data_7I66
# 
_entry.id   7I66 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   7I66         pdb_00007i66 10.2210/pdb7i66/pdb 
WWPDB D_1001408365 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-04-02 ? 
2 'Structure model' 1 1 2025-04-09 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Refinement description' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            pdbx_initial_refinement_model 
# 
_pdbx_database_status.entry_id                        7I66 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2025-03-12 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frank.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lithgo, R.M.'        1  ? 
'Fairhead, M.'        2  ? 
'Koekemoer, L.'       3  ? 
'Balcomb, B.H.'       4  ? 
'Capkin, E.'          5  ? 
'Chandran, A.V.'      6  ? 
'Golding, M.'         7  ? 
'Godoy, A.S.'         8  ? 
'Aschenbrenner, J.C.' 9  ? 
'Marples, P.G.'       10 ? 
'Ni, X.'              11 ? 
'Thompson, W.'        12 ? 
'Tomlinson, C.W.E.'   13 ? 
'Wild, C.'            14 ? 
'Winokan, M.'         15 ? 
'Xavier, M.-A.E.'     16 ? 
'Kenton, N.'          17 ? 
'Tucker, J.'          18 ? 
'DiPoto, M.'          19 ? 
'Lee, A.'             20 ? 
'Fearon, D.'          21 ? 
'von Delft, F.'       22 ? 
# 
_citation.id                        primary 
_citation.title                     
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Lithgo, R.M.'        ? 1  
primary 'Fairhead, M.'        ? 2  
primary 'Koekemoer, L.'       ? 3  
primary 'Balcomb, B.H.'       ? 4  
primary 'Capkin, E.'          ? 5  
primary 'Chandran, A.V.'      ? 6  
primary 'Golding, M.'         ? 7  
primary 'Godoy, A.S.'         ? 8  
primary 'Aschenbrenner, J.C.' ? 9  
primary 'Marples, P.G.'       ? 10 
primary 'Ni, X.'              ? 11 
primary 'Thompson, W.'        ? 12 
primary 'Tomlinson, C.W.E.'   ? 13 
primary 'Wild, C.'            ? 14 
primary 'Winokan, M.'         ? 15 
primary 'Xavier, M.-A.E.'     ? 16 
primary 'Kenton, N.'          ? 17 
primary 'Tucker, J.'          ? 18 
primary 'DiPoto, M.'          ? 19 
primary 'Lee, A.'             ? 20 
primary 'Fearon, D.'          ? 21 
primary 'von Delft, F.'       ? 22 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Protease 2A'                                                     15892.732 1   3.4.22.29 ? ? ? 
2 non-polymer syn '(3S)-1-[2-(methylsulfanyl)phenyl]-6-oxopiperidine-3-carboxamide' 264.343   1   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                        65.409    1   ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                              78.133    1   ?         ? ? ? 
5 water       nat water                                                             18.015    139 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'P2A,Picornain 2A,Protein 2A' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '(3S)-1-[2-(methylsulfanyl)phenyl]-6-oxopiperidine-3-carboxamide' A1B4H 
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 
A1B4H non-polymer         . '(3S)-1-[2-(methylsulfanyl)phenyl]-6-oxopiperidine-3-carboxamide' ? 'C13 H16 N2 O2 S' 264.343 
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        A1B4H 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1B4H 
_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 A1B4H 1   201 201 A1B4H LIG A . 
C 3 ZN    1   202 1   ZN    ZN  A . 
D 4 DMS   1   203 2   DMS   DMS A . 
E 5 HOH   1   301 124 HOH   HOH A . 
E 5 HOH   2   302 135 HOH   HOH A . 
E 5 HOH   3   303 98  HOH   HOH A . 
E 5 HOH   4   304 59  HOH   HOH A . 
E 5 HOH   5   305 18  HOH   HOH A . 
E 5 HOH   6   306 117 HOH   HOH A . 
E 5 HOH   7   307 109 HOH   HOH A . 
E 5 HOH   8   308 50  HOH   HOH A . 
E 5 HOH   9   309 119 HOH   HOH A . 
E 5 HOH   10  310 36  HOH   HOH A . 
E 5 HOH   11  311 29  HOH   HOH A . 
E 5 HOH   12  312 37  HOH   HOH A . 
E 5 HOH   13  313 47  HOH   HOH A . 
E 5 HOH   14  314 88  HOH   HOH A . 
E 5 HOH   15  315 104 HOH   HOH A . 
E 5 HOH   16  316 42  HOH   HOH A . 
E 5 HOH   17  317 25  HOH   HOH A . 
E 5 HOH   18  318 118 HOH   HOH A . 
E 5 HOH   19  319 73  HOH   HOH A . 
E 5 HOH   20  320 74  HOH   HOH A . 
E 5 HOH   21  321 129 HOH   HOH A . 
E 5 HOH   22  322 60  HOH   HOH A . 
E 5 HOH   23  323 32  HOH   HOH A . 
E 5 HOH   24  324 27  HOH   HOH A . 
E 5 HOH   25  325 9   HOH   HOH A . 
E 5 HOH   26  326 13  HOH   HOH A . 
E 5 HOH   27  327 103 HOH   HOH A . 
E 5 HOH   28  328 87  HOH   HOH A . 
E 5 HOH   29  329 8   HOH   HOH A . 
E 5 HOH   30  330 51  HOH   HOH A . 
E 5 HOH   31  331 79  HOH   HOH A . 
E 5 HOH   32  332 94  HOH   HOH A . 
E 5 HOH   33  333 34  HOH   HOH A . 
E 5 HOH   34  334 7   HOH   HOH A . 
E 5 HOH   35  335 97  HOH   HOH A . 
E 5 HOH   36  336 22  HOH   HOH A . 
E 5 HOH   37  337 100 HOH   HOH A . 
E 5 HOH   38  338 83  HOH   HOH A . 
E 5 HOH   39  339 48  HOH   HOH A . 
E 5 HOH   40  340 105 HOH   HOH A . 
E 5 HOH   41  341 78  HOH   HOH A . 
E 5 HOH   42  342 14  HOH   HOH A . 
E 5 HOH   43  343 95  HOH   HOH A . 
E 5 HOH   44  344 139 HOH   HOH A . 
E 5 HOH   45  345 16  HOH   HOH A . 
E 5 HOH   46  346 17  HOH   HOH A . 
E 5 HOH   47  347 85  HOH   HOH A . 
E 5 HOH   48  348 55  HOH   HOH A . 
E 5 HOH   49  349 54  HOH   HOH A . 
E 5 HOH   50  350 12  HOH   HOH A . 
E 5 HOH   51  351 141 HOH   HOH A . 
E 5 HOH   52  352 24  HOH   HOH A . 
E 5 HOH   53  353 82  HOH   HOH A . 
E 5 HOH   54  354 72  HOH   HOH A . 
E 5 HOH   55  355 35  HOH   HOH A . 
E 5 HOH   56  356 23  HOH   HOH A . 
E 5 HOH   57  357 84  HOH   HOH A . 
E 5 HOH   58  358 21  HOH   HOH A . 
E 5 HOH   59  359 58  HOH   HOH A . 
E 5 HOH   60  360 45  HOH   HOH A . 
E 5 HOH   61  361 75  HOH   HOH A . 
E 5 HOH   62  362 53  HOH   HOH A . 
E 5 HOH   63  363 113 HOH   HOH A . 
E 5 HOH   64  364 40  HOH   HOH A . 
E 5 HOH   65  365 19  HOH   HOH A . 
E 5 HOH   66  366 10  HOH   HOH A . 
E 5 HOH   67  367 2   HOH   HOH A . 
E 5 HOH   68  368 102 HOH   HOH A . 
E 5 HOH   69  369 107 HOH   HOH A . 
E 5 HOH   70  370 115 HOH   HOH A . 
E 5 HOH   71  371 39  HOH   HOH A . 
E 5 HOH   72  372 101 HOH   HOH A . 
E 5 HOH   73  373 56  HOH   HOH A . 
E 5 HOH   74  374 114 HOH   HOH A . 
E 5 HOH   75  375 57  HOH   HOH A . 
E 5 HOH   76  376 38  HOH   HOH A . 
E 5 HOH   77  377 63  HOH   HOH A . 
E 5 HOH   78  378 71  HOH   HOH A . 
E 5 HOH   79  379 3   HOH   HOH A . 
E 5 HOH   80  380 6   HOH   HOH A . 
E 5 HOH   81  381 80  HOH   HOH A . 
E 5 HOH   82  382 89  HOH   HOH A . 
E 5 HOH   83  383 90  HOH   HOH A . 
E 5 HOH   84  384 86  HOH   HOH A . 
E 5 HOH   85  385 93  HOH   HOH A . 
E 5 HOH   86  386 4   HOH   HOH A . 
E 5 HOH   87  387 49  HOH   HOH A . 
E 5 HOH   88  388 126 HOH   HOH A . 
E 5 HOH   89  389 112 HOH   HOH A . 
E 5 HOH   90  390 134 HOH   HOH A . 
E 5 HOH   91  391 67  HOH   HOH A . 
E 5 HOH   92  392 30  HOH   HOH A . 
E 5 HOH   93  393 92  HOH   HOH A . 
E 5 HOH   94  394 81  HOH   HOH A . 
E 5 HOH   95  395 91  HOH   HOH A . 
E 5 HOH   96  396 96  HOH   HOH A . 
E 5 HOH   97  397 76  HOH   HOH A . 
E 5 HOH   98  398 26  HOH   HOH A . 
E 5 HOH   99  399 132 HOH   HOH A . 
E 5 HOH   100 400 131 HOH   HOH A . 
E 5 HOH   101 401 5   HOH   HOH A . 
E 5 HOH   102 402 20  HOH   HOH A . 
E 5 HOH   103 403 110 HOH   HOH A . 
E 5 HOH   104 404 33  HOH   HOH A . 
E 5 HOH   105 405 15  HOH   HOH A . 
E 5 HOH   106 406 77  HOH   HOH A . 
E 5 HOH   107 407 111 HOH   HOH A . 
E 5 HOH   108 408 46  HOH   HOH A . 
E 5 HOH   109 409 64  HOH   HOH A . 
E 5 HOH   110 410 28  HOH   HOH A . 
E 5 HOH   111 411 66  HOH   HOH A . 
E 5 HOH   112 412 68  HOH   HOH A . 
E 5 HOH   113 413 122 HOH   HOH A . 
E 5 HOH   114 414 130 HOH   HOH A . 
E 5 HOH   115 415 43  HOH   HOH A . 
E 5 HOH   116 416 133 HOH   HOH A . 
E 5 HOH   117 417 41  HOH   HOH A . 
E 5 HOH   118 418 70  HOH   HOH A . 
E 5 HOH   119 419 123 HOH   HOH A . 
E 5 HOH   120 420 138 HOH   HOH A . 
E 5 HOH   121 421 120 HOH   HOH A . 
E 5 HOH   122 422 108 HOH   HOH A . 
E 5 HOH   123 423 125 HOH   HOH A . 
E 5 HOH   124 424 31  HOH   HOH A . 
E 5 HOH   125 425 61  HOH   HOH A . 
E 5 HOH   126 426 52  HOH   HOH A . 
E 5 HOH   127 427 65  HOH   HOH A . 
E 5 HOH   128 428 44  HOH   HOH A . 
E 5 HOH   129 429 136 HOH   HOH A . 
E 5 HOH   130 430 121 HOH   HOH A . 
E 5 HOH   131 431 140 HOH   HOH A . 
E 5 HOH   132 432 116 HOH   HOH A . 
E 5 HOH   133 433 69  HOH   HOH A . 
E 5 HOH   134 434 127 HOH   HOH A . 
E 5 HOH   135 435 99  HOH   HOH A . 
E 5 HOH   136 436 137 HOH   HOH A . 
E 5 HOH   137 437 106 HOH   HOH A . 
E 5 HOH   138 438 62  HOH   HOH A . 
E 5 HOH   139 439 128 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           7I66 
_cell.length_a           73.367 
_cell.length_b           61.367 
_cell.length_c           32.693 
_cell.angle_alpha        90.00 
_cell.angle_beta         93.12 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I66 
_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          7I66 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.31 
_exptl_crystal.density_percent_sol   46.80 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2025-01-24 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92204 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.92204 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7I66 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             36.63 
_reflns.d_resolution_high            1.46 
_reflns.number_obs                   24586 
_reflns.percent_possible_obs         98.5 
_reflns.pdbx_Rmerge_I_obs            0.121 
_reflns.pdbx_netI_over_sigmaI        5.1 
_reflns.pdbx_redundancy              5.5 
_reflns.pdbx_Rrim_I_all              0.133 
_reflns.pdbx_Rpim_I_all              0.053 
_reflns.pdbx_CC_half                 0.996 
_reflns.pdbx_number_measured_all     135460 
_reflns.pdbx_chi_squared             0.64 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.46 
_reflns_shell.d_res_low                   1.54 
_reflns_shell.number_measured_all         12650 
_reflns_shell.number_unique_obs           3369 
_reflns_shell.Rmerge_I_obs                1.561 
_reflns_shell.pdbx_chi_squared            0.41 
_reflns_shell.pdbx_redundancy             3.8 
_reflns_shell.percent_possible_obs        92.5 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.6 
_reflns_shell.pdbx_Rrim_I_all             1.820 
_reflns_shell.pdbx_Rpim_I_all             0.914 
_reflns_shell.pdbx_CC_half                0.533 
_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                                 7I66 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     24079 
_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                             36.63 
_refine.ls_d_res_high                            1.464 
_refine.ls_percent_reflns_obs                    96.4 
_refine.ls_R_factor_obs                          0.2144 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2139 
_refine.ls_R_factor_R_free                       0.2247 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.880 
_refine.ls_number_reflns_R_free                  1175 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.950 
_refine.correlation_coeff_Fo_to_Fc_free          0.947 
_refine.B_iso_mean                               23.31 
_refine.aniso_B[1][1]                            -3.15890 
_refine.aniso_B[2][2]                            -1.09170 
_refine.aniso_B[3][3]                            4.25060 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -0.72340 
_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             0.080 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.075 
_refine.pdbx_overall_SU_R_Blow_DPI               0.084 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.078 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7I66 
_refine_analyze.Luzzati_coordinate_error_obs    0.23 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1074 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         23 
_refine_hist.number_atoms_solvent             139 
_refine_hist.number_atoms_total               1236 
_refine_hist.d_res_high                       1.464 
_refine_hist.d_res_low                        36.63 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
t_bond_d                  0.011 ? 2.00  1126 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.00  ? 2.00  1532 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  375  'X-RAY DIFFRACTION' SINUSOIDAL   
t_incorr_chiral_ct        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_pseud_angle             ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_trig_c_planes           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_gen_planes              ?     ? 5.00  203  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1126 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           4.04  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           14.16 ? ?     ?    '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  935  'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   51 
_refine_ls_shell.d_res_high                       1.46 
_refine_ls_shell.d_res_low                        1.48 
_refine_ls_shell.number_reflns_R_work             462 
_refine_ls_shell.R_factor_R_work                  0.3709 
_refine_ls_shell.percent_reflns_obs               63.00 
_refine_ls_shell.R_factor_R_free                  0.3789 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            4.15 
_refine_ls_shell.number_reflns_R_free             20 
_refine_ls_shell.number_reflns_all                482 
_refine_ls_shell.R_factor_all                     0.3712 
# 
_struct.entry_id                  7I66 
_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-0037607-001 (A71EV2A-x4922)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I66 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    POLG_CX16G 
_struct_ref.pdbx_db_accession          Q65900 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_struct_ref.pdbx_align_begin           869 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              7I66 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 144 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q65900 
_struct_ref_seq.db_align_beg                  869 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1012 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       7 
_struct_ref_seq.pdbx_auth_seq_align_end       150 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2 AA2 THR A 18  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
HELX_P HELX_P3 AA3 SER A 30  ? ARG A 32  ? SER A 36  ARG A 38  5 ? 3 
HELX_P HELX_P4 AA4 SER A 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
HELX_P HELX_P5 AA5 GLU A 100 ? CYS A 104 ? GLU A 106 CYS A 110 5 ? 5 
HELX_P HELX_P6 AA6 LEU A 134 ? GLU A 139 ? LEU A 140 GLU A 145 5 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 50  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 56  A ZN 202 1_555 ? ? ? ? ? ? ? 2.360 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.265 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.374 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 C ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.125 ? ? 
# 
_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_555 109.3 ? 
2 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 106.5 ? 
3 SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 116.2 ? 
4 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 109.5 ? 
5 SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 99.7  ? 
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_555 115.4 ? 
# 
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 LEU A 35  ? N LEU A 41  O VAL A 12  ? O VAL A 18  
AA2 1 2 O LYS A 64  ? O LYS A 70  N CYS A 59  ? N CYS A 65  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N LEU A 108 ? N LEU A 114 O VAL A 115 ? O VAL A 121 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O 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                   7I66 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     303 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     303 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   2_656 
_pdbx_validate_symm_contact.dist              1.07 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    ASN 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     14 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -96.53 
_pdbx_validate_torsion.psi             34.90 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     439 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   E 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
_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         15.1840 
_pdbx_refine_tls.origin_y         6.5551 
_pdbx_refine_tls.origin_z         14.2159 
_pdbx_refine_tls.T[1][1]          -0.0216 
_pdbx_refine_tls.T[2][2]          -0.0161 
_pdbx_refine_tls.T[3][3]          -0.0302 
_pdbx_refine_tls.T[1][2]          0.0006 
_pdbx_refine_tls.T[1][3]          -0.0216 
_pdbx_refine_tls.T[2][3]          -0.0103 
_pdbx_refine_tls.L[1][1]          1.1771 
_pdbx_refine_tls.L[2][2]          2.0312 
_pdbx_refine_tls.L[3][3]          0.9022 
_pdbx_refine_tls.L[1][2]          1.0127 
_pdbx_refine_tls.L[1][3]          -0.1794 
_pdbx_refine_tls.L[2][3]          -0.6743 
_pdbx_refine_tls.S[1][1]          -0.0699 
_pdbx_refine_tls.S[1][2]          0.0194 
_pdbx_refine_tls.S[1][3]          0.0903 
_pdbx_refine_tls.S[2][1]          0.0668 
_pdbx_refine_tls.S[2][2]          0.0710 
_pdbx_refine_tls.S[2][3]          -0.0501 
_pdbx_refine_tls.S[3][1]          0.0160 
_pdbx_refine_tls.S[3][2]          -0.0444 
_pdbx_refine_tls.S[3][3]          -0.0011 
# 
_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 
A1B4H N1   N  N N 1   
A1B4H C4   C  Y N 2   
A1B4H C5   C  Y N 3   
A1B4H C6   C  Y N 4   
A1B4H C7   C  N N 5   
A1B4H C8   C  N S 6   
A1B4H C10  C  N N 7   
A1B4H O1   O  N N 8   
A1B4H C12  C  N N 9   
A1B4H C11  C  N N 10  
A1B4H C9   C  N N 11  
A1B4H O    O  N N 12  
A1B4H N    N  N N 13  
A1B4H C1   C  Y N 14  
A1B4H S    S  N N 15  
A1B4H C    C  N N 16  
A1B4H C3   C  Y N 17  
A1B4H C2   C  Y N 18  
A1B4H H11  H  N N 19  
A1B4H H10  H  N N 20  
A1B4H H6   H  N N 21  
A1B4H H7   H  N N 22  
A1B4H H9   H  N N 23  
A1B4H H8   H  N N 24  
A1B4H H    H  N N 25  
A1B4H H13  H  N N 26  
A1B4H H12  H  N N 27  
A1B4H H15  H  N N 28  
A1B4H H14  H  N N 29  
A1B4H H2   H  N N 30  
A1B4H H1   H  N N 31  
A1B4H H3   H  N N 32  
A1B4H H5   H  N N 33  
A1B4H H4   H  N N 34  
ALA   N    N  N N 35  
ALA   CA   C  N S 36  
ALA   C    C  N N 37  
ALA   O    O  N N 38  
ALA   CB   C  N N 39  
ALA   OXT  O  N N 40  
ALA   H    H  N N 41  
ALA   H2   H  N N 42  
ALA   HA   H  N N 43  
ALA   HB1  H  N N 44  
ALA   HB2  H  N N 45  
ALA   HB3  H  N N 46  
ALA   HXT  H  N N 47  
ARG   N    N  N N 48  
ARG   CA   C  N S 49  
ARG   C    C  N N 50  
ARG   O    O  N N 51  
ARG   CB   C  N N 52  
ARG   CG   C  N N 53  
ARG   CD   C  N N 54  
ARG   NE   N  N N 55  
ARG   CZ   C  N N 56  
ARG   NH1  N  N N 57  
ARG   NH2  N  N N 58  
ARG   OXT  O  N N 59  
ARG   H    H  N N 60  
ARG   H2   H  N N 61  
ARG   HA   H  N N 62  
ARG   HB2  H  N N 63  
ARG   HB3  H  N N 64  
ARG   HG2  H  N N 65  
ARG   HG3  H  N N 66  
ARG   HD2  H  N N 67  
ARG   HD3  H  N N 68  
ARG   HE   H  N N 69  
ARG   HH11 H  N N 70  
ARG   HH12 H  N N 71  
ARG   HH21 H  N N 72  
ARG   HH22 H  N N 73  
ARG   HXT  H  N N 74  
ASN   N    N  N N 75  
ASN   CA   C  N S 76  
ASN   C    C  N N 77  
ASN   O    O  N N 78  
ASN   CB   C  N N 79  
ASN   CG   C  N N 80  
ASN   OD1  O  N N 81  
ASN   ND2  N  N N 82  
ASN   OXT  O  N N 83  
ASN   H    H  N N 84  
ASN   H2   H  N N 85  
ASN   HA   H  N N 86  
ASN   HB2  H  N N 87  
ASN   HB3  H  N N 88  
ASN   HD21 H  N N 89  
ASN   HD22 H  N N 90  
ASN   HXT  H  N N 91  
ASP   N    N  N N 92  
ASP   CA   C  N S 93  
ASP   C    C  N N 94  
ASP   O    O  N N 95  
ASP   CB   C  N N 96  
ASP   CG   C  N N 97  
ASP   OD1  O  N N 98  
ASP   OD2  O  N N 99  
ASP   OXT  O  N N 100 
ASP   H    H  N N 101 
ASP   H2   H  N N 102 
ASP   HA   H  N N 103 
ASP   HB2  H  N N 104 
ASP   HB3  H  N N 105 
ASP   HD2  H  N N 106 
ASP   HXT  H  N N 107 
CYS   N    N  N N 108 
CYS   CA   C  N R 109 
CYS   C    C  N N 110 
CYS   O    O  N N 111 
CYS   CB   C  N N 112 
CYS   SG   S  N N 113 
CYS   OXT  O  N N 114 
CYS   H    H  N N 115 
CYS   H2   H  N N 116 
CYS   HA   H  N N 117 
CYS   HB2  H  N N 118 
CYS   HB3  H  N N 119 
CYS   HG   H  N N 120 
CYS   HXT  H  N N 121 
DMS   S    S  N N 122 
DMS   O    O  N N 123 
DMS   C1   C  N N 124 
DMS   C2   C  N N 125 
DMS   H11  H  N N 126 
DMS   H12  H  N N 127 
DMS   H13  H  N N 128 
DMS   H21  H  N N 129 
DMS   H22  H  N N 130 
DMS   H23  H  N N 131 
GLN   N    N  N N 132 
GLN   CA   C  N S 133 
GLN   C    C  N N 134 
GLN   O    O  N N 135 
GLN   CB   C  N N 136 
GLN   CG   C  N N 137 
GLN   CD   C  N N 138 
GLN   OE1  O  N N 139 
GLN   NE2  N  N N 140 
GLN   OXT  O  N N 141 
GLN   H    H  N N 142 
GLN   H2   H  N N 143 
GLN   HA   H  N N 144 
GLN   HB2  H  N N 145 
GLN   HB3  H  N N 146 
GLN   HG2  H  N N 147 
GLN   HG3  H  N N 148 
GLN   HE21 H  N N 149 
GLN   HE22 H  N N 150 
GLN   HXT  H  N N 151 
GLU   N    N  N N 152 
GLU   CA   C  N S 153 
GLU   C    C  N N 154 
GLU   O    O  N N 155 
GLU   CB   C  N N 156 
GLU   CG   C  N N 157 
GLU   CD   C  N N 158 
GLU   OE1  O  N N 159 
GLU   OE2  O  N N 160 
GLU   OXT  O  N N 161 
GLU   H    H  N N 162 
GLU   H2   H  N N 163 
GLU   HA   H  N N 164 
GLU   HB2  H  N N 165 
GLU   HB3  H  N N 166 
GLU   HG2  H  N N 167 
GLU   HG3  H  N N 168 
GLU   HE2  H  N N 169 
GLU   HXT  H  N N 170 
GLY   N    N  N N 171 
GLY   CA   C  N N 172 
GLY   C    C  N N 173 
GLY   O    O  N N 174 
GLY   OXT  O  N N 175 
GLY   H    H  N N 176 
GLY   H2   H  N N 177 
GLY   HA2  H  N N 178 
GLY   HA3  H  N N 179 
GLY   HXT  H  N N 180 
HIS   N    N  N N 181 
HIS   CA   C  N S 182 
HIS   C    C  N N 183 
HIS   O    O  N N 184 
HIS   CB   C  N N 185 
HIS   CG   C  Y N 186 
HIS   ND1  N  Y N 187 
HIS   CD2  C  Y N 188 
HIS   CE1  C  Y N 189 
HIS   NE2  N  Y N 190 
HIS   OXT  O  N N 191 
HIS   H    H  N N 192 
HIS   H2   H  N N 193 
HIS   HA   H  N N 194 
HIS   HB2  H  N N 195 
HIS   HB3  H  N N 196 
HIS   HD1  H  N N 197 
HIS   HD2  H  N N 198 
HIS   HE1  H  N N 199 
HIS   HE2  H  N N 200 
HIS   HXT  H  N N 201 
HOH   O    O  N N 202 
HOH   H1   H  N N 203 
HOH   H2   H  N N 204 
ILE   N    N  N N 205 
ILE   CA   C  N S 206 
ILE   C    C  N N 207 
ILE   O    O  N N 208 
ILE   CB   C  N S 209 
ILE   CG1  C  N N 210 
ILE   CG2  C  N N 211 
ILE   CD1  C  N N 212 
ILE   OXT  O  N N 213 
ILE   H    H  N N 214 
ILE   H2   H  N N 215 
ILE   HA   H  N N 216 
ILE   HB   H  N N 217 
ILE   HG12 H  N N 218 
ILE   HG13 H  N N 219 
ILE   HG21 H  N N 220 
ILE   HG22 H  N N 221 
ILE   HG23 H  N N 222 
ILE   HD11 H  N N 223 
ILE   HD12 H  N N 224 
ILE   HD13 H  N N 225 
ILE   HXT  H  N N 226 
LEU   N    N  N N 227 
LEU   CA   C  N S 228 
LEU   C    C  N N 229 
LEU   O    O  N N 230 
LEU   CB   C  N N 231 
LEU   CG   C  N N 232 
LEU   CD1  C  N N 233 
LEU   CD2  C  N N 234 
LEU   OXT  O  N N 235 
LEU   H    H  N N 236 
LEU   H2   H  N N 237 
LEU   HA   H  N N 238 
LEU   HB2  H  N N 239 
LEU   HB3  H  N N 240 
LEU   HG   H  N N 241 
LEU   HD11 H  N N 242 
LEU   HD12 H  N N 243 
LEU   HD13 H  N N 244 
LEU   HD21 H  N N 245 
LEU   HD22 H  N N 246 
LEU   HD23 H  N N 247 
LEU   HXT  H  N N 248 
LYS   N    N  N N 249 
LYS   CA   C  N S 250 
LYS   C    C  N N 251 
LYS   O    O  N N 252 
LYS   CB   C  N N 253 
LYS   CG   C  N N 254 
LYS   CD   C  N N 255 
LYS   CE   C  N N 256 
LYS   NZ   N  N N 257 
LYS   OXT  O  N N 258 
LYS   H    H  N N 259 
LYS   H2   H  N N 260 
LYS   HA   H  N N 261 
LYS   HB2  H  N N 262 
LYS   HB3  H  N N 263 
LYS   HG2  H  N N 264 
LYS   HG3  H  N N 265 
LYS   HD2  H  N N 266 
LYS   HD3  H  N N 267 
LYS   HE2  H  N N 268 
LYS   HE3  H  N N 269 
LYS   HZ1  H  N N 270 
LYS   HZ2  H  N N 271 
LYS   HZ3  H  N N 272 
LYS   HXT  H  N N 273 
MET   N    N  N N 274 
MET   CA   C  N S 275 
MET   C    C  N N 276 
MET   O    O  N N 277 
MET   CB   C  N N 278 
MET   CG   C  N N 279 
MET   SD   S  N N 280 
MET   CE   C  N N 281 
MET   OXT  O  N N 282 
MET   H    H  N N 283 
MET   H2   H  N N 284 
MET   HA   H  N N 285 
MET   HB2  H  N N 286 
MET   HB3  H  N N 287 
MET   HG2  H  N N 288 
MET   HG3  H  N N 289 
MET   HE1  H  N N 290 
MET   HE2  H  N N 291 
MET   HE3  H  N N 292 
MET   HXT  H  N N 293 
PHE   N    N  N N 294 
PHE   CA   C  N S 295 
PHE   C    C  N N 296 
PHE   O    O  N N 297 
PHE   CB   C  N N 298 
PHE   CG   C  Y N 299 
PHE   CD1  C  Y N 300 
PHE   CD2  C  Y N 301 
PHE   CE1  C  Y N 302 
PHE   CE2  C  Y N 303 
PHE   CZ   C  Y N 304 
PHE   OXT  O  N N 305 
PHE   H    H  N N 306 
PHE   H2   H  N N 307 
PHE   HA   H  N N 308 
PHE   HB2  H  N N 309 
PHE   HB3  H  N N 310 
PHE   HD1  H  N N 311 
PHE   HD2  H  N N 312 
PHE   HE1  H  N N 313 
PHE   HE2  H  N N 314 
PHE   HZ   H  N N 315 
PHE   HXT  H  N N 316 
PRO   N    N  N N 317 
PRO   CA   C  N S 318 
PRO   C    C  N N 319 
PRO   O    O  N N 320 
PRO   CB   C  N N 321 
PRO   CG   C  N N 322 
PRO   CD   C  N N 323 
PRO   OXT  O  N N 324 
PRO   H    H  N N 325 
PRO   HA   H  N N 326 
PRO   HB2  H  N N 327 
PRO   HB3  H  N N 328 
PRO   HG2  H  N N 329 
PRO   HG3  H  N N 330 
PRO   HD2  H  N N 331 
PRO   HD3  H  N N 332 
PRO   HXT  H  N N 333 
SER   N    N  N N 334 
SER   CA   C  N S 335 
SER   C    C  N N 336 
SER   O    O  N N 337 
SER   CB   C  N N 338 
SER   OG   O  N N 339 
SER   OXT  O  N N 340 
SER   H    H  N N 341 
SER   H2   H  N N 342 
SER   HA   H  N N 343 
SER   HB2  H  N N 344 
SER   HB3  H  N N 345 
SER   HG   H  N N 346 
SER   HXT  H  N N 347 
THR   N    N  N N 348 
THR   CA   C  N S 349 
THR   C    C  N N 350 
THR   O    O  N N 351 
THR   CB   C  N R 352 
THR   OG1  O  N N 353 
THR   CG2  C  N N 354 
THR   OXT  O  N N 355 
THR   H    H  N N 356 
THR   H2   H  N N 357 
THR   HA   H  N N 358 
THR   HB   H  N N 359 
THR   HG1  H  N N 360 
THR   HG21 H  N N 361 
THR   HG22 H  N N 362 
THR   HG23 H  N N 363 
THR   HXT  H  N N 364 
TRP   N    N  N N 365 
TRP   CA   C  N S 366 
TRP   C    C  N N 367 
TRP   O    O  N N 368 
TRP   CB   C  N N 369 
TRP   CG   C  Y N 370 
TRP   CD1  C  Y N 371 
TRP   CD2  C  Y N 372 
TRP   NE1  N  Y N 373 
TRP   CE2  C  Y N 374 
TRP   CE3  C  Y N 375 
TRP   CZ2  C  Y N 376 
TRP   CZ3  C  Y N 377 
TRP   CH2  C  Y N 378 
TRP   OXT  O  N N 379 
TRP   H    H  N N 380 
TRP   H2   H  N N 381 
TRP   HA   H  N N 382 
TRP   HB2  H  N N 383 
TRP   HB3  H  N N 384 
TRP   HD1  H  N N 385 
TRP   HE1  H  N N 386 
TRP   HE3  H  N N 387 
TRP   HZ2  H  N N 388 
TRP   HZ3  H  N N 389 
TRP   HH2  H  N N 390 
TRP   HXT  H  N N 391 
TYR   N    N  N N 392 
TYR   CA   C  N S 393 
TYR   C    C  N N 394 
TYR   O    O  N N 395 
TYR   CB   C  N N 396 
TYR   CG   C  Y N 397 
TYR   CD1  C  Y N 398 
TYR   CD2  C  Y N 399 
TYR   CE1  C  Y N 400 
TYR   CE2  C  Y N 401 
TYR   CZ   C  Y N 402 
TYR   OH   O  N N 403 
TYR   OXT  O  N N 404 
TYR   H    H  N N 405 
TYR   H2   H  N N 406 
TYR   HA   H  N N 407 
TYR   HB2  H  N N 408 
TYR   HB3  H  N N 409 
TYR   HD1  H  N N 410 
TYR   HD2  H  N N 411 
TYR   HE1  H  N N 412 
TYR   HE2  H  N N 413 
TYR   HH   H  N N 414 
TYR   HXT  H  N N 415 
VAL   N    N  N N 416 
VAL   CA   C  N S 417 
VAL   C    C  N N 418 
VAL   O    O  N N 419 
VAL   CB   C  N N 420 
VAL   CG1  C  N N 421 
VAL   CG2  C  N N 422 
VAL   OXT  O  N N 423 
VAL   H    H  N N 424 
VAL   H2   H  N N 425 
VAL   HA   H  N N 426 
VAL   HB   H  N N 427 
VAL   HG11 H  N N 428 
VAL   HG12 H  N N 429 
VAL   HG13 H  N N 430 
VAL   HG21 H  N N 431 
VAL   HG22 H  N N 432 
VAL   HG23 H  N N 433 
VAL   HXT  H  N N 434 
ZN    ZN   ZN N N 435 
# 
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 
A1B4H C   S    sing N N 1   
A1B4H S   C1   sing N N 2   
A1B4H C1  C2   doub Y N 3   
A1B4H C2  C3   sing Y N 4   
A1B4H C3  C4   doub Y N 5   
A1B4H C4  C5   sing Y N 6   
A1B4H C5  C6   doub Y N 7   
A1B4H C1  C6   sing Y N 8   
A1B4H C6  N    sing N N 9   
A1B4H N   C7   sing N N 10  
A1B4H C7  C8   sing N N 11  
A1B4H C9  C8   sing N N 12  
A1B4H N1  C9   sing N N 13  
A1B4H O   C9   doub N N 14  
A1B4H C8  C10  sing N N 15  
A1B4H C10 C11  sing N N 16  
A1B4H C11 C12  sing N N 17  
A1B4H N   C12  sing N N 18  
A1B4H C12 O1   doub N N 19  
A1B4H N1  H11  sing N N 20  
A1B4H N1  H10  sing N N 21  
A1B4H C4  H6   sing N N 22  
A1B4H C5  H7   sing N N 23  
A1B4H C7  H9   sing N N 24  
A1B4H C7  H8   sing N N 25  
A1B4H C8  H    sing N N 26  
A1B4H C10 H13  sing N N 27  
A1B4H C10 H12  sing N N 28  
A1B4H C11 H15  sing N N 29  
A1B4H C11 H14  sing N N 30  
A1B4H C   H2   sing N N 31  
A1B4H C   H1   sing N N 32  
A1B4H C   H3   sing N N 33  
A1B4H C3  H5   sing N N 34  
A1B4H C2  H4   sing N N 35  
ALA   N   CA   sing N N 36  
ALA   N   H    sing N N 37  
ALA   N   H2   sing N N 38  
ALA   CA  C    sing N N 39  
ALA   CA  CB   sing N N 40  
ALA   CA  HA   sing N N 41  
ALA   C   O    doub N N 42  
ALA   C   OXT  sing N N 43  
ALA   CB  HB1  sing N N 44  
ALA   CB  HB2  sing N N 45  
ALA   CB  HB3  sing N N 46  
ALA   OXT HXT  sing N N 47  
ARG   N   CA   sing N N 48  
ARG   N   H    sing N N 49  
ARG   N   H2   sing N N 50  
ARG   CA  C    sing N N 51  
ARG   CA  CB   sing N N 52  
ARG   CA  HA   sing N N 53  
ARG   C   O    doub N N 54  
ARG   C   OXT  sing N N 55  
ARG   CB  CG   sing N N 56  
ARG   CB  HB2  sing N N 57  
ARG   CB  HB3  sing N N 58  
ARG   CG  CD   sing N N 59  
ARG   CG  HG2  sing N N 60  
ARG   CG  HG3  sing N N 61  
ARG   CD  NE   sing N N 62  
ARG   CD  HD2  sing N N 63  
ARG   CD  HD3  sing N N 64  
ARG   NE  CZ   sing N N 65  
ARG   NE  HE   sing N N 66  
ARG   CZ  NH1  sing N N 67  
ARG   CZ  NH2  doub N N 68  
ARG   NH1 HH11 sing N N 69  
ARG   NH1 HH12 sing N N 70  
ARG   NH2 HH21 sing N N 71  
ARG   NH2 HH22 sing N N 72  
ARG   OXT HXT  sing N N 73  
ASN   N   CA   sing N N 74  
ASN   N   H    sing N N 75  
ASN   N   H2   sing N N 76  
ASN   CA  C    sing N N 77  
ASN   CA  CB   sing N N 78  
ASN   CA  HA   sing N N 79  
ASN   C   O    doub N N 80  
ASN   C   OXT  sing N N 81  
ASN   CB  CG   sing N N 82  
ASN   CB  HB2  sing N N 83  
ASN   CB  HB3  sing N N 84  
ASN   CG  OD1  doub N N 85  
ASN   CG  ND2  sing N N 86  
ASN   ND2 HD21 sing N N 87  
ASN   ND2 HD22 sing N N 88  
ASN   OXT HXT  sing N N 89  
ASP   N   CA   sing N N 90  
ASP   N   H    sing N N 91  
ASP   N   H2   sing N N 92  
ASP   CA  C    sing N N 93  
ASP   CA  CB   sing N N 94  
ASP   CA  HA   sing N N 95  
ASP   C   O    doub N N 96  
ASP   C   OXT  sing N N 97  
ASP   CB  CG   sing N N 98  
ASP   CB  HB2  sing N N 99  
ASP   CB  HB3  sing N N 100 
ASP   CG  OD1  doub N N 101 
ASP   CG  OD2  sing N N 102 
ASP   OD2 HD2  sing N N 103 
ASP   OXT HXT  sing N N 104 
CYS   N   CA   sing N N 105 
CYS   N   H    sing N N 106 
CYS   N   H2   sing N N 107 
CYS   CA  C    sing N N 108 
CYS   CA  CB   sing N N 109 
CYS   CA  HA   sing N N 110 
CYS   C   O    doub N N 111 
CYS   C   OXT  sing N N 112 
CYS   CB  SG   sing N N 113 
CYS   CB  HB2  sing N N 114 
CYS   CB  HB3  sing N N 115 
CYS   SG  HG   sing N N 116 
CYS   OXT HXT  sing N N 117 
DMS   S   O    doub N N 118 
DMS   S   C1   sing N N 119 
DMS   S   C2   sing N N 120 
DMS   C1  H11  sing N N 121 
DMS   C1  H12  sing N N 122 
DMS   C1  H13  sing N N 123 
DMS   C2  H21  sing N N 124 
DMS   C2  H22  sing N N 125 
DMS   C2  H23  sing N N 126 
GLN   N   CA   sing N N 127 
GLN   N   H    sing N N 128 
GLN   N   H2   sing N N 129 
GLN   CA  C    sing N N 130 
GLN   CA  CB   sing N N 131 
GLN   CA  HA   sing N N 132 
GLN   C   O    doub N N 133 
GLN   C   OXT  sing N N 134 
GLN   CB  CG   sing N N 135 
GLN   CB  HB2  sing N N 136 
GLN   CB  HB3  sing N N 137 
GLN   CG  CD   sing N N 138 
GLN   CG  HG2  sing N N 139 
GLN   CG  HG3  sing N N 140 
GLN   CD  OE1  doub N N 141 
GLN   CD  NE2  sing N N 142 
GLN   NE2 HE21 sing N N 143 
GLN   NE2 HE22 sing N N 144 
GLN   OXT HXT  sing N N 145 
GLU   N   CA   sing N N 146 
GLU   N   H    sing N N 147 
GLU   N   H2   sing N N 148 
GLU   CA  C    sing N N 149 
GLU   CA  CB   sing N N 150 
GLU   CA  HA   sing N N 151 
GLU   C   O    doub N N 152 
GLU   C   OXT  sing N N 153 
GLU   CB  CG   sing N N 154 
GLU   CB  HB2  sing N N 155 
GLU   CB  HB3  sing N N 156 
GLU   CG  CD   sing N N 157 
GLU   CG  HG2  sing N N 158 
GLU   CG  HG3  sing N N 159 
GLU   CD  OE1  doub N N 160 
GLU   CD  OE2  sing N N 161 
GLU   OE2 HE2  sing N N 162 
GLU   OXT HXT  sing N N 163 
GLY   N   CA   sing N N 164 
GLY   N   H    sing N N 165 
GLY   N   H2   sing N N 166 
GLY   CA  C    sing N N 167 
GLY   CA  HA2  sing N N 168 
GLY   CA  HA3  sing N N 169 
GLY   C   O    doub N N 170 
GLY   C   OXT  sing N N 171 
GLY   OXT HXT  sing N N 172 
HIS   N   CA   sing N N 173 
HIS   N   H    sing N N 174 
HIS   N   H2   sing N N 175 
HIS   CA  C    sing N N 176 
HIS   CA  CB   sing N N 177 
HIS   CA  HA   sing N N 178 
HIS   C   O    doub N N 179 
HIS   C   OXT  sing N N 180 
HIS   CB  CG   sing N N 181 
HIS   CB  HB2  sing N N 182 
HIS   CB  HB3  sing N N 183 
HIS   CG  ND1  sing Y N 184 
HIS   CG  CD2  doub Y N 185 
HIS   ND1 CE1  doub Y N 186 
HIS   ND1 HD1  sing N N 187 
HIS   CD2 NE2  sing Y N 188 
HIS   CD2 HD2  sing N N 189 
HIS   CE1 NE2  sing Y N 190 
HIS   CE1 HE1  sing N N 191 
HIS   NE2 HE2  sing N N 192 
HIS   OXT HXT  sing N N 193 
HOH   O   H1   sing N N 194 
HOH   O   H2   sing N N 195 
ILE   N   CA   sing N N 196 
ILE   N   H    sing N N 197 
ILE   N   H2   sing N N 198 
ILE   CA  C    sing N N 199 
ILE   CA  CB   sing N N 200 
ILE   CA  HA   sing N N 201 
ILE   C   O    doub N N 202 
ILE   C   OXT  sing N N 203 
ILE   CB  CG1  sing N N 204 
ILE   CB  CG2  sing N N 205 
ILE   CB  HB   sing N N 206 
ILE   CG1 CD1  sing N N 207 
ILE   CG1 HG12 sing N N 208 
ILE   CG1 HG13 sing N N 209 
ILE   CG2 HG21 sing N N 210 
ILE   CG2 HG22 sing N N 211 
ILE   CG2 HG23 sing N N 212 
ILE   CD1 HD11 sing N N 213 
ILE   CD1 HD12 sing N N 214 
ILE   CD1 HD13 sing N N 215 
ILE   OXT HXT  sing N N 216 
LEU   N   CA   sing N N 217 
LEU   N   H    sing N N 218 
LEU   N   H2   sing N N 219 
LEU   CA  C    sing N N 220 
LEU   CA  CB   sing N N 221 
LEU   CA  HA   sing N N 222 
LEU   C   O    doub N N 223 
LEU   C   OXT  sing N N 224 
LEU   CB  CG   sing N N 225 
LEU   CB  HB2  sing N N 226 
LEU   CB  HB3  sing N N 227 
LEU   CG  CD1  sing N N 228 
LEU   CG  CD2  sing N N 229 
LEU   CG  HG   sing N N 230 
LEU   CD1 HD11 sing N N 231 
LEU   CD1 HD12 sing N N 232 
LEU   CD1 HD13 sing N N 233 
LEU   CD2 HD21 sing N N 234 
LEU   CD2 HD22 sing N N 235 
LEU   CD2 HD23 sing N N 236 
LEU   OXT HXT  sing N N 237 
LYS   N   CA   sing N N 238 
LYS   N   H    sing N N 239 
LYS   N   H2   sing N N 240 
LYS   CA  C    sing N N 241 
LYS   CA  CB   sing N N 242 
LYS   CA  HA   sing N N 243 
LYS   C   O    doub N N 244 
LYS   C   OXT  sing N N 245 
LYS   CB  CG   sing N N 246 
LYS   CB  HB2  sing N N 247 
LYS   CB  HB3  sing N N 248 
LYS   CG  CD   sing N N 249 
LYS   CG  HG2  sing N N 250 
LYS   CG  HG3  sing N N 251 
LYS   CD  CE   sing N N 252 
LYS   CD  HD2  sing N N 253 
LYS   CD  HD3  sing N N 254 
LYS   CE  NZ   sing N N 255 
LYS   CE  HE2  sing N N 256 
LYS   CE  HE3  sing N N 257 
LYS   NZ  HZ1  sing N N 258 
LYS   NZ  HZ2  sing N N 259 
LYS   NZ  HZ3  sing N N 260 
LYS   OXT HXT  sing N N 261 
MET   N   CA   sing N N 262 
MET   N   H    sing N N 263 
MET   N   H2   sing N N 264 
MET   CA  C    sing N N 265 
MET   CA  CB   sing N N 266 
MET   CA  HA   sing N N 267 
MET   C   O    doub N N 268 
MET   C   OXT  sing N N 269 
MET   CB  CG   sing N N 270 
MET   CB  HB2  sing N N 271 
MET   CB  HB3  sing N N 272 
MET   CG  SD   sing N N 273 
MET   CG  HG2  sing N N 274 
MET   CG  HG3  sing N N 275 
MET   SD  CE   sing N N 276 
MET   CE  HE1  sing N N 277 
MET   CE  HE2  sing N N 278 
MET   CE  HE3  sing N N 279 
MET   OXT HXT  sing N N 280 
PHE   N   CA   sing N N 281 
PHE   N   H    sing N N 282 
PHE   N   H2   sing N N 283 
PHE   CA  C    sing N N 284 
PHE   CA  CB   sing N N 285 
PHE   CA  HA   sing N N 286 
PHE   C   O    doub N N 287 
PHE   C   OXT  sing N N 288 
PHE   CB  CG   sing N N 289 
PHE   CB  HB2  sing N N 290 
PHE   CB  HB3  sing N N 291 
PHE   CG  CD1  doub Y N 292 
PHE   CG  CD2  sing Y N 293 
PHE   CD1 CE1  sing Y N 294 
PHE   CD1 HD1  sing N N 295 
PHE   CD2 CE2  doub Y N 296 
PHE   CD2 HD2  sing N N 297 
PHE   CE1 CZ   doub Y N 298 
PHE   CE1 HE1  sing N N 299 
PHE   CE2 CZ   sing Y N 300 
PHE   CE2 HE2  sing N N 301 
PHE   CZ  HZ   sing N N 302 
PHE   OXT HXT  sing N N 303 
PRO   N   CA   sing N N 304 
PRO   N   CD   sing N N 305 
PRO   N   H    sing N N 306 
PRO   CA  C    sing N N 307 
PRO   CA  CB   sing N N 308 
PRO   CA  HA   sing N N 309 
PRO   C   O    doub N N 310 
PRO   C   OXT  sing N N 311 
PRO   CB  CG   sing N N 312 
PRO   CB  HB2  sing N N 313 
PRO   CB  HB3  sing N N 314 
PRO   CG  CD   sing N N 315 
PRO   CG  HG2  sing N N 316 
PRO   CG  HG3  sing N N 317 
PRO   CD  HD2  sing N N 318 
PRO   CD  HD3  sing N N 319 
PRO   OXT HXT  sing N N 320 
SER   N   CA   sing N N 321 
SER   N   H    sing N N 322 
SER   N   H2   sing N N 323 
SER   CA  C    sing N N 324 
SER   CA  CB   sing N N 325 
SER   CA  HA   sing N N 326 
SER   C   O    doub N N 327 
SER   C   OXT  sing N N 328 
SER   CB  OG   sing N N 329 
SER   CB  HB2  sing N N 330 
SER   CB  HB3  sing N N 331 
SER   OG  HG   sing N N 332 
SER   OXT HXT  sing N N 333 
THR   N   CA   sing N N 334 
THR   N   H    sing N N 335 
THR   N   H2   sing N N 336 
THR   CA  C    sing N N 337 
THR   CA  CB   sing N N 338 
THR   CA  HA   sing N N 339 
THR   C   O    doub N N 340 
THR   C   OXT  sing N N 341 
THR   CB  OG1  sing N N 342 
THR   CB  CG2  sing N N 343 
THR   CB  HB   sing N N 344 
THR   OG1 HG1  sing N N 345 
THR   CG2 HG21 sing N N 346 
THR   CG2 HG22 sing N N 347 
THR   CG2 HG23 sing N N 348 
THR   OXT HXT  sing N N 349 
TRP   N   CA   sing N N 350 
TRP   N   H    sing N N 351 
TRP   N   H2   sing N N 352 
TRP   CA  C    sing N N 353 
TRP   CA  CB   sing N N 354 
TRP   CA  HA   sing N N 355 
TRP   C   O    doub N N 356 
TRP   C   OXT  sing N N 357 
TRP   CB  CG   sing N N 358 
TRP   CB  HB2  sing N N 359 
TRP   CB  HB3  sing N N 360 
TRP   CG  CD1  doub Y N 361 
TRP   CG  CD2  sing Y N 362 
TRP   CD1 NE1  sing Y N 363 
TRP   CD1 HD1  sing N N 364 
TRP   CD2 CE2  doub Y N 365 
TRP   CD2 CE3  sing Y N 366 
TRP   NE1 CE2  sing Y N 367 
TRP   NE1 HE1  sing N N 368 
TRP   CE2 CZ2  sing Y N 369 
TRP   CE3 CZ3  doub Y N 370 
TRP   CE3 HE3  sing N N 371 
TRP   CZ2 CH2  doub Y N 372 
TRP   CZ2 HZ2  sing N N 373 
TRP   CZ3 CH2  sing Y N 374 
TRP   CZ3 HZ3  sing N N 375 
TRP   CH2 HH2  sing N N 376 
TRP   OXT HXT  sing N N 377 
TYR   N   CA   sing N N 378 
TYR   N   H    sing N N 379 
TYR   N   H2   sing N N 380 
TYR   CA  C    sing N N 381 
TYR   CA  CB   sing N N 382 
TYR   CA  HA   sing N N 383 
TYR   C   O    doub N N 384 
TYR   C   OXT  sing N N 385 
TYR   CB  CG   sing N N 386 
TYR   CB  HB2  sing N N 387 
TYR   CB  HB3  sing N N 388 
TYR   CG  CD1  doub Y N 389 
TYR   CG  CD2  sing Y N 390 
TYR   CD1 CE1  sing Y N 391 
TYR   CD1 HD1  sing N N 392 
TYR   CD2 CE2  doub Y N 393 
TYR   CD2 HD2  sing N N 394 
TYR   CE1 CZ   doub Y N 395 
TYR   CE1 HE1  sing N N 396 
TYR   CE2 CZ   sing Y N 397 
TYR   CE2 HE2  sing N N 398 
TYR   CZ  OH   sing N N 399 
TYR   OH  HH   sing N N 400 
TYR   OXT HXT  sing N N 401 
VAL   N   CA   sing N N 402 
VAL   N   H    sing N N 403 
VAL   N   H2   sing N N 404 
VAL   CA  C    sing N N 405 
VAL   CA  CB   sing N N 406 
VAL   CA  HA   sing N N 407 
VAL   C   O    doub N N 408 
VAL   C   OXT  sing N N 409 
VAL   CB  CG1  sing N N 410 
VAL   CB  CG2  sing N N 411 
VAL   CB  HB   sing N N 412 
VAL   CG1 HG11 sing N N 413 
VAL   CG1 HG12 sing N N 414 
VAL   CG1 HG13 sing N N 415 
VAL   CG2 HG21 sing N N 416 
VAL   CG2 HG22 sing N N 417 
VAL   CG2 HG23 sing N N 418 
VAL   OXT HXT  sing N N 419 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171399 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002344 
_pdbx_deposit_group.group_description   
'Crystollographic structure of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitor' 
_pdbx_deposit_group.group_title         
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8POA 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    7I66 
_atom_sites.fract_transf_matrix[1][1]   0.013630 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000743 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016295 
_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]   0.030633 
_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   ? 19.098 5.773   24.277 1.00 24.61 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 20.256 5.880   23.393 1.00 25.17 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 20.288 4.742   22.386 1.00 23.63 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 19.563 3.748   22.548 1.00 23.39 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 21.558 5.941   24.197 1.00 28.46 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 21.768 4.738   24.919 1.00 32.28 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 21.089 4.915   21.325 1.00 21.70 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 21.272 3.901   20.298 1.00 20.76 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 21.577 4.482   18.933 1.00 19.91 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 21.134 5.599   18.605 1.00 20.09 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 22.306 3.722   18.118 1.00 18.21 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 22.661 4.170   16.781 1.00 18.19 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 22.625 3.000   15.766 1.00 17.04 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 22.596 1.837   16.170 1.00 18.23 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 24.072 4.757   16.817 1.00 19.76 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 22.625 3.313   14.457 1.00 15.79 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.753 2.346   13.373 1.00 16.62 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 24.148 2.544   12.761 1.00 18.21 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.541 3.666   12.489 1.00 18.56 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.699 2.601   12.256 1.00 16.01 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 20.277 2.535   12.812 1.00 15.78 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.854 1.538   11.155 1.00 17.34 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.243 3.215   11.871 1.00 16.06 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.870 1.455   12.489 1.00 19.57 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 26.190 1.482   11.889 1.00 21.08 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 26.169 0.720   10.572 1.00 22.20 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 25.995 -0.491  10.567 1.00 23.26 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.195 0.857   12.855 1.00 20.79 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.366 1.678   14.114 1.00 20.27 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 28.157 2.821   14.119 1.00 20.59 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 26.643 1.386   15.259 1.00 20.34 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 28.319 3.585   15.273 1.00 20.90 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 26.789 2.144   16.415 1.00 21.19 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 27.633 3.240   16.417 1.00 21.91 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 27.734 4.003   17.541 1.00 23.41 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 26.280 1.440   9.445  1.00 21.94 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 26.264 0.862   8.105  1.00 22.44 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.353 1.519   7.275  1.00 23.56 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.390 2.750   7.155  1.00 23.73 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.871 1.018   7.433  1.00 24.01 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.337 2.445   7.557  1.00 24.91 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.923 0.582   5.972  1.00 25.33 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.305 0.716   6.790  1.00 22.88 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.438 1.201   6.018  1.00 23.85 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.257 2.176   6.844  1.00 24.42 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.502 1.908   8.020  1.00 25.71 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.613 3.328   6.286  1.00 24.85 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.339 4.345   7.073  1.00 25.49 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.373 5.397   7.634  1.00 23.86 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.757 6.555   7.788  1.00 24.09 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.449 5.000   6.275  1.00 28.94 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.571 4.039   6.009  1.00 35.80 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.132 3.419   6.934  1.00 37.77 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.912 3.893   4.743  1.00 38.13 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.156 4.987   8.001  1.00 22.73 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.170 5.914   8.539  1.00 21.06 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.654 5.491   9.908  1.00 20.07 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.560 4.286   10.187 1.00 20.38 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.957 6.022   7.587  1.00 20.84 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.277 6.626   6.240  1.00 20.96 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 27.870 7.881   6.140  1.00 22.45 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 26.980 5.950   5.065  1.00 21.79 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.194 8.431   4.897  1.00 23.75 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.250 6.511   3.821  1.00 23.07 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 27.875 7.742   3.740  1.00 24.46 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.180 8.270   2.503  1.00 26.57 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.232 6.492   10.725 1.00 17.03 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.621 6.316   12.047 1.00 15.28 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.312 7.140   12.005 1.00 15.41 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.387 8.331   11.754 1.00 15.41 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.539 6.826   13.185 1.00 16.61 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.854 6.928   14.565 1.00 20.07 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.881 7.299   15.669 1.00 21.09 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 27.374 8.296   16.620 1.00 22.36 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 26.867 8.002   17.817 1.00 23.67 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 26.797 6.737   18.228 1.00 22.76 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 26.448 8.972   18.624 1.00 24.37 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 24.144 6.509   12.178 1.00 15.21 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.839 7.216   12.189 1.00 15.66 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.392 7.296   13.625 1.00 15.57 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 22.215 6.245   14.249 1.00 16.16 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.774 6.461   11.375 1.00 16.09 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.484 7.314   11.241 1.00 15.77 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.327 6.057   9.991  1.00 17.42 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 22.125 8.508   14.109 1.00 15.02 ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 21.685 8.788   15.458 1.00 14.52 ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 20.477 9.743   15.468 1.00 14.22 ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 20.240 10.508  14.492 1.00 13.88 ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 22.839 9.401   16.295 1.00 16.39 ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 23.903 8.349   16.569 1.00 19.28 ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 23.414 10.632  15.592 1.00 16.21 ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 19.738 9.762   16.597 1.00 13.43 ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 18.689 10.808  16.772 1.00 13.97 ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 19.412 12.177  16.781 1.00 14.55 ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 20.428 12.347  17.481 1.00 15.32 ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.956 10.680  18.110 1.00 15.54 ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 17.090 9.439   18.161 1.00 16.51 ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.560 8.383   18.557 1.00 17.95 ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 15.822 9.552   17.788 1.00 16.27 ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 18.903 13.139  16.008 1.00 13.28 ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 19.570 14.446  15.890 1.00 12.98 ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 19.674 15.116  17.251 1.00 14.56 ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 20.707 15.703  17.533 1.00 15.95 ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 18.814 15.331  14.910 1.00 12.65 ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.608 16.592  14.496 1.00 13.46 ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 18.673 17.524  13.706 1.00 14.27 ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.298 18.767  13.220 1.00 17.90 ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.382 19.894  13.921 1.00 18.95 ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 18.984 19.927  15.191 1.00 17.59 ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 19.873 21.004  13.359 1.00 18.56 ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 18.651 14.954  18.130 1.00 15.13 ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 18.723 15.618  19.456 1.00 16.03 ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 19.749 14.996  20.417 1.00 17.76 ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 20.046 15.600  21.471 1.00 18.99 ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 17.345 15.720  20.126 1.00 16.99 ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 16.765 14.414  20.577 1.00 18.14 ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 16.084 13.577  19.706 1.00 18.71 ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 16.771 13.845  21.813 1.00 19.13 ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 15.675 12.550  20.437 1.00 20.40 ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 16.078 12.653  21.707 1.00 20.26 ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 20.258 13.786  20.066 1.00 17.81 ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 21.234 13.092  20.902 1.00 19.47 ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 22.654 13.116  20.293 1.00 19.29 ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 23.571 12.513  20.864 1.00 20.14 ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 20.758 11.664  21.172 1.00 20.55 ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 19.418 11.535  21.910 1.00 21.96 ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 19.060 10.058  22.139 1.00 21.92 ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 19.448 12.310  23.268 1.00 21.63 ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 22.836 13.773  19.104 1.00 17.66 ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 24.148 13.835  18.472 1.00 18.17 ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 25.199 14.456  19.358 1.00 18.30 ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 24.924 15.434  20.028 1.00 18.63 ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 24.058 14.637  17.176 1.00 17.95 ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 26.421 13.898  19.344 1.00 18.44 ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 27.531 14.422  20.154 1.00 19.45 ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 28.354 15.507  19.416 1.00 19.92 ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 28.182 15.702  18.213 1.00 19.68 ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 28.450 13.229  20.527 1.00 21.62 ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 29.120 12.838  19.324 1.00 23.69 ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 27.690 12.080  21.153 1.00 20.86 ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 29.323 16.164  20.108 1.00 21.05 ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 30.244 17.091  19.430 1.00 22.66 ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 30.990 16.374  18.257 1.00 21.47 ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 31.142 16.959  17.186 1.00 21.67 ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 31.303 17.624  20.419 1.00 26.55 ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 30.733 18.414  21.548 1.00 33.70 ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 29.908 19.501  21.323 1.00 36.86 ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 30.941 18.290  22.885 1.00 36.42 ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 29.606 19.978  22.524 1.00 38.22 ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 30.203 19.282  23.495 1.00 38.25 ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 31.454 15.138  18.464 1.00 20.47 ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 32.140 14.379  17.399 1.00 21.51 ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 31.196 14.091  16.194 1.00 19.80 ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 31.611 14.203  15.039 1.00 19.44 ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 32.699 13.066  17.963 1.00 24.62 ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 33.510 12.273  16.950 1.00 32.58 ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.638 12.661  16.606 1.00 35.25 ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 32.972 11.166  16.441 1.00 34.22 ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 29.900 13.777  16.449 1.00 18.91 ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 28.918 13.602  15.376 1.00 18.84 ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 28.829 14.900  14.533 1.00 18.18 ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 28.888 14.828  13.306 1.00 19.33 ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 27.542 13.286  15.956 1.00 18.64 ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 27.395 11.872  16.441 1.00 21.02 ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 27.927 10.952  15.764 1.00 20.78 ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 26.734 11.674  17.485 1.00 20.82 ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 28.733 16.082  15.200 1.00 18.04 ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.646 17.355  14.470 1.00 18.32 ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 29.964 17.711  13.738 1.00 19.48 ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 29.899 18.294  12.646 1.00 19.51 ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 28.180 18.502  15.386 1.00 17.86 ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 26.699 18.515  15.611 1.00 18.39 ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 26.018 17.996  16.677 1.00 18.96 ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 25.713 19.049  14.722 1.00 17.93 ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 24.661 18.212  16.517 1.00 18.47 ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 24.445 18.799  15.296 1.00 18.21 ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 25.771 19.643  13.454 1.00 19.41 ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 23.258 19.246  14.699 1.00 19.29 ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.598 20.065  12.855 1.00 19.68 ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 23.357 19.833  13.456 1.00 19.45 ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 31.123 17.380  14.331 1.00 20.10 ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.442 17.629  13.731 1.00 21.28 ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.672 16.754  12.478 1.00 21.77 ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.545 17.078  11.669 1.00 23.19 ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 33.568 17.363  14.749 1.00 21.63 ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 31.926 15.633  12.353 1.00 19.02 ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 32.033 14.690  11.220 1.00 19.16 ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.672 14.537  10.542 1.00 17.86 ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.326 13.447  10.068 1.00 17.23 ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.543 13.326  11.700 1.00 19.25 ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 33.945 13.397  12.272 1.00 23.39 ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 34.944 13.363  11.537 1.00 25.64 ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 34.044 13.553  13.582 1.00 24.82 ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 29.916 15.653  10.453 1.00 17.82 ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.579 15.674  9.872  1.00 17.05 ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.581 15.316  8.399  1.00 19.14 ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.321 15.928  7.634  1.00 20.33 ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 27.987 17.079  10.036 1.00 17.50 ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.595 17.280  9.460  1.00 18.05 ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.547 16.447  10.210 1.00 20.43 ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.218 18.739  9.405  1.00 17.16 ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.669 14.396  7.979  1.00 18.01 ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.424 14.018  6.579  1.00 18.05 ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 26.064 14.628  6.122  1.00 17.96 ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 25.959 15.240  5.037  1.00 19.69 ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.397 12.470  6.439  1.00 18.17 ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 26.912 12.052  5.046  1.00 19.71 ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 28.782 11.874  6.723  1.00 18.30 ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 25.034 14.478  6.959  1.00 16.92 ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 23.685 14.950  6.656  1.00 17.34 ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 22.866 15.036  7.955  1.00 17.04 ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 23.073 14.222  8.846  1.00 17.21 ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 23.004 13.981  5.663  1.00 16.80 ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.537 14.216  5.427  1.00 17.62 ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 20.974 15.101  4.553  1.00 19.15 ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.452 13.499  6.033  1.00 17.23 ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.587 14.982  4.592  1.00 19.34 ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.251 14.033  5.523  1.00 17.91 ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.380 12.504  7.031  1.00 17.30 ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 18.000 13.495  5.858  1.00 17.30 ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.137 12.003  7.377  1.00 17.57 ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 17.967 12.524  6.821  1.00 17.01 ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 21.998 16.034  8.069  1.00 16.02 ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 21.101 16.199  9.205  1.00 16.67 ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 19.760 16.790  8.737  1.00 17.06 ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 19.743 17.626  7.822  1.00 17.50 ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 21.715 17.011  10.357 1.00 17.83 ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.206 18.399  9.974  1.00 21.24 ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.164 19.500  9.977  1.00 20.01 ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 21.381 20.515  9.276  1.00 23.77 ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 20.099 19.323  10.608 1.00 17.79 ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 18.661 16.377  9.381  1.00 15.93 ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.334 16.893  9.073  1.00 16.05 ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.576 17.041  10.370 1.00 16.90 ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 16.141 16.036  10.950 1.00 18.06 ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.591 15.953  8.119  1.00 17.09 ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.346 16.584  7.528  1.00 22.40 ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 14.688 17.363  8.238  1.00 23.63 ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 15.041 16.304  6.344  1.00 23.34 ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.379 18.306  10.809 1.00 16.41 ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 15.670 18.626  12.044 0.50 17.41 ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 15.683 18.570  12.058 0.50 17.32 ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 14.216 18.133  11.987 1.00 17.48 ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 13.705 17.612  12.973 1.00 19.08 ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 15.691 20.135  12.280 0.50 20.19 ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 15.817 20.036  12.469 0.50 20.00 ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 15.143 20.495  13.537 0.50 22.90 ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 15.505 20.931  11.414 0.50 22.56 ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 13.566 18.265  10.816 1.00 15.51 ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 12.179 17.822  10.679 1.00 16.58 ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 12.043 16.311  10.836 1.00 16.37 ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 10.969 15.858  11.186 1.00 17.76 ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 11.566 18.318  9.367  1.00 19.23 ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 11.899 17.465  8.278  1.00 23.39 ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 13.149 15.521  10.632 1.00 14.56 ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 13.112 14.058  10.785 1.00 15.16 ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 13.693 13.577  12.105 1.00 14.63 ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 13.661 12.381  12.352 1.00 14.41 ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 13.814 13.324  9.618  1.00 16.52 ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 13.212 13.595  8.252  1.00 18.44 ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 14.028 12.950  7.116  1.00 19.18 ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 14.001 11.479  7.186  1.00 16.21 ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 14.058 10.680  6.121  1.00 16.69 ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 14.172 11.197  4.893  1.00 15.40 ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 14.014 9.357   6.272  1.00 17.41 ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 14.360 14.473  12.880 1.00 15.43 ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 15.076 14.079  14.106 1.00 14.39 ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 16.210 13.109  13.772 1.00 13.47 ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 16.479 12.231  14.580 1.00 13.49 ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 14.168 13.548  15.239 1.00 13.74 ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 14.925 13.240  16.530 1.00 16.87 ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 15.822 14.040  16.899 1.00 16.75 ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 14.647 12.180  17.158 1.00 15.91 ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 16.865 13.252  12.575 1.00 12.98 ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 18.000 12.386  12.195 1.00 12.56 ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 19.288 13.152  11.953 1.00 13.59 ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 19.271 14.222  11.357 1.00 14.18 ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.688 11.601  10.913 1.00 12.57 ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 16.627 10.508  11.042 1.00 14.11 ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 16.490 9.749   9.698  1.00 13.63 ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 16.928 9.486   12.176 1.00 16.46 ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 20.410 12.500  12.264 1.00 13.37 ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 21.736 13.001  11.957 1.00 13.85 ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 22.616 11.785  11.594 1.00 14.77 ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 22.529 10.708  12.203 1.00 15.80 ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 22.302 13.823  13.128 1.00 13.38 ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 23.695 14.506  12.862 1.00 14.77 ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 23.851 15.802  13.639 1.00 16.61 ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 24.887 13.565  13.265 1.00 16.04 ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 23.374 11.923  10.520 1.00 14.63 ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 24.319 10.897  10.073 1.00 13.66 ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 25.737 11.533  10.125 1.00 15.84 ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 25.975 12.647  9.616  1.00 16.05 ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 24.005 10.351  8.647  1.00 14.60 ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 25.033 9.308   8.232  1.00 16.23 ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 22.598 9.765   8.585  1.00 14.69 ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 26.656 10.831  10.776 1.00 15.41 ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 28.062 11.266  10.842 1.00 15.51 ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 28.928 10.158  10.224 1.00 17.89 ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 28.442 9.030   10.028 1.00 17.17 ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 28.456 11.562  12.280 1.00 16.03 ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 28.211 10.406  13.069 1.00 19.41 ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 30.202 10.493  9.885  1.00 18.29 ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 31.120 9.518   9.284  1.00 20.60 ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 31.937 8.815   10.366 1.00 23.59 ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 32.254 9.413   11.405 1.00 24.06 ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 32.066 10.221  8.316  1.00 21.93 ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 32.804 11.229  8.990  1.00 25.37 ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 32.338 7.562   10.089 1.00 25.12 ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 33.119 6.735   11.011 1.00 28.30 ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 34.339 6.161   10.290 1.00 31.28 ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 34.286 5.900   9.077  1.00 32.04 ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 32.275 5.553   11.545 1.00 30.13 ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 31.977 4.643   10.477 1.00 32.16 ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 30.978 5.993   12.194 1.00 29.94 ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? 35.404 5.893   11.045 1.00 32.45 ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? 36.605 5.290   10.480 1.00 34.31 ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? 36.381 3.788   10.346 1.00 35.12 ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? 36.705 3.221   9.310  1.00 36.13 ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? 37.865 5.646   11.305 1.00 36.19 ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? 37.598 5.487   12.701 1.00 37.30 ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? 38.342 7.054   11.045 1.00 36.98 ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? 35.792 3.152   11.371 1.00 34.86 ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? 35.489 1.720   11.341 1.00 35.41 ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 34.291 1.412   10.428 1.00 35.05 ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 33.378 2.229   10.286 1.00 35.09 ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? 35.200 1.225   12.746 1.00 36.09 ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 34.273 0.206   9.864  1.00 34.75 ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 33.222 -0.279  8.972  1.00 34.37 ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 32.065 -0.894  9.776  1.00 33.06 ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 32.293 -1.762  10.615 1.00 33.55 ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 33.837 -1.341  8.034  1.00 37.59 ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 32.843 -2.005  7.096  1.00 44.79 ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 32.566 -1.180  5.862  1.00 53.39 ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 33.350 -0.291  5.467  1.00 56.04 ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 31.441 -1.469  5.216  1.00 54.84 ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 30.836 -0.426  9.529  1.00 31.00 ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 29.637 -0.953  10.167 1.00 30.11 ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 28.976 -2.038  9.334  1.00 29.43 ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 29.007 -1.978  8.096  1.00 29.69 ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 28.319 -3.007  9.995  1.00 28.69 ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 27.738 -4.119  9.245  1.00 29.28 ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 26.267 -4.358  9.514  1.00 26.60 ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 25.786 -5.490  9.324  1.00 25.06 ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 28.556 -5.399  9.407  1.00 33.56 ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 29.462 -5.534  10.976 1.00 45.12 ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 25.522 -3.272  9.857  1.00 24.88 ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 24.068 -3.367  9.979  1.00 25.19 ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 23.504 -3.362  8.548  1.00 25.82 ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 24.072 -2.755  7.632  1.00 27.59 ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 23.443 -2.199  10.782 1.00 27.12 ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 23.657 -2.263  12.287 1.00 33.68 ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 23.780 -3.381  12.819 1.00 35.65 ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 23.712 -1.181  12.936 1.00 34.24 ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 22.403 -4.054  8.361  1.00 24.84 ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 21.755 -4.154  7.060  1.00 24.04 ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 20.529 -3.242  7.044  1.00 22.10 ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 19.675 -3.440  7.891  1.00 22.03 ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 21.322 -5.607  6.873  1.00 26.20 ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 22.512 -6.408  6.761  1.00 27.41 ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 20.430 -5.789  5.653  1.00 26.59 ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 20.437 -2.252  6.119  1.00 19.97 ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 19.227 -1.414  6.075  1.00 18.62 ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 18.159 -2.136  5.233  1.00 18.81 ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 18.487 -2.639  4.139  1.00 19.82 ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 19.503 0.019   5.519  1.00 18.26 ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 20.684 0.724   6.219  1.00 19.10 ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 18.246 0.907   5.578  1.00 18.04 ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 20.434 0.952   7.743  1.00 19.82 ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 16.895 -2.149  5.690  1.00 17.30 ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 15.755 -2.721  4.957  1.00 17.88 ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 15.407 -1.827  3.767  1.00 18.86 ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 15.420 -0.608  3.900  1.00 19.23 ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 14.533 -2.754  5.880  1.00 17.67 ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 15.058 -2.425  2.627  1.00 19.48 ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 14.594 -1.684  1.468  1.00 19.51 ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 13.264 -2.377  1.124  1.00 20.03 ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 13.248 -3.351  0.366  1.00 21.79 ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 15.603 -1.771  0.335  1.00 20.78 ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 16.989 -1.258  0.738  1.00 21.67 ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 17.033 0.242   1.105  1.00 21.50 ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 18.405 0.666   1.397  1.00 20.20 ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 18.717 1.790   2.040  1.00 21.89 ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 17.759 2.627   2.442  1.00 18.58 ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 19.984 2.082   2.295  1.00 20.46 ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 12.164 -1.882  1.695  1.00 20.19 ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 10.845 -2.520  1.620  1.00 20.39 ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 9.739  -1.545  2.056  1.00 20.30 ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 10.018 -0.426  2.485  1.00 20.20 ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 10.853 -3.725  2.559  1.00 22.15 ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 11.027 -3.247  4.307  1.00 20.40 ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 8.469  -2.044  2.051  1.00 20.98 ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 7.330  -1.296  2.556  1.00 22.08 ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 6.663  -2.059  3.702  1.00 22.11 ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 5.480  -1.875  3.911  1.00 23.21 ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 6.303  -0.941  1.459  1.00 25.65 ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 5.652  -2.122  0.773  1.00 33.72 ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 5.976  -3.276  1.133  1.00 35.50 ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 4.824  -1.896  -0.149 1.00 38.73 ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 7.395  -2.939  4.440  1.00 20.89 ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 6.856  -3.642  5.636  1.00 18.98 ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 6.136  -2.696  6.565  1.00 18.88 ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 6.564  -1.550  6.748  1.00 20.07 ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 7.961  -4.367  6.415  1.00 19.55 ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 8.622  -5.847  5.605  1.00 22.90 ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 5.105  -3.209  7.220  1.00 17.52 ? 59  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 53  ? 4.396  -2.500  8.273  1.00 16.97 ? 59  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 53  ? 4.318  -3.334  9.559  1.00 16.56 ? 59  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 53  ? 3.520  -3.028  10.443 1.00 16.73 ? 59  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 53  ? 3.005  -2.013  7.854  1.00 18.77 ? 59  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 53  ? 3.014  -0.778  6.977  1.00 22.37 ? 59  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 53  ? 1.577  -0.330  6.720  1.00 28.00 ? 59  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 53  ? 0.980  -0.585  5.650  1.00 28.94 ? 59  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 53  ? 0.974  0.326   7.716  1.00 25.64 ? 59  GLN   A NE2 1 
ATOM   415  N  N   . THR   A 1 54  ? 5.152  -4.390  9.685  1.00 15.11 ? 60  THR   A N   1 
ATOM   416  C  CA  . THR   A 1 54  ? 5.290  -5.204  10.900 1.00 15.54 ? 60  THR   A CA  1 
ATOM   417  C  C   . THR   A 1 54  ? 6.808  -5.357  11.181 1.00 13.98 ? 60  THR   A C   1 
ATOM   418  O  O   . THR   A 1 54  ? 7.633  -5.386  10.247 1.00 14.89 ? 60  THR   A O   1 
ATOM   419  C  CB  . THR   A 1 54  ? 4.533  -6.565  10.829 1.00 20.05 ? 60  THR   A CB  1 
ATOM   420  O  OG1 . THR   A 1 54  ? 5.168  -7.447  9.905  1.00 22.17 ? 60  THR   A OG1 1 
ATOM   421  C  CG2 . THR   A 1 54  ? 3.068  -6.413  10.464 1.00 21.61 ? 60  THR   A CG2 1 
ATOM   422  N  N   . GLY   A 1 55  ? 7.156  -5.401  12.463 1.00 13.26 ? 61  GLY   A N   1 
ATOM   423  C  CA  . GLY   A 1 55  ? 8.567  -5.551  12.832 1.00 13.28 ? 61  GLY   A CA  1 
ATOM   424  C  C   . GLY   A 1 55  ? 8.707  -5.729  14.335 1.00 12.91 ? 61  GLY   A C   1 
ATOM   425  O  O   . GLY   A 1 55  ? 7.725  -5.978  15.036 1.00 13.02 ? 61  GLY   A O   1 
ATOM   426  N  N   . VAL   A 1 56  ? 9.941  -5.659  14.814 1.00 12.42 ? 62  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 56  ? 10.235 -5.776  16.250 1.00 12.46 ? 62  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 56  ? 11.145 -4.605  16.674 1.00 12.82 ? 62  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 56  ? 12.148 -4.320  16.018 1.00 14.18 ? 62  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 56  ? 10.883 -7.145  16.529 1.00 12.25 ? 62  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 56  ? 11.197 -7.278  18.026 1.00 13.29 ? 62  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 56  ? 9.963  -8.298  16.077 1.00 12.40 ? 62  VAL   A CG2 1 
ATOM   433  N  N   . TYR   A 1 57  ? 10.825 -3.946  17.805 1.00 11.57 ? 63  TYR   A N   1 
ATOM   434  C  CA  . TYR   A 1 57  ? 11.707 -2.860  18.289 1.00 11.22 ? 63  TYR   A CA  1 
ATOM   435  C  C   . TYR   A 1 57  ? 12.268 -3.157  19.667 1.00 13.66 ? 63  TYR   A C   1 
ATOM   436  O  O   . TYR   A 1 57  ? 11.673 -3.921  20.412 1.00 14.09 ? 63  TYR   A O   1 
ATOM   437  C  CB  . TYR   A 1 57  ? 11.051 -1.457  18.253 1.00 11.10 ? 63  TYR   A CB  1 
ATOM   438  C  CG  . TYR   A 1 57  ? 10.104 -1.155  19.405 1.00 12.17 ? 63  TYR   A CG  1 
ATOM   439  C  CD1 . TYR   A 1 57  ? 8.825  -1.700  19.442 1.00 13.14 ? 63  TYR   A CD1 1 
ATOM   440  C  CD2 . TYR   A 1 57  ? 10.466 -0.282  20.419 1.00 13.22 ? 63  TYR   A CD2 1 
ATOM   441  C  CE1 . TYR   A 1 57  ? 7.925  -1.371  20.452 1.00 14.49 ? 63  TYR   A CE1 1 
ATOM   442  C  CE2 . TYR   A 1 57  ? 9.570  0.067   21.433 1.00 13.56 ? 63  TYR   A CE2 1 
ATOM   443  C  CZ  . TYR   A 1 57  ? 8.304  -0.500  21.457 1.00 14.25 ? 63  TYR   A CZ  1 
ATOM   444  O  OH  . TYR   A 1 57  ? 7.401  -0.199  22.473 1.00 15.86 ? 63  TYR   A OH  1 
ATOM   445  N  N   . TYR   A 1 58  ? 13.417 -2.537  20.008 1.00 14.44 ? 64  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 58  ? 14.011 -2.693  21.323 1.00 14.92 ? 64  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 58  ? 13.576 -1.492  22.169 1.00 14.59 ? 64  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 58  ? 13.738 -0.345  21.740 1.00 13.99 ? 64  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 58  ? 15.557 -2.771  21.276 1.00 14.41 ? 64  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 58  ? 16.129 -2.926  22.659 1.00 16.13 ? 64  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 58  ? 15.840 -4.045  23.426 1.00 17.26 ? 64  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 58  ? 16.908 -1.923  23.225 1.00 17.37 ? 64  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 58  ? 16.351 -4.191  24.713 1.00 18.11 ? 64  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 58  ? 17.364 -2.021  24.539 1.00 18.23 ? 64  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 58  ? 17.063 -3.150  25.287 1.00 19.50 ? 64  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 58  ? 17.549 -3.272  26.566 1.00 22.83 ? 64  TYR   A OH  1 
ATOM   457  N  N   . CYS   A 1 59  ? 13.024 -1.786  23.382 1.00 14.34 ? 65  CYS   A N   1 
ATOM   458  C  CA  . CYS   A 1 59  ? 12.537 -0.812  24.366 1.00 15.29 ? 65  CYS   A CA  1 
ATOM   459  C  C   . CYS   A 1 59  ? 13.439 -0.877  25.624 1.00 17.31 ? 65  CYS   A C   1 
ATOM   460  O  O   . CYS   A 1 59  ? 13.281 -1.798  26.451 1.00 17.69 ? 65  CYS   A O   1 
ATOM   461  C  CB  . CYS   A 1 59  ? 11.081 -1.127  24.723 1.00 15.95 ? 65  CYS   A CB  1 
ATOM   462  S  SG  . CYS   A 1 59  ? 10.374 -0.007  25.959 1.00 18.33 ? 65  CYS   A SG  1 
ATOM   463  N  N   . SER   A 1 60  ? 14.401 0.071   25.764 1.00 16.48 ? 66  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 60  ? 15.333 0.035   26.873 1.00 17.54 ? 66  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 60  ? 14.673 0.167   28.232 1.00 17.69 ? 66  SER   A C   1 
ATOM   466  O  O   . SER   A 1 60  ? 15.138 -0.451  29.207 1.00 18.62 ? 66  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 60  ? 16.407 1.123   26.753 1.00 21.76 ? 66  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 60  ? 15.881 2.430   26.609 1.00 27.35 ? 66  SER   A OG  1 
ATOM   469  N  N   . SER   A 1 61  ? 13.583 0.969   28.298 1.00 17.51 ? 67  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 61  ? 12.838 1.179   29.556 1.00 18.26 ? 67  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 61  ? 12.080 -0.076  30.060 1.00 18.82 ? 67  SER   A C   1 
ATOM   472  O  O   . SER   A 1 61  ? 11.551 -0.063  31.198 1.00 20.49 ? 67  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 61  ? 11.908 2.381   29.465 1.00 18.59 ? 67  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 61  ? 10.802 2.121   28.612 1.00 20.28 ? 67  SER   A OG  1 
ATOM   475  N  N   . ARG   A 1 62  ? 12.086 -1.162  29.257 1.00 17.68 ? 68  ARG   A N   1 
ATOM   476  C  CA  . ARG   A 1 62  ? 11.544 -2.458  29.694 1.00 17.19 ? 68  ARG   A CA  1 
ATOM   477  C  C   . ARG   A 1 62  ? 12.588 -3.578  29.525 1.00 18.61 ? 68  ARG   A C   1 
ATOM   478  O  O   . ARG   A 1 62  ? 12.278 -4.724  29.837 1.00 20.10 ? 68  ARG   A O   1 
ATOM   479  C  CB  . ARG   A 1 62  ? 10.299 -2.834  28.884 1.00 18.08 ? 68  ARG   A CB  1 
ATOM   480  C  CG  . ARG   A 1 62  ? 9.155  -1.824  29.061 1.00 20.87 ? 68  ARG   A CG  1 
ATOM   481  C  CD  . ARG   A 1 62  ? 8.448  -2.098  30.380 1.00 21.13 ? 68  ARG   A CD  1 
ATOM   482  N  NE  . ARG   A 1 62  ? 7.311  -1.202  30.574 1.00 21.78 ? 68  ARG   A NE  1 
ATOM   483  C  CZ  . ARG   A 1 62  ? 7.366  -0.053  31.240 1.00 23.49 ? 68  ARG   A CZ  1 
ATOM   484  N  NH1 . ARG   A 1 62  ? 8.522  0.386   31.733 1.00 22.67 ? 68  ARG   A NH1 1 
ATOM   485  N  NH2 . ARG   A 1 62  ? 6.265  0.672   31.415 1.00 23.21 ? 68  ARG   A NH2 1 
ATOM   486  N  N   . ARG   A 1 63  ? 13.814 -3.270  28.994 1.00 17.58 ? 69  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 63  ? 14.861 -4.246  28.616 1.00 18.89 ? 69  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 63  ? 14.211 -5.389  27.785 1.00 18.93 ? 69  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 63  ? 14.441 -6.565  28.054 1.00 20.28 ? 69  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 63  ? 15.611 -4.824  29.833 1.00 20.88 ? 69  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 63  ? 16.569 -3.830  30.477 1.00 25.69 ? 69  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 63  ? 17.351 -4.536  31.570 1.00 30.96 ? 69  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 63  ? 18.004 -3.586  32.470 1.00 33.92 ? 69  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 63  ? 17.805 -3.544  33.787 1.00 33.56 ? 69  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 63  ? 16.952 -4.387  34.365 1.00 32.84 ? 69  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 63  ? 18.416 -2.620  34.529 1.00 30.09 ? 69  ARG   A NH2 1 
ATOM   497  N  N   . LYS   A 1 64  ? 13.345 -5.027  26.818 1.00 17.27 ? 70  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 64  ? 12.608 -6.055  26.059 1.00 17.39 ? 70  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 64  ? 12.450 -5.627  24.607 1.00 16.89 ? 70  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 64  ? 12.406 -4.435  24.321 1.00 15.95 ? 70  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 64  ? 11.160 -6.174  26.585 1.00 20.98 ? 70  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 64  ? 10.960 -7.025  27.830 1.00 28.43 ? 70  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 64  ? 9.476  -7.135  28.109 1.00 33.94 ? 70  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 64  ? 9.161  -8.139  29.189 1.00 41.61 ? 70  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 64  ? 9.816  -7.775  30.469 1.00 46.86 ? 70  LYS   A NZ  1 
ATOM   506  N  N   . HIS   A 1 65  ? 12.255 -6.627  23.727 1.00 17.11 ? 71  HIS   A N   1 
ATOM   507  C  CA  . HIS   A 1 65  ? 11.899 -6.385  22.332 1.00 16.80 ? 71  HIS   A CA  1 
ATOM   508  C  C   . HIS   A 1 65  ? 10.399 -6.652  22.201 1.00 17.64 ? 71  HIS   A C   1 
ATOM   509  O  O   . HIS   A 1 65  ? 9.881  -7.631  22.768 1.00 18.89 ? 71  HIS   A O   1 
ATOM   510  C  CB  . HIS   A 1 65  ? 12.641 -7.348  21.387 1.00 17.65 ? 71  HIS   A CB  1 
ATOM   511  C  CG  . HIS   A 1 65  ? 14.125 -7.150  21.364 1.00 17.88 ? 71  HIS   A CG  1 
ATOM   512  N  ND1 . HIS   A 1 65  ? 14.745 -6.390  20.369 1.00 20.07 ? 71  HIS   A ND1 1 
ATOM   513  C  CD2 . HIS   A 1 65  ? 15.080 -7.668  22.170 1.00 16.99 ? 71  HIS   A CD2 1 
ATOM   514  C  CE1 . HIS   A 1 65  ? 16.046 -6.427  20.642 1.00 17.72 ? 71  HIS   A CE1 1 
ATOM   515  N  NE2 . HIS   A 1 65  ? 16.294 -7.161  21.711 1.00 19.24 ? 71  HIS   A NE2 1 
ATOM   516  N  N   . TYR   A 1 66  ? 9.707  -5.818  21.423 1.00 15.17 ? 72  TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 66  ? 8.269  -6.008  21.223 1.00 14.87 ? 72  TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 66  ? 7.914  -6.082  19.727 1.00 14.66 ? 72  TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 66  ? 8.395  -5.250  18.970 1.00 13.45 ? 72  TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 66  ? 7.497  -4.818  21.793 1.00 15.31 ? 72  TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 66  ? 7.501  -4.694  23.294 1.00 16.88 ? 72  TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 66  ? 6.719  -5.530  24.082 1.00 18.81 ? 72  TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 66  ? 8.238  -3.701  23.929 1.00 18.69 ? 72  TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 66  ? 6.715  -5.420  25.472 1.00 19.74 ? 72  TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 66  ? 8.202  -3.548  25.310 1.00 19.59 ? 72  TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 66  ? 7.452  -4.424  26.083 1.00 20.51 ? 72  TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 66  ? 7.422  -4.288  27.466 1.00 22.58 ? 72  TYR   A OH  1 
ATOM   528  N  N   . PRO   A 1 67  ? 7.022  -7.013  19.337 1.00 14.98 ? 73  PRO   A N   1 
ATOM   529  C  CA  . PRO   A 1 67  ? 6.550  -7.070  17.930 1.00 14.98 ? 73  PRO   A CA  1 
ATOM   530  C  C   . PRO   A 1 67  ? 5.455  -5.993  17.740 1.00 15.92 ? 73  PRO   A C   1 
ATOM   531  O  O   . PRO   A 1 67  ? 4.579  -5.860  18.609 1.00 18.57 ? 73  PRO   A O   1 
ATOM   532  C  CB  . PRO   A 1 67  ? 5.948  -8.483  17.821 1.00 16.25 ? 73  PRO   A CB  1 
ATOM   533  C  CG  . PRO   A 1 67  ? 5.464  -8.780  19.239 1.00 16.88 ? 73  PRO   A CG  1 
ATOM   534  C  CD  . PRO   A 1 67  ? 6.418  -8.072  20.176 1.00 15.42 ? 73  PRO   A CD  1 
ATOM   535  N  N   . VAL   A 1 68  ? 5.521  -5.206  16.673 1.00 14.62 ? 74  VAL   A N   1 
ATOM   536  C  CA  . VAL   A 1 68  ? 4.548  -4.137  16.463 1.00 15.46 ? 74  VAL   A CA  1 
ATOM   537  C  C   . VAL   A 1 68  ? 4.093  -4.032  14.996 1.00 15.79 ? 74  VAL   A C   1 
ATOM   538  O  O   . VAL   A 1 68  ? 4.852  -4.310  14.072 1.00 15.26 ? 74  VAL   A O   1 
ATOM   539  C  CB  . VAL   A 1 68  ? 5.109  -2.720  16.853 1.00 16.59 ? 74  VAL   A CB  1 
ATOM   540  C  CG1 . VAL   A 1 68  ? 5.116  -2.453  18.359 1.00 18.19 ? 74  VAL   A CG1 1 
ATOM   541  C  CG2 . VAL   A 1 68  ? 6.468  -2.418  16.220 1.00 16.59 ? 74  VAL   A CG2 1 
ATOM   542  N  N   . SER   A 1 69  ? 2.855  -3.545  14.809 1.00 16.00 ? 75  SER   A N   1 
ATOM   543  C  CA  . SER   A 1 69  ? 2.353  -3.091  13.509 1.00 16.46 ? 75  SER   A CA  1 
ATOM   544  C  C   . SER   A 1 69  ? 2.579  -1.566  13.508 1.00 15.51 ? 75  SER   A C   1 
ATOM   545  O  O   . SER   A 1 69  ? 2.351  -0.915  14.527 1.00 16.31 ? 75  SER   A O   1 
ATOM   546  C  CB  . SER   A 1 69  ? 0.852  -3.350  13.376 1.00 19.73 ? 75  SER   A CB  1 
ATOM   547  O  OG  . SER   A 1 69  ? 0.551  -4.711  13.132 1.00 27.14 ? 75  SER   A OG  1 
ATOM   548  N  N   . PHE   A 1 70  ? 3.043  -0.986  12.384 1.00 14.51 ? 76  PHE   A N   1 
ATOM   549  C  CA  . PHE   A 1 70  ? 3.313  0.452   12.359 1.00 14.42 ? 76  PHE   A CA  1 
ATOM   550  C  C   . PHE   A 1 70  ? 2.840  1.098   11.067 1.00 16.20 ? 76  PHE   A C   1 
ATOM   551  O  O   . PHE   A 1 70  ? 2.823  0.458   10.024 1.00 17.60 ? 76  PHE   A O   1 
ATOM   552  C  CB  . PHE   A 1 70  ? 4.820  0.772   12.596 1.00 13.90 ? 76  PHE   A CB  1 
ATOM   553  C  CG  . PHE   A 1 70  ? 5.808  0.017   11.683 1.00 14.51 ? 76  PHE   A CG  1 
ATOM   554  C  CD1 . PHE   A 1 70  ? 6.359  -1.194  12.078 1.00 14.76 ? 76  PHE   A CD1 1 
ATOM   555  C  CD2 . PHE   A 1 70  ? 6.198  0.550   10.458 1.00 15.47 ? 76  PHE   A CD2 1 
ATOM   556  C  CE1 . PHE   A 1 70  ? 7.220  -1.905  11.215 1.00 15.50 ? 76  PHE   A CE1 1 
ATOM   557  C  CE2 . PHE   A 1 70  ? 7.091  -0.120  9.634  1.00 16.23 ? 76  PHE   A CE2 1 
ATOM   558  C  CZ  . PHE   A 1 70  ? 7.586  -1.352  10.001 1.00 15.14 ? 76  PHE   A CZ  1 
ATOM   559  N  N   . SER   A 1 71  ? 2.490  2.377   11.135 1.00 16.86 ? 77  SER   A N   1 
ATOM   560  C  CA  . SER   A 1 71  ? 1.981  3.094   9.975  1.00 17.75 ? 77  SER   A CA  1 
ATOM   561  C  C   . SER   A 1 71  ? 3.110  3.427   8.946  1.00 17.57 ? 77  SER   A C   1 
ATOM   562  O  O   . SER   A 1 71  ? 4.287  3.334   9.290  1.00 17.56 ? 77  SER   A O   1 
ATOM   563  C  CB  . SER   A 1 71  ? 1.258  4.351   10.454 1.00 19.56 ? 77  SER   A CB  1 
ATOM   564  O  OG  . SER   A 1 71  ? 2.188  5.223   11.080 1.00 20.02 ? 77  SER   A OG  1 
ATOM   565  N  N   . LYS   A 1 72  ? 2.779  3.755   7.654  1.00 17.67 ? 78  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 72  ? 3.810  4.139   6.692  1.00 18.52 ? 78  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 72  ? 4.408  5.522   7.083  1.00 19.18 ? 78  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 72  ? 3.727  6.323   7.727  1.00 20.53 ? 78  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 72  ? 3.267  4.132   5.233  1.00 21.53 ? 78  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 72  ? 2.828  2.738   4.782  1.00 24.98 ? 78  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 72  ? 2.391  2.688   3.316  1.00 29.19 ? 78  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 72  ? 1.996  1.276   2.939  1.00 34.52 ? 78  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 72  ? 1.484  1.178   1.538  1.00 38.50 ? 78  LYS   A NZ  1 
ATOM   574  N  N   . PRO   A 1 73  ? 5.636  5.846   6.659  1.00 19.08 ? 79  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 73  ? 6.233  7.151   7.035  1.00 19.65 ? 79  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 73  ? 5.394  8.333   6.589  1.00 20.08 ? 79  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 73  ? 4.890  8.375   5.442  1.00 19.01 ? 79  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 73  ? 7.585  7.135   6.332  1.00 21.40 ? 79  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 73  ? 7.903  5.653   6.169  1.00 22.06 ? 79  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 73  ? 6.566  5.057   5.838  1.00 19.27 ? 79  PRO   A CD  1 
ATOM   581  N  N   . SER   A 1 74  ? 5.139  9.234   7.531  1.00 20.26 ? 80  SER   A N   1 
ATOM   582  C  CA  . SER   A 1 74  ? 4.260  10.378  7.251  1.00 21.52 ? 80  SER   A CA  1 
ATOM   583  C  C   . SER   A 1 74  ? 4.597  11.613  8.129  1.00 21.80 ? 80  SER   A C   1 
ATOM   584  O  O   . SER   A 1 74  ? 5.504  11.539  8.978  1.00 21.54 ? 80  SER   A O   1 
ATOM   585  C  CB  . SER   A 1 74  ? 2.786  9.960   7.347  1.00 25.96 ? 80  SER   A CB  1 
ATOM   586  O  OG  . SER   A 1 74  ? 2.358  9.736   8.678  1.00 31.10 ? 80  SER   A OG  1 
ATOM   587  N  N   . LEU   A 1 75  ? 3.887  12.740  7.894  1.00 21.21 ? 81  LEU   A N   1 
ATOM   588  C  CA  . LEU   A 1 75  ? 4.028  14.018  8.600  1.00 21.72 ? 81  LEU   A CA  1 
ATOM   589  C  C   . LEU   A 1 75  ? 3.078  13.966  9.771  1.00 22.62 ? 81  LEU   A C   1 
ATOM   590  O  O   . LEU   A 1 75  ? 1.846  13.928  9.557  1.00 22.88 ? 81  LEU   A O   1 
ATOM   591  C  CB  . LEU   A 1 75  ? 3.558  15.173  7.692  1.00 23.09 ? 81  LEU   A CB  1 
ATOM   592  C  CG  . LEU   A 1 75  ? 4.557  16.161  7.127  1.00 26.50 ? 81  LEU   A CG  1 
ATOM   593  C  CD1 . LEU   A 1 75  ? 3.807  17.377  6.586  1.00 28.12 ? 81  LEU   A CD1 1 
ATOM   594  C  CD2 . LEU   A 1 75  ? 5.602  16.614  8.157  1.00 27.23 ? 81  LEU   A CD2 1 
ATOM   595  N  N   . ILE   A 1 76  ? 3.618  13.868  10.997 1.00 22.33 ? 82  ILE   A N   1 
ATOM   596  C  CA  . ILE   A 1 76  ? 2.813  13.724  12.190 1.00 23.60 ? 82  ILE   A CA  1 
ATOM   597  C  C   . ILE   A 1 76  ? 3.149  14.834  13.163 1.00 24.77 ? 82  ILE   A C   1 
ATOM   598  O  O   . ILE   A 1 76  ? 4.329  15.141  13.353 1.00 23.30 ? 82  ILE   A O   1 
ATOM   599  C  CB  . ILE   A 1 76  ? 3.098  12.343  12.816 1.00 25.16 ? 82  ILE   A CB  1 
ATOM   600  C  CG1 . ILE   A 1 76  ? 2.548  11.210  11.957 1.00 26.28 ? 82  ILE   A CG1 1 
ATOM   601  C  CG2 . ILE   A 1 76  ? 2.636  12.226  14.274 1.00 26.32 ? 82  ILE   A CG2 1 
ATOM   602  C  CD1 . ILE   A 1 76  ? 3.260  10.017  12.219 1.00 28.63 ? 82  ILE   A CD1 1 
ATOM   603  N  N   . PHE   A 1 77  ? 2.114  15.427  13.784 1.00 26.11 ? 83  PHE   A N   1 
ATOM   604  C  CA  . PHE   A 1 77  ? 2.323  16.492  14.764 1.00 28.00 ? 83  PHE   A CA  1 
ATOM   605  C  C   . PHE   A 1 77  ? 2.896  15.900  16.061 1.00 27.48 ? 83  PHE   A C   1 
ATOM   606  O  O   . PHE   A 1 77  ? 2.391  14.900  16.567 1.00 28.30 ? 83  PHE   A O   1 
ATOM   607  C  CB  . PHE   A 1 77  ? 1.005  17.263  15.032 1.00 29.61 ? 83  PHE   A CB  1 
ATOM   608  C  CG  . PHE   A 1 77  ? 1.222  18.548  15.793 1.00 32.09 ? 83  PHE   A CG  1 
ATOM   609  C  CD1 . PHE   A 1 77  ? 1.713  19.672  15.157 1.00 34.50 ? 83  PHE   A CD1 1 
ATOM   610  C  CD2 . PHE   A 1 77  ? 1.019  18.604  17.160 1.00 34.11 ? 83  PHE   A CD2 1 
ATOM   611  C  CE1 . PHE   A 1 77  ? 1.918  20.852  15.861 1.00 36.20 ? 83  PHE   A CE1 1 
ATOM   612  C  CE2 . PHE   A 1 77  ? 1.226  19.783  17.864 1.00 35.42 ? 83  PHE   A CE2 1 
ATOM   613  C  CZ  . PHE   A 1 77  ? 1.666  20.898  17.213 1.00 35.84 ? 83  PHE   A CZ  1 
ATOM   614  N  N   . VAL   A 1 78  ? 3.967  16.500  16.572 1.00 26.12 ? 84  VAL   A N   1 
ATOM   615  C  CA  . VAL   A 1 78  ? 4.663  16.031  17.759 1.00 26.45 ? 84  VAL   A CA  1 
ATOM   616  C  C   . VAL   A 1 78  ? 4.677  17.148  18.797 1.00 27.63 ? 84  VAL   A C   1 
ATOM   617  O  O   . VAL   A 1 78  ? 5.134  18.253  18.498 1.00 28.31 ? 84  VAL   A O   1 
ATOM   618  C  CB  . VAL   A 1 78  ? 6.106  15.551  17.403 1.00 26.38 ? 84  VAL   A CB  1 
ATOM   619  C  CG1 . VAL   A 1 78  ? 6.914  15.248  18.667 1.00 26.49 ? 84  VAL   A CG1 1 
ATOM   620  C  CG2 . VAL   A 1 78  ? 6.057  14.328  16.496 1.00 25.89 ? 84  VAL   A CG2 1 
ATOM   621  N  N   . GLU   A 1 79  ? 4.178  16.867  20.012 1.00 28.20 ? 85  GLU   A N   1 
ATOM   622  C  CA  . GLU   A 1 79  ? 4.151  17.844  21.113 1.00 29.16 ? 85  GLU   A CA  1 
ATOM   623  C  C   . GLU   A 1 79  ? 5.530  18.400  21.401 1.00 29.32 ? 85  GLU   A C   1 
ATOM   624  O  O   . GLU   A 1 79  ? 6.546  17.698  21.210 1.00 28.41 ? 85  GLU   A O   1 
ATOM   625  C  CB  . GLU   A 1 79  ? 3.637  17.195  22.406 1.00 32.40 ? 85  GLU   A CB  1 
ATOM   626  C  CG  . GLU   A 1 79  ? 2.200  16.731  22.327 1.00 39.31 ? 85  GLU   A CG  1 
ATOM   627  C  CD  . GLU   A 1 79  ? 1.231  17.841  21.985 1.00 47.99 ? 85  GLU   A CD  1 
ATOM   628  O  OE1 . GLU   A 1 79  ? 1.173  18.838  22.743 1.00 50.43 ? 85  GLU   A OE1 1 
ATOM   629  O  OE2 . GLU   A 1 79  ? 0.545  17.728  20.943 1.00 50.53 ? 85  GLU   A OE2 1 
ATOM   630  N  N   . ALA   A 1 80  ? 5.567  19.665  21.867 1.00 30.26 ? 86  ALA   A N   1 
ATOM   631  C  CA  . ALA   A 1 80  ? 6.803  20.338  22.272 1.00 31.15 ? 86  ALA   A CA  1 
ATOM   632  C  C   . ALA   A 1 80  ? 7.536  19.528  23.355 1.00 32.01 ? 86  ALA   A C   1 
ATOM   633  O  O   . ALA   A 1 80  ? 6.897  18.842  24.166 1.00 32.53 ? 86  ALA   A O   1 
ATOM   634  C  CB  . ALA   A 1 80  ? 6.470  21.713  22.841 1.00 31.61 ? 86  ALA   A CB  1 
ATOM   635  N  N   . SER   A 1 81  ? 8.872  19.594  23.347 1.00 32.13 ? 87  SER   A N   1 
ATOM   636  C  CA  . SER   A 1 81  ? 9.749  18.985  24.354 1.00 32.86 ? 87  SER   A CA  1 
ATOM   637  C  C   . SER   A 1 81  ? 10.879 20.026  24.641 1.00 34.51 ? 87  SER   A C   1 
ATOM   638  O  O   . SER   A 1 81  ? 10.778 21.172  24.183 1.00 34.97 ? 87  SER   A O   1 
ATOM   639  C  CB  . SER   A 1 81  ? 10.327 17.661  23.840 1.00 33.03 ? 87  SER   A CB  1 
ATOM   640  O  OG  . SER   A 1 81  ? 11.266 17.878  22.796 1.00 32.94 ? 87  SER   A OG  1 
ATOM   641  N  N   . GLU   A 1 82  ? 11.943 19.652  25.388 1.00 35.36 ? 88  GLU   A N   1 
ATOM   642  C  CA  . GLU   A 1 82  ? 13.053 20.585  25.613 1.00 36.06 ? 88  GLU   A CA  1 
ATOM   643  C  C   . GLU   A 1 82  ? 14.016 20.652  24.397 1.00 34.91 ? 88  GLU   A C   1 
ATOM   644  O  O   . GLU   A 1 82  ? 14.849 21.558  24.324 1.00 35.04 ? 88  GLU   A O   1 
ATOM   645  C  CB  . GLU   A 1 82  ? 13.783 20.315  26.941 1.00 40.65 ? 88  GLU   A CB  1 
ATOM   646  C  CG  . GLU   A 1 82  ? 14.767 19.156  26.923 1.00 48.00 ? 88  GLU   A CG  1 
ATOM   647  C  CD  . GLU   A 1 82  ? 15.485 18.998  28.255 1.00 57.27 ? 88  GLU   A CD  1 
ATOM   648  O  OE1 . GLU   A 1 82  ? 16.686 18.636  28.249 1.00 58.31 ? 88  GLU   A OE1 1 
ATOM   649  O  OE2 . GLU   A 1 82  ? 14.847 19.253  29.306 1.00 59.74 ? 88  GLU   A OE2 1 
ATOM   650  N  N   . TYR   A 1 83  ? 13.879 19.723  23.412 1.00 33.24 ? 89  TYR   A N   1 
ATOM   651  C  CA  . TYR   A 1 83  ? 14.741 19.743  22.225 1.00 32.71 ? 89  TYR   A CA  1 
ATOM   652  C  C   . TYR   A 1 83  ? 14.106 20.422  21.015 1.00 31.87 ? 89  TYR   A C   1 
ATOM   653  O  O   . TYR   A 1 83  ? 14.822 20.942  20.152 1.00 32.84 ? 89  TYR   A O   1 
ATOM   654  C  CB  . TYR   A 1 83  ? 15.190 18.335  21.843 1.00 32.55 ? 89  TYR   A CB  1 
ATOM   655  C  CG  . TYR   A 1 83  ? 15.836 17.591  22.985 1.00 33.89 ? 89  TYR   A CG  1 
ATOM   656  C  CD1 . TYR   A 1 83  ? 17.182 17.761  23.282 1.00 35.36 ? 89  TYR   A CD1 1 
ATOM   657  C  CD2 . TYR   A 1 83  ? 15.111 16.693  23.749 1.00 35.22 ? 89  TYR   A CD2 1 
ATOM   658  C  CE1 . TYR   A 1 83  ? 17.782 17.062  24.326 1.00 36.61 ? 89  TYR   A CE1 1 
ATOM   659  C  CE2 . TYR   A 1 83  ? 15.699 15.978  24.777 1.00 36.58 ? 89  TYR   A CE2 1 
ATOM   660  C  CZ  . TYR   A 1 83  ? 17.031 16.176  25.077 1.00 38.22 ? 89  TYR   A CZ  1 
ATOM   661  O  OH  . TYR   A 1 83  ? 17.580 15.449  26.109 1.00 40.94 ? 89  TYR   A OH  1 
ATOM   662  N  N   . TYR   A 1 84  ? 12.772 20.424  20.946 1.00 29.78 ? 90  TYR   A N   1 
ATOM   663  C  CA  . TYR   A 1 84  ? 12.074 21.026  19.826 1.00 28.69 ? 90  TYR   A CA  1 
ATOM   664  C  C   . TYR   A 1 84  ? 10.791 21.699  20.296 1.00 29.14 ? 90  TYR   A C   1 
ATOM   665  O  O   . TYR   A 1 84  ? 10.094 21.151  21.159 1.00 28.87 ? 90  TYR   A O   1 
ATOM   666  C  CB  . TYR   A 1 84  ? 11.656 19.926  18.828 1.00 26.95 ? 90  TYR   A CB  1 
ATOM   667  C  CG  . TYR   A 1 84  ? 12.774 19.095  18.218 1.00 24.90 ? 90  TYR   A CG  1 
ATOM   668  C  CD1 . TYR   A 1 84  ? 12.975 17.779  18.604 1.00 24.41 ? 90  TYR   A CD1 1 
ATOM   669  C  CD2 . TYR   A 1 84  ? 13.551 19.592  17.178 1.00 24.53 ? 90  TYR   A CD2 1 
ATOM   670  C  CE1 . TYR   A 1 84  ? 13.939 16.983  17.994 1.00 23.59 ? 90  TYR   A CE1 1 
ATOM   671  C  CE2 . TYR   A 1 84  ? 14.534 18.812  16.571 1.00 23.86 ? 90  TYR   A CE2 1 
ATOM   672  C  CZ  . TYR   A 1 84  ? 14.719 17.498  16.978 1.00 23.27 ? 90  TYR   A CZ  1 
ATOM   673  O  OH  . TYR   A 1 84  ? 15.690 16.700  16.398 1.00 20.46 ? 90  TYR   A OH  1 
ATOM   674  N  N   . PRO   A 1 85  ? 10.374 22.800  19.644 1.00 29.39 ? 91  PRO   A N   1 
ATOM   675  C  CA  . PRO   A 1 85  ? 9.017  23.316  19.930 1.00 29.91 ? 91  PRO   A CA  1 
ATOM   676  C  C   . PRO   A 1 85  ? 7.990  22.335  19.316 1.00 31.00 ? 91  PRO   A C   1 
ATOM   677  O  O   . PRO   A 1 85  ? 8.368  21.389  18.600 1.00 31.47 ? 91  PRO   A O   1 
ATOM   678  C  CB  . PRO   A 1 85  ? 8.976  24.667  19.208 1.00 30.56 ? 91  PRO   A CB  1 
ATOM   679  C  CG  . PRO   A 1 85  ? 10.011 24.579  18.140 1.00 30.76 ? 91  PRO   A CG  1 
ATOM   680  C  CD  . PRO   A 1 85  ? 11.031 23.522  18.532 1.00 28.84 ? 91  PRO   A CD  1 
ATOM   681  N  N   . ALA   A 1 86  ? 6.685  22.578  19.526 1.00 30.80 ? 92  ALA   A N   1 
ATOM   682  C  CA  . ALA   A 1 86  ? 5.625  21.747  18.935 1.00 30.67 ? 92  ALA   A CA  1 
ATOM   683  C  C   . ALA   A 1 86  ? 5.725  21.897  17.409 1.00 30.22 ? 92  ALA   A C   1 
ATOM   684  O  O   . ALA   A 1 86  ? 5.889  23.023  16.928 1.00 31.78 ? 92  ALA   A O   1 
ATOM   685  C  CB  . ALA   A 1 86  ? 4.262  22.234  19.421 1.00 30.50 ? 92  ALA   A CB  1 
ATOM   686  N  N   . ARG   A 1 87  ? 5.809  20.777  16.674 1.00 28.37 ? 93  ARG   A N   1 
ATOM   687  C  CA  . ARG   A 1 87  ? 6.010  20.855  15.231 1.00 26.55 ? 93  ARG   A CA  1 
ATOM   688  C  C   . ARG   A 1 87  ? 5.512  19.603  14.507 1.00 25.66 ? 93  ARG   A C   1 
ATOM   689  O  O   . ARG   A 1 87  ? 5.171  18.622  15.158 1.00 26.55 ? 93  ARG   A O   1 
ATOM   690  C  CB  . ARG   A 1 87  ? 7.515  21.060  14.971 1.00 26.97 ? 93  ARG   A CB  1 
ATOM   691  C  CG  . ARG   A 1 87  ? 8.323  19.747  15.043 1.00 27.01 ? 93  ARG   A CG  1 
ATOM   692  C  CD  . ARG   A 1 87  ? 9.737  19.943  15.477 1.00 27.09 ? 93  ARG   A CD  1 
ATOM   693  N  NE  . ARG   A 1 87  ? 10.653 18.904  14.980 1.00 27.02 ? 93  ARG   A NE  1 
ATOM   694  C  CZ  . ARG   A 1 87  ? 10.764 17.673  15.470 1.00 28.22 ? 93  ARG   A CZ  1 
ATOM   695  N  NH1 . ARG   A 1 87  ? 11.682 16.841  14.988 1.00 26.18 ? 93  ARG   A NH1 1 
ATOM   696  N  NH2 . ARG   A 1 87  ? 9.971  17.267  16.459 1.00 28.44 ? 93  ARG   A NH2 1 
ATOM   697  N  N   . TYR   A 1 88  ? 5.526  19.612  13.166 1.00 25.01 ? 94  TYR   A N   1 
ATOM   698  C  CA  . TYR   A 1 88  ? 5.271  18.398  12.403 1.00 24.50 ? 94  TYR   A CA  1 
ATOM   699  C  C   . TYR   A 1 88  ? 6.633  17.751  12.157 1.00 21.71 ? 94  TYR   A C   1 
ATOM   700  O  O   . TYR   A 1 88  ? 7.560  18.398  11.643 1.00 21.91 ? 94  TYR   A O   1 
ATOM   701  C  CB  . TYR   A 1 88  ? 4.635  18.675  11.047 1.00 26.03 ? 94  TYR   A CB  1 
ATOM   702  C  CG  . TYR   A 1 88  ? 3.177  19.045  11.143 1.00 28.47 ? 94  TYR   A CG  1 
ATOM   703  C  CD1 . TYR   A 1 88  ? 2.196  18.068  11.222 1.00 30.41 ? 94  TYR   A CD1 1 
ATOM   704  C  CD2 . TYR   A 1 88  ? 2.783  20.372  11.226 1.00 30.25 ? 94  TYR   A CD2 1 
ATOM   705  C  CE1 . TYR   A 1 88  ? 0.852  18.404  11.334 1.00 32.28 ? 94  TYR   A CE1 1 
ATOM   706  C  CE2 . TYR   A 1 88  ? 1.440  20.720  11.329 1.00 31.78 ? 94  TYR   A CE2 1 
ATOM   707  C  CZ  . TYR   A 1 88  ? 0.481  19.730  11.414 1.00 33.56 ? 94  TYR   A CZ  1 
ATOM   708  O  OH  . TYR   A 1 88  ? -0.848 20.058  11.514 1.00 36.84 ? 94  TYR   A OH  1 
ATOM   709  N  N   . GLN   A 1 89  ? 6.722  16.464  12.451 1.00 19.80 ? 95  GLN   A N   1 
ATOM   710  C  CA  . GLN   A 1 89  ? 7.910  15.661  12.179 1.00 17.95 ? 95  GLN   A CA  1 
ATOM   711  C  C   . GLN   A 1 89  ? 7.615  14.800  10.945 1.00 17.08 ? 95  GLN   A C   1 
ATOM   712  O  O   . GLN   A 1 89  ? 6.561  14.155  10.860 1.00 16.80 ? 95  GLN   A O   1 
ATOM   713  C  CB  . GLN   A 1 89  ? 8.321  14.825  13.419 1.00 18.09 ? 95  GLN   A CB  1 
ATOM   714  C  CG  . GLN   A 1 89  ? 9.569  13.941  13.182 1.00 18.54 ? 95  GLN   A CG  1 
ATOM   715  C  CD  . GLN   A 1 89  ? 10.212 13.390  14.444 1.00 19.61 ? 95  GLN   A CD  1 
ATOM   716  O  OE1 . GLN   A 1 89  ? 10.271 14.044  15.476 1.00 19.78 ? 95  GLN   A OE1 1 
ATOM   717  N  NE2 . GLN   A 1 89  ? 10.766 12.189  14.356 1.00 16.12 ? 95  GLN   A NE2 1 
ATOM   718  N  N   . SER   A 1 90  ? 8.503  14.814  9.961  1.00 15.75 ? 96  SER   A N   1 
ATOM   719  C  CA  . SER   A 1 90  ? 8.323  14.057  8.734  1.00 15.47 ? 96  SER   A CA  1 
ATOM   720  C  C   . SER   A 1 90  ? 9.003  12.669  8.809  1.00 14.91 ? 96  SER   A C   1 
ATOM   721  O  O   . SER   A 1 90  ? 9.894  12.420  9.662  1.00 14.57 ? 96  SER   A O   1 
ATOM   722  C  CB  . SER   A 1 90  ? 8.883  14.858  7.556  1.00 17.48 ? 96  SER   A CB  1 
ATOM   723  O  OG  . SER   A 1 90  ? 10.293 14.971  7.646  1.00 18.71 ? 96  SER   A OG  1 
ATOM   724  N  N   . HIS   A 1 91  ? 8.567  11.785  7.876  1.00 14.92 ? 97  HIS   A N   1 
ATOM   725  C  CA  . HIS   A 1 91  ? 9.105  10.434  7.719  1.00 14.69 ? 97  HIS   A CA  1 
ATOM   726  C  C   . HIS   A 1 91  ? 8.970  9.640   9.055  1.00 14.68 ? 97  HIS   A C   1 
ATOM   727  O  O   . HIS   A 1 91  ? 9.859  8.849   9.376  1.00 15.63 ? 97  HIS   A O   1 
ATOM   728  C  CB  . HIS   A 1 91  ? 10.565 10.505  7.260  1.00 15.88 ? 97  HIS   A CB  1 
ATOM   729  C  CG  . HIS   A 1 91  ? 10.727 11.152  5.914  1.00 18.59 ? 97  HIS   A CG  1 
ATOM   730  N  ND1 . HIS   A 1 91  ? 10.677 10.410  4.736  1.00 20.53 ? 97  HIS   A ND1 1 
ATOM   731  C  CD2 . HIS   A 1 91  ? 10.844 12.461  5.593  1.00 19.47 ? 97  HIS   A CD2 1 
ATOM   732  C  CE1 . HIS   A 1 91  ? 10.785 11.289  3.749  1.00 20.73 ? 97  HIS   A CE1 1 
ATOM   733  N  NE2 . HIS   A 1 91  ? 10.907 12.525  4.209  1.00 20.77 ? 97  HIS   A NE2 1 
ATOM   734  N  N   . LEU   A 1 92  ? 7.888  9.871   9.797  1.00 13.85 ? 98  LEU   A N   1 
ATOM   735  C  CA  . LEU   A 1 92  ? 7.669  9.221   11.113 1.00 14.41 ? 98  LEU   A CA  1 
ATOM   736  C  C   . LEU   A 1 92  ? 6.628  8.097   10.977 1.00 15.04 ? 98  LEU   A C   1 
ATOM   737  O  O   . LEU   A 1 92  ? 5.601  8.289   10.311 1.00 17.00 ? 98  LEU   A O   1 
ATOM   738  C  CB  . LEU   A 1 92  ? 7.106  10.283  12.099 1.00 14.20 ? 98  LEU   A CB  1 
ATOM   739  C  CG  . LEU   A 1 92  ? 6.977  9.894   13.575 1.00 16.68 ? 98  LEU   A CG  1 
ATOM   740  C  CD1 . LEU   A 1 92  ? 8.300  9.474   14.142 1.00 17.16 ? 98  LEU   A CD1 1 
ATOM   741  C  CD2 . LEU   A 1 92  ? 6.379  11.100  14.359 1.00 17.49 ? 98  LEU   A CD2 1 
ATOM   742  N  N   . MET   A 1 93  ? 6.853  6.976   11.693 1.00 13.85 ? 99  MET   A N   1 
ATOM   743  C  CA  . MET   A 1 93  ? 5.919  5.838   11.694 1.00 13.76 ? 99  MET   A CA  1 
ATOM   744  C  C   . MET   A 1 93  ? 5.428  5.625   13.123 1.00 15.58 ? 99  MET   A C   1 
ATOM   745  O  O   . MET   A 1 93  ? 6.270  5.563   14.004 1.00 17.22 ? 99  MET   A O   1 
ATOM   746  C  CB  . MET   A 1 93  ? 6.686  4.596   11.216 1.00 14.08 ? 99  MET   A CB  1 
ATOM   747  C  CG  . MET   A 1 93  ? 7.200  4.748   9.739  1.00 15.83 ? 99  MET   A CG  1 
ATOM   748  S  SD  . MET   A 1 93  ? 8.332  3.448   9.258  1.00 20.84 ? 99  MET   A SD  1 
ATOM   749  C  CE  . MET   A 1 93  ? 9.716  3.812   10.347 1.00 17.78 ? 99  MET   A CE  1 
ATOM   750  N  N   . LEU   A 1 94  ? 4.098  5.463   13.368 1.00 15.58 ? 100 LEU   A N   1 
ATOM   751  C  CA  . LEU   A 1 94  ? 3.628  5.231   14.737 1.00 15.14 ? 100 LEU   A CA  1 
ATOM   752  C  C   . LEU   A 1 94  ? 3.140  3.800   14.922 1.00 14.37 ? 100 LEU   A C   1 
ATOM   753  O  O   . LEU   A 1 94  ? 2.597  3.171   14.003 1.00 14.61 ? 100 LEU   A O   1 
ATOM   754  C  CB  . LEU   A 1 94  ? 2.389  6.112   15.065 1.00 17.15 ? 100 LEU   A CB  1 
ATOM   755  C  CG  . LEU   A 1 94  ? 2.548  7.625   15.104 1.00 21.00 ? 100 LEU   A CG  1 
ATOM   756  C  CD1 . LEU   A 1 94  ? 1.235  8.262   15.541 1.00 22.80 ? 100 LEU   A CD1 1 
ATOM   757  C  CD2 . LEU   A 1 94  ? 3.683  8.056   16.025 1.00 21.30 ? 100 LEU   A CD2 1 
ATOM   758  N  N   . ALA   A 1 95  ? 3.276  3.311   16.153 1.00 13.96 ? 101 ALA   A N   1 
ATOM   759  C  CA  . ALA   A 1 95  ? 2.774  2.015   16.590 1.00 13.45 ? 101 ALA   A CA  1 
ATOM   760  C  C   . ALA   A 1 95  ? 2.241  2.142   18.028 1.00 15.09 ? 101 ALA   A C   1 
ATOM   761  O  O   . ALA   A 1 95  ? 2.560  3.096   18.741 1.00 16.07 ? 101 ALA   A O   1 
ATOM   762  C  CB  . ALA   A 1 95  ? 3.885  0.990   16.556 1.00 13.83 ? 101 ALA   A CB  1 
ATOM   763  N  N   . VAL   A 1 96  ? 1.359  1.233   18.416 1.00 15.22 ? 102 VAL   A N   1 
ATOM   764  C  CA  . VAL   A 1 96  ? 0.878  1.133   19.771 1.00 15.81 ? 102 VAL   A CA  1 
ATOM   765  C  C   . VAL   A 1 96  ? 1.957  0.376   20.581 1.00 16.38 ? 102 VAL   A C   1 
ATOM   766  O  O   . VAL   A 1 96  ? 2.289  -0.792  20.299 1.00 17.89 ? 102 VAL   A O   1 
ATOM   767  C  CB  . VAL   A 1 96  ? -0.503 0.433   19.864 1.00 16.47 ? 102 VAL   A CB  1 
ATOM   768  C  CG1 . VAL   A 1 96  ? -0.939 0.337   21.306 1.00 17.61 ? 102 VAL   A CG1 1 
ATOM   769  C  CG2 . VAL   A 1 96  ? -1.562 1.195   19.050 1.00 15.95 ? 102 VAL   A CG2 1 
ATOM   770  N  N   . GLY   A 1 97  ? 2.541  1.062   21.545 1.00 17.42 ? 103 GLY   A N   1 
ATOM   771  C  CA  . GLY   A 1 97  ? 3.587  0.463   22.366 1.00 17.92 ? 103 GLY   A CA  1 
ATOM   772  C  C   . GLY   A 1 97  ? 4.180  1.433   23.357 1.00 18.57 ? 103 GLY   A C   1 
ATOM   773  O  O   . GLY   A 1 97  ? 3.863  2.627   23.354 1.00 19.74 ? 103 GLY   A O   1 
ATOM   774  N  N   . HIS   A 1 98  ? 5.069  0.925   24.199 1.00 17.52 ? 104 HIS   A N   1 
ATOM   775  C  CA  . HIS   A 1 98  ? 5.694  1.736   25.223 1.00 17.89 ? 104 HIS   A CA  1 
ATOM   776  C  C   . HIS   A 1 98  ? 6.948  2.453   24.753 1.00 17.39 ? 104 HIS   A C   1 
ATOM   777  O  O   . HIS   A 1 98  ? 7.821  1.822   24.151 1.00 17.53 ? 104 HIS   A O   1 
ATOM   778  C  CB  . HIS   A 1 98  ? 6.009  0.869   26.463 1.00 18.96 ? 104 HIS   A CB  1 
ATOM   779  C  CG  . HIS   A 1 98  ? 6.481  1.718   27.590 1.00 22.03 ? 104 HIS   A CG  1 
ATOM   780  N  ND1 . HIS   A 1 98  ? 5.634  2.648   28.198 1.00 23.45 ? 104 HIS   A ND1 1 
ATOM   781  C  CD2 . HIS   A 1 98  ? 7.719  1.844   28.122 1.00 23.37 ? 104 HIS   A CD2 1 
ATOM   782  C  CE1 . HIS   A 1 98  ? 6.380  3.261   29.108 1.00 23.83 ? 104 HIS   A CE1 1 
ATOM   783  N  NE2 . HIS   A 1 98  ? 7.639  2.805   29.096 1.00 23.72 ? 104 HIS   A NE2 1 
ATOM   784  N  N   . SER   A 1 99  ? 7.092  3.719   25.097 1.00 17.43 ? 105 SER   A N   1 
ATOM   785  C  CA  . SER   A 1 99  ? 8.239  4.532   24.712 1.00 18.62 ? 105 SER   A CA  1 
ATOM   786  C  C   . SER   A 1 99  ? 8.387  5.695   25.702 1.00 22.22 ? 105 SER   A C   1 
ATOM   787  O  O   . SER   A 1 99  ? 7.421  6.427   25.912 1.00 24.76 ? 105 SER   A O   1 
ATOM   788  C  CB  . SER   A 1 99  ? 8.008  5.112   23.315 1.00 20.43 ? 105 SER   A CB  1 
ATOM   789  O  OG  . SER   A 1 99  ? 9.135  5.843   22.864 1.00 24.59 ? 105 SER   A OG  1 
ATOM   790  N  N   . GLU   A 1 100 ? 9.569  5.853   26.295 1.00 20.98 ? 106 GLU   A N   1 
ATOM   791  C  CA  . GLU   A 1 100 ? 9.925  6.940   27.212 1.00 22.18 ? 106 GLU   A CA  1 
ATOM   792  C  C   . GLU   A 1 100 ? 11.082 7.713   26.565 1.00 22.94 ? 106 GLU   A C   1 
ATOM   793  O  O   . GLU   A 1 100 ? 11.768 7.155   25.709 1.00 23.76 ? 106 GLU   A O   1 
ATOM   794  C  CB  . GLU   A 1 100 ? 10.353 6.344   28.579 1.00 24.33 ? 106 GLU   A CB  1 
ATOM   795  C  CG  . GLU   A 1 100 ? 9.183  5.795   29.370 1.00 27.49 ? 106 GLU   A CG  1 
ATOM   796  C  CD  . GLU   A 1 100 ? 9.520  5.116   30.695 1.00 30.94 ? 106 GLU   A CD  1 
ATOM   797  O  OE1 . GLU   A 1 100 ? 10.374 5.649   31.434 1.00 33.42 ? 106 GLU   A OE1 1 
ATOM   798  O  OE2 . GLU   A 1 100 ? 8.907  4.075   31.016 1.00 30.21 ? 106 GLU   A OE2 1 
ATOM   799  N  N   . PRO   A 1 101 ? 11.358 8.985   26.922 1.00 24.12 ? 107 PRO   A N   1 
ATOM   800  C  CA  . PRO   A 1 101 ? 12.435 9.732   26.217 1.00 23.35 ? 107 PRO   A CA  1 
ATOM   801  C  C   . PRO   A 1 101 ? 13.764 8.995   26.032 1.00 21.64 ? 107 PRO   A C   1 
ATOM   802  O  O   . PRO   A 1 101 ? 14.381 9.029   24.949 1.00 21.88 ? 107 PRO   A O   1 
ATOM   803  C  CB  . PRO   A 1 101 ? 12.596 10.990  27.073 1.00 24.40 ? 107 PRO   A CB  1 
ATOM   804  C  CG  . PRO   A 1 101 ? 11.257 11.219  27.632 1.00 25.76 ? 107 PRO   A CG  1 
ATOM   805  C  CD  . PRO   A 1 101 ? 10.635 9.847   27.868 1.00 24.01 ? 107 PRO   A CD  1 
ATOM   806  N  N   . GLY   A 1 102 ? 14.201 8.302   27.079 1.00 20.53 ? 108 GLY   A N   1 
ATOM   807  C  CA  . GLY   A 1 102 ? 15.441 7.544   27.029 1.00 19.76 ? 108 GLY   A CA  1 
ATOM   808  C  C   . GLY   A 1 102 ? 15.455 6.354   26.091 1.00 19.25 ? 108 GLY   A C   1 
ATOM   809  O  O   . GLY   A 1 102 ? 16.514 5.760   25.852 1.00 20.52 ? 108 GLY   A O   1 
ATOM   810  N  N   . ASP   A 1 103 ? 14.274 5.960   25.603 1.00 16.91 ? 109 ASP   A N   1 
ATOM   811  C  CA  . ASP   A 1 103 ? 14.140 4.877   24.635 1.00 16.09 ? 109 ASP   A CA  1 
ATOM   812  C  C   . ASP   A 1 103 ? 14.581 5.295   23.210 1.00 15.85 ? 109 ASP   A C   1 
ATOM   813  O  O   . ASP   A 1 103 ? 14.773 4.422   22.340 1.00 16.63 ? 109 ASP   A O   1 
ATOM   814  C  CB  . ASP   A 1 103 ? 12.699 4.337   24.572 1.00 16.83 ? 109 ASP   A CB  1 
ATOM   815  C  CG  . ASP   A 1 103 ? 12.368 3.512   25.804 1.00 17.41 ? 109 ASP   A CG  1 
ATOM   816  O  OD1 . ASP   A 1 103 ? 13.225 2.774   26.246 1.00 18.36 ? 109 ASP   A OD1 1 
ATOM   817  O  OD2 . ASP   A 1 103 ? 11.245 3.648   26.332 1.00 20.16 ? 109 ASP   A OD2 1 
ATOM   818  N  N   . CYS   A 1 104 ? 14.746 6.608   22.947 1.00 16.36 ? 110 CYS   A N   1 
ATOM   819  C  CA  . CYS   A 1 104 ? 15.223 7.082   21.612 1.00 15.36 ? 110 CYS   A CA  1 
ATOM   820  C  C   . CYS   A 1 104 ? 16.496 6.383   21.196 1.00 14.95 ? 110 CYS   A C   1 
ATOM   821  O  O   . CYS   A 1 104 ? 17.383 6.208   22.028 1.00 15.54 ? 110 CYS   A O   1 
ATOM   822  C  CB  . CYS   A 1 104 ? 15.397 8.595   21.582 1.00 15.88 ? 110 CYS   A CB  1 
ATOM   823  S  SG  . CYS   A 1 104 ? 13.846 9.488   21.531 1.00 17.12 ? 110 CYS   A SG  1 
ATOM   824  N  N   . GLY   A 1 105 ? 16.551 5.925   19.941 1.00 13.43 ? 111 GLY   A N   1 
ATOM   825  C  CA  . GLY   A 1 105 ? 17.732 5.209   19.477 1.00 14.30 ? 111 GLY   A CA  1 
ATOM   826  C  C   . GLY   A 1 105 ? 17.548 3.699   19.374 1.00 16.27 ? 111 GLY   A C   1 
ATOM   827  O  O   . GLY   A 1 105 ? 18.352 3.005   18.731 1.00 17.43 ? 111 GLY   A O   1 
ATOM   828  N  N   . GLY   A 1 106 ? 16.497 3.165   20.000 1.00 15.35 ? 112 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 106 ? 16.190 1.736   19.890 1.00 14.88 ? 112 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 106 ? 15.852 1.397   18.443 1.00 14.22 ? 112 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 106 ? 15.116 2.141   17.796 1.00 14.28 ? 112 GLY   A O   1 
ATOM   832  N  N   . ILE   A 1 107 ? 16.415 0.313   17.928 1.00 13.07 ? 113 ILE   A N   1 
ATOM   833  C  CA  . ILE   A 1 107 ? 16.156 -0.081  16.550 1.00 12.77 ? 113 ILE   A CA  1 
ATOM   834  C  C   . ILE   A 1 107 ? 14.855 -0.840  16.349 1.00 13.03 ? 113 ILE   A C   1 
ATOM   835  O  O   . ILE   A 1 107 ? 14.540 -1.740  17.127 1.00 13.04 ? 113 ILE   A O   1 
ATOM   836  C  CB  . ILE   A 1 107 ? 17.383 -0.894  16.080 1.00 14.32 ? 113 ILE   A CB  1 
ATOM   837  C  CG1 . ILE   A 1 107 ? 18.570 0.047   15.927 1.00 16.19 ? 113 ILE   A CG1 1 
ATOM   838  C  CG2 . ILE   A 1 107 ? 17.115 -1.683  14.801 1.00 15.86 ? 113 ILE   A CG2 1 
ATOM   839  C  CD1 . ILE   A 1 107 ? 19.981 -0.691  15.559 1.00 17.73 ? 113 ILE   A CD1 1 
ATOM   840  N  N   . LEU   A 1 108 ? 14.179 -0.539  15.213 1.00 12.45 ? 114 LEU   A N   1 
ATOM   841  C  CA  . LEU   A 1 108 ? 13.020 -1.264  14.691 1.00 13.16 ? 114 LEU   A CA  1 
ATOM   842  C  C   . LEU   A 1 108 ? 13.554 -2.063  13.497 1.00 13.56 ? 114 LEU   A C   1 
ATOM   843  O  O   . LEU   A 1 108 ? 14.195 -1.498  12.591 1.00 13.24 ? 114 LEU   A O   1 
ATOM   844  C  CB  . LEU   A 1 108 ? 11.943 -0.221  14.227 1.00 13.73 ? 114 LEU   A CB  1 
ATOM   845  C  CG  . LEU   A 1 108 ? 10.749 -0.814  13.466 1.00 14.51 ? 114 LEU   A CG  1 
ATOM   846  C  CD1 . LEU   A 1 108 ? 9.925  -1.774  14.350 1.00 15.23 ? 114 LEU   A CD1 1 
ATOM   847  C  CD2 . LEU   A 1 108 ? 9.828  0.315   12.885 1.00 14.87 ? 114 LEU   A CD2 1 
ATOM   848  N  N   . ARG   A 1 109 ? 13.257 -3.371  13.487 1.00 13.21 ? 115 ARG   A N   1 
ATOM   849  C  CA  . ARG   A 1 109 ? 13.750 -4.270  12.427 1.00 15.64 ? 115 ARG   A CA  1 
ATOM   850  C  C   . ARG   A 1 109 ? 12.633 -5.121  11.876 1.00 16.92 ? 115 ARG   A C   1 
ATOM   851  O  O   . ARG   A 1 109 ? 11.825 -5.630  12.635 1.00 16.54 ? 115 ARG   A O   1 
ATOM   852  C  CB  . ARG   A 1 109 ? 14.716 -5.285  13.049 1.00 18.15 ? 115 ARG   A CB  1 
ATOM   853  C  CG  . ARG   A 1 109 ? 15.971 -4.715  13.623 1.00 24.68 ? 115 ARG   A CG  1 
ATOM   854  C  CD  . ARG   A 1 109 ? 16.807 -5.896  14.089 1.00 27.05 ? 115 ARG   A CD  1 
ATOM   855  N  NE  . ARG   A 1 109 ? 17.392 -6.533  12.912 1.00 32.96 ? 115 ARG   A NE  1 
ATOM   856  C  CZ  . ARG   A 1 109 ? 18.573 -6.205  12.397 1.00 34.99 ? 115 ARG   A CZ  1 
ATOM   857  N  NH1 . ARG   A 1 109 ? 19.013 -6.807  11.304 1.00 33.42 ? 115 ARG   A NH1 1 
ATOM   858  N  NH2 . ARG   A 1 109 ? 19.342 -5.298  12.998 1.00 35.61 ? 115 ARG   A NH2 1 
ATOM   859  N  N   . CYS   A 1 110 ? 12.678 -5.374  10.587 1.00 16.94 ? 116 CYS   A N   1 
ATOM   860  C  CA  . CYS   A 1 110 ? 11.760 -6.343  9.944  1.00 18.82 ? 116 CYS   A CA  1 
ATOM   861  C  C   . CYS   A 1 110 ? 12.622 -7.498  9.377  1.00 21.60 ? 116 CYS   A C   1 
ATOM   862  O  O   . CYS   A 1 110 ? 13.841 -7.497  9.554  1.00 22.76 ? 116 CYS   A O   1 
ATOM   863  C  CB  . CYS   A 1 110 ? 10.972 -5.650  8.842  1.00 19.46 ? 116 CYS   A CB  1 
ATOM   864  S  SG  . CYS   A 1 110 ? 12.010 -5.095  7.469  1.00 17.34 ? 116 CYS   A SG  1 
ATOM   865  N  N   . GLN   A 1 111 ? 12.023 -8.465  8.655  1.00 23.74 ? 117 GLN   A N   1 
ATOM   866  C  CA  . GLN   A 1 111 ? 12.801 -9.558  8.031  1.00 26.19 ? 117 GLN   A CA  1 
ATOM   867  C  C   . GLN   A 1 111 ? 13.921 -9.082  7.062  1.00 26.76 ? 117 GLN   A C   1 
ATOM   868  O  O   . GLN   A 1 111 ? 14.912 -9.799  6.850  1.00 28.09 ? 117 GLN   A O   1 
ATOM   869  C  CB  . GLN   A 1 111 ? 11.842 -10.497 7.272  1.00 29.33 ? 117 GLN   A CB  1 
ATOM   870  C  CG  . GLN   A 1 111 ? 10.986 -9.767  6.232  1.00 33.13 ? 117 GLN   A CG  1 
ATOM   871  C  CD  . GLN   A 1 111 ? 10.068 -10.701 5.471  1.00 38.48 ? 117 GLN   A CD  1 
ATOM   872  O  OE1 . GLN   A 1 111 ? 8.871  -10.423 5.298  1.00 40.66 ? 117 GLN   A OE1 1 
ATOM   873  N  NE2 . GLN   A 1 111 ? 10.609 -11.825 5.003  1.00 36.79 ? 117 GLN   A NE2 1 
ATOM   874  N  N   . HIS   A 1 112 ? 13.778 -7.870  6.508  1.00 24.25 ? 118 HIS   A N   1 
ATOM   875  C  CA  . HIS   A 1 112 ? 14.716 -7.302  5.521  1.00 23.17 ? 118 HIS   A CA  1 
ATOM   876  C  C   . HIS   A 1 112 ? 15.880 -6.506  6.149  1.00 22.58 ? 118 HIS   A C   1 
ATOM   877  O  O   . HIS   A 1 112 ? 16.878 -6.202  5.472  1.00 23.61 ? 118 HIS   A O   1 
ATOM   878  C  CB  . HIS   A 1 112 ? 13.935 -6.430  4.504  1.00 22.04 ? 118 HIS   A CB  1 
ATOM   879  C  CG  . HIS   A 1 112 ? 12.791 -7.141  3.821  1.00 24.04 ? 118 HIS   A CG  1 
ATOM   880  N  ND1 . HIS   A 1 112 ? 11.466 -6.883  4.154  1.00 23.85 ? 118 HIS   A ND1 1 
ATOM   881  C  CD2 . HIS   A 1 112 ? 12.813 -8.070  2.835  1.00 25.53 ? 118 HIS   A CD2 1 
ATOM   882  C  CE1 . HIS   A 1 112 ? 10.732 -7.675  3.387  1.00 25.95 ? 118 HIS   A CE1 1 
ATOM   883  N  NE2 . HIS   A 1 112 ? 11.496 -8.409  2.576  1.00 26.83 ? 118 HIS   A NE2 1 
ATOM   884  N  N   . GLY   A 1 113 ? 15.764 -6.162  7.429  1.00 20.43 ? 119 GLY   A N   1 
ATOM   885  C  CA  . GLY   A 1 113 ? 16.818 -5.385  8.085  1.00 17.96 ? 119 GLY   A CA  1 
ATOM   886  C  C   . GLY   A 1 113 ? 16.294 -4.264  8.967  1.00 15.30 ? 119 GLY   A C   1 
ATOM   887  O  O   . GLY   A 1 113 ? 15.170 -4.320  9.441  1.00 15.95 ? 119 GLY   A O   1 
ATOM   888  N  N   . VAL   A 1 114 ? 17.126 -3.251  9.191  1.00 14.53 ? 120 VAL   A N   1 
ATOM   889  C  CA  . VAL   A 1 114 ? 16.782 -2.101  10.007 1.00 14.45 ? 120 VAL   A CA  1 
ATOM   890  C  C   . VAL   A 1 114 ? 15.813 -1.200  9.274  1.00 14.90 ? 120 VAL   A C   1 
ATOM   891  O  O   . VAL   A 1 114 ? 16.089 -0.807  8.123  1.00 15.88 ? 120 VAL   A O   1 
ATOM   892  C  CB  . VAL   A 1 114 ? 18.060 -1.306  10.330 1.00 15.49 ? 120 VAL   A CB  1 
ATOM   893  C  CG1 . VAL   A 1 114 ? 17.708 -0.045  11.119 1.00 16.82 ? 120 VAL   A CG1 1 
ATOM   894  C  CG2 . VAL   A 1 114 ? 19.048 -2.175  11.119 1.00 16.68 ? 120 VAL   A CG2 1 
ATOM   895  N  N   . VAL   A 1 115 ? 14.724 -0.828  9.936  1.00 13.11 ? 121 VAL   A N   1 
ATOM   896  C  CA  . VAL   A 1 115 ? 13.684 0.050   9.392  1.00 13.63 ? 121 VAL   A CA  1 
ATOM   897  C  C   . VAL   A 1 115 ? 13.849 1.488   9.859  1.00 13.40 ? 121 VAL   A C   1 
ATOM   898  O  O   . VAL   A 1 115 ? 13.656 2.432   9.087  1.00 14.37 ? 121 VAL   A O   1 
ATOM   899  C  CB  . VAL   A 1 115 ? 12.296 -0.531  9.798  1.00 14.02 ? 121 VAL   A CB  1 
ATOM   900  C  CG1 . VAL   A 1 115 ? 11.160 0.363   9.347  1.00 13.73 ? 121 VAL   A CG1 1 
ATOM   901  C  CG2 . VAL   A 1 115 ? 12.112 -1.940  9.267  1.00 15.59 ? 121 VAL   A CG2 1 
ATOM   902  N  N   . GLY   A 1 116 ? 14.132 1.643   11.158 1.00 12.23 ? 122 GLY   A N   1 
ATOM   903  C  CA  . GLY   A 1 116 ? 14.310 2.983   11.715 1.00 13.04 ? 122 GLY   A CA  1 
ATOM   904  C  C   . GLY   A 1 116 ? 14.701 2.965   13.187 1.00 13.93 ? 122 GLY   A C   1 
ATOM   905  O  O   . GLY   A 1 116 ? 15.055 1.912   13.720 1.00 14.03 ? 122 GLY   A O   1 
ATOM   906  N  N   . ILE   A 1 117 ? 14.613 4.131   13.840 1.00 12.45 ? 123 ILE   A N   1 
ATOM   907  C  CA  . ILE   A 1 117 ? 14.968 4.191   15.265 1.00 12.36 ? 123 ILE   A CA  1 
ATOM   908  C  C   . ILE   A 1 117 ? 13.894 4.895   16.045 1.00 12.34 ? 123 ILE   A C   1 
ATOM   909  O  O   . ILE   A 1 117 ? 13.272 5.835   15.529 1.00 11.61 ? 123 ILE   A O   1 
ATOM   910  C  CB  . ILE   A 1 117 ? 16.362 4.873   15.459 1.00 12.98 ? 123 ILE   A CB  1 
ATOM   911  C  CG1 . ILE   A 1 117 ? 16.429 6.236   14.759 1.00 14.72 ? 123 ILE   A CG1 1 
ATOM   912  C  CG2 . ILE   A 1 117 ? 17.536 3.938   14.986 1.00 15.68 ? 123 ILE   A CG2 1 
ATOM   913  C  CD1 . ILE   A 1 117 ? 17.757 6.986   15.236 1.00 17.45 ? 123 ILE   A CD1 1 
ATOM   914  N  N   . VAL   A 1 118 ? 13.674 4.517   17.330 1.00 12.32 ? 124 VAL   A N   1 
ATOM   915  C  CA  . VAL   A 1 118 ? 12.685 5.218   18.149 1.00 12.27 ? 124 VAL   A CA  1 
ATOM   916  C  C   . VAL   A 1 118 ? 12.989 6.752   18.172 1.00 12.77 ? 124 VAL   A C   1 
ATOM   917  O  O   . VAL   A 1 118 ? 14.148 7.127   18.368 1.00 12.96 ? 124 VAL   A O   1 
ATOM   918  C  CB  . VAL   A 1 118 ? 12.706 4.645   19.599 1.00 13.29 ? 124 VAL   A CB  1 
ATOM   919  C  CG1 . VAL   A 1 118 ? 11.845 5.515   20.511 1.00 14.44 ? 124 VAL   A CG1 1 
ATOM   920  C  CG2 . VAL   A 1 118 ? 12.204 3.188   19.614 1.00 13.45 ? 124 VAL   A CG2 1 
ATOM   921  N  N   . SER   A 1 119 ? 11.970 7.594   18.002 1.00 13.12 ? 125 SER   A N   1 
ATOM   922  C  CA  . SER   A 1 119 ? 12.180 9.036   18.016 1.00 13.15 ? 125 SER   A CA  1 
ATOM   923  C  C   . SER   A 1 119 ? 11.091 9.755   18.801 1.00 15.25 ? 125 SER   A C   1 
ATOM   924  O  O   . SER   A 1 119 ? 11.378 10.815  19.350 1.00 16.81 ? 125 SER   A O   1 
ATOM   925  C  CB  . SER   A 1 119 ? 12.240 9.535   16.580 1.00 14.47 ? 125 SER   A CB  1 
ATOM   926  O  OG  . SER   A 1 119 ? 12.312 10.947  16.462 1.00 17.18 ? 125 SER   A OG  1 
ATOM   927  N  N   . THR   A 1 120 ? 9.862  9.183   18.929 1.00 15.60 ? 126 THR   A N   1 
ATOM   928  C  CA  . THR   A 1 120 ? 8.810  9.879   19.718 1.00 16.78 ? 126 THR   A CA  1 
ATOM   929  C  C   . THR   A 1 120 ? 8.071  8.864   20.628 1.00 19.34 ? 126 THR   A C   1 
ATOM   930  O  O   . THR   A 1 120 ? 8.210  7.644   20.448 1.00 17.79 ? 126 THR   A O   1 
ATOM   931  C  CB  . THR   A 1 120 ? 7.840  10.632  18.777 1.00 17.05 ? 126 THR   A CB  1 
ATOM   932  O  OG1 . THR   A 1 120 ? 7.031  9.667   18.099 1.00 17.40 ? 126 THR   A OG1 1 
ATOM   933  C  CG2 . THR   A 1 120 ? 8.558  11.481  17.723 1.00 16.88 ? 126 THR   A CG2 1 
ATOM   934  N  N   . GLY   A 1 121 ? 7.310  9.358   21.601 1.00 21.51 ? 127 GLY   A N   1 
ATOM   935  C  CA  . GLY   A 1 121 ? 6.601  8.467   22.517 1.00 23.98 ? 127 GLY   A CA  1 
ATOM   936  C  C   . GLY   A 1 121 ? 5.496  9.157   23.286 1.00 27.04 ? 127 GLY   A C   1 
ATOM   937  O  O   . GLY   A 1 121 ? 5.131  10.274  22.950 1.00 28.30 ? 127 GLY   A O   1 
ATOM   938  N  N   . GLY   A 1 122 ? 5.002  8.508   24.334 1.00 28.25 ? 128 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 122 ? 3.928  9.045   25.165 1.00 29.44 ? 128 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 122 ? 2.529  8.665   24.711 1.00 29.62 ? 128 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 122 ? 2.316  8.356   23.536 1.00 29.84 ? 128 GLY   A O   1 
ATOM   942  N  N   . ASN   A 1 123 ? 1.558  8.698   25.636 1.00 29.18 ? 129 ASN   A N   1 
ATOM   943  C  CA  . ASN   A 1 123 ? 0.153  8.367   25.364 1.00 29.92 ? 129 ASN   A CA  1 
ATOM   944  C  C   . ASN   A 1 123 ? -0.056 6.910   24.907 1.00 27.77 ? 129 ASN   A C   1 
ATOM   945  O  O   . ASN   A 1 123 ? -1.049 6.636   24.229 1.00 28.87 ? 129 ASN   A O   1 
ATOM   946  C  CB  . ASN   A 1 123 ? -0.469 9.320   24.311 1.00 33.37 ? 129 ASN   A CB  1 
ATOM   947  C  CG  . ASN   A 1 123 ? -0.892 10.688  24.803 1.00 38.46 ? 129 ASN   A CG  1 
ATOM   948  O  OD1 . ASN   A 1 123 ? -0.929 10.963  26.008 1.00 39.78 ? 129 ASN   A OD1 1 
ATOM   949  N  ND2 . ASN   A 1 123 ? -1.253 11.570  23.861 1.00 39.43 ? 129 ASN   A ND2 1 
ATOM   950  N  N   . GLY   A 1 124 ? 0.881  6.013   25.217 1.00 24.03 ? 130 GLY   A N   1 
ATOM   951  C  CA  . GLY   A 1 124 ? 0.769  4.635   24.784 1.00 21.96 ? 130 GLY   A CA  1 
ATOM   952  C  C   . GLY   A 1 124 ? 1.177  4.429   23.327 1.00 19.70 ? 130 GLY   A C   1 
ATOM   953  O  O   . GLY   A 1 124 ? 0.841  3.407   22.738 1.00 19.87 ? 130 GLY   A O   1 
ATOM   954  N  N   . LEU   A 1 125 ? 1.872  5.389   22.729 1.00 17.77 ? 131 LEU   A N   1 
ATOM   955  C  CA  . LEU   A 1 125 ? 2.306  5.268   21.336 1.00 18.04 ? 131 LEU   A CA  1 
ATOM   956  C  C   . LEU   A 1 125 ? 3.859  5.291   21.274 1.00 17.54 ? 131 LEU   A C   1 
ATOM   957  O  O   . LEU   A 1 125 ? 4.519  5.752   22.207 1.00 18.65 ? 131 LEU   A O   1 
ATOM   958  C  CB  . LEU   A 1 125 ? 1.756  6.451   20.505 1.00 18.71 ? 131 LEU   A CB  1 
ATOM   959  C  CG  . LEU   A 1 125 ? 0.242  6.568   20.422 1.00 21.50 ? 131 LEU   A CG  1 
ATOM   960  C  CD1 . LEU   A 1 125 ? -0.189 7.860   19.754 1.00 23.03 ? 131 LEU   A CD1 1 
ATOM   961  C  CD2 . LEU   A 1 125 ? -0.354 5.387   19.652 1.00 22.08 ? 131 LEU   A CD2 1 
ATOM   962  N  N   . VAL   A 1 126 ? 4.423  4.759   20.199 1.00 15.11 ? 132 VAL   A N   1 
ATOM   963  C  CA  . VAL   A 1 126 ? 5.867  4.799   19.983 1.00 13.35 ? 132 VAL   A CA  1 
ATOM   964  C  C   . VAL   A 1 126 ? 6.039  5.219   18.510 1.00 13.89 ? 132 VAL   A C   1 
ATOM   965  O  O   . VAL   A 1 126 ? 5.347  4.659   17.645 1.00 15.23 ? 132 VAL   A O   1 
ATOM   966  C  CB  . VAL   A 1 126 ? 6.618  3.461   20.288 1.00 14.89 ? 132 VAL   A CB  1 
ATOM   967  C  CG1 . VAL   A 1 126 ? 6.047  2.261   19.549 1.00 15.04 ? 132 VAL   A CG1 1 
ATOM   968  C  CG2 . VAL   A 1 126 ? 8.114  3.596   20.019 1.00 16.56 ? 132 VAL   A CG2 1 
ATOM   969  N  N   . GLY   A 1 127 ? 6.893  6.230   18.264 1.00 12.82 ? 133 GLY   A N   1 
ATOM   970  C  CA  . GLY   A 1 127 ? 7.125  6.727   16.920 1.00 12.26 ? 133 GLY   A CA  1 
ATOM   971  C  C   . GLY   A 1 127 ? 8.549  6.455   16.481 1.00 13.16 ? 133 GLY   A C   1 
ATOM   972  O  O   . GLY   A 1 127 ? 9.482  6.662   17.258 1.00 13.75 ? 133 GLY   A O   1 
ATOM   973  N  N   . PHE   A 1 128 ? 8.719  5.970   15.238 1.00 12.25 ? 134 PHE   A N   1 
ATOM   974  C  CA  . PHE   A 1 128 ? 10.050 5.614   14.686 1.00 12.86 ? 134 PHE   A CA  1 
ATOM   975  C  C   . PHE   A 1 128 ? 10.417 6.498   13.484 1.00 14.28 ? 134 PHE   A C   1 
ATOM   976  O  O   . PHE   A 1 128 ? 9.589  6.709   12.575 1.00 14.71 ? 134 PHE   A O   1 
ATOM   977  C  CB  . PHE   A 1 128 ? 10.035 4.170   14.157 1.00 13.47 ? 134 PHE   A CB  1 
ATOM   978  C  CG  . PHE   A 1 128 ? 9.535  3.177   15.186 1.00 14.30 ? 134 PHE   A CG  1 
ATOM   979  C  CD1 . PHE   A 1 128 ? 10.389 2.667   16.153 1.00 14.56 ? 134 PHE   A CD1 1 
ATOM   980  C  CD2 . PHE   A 1 128 ? 8.208  2.763   15.187 1.00 14.23 ? 134 PHE   A CD2 1 
ATOM   981  C  CE1 . PHE   A 1 128 ? 9.924  1.761   17.110 1.00 15.16 ? 134 PHE   A CE1 1 
ATOM   982  C  CE2 . PHE   A 1 128 ? 7.746  1.852   16.136 1.00 15.49 ? 134 PHE   A CE2 1 
ATOM   983  C  CZ  . PHE   A 1 128 ? 8.611  1.346   17.088 1.00 15.05 ? 134 PHE   A CZ  1 
ATOM   984  N  N   . ALA   A 1 129 ? 11.660 7.008   13.482 1.00 13.59 ? 135 ALA   A N   1 
ATOM   985  C  CA  . ALA   A 1 129 ? 12.131 7.764   12.322 1.00 14.04 ? 135 ALA   A CA  1 
ATOM   986  C  C   . ALA   A 1 129 ? 12.564 6.734   11.277 1.00 14.02 ? 135 ALA   A C   1 
ATOM   987  O  O   . ALA   A 1 129 ? 13.471 5.927   11.531 1.00 13.84 ? 135 ALA   A O   1 
ATOM   988  C  CB  . ALA   A 1 129 ? 13.320 8.664   12.720 1.00 13.78 ? 135 ALA   A CB  1 
ATOM   989  N  N   . ASP   A 1 130 ? 11.965 6.774   10.065 1.00 13.22 ? 136 ASP   A N   1 
ATOM   990  C  CA  . ASP   A 1 130 ? 12.302 5.819   9.010  1.00 14.03 ? 136 ASP   A CA  1 
ATOM   991  C  C   . ASP   A 1 130 ? 13.679 6.157   8.430  1.00 14.67 ? 136 ASP   A C   1 
ATOM   992  O  O   . ASP   A 1 130 ? 14.045 7.325   8.351  1.00 15.86 ? 136 ASP   A O   1 
ATOM   993  C  CB  . ASP   A 1 130 ? 11.242 5.939   7.868  1.00 16.40 ? 136 ASP   A CB  1 
ATOM   994  C  CG  . ASP   A 1 130 ? 11.427 4.932   6.740  1.00 19.25 ? 136 ASP   A CG  1 
ATOM   995  O  OD1 . ASP   A 1 130 ? 11.589 3.741   7.031  1.00 18.12 ? 136 ASP   A OD1 1 
ATOM   996  O  OD2 . ASP   A 1 130 ? 11.461 5.353   5.558  1.00 23.22 ? 136 ASP   A OD2 1 
ATOM   997  N  N   . VAL   A 1 131 ? 14.438 5.131   8.007  1.00 13.64 ? 137 VAL   A N   1 
ATOM   998  C  CA  . VAL   A 1 131 ? 15.706 5.336   7.307  1.00 13.48 ? 137 VAL   A CA  1 
ATOM   999  C  C   . VAL   A 1 131 ? 15.702 4.565   5.947  1.00 14.64 ? 137 VAL   A C   1 
ATOM   1000 O  O   . VAL   A 1 131 ? 16.703 4.609   5.252  1.00 15.79 ? 137 VAL   A O   1 
ATOM   1001 C  CB  . VAL   A 1 131 ? 16.919 4.917   8.155  1.00 13.49 ? 137 VAL   A CB  1 
ATOM   1002 C  CG1 . VAL   A 1 131 ? 17.009 5.760   9.435  1.00 13.08 ? 137 VAL   A CG1 1 
ATOM   1003 C  CG2 . VAL   A 1 131 ? 16.860 3.413   8.478  1.00 13.60 ? 137 VAL   A CG2 1 
ATOM   1004 N  N   . ARG   A 1 132 ? 14.624 3.798   5.627  1.00 13.87 ? 138 ARG   A N   1 
ATOM   1005 C  CA  . ARG   A 1 132 ? 14.579 2.980   4.417  1.00 13.37 ? 138 ARG   A CA  1 
ATOM   1006 C  C   . ARG   A 1 132 ? 14.684 3.779   3.129  1.00 16.63 ? 138 ARG   A C   1 
ATOM   1007 O  O   . ARG   A 1 132 ? 15.026 3.187   2.078  1.00 19.29 ? 138 ARG   A O   1 
ATOM   1008 C  CB  . ARG   A 1 132 ? 13.314 2.133   4.375  1.00 13.86 ? 138 ARG   A CB  1 
ATOM   1009 C  CG  . ARG   A 1 132 ? 13.262 1.120   5.491  1.00 15.18 ? 138 ARG   A CG  1 
ATOM   1010 C  CD  . ARG   A 1 132 ? 11.971 0.381   5.477  1.00 14.65 ? 138 ARG   A CD  1 
ATOM   1011 N  NE  . ARG   A 1 132 ? 10.853 1.227   5.886  1.00 15.34 ? 138 ARG   A NE  1 
ATOM   1012 C  CZ  . ARG   A 1 132 ? 9.608  0.799   6.047  1.00 19.38 ? 138 ARG   A CZ  1 
ATOM   1013 N  NH1 . ARG   A 1 132 ? 9.289  -0.459  5.766  1.00 18.39 ? 138 ARG   A NH1 1 
ATOM   1014 N  NH2 . ARG   A 1 132 ? 8.662  1.633   6.473  1.00 19.83 ? 138 ARG   A NH2 1 
ATOM   1015 N  N   . ASP   A 1 133 ? 14.376 5.085   3.164  1.00 15.33 ? 139 ASP   A N   1 
ATOM   1016 C  CA  . ASP   A 1 133 ? 14.470 5.895   1.955  1.00 15.67 ? 139 ASP   A CA  1 
ATOM   1017 C  C   . ASP   A 1 133 ? 15.884 6.440   1.698  1.00 16.87 ? 139 ASP   A C   1 
ATOM   1018 O  O   . ASP   A 1 133 ? 16.166 6.951   0.590  1.00 17.55 ? 139 ASP   A O   1 
ATOM   1019 C  CB  . ASP   A 1 133 ? 13.460 7.057   2.003  1.00 17.85 ? 139 ASP   A CB  1 
ATOM   1020 C  CG  . ASP   A 1 133 ? 13.771 8.061   3.102  1.00 22.22 ? 139 ASP   A CG  1 
ATOM   1021 O  OD1 . ASP   A 1 133 ? 13.996 7.622   4.279  1.00 20.12 ? 139 ASP   A OD1 1 
ATOM   1022 O  OD2 . ASP   A 1 133 ? 13.820 9.271   2.797  1.00 23.79 ? 139 ASP   A OD2 1 
ATOM   1023 N  N   . LEU   A 1 134 ? 16.799 6.318   2.693  1.00 16.84 ? 140 LEU   A N   1 
ATOM   1024 C  CA  . LEU   A 1 134 ? 18.166 6.887   2.568  1.00 16.50 ? 140 LEU   A CA  1 
ATOM   1025 C  C   . LEU   A 1 134 ? 19.049 5.901   1.836  1.00 17.40 ? 140 LEU   A C   1 
ATOM   1026 O  O   . LEU   A 1 134 ? 19.840 5.182   2.456  1.00 17.53 ? 140 LEU   A O   1 
ATOM   1027 C  CB  . LEU   A 1 134 ? 18.725 7.171   3.996  1.00 16.51 ? 140 LEU   A CB  1 
ATOM   1028 C  CG  . LEU   A 1 134 ? 17.838 8.121   4.827  1.00 16.99 ? 140 LEU   A CG  1 
ATOM   1029 C  CD1 . LEU   A 1 134 ? 18.408 8.343   6.265  1.00 15.60 ? 140 LEU   A CD1 1 
ATOM   1030 C  CD2 . LEU   A 1 134 ? 17.624 9.494   4.099  1.00 18.23 ? 140 LEU   A CD2 1 
ATOM   1031 N  N   . LEU   A 1 135 ? 18.804 5.745   0.524  1.00 17.08 ? 141 LEU   A N   1 
ATOM   1032 C  CA  . LEU   A 1 135 ? 19.504 4.709   -0.244 1.00 18.68 ? 141 LEU   A CA  1 
ATOM   1033 C  C   . LEU   A 1 135 ? 21.022 4.910   -0.254 1.00 20.91 ? 141 LEU   A C   1 
ATOM   1034 O  O   . LEU   A 1 135 ? 21.782 3.937   -0.380 1.00 22.64 ? 141 LEU   A O   1 
ATOM   1035 C  CB  . LEU   A 1 135 ? 18.957 4.599   -1.693 1.00 19.58 ? 141 LEU   A CB  1 
ATOM   1036 C  CG  . LEU   A 1 135 ? 17.446 4.698   -1.907 1.00 21.08 ? 141 LEU   A CG  1 
ATOM   1037 C  CD1 . LEU   A 1 135 ? 17.095 4.493   -3.429 1.00 22.23 ? 141 LEU   A CD1 1 
ATOM   1038 C  CD2 . LEU   A 1 135 ? 16.684 3.694   -1.044 1.00 21.57 ? 141 LEU   A CD2 1 
ATOM   1039 N  N   . TRP   A 1 136 ? 21.470 6.168   -0.101 1.00 21.01 ? 142 TRP   A N   1 
ATOM   1040 C  CA  . TRP   A 1 136 ? 22.891 6.506   -0.092 1.00 20.78 ? 142 TRP   A CA  1 
ATOM   1041 C  C   . TRP   A 1 136 ? 23.657 5.920   1.088  1.00 21.88 ? 142 TRP   A C   1 
ATOM   1042 O  O   . TRP   A 1 136 ? 24.877 5.822   1.008  1.00 21.93 ? 142 TRP   A O   1 
ATOM   1043 C  CB  . TRP   A 1 136 ? 23.099 8.012   -0.169 1.00 19.73 ? 142 TRP   A CB  1 
ATOM   1044 C  CG  . TRP   A 1 136 ? 22.354 8.793   0.861  1.00 19.22 ? 142 TRP   A CG  1 
ATOM   1045 C  CD1 . TRP   A 1 136 ? 21.138 9.392   0.717  1.00 19.35 ? 142 TRP   A CD1 1 
ATOM   1046 C  CD2 . TRP   A 1 136 ? 22.800 9.101   2.197  1.00 19.09 ? 142 TRP   A CD2 1 
ATOM   1047 N  NE1 . TRP   A 1 136 ? 20.800 10.057  1.876  1.00 19.91 ? 142 TRP   A NE1 1 
ATOM   1048 C  CE2 . TRP   A 1 136 ? 21.826 9.932   2.781  1.00 20.09 ? 142 TRP   A CE2 1 
ATOM   1049 C  CE3 . TRP   A 1 136 ? 23.992 8.869   2.900  1.00 19.85 ? 142 TRP   A CE3 1 
ATOM   1050 C  CZ2 . TRP   A 1 136 ? 21.953 10.430  4.081  1.00 20.80 ? 142 TRP   A CZ2 1 
ATOM   1051 C  CZ3 . TRP   A 1 136 ? 24.107 9.351   4.198  1.00 20.20 ? 142 TRP   A CZ3 1 
ATOM   1052 C  CH2 . TRP   A 1 136 ? 23.114 10.151  4.753  1.00 21.03 ? 142 TRP   A CH2 1 
ATOM   1053 N  N   . LEU   A 1 137 ? 22.953 5.435   2.149  1.00 21.74 ? 143 LEU   A N   1 
ATOM   1054 C  CA  . LEU   A 1 137 ? 23.620 4.818   3.308  1.00 23.69 ? 143 LEU   A CA  1 
ATOM   1055 C  C   . LEU   A 1 137 ? 24.436 3.576   2.904  1.00 28.29 ? 143 LEU   A C   1 
ATOM   1056 O  O   . LEU   A 1 137 ? 25.445 3.275   3.550  1.00 28.96 ? 143 LEU   A O   1 
ATOM   1057 C  CB  . LEU   A 1 137 ? 22.594 4.413   4.378  1.00 22.88 ? 143 LEU   A CB  1 
ATOM   1058 C  CG  . LEU   A 1 137 ? 21.973 5.532   5.187  1.00 22.43 ? 143 LEU   A CG  1 
ATOM   1059 C  CD1 . LEU   A 1 137 ? 20.932 4.970   6.147  1.00 22.25 ? 143 LEU   A CD1 1 
ATOM   1060 C  CD2 . LEU   A 1 137 ? 23.051 6.333   5.956  1.00 23.42 ? 143 LEU   A CD2 1 
ATOM   1061 N  N   . ASP   A 1 138 ? 24.014 2.884   1.813  1.00 30.94 ? 144 ASP   A N   1 
ATOM   1062 C  CA  . ASP   A 1 138 ? 24.617 1.670   1.265  1.00 35.27 ? 144 ASP   A CA  1 
ATOM   1063 C  C   . ASP   A 1 138 ? 25.636 1.871   0.168  1.00 39.54 ? 144 ASP   A C   1 
ATOM   1064 O  O   . ASP   A 1 138 ? 25.971 0.901   -0.515 1.00 40.41 ? 144 ASP   A O   1 
ATOM   1065 C  CB  . ASP   A 1 138 ? 23.518 0.760   0.714  1.00 37.64 ? 144 ASP   A CB  1 
ATOM   1066 C  CG  . ASP   A 1 138 ? 22.792 0.073   1.819  1.00 43.31 ? 144 ASP   A CG  1 
ATOM   1067 O  OD1 . ASP   A 1 138 ? 23.464 -0.367  2.787  1.00 45.41 ? 144 ASP   A OD1 1 
ATOM   1068 O  OD2 . ASP   A 1 138 ? 21.564 -0.013  1.744  1.00 45.18 ? 144 ASP   A OD2 1 
ATOM   1069 N  N   . GLU   A 1 139 ? 26.120 3.097   -0.023 1.00 41.48 ? 145 GLU   A N   1 
ATOM   1070 C  CA  . GLU   A 1 139 ? 27.124 3.367   -1.044 1.00 43.71 ? 145 GLU   A CA  1 
ATOM   1071 C  C   . GLU   A 1 139 ? 28.079 4.466   -0.584 1.00 45.13 ? 145 GLU   A C   1 
ATOM   1072 O  O   . GLU   A 1 139 ? 28.697 5.149   -1.409 1.00 46.44 ? 145 GLU   A O   1 
ATOM   1073 C  CB  . GLU   A 1 139 ? 26.455 3.735   -2.375 1.00 47.03 ? 145 GLU   A CB  1 
ATOM   1074 C  CG  . GLU   A 1 139 ? 25.537 4.940   -2.281 1.00 52.76 ? 145 GLU   A CG  1 
ATOM   1075 C  CD  . GLU   A 1 139 ? 24.514 5.016   -3.394 1.00 60.17 ? 145 GLU   A CD  1 
ATOM   1076 O  OE1 . GLU   A 1 139 ? 24.070 6.143   -3.716 1.00 61.49 ? 145 GLU   A OE1 1 
ATOM   1077 O  OE2 . GLU   A 1 139 ? 24.159 3.949   -3.947 1.00 62.48 ? 145 GLU   A OE2 1 
HETATM 1078 N  N1  . A1B4H B 2 .   ? 11.498 13.564  18.121 1.00 27.14 ? 201 A1B4H A N1  1 
HETATM 1079 C  C4  . A1B4H B 2 .   ? 8.159  12.823  25.441 1.00 31.03 ? 201 A1B4H A C4  1 
HETATM 1080 C  C5  . A1B4H B 2 .   ? 9.045  13.396  24.544 1.00 30.63 ? 201 A1B4H A C5  1 
HETATM 1081 C  C6  . A1B4H B 2 .   ? 9.815  12.584  23.713 1.00 31.18 ? 201 A1B4H A C6  1 
HETATM 1082 C  C7  . A1B4H B 2 .   ? 10.357 13.468  21.437 1.00 29.72 ? 201 A1B4H A C7  1 
HETATM 1083 C  C8  . A1B4H B 2 .   ? 11.531 13.843  20.519 1.00 29.17 ? 201 A1B4H A C8  1 
HETATM 1084 C  C10 . A1B4H B 2 .   ? 12.389 14.879  21.249 1.00 29.90 ? 201 A1B4H A C10 1 
HETATM 1085 O  O1  . A1B4H B 2 .   ? 12.300 13.247  24.520 1.00 32.16 ? 201 A1B4H A O1  1 
HETATM 1086 C  C12 . A1B4H B 2 .   ? 12.005 13.523  23.370 1.00 30.94 ? 201 A1B4H A C12 1 
HETATM 1087 C  C11 . A1B4H B 2 .   ? 12.994 14.245  22.495 1.00 30.48 ? 201 A1B4H A C11 1 
HETATM 1088 C  C9  . A1B4H B 2 .   ? 11.143 14.338  19.136 1.00 28.40 ? 201 A1B4H A C9  1 
HETATM 1089 O  O   . A1B4H B 2 .   ? 10.548 15.409  18.984 1.00 28.24 ? 201 A1B4H A O   1 
HETATM 1090 N  N   . A1B4H B 2 .   ? 10.776 13.202  22.842 1.00 30.59 ? 201 A1B4H A N   1 
HETATM 1091 C  C1  . A1B4H B 2 .   ? 9.695  11.193  23.808 1.00 31.37 ? 201 A1B4H A C1  1 
HETATM 1092 S  S   . A1B4H B 2 .   ? 10.825 10.226  22.856 1.00 31.17 ? 201 A1B4H A S   1 
HETATM 1093 C  C   . A1B4H B 2 .   ? 10.342 8.543   23.180 1.00 30.49 ? 201 A1B4H A C   1 
HETATM 1094 C  C3  . A1B4H B 2 .   ? 8.021  11.448  25.509 1.00 31.38 ? 201 A1B4H A C3  1 
HETATM 1095 C  C2  . A1B4H B 2 .   ? 8.781  10.626  24.692 1.00 31.09 ? 201 A1B4H A C2  1 
HETATM 1096 ZN ZN  . ZN    C 3 .   ? 10.816 -5.312  5.429  1.00 20.26 2 202 ZN    A ZN  1 
HETATM 1097 S  S   . DMS   D 4 .   ? 14.304 20.873  7.583  1.00 73.86 ? 203 DMS   A S   1 
HETATM 1098 O  O   . DMS   D 4 .   ? 14.604 20.049  8.794  1.00 73.49 ? 203 DMS   A O   1 
HETATM 1099 C  C1  . DMS   D 4 .   ? 15.821 21.031  6.591  1.00 73.85 ? 203 DMS   A C1  1 
HETATM 1100 C  C2  . DMS   D 4 .   ? 13.393 19.864  6.374  1.00 73.77 ? 203 DMS   A C2  1 
HETATM 1101 O  O   . HOH   E 5 .   ? 10.997 23.459  23.654 1.00 27.77 ? 301 HOH   A O   1 
HETATM 1102 O  O   . HOH   E 5 .   ? 12.607 6.313   31.022 1.00 30.68 ? 302 HOH   A O   1 
HETATM 1103 O  O   . HOH   E 5 .   ? 35.750 14.764  16.855 1.00 35.09 ? 303 HOH   A O   1 
HETATM 1104 O  O   . HOH   E 5 .   ? 22.483 -2.113  4.115  1.00 30.23 ? 304 HOH   A O   1 
HETATM 1105 O  O   . HOH   E 5 .   ? 10.598 7.578   4.653  1.00 22.91 ? 305 HOH   A O   1 
HETATM 1106 O  O   . HOH   E 5 .   ? 2.946  7.617   10.020 1.00 34.24 ? 306 HOH   A O   1 
HETATM 1107 O  O   . HOH   E 5 .   ? 27.641 15.321  3.080  1.00 35.50 ? 307 HOH   A O   1 
HETATM 1108 O  O   . HOH   E 5 .   ? 15.736 -11.485 5.068  1.00 51.72 ? 308 HOH   A O   1 
HETATM 1109 O  O   . HOH   E 5 .   ? 26.844 7.386   0.292  1.00 39.23 ? 309 HOH   A O   1 
HETATM 1110 O  O   . HOH   E 5 .   ? 8.090  -4.687  0.520  1.00 29.89 ? 310 HOH   A O   1 
HETATM 1111 O  O   . HOH   E 5 .   ? 23.540 21.178  7.953  1.00 26.82 ? 311 HOH   A O   1 
HETATM 1112 O  O   . HOH   E 5 .   ? 19.926 21.709  7.440  1.00 60.70 ? 312 HOH   A O   1 
HETATM 1113 O  O   . HOH   E 5 .   ? 8.264  18.756  18.445 1.00 28.72 ? 313 HOH   A O   1 
HETATM 1114 O  O   . HOH   E 5 .   ? 6.843  16.270  24.769 1.00 36.11 ? 314 HOH   A O   1 
HETATM 1115 O  O   . HOH   E 5 .   ? 6.979  15.326  22.294 1.00 36.75 ? 315 HOH   A O   1 
HETATM 1116 O  O   . HOH   E 5 .   ? 30.938 19.853  10.775 1.00 30.85 ? 316 HOH   A O   1 
HETATM 1117 O  O   . HOH   E 5 .   ? 10.436 4.268   3.360  1.00 21.13 ? 317 HOH   A O   1 
HETATM 1118 O  O   . HOH   E 5 .   ? 17.872 -7.541  3.403  1.00 36.29 ? 318 HOH   A O   1 
HETATM 1119 O  O   . HOH   E 5 .   ? 4.479  5.333   24.834 1.00 26.95 ? 319 HOH   A O   1 
HETATM 1120 O  O   . HOH   E 5 .   ? 29.484 2.460   10.472 1.00 25.04 ? 320 HOH   A O   1 
HETATM 1121 O  O   . HOH   E 5 .   ? 0.997  -3.086  19.862 1.00 29.92 ? 321 HOH   A O   1 
HETATM 1122 O  O   . HOH   E 5 .   ? 12.190 -6.979  31.445 1.00 53.34 ? 322 HOH   A O   1 
HETATM 1123 O  O   . HOH   E 5 .   ? 3.780  -5.445  21.141 1.00 25.90 ? 323 HOH   A O   1 
HETATM 1124 O  O   . HOH   E 5 .   ? 9.629  17.310  20.648 1.00 27.87 ? 324 HOH   A O   1 
HETATM 1125 O  O   . HOH   E 5 .   ? 20.192 8.103   19.043 1.00 16.56 ? 325 HOH   A O   1 
HETATM 1126 O  O   . HOH   E 5 .   ? 11.388 16.468  5.694  1.00 57.49 ? 326 HOH   A O   1 
HETATM 1127 O  O   . HOH   E 5 .   ? 35.026 13.933  8.903  1.00 40.55 ? 327 HOH   A O   1 
HETATM 1128 O  O   . HOH   E 5 .   ? 19.041 -1.182  27.392 1.00 31.16 ? 328 HOH   A O   1 
HETATM 1129 O  O   . HOH   E 5 .   ? 0.517  -0.783  16.509 1.00 14.86 ? 329 HOH   A O   1 
HETATM 1130 O  O   . HOH   E 5 .   ? 23.222 17.452  19.386 1.00 31.15 ? 330 HOH   A O   1 
HETATM 1131 O  O   . HOH   E 5 .   ? 10.162 -5.421  31.786 1.00 33.35 ? 331 HOH   A O   1 
HETATM 1132 O  O   . HOH   E 5 .   ? 15.425 10.632  1.070  1.00 36.70 ? 332 HOH   A O   1 
HETATM 1133 O  O   . HOH   E 5 .   ? 17.842 1.711   23.111 1.00 22.33 ? 333 HOH   A O   1 
HETATM 1134 O  O   . HOH   E 5 .   ? 11.502 1.441   33.482 1.00 17.95 ? 334 HOH   A O   1 
HETATM 1135 O  O   . HOH   E 5 .   ? 17.777 -0.356  29.923 1.00 41.00 ? 335 HOH   A O   1 
HETATM 1136 O  O   . HOH   E 5 .   ? 8.799  2.021   2.838  1.00 22.60 ? 336 HOH   A O   1 
HETATM 1137 O  O   . HOH   E 5 .   ? 27.952 2.723   2.545  1.00 40.53 ? 337 HOH   A O   1 
HETATM 1138 O  O   . HOH   E 5 .   ? 21.680 18.289  17.635 1.00 36.72 ? 338 HOH   A O   1 
HETATM 1139 O  O   . HOH   E 5 .   ? 6.275  -6.219  29.084 1.00 30.94 ? 339 HOH   A O   1 
HETATM 1140 O  O   . HOH   E 5 .   ? 11.145 15.111  3.231  1.00 47.24 ? 340 HOH   A O   1 
HETATM 1141 O  O   . HOH   E 5 .   ? 23.523 -0.768  15.789 1.00 35.44 ? 341 HOH   A O   1 
HETATM 1142 O  O   . HOH   E 5 .   ? 17.833 20.480  9.452  1.00 18.96 ? 342 HOH   A O   1 
HETATM 1143 O  O   . HOH   E 5 .   ? 5.234  -7.341  7.113  1.00 52.32 ? 343 HOH   A O   1 
HETATM 1144 O  O   . HOH   E 5 .   ? 6.091  7.459   28.145 1.00 49.84 ? 344 HOH   A O   1 
HETATM 1145 O  O   . HOH   E 5 .   ? 11.364 10.982  11.584 1.00 18.18 ? 345 HOH   A O   1 
HETATM 1146 O  O   . HOH   E 5 .   ? 15.857 11.289  24.145 1.00 25.31 ? 346 HOH   A O   1 
HETATM 1147 O  O   . HOH   E 5 .   ? 2.918  3.008   27.583 1.00 31.87 ? 347 HOH   A O   1 
HETATM 1148 O  O   . HOH   E 5 .   ? 9.356  20.560  11.662 1.00 39.46 ? 348 HOH   A O   1 
HETATM 1149 O  O   . HOH   E 5 .   ? 0.119  1.274   24.432 1.00 27.12 ? 349 HOH   A O   1 
HETATM 1150 O  O   . HOH   E 5 .   ? 14.897 1.726   23.268 1.00 15.58 ? 350 HOH   A O   1 
HETATM 1151 O  O   . HOH   E 5 .   ? 16.871 -8.359  10.311 1.00 50.23 ? 351 HOH   A O   1 
HETATM 1152 O  O   . HOH   E 5 .   ? 9.817  3.845   33.682 1.00 26.31 ? 352 HOH   A O   1 
HETATM 1153 O  O   . HOH   E 5 .   ? 26.182 3.230   19.778 1.00 40.50 ? 353 HOH   A O   1 
HETATM 1154 O  O   . HOH   E 5 .   ? 21.518 -5.579  10.799 1.00 34.41 ? 354 HOH   A O   1 
HETATM 1155 O  O   . HOH   E 5 .   ? 30.203 10.227  19.573 1.00 32.89 ? 355 HOH   A O   1 
HETATM 1156 O  O   . HOH   E 5 .   ? 18.014 18.175  17.210 1.00 18.56 ? 356 HOH   A O   1 
HETATM 1157 O  O   . HOH   E 5 .   ? 13.599 8.451   29.856 1.00 31.87 ? 357 HOH   A O   1 
HETATM 1158 O  O   . HOH   E 5 .   ? 3.828  -5.554  6.228  1.00 32.29 ? 358 HOH   A O   1 
HETATM 1159 O  O   . HOH   E 5 .   ? 0.205  3.195   6.553  1.00 32.56 ? 359 HOH   A O   1 
HETATM 1160 O  O   . HOH   E 5 .   ? 31.153 19.808  16.980 1.00 26.62 ? 360 HOH   A O   1 
HETATM 1161 O  O   . HOH   E 5 .   ? 6.520  12.372  21.595 1.00 30.27 ? 361 HOH   A O   1 
HETATM 1162 O  O   . HOH   E 5 .   ? 30.046 3.867   3.529  1.00 38.89 ? 362 HOH   A O   1 
HETATM 1163 O  O   . HOH   E 5 .   ? 18.496 3.520   26.171 1.00 35.33 ? 363 HOH   A O   1 
HETATM 1164 O  O   . HOH   E 5 .   ? 6.849  3.099   32.825 1.00 30.40 ? 364 HOH   A O   1 
HETATM 1165 O  O   . HOH   E 5 .   ? 14.689 -5.004  17.175 1.00 24.93 ? 365 HOH   A O   1 
HETATM 1166 O  O   . HOH   E 5 .   ? 5.840  1.214   6.077  1.00 28.30 ? 366 HOH   A O   1 
HETATM 1167 O  O   . HOH   E 5 .   ? 13.118 9.823   9.447  1.00 16.21 ? 367 HOH   A O   1 
HETATM 1168 O  O   . HOH   E 5 .   ? 18.120 18.501  5.578  1.00 37.76 ? 368 HOH   A O   1 
HETATM 1169 O  O   . HOH   E 5 .   ? -0.621 14.689  13.107 1.00 29.81 ? 369 HOH   A O   1 
HETATM 1170 O  O   . HOH   E 5 .   ? 7.787  -8.870  24.373 1.00 35.21 ? 370 HOH   A O   1 
HETATM 1171 O  O   . HOH   E 5 .   ? 8.156  -7.830  8.747  1.00 35.98 ? 371 HOH   A O   1 
HETATM 1172 O  O   . HOH   E 5 .   ? 19.157 8.270   25.782 1.00 35.06 ? 372 HOH   A O   1 
HETATM 1173 O  O   . HOH   E 5 .   ? 1.962  12.742  5.699  1.00 34.48 ? 373 HOH   A O   1 
HETATM 1174 O  O   . HOH   E 5 .   ? 31.977 1.377   3.491  1.00 37.24 ? 374 HOH   A O   1 
HETATM 1175 O  O   . HOH   E 5 .   ? 4.266  9.901   19.057 1.00 31.19 ? 375 HOH   A O   1 
HETATM 1176 O  O   . HOH   E 5 .   ? 11.878 17.160  26.943 1.00 48.86 ? 376 HOH   A O   1 
HETATM 1177 O  O   . HOH   E 5 .   ? 3.357  14.055  20.421 1.00 42.09 ? 377 HOH   A O   1 
HETATM 1178 O  O   . HOH   E 5 .   ? 6.769  12.252  5.551  1.00 24.96 ? 378 HOH   A O   1 
HETATM 1179 O  O   . HOH   E 5 .   ? 15.513 -5.187  1.603  1.00 23.86 ? 379 HOH   A O   1 
HETATM 1180 O  O   . HOH   E 5 .   ? 12.133 20.656  13.065 1.00 33.64 ? 380 HOH   A O   1 
HETATM 1181 O  O   . HOH   E 5 .   ? 23.845 1.534   19.457 1.00 32.30 ? 381 HOH   A O   1 
HETATM 1182 O  O   . HOH   E 5 .   ? 21.845 15.574  23.868 1.00 32.93 ? 382 HOH   A O   1 
HETATM 1183 O  O   . HOH   E 5 .   ? 30.386 9.853   17.204 1.00 35.45 ? 383 HOH   A O   1 
HETATM 1184 O  O   . HOH   E 5 .   ? 31.787 13.781  21.120 1.00 29.26 ? 384 HOH   A O   1 
HETATM 1185 O  O   . HOH   E 5 .   ? 3.893  -2.834  21.829 1.00 36.06 ? 385 HOH   A O   1 
HETATM 1186 O  O   . HOH   E 5 .   ? 5.190  -2.091  24.133 1.00 22.79 ? 386 HOH   A O   1 
HETATM 1187 O  O   . HOH   E 5 .   ? 18.755 12.284  1.902  1.00 37.83 ? 387 HOH   A O   1 
HETATM 1188 O  O   . HOH   E 5 .   ? 18.480 -1.295  19.447 1.00 25.60 ? 388 HOH   A O   1 
HETATM 1189 O  O   . HOH   E 5 .   ? 0.056  11.984  21.161 1.00 44.34 ? 389 HOH   A O   1 
HETATM 1190 O  O   . HOH   E 5 .   ? 36.256 2.160   3.913  1.00 40.83 ? 390 HOH   A O   1 
HETATM 1191 O  O   . HOH   E 5 .   ? 19.946 22.983  15.661 1.00 24.17 ? 391 HOH   A O   1 
HETATM 1192 O  O   . HOH   E 5 .   ? 14.798 13.932  3.724  1.00 29.09 ? 392 HOH   A O   1 
HETATM 1193 O  O   . HOH   E 5 .   ? 31.598 8.348   5.478  1.00 33.88 ? 393 HOH   A O   1 
HETATM 1194 O  O   . HOH   E 5 .   ? 26.323 -2.651  14.353 1.00 29.29 ? 394 HOH   A O   1 
HETATM 1195 O  O   . HOH   E 5 .   ? 35.215 19.637  11.918 1.00 34.18 ? 395 HOH   A O   1 
HETATM 1196 O  O   . HOH   E 5 .   ? 21.167 18.454  21.609 1.00 40.11 ? 396 HOH   A O   1 
HETATM 1197 O  O   . HOH   E 5 .   ? 28.650 -2.858  13.048 1.00 30.72 ? 397 HOH   A O   1 
HETATM 1198 O  O   . HOH   E 5 .   ? 11.928 -8.719  12.909 1.00 26.53 ? 398 HOH   A O   1 
HETATM 1199 O  O   . HOH   E 5 .   ? 29.069 15.637  23.158 1.00 43.39 ? 399 HOH   A O   1 
HETATM 1200 O  O   . HOH   E 5 .   ? 17.493 19.464  19.456 1.00 28.65 ? 400 HOH   A O   1 
HETATM 1201 O  O   . HOH   E 5 .   ? 22.567 18.333  6.015  1.00 24.72 ? 401 HOH   A O   1 
HETATM 1202 O  O   . HOH   E 5 .   ? 1.507  -2.939  17.579 1.00 27.77 ? 402 HOH   A O   1 
HETATM 1203 O  O   . HOH   E 5 .   ? 31.403 18.040  8.682  1.00 38.69 ? 403 HOH   A O   1 
HETATM 1204 O  O   . HOH   E 5 .   ? 16.214 23.104  14.973 1.00 36.09 ? 404 HOH   A O   1 
HETATM 1205 O  O   . HOH   E 5 .   ? 22.187 7.917   21.118 1.00 23.89 ? 405 HOH   A O   1 
HETATM 1206 O  O   . HOH   E 5 .   ? 31.207 1.766   12.699 1.00 29.73 ? 406 HOH   A O   1 
HETATM 1207 O  O   . HOH   E 5 .   ? 17.836 10.283  0.424  1.00 45.60 ? 407 HOH   A O   1 
HETATM 1208 O  O   . HOH   E 5 .   ? 6.209  22.322  11.372 1.00 36.16 ? 408 HOH   A O   1 
HETATM 1209 O  O   . HOH   E 5 .   ? 24.315 6.527   20.456 1.00 39.95 ? 409 HOH   A O   1 
HETATM 1210 O  O   . HOH   E 5 .   ? 4.425  -1.861  29.014 1.00 41.07 ? 410 HOH   A O   1 
HETATM 1211 O  O   . HOH   E 5 .   ? 7.181  -6.006  2.651  1.00 35.00 ? 411 HOH   A O   1 
HETATM 1212 O  O   . HOH   E 5 .   ? 2.947  12.014  18.178 1.00 50.40 ? 412 HOH   A O   1 
HETATM 1213 O  O   . HOH   E 5 .   ? 19.007 6.457   28.026 1.00 37.23 ? 413 HOH   A O   1 
HETATM 1214 O  O   . HOH   E 5 .   ? 20.078 8.135   -2.494 1.00 37.81 ? 414 HOH   A O   1 
HETATM 1215 O  O   . HOH   E 5 .   ? 0.347  -4.674  16.839 1.00 55.59 ? 415 HOH   A O   1 
HETATM 1216 O  O   . HOH   E 5 .   ? 24.293 14.439  23.630 1.00 58.90 ? 416 HOH   A O   1 
HETATM 1217 O  O   . HOH   E 5 .   ? 36.876 6.087   6.613  1.00 57.71 ? 417 HOH   A O   1 
HETATM 1218 O  O   . HOH   E 5 .   ? 28.086 21.128  18.694 1.00 45.74 ? 418 HOH   A O   1 
HETATM 1219 O  O   . HOH   E 5 .   ? 8.344  22.015  26.757 1.00 37.98 ? 419 HOH   A O   1 
HETATM 1220 O  O   . HOH   E 5 .   ? 3.095  13.301  23.014 1.00 50.33 ? 420 HOH   A O   1 
HETATM 1221 O  O   . HOH   E 5 .   ? 17.646 10.400  26.109 1.00 34.57 ? 421 HOH   A O   1 
HETATM 1222 O  O   . HOH   E 5 .   ? 31.717 7.738   15.578 1.00 34.70 ? 422 HOH   A O   1 
HETATM 1223 O  O   . HOH   E 5 .   ? 15.692 -10.339 11.278 1.00 45.74 ? 423 HOH   A O   1 
HETATM 1224 O  O   . HOH   E 5 .   ? 21.266 21.146  18.040 1.00 24.83 ? 424 HOH   A O   1 
HETATM 1225 O  O   . HOH   E 5 .   ? 1.867  0.950   26.456 1.00 34.27 ? 425 HOH   A O   1 
HETATM 1226 O  O   . HOH   E 5 .   ? 12.054 22.568  15.072 1.00 35.91 ? 426 HOH   A O   1 
HETATM 1227 O  O   . HOH   E 5 .   ? 13.335 12.947  1.128  1.00 51.30 ? 427 HOH   A O   1 
HETATM 1228 O  O   . HOH   E 5 .   ? 8.883  6.340   2.731  1.00 40.11 ? 428 HOH   A O   1 
HETATM 1229 O  O   . HOH   E 5 .   ? 6.374  2.494   3.302  1.00 34.76 ? 429 HOH   A O   1 
HETATM 1230 O  O   . HOH   E 5 .   ? 32.918 20.978  14.954 1.00 31.85 ? 430 HOH   A O   1 
HETATM 1231 O  O   . HOH   E 5 .   ? 20.003 12.228  26.677 1.00 43.63 ? 431 HOH   A O   1 
HETATM 1232 O  O   . HOH   E 5 .   ? 32.053 3.529   14.548 1.00 36.74 ? 432 HOH   A O   1 
HETATM 1233 O  O   . HOH   E 5 .   ? 8.955  -9.313  12.435 1.00 37.39 ? 433 HOH   A O   1 
HETATM 1234 O  O   . HOH   E 5 .   ? 34.626 19.154  18.513 1.00 29.83 ? 434 HOH   A O   1 
HETATM 1235 O  O   . HOH   E 5 .   ? 33.358 21.458  12.364 1.00 40.08 ? 435 HOH   A O   1 
HETATM 1236 O  O   . HOH   E 5 .   ? 29.987 21.728  9.383  1.00 35.36 ? 436 HOH   A O   1 
HETATM 1237 O  O   . HOH   E 5 .   ? 22.583 -2.820  17.540 1.00 40.32 ? 437 HOH   A O   1 
HETATM 1238 O  O   . HOH   E 5 .   ? 9.786  24.322  13.831 1.00 46.31 ? 438 HOH   A O   1 
HETATM 1239 O  O   . HOH   E 5 .   ? 35.794 20.284  16.323 0.50 57.95 ? 439 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   ? 0.3524 0.3063 0.2763 -0.0122 -0.0602 -0.0131 7   SER   A N   
2    C CA  . SER   A 1   ? 0.3497 0.3119 0.2946 -0.0102 -0.0647 -0.0093 7   SER   A CA  
3    C C   . SER   A 1   ? 0.3216 0.2930 0.2831 -0.0051 -0.0608 -0.0062 7   SER   A C   
4    O O   . SER   A 1   ? 0.3207 0.2913 0.2767 -0.0041 -0.0575 -0.0056 7   SER   A O   
5    C CB  . SER   A 1   ? 0.3921 0.3519 0.3376 -0.0159 -0.0775 -0.0039 7   SER   A CB  
6    O OG  . SER   A 1   ? 0.4416 0.4005 0.3844 -0.0181 -0.0834 0.0022  7   SER   A OG  
7    N N   . GLY   A 2   ? 0.2884 0.2675 0.2688 -0.0024 -0.0602 -0.0047 8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.2693 0.2548 0.2645 0.0015  -0.0550 -0.0027 8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.2523 0.2440 0.2602 0.0035  -0.0494 -0.0045 8   GLY   A C   
10   O O   . GLY   A 2   ? 0.2561 0.2477 0.2595 0.0028  -0.0475 -0.0079 8   GLY   A O   
11   N N   . ALA   A 3   ? 0.2238 0.2203 0.2477 0.0058  -0.0460 -0.0023 9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.2186 0.2200 0.2527 0.0064  -0.0395 -0.0040 9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.2019 0.2038 0.2419 0.0082  -0.0301 -0.0049 9   ALA   A C   
14   O O   . ALA   A 3   ? 0.2175 0.2163 0.2587 0.0098  -0.0297 -0.0033 9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.2312 0.2375 0.2821 0.0059  -0.0444 -0.0003 9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.1846 0.1888 0.2267 0.0071  -0.0224 -0.0076 10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.1944 0.1969 0.2401 0.0071  -0.0121 -0.0096 10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.2065 0.2135 0.2717 0.0080  -0.0078 -0.0083 10  ILE   A C   
19   O O   . ILE   A 4   ? 0.2083 0.2200 0.2770 0.0063  -0.0100 -0.0076 10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.1923 0.1931 0.2229 0.0027  -0.0063 -0.0133 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.1953 0.1939 0.2105 0.0017  -0.0103 -0.0136 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.2110 0.2069 0.2408 0.0007  0.0049  -0.0164 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.2019 0.2020 0.2064 -0.0030 -0.0086 -0.0145 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.2199 0.2251 0.2986 0.0107  -0.0006 -0.0078 11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.2302 0.2399 0.3309 0.0123  0.0060  -0.0064 11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.2475 0.2509 0.3451 0.0108  0.0221  -0.0120 11  TYR   A C   
27   O O   . TYR   A 5   ? 0.2636 0.2594 0.3609 0.0127  0.0281  -0.0137 11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.2175 0.2305 0.3418 0.0174  0.0007  0.0004  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.2090 0.2270 0.3341 0.0165  -0.0155 0.0061  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.2070 0.2327 0.3425 0.0147  -0.0206 0.0090  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.2160 0.2296 0.3274 0.0162  -0.0251 0.0077  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.2111 0.2389 0.3442 0.0123  -0.0354 0.0135  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.2273 0.2428 0.3350 0.0137  -0.0390 0.0120  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.2309 0.2529 0.3489 0.0116  -0.0442 0.0146  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.2526 0.2738 0.3632 0.0076  -0.0576 0.0178  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.2456 0.2502 0.3378 0.0061  0.0291  -0.0152 12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.2572 0.2541 0.3413 0.0021  0.0450  -0.0212 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.2652 0.2674 0.3628 0.0005  0.0533  -0.0212 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.2657 0.2749 0.3611 -0.0027 0.0468  -0.0189 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.2895 0.2800 0.3429 -0.0056 0.0446  -0.0252 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.3011 0.2990 0.3466 -0.0087 0.0333  -0.0221 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.3134 0.2948 0.3542 -0.0127 0.0602  -0.0313 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.2518 0.2511 0.3665 0.0032  0.0679  -0.0231 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.2567 0.2614 0.3879 0.0021  0.0784  -0.0230 13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.2513 0.2707 0.4060 0.0057  0.0658  -0.0147 13  GLY   A C   
46   O O   . GLY   A 7   ? 0.2607 0.2848 0.4314 0.0117  0.0549  -0.0089 13  GLY   A O   
47   N N   . ASN   A 8   ? 0.2546 0.2805 0.4090 0.0009  0.0656  -0.0136 14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.2519 0.2906 0.4259 0.0028  0.0523  -0.0058 14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.2383 0.2771 0.3911 -0.0006 0.0357  -0.0046 14  ASN   A C   
50   O O   . ASN   A 8   ? 0.2372 0.2828 0.3953 -0.0030 0.0278  -0.0008 14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.2872 0.3337 0.4787 0.0001  0.0613  -0.0040 14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.3633 0.4122 0.5847 0.0054  0.0767  -0.0033 14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.3779 0.4318 0.6252 0.0127  0.0716  0.0025  14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.3951 0.4398 0.6140 0.0016  0.0962  -0.0088 14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.2338 0.2649 0.3650 -0.0006 0.0308  -0.0076 15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.2190 0.2493 0.3320 -0.0029 0.0174  -0.0068 15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.2079 0.2362 0.3183 0.0014  0.0063  -0.0051 15  TYR   A C   
58   O O   . TYR   A 9   ? 0.2124 0.2368 0.3251 0.0049  0.0099  -0.0060 15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.2272 0.2507 0.3137 -0.0088 0.0218  -0.0114 15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.2300 0.2541 0.3123 -0.0156 0.0305  -0.0125 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.2438 0.2747 0.3346 -0.0178 0.0258  -0.0087 15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.2479 0.2645 0.3155 -0.0211 0.0433  -0.0172 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.2616 0.2929 0.3479 -0.0248 0.0339  -0.0090 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.2669 0.2829 0.3268 -0.0291 0.0513  -0.0180 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.2784 0.3023 0.3486 -0.0307 0.0467  -0.0136 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.3081 0.3312 0.3703 -0.0393 0.0550  -0.0139 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.1716 0.2008 0.2746 0.0004  -0.0063 -0.0032 16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.1532 0.1791 0.2483 0.0027  -0.0167 -0.0022 16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.1633 0.1849 0.2371 0.0000  -0.0199 -0.0050 16  ARG   A C   
70   O O   . ARG   A 10  ? 0.1630 0.1862 0.2362 -0.0027 -0.0229 -0.0044 16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.1643 0.1942 0.2725 0.0031  -0.0283 0.0032  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.2149 0.2391 0.3087 0.0030  -0.0393 0.0035  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.2230 0.2500 0.3282 0.0012  -0.0516 0.0096  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.2473 0.2676 0.3347 -0.0026 -0.0611 0.0081  16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.2711 0.2844 0.3440 -0.0037 -0.0679 0.0080  16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.2589 0.2720 0.3338 -0.0013 -0.0679 0.0105  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.2883 0.2936 0.3439 -0.0078 -0.0742 0.0055  16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.1674 0.1841 0.2264 0.0007  -0.0188 -0.0075 17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.1793 0.1931 0.2225 -0.0011 -0.0214 -0.0090 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.1815 0.1917 0.2185 0.0011  -0.0290 -0.0090 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.1906 0.1985 0.2251 0.0030  -0.0292 -0.0089 17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.1895 0.2009 0.2209 -0.0031 -0.0149 -0.0110 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.1890 0.2001 0.2099 -0.0051 -0.0178 -0.0105 17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.2054 0.2174 0.2392 -0.0066 -0.0056 -0.0122 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.1765 0.1848 0.2094 0.0002  -0.0341 -0.0092 18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.1752 0.1777 0.1989 0.0010  -0.0398 -0.0103 18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.1755 0.1744 0.1903 0.0010  -0.0385 -0.0124 18  VAL   A C   
88   O O   . VAL   A 12  ? 0.1692 0.1706 0.1878 -0.0001 -0.0363 -0.0115 18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.1977 0.1986 0.2266 -0.0008 -0.0478 -0.0086 18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.2291 0.2341 0.2695 -0.0002 -0.0504 -0.0048 18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.1919 0.1952 0.2287 -0.0030 -0.0486 -0.0079 18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.1713 0.1638 0.1751 0.0018  -0.0397 -0.0146 19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.1813 0.1693 0.1801 0.0026  -0.0373 -0.0167 19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.1887 0.1728 0.1915 0.0009  -0.0410 -0.0172 19  ASN   A C   
95   O O   . ASN   A 13  ? 0.2002 0.1806 0.2014 -0.0016 -0.0467 -0.0176 19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.2084 0.1882 0.1940 0.0033  -0.0364 -0.0200 19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.2209 0.2039 0.2024 0.0046  -0.0326 -0.0192 19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.2401 0.2234 0.2185 0.0038  -0.0350 -0.0182 19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.2166 0.2022 0.1995 0.0064  -0.0271 -0.0189 19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.1704 0.1553 0.1788 0.0014  -0.0386 -0.0162 20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.1665 0.1473 0.1796 -0.0005 -0.0419 -0.0162 20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.1942 0.1622 0.1967 -0.0016 -0.0441 -0.0209 20  ARG   A C   
103  O O   . ARG   A 14  ? 0.2131 0.1771 0.2158 -0.0053 -0.0497 -0.0211 20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.1590 0.1417 0.1799 0.0004  -0.0390 -0.0134 20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.1680 0.1480 0.1957 -0.0023 -0.0426 -0.0119 20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.1755 0.1555 0.2111 -0.0011 -0.0403 -0.0083 20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.2202 0.1971 0.2629 -0.0038 -0.0436 -0.0059 20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.2378 0.2025 0.2796 -0.0035 -0.0445 -0.0090 20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.2275 0.1813 0.2596 -0.0013 -0.0419 -0.0154 20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.2314 0.1933 0.2806 -0.0063 -0.0475 -0.0059 20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.2073 0.1682 0.1992 0.0004  -0.0396 -0.0247 21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.2287 0.1742 0.2061 -0.0022 -0.0401 -0.0304 21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.2555 0.1976 0.2216 -0.0074 -0.0479 -0.0308 21  HIS   A C   
114  O O   . HIS   A 15  ? 0.2807 0.2090 0.2320 -0.0123 -0.0506 -0.0350 21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.2462 0.1839 0.2155 0.0011  -0.0310 -0.0348 21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.2618 0.2037 0.2238 0.0021  -0.0284 -0.0346 21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.2612 0.2162 0.2337 0.0057  -0.0257 -0.0302 21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.2830 0.2168 0.2269 -0.0011 -0.0287 -0.0380 21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.2862 0.2406 0.2483 0.0053  -0.0239 -0.0312 21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.2942 0.2364 0.2391 0.0013  -0.0257 -0.0356 21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.2501 0.2037 0.2227 -0.0070 -0.0513 -0.0262 22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.2735 0.2262 0.2403 -0.0115 -0.0597 -0.0241 22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.2627 0.2244 0.2460 -0.0136 -0.0670 -0.0186 22  LEU   A C   
124  O O   . LEU   A 16  ? 0.2722 0.2359 0.2570 -0.0171 -0.0750 -0.0146 22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.2868 0.2439 0.2500 -0.0094 -0.0578 -0.0225 22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.3128 0.2618 0.2599 -0.0083 -0.0506 -0.0272 22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.3115 0.2654 0.2560 -0.0070 -0.0498 -0.0246 22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.3213 0.2534 0.2472 -0.0143 -0.0525 -0.0324 22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.2352 0.2033 0.2326 -0.0118 -0.0642 -0.0173 23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.2330 0.2101 0.2472 -0.0138 -0.0691 -0.0122 23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.2375 0.2088 0.2492 -0.0205 -0.0795 -0.0107 23  ALA   A C   
132  O O   . ALA   A 17  ? 0.2506 0.2090 0.2484 -0.0241 -0.0813 -0.0150 23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.2251 0.2069 0.2499 -0.0125 -0.0643 -0.0116 23  ALA   A CB  
134  N N   . THR   A 18  ? 0.2312 0.2117 0.2576 -0.0226 -0.0861 -0.0043 24  THR   A N   
135  C CA  . THR   A 18  ? 0.2449 0.2223 0.2719 -0.0304 -0.0982 -0.0006 24  THR   A CA  
136  C C   . THR   A 18  ? 0.2449 0.2262 0.2859 -0.0333 -0.1001 0.0016  24  THR   A C   
137  O O   . THR   A 18  ? 0.2358 0.2241 0.2879 -0.0291 -0.0920 0.0013  24  THR   A O   
138  C CB  . THR   A 18  ? 0.2645 0.2518 0.3053 -0.0311 -0.1052 0.0074  24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.2769 0.2792 0.3442 -0.0265 -0.0999 0.0118  24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.2599 0.2440 0.2887 -0.0283 -0.1033 0.0063  24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.2604 0.2379 0.3014 -0.0417 -0.1118 0.0049  25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.2736 0.2567 0.3307 -0.0453 -0.1146 0.0086  25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.2421 0.2450 0.3287 -0.0404 -0.1093 0.0151  25  HIS   A C   
144  O O   . HIS   A 19  ? 0.2395 0.2475 0.3365 -0.0393 -0.1033 0.0153  25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.3250 0.3035 0.3802 -0.0562 -0.1298 0.0133  25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.4333 0.3897 0.4575 -0.0632 -0.1343 0.0062  25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.4827 0.4251 0.4929 -0.0622 -0.1269 -0.0022 25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.4778 0.4232 0.4829 -0.0721 -0.1452 0.0067  25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.5155 0.4381 0.4985 -0.0697 -0.1315 -0.0079 25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.5178 0.4409 0.4945 -0.0766 -0.1427 -0.0030 25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.2218 0.2345 0.3213 -0.0379 -0.1108 0.0204  26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.2202 0.2494 0.3476 -0.0328 -0.1032 0.0255  26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.1997 0.2297 0.3229 -0.0259 -0.0878 0.0195  26  ASN   A C   
154  O O   . ASN   A 20  ? 0.1874 0.2260 0.3254 -0.0247 -0.0797 0.0208  26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.2523 0.2891 0.3940 -0.0307 -0.1073 0.0322  26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.3375 0.3898 0.5105 -0.0253 -0.0981 0.0374  26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.3599 0.4227 0.5568 -0.0280 -0.1003 0.0439  26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.3575 0.4112 0.5315 -0.0181 -0.0869 0.0344  26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.1986 0.2194 0.3004 -0.0226 -0.0838 0.0132  27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.1997 0.2205 0.2956 -0.0180 -0.0716 0.0084  27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.1920 0.2114 0.2872 -0.0207 -0.0693 0.0073  27  ASP   A C   
162  O O   . ASP   A 21  ? 0.2019 0.2278 0.3047 -0.0198 -0.0609 0.0079  27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.2076 0.2187 0.2819 -0.0153 -0.0700 0.0030  27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.2372 0.2501 0.3112 -0.0120 -0.0692 0.0039  27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.2261 0.2477 0.3158 -0.0092 -0.0637 0.0067  27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.2429 0.2474 0.3007 -0.0124 -0.0730 0.0016  27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.1968 0.2065 0.2821 -0.0248 -0.0766 0.0058  28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.2013 0.2081 0.2868 -0.0274 -0.0753 0.0054  28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.2057 0.2231 0.3114 -0.0314 -0.0762 0.0112  28  TRP   A C   
170  O O   . TRP   A 22  ? 0.2040 0.2239 0.3134 -0.0325 -0.0709 0.0122  28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.2059 0.1971 0.2758 -0.0306 -0.0813 0.0015  28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.2212 0.2028 0.2749 -0.0261 -0.0759 -0.0042 28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.2359 0.2096 0.2748 -0.0244 -0.0763 -0.0085 28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.2161 0.1962 0.2689 -0.0232 -0.0692 -0.0051 28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.2345 0.2022 0.2649 -0.0200 -0.0692 -0.0124 28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.2265 0.1989 0.2666 -0.0189 -0.0653 -0.0097 28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.2300 0.2154 0.2922 -0.0242 -0.0662 -0.0014 28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.2411 0.2111 0.2805 -0.0155 -0.0595 -0.0101 28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.2354 0.2178 0.2947 -0.0215 -0.0615 -0.0015 28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.2379 0.2136 0.2876 -0.0168 -0.0584 -0.0054 28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.2069 0.2307 0.3262 -0.0341 -0.0831 0.0160  29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.2101 0.2459 0.3527 -0.0377 -0.0837 0.0226  29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.2074 0.2553 0.3646 -0.0336 -0.0704 0.0240  29  ALA   A C   
184  O O   . ALA   A 23  ? 0.2167 0.2737 0.3909 -0.0364 -0.0664 0.0281  29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.2083 0.2491 0.3646 -0.0416 -0.0952 0.0289  29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.1751 0.2223 0.3252 -0.0277 -0.0631 0.0204  30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.1714 0.2262 0.3305 -0.0245 -0.0493 0.0200  30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.1644 0.2121 0.3023 -0.0227 -0.0418 0.0142  30  ASN   A C   
189  O O   . ASN   A 24  ? 0.1567 0.2054 0.2924 -0.0195 -0.0327 0.0118  30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.1657 0.2264 0.3394 -0.0198 -0.0477 0.0222  30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.2062 0.2766 0.4060 -0.0218 -0.0554 0.0303  30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.2233 0.3044 0.4464 -0.0225 -0.0484 0.0344  30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.2266 0.2934 0.4229 -0.0239 -0.0699 0.0331  30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.1711 0.2113 0.2947 -0.0254 -0.0457 0.0126  31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.1692 0.2035 0.2752 -0.0245 -0.0412 0.0092  31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.1941 0.2330 0.3001 -0.0270 -0.0301 0.0097  31  LEU   A C   
197  O O   . LEU   A 25  ? 0.2050 0.2483 0.3191 -0.0316 -0.0275 0.0127  31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.1804 0.2067 0.2779 -0.0269 -0.0476 0.0093  31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.1936 0.2149 0.2775 -0.0262 -0.0447 0.0081  31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.2285 0.2457 0.3019 -0.0211 -0.0443 0.0042  31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.1853 0.1998 0.2670 -0.0286 -0.0497 0.0098  31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.1844 0.2211 0.2786 -0.0254 -0.0238 0.0067  32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.1873 0.2248 0.2740 -0.0297 -0.0136 0.0063  32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.1934 0.2256 0.2635 -0.0327 -0.0171 0.0073  32  VAL   A C   
205  O O   . VAL   A 26  ? 0.2169 0.2493 0.2818 -0.0392 -0.0151 0.0104  32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.1893 0.2267 0.2743 -0.0270 -0.0045 0.0025  32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.2146 0.2492 0.2849 -0.0332 0.0055  0.0009  32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.1818 0.2254 0.2880 -0.0240 0.0001  0.0031  32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.1839 0.2119 0.2471 -0.0282 -0.0224 0.0057  33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.1940 0.2184 0.2464 -0.0297 -0.0256 0.0077  33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.1922 0.2122 0.2431 -0.0233 -0.0314 0.0056  33  TRP   A C   
212  O O   . TRP   A 27  ? 0.1944 0.2138 0.2458 -0.0190 -0.0310 0.0020  33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.1912 0.2158 0.2313 -0.0338 -0.0193 0.0074  33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.2052 0.2279 0.2364 -0.0353 -0.0236 0.0107  33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.2255 0.2485 0.2538 -0.0413 -0.0272 0.0171  33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.2023 0.2237 0.2284 -0.0314 -0.0247 0.0091  33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.2295 0.2522 0.2534 -0.0409 -0.0310 0.0202  33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.2120 0.2338 0.2347 -0.0347 -0.0291 0.0150  33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.2039 0.2240 0.2295 -0.0254 -0.0230 0.0042  33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.2053 0.2275 0.2244 -0.0327 -0.0306 0.0158  33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.2096 0.2288 0.2293 -0.0236 -0.0244 0.0044  33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.2026 0.2234 0.2202 -0.0269 -0.0279 0.0101  33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.1809 0.1972 0.2307 -0.0229 -0.0360 0.0080  34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.1915 0.2024 0.2393 -0.0173 -0.0389 0.0057  34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.1969 0.2069 0.2444 -0.0176 -0.0401 0.0102  34  GLU   A C   
226  O O   . GLU   A 28  ? 0.2009 0.2120 0.2521 -0.0219 -0.0421 0.0157  34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.2072 0.2116 0.2587 -0.0149 -0.0433 0.0028  34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.2491 0.2507 0.3071 -0.0182 -0.0468 0.0060  34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.2352 0.2303 0.2949 -0.0167 -0.0484 0.0082  34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.2811 0.2753 0.3467 -0.0202 -0.0508 0.0129  34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.2094 0.2006 0.2660 -0.0121 -0.0468 0.0061  34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.1840 0.1925 0.2288 -0.0132 -0.0392 0.0087  35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.1839 0.1929 0.2330 -0.0125 -0.0403 0.0140  35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.1962 0.1993 0.2468 -0.0056 -0.0386 0.0100  35  ASP   A C   
235  O O   . ASP   A 29  ? 0.2124 0.2167 0.2570 -0.0032 -0.0358 0.0067  35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.1965 0.2126 0.2405 -0.0169 -0.0395 0.0183  35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.2600 0.2791 0.3119 -0.0184 -0.0429 0.0271  35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.2732 0.2890 0.3355 -0.0125 -0.0431 0.0279  35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.2716 0.2958 0.3194 -0.0260 -0.0452 0.0336  35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.1899 0.1857 0.2480 -0.0027 -0.0393 0.0102  36  SER   A N   
241  C CA  A SER   A 30  ? 0.2051 0.1926 0.2639 0.0034  -0.0355 0.0054  36  SER   A CA  
242  C CA  B SER   A 30  ? 0.2041 0.1917 0.2624 0.0033  -0.0354 0.0052  36  SER   A CA  
243  C C   . SER   A 30  ? 0.2023 0.1954 0.2665 0.0064  -0.0321 0.0091  36  SER   A C   
244  O O   . SER   A 30  ? 0.2253 0.2154 0.2845 0.0101  -0.0274 0.0041  36  SER   A O   
245  C CB  A SER   A 30  ? 0.2409 0.2181 0.3080 0.0051  -0.0357 0.0055  36  SER   A CB  
246  C CB  B SER   A 30  ? 0.2397 0.2159 0.3044 0.0052  -0.0354 0.0040  36  SER   A CB  
247  O OG  A SER   A 30  ? 0.2798 0.2455 0.3448 0.0103  -0.0299 -0.0010 36  SER   A OG  
248  O OG  B SER   A 30  ? 0.2666 0.2457 0.3447 0.0036  -0.0384 0.0125  36  SER   A OG  
249  N N   . SER   A 31  ? 0.1712 0.1730 0.2452 0.0036  -0.0351 0.0186  37  SER   A N   
250  C CA  . SER   A 31  ? 0.1797 0.1886 0.2617 0.0053  -0.0335 0.0242  37  SER   A CA  
251  C C   . SER   A 31  ? 0.1795 0.1937 0.2489 0.0035  -0.0320 0.0211  37  SER   A C   
252  O O   . SER   A 31  ? 0.1943 0.2123 0.2683 0.0061  -0.0290 0.0228  37  SER   A O   
253  C CB  . SER   A 31  ? 0.2062 0.2232 0.3011 0.0008  -0.0394 0.0368  37  SER   A CB  
254  O OG  . SER   A 31  ? 0.2603 0.2846 0.3439 -0.0079 -0.0439 0.0403  37  SER   A OG  
255  N N   . ARG   A 32  ? 0.1612 0.1753 0.2166 -0.0005 -0.0332 0.0166  38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.1716 0.1888 0.2156 -0.0020 -0.0313 0.0134  38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.1701 0.1805 0.2053 0.0021  -0.0281 0.0046  38  ARG   A C   
258  O O   . ARG   A 32  ? 0.1697 0.1815 0.1965 0.0015  -0.0266 0.0023  38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.1904 0.2115 0.2257 -0.0094 -0.0332 0.0150  38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.2117 0.2388 0.2501 -0.0164 -0.0372 0.0242  38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.2250 0.2528 0.2510 -0.0249 -0.0371 0.0240  38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.1916 0.2188 0.2057 -0.0266 -0.0333 0.0195  38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.2017 0.2289 0.2036 -0.0354 -0.0322 0.0206  38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.1863 0.2146 0.1843 -0.0441 -0.0349 0.0262  38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.2149 0.2396 0.2069 -0.0363 -0.0282 0.0160  38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.1829 0.1850 0.2183 0.0048  -0.0282 0.0002  39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.1756 0.1706 0.2007 0.0064  -0.0274 -0.0071 39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.1646 0.1630 0.1844 0.0032  -0.0300 -0.0079 39  ASP   A C   
269  O O   . ASP   A 33  ? 0.1681 0.1644 0.1803 0.0040  -0.0297 -0.0112 39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.1706 0.1620 0.1894 0.0097  -0.0227 -0.0105 39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.2176 0.2002 0.2232 0.0095  -0.0234 -0.0170 39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.2193 0.1946 0.2226 0.0082  -0.0265 -0.0196 39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.2082 0.1909 0.2052 0.0096  -0.0219 -0.0185 39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.1551 0.1585 0.1795 -0.0005 -0.0317 -0.0045 40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.1494 0.1558 0.1720 -0.0030 -0.0318 -0.0055 40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.1605 0.1665 0.1892 -0.0050 -0.0344 -0.0052 40  LEU   A C   
277  O O   . LEU   A 34  ? 0.1664 0.1724 0.2000 -0.0068 -0.0359 -0.0024 40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.1483 0.1605 0.1689 -0.0071 -0.0289 -0.0025 40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.1695 0.1828 0.1836 -0.0068 -0.0266 -0.0026 40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.1642 0.1806 0.1729 -0.0131 -0.0241 -0.0003 40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.2019 0.2119 0.2114 -0.0033 -0.0256 -0.0069 40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.1570 0.1640 0.1872 -0.0051 -0.0349 -0.0068 41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.1594 0.1685 0.1983 -0.0074 -0.0368 -0.0056 41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.1677 0.1818 0.2115 -0.0077 -0.0329 -0.0056 41  LEU   A C   
285  O O   . LEU   A 35  ? 0.1819 0.1952 0.2232 -0.0052 -0.0322 -0.0071 41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.1551 0.1583 0.1948 -0.0070 -0.0431 -0.0070 41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.1682 0.1741 0.2188 -0.0104 -0.0466 -0.0047 41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.1950 0.1926 0.2434 -0.0120 -0.0527 -0.0057 41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.1797 0.1907 0.2389 -0.0103 -0.0482 -0.0035 41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.1622 0.1809 0.2130 -0.0110 -0.0292 -0.0038 42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.1459 0.1686 0.2046 -0.0111 -0.0231 -0.0040 42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.1666 0.1939 0.2411 -0.0122 -0.0253 -0.0014 42  VAL   A C   
293  O O   . VAL   A 36  ? 0.1682 0.1966 0.2449 -0.0158 -0.0269 0.0005  42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.1597 0.1830 0.2118 -0.0152 -0.0138 -0.0047 42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.1767 0.2020 0.2380 -0.0147 -0.0050 -0.0061 42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.1670 0.1866 0.2045 -0.0154 -0.0133 -0.0061 42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.1562 0.1864 0.2430 -0.0095 -0.0263 -0.0004 43  SER   A N   
298  C CA  . SER   A 37  ? 0.1489 0.1855 0.2547 -0.0108 -0.0286 0.0035  43  SER   A CA  
299  C C   . SER   A 37  ? 0.1719 0.2142 0.2935 -0.0090 -0.0184 0.0043  43  SER   A C   
300  O O   . SER   A 37  ? 0.1658 0.2049 0.2818 -0.0065 -0.0116 0.0014  43  SER   A O   
301  C CB  . SER   A 37  ? 0.1548 0.1900 0.2643 -0.0102 -0.0408 0.0059  43  SER   A CB  
302  O OG  . SER   A 37  ? 0.1989 0.2321 0.3063 -0.0065 -0.0421 0.0055  43  SER   A OG  
303  N N   . SER   A 38  ? 0.1676 0.2177 0.3097 -0.0105 -0.0164 0.0081  44  SER   A N   
304  C CA  . SER   A 38  ? 0.1885 0.2442 0.3500 -0.0083 -0.0045 0.0090  44  SER   A CA  
305  C C   . SER   A 38  ? 0.2174 0.2782 0.4007 -0.0037 -0.0108 0.0143  44  SER   A C   
306  O O   . SER   A 38  ? 0.2211 0.2840 0.4089 -0.0049 -0.0249 0.0189  44  SER   A O   
307  C CB  . SER   A 38  ? 0.1986 0.2612 0.3735 -0.0124 0.0024  0.0112  44  SER   A CB  
308  O OG  . SER   A 38  ? 0.2358 0.3044 0.4237 -0.0145 -0.0095 0.0170  44  SER   A OG  
309  N N   . THR   A 39  ? 0.2316 0.2936 0.4291 0.0008  -0.0002 0.0141  45  THR   A N   
310  C CA  . THR   A 39  ? 0.2621 0.3292 0.4840 0.0057  -0.0053 0.0206  45  THR   A CA  
311  C C   . THR   A 39  ? 0.2863 0.3616 0.5404 0.0087  0.0085  0.0237  45  THR   A C   
312  O O   . THR   A 39  ? 0.2983 0.3705 0.5486 0.0081  0.0257  0.0177  45  THR   A O   
313  C CB  . THR   A 39  ? 0.2921 0.3506 0.5019 0.0098  -0.0054 0.0180  45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.3213 0.3740 0.5268 0.0117  0.0122  0.0116  45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.3029 0.3531 0.4815 0.0073  -0.0157 0.0143  45  THR   A CG2 
316  N N   . THR   A 40  ? 0.2873 0.3723 0.5732 0.0116  0.0014  0.0332  46  THR   A N   
317  C CA  . THR   A 40  ? 0.2955 0.3896 0.6186 0.0158  0.0147  0.0376  46  THR   A CA  
318  C C   . THR   A 40  ? 0.3063 0.3931 0.6348 0.0227  0.0269  0.0346  46  THR   A C   
319  O O   . THR   A 40  ? 0.3166 0.4013 0.6550 0.0251  0.0473  0.0299  46  THR   A O   
320  C CB  . THR   A 40  ? 0.3022 0.4113 0.6614 0.0155  0.0014  0.0510  46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.3187 0.4262 0.6724 0.0150  -0.0188 0.0570  46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.3094 0.4261 0.6697 0.0085  -0.0039 0.0532  46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.3080 0.3892 0.6275 0.0250  0.0152  0.0366  47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.3168 0.3893 0.6393 0.0311  0.0249  0.0341  47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.3292 0.3870 0.6157 0.0291  0.0380  0.0210  47  ALA   A C   
326  O O   . ALA   A 41  ? 0.3415 0.3952 0.5963 0.0233  0.0325  0.0157  47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.3262 0.3974 0.6479 0.0328  0.0069  0.0413  47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.3264 0.3755 0.6184 0.0334  0.0546  0.0164  48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.3376 0.3714 0.5970 0.0303  0.0676  0.0045  48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.3316 0.3563 0.5680 0.0307  0.0570  0.0034  48  GLN   A C   
331  O O   . GLN   A 42  ? 0.3324 0.3566 0.5857 0.0362  0.0519  0.0092  48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.3749 0.4015 0.6517 0.0342  0.0915  -0.0002 48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.4835 0.4919 0.7266 0.0298  0.1059  -0.0125 48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.6018 0.6072 0.8196 0.0207  0.1154  -0.0202 48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 0.6274 0.6431 0.8586 0.0188  0.1180  -0.0176 48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.6374 0.6284 0.8181 0.0138  0.1201  -0.0289 48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.3199 0.3381 0.5198 0.0246  0.0532  -0.0030 49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.3192 0.3290 0.4958 0.0240  0.0450  -0.0048 49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.3210 0.3162 0.4811 0.0226  0.0599  -0.0131 49  GLY   A C   
340  O O   . GLY   A 43  ? 0.3292 0.3189 0.4799 0.0182  0.0745  -0.0201 49  GLY   A O   
341  N N   . CYS   A 44  ? 0.3165 0.3040 0.4696 0.0247  0.0558  -0.0127 50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.3342 0.3061 0.4722 0.0228  0.0696  -0.0204 50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.3129 0.2778 0.4200 0.0180  0.0621  -0.0232 50  CYS   A C   
344  O O   . CYS   A 44  ? 0.3007 0.2527 0.3989 0.0174  0.0692  -0.0270 50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.3814 0.3472 0.5464 0.0301  0.0795  -0.0185 50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.5115 0.4898 0.7128 0.0388  0.0631  -0.0042 50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.2941 0.2665 0.3848 0.0141  0.0492  -0.0215 51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.3089 0.2763 0.3720 0.0091  0.0434  -0.0238 51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.3268 0.2862 0.3682 0.0007  0.0544  -0.0312 51  ASP   A C   
350  O O   . ASP   A 45  ? 0.3481 0.3094 0.3910 -0.0023 0.0618  -0.0335 51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.3327 0.3100 0.3877 0.0081  0.0281  -0.0198 51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.4107 0.3926 0.4765 0.0132  0.0157  -0.0132 51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.4352 0.4116 0.5078 0.0165  0.0161  -0.0111 51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.4150 0.4046 0.4812 0.0132  0.0055  -0.0100 51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.3243 0.2746 0.3448 -0.0042 0.0550  -0.0342 52  THR   A N   
356  C CA  . THR   A 46  ? 0.3253 0.2665 0.3217 -0.0144 0.0633  -0.0402 52  THR   A CA  
357  C C   . THR   A 46  ? 0.3043 0.2526 0.2828 -0.0206 0.0516  -0.0373 52  THR   A C   
358  O O   . THR   A 46  ? 0.3040 0.2545 0.2787 -0.0191 0.0424  -0.0342 52  THR   A O   
359  C CB  . THR   A 46  ? 0.3614 0.2867 0.3473 -0.0169 0.0711  -0.0447 52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.3728 0.2905 0.3781 -0.0108 0.0842  -0.0474 52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.3800 0.2945 0.3357 -0.0299 0.0766  -0.0501 52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.2792 0.2313 0.2483 -0.0273 0.0520  -0.0376 53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.2644 0.2231 0.2199 -0.0328 0.0408  -0.0335 53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.2783 0.2270 0.2094 -0.0439 0.0433  -0.0358 53  ILE   A C   
365  O O   . ILE   A 47  ? 0.2992 0.2364 0.2175 -0.0516 0.0544  -0.0413 53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.2563 0.2238 0.2137 -0.0356 0.0377  -0.0308 53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.2563 0.2324 0.2370 -0.0265 0.0360  -0.0289 53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.2539 0.2289 0.2027 -0.0397 0.0259  -0.0252 53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.2594 0.2425 0.2513 -0.0180 0.0246  -0.0248 53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.2602 0.2128 0.1841 -0.0460 0.0334  -0.0316 54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.2773 0.2228 0.1792 -0.0578 0.0325  -0.0316 54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.2933 0.2413 0.1820 -0.0690 0.0300  -0.0289 54  ALA   A C   
373  O O   . ALA   A 48  ? 0.2907 0.2505 0.1892 -0.0661 0.0232  -0.0239 54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.2714 0.2247 0.1755 -0.0557 0.0217  -0.0259 54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.3130 0.2489 0.1782 -0.0826 0.0348  -0.0318 55  ARG   A N   
376  C CA  . ARG   A 49  ? 0.3185 0.2555 0.1673 -0.0960 0.0306  -0.0278 55  ARG   A CA  
377  C C   . ARG   A 49  ? 0.3330 0.2651 0.1628 -0.1082 0.0242  -0.0246 55  ARG   A C   
378  O O   . ARG   A 49  ? 0.3685 0.2838 0.1758 -0.1191 0.0318  -0.0306 55  ARG   A O   
379  C CB  . ARG   A 49  ? 0.3432 0.2679 0.1783 -0.1034 0.0438  -0.0348 55  ARG   A CB  
380  C CG  . ARG   A 49  ? 0.3454 0.2753 0.2027 -0.0910 0.0512  -0.0378 55  ARG   A CG  
381  C CD  . ARG   A 49  ? 0.3319 0.2791 0.2060 -0.0853 0.0404  -0.0299 55  ARG   A CD  
382  N NE  . ARG   A 49  ? 0.3077 0.2585 0.2011 -0.0757 0.0475  -0.0328 55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.3183 0.2824 0.2311 -0.0675 0.0398  -0.0277 55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.2721 0.2460 0.1878 -0.0669 0.0263  -0.0203 55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.2933 0.2604 0.2237 -0.0599 0.0459  -0.0299 55  ARG   A NH2 
386  N N   . CYS   A 50  ? 0.3272 0.2732 0.1667 -0.1065 0.0108  -0.0153 56  CYS   A N   
387  C CA  . CYS   A 50  ? 0.3335 0.2788 0.1622 -0.1158 0.0032  -0.0105 56  CYS   A CA  
388  C C   . CYS   A 50  ? 0.3207 0.2851 0.1656 -0.1138 -0.0110 0.0018  56  CYS   A C   
389  O O   . CYS   A 50  ? 0.3093 0.2853 0.1727 -0.1044 -0.0139 0.0052  56  CYS   A O   
390  C CB  . CYS   A 50  ? 0.3569 0.2954 0.1895 -0.1083 0.0083  -0.0159 56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.3193 0.2729 0.1831 -0.0878 0.0050  -0.0136 56  CYS   A SG  
392  N N   . ASP   A 51  ? 0.3299 0.2971 0.1700 -0.1218 -0.0189 0.0082  57  ASP   A N   
393  C CA  . ASP   A 51  ? 0.3314 0.3168 0.1907 -0.1190 -0.0305 0.0200  57  ASP   A CA  
394  C C   . ASP   A 51  ? 0.3273 0.3162 0.1967 -0.1119 -0.0306 0.0201  57  ASP   A C   
395  O O   . ASP   A 51  ? 0.3338 0.3346 0.2134 -0.1144 -0.0391 0.0299  57  ASP   A O   
396  C CB  . ASP   A 51  ? 0.3779 0.3684 0.2282 -0.1360 -0.0423 0.0317  57  ASP   A CB  
397  C CG  . ASP   A 51  ? 0.4922 0.4714 0.3178 -0.1530 -0.0445 0.0318  57  ASP   A CG  
398  O OD1 . ASP   A 51  ? 0.5224 0.4886 0.3377 -0.1512 -0.0358 0.0221  57  ASP   A OD1 
399  O OD2 . ASP   A 51  ? 0.5576 0.5402 0.3739 -0.1691 -0.0555 0.0422  57  ASP   A OD2 
400  N N   . CYS   A 52  ? 0.3158 0.2946 0.1833 -0.1035 -0.0213 0.0103  58  CYS   A N   
401  C CA  . CYS   A 52  ? 0.2876 0.2693 0.1644 -0.0962 -0.0211 0.0105  58  CYS   A CA  
402  C C   . CYS   A 52  ? 0.2726 0.2721 0.1725 -0.0870 -0.0268 0.0182  58  CYS   A C   
403  O O   . CYS   A 52  ? 0.2810 0.2878 0.1937 -0.0794 -0.0272 0.0192  58  CYS   A O   
404  C CB  . CYS   A 52  ? 0.2981 0.2690 0.1755 -0.0857 -0.0115 0.0006  58  CYS   A CB  
405  S SG  . CYS   A 52  ? 0.3564 0.3036 0.2100 -0.0947 -0.0019 -0.0091 58  CYS   A SG  
406  N N   . GLN   A 53  ? 0.2515 0.2568 0.1572 -0.0873 -0.0296 0.0228  59  GLN   A N   
407  C CA  . GLN   A 53  ? 0.2324 0.2526 0.1598 -0.0779 -0.0316 0.0286  59  GLN   A CA  
408  C C   . GLN   A 53  ? 0.2276 0.2449 0.1568 -0.0707 -0.0268 0.0248  59  GLN   A C   
409  O O   . GLN   A 53  ? 0.2214 0.2493 0.1649 -0.0655 -0.0272 0.0295  59  GLN   A O   
410  C CB  . GLN   A 53  ? 0.2464 0.2812 0.1857 -0.0851 -0.0401 0.0413  59  GLN   A CB  
411  C CG  . GLN   A 53  ? 0.2871 0.3292 0.2337 -0.0880 -0.0458 0.0476  59  GLN   A CG  
412  C CD  . GLN   A 53  ? 0.3471 0.4055 0.3114 -0.0938 -0.0548 0.0622  59  GLN   A CD  
413  O OE1 . GLN   A 53  ? 0.3613 0.4211 0.3174 -0.1088 -0.0635 0.0702  59  GLN   A OE1 
414  N NE2 . GLN   A 53  ? 0.3046 0.3755 0.2941 -0.0827 -0.0526 0.0663  59  GLN   A NE2 
415  N N   . THR   A 54  ? 0.2187 0.2213 0.1341 -0.0704 -0.0216 0.0167  60  THR   A N   
416  C CA  . THR   A 54  ? 0.2256 0.2235 0.1414 -0.0636 -0.0177 0.0133  60  THR   A CA  
417  C C   . THR   A 54  ? 0.2106 0.1973 0.1234 -0.0559 -0.0122 0.0048  60  THR   A C   
418  O O   . THR   A 54  ? 0.2273 0.2059 0.1328 -0.0589 -0.0096 0.0004  60  THR   A O   
419  C CB  . THR   A 54  ? 0.2885 0.2799 0.1935 -0.0726 -0.0184 0.0149  60  THR   A CB  
420  O OG1 . THR   A 54  ? 0.3266 0.3015 0.2142 -0.0801 -0.0155 0.0090  60  THR   A OG1 
421  C CG2 . THR   A 54  ? 0.3024 0.3061 0.2125 -0.0816 -0.0248 0.0246  60  THR   A CG2 
422  N N   . GLY   A 55  ? 0.1991 0.1862 0.1183 -0.0466 -0.0105 0.0033  61  GLY   A N   
423  C CA  . GLY   A 55  ? 0.2021 0.1805 0.1221 -0.0394 -0.0071 -0.0025 61  GLY   A CA  
424  C C   . GLY   A 55  ? 0.1958 0.1746 0.1201 -0.0321 -0.0075 -0.0019 61  GLY   A C   
425  O O   . GLY   A 55  ? 0.1960 0.1791 0.1197 -0.0332 -0.0086 0.0017  61  GLY   A O   
426  N N   . VAL   A 56  ? 0.1898 0.1639 0.1181 -0.0255 -0.0067 -0.0050 62  VAL   A N   
427  C CA  . VAL   A 56  ? 0.1900 0.1632 0.1203 -0.0199 -0.0085 -0.0039 62  VAL   A CA  
428  C C   . VAL   A 56  ? 0.1909 0.1678 0.1283 -0.0138 -0.0104 -0.0052 62  VAL   A C   
429  O O   . VAL   A 56  ? 0.2069 0.1822 0.1497 -0.0121 -0.0096 -0.0076 62  VAL   A O   
430  C CB  . VAL   A 56  ? 0.1919 0.1534 0.1201 -0.0196 -0.0076 -0.0043 62  VAL   A CB  
431  C CG1 . VAL   A 56  ? 0.2053 0.1657 0.1340 -0.0155 -0.0114 -0.0015 62  VAL   A CG1 
432  C CG2 . VAL   A 56  ? 0.1986 0.1545 0.1181 -0.0267 -0.0057 -0.0034 62  VAL   A CG2 
433  N N   . TYR   A 57  ? 0.1741 0.1549 0.1108 -0.0112 -0.0124 -0.0039 63  TYR   A N   
434  C CA  . TYR   A 57  ? 0.1677 0.1498 0.1087 -0.0067 -0.0148 -0.0055 63  TYR   A CA  
435  C C   . TYR   A 57  ? 0.2018 0.1787 0.1384 -0.0051 -0.0185 -0.0042 63  TYR   A C   
436  O O   . TYR   A 57  ? 0.2108 0.1847 0.1398 -0.0072 -0.0185 -0.0021 63  TYR   A O   
437  C CB  . TYR   A 57  ? 0.1629 0.1524 0.1066 -0.0058 -0.0136 -0.0060 63  TYR   A CB  
438  C CG  . TYR   A 57  ? 0.1778 0.1685 0.1162 -0.0055 -0.0118 -0.0053 63  TYR   A CG  
439  C CD1 . TYR   A 57  ? 0.1895 0.1838 0.1261 -0.0084 -0.0087 -0.0027 63  TYR   A CD1 
440  C CD2 . TYR   A 57  ? 0.1933 0.1810 0.1280 -0.0032 -0.0124 -0.0075 63  TYR   A CD2 
441  C CE1 . TYR   A 57  ? 0.2070 0.2030 0.1404 -0.0080 -0.0047 -0.0022 63  TYR   A CE1 
442  C CE2 . TYR   A 57  ? 0.2000 0.1871 0.1282 -0.0034 -0.0081 -0.0080 63  TYR   A CE2 
443  C CZ  . TYR   A 57  ? 0.2071 0.1987 0.1355 -0.0055 -0.0036 -0.0054 63  TYR   A CZ  
444  O OH  . TYR   A 57  ? 0.2295 0.2206 0.1526 -0.0057 0.0026  -0.0061 63  TYR   A OH  
445  N N   . TYR   A 58  ? 0.2107 0.1863 0.1516 -0.0025 -0.0224 -0.0048 64  TYR   A N   
446  C CA  . TYR   A 58  ? 0.2203 0.1909 0.1559 -0.0027 -0.0280 -0.0025 64  TYR   A CA  
447  C C   . TYR   A 58  ? 0.2190 0.1899 0.1454 -0.0035 -0.0280 -0.0047 64  TYR   A C   
448  O O   . TYR   A 58  ? 0.2088 0.1829 0.1400 -0.0018 -0.0270 -0.0075 64  TYR   A O   
449  C CB  . TYR   A 58  ? 0.2107 0.1796 0.1574 -0.0005 -0.0335 -0.0004 64  TYR   A CB  
450  C CG  . TYR   A 58  ? 0.2361 0.2001 0.1767 -0.0025 -0.0416 0.0038  64  TYR   A CG  
451  C CD1 . TYR   A 58  ? 0.2545 0.2132 0.1878 -0.0049 -0.0440 0.0081  64  TYR   A CD1 
452  C CD2 . TYR   A 58  ? 0.2521 0.2160 0.1920 -0.0034 -0.0476 0.0040  64  TYR   A CD2 
453  C CE1 . TYR   A 58  ? 0.2696 0.2233 0.1951 -0.0085 -0.0527 0.0132  64  TYR   A CE1 
454  C CE2 . TYR   A 58  ? 0.2680 0.2264 0.1984 -0.0076 -0.0563 0.0085  64  TYR   A CE2 
455  C CZ  . TYR   A 58  ? 0.2884 0.2418 0.2109 -0.0104 -0.0590 0.0133  64  TYR   A CZ  
456  O OH  . TYR   A 58  ? 0.3361 0.2836 0.2477 -0.0160 -0.0688 0.0189  64  TYR   A OH  
457  N N   . CYS   A 59  ? 0.2222 0.1883 0.1345 -0.0065 -0.0283 -0.0036 65  CYS   A N   
458  C CA  . CYS   A 59  ? 0.2395 0.2023 0.1390 -0.0084 -0.0260 -0.0066 65  CYS   A CA  
459  C C   . CYS   A 59  ? 0.2722 0.2262 0.1591 -0.0126 -0.0341 -0.0044 65  CYS   A C   
460  O O   . CYS   A 59  ? 0.2822 0.2314 0.1584 -0.0165 -0.0366 -0.0007 65  CYS   A O   
461  C CB  . CYS   A 59  ? 0.2500 0.2140 0.1420 -0.0101 -0.0183 -0.0069 65  CYS   A CB  
462  S SG  . CYS   A 59  ? 0.2874 0.2454 0.1635 -0.0123 -0.0113 -0.0118 65  CYS   A SG  
463  N N   . SER   A 60  ? 0.2621 0.2141 0.1502 -0.0128 -0.0392 -0.0058 66  SER   A N   
464  C CA  . SER   A 60  ? 0.2818 0.2260 0.1587 -0.0183 -0.0491 -0.0024 66  SER   A CA  
465  C C   . SER   A 60  ? 0.2957 0.2299 0.1466 -0.0251 -0.0472 -0.0041 66  SER   A C   
466  O O   . SER   A 60  ? 0.3138 0.2414 0.1522 -0.0315 -0.0556 0.0012  66  SER   A O   
467  C CB  . SER   A 60  ? 0.3335 0.2773 0.2158 -0.0185 -0.0550 -0.0036 66  SER   A CB  
468  O OG  . SER   A 60  ? 0.4063 0.3485 0.2842 -0.0175 -0.0479 -0.0109 66  SER   A OG  
469  N N   . SER   A 61  ? 0.2964 0.2292 0.1397 -0.0242 -0.0358 -0.0111 67  SER   A N   
470  C CA  . SER   A 61  ? 0.3179 0.2401 0.1358 -0.0306 -0.0300 -0.0144 67  SER   A CA  
471  C C   . SER   A 61  ? 0.3280 0.2499 0.1372 -0.0337 -0.0277 -0.0103 67  SER   A C   
472  O O   . SER   A 61  ? 0.3602 0.2725 0.1459 -0.0405 -0.0233 -0.0121 67  SER   A O   
473  C CB  . SER   A 61  ? 0.3231 0.2437 0.1396 -0.0278 -0.0167 -0.0228 67  SER   A CB  
474  O OG  . SER   A 61  ? 0.3353 0.2669 0.1685 -0.0215 -0.0073 -0.0227 67  SER   A OG  
475  N N   . ARG   A 62  ? 0.3050 0.2356 0.1311 -0.0297 -0.0305 -0.0048 68  ARG   A N   
476  C CA  . ARG   A 62  ? 0.3014 0.2310 0.1208 -0.0330 -0.0305 0.0004  68  ARG   A CA  
477  C C   . ARG   A 62  ? 0.3162 0.2460 0.1450 -0.0332 -0.0429 0.0087  68  ARG   A C   
478  O O   . ARG   A 62  ? 0.3370 0.2649 0.1621 -0.0358 -0.0444 0.0140  68  ARG   A O   
479  C CB  . ARG   A 62  ? 0.3057 0.2444 0.1368 -0.0287 -0.0202 -0.0008 68  ARG   A CB  
480  C CG  . ARG   A 62  ? 0.3419 0.2820 0.1690 -0.0277 -0.0070 -0.0073 68  ARG   A CG  
481  C CD  . ARG   A 62  ? 0.3556 0.2875 0.1597 -0.0348 -0.0011 -0.0075 68  ARG   A CD  
482  N NE  . ARG   A 62  ? 0.3638 0.2968 0.1668 -0.0333 0.0139  -0.0137 68  ARG   A NE  
483  C CZ  . ARG   A 62  ? 0.3930 0.3167 0.1830 -0.0349 0.0200  -0.0205 68  ARG   A CZ  
484  N NH1 . ARG   A 62  ? 0.3908 0.3039 0.1666 -0.0390 0.0108  -0.0220 68  ARG   A NH1 
485  N NH2 . ARG   A 62  ? 0.3885 0.3128 0.1806 -0.0328 0.0356  -0.0258 68  ARG   A NH2 
486  N N   . ARG   A 63  ? 0.2975 0.2296 0.1410 -0.0300 -0.0509 0.0103  69  ARG   A N   
487  C CA  . ARG   A 63  ? 0.3077 0.2417 0.1682 -0.0279 -0.0603 0.0179  69  ARG   A CA  
488  C C   . ARG   A 63  ? 0.3032 0.2409 0.1750 -0.0240 -0.0544 0.0191  69  ARG   A C   
489  O O   . ARG   A 63  ? 0.3208 0.2549 0.1947 -0.0255 -0.0593 0.0259  69  ARG   A O   
490  C CB  . ARG   A 63  ? 0.3392 0.2653 0.1888 -0.0352 -0.0730 0.0268  69  ARG   A CB  
491  C CG  . ARG   A 63  ? 0.4038 0.3263 0.2460 -0.0401 -0.0821 0.0275  69  ARG   A CG  
492  C CD  . ARG   A 63  ? 0.4753 0.3913 0.3096 -0.0482 -0.0970 0.0387  69  ARG   A CD  
493  N NE  . ARG   A 63  ? 0.5207 0.4301 0.3379 -0.0570 -0.1061 0.0394  69  ARG   A NE  
494  C CZ  . ARG   A 63  ? 0.5303 0.4281 0.3165 -0.0690 -0.1114 0.0417  69  ARG   A CZ  
495  N NH1 . ARG   A 63  ? 0.5282 0.4209 0.2984 -0.0730 -0.1077 0.0437  69  ARG   A NH1 
496  N NH2 . ARG   A 63  ? 0.4948 0.3850 0.2635 -0.0781 -0.1196 0.0413  69  ARG   A NH2 
497  N N   . LYS   A 64  ? 0.2781 0.2222 0.1558 -0.0200 -0.0443 0.0129  70  LYS   A N   
498  C CA  . LYS   A 64  ? 0.2767 0.2231 0.1611 -0.0185 -0.0390 0.0137  70  LYS   A CA  
499  C C   . LYS   A 64  ? 0.2631 0.2168 0.1620 -0.0137 -0.0331 0.0090  70  LYS   A C   
500  O O   . LYS   A 64  ? 0.2491 0.2072 0.1497 -0.0119 -0.0306 0.0046  70  LYS   A O   
501  C CB  . LYS   A 64  ? 0.3268 0.2735 0.1971 -0.0224 -0.0319 0.0126  70  LYS   A CB  
502  C CG  . LYS   A 64  ? 0.4290 0.3680 0.2832 -0.0286 -0.0354 0.0180  70  LYS   A CG  
503  C CD  . LYS   A 64  ? 0.5011 0.4426 0.3456 -0.0318 -0.0261 0.0165  70  LYS   A CD  
504  C CE  . LYS   A 64  ? 0.6059 0.5402 0.4349 -0.0386 -0.0285 0.0224  70  LYS   A CE  
505  N NZ  . LYS   A 64  ? 0.6813 0.6070 0.4920 -0.0440 -0.0348 0.0243  70  LYS   A NZ  
506  N N   . HIS   A 65  ? 0.2632 0.2167 0.1700 -0.0130 -0.0306 0.0099  71  HIS   A N   
507  C CA  . HIS   A 65  ? 0.2546 0.2136 0.1702 -0.0112 -0.0248 0.0060  71  HIS   A CA  
508  C C   . HIS   A 65  ? 0.2662 0.2286 0.1753 -0.0147 -0.0195 0.0059  71  HIS   A C   
509  O O   . HIS   A 65  ? 0.2858 0.2440 0.1877 -0.0181 -0.0197 0.0093  71  HIS   A O   
510  C CB  . HIS   A 65  ? 0.2635 0.2177 0.1896 -0.0096 -0.0244 0.0064  71  HIS   A CB  
511  C CG  . HIS   A 65  ? 0.2628 0.2155 0.2009 -0.0056 -0.0284 0.0073  71  HIS   A CG  
512  N ND1 . HIS   A 65  ? 0.2859 0.2428 0.2340 -0.0027 -0.0258 0.0036  71  HIS   A ND1 
513  C CD2 . HIS   A 65  ? 0.2514 0.1994 0.1946 -0.0044 -0.0350 0.0127  71  HIS   A CD2 
514  C CE1 . HIS   A 65  ? 0.2526 0.2081 0.2125 0.0004  -0.0303 0.0065  71  HIS   A CE1 
515  N NE2 . HIS   A 65  ? 0.2740 0.2246 0.2323 -0.0005 -0.0364 0.0124  71  HIS   A NE2 
516  N N   . TYR   A 66  ? 0.2310 0.2013 0.1441 -0.0144 -0.0153 0.0033  72  TYR   A N   
517  C CA  . TYR   A 66  ? 0.2260 0.2019 0.1373 -0.0181 -0.0110 0.0048  72  TYR   A CA  
518  C C   . TYR   A 66  ? 0.2196 0.1997 0.1378 -0.0202 -0.0096 0.0043  72  TYR   A C   
519  O O   . TYR   A 66  ? 0.2011 0.1842 0.1256 -0.0180 -0.0099 0.0020  72  TYR   A O   
520  C CB  . TYR   A 66  ? 0.2291 0.2120 0.1405 -0.0168 -0.0070 0.0039  72  TYR   A CB  
521  C CG  . TYR   A 66  ? 0.2545 0.2326 0.1544 -0.0172 -0.0063 0.0037  72  TYR   A CG  
522  C CD1 . TYR   A 66  ? 0.2825 0.2587 0.1734 -0.0213 -0.0040 0.0068  72  TYR   A CD1 
523  C CD2 . TYR   A 66  ? 0.2799 0.2545 0.1757 -0.0148 -0.0076 0.0006  72  TYR   A CD2 
524  C CE1 . TYR   A 66  ? 0.3010 0.2713 0.1777 -0.0234 -0.0028 0.0067  72  TYR   A CE1 
525  C CE2 . TYR   A 66  ? 0.2984 0.2665 0.1793 -0.0172 -0.0066 0.0000  72  TYR   A CE2 
526  C CZ  . TYR   A 66  ? 0.3143 0.2800 0.1849 -0.0217 -0.0041 0.0030  72  TYR   A CZ  
527  O OH  . TYR   A 66  ? 0.3493 0.3071 0.2016 -0.0257 -0.0027 0.0025  72  TYR   A OH  
528  N N   . PRO   A 67  ? 0.2246 0.2046 0.1401 -0.0257 -0.0085 0.0069  73  PRO   A N   
529  C CA  . PRO   A 67  ? 0.2225 0.2057 0.1409 -0.0305 -0.0082 0.0072  73  PRO   A CA  
530  C C   . PRO   A 67  ? 0.2272 0.2240 0.1537 -0.0311 -0.0072 0.0102  73  PRO   A C   
531  O O   . PRO   A 67  ? 0.2583 0.2609 0.1866 -0.0308 -0.0048 0.0130  73  PRO   A O   
532  C CB  . PRO   A 67  ? 0.2430 0.2200 0.1543 -0.0371 -0.0082 0.0096  73  PRO   A CB  
533  C CG  . PRO   A 67  ? 0.2518 0.2298 0.1598 -0.0361 -0.0076 0.0126  73  PRO   A CG  
534  C CD  . PRO   A 67  ? 0.2339 0.2100 0.1420 -0.0292 -0.0082 0.0103  73  PRO   A CD  
535  N N   . VAL   A 68  ? 0.2070 0.2088 0.1395 -0.0318 -0.0084 0.0100  74  VAL   A N   
536  C CA  . VAL   A 68  ? 0.2095 0.2244 0.1536 -0.0317 -0.0081 0.0142  74  VAL   A CA  
537  C C   . VAL   A 68  ? 0.2111 0.2308 0.1581 -0.0390 -0.0118 0.0180  74  VAL   A C   
538  O O   . VAL   A 68  ? 0.2094 0.2217 0.1488 -0.0423 -0.0134 0.0149  74  VAL   A O   
539  C CB  . VAL   A 68  ? 0.2205 0.2380 0.1718 -0.0239 -0.0066 0.0114  74  VAL   A CB  
540  C CG1 . VAL   A 68  ? 0.2423 0.2577 0.1913 -0.0186 -0.0026 0.0092  74  VAL   A CG1 
541  C CG2 . VAL   A 68  ? 0.2236 0.2347 0.1722 -0.0220 -0.0088 0.0068  74  VAL   A CG2 
542  N N   . SER   A 69  ? 0.2056 0.2380 0.1646 -0.0417 -0.0129 0.0252  75  SER   A N   
543  C CA  . SER   A 69  ? 0.2069 0.2467 0.1719 -0.0486 -0.0183 0.0311  75  SER   A CA  
544  C C   . SER   A 69  ? 0.1879 0.2346 0.1669 -0.0414 -0.0177 0.0317  75  SER   A C   
545  O O   . SER   A 69  ? 0.1934 0.2441 0.1823 -0.0334 -0.0128 0.0310  75  SER   A O   
546  C CB  . SER   A 69  ? 0.2408 0.2927 0.2163 -0.0553 -0.0209 0.0409  75  SER   A CB  
547  O OG  . SER   A 69  ? 0.3412 0.3867 0.3034 -0.0644 -0.0230 0.0415  75  SER   A OG  
548  N N   . PHE   A 70  ? 0.1756 0.2220 0.1538 -0.0446 -0.0220 0.0325  76  PHE   A N   
549  C CA  . PHE   A 70  ? 0.1685 0.2199 0.1597 -0.0381 -0.0218 0.0332  76  PHE   A CA  
550  C C   . PHE   A 70  ? 0.1858 0.2451 0.1848 -0.0453 -0.0289 0.0418  76  PHE   A C   
551  O O   . PHE   A 70  ? 0.2086 0.2648 0.1953 -0.0560 -0.0338 0.0439  76  PHE   A O   
552  C CB  . PHE   A 70  ? 0.1683 0.2092 0.1508 -0.0320 -0.0191 0.0240  76  PHE   A CB  
553  C CG  . PHE   A 70  ? 0.1849 0.2154 0.1510 -0.0379 -0.0205 0.0194  76  PHE   A CG  
554  C CD1 . PHE   A 70  ? 0.1957 0.2159 0.1493 -0.0381 -0.0175 0.0137  76  PHE   A CD1 
555  C CD2 . PHE   A 70  ? 0.1978 0.2282 0.1617 -0.0431 -0.0237 0.0209  76  PHE   A CD2 
556  C CE1 . PHE   A 70  ? 0.2129 0.2226 0.1536 -0.0431 -0.0164 0.0092  76  PHE   A CE1 
557  C CE2 . PHE   A 70  ? 0.2161 0.2359 0.1646 -0.0487 -0.0223 0.0158  76  PHE   A CE2 
558  C CZ  . PHE   A 70  ? 0.2094 0.2187 0.1472 -0.0484 -0.0180 0.0097  76  PHE   A CZ  
559  N N   . SER   A 71  ? 0.1848 0.2529 0.2030 -0.0400 -0.0293 0.0468  77  SER   A N   
560  C CA  . SER   A 71  ? 0.1895 0.2663 0.2184 -0.0466 -0.0372 0.0572  77  SER   A CA  
561  C C   . SER   A 71  ? 0.1948 0.2634 0.2096 -0.0511 -0.0407 0.0537  77  SER   A C   
562  O O   . SER   A 71  ? 0.2020 0.2602 0.2050 -0.0461 -0.0357 0.0434  77  SER   A O   
563  C CB  . SER   A 71  ? 0.1994 0.2872 0.2564 -0.0382 -0.0353 0.0638  77  SER   A CB  
564  O OG  . SER   A 71  ? 0.2077 0.2881 0.2650 -0.0282 -0.0295 0.0554  77  SER   A OG  
565  N N   . LYS   A 72  ? 0.1944 0.2676 0.2093 -0.0617 -0.0495 0.0629  78  LYS   A N   
566  C CA  . LYS   A 72  ? 0.2124 0.2779 0.2136 -0.0665 -0.0515 0.0600  78  LYS   A CA  
567  C C   . LYS   A 72  ? 0.2153 0.2821 0.2313 -0.0557 -0.0491 0.0585  78  LYS   A C   
568  O O   . LYS   A 72  ? 0.2221 0.2973 0.2607 -0.0478 -0.0484 0.0635  78  LYS   A O   
569  C CB  . LYS   A 72  ? 0.2516 0.3205 0.2459 -0.0827 -0.0621 0.0709  78  LYS   A CB  
570  C CG  . LYS   A 72  ? 0.3037 0.3674 0.2782 -0.0953 -0.0643 0.0707  78  LYS   A CG  
571  C CD  . LYS   A 72  ? 0.3613 0.4251 0.3226 -0.1140 -0.0751 0.0805  78  LYS   A CD  
572  C CE  . LYS   A 72  ? 0.4390 0.4947 0.3779 -0.1270 -0.0764 0.0787  78  LYS   A CE  
573  N NZ  . LYS   A 72  ? 0.4952 0.5498 0.4179 -0.1477 -0.0880 0.0887  78  LYS   A NZ  
574  N N   . PRO   A 73  ? 0.2207 0.2791 0.2252 -0.0558 -0.0474 0.0521  79  PRO   A N   
575  C CA  . PRO   A 73  ? 0.2235 0.2821 0.2410 -0.0465 -0.0456 0.0506  79  PRO   A CA  
576  C C   . PRO   A 73  ? 0.2186 0.2872 0.2572 -0.0473 -0.0523 0.0632  79  PRO   A C   
577  O O   . PRO   A 73  ? 0.2040 0.2775 0.2410 -0.0587 -0.0609 0.0735  79  PRO   A O   
578  C CB  . PRO   A 73  ? 0.2544 0.3038 0.2551 -0.0505 -0.0441 0.0441  79  PRO   A CB  
579  C CG  . PRO   A 73  ? 0.2723 0.3137 0.2522 -0.0561 -0.0403 0.0373  79  PRO   A CG  
580  C CD  . PRO   A 73  ? 0.2349 0.2824 0.2149 -0.0643 -0.0458 0.0456  79  PRO   A CD  
581  N N   . SER   A 74  ? 0.2132 0.2847 0.2720 -0.0358 -0.0484 0.0631  80  SER   A N   
582  C CA  . SER   A 74  ? 0.2174 0.2983 0.3019 -0.0343 -0.0533 0.0755  80  SER   A CA  
583  C C   . SER   A 74  ? 0.2172 0.2940 0.3173 -0.0217 -0.0470 0.0712  80  SER   A C   
584  O O   . SER   A 74  ? 0.2208 0.2879 0.3096 -0.0153 -0.0399 0.0587  80  SER   A O   
585  C CB  . SER   A 74  ? 0.2642 0.3571 0.3652 -0.0363 -0.0558 0.0858  80  SER   A CB  
586  O OG  . SER   A 74  ? 0.3262 0.4194 0.4360 -0.0260 -0.0461 0.0799  80  SER   A OG  
587  N N   . LEU   A 75  ? 0.1989 0.2823 0.3248 -0.0189 -0.0502 0.0821  81  LEU   A N   
588  C CA  . LEU   A 75  ? 0.2011 0.2797 0.3445 -0.0080 -0.0442 0.0796  81  LEU   A CA  
589  C C   . LEU   A 75  ? 0.2061 0.2873 0.3662 0.0013  -0.0345 0.0779  81  LEU   A C   
590  O O   . LEU   A 75  ? 0.1978 0.2913 0.3801 0.0006  -0.0367 0.0897  81  LEU   A O   
591  C CB  . LEU   A 75  ? 0.2085 0.2935 0.3752 -0.0101 -0.0523 0.0943  81  LEU   A CB  
592  C CG  . LEU   A 75  ? 0.2556 0.3331 0.4181 -0.0116 -0.0562 0.0939  81  LEU   A CG  
593  C CD1 . LEU   A 75  ? 0.2638 0.3476 0.4571 -0.0104 -0.0622 0.1094  81  LEU   A CD1 
594  C CD2 . LEU   A 75  ? 0.2727 0.3361 0.4259 -0.0026 -0.0466 0.0786  81  LEU   A CD2 
595  N N   . ILE   A 76  ? 0.2098 0.2801 0.3584 0.0088  -0.0241 0.0638  82  ILE   A N   
596  C CA  . ILE   A 76  ? 0.2227 0.2930 0.3810 0.0165  -0.0130 0.0601  82  ILE   A CA  
597  C C   . ILE   A 76  ? 0.2401 0.2977 0.4034 0.0260  -0.0029 0.0516  82  ILE   A C   
598  O O   . ILE   A 76  ? 0.2313 0.2770 0.3768 0.0260  -0.0034 0.0425  82  ILE   A O   
599  C CB  . ILE   A 76  ? 0.2517 0.3190 0.3853 0.0139  -0.0100 0.0511  82  ILE   A CB  
600  C CG1 . ILE   A 76  ? 0.2633 0.3418 0.3933 0.0044  -0.0182 0.0594  82  ILE   A CG1 
601  C CG2 . ILE   A 76  ? 0.2678 0.3300 0.4022 0.0213  0.0031  0.0432  82  ILE   A CG2 
602  C CD1 . ILE   A 76  ? 0.3043 0.3764 0.4073 0.0006  -0.0179 0.0504  82  ILE   A CD1 
603  N N   . PHE   A 77  ? 0.2483 0.3077 0.4361 0.0336  0.0068  0.0544  83  PHE   A N   
604  C CA  . PHE   A 77  ? 0.2760 0.3205 0.4676 0.0423  0.0186  0.0452  83  PHE   A CA  
605  C C   . PHE   A 77  ? 0.2833 0.3146 0.4461 0.0432  0.0276  0.0295  83  PHE   A C   
606  O O   . PHE   A 77  ? 0.2944 0.3303 0.4505 0.0421  0.0316  0.0281  83  PHE   A O   
607  C CB  . PHE   A 77  ? 0.2824 0.3320 0.5105 0.0504  0.0287  0.0528  83  PHE   A CB  
608  C CG  . PHE   A 77  ? 0.3175 0.3497 0.5520 0.0586  0.0406  0.0445  83  PHE   A CG  
609  C CD1 . PHE   A 77  ? 0.3465 0.3733 0.5910 0.0596  0.0349  0.0482  83  PHE   A CD1 
610  C CD2 . PHE   A 77  ? 0.3502 0.3694 0.5765 0.0641  0.0576  0.0320  83  PHE   A CD2 
611  C CE1 . PHE   A 77  ? 0.3726 0.3811 0.6218 0.0665  0.0462  0.0400  83  PHE   A CE1 
612  C CE2 . PHE   A 77  ? 0.3723 0.3725 0.6011 0.0704  0.0695  0.0231  83  PHE   A CE2 
613  C CZ  . PHE   A 77  ? 0.3755 0.3701 0.6163 0.0718  0.0637  0.0271  83  PHE   A CZ  
614  N N   . VAL   A 78  ? 0.2776 0.2923 0.4227 0.0441  0.0293  0.0189  84  VAL   A N   
615  C CA  . VAL   A 78  ? 0.2960 0.2970 0.4119 0.0431  0.0350  0.0052  84  VAL   A CA  
616  C C   . VAL   A 78  ? 0.3173 0.3000 0.4324 0.0485  0.0477  -0.0042 84  VAL   A C   
617  O O   . VAL   A 78  ? 0.3264 0.3011 0.4482 0.0502  0.0460  -0.0045 84  VAL   A O   
618  C CB  . VAL   A 78  ? 0.3044 0.3021 0.3960 0.0366  0.0233  0.0013  84  VAL   A CB  
619  C CG1 . VAL   A 78  ? 0.3200 0.3027 0.3837 0.0351  0.0273  -0.0112 84  VAL   A CG1 
620  C CG2 . VAL   A 78  ? 0.2941 0.3066 0.3830 0.0309  0.0139  0.0084  84  VAL   A CG2 
621  N N   . GLU   A 79  ? 0.3305 0.3051 0.4360 0.0505  0.0608  -0.0121 85  GLU   A N   
622  C CA  . GLU   A 79  ? 0.3516 0.3054 0.4510 0.0542  0.0753  -0.0230 85  GLU   A CA  
623  C C   . GLU   A 79  ? 0.3676 0.3041 0.4425 0.0499  0.0695  -0.0320 85  GLU   A C   
624  O O   . GLU   A 79  ? 0.3617 0.3008 0.4168 0.0436  0.0569  -0.0327 85  GLU   A O   
625  C CB  . GLU   A 79  ? 0.4007 0.3473 0.4828 0.0535  0.0887  -0.0314 85  GLU   A CB  
626  C CG  . GLU   A 79  ? 0.4747 0.4369 0.5822 0.0580  0.0976  -0.0235 85  GLU   A CG  
627  C CD  . GLU   A 79  ? 0.5709 0.5359 0.7167 0.0667  0.1077  -0.0174 85  GLU   A CD  
628  O OE1 . GLU   A 79  ? 0.6085 0.5543 0.7533 0.0709  0.1223  -0.0266 85  GLU   A OE1 
629  O OE2 . GLU   A 79  ? 0.5859 0.5712 0.7626 0.0688  0.1007  -0.0031 85  GLU   A OE2 
630  N N   . ALA   A 80  ? 0.3847 0.3031 0.4621 0.0531  0.0790  -0.0386 86  ALA   A N   
631  C CA  . ALA   A 80  ? 0.4101 0.3092 0.4641 0.0483  0.0747  -0.0477 86  ALA   A CA  
632  C C   . ALA   A 80  ? 0.4371 0.3259 0.4532 0.0404  0.0731  -0.0573 86  ALA   A C   
633  O O   . ALA   A 80  ? 0.4475 0.3351 0.4533 0.0400  0.0825  -0.0610 86  ALA   A O   
634  C CB  . ALA   A 80  ? 0.4209 0.2989 0.4813 0.0528  0.0893  -0.0550 86  ALA   A CB  
635  N N   . SER   A 81  ? 0.4473 0.3297 0.4440 0.0337  0.0607  -0.0601 87  SER   A N   
636  C CA  . SER   A 81  ? 0.4718 0.3432 0.4337 0.0250  0.0562  -0.0676 87  SER   A CA  
637  C C   . SER   A 81  ? 0.5039 0.3565 0.4510 0.0195  0.0510  -0.0740 87  SER   A C   
638  O O   . SER   A 81  ? 0.5064 0.3530 0.4695 0.0234  0.0543  -0.0738 87  SER   A O   
639  C CB  . SER   A 81  ? 0.4689 0.3586 0.4276 0.0216  0.0420  -0.0605 87  SER   A CB  
640  O OG  . SER   A 81  ? 0.4615 0.3597 0.4302 0.0205  0.0287  -0.0547 87  SER   A OG  
641  N N   . GLU   A 82  ? 0.5274 0.3707 0.4454 0.0099  0.0423  -0.0785 88  GLU   A N   
642  C CA  . GLU   A 82  ? 0.5460 0.3733 0.4509 0.0033  0.0353  -0.0831 88  GLU   A CA  
643  C C   . GLU   A 82  ? 0.5203 0.3633 0.4429 0.0034  0.0198  -0.0740 88  GLU   A C   
644  O O   . GLU   A 82  ? 0.5264 0.3592 0.4459 -0.0007 0.0142  -0.0758 88  GLU   A O   
645  C CB  . GLU   A 82  ? 0.6226 0.4321 0.4899 -0.0084 0.0317  -0.0907 88  GLU   A CB  
646  C CG  . GLU   A 82  ? 0.7140 0.5369 0.5727 -0.0145 0.0151  -0.0843 88  GLU   A CG  
647  C CD  . GLU   A 82  ? 0.8497 0.6543 0.6721 -0.0274 0.0098  -0.0901 88  GLU   A CD  
648  O OE1 . GLU   A 82  ? 0.8630 0.6725 0.6800 -0.0344 -0.0066 -0.0850 88  GLU   A OE1 
649  O OE2 . GLU   A 82  ? 0.8952 0.6801 0.6946 -0.0310 0.0223  -0.0994 88  GLU   A OE2 
650  N N   . TYR   A 83  ? 0.4851 0.3520 0.4258 0.0076  0.0138  -0.0645 89  TYR   A N   
651  C CA  . TYR   A 83  ? 0.4685 0.3497 0.4247 0.0072  0.0015  -0.0565 89  TYR   A CA  
652  C C   . TYR   A 83  ? 0.4456 0.3359 0.4294 0.0140  0.0042  -0.0500 89  TYR   A C   
653  O O   . TYR   A 83  ? 0.4529 0.3478 0.4470 0.0126  -0.0036 -0.0453 89  TYR   A O   
654  C CB  . TYR   A 83  ? 0.4605 0.3594 0.4166 0.0056  -0.0072 -0.0505 89  TYR   A CB  
655  C CG  . TYR   A 83  ? 0.4881 0.3798 0.4199 -0.0012 -0.0118 -0.0544 89  TYR   A CG  
656  C CD1 . TYR   A 83  ? 0.5116 0.3983 0.4335 -0.0086 -0.0229 -0.0545 89  TYR   A CD1 
657  C CD2 . TYR   A 83  ? 0.5092 0.4001 0.4291 -0.0011 -0.0060 -0.0566 89  TYR   A CD2 
658  C CE1 . TYR   A 83  ? 0.5363 0.4173 0.4374 -0.0159 -0.0292 -0.0560 89  TYR   A CE1 
659  C CE2 . TYR   A 83  ? 0.5361 0.4205 0.4334 -0.0083 -0.0116 -0.0586 89  TYR   A CE2 
660  C CZ  . TYR   A 83  ? 0.5616 0.4410 0.4497 -0.0158 -0.0236 -0.0580 89  TYR   A CZ  
661  O OH  . TYR   A 83  ? 0.6050 0.4786 0.4719 -0.0237 -0.0306 -0.0582 89  TYR   A OH  
662  N N   . TYR   A 84  ? 0.4137 0.3072 0.4107 0.0207  0.0149  -0.0486 90  TYR   A N   
663  C CA  . TYR   A 84  ? 0.3873 0.2904 0.4124 0.0266  0.0162  -0.0404 90  TYR   A CA  
664  C C   . TYR   A 84  ? 0.3919 0.2862 0.4292 0.0334  0.0311  -0.0429 90  TYR   A C   
665  O O   . TYR   A 84  ? 0.3924 0.2834 0.4211 0.0348  0.0408  -0.0478 90  TYR   A O   
666  C CB  . TYR   A 84  ? 0.3535 0.2797 0.3909 0.0277  0.0109  -0.0306 90  TYR   A CB  
667  C CG  . TYR   A 84  ? 0.3267 0.2634 0.3560 0.0221  -0.0011 -0.0274 90  TYR   A CG  
668  C CD1 . TYR   A 84  ? 0.3231 0.2655 0.3389 0.0197  -0.0032 -0.0289 90  TYR   A CD1 
669  C CD2 . TYR   A 84  ? 0.3176 0.2593 0.3554 0.0196  -0.0094 -0.0221 90  TYR   A CD2 
670  C CE1 . TYR   A 84  ? 0.3107 0.2627 0.3229 0.0156  -0.0123 -0.0257 90  TYR   A CE1 
671  C CE2 . TYR   A 84  ? 0.3074 0.2590 0.3402 0.0150  -0.0179 -0.0193 90  TYR   A CE2 
672  C CZ  . TYR   A 84  ? 0.3023 0.2588 0.3232 0.0134  -0.0189 -0.0213 90  TYR   A CZ  
673  O OH  . TYR   A 84  ? 0.2645 0.2298 0.2830 0.0097  -0.0256 -0.0188 90  TYR   A OH  
674  N N   . PRO   A 85  ? 0.3877 0.2805 0.4485 0.0381  0.0336  -0.0379 91  PRO   A N   
675  C CA  . PRO   A 85  ? 0.3890 0.2777 0.4698 0.0463  0.0484  -0.0376 91  PRO   A CA  
676  C C   . PRO   A 85  ? 0.3889 0.3009 0.4882 0.0497  0.0478  -0.0273 91  PRO   A C   
677  O O   . PRO   A 85  ? 0.3906 0.3190 0.4860 0.0455  0.0360  -0.0211 91  PRO   A O   
678  C CB  . PRO   A 85  ? 0.3911 0.2747 0.4954 0.0498  0.0476  -0.0321 91  PRO   A CB  
679  C CG  . PRO   A 85  ? 0.3904 0.2850 0.4933 0.0440  0.0306  -0.0249 91  PRO   A CG  
680  C CD  . PRO   A 85  ? 0.3750 0.2721 0.4487 0.0365  0.0229  -0.0305 91  PRO   A CD  
681  N N   . ALA   A 86  ? 0.3784 0.2921 0.4999 0.0571  0.0606  -0.0247 92  ALA   A N   
682  C CA  . ALA   A 86  ? 0.3623 0.2984 0.5047 0.0597  0.0596  -0.0135 92  ALA   A CA  
683  C C   . ALA   A 86  ? 0.3442 0.2971 0.5068 0.0580  0.0447  0.0012  92  ALA   A C   
684  O O   . ALA   A 86  ? 0.3609 0.3080 0.5385 0.0600  0.0427  0.0050  92  ALA   A O   
685  C CB  . ALA   A 86  ? 0.3523 0.2862 0.5204 0.0684  0.0767  -0.0124 92  ALA   A CB  
686  N N   . ARG   A 87  ? 0.3166 0.2872 0.4741 0.0527  0.0336  0.0081  93  ARG   A N   
687  C CA  . ARG   A 87  ? 0.2849 0.2692 0.4546 0.0485  0.0194  0.0209  93  ARG   A CA  
688  C C   . ARG   A 87  ? 0.2668 0.2707 0.4374 0.0438  0.0119  0.0297  93  ARG   A C   
689  O O   . ARG   A 87  ? 0.2808 0.2873 0.4409 0.0438  0.0169  0.0251  93  ARG   A O   
690  C CB  . ARG   A 87  ? 0.3002 0.2764 0.4481 0.0426  0.0105  0.0155  93  ARG   A CB  
691  C CG  . ARG   A 87  ? 0.3081 0.2889 0.4292 0.0362  0.0048  0.0104  93  ARG   A CG  
692  C CD  . ARG   A 87  ? 0.3207 0.2890 0.4198 0.0326  0.0018  0.0010  93  ARG   A CD  
693  N NE  . ARG   A 87  ? 0.3224 0.2988 0.4057 0.0262  -0.0070 0.0012  93  ARG   A NE  
694  C CZ  . ARG   A 87  ? 0.3415 0.3209 0.4097 0.0245  -0.0063 -0.0030 93  ARG   A CZ  
695  N NH1 . ARG   A 87  ? 0.3177 0.3025 0.3744 0.0194  -0.0133 -0.0028 93  ARG   A NH1 
696  N NH2 . ARG   A 87  ? 0.3465 0.3227 0.4112 0.0279  0.0020  -0.0072 93  ARG   A NH2 
697  N N   . TYR   A 88  ? 0.2514 0.2675 0.4316 0.0384  -0.0004 0.0420  94  TYR   A N   
698  C CA  . TYR   A 88  ? 0.2418 0.2731 0.4159 0.0313  -0.0087 0.0489  94  TYR   A CA  
699  C C   . TYR   A 88  ? 0.2178 0.2449 0.3623 0.0245  -0.0148 0.0415  94  TYR   A C   
700  O O   . TYR   A 88  ? 0.2235 0.2455 0.3634 0.0218  -0.0200 0.0412  94  TYR   A O   
701  C CB  . TYR   A 88  ? 0.2496 0.2948 0.4446 0.0265  -0.0193 0.0660  94  TYR   A CB  
702  C CG  . TYR   A 88  ? 0.2663 0.3207 0.4950 0.0322  -0.0153 0.0769  94  TYR   A CG  
703  C CD1 . TYR   A 88  ? 0.2845 0.3516 0.5193 0.0308  -0.0144 0.0819  94  TYR   A CD1 
704  C CD2 . TYR   A 88  ? 0.2810 0.3309 0.5373 0.0395  -0.0112 0.0819  94  TYR   A CD2 
705  C CE1 . TYR   A 88  ? 0.2932 0.3705 0.5628 0.0362  -0.0102 0.0928  94  TYR   A CE1 
706  C CE2 . TYR   A 88  ? 0.2854 0.3445 0.5775 0.0457  -0.0063 0.0927  94  TYR   A CE2 
707  C CZ  . TYR   A 88  ? 0.3008 0.3742 0.6001 0.0442  -0.0055 0.0980  94  TYR   A CZ  
708  O OH  . TYR   A 88  ? 0.3257 0.4101 0.6639 0.0503  -0.0004 0.1098  94  TYR   A OH  
709  N N   . GLN   A 89  ? 0.1984 0.2285 0.3255 0.0216  -0.0142 0.0367  95  GLN   A N   
710  C CA  . GLN   A 89  ? 0.1838 0.2117 0.2867 0.0155  -0.0190 0.0309  95  GLN   A CA  
711  C C   . GLN   A 89  ? 0.1696 0.2093 0.2701 0.0071  -0.0269 0.0397  95  GLN   A C   
712  O O   . GLN   A 89  ? 0.1609 0.2094 0.2681 0.0058  -0.0269 0.0454  95  GLN   A O   
713  C CB  . GLN   A 89  ? 0.1943 0.2147 0.2785 0.0178  -0.0129 0.0192  95  GLN   A CB  
714  C CG  . GLN   A 89  ? 0.2074 0.2260 0.2710 0.0125  -0.0175 0.0142  95  GLN   A CG  
715  C CD  . GLN   A 89  ? 0.2295 0.2389 0.2766 0.0146  -0.0135 0.0039  95  GLN   A CD  
716  O OE1 . GLN   A 89  ? 0.2355 0.2352 0.2807 0.0185  -0.0086 -0.0019 95  GLN   A OE1 
717  N NE2 . GLN   A 89  ? 0.1891 0.2003 0.2231 0.0110  -0.0159 0.0018  95  GLN   A NE2 
718  N N   . SER   A 90  ? 0.1560 0.1956 0.2469 0.0004  -0.0334 0.0412  96  SER   A N   
719  C CA  . SER   A 90  ? 0.1521 0.1995 0.2361 -0.0096 -0.0401 0.0484  96  SER   A CA  
720  C C   . SER   A 90  ? 0.1535 0.1981 0.2150 -0.0134 -0.0381 0.0402  96  SER   A C   
721  O O   . SER   A 90  ? 0.1549 0.1920 0.2069 -0.0089 -0.0334 0.0300  96  SER   A O   
722  C CB  . SER   A 90  ? 0.1773 0.2249 0.2620 -0.0160 -0.0469 0.0548  96  SER   A CB  
723  O OG  . SER   A 90  ? 0.2000 0.2396 0.2715 -0.0160 -0.0449 0.0460  96  SER   A OG  
724  N N   . HIS   A 91  ? 0.1545 0.2045 0.2080 -0.0225 -0.0422 0.0455  97  HIS   A N   
725  C CA  . HIS   A 91  ? 0.1595 0.2058 0.1927 -0.0273 -0.0401 0.0390  97  HIS   A CA  
726  C C   . HIS   A 91  ? 0.1612 0.2047 0.1919 -0.0201 -0.0339 0.0313  97  HIS   A C   
727  O O   . HIS   A 91  ? 0.1797 0.2169 0.1972 -0.0195 -0.0305 0.0232  97  HIS   A O   
728  C CB  . HIS   A 91  ? 0.1809 0.2204 0.2022 -0.0297 -0.0386 0.0330  97  HIS   A CB  
729  C CG  . HIS   A 91  ? 0.2150 0.2564 0.2348 -0.0386 -0.0440 0.0403  97  HIS   A CG  
730  N ND1 . HIS   A 91  ? 0.2450 0.2860 0.2490 -0.0507 -0.0460 0.0430  97  HIS   A ND1 
731  C CD2 . HIS   A 91  ? 0.2219 0.2646 0.2531 -0.0380 -0.0478 0.0458  97  HIS   A CD2 
732  C CE1 . HIS   A 91  ? 0.2467 0.2892 0.2517 -0.0575 -0.0513 0.0504  97  HIS   A CE1 
733  N NE2 . HIS   A 91  ? 0.2410 0.2850 0.2631 -0.0500 -0.0528 0.0527  97  HIS   A NE2 
734  N N   . LEU   A 92  ? 0.1448 0.1928 0.1888 -0.0149 -0.0321 0.0344  98  LEU   A N   
735  C CA  . LEU   A 92  ? 0.1540 0.1989 0.1947 -0.0089 -0.0258 0.0278  98  LEU   A CA  
736  C C   . LEU   A 92  ? 0.1605 0.2117 0.1994 -0.0136 -0.0265 0.0322  98  LEU   A C   
737  O O   . LEU   A 92  ? 0.1782 0.2386 0.2291 -0.0178 -0.0308 0.0423  98  LEU   A O   
738  C CB  . LEU   A 92  ? 0.1461 0.1907 0.2028 -0.0001 -0.0209 0.0276  98  LEU   A CB  
739  C CG  . LEU   A 92  ? 0.1813 0.2201 0.2324 0.0058  -0.0132 0.0199  98  LEU   A CG  
740  C CD1 . LEU   A 92  ? 0.1967 0.2256 0.2297 0.0062  -0.0128 0.0105  98  LEU   A CD1 
741  C CD2 . LEU   A 92  ? 0.1871 0.2236 0.2538 0.0132  -0.0066 0.0196  98  LEU   A CD2 
742  N N   . MET   A 93  ? 0.1514 0.1977 0.1773 -0.0129 -0.0228 0.0256  99  MET   A N   
743  C CA  . MET   A 93  ? 0.1498 0.2004 0.1726 -0.0174 -0.0230 0.0289  99  MET   A CA  
744  C C   . MET   A 93  ? 0.1722 0.2219 0.1979 -0.0106 -0.0163 0.0254  99  MET   A C   
745  O O   . MET   A 93  ? 0.1990 0.2401 0.2153 -0.0060 -0.0127 0.0172  99  MET   A O   
746  C CB  . MET   A 93  ? 0.1628 0.2062 0.1659 -0.0236 -0.0239 0.0241  99  MET   A CB  
747  C CG  . MET   A 93  ? 0.1876 0.2299 0.1839 -0.0320 -0.0286 0.0266  99  MET   A CG  
748  S SD  . MET   A 93  ? 0.2622 0.2927 0.2369 -0.0372 -0.0257 0.0185  99  MET   A SD  
749  C CE  . MET   A 93  ? 0.2248 0.2490 0.2017 -0.0262 -0.0210 0.0098  99  MET   A CE  
750  N N   . LEU   A 94  ? 0.1652 0.2237 0.2030 -0.0109 -0.0146 0.0318  100 LEU   A N   
751  C CA  . LEU   A 94  ? 0.1600 0.2168 0.1985 -0.0054 -0.0065 0.0280  100 LEU   A CA  
752  C C   . LEU   A 94  ? 0.1530 0.2110 0.1819 -0.0106 -0.0066 0.0289  100 LEU   A C   
753  O O   . LEU   A 94  ? 0.1538 0.2179 0.1835 -0.0184 -0.0122 0.0355  100 LEU   A O   
754  C CB  . LEU   A 94  ? 0.1742 0.2404 0.2371 -0.0007 -0.0014 0.0344  100 LEU   A CB  
755  C CG  . LEU   A 94  ? 0.2185 0.2832 0.2961 0.0058  0.0011  0.0343  100 LEU   A CG  
756  C CD1 . LEU   A 94  ? 0.2298 0.3031 0.3333 0.0110  0.0087  0.0405  100 LEU   A CD1 
757  C CD2 . LEU   A 94  ? 0.2323 0.2825 0.2945 0.0109  0.0058  0.0226  100 LEU   A CD2 
758  N N   . ALA   A 95  ? 0.1533 0.2047 0.1724 -0.0072 -0.0005 0.0227  101 ALA   A N   
759  C CA  . ALA   A 95  ? 0.1496 0.2011 0.1602 -0.0111 0.0007  0.0234  101 ALA   A CA  
760  C C   . ALA   A 95  ? 0.1707 0.2207 0.1822 -0.0062 0.0101  0.0206  101 ALA   A C   
761  O O   . ALA   A 95  ? 0.1845 0.2293 0.1969 -0.0002 0.0155  0.0156  101 ALA   A O   
762  C CB  . ALA   A 95  ? 0.1649 0.2053 0.1552 -0.0139 -0.0027 0.0177  101 ALA   A CB  
763  N N   . VAL   A 96  ? 0.1709 0.2252 0.1822 -0.0096 0.0127  0.0240  102 VAL   A N   
764  C CA  . VAL   A 96  ? 0.1804 0.2321 0.1883 -0.0068 0.0223  0.0212  102 VAL   A CA  
765  C C   . VAL   A 96  ? 0.2008 0.2381 0.1834 -0.0077 0.0209  0.0138  102 VAL   A C   
766  O O   . VAL   A 96  ? 0.2246 0.2586 0.1965 -0.0126 0.0152  0.0147  102 VAL   A O   
767  C CB  . VAL   A 96  ? 0.1814 0.2443 0.2002 -0.0108 0.0256  0.0288  102 VAL   A CB  
768  C CG1 . VAL   A 96  ? 0.1991 0.2581 0.2120 -0.0084 0.0371  0.0252  102 VAL   A CG1 
769  C CG2 . VAL   A 96  ? 0.1599 0.2386 0.2076 -0.0102 0.0253  0.0384  102 VAL   A CG2 
770  N N   . GLY   A 97  ? 0.2200 0.2480 0.1937 -0.0036 0.0256  0.0071  103 GLY   A N   
771  C CA  . GLY   A 97  ? 0.2381 0.2531 0.1896 -0.0051 0.0228  0.0018  103 GLY   A CA  
772  C C   . GLY   A 97  ? 0.2530 0.2577 0.1948 -0.0020 0.0270  -0.0051 103 GLY   A C   
773  O O   . GLY   A 97  ? 0.2641 0.2701 0.2160 0.0021  0.0330  -0.0069 103 GLY   A O   
774  N N   . HIS   A 98  ? 0.2502 0.2436 0.1720 -0.0046 0.0234  -0.0083 104 HIS   A N   
775  C CA  . HIS   A 98  ? 0.2635 0.2451 0.1711 -0.0043 0.0258  -0.0146 104 HIS   A CA  
776  C C   . HIS   A 98  ? 0.2581 0.2357 0.1669 -0.0023 0.0181  -0.0171 104 HIS   A C   
777  O O   . HIS   A 98  ? 0.2591 0.2378 0.1691 -0.0031 0.0088  -0.0148 104 HIS   A O   
778  C CB  . HIS   A 98  ? 0.2884 0.2596 0.1725 -0.0100 0.0243  -0.0152 104 HIS   A CB  
779  C CG  . HIS   A 98  ? 0.3379 0.2956 0.2037 -0.0120 0.0274  -0.0215 104 HIS   A CG  
780  N ND1 . HIS   A 98  ? 0.3578 0.3117 0.2216 -0.0108 0.0409  -0.0266 104 HIS   A ND1 
781  C CD2 . HIS   A 98  ? 0.3635 0.3105 0.2138 -0.0153 0.0186  -0.0234 104 HIS   A CD2 
782  C CE1 . HIS   A 98  ? 0.3746 0.3134 0.2175 -0.0145 0.0402  -0.0323 104 HIS   A CE1 
783  N NE2 . HIS   A 98  ? 0.3773 0.3124 0.2118 -0.0178 0.0259  -0.0300 104 HIS   A NE2 
784  N N   . SER   A 99  ? 0.2610 0.2326 0.1688 -0.0002 0.0224  -0.0221 105 SER   A N   
785  C CA  . SER   A 99  ? 0.2769 0.2445 0.1862 0.0012  0.0156  -0.0245 105 SER   A CA  
786  C C   . SER   A 99  ? 0.3309 0.2854 0.2278 0.0006  0.0214  -0.0315 105 SER   A C   
787  O O   . SER   A 99  ? 0.3615 0.3153 0.2641 0.0033  0.0329  -0.0342 105 SER   A O   
788  C CB  . SER   A 99  ? 0.2885 0.2671 0.2205 0.0056  0.0149  -0.0215 105 SER   A CB  
789  O OG  . SER   A 99  ? 0.3415 0.3172 0.2758 0.0065  0.0084  -0.0232 105 SER   A OG  
790  N N   . GLU   A 100 ? 0.3241 0.2681 0.2052 -0.0035 0.0138  -0.0341 106 GLU   A N   
791  C CA  . GLU   A 100 ? 0.3496 0.2784 0.2147 -0.0064 0.0170  -0.0411 106 GLU   A CA  
792  C C   . GLU   A 100 ? 0.3568 0.2852 0.2298 -0.0054 0.0078  -0.0413 106 GLU   A C   
793  O O   . GLU   A 100 ? 0.3599 0.2980 0.2447 -0.0041 -0.0015 -0.0360 106 GLU   A O   
794  C CB  . GLU   A 100 ? 0.3908 0.3067 0.2269 -0.0151 0.0135  -0.0425 106 GLU   A CB  
795  C CG  . GLU   A 100 ? 0.4354 0.3488 0.2603 -0.0172 0.0249  -0.0437 106 GLU   A CG  
796  C CD  . GLU   A 100 ? 0.4934 0.3944 0.2879 -0.0271 0.0212  -0.0438 106 GLU   A CD  
797  O OE1 . GLU   A 100 ? 0.5362 0.4231 0.3104 -0.0339 0.0156  -0.0471 106 GLU   A OE1 
798  O OE2 . GLU   A 100 ? 0.4845 0.3890 0.2743 -0.0291 0.0235  -0.0401 106 GLU   A OE2 
799  N N   . PRO   A 101 ? 0.3776 0.2945 0.2445 -0.0063 0.0107  -0.0472 107 PRO   A N   
800  C CA  . PRO   A 101 ? 0.3642 0.2821 0.2407 -0.0055 0.0018  -0.0465 107 PRO   A CA  
801  C C   . PRO   A 101 ? 0.3413 0.2637 0.2174 -0.0091 -0.0129 -0.0412 107 PRO   A C   
802  O O   . PRO   A 101 ? 0.3349 0.2674 0.2291 -0.0060 -0.0187 -0.0373 107 PRO   A O   
803  C CB  . PRO   A 101 ? 0.3890 0.2886 0.2495 -0.0092 0.0065  -0.0545 107 PRO   A CB  
804  C CG  . PRO   A 101 ? 0.4097 0.3033 0.2657 -0.0070 0.0225  -0.0595 107 PRO   A CG  
805  C CD  . PRO   A 101 ? 0.3857 0.2879 0.2387 -0.0076 0.0238  -0.0552 107 PRO   A CD  
806  N N   . GLY   A 102 ? 0.3361 0.2511 0.1926 -0.0159 -0.0185 -0.0404 108 GLY   A N   
807  C CA  . GLY   A 102 ? 0.3243 0.2435 0.1831 -0.0191 -0.0324 -0.0340 108 GLY   A CA  
808  C C   . GLY   A 102 ? 0.3068 0.2406 0.1841 -0.0143 -0.0348 -0.0276 108 GLY   A C   
809  O O   . GLY   A 102 ? 0.3185 0.2570 0.2040 -0.0152 -0.0446 -0.0221 108 GLY   A O   
810  N N   . ASP   A 103 ? 0.2728 0.2131 0.1567 -0.0097 -0.0256 -0.0279 109 ASP   A N   
811  C CA  . ASP   A 103 ? 0.2534 0.2055 0.1523 -0.0061 -0.0263 -0.0229 109 ASP   A CA  
812  C C   . ASP   A 103 ? 0.2406 0.2019 0.1598 -0.0018 -0.0275 -0.0217 109 ASP   A C   
813  O O   . ASP   A 103 ? 0.2443 0.2131 0.1744 -0.0001 -0.0289 -0.0181 109 ASP   A O   
814  C CB  . ASP   A 103 ? 0.2617 0.2176 0.1603 -0.0044 -0.0171 -0.0230 109 ASP   A CB  
815  C CG  . ASP   A 103 ? 0.2776 0.2265 0.1576 -0.0092 -0.0167 -0.0223 109 ASP   A CG  
816  O OD1 . ASP   A 103 ? 0.2926 0.2383 0.1666 -0.0126 -0.0255 -0.0187 109 ASP   A OD1 
817  O OD2 . ASP   A 103 ? 0.3158 0.2622 0.1881 -0.0096 -0.0073 -0.0250 109 ASP   A OD2 
818  N N   . CYS   A 104 ? 0.2463 0.2057 0.1695 -0.0007 -0.0263 -0.0248 110 CYS   A N   
819  C CA  . CYS   A 104 ? 0.2251 0.1926 0.1658 0.0021  -0.0277 -0.0231 110 CYS   A CA  
820  C C   . CYS   A 104 ? 0.2160 0.1876 0.1644 0.0012  -0.0350 -0.0194 110 CYS   A C   
821  O O   . CYS   A 104 ? 0.2270 0.1937 0.1696 -0.0018 -0.0419 -0.0182 110 CYS   A O   
822  C CB  . CYS   A 104 ? 0.2327 0.1955 0.1753 0.0024  -0.0270 -0.0264 110 CYS   A CB  
823  S SG  . CYS   A 104 ? 0.2479 0.2094 0.1931 0.0059  -0.0160 -0.0293 110 CYS   A SG  
824  N N   . GLY   A 105 ? 0.1897 0.1697 0.1508 0.0033  -0.0332 -0.0171 111 GLY   A N   
825  C CA  . GLY   A 105 ? 0.1964 0.1797 0.1671 0.0033  -0.0372 -0.0141 111 GLY   A CA  
826  C C   . GLY   A 105 ? 0.2210 0.2054 0.1919 0.0037  -0.0357 -0.0118 111 GLY   A C   
827  O O   . GLY   A 105 ? 0.2312 0.2183 0.2126 0.0046  -0.0358 -0.0098 111 GLY   A O   
828  N N   . GLY   A 106 ? 0.2139 0.1955 0.1737 0.0030  -0.0333 -0.0122 112 GLY   A N   
829  C CA  . GLY   A 106 ? 0.2083 0.1898 0.1673 0.0028  -0.0317 -0.0101 112 GLY   A CA  
830  C C   . GLY   A 106 ? 0.1960 0.1823 0.1621 0.0032  -0.0262 -0.0106 112 GLY   A C   
831  O O   . GLY   A 106 ? 0.1953 0.1854 0.1619 0.0029  -0.0231 -0.0118 112 GLY   A O   
832  N N   . ILE   A 107 ? 0.1800 0.1650 0.1517 0.0034  -0.0251 -0.0094 113 ILE   A N   
833  C CA  . ILE   A 107 ? 0.1748 0.1613 0.1490 0.0020  -0.0193 -0.0106 113 ILE   A CA  
834  C C   . ILE   A 107 ? 0.1815 0.1671 0.1467 -0.0010 -0.0162 -0.0104 113 ILE   A C   
835  O O   . ILE   A 107 ? 0.1846 0.1664 0.1447 -0.0012 -0.0171 -0.0090 113 ILE   A O   
836  C CB  . ILE   A 107 ? 0.1920 0.1756 0.1766 0.0034  -0.0173 -0.0104 113 ILE   A CB  
837  C CG1 . ILE   A 107 ? 0.2105 0.1979 0.2067 0.0053  -0.0194 -0.0101 113 ILE   A CG1 
838  C CG2 . ILE   A 107 ? 0.2132 0.1937 0.1957 0.0005  -0.0097 -0.0127 113 ILE   A CG2 
839  C CD1 . ILE   A 107 ? 0.2250 0.2110 0.2377 0.0078  -0.0167 -0.0088 113 ILE   A CD1 
840  N N   . LEU   A 108 ? 0.1734 0.1624 0.1372 -0.0044 -0.0131 -0.0110 114 LEU   A N   
841  C CA  . LEU   A 108 ? 0.1849 0.1737 0.1414 -0.0092 -0.0108 -0.0099 114 LEU   A CA  
842  C C   . LEU   A 108 ? 0.1926 0.1757 0.1472 -0.0129 -0.0064 -0.0121 114 LEU   A C   
843  O O   . LEU   A 108 ? 0.1872 0.1711 0.1449 -0.0139 -0.0044 -0.0136 114 LEU   A O   
844  C CB  . LEU   A 108 ? 0.1891 0.1860 0.1465 -0.0115 -0.0117 -0.0076 114 LEU   A CB  
845  C CG  . LEU   A 108 ? 0.2001 0.1990 0.1521 -0.0183 -0.0110 -0.0047 114 LEU   A CG  
846  C CD1 . LEU   A 108 ? 0.2113 0.2088 0.1586 -0.0188 -0.0107 -0.0032 114 LEU   A CD1 
847  C CD2 . LEU   A 108 ? 0.1996 0.2080 0.1575 -0.0206 -0.0133 -0.0003 114 LEU   A CD2 
848  N N   . ARG   A 109 ? 0.1925 0.1686 0.1408 -0.0155 -0.0040 -0.0125 115 ARG   A N   
849  C CA  . ARG   A 109 ? 0.2276 0.1945 0.1721 -0.0194 0.0022  -0.0159 115 ARG   A CA  
850  C C   . ARG   A 109 ? 0.2497 0.2119 0.1812 -0.0275 0.0035  -0.0156 115 ARG   A C   
851  O O   . ARG   A 109 ? 0.2456 0.2086 0.1743 -0.0278 0.0007  -0.0129 115 ARG   A O   
852  C CB  . ARG   A 109 ? 0.2599 0.2186 0.2112 -0.0144 0.0046  -0.0169 115 ARG   A CB  
853  C CG  . ARG   A 109 ? 0.3365 0.2986 0.3024 -0.0073 0.0026  -0.0161 115 ARG   A CG  
854  C CD  . ARG   A 109 ? 0.3664 0.3202 0.3412 -0.0034 0.0048  -0.0153 115 ARG   A CD  
855  N NE  . ARG   A 109 ? 0.4435 0.3886 0.4203 -0.0050 0.0150  -0.0199 115 ARG   A NE  
856  C CZ  . ARG   A 109 ? 0.4646 0.4104 0.4546 -0.0019 0.0201  -0.0215 115 ARG   A CZ  
857  N NH1 . ARG   A 109 ? 0.4480 0.3844 0.4377 -0.0042 0.0317  -0.0266 115 ARG   A NH1 
858  N NH2 . ARG   A 109 ? 0.4647 0.4200 0.4683 0.0029  0.0142  -0.0181 115 ARG   A NH2 
859  N N   . CYS   A 110 ? 0.2550 0.2110 0.1777 -0.0348 0.0082  -0.0185 116 CYS   A N   
860  C CA  . CYS   A 110 ? 0.2865 0.2346 0.1941 -0.0446 0.0096  -0.0189 116 CYS   A CA  
861  C C   . CYS   A 110 ? 0.3292 0.2602 0.2312 -0.0463 0.0192  -0.0254 116 CYS   A C   
862  O O   . CYS   A 110 ? 0.3411 0.2691 0.2545 -0.0389 0.0242  -0.0282 116 CYS   A O   
863  C CB  . CYS   A 110 ? 0.2959 0.2492 0.1942 -0.0545 0.0065  -0.0164 116 CYS   A CB  
864  S SG  . CYS   A 110 ? 0.2727 0.2206 0.1654 -0.0588 0.0128  -0.0212 116 CYS   A SG  
865  N N   . GLN   A 111 ? 0.3658 0.2848 0.2512 -0.0563 0.0224  -0.0277 117 GLN   A N   
866  C CA  . GLN   A 111 ? 0.4055 0.3052 0.2843 -0.0586 0.0338  -0.0351 117 GLN   A CA  
867  C C   . GLN   A 111 ? 0.4140 0.3092 0.2935 -0.0586 0.0431  -0.0408 117 GLN   A C   
868  O O   . GLN   A 111 ? 0.4337 0.3157 0.3178 -0.0552 0.0544  -0.0467 117 GLN   A O   
869  C CB  . GLN   A 111 ? 0.4572 0.3438 0.3133 -0.0724 0.0352  -0.0370 117 GLN   A CB  
870  C CG  . GLN   A 111 ? 0.5089 0.4010 0.3490 -0.0854 0.0298  -0.0345 117 GLN   A CG  
871  C CD  . GLN   A 111 ? 0.5892 0.4677 0.4053 -0.1010 0.0297  -0.0356 117 GLN   A CD  
872  O OE1 . GLN   A 111 ? 0.6159 0.5035 0.4253 -0.1101 0.0195  -0.0286 117 GLN   A OE1 
873  N NE2 . GLN   A 111 ? 0.5794 0.4353 0.3833 -0.1048 0.0412  -0.0442 117 GLN   A NE2 
874  N N   . HIS   A 112 ? 0.3793 0.2855 0.2565 -0.0621 0.0389  -0.0385 118 HIS   A N   
875  C CA  . HIS   A 112 ? 0.3673 0.2705 0.2427 -0.0641 0.0470  -0.0429 118 HIS   A CA  
876  C C   . HIS   A 112 ? 0.3481 0.2619 0.2478 -0.0513 0.0475  -0.0418 118 HIS   A C   
877  O O   . HIS   A 112 ? 0.3610 0.2718 0.2641 -0.0510 0.0563  -0.0458 118 HIS   A O   
878  C CB  . HIS   A 112 ? 0.3568 0.2652 0.2154 -0.0766 0.0412  -0.0399 118 HIS   A CB  
879  C CG  . HIS   A 112 ? 0.3934 0.2923 0.2277 -0.0915 0.0388  -0.0395 118 HIS   A CG  
880  N ND1 . HIS   A 112 ? 0.3876 0.2980 0.2208 -0.0956 0.0258  -0.0311 118 HIS   A ND1 
881  C CD2 . HIS   A 112 ? 0.4267 0.3055 0.2377 -0.1035 0.0479  -0.0464 118 HIS   A CD2 
882  C CE1 . HIS   A 112 ? 0.4258 0.3241 0.2362 -0.1102 0.0259  -0.0322 118 HIS   A CE1 
883  N NE2 . HIS   A 112 ? 0.4490 0.3270 0.2433 -0.1159 0.0389  -0.0418 118 HIS   A NE2 
884  N N   . GLY   A 113 ? 0.3117 0.2374 0.2271 -0.0418 0.0383  -0.0363 119 GLY   A N   
885  C CA  . GLY   A 113 ? 0.2702 0.2055 0.2068 -0.0314 0.0368  -0.0345 119 GLY   A CA  
886  C C   . GLY   A 113 ? 0.2292 0.1797 0.1723 -0.0275 0.0247  -0.0283 119 GLY   A C   
887  O O   . GLY   A 113 ? 0.2385 0.1925 0.1751 -0.0295 0.0181  -0.0250 119 GLY   A O   
888  N N   . VAL   A 114 ? 0.2122 0.1711 0.1687 -0.0220 0.0227  -0.0270 120 VAL   A N   
889  C CA  . VAL   A 114 ? 0.2054 0.1760 0.1677 -0.0183 0.0129  -0.0225 120 VAL   A CA  
890  C C   . VAL   A 114 ? 0.2124 0.1885 0.1651 -0.0250 0.0093  -0.0203 120 VAL   A C   
891  O O   . VAL   A 114 ? 0.2269 0.2018 0.1745 -0.0307 0.0131  -0.0216 120 VAL   A O   
892  C CB  . VAL   A 114 ? 0.2114 0.1873 0.1901 -0.0120 0.0122  -0.0219 120 VAL   A CB  
893  C CG1 . VAL   A 114 ? 0.2239 0.2091 0.2060 -0.0093 0.0030  -0.0183 120 VAL   A CG1 
894  C CG2 . VAL   A 114 ? 0.2231 0.1952 0.2154 -0.0054 0.0139  -0.0217 120 VAL   A CG2 
895  N N   . VAL   A 115 ? 0.1881 0.1705 0.1395 -0.0245 0.0023  -0.0163 121 VAL   A N   
896  C CA  . VAL   A 115 ? 0.1936 0.1831 0.1411 -0.0298 -0.0023 -0.0121 121 VAL   A CA  
897  C C   . VAL   A 115 ? 0.1842 0.1820 0.1429 -0.0245 -0.0069 -0.0096 121 VAL   A C   
898  O O   . VAL   A 115 ? 0.1948 0.1971 0.1543 -0.0282 -0.0091 -0.0067 121 VAL   A O   
899  C CB  . VAL   A 115 ? 0.1998 0.1910 0.1420 -0.0325 -0.0056 -0.0088 121 VAL   A CB  
900  C CG1 . VAL   A 115 ? 0.1925 0.1929 0.1361 -0.0371 -0.0111 -0.0025 121 VAL   A CG1 
901  C CG2 . VAL   A 115 ? 0.2273 0.2085 0.1567 -0.0391 -0.0014 -0.0114 121 VAL   A CG2 
902  N N   . GLY   A 116 ? 0.1665 0.1655 0.1326 -0.0168 -0.0089 -0.0103 122 GLY   A N   
903  C CA  . GLY   A 116 ? 0.1724 0.1763 0.1469 -0.0123 -0.0127 -0.0090 122 GLY   A CA  
904  C C   . GLY   A 116 ? 0.1832 0.1853 0.1608 -0.0059 -0.0147 -0.0105 122 GLY   A C   
905  O O   . GLY   A 116 ? 0.1866 0.1843 0.1621 -0.0046 -0.0137 -0.0118 122 GLY   A O   
906  N N   . ILE   A 117 ? 0.1624 0.1666 0.1440 -0.0029 -0.0175 -0.0101 123 ILE   A N   
907  C CA  . ILE   A 117 ? 0.1629 0.1634 0.1432 0.0010  -0.0199 -0.0117 123 ILE   A CA  
908  C C   . ILE   A 117 ? 0.1633 0.1642 0.1412 0.0025  -0.0195 -0.0115 123 ILE   A C   
909  O O   . ILE   A 117 ? 0.1512 0.1557 0.1343 0.0024  -0.0187 -0.0100 123 ILE   A O   
910  C CB  . ILE   A 117 ? 0.1691 0.1683 0.1557 0.0026  -0.0230 -0.0127 123 ILE   A CB  
911  C CG1 . ILE   A 117 ? 0.1883 0.1905 0.1806 0.0019  -0.0235 -0.0122 123 ILE   A CG1 
912  C CG2 . ILE   A 117 ? 0.2017 0.2002 0.1939 0.0024  -0.0220 -0.0126 123 ILE   A CG2 
913  C CD1 . ILE   A 117 ? 0.2216 0.2219 0.2194 0.0030  -0.0277 -0.0130 123 ILE   A CD1 
914  N N   . VAL   A 118 ? 0.1671 0.1635 0.1376 0.0038  -0.0196 -0.0129 124 VAL   A N   
915  C CA  . VAL   A 118 ? 0.1679 0.1629 0.1354 0.0052  -0.0167 -0.0139 124 VAL   A CA  
916  C C   . VAL   A 118 ? 0.1733 0.1663 0.1456 0.0069  -0.0171 -0.0157 124 VAL   A C   
917  O O   . VAL   A 118 ? 0.1773 0.1664 0.1488 0.0066  -0.0212 -0.0173 124 VAL   A O   
918  C CB  . VAL   A 118 ? 0.1874 0.1753 0.1423 0.0047  -0.0168 -0.0157 124 VAL   A CB  
919  C CG1 . VAL   A 118 ? 0.2048 0.1888 0.1549 0.0059  -0.0116 -0.0184 124 VAL   A CG1 
920  C CG2 . VAL   A 118 ? 0.1902 0.1796 0.1411 0.0030  -0.0159 -0.0134 124 VAL   A CG2 
921  N N   . SER   A 119 ? 0.1747 0.1701 0.1535 0.0086  -0.0129 -0.0147 125 SER   A N   
922  C CA  . SER   A 119 ? 0.1744 0.1664 0.1588 0.0105  -0.0126 -0.0163 125 SER   A CA  
923  C C   . SER   A 119 ? 0.2019 0.1899 0.1876 0.0134  -0.0053 -0.0182 125 SER   A C   
924  O O   . SER   A 119 ? 0.2252 0.2044 0.2090 0.0146  -0.0036 -0.0222 125 SER   A O   
925  C CB  . SER   A 119 ? 0.1845 0.1838 0.1814 0.0097  -0.0151 -0.0117 125 SER   A CB  
926  O OG  . SER   A 119 ? 0.2171 0.2136 0.2219 0.0114  -0.0148 -0.0119 125 SER   A OG  
927  N N   . THR   A 120 ? 0.2036 0.1968 0.1924 0.0142  -0.0001 -0.0157 126 THR   A N   
928  C CA  . THR   A 120 ? 0.2185 0.2080 0.2111 0.0176  0.0093  -0.0177 126 THR   A CA  
929  C C   . THR   A 120 ? 0.2543 0.2434 0.2372 0.0166  0.0147  -0.0188 126 THR   A C   
930  O O   . THR   A 120 ? 0.2352 0.2287 0.2120 0.0135  0.0104  -0.0164 126 THR   A O   
931  C CB  . THR   A 120 ? 0.2111 0.2100 0.2269 0.0206  0.0116  -0.0111 126 THR   A CB  
932  O OG1 . THR   A 120 ? 0.2090 0.2204 0.2319 0.0185  0.0098  -0.0042 126 THR   A OG1 
933  C CG2 . THR   A 120 ? 0.2055 0.2060 0.2301 0.0202  0.0049  -0.0084 126 THR   A CG2 
934  N N   . GLY   A 121 ? 0.2844 0.2672 0.2656 0.0188  0.0251  -0.0225 127 GLY   A N   
935  C CA  . GLY   A 121 ? 0.3194 0.3012 0.2904 0.0171  0.0314  -0.0236 127 GLY   A CA  
936  C C   . GLY   A 121 ? 0.3576 0.3354 0.3342 0.0205  0.0458  -0.0264 127 GLY   A C   
937  O O   . GLY   A 121 ? 0.3679 0.3459 0.3614 0.0252  0.0508  -0.0261 127 GLY   A O   
938  N N   . GLY   A 122 ? 0.3791 0.3524 0.3417 0.0181  0.0532  -0.0293 128 GLY   A N   
939  C CA  . GLY   A 122 ? 0.3946 0.3632 0.3609 0.0209  0.0697  -0.0328 128 GLY   A CA  
940  C C   . GLY   A 122 ? 0.3830 0.3681 0.3743 0.0240  0.0762  -0.0248 128 GLY   A C   
941  O O   . GLY   A 122 ? 0.3744 0.3747 0.3847 0.0246  0.0674  -0.0159 128 GLY   A O   
942  N N   . ASN   A 123 ? 0.3784 0.3605 0.3698 0.0250  0.0918  -0.0275 129 ASN   A N   
943  C CA  . ASN   A 123 ? 0.3737 0.3721 0.3912 0.0277  0.0997  -0.0194 129 ASN   A CA  
944  C C   . ASN   A 123 ? 0.3425 0.3543 0.3584 0.0224  0.0895  -0.0115 129 ASN   A C   
945  O O   . ASN   A 123 ? 0.3423 0.3710 0.3838 0.0235  0.0895  -0.0019 129 ASN   A O   
946  C CB  . ASN   A 123 ? 0.4006 0.4114 0.4557 0.0346  0.1002  -0.0117 129 ASN   A CB  
947  C CG  . ASN   A 123 ? 0.4637 0.4651 0.5326 0.0416  0.1163  -0.0169 129 ASN   A CG  
948  O OD1 . ASN   A 123 ? 0.4919 0.4769 0.5426 0.0413  0.1308  -0.0272 129 ASN   A OD1 
949  N ND2 . ASN   A 123 ? 0.4620 0.4726 0.5634 0.0475  0.1144  -0.0094 129 ASN   A ND2 
950  N N   . GLY   A 124 ? 0.3070 0.3110 0.2951 0.0164  0.0800  -0.0146 130 GLY   A N   
951  C CA  . GLY   A 124 ? 0.2784 0.2921 0.2639 0.0114  0.0708  -0.0080 130 GLY   A CA  
952  C C   . GLY   A 124 ? 0.2424 0.2660 0.2402 0.0109  0.0564  -0.0015 130 GLY   A C   
953  O O   . GLY   A 124 ? 0.2403 0.2731 0.2414 0.0069  0.0501  0.0049  130 GLY   A O   
954  N N   . LEU   A 125 ? 0.2170 0.2379 0.2204 0.0141  0.0518  -0.0032 131 LEU   A N   
955  C CA  . LEU   A 125 ? 0.2147 0.2437 0.2272 0.0127  0.0393  0.0024  131 LEU   A CA  
956  C C   . LEU   A 125 ? 0.2183 0.2361 0.2123 0.0114  0.0308  -0.0035 131 LEU   A C   
957  O O   . LEU   A 125 ? 0.2412 0.2465 0.2207 0.0125  0.0338  -0.0108 131 LEU   A O   
958  C CB  . LEU   A 125 ? 0.2113 0.2489 0.2507 0.0170  0.0404  0.0078  131 LEU   A CB  
959  C CG  . LEU   A 125 ? 0.2336 0.2847 0.2988 0.0189  0.0478  0.0160  131 LEU   A CG  
960  C CD1 . LEU   A 125 ? 0.2414 0.2990 0.3347 0.0241  0.0491  0.0215  131 LEU   A CD1 
961  C CD2 . LEU   A 125 ? 0.2350 0.2991 0.3048 0.0123  0.0398  0.0251  131 LEU   A CD2 
962  N N   . VAL   A 126 ? 0.1859 0.2080 0.1802 0.0084  0.0206  -0.0001 132 VAL   A N   
963  C CA  . VAL   A 126 ? 0.1702 0.1843 0.1528 0.0077  0.0133  -0.0043 132 VAL   A CA  
964  C C   . VAL   A 126 ? 0.1701 0.1919 0.1659 0.0069  0.0070  0.0004  132 VAL   A C   
965  O O   . VAL   A 126 ? 0.1816 0.2124 0.1848 0.0034  0.0044  0.0068  132 VAL   A O   
966  C CB  . VAL   A 126 ? 0.1972 0.2059 0.1628 0.0038  0.0083  -0.0058 132 VAL   A CB  
967  C CG1 . VAL   A 126 ? 0.1960 0.2117 0.1639 -0.0004 0.0056  -0.0005 132 VAL   A CG1 
968  C CG2 . VAL   A 126 ? 0.2225 0.2249 0.1820 0.0039  0.0014  -0.0089 132 VAL   A CG2 
969  N N   . GLY   A 127 ? 0.1574 0.1748 0.1550 0.0092  0.0047  -0.0023 133 GLY   A N   
970  C CA  . GLY   A 127 ? 0.1448 0.1681 0.1528 0.0077  -0.0009 0.0022  133 GLY   A CA  
971  C C   . GLY   A 127 ? 0.1613 0.1794 0.1592 0.0056  -0.0066 -0.0011 133 GLY   A C   
972  O O   . GLY   A 127 ? 0.1745 0.1842 0.1639 0.0074  -0.0068 -0.0066 133 GLY   A O   
973  N N   . PHE   A 128 ? 0.1480 0.1707 0.1467 0.0009  -0.0111 0.0026  134 PHE   A N   
974  C CA  . PHE   A 128 ? 0.1596 0.1780 0.1509 -0.0013 -0.0145 -0.0003 134 PHE   A CA  
975  C C   . PHE   A 128 ? 0.1743 0.1958 0.1725 -0.0035 -0.0175 0.0026  134 PHE   A C   
976  O O   . PHE   A 128 ? 0.1754 0.2036 0.1798 -0.0073 -0.0194 0.0088  134 PHE   A O   
977  C CB  . PHE   A 128 ? 0.1703 0.1883 0.1533 -0.0063 -0.0151 0.0003  134 PHE   A CB  
978  C CG  . PHE   A 128 ? 0.1838 0.1993 0.1602 -0.0054 -0.0127 -0.0009 134 PHE   A CG  
979  C CD1 . PHE   A 128 ? 0.1920 0.2002 0.1609 -0.0029 -0.0126 -0.0051 134 PHE   A CD1 
980  C CD2 . PHE   A 128 ? 0.1802 0.2014 0.1590 -0.0078 -0.0114 0.0034  134 PHE   A CD2 
981  C CE1 . PHE   A 128 ? 0.2030 0.2083 0.1647 -0.0031 -0.0110 -0.0053 134 PHE   A CE1 
982  C CE2 . PHE   A 128 ? 0.1991 0.2180 0.1715 -0.0077 -0.0089 0.0027  134 PHE   A CE2 
983  C CZ  . PHE   A 128 ? 0.1995 0.2099 0.1623 -0.0055 -0.0087 -0.0018 134 PHE   A CZ  
984  N N   . ALA   A 129 ? 0.1675 0.1845 0.1646 -0.0021 -0.0188 -0.0010 135 ALA   A N   
985  C CA  . ALA   A 129 ? 0.1708 0.1902 0.1727 -0.0051 -0.0213 0.0017  135 ALA   A CA  
986  C C   . ALA   A 129 ? 0.1732 0.1924 0.1670 -0.0113 -0.0210 0.0017  135 ALA   A C   
987  O O   . ALA   A 129 ? 0.1744 0.1888 0.1628 -0.0105 -0.0190 -0.0028 135 ALA   A O   
988  C CB  . ALA   A 129 ? 0.1681 0.1829 0.1725 -0.0020 -0.0223 -0.0020 135 ALA   A CB  
989  N N   . ASP   A 130 ? 0.1621 0.1853 0.1550 -0.0181 -0.0229 0.0070  136 ASP   A N   
990  C CA  . ASP   A 130 ? 0.1772 0.1975 0.1585 -0.0258 -0.0213 0.0061  136 ASP   A CA  
991  C C   . ASP   A 130 ? 0.1868 0.2036 0.1670 -0.0268 -0.0191 0.0029  136 ASP   A C   
992  O O   . ASP   A 130 ? 0.1985 0.2176 0.1864 -0.0250 -0.0214 0.0046  136 ASP   A O   
993  C CB  . ASP   A 130 ? 0.2065 0.2316 0.1851 -0.0350 -0.0255 0.0138  136 ASP   A CB  
994  C CG  . ASP   A 130 ? 0.2499 0.2695 0.2118 -0.0454 -0.0235 0.0126  136 ASP   A CG  
995  O OD1 . ASP   A 130 ? 0.2405 0.2540 0.1941 -0.0453 -0.0192 0.0074  136 ASP   A OD1 
996  O OD2 . ASP   A 130 ? 0.3022 0.3220 0.2581 -0.0542 -0.0259 0.0165  136 ASP   A OD2 
997  N N   . VAL   A 131 ? 0.1785 0.1895 0.1502 -0.0296 -0.0139 -0.0017 137 VAL   A N   
998  C CA  . VAL   A 131 ? 0.1775 0.1856 0.1491 -0.0314 -0.0097 -0.0045 137 VAL   A CA  
999  C C   . VAL   A 131 ? 0.1992 0.2016 0.1555 -0.0419 -0.0044 -0.0057 137 VAL   A C   
1000 O O   . VAL   A 131 ? 0.2155 0.2145 0.1699 -0.0446 0.0014  -0.0086 137 VAL   A O   
1001 C CB  . VAL   A 131 ? 0.1759 0.1813 0.1554 -0.0240 -0.0061 -0.0095 137 VAL   A CB  
1002 C CG1 . VAL   A 131 ? 0.1660 0.1748 0.1561 -0.0163 -0.0117 -0.0086 137 VAL   A CG1 
1003 C CG2 . VAL   A 131 ? 0.1811 0.1805 0.1553 -0.0232 -0.0017 -0.0130 137 VAL   A CG2 
1004 N N   . ARG   A 132 ? 0.1940 0.1942 0.1388 -0.0483 -0.0057 -0.0040 138 ARG   A N   
1005 C CA  . ARG   A 132 ? 0.1967 0.1884 0.1228 -0.0598 -0.0007 -0.0061 138 ARG   A CA  
1006 C C   . ARG   A 132 ? 0.2408 0.2328 0.1581 -0.0701 -0.0018 -0.0025 138 ARG   A C   
1007 O O   . ARG   A 132 ? 0.2836 0.2660 0.1833 -0.0801 0.0052  -0.0062 138 ARG   A O   
1008 C CB  . ARG   A 132 ? 0.2070 0.1971 0.1226 -0.0658 -0.0041 -0.0036 138 ARG   A CB  
1009 C CG  . ARG   A 132 ? 0.2232 0.2104 0.1432 -0.0580 -0.0015 -0.0076 138 ARG   A CG  
1010 C CD  . ARG   A 132 ? 0.2196 0.2063 0.1308 -0.0643 -0.0055 -0.0042 138 ARG   A CD  
1011 N NE  . ARG   A 132 ? 0.2205 0.2198 0.1426 -0.0628 -0.0147 0.0043  138 ARG   A NE  
1012 C CZ  . ARG   A 132 ? 0.2708 0.2740 0.1918 -0.0668 -0.0195 0.0095  138 ARG   A CZ  
1013 N NH1 . ARG   A 132 ? 0.2659 0.2605 0.1722 -0.0741 -0.0173 0.0071  138 ARG   A NH1 
1014 N NH2 . ARG   A 132 ? 0.2675 0.2829 0.2031 -0.0638 -0.0261 0.0173  138 ARG   A NH2 
1015 N N   . ASP   A 133 ? 0.2178 0.2190 0.1457 -0.0686 -0.0099 0.0047  139 ASP   A N   
1016 C CA  . ASP   A 133 ? 0.2245 0.2262 0.1446 -0.0790 -0.0123 0.0096  139 ASP   A CA  
1017 C C   . ASP   A 133 ? 0.2390 0.2388 0.1633 -0.0766 -0.0055 0.0054  139 ASP   A C   
1018 O O   . ASP   A 133 ? 0.2516 0.2494 0.1657 -0.0866 -0.0048 0.0081  139 ASP   A O   
1019 C CB  . ASP   A 133 ? 0.2450 0.2569 0.1764 -0.0793 -0.0243 0.0206  139 ASP   A CB  
1020 C CG  . ASP   A 133 ? 0.2907 0.3091 0.2444 -0.0658 -0.0264 0.0209  139 ASP   A CG  
1021 O OD1 . ASP   A 133 ? 0.2617 0.2796 0.2233 -0.0553 -0.0231 0.0150  139 ASP   A OD1 
1022 O OD2 . ASP   A 133 ? 0.3066 0.3290 0.2685 -0.0664 -0.0313 0.0269  139 ASP   A OD2 
1023 N N   . LEU   A 134 ? 0.2335 0.2340 0.1723 -0.0646 -0.0007 -0.0004 140 LEU   A N   
1024 C CA  . LEU   A 134 ? 0.2261 0.2270 0.1737 -0.0617 0.0048  -0.0031 140 LEU   A CA  
1025 C C   . LEU   A 134 ? 0.2440 0.2359 0.1813 -0.0664 0.0181  -0.0103 140 LEU   A C   
1026 O O   . LEU   A 134 ? 0.2431 0.2328 0.1903 -0.0586 0.0251  -0.0159 140 LEU   A O   
1027 C CB  . LEU   A 134 ? 0.2178 0.2237 0.1860 -0.0481 0.0025  -0.0049 140 LEU   A CB  
1028 C CG  . LEU   A 134 ? 0.2187 0.2309 0.1960 -0.0429 -0.0082 0.0005  140 LEU   A CG  
1029 C CD1 . LEU   A 134 ? 0.1955 0.2094 0.1876 -0.0317 -0.0101 -0.0022 140 LEU   A CD1 
1030 C CD2 . LEU   A 134 ? 0.2326 0.2485 0.2117 -0.0481 -0.0140 0.0075  140 LEU   A CD2 
1031 N N   . LEU   A 135 ? 0.2491 0.2344 0.1652 -0.0801 0.0218  -0.0099 141 LEU   A N   
1032 C CA  . LEU   A 135 ? 0.2781 0.2514 0.1804 -0.0861 0.0369  -0.0181 141 LEU   A CA  
1033 C C   . LEU   A 135 ? 0.3011 0.2752 0.2183 -0.0805 0.0479  -0.0224 141 LEU   A C   
1034 O O   . LEU   A 135 ? 0.3254 0.2915 0.2434 -0.0787 0.0619  -0.0300 141 LEU   A O   
1035 C CB  . LEU   A 135 ? 0.3025 0.2666 0.1747 -0.1044 0.0387  -0.0170 141 LEU   A CB  
1036 C CG  . LEU   A 135 ? 0.3254 0.2914 0.1844 -0.1130 0.0249  -0.0091 141 LEU   A CG  
1037 C CD1 . LEU   A 135 ? 0.3548 0.3094 0.1805 -0.1339 0.0272  -0.0081 141 LEU   A CD1 
1038 C CD2 . LEU   A 135 ? 0.3310 0.2958 0.1927 -0.1071 0.0224  -0.0111 141 LEU   A CD2 
1039 N N   . TRP   A 136 ? 0.2944 0.2784 0.2256 -0.0775 0.0419  -0.0173 142 TRP   A N   
1040 C CA  . TRP   A 136 ? 0.2847 0.2720 0.2328 -0.0729 0.0505  -0.0195 142 TRP   A CA  
1041 C C   . TRP   A 136 ? 0.2895 0.2801 0.2617 -0.0591 0.0533  -0.0227 142 TRP   A C   
1042 O O   . TRP   A 136 ? 0.2847 0.2768 0.2718 -0.0558 0.0632  -0.0252 142 TRP   A O   
1043 C CB  . TRP   A 136 ? 0.2656 0.2618 0.2222 -0.0739 0.0417  -0.0124 142 TRP   A CB  
1044 C CG  . TRP   A 136 ? 0.2528 0.2568 0.2205 -0.0666 0.0260  -0.0066 142 TRP   A CG  
1045 C CD1 . TRP   A 136 ? 0.2568 0.2623 0.2159 -0.0710 0.0147  -0.0002 142 TRP   A CD1 
1046 C CD2 . TRP   A 136 ? 0.2416 0.2520 0.2315 -0.0542 0.0205  -0.0065 142 TRP   A CD2 
1047 N NE1 . TRP   A 136 ? 0.2566 0.2683 0.2316 -0.0612 0.0046  0.0028  142 TRP   A NE1 
1048 C CE2 . TRP   A 136 ? 0.2525 0.2665 0.2442 -0.0518 0.0077  -0.0012 142 TRP   A CE2 
1049 C CE3 . TRP   A 136 ? 0.2439 0.2574 0.2531 -0.0461 0.0249  -0.0093 142 TRP   A CE3 
1050 C CZ2 . TRP   A 136 ? 0.2549 0.2730 0.2622 -0.0421 0.0005  -0.0006 142 TRP   A CZ2 
1051 C CZ3 . TRP   A 136 ? 0.2413 0.2600 0.2661 -0.0373 0.0154  -0.0073 142 TRP   A CZ3 
1052 C CH2 . TRP   A 136 ? 0.2525 0.2723 0.2742 -0.0358 0.0039  -0.0037 142 TRP   A CH2 
1053 N N   . LEU   A 137 ? 0.2861 0.2777 0.2623 -0.0518 0.0452  -0.0223 143 LEU   A N   
1054 C CA  . LEU   A 137 ? 0.3029 0.2971 0.3000 -0.0400 0.0461  -0.0241 143 LEU   A CA  
1055 C C   . LEU   A 137 ? 0.3628 0.3488 0.3634 -0.0392 0.0624  -0.0304 143 LEU   A C   
1056 O O   . LEU   A 137 ? 0.3621 0.3520 0.3863 -0.0305 0.0657  -0.0303 143 LEU   A O   
1057 C CB  . LEU   A 137 ? 0.2933 0.2877 0.2883 -0.0348 0.0360  -0.0227 143 LEU   A CB  
1058 C CG  . LEU   A 137 ? 0.2836 0.2859 0.2829 -0.0316 0.0218  -0.0173 143 LEU   A CG  
1059 C CD1 . LEU   A 137 ? 0.2830 0.2841 0.2782 -0.0276 0.0153  -0.0169 143 LEU   A CD1 
1060 C CD2 . LEU   A 137 ? 0.2868 0.2962 0.3068 -0.0250 0.0178  -0.0151 143 LEU   A CD2 
1061 N N   . ASP   A 138 ? 0.4079 0.3820 0.3856 -0.0488 0.0726  -0.0354 144 ASP   A N   
1062 C CA  . ASP   A 138 ? 0.4675 0.4295 0.4433 -0.0498 0.0904  -0.0430 144 ASP   A CA  
1063 C C   . ASP   A 138 ? 0.5228 0.4813 0.4984 -0.0555 0.1065  -0.0466 144 ASP   A C   
1064 O O   . ASP   A 138 ? 0.5409 0.4860 0.5084 -0.0591 0.1237  -0.0542 144 ASP   A O   
1065 C CB  . ASP   A 138 ? 0.5118 0.4598 0.4585 -0.0589 0.0929  -0.0473 144 ASP   A CB  
1066 C CG  . ASP   A 138 ? 0.5820 0.5304 0.5332 -0.0516 0.0837  -0.0458 144 ASP   A CG  
1067 O OD1 . ASP   A 138 ? 0.5993 0.5513 0.5747 -0.0400 0.0844  -0.0454 144 ASP   A OD1 
1068 O OD2 . ASP   A 138 ? 0.6129 0.5589 0.5450 -0.0580 0.0752  -0.0442 144 ASP   A OD2 
1069 N N   . GLU   A 139 ? 0.5411 0.5102 0.5248 -0.0568 0.1022  -0.0418 145 GLU   A N   
1070 C CA  . GLU   A 139 ? 0.5697 0.5368 0.5544 -0.0626 0.1177  -0.0446 145 GLU   A CA  
1071 C C   . GLU   A 139 ? 0.5731 0.5560 0.5856 -0.0564 0.1122  -0.0382 145 GLU   A C   
1072 O O   . GLU   A 139 ? 0.5895 0.5743 0.6008 -0.0630 0.1194  -0.0376 145 GLU   A O   
1073 C CB  . GLU   A 139 ? 0.6268 0.5846 0.5756 -0.0795 0.1202  -0.0459 145 GLU   A CB  
1074 C CG  . GLU   A 139 ? 0.6995 0.6660 0.6391 -0.0840 0.1002  -0.0372 145 GLU   A CG  
1075 C CD  . GLU   A 139 ? 0.8089 0.7655 0.7119 -0.1007 0.0978  -0.0365 145 GLU   A CD  
1076 O OE1 . GLU   A 139 ? 0.8257 0.7886 0.7220 -0.1072 0.0858  -0.0287 145 GLU   A OE1 
1077 O OE2 . GLU   A 139 ? 0.8503 0.7922 0.7314 -0.1080 0.1076  -0.0433 145 GLU   A OE2 
1078 N N1  . A1B4H B .   ? 0.3482 0.3250 0.3579 0.0185  -0.0038 -0.0195 201 A1B4H A N1  
1079 C C4  . A1B4H B .   ? 0.4434 0.3619 0.3738 0.0167  0.0509  -0.0540 201 A1B4H A C4  
1080 C C5  . A1B4H B .   ? 0.4340 0.3555 0.3741 0.0174  0.0405  -0.0514 201 A1B4H A C5  
1081 C C6  . A1B4H B .   ? 0.4357 0.3696 0.3794 0.0156  0.0270  -0.0450 201 A1B4H A C6  
1082 C C7  . A1B4H B .   ? 0.4002 0.3506 0.3782 0.0199  0.0158  -0.0353 201 A1B4H A C7  
1083 C C8  . A1B4H B .   ? 0.3906 0.3442 0.3737 0.0180  0.0052  -0.0325 201 A1B4H A C8  
1084 C C10 . A1B4H B .   ? 0.4092 0.3464 0.3805 0.0156  0.0043  -0.0392 201 A1B4H A C10 
1085 O O1  . A1B4H B .   ? 0.4649 0.3783 0.3789 0.0052  0.0108  -0.0518 201 A1B4H A O1  
1086 C C12 . A1B4H B .   ? 0.4381 0.3631 0.3744 0.0104  0.0106  -0.0469 201 A1B4H A C12 
1087 C C11 . A1B4H B .   ? 0.4280 0.3553 0.3746 0.0101  0.0020  -0.0445 201 A1B4H A C11 
1088 C C9  . A1B4H B .   ? 0.3696 0.3345 0.3752 0.0208  0.0033  -0.0251 201 A1B4H A C9  
1089 O O   . A1B4H B .   ? 0.3640 0.3260 0.3829 0.0244  0.0084  -0.0243 201 A1B4H A O   
1090 N N   . A1B4H B .   ? 0.4245 0.3607 0.3770 0.0155  0.0176  -0.0428 201 A1B4H A N   
1091 C C1  . A1B4H B .   ? 0.4375 0.3795 0.3751 0.0133  0.0235  -0.0416 201 A1B4H A C1  
1092 S S   . A1B4H B .   ? 0.4302 0.3834 0.3710 0.0109  0.0086  -0.0354 201 A1B4H A S   
1093 C C   . A1B4H B .   ? 0.4220 0.3815 0.3552 0.0086  0.0084  -0.0321 201 A1B4H A C   
1094 C C3  . A1B4H B .   ? 0.4465 0.3746 0.3710 0.0141  0.0466  -0.0497 201 A1B4H A C3  
1095 C C2  . A1B4H B .   ? 0.4378 0.3773 0.3662 0.0125  0.0327  -0.0435 201 A1B4H A C2  
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