A CA  1 
ATOM   790  C  CA  B SER   A 1 99  ? 8.564  4.928   24.998 0.50 19.69 ? 105 SER   A CA  1 
ATOM   791  C  C   A SER   A 1 99  ? 8.702  6.191   25.804 0.50 22.12 ? 105 SER   A C   1 
ATOM   792  C  C   B SER   A 1 99  ? 8.674  6.013   26.062 0.50 21.07 ? 105 SER   A C   1 
ATOM   793  O  O   A SER   A 1 99  ? 7.748  6.929   26.054 0.50 23.26 ? 105 SER   A O   1 
ATOM   794  O  O   B SER   A 1 99  ? 7.668  6.522   26.598 0.50 21.93 ? 105 SER   A O   1 
ATOM   795  C  CB  A SER   A 1 99  ? 8.328  5.695   23.385 0.50 23.56 ? 105 SER   A CB  1 
ATOM   796  C  CB  B SER   A 1 99  ? 8.730  5.490   23.590 0.50 19.86 ? 105 SER   A CB  1 
ATOM   797  O  OG  A SER   A 1 99  ? 9.380  6.574   23.020 0.50 27.23 ? 105 SER   A OG  1 
ATOM   798  O  OG  B SER   A 1 99  ? 7.783  6.516   23.374 0.50 20.49 ? 105 SER   A OG  1 
ATOM   799  N  N   . GLU   A 1 100 ? 9.904  6.292   26.413 1.00 21.23 ? 106 GLU   A N   1 
ATOM   800  C  CA  . GLU   A 1 100 ? 10.320 7.347   27.354 1.00 22.13 ? 106 GLU   A CA  1 
ATOM   801  C  C   . GLU   A 1 100 ? 11.483 8.086   26.671 1.00 23.12 ? 106 GLU   A C   1 
ATOM   802  O  O   . GLU   A 1 100 ? 12.058 7.552   25.714 1.00 22.40 ? 106 GLU   A O   1 
ATOM   803  C  CB  . GLU   A 1 100 ? 10.789 6.719   28.668 1.00 24.18 ? 106 GLU   A CB  1 
ATOM   804  C  CG  . GLU   A 1 100 ? 9.611  6.184   29.442 1.00 28.15 ? 106 GLU   A CG  1 
ATOM   805  C  CD  . GLU   A 1 100 ? 10.008 5.473   30.723 1.00 30.08 ? 106 GLU   A CD  1 
ATOM   806  O  OE1 . GLU   A 1 100 ? 10.932 5.955   31.411 1.00 35.73 ? 106 GLU   A OE1 1 
ATOM   807  O  OE2 . GLU   A 1 100 ? 9.417  4.415   31.023 1.00 28.39 ? 106 GLU   A OE2 1 
ATOM   808  N  N   . PRO   A 1 101 ? 11.829 9.321   27.076 1.00 23.76 ? 107 PRO   A N   1 
ATOM   809  C  CA  . PRO   A 1 101 ? 12.889 10.065  26.362 1.00 22.43 ? 107 PRO   A CA  1 
ATOM   810  C  C   . PRO   A 1 101 ? 14.189 9.312   26.089 1.00 21.63 ? 107 PRO   A C   1 
ATOM   811  O  O   . PRO   A 1 101 ? 14.715 9.363   24.965 1.00 22.76 ? 107 PRO   A O   1 
ATOM   812  C  CB  . PRO   A 1 101 ? 13.134 11.276  27.279 1.00 23.94 ? 107 PRO   A CB  1 
ATOM   813  C  CG  . PRO   A 1 101 ? 11.776 11.533  27.825 1.00 25.30 ? 107 PRO   A CG  1 
ATOM   814  C  CD  . PRO   A 1 101 ? 11.204 10.154  28.117 1.00 23.69 ? 107 PRO   A CD  1 
ATOM   815  N  N   . GLY   A 1 102 ? 14.687 8.602   27.098 1.00 20.42 ? 108 GLY   A N   1 
ATOM   816  C  CA  . GLY   A 1 102 ? 15.928 7.837   26.968 1.00 20.52 ? 108 GLY   A CA  1 
ATOM   817  C  C   . GLY   A 1 102 ? 15.846 6.642   26.035 1.00 19.12 ? 108 GLY   A C   1 
ATOM   818  O  O   . GLY   A 1 102 ? 16.853 5.988   25.773 1.00 20.34 ? 108 GLY   A O   1 
ATOM   819  N  N   . ASP   A 1 103 ? 14.634 6.294   25.595 1.00 18.00 ? 109 ASP   A N   1 
ATOM   820  C  CA  . ASP   A 1 103 ? 14.462 5.219   24.609 1.00 16.73 ? 109 ASP   A CA  1 
ATOM   821  C  C   . ASP   A 1 103 ? 14.845 5.663   23.184 1.00 16.70 ? 109 ASP   A C   1 
ATOM   822  O  O   . ASP   A 1 103 ? 14.991 4.824   22.280 1.00 16.92 ? 109 ASP   A O   1 
ATOM   823  C  CB  . ASP   A 1 103 ? 13.005 4.718   24.587 1.00 16.97 ? 109 ASP   A CB  1 
ATOM   824  C  CG  . ASP   A 1 103 ? 12.686 3.928   25.828 1.00 19.22 ? 109 ASP   A CG  1 
ATOM   825  O  OD1 . ASP   A 1 103 ? 13.584 3.205   26.307 1.00 19.84 ? 109 ASP   A OD1 1 
ATOM   826  O  OD2 . ASP   A 1 103 ? 11.524 4.008   26.311 1.00 19.35 ? 109 ASP   A OD2 1 
ATOM   827  N  N   . CYS   A 1 104 ? 15.015 7.003   22.964 1.00 16.74 ? 110 CYS   A N   1 
ATOM   828  C  CA  . CYS   A 1 104 ? 15.455 7.475   21.633 1.00 17.59 ? 110 CYS   A CA  1 
ATOM   829  C  C   . CYS   A 1 104 ? 16.712 6.789   21.183 1.00 17.51 ? 110 CYS   A C   1 
ATOM   830  O  O   . CYS   A 1 104 ? 17.653 6.639   21.982 1.00 19.32 ? 110 CYS   A O   1 
ATOM   831  C  CB  . CYS   A 1 104 ? 15.638 8.984   21.646 1.00 17.73 ? 110 CYS   A CB  1 
ATOM   832  S  SG  . CYS   A 1 104 ? 14.067 9.892   21.566 1.00 20.34 ? 110 CYS   A SG  1 
ATOM   833  N  N   . GLY   A 1 105 ? 16.737 6.366   19.925 1.00 16.15 ? 111 GLY   A N   1 
ATOM   834  C  CA  . GLY   A 1 105 ? 17.902 5.667   19.406 1.00 16.32 ? 111 GLY   A CA  1 
ATOM   835  C  C   . GLY   A 1 105 ? 17.729 4.161   19.341 1.00 16.93 ? 111 GLY   A C   1 
ATOM   836  O  O   . GLY   A 1 105 ? 18.512 3.477   18.685 1.00 17.45 ? 111 GLY   A O   1 
ATOM   837  N  N   . GLY   A 1 106 ? 16.692 3.641   20.006 1.00 16.33 ? 112 GLY   A N   1 
ATOM   838  C  CA  . GLY   A 1 106 ? 16.392 2.213   19.899 1.00 15.11 ? 112 GLY   A CA  1 
ATOM   839  C  C   . GLY   A 1 106 ? 16.010 1.889   18.455 1.00 14.96 ? 112 GLY   A C   1 
ATOM   840  O  O   . GLY   A 1 106 ? 15.277 2.653   17.817 1.00 15.73 ? 112 GLY   A O   1 
ATOM   841  N  N   . ILE   A 1 107 ? 16.537 0.769   17.935 1.00 14.16 ? 113 ILE   A N   1 
ATOM   842  C  CA  . ILE   A 1 107 ? 16.271 0.428   16.537 1.00 14.44 ? 113 ILE   A CA  1 
ATOM   843  C  C   . ILE   A 1 107 ? 14.979 -0.342  16.346 1.00 14.13 ? 113 ILE   A C   1 
ATOM   844  O  O   . ILE   A 1 107 ? 14.654 -1.251  17.134 1.00 15.43 ? 113 ILE   A O   1 
ATOM   845  C  CB  . ILE   A 1 107 ? 17.501 -0.338  15.999 1.00 15.49 ? 113 ILE   A CB  1 
ATOM   846  C  CG1 . ILE   A 1 107 ? 18.637 0.660   15.780 1.00 17.59 ? 113 ILE   A CG1 1 
ATOM   847  C  CG2 . ILE   A 1 107 ? 17.185 -1.039  14.664 1.00 18.28 ? 113 ILE   A CG2 1 
ATOM   848  C  CD1 . ILE   A 1 107 ? 20.079 -0.107  15.415 1.00 20.64 ? 113 ILE   A CD1 1 
ATOM   849  N  N   . LEU   A 1 108 ? 14.248 0.007   15.253 1.00 13.93 ? 114 LEU   A N   1 
ATOM   850  C  CA  . LEU   A 1 108 ? 13.085 -0.733  14.730 1.00 14.03 ? 114 LEU   A CA  1 
ATOM   851  C  C   . LEU   A 1 108 ? 13.616 -1.497  13.512 1.00 14.89 ? 114 LEU   A C   1 
ATOM   852  O  O   . LEU   A 1 108 ? 14.239 -0.885  12.616 1.00 14.55 ? 114 LEU   A O   1 
ATOM   853  C  CB  . LEU   A 1 108 ? 12.001 0.299   14.320 1.00 13.70 ? 114 LEU   A CB  1 
ATOM   854  C  CG  . LEU   A 1 108 ? 10.849 -0.307  13.533 1.00 14.81 ? 114 LEU   A CG  1 
ATOM   855  C  CD1 . LEU   A 1 108 ? 9.996  -1.266  14.406 1.00 16.19 ? 114 LEU   A CD1 1 
ATOM   856  C  CD2 . LEU   A 1 108 ? 9.945  0.828   12.943 1.00 16.08 ? 114 LEU   A CD2 1 
ATOM   857  N  N   . ARG   A 1 109 ? 13.428 -2.846  13.518 1.00 15.60 ? 115 ARG   A N   1 
ATOM   858  C  CA  . ARG   A 1 109 ? 13.928 -3.742  12.462 1.00 16.99 ? 115 ARG   A CA  1 
ATOM   859  C  C   . ARG   A 1 109 ? 12.795 -4.568  11.921 1.00 17.44 ? 115 ARG   A C   1 
ATOM   860  O  O   . ARG   A 1 109 ? 11.889 -4.982  12.642 1.00 18.06 ? 115 ARG   A O   1 
ATOM   861  C  CB  . ARG   A 1 109 ? 14.954 -4.724  13.092 1.00 19.97 ? 115 ARG   A CB  1 
ATOM   862  C  CG  . ARG   A 1 109 ? 16.185 -4.098  13.728 1.00 26.03 ? 115 ARG   A CG  1 
ATOM   863  C  CD  . ARG   A 1 109 ? 17.170 -5.180  14.165 1.00 28.80 ? 115 ARG   A CD  1 
ATOM   864  N  NE  . ARG   A 1 109 ? 17.964 -5.586  13.012 1.00 33.37 ? 115 ARG   A NE  1 
ATOM   865  C  CZ  . ARG   A 1 109 ? 19.131 -5.046  12.678 1.00 33.86 ? 115 ARG   A CZ  1 
ATOM   866  N  NH1 . ARG   A 1 109 ? 19.711 -4.157  13.471 1.00 29.90 ? 115 ARG   A NH1 1 
ATOM   867  N  NH2 . ARG   A 1 109 ? 19.747 -5.426  11.577 1.00 35.17 ? 115 ARG   A NH2 1 
ATOM   868  N  N   . CYS   A 1 110 ? 12.882 -4.880  10.641 1.00 17.48 ? 116 CYS   A N   1 
ATOM   869  C  CA  . CYS   A 1 110 ? 12.015 -5.882  10.001 1.00 18.41 ? 116 CYS   A CA  1 
ATOM   870  C  C   . CYS   A 1 110 ? 12.945 -7.010  9.422  1.00 19.89 ? 116 CYS   A C   1 
ATOM   871  O  O   . CYS   A 1 110 ? 14.168 -6.980  9.625  1.00 20.50 ? 116 CYS   A O   1 
ATOM   872  C  CB  . CYS   A 1 110 ? 11.194 -5.223  8.898  1.00 18.73 ? 116 CYS   A CB  1 
ATOM   873  S  SG  . CYS   A 1 110 ? 12.198 -4.629  7.484  1.00 18.81 ? 116 CYS   A SG  1 
ATOM   874  N  N   . GLN   A 1 111 ? 12.367 -8.007  8.688  1.00 22.22 ? 117 GLN   A N   1 
ATOM   875  C  CA  . GLN   A 1 111 ? 13.197 -9.065  8.098  1.00 23.60 ? 117 GLN   A CA  1 
ATOM   876  C  C   . GLN   A 1 111 ? 14.225 -8.558  7.073  1.00 24.18 ? 117 GLN   A C   1 
ATOM   877  O  O   . GLN   A 1 111 ? 15.198 -9.257  6.770  1.00 25.25 ? 117 GLN   A O   1 
ATOM   878  C  CB  . GLN   A 1 111 ? 12.306 -10.132 7.430  1.00 26.16 ? 117 GLN   A CB  1 
ATOM   879  C  CG  . GLN   A 1 111 ? 11.510 -9.537  6.266  1.00 31.68 ? 117 GLN   A CG  1 
ATOM   880  C  CD  . GLN   A 1 111 ? 10.565 -10.519 5.615  1.00 40.89 ? 117 GLN   A CD  1 
ATOM   881  O  OE1 . GLN   A 1 111 ? 9.346  -10.304 5.573  1.00 43.83 ? 117 GLN   A OE1 1 
ATOM   882  N  NE2 . GLN   A 1 111 ? 11.122 -11.585 5.068  1.00 41.69 ? 117 GLN   A NE2 1 
ATOM   883  N  N   . HIS   A 1 112 ? 14.065 -7.321  6.586  1.00 21.98 ? 118 HIS   A N   1 
ATOM   884  C  CA  . HIS   A 1 112 ? 14.958 -6.740  5.591  1.00 21.40 ? 118 HIS   A CA  1 
ATOM   885  C  C   . HIS   A 1 112 ? 16.096 -5.878  6.191  1.00 21.07 ? 118 HIS   A C   1 
ATOM   886  O  O   . HIS   A 1 112 ? 17.002 -5.432  5.461  1.00 22.28 ? 118 HIS   A O   1 
ATOM   887  C  CB  . HIS   A 1 112 ? 14.136 -5.920  4.562  1.00 21.86 ? 118 HIS   A CB  1 
ATOM   888  C  CG  . HIS   A 1 112 ? 12.993 -6.679  3.962  1.00 23.31 ? 118 HIS   A CG  1 
ATOM   889  N  ND1 . HIS   A 1 112 ? 11.680 -6.412  4.295  1.00 23.99 ? 118 HIS   A ND1 1 
ATOM   890  C  CD2 . HIS   A 1 112 ? 13.007 -7.622  2.985  1.00 25.47 ? 118 HIS   A CD2 1 
ATOM   891  C  CE1 . HIS   A 1 112 ? 10.939 -7.247  3.580  1.00 26.73 ? 118 HIS   A CE1 1 
ATOM   892  N  NE2 . HIS   A 1 112 ? 11.694 -7.993  2.772  1.00 26.87 ? 118 HIS   A NE2 1 
ATOM   893  N  N   . GLY   A 1 113 ? 16.057 -5.640  7.515  1.00 19.52 ? 119 GLY   A N   1 
ATOM   894  C  CA  . GLY   A 1 113 ? 17.103 -4.824  8.129  1.00 19.08 ? 119 GLY   A CA  1 
ATOM   895  C  C   . GLY   A 1 113 ? 16.543 -3.691  8.964  1.00 17.29 ? 119 GLY   A C   1 
ATOM   896  O  O   . GLY   A 1 113 ? 15.407 -3.765  9.430  1.00 18.95 ? 119 GLY   A O   1 
ATOM   897  N  N   . VAL   A 1 114 ? 17.327 -2.649  9.133  1.00 16.40 ? 120 VAL   A N   1 
ATOM   898  C  CA  . VAL   A 1 114 ? 16.938 -1.498  9.965  1.00 16.57 ? 120 VAL   A CA  1 
ATOM   899  C  C   . VAL   A 1 114 ? 15.947 -0.626  9.253  1.00 16.10 ? 120 VAL   A C   1 
ATOM   900  O  O   . VAL   A 1 114 ? 16.220 -0.205  8.114  1.00 17.09 ? 120 VAL   A O   1 
ATOM   901  C  CB  . VAL   A 1 114 ? 18.180 -0.688  10.317 1.00 17.67 ? 120 VAL   A CB  1 
ATOM   902  C  CG1 . VAL   A 1 114 ? 17.809 0.566   11.096 1.00 17.50 ? 120 VAL   A CG1 1 
ATOM   903  C  CG2 . VAL   A 1 114 ? 19.167 -1.542  11.108 1.00 19.41 ? 120 VAL   A CG2 1 
ATOM   904  N  N   . VAL   A 1 115 ? 14.824 -0.327  9.920  1.00 15.07 ? 121 VAL   A N   1 
ATOM   905  C  CA  . VAL   A 1 115 ? 13.753 0.529   9.379  1.00 15.26 ? 121 VAL   A CA  1 
ATOM   906  C  C   . VAL   A 1 115 ? 13.903 1.962   9.890  1.00 14.94 ? 121 VAL   A C   1 
ATOM   907  O  O   . VAL   A 1 115 ? 13.743 2.913   9.151  1.00 15.65 ? 121 VAL   A O   1 
ATOM   908  C  CB  . VAL   A 1 115 ? 12.395 -0.042  9.816  1.00 16.35 ? 121 VAL   A CB  1 
ATOM   909  C  CG1 . VAL   A 1 115 ? 11.254 0.838   9.350  1.00 17.51 ? 121 VAL   A CG1 1 
ATOM   910  C  CG2 . VAL   A 1 115 ? 12.237 -1.458  9.288  1.00 17.39 ? 121 VAL   A CG2 1 
ATOM   911  N  N   . GLY   A 1 116 ? 14.214 2.109   11.188 1.00 14.34 ? 122 GLY   A N   1 
ATOM   912  C  CA  . GLY   A 1 116 ? 14.339 3.456   11.749 1.00 15.07 ? 122 GLY   A CA  1 
ATOM   913  C  C   . GLY   A 1 116 ? 14.741 3.433   13.207 1.00 14.70 ? 122 GLY   A C   1 
ATOM   914  O  O   . GLY   A 1 116 ? 15.119 2.371   13.732 1.00 15.31 ? 122 GLY   A O   1 
ATOM   915  N  N   . ILE   A 1 117 ? 14.669 4.614   13.851 1.00 14.78 ? 123 ILE   A N   1 
ATOM   916  C  CA  . ILE   A 1 117 ? 15.048 4.690   15.249 1.00 14.45 ? 123 ILE   A CA  1 
ATOM   917  C  C   . ILE   A 1 117 ? 13.981 5.408   16.055 1.00 14.43 ? 123 ILE   A C   1 
ATOM   918  O  O   . ILE   A 1 117 ? 13.330 6.359   15.553 1.00 14.82 ? 123 ILE   A O   1 
ATOM   919  C  CB  . ILE   A 1 117 ? 16.425 5.361   15.472 1.00 15.61 ? 123 ILE   A CB  1 
ATOM   920  C  CG1 . ILE   A 1 117 ? 16.479 6.760   14.819 1.00 17.23 ? 123 ILE   A CG1 1 
ATOM   921  C  CG2 . ILE   A 1 117 ? 17.589 4.424   15.057 1.00 18.13 ? 123 ILE   A CG2 1 
ATOM   922  C  CD1 . ILE   A 1 117 ? 17.867 7.496   15.225 1.00 19.42 ? 123 ILE   A CD1 1 
ATOM   923  N  N   . VAL   A 1 118 ? 13.822 5.017   17.348 1.00 13.36 ? 124 VAL   A N   1 
ATOM   924  C  CA  . VAL   A 1 118 ? 12.853 5.725   18.208 1.00 13.82 ? 124 VAL   A CA  1 
ATOM   925  C  C   . VAL   A 1 118 ? 13.207 7.215   18.286 1.00 14.93 ? 124 VAL   A C   1 
ATOM   926  O  O   . VAL   A 1 118 ? 14.369 7.556   18.485 1.00 15.22 ? 124 VAL   A O   1 
ATOM   927  C  CB  . VAL   A 1 118 ? 12.827 5.147   19.648 1.00 15.00 ? 124 VAL   A CB  1 
ATOM   928  C  CG1 . VAL   A 1 118 ? 11.910 5.984   20.551 1.00 17.08 ? 124 VAL   A CG1 1 
ATOM   929  C  CG2 . VAL   A 1 118 ? 12.414 3.664   19.662 1.00 15.77 ? 124 VAL   A CG2 1 
ATOM   930  N  N   . SER   A 1 119 ? 12.201 8.085   18.103 1.00 14.64 ? 125 SER   A N   1 
ATOM   931  C  CA  . SER   A 1 119 ? 12.366 9.519   18.092 1.00 15.15 ? 125 SER   A CA  1 
ATOM   932  C  C   . SER   A 1 119 ? 11.328 10.261  18.919 1.00 17.57 ? 125 SER   A C   1 
ATOM   933  O  O   . SER   A 1 119 ? 11.640 11.348  19.461 1.00 18.36 ? 125 SER   A O   1 
ATOM   934  C  CB  . SER   A 1 119 ? 12.344 9.986   16.645 1.00 16.41 ? 125 SER   A CB  1 
ATOM   935  O  OG  . SER   A 1 119 ? 12.430 11.408  16.558 1.00 17.75 ? 125 SER   A OG  1 
ATOM   936  N  N   . THR   A 1 120 ? 10.103 9.724   19.018 1.00 17.72 ? 126 THR   A N   1 
ATOM   937  C  CA  . THR   A 1 120 ? 9.044  10.434  19.776 1.00 18.34 ? 126 THR   A CA  1 
ATOM   938  C  C   . THR   A 1 120 ? 8.280  9.503   20.711 1.00 18.83 ? 126 THR   A C   1 
ATOM   939  O  O   . THR   A 1 120 ? 8.346  8.256   20.578 1.00 17.97 ? 126 THR   A O   1 
ATOM   940  C  CB  . THR   A 1 120 ? 8.066  11.173  18.823 1.00 19.75 ? 126 THR   A CB  1 
ATOM   941  O  OG1 . THR   A 1 120 ? 7.220  10.198  18.186 1.00 20.86 ? 126 THR   A OG1 1 
ATOM   942  C  CG2 . THR   A 1 120 ? 8.755  12.041  17.806 1.00 19.45 ? 126 THR   A CG2 1 
ATOM   943  N  N   . GLY   A 1 121 ? 7.530  10.105  21.638 1.00 20.71 ? 127 GLY   A N   1 
ATOM   944  C  CA  . GLY   A 1 121 ? 6.667  9.342   22.523 1.00 24.13 ? 127 GLY   A CA  1 
ATOM   945  C  C   . GLY   A 1 121 ? 5.618  10.245  23.151 1.00 27.20 ? 127 GLY   A C   1 
ATOM   946  O  O   . GLY   A 1 121 ? 5.677  11.474  23.054 1.00 29.36 ? 127 GLY   A O   1 
ATOM   947  N  N   . GLY   A 1 122 ? 4.731  9.635   23.882 1.00 28.97 ? 128 GLY   A N   1 
ATOM   948  C  CA  . GLY   A 1 122 ? 3.634  10.338  24.546 1.00 29.88 ? 128 GLY   A CA  1 
ATOM   949  C  C   . GLY   A 1 122 ? 2.318  9.685   24.183 1.00 30.59 ? 128 GLY   A C   1 
ATOM   950  O  O   . GLY   A 1 122 ? 2.180  9.104   23.094 1.00 30.31 ? 128 GLY   A O   1 
ATOM   951  N  N   . ASN   A 1 123 ? 1.335  9.758   25.105 1.00 30.14 ? 129 ASN   A N   1 
ATOM   952  C  CA  . ASN   A 1 123 ? -0.003 9.203   24.894 1.00 31.00 ? 129 ASN   A CA  1 
ATOM   953  C  C   . ASN   A 1 123 ? -0.027 7.731   24.482 1.00 30.01 ? 129 ASN   A C   1 
ATOM   954  O  O   . ASN   A 1 123 ? -0.944 7.317   23.768 1.00 31.05 ? 129 ASN   A O   1 
ATOM   955  C  CB  . ASN   A 1 123 ? -0.757 10.058  23.884 1.00 33.79 ? 129 ASN   A CB  1 
ATOM   956  C  CG  . ASN   A 1 123 ? -0.978 11.461  24.400 1.00 41.35 ? 129 ASN   A CG  1 
ATOM   957  O  OD1 . ASN   A 1 123 ? -1.104 11.681  25.606 1.00 44.80 ? 129 ASN   A OD1 1 
ATOM   958  N  ND2 . ASN   A 1 123 ? -1.049 12.429  23.508 1.00 43.16 ? 129 ASN   A ND2 1 
ATOM   959  N  N   . GLY   A 1 124 ? 0.936  6.943   24.957 1.00 27.91 ? 130 GLY   A N   1 
ATOM   960  C  CA  . GLY   A 1 124 ? 0.965  5.526   24.647 1.00 26.10 ? 130 GLY   A CA  1 
ATOM   961  C  C   . GLY   A 1 124 ? 1.333  5.189   23.207 1.00 23.42 ? 130 GLY   A C   1 
ATOM   962  O  O   . GLY   A 1 124 ? 1.041  4.084   22.742 1.00 21.78 ? 130 GLY   A O   1 
ATOM   963  N  N   . LEU   A 1 125 ? 1.927  6.141   22.490 1.00 20.89 ? 131 LEU   A N   1 
ATOM   964  C  CA  . LEU   A 1 125 ? 2.367  5.936   21.124 1.00 20.43 ? 131 LEU   A CA  1 
ATOM   965  C  C   . LEU   A 1 125 ? 3.907  6.068   21.109 1.00 21.32 ? 131 LEU   A C   1 
ATOM   966  O  O   . LEU   A 1 125 ? 4.490  6.792   21.933 1.00 24.73 ? 131 LEU   A O   1 
ATOM   967  C  CB  . LEU   A 1 125 ? 1.771  6.997   20.193 1.00 22.36 ? 131 LEU   A CB  1 
ATOM   968  C  CG  . LEU   A 1 125 ? 0.231  6.995   20.114 1.00 23.75 ? 131 LEU   A CG  1 
ATOM   969  C  CD1 . LEU   A 1 125 ? -0.283 8.313   19.580 1.00 26.99 ? 131 LEU   A CD1 1 
ATOM   970  C  CD2 . LEU   A 1 125 ? -0.262 5.801   19.292 1.00 23.20 ? 131 LEU   A CD2 1 
ATOM   971  N  N   . VAL   A 1 126 ? 4.532  5.347   20.222 1.00 16.90 ? 132 VAL   A N   1 
ATOM   972  C  CA  . VAL   A 1 126 ? 5.978  5.474   20.021 1.00 16.40 ? 132 VAL   A CA  1 
ATOM   973  C  C   . VAL   A 1 126 ? 6.174  5.868   18.563 1.00 16.29 ? 132 VAL   A C   1 
ATOM   974  O  O   . VAL   A 1 126 ? 5.497  5.322   17.668 1.00 16.81 ? 132 VAL   A O   1 
ATOM   975  C  CB  . VAL   A 1 126 ? 6.746  4.170   20.377 1.00 17.45 ? 132 VAL   A CB  1 
ATOM   976  C  CG1 . VAL   A 1 126 ? 6.142  2.943   19.719 1.00 18.53 ? 132 VAL   A CG1 1 
ATOM   977  C  CG2 . VAL   A 1 126 ? 8.245  4.277   20.056 1.00 17.94 ? 132 VAL   A CG2 1 
ATOM   978  N  N   . GLY   A 1 127 ? 7.024  6.876   18.329 1.00 15.00 ? 133 GLY   A N   1 
ATOM   979  C  CA  . GLY   A 1 127 ? 7.283  7.289   16.957 1.00 15.38 ? 133 GLY   A CA  1 
ATOM   980  C  C   . GLY   A 1 127 ? 8.723  7.025   16.543 1.00 14.77 ? 133 GLY   A C   1 
ATOM   981  O  O   . GLY   A 1 127 ? 9.646  7.142   17.346 1.00 15.55 ? 133 GLY   A O   1 
ATOM   982  N  N   . PHE   A 1 128 ? 8.885  6.562   15.301 1.00 13.66 ? 134 PHE   A N   1 
ATOM   983  C  CA  . PHE   A 1 128 ? 10.208 6.187   14.769 1.00 14.29 ? 134 PHE   A CA  1 
ATOM   984  C  C   . PHE   A 1 128 ? 10.546 7.062   13.547 1.00 14.40 ? 134 PHE   A C   1 
ATOM   985  O  O   . PHE   A 1 128 ? 9.722  7.206   12.614 1.00 15.28 ? 134 PHE   A O   1 
ATOM   986  C  CB  . PHE   A 1 128 ? 10.163 4.709   14.258 1.00 14.48 ? 134 PHE   A CB  1 
ATOM   987  C  CG  . PHE   A 1 128 ? 9.638  3.731   15.274 1.00 14.04 ? 134 PHE   A CG  1 
ATOM   988  C  CD1 . PHE   A 1 128 ? 10.484 3.165   16.228 1.00 14.64 ? 134 PHE   A CD1 1 
ATOM   989  C  CD2 . PHE   A 1 128 ? 8.293  3.370   15.283 1.00 15.51 ? 134 PHE   A CD2 1 
ATOM   990  C  CE1 . PHE   A 1 128 ? 9.983  2.255   17.157 1.00 15.43 ? 134 PHE   A CE1 1 
ATOM   991  C  CE2 . PHE   A 1 128 ? 7.823  2.411   16.156 1.00 16.51 ? 134 PHE   A CE2 1 
ATOM   992  C  CZ  . PHE   A 1 128 ? 8.658  1.893   17.128 1.00 15.47 ? 134 PHE   A CZ  1 
ATOM   993  N  N   . ALA   A 1 129 ? 11.786 7.552   13.542 1.00 14.40 ? 135 ALA   A N   1 
ATOM   994  C  CA  . ALA   A 1 129 ? 12.270 8.294   12.390 1.00 14.82 ? 135 ALA   A CA  1 
ATOM   995  C  C   . ALA   A 1 129 ? 12.693 7.251   11.328 1.00 15.68 ? 135 ALA   A C   1 
ATOM   996  O  O   . ALA   A 1 129 ? 13.610 6.455   11.559 1.00 16.27 ? 135 ALA   A O   1 
ATOM   997  C  CB  . ALA   A 1 129 ? 13.476 9.181   12.790 1.00 15.34 ? 135 ALA   A CB  1 
ATOM   998  N  N   . ASP   A 1 130 ? 12.065 7.289   10.134 1.00 15.44 ? 136 ASP   A N   1 
ATOM   999  C  CA  . ASP   A 1 130 ? 12.384 6.347   9.069  1.00 15.64 ? 136 ASP   A CA  1 
ATOM   1000 C  C   . ASP   A 1 130 ? 13.750 6.670   8.497  1.00 16.73 ? 136 ASP   A C   1 
ATOM   1001 O  O   . ASP   A 1 130 ? 14.097 7.848   8.347  1.00 17.13 ? 136 ASP   A O   1 
ATOM   1002 C  CB  . ASP   A 1 130 ? 11.341 6.469   7.928  1.00 17.52 ? 136 ASP   A CB  1 
ATOM   1003 C  CG  . ASP   A 1 130 ? 11.558 5.464   6.807  1.00 20.82 ? 136 ASP   A CG  1 
ATOM   1004 O  OD1 . ASP   A 1 130 ? 11.662 4.285   7.096  1.00 20.92 ? 136 ASP   A OD1 1 
ATOM   1005 O  OD2 . ASP   A 1 130 ? 11.646 5.889   5.633  1.00 25.31 ? 136 ASP   A OD2 1 
ATOM   1006 N  N   . VAL   A 1 131 ? 14.514 5.620   8.078  1.00 15.90 ? 137 VAL   A N   1 
ATOM   1007 C  CA  . VAL   A 1 131 ? 15.786 5.818   7.370  1.00 16.38 ? 137 VAL   A CA  1 
ATOM   1008 C  C   . VAL   A 1 131 ? 15.814 5.070   6.007  1.00 17.61 ? 137 VAL   A C   1 
ATOM   1009 O  O   . VAL   A 1 131 ? 16.805 5.116   5.292  1.00 17.84 ? 137 VAL   A O   1 
ATOM   1010 C  CB  . VAL   A 1 131 ? 17.000 5.364   8.220  1.00 17.55 ? 137 VAL   A CB  1 
ATOM   1011 C  CG1 . VAL   A 1 131 ? 17.145 6.208   9.505  1.00 18.05 ? 137 VAL   A CG1 1 
ATOM   1012 C  CG2 . VAL   A 1 131 ? 16.922 3.873   8.523  1.00 17.96 ? 137 VAL   A CG2 1 
ATOM   1013 N  N   . ARG   A 1 132 ? 14.739 4.333   5.667  1.00 17.28 ? 138 ARG   A N   1 
ATOM   1014 C  CA  . ARG   A 1 132 ? 14.711 3.521   4.451  1.00 16.97 ? 138 ARG   A CA  1 
ATOM   1015 C  C   . ARG   A 1 132 ? 14.798 4.310   3.177  1.00 19.71 ? 138 ARG   A C   1 
ATOM   1016 O  O   . ARG   A 1 132 ? 15.157 3.717   2.149  1.00 21.21 ? 138 ARG   A O   1 
ATOM   1017 C  CB  . ARG   A 1 132 ? 13.438 2.671   4.438  1.00 16.92 ? 138 ARG   A CB  1 
ATOM   1018 C  CG  . ARG   A 1 132 ? 13.398 1.638   5.583  1.00 16.79 ? 138 ARG   A CG  1 
ATOM   1019 C  CD  . ARG   A 1 132 ? 12.112 0.850   5.538  1.00 17.95 ? 138 ARG   A CD  1 
ATOM   1020 N  NE  . ARG   A 1 132 ? 11.004 1.736   5.884  1.00 16.88 ? 138 ARG   A NE  1 
ATOM   1021 C  CZ  . ARG   A 1 132 ? 9.756  1.336   6.061  1.00 18.92 ? 138 ARG   A CZ  1 
ATOM   1022 N  NH1 . ARG   A 1 132 ? 9.405  0.078   5.776  1.00 18.89 ? 138 ARG   A NH1 1 
ATOM   1023 N  NH2 . ARG   A 1 132 ? 8.837  2.188   6.523  1.00 19.58 ? 138 ARG   A NH2 1 
ATOM   1024 N  N   . ASP   A 1 133 ? 14.420 5.590   3.201  1.00 18.91 ? 139 ASP   A N   1 
ATOM   1025 C  CA  . ASP   A 1 133 ? 14.490 6.380   1.972  1.00 19.93 ? 139 ASP   A CA  1 
ATOM   1026 C  C   . ASP   A 1 133 ? 15.922 6.923   1.710  1.00 21.65 ? 139 ASP   A C   1 
ATOM   1027 O  O   . ASP   A 1 133 ? 16.186 7.481   0.632  1.00 23.78 ? 139 ASP   A O   1 
ATOM   1028 C  CB  . ASP   A 1 133 ? 13.505 7.561   2.055  1.00 22.23 ? 139 ASP   A CB  1 
ATOM   1029 C  CG  . ASP   A 1 133 ? 13.856 8.558   3.146  1.00 25.81 ? 139 ASP   A CG  1 
ATOM   1030 O  OD1 . ASP   A 1 133 ? 14.190 8.116   4.276  1.00 24.64 ? 139 ASP   A OD1 1 
ATOM   1031 O  OD2 . ASP   A 1 133 ? 13.815 9.793   2.872  1.00 27.22 ? 139 ASP   A OD2 1 
ATOM   1032 N  N   . LEU   A 1 134 ? 16.842 6.810   2.691  1.00 20.21 ? 140 LEU   A N   1 
ATOM   1033 C  CA  . LEU   A 1 134 ? 18.192 7.396   2.536  1.00 20.42 ? 140 LEU   A CA  1 
ATOM   1034 C  C   . LEU   A 1 134 ? 19.059 6.397   1.803  1.00 20.34 ? 140 LEU   A C   1 
ATOM   1035 O  O   . LEU   A 1 134 ? 19.850 5.654   2.409  1.00 19.51 ? 140 LEU   A O   1 
ATOM   1036 C  CB  . LEU   A 1 134 ? 18.747 7.719   3.927  1.00 20.13 ? 140 LEU   A CB  1 
ATOM   1037 C  CG  . LEU   A 1 134 ? 17.872 8.695   4.730  1.00 21.34 ? 140 LEU   A CG  1 
ATOM   1038 C  CD1 . LEU   A 1 134 ? 18.437 8.862   6.173  1.00 21.83 ? 140 LEU   A CD1 1 
ATOM   1039 C  CD2 . LEU   A 1 134 ? 17.774 10.077  4.027  1.00 23.02 ? 140 LEU   A CD2 1 
ATOM   1040 N  N   . LEU   A 1 135 ? 18.872 6.318   0.468  1.00 20.15 ? 141 LEU   A N   1 
ATOM   1041 C  CA  . LEU   A 1 135 ? 19.559 5.270   -0.299 1.00 21.25 ? 141 LEU   A CA  1 
ATOM   1042 C  C   . LEU   A 1 135 ? 21.061 5.426   -0.308 1.00 24.05 ? 141 LEU   A C   1 
ATOM   1043 O  O   . LEU   A 1 135 ? 21.773 4.419   -0.401 1.00 25.75 ? 141 LEU   A O   1 
ATOM   1044 C  CB  . LEU   A 1 135 ? 19.043 5.133   -1.761 1.00 22.31 ? 141 LEU   A CB  1 
ATOM   1045 C  CG  . LEU   A 1 135 ? 17.529 5.122   -1.935 1.00 24.50 ? 141 LEU   A CG  1 
ATOM   1046 C  CD1 . LEU   A 1 135 ? 17.192 4.893   -3.416 1.00 26.15 ? 141 LEU   A CD1 1 
ATOM   1047 C  CD2 . LEU   A 1 135 ? 16.814 4.049   -1.058 1.00 25.32 ? 141 LEU   A CD2 1 
ATOM   1048 N  N   . TRP   A 1 136 ? 21.548 6.679   -0.158 1.00 23.55 ? 142 TRP   A N   1 
ATOM   1049 C  CA  . TRP   A 1 136 ? 22.976 6.950   -0.161 1.00 24.04 ? 142 TRP   A CA  1 
ATOM   1050 C  C   . TRP   A 1 136 ? 23.723 6.322   1.013  1.00 24.59 ? 142 TRP   A C   1 
ATOM   1051 O  O   . TRP   A 1 136 ? 24.941 6.187   0.950  1.00 26.08 ? 142 TRP   A O   1 
ATOM   1052 C  CB  . TRP   A 1 136 ? 23.250 8.466   -0.250 1.00 23.92 ? 142 TRP   A CB  1 
ATOM   1053 C  CG  . TRP   A 1 136 ? 22.541 9.285   0.788  1.00 23.83 ? 142 TRP   A CG  1 
ATOM   1054 C  CD1 . TRP   A 1 136 ? 21.297 9.850   0.696  1.00 24.16 ? 142 TRP   A CD1 1 
ATOM   1055 C  CD2 . TRP   A 1 136 ? 23.003 9.540   2.132  1.00 23.50 ? 142 TRP   A CD2 1 
ATOM   1056 N  NE1 . TRP   A 1 136 ? 20.991 10.502  1.869  1.00 24.42 ? 142 TRP   A NE1 1 
ATOM   1057 C  CE2 . TRP   A 1 136 ? 22.057 10.384  2.743  1.00 23.90 ? 142 TRP   A CE2 1 
ATOM   1058 C  CE3 . TRP   A 1 136 ? 24.199 9.247   2.819  1.00 24.30 ? 142 TRP   A CE3 1 
ATOM   1059 C  CZ2 . TRP   A 1 136 ? 22.209 10.841  4.058  1.00 25.04 ? 142 TRP   A CZ2 1 
ATOM   1060 C  CZ3 . TRP   A 1 136 ? 24.362 9.724   4.107  1.00 25.22 ? 142 TRP   A CZ3 1 
ATOM   1061 C  CH2 . TRP   A 1 136 ? 23.386 10.527  4.706  1.00 24.63 ? 142 TRP   A CH2 1 
ATOM   1062 N  N   . LEU   A 1 137 ? 23.018 5.926   2.105  1.00 24.37 ? 143 LEU   A N   1 
ATOM   1063 C  CA  . LEU   A 1 137 ? 23.674 5.315   3.256  1.00 27.19 ? 143 LEU   A CA  1 
ATOM   1064 C  C   . LEU   A 1 137 ? 24.433 4.029   2.890  1.00 33.22 ? 143 LEU   A C   1 
ATOM   1065 O  O   . LEU   A 1 137 ? 25.377 3.670   3.601  1.00 34.35 ? 143 LEU   A O   1 
ATOM   1066 C  CB  . LEU   A 1 137 ? 22.611 4.985   4.315  1.00 25.59 ? 143 LEU   A CB  1 
ATOM   1067 C  CG  . LEU   A 1 137 ? 22.089 6.128   5.147  1.00 24.85 ? 143 LEU   A CG  1 
ATOM   1068 C  CD1 . LEU   A 1 137 ? 21.019 5.622   6.126  1.00 25.19 ? 143 LEU   A CD1 1 
ATOM   1069 C  CD2 . LEU   A 1 137 ? 23.231 6.789   5.956  1.00 26.17 ? 143 LEU   A CD2 1 
ATOM   1070 N  N   . ASP   A 1 138 ? 24.014 3.329   1.808  1.00 36.05 ? 144 ASP   A N   1 
ATOM   1071 C  CA  . ASP   A 1 138 ? 24.648 2.080   1.361  1.00 40.85 ? 144 ASP   A CA  1 
ATOM   1072 C  C   . ASP   A 1 138 ? 25.586 2.234   0.161  1.00 44.14 ? 144 ASP   A C   1 
ATOM   1073 O  O   . ASP   A 1 138 ? 25.930 1.225   -0.462 1.00 44.90 ? 144 ASP   A O   1 
ATOM   1074 C  CB  . ASP   A 1 138 ? 23.600 1.046   0.972  1.00 44.05 ? 144 ASP   A CB  1 
ATOM   1075 C  CG  . ASP   A 1 138 ? 22.552 0.770   2.000  1.00 52.12 ? 144 ASP   A CG  1 
ATOM   1076 O  OD1 . ASP   A 1 138 ? 22.802 1.041   3.198  1.00 54.23 ? 144 ASP   A OD1 1 
ATOM   1077 O  OD2 . ASP   A 1 138 ? 21.484 0.268   1.623  1.00 55.65 ? 144 ASP   A OD2 1 
ATOM   1078 N  N   . GLU   A 1 139 ? 25.981 3.462   -0.192 1.00 45.70 ? 145 GLU   A N   1 
ATOM   1079 C  CA  . GLU   A 1 139 ? 26.919 3.681   -1.293 1.00 47.72 ? 145 GLU   A CA  1 
ATOM   1080 C  C   . GLU   A 1 139 ? 28.037 4.619   -0.841 1.00 48.91 ? 145 GLU   A C   1 
ATOM   1081 O  O   . GLU   A 1 139 ? 28.786 5.145   -1.667 1.00 49.79 ? 145 GLU   A O   1 
ATOM   1082 C  CB  . GLU   A 1 139 ? 26.202 4.228   -2.541 1.00 50.76 ? 145 GLU   A CB  1 
ATOM   1083 C  CG  . GLU   A 1 139 ? 25.554 5.581   -2.332 1.00 56.09 ? 145 GLU   A CG  1 
ATOM   1084 C  CD  . GLU   A 1 139 ? 24.588 5.991   -3.424 1.00 63.62 ? 145 GLU   A CD  1 
ATOM   1085 O  OE1 . GLU   A 1 139 ? 24.448 7.212   -3.668 1.00 64.74 ? 145 GLU   A OE1 1 
ATOM   1086 O  OE2 . GLU   A 1 139 ? 23.967 5.092   -4.034 1.00 66.88 ? 145 GLU   A OE2 1 
HETATM 1087 N  N1  . A1BTF B 2 .   ? 11.675 14.090  18.112 1.00 23.36 ? 201 A1BTF A N1  1 
HETATM 1088 C  C4  . A1BTF B 2 .   ? 8.202  11.559  25.849 1.00 32.53 ? 201 A1BTF A C4  1 
HETATM 1089 C  C5  . A1BTF B 2 .   ? 8.994  12.337  25.019 1.00 32.27 ? 201 A1BTF A C5  1 
HETATM 1090 C  C6  . A1BTF B 2 .   ? 9.859  11.724  24.111 1.00 31.13 ? 201 A1BTF A C6  1 
HETATM 1091 C  C7  . A1BTF B 2 .   ? 11.887 12.944  23.385 1.00 29.82 ? 201 A1BTF A C7  1 
HETATM 1092 C  C8  . A1BTF B 2 .   ? 12.405 13.958  22.412 1.00 27.58 ? 201 A1BTF A C8  1 
HETATM 1093 C  C10 . A1BTF B 2 .   ? 13.863 15.823  21.983 1.00 25.49 ? 201 A1BTF A C10 1 
HETATM 1094 C  C13 . A1BTF B 2 .   ? 12.415 15.042  20.229 1.00 25.09 ? 201 A1BTF A C13 1 
HETATM 1095 C  C15 . A1BTF B 2 .   ? 11.935 14.053  21.103 1.00 26.43 ? 201 A1BTF A C15 1 
HETATM 1096 O  O1  . A1BTF B 2 .   ? 11.431 16.315  18.461 1.00 26.44 ? 201 A1BTF A O1  1 
HETATM 1097 C  C14 . A1BTF B 2 .   ? 11.814 15.183  18.860 1.00 25.45 ? 201 A1BTF A C14 1 
HETATM 1098 C  C11 . A1BTF B 2 .   ? 13.413 15.938  20.667 1.00 25.24 ? 201 A1BTF A C11 1 
HETATM 1099 C  C12 . A1BTF B 2 .   ? 14.010 16.991  19.769 1.00 25.09 ? 201 A1BTF A C12 1 
HETATM 1100 C  C9  . A1BTF B 2 .   ? 13.373 14.858  22.842 1.00 27.06 ? 201 A1BTF A C9  1 
HETATM 1101 O  O   . A1BTF B 2 .   ? 12.586 12.549  24.312 1.00 30.44 ? 201 A1BTF A O   1 
HETATM 1102 N  N   . A1BTF B 2 .   ? 10.605 12.537  23.213 1.00 30.63 ? 201 A1BTF A N   1 
HETATM 1103 C  C1  . A1BTF B 2 .   ? 9.938  10.321  24.031 1.00 31.23 ? 201 A1BTF A C1  1 
HETATM 1104 C  C   . A1BTF B 2 .   ? 10.871 9.616   23.080 1.00 30.87 ? 201 A1BTF A C   1 
HETATM 1105 C  C3  . A1BTF B 2 .   ? 8.267  10.188  25.779 1.00 32.00 ? 201 A1BTF A C3  1 
HETATM 1106 C  C2  . A1BTF B 2 .   ? 9.118  9.577   24.877 1.00 31.47 ? 201 A1BTF A C2  1 
HETATM 1107 ZN ZN  . ZN    C 3 .   ? 10.991 -4.850  5.514  1.00 21.13 2 202 ZN    A ZN  1 
HETATM 1108 S  S   . DMS   D 4 .   ? 19.797 -0.422  19.853 1.00 37.92 ? 203 DMS   A S   1 
HETATM 1109 O  O   . DMS   D 4 .   ? 18.414 -0.771  19.479 1.00 32.29 ? 203 DMS   A O   1 
HETATM 1110 C  C1  . DMS   D 4 .   ? 19.961 0.326   21.483 1.00 38.06 ? 203 DMS   A C1  1 
HETATM 1111 C  C2  . DMS   D 4 .   ? 20.559 0.930   18.874 1.00 37.53 ? 203 DMS   A C2  1 
HETATM 1112 S  S   . DMS   E 4 .   ? 7.449  14.294  21.187 1.00 36.39 ? 204 DMS   A S   1 
HETATM 1113 O  O   . DMS   E 4 .   ? 8.312  13.086  21.530 1.00 35.10 ? 204 DMS   A O   1 
HETATM 1114 C  C1  . DMS   E 4 .   ? 8.579  15.531  20.520 1.00 36.07 ? 204 DMS   A C1  1 
HETATM 1115 C  C2  . DMS   E 4 .   ? 7.097  15.124  22.771 1.00 36.59 ? 204 DMS   A C2  1 
HETATM 1116 O  O   . HOH   F 5 .   ? 12.958 7.018   31.051 1.00 41.69 ? 301 HOH   A O   1 
HETATM 1117 O  O   . HOH   F 5 .   ? 14.859 17.758  14.893 1.00 36.34 ? 302 HOH   A O   1 
HETATM 1118 O  O   . HOH   F 5 .   ? 8.740  22.002  26.898 1.00 53.37 ? 303 HOH   A O   1 
HETATM 1119 O  O   . HOH   F 5 .   ? 22.552 -1.358  3.973  1.00 29.03 ? 304 HOH   A O   1 
HETATM 1120 O  O   . HOH   F 5 .   ? 2.823  8.110   10.011 1.00 34.50 ? 305 HOH   A O   1 
HETATM 1121 O  O   . HOH   F 5 .   ? 21.811 -5.151  10.096 1.00 64.23 ? 306 HOH   A O   1 
HETATM 1122 O  O   . HOH   F 5 .   ? 10.784 8.125   4.704  1.00 26.12 ? 307 HOH   A O   1 
HETATM 1123 O  O   . HOH   F 5 .   ? 26.377 -2.445  14.281 1.00 33.94 ? 308 HOH   A O   1 
HETATM 1124 O  O   . HOH   F 5 .   ? 23.756 21.436  8.084  1.00 27.77 ? 309 HOH   A O   1 
HETATM 1125 O  O   . HOH   F 5 .   ? 30.979 9.855   13.541 1.00 39.05 ? 310 HOH   A O   1 
HETATM 1126 O  O   . HOH   F 5 .   ? 24.342 -6.577  7.998  1.00 37.78 ? 311 HOH   A O   1 
HETATM 1127 O  O   . HOH   F 5 .   ? 8.553  18.937  19.038 1.00 30.39 ? 312 HOH   A O   1 
HETATM 1128 O  O   . HOH   F 5 .   ? 19.294 -0.869  27.340 1.00 29.85 ? 313 HOH   A O   1 
HETATM 1129 O  O   . HOH   F 5 .   ? 27.092 7.767   0.194  1.00 46.65 ? 314 HOH   A O   1 
HETATM 1130 O  O   . HOH   F 5 .   ? 20.434 8.516   18.957 1.00 19.45 ? 315 HOH   A O   1 
HETATM 1131 O  O   . HOH   F 5 .   ? 15.234 12.173  24.142 1.00 28.64 ? 316 HOH   A O   1 
HETATM 1132 O  O   . HOH   F 5 .   ? 0.598  -0.229  16.534 1.00 16.24 ? 317 HOH   A O   1 
HETATM 1133 O  O   . HOH   F 5 .   ? 27.906 3.054   2.951  1.00 46.91 ? 318 HOH   A O   1 
HETATM 1134 O  O   . HOH   F 5 .   ? 3.871  -4.835  21.166 1.00 28.68 ? 319 HOH   A O   1 
HETATM 1135 O  O   . HOH   F 5 .   ? 11.836 16.738  5.769  1.00 56.67 ? 320 HOH   A O   1 
HETATM 1136 O  O   . HOH   F 5 .   ? 26.644 3.498   19.847 1.00 40.00 ? 321 HOH   A O   1 
HETATM 1137 O  O   . HOH   F 5 .   ? 10.360 -4.934  31.697 1.00 38.42 ? 322 HOH   A O   1 
HETATM 1138 O  O   . HOH   F 5 .   ? 29.558 2.875   10.514 1.00 27.65 ? 323 HOH   A O   1 
HETATM 1139 O  O   . HOH   F 5 .   ? 22.442 2.795   24.001 1.00 63.20 ? 324 HOH   A O   1 
HETATM 1140 O  O   . HOH   F 5 .   ? 18.057 -3.195  18.324 1.00 30.55 ? 325 HOH   A O   1 
HETATM 1141 O  O   . HOH   F 5 .   ? 0.074  2.214   24.457 1.00 30.99 ? 326 HOH   A O   1 
HETATM 1142 O  O   . HOH   F 5 .   ? 0.964  -2.442  19.938 1.00 29.92 ? 327 HOH   A O   1 
HETATM 1143 O  O   . HOH   F 5 .   ? 6.239  -5.506  28.879 1.00 35.87 ? 328 HOH   A O   1 
HETATM 1144 O  O   . HOH   F 5 .   ? 5.143  7.558   26.767 1.00 69.64 ? 329 HOH   A O   1 
HETATM 1145 O  O   . HOH   F 5 .   ? 15.738 17.107  16.460 1.00 34.31 ? 330 HOH   A O   1 
HETATM 1146 O  O   . HOH   F 5 .   ? 11.470 11.486  11.544 1.00 18.55 ? 331 HOH   A O   1 
HETATM 1147 O  O   . HOH   F 5 .   ? 31.096 20.177  10.758 1.00 38.48 ? 332 HOH   A O   1 
HETATM 1148 O  O   . HOH   F 5 .   ? -0.551 15.539  9.796  1.00 47.77 ? 333 HOH   A O   1 
HETATM 1149 O  O   . HOH   F 5 .   ? 4.539  7.344   3.221  1.00 44.52 ? 334 HOH   A O   1 
HETATM 1150 O  O   . HOH   F 5 .   ? 10.448 4.719   3.447  1.00 25.78 ? 335 HOH   A O   1 
HETATM 1151 O  O   . HOH   F 5 .   ? 3.280  3.465   27.655 1.00 34.69 ? 336 HOH   A O   1 
HETATM 1152 O  O   . HOH   F 5 .   ? 14.114 18.412  24.283 1.00 34.55 ? 337 HOH   A O   1 
HETATM 1153 O  O   . HOH   F 5 .   ? 4.792  9.912   19.507 1.00 33.11 ? 338 HOH   A O   1 
HETATM 1154 O  O   . HOH   F 5 .   ? 10.749 18.268  20.325 1.00 31.17 ? 339 HOH   A O   1 
HETATM 1155 O  O   . HOH   F 5 .   ? 11.042 15.660  3.378  1.00 52.87 ? 340 HOH   A O   1 
HETATM 1156 O  O   . HOH   F 5 .   ? 8.925  2.410   2.828  1.00 28.83 ? 341 HOH   A O   1 
HETATM 1157 O  O   . HOH   F 5 .   ? 15.138 2.155   23.236 1.00 18.07 ? 342 HOH   A O   1 
HETATM 1158 O  O   . HOH   F 5 .   ? 19.432 8.701   25.710 1.00 33.50 ? 343 HOH   A O   1 
HETATM 1159 O  O   . HOH   F 5 .   ? 6.113  1.598   6.087  1.00 28.12 ? 344 HOH   A O   1 
HETATM 1160 O  O   . HOH   F 5 .   ? 30.532 10.599  19.442 1.00 42.60 ? 345 HOH   A O   1 
HETATM 1161 O  O   . HOH   F 5 .   ? 23.060 17.534  19.169 1.00 33.48 ? 346 HOH   A O   1 
HETATM 1162 O  O   . HOH   F 5 .   ? 13.969 20.307  6.791  1.00 46.93 ? 347 HOH   A O   1 
HETATM 1163 O  O   . HOH   F 5 .   ? 14.169 8.814   29.857 1.00 28.79 ? 348 HOH   A O   1 
HETATM 1164 O  O   . HOH   F 5 .   ? 4.813  5.834   24.562 1.00 38.35 ? 349 HOH   A O   1 
HETATM 1165 O  O   . HOH   F 5 .   ? 19.678 -3.794  16.273 1.00 34.65 ? 350 HOH   A O   1 
HETATM 1166 O  O   . HOH   F 5 .   ? 23.534 -0.522  16.156 1.00 33.19 ? 351 HOH   A O   1 
HETATM 1167 O  O   . HOH   F 5 .   ? 10.288 4.106   33.696 1.00 34.94 ? 352 HOH   A O   1 
HETATM 1168 O  O   . HOH   F 5 .   ? 13.343 1.938   0.883  1.00 24.90 ? 353 HOH   A O   1 
HETATM 1169 O  O   . HOH   F 5 .   ? 17.905 18.551  17.056 1.00 25.99 ? 354 HOH   A O   1 
HETATM 1170 O  O   . HOH   F 5 .   ? 14.908 14.643  4.209  1.00 28.35 ? 355 HOH   A O   1 
HETATM 1171 O  O   . HOH   F 5 .   ? 0.226  4.356   6.775  1.00 29.59 ? 356 HOH   A O   1 
HETATM 1172 O  O   . HOH   F 5 .   ? 16.755 -7.539  10.702 1.00 39.41 ? 357 HOH   A O   1 
HETATM 1173 O  O   . HOH   F 5 .   ? 13.270 10.362  9.441  1.00 17.98 ? 358 HOH   A O   1 
HETATM 1174 O  O   . HOH   F 5 .   ? 18.074 20.823  9.048  1.00 23.05 ? 359 HOH   A O   1 
HETATM 1175 O  O   . HOH   F 5 .   ? 30.094 4.245   3.505  1.00 37.68 ? 360 HOH   A O   1 
HETATM 1176 O  O   . HOH   F 5 .   ? 9.656  -8.726  9.343  1.00 46.26 ? 361 HOH   A O   1 
HETATM 1177 O  O   . HOH   F 5 .   ? 31.338 20.053  16.850 1.00 38.25 ? 362 HOH   A O   1 
HETATM 1178 O  O   . HOH   F 5 .   ? 3.830  -4.996  6.320  1.00 34.55 ? 363 HOH   A O   1 
HETATM 1179 O  O   . HOH   F 5 .   ? 18.124 1.976   23.129 1.00 22.76 ? 364 HOH   A O   1 
HETATM 1180 O  O   . HOH   F 5 .   ? 2.083  13.168  5.610  1.00 40.19 ? 365 HOH   A O   1 
HETATM 1181 O  O   . HOH   F 5 .   ? 7.926  -7.229  8.532  1.00 38.23 ? 366 HOH   A O   1 
HETATM 1182 O  O   . HOH   F 5 .   ? 19.014 12.629  1.603  1.00 37.98 ? 367 HOH   A O   1 
HETATM 1183 O  O   . HOH   F 5 .   ? 5.316  -1.384  24.068 1.00 24.76 ? 368 HOH   A O   1 
HETATM 1184 O  O   . HOH   F 5 .   ? 28.614 -2.509  12.723 1.00 33.47 ? 369 HOH   A O   1 
HETATM 1185 O  O   . HOH   F 5 .   ? 16.253 22.384  8.158  1.00 58.95 ? 370 HOH   A O   1 
HETATM 1186 O  O   . HOH   F 5 .   ? 3.158  14.532  20.562 1.00 37.64 ? 371 HOH   A O   1 
HETATM 1187 O  O   . HOH   F 5 .   ? 6.514  22.714  11.938 1.00 36.53 ? 372 HOH   A O   1 
HETATM 1188 O  O   . HOH   F 5 .   ? 7.169  3.796   32.876 1.00 36.87 ? 373 HOH   A O   1 
HETATM 1189 O  O   . HOH   F 5 .   ? 19.034 3.904   25.867 1.00 45.54 ? 374 HOH   A O   1 
HETATM 1190 O  O   . HOH   F 5 .   ? 14.819 -4.446  17.244 1.00 28.73 ? 375 HOH   A O   1 
HETATM 1191 O  O   . HOH   F 5 .   ? -0.693 -4.485  15.842 0.50 31.12 ? 376 HOH   A O   1 
HETATM 1192 O  O   . HOH   F 5 .   ? 6.883  12.890  5.631  1.00 28.34 ? 377 HOH   A O   1 
HETATM 1193 O  O   . HOH   F 5 .   ? 18.478 -5.655  27.162 1.00 51.13 ? 378 HOH   A O   1 
HETATM 1194 O  O   . HOH   F 5 .   ? 19.812 3.242   28.383 1.00 47.60 ? 379 HOH   A O   1 
HETATM 1195 O  O   . HOH   F 5 .   ? 15.595 -4.754  1.453  1.00 37.17 ? 380 HOH   A O   1 
HETATM 1196 O  O   . HOH   F 5 .   ? 31.469 2.254   12.569 1.00 32.24 ? 381 HOH   A O   1 
HETATM 1197 O  O   . HOH   F 5 .   ? 31.845 8.652   5.368  1.00 43.46 ? 382 HOH   A O   1 
HETATM 1198 O  O   . HOH   F 5 .   ? 19.803 23.271  15.595 1.00 27.20 ? 383 HOH   A O   1 
HETATM 1199 O  O   . HOH   F 5 .   ? 1.299  -2.728  17.339 1.00 25.99 ? 384 HOH   A O   1 
HETATM 1200 O  O   . HOH   F 5 .   ? 4.100  -2.187  21.761 1.00 30.01 ? 385 HOH   A O   1 
HETATM 1201 O  O   . HOH   F 5 .   ? 23.994 1.949   19.610 1.00 33.42 ? 386 HOH   A O   1 
HETATM 1202 O  O   . HOH   F 5 .   ? 31.870 14.181  21.295 1.00 32.69 ? 387 HOH   A O   1 
HETATM 1203 O  O   . HOH   F 5 .   ? 31.603 18.355  8.605  1.00 45.32 ? 388 HOH   A O   1 
HETATM 1204 O  O   . HOH   F 5 .   ? 2.680  -2.674  3.912  1.00 60.59 ? 389 HOH   A O   1 
HETATM 1205 O  O   . HOH   F 5 .   ? 7.134  10.739  4.073  1.00 52.13 ? 390 HOH   A O   1 
HETATM 1206 O  O   . HOH   F 5 .   ? 18.422 8.778   -1.476 1.00 32.22 ? 391 HOH   A O   1 
HETATM 1207 O  O   . HOH   F 5 .   ? 0.618  -3.263  9.887  1.00 44.92 ? 392 HOH   A O   1 
HETATM 1208 O  O   . HOH   F 5 .   ? 28.971 16.130  23.227 1.00 43.66 ? 393 HOH   A O   1 
HETATM 1209 O  O   . HOH   F 5 .   ? 22.308 8.475   21.143 1.00 26.46 ? 394 HOH   A O   1 
HETATM 1210 O  O   . HOH   F 5 .   ? 24.590 6.785   20.237 1.00 49.24 ? 395 HOH   A O   1 
HETATM 1211 O  O   . HOH   F 5 .   ? 22.613 18.395  5.476  1.00 35.59 ? 396 HOH   A O   1 
HETATM 1212 O  O   . HOH   F 5 .   ? 12.255 -8.202  12.908 1.00 39.24 ? 397 HOH   A O   1 
HETATM 1213 O  O   . HOH   F 5 .   ? 14.519 -11.122 4.159  1.00 60.36 ? 398 HOH   A O   1 
HETATM 1214 O  O   . HOH   F 5 .   ? 17.542 10.866  25.977 1.00 47.32 ? 399 HOH   A O   1 
HETATM 1215 O  O   . HOH   F 5 .   ? 16.531 23.371  14.901 1.00 43.40 ? 400 HOH   A O   1 
HETATM 1216 O  O   . HOH   F 5 .   ? 18.693 -5.312  19.715 1.00 32.28 ? 401 HOH   A O   1 
HETATM 1217 O  O   . HOH   F 5 .   ? 21.080 21.575  17.798 1.00 37.16 ? 402 HOH   A O   1 
HETATM 1218 O  O   . HOH   F 5 .   ? 17.721 10.795  0.298  1.00 46.72 ? 403 HOH   A O   1 
HETATM 1219 O  O   . HOH   F 5 .   ? 9.086  19.228  6.503  1.00 49.25 ? 404 HOH   A O   1 
HETATM 1220 O  O   . HOH   F 5 .   ? 6.411  2.426   3.400  1.00 34.11 ? 405 HOH   A O   1 
HETATM 1221 O  O   . HOH   F 5 .   ? 2.050  1.514   26.580 1.00 43.64 ? 406 HOH   A O   1 
HETATM 1222 O  O   . HOH   F 5 .   ? 0.981  -1.507  23.840 1.00 46.16 ? 407 HOH   A O   1 
HETATM 1223 O  O   . HOH   F 5 .   ? 9.308  -8.453  12.294 1.00 39.06 ? 408 HOH   A O   1 
HETATM 1224 O  O   . HOH   F 5 .   ? 8.868  7.080   2.665  1.00 41.30 ? 409 HOH   A O   1 
HETATM 1225 O  O   . HOH   F 5 .   ? 33.079 21.389  15.077 1.00 41.06 ? 410 HOH   A O   1 
HETATM 1226 O  O   . HOH   F 5 .   ? 15.189 11.077  -1.569 1.00 53.23 ? 411 HOH   A O   1 
HETATM 1227 O  O   . HOH   F 5 .   ? 17.262 15.031  25.443 1.00 50.55 ? 412 HOH   A O   1 
HETATM 1228 O  O   . HOH   F 5 .   ? 24.776 19.990  6.291  1.00 40.27 ? 413 HOH   A O   1 
HETATM 1229 O  O   . HOH   F 5 .   ? 5.868  4.835   2.394  1.00 49.50 ? 414 HOH   A O   1 
HETATM 1230 O  O   . HOH   F 5 .   ? 20.959 -4.328  23.555 1.00 53.71 ? 415 HOH   A O   1 
HETATM 1231 O  O   . HOH   F 5 .   ? 21.961 11.400  -2.789 1.00 55.33 ? 416 HOH   A O   1 
HETATM 1232 O  O   . HOH   F 5 .   ? 23.291 1.024   22.297 1.00 54.86 ? 417 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   ? 0.3188 0.3078 0.3277 -0.0114 -0.0297 -0.0200 7   SER   A N   
2    C CA  . SER   A 1   ? 0.3145 0.3077 0.3391 -0.0085 -0.0324 -0.0179 7   SER   A CA  
3    C C   . SER   A 1   ? 0.3072 0.3026 0.3384 -0.0051 -0.0306 -0.0140 7   SER   A C   
4    O O   . SER   A 1   ? 0.3393 0.3325 0.3622 -0.0052 -0.0293 -0.0123 7   SER   A O   
5    C CB  . SER   A 1   ? 0.3563 0.3492 0.3828 -0.0108 -0.0416 -0.0168 7   SER   A CB  
6    O OG  . SER   A 1   ? 0.4101 0.4000 0.4279 -0.0126 -0.0477 -0.0128 7   SER   A OG  
7    N N   . GLY   A 2   ? 0.2684 0.2678 0.3140 -0.0026 -0.0296 -0.0133 8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.2361 0.2366 0.2879 -0.0001 -0.0266 -0.0110 8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.2187 0.2230 0.2814 0.0011  -0.0213 -0.0120 8   GLY   A C   
10   O O   . GLY   A 2   ? 0.2336 0.2393 0.2968 0.0002  -0.0187 -0.0135 8   GLY   A O   
11   N N   . ALA   A 3   ? 0.2113 0.2167 0.2828 0.0026  -0.0191 -0.0110 9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.2089 0.2173 0.2886 0.0026  -0.0130 -0.0120 9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.1995 0.2064 0.2800 0.0029  -0.0076 -0.0121 9   ALA   A C   
14   O O   . ALA   A 3   ? 0.2191 0.2230 0.2989 0.0042  -0.0093 -0.0112 9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.2250 0.2369 0.3201 0.0032  -0.0151 -0.0126 9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.1865 0.1947 0.2675 0.0011  -0.0010 -0.0131 10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.1941 0.2004 0.2752 0.0000  0.0059  -0.0146 10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.2051 0.2140 0.3014 0.0003  0.0104  -0.0166 10  ILE   A C   
19   O O   . ILE   A 4   ? 0.2037 0.2160 0.3043 -0.0010 0.0112  -0.0164 10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.2044 0.2100 0.2728 -0.0041 0.0105  -0.0142 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.2112 0.2157 0.2679 -0.0045 0.0064  -0.0120 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.2308 0.2329 0.2962 -0.0067 0.0179  -0.0168 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.2316 0.2374 0.2795 -0.0085 0.0083  -0.0099 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.2253 0.2323 0.3312 0.0019  0.0142  -0.0185 11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.2320 0.2418 0.3548 0.0023  0.0199  -0.0209 11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.2512 0.2573 0.3701 -0.0009 0.0312  -0.0250 11  TYR   A C   
27   O O   . TYR   A 5   ? 0.2700 0.2713 0.3894 0.0003  0.0337  -0.0267 11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.2301 0.2413 0.3726 0.0070  0.0149  -0.0198 11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.2416 0.2563 0.3865 0.0084  0.0036  -0.0162 11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.2466 0.2667 0.4024 0.0078  0.0021  -0.0161 11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.2614 0.2732 0.3951 0.0091  -0.0048 -0.0133 11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.2534 0.2757 0.4094 0.0080  -0.0081 -0.0137 11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.2683 0.2821 0.4010 0.0090  -0.0144 -0.0109 11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.2756 0.2943 0.4189 0.0083  -0.0161 -0.0114 11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.3061 0.3258 0.4466 0.0071  -0.0253 -0.0098 11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.2458 0.2533 0.3597 -0.0056 0.0381  -0.0265 12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.2646 0.2679 0.3709 -0.0106 0.0494  -0.0309 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.2853 0.2918 0.4020 -0.0133 0.0579  -0.0335 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.2839 0.2947 0.4005 -0.0149 0.0555  -0.0307 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.3038 0.3040 0.3853 -0.0164 0.0487  -0.0291 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.3022 0.3068 0.3782 -0.0179 0.0427  -0.0241 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.3448 0.3403 0.4151 -0.0236 0.0600  -0.0337 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.2949 0.2994 0.4237 -0.0132 0.0683  -0.0390 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.2951 0.3029 0.4366 -0.0158 0.0782  -0.0423 13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.2857 0.3015 0.4468 -0.0115 0.0709  -0.0386 13  GLY   A C   
46   O O   . GLY   A 7   ? 0.3038 0.3219 0.4789 -0.0051 0.0619  -0.0361 13  GLY   A O   
47   N N   . ASN   A 8   ? 0.2770 0.2966 0.4372 -0.0156 0.0733  -0.0374 14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.2771 0.3037 0.4543 -0.0125 0.0659  -0.0340 14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.2645 0.2914 0.4266 -0.0133 0.0551  -0.0285 14  ASN   A C   
50   O O   . ASN   A 8   ? 0.2564 0.2872 0.4243 -0.0145 0.0526  -0.0263 14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.3174 0.3483 0.5090 -0.0159 0.0759  -0.0364 14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.4016 0.4337 0.6161 -0.0134 0.0858  -0.0418 14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.4261 0.4634 0.6662 -0.0074 0.0806  -0.0409 14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.4303 0.4572 0.6363 -0.0181 0.0998  -0.0476 14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.2438 0.2666 0.3891 -0.0123 0.0489  -0.0266 15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.2322 0.2550 0.3653 -0.0125 0.0397  -0.0221 15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.2151 0.2369 0.3473 -0.0073 0.0296  -0.0206 15  TYR   A C   
58   O O   . TYR   A 9   ? 0.2211 0.2402 0.3531 -0.0049 0.0298  -0.0220 15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.2487 0.2674 0.3593 -0.0179 0.0423  -0.0203 15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.2736 0.2921 0.3791 -0.0249 0.0510  -0.0205 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.2912 0.3132 0.4052 -0.0266 0.0511  -0.0183 15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.3030 0.3172 0.3937 -0.0309 0.0593  -0.0227 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.3109 0.3322 0.4190 -0.0338 0.0593  -0.0178 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.3241 0.3373 0.4068 -0.0388 0.0674  -0.0225 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.3363 0.3532 0.4278 -0.0402 0.0673  -0.0197 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.3884 0.4041 0.4712 -0.0488 0.0753  -0.0187 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.1981 0.2213 0.3283 -0.0064 0.0214  -0.0178 16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.1937 0.2154 0.3190 -0.0031 0.0124  -0.0165 16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.1882 0.2080 0.2989 -0.0050 0.0102  -0.0143 16  ARG   A C   
70   O O   . ARG   A 10  ? 0.1925 0.2137 0.3051 -0.0069 0.0102  -0.0130 16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.2097 0.2347 0.3491 -0.0007 0.0051  -0.0162 16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.2417 0.2647 0.3730 0.0006  -0.0042 -0.0151 16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.2488 0.2746 0.3925 0.0016  -0.0122 -0.0149 16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.2491 0.2733 0.3849 0.0001  -0.0183 -0.0152 16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.2777 0.2989 0.4041 0.0000  -0.0254 -0.0149 16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.2897 0.3095 0.4135 0.0017  -0.0282 -0.0131 16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.2825 0.3015 0.4017 -0.0022 -0.0292 -0.0165 16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.1852 0.2019 0.2829 -0.0046 0.0088  -0.0135 17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.1837 0.1993 0.2706 -0.0060 0.0067  -0.0111 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.1804 0.1949 0.2653 -0.0032 0.0002  -0.0115 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.1905 0.2032 0.2718 -0.0015 -0.0020 -0.0122 17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.2031 0.2165 0.2771 -0.0084 0.0097  -0.0098 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.2136 0.2273 0.2808 -0.0100 0.0074  -0.0062 17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.2195 0.2326 0.2925 -0.0123 0.0171  -0.0108 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.1711 0.1859 0.2573 -0.0034 -0.0022 -0.0111 18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.1799 0.1928 0.2626 -0.0020 -0.0068 -0.0126 18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.1772 0.1890 0.2563 -0.0026 -0.0059 -0.0117 18  VAL   A C   
88   O O   . VAL   A 12  ? 0.1916 0.2045 0.2739 -0.0039 -0.0034 -0.0090 18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.1990 0.2124 0.2898 -0.0018 -0.0110 -0.0148 18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.2354 0.2503 0.3323 -0.0007 -0.0135 -0.0149 18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.2072 0.2222 0.3077 -0.0033 -0.0092 -0.0146 18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.1628 0.1722 0.2365 -0.0019 -0.0077 -0.0137 19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.1747 0.1830 0.2497 -0.0020 -0.0060 -0.0138 19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.1704 0.1781 0.2551 -0.0025 -0.0063 -0.0150 19  ASN   A C   
95   O O   . ASN   A 13  ? 0.1760 0.1828 0.2625 -0.0031 -0.0091 -0.0181 19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.1857 0.1909 0.2533 -0.0018 -0.0065 -0.0174 19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.1904 0.1957 0.2488 -0.0016 -0.0059 -0.0160 19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.2003 0.2047 0.2522 -0.0018 -0.0084 -0.0162 19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.2008 0.2074 0.2600 -0.0014 -0.0028 -0.0141 19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.1653 0.1733 0.2570 -0.0028 -0.0042 -0.0121 20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.1706 0.1774 0.2725 -0.0036 -0.0042 -0.0128 20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.1801 0.1826 0.2821 -0.0037 -0.0051 -0.0191 20  ARG   A C   
103  O O   . ARG   A 14  ? 0.1912 0.1927 0.2978 -0.0052 -0.0070 -0.0216 20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.1791 0.1859 0.2883 -0.0039 -0.0023 -0.0077 20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.1796 0.1849 0.2998 -0.0052 -0.0021 -0.0067 20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.1926 0.1975 0.3204 -0.0054 -0.0012 -0.0002 20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.1930 0.1958 0.3316 -0.0071 -0.0011 0.0024  20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.2229 0.2210 0.3712 -0.0063 -0.0004 -0.0012 20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.2413 0.2361 0.3882 -0.0043 0.0008  -0.0084 20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.2224 0.2182 0.3810 -0.0081 -0.0004 0.0021  20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.1881 0.1880 0.2841 -0.0030 -0.0035 -0.0220 21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.2017 0.1963 0.2949 -0.0044 -0.0033 -0.0292 21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.2314 0.2252 0.3147 -0.0067 -0.0082 -0.0325 21  HIS   A C   
114  O O   . HIS   A 15  ? 0.2670 0.2561 0.3467 -0.0095 -0.0092 -0.0383 21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.2192 0.2108 0.3096 -0.0037 0.0014  -0.0321 21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.2349 0.2278 0.3130 -0.0036 0.0015  -0.0319 21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.2374 0.2349 0.3158 -0.0018 0.0020  -0.0260 21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.2538 0.2433 0.3183 -0.0059 0.0013  -0.0367 21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.2499 0.2466 0.3168 -0.0025 0.0026  -0.0277 21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.2619 0.2539 0.3196 -0.0050 0.0020  -0.0337 21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.2162 0.2140 0.2959 -0.0060 -0.0115 -0.0289 22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.2268 0.2245 0.3006 -0.0078 -0.0174 -0.0302 22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.2357 0.2376 0.3207 -0.0078 -0.0208 -0.0279 22  LEU   A C   
124  O O   . LEU   A 16  ? 0.2567 0.2598 0.3413 -0.0091 -0.0267 -0.0279 22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.2305 0.2289 0.2936 -0.0070 -0.0187 -0.0281 22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.2658 0.2604 0.3178 -0.0077 -0.0149 -0.0306 22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.2769 0.2719 0.3189 -0.0073 -0.0161 -0.0279 22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.2913 0.2802 0.3346 -0.0118 -0.0159 -0.0368 22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.2150 0.2195 0.3112 -0.0068 -0.0172 -0.0254 23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.2289 0.2375 0.3364 -0.0073 -0.0188 -0.0237 23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.2332 0.2411 0.3458 -0.0101 -0.0242 -0.0270 23  ALA   A C   
132  O O   . ALA   A 17  ? 0.2360 0.2392 0.3458 -0.0122 -0.0244 -0.0309 23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.2316 0.2416 0.3473 -0.0071 -0.0137 -0.0207 23  ALA   A CB  
134  N N   . THR   A 18  ? 0.2316 0.2439 0.3521 -0.0104 -0.0284 -0.0256 24  THR   A N   
135  C CA  . THR   A 18  ? 0.2385 0.2514 0.3652 -0.0138 -0.0352 -0.0277 24  THR   A CA  
136  C C   . THR   A 18  ? 0.2452 0.2607 0.3876 -0.0151 -0.0328 -0.0275 24  THR   A C   
137  O O   . THR   A 18  ? 0.2413 0.2584 0.3890 -0.0136 -0.0262 -0.0251 24  THR   A O   
138  C CB  . THR   A 18  ? 0.2493 0.2667 0.3806 -0.0132 -0.0418 -0.0250 24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.2518 0.2751 0.3982 -0.0107 -0.0377 -0.0219 24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.2695 0.2842 0.3862 -0.0119 -0.0439 -0.0239 24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.2576 0.2738 0.4074 -0.0189 -0.0388 -0.0296 25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.2579 0.2773 0.4242 -0.0206 -0.0369 -0.0291 25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.2438 0.2707 0.4238 -0.0182 -0.0331 -0.0249 25  HIS   A C   
144  O O   . HIS   A 19  ? 0.2481 0.2764 0.4361 -0.0186 -0.0266 -0.0234 25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.2966 0.3164 0.4693 -0.0256 -0.0453 -0.0319 25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.4281 0.4392 0.5876 -0.0295 -0.0474 -0.0376 25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.4793 0.4849 0.6410 -0.0309 -0.0421 -0.0405 25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.4777 0.4844 0.6220 -0.0327 -0.0536 -0.0410 25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.5051 0.5028 0.6538 -0.0346 -0.0443 -0.0465 25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.5093 0.5073 0.6456 -0.0361 -0.0509 -0.0472 25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.2250 0.2561 0.4074 -0.0161 -0.0364 -0.0230 26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.2258 0.2634 0.4225 -0.0138 -0.0312 -0.0202 26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.2081 0.2435 0.3960 -0.0119 -0.0214 -0.0190 26  ASN   A C   
154  O O   . ASN   A 20  ? 0.2114 0.2498 0.4079 -0.0124 -0.0140 -0.0178 26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.2662 0.3076 0.4686 -0.0115 -0.0368 -0.0184 26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.3768 0.4244 0.5967 -0.0090 -0.0303 -0.0166 26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.4148 0.4682 0.6542 -0.0103 -0.0285 -0.0164 26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.4140 0.4601 0.6279 -0.0056 -0.0260 -0.0157 26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.1990 0.2290 0.3687 -0.0103 -0.0211 -0.0193 27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.1998 0.2279 0.3612 -0.0094 -0.0132 -0.0175 27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.2038 0.2308 0.3683 -0.0121 -0.0087 -0.0164 27  ASP   A C   
162  O O   . ASP   A 21  ? 0.2156 0.2439 0.3812 -0.0132 -0.0020 -0.0139 27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.1967 0.2198 0.3407 -0.0079 -0.0143 -0.0178 27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.2369 0.2602 0.3753 -0.0056 -0.0170 -0.0177 27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.2479 0.2743 0.3926 -0.0043 -0.0139 -0.0166 27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.2366 0.2566 0.3644 -0.0053 -0.0215 -0.0189 27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.2163 0.2398 0.3811 -0.0136 -0.0121 -0.0181 28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.2118 0.2330 0.3809 -0.0160 -0.0086 -0.0164 28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.2218 0.2478 0.4063 -0.0189 -0.0059 -0.0152 28  TRP   A C   
170  O O   . TRP   A 22  ? 0.2260 0.2515 0.4123 -0.0211 -0.0004 -0.0118 28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.2035 0.2187 0.3710 -0.0170 -0.0122 -0.0196 28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.2080 0.2182 0.3639 -0.0149 -0.0110 -0.0196 28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.2241 0.2313 0.3696 -0.0135 -0.0138 -0.0232 28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.2020 0.2098 0.3565 -0.0144 -0.0068 -0.0152 28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.2184 0.2221 0.3578 -0.0117 -0.0106 -0.0220 28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.2166 0.2209 0.3622 -0.0121 -0.0069 -0.0166 28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.2135 0.2220 0.3733 -0.0163 -0.0031 -0.0095 28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.2136 0.2157 0.3586 -0.0110 -0.0042 -0.0124 28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.2144 0.2200 0.3715 -0.0158 -0.0014 -0.0048 28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.2148 0.2178 0.3660 -0.0128 -0.0022 -0.0061 28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.2259 0.2566 0.4214 -0.0191 -0.0097 -0.0173 29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.2413 0.2777 0.4541 -0.0216 -0.0066 -0.0165 29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.2438 0.2842 0.4589 -0.0213 0.0021  -0.0145 29  ALA   A C   
184  O O   . ALA   A 23  ? 0.2551 0.2996 0.4828 -0.0241 0.0076  -0.0137 29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.2462 0.2876 0.4725 -0.0220 -0.0141 -0.0187 29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.2156 0.2549 0.4191 -0.0183 0.0035  -0.0144 30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.2144 0.2559 0.4172 -0.0185 0.0125  -0.0137 30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.2158 0.2519 0.3985 -0.0193 0.0159  -0.0113 30  ASN   A C   
189  O O   . ASN   A 24  ? 0.2136 0.2492 0.3883 -0.0185 0.0200  -0.0117 30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.2206 0.2654 0.4298 -0.0147 0.0108  -0.0157 30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.2620 0.3134 0.4943 -0.0143 0.0073  -0.0168 30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.2733 0.3296 0.5213 -0.0160 0.0143  -0.0173 30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.2892 0.3410 0.5241 -0.0130 -0.0037 -0.0170 30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.2185 0.2504 0.3942 -0.0209 0.0137  -0.0088 31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.2169 0.2446 0.3767 -0.0217 0.0151  -0.0053 31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.2418 0.2698 0.3946 -0.0261 0.0232  -0.0027 31  LEU   A C   
197  O O   . LEU   A 25  ? 0.2611 0.2906 0.4206 -0.0303 0.0283  -0.0014 31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.2166 0.2402 0.3766 -0.0228 0.0117  -0.0025 31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.2282 0.2480 0.3761 -0.0236 0.0116  0.0025  31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.2405 0.2591 0.3790 -0.0194 0.0081  0.0005  31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.2407 0.2565 0.3945 -0.0248 0.0093  0.0059  31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.2386 0.2647 0.3770 -0.0260 0.0247  -0.0019 32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.2497 0.2745 0.3761 -0.0316 0.0315  0.0007  32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.2650 0.2861 0.3786 -0.0341 0.0275  0.0074  32  VAL   A C   
205  O O   . VAL   A 26  ? 0.2903 0.3098 0.3985 -0.0401 0.0298  0.0128  32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.2674 0.2924 0.3874 -0.0306 0.0356  -0.0034 32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.2846 0.3066 0.3874 -0.0374 0.0419  -0.0013 32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.2665 0.2953 0.4026 -0.0284 0.0401  -0.0089 32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.2462 0.2661 0.3566 -0.0296 0.0211  0.0075  33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.2342 0.2517 0.3362 -0.0309 0.0171  0.0137  33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.2207 0.2374 0.3264 -0.0248 0.0111  0.0120  33  TRP   A C   
212  O O   . TRP   A 27  ? 0.2243 0.2419 0.3306 -0.0207 0.0103  0.0065  33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.2513 0.2682 0.3370 -0.0351 0.0197  0.0153  33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.2695 0.2851 0.3466 -0.0367 0.0145  0.0220  33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.3016 0.3160 0.3742 -0.0425 0.0123  0.0306  33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.2578 0.2737 0.3319 -0.0328 0.0102  0.0214  33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.3107 0.3252 0.3788 -0.0422 0.0066  0.0355  33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.2759 0.2915 0.3453 -0.0361 0.0058  0.0296  33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.2517 0.2682 0.3268 -0.0272 0.0097  0.0153  33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.2740 0.2906 0.3414 -0.0338 0.0015  0.0311  33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.2642 0.2808 0.3349 -0.0254 0.0059  0.0167  33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.2706 0.2876 0.3383 -0.0285 0.0022  0.0242  33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.2017 0.2166 0.3107 -0.0244 0.0073  0.0166  34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.2075 0.2213 0.3194 -0.0194 0.0034  0.0148  34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.1984 0.2111 0.3109 -0.0204 0.0005  0.0223  34  GLU   A C   
226  O O   . GLU   A 28  ? 0.2136 0.2254 0.3285 -0.0243 -0.0001 0.0293  34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.2159 0.2279 0.3387 -0.0160 0.0021  0.0096  34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.2127 0.2226 0.3465 -0.0180 0.0023  0.0122  34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.2396 0.2460 0.3807 -0.0174 0.0002  0.0171  34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.2850 0.2894 0.4335 -0.0202 0.0003  0.0221  34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.2369 0.2425 0.3778 -0.0141 -0.0012 0.0161  34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.1862 0.1992 0.2973 -0.0171 -0.0015 0.0215  35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.1883 0.2014 0.3044 -0.0173 -0.0047 0.0287  35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.1926 0.2044 0.3172 -0.0117 -0.0049 0.0242  35  ASP   A C   
235  O O   . ASP   A 29  ? 0.1936 0.2067 0.3116 -0.0096 -0.0042 0.0197  35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.2141 0.2299 0.3184 -0.0211 -0.0065 0.0342  35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.2785 0.2954 0.3896 -0.0225 -0.0113 0.0439  35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.3189 0.3347 0.4454 -0.0183 -0.0124 0.0446  35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.2788 0.2974 0.3801 -0.0282 -0.0141 0.0509  35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.1991 0.2078 0.3382 -0.0098 -0.0049 0.0246  36  SER   A N   
241  C CA  . SER   A 30  ? 0.2142 0.2205 0.3620 -0.0053 -0.0033 0.0192  36  SER   A CA  
242  C C   . SER   A 30  ? 0.2407 0.2499 0.3910 -0.0036 -0.0041 0.0227  36  SER   A C   
243  O O   . SER   A 30  ? 0.2775 0.2861 0.4274 -0.0007 -0.0014 0.0162  36  SER   A O   
244  C CB  . SER   A 30  ? 0.2437 0.2450 0.4077 -0.0042 -0.0024 0.0194  36  SER   A CB  
245  O OG  . SER   A 30  ? 0.2769 0.2785 0.4509 -0.0060 -0.0054 0.0302  36  SER   A OG  
246  N N   . SER   A 31  ? 0.2066 0.2192 0.3572 -0.0064 -0.0079 0.0326  37  SER   A N   
247  C CA  . SER   A 31  ? 0.1974 0.2138 0.3518 -0.0054 -0.0096 0.0366  37  SER   A CA  
248  C C   . SER   A 31  ? 0.1918 0.2112 0.3299 -0.0062 -0.0089 0.0326  37  SER   A C   
249  O O   . SER   A 31  ? 0.2093 0.2315 0.3507 -0.0047 -0.0089 0.0330  37  SER   A O   
250  C CB  . SER   A 31  ? 0.2506 0.2698 0.4118 -0.0089 -0.0156 0.0496  37  SER   A CB  
251  O OG  . SER   A 31  ? 0.3407 0.3619 0.4839 -0.0150 -0.0184 0.0537  37  SER   A OG  
252  N N   . ARG   A 32  ? 0.1844 0.2029 0.3071 -0.0082 -0.0078 0.0283  38  ARG   A N   
253  C CA  . ARG   A 32  ? 0.1849 0.2051 0.2929 -0.0091 -0.0072 0.0248  38  ARG   A CA  
254  C C   . ARG   A 32  ? 0.1814 0.1991 0.2843 -0.0059 -0.0039 0.0151  38  ARG   A C   
255  O O   . ARG   A 32  ? 0.1817 0.2001 0.2737 -0.0063 -0.0035 0.0124  38  ARG   A O   
256  C CB  . ARG   A 32  ? 0.2093 0.2301 0.3038 -0.0143 -0.0079 0.0274  38  ARG   A CB  
257  C CG  . ARG   A 32  ? 0.2161 0.2392 0.3095 -0.0196 -0.0120 0.0375  38  ARG   A CG  
258  C CD  . ARG   A 32  ? 0.2206 0.2427 0.2985 -0.0258 -0.0109 0.0382  38  ARG   A CD  
259  N NE  . ARG   A 32  ? 0.2180 0.2402 0.2824 -0.0270 -0.0089 0.0335  38  ARG   A NE  
260  C CZ  . ARG   A 32  ? 0.2246 0.2464 0.2745 -0.0334 -0.0083 0.0349  38  ARG   A CZ  
261  N NH1 . ARG   A 32  ? 0.2462 0.2675 0.2908 -0.0401 -0.0097 0.0414  38  ARG   A NH1 
262  N NH2 . ARG   A 32  ? 0.2299 0.2508 0.2695 -0.0340 -0.0061 0.0299  38  ARG   A NH2 
263  N N   . ASP   A 33  ? 0.1904 0.2048 0.2997 -0.0038 -0.0023 0.0103  39  ASP   A N   
264  C CA  . ASP   A 33  ? 0.1749 0.1867 0.2776 -0.0023 -0.0008 0.0020  39  ASP   A CA  
265  C C   . ASP   A 33  ? 0.1770 0.1896 0.2697 -0.0039 -0.0017 0.0009  39  ASP   A C   
266  O O   . ASP   A 33  ? 0.1823 0.1941 0.2676 -0.0030 -0.0018 -0.0036 39  ASP   A O   
267  C CB  . ASP   A 33  ? 0.1736 0.1848 0.2723 -0.0005 0.0010  -0.0023 39  ASP   A CB  
268  C CG  . ASP   A 33  ? 0.1940 0.2016 0.2850 -0.0001 0.0015  -0.0099 39  ASP   A CG  
269  O OD1 . ASP   A 33  ? 0.2151 0.2200 0.3100 -0.0003 0.0011  -0.0131 39  ASP   A OD1 
270  O OD2 . ASP   A 33  ? 0.1920 0.1994 0.2730 -0.0001 0.0017  -0.0122 39  ASP   A OD2 
271  N N   . LEU   A 34  ? 0.1729 0.1869 0.2663 -0.0066 -0.0019 0.0051  40  LEU   A N   
272  C CA  . LEU   A 34  ? 0.1660 0.1806 0.2530 -0.0082 -0.0009 0.0034  40  LEU   A CA  
273  C C   . LEU   A 34  ? 0.1673 0.1816 0.2615 -0.0092 -0.0001 0.0027  40  LEU   A C   
274  O O   . LEU   A 34  ? 0.1785 0.1924 0.2794 -0.0108 -0.0002 0.0065  40  LEU   A O   
275  C CB  . LEU   A 34  ? 0.1768 0.1930 0.2554 -0.0119 0.0000  0.0077  40  LEU   A CB  
276  C CG  . LEU   A 34  ? 0.2031 0.2199 0.2731 -0.0119 -0.0005 0.0079  40  LEU   A CG  
277  C CD1 . LEU   A 34  ? 0.2174 0.2347 0.2775 -0.0172 0.0006  0.0114  40  LEU   A CD1 
278  C CD2 . LEU   A 34  ? 0.1944 0.2097 0.2605 -0.0090 -0.0002 0.0020  40  LEU   A CD2 
279  N N   . LEU   A 35  ? 0.1670 0.1819 0.2608 -0.0088 0.0005  -0.0013 41  LEU   A N   
280  C CA  . LEU   A 35  ? 0.1751 0.1909 0.2769 -0.0101 0.0019  -0.0022 41  LEU   A CA  
281  C C   . LEU   A 35  ? 0.1842 0.2018 0.2841 -0.0107 0.0045  -0.0043 41  LEU   A C   
282  O O   . LEU   A 35  ? 0.1823 0.1996 0.2782 -0.0084 0.0032  -0.0068 41  LEU   A O   
283  C CB  . LEU   A 35  ? 0.1722 0.1867 0.2822 -0.0084 -0.0010 -0.0062 41  LEU   A CB  
284  C CG  . LEU   A 35  ? 0.1863 0.2024 0.3071 -0.0101 -0.0002 -0.0070 41  LEU   A CG  
285  C CD1 . LEU   A 35  ? 0.1872 0.2008 0.3159 -0.0102 -0.0027 -0.0090 41  LEU   A CD1 
286  C CD2 . LEU   A 35  ? 0.1947 0.2136 0.3192 -0.0091 -0.0012 -0.0104 41  LEU   A CD2 
287  N N   . VAL   A 36  ? 0.1771 0.1960 0.2801 -0.0139 0.0089  -0.0031 42  VAL   A N   
288  C CA  . VAL   A 36  ? 0.1775 0.1980 0.2821 -0.0144 0.0133  -0.0059 42  VAL   A CA  
289  C C   . VAL   A 36  ? 0.1878 0.2110 0.3071 -0.0148 0.0148  -0.0075 42  VAL   A C   
290  O O   . VAL   A 36  ? 0.1997 0.2231 0.3229 -0.0177 0.0160  -0.0051 42  VAL   A O   
291  C CB  . VAL   A 36  ? 0.1924 0.2119 0.2865 -0.0193 0.0192  -0.0040 42  VAL   A CB  
292  C CG1 . VAL   A 36  ? 0.2018 0.2219 0.2995 -0.0201 0.0261  -0.0081 42  VAL   A CG1 
293  C CG2 . VAL   A 36  ? 0.2020 0.2193 0.2827 -0.0195 0.0169  -0.0020 42  VAL   A CG2 
294  N N   . SER   A 37  ? 0.1795 0.2048 0.3081 -0.0120 0.0138  -0.0110 43  SER   A N   
295  C CA  . SER   A 37  ? 0.1866 0.2158 0.3322 -0.0123 0.0148  -0.0125 43  SER   A CA  
296  C C   . SER   A 37  ? 0.2022 0.2337 0.3556 -0.0124 0.0218  -0.0149 43  SER   A C   
297  O O   . SER   A 37  ? 0.2043 0.2336 0.3502 -0.0114 0.0242  -0.0160 43  SER   A O   
298  C CB  . SER   A 37  ? 0.1958 0.2262 0.3499 -0.0093 0.0063  -0.0140 43  SER   A CB  
299  O OG  . SER   A 37  ? 0.2127 0.2424 0.3641 -0.0060 0.0021  -0.0151 43  SER   A OG  
300  N N   . SER   A 38  ? 0.2075 0.2433 0.3773 -0.0138 0.0258  -0.0160 44  SER   A N   
301  C CA  . SER   A 38  ? 0.2374 0.2755 0.4182 -0.0137 0.0341  -0.0191 44  SER   A CA  
302  C C   . SER   A 38  ? 0.2551 0.2969 0.4542 -0.0086 0.0285  -0.0204 44  SER   A C   
303  O O   . SER   A 38  ? 0.2577 0.3017 0.4638 -0.0069 0.0189  -0.0190 44  SER   A O   
304  C CB  . SER   A 38  ? 0.2740 0.3152 0.4645 -0.0184 0.0429  -0.0196 44  SER   A CB  
305  O OG  . SER   A 38  ? 0.3050 0.3500 0.5092 -0.0181 0.0370  -0.0182 44  SER   A OG  
306  N N   . THR   A 39  ? 0.2770 0.3188 0.4834 -0.0066 0.0340  -0.0229 45  THR   A N   
307  C CA  . THR   A 39  ? 0.3045 0.3496 0.5301 -0.0016 0.0282  -0.0228 45  THR   A CA  
308  C C   . THR   A 39  ? 0.3415 0.3912 0.5919 -0.0012 0.0381  -0.0258 45  THR   A C   
309  O O   . THR   A 39  ? 0.3479 0.3955 0.5938 -0.0045 0.0511  -0.0292 45  THR   A O   
310  C CB  . THR   A 39  ? 0.3259 0.3656 0.5405 0.0016  0.0252  -0.0226 45  THR   A CB  
311  O OG1 . THR   A 39  ? 0.3506 0.3866 0.5594 0.0000  0.0372  -0.0261 45  THR   A OG1 
312  C CG2 . THR   A 39  ? 0.3249 0.3601 0.5157 0.0010  0.0174  -0.0203 45  THR   A CG2 
313  N N   . THR   A 40  ? 0.3674 0.4231 0.6434 0.0024  0.0321  -0.0244 46  THR   A N   
314  C CA  . THR   A 40  ? 0.3950 0.4557 0.6992 0.0037  0.0417  -0.0272 46  THR   A CA  
315  C C   . THR   A 40  ? 0.4248 0.4810 0.7322 0.0075  0.0462  -0.0292 46  THR   A C   
316  O O   . THR   A 40  ? 0.4455 0.5006 0.7611 0.0067  0.0608  -0.0343 46  THR   A O   
317  C CB  . THR   A 40  ? 0.4086 0.4786 0.7431 0.0056  0.0336  -0.0243 46  THR   A CB  
318  O OG1 . THR   A 40  ? 0.4249 0.4948 0.7576 0.0084  0.0167  -0.0194 46  THR   A OG1 
319  C CG2 . THR   A 40  ? 0.4210 0.4957 0.7585 0.0008  0.0351  -0.0243 46  THR   A CG2 
320  N N   . ALA   A 41  ? 0.4258 0.4787 0.7264 0.0112  0.0345  -0.0256 47  ALA   A N   
321  C CA  . ALA   A 41  ? 0.4306 0.4783 0.7345 0.0148  0.0377  -0.0268 47  ALA   A CA  
322  C C   . ALA   A 41  ? 0.4404 0.4792 0.7150 0.0117  0.0464  -0.0307 47  ALA   A C   
323  O O   . ALA   A 41  ? 0.4469 0.4832 0.6956 0.0081  0.0435  -0.0296 47  ALA   A O   
324  C CB  . ALA   A 41  ? 0.4314 0.4786 0.7377 0.0189  0.0215  -0.0206 47  ALA   A CB  
325  N N   . GLN   A 42  ? 0.4356 0.4696 0.7154 0.0127  0.0572  -0.0351 48  GLN   A N   
326  C CA  . GLN   A 42  ? 0.4464 0.4717 0.6994 0.0088  0.0657  -0.0393 48  GLN   A CA  
327  C C   . GLN   A 42  ? 0.4306 0.4499 0.6663 0.0109  0.0557  -0.0358 48  GLN   A C   
328  O O   . GLN   A 42  ? 0.4376 0.4558 0.6876 0.0160  0.0496  -0.0332 48  GLN   A O   
329  C CB  . GLN   A 42  ? 0.4817 0.5032 0.7473 0.0081  0.0826  -0.0468 48  GLN   A CB  
330  C CG  . GLN   A 42  ? 0.5717 0.5836 0.8089 0.0024  0.0924  -0.0520 48  GLN   A CG  
331  C CD  . GLN   A 42  ? 0.6641 0.6756 0.8910 -0.0055 0.1069  -0.0576 48  GLN   A CD  
332  O OE1 . GLN   A 42  ? 0.6804 0.6979 0.9264 -0.0061 0.1139  -0.0595 48  GLN   A OE1 
333  N NE2 . GLN   A 42  ? 0.6902 0.6946 0.8862 -0.0125 0.1115  -0.0600 48  GLN   A NE2 
334  N N   . GLY   A 43  ? 0.4051 0.4208 0.6112 0.0067  0.0539  -0.0352 49  GLY   A N   
335  C CA  . GLY   A 43  ? 0.3942 0.4041 0.5813 0.0073  0.0468  -0.0327 49  GLY   A CA  
336  C C   . GLY   A 43  ? 0.3810 0.3828 0.5574 0.0047  0.0573  -0.0378 49  GLY   A C   
337  O O   . GLY   A 43  ? 0.3923 0.3925 0.5687 0.0006  0.0703  -0.0436 49  GLY   A O   
338  N N   . CYS   A 44  ? 0.3503 0.3464 0.5174 0.0062  0.0523  -0.0362 50  CYS   A N   
339  C CA  . CYS   A 44  ? 0.3498 0.3373 0.5071 0.0032  0.0621  -0.0415 50  CYS   A CA  
340  C C   . CYS   A 44  ? 0.3343 0.3172 0.4663 0.0006  0.0562  -0.0391 50  CYS   A C   
341  O O   . CYS   A 44  ? 0.3689 0.3441 0.4948 -0.0009 0.0612  -0.0424 50  CYS   A O   
342  C CB  . CYS   A 44  ? 0.3679 0.3513 0.5490 0.0077  0.0678  -0.0446 50  CYS   A CB  
343  S SG  . CYS   A 44  ? 0.4536 0.4393 0.6559 0.0161  0.0526  -0.0363 50  CYS   A SG  
344  N N   . ASP   A 45  ? 0.3072 0.2945 0.4254 -0.0003 0.0467  -0.0339 51  ASP   A N   
345  C CA  . ASP   A 45  ? 0.3100 0.2943 0.4054 -0.0033 0.0419  -0.0316 51  ASP   A CA  
346  C C   . ASP   A 45  ? 0.3115 0.2928 0.3896 -0.0111 0.0512  -0.0357 51  ASP   A C   
347  O O   . ASP   A 45  ? 0.3426 0.3251 0.4241 -0.0142 0.0595  -0.0393 51  ASP   A O   
348  C CB  . ASP   A 45  ? 0.3443 0.3340 0.4321 -0.0023 0.0309  -0.0257 51  ASP   A CB  
349  C CG  . ASP   A 45  ? 0.4115 0.4030 0.5074 0.0030  0.0202  -0.0212 51  ASP   A CG  
350  O OD1 . ASP   A 45  ? 0.4513 0.4390 0.5552 0.0059  0.0185  -0.0205 51  ASP   A OD1 
351  O OD2 . ASP   A 45  ? 0.3520 0.3482 0.4456 0.0035  0.0133  -0.0182 51  ASP   A OD2 
352  N N   . THR   A 46  ? 0.2643 0.2415 0.3241 -0.0150 0.0498  -0.0352 52  THR   A N   
353  C CA  . THR   A 46  ? 0.2617 0.2361 0.3028 -0.0237 0.0562  -0.0379 52  THR   A CA  
354  C C   . THR   A 46  ? 0.2469 0.2253 0.2727 -0.0265 0.0475  -0.0318 52  THR   A C   
355  O O   . THR   A 46  ? 0.2594 0.2378 0.2825 -0.0239 0.0404  -0.0285 52  THR   A O   
356  C CB  . THR   A 46  ? 0.3037 0.2691 0.3375 -0.0270 0.0623  -0.0430 52  THR   A CB  
357  O OG1 . THR   A 46  ? 0.3226 0.2840 0.3727 -0.0248 0.0723  -0.0494 52  THR   A OG1 
358  C CG2 . THR   A 46  ? 0.3182 0.2803 0.3285 -0.0377 0.0667  -0.0451 52  THR   A CG2 
359  N N   . ILE   A 47  ? 0.2487 0.2301 0.2649 -0.0323 0.0487  -0.0302 53  ILE   A N   
360  C CA  . ILE   A 47  ? 0.2357 0.2210 0.2408 -0.0349 0.0407  -0.0239 53  ILE   A CA  
361  C C   . ILE   A 47  ? 0.2402 0.2210 0.2270 -0.0428 0.0417  -0.0245 53  ILE   A C   
362  O O   . ILE   A 47  ? 0.2559 0.2317 0.2331 -0.0498 0.0497  -0.0291 53  ILE   A O   
363  C CB  . ILE   A 47  ? 0.2498 0.2399 0.2542 -0.0378 0.0403  -0.0205 53  ILE   A CB  
364  C CG1 . ILE   A 47  ? 0.2641 0.2580 0.2865 -0.0315 0.0406  -0.0210 53  ILE   A CG1 
365  C CG2 . ILE   A 47  ? 0.2520 0.2463 0.2495 -0.0395 0.0316  -0.0133 53  ILE   A CG2 
366  C CD1 . ILE   A 47  ? 0.2709 0.2681 0.3031 -0.0237 0.0318  -0.0180 53  ILE   A CD1 
367  N N   . ALA   A 48  ? 0.2382 0.2207 0.2201 -0.0425 0.0343  -0.0201 54  ALA   A N   
368  C CA  . ALA   A 48  ? 0.2456 0.2251 0.2114 -0.0504 0.0336  -0.0197 54  ALA   A CA  
369  C C   . ALA   A 48  ? 0.2541 0.2359 0.2073 -0.0593 0.0323  -0.0159 54  ALA   A C   
370  O O   . ALA   A 48  ? 0.2494 0.2372 0.2079 -0.0576 0.0280  -0.0105 54  ALA   A O   
371  C CB  . ALA   A 48  ? 0.2464 0.2291 0.2134 -0.0475 0.0254  -0.0150 54  ALA   A CB  
372  N N   . ARG   A 49  ? 0.2677 0.2441 0.2035 -0.0695 0.0360  -0.0187 55  ARG   A N   
373  C CA  . ARG   A 49  ? 0.2849 0.2627 0.2053 -0.0800 0.0337  -0.0141 55  ARG   A CA  
374  C C   . ARG   A 49  ? 0.3056 0.2819 0.2129 -0.0871 0.0285  -0.0122 55  ARG   A C   
375  O O   . ARG   A 49  ? 0.3402 0.3088 0.2330 -0.0949 0.0341  -0.0183 55  ARG   A O   
376  C CB  . ARG   A 49  ? 0.3142 0.2861 0.2243 -0.0872 0.0444  -0.0203 55  ARG   A CB  
377  C CG  . ARG   A 49  ? 0.3165 0.2903 0.2436 -0.0793 0.0504  -0.0231 55  ARG   A CG  
378  C CD  . ARG   A 49  ? 0.3477 0.3298 0.2853 -0.0748 0.0431  -0.0148 55  ARG   A CD  
379  N NE  . ARG   A 49  ? 0.3136 0.2968 0.2663 -0.0689 0.0495  -0.0184 55  ARG   A NE  
380  C CZ  . ARG   A 49  ? 0.3168 0.3061 0.2828 -0.0631 0.0448  -0.0135 55  ARG   A CZ  
381  N NH1 . ARG   A 49  ? 0.3150 0.3093 0.2819 -0.0620 0.0348  -0.0052 55  ARG   A NH1 
382  N NH2 . ARG   A 49  ? 0.3185 0.3089 0.2989 -0.0581 0.0502  -0.0170 55  ARG   A NH2 
383  N N   . CYS   A 50  ? 0.2919 0.2756 0.2053 -0.0847 0.0182  -0.0039 56  CYS   A N   
384  C CA  . CYS   A 50  ? 0.3001 0.2843 0.2072 -0.0892 0.0123  -0.0013 56  CYS   A CA  
385  C C   . CYS   A 50  ? 0.2932 0.2874 0.2103 -0.0869 0.0013  0.0091  56  CYS   A C   
386  O O   . CYS   A 50  ? 0.2850 0.2847 0.2149 -0.0806 -0.0010 0.0134  56  CYS   A O   
387  C CB  . CYS   A 50  ? 0.3075 0.2872 0.2210 -0.0828 0.0161  -0.0076 56  CYS   A CB  
388  S SG  . CYS   A 50  ? 0.2787 0.2645 0.2153 -0.0680 0.0131  -0.0051 56  CYS   A SG  
389  N N   . ASP   A 51  ? 0.3147 0.3111 0.2286 -0.0914 -0.0049 0.0125  57  ASP   A N   
390  C CA  . ASP   A 51  ? 0.3211 0.3273 0.2485 -0.0884 -0.0142 0.0218  57  ASP   A CA  
391  C C   . ASP   A 51  ? 0.3192 0.3267 0.2564 -0.0823 -0.0141 0.0198  57  ASP   A C   
392  O O   . ASP   A 51  ? 0.3250 0.3393 0.2697 -0.0833 -0.0208 0.0260  57  ASP   A O   
393  C CB  . ASP   A 51  ? 0.3733 0.3837 0.2917 -0.1001 -0.0234 0.0303  57  ASP   A CB  
394  C CG  . ASP   A 51  ? 0.4661 0.4714 0.3674 -0.1105 -0.0238 0.0271  57  ASP   A CG  
395  O OD1 . ASP   A 51  ? 0.4784 0.4763 0.3757 -0.1083 -0.0162 0.0179  57  ASP   A OD1 
396  O OD2 . ASP   A 51  ? 0.5348 0.5431 0.4269 -0.1214 -0.0321 0.0340  57  ASP   A OD2 
397  N N   . CYS   A 52  ? 0.2884 0.2898 0.2274 -0.0758 -0.0069 0.0119  58  CYS   A N   
398  C CA  . CYS   A 52  ? 0.2701 0.2718 0.2170 -0.0704 -0.0067 0.0106  58  CYS   A CA  
399  C C   . CYS   A 52  ? 0.2676 0.2785 0.2311 -0.0638 -0.0112 0.0165  58  CYS   A C   
400  O O   . CYS   A 52  ? 0.2634 0.2778 0.2352 -0.0592 -0.0117 0.0188  58  CYS   A O   
401  C CB  . CYS   A 52  ? 0.2911 0.2852 0.2395 -0.0637 0.0005  0.0031  58  CYS   A CB  
402  S SG  . CYS   A 52  ? 0.3144 0.2962 0.2480 -0.0700 0.0077  -0.0054 58  CYS   A SG  
403  N N   . GLN   A 53  ? 0.2421 0.2564 0.2109 -0.0637 -0.0135 0.0186  59  GLN   A N   
404  C CA  . GLN   A 53  ? 0.2345 0.2563 0.2197 -0.0573 -0.0152 0.0223  59  GLN   A CA  
405  C C   . GLN   A 53  ? 0.2207 0.2391 0.2074 -0.0527 -0.0111 0.0182  59  GLN   A C   
406  O O   . GLN   A 53  ? 0.2174 0.2413 0.2148 -0.0497 -0.0114 0.0204  59  GLN   A O   
407  C CB  . GLN   A 53  ? 0.2500 0.2812 0.2441 -0.0619 -0.0220 0.0303  59  GLN   A CB  
408  C CG  . GLN   A 53  ? 0.3092 0.3454 0.3073 -0.0644 -0.0275 0.0369  59  GLN   A CG  
409  C CD  . GLN   A 53  ? 0.3284 0.3750 0.3409 -0.0674 -0.0350 0.0460  59  GLN   A CD  
410  O OE1 . GLN   A 53  ? 0.3598 0.4087 0.3662 -0.0765 -0.0419 0.0515  59  GLN   A OE1 
411  N NE2 . GLN   A 53  ? 0.2842 0.3371 0.3164 -0.0605 -0.0337 0.0476  59  GLN   A NE2 
412  N N   . THR   A 54  ? 0.2200 0.2291 0.1964 -0.0526 -0.0069 0.0123  60  THR   A N   
413  C CA  . THR   A 54  ? 0.2200 0.2247 0.1972 -0.0481 -0.0036 0.0093  60  THR   A CA  
414  C C   . THR   A 54  ? 0.2230 0.2201 0.1971 -0.0437 0.0000  0.0044  60  THR   A C   
415  O O   . THR   A 54  ? 0.2467 0.2400 0.2154 -0.0459 0.0017  0.0018  60  THR   A O   
416  C CB  . THR   A 54  ? 0.2662 0.2667 0.2368 -0.0534 -0.0033 0.0085  60  THR   A CB  
417  O OG1 . THR   A 54  ? 0.3342 0.3269 0.2937 -0.0585 -0.0016 0.0047  60  THR   A OG1 
418  C CG2 . THR   A 54  ? 0.2693 0.2781 0.2449 -0.0585 -0.0073 0.0137  60  THR   A CG2 
419  N N   . GLY   A 55  ? 0.2168 0.2120 0.1945 -0.0379 0.0013  0.0033  61  GLY   A N   
420  C CA  . GLY   A 55  ? 0.2176 0.2069 0.1957 -0.0332 0.0034  -0.0001 61  GLY   A CA  
421  C C   . GLY   A 55  ? 0.2044 0.1919 0.1845 -0.0286 0.0030  0.0003  61  GLY   A C   
422  O O   . GLY   A 55  ? 0.2146 0.2040 0.1938 -0.0299 0.0026  0.0023  61  GLY   A O   
423  N N   . VAL   A 56  ? 0.1938 0.1778 0.1764 -0.0242 0.0030  -0.0014 62  VAL   A N   
424  C CA  . VAL   A 56  ? 0.2005 0.1820 0.1831 -0.0208 0.0014  -0.0006 62  VAL   A CA  
425  C C   . VAL   A 56  ? 0.1947 0.1791 0.1829 -0.0167 0.0000  -0.0014 62  VAL   A C   
426  O O   . VAL   A 56  ? 0.1991 0.1834 0.1919 -0.0152 0.0005  -0.0030 62  VAL   A O   
427  C CB  . VAL   A 56  ? 0.2220 0.1946 0.2032 -0.0202 0.0013  -0.0010 62  VAL   A CB  
428  C CG1 . VAL   A 56  ? 0.2383 0.2079 0.2188 -0.0175 -0.0020 0.0012  62  VAL   A CG1 
429  C CG2 . VAL   A 56  ? 0.2374 0.2061 0.2129 -0.0249 0.0030  -0.0006 62  VAL   A CG2 
430  N N   . TYR   A 57  ? 0.1859 0.1723 0.1731 -0.0155 -0.0013 -0.0007 63  TYR   A N   
431  C CA  . TYR   A 57  ? 0.1764 0.1646 0.1678 -0.0123 -0.0029 -0.0019 63  TYR   A CA  
432  C C   . TYR   A 57  ? 0.1984 0.1823 0.1852 -0.0115 -0.0061 -0.0013 63  TYR   A C   
433  O O   . TYR   A 57  ? 0.2062 0.1868 0.1853 -0.0137 -0.0062 0.0004  63  TYR   A O   
434  C CB  . TYR   A 57  ? 0.1695 0.1641 0.1651 -0.0121 -0.0014 -0.0025 63  TYR   A CB  
435  C CG  . TYR   A 57  ? 0.1817 0.1773 0.1737 -0.0132 0.0002  -0.0028 63  TYR   A CG  
436  C CD1 . TYR   A 57  ? 0.1991 0.1961 0.1889 -0.0159 0.0026  -0.0014 63  TYR   A CD1 
437  C CD2 . TYR   A 57  ? 0.1944 0.1892 0.1852 -0.0121 0.0000  -0.0051 63  TYR   A CD2 
438  C CE1 . TYR   A 57  ? 0.2169 0.2152 0.2049 -0.0172 0.0059  -0.0023 63  TYR   A CE1 
439  C CE2 . TYR   A 57  ? 0.2038 0.1988 0.1905 -0.0139 0.0033  -0.0066 63  TYR   A CE2 
440  C CZ  . TYR   A 57  ? 0.2154 0.2122 0.2010 -0.0163 0.0068  -0.0052 63  TYR   A CZ  
441  O OH  . TYR   A 57  ? 0.2514 0.2486 0.2342 -0.0183 0.0117  -0.0073 63  TYR   A OH  
442  N N   . TYR   A 58  ? 0.1920 0.1759 0.1833 -0.0091 -0.0090 -0.0021 64  TYR   A N   
443  C CA  . TYR   A 58  ? 0.2032 0.1833 0.1896 -0.0093 -0.0137 -0.0008 64  TYR   A CA  
444  C C   . TYR   A 58  ? 0.2126 0.1948 0.1938 -0.0107 -0.0129 -0.0031 64  TYR   A C   
445  O O   . TYR   A 58  ? 0.2036 0.1899 0.1914 -0.0093 -0.0116 -0.0056 64  TYR   A O   
446  C CB  . TYR   A 58  ? 0.2070 0.1859 0.2022 -0.0065 -0.0184 -0.0001 64  TYR   A CB  
447  C CG  . TYR   A 58  ? 0.2292 0.2046 0.2187 -0.0078 -0.0251 0.0024  64  TYR   A CG  
448  C CD1 . TYR   A 58  ? 0.2408 0.2104 0.2222 -0.0099 -0.0282 0.0065  64  TYR   A CD1 
449  C CD2 . TYR   A 58  ? 0.2404 0.2178 0.2319 -0.0078 -0.0289 0.0012  64  TYR   A CD2 
450  C CE1 . TYR   A 58  ? 0.2628 0.2288 0.2366 -0.0124 -0.0354 0.0099  64  TYR   A CE1 
451  C CE2 . TYR   A 58  ? 0.2547 0.2286 0.2386 -0.0104 -0.0361 0.0039  64  TYR   A CE2 
452  C CZ  . TYR   A 58  ? 0.2791 0.2474 0.2535 -0.0130 -0.0396 0.0085  64  TYR   A CZ  
453  O OH  . TYR   A 58  ? 0.3261 0.2905 0.2911 -0.0168 -0.0478 0.0123  64  TYR   A OH  
454  N N   . CYS   A 59  ? 0.2147 0.1933 0.1840 -0.0140 -0.0136 -0.0023 65  CYS   A N   
455  C CA  . CYS   A 59  ? 0.2226 0.2014 0.1846 -0.0165 -0.0113 -0.0055 65  CYS   A CA  
456  C C   . CYS   A 59  ? 0.2477 0.2215 0.2000 -0.0192 -0.0179 -0.0044 65  CYS   A C   
457  O O   . CYS   A 59  ? 0.2630 0.2317 0.2036 -0.0226 -0.0204 -0.0011 65  CYS   A O   
458  C CB  . CYS   A 59  ? 0.2350 0.2138 0.1899 -0.0196 -0.0054 -0.0058 65  CYS   A CB  
459  S SG  . CYS   A 59  ? 0.2774 0.2553 0.2232 -0.0234 0.0002  -0.0112 65  CYS   A SG  
460  N N   A SER   A 60  ? 0.2473 0.2223 0.2037 -0.0183 -0.0211 -0.0066 66  SER   A N   
461  N N   B SER   A 60  ? 0.2442 0.2193 0.2009 -0.0183 -0.0211 -0.0066 66  SER   A N   
462  C CA  A SER   A 60  ? 0.2627 0.2335 0.2107 -0.0216 -0.0290 -0.0049 66  SER   A CA  
463  C CA  B SER   A 60  ? 0.2560 0.2269 0.2043 -0.0215 -0.0290 -0.0049 66  SER   A CA  
464  C C   A SER   A 60  ? 0.2750 0.2408 0.2030 -0.0284 -0.0278 -0.0069 66  SER   A C   
465  C C   B SER   A 60  ? 0.2662 0.2319 0.1943 -0.0282 -0.0276 -0.0064 66  SER   A C   
466  O O   A SER   A 60  ? 0.2815 0.2423 0.1972 -0.0330 -0.0352 -0.0034 66  SER   A O   
467  O O   B SER   A 60  ? 0.2659 0.2264 0.1819 -0.0324 -0.0344 -0.0019 66  SER   A O   
468  C CB  A SER   A 60  ? 0.2806 0.2544 0.2390 -0.0196 -0.0327 -0.0071 66  SER   A CB  
469  C CB  B SER   A 60  ? 0.2727 0.2463 0.2296 -0.0201 -0.0321 -0.0077 66  SER   A CB  
470  O OG  A SER   A 60  ? 0.3013 0.2762 0.2576 -0.0210 -0.0271 -0.0133 66  SER   A OG  
471  O OG  B SER   A 60  ? 0.2927 0.2633 0.2446 -0.0231 -0.0418 -0.0047 66  SER   A OG  
472  N N   . SER   A 61  ? 0.2662 0.2332 0.1912 -0.0296 -0.0184 -0.0124 67  SER   A N   
473  C CA  . SER   A 61  ? 0.2772 0.2392 0.1832 -0.0365 -0.0143 -0.0156 67  SER   A CA  
474  C C   . SER   A 61  ? 0.2959 0.2541 0.1896 -0.0402 -0.0134 -0.0112 67  SER   A C   
475  O O   . SER   A 61  ? 0.3180 0.2712 0.1933 -0.0471 -0.0103 -0.0131 67  SER   A O   
476  C CB  . SER   A 61  ? 0.2831 0.2473 0.1929 -0.0364 -0.0034 -0.0235 67  SER   A CB  
477  O OG  . SER   A 61  ? 0.2907 0.2602 0.2129 -0.0324 0.0035  -0.0230 67  SER   A OG  
478  N N   . ARG   A 62  ? 0.2781 0.2381 0.1808 -0.0363 -0.0153 -0.0057 68  ARG   A N   
479  C CA  . ARG   A 62  ? 0.2882 0.2438 0.1804 -0.0397 -0.0158 -0.0006 68  ARG   A CA  
480  C C   . ARG   A 62  ? 0.3038 0.2562 0.1997 -0.0378 -0.0261 0.0072  68  ARG   A C   
481  O O   . ARG   A 62  ? 0.3245 0.2724 0.2137 -0.0402 -0.0277 0.0126  68  ARG   A O   
482  C CB  . ARG   A 62  ? 0.3004 0.2600 0.2002 -0.0378 -0.0071 -0.0016 68  ARG   A CB  
483  C CG  . ARG   A 62  ? 0.3197 0.2826 0.2189 -0.0396 0.0034  -0.0085 68  ARG   A CG  
484  C CD  . ARG   A 62  ? 0.3554 0.3125 0.2342 -0.0475 0.0078  -0.0094 68  ARG   A CD  
485  N NE  . ARG   A 62  ? 0.3831 0.3433 0.2640 -0.0491 0.0199  -0.0166 68  ARG   A NE  
486  C CZ  . ARG   A 62  ? 0.3988 0.3576 0.2754 -0.0513 0.0243  -0.0237 68  ARG   A CZ  
487  N NH1 . ARG   A 62  ? 0.3891 0.3440 0.2582 -0.0525 0.0166  -0.0243 68  ARG   A NH1 
488  N NH2 . ARG   A 62  ? 0.4193 0.3806 0.3007 -0.0524 0.0365  -0.0304 68  ARG   A NH2 
489  N N   . ARG   A 63  ? 0.3011 0.2557 0.2096 -0.0335 -0.0328 0.0082  69  ARG   A N   
490  C CA  . ARG   A 63  ? 0.3103 0.2631 0.2292 -0.0301 -0.0412 0.0149  69  ARG   A CA  
491  C C   . ARG   A 63  ? 0.3188 0.2707 0.2440 -0.0276 -0.0370 0.0171  69  ARG   A C   
492  O O   . ARG   A 63  ? 0.3413 0.2876 0.2652 -0.0284 -0.0418 0.0234  69  ARG   A O   
493  C CB  . ARG   A 63  ? 0.3432 0.2896 0.2508 -0.0351 -0.0522 0.0218  69  ARG   A CB  
494  C CG  . ARG   A 63  ? 0.4076 0.3547 0.3085 -0.0386 -0.0573 0.0194  69  ARG   A CG  
495  C CD  . ARG   A 63  ? 0.4564 0.4091 0.3777 -0.0328 -0.0614 0.0185  69  ARG   A CD  
496  N NE  . ARG   A 63  ? 0.5056 0.4575 0.4224 -0.0368 -0.0713 0.0199  69  ARG   A NE  
497  C CZ  . ARG   A 63  ? 0.5142 0.4686 0.4282 -0.0387 -0.0695 0.0133  69  ARG   A CZ  
498  N NH1 . ARG   A 63  ? 0.4672 0.4248 0.3834 -0.0364 -0.0581 0.0053  69  ARG   A NH1 
499  N NH2 . ARG   A 63  ? 0.5498 0.5033 0.4594 -0.0432 -0.0795 0.0151  69  ARG   A NH2 
500  N N   . LYS   A 64  ? 0.2905 0.2476 0.2221 -0.0252 -0.0284 0.0121  70  LYS   A N   
501  C CA  . LYS   A 64  ? 0.2927 0.2490 0.2283 -0.0242 -0.0242 0.0134  70  LYS   A CA  
502  C C   . LYS   A 64  ? 0.2569 0.2193 0.2060 -0.0201 -0.0190 0.0094  70  LYS   A C   
503  O O   . LYS   A 64  ? 0.2442 0.2121 0.1976 -0.0187 -0.0165 0.0054  70  LYS   A O   
504  C CB  . LYS   A 64  ? 0.3637 0.3191 0.2866 -0.0293 -0.0182 0.0129  70  LYS   A CB  
505  C CG  . LYS   A 64  ? 0.4697 0.4171 0.3773 -0.0347 -0.0222 0.0186  70  LYS   A CG  
506  C CD  . LYS   A 64  ? 0.5648 0.5123 0.4604 -0.0401 -0.0144 0.0169  70  LYS   A CD  
507  C CE  . LYS   A 64  ? 0.6541 0.5932 0.5319 -0.0468 -0.0179 0.0226  70  LYS   A CE  
508  N NZ  . LYS   A 64  ? 0.7063 0.6412 0.5750 -0.0489 -0.0269 0.0255  70  LYS   A NZ  
509  N N   . HIS   A 65  ? 0.2444 0.2054 0.1993 -0.0190 -0.0173 0.0106  71  HIS   A N   
510  C CA  . HIS   A 65  ? 0.2330 0.1988 0.1965 -0.0172 -0.0124 0.0074  71  HIS   A CA  
511  C C   . HIS   A 65  ? 0.2478 0.2153 0.2062 -0.0207 -0.0074 0.0072  71  HIS   A C   
512  O O   . HIS   A 65  ? 0.2794 0.2420 0.2302 -0.0239 -0.0074 0.0100  71  HIS   A O   
513  C CB  . HIS   A 65  ? 0.2379 0.2001 0.2103 -0.0149 -0.0131 0.0079  71  HIS   A CB  
514  C CG  . HIS   A 65  ? 0.2411 0.2025 0.2228 -0.0112 -0.0173 0.0083  71  HIS   A CG  
515  N ND1 . HIS   A 65  ? 0.2670 0.2331 0.2589 -0.0084 -0.0155 0.0049  71  HIS   A ND1 
516  C CD2 . HIS   A 65  ? 0.2524 0.2089 0.2359 -0.0103 -0.0236 0.0124  71  HIS   A CD2 
517  C CE1 . HIS   A 65  ? 0.2448 0.2093 0.2452 -0.0056 -0.0201 0.0065  71  HIS   A CE1 
518  N NE2 . HIS   A 65  ? 0.2864 0.2456 0.2829 -0.0065 -0.0257 0.0112  71  HIS   A NE2 
519  N N   . TYR   A 66  ? 0.2236 0.1981 0.1871 -0.0205 -0.0034 0.0045  72  TYR   A N   
520  C CA  . TYR   A 66  ? 0.2230 0.2010 0.1854 -0.0237 0.0008  0.0047  72  TYR   A CA  
521  C C   . TYR   A 66  ? 0.2135 0.1953 0.1831 -0.0240 0.0019  0.0041  72  TYR   A C   
522  O O   . TYR   A 66  ? 0.2187 0.2043 0.1947 -0.0219 0.0015  0.0026  72  TYR   A O   
523  C CB  . TYR   A 66  ? 0.2323 0.2164 0.1963 -0.0240 0.0043  0.0026  72  TYR   A CB  
524  C CG  . TYR   A 66  ? 0.2592 0.2396 0.2129 -0.0259 0.0050  0.0022  72  TYR   A CG  
525  C CD1 . TYR   A 66  ? 0.2810 0.2585 0.2258 -0.0302 0.0075  0.0039  72  TYR   A CD1 
526  C CD2 . TYR   A 66  ? 0.2758 0.2560 0.2281 -0.0244 0.0038  -0.0004 72  TYR   A CD2 
527  C CE1 . TYR   A 66  ? 0.3001 0.2735 0.2325 -0.0334 0.0087  0.0033  72  TYR   A CE1 
528  C CE2 . TYR   A 66  ? 0.2976 0.2737 0.2375 -0.0277 0.0044  -0.0013 72  TYR   A CE2 
529  C CZ  . TYR   A 66  ? 0.3177 0.2903 0.2470 -0.0324 0.0071  0.0006  72  TYR   A CZ  
530  O OH  . TYR   A 66  ? 0.3476 0.3157 0.2621 -0.0371 0.0086  -0.0006 72  TYR   A OH  
531  N N   . PRO   A 67  ? 0.2175 0.1980 0.1849 -0.0276 0.0032  0.0055  73  PRO   A N   
532  C CA  . PRO   A 67  ? 0.2187 0.2029 0.1904 -0.0298 0.0037  0.0051  73  PRO   A CA  
533  C C   . PRO   A 67  ? 0.2299 0.2240 0.2085 -0.0308 0.0051  0.0060  73  PRO   A C   
534  O O   . PRO   A 67  ? 0.2556 0.2522 0.2345 -0.0320 0.0076  0.0069  73  PRO   A O   
535  C CB  . PRO   A 67  ? 0.2309 0.2098 0.1975 -0.0342 0.0043  0.0063  73  PRO   A CB  
536  C CG  . PRO   A 67  ? 0.2420 0.2189 0.2037 -0.0351 0.0053  0.0083  73  PRO   A CG  
537  C CD  . PRO   A 67  ? 0.2268 0.2024 0.1870 -0.0309 0.0040  0.0077  73  PRO   A CD  
538  N N   . VAL   A 68  ? 0.2125 0.2118 0.1971 -0.0307 0.0039  0.0061  74  VAL   A N   
539  C CA  . VAL   A 68  ? 0.2103 0.2188 0.2046 -0.0311 0.0043  0.0081  74  VAL   A CA  
540  C C   . VAL   A 68  ? 0.2009 0.2138 0.1984 -0.0349 0.0014  0.0106  74  VAL   A C   
541  O O   . VAL   A 68  ? 0.2136 0.2226 0.2054 -0.0363 -0.0001 0.0096  74  VAL   A O   
542  C CB  . VAL   A 68  ? 0.2381 0.2492 0.2386 -0.0263 0.0048  0.0067  74  VAL   A CB  
543  C CG1 . VAL   A 68  ? 0.2660 0.2744 0.2634 -0.0243 0.0080  0.0043  74  VAL   A CG1 
544  C CG2 . VAL   A 68  ? 0.2473 0.2551 0.2458 -0.0241 0.0028  0.0052  74  VAL   A CG2 
545  N N   . SER   A 69  ? 0.1891 0.2107 0.1970 -0.0368 0.0005  0.0142  75  SER   A N   
546  C CA  . SER   A 69  ? 0.1912 0.2188 0.2047 -0.0403 -0.0039 0.0183  75  SER   A CA  
547  C C   . SER   A 69  ? 0.1801 0.2130 0.2055 -0.0358 -0.0042 0.0197  75  SER   A C   
548  O O   . SER   A 69  ? 0.2073 0.2422 0.2410 -0.0315 -0.0005 0.0182  75  SER   A O   
549  C CB  . SER   A 69  ? 0.2204 0.2553 0.2421 -0.0449 -0.0057 0.0226  75  SER   A CB  
550  O OG  . SER   A 69  ? 0.3230 0.3529 0.3342 -0.0499 -0.0055 0.0214  75  SER   A OG  
551  N N   . PHE   A 70  ? 0.1710 0.2045 0.1957 -0.0370 -0.0078 0.0218  76  PHE   A N   
552  C CA  . PHE   A 70  ? 0.1793 0.2166 0.2153 -0.0330 -0.0084 0.0235  76  PHE   A CA  
553  C C   . PHE   A 70  ? 0.1886 0.2318 0.2310 -0.0371 -0.0145 0.0305  76  PHE   A C   
554  O O   . PHE   A 70  ? 0.1971 0.2395 0.2296 -0.0437 -0.0183 0.0327  76  PHE   A O   
555  C CB  . PHE   A 70  ? 0.1787 0.2094 0.2076 -0.0291 -0.0062 0.0188  76  PHE   A CB  
556  C CG  . PHE   A 70  ? 0.1839 0.2086 0.1989 -0.0324 -0.0069 0.0169  76  PHE   A CG  
557  C CD1 . PHE   A 70  ? 0.1975 0.2153 0.2020 -0.0327 -0.0044 0.0126  76  PHE   A CD1 
558  C CD2 . PHE   A 70  ? 0.2056 0.2310 0.2187 -0.0354 -0.0095 0.0195  76  PHE   A CD2 
559  C CE1 . PHE   A 70  ? 0.2176 0.2293 0.2119 -0.0355 -0.0035 0.0100  76  PHE   A CE1 
560  C CE2 . PHE   A 70  ? 0.2118 0.2312 0.2124 -0.0388 -0.0081 0.0165  76  PHE   A CE2 
561  C CZ  . PHE   A 70  ? 0.2153 0.2279 0.2075 -0.0386 -0.0047 0.0114  76  PHE   A CZ  
562  N N   . SER   A 71  ? 0.1781 0.2268 0.2369 -0.0337 -0.0155 0.0341  77  SER   A N   
563  C CA  . SER   A 71  ? 0.1928 0.2474 0.2600 -0.0376 -0.0226 0.0426  77  SER   A CA  
564  C C   . SER   A 71  ? 0.2019 0.2519 0.2567 -0.0404 -0.0250 0.0434  77  SER   A C   
565  O O   . SER   A 71  ? 0.2159 0.2594 0.2621 -0.0372 -0.0205 0.0372  77  SER   A O   
566  C CB  . SER   A 71  ? 0.1885 0.2497 0.2800 -0.0327 -0.0225 0.0466  77  SER   A CB  
567  O OG  . SER   A 71  ? 0.2227 0.2795 0.3167 -0.0265 -0.0177 0.0417  77  SER   A OG  
568  N N   . LYS   A 72  ? 0.2069 0.2603 0.2608 -0.0470 -0.0323 0.0513  78  LYS   A N   
569  C CA  . LYS   A 72  ? 0.2235 0.2725 0.2654 -0.0506 -0.0339 0.0524  78  LYS   A CA  
570  C C   . LYS   A 72  ? 0.2322 0.2815 0.2873 -0.0441 -0.0324 0.0532  78  LYS   A C   
571  O O   . LYS   A 72  ? 0.2406 0.2949 0.3160 -0.0390 -0.0328 0.0561  78  LYS   A O   
572  C CB  . LYS   A 72  ? 0.2615 0.3140 0.2980 -0.0607 -0.0429 0.0617  78  LYS   A CB  
573  C CG  . LYS   A 72  ? 0.3134 0.3634 0.3323 -0.0687 -0.0439 0.0594  78  LYS   A CG  
574  C CD  . LYS   A 72  ? 0.3840 0.4368 0.3944 -0.0804 -0.0535 0.0684  78  LYS   A CD  
575  C CE  . LYS   A 72  ? 0.4622 0.5107 0.4529 -0.0891 -0.0533 0.0642  78  LYS   A CE  
576  N NZ  . LYS   A 72  ? 0.5136 0.5620 0.4884 -0.1026 -0.0617 0.0710  78  LYS   A NZ  
577  N N   . PRO   A 73  ? 0.2255 0.2694 0.2706 -0.0446 -0.0301 0.0506  79  PRO   A N   
578  C CA  . PRO   A 73  ? 0.2275 0.2709 0.2847 -0.0389 -0.0286 0.0511  79  PRO   A CA  
579  C C   . PRO   A 73  ? 0.2333 0.2827 0.3089 -0.0393 -0.0351 0.0614  79  PRO   A C   
580  O O   . PRO   A 73  ? 0.2408 0.2928 0.3122 -0.0468 -0.0423 0.0701  79  PRO   A O   
581  C CB  . PRO   A 73  ? 0.2521 0.2898 0.2942 -0.0423 -0.0264 0.0486  79  PRO   A CB  
582  C CG  . PRO   A 73  ? 0.2760 0.3094 0.2998 -0.0462 -0.0231 0.0424  79  PRO   A CG  
583  C CD  . PRO   A 73  ? 0.2449 0.2824 0.2683 -0.0503 -0.0277 0.0464  79  PRO   A CD  
584  N N   . SER   A 74  ? 0.2084 0.2594 0.3040 -0.0318 -0.0326 0.0606  80  SER   A N   
585  C CA  . SER   A 74  ? 0.2274 0.2840 0.3451 -0.0310 -0.0381 0.0704  80  SER   A CA  
586  C C   . SER   A 74  ? 0.2234 0.2778 0.3592 -0.0232 -0.0335 0.0676  80  SER   A C   
587  O O   . SER   A 74  ? 0.2070 0.2560 0.3361 -0.0191 -0.0266 0.0580  80  SER   A O   
588  C CB  . SER   A 74  ? 0.2901 0.3542 0.4207 -0.0318 -0.0416 0.0751  80  SER   A CB  
589  O OG  . SER   A 74  ? 0.3739 0.4386 0.5154 -0.0249 -0.0340 0.0674  80  SER   A OG  
590  N N   . LEU   A 75  ? 0.2147 0.2731 0.3736 -0.0218 -0.0380 0.0766  81  LEU   A N   
591  C CA  . LEU   A 75  ? 0.2301 0.2858 0.4087 -0.0151 -0.0339 0.0748  81  LEU   A CA  
592  C C   . LEU   A 75  ? 0.2476 0.3064 0.4458 -0.0091 -0.0281 0.0702  81  LEU   A C   
593  O O   . LEU   A 75  ? 0.2560 0.3221 0.4720 -0.0095 -0.0320 0.0775  81  LEU   A O   
594  C CB  . LEU   A 75  ? 0.2322 0.2896 0.4262 -0.0175 -0.0422 0.0881  81  LEU   A CB  
595  C CG  . LEU   A 75  ? 0.2441 0.2969 0.4568 -0.0116 -0.0385 0.0870  81  LEU   A CG  
596  C CD1 . LEU   A 75  ? 0.2466 0.2918 0.4419 -0.0113 -0.0333 0.0784  81  LEU   A CD1 
597  C CD2 . LEU   A 75  ? 0.2602 0.3149 0.4905 -0.0140 -0.0476 0.1018  81  LEU   A CD2 
598  N N   . ILE   A 76  ? 0.2493 0.3030 0.4420 -0.0045 -0.0186 0.0577  82  ILE   A N   
599  C CA  . ILE   A 76  ? 0.2545 0.3099 0.4595 -0.0002 -0.0111 0.0511  82  ILE   A CA  
600  C C   . ILE   A 76  ? 0.2659 0.3159 0.4853 0.0055  -0.0032 0.0441  82  ILE   A C   
601  O O   . ILE   A 76  ? 0.2557 0.2988 0.4635 0.0060  -0.0012 0.0385  82  ILE   A O   
602  C CB  . ILE   A 76  ? 0.2803 0.3335 0.4609 -0.0018 -0.0070 0.0424  82  ILE   A CB  
603  C CG1 . ILE   A 76  ? 0.3061 0.3638 0.4737 -0.0078 -0.0140 0.0486  82  ILE   A CG1 
604  C CG2 . ILE   A 76  ? 0.2960 0.3488 0.4827 0.0017  0.0026  0.0335  82  ILE   A CG2 
605  C CD1 . ILE   A 76  ? 0.3464 0.4012 0.4922 -0.0096 -0.0110 0.0417  82  ILE   A CD1 
606  N N   . PHE   A 77  ? 0.2686 0.3215 0.5133 0.0095  0.0021  0.0433  83  PHE   A N   
607  C CA  . PHE   A 77  ? 0.2935 0.3401 0.5513 0.0143  0.0113  0.0349  83  PHE   A CA  
608  C C   . PHE   A 77  ? 0.3149 0.3560 0.5524 0.0142  0.0202  0.0212  83  PHE   A C   
609  O O   . PHE   A 77  ? 0.3536 0.3981 0.5855 0.0131  0.0235  0.0185  83  PHE   A O   
610  C CB  . PHE   A 77  ? 0.3037 0.3545 0.5974 0.0185  0.0157  0.0376  83  PHE   A CB  
611  C CG  . PHE   A 77  ? 0.3312 0.3737 0.6386 0.0229  0.0255  0.0286  83  PHE   A CG  
612  C CD1 . PHE   A 77  ? 0.3539 0.3912 0.6694 0.0241  0.0221  0.0322  83  PHE   A CD1 
613  C CD2 . PHE   A 77  ? 0.3533 0.3921 0.6621 0.0248  0.0385  0.0158  83  PHE   A CD2 
614  C CE1 . PHE   A 77  ? 0.3703 0.3987 0.6968 0.0274  0.0313  0.0229  83  PHE   A CE1 
615  C CE2 . PHE   A 77  ? 0.3664 0.3964 0.6858 0.0277  0.0482  0.0063  83  PHE   A CE2 
616  C CZ  . PHE   A 77  ? 0.3695 0.3943 0.6980 0.0291  0.0444  0.0097  83  PHE   A CZ  
617  N N   . VAL   A 78  ? 0.3000 0.3326 0.5254 0.0146  0.0234  0.0133  84  VAL   A N   
618  C CA  . VAL   A 78  ? 0.3066 0.3334 0.5117 0.0136  0.0305  0.0011  84  VAL   A CA  
619  C C   . VAL   A 78  ? 0.3016 0.3208 0.5167 0.0159  0.0402  -0.0088 84  VAL   A C   
620  O O   . VAL   A 78  ? 0.3152 0.3306 0.5429 0.0177  0.0395  -0.0078 84  VAL   A O   
621  C CB  . VAL   A 78  ? 0.3285 0.3522 0.5056 0.0105  0.0249  -0.0002 84  VAL   A CB  
622  C CG1 . VAL   A 78  ? 0.3337 0.3635 0.4999 0.0077  0.0178  0.0074  84  VAL   A CG1 
623  C CG2 . VAL   A 78  ? 0.3358 0.3555 0.5142 0.0107  0.0210  0.0016  84  VAL   A CG2 
624  N N   . GLU   A 79  ? 0.3027 0.3188 0.5100 0.0151  0.0494  -0.0189 85  GLU   A N   
625  C CA  . GLU   A 79  ? 0.3114 0.3192 0.5252 0.0159  0.0603  -0.0301 85  GLU   A CA  
626  C C   . GLU   A 79  ? 0.3187 0.3176 0.5159 0.0139  0.0584  -0.0362 85  GLU   A C   
627  O O   . GLU   A 79  ? 0.3126 0.3122 0.4909 0.0118  0.0499  -0.0329 85  GLU   A O   
628  C CB  . GLU   A 79  ? 0.3591 0.3655 0.5634 0.0136  0.0708  -0.0394 85  GLU   A CB  
629  C CG  . GLU   A 79  ? 0.4373 0.4519 0.6646 0.0159  0.0756  -0.0354 85  GLU   A CG  
630  C CD  . GLU   A 79  ? 0.5658 0.5803 0.8286 0.0205  0.0819  -0.0352 85  GLU   A CD  
631  O OE1 . GLU   A 79  ? 0.5878 0.6112 0.8760 0.0237  0.0770  -0.0243 85  GLU   A OE1 
632  O OE2 . GLU   A 79  ? 0.6080 0.6133 0.8737 0.0207  0.0912  -0.0457 85  GLU   A OE2 
633  N N   . ALA   A 80  ? 0.3259 0.3165 0.5312 0.0142  0.0669  -0.0455 86  ALA   A N   
634  C CA  . ALA   A 80  ? 0.3412 0.3230 0.5320 0.0115  0.0658  -0.0524 86  ALA   A CA  
635  C C   . ALA   A 80  ? 0.3642 0.3432 0.5227 0.0062  0.0648  -0.0587 86  ALA   A C   
636  O O   . ALA   A 80  ? 0.3699 0.3502 0.5186 0.0044  0.0698  -0.0620 86  ALA   A O   
637  C CB  . ALA   A 80  ? 0.3416 0.3142 0.5466 0.0119  0.0770  -0.0628 86  ALA   A CB  
638  N N   . SER   A 81  ? 0.3653 0.3406 0.5085 0.0036  0.0579  -0.0597 87  SER   A N   
639  C CA  . SER   A 81  ? 0.3839 0.3557 0.4986 -0.0016 0.0551  -0.0650 87  SER   A CA  
640  C C   . SER   A 81  ? 0.4072 0.3685 0.5150 -0.0057 0.0590  -0.0759 87  SER   A C   
641  O O   . SER   A 81  ? 0.4092 0.3658 0.5350 -0.0040 0.0654  -0.0800 87  SER   A O   
642  C CB  . SER   A 81  ? 0.3742 0.3514 0.4786 -0.0016 0.0433  -0.0565 87  SER   A CB  
643  O OG  . SER   A 81  ? 0.3708 0.3474 0.4845 -0.0004 0.0381  -0.0534 87  SER   A OG  
644  N N   . GLU   A 82  ? 0.4328 0.3898 0.5154 -0.0115 0.0553  -0.0808 88  GLU   A N   
645  C CA  . GLU   A 82  ? 0.4593 0.4060 0.5321 -0.0172 0.0583  -0.0916 88  GLU   A CA  
646  C C   . GLU   A 82  ? 0.4595 0.4031 0.5481 -0.0156 0.0560  -0.0918 88  GLU   A C   
647  O O   . GLU   A 82  ? 0.4499 0.3848 0.5442 -0.0177 0.0638  -0.1011 88  GLU   A O   
648  C CB  . GLU   A 82  ? 0.5218 0.4661 0.5656 -0.0241 0.0509  -0.0937 88  GLU   A CB  
649  C CG  . GLU   A 82  ? 0.6203 0.5533 0.6491 -0.0320 0.0547  -0.1058 88  GLU   A CG  
650  C CD  . GLU   A 82  ? 0.7609 0.6911 0.7600 -0.0401 0.0469  -0.1072 88  GLU   A CD  
651  O OE1 . GLU   A 82  ? 0.7839 0.7201 0.7736 -0.0393 0.0408  -0.0997 88  GLU   A OE1 
652  O OE2 . GLU   A 82  ? 0.8215 0.7432 0.8071 -0.0476 0.0463  -0.1155 88  GLU   A OE2 
653  N N   . TYR   A 83  ? 0.4636 0.4138 0.5592 -0.0125 0.0461  -0.0820 89  TYR   A N   
654  C CA  . TYR   A 83  ? 0.4706 0.4184 0.5796 -0.0118 0.0431  -0.0810 89  TYR   A CA  
655  C C   . TYR   A 83  ? 0.4596 0.4134 0.5920 -0.0055 0.0412  -0.0705 89  TYR   A C   
656  O O   . TYR   A 83  ? 0.4671 0.4201 0.6087 -0.0053 0.0370  -0.0675 89  TYR   A O   
657  C CB  . TYR   A 83  ? 0.4899 0.4391 0.5846 -0.0156 0.0325  -0.0794 89  TYR   A CB  
658  C CG  . TYR   A 83  ? 0.5311 0.4739 0.6020 -0.0231 0.0319  -0.0884 89  TYR   A CG  
659  C CD1 . TYR   A 83  ? 0.5569 0.4892 0.6241 -0.0283 0.0378  -0.0998 89  TYR   A CD1 
660  C CD2 . TYR   A 83  ? 0.5601 0.5067 0.6118 -0.0256 0.0253  -0.0855 89  TYR   A CD2 
661  C CE1 . TYR   A 83  ? 0.5884 0.5142 0.6308 -0.0368 0.0366  -0.1079 89  TYR   A CE1 
662  C CE2 . TYR   A 83  ? 0.5877 0.5283 0.6164 -0.0334 0.0235  -0.0925 89  TYR   A CE2 
663  C CZ  . TYR   A 83  ? 0.6119 0.5422 0.6348 -0.0394 0.0289  -0.1036 89  TYR   A CZ  
664  O OH  . TYR   A 83  ? 0.6610 0.5846 0.6585 -0.0488 0.0266  -0.1105 89  TYR   A OH  
665  N N   . TYR   A 84  ? 0.4440 0.4037 0.5861 -0.0013 0.0438  -0.0646 90  TYR   A N   
666  C CA  . TYR   A 84  ? 0.4338 0.4000 0.5957 0.0035  0.0403  -0.0530 90  TYR   A CA  
667  C C   . TYR   A 84  ? 0.3971 0.3653 0.5778 0.0075  0.0471  -0.0511 90  TYR   A C   
668  O O   . TYR   A 84  ? 0.4136 0.3826 0.5876 0.0070  0.0526  -0.0555 90  TYR   A O   
669  C CB  . TYR   A 84  ? 0.4506 0.4256 0.6014 0.0036  0.0316  -0.0438 90  TYR   A CB  
670  C CG  . TYR   A 84  ? 0.4975 0.4740 0.6488 0.0028  0.0243  -0.0383 90  TYR   A CG  
671  C CD1 . TYR   A 84  ? 0.5335 0.5112 0.6684 -0.0002 0.0189  -0.0397 90  TYR   A CD1 
672  C CD2 . TYR   A 84  ? 0.5187 0.4956 0.6883 0.0046  0.0230  -0.0314 90  TYR   A CD2 
673  C CE1 . TYR   A 84  ? 0.5570 0.5366 0.6944 -0.0011 0.0135  -0.0351 90  TYR   A CE1 
674  C CE2 . TYR   A 84  ? 0.5402 0.5184 0.7097 0.0030  0.0173  -0.0265 90  TYR   A CE2 
675  C CZ  . TYR   A 84  ? 0.5681 0.5478 0.7219 0.0002  0.0132  -0.0289 90  TYR   A CZ  
676  O OH  . TYR   A 84  ? 0.6089 0.5904 0.7646 -0.0014 0.0089  -0.0244 90  TYR   A OH  
677  N N   . PRO   A 85  ? 0.3519 0.3213 0.5573 0.0112  0.0465  -0.0436 91  PRO   A N   
678  C CA  . PRO   A 85  ? 0.3290 0.3010 0.5568 0.0152  0.0524  -0.0409 91  PRO   A CA  
679  C C   . PRO   A 85  ? 0.3390 0.3218 0.5666 0.0167  0.0475  -0.0309 91  PRO   A C   
680  O O   . PRO   A 85  ? 0.3550 0.3430 0.5664 0.0148  0.0393  -0.0249 91  PRO   A O   
681  C CB  . PRO   A 85  ? 0.3234 0.2928 0.5777 0.0181  0.0510  -0.0345 91  PRO   A CB  
682  C CG  . PRO   A 85  ? 0.3387 0.3098 0.5817 0.0157  0.0409  -0.0276 91  PRO   A CG  
683  C CD  . PRO   A 85  ? 0.3373 0.3052 0.5528 0.0114  0.0408  -0.0373 91  PRO   A CD  
684  N N   . ALA   A 86  ? 0.3259 0.3120 0.5733 0.0198  0.0532  -0.0295 92  ALA   A N   
685  C CA  . ALA   A 86  ? 0.3308 0.3272 0.5830 0.0210  0.0486  -0.0196 92  ALA   A CA  
686  C C   . ALA   A 86  ? 0.3306 0.3317 0.5949 0.0219  0.0381  -0.0052 92  ALA   A C   
687  O O   . ALA   A 86  ? 0.3487 0.3459 0.6324 0.0238  0.0380  -0.0023 92  ALA   A O   
688  C CB  . ALA   A 86  ? 0.3185 0.3171 0.5944 0.0242  0.0577  -0.0216 92  ALA   A CB  
689  N N   . ARG   A 87  ? 0.3095 0.3184 0.5624 0.0199  0.0296  0.0037  93  ARG   A N   
690  C CA  . ARG   A 87  ? 0.2918 0.3048 0.5515 0.0189  0.0195  0.0174  93  ARG   A CA  
691  C C   . ARG   A 87  ? 0.2729 0.2947 0.5227 0.0163  0.0126  0.0257  93  ARG   A C   
692  O O   . ARG   A 87  ? 0.2789 0.3032 0.5166 0.0157  0.0158  0.0205  93  ARG   A O   
693  C CB  . ARG   A 87  ? 0.3112 0.3188 0.5572 0.0164  0.0157  0.0169  93  ARG   A CB  
694  C CG  . ARG   A 87  ? 0.3624 0.3682 0.5786 0.0133  0.0157  0.0090  93  ARG   A CG  
695  C CD  . ARG   A 87  ? 0.4346 0.4448 0.6355 0.0096  0.0074  0.0173  93  ARG   A CD  
696  N NE  . ARG   A 87  ? 0.4460 0.4544 0.6239 0.0072  0.0069  0.0111  93  ARG   A NE  
697  C CZ  . ARG   A 87  ? 0.4643 0.4729 0.6269 0.0069  0.0093  0.0041  93  ARG   A CZ  
698  N NH1 . ARG   A 87  ? 0.4467 0.4539 0.5922 0.0049  0.0079  0.0001  93  ARG   A NH1 
699  N NH2 . ARG   A 87  ? 0.4649 0.4750 0.6307 0.0085  0.0134  0.0013  93  ARG   A NH2 
700  N N   . TYR   A 88  ? 0.2629 0.2889 0.5163 0.0140  0.0032  0.0386  94  TYR   A N   
701  C CA  . TYR   A 88  ? 0.2617 0.2949 0.5015 0.0099  -0.0039 0.0459  94  TYR   A CA  
702  C C   . TYR   A 88  ? 0.2426 0.2728 0.4538 0.0060  -0.0058 0.0425  94  TYR   A C   
703  O O   . TYR   A 88  ? 0.2601 0.2864 0.4684 0.0046  -0.0080 0.0444  94  TYR   A O   
704  C CB  . TYR   A 88  ? 0.2780 0.3162 0.5320 0.0075  -0.0137 0.0614  94  TYR   A CB  
705  C CG  . TYR   A 88  ? 0.2984 0.3423 0.5820 0.0107  -0.0138 0.0672  94  TYR   A CG  
706  C CD1 . TYR   A 88  ? 0.3201 0.3721 0.6039 0.0092  -0.0159 0.0701  94  TYR   A CD1 
707  C CD2 . TYR   A 88  ? 0.3152 0.3564 0.6286 0.0155  -0.0109 0.0690  94  TYR   A CD2 
708  C CE1 . TYR   A 88  ? 0.3343 0.3927 0.6484 0.0123  -0.0157 0.0754  94  TYR   A CE1 
709  C CE2 . TYR   A 88  ? 0.3236 0.3706 0.6684 0.0190  -0.0104 0.0743  94  TYR   A CE2 
710  C CZ  . TYR   A 88  ? 0.3397 0.3959 0.6853 0.0175  -0.0128 0.0776  94  TYR   A CZ  
711  O OH  . TYR   A 88  ? 0.3713 0.4342 0.7510 0.0211  -0.0119 0.0828  94  TYR   A OH  
712  N N   . GLN   A 89  ? 0.2088 0.2409 0.4006 0.0042  -0.0048 0.0377  95  GLN   A N   
713  C CA  . GLN   A 89  ? 0.2074 0.2371 0.3746 0.0009  -0.0063 0.0346  95  GLN   A CA  
714  C C   . GLN   A 89  ? 0.1904 0.2252 0.3478 -0.0043 -0.0130 0.0433  95  GLN   A C   
715  O O   . GLN   A 89  ? 0.1999 0.2398 0.3602 -0.0052 -0.0147 0.0465  95  GLN   A O   
716  C CB  . GLN   A 89  ? 0.2089 0.2361 0.3616 0.0021  -0.0007 0.0235  95  GLN   A CB  
717  C CG  . GLN   A 89  ? 0.2125 0.2374 0.3435 -0.0006 -0.0022 0.0206  95  GLN   A CG  
718  C CD  . GLN   A 89  ? 0.2133 0.2343 0.3327 0.0008  0.0021  0.0104  95  GLN   A CD  
719  O OE1 . GLN   A 89  ? 0.2450 0.2626 0.3696 0.0032  0.0064  0.0041  95  GLN   A OE1 
720  N NE2 . GLN   A 89  ? 0.1894 0.2102 0.2921 -0.0012 0.0008  0.0087  95  GLN   A NE2 
721  N N   . SER   A 90  ? 0.1821 0.2152 0.3276 -0.0085 -0.0164 0.0468  96  SER   A N   
722  C CA  . SER   A 90  ? 0.1750 0.2115 0.3083 -0.0150 -0.0222 0.0543  96  SER   A CA  
723  C C   . SER   A 90  ? 0.1860 0.2209 0.2967 -0.0174 -0.0196 0.0474  96  SER   A C   
724  O O   . SER   A 90  ? 0.1972 0.2283 0.3018 -0.0143 -0.0145 0.0382  96  SER   A O   
725  C CB  . SER   A 90  ? 0.1982 0.2332 0.3306 -0.0196 -0.0267 0.0626  96  SER   A CB  
726  O OG  . SER   A 90  ? 0.2250 0.2550 0.3485 -0.0193 -0.0225 0.0563  96  SER   A OG  
727  N N   . HIS   A 91  ? 0.1843 0.2217 0.2834 -0.0234 -0.0236 0.0522  97  HIS   A N   
728  C CA  . HIS   A 91  ? 0.1914 0.2267 0.2700 -0.0266 -0.0212 0.0466  97  HIS   A CA  
729  C C   . HIS   A 91  ? 0.1940 0.2283 0.2718 -0.0215 -0.0164 0.0378  97  HIS   A C   
730  O O   . HIS   A 91  ? 0.1890 0.2196 0.2547 -0.0212 -0.0129 0.0311  97  HIS   A O   
731  C CB  . HIS   A 91  ? 0.1953 0.2260 0.2629 -0.0287 -0.0183 0.0433  97  HIS   A CB  
732  C CG  . HIS   A 91  ? 0.2339 0.2646 0.2982 -0.0353 -0.0222 0.0518  97  HIS   A CG  
733  N ND1 . HIS   A 91  ? 0.2704 0.3003 0.3169 -0.0438 -0.0237 0.0544  97  HIS   A ND1 
734  C CD2 . HIS   A 91  ? 0.2376 0.2683 0.3132 -0.0351 -0.0247 0.0580  97  HIS   A CD2 
735  C CE1 . HIS   A 91  ? 0.2688 0.2984 0.3146 -0.0491 -0.0271 0.0623  97  HIS   A CE1 
736  N NE2 . HIS   A 91  ? 0.2563 0.2866 0.3203 -0.0440 -0.0284 0.0655  97  HIS   A NE2 
737  N N   . LEU   A 92  ? 0.1788 0.2164 0.2697 -0.0182 -0.0164 0.0386  98  LEU   A N   
738  C CA  . LEU   A 92  ? 0.1758 0.2124 0.2657 -0.0143 -0.0116 0.0311  98  LEU   A CA  
739  C C   . LEU   A 92  ? 0.1767 0.2167 0.2617 -0.0174 -0.0131 0.0330  98  LEU   A C   
740  O O   . LEU   A 92  ? 0.1801 0.2255 0.2733 -0.0203 -0.0177 0.0406  98  LEU   A O   
741  C CB  . LEU   A 92  ? 0.1833 0.2205 0.2912 -0.0089 -0.0083 0.0292  98  LEU   A CB  
742  C CG  . LEU   A 92  ? 0.2015 0.2363 0.3065 -0.0057 -0.0022 0.0205  98  LEU   A CG  
743  C CD1 . LEU   A 92  ? 0.2235 0.2523 0.3141 -0.0049 -0.0002 0.0134  98  LEU   A CD1 
744  C CD2 . LEU   A 92  ? 0.2018 0.2367 0.3250 -0.0016 0.0022  0.0182  98  LEU   A CD2 
745  N N   . MET   A 93  ? 0.1752 0.2121 0.2483 -0.0169 -0.0097 0.0266  99  MET   A N   
746  C CA  . MET   A 93  ? 0.1705 0.2095 0.2382 -0.0199 -0.0103 0.0273  99  MET   A CA  
747  C C   . MET   A 93  ? 0.1752 0.2138 0.2466 -0.0162 -0.0053 0.0222  99  MET   A C   
748  O O   . MET   A 93  ? 0.1845 0.2181 0.2505 -0.0131 -0.0017 0.0160  99  MET   A O   
749  C CB  . MET   A 93  ? 0.1805 0.2145 0.2292 -0.0236 -0.0103 0.0245  99  MET   A CB  
750  C CG  . MET   A 93  ? 0.2164 0.2498 0.2585 -0.0286 -0.0136 0.0284  99  MET   A CG  
751  S SD  . MET   A 93  ? 0.2478 0.2742 0.2703 -0.0323 -0.0108 0.0230  99  MET   A SD  
752  C CE  . MET   A 93  ? 0.2692 0.2909 0.2937 -0.0253 -0.0061 0.0158  99  MET   A CE  
753  N N   . LEU   A 94  ? 0.1711 0.2150 0.2519 -0.0169 -0.0049 0.0248  100 LEU   A N   
754  C CA  . LEU   A 94  ? 0.1681 0.2111 0.2514 -0.0142 0.0014  0.0194  100 LEU   A CA  
755  C C   . LEU   A 94  ? 0.1638 0.2063 0.2361 -0.0176 0.0019  0.0186  100 LEU   A C   
756  O O   . LEU   A 94  ? 0.1743 0.2199 0.2449 -0.0220 -0.0025 0.0233  100 LEU   A O   
757  C CB  . LEU   A 94  ? 0.1867 0.2364 0.2931 -0.0120 0.0040  0.0218  100 LEU   A CB  
758  C CG  . LEU   A 94  ? 0.2335 0.2831 0.3550 -0.0080 0.0050  0.0221  100 LEU   A CG  
759  C CD1 . LEU   A 94  ? 0.2511 0.3066 0.3973 -0.0056 0.0092  0.0235  100 LEU   A CD1 
760  C CD2 . LEU   A 94  ? 0.2650 0.3068 0.3766 -0.0052 0.0094  0.0140  100 LEU   A CD2 
761  N N   . ALA   A 95  ? 0.1552 0.1933 0.2198 -0.0162 0.0071  0.0128  101 ALA   A N   
762  C CA  . ALA   A 95  ? 0.1641 0.2011 0.2198 -0.0193 0.0085  0.0121  101 ALA   A CA  
763  C C   . ALA   A 95  ? 0.1698 0.2062 0.2280 -0.0179 0.0158  0.0076  101 ALA   A C   
764  O O   . ALA   A 95  ? 0.1865 0.2207 0.2478 -0.0148 0.0196  0.0035  101 ALA   A O   
765  C CB  . ALA   A 95  ? 0.1855 0.2143 0.2221 -0.0204 0.0069  0.0094  101 ALA   A CB  
766  N N   . VAL   A 96  ? 0.1710 0.2088 0.2273 -0.0209 0.0183  0.0081  102 VAL   A N   
767  C CA  . VAL   A 96  ? 0.1684 0.2043 0.2226 -0.0211 0.0261  0.0036  102 VAL   A CA  
768  C C   . VAL   A 96  ? 0.1981 0.2242 0.2305 -0.0219 0.0258  0.0000  102 VAL   A C   
769  O O   . VAL   A 96  ? 0.2274 0.2497 0.2482 -0.0243 0.0221  0.0019  102 VAL   A O   
770  C CB  . VAL   A 96  ? 0.1801 0.2217 0.2413 -0.0247 0.0290  0.0061  102 VAL   A CB  
771  C CG1 . VAL   A 96  ? 0.1943 0.2330 0.2504 -0.0260 0.0383  0.0010  102 VAL   A CG1 
772  C CG2 . VAL   A 96  ? 0.1837 0.2359 0.2695 -0.0239 0.0277  0.0109  102 VAL   A CG2 
773  N N   . GLY   A 97  ? 0.2174 0.2391 0.2452 -0.0202 0.0292  -0.0050 103 GLY   A N   
774  C CA  . GLY   A 97  ? 0.2445 0.2574 0.2528 -0.0213 0.0274  -0.0073 103 GLY   A CA  
775  C C   . GLY   A 97  ? 0.2627 0.2714 0.2666 -0.0203 0.0302  -0.0127 103 GLY   A C   
776  O O   . GLY   A 97  ? 0.2709 0.2827 0.2873 -0.0181 0.0340  -0.0153 103 GLY   A O   
777  N N   . HIS   A 98  ? 0.2693 0.2704 0.2555 -0.0223 0.0277  -0.0140 104 HIS   A N   
778  C CA  . HIS   A 98  ? 0.2676 0.2637 0.2461 -0.0230 0.0296  -0.0193 104 HIS   A CA  
779  C C   . HIS   A 98  ? 0.2547 0.2498 0.2362 -0.0198 0.0236  -0.0197 104 HIS   A C   
780  O O   . HIS   A 98  ? 0.2469 0.2415 0.2274 -0.0182 0.0167  -0.0159 104 HIS   A O   
781  C CB  . HIS   A 98  ? 0.2726 0.2610 0.2297 -0.0281 0.0286  -0.0194 104 HIS   A CB  
782  C CG  . HIS   A 98  ? 0.2925 0.2752 0.2380 -0.0309 0.0302  -0.0249 104 HIS   A CG  
783  N ND1 . HIS   A 98  ? 0.3244 0.3071 0.2715 -0.0329 0.0402  -0.0314 104 HIS   A ND1 
784  C CD2 . HIS   A 98  ? 0.3032 0.2803 0.2370 -0.0322 0.0232  -0.0250 104 HIS   A CD2 
785  C CE1 . HIS   A 98  ? 0.3391 0.3152 0.2724 -0.0362 0.0392  -0.0359 104 HIS   A CE1 
786  N NE2 . HIS   A 98  ? 0.3228 0.2959 0.2483 -0.0359 0.0283  -0.0317 104 HIS   A NE2 
787  N N   A SER   A 99  ? 0.2596 0.2541 0.2459 -0.0189 0.0269  -0.0247 105 SER   A N   
788  N N   B SER   A 99  ? 0.2522 0.2464 0.2374 -0.0192 0.0269  -0.0247 105 SER   A N   
789  C CA  A SER   A 99  ? 0.2751 0.2686 0.2650 -0.0164 0.0219  -0.0256 105 SER   A CA  
790  C CA  B SER   A 99  ? 0.2566 0.2489 0.2428 -0.0172 0.0217  -0.0259 105 SER   A CA  
791  C C   A SER   A 99  ? 0.2885 0.2775 0.2745 -0.0184 0.0263  -0.0328 105 SER   A C   
792  C C   B SER   A 99  ? 0.2769 0.2648 0.2587 -0.0195 0.0265  -0.0331 105 SER   A C   
793  O O   A SER   A 99  ? 0.2997 0.2900 0.2939 -0.0184 0.0347  -0.0368 105 SER   A O   
794  O O   B SER   A 99  ? 0.2869 0.2747 0.2715 -0.0210 0.0356  -0.0377 105 SER   A O   
795  C CB  A SER   A 99  ? 0.2956 0.2955 0.3043 -0.0121 0.0210  -0.0226 105 SER   A CB  
796  C CB  B SER   A 99  ? 0.2510 0.2490 0.2545 -0.0127 0.0193  -0.0228 105 SER   A CB  
797  O OG  A SER   A 99  ? 0.3405 0.3397 0.3545 -0.0099 0.0176  -0.0236 105 SER   A OG  
798  O OG  B SER   A 99  ? 0.2528 0.2546 0.2712 -0.0111 0.0255  -0.0246 105 SER   A OG  
799  N N   . GLU   A 100 ? 0.2828 0.2666 0.2574 -0.0204 0.0208  -0.0345 106 GLU   A N   
800  C CA  . GLU   A 100 ? 0.2979 0.2764 0.2665 -0.0234 0.0232  -0.0416 106 GLU   A CA  
801  C C   . GLU   A 100 ? 0.3067 0.2864 0.2853 -0.0202 0.0171  -0.0408 106 GLU   A C   
802  O O   . GLU   A 100 ? 0.2940 0.2777 0.2792 -0.0168 0.0108  -0.0350 106 GLU   A O   
803  C CB  . GLU   A 100 ? 0.3342 0.3056 0.2789 -0.0301 0.0200  -0.0429 106 GLU   A CB  
804  C CG  . GLU   A 100 ? 0.3888 0.3580 0.3226 -0.0344 0.0280  -0.0448 106 GLU   A CG  
805  C CD  . GLU   A 100 ? 0.4244 0.3861 0.3322 -0.0422 0.0243  -0.0446 106 GLU   A CD  
806  O OE1 . GLU   A 100 ? 0.5015 0.4580 0.3982 -0.0462 0.0195  -0.0474 106 GLU   A OE1 
807  O OE2 . GLU   A 100 ? 0.4065 0.3673 0.3048 -0.0449 0.0254  -0.0410 106 GLU   A OE2 
808  N N   . PRO   A 101 ? 0.3151 0.2916 0.2962 -0.0213 0.0195  -0.0470 107 PRO   A N   
809  C CA  . PRO   A 101 ? 0.2939 0.2721 0.2864 -0.0184 0.0142  -0.0460 107 PRO   A CA  
810  C C   . PRO   A 101 ? 0.2847 0.2639 0.2733 -0.0181 0.0036  -0.0407 107 PRO   A C   
811  O O   . PRO   A 101 ? 0.2931 0.2770 0.2947 -0.0141 0.0004  -0.0366 107 PRO   A O   
812  C CB  . PRO   A 101 ? 0.3165 0.2883 0.3051 -0.0221 0.0178  -0.0545 107 PRO   A CB  
813  C CG  . PRO   A 101 ? 0.3345 0.3043 0.3225 -0.0234 0.0291  -0.0597 107 PRO   A CG  
814  C CD  . PRO   A 101 ? 0.3179 0.2889 0.2933 -0.0253 0.0286  -0.0557 107 PRO   A CD  
815  N N   . GLY   A 102 ? 0.2764 0.2514 0.2480 -0.0228 -0.0014 -0.0406 108 GLY   A N   
816  C CA  . GLY   A 102 ? 0.2777 0.2537 0.2481 -0.0225 -0.0117 -0.0352 108 GLY   A CA  
817  C C   . GLY   A 102 ? 0.2566 0.2368 0.2331 -0.0185 -0.0137 -0.0284 108 GLY   A C   
818  O O   . GLY   A 102 ? 0.2706 0.2520 0.2504 -0.0173 -0.0209 -0.0241 108 GLY   A O   
819  N N   . ASP   A 103 ? 0.2413 0.2234 0.2194 -0.0169 -0.0073 -0.0276 109 ASP   A N   
820  C CA  . ASP   A 103 ? 0.2222 0.2077 0.2058 -0.0138 -0.0084 -0.0221 109 ASP   A CA  
821  C C   . ASP   A 103 ? 0.2147 0.2054 0.2144 -0.0095 -0.0083 -0.0204 109 ASP   A C   
822  O O   . ASP   A 103 ? 0.2154 0.2082 0.2192 -0.0076 -0.0095 -0.0165 109 ASP   A O   
823  C CB  . ASP   A 103 ? 0.2260 0.2123 0.2063 -0.0144 -0.0022 -0.0216 109 ASP   A CB  
824  C CG  . ASP   A 103 ? 0.2621 0.2432 0.2252 -0.0191 -0.0026 -0.0216 109 ASP   A CG  
825  O OD1 . ASP   A 103 ? 0.2736 0.2513 0.2289 -0.0207 -0.0098 -0.0186 109 ASP   A OD1 
826  O OD2 . ASP   A 103 ? 0.2655 0.2460 0.2237 -0.0214 0.0044  -0.0241 109 ASP   A OD2 
827  N N   . CYS   A 104 ? 0.2119 0.2039 0.2203 -0.0086 -0.0062 -0.0234 110 CYS   A N   
828  C CA  . CYS   A 104 ? 0.2167 0.2130 0.2388 -0.0056 -0.0064 -0.0212 110 CYS   A CA  
829  C C   . CYS   A 104 ? 0.2145 0.2116 0.2393 -0.0047 -0.0115 -0.0185 110 CYS   A C   
830  O O   . CYS   A 104 ? 0.2393 0.2341 0.2607 -0.0059 -0.0165 -0.0192 110 CYS   A O   
831  C CB  . CYS   A 104 ? 0.2157 0.2118 0.2461 -0.0054 -0.0045 -0.0245 110 CYS   A CB  
832  S SG  . CYS   A 104 ? 0.2463 0.2432 0.2834 -0.0046 0.0032  -0.0262 110 CYS   A SG  
833  N N   . GLY   A 105 ? 0.1942 0.1944 0.2252 -0.0030 -0.0102 -0.0154 111 GLY   A N   
834  C CA  . GLY   A 105 ? 0.1946 0.1953 0.2301 -0.0020 -0.0131 -0.0137 111 GLY   A CA  
835  C C   . GLY   A 105 ? 0.2048 0.2037 0.2349 -0.0019 -0.0137 -0.0114 111 GLY   A C   
836  O O   . GLY   A 105 ? 0.2094 0.2086 0.2452 -0.0008 -0.0140 -0.0103 111 GLY   A O   
837  N N   . GLY   A 106 ? 0.2012 0.1978 0.2214 -0.0033 -0.0130 -0.0111 112 GLY   A N   
838  C CA  . GLY   A 106 ? 0.1882 0.1824 0.2034 -0.0036 -0.0131 -0.0088 112 GLY   A CA  
839  C C   . GLY   A 106 ? 0.1844 0.1808 0.2034 -0.0034 -0.0091 -0.0079 112 GLY   A C   
840  O O   . GLY   A 106 ? 0.1924 0.1921 0.2132 -0.0041 -0.0062 -0.0079 112 GLY   A O   
841  N N   . ILE   A 107 ? 0.1745 0.1686 0.1951 -0.0030 -0.0090 -0.0070 113 ILE   A N   
842  C CA  . ILE   A 107 ? 0.1773 0.1722 0.1990 -0.0042 -0.0047 -0.0071 113 ILE   A CA  
843  C C   . ILE   A 107 ? 0.1766 0.1702 0.1900 -0.0068 -0.0030 -0.0059 113 ILE   A C   
844  O O   . ILE   A 107 ? 0.1961 0.1860 0.2041 -0.0070 -0.0045 -0.0050 113 ILE   A O   
845  C CB  . ILE   A 107 ? 0.1890 0.1815 0.2178 -0.0029 -0.0037 -0.0081 113 ILE   A CB  
846  C CG1 . ILE   A 107 ? 0.2112 0.2071 0.2502 -0.0014 -0.0039 -0.0092 113 ILE   A CG1 
847  C CG2 . ILE   A 107 ? 0.2259 0.2168 0.2519 -0.0056 0.0016  -0.0092 113 ILE   A CG2 
848  C CD1 . ILE   A 107 ? 0.2463 0.2406 0.2974 0.0007  -0.0025 -0.0105 113 ILE   A CD1 
849  N N   . LEU   A 108 ? 0.1735 0.1701 0.1859 -0.0093 -0.0005 -0.0052 114 LEU   A N   
850  C CA  . LEU   A 108 ? 0.1770 0.1732 0.1829 -0.0129 0.0008  -0.0039 114 LEU   A CA  
851  C C   . LEU   A 108 ? 0.1895 0.1826 0.1937 -0.0153 0.0037  -0.0055 114 LEU   A C   
852  O O   . LEU   A 108 ? 0.1837 0.1785 0.1907 -0.0161 0.0055  -0.0063 114 LEU   A O   
853  C CB  . LEU   A 108 ? 0.1702 0.1725 0.1779 -0.0146 0.0006  -0.0015 114 LEU   A CB  
854  C CG  . LEU   A 108 ? 0.1855 0.1889 0.1884 -0.0193 0.0008  0.0007  114 LEU   A CG  
855  C CD1 . LEU   A 108 ? 0.2051 0.2065 0.2037 -0.0199 0.0009  0.0010  114 LEU   A CD1 
856  C CD2 . LEU   A 108 ? 0.1975 0.2077 0.2059 -0.0210 -0.0007 0.0046  114 LEU   A CD2 
857  N N   . ARG   A 109 ? 0.2019 0.1896 0.2012 -0.0168 0.0049  -0.0064 115 ARG   A N   
858  C CA  . ARG   A 109 ? 0.2218 0.2046 0.2191 -0.0195 0.0091  -0.0093 115 ARG   A CA  
859  C C   . ARG   A 109 ? 0.2313 0.2118 0.2193 -0.0249 0.0100  -0.0090 115 ARG   A C   
860  O O   . ARG   A 109 ? 0.2402 0.2207 0.2254 -0.0253 0.0077  -0.0069 115 ARG   A O   
861  C CB  . ARG   A 109 ? 0.2597 0.2362 0.2630 -0.0157 0.0098  -0.0111 115 ARG   A CB  
862  C CG  . ARG   A 109 ? 0.3322 0.3107 0.3463 -0.0106 0.0078  -0.0111 115 ARG   A CG  
863  C CD  . ARG   A 109 ? 0.3664 0.3389 0.3890 -0.0075 0.0080  -0.0118 115 ARG   A CD  
864  N NE  . ARG   A 109 ? 0.4233 0.3930 0.4517 -0.0084 0.0148  -0.0162 115 ARG   A NE  
865  C CZ  . ARG   A 109 ? 0.4248 0.3971 0.4644 -0.0062 0.0172  -0.0181 115 ARG   A CZ  
866  N NH1 . ARG   A 109 ? 0.3706 0.3480 0.4176 -0.0027 0.0120  -0.0156 115 ARG   A NH1 
867  N NH2 . ARG   A 109 ? 0.4411 0.4106 0.4847 -0.0080 0.0252  -0.0229 115 ARG   A NH2 
868  N N   . CYS   A 110 ? 0.2345 0.2126 0.2171 -0.0300 0.0137  -0.0115 116 CYS   A N   
869  C CA  . CYS   A 110 ? 0.2509 0.2249 0.2238 -0.0364 0.0150  -0.0125 116 CYS   A CA  
870  C C   . CYS   A 110 ? 0.2731 0.2375 0.2450 -0.0376 0.0217  -0.0187 116 CYS   A C   
871  O O   . CYS   A 110 ? 0.2784 0.2409 0.2597 -0.0328 0.0245  -0.0211 116 CYS   A O   
872  C CB  . CYS   A 110 ? 0.2559 0.2348 0.2210 -0.0433 0.0133  -0.0102 116 CYS   A CB  
873  S SG  . CYS   A 110 ? 0.2587 0.2366 0.2195 -0.0474 0.0180  -0.0132 116 CYS   A SG  
874  N N   . GLN   A 111 ? 0.3079 0.2664 0.2701 -0.0444 0.0244  -0.0214 117 GLN   A N   
875  C CA  . GLN   A 111 ? 0.3287 0.2771 0.2907 -0.0460 0.0322  -0.0284 117 GLN   A CA  
876  C C   . GLN   A 111 ? 0.3363 0.2842 0.2983 -0.0479 0.0387  -0.0329 117 GLN   A C   
877  O O   . GLN   A 111 ? 0.3504 0.2910 0.3180 -0.0469 0.0465  -0.0391 117 GLN   A O   
878  C CB  . GLN   A 111 ? 0.3677 0.3092 0.3171 -0.0544 0.0342  -0.0312 117 GLN   A CB  
879  C CG  . GLN   A 111 ? 0.4410 0.3868 0.3759 -0.0639 0.0324  -0.0301 117 GLN   A CG  
880  C CD  . GLN   A 111 ? 0.5641 0.5039 0.4857 -0.0734 0.0330  -0.0325 117 GLN   A CD  
881  O OE1 . GLN   A 111 ? 0.6014 0.5469 0.5171 -0.0782 0.0262  -0.0273 117 GLN   A OE1 
882  N NE2 . GLN   A 111 ? 0.5793 0.5075 0.4970 -0.0768 0.0413  -0.0406 117 GLN   A NE2 
883  N N   . HIS   A 112 ? 0.3072 0.2629 0.2650 -0.0502 0.0360  -0.0297 118 HIS   A N   
884  C CA  . HIS   A 112 ? 0.3005 0.2562 0.2565 -0.0531 0.0420  -0.0331 118 HIS   A CA  
885  C C   . HIS   A 112 ? 0.2894 0.2500 0.2612 -0.0449 0.0421  -0.0320 118 HIS   A C   
886  O O   . HIS   A 112 ? 0.3042 0.2648 0.2775 -0.0465 0.0481  -0.0352 118 HIS   A O   
887  C CB  . HIS   A 112 ? 0.3098 0.2700 0.2506 -0.0621 0.0387  -0.0295 118 HIS   A CB  
888  C CG  . HIS   A 112 ? 0.3346 0.2911 0.2599 -0.0711 0.0370  -0.0297 118 HIS   A CG  
889  N ND1 . HIS   A 112 ? 0.3419 0.3047 0.2650 -0.0726 0.0278  -0.0228 118 HIS   A ND1 
890  C CD2 . HIS   A 112 ? 0.3696 0.3170 0.2813 -0.0800 0.0437  -0.0364 118 HIS   A CD2 
891  C CE1 . HIS   A 112 ? 0.3829 0.3406 0.2920 -0.0819 0.0281  -0.0248 118 HIS   A CE1 
892  N NE2 . HIS   A 112 ? 0.3908 0.3387 0.2914 -0.0870 0.0375  -0.0333 118 HIS   A NE2 
893  N N   . GLY   A 113 ? 0.2647 0.2293 0.2476 -0.0370 0.0356  -0.0277 119 GLY   A N   
894  C CA  . GLY   A 113 ? 0.2529 0.2221 0.2501 -0.0302 0.0346  -0.0266 119 GLY   A CA  
895  C C   . GLY   A 113 ? 0.2269 0.2040 0.2260 -0.0269 0.0263  -0.0204 119 GLY   A C   
896  O O   . GLY   A 113 ? 0.2493 0.2279 0.2428 -0.0277 0.0214  -0.0170 119 GLY   A O   
897  N N   . VAL   A 114 ? 0.2111 0.1929 0.2189 -0.0237 0.0256  -0.0194 120 VAL   A N   
898  C CA  . VAL   A 114 ? 0.2100 0.1982 0.2213 -0.0205 0.0188  -0.0148 120 VAL   A CA  
899  C C   . VAL   A 114 ? 0.2053 0.1977 0.2085 -0.0253 0.0168  -0.0112 120 VAL   A C   
900  O O   . VAL   A 114 ? 0.2191 0.2119 0.2182 -0.0300 0.0200  -0.0115 120 VAL   A O   
901  C CB  . VAL   A 114 ? 0.2188 0.2100 0.2426 -0.0162 0.0189  -0.0154 120 VAL   A CB  
902  C CG1 . VAL   A 114 ? 0.2140 0.2105 0.2406 -0.0137 0.0130  -0.0117 120 VAL   A CG1 
903  C CG2 . VAL   A 114 ? 0.2383 0.2263 0.2730 -0.0112 0.0191  -0.0175 120 VAL   A CG2 
904  N N   . VAL   A 115 ? 0.1917 0.1873 0.1936 -0.0244 0.0116  -0.0074 121 VAL   A N   
905  C CA  . VAL   A 115 ? 0.1936 0.1941 0.1921 -0.0281 0.0083  -0.0026 121 VAL   A CA  
906  C C   . VAL   A 115 ? 0.1847 0.1902 0.1928 -0.0243 0.0056  0.0001  121 VAL   A C   
907  O O   . VAL   A 115 ? 0.1923 0.2008 0.2013 -0.0269 0.0044  0.0035  121 VAL   A O   
908  C CB  . VAL   A 115 ? 0.2084 0.2098 0.2031 -0.0294 0.0053  -0.0003 121 VAL   A CB  
909  C CG1 . VAL   A 115 ? 0.2208 0.2282 0.2163 -0.0326 0.0012  0.0055  121 VAL   A CG1 
910  C CG2 . VAL   A 115 ? 0.2268 0.2223 0.2118 -0.0338 0.0080  -0.0032 121 VAL   A CG2 
911  N N   . GLY   A 116 ? 0.1749 0.1803 0.1897 -0.0185 0.0043  -0.0015 122 GLY   A N   
912  C CA  . GLY   A 116 ? 0.1801 0.1890 0.2035 -0.0154 0.0023  -0.0002 122 GLY   A CA  
913  C C   . GLY   A 116 ? 0.1746 0.1821 0.2017 -0.0107 0.0009  -0.0028 122 GLY   A C   
914  O O   . GLY   A 116 ? 0.1845 0.1885 0.2086 -0.0096 0.0011  -0.0048 122 GLY   A O   
915  N N   . ILE   A 117 ? 0.1729 0.1825 0.2062 -0.0085 -0.0005 -0.0025 123 ILE   A N   
916  C CA  . ILE   A 117 ? 0.1690 0.1768 0.2032 -0.0056 -0.0020 -0.0053 123 ILE   A CA  
917  C C   . ILE   A 117 ? 0.1681 0.1770 0.2033 -0.0050 -0.0019 -0.0053 123 ILE   A C   
918  O O   . ILE   A 117 ? 0.1698 0.1819 0.2113 -0.0054 -0.0011 -0.0032 123 ILE   A O   
919  C CB  . ILE   A 117 ? 0.1815 0.1890 0.2224 -0.0039 -0.0031 -0.0073 123 ILE   A CB  
920  C CG1 . ILE   A 117 ? 0.1988 0.2090 0.2471 -0.0043 -0.0023 -0.0060 123 ILE   A CG1 
921  C CG2 . ILE   A 117 ? 0.2135 0.2194 0.2558 -0.0036 -0.0026 -0.0083 123 ILE   A CG2 
922  C CD1 . ILE   A 117 ? 0.2239 0.2339 0.2799 -0.0029 -0.0037 -0.0084 123 ILE   A CD1 
923  N N   . VAL   A 118 ? 0.1571 0.1634 0.1869 -0.0044 -0.0024 -0.0076 124 VAL   A N   
924  C CA  . VAL   A 118 ? 0.1626 0.1694 0.1933 -0.0043 -0.0003 -0.0091 124 VAL   A CA  
925  C C   . VAL   A 118 ? 0.1735 0.1809 0.2130 -0.0031 0.0003  -0.0109 124 VAL   A C   
926  O O   . VAL   A 118 ? 0.1773 0.1831 0.2178 -0.0026 -0.0019 -0.0127 124 VAL   A O   
927  C CB  . VAL   A 118 ? 0.1822 0.1848 0.2028 -0.0052 -0.0007 -0.0119 124 VAL   A CB  
928  C CG1 . VAL   A 118 ? 0.2085 0.2108 0.2297 -0.0058 0.0035  -0.0150 124 VAL   A CG1 
929  C CG2 . VAL   A 118 ? 0.1952 0.1963 0.2076 -0.0066 -0.0012 -0.0097 124 VAL   A CG2 
930  N N   . SER   A 119 ? 0.1661 0.1760 0.2140 -0.0027 0.0031  -0.0101 125 SER   A N   
931  C CA  . SER   A 119 ? 0.1692 0.1790 0.2276 -0.0014 0.0042  -0.0113 125 SER   A CA  
932  C C   . SER   A 119 ? 0.1980 0.2072 0.2624 -0.0008 0.0090  -0.0144 125 SER   A C   
933  O O   . SER   A 119 ? 0.2073 0.2135 0.2769 -0.0002 0.0110  -0.0184 125 SER   A O   
934  C CB  . SER   A 119 ? 0.1808 0.1944 0.2483 -0.0015 0.0026  -0.0056 125 SER   A CB  
935  O OG  . SER   A 119 ? 0.1938 0.2070 0.2734 -0.0003 0.0035  -0.0056 125 SER   A OG  
936  N N   . THR   A 120 ? 0.1990 0.2107 0.2637 -0.0012 0.0116  -0.0129 126 THR   A N   
937  C CA  . THR   A 120 ? 0.2040 0.2155 0.2774 -0.0005 0.0179  -0.0163 126 THR   A CA  
938  C C   . THR   A 120 ? 0.2137 0.2245 0.2772 -0.0024 0.0217  -0.0190 126 THR   A C   
939  O O   . THR   A 120 ? 0.2064 0.2176 0.2586 -0.0041 0.0187  -0.0165 126 THR   A O   
940  C CB  . THR   A 120 ? 0.2133 0.2305 0.3066 0.0013  0.0185  -0.0107 126 THR   A CB  
941  O OG1 . THR   A 120 ? 0.2258 0.2482 0.3184 -0.0001 0.0164  -0.0051 126 THR   A OG1 
942  C CG2 . THR   A 120 ? 0.2065 0.2242 0.3084 0.0023  0.0143  -0.0065 126 THR   A CG2 
943  N N   . GLY   A 121 ? 0.2366 0.2457 0.3048 -0.0026 0.0291  -0.0242 127 GLY   A N   
944  C CA  . GLY   A 121 ? 0.2827 0.2912 0.3428 -0.0051 0.0343  -0.0269 127 GLY   A CA  
945  C C   . GLY   A 121 ? 0.3170 0.3257 0.3906 -0.0045 0.0442  -0.0318 127 GLY   A C   
946  O O   . GLY   A 121 ? 0.3400 0.3477 0.4278 -0.0022 0.0469  -0.0342 127 GLY   A O   
947  N N   . GLY   A 122 ? 0.3410 0.3500 0.4097 -0.0070 0.0504  -0.0342 128 GLY   A N   
948  C CA  . GLY   A 122 ? 0.3479 0.3574 0.4301 -0.0069 0.0619  -0.0397 128 GLY   A CA  
949  C C   . GLY   A 122 ? 0.3502 0.3677 0.4443 -0.0067 0.0645  -0.0349 128 GLY   A C   
950  O O   . GLY   A 122 ? 0.3429 0.3666 0.4423 -0.0056 0.0565  -0.0264 128 GLY   A O   
951  N N   . ASN   A 123 ? 0.3433 0.3604 0.4414 -0.0087 0.0761  -0.0407 129 ASN   A N   
952  C CA  . ASN   A 123 ? 0.3468 0.3721 0.4591 -0.0089 0.0801  -0.0368 129 ASN   A CA  
953  C C   . ASN   A 123 ? 0.3379 0.3662 0.4360 -0.0117 0.0723  -0.0301 129 ASN   A C   
954  O O   . ASN   A 123 ? 0.3432 0.3800 0.4565 -0.0112 0.0705  -0.0237 129 ASN   A O   
955  C CB  . ASN   A 123 ? 0.3679 0.4020 0.5141 -0.0039 0.0792  -0.0312 129 ASN   A CB  
956  C CG  . ASN   A 123 ? 0.4585 0.4895 0.6230 -0.0011 0.0894  -0.0385 129 ASN   A CG  
957  O OD1 . ASN   A 123 ? 0.5072 0.5316 0.6632 -0.0038 0.1011  -0.0488 129 ASN   A OD1 
958  N ND2 . ASN   A 123 ? 0.4718 0.5066 0.6615 0.0038  0.0856  -0.0335 129 ASN   A ND2 
959  N N   . GLY   A 124 ? 0.3230 0.3440 0.3936 -0.0150 0.0680  -0.0314 130 GLY   A N   
960  C CA  . GLY   A 124 ? 0.3042 0.3261 0.3614 -0.0176 0.0615  -0.0257 130 GLY   A CA  
961  C C   . GLY   A 124 ? 0.2668 0.2933 0.3297 -0.0152 0.0503  -0.0176 130 GLY   A C   
962  O O   . GLY   A 124 ? 0.2468 0.2757 0.3049 -0.0173 0.0461  -0.0127 130 GLY   A O   
963  N N   . LEU   A 125 ? 0.2312 0.2586 0.3040 -0.0115 0.0461  -0.0164 131 LEU   A N   
964  C CA  . LEU   A 125 ? 0.2233 0.2540 0.2991 -0.0102 0.0364  -0.0094 131 LEU   A CA  
965  C C   . LEU   A 125 ? 0.2415 0.2655 0.3032 -0.0093 0.0313  -0.0113 131 LEU   A C   
966  O O   . LEU   A 125 ? 0.2878 0.3065 0.3454 -0.0087 0.0346  -0.0171 131 LEU   A O   
967  C CB  . LEU   A 125 ? 0.2370 0.2749 0.3378 -0.0073 0.0352  -0.0049 131 LEU   A CB  
968  C CG  . LEU   A 125 ? 0.2451 0.2914 0.3660 -0.0077 0.0393  -0.0018 131 LEU   A CG  
969  C CD1 . LEU   A 125 ? 0.2752 0.3269 0.4236 -0.0040 0.0396  0.0013  131 LEU   A CD1 
970  C CD2 . LEU   A 125 ? 0.2377 0.2889 0.3547 -0.0112 0.0328  0.0050  131 LEU   A CD2 
971  N N   . VAL   A 126 ? 0.1879 0.2118 0.2425 -0.0099 0.0241  -0.0069 132 VAL   A N   
972  C CA  . VAL   A 126 ? 0.1861 0.2053 0.2318 -0.0088 0.0193  -0.0079 132 VAL   A CA  
973  C C   . VAL   A 126 ? 0.1801 0.2034 0.2354 -0.0078 0.0142  -0.0026 132 VAL   A C   
974  O O   . VAL   A 126 ? 0.1841 0.2119 0.2426 -0.0097 0.0116  0.0025  132 VAL   A O   
975  C CB  . VAL   A 126 ? 0.2073 0.2209 0.2346 -0.0108 0.0161  -0.0083 132 VAL   A CB  
976  C CG1 . VAL   A 126 ? 0.2213 0.2370 0.2457 -0.0132 0.0142  -0.0041 132 VAL   A CG1 
977  C CG2 . VAL   A 126 ? 0.2163 0.2264 0.2389 -0.0094 0.0112  -0.0088 132 VAL   A CG2 
978  N N   . GLY   A 127 ? 0.1627 0.1846 0.2226 -0.0057 0.0129  -0.0035 133 GLY   A N   
979  C CA  . GLY   A 127 ? 0.1641 0.1893 0.2311 -0.0057 0.0083  0.0019  133 GLY   A CA  
980  C C   . GLY   A 127 ? 0.1609 0.1822 0.2180 -0.0059 0.0049  0.0011  133 GLY   A C   
981  O O   . GLY   A 127 ? 0.1741 0.1910 0.2257 -0.0047 0.0056  -0.0035 133 GLY   A O   
982  N N   . PHE   A 128 ? 0.1472 0.1702 0.2017 -0.0082 0.0015  0.0055  134 PHE   A N   
983  C CA  . PHE   A 128 ? 0.1589 0.1786 0.2054 -0.0088 -0.0003 0.0045  134 PHE   A CA  
984  C C   . PHE   A 128 ? 0.1576 0.1795 0.2102 -0.0101 -0.0023 0.0087  134 PHE   A C   
985  O O   . PHE   A 128 ? 0.1663 0.1920 0.2223 -0.0129 -0.0045 0.0143  134 PHE   A O   
986  C CB  . PHE   A 128 ? 0.1655 0.1837 0.2009 -0.0119 -0.0011 0.0052  134 PHE   A CB  
987  C CG  . PHE   A 128 ? 0.1627 0.1789 0.1920 -0.0118 0.0004  0.0030  134 PHE   A CG  
988  C CD1 . PHE   A 128 ? 0.1742 0.1854 0.1967 -0.0101 0.0007  -0.0007 134 PHE   A CD1 
989  C CD2 . PHE   A 128 ? 0.1797 0.1991 0.2105 -0.0137 0.0009  0.0054  134 PHE   A CD2 
990  C CE1 . PHE   A 128 ? 0.1874 0.1960 0.2029 -0.0109 0.0016  -0.0018 134 PHE   A CE1 
991  C CE2 . PHE   A 128 ? 0.1953 0.2125 0.2196 -0.0144 0.0026  0.0037  134 PHE   A CE2 
992  C CZ  . PHE   A 128 ? 0.1868 0.1982 0.2028 -0.0130 0.0031  0.0002  134 PHE   A CZ  
993  N N   . ALA   A 129 ? 0.1583 0.1777 0.2113 -0.0088 -0.0020 0.0064  135 ALA   A N   
994  C CA  . ALA   A 129 ? 0.1620 0.1826 0.2186 -0.0108 -0.0033 0.0101  135 ALA   A CA  
995  C C   . ALA   A 129 ? 0.1769 0.1965 0.2224 -0.0150 -0.0032 0.0109  135 ALA   A C   
996  O O   . ALA   A 129 ? 0.1874 0.2038 0.2272 -0.0143 -0.0013 0.0066  135 ALA   A O   
997  C CB  . ALA   A 129 ? 0.1675 0.1859 0.2294 -0.0084 -0.0025 0.0069  135 ALA   A CB  
998  N N   . ASP   A 130 ? 0.1740 0.1959 0.2169 -0.0198 -0.0053 0.0166  136 ASP   A N   
999  C CA  . ASP   A 130 ? 0.1813 0.2012 0.2117 -0.0252 -0.0043 0.0166  136 ASP   A CA  
1000 C C   . ASP   A 130 ? 0.1964 0.2139 0.2253 -0.0263 -0.0013 0.0146  136 ASP   A C   
1001 O O   . ASP   A 130 ? 0.1986 0.2173 0.2351 -0.0256 -0.0022 0.0171  136 ASP   A O   
1002 C CB  . ASP   A 130 ? 0.2053 0.2282 0.2320 -0.0316 -0.0084 0.0238  136 ASP   A CB  
1003 C CG  . ASP   A 130 ? 0.2536 0.2734 0.2643 -0.0390 -0.0069 0.0230  136 ASP   A CG  
1004 O OD1 . ASP   A 130 ? 0.2581 0.2747 0.2620 -0.0388 -0.0041 0.0179  136 ASP   A OD1 
1005 O OD2 . ASP   A 130 ? 0.3124 0.3323 0.3171 -0.0453 -0.0084 0.0275  136 ASP   A OD2 
1006 N N   . VAL   A 131 ? 0.1901 0.2039 0.2100 -0.0285 0.0028  0.0101  137 VAL   A N   
1007 C CA  . VAL   A 131 ? 0.1971 0.2091 0.2161 -0.0306 0.0071  0.0080  137 VAL   A CA  
1008 C C   . VAL   A 131 ? 0.2186 0.2276 0.2232 -0.0387 0.0107  0.0076  137 VAL   A C   
1009 O O   . VAL   A 131 ? 0.2230 0.2299 0.2250 -0.0417 0.0159  0.0052  137 VAL   A O   
1010 C CB  . VAL   A 131 ? 0.2104 0.2204 0.2361 -0.0252 0.0105  0.0016  137 VAL   A CB  
1011 C CG1 . VAL   A 131 ? 0.2122 0.2242 0.2494 -0.0189 0.0071  0.0014  137 VAL   A CG1 
1012 C CG2 . VAL   A 131 ? 0.2185 0.2249 0.2388 -0.0246 0.0125  -0.0025 137 VAL   A CG2 
1013 N N   . ARG   A 132 ? 0.2178 0.2263 0.2127 -0.0429 0.0084  0.0094  138 ARG   A N   
1014 C CA  . ARG   A 132 ? 0.2205 0.2249 0.1994 -0.0516 0.0118  0.0079  138 ARG   A CA  
1015 C C   . ARG   A 132 ? 0.2578 0.2627 0.2283 -0.0598 0.0114  0.0127  138 ARG   A C   
1016 O O   . ARG   A 132 ? 0.2832 0.2835 0.2392 -0.0677 0.0167  0.0096  138 ARG   A O   
1017 C CB  . ARG   A 132 ? 0.2225 0.2268 0.1936 -0.0549 0.0079  0.0094  138 ARG   A CB  
1018 C CG  . ARG   A 132 ? 0.2199 0.2220 0.1959 -0.0485 0.0095  0.0042  138 ARG   A CG  
1019 C CD  . ARG   A 132 ? 0.2369 0.2392 0.2060 -0.0523 0.0059  0.0062  138 ARG   A CD  
1020 N NE  . ARG   A 132 ? 0.2183 0.2277 0.1953 -0.0509 -0.0014 0.0135  138 ARG   A NE  
1021 C CZ  . ARG   A 132 ? 0.2434 0.2555 0.2201 -0.0528 -0.0057 0.0167  138 ARG   A CZ  
1022 N NH1 . ARG   A 132 ? 0.2479 0.2559 0.2139 -0.0576 -0.0043 0.0137  138 ARG   A NH1 
1023 N NH2 . ARG   A 132 ? 0.2454 0.2643 0.2341 -0.0501 -0.0109 0.0227  138 ARG   A NH2 
1024 N N   . ASP   A 133 ? 0.2436 0.2530 0.2219 -0.0588 0.0055  0.0203  139 ASP   A N   
1025 C CA  . ASP   A 133 ? 0.2593 0.2687 0.2291 -0.0673 0.0040  0.0265  139 ASP   A CA  
1026 C C   . ASP   A 133 ? 0.2809 0.2883 0.2535 -0.0670 0.0111  0.0232  139 ASP   A C   
1027 O O   . ASP   A 133 ? 0.3114 0.3175 0.2746 -0.0751 0.0120  0.0273  139 ASP   A O   
1028 C CB  . ASP   A 133 ? 0.2833 0.2981 0.2632 -0.0664 -0.0055 0.0371  139 ASP   A CB  
1029 C CG  . ASP   A 133 ? 0.3210 0.3384 0.3211 -0.0565 -0.0061 0.0370  139 ASP   A CG  
1030 O OD1 . ASP   A 133 ? 0.3039 0.3209 0.3116 -0.0487 -0.0029 0.0299  139 ASP   A OD1 
1031 O OD2 . ASP   A 133 ? 0.3358 0.3549 0.3436 -0.0571 -0.0098 0.0440  139 ASP   A OD2 
1032 N N   . LEU   A 134 ? 0.2583 0.2657 0.2440 -0.0584 0.0157  0.0164  140 LEU   A N   
1033 C CA  . LEU   A 134 ? 0.2589 0.2657 0.2511 -0.0577 0.0217  0.0137  140 LEU   A CA  
1034 C C   . LEU   A 134 ? 0.2628 0.2650 0.2450 -0.0626 0.0318  0.0062  140 LEU   A C   
1035 O O   . LEU   A 134 ? 0.2498 0.2508 0.2406 -0.0572 0.0373  -0.0013 140 LEU   A O   
1036 C CB  . LEU   A 134 ? 0.2482 0.2575 0.2593 -0.0471 0.0207  0.0105  140 LEU   A CB  
1037 C CG  . LEU   A 134 ? 0.2590 0.2717 0.2802 -0.0422 0.0125  0.0162  140 LEU   A CG  
1038 C CD1 . LEU   A 134 ? 0.2599 0.2738 0.2960 -0.0331 0.0120  0.0115  140 LEU   A CD1 
1039 C CD2 . LEU   A 134 ? 0.2790 0.2930 0.3025 -0.0462 0.0094  0.0241  140 LEU   A CD2 
1040 N N   . LEU   A 135 ? 0.2676 0.2667 0.2313 -0.0738 0.0345  0.0083  141 LEU   A N   
1041 C CA  . LEU   A 135 ? 0.2873 0.2807 0.2393 -0.0799 0.0457  -0.0002 141 LEU   A CA  
1042 C C   . LEU   A 135 ? 0.3192 0.3122 0.2823 -0.0775 0.0558  -0.0063 141 LEU   A C   
1043 O O   . LEU   A 135 ? 0.3416 0.3309 0.3059 -0.0773 0.0657  -0.0153 141 LEU   A O   
1044 C CB  . LEU   A 135 ? 0.3108 0.2998 0.2369 -0.0943 0.0469  0.0025  141 LEU   A CB  
1045 C CG  . LEU   A 135 ? 0.3417 0.3321 0.2570 -0.0986 0.0354  0.0106  141 LEU   A CG  
1046 C CD1 . LEU   A 135 ? 0.3736 0.3589 0.2613 -0.1145 0.0369  0.0125  141 LEU   A CD1 
1047 C CD2 . LEU   A 135 ? 0.3506 0.3410 0.2705 -0.0923 0.0325  0.0067  141 LEU   A CD2 
1048 N N   . TRP   A 136 ? 0.3079 0.3049 0.2819 -0.0754 0.0535  -0.0015 142 TRP   A N   
1049 C CA  . TRP   A 136 ? 0.3095 0.3074 0.2964 -0.0735 0.0625  -0.0064 142 TRP   A CA  
1050 C C   . TRP   A 136 ? 0.3089 0.3088 0.3167 -0.0627 0.0645  -0.0132 142 TRP   A C   
1051 O O   . TRP   A 136 ? 0.3236 0.3240 0.3432 -0.0614 0.0733  -0.0187 142 TRP   A O   
1052 C CB  . TRP   A 136 ? 0.3046 0.3060 0.2983 -0.0743 0.0586  0.0009  142 TRP   A CB  
1053 C CG  . TRP   A 136 ? 0.2981 0.3036 0.3037 -0.0665 0.0465  0.0073  142 TRP   A CG  
1054 C CD1 . TRP   A 136 ? 0.3043 0.3103 0.3032 -0.0683 0.0367  0.0159  142 TRP   A CD1 
1055 C CD2 . TRP   A 136 ? 0.2858 0.2948 0.3124 -0.0559 0.0434  0.0048  142 TRP   A CD2 
1056 N NE1 . TRP   A 136 ? 0.3011 0.3105 0.3164 -0.0593 0.0294  0.0182  142 TRP   A NE1 
1057 C CE2 . TRP   A 136 ? 0.2889 0.2998 0.3196 -0.0523 0.0332  0.0114  142 TRP   A CE2 
1058 C CE3 . TRP   A 136 ? 0.2897 0.3006 0.3328 -0.0499 0.0482  -0.0019 142 TRP   A CE3 
1059 C CZ2 . TRP   A 136 ? 0.2969 0.3104 0.3442 -0.0435 0.0285  0.0102  142 TRP   A CZ2 
1060 C CZ3 . TRP   A 136 ? 0.2949 0.3089 0.3543 -0.0416 0.0417  -0.0019 142 TRP   A CZ3 
1061 C CH2 . TRP   A 136 ? 0.2869 0.3018 0.3470 -0.0388 0.0325  0.0037  142 TRP   A CH2 
1062 N N   . LEU   A 137 ? 0.3037 0.3049 0.3172 -0.0551 0.0563  -0.0124 143 LEU   A N   
1063 C CA  . LEU   A 137 ? 0.3330 0.3356 0.3646 -0.0457 0.0564  -0.0174 143 LEU   A CA  
1064 C C   . LEU   A 137 ? 0.4099 0.4085 0.4437 -0.0465 0.0673  -0.0258 143 LEU   A C   
1065 O O   . LEU   A 137 ? 0.4173 0.4177 0.4702 -0.0398 0.0694  -0.0296 143 LEU   A O   
1066 C CB  . LEU   A 137 ? 0.3126 0.3158 0.3438 -0.0400 0.0467  -0.0148 143 LEU   A CB  
1067 C CG  . LEU   A 137 ? 0.2999 0.3072 0.3372 -0.0358 0.0371  -0.0089 143 LEU   A CG  
1068 C CD1 . LEU   A 137 ? 0.3048 0.3120 0.3402 -0.0313 0.0300  -0.0077 143 LEU   A CD1 
1069 C CD2 . LEU   A 137 ? 0.3091 0.3199 0.3653 -0.0301 0.0365  -0.0103 143 LEU   A CD2 
1070 N N   . ASP   A 138 ? 0.4539 0.4468 0.4689 -0.0549 0.0739  -0.0287 144 ASP   A N   
1071 C CA  . ASP   A 138 ? 0.5163 0.5035 0.5322 -0.0566 0.0859  -0.0378 144 ASP   A CA  
1072 C C   . ASP   A 138 ? 0.5601 0.5450 0.5718 -0.0648 0.0996  -0.0428 144 ASP   A C   
1073 O O   . ASP   A 138 ? 0.5729 0.5517 0.5815 -0.0683 0.1113  -0.0511 144 ASP   A O   
1074 C CB  . ASP   A 138 ? 0.5652 0.5460 0.5623 -0.0614 0.0858  -0.0399 144 ASP   A CB  
1075 C CG  . ASP   A 138 ? 0.6669 0.6491 0.6644 -0.0555 0.0738  -0.0353 144 ASP   A CG  
1076 O OD1 . ASP   A 138 ? 0.6862 0.6730 0.7012 -0.0461 0.0674  -0.0330 144 ASP   A OD1 
1077 O OD2 . ASP   A 138 ? 0.7185 0.6973 0.6985 -0.0610 0.0710  -0.0341 144 ASP   A OD2 
1078 N N   . GLU   A 139 ? 0.5791 0.5678 0.5897 -0.0685 0.0992  -0.0381 145 GLU   A N   
1079 C CA  . GLU   A 139 ? 0.6066 0.5933 0.6131 -0.0768 0.1130  -0.0426 145 GLU   A CA  
1080 C C   . GLU   A 139 ? 0.6115 0.6052 0.6415 -0.0718 0.1142  -0.0412 145 GLU   A C   
1081 O O   . GLU   A 139 ? 0.6233 0.6170 0.6513 -0.0787 0.1238  -0.0425 145 GLU   A O   
1082 C CB  . GLU   A 139 ? 0.6564 0.6393 0.6330 -0.0903 0.1128  -0.0379 145 GLU   A CB  
1083 C CG  . GLU   A 139 ? 0.7231 0.7110 0.6973 -0.0902 0.0996  -0.0261 145 GLU   A CG  
1084 C CD  . GLU   A 139 ? 0.8291 0.8134 0.7747 -0.1021 0.0946  -0.0191 145 GLU   A CD  
1085 O OE1 . GLU   A 139 ? 0.8445 0.8305 0.7847 -0.1076 0.0915  -0.0114 145 GLU   A OE1 
1086 O OE2 . GLU   A 139 ? 0.8774 0.8573 0.8065 -0.1063 0.0931  -0.0208 145 GLU   A OE2 
1087 N N1  . A1BTF B .   ? 0.2593 0.2665 0.3619 0.0030  0.0118  -0.0139 201 A1BTF A N1  
1088 C C4  . A1BTF B .   ? 0.4045 0.3910 0.4404 -0.0120 0.0464  -0.0518 201 A1BTF A C4  
1089 C C5  . A1BTF B .   ? 0.3971 0.3846 0.4444 -0.0088 0.0412  -0.0494 201 A1BTF A C5  
1090 C C6  . A1BTF B .   ? 0.3822 0.3731 0.4274 -0.0073 0.0315  -0.0423 201 A1BTF A C6  
1091 C C7  . A1BTF B .   ? 0.3640 0.3527 0.4163 -0.0058 0.0226  -0.0418 201 A1BTF A C7  
1092 C C8  . A1BTF B .   ? 0.3298 0.3201 0.3979 -0.0031 0.0205  -0.0390 201 A1BTF A C8  
1093 C C10 . A1BTF B .   ? 0.2998 0.2861 0.3824 -0.0028 0.0177  -0.0412 201 A1BTF A C10 
1094 C C13 . A1BTF B .   ? 0.2869 0.2837 0.3827 0.0016  0.0173  -0.0284 201 A1BTF A C13 
1095 C C15 . A1BTF B .   ? 0.3085 0.3047 0.3909 0.0000  0.0193  -0.0316 201 A1BTF A C15 
1096 O O1  . A1BTF B .   ? 0.2922 0.2943 0.4183 0.0053  0.0172  -0.0176 201 A1BTF A O1  
1097 C C14 . A1BTF B .   ? 0.2851 0.2876 0.3943 0.0036  0.0155  -0.0196 201 A1BTF A C14 
1098 C C11 . A1BTF B .   ? 0.2903 0.2821 0.3867 0.0004  0.0168  -0.0333 201 A1BTF A C11 
1099 C C12 . A1BTF B .   ? 0.2837 0.2756 0.3939 0.0014  0.0147  -0.0298 201 A1BTF A C12 
1100 C C9  . A1BTF B .   ? 0.3250 0.3104 0.3930 -0.0047 0.0194  -0.0438 201 A1BTF A C9  
1101 O O   . A1BTF B .   ? 0.3786 0.3631 0.4149 -0.0094 0.0200  -0.0453 201 A1BTF A O   
1102 N N   . A1BTF B .   ? 0.3715 0.3637 0.4287 -0.0046 0.0273  -0.0397 201 A1BTF A N   
1103 C C1  . A1BTF B .   ? 0.3870 0.3798 0.4198 -0.0085 0.0269  -0.0379 201 A1BTF A C1  
1104 C C   . A1BTF B .   ? 0.3820 0.3776 0.4133 -0.0071 0.0182  -0.0315 201 A1BTF A C   
1105 C C3  . A1BTF B .   ? 0.4015 0.3900 0.4244 -0.0135 0.0412  -0.0467 201 A1BTF A C3  
1106 C C2  . A1BTF B .   ? 0.3942 0.3855 0.4161 -0.0115 0.0315  -0.0399 201 A1BTF A C2  
# 
