data_7I68
# 
_entry.id   7I68 
# 
_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   7I68         pdb_00007i68 10.2210/pdb7i68/pdb 
WWPDB D_1001408367 ?            ?                   
# 
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                        7I68 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2025-03-12 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frank.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lithgo, R.M.'        1  ? 
'Fairhead, M.'        2  ? 
'Koekemoer, L.'       3  ? 
'Balcomb, B.H.'       4  ? 
'Capkin, E.'          5  ? 
'Chandran, A.V.'      6  ? 
'Golding, M.'         7  ? 
'Godoy, A.S.'         8  ? 
'Aschenbrenner, J.C.' 9  ? 
'Marples, P.G.'       10 ? 
'Ni, X.'              11 ? 
'Thompson, W.'        12 ? 
'Tomlinson, C.W.E.'   13 ? 
'Wild, C.'            14 ? 
'Winokan, M.'         15 ? 
'Xavier, M.-A.E.'     16 ? 
'Kenton, N.'          17 ? 
'Tucker, J.'          18 ? 
'DiPoto, M.'          19 ? 
'Lee, A.'             20 ? 
'Fearon, D.'          21 ? 
'von Delft, F.'       22 ? 
# 
_citation.id                        primary 
_citation.title                     
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Lithgo, R.M.'        ? 1  
primary 'Fairhead, M.'        ? 2  
primary 'Koekemoer, L.'       ? 3  
primary 'Balcomb, B.H.'       ? 4  
primary 'Capkin, E.'          ? 5  
primary 'Chandran, A.V.'      ? 6  
primary 'Golding, M.'         ? 7  
primary 'Godoy, A.S.'         ? 8  
primary 'Aschenbrenner, J.C.' ? 9  
primary 'Marples, P.G.'       ? 10 
primary 'Ni, X.'              ? 11 
primary 'Thompson, W.'        ? 12 
primary 'Tomlinson, C.W.E.'   ? 13 
primary 'Wild, C.'            ? 14 
primary 'Winokan, M.'         ? 15 
primary 'Xavier, M.-A.E.'     ? 16 
primary 'Kenton, N.'          ? 17 
primary 'Tucker, J.'          ? 18 
primary 'DiPoto, M.'          ? 19 
primary 'Lee, A.'             ? 20 
primary 'Fearon, D.'          ? 21 
primary 'von Delft, F.'       ? 22 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Protease 2A'                                                   15892.732 1   3.4.22.29 ? ? ? 
2 non-polymer syn '(3S)-1-[(3-methylphenyl)methyl]-6-oxopiperidine-3-carboxamide' 246.305   1   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                      65.409    1   ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                            78.133    3   ?         ? ? ? 
5 water       nat water                                                           18.015    156 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'P2A,Picornain 2A,Protein 2A' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '(3S)-1-[(3-methylphenyl)methyl]-6-oxopiperidine-3-carboxamide' A1B4F 
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 
A1B4F non-polymer         . '(3S)-1-[(3-methylphenyl)methyl]-6-oxopiperidine-3-carboxamide' ? 'C14 H18 N2 O2'  246.305 
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        A1B4F 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1B4F 
_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 A1B4F 1   201 201 A1B4F LIG A . 
C 3 ZN    1   202 1   ZN    ZN  A . 
D 4 DMS   1   203 0   DMS   DMS A . 
E 4 DMS   1   204 1   DMS   DMS A . 
F 4 DMS   1   205 2   DMS   DMS A . 
G 5 HOH   1   301 49  HOH   HOH A . 
G 5 HOH   2   302 137 HOH   HOH A . 
G 5 HOH   3   303 262 HOH   HOH A . 
G 5 HOH   4   304 43  HOH   HOH A . 
G 5 HOH   5   305 30  HOH   HOH A . 
G 5 HOH   6   306 68  HOH   HOH A . 
G 5 HOH   7   307 271 HOH   HOH A . 
G 5 HOH   8   308 26  HOH   HOH A . 
G 5 HOH   9   309 119 HOH   HOH A . 
G 5 HOH   10  310 104 HOH   HOH A . 
G 5 HOH   11  311 42  HOH   HOH A . 
G 5 HOH   12  312 4   HOH   HOH A . 
G 5 HOH   13  313 178 HOH   HOH A . 
G 5 HOH   14  314 161 HOH   HOH A . 
G 5 HOH   15  315 146 HOH   HOH A . 
G 5 HOH   16  316 20  HOH   HOH A . 
G 5 HOH   17  317 252 HOH   HOH A . 
G 5 HOH   18  318 256 HOH   HOH A . 
G 5 HOH   19  319 111 HOH   HOH A . 
G 5 HOH   20  320 33  HOH   HOH A . 
G 5 HOH   21  321 167 HOH   HOH A . 
G 5 HOH   22  322 55  HOH   HOH A . 
G 5 HOH   23  323 77  HOH   HOH A . 
G 5 HOH   24  324 59  HOH   HOH A . 
G 5 HOH   25  325 263 HOH   HOH A . 
G 5 HOH   26  326 266 HOH   HOH A . 
G 5 HOH   27  327 34  HOH   HOH A . 
G 5 HOH   28  328 211 HOH   HOH A . 
G 5 HOH   29  329 24  HOH   HOH A . 
G 5 HOH   30  330 275 HOH   HOH A . 
G 5 HOH   31  331 181 HOH   HOH A . 
G 5 HOH   32  332 205 HOH   HOH A . 
G 5 HOH   33  333 2   HOH   HOH A . 
G 5 HOH   34  334 214 HOH   HOH A . 
G 5 HOH   35  335 107 HOH   HOH A . 
G 5 HOH   36  336 28  HOH   HOH A . 
G 5 HOH   37  337 9   HOH   HOH A . 
G 5 HOH   38  338 13  HOH   HOH A . 
G 5 HOH   39  339 169 HOH   HOH A . 
G 5 HOH   40  340 37  HOH   HOH A . 
G 5 HOH   41  341 264 HOH   HOH A . 
G 5 HOH   42  342 25  HOH   HOH A . 
G 5 HOH   43  343 70  HOH   HOH A . 
G 5 HOH   44  344 219 HOH   HOH A . 
G 5 HOH   45  345 57  HOH   HOH A . 
G 5 HOH   46  346 273 HOH   HOH A . 
G 5 HOH   47  347 286 HOH   HOH A . 
G 5 HOH   48  348 82  HOH   HOH A . 
G 5 HOH   49  349 15  HOH   HOH A . 
G 5 HOH   50  350 144 HOH   HOH A . 
G 5 HOH   51  351 269 HOH   HOH A . 
G 5 HOH   52  352 29  HOH   HOH A . 
G 5 HOH   53  353 261 HOH   HOH A . 
G 5 HOH   54  354 103 HOH   HOH A . 
G 5 HOH   55  355 85  HOH   HOH A . 
G 5 HOH   56  356 272 HOH   HOH A . 
G 5 HOH   57  357 105 HOH   HOH A . 
G 5 HOH   58  358 254 HOH   HOH A . 
G 5 HOH   59  359 259 HOH   HOH A . 
G 5 HOH   60  360 186 HOH   HOH A . 
G 5 HOH   61  361 36  HOH   HOH A . 
G 5 HOH   62  362 183 HOH   HOH A . 
G 5 HOH   63  363 16  HOH   HOH A . 
G 5 HOH   64  364 7   HOH   HOH A . 
G 5 HOH   65  365 50  HOH   HOH A . 
G 5 HOH   66  366 19  HOH   HOH A . 
G 5 HOH   67  367 268 HOH   HOH A . 
G 5 HOH   68  368 287 HOH   HOH A . 
G 5 HOH   69  369 267 HOH   HOH A . 
G 5 HOH   70  370 177 HOH   HOH A . 
G 5 HOH   71  371 83  HOH   HOH A . 
G 5 HOH   72  372 84  HOH   HOH A . 
G 5 HOH   73  373 126 HOH   HOH A . 
G 5 HOH   74  374 52  HOH   HOH A . 
G 5 HOH   75  375 260 HOH   HOH A . 
G 5 HOH   76  376 106 HOH   HOH A . 
G 5 HOH   77  377 12  HOH   HOH A . 
G 5 HOH   78  378 11  HOH   HOH A . 
G 5 HOH   79  379 60  HOH   HOH A . 
G 5 HOH   80  380 102 HOH   HOH A . 
G 5 HOH   81  381 27  HOH   HOH A . 
G 5 HOH   82  382 216 HOH   HOH A . 
G 5 HOH   83  383 39  HOH   HOH A . 
G 5 HOH   84  384 62  HOH   HOH A . 
G 5 HOH   85  385 8   HOH   HOH A . 
G 5 HOH   86  386 274 HOH   HOH A . 
G 5 HOH   87  387 265 HOH   HOH A . 
G 5 HOH   88  388 95  HOH   HOH A . 
G 5 HOH   89  389 203 HOH   HOH A . 
G 5 HOH   90  390 51  HOH   HOH A . 
G 5 HOH   91  391 255 HOH   HOH A . 
G 5 HOH   92  392 148 HOH   HOH A . 
G 5 HOH   93  393 93  HOH   HOH A . 
G 5 HOH   94  394 174 HOH   HOH A . 
G 5 HOH   95  395 35  HOH   HOH A . 
G 5 HOH   96  396 231 HOH   HOH A . 
G 5 HOH   97  397 96  HOH   HOH A . 
G 5 HOH   98  398 40  HOH   HOH A . 
G 5 HOH   99  399 176 HOH   HOH A . 
G 5 HOH   100 400 23  HOH   HOH A . 
G 5 HOH   101 401 89  HOH   HOH A . 
G 5 HOH   102 402 168 HOH   HOH A . 
G 5 HOH   103 403 270 HOH   HOH A . 
G 5 HOH   104 404 159 HOH   HOH A . 
G 5 HOH   105 405 10  HOH   HOH A . 
G 5 HOH   106 406 123 HOH   HOH A . 
G 5 HOH   107 407 76  HOH   HOH A . 
G 5 HOH   108 408 90  HOH   HOH A . 
G 5 HOH   109 409 38  HOH   HOH A . 
G 5 HOH   110 410 285 HOH   HOH A . 
G 5 HOH   111 411 284 HOH   HOH A . 
G 5 HOH   112 412 80  HOH   HOH A . 
G 5 HOH   113 413 253 HOH   HOH A . 
G 5 HOH   114 414 175 HOH   HOH A . 
G 5 HOH   115 415 248 HOH   HOH A . 
G 5 HOH   116 416 258 HOH   HOH A . 
G 5 HOH   117 417 233 HOH   HOH A . 
G 5 HOH   118 418 155 HOH   HOH A . 
G 5 HOH   119 419 201 HOH   HOH A . 
G 5 HOH   120 420 136 HOH   HOH A . 
G 5 HOH   121 421 158 HOH   HOH A . 
G 5 HOH   122 422 128 HOH   HOH A . 
G 5 HOH   123 423 69  HOH   HOH A . 
G 5 HOH   124 424 207 HOH   HOH A . 
G 5 HOH   125 425 280 HOH   HOH A . 
G 5 HOH   126 426 215 HOH   HOH A . 
G 5 HOH   127 427 138 HOH   HOH A . 
G 5 HOH   128 428 229 HOH   HOH A . 
G 5 HOH   129 429 152 HOH   HOH A . 
G 5 HOH   130 430 288 HOH   HOH A . 
G 5 HOH   131 431 213 HOH   HOH A . 
G 5 HOH   132 432 171 HOH   HOH A . 
G 5 HOH   133 433 99  HOH   HOH A . 
G 5 HOH   134 434 112 HOH   HOH A . 
G 5 HOH   135 435 91  HOH   HOH A . 
G 5 HOH   136 436 277 HOH   HOH A . 
G 5 HOH   137 437 92  HOH   HOH A . 
G 5 HOH   138 438 276 HOH   HOH A . 
G 5 HOH   139 439 134 HOH   HOH A . 
G 5 HOH   140 440 190 HOH   HOH A . 
G 5 HOH   141 441 282 HOH   HOH A . 
G 5 HOH   142 442 279 HOH   HOH A . 
G 5 HOH   143 443 281 HOH   HOH A . 
G 5 HOH   144 444 86  HOH   HOH A . 
G 5 HOH   145 445 61  HOH   HOH A . 
G 5 HOH   146 446 283 HOH   HOH A . 
G 5 HOH   147 447 113 HOH   HOH A . 
G 5 HOH   148 448 56  HOH   HOH A . 
G 5 HOH   149 449 242 HOH   HOH A . 
G 5 HOH   150 450 122 HOH   HOH A . 
G 5 HOH   151 451 153 HOH   HOH A . 
G 5 HOH   152 452 209 HOH   HOH A . 
G 5 HOH   153 453 156 HOH   HOH A . 
G 5 HOH   154 454 208 HOH   HOH A . 
G 5 HOH   155 455 221 HOH   HOH A . 
G 5 HOH   156 456 278 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           7I68 
_cell.length_a           88.440 
_cell.length_b           57.330 
_cell.length_c           32.450 
_cell.angle_alpha        90.00 
_cell.angle_beta         91.52 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I68 
_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          7I68 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.59 
_exptl_crystal.density_percent_sol   52.46 
_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                     7I68 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             28.67 
_reflns.d_resolution_high            1.65 
_reflns.number_obs                   19533 
_reflns.percent_possible_obs         99.8 
_reflns.pdbx_Rmerge_I_obs            0.121 
_reflns.pdbx_netI_over_sigmaI        7.5 
_reflns.pdbx_redundancy              5.9 
_reflns.pdbx_Rrim_I_all              0.132 
_reflns.pdbx_Rpim_I_all              0.052 
_reflns.pdbx_CC_half                 0.995 
_reflns.pdbx_number_measured_all     116194 
_reflns.pdbx_chi_squared             0.98 
_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                  1.65 
_reflns_shell.d_res_low                   1.69 
_reflns_shell.number_measured_all         7276 
_reflns_shell.number_unique_obs           1444 
_reflns_shell.Rmerge_I_obs                1.618 
_reflns_shell.pdbx_chi_squared            0.71 
_reflns_shell.pdbx_redundancy             5.0 
_reflns_shell.percent_possible_obs        99.7 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.9 
_reflns_shell.pdbx_Rrim_I_all             1.804 
_reflns_shell.pdbx_Rpim_I_all             0.784 
_reflns_shell.pdbx_CC_half                0.406 
_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                                 7I68 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     19530 
_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                             28.66 
_refine.ls_d_res_high                            1.650 
_refine.ls_percent_reflns_obs                    99.7 
_refine.ls_R_factor_obs                          0.1980 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1960 
_refine.ls_R_factor_R_free                       0.2349 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.020 
_refine.ls_number_reflns_R_free                  980 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.965 
_refine.correlation_coeff_Fo_to_Fc_free          0.951 
_refine.B_iso_mean                               32.72 
_refine.aniso_B[1][1]                            -2.41110 
_refine.aniso_B[2][2]                            -0.78150 
_refine.aniso_B[3][3]                            3.19260 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -0.12200 
_refine.aniso_B[2][3]                            0.00000 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             0.096 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.099 
_refine.pdbx_overall_SU_R_Blow_DPI               0.102 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.103 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7I68 
_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         31 
_refine_hist.number_atoms_solvent             156 
_refine_hist.number_atoms_total               1261 
_refine_hist.d_res_high                       1.650 
_refine_hist.d_res_low                        28.66 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
t_bond_d                  0.010 ? 2.00  1139 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               0.97  ? 2.00  1549 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  378  '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  205  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1139 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           4.01  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           16.17 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  139  '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  1156 'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   50 
_refine_ls_shell.d_res_high                       1.65 
_refine_ls_shell.d_res_low                        1.66 
_refine_ls_shell.number_reflns_R_work             383 
_refine_ls_shell.R_factor_R_work                  0.3204 
_refine_ls_shell.percent_reflns_obs               98.53 
_refine_ls_shell.R_factor_R_free                  0.3680 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            4.01 
_refine_ls_shell.number_reflns_R_free             16 
_refine_ls_shell.number_reflns_all                399 
_refine_ls_shell.R_factor_all                     0.3223 
# 
_struct.entry_id                  7I68 
_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-0037630-001 (A71EV2A-x4928)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I68 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 4 ? 
F N N 4 ? 
G 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              7I68 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 144 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q65900 
_struct_ref_seq.db_align_beg                  869 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1012 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       7 
_struct_ref_seq.pdbx_auth_seq_align_end       150 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_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 ? ? ? ? ? ? ? 2.340 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.363 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.270 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 C ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.061 ? ? 
# 
_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_555 110.2 ? 
2 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 109.4 ? 
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_555 116.6 ? 
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_555 104.9 ? 
5 SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 100.2 ? 
6 SG ? A CYS 110 ? A CYS 116 ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 114.8 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA1 2 LEU A 34  ? CYS A 44  ? LEU A 40  CYS A 50  
AA1 3 ILE A 4   ? ASN A 13  ? ILE A 10  ASN A 19  
AA2 1 LYS A 64  ? SER A 69  ? LYS A 70  SER A 75  
AA2 2 THR A 54  ? CYS A 59  ? THR A 60  CYS A 65  
AA2 3 ILE A 107 ? CYS A 110 ? ILE A 113 CYS A 116 
AA2 4 GLY A 113 ? GLY A 122 ? GLY A 119 GLY A 128 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 26  ? N VAL A 32  O VAL A 36  ? O VAL A 42  
AA1 2 3 N LEU A 35  ? N LEU A 41  O VAL A 12  ? O VAL A 18  
AA2 1 2 O LYS A 64  ? O LYS A 70  N CYS A 59  ? N CYS A 65  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N LEU A 108 ? N LEU A 114 O VAL A 115 ? O VAL A 121 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O 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                   7I68 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 14  ? ? -102.38 40.31  
2 1 SER A 125 ? ? -135.96 -32.40 
# 
_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         15.3779 
_pdbx_refine_tls.origin_y         7.5313 
_pdbx_refine_tls.origin_z         13.5272 
_pdbx_refine_tls.T[1][1]          -0.0661 
_pdbx_refine_tls.T[2][2]          -0.0315 
_pdbx_refine_tls.T[3][3]          0.0386 
_pdbx_refine_tls.T[1][2]          -0.0143 
_pdbx_refine_tls.T[1][3]          -0.0192 
_pdbx_refine_tls.T[2][3]          0.0060 
_pdbx_refine_tls.L[1][1]          1.2094 
_pdbx_refine_tls.L[2][2]          3.2319 
_pdbx_refine_tls.L[3][3]          0.3498 
_pdbx_refine_tls.L[1][2]          0.7909 
_pdbx_refine_tls.L[1][3]          -0.5903 
_pdbx_refine_tls.L[2][3]          -1.1856 
_pdbx_refine_tls.S[1][1]          -0.0554 
_pdbx_refine_tls.S[1][2]          0.0074 
_pdbx_refine_tls.S[1][3]          0.1003 
_pdbx_refine_tls.S[2][1]          0.0825 
_pdbx_refine_tls.S[2][2]          -0.0180 
_pdbx_refine_tls.S[2][3]          -0.1305 
_pdbx_refine_tls.S[3][1]          -0.0107 
_pdbx_refine_tls.S[3][2]          -0.0349 
_pdbx_refine_tls.S[3][3]          0.0734 
# 
_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 
A1B4F N1   N  N N 1   
A1B4F C4   C  Y N 2   
A1B4F C5   C  Y N 3   
A1B4F C6   C  N N 4   
A1B4F C7   C  N N 5   
A1B4F C8   C  N S 6   
A1B4F C10  C  N N 7   
A1B4F C13  C  Y N 8   
A1B4F O1   O  N N 9   
A1B4F C12  C  N N 10  
A1B4F C11  C  N N 11  
A1B4F C9   C  N N 12  
A1B4F O    O  N N 13  
A1B4F N    N  N N 14  
A1B4F C3   C  Y N 15  
A1B4F C2   C  Y N 16  
A1B4F C1   C  Y N 17  
A1B4F C    C  N N 18  
A1B4F H12  H  N N 19  
A1B4F H11  H  N N 20  
A1B4F H6   H  N N 21  
A1B4F H8   H  N N 22  
A1B4F H7   H  N N 23  
A1B4F H10  H  N N 24  
A1B4F H9   H  N N 25  
A1B4F H    H  N N 26  
A1B4F H14  H  N N 27  
A1B4F H13  H  N N 28  
A1B4F H17  H  N N 29  
A1B4F H16  H  N N 30  
A1B4F H15  H  N N 31  
A1B4F H5   H  N N 32  
A1B4F H4   H  N N 33  
A1B4F H2   H  N N 34  
A1B4F H3   H  N N 35  
A1B4F H1   H  N N 36  
ALA   N    N  N N 37  
ALA   CA   C  N S 38  
ALA   C    C  N N 39  
ALA   O    O  N N 40  
ALA   CB   C  N N 41  
ALA   OXT  O  N N 42  
ALA   H    H  N N 43  
ALA   H2   H  N N 44  
ALA   HA   H  N N 45  
ALA   HB1  H  N N 46  
ALA   HB2  H  N N 47  
ALA   HB3  H  N N 48  
ALA   HXT  H  N N 49  
ARG   N    N  N N 50  
ARG   CA   C  N S 51  
ARG   C    C  N N 52  
ARG   O    O  N N 53  
ARG   CB   C  N N 54  
ARG   CG   C  N N 55  
ARG   CD   C  N N 56  
ARG   NE   N  N N 57  
ARG   CZ   C  N N 58  
ARG   NH1  N  N N 59  
ARG   NH2  N  N N 60  
ARG   OXT  O  N N 61  
ARG   H    H  N N 62  
ARG   H2   H  N N 63  
ARG   HA   H  N N 64  
ARG   HB2  H  N N 65  
ARG   HB3  H  N N 66  
ARG   HG2  H  N N 67  
ARG   HG3  H  N N 68  
ARG   HD2  H  N N 69  
ARG   HD3  H  N N 70  
ARG   HE   H  N N 71  
ARG   HH11 H  N N 72  
ARG   HH12 H  N N 73  
ARG   HH21 H  N N 74  
ARG   HH22 H  N N 75  
ARG   HXT  H  N N 76  
ASN   N    N  N N 77  
ASN   CA   C  N S 78  
ASN   C    C  N N 79  
ASN   O    O  N N 80  
ASN   CB   C  N N 81  
ASN   CG   C  N N 82  
ASN   OD1  O  N N 83  
ASN   ND2  N  N N 84  
ASN   OXT  O  N N 85  
ASN   H    H  N N 86  
ASN   H2   H  N N 87  
ASN   HA   H  N N 88  
ASN   HB2  H  N N 89  
ASN   HB3  H  N N 90  
ASN   HD21 H  N N 91  
ASN   HD22 H  N N 92  
ASN   HXT  H  N N 93  
ASP   N    N  N N 94  
ASP   CA   C  N S 95  
ASP   C    C  N N 96  
ASP   O    O  N N 97  
ASP   CB   C  N N 98  
ASP   CG   C  N N 99  
ASP   OD1  O  N N 100 
ASP   OD2  O  N N 101 
ASP   OXT  O  N N 102 
ASP   H    H  N N 103 
ASP   H2   H  N N 104 
ASP   HA   H  N N 105 
ASP   HB2  H  N N 106 
ASP   HB3  H  N N 107 
ASP   HD2  H  N N 108 
ASP   HXT  H  N N 109 
CYS   N    N  N N 110 
CYS   CA   C  N R 111 
CYS   C    C  N N 112 
CYS   O    O  N N 113 
CYS   CB   C  N N 114 
CYS   SG   S  N N 115 
CYS   OXT  O  N N 116 
CYS   H    H  N N 117 
CYS   H2   H  N N 118 
CYS   HA   H  N N 119 
CYS   HB2  H  N N 120 
CYS   HB3  H  N N 121 
CYS   HG   H  N N 122 
CYS   HXT  H  N N 123 
DMS   S    S  N N 124 
DMS   O    O  N N 125 
DMS   C1   C  N N 126 
DMS   C2   C  N N 127 
DMS   H11  H  N N 128 
DMS   H12  H  N N 129 
DMS   H13  H  N N 130 
DMS   H21  H  N N 131 
DMS   H22  H  N N 132 
DMS   H23  H  N N 133 
GLN   N    N  N N 134 
GLN   CA   C  N S 135 
GLN   C    C  N N 136 
GLN   O    O  N N 137 
GLN   CB   C  N N 138 
GLN   CG   C  N N 139 
GLN   CD   C  N N 140 
GLN   OE1  O  N N 141 
GLN   NE2  N  N N 142 
GLN   OXT  O  N N 143 
GLN   H    H  N N 144 
GLN   H2   H  N N 145 
GLN   HA   H  N N 146 
GLN   HB2  H  N N 147 
GLN   HB3  H  N N 148 
GLN   HG2  H  N N 149 
GLN   HG3  H  N N 150 
GLN   HE21 H  N N 151 
GLN   HE22 H  N N 152 
GLN   HXT  H  N N 153 
GLU   N    N  N N 154 
GLU   CA   C  N S 155 
GLU   C    C  N N 156 
GLU   O    O  N N 157 
GLU   CB   C  N N 158 
GLU   CG   C  N N 159 
GLU   CD   C  N N 160 
GLU   OE1  O  N N 161 
GLU   OE2  O  N N 162 
GLU   OXT  O  N N 163 
GLU   H    H  N N 164 
GLU   H2   H  N N 165 
GLU   HA   H  N N 166 
GLU   HB2  H  N N 167 
GLU   HB3  H  N N 168 
GLU   HG2  H  N N 169 
GLU   HG3  H  N N 170 
GLU   HE2  H  N N 171 
GLU   HXT  H  N N 172 
GLY   N    N  N N 173 
GLY   CA   C  N N 174 
GLY   C    C  N N 175 
GLY   O    O  N N 176 
GLY   OXT  O  N N 177 
GLY   H    H  N N 178 
GLY   H2   H  N N 179 
GLY   HA2  H  N N 180 
GLY   HA3  H  N N 181 
GLY   HXT  H  N N 182 
HIS   N    N  N N 183 
HIS   CA   C  N S 184 
HIS   C    C  N N 185 
HIS   O    O  N N 186 
HIS   CB   C  N N 187 
HIS   CG   C  Y N 188 
HIS   ND1  N  Y N 189 
HIS   CD2  C  Y N 190 
HIS   CE1  C  Y N 191 
HIS   NE2  N  Y N 192 
HIS   OXT  O  N N 193 
HIS   H    H  N N 194 
HIS   H2   H  N N 195 
HIS   HA   H  N N 196 
HIS   HB2  H  N N 197 
HIS   HB3  H  N N 198 
HIS   HD1  H  N N 199 
HIS   HD2  H  N N 200 
HIS   HE1  H  N N 201 
HIS   HE2  H  N N 202 
HIS   HXT  H  N N 203 
HOH   O    O  N N 204 
HOH   H1   H  N N 205 
HOH   H2   H  N N 206 
ILE   N    N  N N 207 
ILE   CA   C  N S 208 
ILE   C    C  N N 209 
ILE   O    O  N N 210 
ILE   CB   C  N S 211 
ILE   CG1  C  N N 212 
ILE   CG2  C  N N 213 
ILE   CD1  C  N N 214 
ILE   OXT  O  N N 215 
ILE   H    H  N N 216 
ILE   H2   H  N N 217 
ILE   HA   H  N N 218 
ILE   HB   H  N N 219 
ILE   HG12 H  N N 220 
ILE   HG13 H  N N 221 
ILE   HG21 H  N N 222 
ILE   HG22 H  N N 223 
ILE   HG23 H  N N 224 
ILE   HD11 H  N N 225 
ILE   HD12 H  N N 226 
ILE   HD13 H  N N 227 
ILE   HXT  H  N N 228 
LEU   N    N  N N 229 
LEU   CA   C  N S 230 
LEU   C    C  N N 231 
LEU   O    O  N N 232 
LEU   CB   C  N N 233 
LEU   CG   C  N N 234 
LEU   CD1  C  N N 235 
LEU   CD2  C  N N 236 
LEU   OXT  O  N N 237 
LEU   H    H  N N 238 
LEU   H2   H  N N 239 
LEU   HA   H  N N 240 
LEU   HB2  H  N N 241 
LEU   HB3  H  N N 242 
LEU   HG   H  N N 243 
LEU   HD11 H  N N 244 
LEU   HD12 H  N N 245 
LEU   HD13 H  N N 246 
LEU   HD21 H  N N 247 
LEU   HD22 H  N N 248 
LEU   HD23 H  N N 249 
LEU   HXT  H  N N 250 
LYS   N    N  N N 251 
LYS   CA   C  N S 252 
LYS   C    C  N N 253 
LYS   O    O  N N 254 
LYS   CB   C  N N 255 
LYS   CG   C  N N 256 
LYS   CD   C  N N 257 
LYS   CE   C  N N 258 
LYS   NZ   N  N N 259 
LYS   OXT  O  N N 260 
LYS   H    H  N N 261 
LYS   H2   H  N N 262 
LYS   HA   H  N N 263 
LYS   HB2  H  N N 264 
LYS   HB3  H  N N 265 
LYS   HG2  H  N N 266 
LYS   HG3  H  N N 267 
LYS   HD2  H  N N 268 
LYS   HD3  H  N N 269 
LYS   HE2  H  N N 270 
LYS   HE3  H  N N 271 
LYS   HZ1  H  N N 272 
LYS   HZ2  H  N N 273 
LYS   HZ3  H  N N 274 
LYS   HXT  H  N N 275 
MET   N    N  N N 276 
MET   CA   C  N S 277 
MET   C    C  N N 278 
MET   O    O  N N 279 
MET   CB   C  N N 280 
MET   CG   C  N N 281 
MET   SD   S  N N 282 
MET   CE   C  N N 283 
MET   OXT  O  N N 284 
MET   H    H  N N 285 
MET   H2   H  N N 286 
MET   HA   H  N N 287 
MET   HB2  H  N N 288 
MET   HB3  H  N N 289 
MET   HG2  H  N N 290 
MET   HG3  H  N N 291 
MET   HE1  H  N N 292 
MET   HE2  H  N N 293 
MET   HE3  H  N N 294 
MET   HXT  H  N N 295 
PHE   N    N  N N 296 
PHE   CA   C  N S 297 
PHE   C    C  N N 298 
PHE   O    O  N N 299 
PHE   CB   C  N N 300 
PHE   CG   C  Y N 301 
PHE   CD1  C  Y N 302 
PHE   CD2  C  Y N 303 
PHE   CE1  C  Y N 304 
PHE   CE2  C  Y N 305 
PHE   CZ   C  Y N 306 
PHE   OXT  O  N N 307 
PHE   H    H  N N 308 
PHE   H2   H  N N 309 
PHE   HA   H  N N 310 
PHE   HB2  H  N N 311 
PHE   HB3  H  N N 312 
PHE   HD1  H  N N 313 
PHE   HD2  H  N N 314 
PHE   HE1  H  N N 315 
PHE   HE2  H  N N 316 
PHE   HZ   H  N N 317 
PHE   HXT  H  N N 318 
PRO   N    N  N N 319 
PRO   CA   C  N S 320 
PRO   C    C  N N 321 
PRO   O    O  N N 322 
PRO   CB   C  N N 323 
PRO   CG   C  N N 324 
PRO   CD   C  N N 325 
PRO   OXT  O  N N 326 
PRO   H    H  N N 327 
PRO   HA   H  N N 328 
PRO   HB2  H  N N 329 
PRO   HB3  H  N N 330 
PRO   HG2  H  N N 331 
PRO   HG3  H  N N 332 
PRO   HD2  H  N N 333 
PRO   HD3  H  N N 334 
PRO   HXT  H  N N 335 
SER   N    N  N N 336 
SER   CA   C  N S 337 
SER   C    C  N N 338 
SER   O    O  N N 339 
SER   CB   C  N N 340 
SER   OG   O  N N 341 
SER   OXT  O  N N 342 
SER   H    H  N N 343 
SER   H2   H  N N 344 
SER   HA   H  N N 345 
SER   HB2  H  N N 346 
SER   HB3  H  N N 347 
SER   HG   H  N N 348 
SER   HXT  H  N N 349 
THR   N    N  N N 350 
THR   CA   C  N S 351 
THR   C    C  N N 352 
THR   O    O  N N 353 
THR   CB   C  N R 354 
THR   OG1  O  N N 355 
THR   CG2  C  N N 356 
THR   OXT  O  N N 357 
THR   H    H  N N 358 
THR   H2   H  N N 359 
THR   HA   H  N N 360 
THR   HB   H  N N 361 
THR   HG1  H  N N 362 
THR   HG21 H  N N 363 
THR   HG22 H  N N 364 
THR   HG23 H  N N 365 
THR   HXT  H  N N 366 
TRP   N    N  N N 367 
TRP   CA   C  N S 368 
TRP   C    C  N N 369 
TRP   O    O  N N 370 
TRP   CB   C  N N 371 
TRP   CG   C  Y N 372 
TRP   CD1  C  Y N 373 
TRP   CD2  C  Y N 374 
TRP   NE1  N  Y N 375 
TRP   CE2  C  Y N 376 
TRP   CE3  C  Y N 377 
TRP   CZ2  C  Y N 378 
TRP   CZ3  C  Y N 379 
TRP   CH2  C  Y N 380 
TRP   OXT  O  N N 381 
TRP   H    H  N N 382 
TRP   H2   H  N N 383 
TRP   HA   H  N N 384 
TRP   HB2  H  N N 385 
TRP   HB3  H  N N 386 
TRP   HD1  H  N N 387 
TRP   HE1  H  N N 388 
TRP   HE3  H  N N 389 
TRP   HZ2  H  N N 390 
TRP   HZ3  H  N N 391 
TRP   HH2  H  N N 392 
TRP   HXT  H  N N 393 
TYR   N    N  N N 394 
TYR   CA   C  N S 395 
TYR   C    C  N N 396 
TYR   O    O  N N 397 
TYR   CB   C  N N 398 
TYR   CG   C  Y N 399 
TYR   CD1  C  Y N 400 
TYR   CD2  C  Y N 401 
TYR   CE1  C  Y N 402 
TYR   CE2  C  Y N 403 
TYR   CZ   C  Y N 404 
TYR   OH   O  N N 405 
TYR   OXT  O  N N 406 
TYR   H    H  N N 407 
TYR   H2   H  N N 408 
TYR   HA   H  N N 409 
TYR   HB2  H  N N 410 
TYR   HB3  H  N N 411 
TYR   HD1  H  N N 412 
TYR   HD2  H  N N 413 
TYR   HE1  H  N N 414 
TYR   HE2  H  N N 415 
TYR   HH   H  N N 416 
TYR   HXT  H  N N 417 
VAL   N    N  N N 418 
VAL   CA   C  N S 419 
VAL   C    C  N N 420 
VAL   O    O  N N 421 
VAL   CB   C  N N 422 
VAL   CG1  C  N N 423 
VAL   CG2  C  N N 424 
VAL   OXT  O  N N 425 
VAL   H    H  N N 426 
VAL   H2   H  N N 427 
VAL   HA   H  N N 428 
VAL   HB   H  N N 429 
VAL   HG11 H  N N 430 
VAL   HG12 H  N N 431 
VAL   HG13 H  N N 432 
VAL   HG21 H  N N 433 
VAL   HG22 H  N N 434 
VAL   HG23 H  N N 435 
VAL   HXT  H  N N 436 
ZN    ZN   ZN N N 437 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1B4F C   C1   sing N N 1   
A1B4F C1  C2   sing Y N 2   
A1B4F C2  C3   doub Y N 3   
A1B4F C3  C4   sing Y N 4   
A1B4F C4  C5   doub Y N 5   
A1B4F C5  C6   sing N N 6   
A1B4F C6  N    sing N N 7   
A1B4F N   C7   sing N N 8   
A1B4F C7  C8   sing N N 9   
A1B4F C9  C8   sing N N 10  
A1B4F N1  C9   sing N N 11  
A1B4F O   C9   doub N N 12  
A1B4F C8  C10  sing N N 13  
A1B4F C10 C11  sing N N 14  
A1B4F C11 C12  sing N N 15  
A1B4F N   C12  sing N N 16  
A1B4F C12 O1   doub N N 17  
A1B4F C13 C5   sing Y N 18  
A1B4F C1  C13  doub Y N 19  
A1B4F N1  H12  sing N N 20  
A1B4F N1  H11  sing N N 21  
A1B4F C4  H6   sing N N 22  
A1B4F C6  H8   sing N N 23  
A1B4F C6  H7   sing N N 24  
A1B4F C7  H10  sing N N 25  
A1B4F C7  H9   sing N N 26  
A1B4F C8  H    sing N N 27  
A1B4F C10 H14  sing N N 28  
A1B4F C10 H13  sing N N 29  
A1B4F C13 H17  sing N N 30  
A1B4F C11 H16  sing N N 31  
A1B4F C11 H15  sing N N 32  
A1B4F C3  H5   sing N N 33  
A1B4F C2  H4   sing N N 34  
A1B4F C   H2   sing N N 35  
A1B4F C   H3   sing N N 36  
A1B4F C   H1   sing N N 37  
ALA   N   CA   sing N N 38  
ALA   N   H    sing N N 39  
ALA   N   H2   sing N N 40  
ALA   CA  C    sing N N 41  
ALA   CA  CB   sing N N 42  
ALA   CA  HA   sing N N 43  
ALA   C   O    doub N N 44  
ALA   C   OXT  sing N N 45  
ALA   CB  HB1  sing N N 46  
ALA   CB  HB2  sing N N 47  
ALA   CB  HB3  sing N N 48  
ALA   OXT HXT  sing N N 49  
ARG   N   CA   sing N N 50  
ARG   N   H    sing N N 51  
ARG   N   H2   sing N N 52  
ARG   CA  C    sing N N 53  
ARG   CA  CB   sing N N 54  
ARG   CA  HA   sing N N 55  
ARG   C   O    doub N N 56  
ARG   C   OXT  sing N N 57  
ARG   CB  CG   sing N N 58  
ARG   CB  HB2  sing N N 59  
ARG   CB  HB3  sing N N 60  
ARG   CG  CD   sing N N 61  
ARG   CG  HG2  sing N N 62  
ARG   CG  HG3  sing N N 63  
ARG   CD  NE   sing N N 64  
ARG   CD  HD2  sing N N 65  
ARG   CD  HD3  sing N N 66  
ARG   NE  CZ   sing N N 67  
ARG   NE  HE   sing N N 68  
ARG   CZ  NH1  sing N N 69  
ARG   CZ  NH2  doub N N 70  
ARG   NH1 HH11 sing N N 71  
ARG   NH1 HH12 sing N N 72  
ARG   NH2 HH21 sing N N 73  
ARG   NH2 HH22 sing N N 74  
ARG   OXT HXT  sing N N 75  
ASN   N   CA   sing N N 76  
ASN   N   H    sing N N 77  
ASN   N   H2   sing N N 78  
ASN   CA  C    sing N N 79  
ASN   CA  CB   sing N N 80  
ASN   CA  HA   sing N N 81  
ASN   C   O    doub N N 82  
ASN   C   OXT  sing N N 83  
ASN   CB  CG   sing N N 84  
ASN   CB  HB2  sing N N 85  
ASN   CB  HB3  sing N N 86  
ASN   CG  OD1  doub N N 87  
ASN   CG  ND2  sing N N 88  
ASN   ND2 HD21 sing N N 89  
ASN   ND2 HD22 sing N N 90  
ASN   OXT HXT  sing N N 91  
ASP   N   CA   sing N N 92  
ASP   N   H    sing N N 93  
ASP   N   H2   sing N N 94  
ASP   CA  C    sing N N 95  
ASP   CA  CB   sing N N 96  
ASP   CA  HA   sing N N 97  
ASP   C   O    doub N N 98  
ASP   C   OXT  sing N N 99  
ASP   CB  CG   sing N N 100 
ASP   CB  HB2  sing N N 101 
ASP   CB  HB3  sing N N 102 
ASP   CG  OD1  doub N N 103 
ASP   CG  OD2  sing N N 104 
ASP   OD2 HD2  sing N N 105 
ASP   OXT HXT  sing N N 106 
CYS   N   CA   sing N N 107 
CYS   N   H    sing N N 108 
CYS   N   H2   sing N N 109 
CYS   CA  C    sing N N 110 
CYS   CA  CB   sing N N 111 
CYS   CA  HA   sing N N 112 
CYS   C   O    doub N N 113 
CYS   C   OXT  sing N N 114 
CYS   CB  SG   sing N N 115 
CYS   CB  HB2  sing N N 116 
CYS   CB  HB3  sing N N 117 
CYS   SG  HG   sing N N 118 
CYS   OXT HXT  sing N N 119 
DMS   S   O    doub N N 120 
DMS   S   C1   sing N N 121 
DMS   S   C2   sing N N 122 
DMS   C1  H11  sing N N 123 
DMS   C1  H12  sing N N 124 
DMS   C1  H13  sing N N 125 
DMS   C2  H21  sing N N 126 
DMS   C2  H22  sing N N 127 
DMS   C2  H23  sing N N 128 
GLN   N   CA   sing N N 129 
GLN   N   H    sing N N 130 
GLN   N   H2   sing N N 131 
GLN   CA  C    sing N N 132 
GLN   CA  CB   sing N N 133 
GLN   CA  HA   sing N N 134 
GLN   C   O    doub N N 135 
GLN   C   OXT  sing N N 136 
GLN   CB  CG   sing N N 137 
GLN   CB  HB2  sing N N 138 
GLN   CB  HB3  sing N N 139 
GLN   CG  CD   sing N N 140 
GLN   CG  HG2  sing N N 141 
GLN   CG  HG3  sing N N 142 
GLN   CD  OE1  doub N N 143 
GLN   CD  NE2  sing N N 144 
GLN   NE2 HE21 sing N N 145 
GLN   NE2 HE22 sing N N 146 
GLN   OXT HXT  sing N N 147 
GLU   N   CA   sing N N 148 
GLU   N   H    sing N N 149 
GLU   N   H2   sing N N 150 
GLU   CA  C    sing N N 151 
GLU   CA  CB   sing N N 152 
GLU   CA  HA   sing N N 153 
GLU   C   O    doub N N 154 
GLU   C   OXT  sing N N 155 
GLU   CB  CG   sing N N 156 
GLU   CB  HB2  sing N N 157 
GLU   CB  HB3  sing N N 158 
GLU   CG  CD   sing N N 159 
GLU   CG  HG2  sing N N 160 
GLU   CG  HG3  sing N N 161 
GLU   CD  OE1  doub N N 162 
GLU   CD  OE2  sing N N 163 
GLU   OE2 HE2  sing N N 164 
GLU   OXT HXT  sing N N 165 
GLY   N   CA   sing N N 166 
GLY   N   H    sing N N 167 
GLY   N   H2   sing N N 168 
GLY   CA  C    sing N N 169 
GLY   CA  HA2  sing N N 170 
GLY   CA  HA3  sing N N 171 
GLY   C   O    doub N N 172 
GLY   C   OXT  sing N N 173 
GLY   OXT HXT  sing N N 174 
HIS   N   CA   sing N N 175 
HIS   N   H    sing N N 176 
HIS   N   H2   sing N N 177 
HIS   CA  C    sing N N 178 
HIS   CA  CB   sing N N 179 
HIS   CA  HA   sing N N 180 
HIS   C   O    doub N N 181 
HIS   C   OXT  sing N N 182 
HIS   CB  CG   sing N N 183 
HIS   CB  HB2  sing N N 184 
HIS   CB  HB3  sing N N 185 
HIS   CG  ND1  sing Y N 186 
HIS   CG  CD2  doub Y N 187 
HIS   ND1 CE1  doub Y N 188 
HIS   ND1 HD1  sing N N 189 
HIS   CD2 NE2  sing Y N 190 
HIS   CD2 HD2  sing N N 191 
HIS   CE1 NE2  sing Y N 192 
HIS   CE1 HE1  sing N N 193 
HIS   NE2 HE2  sing N N 194 
HIS   OXT HXT  sing N N 195 
HOH   O   H1   sing N N 196 
HOH   O   H2   sing N N 197 
ILE   N   CA   sing N N 198 
ILE   N   H    sing N N 199 
ILE   N   H2   sing N N 200 
ILE   CA  C    sing N N 201 
ILE   CA  CB   sing N N 202 
ILE   CA  HA   sing N N 203 
ILE   C   O    doub N N 204 
ILE   C   OXT  sing N N 205 
ILE   CB  CG1  sing N N 206 
ILE   CB  CG2  sing N N 207 
ILE   CB  HB   sing N N 208 
ILE   CG1 CD1  sing N N 209 
ILE   CG1 HG12 sing N N 210 
ILE   CG1 HG13 sing N N 211 
ILE   CG2 HG21 sing N N 212 
ILE   CG2 HG22 sing N N 213 
ILE   CG2 HG23 sing N N 214 
ILE   CD1 HD11 sing N N 215 
ILE   CD1 HD12 sing N N 216 
ILE   CD1 HD13 sing N N 217 
ILE   OXT HXT  sing N N 218 
LEU   N   CA   sing N N 219 
LEU   N   H    sing N N 220 
LEU   N   H2   sing N N 221 
LEU   CA  C    sing N N 222 
LEU   CA  CB   sing N N 223 
LEU   CA  HA   sing N N 224 
LEU   C   O    doub N N 225 
LEU   C   OXT  sing N N 226 
LEU   CB  CG   sing N N 227 
LEU   CB  HB2  sing N N 228 
LEU   CB  HB3  sing N N 229 
LEU   CG  CD1  sing N N 230 
LEU   CG  CD2  sing N N 231 
LEU   CG  HG   sing N N 232 
LEU   CD1 HD11 sing N N 233 
LEU   CD1 HD12 sing N N 234 
LEU   CD1 HD13 sing N N 235 
LEU   CD2 HD21 sing N N 236 
LEU   CD2 HD22 sing N N 237 
LEU   CD2 HD23 sing N N 238 
LEU   OXT HXT  sing N N 239 
LYS   N   CA   sing N N 240 
LYS   N   H    sing N N 241 
LYS   N   H2   sing N N 242 
LYS   CA  C    sing N N 243 
LYS   CA  CB   sing N N 244 
LYS   CA  HA   sing N N 245 
LYS   C   O    doub N N 246 
LYS   C   OXT  sing N N 247 
LYS   CB  CG   sing N N 248 
LYS   CB  HB2  sing N N 249 
LYS   CB  HB3  sing N N 250 
LYS   CG  CD   sing N N 251 
LYS   CG  HG2  sing N N 252 
LYS   CG  HG3  sing N N 253 
LYS   CD  CE   sing N N 254 
LYS   CD  HD2  sing N N 255 
LYS   CD  HD3  sing N N 256 
LYS   CE  NZ   sing N N 257 
LYS   CE  HE2  sing N N 258 
LYS   CE  HE3  sing N N 259 
LYS   NZ  HZ1  sing N N 260 
LYS   NZ  HZ2  sing N N 261 
LYS   NZ  HZ3  sing N N 262 
LYS   OXT HXT  sing N N 263 
MET   N   CA   sing N N 264 
MET   N   H    sing N N 265 
MET   N   H2   sing N N 266 
MET   CA  C    sing N N 267 
MET   CA  CB   sing N N 268 
MET   CA  HA   sing N N 269 
MET   C   O    doub N N 270 
MET   C   OXT  sing N N 271 
MET   CB  CG   sing N N 272 
MET   CB  HB2  sing N N 273 
MET   CB  HB3  sing N N 274 
MET   CG  SD   sing N N 275 
MET   CG  HG2  sing N N 276 
MET   CG  HG3  sing N N 277 
MET   SD  CE   sing N N 278 
MET   CE  HE1  sing N N 279 
MET   CE  HE2  sing N N 280 
MET   CE  HE3  sing N N 281 
MET   OXT HXT  sing N N 282 
PHE   N   CA   sing N N 283 
PHE   N   H    sing N N 284 
PHE   N   H2   sing N N 285 
PHE   CA  C    sing N N 286 
PHE   CA  CB   sing N N 287 
PHE   CA  HA   sing N N 288 
PHE   C   O    doub N N 289 
PHE   C   OXT  sing N N 290 
PHE   CB  CG   sing N N 291 
PHE   CB  HB2  sing N N 292 
PHE   CB  HB3  sing N N 293 
PHE   CG  CD1  doub Y N 294 
PHE   CG  CD2  sing Y N 295 
PHE   CD1 CE1  sing Y N 296 
PHE   CD1 HD1  sing N N 297 
PHE   CD2 CE2  doub Y N 298 
PHE   CD2 HD2  sing N N 299 
PHE   CE1 CZ   doub Y N 300 
PHE   CE1 HE1  sing N N 301 
PHE   CE2 CZ   sing Y N 302 
PHE   CE2 HE2  sing N N 303 
PHE   CZ  HZ   sing N N 304 
PHE   OXT HXT  sing N N 305 
PRO   N   CA   sing N N 306 
PRO   N   CD   sing N N 307 
PRO   N   H    sing N N 308 
PRO   CA  C    sing N N 309 
PRO   CA  CB   sing N N 310 
PRO   CA  HA   sing N N 311 
PRO   C   O    doub N N 312 
PRO   C   OXT  sing N N 313 
PRO   CB  CG   sing N N 314 
PRO   CB  HB2  sing N N 315 
PRO   CB  HB3  sing N N 316 
PRO   CG  CD   sing N N 317 
PRO   CG  HG2  sing N N 318 
PRO   CG  HG3  sing N N 319 
PRO   CD  HD2  sing N N 320 
PRO   CD  HD3  sing N N 321 
PRO   OXT HXT  sing N N 322 
SER   N   CA   sing N N 323 
SER   N   H    sing N N 324 
SER   N   H2   sing N N 325 
SER   CA  C    sing N N 326 
SER   CA  CB   sing N N 327 
SER   CA  HA   sing N N 328 
SER   C   O    doub N N 329 
SER   C   OXT  sing N N 330 
SER   CB  OG   sing N N 331 
SER   CB  HB2  sing N N 332 
SER   CB  HB3  sing N N 333 
SER   OG  HG   sing N N 334 
SER   OXT HXT  sing N N 335 
THR   N   CA   sing N N 336 
THR   N   H    sing N N 337 
THR   N   H2   sing N N 338 
THR   CA  C    sing N N 339 
THR   CA  CB   sing N N 340 
THR   CA  HA   sing N N 341 
THR   C   O    doub N N 342 
THR   C   OXT  sing N N 343 
THR   CB  OG1  sing N N 344 
THR   CB  CG2  sing N N 345 
THR   CB  HB   sing N N 346 
THR   OG1 HG1  sing N N 347 
THR   CG2 HG21 sing N N 348 
THR   CG2 HG22 sing N N 349 
THR   CG2 HG23 sing N N 350 
THR   OXT HXT  sing N N 351 
TRP   N   CA   sing N N 352 
TRP   N   H    sing N N 353 
TRP   N   H2   sing N N 354 
TRP   CA  C    sing N N 355 
TRP   CA  CB   sing N N 356 
TRP   CA  HA   sing N N 357 
TRP   C   O    doub N N 358 
TRP   C   OXT  sing N N 359 
TRP   CB  CG   sing N N 360 
TRP   CB  HB2  sing N N 361 
TRP   CB  HB3  sing N N 362 
TRP   CG  CD1  doub Y N 363 
TRP   CG  CD2  sing Y N 364 
TRP   CD1 NE1  sing Y N 365 
TRP   CD1 HD1  sing N N 366 
TRP   CD2 CE2  doub Y N 367 
TRP   CD2 CE3  sing Y N 368 
TRP   NE1 CE2  sing Y N 369 
TRP   NE1 HE1  sing N N 370 
TRP   CE2 CZ2  sing Y N 371 
TRP   CE3 CZ3  doub Y N 372 
TRP   CE3 HE3  sing N N 373 
TRP   CZ2 CH2  doub Y N 374 
TRP   CZ2 HZ2  sing N N 375 
TRP   CZ3 CH2  sing Y N 376 
TRP   CZ3 HZ3  sing N N 377 
TRP   CH2 HH2  sing N N 378 
TRP   OXT HXT  sing N N 379 
TYR   N   CA   sing N N 380 
TYR   N   H    sing N N 381 
TYR   N   H2   sing N N 382 
TYR   CA  C    sing N N 383 
TYR   CA  CB   sing N N 384 
TYR   CA  HA   sing N N 385 
TYR   C   O    doub N N 386 
TYR   C   OXT  sing N N 387 
TYR   CB  CG   sing N N 388 
TYR   CB  HB2  sing N N 389 
TYR   CB  HB3  sing N N 390 
TYR   CG  CD1  doub Y N 391 
TYR   CG  CD2  sing Y N 392 
TYR   CD1 CE1  sing Y N 393 
TYR   CD1 HD1  sing N N 394 
TYR   CD2 CE2  doub Y N 395 
TYR   CD2 HD2  sing N N 396 
TYR   CE1 CZ   doub Y N 397 
TYR   CE1 HE1  sing N N 398 
TYR   CE2 CZ   sing Y N 399 
TYR   CE2 HE2  sing N N 400 
TYR   CZ  OH   sing N N 401 
TYR   OH  HH   sing N N 402 
TYR   OXT HXT  sing N N 403 
VAL   N   CA   sing N N 404 
VAL   N   H    sing N N 405 
VAL   N   H2   sing N N 406 
VAL   CA  C    sing N N 407 
VAL   CA  CB   sing N N 408 
VAL   CA  HA   sing N N 409 
VAL   C   O    doub N N 410 
VAL   C   OXT  sing N N 411 
VAL   CB  CG1  sing N N 412 
VAL   CB  CG2  sing N N 413 
VAL   CB  HB   sing N N 414 
VAL   CG1 HG11 sing N N 415 
VAL   CG1 HG12 sing N N 416 
VAL   CG1 HG13 sing N N 417 
VAL   CG2 HG21 sing N N 418 
VAL   CG2 HG22 sing N N 419 
VAL   CG2 HG23 sing N N 420 
VAL   OXT HXT  sing N N 421 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171399 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_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                    7I68 
_atom_sites.fract_transf_matrix[1][1]   0.011307 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000300 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017443 
_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]   0.030827 
_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   ? 19.601 6.767   23.366 1.00 32.66 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 20.716 6.928   22.442 1.00 32.67 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 20.763 5.787   21.440 1.00 30.99 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 20.043 4.789   21.603 1.00 31.88 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 22.023 7.013   23.228 1.00 34.72 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 22.246 5.804   23.925 1.00 39.21 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 21.462 5.998   20.331 1.00 28.58 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 21.618 4.950   19.331 1.00 27.78 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 21.981 5.491   17.969 1.00 27.57 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 21.670 6.634   17.673 1.00 28.30 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 22.569 4.662   17.109 1.00 26.80 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 22.929 5.094   15.764 1.00 27.57 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 22.852 3.953   14.766 1.00 27.37 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 22.926 2.794   15.157 1.00 28.74 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 24.368 5.652   15.794 1.00 28.13 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 22.796 4.264   13.477 1.00 25.89 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.865 3.264   12.417 1.00 26.06 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 24.223 3.430   11.746 1.00 28.30 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.628 4.561   11.440 1.00 29.21 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.741 3.507   11.376 1.00 25.46 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 20.371 3.631   12.018 1.00 24.53 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.757 2.446   10.272 1.00 26.59 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.355 4.296   11.055 1.00 24.40 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.948 2.320   11.499 1.00 29.34 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 26.244 2.388   10.827 1.00 30.34 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 26.150 1.657   9.507  1.00 31.16 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 26.025 0.433   9.496  1.00 31.64 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.328 1.758   11.713 1.00 31.19 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.537 2.577   12.958 1.00 31.60 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 28.335 3.717   12.940 1.00 32.89 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 26.913 2.237   14.147 1.00 32.27 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 28.477 4.516   14.070 1.00 33.41 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 27.060 3.017   15.285 1.00 33.16 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 27.873 4.138   15.252 1.00 34.34 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 27.973 4.939   16.359 1.00 35.94 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 26.192 2.384   8.406  1.00 30.80 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 26.040 1.812   7.074  1.00 32.15 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.104 2.396   6.175  1.00 33.41 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.236 3.625   6.064  1.00 33.36 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.615 2.045   6.514  1.00 33.32 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.152 3.497   6.703  1.00 32.97 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.515 1.600   5.059  1.00 34.37 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 27.951 1.528   5.614  1.00 34.49 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.087 1.955   4.804  1.00 35.60 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 29.982 2.882   5.606  1.00 36.27 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.214 2.624   6.785  1.00 37.47 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.308 4.042   5.053  1.00 36.42 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.083 5.029   5.796  1.00 36.44 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.176 6.143   6.312  1.00 34.57 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.558 7.304   6.298  1.00 34.11 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.269 5.542   4.995  1.00 39.71 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.313 4.469   4.842  1.00 47.29 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.163 4.253   5.724  1.00 48.72 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.230 3.733   3.744  1.00 49.48 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 28.978 5.781   6.789  1.00 33.14 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.030 6.758   7.342  1.00 31.05 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.571 6.358   8.735  1.00 30.45 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.515 5.174   9.080  1.00 31.10 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.804 6.943   6.447  1.00 29.54 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.107 7.457   5.061  1.00 30.14 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 27.734 8.679   4.873  1.00 31.70 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 26.769 6.722   3.939  1.00 32.13 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.023 9.151   3.599  1.00 32.94 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.018 7.200   2.659  1.00 33.55 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 27.640 8.419   2.495  1.00 34.72 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 27.907 8.887   1.231  1.00 38.05 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.236 7.356   9.531  1.00 28.59 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.707 7.159   10.876 1.00 26.90 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.434 7.984   10.906 1.00 26.26 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.506 9.195   10.704 1.00 26.21 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.678 7.722   11.910 1.00 27.63 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 27.123 7.850   13.337 1.00 28.47 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 28.250 8.189   14.303 1.00 32.60 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 27.851 9.193   15.295 1.00 34.21 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 27.377 8.912   16.503 1.00 36.14 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 27.143 7.653   16.856 1.00 37.01 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 27.038 9.892   17.333 1.00 32.23 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 24.274 7.359   11.173 1.00 25.16 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.998 8.086   11.218 1.00 25.18 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.579 8.214   12.668 1.00 26.20 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 22.422 7.184   13.339 1.00 27.01 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.890 7.372   10.416 1.00 25.22 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.612 8.235   10.356 1.00 25.10 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.381 7.014   9.016  1.00 25.78 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 22.323 9.437   13.146 1.00 25.28 ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 21.860 9.602   14.529 1.00 25.24 ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 20.686 10.596  14.599 1.00 24.39 ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 20.457 11.342  13.651 1.00 25.28 ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 22.998 10.141  15.417 1.00 27.12 ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 24.144 9.145   15.524 1.00 29.36 ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 23.489 11.486  14.887 1.00 27.85 ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 19.984 10.687  15.760 1.00 22.59 ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 19.019 11.769  15.970 1.00 22.50 ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 19.806 13.084  15.921 1.00 24.30 ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 20.885 13.198  16.551 1.00 24.08 ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 18.390 11.659  17.349 1.00 22.17 ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 17.483 10.430  17.439 1.00 24.09 ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.918 9.366   17.833 1.00 25.79 ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 16.247 10.542  17.011 1.00 22.59 ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 19.312 14.070  15.153 1.00 24.54 ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 20.023 15.349  15.021 1.00 25.15 ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 20.273 15.988  16.372 1.00 27.41 ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 21.395 16.439  16.637 1.00 28.28 ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 19.230 16.297  14.134 1.00 25.46 ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 20.024 17.534  13.708 1.00 24.96 ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 19.037 18.473  13.040 1.00 25.90 ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.658 19.711  12.561 1.00 29.14 ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.705 20.845  13.257 1.00 33.74 ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 19.315 20.872  14.526 1.00 32.95 ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 20.208 21.945  12.710 1.00 33.98 ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 19.284 15.867  17.285 1.00 27.87 ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 19.395 16.444  18.623 1.00 28.32 ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 20.413 15.744  19.515 1.00 29.15 ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 20.822 16.324  20.523 1.00 30.58 ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 18.027 16.547  19.281 1.00 28.99 ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 17.459 15.256  19.775 1.00 30.06 ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 16.728 14.407  18.948 1.00 31.64 ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 17.460 14.748  21.029 1.00 31.04 ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 16.347 13.407  19.721 1.00 31.89 ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 16.768 13.574  20.982 1.00 31.34 ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 20.912 14.569  19.117 1.00 29.42 ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 21.948 13.869  19.887 1.00 29.97 ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 23.317 13.831  19.172 1.00 30.90 ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 24.225 13.116  19.624 1.00 29.53 ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 21.461 12.422  20.179 1.00 29.59 ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 20.169 12.316  20.984 1.00 30.55 ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 19.763 10.844  21.186 1.00 29.57 ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 20.317 13.010  22.351 1.00 30.98 ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 23.461 14.533  18.015 1.00 31.37 ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 24.728 14.495  17.276 1.00 32.90 ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 25.862 15.073  18.110 1.00 33.14 ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 25.616 16.009  18.852 1.00 33.48 ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 24.597 15.285  15.979 1.00 33.09 ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 27.089 14.524  17.993 1.00 32.79 ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 28.265 15.017  18.741 1.00 33.61 ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 29.034 16.086  17.939 1.00 34.53 ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 28.759 16.302  16.755 1.00 33.47 ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 29.194 13.828  19.069 1.00 36.28 ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 29.767 13.370  17.834 1.00 38.38 ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 28.457 12.671  19.757 1.00 36.57 ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 30.089 16.707  18.555 1.00 35.50 ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 30.910 17.673  17.843 1.00 38.01 ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 31.561 17.010  16.619 1.00 37.38 ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 31.568 17.616  15.546 1.00 37.17 ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 31.984 18.193  18.799 1.00 42.15 ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 31.535 19.401  19.560 1.00 49.78 ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 30.214 19.553  19.968 1.00 52.81 ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 32.239 20.493  19.937 1.00 51.65 ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 30.165 20.721  20.579 1.00 53.61 ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 31.353 21.329  20.570 1.00 53.21 ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 32.032 15.766  16.776 1.00 36.93 ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 32.647 14.998  15.690 1.00 38.82 ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 31.649 14.777  14.540 1.00 38.05 ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 32.028 14.909  13.375 1.00 38.79 ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 33.159 13.655  16.187 1.00 43.06 ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 34.163 13.047  15.244 1.00 51.69 ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 35.349 13.410  15.251 1.00 55.18 ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 33.714 12.107  14.411 1.00 53.55 ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 30.375 14.467  14.857 1.00 35.69 ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 29.359 14.332  13.819 1.00 34.13 ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 29.174 15.665  13.045 1.00 32.82 ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 29.017 15.636  11.821 1.00 33.26 ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 27.998 13.991  14.429 1.00 33.79 ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 27.891 12.605  14.956 1.00 34.83 ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 28.395 11.688  14.296 1.00 36.27 ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 27.291 12.436  16.024 1.00 35.16 ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 29.081 16.797  13.746 1.00 32.11 ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.885 18.094  13.056 1.00 33.10 ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 30.132 18.457  12.232 1.00 33.45 ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 29.984 18.979  11.131 1.00 32.70 ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 28.592 19.232  14.048 1.00 33.42 ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 27.177 19.230  14.521 1.00 34.72 ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 26.721 18.828  15.743 1.00 35.84 ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 26.029 19.598  13.759 1.00 34.09 ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 25.353 18.941  15.793 1.00 36.06 ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 24.900 19.424  14.588 1.00 35.34 ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 25.839 20.073  12.452 1.00 34.17 ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 23.607 19.752  14.169 1.00 35.10 ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.565 20.434  12.053 1.00 34.98 ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 23.455 20.204  12.881 1.00 35.33 ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 31.340 18.133  12.753 1.00 34.02 ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.626 18.389  12.060 1.00 34.80 ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.734 17.498  10.810 1.00 36.07 ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.349 17.892  9.816  1.00 37.12 ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 33.798 18.094  12.993 1.00 34.85 ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 32.136 16.293  10.862 1.00 35.12 ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 32.176 15.381  9.725  1.00 35.43 ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.801 15.239  9.095  1.00 33.85 ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.466 14.169  8.593  1.00 34.26 ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.738 14.040  10.162 1.00 38.11 ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 34.169 14.211  10.554 1.00 42.42 ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 35.046 14.374  9.700  1.00 44.25 ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 34.429 14.250  11.852 1.00 43.26 ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 30.010 16.337  9.104  1.00 31.39 ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.652 16.317  8.613  1.00 29.61 ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.559 15.983  7.147  1.00 30.41 ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.260 16.579  6.334  1.00 30.15 ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 27.949 17.663  8.921  1.00 28.52 ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.557 17.878  8.371  1.00 28.90 ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.553 16.959  9.098  1.00 29.51 ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.112 19.331  8.535  1.00 28.73 ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.617 15.088  6.805  1.00 29.31 ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.307 14.750  5.417  1.00 29.60 ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 25.961 15.409  5.056  1.00 29.45 ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 25.847 16.098  4.041  1.00 30.51 ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.237 13.204  5.205  1.00 29.82 ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 26.727 12.866  3.806  1.00 30.79 ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 28.597 12.558  5.454  1.00 29.10 ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 24.972 15.256  5.925  1.00 27.95 ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 23.629 15.774  5.680  1.00 27.87 ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 22.853 15.821  6.996  1.00 26.71 ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 23.025 14.937  7.825  1.00 26.65 ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 22.895 14.840  4.701  1.00 28.18 ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.439 15.106  4.553  1.00 28.80 ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 20.844 16.051  3.761  1.00 30.42 ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.375 14.409  5.220  1.00 28.18 ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.472 15.977  3.893  1.00 29.91 ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.163 15.006  4.815  1.00 28.89 ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.337 13.407  6.201  1.00 28.64 ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 17.923 14.539  5.256  1.00 28.97 ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.107 12.948  6.632  1.00 28.56 ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 17.922 13.537  6.183  1.00 28.69 ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 22.011 16.841  7.177  1.00 24.85 ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 21.164 16.921  8.360  1.00 24.09 ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 19.882 17.659  8.013  1.00 24.79 ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 19.863 18.506  7.100  1.00 24.62 ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 21.873 17.556  9.564  1.00 24.34 ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.459 18.952  9.257  1.00 28.71 ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.528 20.156  9.334  1.00 32.68 ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 21.877 21.207  8.749  1.00 33.50 ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 20.453 20.052  9.966  1.00 31.19 ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 18.794 17.297  8.697  1.00 23.72 ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.510 17.961  8.462  1.00 23.68 ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.817 18.068  9.814  1.00 24.33 ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 16.384 17.046  10.364 1.00 24.69 ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.708 17.143  7.460  1.00 25.13 ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.412 17.769  7.024  1.00 31.69 ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 14.892 18.601  7.765  1.00 32.40 ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 14.944 17.442  5.916  1.00 33.69 ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.687 19.302  10.348 1.00 23.83 ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 16.040 19.549  11.632 0.50 24.27 ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 16.053 19.467  11.659 0.50 24.45 ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 14.576 19.059  11.591 1.00 24.61 ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 14.081 18.500  12.568 1.00 25.30 ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 16.070 21.046  11.930 0.50 25.09 ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 16.184 20.899  12.173 0.50 26.04 ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 15.375 21.341  13.124 0.50 26.31 ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 15.327 21.752  11.441 0.50 28.09 ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 13.888 19.287  10.442 1.00 24.25 ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 12.485 18.853  10.335 1.00 25.05 ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 12.327 17.329  10.398 1.00 24.79 ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 11.230 16.866  10.640 1.00 25.91 ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 11.791 19.423  9.100  1.00 30.04 ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 12.204 18.723  7.939  1.00 34.31 ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 13.383 16.555  10.185 1.00 23.59 ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 13.328 15.089  10.292 1.00 23.48 ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 13.980 14.558  11.598 1.00 24.37 ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 13.880 13.353  11.878 1.00 24.10 ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 14.038 14.435  9.084  1.00 22.21 ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 13.319 14.697  7.791  1.00 24.54 ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 14.037 14.091  6.607  1.00 26.19 ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 14.041 12.630  6.665  1.00 25.91 ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 14.108 11.836  5.598  1.00 26.65 ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 14.186 12.358  4.373  1.00 24.22 ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 14.105 10.516  5.744  1.00 25.72 ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 14.683 15.434  12.350 1.00 24.24 ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 15.466 15.094  13.530 1.00 23.45 ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 16.545 14.075  13.115 1.00 23.11 ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 16.865 13.176  13.892 1.00 22.76 ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 14.589 14.520  14.660 1.00 24.63 ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 15.377 14.217  15.932 1.00 26.17 ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 16.265 15.017  16.282 1.00 25.33 ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 15.097 13.163  16.583 1.00 25.05 ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 17.124 14.200  11.888 1.00 22.93 ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 18.190 13.273  11.474 1.00 23.22 ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 19.506 14.019  11.198 1.00 24.05 ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 19.486 15.148  10.704 1.00 23.69 ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.807 12.490  10.216 1.00 23.66 ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 16.702 11.398  10.375 1.00 23.61 ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 16.522 10.649  9.066  1.00 22.63 ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 17.049 10.423  11.460 1.00 23.34 ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 20.626 13.328  11.407 1.00 23.62 ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 21.952 13.835  11.073 1.00 24.95 ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 22.772 12.619  10.611 1.00 25.06 ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 22.649 11.528  11.195 1.00 26.78 ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 22.639 14.518  12.265 1.00 26.26 ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 24.004 15.158  11.945 1.00 28.52 ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 24.122 16.516  12.544 1.00 28.19 ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 25.157 14.267  12.371 1.00 30.70 ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 23.486 12.752  9.500  1.00 24.48 ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 24.377 11.688  9.007  1.00 25.43 ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 25.788 12.295  8.974  1.00 27.29 ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 25.986 13.377  8.410  1.00 27.28 ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 24.002 11.172  7.602  1.00 26.26 ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 25.038 10.170  7.106  1.00 26.81 ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 22.595 10.561  7.590  1.00 25.31 ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 26.751 11.583  9.532  1.00 28.08 ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 28.156 11.997  9.523  1.00 30.41 ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 29.001 10.883  8.916  1.00 32.45 ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 28.567 9.743   8.842  1.00 31.04 ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 28.639 12.323  10.931 1.00 30.85 ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 28.478 11.182  11.744 1.00 32.22 ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 30.213 11.220  8.450  1.00 33.47 ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 31.102 10.232  7.854  1.00 36.22 ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 31.900 9.503   8.921  1.00 38.44 ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 32.087 10.011  10.025 1.00 39.96 ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 32.047 10.899  6.863  1.00 39.92 ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 32.664 12.015  7.484  1.00 44.25 ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 32.322 8.282   8.615  1.00 38.62 ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 33.105 7.481   9.538  1.00 40.75 ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 34.351 6.973   8.827  1.00 43.72 ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 34.392 6.897   7.591  1.00 44.12 ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 32.286 6.273   10.051 1.00 41.48 ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 32.021 5.392   8.956  1.00 42.24 ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 31.002 6.676   10.724 1.00 40.83 ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? 35.361 6.616   9.607  1.00 45.71 ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? 36.589 6.069   9.054  1.00 48.13 ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? 36.464 4.549   8.861  1.00 47.76 ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? 37.030 3.999   7.918  1.00 48.61 ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? 37.763 6.518   9.922  1.00 52.01 ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? 37.546 6.024   11.247 1.00 54.83 ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? 37.871 8.019   9.978  1.00 52.55 ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? 35.695 3.875   9.726  1.00 46.98 ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? 35.502 2.436   9.645  1.00 46.11 ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 34.196 2.081   8.951  1.00 45.54 ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 33.213 2.821   9.056  1.00 45.28 ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? 35.526 1.832   11.041 1.00 46.26 ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 34.168 0.935   8.263  1.00 44.67 ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 32.963 0.503   7.575  1.00 44.27 ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 31.954 -0.064  8.570  1.00 41.48 ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 32.339 -0.821  9.460  1.00 41.63 ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 33.302 -0.542  6.509  1.00 49.00 ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 33.396 0.050   5.104  1.00 57.13 ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 32.550 -0.693  4.088  1.00 66.14 ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 32.859 -0.700  2.891  1.00 69.09 ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 31.460 -1.332  4.528  1.00 67.30 ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 30.683 0.323   8.422  1.00 38.52 ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 29.586 -0.178  9.242  1.00 37.38 ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 28.956 -1.422  8.656  1.00 36.60 ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 29.187 -1.753  7.485  1.00 37.83 ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 28.167 -2.132  9.459  1.00 34.86 ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 27.592 -3.406  9.048  1.00 35.17 ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 26.083 -3.442  8.947  1.00 34.11 ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 25.524 -4.528  8.735  1.00 34.46 ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 28.085 -4.510  9.976  1.00 37.21 ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 29.880 -4.593  10.118 1.00 43.02 ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 25.400 -2.315  9.169  1.00 32.35 ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 23.940 -2.300  9.099  1.00 31.51 ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 23.495 -2.215  7.633  1.00 31.74 ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 24.183 -1.641  6.781  1.00 32.57 ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 23.372 -1.107  9.905  1.00 32.49 ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 23.548 -1.227  11.410 1.00 37.49 ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 23.458 -2.364  11.930 1.00 38.01 ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 23.789 -0.185  12.070 1.00 35.62 ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 22.349 -2.795  7.341  1.00 31.81 ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 21.737 -2.732  6.012  1.00 32.67 ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 20.467 -1.882  6.155  1.00 30.76 ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 19.713 -2.102  7.085  1.00 30.98 ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 21.356 -4.142  5.548  1.00 35.18 ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 22.567 -4.818  5.192  1.00 37.29 ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 20.387 -4.132  4.346  1.00 35.39 ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 20.248 -0.930  5.266  1.00 28.56 ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 19.054 -0.085  5.325  1.00 28.22 ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 17.992 -0.811  4.519  1.00 29.62 ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 18.274 -1.215  3.382  1.00 31.24 ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 19.302 1.302   4.688  1.00 27.54 ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 20.494 2.047   5.325  1.00 28.23 ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 18.028 2.161   4.746  1.00 27.08 ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 20.393 2.149   6.940  1.00 28.86 ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 16.800 -0.976  5.070  1.00 27.81 ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 15.678 -1.559  4.338  1.00 27.61 ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 15.292 -0.645  3.151  1.00 27.05 ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 15.277 0.571   3.292  1.00 25.92 ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 14.482 -1.688  5.267  1.00 27.20 ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 14.971 -1.231  1.997  1.00 27.41 ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 14.461 -0.481  0.856  1.00 28.06 ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 13.144 -1.180  0.561  1.00 29.05 ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 13.121 -2.200  -0.135 1.00 29.74 ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 15.404 -0.544  -0.333 1.00 28.57 ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 16.795 0.038   -0.054 1.00 31.81 ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 16.782 1.508   0.314  1.00 33.04 ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 18.122 1.940   0.707  1.00 34.03 ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 18.391 3.066   1.367  1.00 34.92 ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 17.417 3.895   1.704  1.00 31.04 ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 19.631 3.349   1.724  1.00 35.38 ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 12.066 -0.687  1.175  1.00 29.17 ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 10.771 -1.363  1.132  1.00 29.47 ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 9.637  -0.433  1.613  1.00 29.94 ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 9.906  0.688   2.033  1.00 28.92 ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 10.874 -2.560  2.060  1.00 27.73 ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 11.033 -2.076  3.795  1.00 28.67 ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 8.381  -0.967  1.673  1.00 31.00 ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 7.278  -0.216  2.252  1.00 32.47 ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 6.668  -0.986  3.426  1.00 32.22 ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 5.468  -0.859  3.667  1.00 32.99 ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 6.189  0.139   1.212  1.00 37.26 ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 5.478  -1.019  0.570  1.00 45.48 ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 5.774  -2.165  0.928  1.00 46.92 ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 4.628  -0.776  -0.322 1.00 50.40 ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 7.464  -1.809  4.156  1.00 29.61 ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 6.950  -2.536  5.334  1.00 27.47 ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 6.282  -1.598  6.311  1.00 26.26 ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 6.684  -0.446  6.456  1.00 25.46 ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 8.053  -3.314  6.051  1.00 26.73 ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 8.655  -4.781  5.177  1.00 29.57 ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 5.263  -2.105  6.975  1.00 24.97 ? 59  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 53  ? 4.616  -1.378  8.045  1.00 24.68 ? 59  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 53  ? 4.579  -2.224  9.317  1.00 24.21 ? 59  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 53  ? 3.797  -1.909  10.210 1.00 24.14 ? 59  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 53  ? 3.192  -0.948  7.663  1.00 28.49 ? 59  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 53  ? 3.131  0.265   6.783  1.00 32.54 ? 59  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 53  ? 1.692  0.703   6.621  1.00 34.75 ? 59  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 53  ? 1.099  0.545   5.551  1.00 36.44 ? 59  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 53  ? 1.092  1.227   7.690  1.00 33.81 ? 59  GLN   A NE2 1 
ATOM   415  N  N   . THR   A 1 54  ? 5.379  -3.347  9.388  1.00 22.92 ? 60  THR   A N   1 
ATOM   416  C  CA  . THR   A 1 54  ? 5.525  -4.162  10.577 1.00 22.33 ? 60  THR   A CA  1 
ATOM   417  C  C   . THR   A 1 54  ? 7.046  -4.371  10.769 1.00 21.39 ? 60  THR   A C   1 
ATOM   418  O  O   . THR   A 1 54  ? 7.824  -4.415  9.821  1.00 22.16 ? 60  THR   A O   1 
ATOM   419  C  CB  . THR   A 1 54  ? 4.749  -5.482  10.543 1.00 25.08 ? 60  THR   A CB  1 
ATOM   420  O  OG1 . THR   A 1 54  ? 5.278  -6.277  9.480  1.00 28.60 ? 60  THR   A OG1 1 
ATOM   421  C  CG2 . THR   A 1 54  ? 3.256  -5.273  10.275 1.00 25.52 ? 60  THR   A CG2 1 
ATOM   422  N  N   . GLY   A 1 55  ? 7.432  -4.439  12.010 1.00 20.14 ? 61  GLY   A N   1 
ATOM   423  C  CA  . GLY   A 1 55  ? 8.835  -4.532  12.367 1.00 19.67 ? 61  GLY   A CA  1 
ATOM   424  C  C   . GLY   A 1 55  ? 8.998  -4.676  13.855 1.00 20.09 ? 61  GLY   A C   1 
ATOM   425  O  O   . GLY   A 1 55  ? 8.059  -5.041  14.527 1.00 22.01 ? 61  GLY   A O   1 
ATOM   426  N  N   . VAL   A 1 56  ? 10.221 -4.557  14.316 1.00 19.85 ? 62  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 56  ? 10.528 -4.694  15.743 1.00 20.08 ? 62  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 56  ? 11.399 -3.494  16.121 1.00 20.55 ? 62  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 56  ? 12.284 -3.135  15.372 1.00 21.46 ? 62  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 56  ? 11.271 -6.057  16.016 1.00 21.92 ? 62  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 56  ? 11.663 -6.160  17.493 1.00 23.26 ? 62  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 56  ? 10.354 -7.220  15.699 1.00 22.71 ? 62  VAL   A CG2 1 
ATOM   433  N  N   . TYR   A 1 57  ? 11.174 -2.868  17.288 1.00 19.88 ? 63  TYR   A N   1 
ATOM   434  C  CA  . TYR   A 1 57  ? 12.031 -1.742  17.703 1.00 19.10 ? 63  TYR   A CA  1 
ATOM   435  C  C   . TYR   A 1 57  ? 12.600 -1.992  19.066 1.00 20.00 ? 63  TYR   A C   1 
ATOM   436  O  O   . TYR   A 1 57  ? 11.984 -2.693  19.835 1.00 21.18 ? 63  TYR   A O   1 
ATOM   437  C  CB  . TYR   A 1 57  ? 11.273 -0.387  17.646 1.00 20.32 ? 63  TYR   A CB  1 
ATOM   438  C  CG  . TYR   A 1 57  ? 10.397 -0.086  18.836 1.00 21.54 ? 63  TYR   A CG  1 
ATOM   439  C  CD1 . TYR   A 1 57  ? 9.127  -0.648  18.950 1.00 22.03 ? 63  TYR   A CD1 1 
ATOM   440  C  CD2 . TYR   A 1 57  ? 10.816 0.793   19.829 1.00 23.23 ? 63  TYR   A CD2 1 
ATOM   441  C  CE1 . TYR   A 1 57  ? 8.292  -0.331  20.014 1.00 24.02 ? 63  TYR   A CE1 1 
ATOM   442  C  CE2 . TYR   A 1 57  ? 9.978  1.125   20.897 1.00 23.11 ? 63  TYR   A CE2 1 
ATOM   443  C  CZ  . TYR   A 1 57  ? 8.730  0.533   20.999 1.00 23.87 ? 63  TYR   A CZ  1 
ATOM   444  O  OH  . TYR   A 1 57  ? 7.886  0.827   22.042 1.00 25.12 ? 63  TYR   A OH  1 
ATOM   445  N  N   . TYR   A 1 58  ? 13.733 -1.387  19.369 1.00 19.94 ? 64  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 58  ? 14.339 -1.542  20.685 1.00 20.92 ? 64  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 58  ? 13.892 -0.378  21.517 1.00 21.57 ? 64  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 58  ? 14.194 0.760   21.161 1.00 22.27 ? 64  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 58  ? 15.864 -1.508  20.582 1.00 20.44 ? 64  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 58  ? 16.476 -1.606  21.956 1.00 21.92 ? 64  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 58  ? 16.174 -2.675  22.798 1.00 23.06 ? 64  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 58  ? 17.330 -0.613  22.435 1.00 22.65 ? 64  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 58  ? 16.722 -2.767  24.073 1.00 23.95 ? 64  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 58  ? 17.900 -0.709  23.707 1.00 24.23 ? 64  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 58  ? 17.569 -1.772  24.525 1.00 25.32 ? 64  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 58  ? 18.079 -1.868  25.799 1.00 28.13 ? 64  TYR   A OH  1 
ATOM   457  N  N   . CYS   A 1 59  ? 13.406 -0.670  22.716 1.00 21.63 ? 65  CYS   A N   1 
ATOM   458  C  CA  . CYS   A 1 59  ? 12.981 0.333   23.665 1.00 22.04 ? 65  CYS   A CA  1 
ATOM   459  C  C   . CYS   A 1 59  ? 13.909 0.232   24.888 1.00 23.15 ? 65  CYS   A C   1 
ATOM   460  O  O   . CYS   A 1 59  ? 13.731 -0.650  25.716 1.00 24.02 ? 65  CYS   A O   1 
ATOM   461  C  CB  . CYS   A 1 59  ? 11.525 0.082   24.034 1.00 23.46 ? 65  CYS   A CB  1 
ATOM   462  S  SG  . CYS   A 1 59  ? 10.919 1.071   25.429 1.00 25.68 ? 65  CYS   A SG  1 
ATOM   463  N  N   . SER   A 1 60  ? 14.897 1.132   25.007 1.00 22.99 ? 66  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 60  ? 15.846 1.072   26.100 1.00 23.96 ? 66  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 60  ? 15.191 1.254   27.464 1.00 24.76 ? 66  SER   A C   1 
ATOM   466  O  O   . SER   A 1 60  ? 15.681 0.680   28.424 1.00 26.19 ? 66  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 60  ? 16.980 2.093   25.928 1.00 27.33 ? 66  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 60  ? 16.487 3.420   26.000 1.00 31.47 ? 66  SER   A OG  1 
ATOM   469  N  N   . SER   A 1 61  ? 14.104 2.056   27.560 1.00 24.05 ? 67  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 61  ? 13.420 2.278   28.862 1.00 24.42 ? 67  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 61  ? 12.670 1.012   29.374 1.00 24.98 ? 67  SER   A C   1 
ATOM   472  O  O   . SER   A 1 61  ? 12.200 0.994   30.522 1.00 25.87 ? 67  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 61  ? 12.452 3.458   28.776 1.00 25.57 ? 67  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 61  ? 11.427 3.222   27.819 1.00 26.77 ? 67  SER   A OG  1 
ATOM   475  N  N   . ARG   A 1 62  ? 12.610 -0.036  28.565 1.00 25.02 ? 68  ARG   A N   1 
ATOM   476  C  CA  . ARG   A 1 62  ? 12.032 -1.311  28.986 1.00 25.49 ? 68  ARG   A CA  1 
ATOM   477  C  C   . ARG   A 1 62  ? 13.053 -2.463  28.788 1.00 27.00 ? 68  ARG   A C   1 
ATOM   478  O  O   . ARG   A 1 62  ? 12.727 -3.611  29.104 1.00 27.31 ? 68  ARG   A O   1 
ATOM   479  C  CB  . ARG   A 1 62  ? 10.780 -1.600  28.125 1.00 25.98 ? 68  ARG   A CB  1 
ATOM   480  C  CG  . ARG   A 1 62  ? 9.586  -0.677  28.425 1.00 26.80 ? 68  ARG   A CG  1 
ATOM   481  C  CD  . ARG   A 1 62  ? 8.976  -1.054  29.784 1.00 28.70 ? 68  ARG   A CD  1 
ATOM   482  N  NE  . ARG   A 1 62  ? 7.846  -0.183  30.122 1.00 31.64 ? 68  ARG   A NE  1 
ATOM   483  C  CZ  . ARG   A 1 62  ? 7.963  1.005   30.700 1.00 31.60 ? 68  ARG   A CZ  1 
ATOM   484  N  NH1 . ARG   A 1 62  ? 9.161  1.465   31.056 1.00 29.77 ? 68  ARG   A NH1 1 
ATOM   485  N  NH2 . ARG   A 1 62  ? 6.887  1.750   30.922 1.00 32.29 ? 68  ARG   A NH2 1 
ATOM   486  N  N   . ARG   A 1 63  ? 14.284 -2.184  28.237 1.00 26.68 ? 69  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 63  ? 15.301 -3.187  27.841 1.00 26.88 ? 69  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 63  ? 14.595 -4.305  27.032 1.00 26.92 ? 69  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 63  ? 14.712 -5.491  27.360 1.00 28.38 ? 69  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 63  ? 16.007 -3.770  29.074 1.00 28.08 ? 69  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 63  ? 16.980 -2.803  29.694 1.00 30.65 ? 69  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 63  ? 17.698 -3.481  30.848 1.00 33.86 ? 69  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 63  ? 18.447 -2.516  31.649 1.00 37.71 ? 69  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 63  ? 18.351 -2.396  32.970 1.00 40.15 ? 69  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 63  ? 17.513 -3.163  33.654 1.00 39.17 ? 69  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 63  ? 19.081 -1.490  33.617 1.00 39.74 ? 69  ARG   A NH2 1 
ATOM   497  N  N   . LYS   A 1 64  ? 13.751 -3.902  26.070 1.00 25.40 ? 70  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 64  ? 12.911 -4.865  25.355 1.00 24.93 ? 70  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 64  ? 12.785 -4.495  23.906 1.00 24.00 ? 70  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 64  ? 12.828 -3.311  23.575 1.00 24.32 ? 70  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 64  ? 11.506 -4.849  25.986 1.00 28.27 ? 70  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 64  ? 10.658 -6.064  25.700 1.00 35.60 ? 70  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 64  ? 10.226 -6.712  26.997 1.00 41.30 ? 70  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 64  ? 8.939  -7.482  26.791 1.00 47.19 ? 70  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 64  ? 9.094  -8.547  25.768 1.00 50.27 ? 70  LYS   A NZ  1 
ATOM   506  N  N   . HIS   A 1 65  ? 12.579 -5.480  23.040 1.00 22.37 ? 71  HIS   A N   1 
ATOM   507  C  CA  . HIS   A 1 65  ? 12.385 -5.284  21.591 1.00 20.97 ? 71  HIS   A CA  1 
ATOM   508  C  C   . HIS   A 1 65  ? 10.926 -5.658  21.340 1.00 22.30 ? 71  HIS   A C   1 
ATOM   509  O  O   . HIS   A 1 65  ? 10.505 -6.788  21.667 1.00 23.08 ? 71  HIS   A O   1 
ATOM   510  C  CB  . HIS   A 1 65  ? 13.289 -6.280  20.846 1.00 21.44 ? 71  HIS   A CB  1 
ATOM   511  C  CG  . HIS   A 1 65  ? 14.748 -6.066  21.126 1.00 23.08 ? 71  HIS   A CG  1 
ATOM   512  N  ND1 . HIS   A 1 65  ? 15.560 -5.388  20.239 1.00 25.06 ? 71  HIS   A ND1 1 
ATOM   513  C  CD2 . HIS   A 1 65  ? 15.465 -6.384  22.227 1.00 23.78 ? 71  HIS   A CD2 1 
ATOM   514  C  CE1 . HIS   A 1 65  ? 16.755 -5.355  20.804 1.00 25.41 ? 71  HIS   A CE1 1 
ATOM   515  N  NE2 . HIS   A 1 65  ? 16.735 -5.912  22.021 1.00 26.22 ? 71  HIS   A NE2 1 
ATOM   516  N  N   . TYR   A 1 66  ? 10.134 -4.697  20.867 1.00 19.82 ? 72  TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 66  ? 8.720  -4.920  20.699 1.00 19.65 ? 72  TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 66  ? 8.329  -5.045  19.247 1.00 20.03 ? 72  TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 66  ? 8.670  -4.187  18.457 1.00 20.24 ? 72  TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 66  ? 7.964  -3.703  21.245 1.00 19.80 ? 72  TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 66  ? 8.000  -3.568  22.754 1.00 20.35 ? 72  TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 66  ? 7.217  -4.380  23.557 1.00 22.17 ? 72  TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 66  ? 8.785  -2.598  23.366 1.00 21.46 ? 72  TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 66  ? 7.228  -4.248  24.945 1.00 23.61 ? 72  TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 66  ? 8.774  -2.427  24.752 1.00 22.45 ? 72  TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 66  ? 8.007  -3.265  25.533 1.00 24.45 ? 72  TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 66  ? 7.989  -3.103  26.903 1.00 26.68 ? 72  TYR   A OH  1 
ATOM   528  N  N   . PRO   A 1 67  ? 7.515  -6.036  18.912 1.00 21.66 ? 73  PRO   A N   1 
ATOM   529  C  CA  . PRO   A 1 67  ? 6.994  -6.125  17.533 1.00 22.32 ? 73  PRO   A CA  1 
ATOM   530  C  C   . PRO   A 1 67  ? 5.909  -5.029  17.413 1.00 23.39 ? 73  PRO   A C   1 
ATOM   531  O  O   . PRO   A 1 67  ? 5.131  -4.837  18.357 1.00 24.78 ? 73  PRO   A O   1 
ATOM   532  C  CB  . PRO   A 1 67  ? 6.367  -7.542  17.470 1.00 24.12 ? 73  PRO   A CB  1 
ATOM   533  C  CG  . PRO   A 1 67  ? 6.090  -7.895  18.872 1.00 25.43 ? 73  PRO   A CG  1 
ATOM   534  C  CD  . PRO   A 1 67  ? 7.034  -7.145  19.767 1.00 22.67 ? 73  PRO   A CD  1 
ATOM   535  N  N   . VAL   A 1 68  ? 5.897  -4.278  16.303 1.00 21.64 ? 74  VAL   A N   1 
ATOM   536  C  CA  . VAL   A 1 68  ? 4.957  -3.173  16.139 1.00 23.39 ? 74  VAL   A CA  1 
ATOM   537  C  C   . VAL   A 1 68  ? 4.488  -3.100  14.689 1.00 24.22 ? 74  VAL   A C   1 
ATOM   538  O  O   . VAL   A 1 68  ? 5.189  -3.530  13.770 1.00 23.78 ? 74  VAL   A O   1 
ATOM   539  C  CB  . VAL   A 1 68  ? 5.627  -1.806  16.506 1.00 25.77 ? 74  VAL   A CB  1 
ATOM   540  C  CG1 . VAL   A 1 68  ? 5.706  -1.604  18.020 1.00 27.53 ? 74  VAL   A CG1 1 
ATOM   541  C  CG2 . VAL   A 1 68  ? 6.989  -1.609  15.831 1.00 25.52 ? 74  VAL   A CG2 1 
ATOM   542  N  N   . SER   A 1 69  ? 3.316  -2.482  14.514 1.00 23.09 ? 75  SER   A N   1 
ATOM   543  C  CA  . SER   A 1 69  ? 2.739  -2.057  13.249 1.00 24.39 ? 75  SER   A CA  1 
ATOM   544  C  C   . SER   A 1 69  ? 2.958  -0.544  13.274 1.00 23.82 ? 75  SER   A C   1 
ATOM   545  O  O   . SER   A 1 69  ? 2.737  0.086   14.301 1.00 24.70 ? 75  SER   A O   1 
ATOM   546  C  CB  . SER   A 1 69  ? 1.241  -2.319  13.212 1.00 27.71 ? 75  SER   A CB  1 
ATOM   547  O  OG  . SER   A 1 69  ? 0.961  -3.706  13.135 1.00 35.21 ? 75  SER   A OG  1 
ATOM   548  N  N   . PHE   A 1 70  ? 3.358  0.038   12.170 1.00 21.99 ? 76  PHE   A N   1 
ATOM   549  C  CA  . PHE   A 1 70  ? 3.637  1.475   12.141 1.00 22.37 ? 76  PHE   A CA  1 
ATOM   550  C  C   . PHE   A 1 70  ? 3.097  2.128   10.905 1.00 24.58 ? 76  PHE   A C   1 
ATOM   551  O  O   . PHE   A 1 70  ? 2.978  1.492   9.869  1.00 26.35 ? 76  PHE   A O   1 
ATOM   552  C  CB  . PHE   A 1 70  ? 5.156  1.778   12.350 1.00 21.26 ? 76  PHE   A CB  1 
ATOM   553  C  CG  . PHE   A 1 70  ? 6.100  1.048   11.429 1.00 20.58 ? 76  PHE   A CG  1 
ATOM   554  C  CD1 . PHE   A 1 70  ? 6.604  -0.202  11.768 1.00 20.52 ? 76  PHE   A CD1 1 
ATOM   555  C  CD2 . PHE   A 1 70  ? 6.473  1.607   10.211 1.00 20.98 ? 76  PHE   A CD2 1 
ATOM   556  C  CE1 . PHE   A 1 70  ? 7.473  -0.880  10.899 1.00 20.56 ? 76  PHE   A CE1 1 
ATOM   557  C  CE2 . PHE   A 1 70  ? 7.332  0.931   9.343  1.00 21.58 ? 76  PHE   A CE2 1 
ATOM   558  C  CZ  . PHE   A 1 70  ? 7.835  -0.303  9.697  1.00 20.53 ? 76  PHE   A CZ  1 
ATOM   559  N  N   . SER   A 1 71  ? 2.774  3.410   11.004 1.00 25.50 ? 77  SER   A N   1 
ATOM   560  C  CA  . SER   A 1 71  ? 2.206  4.159   9.894  1.00 26.18 ? 77  SER   A CA  1 
ATOM   561  C  C   . SER   A 1 71  ? 3.280  4.478   8.823  1.00 27.28 ? 77  SER   A C   1 
ATOM   562  O  O   . SER   A 1 71  ? 4.468  4.347   9.092  1.00 28.35 ? 77  SER   A O   1 
ATOM   563  C  CB  . SER   A 1 71  ? 1.569  5.449   10.439 1.00 26.38 ? 77  SER   A CB  1 
ATOM   564  O  OG  . SER   A 1 71  ? 2.571  6.311   10.955 1.00 27.13 ? 77  SER   A OG  1 
ATOM   565  N  N   . LYS   A 1 72  ? 2.876  4.884   7.614  1.00 28.08 ? 78  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 72  ? 3.846  5.261   6.575  1.00 29.23 ? 78  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 72  ? 4.462  6.636   6.905  1.00 29.03 ? 78  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 72  ? 3.846  7.430   7.610  1.00 29.08 ? 78  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 72  ? 3.186  5.253   5.178  1.00 32.60 ? 78  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 72  ? 2.962  3.802   4.681  1.00 38.10 ? 78  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 72  ? 2.256  3.711   3.339  1.00 43.11 ? 78  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 72  ? 2.476  2.328   2.757  1.00 47.00 ? 78  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 72  ? 1.721  2.114   1.488  1.00 49.28 ? 78  LYS   A NZ  1 
ATOM   574  N  N   . PRO   A 1 73  ? 5.678  6.928   6.422  1.00 29.32 ? 79  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 73  ? 6.325  8.220   6.772  1.00 28.92 ? 79  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 73  ? 5.458  9.410   6.426  1.00 28.15 ? 79  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 73  ? 4.998  9.506   5.284  1.00 28.99 ? 79  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 73  ? 7.587  8.216   5.921  1.00 30.59 ? 79  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 73  ? 7.901  6.749   5.753  1.00 31.71 ? 79  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 73  ? 6.557  6.092   5.585  1.00 29.57 ? 79  PRO   A CD  1 
ATOM   581  N  N   A SER   A 1 74  ? 5.182  10.284  7.393  0.50 27.52 ? 80  SER   A N   1 
ATOM   582  N  N   B SER   A 1 74  ? 5.185  10.281  7.395  0.50 27.44 ? 80  SER   A N   1 
ATOM   583  C  CA  A SER   A 1 74  ? 4.315  11.440  7.131  0.50 28.66 ? 80  SER   A CA  1 
ATOM   584  C  CA  B SER   A 1 74  ? 4.296  11.426  7.153  0.50 28.52 ? 80  SER   A CA  1 
ATOM   585  C  C   A SER   A 1 74  ? 4.692  12.684  7.966  0.50 29.20 ? 80  SER   A C   1 
ATOM   586  C  C   B SER   A 1 74  ? 4.711  12.688  7.946  0.50 29.12 ? 80  SER   A C   1 
ATOM   587  O  O   A SER   A 1 74  ? 5.593  12.628  8.802  0.50 28.73 ? 80  SER   A O   1 
ATOM   588  O  O   B SER   A 1 74  ? 5.631  12.641  8.760  0.50 28.62 ? 80  SER   A O   1 
ATOM   589  C  CB  A SER   A 1 74  ? 2.840  11.062  7.286  0.50 30.54 ? 80  SER   A CB  1 
ATOM   590  C  CB  B SER   A 1 74  ? 2.837  11.059  7.450  0.50 30.30 ? 80  SER   A CB  1 
ATOM   591  O  OG  A SER   A 1 74  ? 2.466  10.839  8.635  0.50 32.56 ? 80  SER   A OG  1 
ATOM   592  O  OG  B SER   A 1 74  ? 2.516  9.681   7.327  0.50 31.84 ? 80  SER   A OG  1 
ATOM   593  N  N   . LEU   A 1 75  ? 4.028  13.808  7.704  1.00 29.59 ? 81  LEU   A N   1 
ATOM   594  C  CA  . LEU   A 1 75  ? 4.292  15.076  8.386  1.00 31.15 ? 81  LEU   A CA  1 
ATOM   595  C  C   . LEU   A 1 75  ? 3.382  15.102  9.613  1.00 32.11 ? 81  LEU   A C   1 
ATOM   596  O  O   . LEU   A 1 75  ? 2.149  15.102  9.474  1.00 32.64 ? 81  LEU   A O   1 
ATOM   597  C  CB  . LEU   A 1 75  ? 3.926  16.213  7.417  1.00 31.43 ? 81  LEU   A CB  1 
ATOM   598  C  CG  . LEU   A 1 75  ? 4.375  17.624  7.815  1.00 34.05 ? 81  LEU   A CG  1 
ATOM   599  C  CD1 . LEU   A 1 75  ? 5.841  17.699  8.053  1.00 33.41 ? 81  LEU   A CD1 1 
ATOM   600  C  CD2 . LEU   A 1 75  ? 3.904  18.656  6.796  1.00 36.03 ? 81  LEU   A CD2 1 
ATOM   601  N  N   . ILE   A 1 76  ? 3.974  15.073  10.806 1.00 31.67 ? 82  ILE   A N   1 
ATOM   602  C  CA  . ILE   A 1 76  ? 3.205  14.953  12.043 1.00 33.26 ? 82  ILE   A CA  1 
ATOM   603  C  C   . ILE   A 1 76  ? 3.540  16.060  13.012 1.00 33.38 ? 82  ILE   A C   1 
ATOM   604  O  O   . ILE   A 1 76  ? 4.718  16.351  13.197 1.00 32.57 ? 82  ILE   A O   1 
ATOM   605  C  CB  . ILE   A 1 76  ? 3.549  13.577  12.672 1.00 34.88 ? 82  ILE   A CB  1 
ATOM   606  C  CG1 . ILE   A 1 76  ? 3.117  12.403  11.755 1.00 37.61 ? 82  ILE   A CG1 1 
ATOM   607  C  CG2 . ILE   A 1 76  ? 3.011  13.430  14.114 1.00 34.72 ? 82  ILE   A CG2 1 
ATOM   608  C  CD1 . ILE   A 1 76  ? 1.661  12.223  11.624 1.00 40.76 ? 82  ILE   A CD1 1 
ATOM   609  N  N   . PHE   A 1 77  ? 2.529  16.619  13.691 1.00 33.41 ? 83  PHE   A N   1 
ATOM   610  C  CA  . PHE   A 1 77  ? 2.783  17.661  14.675 1.00 33.98 ? 83  PHE   A CA  1 
ATOM   611  C  C   . PHE   A 1 77  ? 3.392  17.070  15.934 1.00 33.24 ? 83  PHE   A C   1 
ATOM   612  O  O   . PHE   A 1 77  ? 2.872  16.098  16.498 1.00 34.06 ? 83  PHE   A O   1 
ATOM   613  C  CB  . PHE   A 1 77  ? 1.511  18.444  15.026 1.00 35.21 ? 83  PHE   A CB  1 
ATOM   614  C  CG  . PHE   A 1 77  ? 1.846  19.716  15.764 1.00 37.49 ? 83  PHE   A CG  1 
ATOM   615  C  CD1 . PHE   A 1 77  ? 2.472  20.769  15.114 1.00 39.05 ? 83  PHE   A CD1 1 
ATOM   616  C  CD2 . PHE   A 1 77  ? 1.575  19.844  17.115 1.00 39.55 ? 83  PHE   A CD2 1 
ATOM   617  C  CE1 . PHE   A 1 77  ? 2.774  21.939  15.789 1.00 40.36 ? 83  PHE   A CE1 1 
ATOM   618  C  CE2 . PHE   A 1 77  ? 1.894  21.016  17.792 1.00 40.43 ? 83  PHE   A CE2 1 
ATOM   619  C  CZ  . PHE   A 1 77  ? 2.487  22.050  17.128 1.00 40.44 ? 83  PHE   A CZ  1 
ATOM   620  N  N   . VAL   A 1 78  ? 4.540  17.608  16.331 1.00 31.50 ? 84  VAL   A N   1 
ATOM   621  C  CA  . VAL   A 1 78  ? 5.265  17.127  17.495 1.00 31.00 ? 84  VAL   A CA  1 
ATOM   622  C  C   . VAL   A 1 78  ? 5.358  18.219  18.552 1.00 31.27 ? 84  VAL   A C   1 
ATOM   623  O  O   . VAL   A 1 78  ? 5.879  19.301  18.279 1.00 31.36 ? 84  VAL   A O   1 
ATOM   624  C  CB  . VAL   A 1 78  ? 6.661  16.612  17.068 1.00 30.70 ? 84  VAL   A CB  1 
ATOM   625  C  CG1 . VAL   A 1 78  ? 7.500  16.220  18.284 1.00 30.94 ? 84  VAL   A CG1 1 
ATOM   626  C  CG2 . VAL   A 1 78  ? 6.529  15.443  16.106 1.00 29.28 ? 84  VAL   A CG2 1 
ATOM   627  N  N   . GLU   A 1 79  ? 4.847  17.946  19.749 1.00 31.62 ? 85  GLU   A N   1 
ATOM   628  C  CA  . GLU   A 1 79  ? 4.872  18.908  20.843 1.00 32.98 ? 85  GLU   A CA  1 
ATOM   629  C  C   . GLU   A 1 79  ? 6.279  19.404  21.199 1.00 33.63 ? 85  GLU   A C   1 
ATOM   630  O  O   . GLU   A 1 79  ? 7.279  18.741  20.892 1.00 33.23 ? 85  GLU   A O   1 
ATOM   631  C  CB  . GLU   A 1 79  ? 4.210  18.294  22.089 1.00 35.28 ? 85  GLU   A CB  1 
ATOM   632  C  CG  . GLU   A 1 79  ? 2.732  18.041  21.877 1.00 41.61 ? 85  GLU   A CG  1 
ATOM   633  C  CD  . GLU   A 1 79  ? 1.947  19.322  21.678 1.00 50.17 ? 85  GLU   A CD  1 
ATOM   634  O  OE1 . GLU   A 1 79  ? 2.179  20.285  22.444 1.00 52.21 ? 85  GLU   A OE1 1 
ATOM   635  O  OE2 . GLU   A 1 79  ? 1.114  19.372  20.744 1.00 52.40 ? 85  GLU   A OE2 1 
ATOM   636  N  N   . ALA   A 1 80  ? 6.355  20.551  21.897 1.00 33.30 ? 86  ALA   A N   1 
ATOM   637  C  CA  . ALA   A 1 80  ? 7.642  21.096  22.331 1.00 34.35 ? 86  ALA   A CA  1 
ATOM   638  C  C   . ALA   A 1 80  ? 8.328  20.118  23.278 1.00 34.94 ? 86  ALA   A C   1 
ATOM   639  O  O   . ALA   A 1 80  ? 7.655  19.389  24.013 1.00 34.79 ? 86  ALA   A O   1 
ATOM   640  C  CB  . ALA   A 1 80  ? 7.444  22.426  23.039 1.00 34.68 ? 86  ALA   A CB  1 
ATOM   641  N  N   . SER   A 1 81  ? 9.656  20.099  23.235 1.00 34.90 ? 87  SER   A N   1 
ATOM   642  C  CA  . SER   A 1 81  ? 10.496 19.240  24.056 1.00 35.29 ? 87  SER   A CA  1 
ATOM   643  C  C   . SER   A 1 81  ? 11.737 20.046  24.508 1.00 37.25 ? 87  SER   A C   1 
ATOM   644  O  O   . SER   A 1 81  ? 11.876 21.223  24.164 1.00 37.44 ? 87  SER   A O   1 
ATOM   645  C  CB  . SER   A 1 81  ? 10.938 18.030  23.240 1.00 34.79 ? 87  SER   A CB  1 
ATOM   646  O  OG  . SER   A 1 81  ? 11.881 18.403  22.244 1.00 35.09 ? 87  SER   A OG  1 
ATOM   647  N  N   . GLU   A 1 82  ? 12.687 19.382  25.188 1.00 38.39 ? 88  GLU   A N   1 
ATOM   648  C  CA  . GLU   A 1 82  ? 13.912 20.051  25.602 1.00 39.67 ? 88  GLU   A CA  1 
ATOM   649  C  C   . GLU   A 1 82  ? 14.788 20.418  24.400 1.00 38.95 ? 88  GLU   A C   1 
ATOM   650  O  O   . GLU   A 1 82  ? 15.577 21.346  24.509 1.00 39.44 ? 88  GLU   A O   1 
ATOM   651  C  CB  . GLU   A 1 82  ? 14.670 19.179  26.614 1.00 45.09 ? 88  GLU   A CB  1 
ATOM   652  C  CG  . GLU   A 1 82  ? 13.800 18.801  27.808 1.00 54.16 ? 88  GLU   A CG  1 
ATOM   653  C  CD  . GLU   A 1 82  ? 14.354 19.120  29.179 1.00 67.50 ? 88  GLU   A CD  1 
ATOM   654  O  OE1 . GLU   A 1 82  ? 13.544 19.357  30.105 1.00 70.61 ? 88  GLU   A OE1 1 
ATOM   655  O  OE2 . GLU   A 1 82  ? 15.597 19.134  29.330 1.00 71.89 ? 88  GLU   A OE2 1 
ATOM   656  N  N   . TYR   A 1 83  ? 14.592 19.775  23.226 1.00 37.50 ? 89  TYR   A N   1 
ATOM   657  C  CA  . TYR   A 1 83  ? 15.440 20.001  22.063 1.00 36.89 ? 89  TYR   A CA  1 
ATOM   658  C  C   . TYR   A 1 83  ? 14.838 20.771  20.886 1.00 35.01 ? 89  TYR   A C   1 
ATOM   659  O  O   . TYR   A 1 83  ? 15.593 21.221  20.022 1.00 35.16 ? 89  TYR   A O   1 
ATOM   660  C  CB  . TYR   A 1 83  ? 15.951 18.644  21.571 1.00 37.80 ? 89  TYR   A CB  1 
ATOM   661  C  CG  . TYR   A 1 83  ? 16.957 18.041  22.525 1.00 40.25 ? 89  TYR   A CG  1 
ATOM   662  C  CD1 . TYR   A 1 83  ? 18.288 18.423  22.492 1.00 41.62 ? 89  TYR   A CD1 1 
ATOM   663  C  CD2 . TYR   A 1 83  ? 16.568 17.121  23.489 1.00 42.48 ? 89  TYR   A CD2 1 
ATOM   664  C  CE1 . TYR   A 1 83  ? 19.221 17.866  23.356 1.00 43.74 ? 89  TYR   A CE1 1 
ATOM   665  C  CE2 . TYR   A 1 83  ? 17.491 16.567  24.374 1.00 44.20 ? 89  TYR   A CE2 1 
ATOM   666  C  CZ  . TYR   A 1 83  ? 18.818 16.940  24.302 1.00 46.02 ? 89  TYR   A CZ  1 
ATOM   667  O  OH  . TYR   A 1 83  ? 19.746 16.400  25.166 1.00 49.78 ? 89  TYR   A OH  1 
ATOM   668  N  N   . TYR   A 1 84  ? 13.514 20.862  20.791 1.00 33.02 ? 90  TYR   A N   1 
ATOM   669  C  CA  . TYR   A 1 84  ? 12.870 21.580  19.695 1.00 31.59 ? 90  TYR   A CA  1 
ATOM   670  C  C   . TYR   A 1 84  ? 11.643 22.258  20.228 1.00 32.64 ? 90  TYR   A C   1 
ATOM   671  O  O   . TYR   A 1 84  ? 10.933 21.677  21.067 1.00 33.14 ? 90  TYR   A O   1 
ATOM   672  C  CB  . TYR   A 1 84  ? 12.381 20.621  18.578 1.00 29.53 ? 90  TYR   A CB  1 
ATOM   673  C  CG  . TYR   A 1 84  ? 13.435 19.838  17.843 1.00 27.68 ? 90  TYR   A CG  1 
ATOM   674  C  CD1 . TYR   A 1 84  ? 14.147 20.404  16.789 1.00 27.53 ? 90  TYR   A CD1 1 
ATOM   675  C  CD2 . TYR   A 1 84  ? 13.662 18.499  18.136 1.00 27.61 ? 90  TYR   A CD2 1 
ATOM   676  C  CE1 . TYR   A 1 84  ? 15.072 19.662  16.065 1.00 26.40 ? 90  TYR   A CE1 1 
ATOM   677  C  CE2 . TYR   A 1 84  ? 14.614 17.762  17.449 1.00 27.24 ? 90  TYR   A CE2 1 
ATOM   678  C  CZ  . TYR   A 1 84  ? 15.310 18.342  16.409 1.00 27.40 ? 90  TYR   A CZ  1 
ATOM   679  O  OH  . TYR   A 1 84  ? 16.281 17.604  15.764 1.00 26.65 ? 90  TYR   A OH  1 
ATOM   680  N  N   . PRO   A 1 85  ? 11.271 23.419  19.663 1.00 33.10 ? 91  PRO   A N   1 
ATOM   681  C  CA  . PRO   A 1 85  ? 9.940  23.975  19.983 1.00 33.54 ? 91  PRO   A CA  1 
ATOM   682  C  C   . PRO   A 1 85  ? 8.849  23.117  19.301 1.00 33.16 ? 91  PRO   A C   1 
ATOM   683  O  O   . PRO   A 1 85  ? 9.173  22.208  18.505 1.00 33.08 ? 91  PRO   A O   1 
ATOM   684  C  CB  . PRO   A 1 85  ? 9.986  25.381  19.352 1.00 34.61 ? 91  PRO   A CB  1 
ATOM   685  C  CG  . PRO   A 1 85  ? 10.877 25.223  18.179 1.00 35.03 ? 91  PRO   A CG  1 
ATOM   686  C  CD  . PRO   A 1 85  ? 11.936 24.184  18.582 1.00 32.98 ? 91  PRO   A CD  1 
ATOM   687  N  N   . ALA   A 1 86  ? 7.558  23.411  19.556 1.00 32.72 ? 92  ALA   A N   1 
ATOM   688  C  CA  . ALA   A 1 86  ? 6.454  22.678  18.908 1.00 33.00 ? 92  ALA   A CA  1 
ATOM   689  C  C   . ALA   A 1 86  ? 6.544  22.877  17.390 1.00 32.99 ? 92  ALA   A C   1 
ATOM   690  O  O   . ALA   A 1 86  ? 6.765  24.000  16.953 1.00 33.98 ? 92  ALA   A O   1 
ATOM   691  C  CB  . ALA   A 1 86  ? 5.114  23.172  19.433 1.00 33.82 ? 92  ALA   A CB  1 
ATOM   692  N  N   . ARG   A 1 87  ? 6.553  21.790  16.600 1.00 32.12 ? 93  ARG   A N   1 
ATOM   693  C  CA  . ARG   A 1 87  ? 6.703  21.920  15.138 1.00 31.54 ? 93  ARG   A CA  1 
ATOM   694  C  C   . ARG   A 1 87  ? 6.164  20.686  14.417 1.00 31.95 ? 93  ARG   A C   1 
ATOM   695  O  O   . ARG   A 1 87  ? 5.828  19.708  15.076 1.00 33.28 ? 93  ARG   A O   1 
ATOM   696  C  CB  . ARG   A 1 87  ? 8.195  22.157  14.758 1.00 30.57 ? 93  ARG   A CB  1 
ATOM   697  C  CG  . ARG   A 1 87  ? 9.023  20.847  14.666 1.00 29.75 ? 93  ARG   A CG  1 
ATOM   698  C  CD  . ARG   A 1 87  ? 10.406 20.890  15.271 1.00 29.60 ? 93  ARG   A CD  1 
ATOM   699  N  NE  . ARG   A 1 87  ? 11.259 19.807  14.749 1.00 27.85 ? 93  ARG   A NE  1 
ATOM   700  C  CZ  . ARG   A 1 87  ? 11.222 18.544  15.164 1.00 29.00 ? 93  ARG   A CZ  1 
ATOM   701  N  NH1 . ARG   A 1 87  ? 10.349 18.170  16.104 1.00 27.48 ? 93  ARG   A NH1 1 
ATOM   702  N  NH2 . ARG   A 1 87  ? 12.052 17.638  14.640 1.00 26.39 ? 93  ARG   A NH2 1 
ATOM   703  N  N   . TYR   A 1 88  ? 6.124  20.707  13.069 1.00 30.53 ? 94  TYR   A N   1 
ATOM   704  C  CA  . TYR   A 1 88  ? 5.791  19.519  12.325 1.00 30.51 ? 94  TYR   A CA  1 
ATOM   705  C  C   . TYR   A 1 88  ? 7.110  18.832  12.005 1.00 28.71 ? 94  TYR   A C   1 
ATOM   706  O  O   . TYR   A 1 88  ? 8.057  19.463  11.511 1.00 29.87 ? 94  TYR   A O   1 
ATOM   707  C  CB  . TYR   A 1 88  ? 5.084  19.830  11.018 1.00 31.46 ? 94  TYR   A CB  1 
ATOM   708  C  CG  . TYR   A 1 88  ? 3.654  20.249  11.217 1.00 32.47 ? 94  TYR   A CG  1 
ATOM   709  C  CD1 . TYR   A 1 88  ? 2.640  19.310  11.262 1.00 33.20 ? 94  TYR   A CD1 1 
ATOM   710  C  CD2 . TYR   A 1 88  ? 3.321  21.583  11.428 1.00 34.13 ? 94  TYR   A CD2 1 
ATOM   711  C  CE1 . TYR   A 1 88  ? 1.320  19.683  11.454 1.00 34.96 ? 94  TYR   A CE1 1 
ATOM   712  C  CE2 . TYR   A 1 88  ? 1.998  21.977  11.598 1.00 35.21 ? 94  TYR   A CE2 1 
ATOM   713  C  CZ  . TYR   A 1 88  ? 1.001  21.016  11.632 1.00 36.56 ? 94  TYR   A CZ  1 
ATOM   714  O  OH  . TYR   A 1 88  ? -0.312 21.346  11.830 1.00 39.06 ? 94  TYR   A OH  1 
ATOM   715  N  N   . GLN   A 1 89  ? 7.163  17.548  12.276 1.00 26.42 ? 95  GLN   A N   1 
ATOM   716  C  CA  . GLN   A 1 89  ? 8.317  16.719  11.946 1.00 25.56 ? 95  GLN   A CA  1 
ATOM   717  C  C   . GLN   A 1 89  ? 7.927  15.886  10.738 1.00 25.55 ? 95  GLN   A C   1 
ATOM   718  O  O   . GLN   A 1 89  ? 6.850  15.262  10.744 1.00 26.38 ? 95  GLN   A O   1 
ATOM   719  C  CB  . GLN   A 1 89  ? 8.692  15.788  13.111 1.00 26.47 ? 95  GLN   A CB  1 
ATOM   720  C  CG  . GLN   A 1 89  ? 9.941  14.912  12.757 1.00 28.07 ? 95  GLN   A CG  1 
ATOM   721  C  CD  . GLN   A 1 89  ? 10.665 14.360  13.961 1.00 28.33 ? 95  GLN   A CD  1 
ATOM   722  O  OE1 . GLN   A 1 89  ? 10.794 15.029  14.982 1.00 26.27 ? 95  GLN   A OE1 1 
ATOM   723  N  NE2 . GLN   A 1 89  ? 11.145 13.112  13.847 1.00 27.60 ? 95  GLN   A NE2 1 
ATOM   724  N  N   . SER   A 1 90  ? 8.771  15.876  9.702  1.00 24.83 ? 96  SER   A N   1 
ATOM   725  C  CA  . SER   A 1 90  ? 8.514  15.161  8.464  1.00 24.59 ? 96  SER   A CA  1 
ATOM   726  C  C   . SER   A 1 90  ? 9.107  13.729  8.461  1.00 23.81 ? 96  SER   A C   1 
ATOM   727  O  O   . SER   A 1 90  ? 9.994  13.417  9.268  1.00 23.50 ? 96  SER   A O   1 
ATOM   728  C  CB  . SER   A 1 90  ? 9.029  15.967  7.266  1.00 25.68 ? 96  SER   A CB  1 
ATOM   729  O  OG  . SER   A 1 90  ? 10.443 16.100  7.343  1.00 27.49 ? 96  SER   A OG  1 
ATOM   730  N  N   . HIS   A 1 91  ? 8.599  12.869  7.558  1.00 23.49 ? 97  HIS   A N   1 
ATOM   731  C  CA  . HIS   A 1 91  ? 9.086  11.483  7.406  1.00 23.86 ? 97  HIS   A CA  1 
ATOM   732  C  C   . HIS   A 1 91  ? 8.975  10.696  8.725  1.00 23.28 ? 97  HIS   A C   1 
ATOM   733  O  O   . HIS   A 1 91  ? 9.843  9.900   9.024  1.00 23.55 ? 97  HIS   A O   1 
ATOM   734  C  CB  . HIS   A 1 91  ? 10.534 11.482  6.892  1.00 24.54 ? 97  HIS   A CB  1 
ATOM   735  C  CG  . HIS   A 1 91  ? 10.694 12.184  5.571  1.00 27.28 ? 97  HIS   A CG  1 
ATOM   736  N  ND1 . HIS   A 1 91  ? 10.744 11.482  4.386  1.00 30.59 ? 97  HIS   A ND1 1 
ATOM   737  C  CD2 . HIS   A 1 91  ? 10.775 13.508  5.292  1.00 28.02 ? 97  HIS   A CD2 1 
ATOM   738  C  CE1 . HIS   A 1 91  ? 10.842 12.392  3.426  1.00 30.69 ? 97  HIS   A CE1 1 
ATOM   739  N  NE2 . HIS   A 1 91  ? 10.853 13.624  3.922  1.00 29.37 ? 97  HIS   A NE2 1 
ATOM   740  N  N   . LEU   A 1 92  ? 7.962  10.990  9.532  1.00 23.56 ? 98  LEU   A N   1 
ATOM   741  C  CA  . LEU   A 1 92  ? 7.790  10.334  10.835 1.00 23.50 ? 98  LEU   A CA  1 
ATOM   742  C  C   . LEU   A 1 92  ? 6.747  9.188   10.729 1.00 24.24 ? 98  LEU   A C   1 
ATOM   743  O  O   . LEU   A 1 92  ? 5.687  9.353   10.095 1.00 24.85 ? 98  LEU   A O   1 
ATOM   744  C  CB  . LEU   A 1 92  ? 7.309  11.387  11.850 1.00 23.60 ? 98  LEU   A CB  1 
ATOM   745  C  CG  . LEU   A 1 92  ? 7.204  10.964  13.314 1.00 25.73 ? 98  LEU   A CG  1 
ATOM   746  C  CD1 . LEU   A 1 92  ? 8.576  10.564  13.862 1.00 25.89 ? 98  LEU   A CD1 1 
ATOM   747  C  CD2 . LEU   A 1 92  ? 6.664  12.139  14.142 1.00 26.71 ? 98  LEU   A CD2 1 
ATOM   748  N  N   . MET   A 1 93  ? 7.016  8.065   11.397 1.00 23.23 ? 99  MET   A N   1 
ATOM   749  C  CA  . MET   A 1 93  ? 6.100  6.919   11.395 1.00 22.66 ? 99  MET   A CA  1 
ATOM   750  C  C   . MET   A 1 93  ? 5.711  6.655   12.836 1.00 23.47 ? 99  MET   A C   1 
ATOM   751  O  O   . MET   A 1 93  ? 6.581  6.689   13.688 1.00 24.40 ? 99  MET   A O   1 
ATOM   752  C  CB  . MET   A 1 93  ? 6.806  5.684   10.836 1.00 23.59 ? 99  MET   A CB  1 
ATOM   753  C  CG  . MET   A 1 93  ? 7.309  5.893   9.403  1.00 24.88 ? 99  MET   A CG  1 
ATOM   754  S  SD  . MET   A 1 93  ? 8.376  4.559   8.879  1.00 28.19 ? 99  MET   A SD  1 
ATOM   755  C  CE  . MET   A 1 93  ? 9.778  4.804   9.872  1.00 25.81 ? 99  MET   A CE  1 
ATOM   756  N  N   . LEU   A 1 94  ? 4.406  6.458   13.132 1.00 23.53 ? 100 LEU   A N   1 
ATOM   757  C  CA  . LEU   A 1 94  ? 3.979  6.215   14.507 1.00 23.72 ? 100 LEU   A CA  1 
ATOM   758  C  C   . LEU   A 1 94  ? 3.546  4.761   14.681 1.00 23.42 ? 100 LEU   A C   1 
ATOM   759  O  O   . LEU   A 1 94  ? 3.037  4.117   13.761 1.00 24.31 ? 100 LEU   A O   1 
ATOM   760  C  CB  . LEU   A 1 94  ? 2.767  7.125   14.928 1.00 25.27 ? 100 LEU   A CB  1 
ATOM   761  C  CG  . LEU   A 1 94  ? 2.923  8.618   14.839 1.00 27.71 ? 100 LEU   A CG  1 
ATOM   762  C  CD1 . LEU   A 1 94  ? 1.686  9.329   15.405 1.00 29.88 ? 100 LEU   A CD1 1 
ATOM   763  C  CD2 . LEU   A 1 94  ? 4.187  9.088   15.542 1.00 28.57 ? 100 LEU   A CD2 1 
ATOM   764  N  N   . ALA   A 1 95  ? 3.650  4.309   15.910 1.00 22.49 ? 101 ALA   A N   1 
ATOM   765  C  CA  . ALA   A 1 95  ? 3.206  3.001   16.351 1.00 22.34 ? 101 ALA   A CA  1 
ATOM   766  C  C   . ALA   A 1 95  ? 2.697  3.156   17.779 1.00 23.58 ? 101 ALA   A C   1 
ATOM   767  O  O   . ALA   A 1 95  ? 3.068  4.099   18.491 1.00 25.24 ? 101 ALA   A O   1 
ATOM   768  C  CB  . ALA   A 1 95  ? 4.385  2.010   16.339 1.00 21.78 ? 101 ALA   A CB  1 
ATOM   769  N  N   . VAL   A 1 96  ? 1.843  2.224   18.194 1.00 21.64 ? 102 VAL   A N   1 
ATOM   770  C  CA  . VAL   A 1 96  ? 1.390  2.135   19.557 1.00 22.94 ? 102 VAL   A CA  1 
ATOM   771  C  C   . VAL   A 1 96  ? 2.463  1.364   20.263 1.00 25.09 ? 102 VAL   A C   1 
ATOM   772  O  O   . VAL   A 1 96  ? 2.799  0.222   19.893 1.00 26.43 ? 102 VAL   A O   1 
ATOM   773  C  CB  . VAL   A 1 96  ? 0.016  1.428   19.622 1.00 23.87 ? 102 VAL   A CB  1 
ATOM   774  C  CG1 . VAL   A 1 96  ? -0.406 1.199   21.073 1.00 25.20 ? 102 VAL   A CG1 1 
ATOM   775  C  CG2 . VAL   A 1 96  ? -1.026 2.290   18.911 1.00 24.01 ? 102 VAL   A CG2 1 
ATOM   776  N  N   . GLY   A 1 97  ? 3.080  2.018   21.221 1.00 25.99 ? 103 GLY   A N   1 
ATOM   777  C  CA  . GLY   A 1 97  ? 4.192  1.417   21.942 1.00 26.59 ? 103 GLY   A CA  1 
ATOM   778  C  C   . GLY   A 1 97  ? 4.796  2.368   22.945 1.00 27.00 ? 103 GLY   A C   1 
ATOM   779  O  O   . GLY   A 1 97  ? 4.482  3.575   22.947 1.00 27.54 ? 103 GLY   A O   1 
ATOM   780  N  N   . HIS   A 1 98  ? 5.610  1.817   23.855 1.00 25.87 ? 104 HIS   A N   1 
ATOM   781  C  CA  . HIS   A 1 98  ? 6.211  2.653   24.866 1.00 26.52 ? 104 HIS   A CA  1 
ATOM   782  C  C   . HIS   A 1 98  ? 7.452  3.391   24.357 1.00 25.99 ? 104 HIS   A C   1 
ATOM   783  O  O   . HIS   A 1 98  ? 8.271  2.815   23.663 1.00 25.15 ? 104 HIS   A O   1 
ATOM   784  C  CB  . HIS   A 1 98  ? 6.536  1.866   26.141 1.00 27.49 ? 104 HIS   A CB  1 
ATOM   785  C  CG  . HIS   A 1 98  ? 7.128  2.737   27.209 1.00 30.46 ? 104 HIS   A CG  1 
ATOM   786  N  ND1 . HIS   A 1 98  ? 6.376  3.721   27.839 1.00 32.52 ? 104 HIS   A ND1 1 
ATOM   787  C  CD2 . HIS   A 1 98  ? 8.410  2.818   27.650 1.00 31.38 ? 104 HIS   A CD2 1 
ATOM   788  C  CE1 . HIS   A 1 98  ? 7.211  4.331   28.668 1.00 33.16 ? 104 HIS   A CE1 1 
ATOM   789  N  NE2 . HIS   A 1 98  ? 8.441  3.807   28.602 1.00 32.32 ? 104 HIS   A NE2 1 
ATOM   790  N  N   . SER   A 1 99  ? 7.601  4.636   24.750 1.00 26.04 ? 105 SER   A N   1 
ATOM   791  C  CA  . SER   A 1 99  ? 8.819  5.399   24.500 1.00 27.27 ? 105 SER   A CA  1 
ATOM   792  C  C   . SER   A 1 99  ? 8.997  6.560   25.463 1.00 28.66 ? 105 SER   A C   1 
ATOM   793  O  O   . SER   A 1 99  ? 8.015  7.143   25.894 1.00 30.27 ? 105 SER   A O   1 
ATOM   794  C  CB  . SER   A 1 99  ? 8.939  5.853   23.058 1.00 29.58 ? 105 SER   A CB  1 
ATOM   795  O  OG  . SER   A 1 99  ? 7.920  6.776   22.742 1.00 32.60 ? 105 SER   A OG  1 
ATOM   796  N  N   . GLU   A 1 100 ? 10.252 6.831   25.855 1.00 27.31 ? 106 GLU   A N   1 
ATOM   797  C  CA  . GLU   A 1 100 ? 10.670 7.963   26.684 1.00 28.70 ? 106 GLU   A CA  1 
ATOM   798  C  C   . GLU   A 1 100 ? 11.779 8.728   25.946 1.00 29.78 ? 106 GLU   A C   1 
ATOM   799  O  O   . GLU   A 1 100 ? 12.433 8.150   25.077 1.00 30.22 ? 106 GLU   A O   1 
ATOM   800  C  CB  . GLU   A 1 100 ? 11.143 7.455   28.053 1.00 31.07 ? 106 GLU   A CB  1 
ATOM   801  C  CG  . GLU   A 1 100 ? 10.030 6.729   28.758 1.00 33.82 ? 106 GLU   A CG  1 
ATOM   802  C  CD  . GLU   A 1 100 ? 10.386 6.193   30.129 1.00 38.94 ? 106 GLU   A CD  1 
ATOM   803  O  OE1 . GLU   A 1 100 ? 11.271 6.785   30.781 1.00 39.42 ? 106 GLU   A OE1 1 
ATOM   804  O  OE2 . GLU   A 1 100 ? 9.785  5.181   30.549 1.00 39.67 ? 106 GLU   A OE2 1 
ATOM   805  N  N   . PRO   A 1 101 ? 12.029 10.018  26.239 1.00 31.22 ? 107 PRO   A N   1 
ATOM   806  C  CA  . PRO   A 1 101 ? 13.047 10.768  25.456 1.00 31.49 ? 107 PRO   A CA  1 
ATOM   807  C  C   . PRO   A 1 101 ? 14.382 10.032  25.202 1.00 31.25 ? 107 PRO   A C   1 
ATOM   808  O  O   . PRO   A 1 101 ? 14.862 9.992   24.065 1.00 31.81 ? 107 PRO   A O   1 
ATOM   809  C  CB  . PRO   A 1 101 ? 13.226 12.072  26.244 1.00 32.35 ? 107 PRO   A CB  1 
ATOM   810  C  CG  . PRO   A 1 101 ? 11.890 12.276  26.916 1.00 33.12 ? 107 PRO   A CG  1 
ATOM   811  C  CD  . PRO   A 1 101 ? 11.340 10.881  27.225 1.00 30.91 ? 107 PRO   A CD  1 
ATOM   812  N  N   . GLY   A 1 102 ? 14.933 9.404   26.236 1.00 29.89 ? 108 GLY   A N   1 
ATOM   813  C  CA  . GLY   A 1 102 ? 16.179 8.646   26.159 1.00 29.60 ? 108 GLY   A CA  1 
ATOM   814  C  C   . GLY   A 1 102 ? 16.127 7.407   25.277 1.00 28.77 ? 108 GLY   A C   1 
ATOM   815  O  O   . GLY   A 1 102 ? 17.162 6.801   25.004 1.00 29.57 ? 108 GLY   A O   1 
ATOM   816  N  N   . ASP   A 1 103 ? 14.935 7.011   24.826 1.00 27.05 ? 109 ASP   A N   1 
ATOM   817  C  CA  . ASP   A 1 103 ? 14.765 5.925   23.886 1.00 25.61 ? 109 ASP   A CA  1 
ATOM   818  C  C   . ASP   A 1 103 ? 15.108 6.323   22.452 1.00 23.69 ? 109 ASP   A C   1 
ATOM   819  O  O   . ASP   A 1 103 ? 15.256 5.438   21.594 1.00 23.45 ? 109 ASP   A O   1 
ATOM   820  C  CB  . ASP   A 1 103 ? 13.349 5.355   23.906 1.00 26.57 ? 109 ASP   A CB  1 
ATOM   821  C  CG  . ASP   A 1 103 ? 13.036 4.596   25.161 1.00 27.23 ? 109 ASP   A CG  1 
ATOM   822  O  OD1 . ASP   A 1 103 ? 13.950 3.987   25.719 1.00 26.53 ? 109 ASP   A OD1 1 
ATOM   823  O  OD2 . ASP   A 1 103 ? 11.880 4.619   25.582 1.00 26.59 ? 109 ASP   A OD2 1 
ATOM   824  N  N   . CYS   A 1 104 ? 15.279 7.623   22.165 1.00 23.28 ? 110 CYS   A N   1 
ATOM   825  C  CA  . CYS   A 1 104 ? 15.690 8.069   20.815 1.00 23.05 ? 110 CYS   A CA  1 
ATOM   826  C  C   . CYS   A 1 104 ? 16.955 7.352   20.373 1.00 23.93 ? 110 CYS   A C   1 
ATOM   827  O  O   . CYS   A 1 104 ? 17.878 7.219   21.175 1.00 24.43 ? 110 CYS   A O   1 
ATOM   828  C  CB  . CYS   A 1 104 ? 15.891 9.579   20.784 1.00 23.97 ? 110 CYS   A CB  1 
ATOM   829  S  SG  . CYS   A 1 104 ? 14.357 10.526  20.849 1.00 26.71 ? 110 CYS   A SG  1 
ATOM   830  N  N   . GLY   A 1 105 ? 17.018 6.957   19.112 1.00 23.44 ? 111 GLY   A N   1 
ATOM   831  C  CA  . GLY   A 1 105 ? 18.188 6.232   18.639 1.00 24.79 ? 111 GLY   A CA  1 
ATOM   832  C  C   . GLY   A 1 105 ? 17.943 4.737   18.561 1.00 25.03 ? 111 GLY   A C   1 
ATOM   833  O  O   . GLY   A 1 105 ? 18.654 4.037   17.818 1.00 26.23 ? 111 GLY   A O   1 
ATOM   834  N  N   . GLY   A 1 106 ? 16.928 4.227   19.301 1.00 23.13 ? 112 GLY   A N   1 
ATOM   835  C  CA  . GLY   A 1 106 ? 16.550 2.817   19.218 1.00 22.02 ? 112 GLY   A CA  1 
ATOM   836  C  C   . GLY   A 1 106 ? 16.164 2.443   17.790 1.00 21.32 ? 112 GLY   A C   1 
ATOM   837  O  O   . GLY   A 1 106 ? 15.411 3.165   17.145 1.00 19.93 ? 112 GLY   A O   1 
ATOM   838  N  N   . ILE   A 1 107 ? 16.691 1.337   17.276 1.00 20.38 ? 113 ILE   A N   1 
ATOM   839  C  CA  . ILE   A 1 107 ? 16.421 0.963   15.896 1.00 20.46 ? 113 ILE   A CA  1 
ATOM   840  C  C   . ILE   A 1 107 ? 15.083 0.267   15.722 1.00 20.79 ? 113 ILE   A C   1 
ATOM   841  O  O   . ILE   A 1 107 ? 14.712 -0.555  16.564 1.00 21.38 ? 113 ILE   A O   1 
ATOM   842  C  CB  . ILE   A 1 107 ? 17.627 0.107   15.337 1.00 22.59 ? 113 ILE   A CB  1 
ATOM   843  C  CG1 . ILE   A 1 107 ? 18.757 1.070   14.867 1.00 24.66 ? 113 ILE   A CG1 1 
ATOM   844  C  CG2 . ILE   A 1 107 ? 17.219 -0.763  14.155 1.00 23.86 ? 113 ILE   A CG2 1 
ATOM   845  C  CD1 . ILE   A 1 107 ? 20.099 0.382   14.562 1.00 27.22 ? 113 ILE   A CD1 1 
ATOM   846  N  N   . LEU   A 1 108 ? 14.396 0.591   14.615 1.00 19.64 ? 114 LEU   A N   1 
ATOM   847  C  CA  . LEU   A 1 108 ? 13.206 -0.099  14.145 1.00 18.98 ? 114 LEU   A CA  1 
ATOM   848  C  C   . LEU   A 1 108 ? 13.712 -0.886  12.928 1.00 20.91 ? 114 LEU   A C   1 
ATOM   849  O  O   . LEU   A 1 108 ? 14.357 -0.315  12.038 1.00 20.56 ? 114 LEU   A O   1 
ATOM   850  C  CB  . LEU   A 1 108 ? 12.162 0.906   13.647 1.00 19.09 ? 114 LEU   A CB  1 
ATOM   851  C  CG  . LEU   A 1 108 ? 10.954 0.280   12.902 1.00 20.52 ? 114 LEU   A CG  1 
ATOM   852  C  CD1 . LEU   A 1 108 ? 10.123 -0.612  13.916 1.00 21.32 ? 114 LEU   A CD1 1 
ATOM   853  C  CD2 . LEU   A 1 108 ? 10.066 1.416   12.360 1.00 21.97 ? 114 LEU   A CD2 1 
ATOM   854  N  N   . ARG   A 1 109 ? 13.439 -2.170  12.926 1.00 21.51 ? 115 ARG   A N   1 
ATOM   855  C  CA  . ARG   A 1 109 ? 13.831 -3.020  11.821 1.00 23.02 ? 115 ARG   A CA  1 
ATOM   856  C  C   . ARG   A 1 109 ? 12.726 -3.894  11.313 1.00 22.84 ? 115 ARG   A C   1 
ATOM   857  O  O   . ARG   A 1 109 ? 11.888 -4.339  12.061 1.00 20.89 ? 115 ARG   A O   1 
ATOM   858  C  CB  . ARG   A 1 109 ? 15.073 -3.852  12.130 1.00 26.26 ? 115 ARG   A CB  1 
ATOM   859  C  CG  . ARG   A 1 109 ? 15.009 -4.817  13.283 1.00 35.79 ? 115 ARG   A CG  1 
ATOM   860  C  CD  . ARG   A 1 109 ? 16.305 -5.657  13.258 1.00 42.29 ? 115 ARG   A CD  1 
ATOM   861  N  NE  . ARG   A 1 109 ? 17.489 -4.847  13.579 1.00 46.23 ? 115 ARG   A NE  1 
ATOM   862  C  CZ  . ARG   A 1 109 ? 18.483 -4.580  12.733 1.00 47.98 ? 115 ARG   A CZ  1 
ATOM   863  N  NH1 . ARG   A 1 109 ? 18.451 -5.044  11.490 1.00 49.61 ? 115 ARG   A NH1 1 
ATOM   864  N  NH2 . ARG   A 1 109 ? 19.509 -3.834  13.121 1.00 45.18 ? 115 ARG   A NH2 1 
ATOM   865  N  N   . CYS   A 1 110 ? 12.774 -4.182  10.016 1.00 23.55 ? 116 CYS   A N   1 
ATOM   866  C  CA  . CYS   A 1 110 ? 11.858 -5.127  9.409  1.00 25.34 ? 116 CYS   A CA  1 
ATOM   867  C  C   . CYS   A 1 110 ? 12.746 -6.279  8.806  1.00 27.14 ? 116 CYS   A C   1 
ATOM   868  O  O   . CYS   A 1 110 ? 13.982 -6.245  8.925  1.00 27.28 ? 116 CYS   A O   1 
ATOM   869  C  CB  . CYS   A 1 110 ? 11.079 -4.397  8.326  1.00 25.35 ? 116 CYS   A CB  1 
ATOM   870  S  SG  . CYS   A 1 110 ? 12.090 -3.913  6.904  1.00 26.18 ? 116 CYS   A SG  1 
ATOM   871  N  N   . GLN   A 1 111 ? 12.129 -7.243  8.111  1.00 29.05 ? 117 GLN   A N   1 
ATOM   872  C  CA  . GLN   A 1 111 ? 12.888 -8.308  7.442  1.00 31.52 ? 117 GLN   A CA  1 
ATOM   873  C  C   . GLN   A 1 111 ? 13.948 -7.794  6.484  1.00 32.71 ? 117 GLN   A C   1 
ATOM   874  O  O   . GLN   A 1 111 ? 14.898 -8.526  6.179  1.00 35.27 ? 117 GLN   A O   1 
ATOM   875  C  CB  . GLN   A 1 111 ? 11.919 -9.251  6.699  1.00 34.24 ? 117 GLN   A CB  1 
ATOM   876  C  CG  . GLN   A 1 111 ? 11.239 -8.636  5.479  1.00 38.11 ? 117 GLN   A CG  1 
ATOM   877  C  CD  . GLN   A 1 111 ? 10.208 -9.570  4.870  1.00 43.21 ? 117 GLN   A CD  1 
ATOM   878  O  OE1 . GLN   A 1 111 ? 9.000  -9.437  5.107  1.00 43.97 ? 117 GLN   A OE1 1 
ATOM   879  N  NE2 . GLN   A 1 111 ? 10.666 -10.530 4.076  1.00 43.03 ? 117 GLN   A NE2 1 
ATOM   880  N  N   . HIS   A 1 112 ? 13.817 -6.555  5.986  1.00 31.80 ? 118 HIS   A N   1 
ATOM   881  C  CA  . HIS   A 1 112 ? 14.769 -6.042  4.980  1.00 31.45 ? 118 HIS   A CA  1 
ATOM   882  C  C   . HIS   A 1 112 ? 15.939 -5.276  5.515  1.00 31.18 ? 118 HIS   A C   1 
ATOM   883  O  O   . HIS   A 1 112 ? 16.858 -4.958  4.759  1.00 31.83 ? 118 HIS   A O   1 
ATOM   884  C  CB  . HIS   A 1 112 ? 14.062 -5.184  3.942  1.00 31.39 ? 118 HIS   A CB  1 
ATOM   885  C  CG  . HIS   A 1 112 ? 12.885 -5.875  3.328  1.00 32.52 ? 118 HIS   A CG  1 
ATOM   886  N  ND1 . HIS   A 1 112 ? 11.608 -5.519  3.662  1.00 32.96 ? 118 HIS   A ND1 1 
ATOM   887  C  CD2 . HIS   A 1 112 ? 12.840 -6.838  2.371  1.00 34.29 ? 118 HIS   A CD2 1 
ATOM   888  C  CE1 . HIS   A 1 112 ? 10.806 -6.298  2.943  1.00 33.96 ? 118 HIS   A CE1 1 
ATOM   889  N  NE2 . HIS   A 1 112 ? 11.503 -7.114  2.153  1.00 34.95 ? 118 HIS   A NE2 1 
ATOM   890  N  N   . GLY   A 1 113 ? 15.885 -4.916  6.788  1.00 29.02 ? 119 GLY   A N   1 
ATOM   891  C  CA  . GLY   A 1 113 ? 16.962 -4.157  7.385  1.00 27.75 ? 119 GLY   A CA  1 
ATOM   892  C  C   . GLY   A 1 113 ? 16.437 -3.061  8.288  1.00 26.16 ? 119 GLY   A C   1 
ATOM   893  O  O   . GLY   A 1 113 ? 15.317 -3.132  8.769  1.00 25.47 ? 119 GLY   A O   1 
ATOM   894  N  N   . VAL   A 1 114 ? 17.271 -2.056  8.515  1.00 24.52 ? 120 VAL   A N   1 
ATOM   895  C  CA  . VAL   A 1 114 ? 16.911 -0.902  9.316  1.00 24.25 ? 120 VAL   A CA  1 
ATOM   896  C  C   . VAL   A 1 114 ? 15.943 -0.005  8.594  1.00 23.47 ? 120 VAL   A C   1 
ATOM   897  O  O   . VAL   A 1 114 ? 16.188 0.422   7.450  1.00 24.46 ? 120 VAL   A O   1 
ATOM   898  C  CB  . VAL   A 1 114 ? 18.173 -0.115  9.727  1.00 25.35 ? 120 VAL   A CB  1 
ATOM   899  C  CG1 . VAL   A 1 114 ? 17.783 1.124   10.548 1.00 25.85 ? 120 VAL   A CG1 1 
ATOM   900  C  CG2 . VAL   A 1 114 ? 19.122 -1.022  10.516 1.00 26.92 ? 120 VAL   A CG2 1 
ATOM   901  N  N   . VAL   A 1 115 ? 14.854 0.306   9.268  1.00 22.36 ? 121 VAL   A N   1 
ATOM   902  C  CA  . VAL   A 1 115 ? 13.799 1.169   8.770  1.00 21.95 ? 121 VAL   A CA  1 
ATOM   903  C  C   . VAL   A 1 115 ? 13.971 2.613   9.251  1.00 22.34 ? 121 VAL   A C   1 
ATOM   904  O  O   . VAL   A 1 115 ? 13.665 3.551   8.534  1.00 22.73 ? 121 VAL   A O   1 
ATOM   905  C  CB  . VAL   A 1 115 ? 12.426 0.594   9.204  1.00 21.92 ? 121 VAL   A CB  1 
ATOM   906  C  CG1 . VAL   A 1 115 ? 11.268 1.535   8.861  1.00 22.05 ? 121 VAL   A CG1 1 
ATOM   907  C  CG2 . VAL   A 1 115 ? 12.200 -0.795  8.665  1.00 21.23 ? 121 VAL   A CG2 1 
ATOM   908  N  N   . GLY   A 1 116 ? 14.333 2.780   10.531 1.00 21.37 ? 122 GLY   A N   1 
ATOM   909  C  CA  . GLY   A 1 116 ? 14.506 4.105   11.096 1.00 21.68 ? 122 GLY   A CA  1 
ATOM   910  C  C   . GLY   A 1 116 ? 14.884 4.027   12.552 1.00 21.61 ? 122 GLY   A C   1 
ATOM   911  O  O   . GLY   A 1 116 ? 15.242 2.947   13.032 1.00 22.95 ? 122 GLY   A O   1 
ATOM   912  N  N   . ILE   A 1 117 ? 14.839 5.154   13.248 1.00 20.30 ? 123 ILE   A N   1 
ATOM   913  C  CA  . ILE   A 1 117 ? 15.220 5.193   14.673 1.00 19.40 ? 123 ILE   A CA  1 
ATOM   914  C  C   . ILE   A 1 117 ? 14.177 5.914   15.474 1.00 20.07 ? 123 ILE   A C   1 
ATOM   915  O  O   . ILE   A 1 117 ? 13.569 6.853   14.986 1.00 20.09 ? 123 ILE   A O   1 
ATOM   916  C  CB  . ILE   A 1 117 ? 16.600 5.902   14.886 1.00 20.88 ? 123 ILE   A CB  1 
ATOM   917  C  CG1 . ILE   A 1 117 ? 16.612 7.249   14.182 1.00 21.87 ? 123 ILE   A CG1 1 
ATOM   918  C  CG2 . ILE   A 1 117 ? 17.779 4.985   14.469 1.00 22.86 ? 123 ILE   A CG2 1 
ATOM   919  C  CD1 . ILE   A 1 117 ? 17.965 8.072   14.329 1.00 22.82 ? 123 ILE   A CD1 1 
ATOM   920  N  N   . VAL   A 1 118 ? 13.981 5.538   16.769 1.00 20.48 ? 124 VAL   A N   1 
ATOM   921  C  CA  . VAL   A 1 118 ? 13.048 6.243   17.628 1.00 20.18 ? 124 VAL   A CA  1 
ATOM   922  C  C   . VAL   A 1 118 ? 13.366 7.746   17.647 1.00 21.44 ? 124 VAL   A C   1 
ATOM   923  O  O   . VAL   A 1 118 ? 14.551 8.142   17.800 1.00 20.58 ? 124 VAL   A O   1 
ATOM   924  C  CB  . VAL   A 1 118 ? 13.108 5.652   19.043 1.00 20.77 ? 124 VAL   A CB  1 
ATOM   925  C  CG1 . VAL   A 1 118 ? 12.275 6.491   20.004 1.00 22.17 ? 124 VAL   A CG1 1 
ATOM   926  C  CG2 . VAL   A 1 118 ? 12.607 4.193   19.038 1.00 21.83 ? 124 VAL   A CG2 1 
ATOM   927  N  N   . SER   A 1 119 ? 12.341 8.562   17.496 1.00 21.21 ? 125 SER   A N   1 
ATOM   928  C  CA  . SER   A 1 119 ? 12.561 10.017  17.475 1.00 21.88 ? 125 SER   A CA  1 
ATOM   929  C  C   . SER   A 1 119 ? 11.535 10.763  18.313 1.00 24.24 ? 125 SER   A C   1 
ATOM   930  O  O   . SER   A 1 119 ? 11.873 11.782  18.916 1.00 24.96 ? 125 SER   A O   1 
ATOM   931  C  CB  . SER   A 1 119 ? 12.569 10.528  16.035 1.00 21.60 ? 125 SER   A CB  1 
ATOM   932  O  OG  . SER   A 1 119 ? 12.709 11.947  15.986 1.00 24.87 ? 125 SER   A OG  1 
ATOM   933  N  N   . THR   A 1 120 ? 10.273 10.242  18.392 1.00 24.08 ? 126 THR   A N   1 
ATOM   934  C  CA  . THR   A 1 120 ? 9.253  10.926  19.191 1.00 25.23 ? 126 THR   A CA  1 
ATOM   935  C  C   . THR   A 1 120 ? 8.457  9.908   20.046 1.00 27.66 ? 126 THR   A C   1 
ATOM   936  O  O   . THR   A 1 120 ? 8.612  8.684   19.883 1.00 27.32 ? 126 THR   A O   1 
ATOM   937  C  CB  . THR   A 1 120 ? 8.301  11.762  18.264 1.00 25.56 ? 126 THR   A CB  1 
ATOM   938  O  OG1 . THR   A 1 120 ? 7.407  10.866  17.624 1.00 25.96 ? 126 THR   A OG1 1 
ATOM   939  C  CG2 . THR   A 1 120 ? 9.029  12.576  17.209 1.00 25.26 ? 126 THR   A CG2 1 
ATOM   940  N  N   . GLY   A 1 121 ? 7.578  10.409  20.916 1.00 29.64 ? 127 GLY   A N   1 
ATOM   941  C  CA  . GLY   A 1 121 ? 6.753  9.528   21.724 1.00 31.55 ? 127 GLY   A CA  1 
ATOM   942  C  C   . GLY   A 1 121 ? 5.837  10.267  22.659 1.00 34.51 ? 127 GLY   A C   1 
ATOM   943  O  O   . GLY   A 1 121 ? 5.657  11.475  22.539 1.00 34.64 ? 127 GLY   A O   1 
ATOM   944  N  N   . GLY   A 1 122 ? 5.354  9.543   23.651 1.00 37.16 ? 128 GLY   A N   1 
ATOM   945  C  CA  . GLY   A 1 122 ? 4.438  10.075  24.645 1.00 39.00 ? 128 GLY   A CA  1 
ATOM   946  C  C   . GLY   A 1 122 ? 3.029  9.597   24.363 1.00 40.42 ? 128 GLY   A C   1 
ATOM   947  O  O   . GLY   A 1 122 ? 2.674  9.370   23.202 1.00 40.72 ? 128 GLY   A O   1 
ATOM   948  N  N   . ASN   A 1 123 ? 2.232  9.410   25.428 1.00 40.82 ? 129 ASN   A N   1 
ATOM   949  C  CA  . ASN   A 1 123 ? 0.832  8.986   25.341 1.00 41.15 ? 129 ASN   A CA  1 
ATOM   950  C  C   . ASN   A 1 123 ? 0.610  7.578   24.816 1.00 39.05 ? 129 ASN   A C   1 
ATOM   951  O  O   . ASN   A 1 123 ? -0.456 7.289   24.267 1.00 40.24 ? 129 ASN   A O   1 
ATOM   952  C  CB  . ASN   A 1 123 ? 0.023  9.985   24.512 1.00 43.95 ? 129 ASN   A CB  1 
ATOM   953  C  CG  . ASN   A 1 123 ? -0.221 11.290  25.225 1.00 49.45 ? 129 ASN   A CG  1 
ATOM   954  O  OD1 . ASN   A 1 123 ? -0.299 11.340  26.463 1.00 51.04 ? 129 ASN   A OD1 1 
ATOM   955  N  ND2 . ASN   A 1 123 ? -0.385 12.360  24.447 1.00 50.16 ? 129 ASN   A ND2 1 
ATOM   956  N  N   . GLY   A 1 124 ? 1.569  6.685   25.034 1.00 35.62 ? 130 GLY   A N   1 
ATOM   957  C  CA  . GLY   A 1 124 ? 1.432  5.316   24.553 1.00 32.24 ? 130 GLY   A CA  1 
ATOM   958  C  C   . GLY   A 1 124 ? 1.727  5.180   23.074 1.00 28.64 ? 130 GLY   A C   1 
ATOM   959  O  O   . GLY   A 1 124 ? 1.417  4.154   22.474 1.00 28.10 ? 130 GLY   A O   1 
ATOM   960  N  N   . LEU   A 1 125 ? 2.364  6.197   22.485 1.00 27.46 ? 131 LEU   A N   1 
ATOM   961  C  CA  . LEU   A 1 125 ? 2.800  6.133   21.107 1.00 27.66 ? 131 LEU   A CA  1 
ATOM   962  C  C   . LEU   A 1 125 ? 4.352  6.192   21.049 1.00 27.94 ? 131 LEU   A C   1 
ATOM   963  O  O   . LEU   A 1 125 ? 5.026  6.546   22.032 1.00 29.30 ? 131 LEU   A O   1 
ATOM   964  C  CB  . LEU   A 1 125 ? 2.205  7.292   20.297 1.00 28.73 ? 131 LEU   A CB  1 
ATOM   965  C  CG  . LEU   A 1 125 ? 0.678  7.332   20.208 1.00 32.32 ? 131 LEU   A CG  1 
ATOM   966  C  CD1 . LEU   A 1 125 ? 0.212  8.704   19.790 1.00 34.89 ? 131 LEU   A CD1 1 
ATOM   967  C  CD2 . LEU   A 1 125 ? 0.155  6.254   19.291 1.00 32.97 ? 131 LEU   A CD2 1 
ATOM   968  N  N   . VAL   A 1 126 ? 4.912  5.782   19.902 1.00 24.82 ? 132 VAL   A N   1 
ATOM   969  C  CA  . VAL   A 1 126 ? 6.326  5.884   19.641 1.00 23.13 ? 132 VAL   A CA  1 
ATOM   970  C  C   . VAL   A 1 126 ? 6.437  6.269   18.162 1.00 22.43 ? 132 VAL   A C   1 
ATOM   971  O  O   . VAL   A 1 126 ? 5.696  5.770   17.346 1.00 23.35 ? 132 VAL   A O   1 
ATOM   972  C  CB  . VAL   A 1 126 ? 7.111  4.580   19.989 1.00 22.88 ? 132 VAL   A CB  1 
ATOM   973  C  CG1 . VAL   A 1 126 ? 6.495  3.334   19.378 1.00 21.86 ? 132 VAL   A CG1 1 
ATOM   974  C  CG2 . VAL   A 1 126 ? 8.592  4.712   19.631 1.00 22.54 ? 132 VAL   A CG2 1 
ATOM   975  N  N   . GLY   A 1 127 ? 7.261  7.244   17.868 1.00 21.48 ? 133 GLY   A N   1 
ATOM   976  C  CA  . GLY   A 1 127 ? 7.477  7.720   16.514 1.00 22.15 ? 133 GLY   A CA  1 
ATOM   977  C  C   . GLY   A 1 127 ? 8.892  7.442   16.058 1.00 22.27 ? 133 GLY   A C   1 
ATOM   978  O  O   . GLY   A 1 127 ? 9.838  7.611   16.827 1.00 23.02 ? 133 GLY   A O   1 
ATOM   979  N  N   . PHE   A 1 128 ? 9.062  7.051   14.798 1.00 21.59 ? 134 PHE   A N   1 
ATOM   980  C  CA  . PHE   A 1 128 ? 10.363 6.698   14.270 1.00 20.71 ? 134 PHE   A CA  1 
ATOM   981  C  C   . PHE   A 1 128 ? 10.652 7.562   13.067 1.00 21.33 ? 134 PHE   A C   1 
ATOM   982  O  O   . PHE   A 1 128 ? 9.787  7.718   12.206 1.00 21.40 ? 134 PHE   A O   1 
ATOM   983  C  CB  . PHE   A 1 128 ? 10.359 5.245   13.787 1.00 19.69 ? 134 PHE   A CB  1 
ATOM   984  C  CG  . PHE   A 1 128 ? 9.822  4.280   14.811 1.00 19.89 ? 134 PHE   A CG  1 
ATOM   985  C  CD1 . PHE   A 1 128 ? 10.661 3.714   15.750 1.00 19.73 ? 134 PHE   A CD1 1 
ATOM   986  C  CD2 . PHE   A 1 128 ? 8.492  3.861   14.767 1.00 20.31 ? 134 PHE   A CD2 1 
ATOM   987  C  CE1 . PHE   A 1 128 ? 10.171 2.820   16.698 1.00 20.44 ? 134 PHE   A CE1 1 
ATOM   988  C  CE2 . PHE   A 1 128 ? 8.004  2.958   15.724 1.00 21.51 ? 134 PHE   A CE2 1 
ATOM   989  C  CZ  . PHE   A 1 128 ? 8.858  2.421   16.656 1.00 21.32 ? 134 PHE   A CZ  1 
ATOM   990  N  N   . ALA   A 1 129 ? 11.882 8.078   13.002 1.00 20.35 ? 135 ALA   A N   1 
ATOM   991  C  CA  . ALA   A 1 129 ? 12.333 8.864   11.881 1.00 21.07 ? 135 ALA   A CA  1 
ATOM   992  C  C   . ALA   A 1 129 ? 12.716 7.852   10.789 1.00 21.76 ? 135 ALA   A C   1 
ATOM   993  O  O   . ALA   A 1 129 ? 13.621 7.044   10.977 1.00 20.87 ? 135 ALA   A O   1 
ATOM   994  C  CB  . ALA   A 1 129 ? 13.567 9.730   12.292 1.00 21.03 ? 135 ALA   A CB  1 
ATOM   995  N  N   . ASP   A 1 130 ? 12.035 7.908   9.617  1.00 22.97 ? 136 ASP   A N   1 
ATOM   996  C  CA  . ASP   A 1 130 ? 12.337 6.975   8.519  1.00 24.07 ? 136 ASP   A CA  1 
ATOM   997  C  C   . ASP   A 1 130 ? 13.676 7.262   7.887  1.00 24.53 ? 136 ASP   A C   1 
ATOM   998  O  O   . ASP   A 1 130 ? 14.025 8.433   7.711  1.00 24.42 ? 136 ASP   A O   1 
ATOM   999  C  CB  . ASP   A 1 130 ? 11.272 7.114   7.408  1.00 24.51 ? 136 ASP   A CB  1 
ATOM   1000 C  CG  . ASP   A 1 130 ? 11.405 6.076   6.309  1.00 29.68 ? 136 ASP   A CG  1 
ATOM   1001 O  OD1 . ASP   A 1 130 ? 11.471 4.887   6.630  1.00 31.34 ? 136 ASP   A OD1 1 
ATOM   1002 O  OD2 . ASP   A 1 130 ? 11.490 6.461   5.130  1.00 33.06 ? 136 ASP   A OD2 1 
ATOM   1003 N  N   . VAL   A 1 131 ? 14.412 6.208   7.470  1.00 23.86 ? 137 VAL   A N   1 
ATOM   1004 C  CA  . VAL   A 1 131 ? 15.681 6.395   6.731  1.00 24.78 ? 137 VAL   A CA  1 
ATOM   1005 C  C   . VAL   A 1 131 ? 15.670 5.655   5.378  1.00 25.57 ? 137 VAL   A C   1 
ATOM   1006 O  O   . VAL   A 1 131 ? 16.599 5.820   4.609  1.00 26.05 ? 137 VAL   A O   1 
ATOM   1007 C  CB  . VAL   A 1 131 ? 16.946 6.007   7.531  1.00 25.17 ? 137 VAL   A CB  1 
ATOM   1008 C  CG1 . VAL   A 1 131 ? 16.999 6.782   8.845  1.00 24.51 ? 137 VAL   A CG1 1 
ATOM   1009 C  CG2 . VAL   A 1 131 ? 16.949 4.506   7.806  1.00 25.24 ? 137 VAL   A CG2 1 
ATOM   1010 N  N   . ARG   A 1 132 ? 14.608 4.882   5.072  1.00 25.01 ? 138 ARG   A N   1 
ATOM   1011 C  CA  . ARG   A 1 132 ? 14.535 4.106   3.835  1.00 24.47 ? 138 ARG   A CA  1 
ATOM   1012 C  C   . ARG   A 1 132 ? 14.551 4.918   2.562  1.00 26.73 ? 138 ARG   A C   1 
ATOM   1013 O  O   . ARG   A 1 132 ? 14.861 4.341   1.520  1.00 28.29 ? 138 ARG   A O   1 
ATOM   1014 C  CB  . ARG   A 1 132 ? 13.323 3.176   3.830  1.00 22.37 ? 138 ARG   A CB  1 
ATOM   1015 C  CG  . ARG   A 1 132 ? 13.279 2.289   5.080  1.00 20.48 ? 138 ARG   A CG  1 
ATOM   1016 C  CD  . ARG   A 1 132 ? 11.977 1.466   5.065  1.00 22.77 ? 138 ARG   A CD  1 
ATOM   1017 N  NE  . ARG   A 1 132 ? 10.849 2.330   5.446  1.00 22.92 ? 138 ARG   A NE  1 
ATOM   1018 C  CZ  . ARG   A 1 132 ? 9.610  1.894   5.647  1.00 24.51 ? 138 ARG   A CZ  1 
ATOM   1019 N  NH1 . ARG   A 1 132 ? 9.296  0.627   5.396  1.00 25.51 ? 138 ARG   A NH1 1 
ATOM   1020 N  NH2 . ARG   A 1 132 ? 8.671  2.724   6.095  1.00 24.80 ? 138 ARG   A NH2 1 
ATOM   1021 N  N   . ASP   A 1 133 ? 14.156 6.205   2.599  1.00 26.70 ? 139 ASP   A N   1 
ATOM   1022 C  CA  . ASP   A 1 133 ? 14.199 7.053   1.404  1.00 27.35 ? 139 ASP   A CA  1 
ATOM   1023 C  C   . ASP   A 1 133 ? 15.622 7.629   1.150  1.00 27.62 ? 139 ASP   A C   1 
ATOM   1024 O  O   . ASP   A 1 133 ? 15.869 8.183   0.077  1.00 28.93 ? 139 ASP   A O   1 
ATOM   1025 C  CB  . ASP   A 1 133 ? 13.193 8.201   1.535  1.00 28.95 ? 139 ASP   A CB  1 
ATOM   1026 C  CG  . ASP   A 1 133 ? 13.594 9.199   2.598  1.00 31.11 ? 139 ASP   A CG  1 
ATOM   1027 O  OD1 . ASP   A 1 133 ? 13.875 8.766   3.747  1.00 29.29 ? 139 ASP   A OD1 1 
ATOM   1028 O  OD2 . ASP   A 1 133 ? 13.641 10.406  2.284  1.00 33.25 ? 139 ASP   A OD2 1 
ATOM   1029 N  N   . LEU   A 1 134 ? 16.558 7.480   2.099  1.00 26.49 ? 140 LEU   A N   1 
ATOM   1030 C  CA  . LEU   A 1 134 ? 17.920 8.007   1.929  1.00 27.12 ? 140 LEU   A CA  1 
ATOM   1031 C  C   . LEU   A 1 134 ? 18.747 6.974   1.167  1.00 28.83 ? 140 LEU   A C   1 
ATOM   1032 O  O   . LEU   A 1 134 ? 19.599 6.286   1.733  1.00 28.69 ? 140 LEU   A O   1 
ATOM   1033 C  CB  . LEU   A 1 134 ? 18.514 8.296   3.319  1.00 26.22 ? 140 LEU   A CB  1 
ATOM   1034 C  CG  . LEU   A 1 134 ? 17.709 9.313   4.145  1.00 26.87 ? 140 LEU   A CG  1 
ATOM   1035 C  CD1 . LEU   A 1 134 ? 18.255 9.447   5.561  1.00 27.25 ? 140 LEU   A CD1 1 
ATOM   1036 C  CD2 . LEU   A 1 134 ? 17.654 10.659  3.463  1.00 27.48 ? 140 LEU   A CD2 1 
ATOM   1037 N  N   . LEU   A 1 135 ? 18.493 6.874   -0.150 1.00 30.03 ? 141 LEU   A N   1 
ATOM   1038 C  CA  . LEU   A 1 135 ? 19.112 5.874   -1.000 1.00 31.39 ? 141 LEU   A CA  1 
ATOM   1039 C  C   . LEU   A 1 135 ? 20.616 6.014   -1.084 1.00 32.61 ? 141 LEU   A C   1 
ATOM   1040 O  O   . LEU   A 1 135 ? 21.325 5.018   -1.247 1.00 33.34 ? 141 LEU   A O   1 
ATOM   1041 C  CB  . LEU   A 1 135 ? 18.492 5.910   -2.406 1.00 31.77 ? 141 LEU   A CB  1 
ATOM   1042 C  CG  . LEU   A 1 135 ? 16.955 5.910   -2.509 1.00 34.16 ? 141 LEU   A CG  1 
ATOM   1043 C  CD1 . LEU   A 1 135 ? 16.499 5.793   -3.974 1.00 35.98 ? 141 LEU   A CD1 1 
ATOM   1044 C  CD2 . LEU   A 1 135 ? 16.310 4.805   -1.686 1.00 34.82 ? 141 LEU   A CD2 1 
ATOM   1045 N  N   . TRP   A 1 136 ? 21.115 7.257   -1.008 1.00 32.42 ? 142 TRP   A N   1 
ATOM   1046 C  CA  . TRP   A 1 136 ? 22.540 7.513   -1.054 1.00 32.48 ? 142 TRP   A CA  1 
ATOM   1047 C  C   . TRP   A 1 136 ? 23.284 6.868   0.121  1.00 34.09 ? 142 TRP   A C   1 
ATOM   1048 O  O   . TRP   A 1 136 ? 24.489 6.741   0.036  1.00 35.05 ? 142 TRP   A O   1 
ATOM   1049 C  CB  . TRP   A 1 136 ? 22.809 9.019   -1.128 1.00 31.65 ? 142 TRP   A CB  1 
ATOM   1050 C  CG  . TRP   A 1 136 ? 22.129 9.799   -0.045 1.00 30.68 ? 142 TRP   A CG  1 
ATOM   1051 C  CD1 . TRP   A 1 136 ? 20.948 10.476  -0.136 1.00 30.86 ? 142 TRP   A CD1 1 
ATOM   1052 C  CD2 . TRP   A 1 136 ? 22.644 10.059  1.266  1.00 30.16 ? 142 TRP   A CD2 1 
ATOM   1053 N  NE1 . TRP   A 1 136 ? 20.673 11.100  1.055  1.00 31.52 ? 142 TRP   A NE1 1 
ATOM   1054 C  CE2 . TRP   A 1 136 ? 21.711 10.879  1.927  1.00 30.94 ? 142 TRP   A CE2 1 
ATOM   1055 C  CE3 . TRP   A 1 136 ? 23.819 9.696   1.938  1.00 30.52 ? 142 TRP   A CE3 1 
ATOM   1056 C  CZ2 . TRP   A 1 136 ? 21.901 11.313  3.239  1.00 31.26 ? 142 TRP   A CZ2 1 
ATOM   1057 C  CZ3 . TRP   A 1 136 ? 24.011 10.139  3.231  1.00 30.99 ? 142 TRP   A CZ3 1 
ATOM   1058 C  CH2 . TRP   A 1 136 ? 23.055 10.932  3.868  1.00 31.01 ? 142 TRP   A CH2 1 
ATOM   1059 N  N   . LEU   A 1 137 ? 22.588 6.424   1.200  1.00 34.53 ? 143 LEU   A N   1 
ATOM   1060 C  CA  . LEU   A 1 137 ? 23.278 5.734   2.287  1.00 36.13 ? 143 LEU   A CA  1 
ATOM   1061 C  C   . LEU   A 1 137 ? 23.903 4.408   1.777  1.00 39.39 ? 143 LEU   A C   1 
ATOM   1062 O  O   . LEU   A 1 137 ? 24.861 3.942   2.369  1.00 39.80 ? 143 LEU   A O   1 
ATOM   1063 C  CB  . LEU   A 1 137 ? 22.326 5.429   3.451  1.00 35.42 ? 143 LEU   A CB  1 
ATOM   1064 C  CG  . LEU   A 1 137 ? 21.876 6.595   4.315  1.00 35.23 ? 143 LEU   A CG  1 
ATOM   1065 C  CD1 . LEU   A 1 137 ? 20.767 6.138   5.283  1.00 34.90 ? 143 LEU   A CD1 1 
ATOM   1066 C  CD2 . LEU   A 1 137 ? 23.030 7.138   5.125  1.00 35.83 ? 143 LEU   A CD2 1 
ATOM   1067 N  N   . ASP   A 1 138 ? 23.354 3.802   0.692  1.00 41.86 ? 144 ASP   A N   1 
ATOM   1068 C  CA  . ASP   A 1 138 ? 23.804 2.512   0.130  1.00 44.42 ? 144 ASP   A CA  1 
ATOM   1069 C  C   . ASP   A 1 138 ? 25.038 2.599   -0.752 1.00 47.77 ? 144 ASP   A C   1 
ATOM   1070 O  O   . ASP   A 1 138 ? 25.549 1.551   -1.147 1.00 48.50 ? 144 ASP   A O   1 
ATOM   1071 C  CB  . ASP   A 1 138 ? 22.699 1.877   -0.728 1.00 44.97 ? 144 ASP   A CB  1 
ATOM   1072 C  CG  . ASP   A 1 138 ? 21.434 1.494   -0.009 1.00 48.31 ? 144 ASP   A CG  1 
ATOM   1073 O  OD1 . ASP   A 1 138 ? 21.425 1.531   1.241  1.00 47.55 ? 144 ASP   A OD1 1 
ATOM   1074 O  OD2 . ASP   A 1 138 ? 20.442 1.158   -0.696 1.00 50.65 ? 144 ASP   A OD2 1 
ATOM   1075 N  N   . GLU   A 1 139 ? 25.478 3.807   -1.128 1.00 49.60 ? 145 GLU   A N   1 
ATOM   1076 C  CA  . GLU   A 1 139 ? 26.644 3.930   -1.999 1.00 51.96 ? 145 GLU   A CA  1 
ATOM   1077 C  C   . GLU   A 1 139 ? 27.647 4.978   -1.521 1.00 53.09 ? 145 GLU   A C   1 
ATOM   1078 O  O   . GLU   A 1 139 ? 27.246 5.987   -0.946 1.00 53.78 ? 145 GLU   A O   1 
ATOM   1079 C  CB  . GLU   A 1 139 ? 26.205 4.205   -3.445 1.00 56.30 ? 145 GLU   A CB  1 
ATOM   1080 C  CG  . GLU   A 1 139 ? 25.293 5.410   -3.591 1.00 63.15 ? 145 GLU   A CG  1 
ATOM   1081 C  CD  . GLU   A 1 139 ? 24.155 5.177   -4.564 1.00 72.17 ? 145 GLU   A CD  1 
ATOM   1082 O  OE1 . GLU   A 1 139 ? 23.716 6.153   -5.217 1.00 72.99 ? 145 GLU   A OE1 1 
ATOM   1083 O  OE2 . GLU   A 1 139 ? 23.702 4.013   -4.673 1.00 75.76 ? 145 GLU   A OE2 1 
HETATM 1084 N  N1  . A1B4F B 2 .   ? 12.036 14.384  17.492 1.00 27.95 ? 201 A1B4F A N1  1 
HETATM 1085 C  C4  . A1B4F B 2 .   ? 9.064  12.324  24.266 1.00 29.42 ? 201 A1B4F A C4  1 
HETATM 1086 C  C5  . A1B4F B 2 .   ? 9.993  12.680  23.300 1.00 29.82 ? 201 A1B4F A C5  1 
HETATM 1087 C  C6  . A1B4F B 2 .   ? 10.323 14.145  23.109 1.00 30.71 ? 201 A1B4F A C6  1 
HETATM 1088 C  C7  . A1B4F B 2 .   ? 11.026 14.736  20.853 1.00 30.07 ? 201 A1B4F A C7  1 
HETATM 1089 C  C8  . A1B4F B 2 .   ? 12.206 14.668  19.878 1.00 30.14 ? 201 A1B4F A C8  1 
HETATM 1090 C  C10 . A1B4F B 2 .   ? 13.384 15.481  20.422 1.00 30.86 ? 201 A1B4F A C10 1 
HETATM 1091 C  C13 . A1B4F B 2 .   ? 10.639 11.667  22.591 1.00 29.14 ? 201 A1B4F A C13 1 
HETATM 1092 O  O1  . A1B4F B 2 .   ? 12.902 14.559  23.956 1.00 32.77 ? 201 A1B4F A O1  1 
HETATM 1093 C  C12 . A1B4F B 2 .   ? 12.682 14.641  22.755 1.00 30.84 ? 201 A1B4F A C12 1 
HETATM 1094 C  C11 . A1B4F B 2 .   ? 13.802 15.012  21.819 1.00 31.08 ? 201 A1B4F A C11 1 
HETATM 1095 C  C9  . A1B4F B 2 .   ? 11.757 15.171  18.517 1.00 29.04 ? 201 A1B4F A C9  1 
HETATM 1096 O  O   . A1B4F B 2 .   ? 11.119 16.222  18.401 1.00 28.64 ? 201 A1B4F A O   1 
HETATM 1097 N  N   . A1B4F B 2 .   ? 11.447 14.460  22.232 1.00 30.33 ? 201 A1B4F A N   1 
HETATM 1098 C  C3  . A1B4F B 2 .   ? 8.808  10.994  24.539 1.00 29.66 ? 201 A1B4F A C3  1 
HETATM 1099 C  C2  . A1B4F B 2 .   ? 9.479  10.004  23.844 1.00 28.98 ? 201 A1B4F A C2  1 
HETATM 1100 C  C1  . A1B4F B 2 .   ? 10.396 10.322  22.857 1.00 28.87 ? 201 A1B4F A C1  1 
HETATM 1101 C  C   . A1B4F B 2 .   ? 11.169 9.235   22.146 1.00 29.32 ? 201 A1B4F A C   1 
HETATM 1102 ZN ZN  . ZN    C 3 .   ? 10.907 -4.093  4.975  1.00 28.11 2 202 ZN    A ZN  1 
HETATM 1103 S  S   . DMS   D 4 .   ? 14.912 21.147  6.714  1.00 88.50 ? 203 DMS   A S   1 
HETATM 1104 O  O   . DMS   D 4 .   ? 14.538 21.451  8.148  1.00 88.26 ? 203 DMS   A O   1 
HETATM 1105 C  C1  . DMS   D 4 .   ? 13.398 21.122  5.708  1.00 88.40 ? 203 DMS   A C1  1 
HETATM 1106 C  C2  . DMS   D 4 .   ? 15.635 22.643  5.971  1.00 88.57 ? 203 DMS   A C2  1 
HETATM 1107 S  S   . DMS   E 4 .   ? 19.786 -3.309  21.754 1.00 95.73 ? 204 DMS   A S   1 
HETATM 1108 O  O   . DMS   E 4 .   ? 20.632 -4.050  22.743 1.00 95.74 ? 204 DMS   A O   1 
HETATM 1109 C  C1  . DMS   E 4 .   ? 20.742 -1.850  21.246 1.00 95.82 ? 204 DMS   A C1  1 
HETATM 1110 C  C2  . DMS   E 4 .   ? 19.867 -4.178  20.157 1.00 95.60 ? 204 DMS   A C2  1 
HETATM 1111 S  S   . DMS   F 4 .   ? 3.903  11.342  18.637 1.00 84.27 ? 205 DMS   A S   1 
HETATM 1112 O  O   . DMS   F 4 .   ? 4.993  12.366  18.562 1.00 84.23 ? 205 DMS   A O   1 
HETATM 1113 C  C1  . DMS   F 4 .   ? 3.119  11.486  20.268 1.00 84.22 ? 205 DMS   A C1  1 
HETATM 1114 C  C2  . DMS   F 4 .   ? 4.621  9.719   18.965 1.00 84.28 ? 205 DMS   A C2  1 
HETATM 1115 O  O   . HOH   G 5 .   ? 22.435 -5.250  22.006 1.00 45.29 ? 301 HOH   A O   1 
HETATM 1116 O  O   . HOH   G 5 .   ? 13.314 8.144   30.467 1.00 55.84 ? 302 HOH   A O   1 
HETATM 1117 O  O   . HOH   G 5 .   ? 4.043  21.996  22.711 1.00 40.41 ? 303 HOH   A O   1 
HETATM 1118 O  O   . HOH   G 5 .   ? 4.973  6.283   24.589 1.00 37.25 ? 304 HOH   A O   1 
HETATM 1119 O  O   . HOH   G 5 .   ? 2.958  8.585   9.792  1.00 42.31 ? 305 HOH   A O   1 
HETATM 1120 O  O   . HOH   G 5 .   ? 6.784  -4.874  28.344 1.00 38.93 ? 306 HOH   A O   1 
HETATM 1121 O  O   . HOH   G 5 .   ? 12.705 16.196  25.978 1.00 45.33 ? 307 HOH   A O   1 
HETATM 1122 O  O   . HOH   G 5 .   ? 29.347 3.230   9.172  1.00 31.69 ? 308 HOH   A O   1 
HETATM 1123 O  O   . HOH   G 5 .   ? 22.093 -4.600  11.823 1.00 50.20 ? 309 HOH   A O   1 
HETATM 1124 O  O   . HOH   G 5 .   ? 4.474  -4.613  20.902 1.00 38.59 ? 310 HOH   A O   1 
HETATM 1125 O  O   . HOH   G 5 .   ? 34.551 20.217  9.477  1.00 28.48 ? 311 HOH   A O   1 
HETATM 1126 O  O   . HOH   G 5 .   ? 20.703 9.057   18.082 1.00 26.67 ? 312 HOH   A O   1 
HETATM 1127 O  O   . HOH   G 5 .   ? 31.177 11.139  17.732 1.00 45.48 ? 313 HOH   A O   1 
HETATM 1128 O  O   . HOH   G 5 .   ? 5.080  1.018   -2.224 1.00 45.67 ? 314 HOH   A O   1 
HETATM 1129 O  O   . HOH   G 5 .   ? 30.725 18.794  6.292  1.00 46.84 ? 315 HOH   A O   1 
HETATM 1130 O  O   . HOH   G 5 .   ? 10.719 4.928   33.034 1.00 34.52 ? 316 HOH   A O   1 
HETATM 1131 O  O   . HOH   G 5 .   ? 16.633 12.350  23.351 1.00 32.13 ? 317 HOH   A O   1 
HETATM 1132 O  O   . HOH   G 5 .   ? 10.324 18.178  20.083 1.00 31.05 ? 318 HOH   A O   1 
HETATM 1133 O  O   . HOH   G 5 .   ? 15.043 11.771  0.452  1.00 43.54 ? 319 HOH   A O   1 
HETATM 1134 O  O   . HOH   G 5 .   ? 0.935  0.136   16.287 1.00 21.64 ? 320 HOH   A O   1 
HETATM 1135 O  O   . HOH   G 5 .   ? 6.664  13.524  21.130 1.00 33.47 ? 321 HOH   A O   1 
HETATM 1136 O  O   . HOH   G 5 .   ? 8.796  19.555  18.317 1.00 29.01 ? 322 HOH   A O   1 
HETATM 1137 O  O   . HOH   G 5 .   ? 23.680 0.179   14.730 1.00 33.66 ? 323 HOH   A O   1 
HETATM 1138 O  O   . HOH   G 5 .   ? 10.550 8.787   4.163  1.00 33.65 ? 324 HOH   A O   1 
HETATM 1139 O  O   . HOH   G 5 .   ? 15.171 -5.073  17.597 1.00 37.28 ? 325 HOH   A O   1 
HETATM 1140 O  O   . HOH   G 5 .   ? 12.700 21.524  12.918 1.00 31.30 ? 326 HOH   A O   1 
HETATM 1141 O  O   . HOH   G 5 .   ? 19.938 0.000   26.345 1.00 43.50 ? 327 HOH   A O   1 
HETATM 1142 O  O   . HOH   G 5 .   ? 19.081 0.799   -2.991 1.00 44.09 ? 328 HOH   A O   1 
HETATM 1143 O  O   . HOH   G 5 .   ? 10.265 5.408   2.971  1.00 31.07 ? 329 HOH   A O   1 
HETATM 1144 O  O   . HOH   G 5 .   ? 16.928 17.059  28.224 1.00 57.22 ? 330 HOH   A O   1 
HETATM 1145 O  O   . HOH   G 5 .   ? 21.904 21.334  6.046  1.00 42.30 ? 331 HOH   A O   1 
HETATM 1146 O  O   . HOH   G 5 .   ? 20.786 -0.882  -2.456 1.00 48.00 ? 332 HOH   A O   1 
HETATM 1147 O  O   . HOH   G 5 .   ? 15.316 2.831   22.516 1.00 23.72 ? 333 HOH   A O   1 
HETATM 1148 O  O   . HOH   G 5 .   ? 18.833 4.997   26.164 1.00 42.84 ? 334 HOH   A O   1 
HETATM 1149 O  O   . HOH   G 5 .   ? 26.736 4.019   18.600 1.00 48.21 ? 335 HOH   A O   1 
HETATM 1150 O  O   . HOH   G 5 .   ? 11.698 11.984  11.002 1.00 22.25 ? 336 HOH   A O   1 
HETATM 1151 O  O   . HOH   G 5 .   ? 12.106 2.573   32.740 1.00 27.46 ? 337 HOH   A O   1 
HETATM 1152 O  O   . HOH   G 5 .   ? 0.416  15.051  17.056 1.00 48.68 ? 338 HOH   A O   1 
HETATM 1153 O  O   . HOH   G 5 .   ? 8.082  -3.351  0.049  1.00 38.95 ? 339 HOH   A O   1 
HETATM 1154 O  O   . HOH   G 5 .   ? 1.397  -2.124  19.684 1.00 35.46 ? 340 HOH   A O   1 
HETATM 1155 O  O   . HOH   G 5 .   ? 10.770 23.721  24.478 1.00 43.21 ? 341 HOH   A O   1 
HETATM 1156 O  O   . HOH   G 5 .   ? 0.888  2.087   24.216 1.00 40.10 ? 342 HOH   A O   1 
HETATM 1157 O  O   . HOH   G 5 .   ? 31.327 8.771   4.093  1.00 41.73 ? 343 HOH   A O   1 
HETATM 1158 O  O   . HOH   G 5 .   ? 4.395  7.985   3.063  1.00 55.36 ? 344 HOH   A O   1 
HETATM 1159 O  O   . HOH   G 5 .   ? 17.560 -6.380  2.496  1.00 54.99 ? 345 HOH   A O   1 
HETATM 1160 O  O   . HOH   G 5 .   ? 28.109 -1.770  12.206 1.00 43.43 ? 346 HOH   A O   1 
HETATM 1161 O  O   . HOH   G 5 .   ? 11.359 17.885  5.426  1.00 63.43 ? 347 HOH   A O   1 
HETATM 1162 O  O   . HOH   G 5 .   ? 14.347 9.754   28.926 1.00 38.92 ? 348 HOH   A O   1 
HETATM 1163 O  O   . HOH   G 5 .   ? 16.173 -2.890  16.910 1.00 33.35 ? 349 HOH   A O   1 
HETATM 1164 O  O   . HOH   G 5 .   ? 6.381  8.313   27.815 1.00 58.45 ? 350 HOH   A O   1 
HETATM 1165 O  O   . HOH   G 5 .   ? 15.888 23.491  18.441 1.00 41.98 ? 351 HOH   A O   1 
HETATM 1166 O  O   . HOH   G 5 .   ? 18.301 2.764   22.389 1.00 26.92 ? 352 HOH   A O   1 
HETATM 1167 O  O   . HOH   G 5 .   ? 27.011 9.506   20.091 1.00 57.29 ? 353 HOH   A O   1 
HETATM 1168 O  O   . HOH   G 5 .   ? 27.212 -1.314  5.562  1.00 52.03 ? 354 HOH   A O   1 
HETATM 1169 O  O   . HOH   G 5 .   ? 17.934 20.448  18.695 1.00 45.97 ? 355 HOH   A O   1 
HETATM 1170 O  O   . HOH   G 5 .   ? 33.884 -3.149  9.219  1.00 41.01 ? 356 HOH   A O   1 
HETATM 1171 O  O   . HOH   G 5 .   ? 14.335 14.902  3.191  1.00 40.03 ? 357 HOH   A O   1 
HETATM 1172 O  O   . HOH   G 5 .   ? 24.415 22.410  8.646  1.00 29.68 ? 358 HOH   A O   1 
HETATM 1173 O  O   . HOH   G 5 .   ? 16.620 17.410  3.657  1.00 47.45 ? 359 HOH   A O   1 
HETATM 1174 O  O   . HOH   G 5 .   ? 16.664 23.503  14.394 1.00 55.58 ? 360 HOH   A O   1 
HETATM 1175 O  O   . HOH   G 5 .   ? 22.031 -0.549  3.051  1.00 37.87 ? 361 HOH   A O   1 
HETATM 1176 O  O   . HOH   G 5 .   ? 5.511  20.014  25.741 1.00 49.67 ? 362 HOH   A O   1 
HETATM 1177 O  O   . HOH   G 5 .   ? 18.140 21.389  9.039  1.00 30.20 ? 363 HOH   A O   1 
HETATM 1178 O  O   . HOH   G 5 .   ? 8.748  3.233   2.466  1.00 36.16 ? 364 HOH   A O   1 
HETATM 1179 O  O   . HOH   G 5 .   ? 18.609 19.018  16.550 1.00 27.18 ? 365 HOH   A O   1 
HETATM 1180 O  O   . HOH   G 5 .   ? 5.781  2.230   6.159  1.00 42.65 ? 366 HOH   A O   1 
HETATM 1181 O  O   . HOH   G 5 .   ? 3.633  3.863   27.117 1.00 39.23 ? 367 HOH   A O   1 
HETATM 1182 O  O   . HOH   G 5 .   ? 11.061 16.386  3.241  1.00 48.62 ? 368 HOH   A O   1 
HETATM 1183 O  O   . HOH   G 5 .   ? 29.763 4.787   2.345  1.00 47.87 ? 369 HOH   A O   1 
HETATM 1184 O  O   . HOH   G 5 .   ? 0.344  4.183   6.466  1.00 44.77 ? 370 HOH   A O   1 
HETATM 1185 O  O   . HOH   G 5 .   ? 31.757 0.260   12.051 1.00 53.79 ? 371 HOH   A O   1 
HETATM 1186 O  O   . HOH   G 5 .   ? 19.807 9.204   24.880 1.00 32.49 ? 372 HOH   A O   1 
HETATM 1187 O  O   . HOH   G 5 .   ? 6.235  -7.197  13.974 1.00 42.54 ? 373 HOH   A O   1 
HETATM 1188 O  O   . HOH   G 5 .   ? 27.727 16.248  1.851  1.00 54.06 ? 374 HOH   A O   1 
HETATM 1189 O  O   . HOH   G 5 .   ? 7.658  16.112  22.050 1.00 33.20 ? 375 HOH   A O   1 
HETATM 1190 O  O   . HOH   G 5 .   ? 4.160  -4.711  6.309  1.00 43.42 ? 376 HOH   A O   1 
HETATM 1191 O  O   . HOH   G 5 .   ? 13.262 10.956  8.958  1.00 20.41 ? 377 HOH   A O   1 
HETATM 1192 O  O   . HOH   G 5 .   ? 5.720  -1.098  23.788 1.00 28.37 ? 378 HOH   A O   1 
HETATM 1193 O  O   . HOH   G 5 .   ? 23.280 -6.132  7.771  1.00 68.52 ? 379 HOH   A O   1 
HETATM 1194 O  O   . HOH   G 5 .   ? 29.972 16.472  21.472 1.00 55.16 ? 380 HOH   A O   1 
HETATM 1195 O  O   . HOH   G 5 .   ? 23.676 18.053  18.031 1.00 40.05 ? 381 HOH   A O   1 
HETATM 1196 O  O   . HOH   G 5 .   ? 11.391 11.084  0.525  1.00 58.82 ? 382 HOH   A O   1 
HETATM 1197 O  O   . HOH   G 5 .   ? 36.764 -0.306  7.660  1.00 51.23 ? 383 HOH   A O   1 
HETATM 1198 O  O   . HOH   G 5 .   ? 30.243 20.389  8.560  1.00 29.86 ? 384 HOH   A O   1 
HETATM 1199 O  O   . HOH   G 5 .   ? 6.728  13.429  5.351  1.00 28.88 ? 385 HOH   A O   1 
HETATM 1200 O  O   . HOH   G 5 .   ? 7.049  25.524  21.549 1.00 37.78 ? 386 HOH   A O   1 
HETATM 1201 O  O   . HOH   G 5 .   ? 7.697  16.582  24.920 1.00 43.65 ? 387 HOH   A O   1 
HETATM 1202 O  O   . HOH   G 5 .   ? 20.901 -4.635  9.149  1.00 41.36 ? 388 HOH   A O   1 
HETATM 1203 O  O   . HOH   G 5 .   ? 4.182  15.127  20.418 1.00 43.05 ? 389 HOH   A O   1 
HETATM 1204 O  O   . HOH   G 5 .   ? 18.872 -0.076  18.737 1.00 32.59 ? 390 HOH   A O   1 
HETATM 1205 O  O   . HOH   G 5 .   ? 30.732 -3.917  6.120  1.00 48.30 ? 391 HOH   A O   1 
HETATM 1206 O  O   . HOH   G 5 .   ? 13.773 -6.567  29.992 1.00 52.32 ? 392 HOH   A O   1 
HETATM 1207 O  O   . HOH   G 5 .   ? 5.487  26.506  17.993 1.00 57.89 ? 393 HOH   A O   1 
HETATM 1208 O  O   . HOH   G 5 .   ? 7.503  4.281   32.414 1.00 41.06 ? 394 HOH   A O   1 
HETATM 1209 O  O   . HOH   G 5 .   ? 18.447 19.727  4.750  1.00 48.06 ? 395 HOH   A O   1 
HETATM 1210 O  O   . HOH   G 5 .   ? 8.372  20.547  8.727  1.00 46.64 ? 396 HOH   A O   1 
HETATM 1211 O  O   . HOH   G 5 .   ? 2.232  13.817  5.281  1.00 48.87 ? 397 HOH   A O   1 
HETATM 1212 O  O   . HOH   G 5 .   ? 15.447 -4.034  0.913  1.00 40.64 ? 398 HOH   A O   1 
HETATM 1213 O  O   . HOH   G 5 .   ? 6.647  23.381  11.705 1.00 40.10 ? 399 HOH   A O   1 
HETATM 1214 O  O   . HOH   G 5 .   ? 22.517 19.052  5.131  1.00 29.66 ? 400 HOH   A O   1 
HETATM 1215 O  O   . HOH   G 5 .   ? 24.199 2.323   18.280 1.00 48.54 ? 401 HOH   A O   1 
HETATM 1216 O  O   . HOH   G 5 .   ? -0.320 15.730  12.919 1.00 43.21 ? 402 HOH   A O   1 
HETATM 1217 O  O   . HOH   G 5 .   ? 32.747 14.514  19.507 1.00 58.57 ? 403 HOH   A O   1 
HETATM 1218 O  O   . HOH   G 5 .   ? 17.717 9.377   -2.117 1.00 49.94 ? 404 HOH   A O   1 
HETATM 1219 O  O   . HOH   G 5 .   ? 22.734 8.810   19.937 1.00 31.44 ? 405 HOH   A O   1 
HETATM 1220 O  O   . HOH   G 5 .   ? 8.875  -7.104  8.659  1.00 48.08 ? 406 HOH   A O   1 
HETATM 1221 O  O   . HOH   G 5 .   ? 6.335  -3.318  -1.914 1.00 47.91 ? 407 HOH   A O   1 
HETATM 1222 O  O   . HOH   G 5 .   ? 20.651 1.652   18.083 1.00 54.20 ? 408 HOH   A O   1 
HETATM 1223 O  O   . HOH   G 5 .   ? 4.451  -1.847  21.591 1.00 35.38 ? 409 HOH   A O   1 
HETATM 1224 O  O   . HOH   G 5 .   ? 2.727  6.273   27.939 1.00 50.15 ? 410 HOH   A O   1 
HETATM 1225 O  O   . HOH   G 5 .   ? 4.005  9.683   28.031 1.00 49.43 ? 411 HOH   A O   1 
HETATM 1226 O  O   . HOH   G 5 .   ? 1.706  -2.361  17.246 1.00 33.43 ? 412 HOH   A O   1 
HETATM 1227 O  O   . HOH   G 5 .   ? 32.482 14.768  5.765  1.00 60.82 ? 413 HOH   A O   1 
HETATM 1228 O  O   . HOH   G 5 .   ? 7.321  -4.791  2.198  1.00 44.95 ? 414 HOH   A O   1 
HETATM 1229 O  O   . HOH   G 5 .   ? 26.058 -1.960  13.938 1.00 64.02 ? 415 HOH   A O   1 
HETATM 1230 O  O   . HOH   G 5 .   ? 10.721 -4.357  -0.904 1.00 51.29 ? 416 HOH   A O   1 
HETATM 1231 O  O   . HOH   G 5 .   ? 19.685 7.464   27.070 1.00 38.67 ? 417 HOH   A O   1 
HETATM 1232 O  O   . HOH   G 5 .   ? 5.068  -1.142  28.554 1.00 45.44 ? 418 HOH   A O   1 
HETATM 1233 O  O   . HOH   G 5 .   ? 3.624  -4.032  2.722  1.00 70.19 ? 419 HOH   A O   1 
HETATM 1234 O  O   . HOH   G 5 .   ? 18.453 19.126  27.495 1.00 52.04 ? 420 HOH   A O   1 
HETATM 1235 O  O   . HOH   G 5 .   ? 17.424 11.233  -0.111 1.00 53.48 ? 421 HOH   A O   1 
HETATM 1236 O  O   . HOH   G 5 .   ? 7.229  11.745  3.914  1.00 50.49 ? 422 HOH   A O   1 
HETATM 1237 O  O   . HOH   G 5 .   ? 24.938 7.493   19.515 1.00 43.23 ? 423 HOH   A O   1 
HETATM 1238 O  O   . HOH   G 5 .   ? 20.011 9.367   -3.525 1.00 42.68 ? 424 HOH   A O   1 
HETATM 1239 O  O   . HOH   G 5 .   ? -0.174 23.968  14.237 1.00 60.11 ? 425 HOH   A O   1 
HETATM 1240 O  O   . HOH   G 5 .   ? 17.909 -6.191  25.850 1.00 44.57 ? 426 HOH   A O   1 
HETATM 1241 O  O   . HOH   G 5 .   ? 2.091  -6.485  17.105 1.00 60.91 ? 427 HOH   A O   1 
HETATM 1242 O  O   . HOH   G 5 .   ? 25.918 10.892  -1.127 1.00 73.21 ? 428 HOH   A O   1 
HETATM 1243 O  O   . HOH   G 5 .   ? 6.296  3.035   3.248  1.00 43.78 ? 429 HOH   A O   1 
HETATM 1244 O  O   . HOH   G 5 .   ? 19.228 22.011  20.681 1.00 63.33 ? 430 HOH   A O   1 
HETATM 1245 O  O   . HOH   G 5 .   ? 3.255  -6.733  14.500 1.00 50.57 ? 431 HOH   A O   1 
HETATM 1246 O  O   . HOH   G 5 .   ? 2.972  14.186  22.573 1.00 50.32 ? 432 HOH   A O   1 
HETATM 1247 O  O   . HOH   G 5 .   ? 4.603  -1.536  26.077 1.00 42.53 ? 433 HOH   A O   1 
HETATM 1248 O  O   . HOH   G 5 .   ? 37.091 16.835  12.970 1.00 54.63 ? 434 HOH   A O   1 
HETATM 1249 O  O   . HOH   G 5 .   ? 22.437 -5.699  14.945 1.00 84.68 ? 435 HOH   A O   1 
HETATM 1250 O  O   . HOH   G 5 .   ? 2.515  2.008   26.269 1.00 37.68 ? 436 HOH   A O   1 
HETATM 1251 O  O   . HOH   G 5 .   ? 6.200  -8.179  23.105 1.00 45.28 ? 437 HOH   A O   1 
HETATM 1252 O  O   . HOH   G 5 .   ? 12.588 23.574  14.843 1.00 39.80 ? 438 HOH   A O   1 
HETATM 1253 O  O   . HOH   G 5 .   ? 18.449 11.462  24.981 1.00 41.38 ? 439 HOH   A O   1 
HETATM 1254 O  O   . HOH   G 5 .   ? 6.507  25.744  13.367 1.00 61.18 ? 440 HOH   A O   1 
HETATM 1255 O  O   . HOH   G 5 .   ? 10.004 15.804  26.502 1.00 47.81 ? 441 HOH   A O   1 
HETATM 1256 O  O   . HOH   G 5 .   ? 6.266  7.340   30.432 1.00 53.83 ? 442 HOH   A O   1 
HETATM 1257 O  O   . HOH   G 5 .   ? -1.923 -1.334  8.945  1.00 48.33 ? 443 HOH   A O   1 
HETATM 1258 O  O   . HOH   G 5 .   ? 8.878  7.826   2.187  1.00 44.64 ? 444 HOH   A O   1 
HETATM 1259 O  O   . HOH   G 5 .   ? 18.631 -2.436  17.603 1.00 40.69 ? 445 HOH   A O   1 
HETATM 1260 O  O   . HOH   G 5 .   ? 14.989 15.043  27.667 1.00 50.76 ? 446 HOH   A O   1 
HETATM 1261 O  O   . HOH   G 5 .   ? 14.754 24.274  16.212 1.00 45.09 ? 447 HOH   A O   1 
HETATM 1262 O  O   . HOH   G 5 .   ? 23.467 9.917   22.722 1.00 42.46 ? 448 HOH   A O   1 
HETATM 1263 O  O   . HOH   G 5 .   ? 6.173  22.665  8.816  1.00 59.30 ? 449 HOH   A O   1 
HETATM 1264 O  O   . HOH   G 5 .   ? 31.679 6.675   14.208 1.00 50.50 ? 450 HOH   A O   1 
HETATM 1265 O  O   . HOH   G 5 .   ? 22.310 10.354  24.759 1.00 46.88 ? 451 HOH   A O   1 
HETATM 1266 O  O   . HOH   G 5 .   ? 3.368  -3.823  26.782 1.00 70.56 ? 452 HOH   A O   1 
HETATM 1267 O  O   . HOH   G 5 .   ? 29.935 -0.859  13.694 1.00 53.57 ? 453 HOH   A O   1 
HETATM 1268 O  O   . HOH   G 5 .   ? 4.242  -6.460  22.753 1.00 49.61 ? 454 HOH   A O   1 
HETATM 1269 O  O   . HOH   G 5 .   ? 5.932  5.352   1.919  1.00 54.70 ? 455 HOH   A O   1 
HETATM 1270 O  O   . HOH   G 5 .   ? 10.513 25.089  14.010 1.00 42.65 ? 456 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   ? 0.4190 0.3803 0.4415 -0.0458 -0.0874 0.0152  7   SER   A N   
2    C CA  . SER   A 1   ? 0.4030 0.3784 0.4598 -0.0449 -0.0927 0.0231  7   SER   A CA  
3    C C   . SER   A 1   ? 0.3670 0.3603 0.4501 -0.0382 -0.0824 0.0280  7   SER   A C   
4    O O   . SER   A 1   ? 0.3802 0.3756 0.4556 -0.0356 -0.0746 0.0263  7   SER   A O   
5    C CB  . SER   A 1   ? 0.4293 0.3990 0.4909 -0.0542 -0.1131 0.0335  7   SER   A CB  
6    O OG  . SER   A 1   ? 0.4863 0.4572 0.5463 -0.0572 -0.1186 0.0415  7   SER   A OG  
7    N N   . GLY   A 2   ? 0.3235 0.3275 0.4350 -0.0352 -0.0795 0.0324  8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.3018 0.3180 0.4356 -0.0301 -0.0678 0.0366  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.2906 0.3131 0.4438 -0.0262 -0.0597 0.0370  8   GLY   A C   
10   O O   . GLY   A 2   ? 0.3030 0.3229 0.4493 -0.0256 -0.0601 0.0316  8   GLY   A O   
11   N N   . ALA   A 3   ? 0.2711 0.3001 0.4470 -0.0234 -0.0501 0.0432  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.2751 0.3067 0.4656 -0.0201 -0.0399 0.0438  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.2700 0.3030 0.4669 -0.0172 -0.0229 0.0441  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.2854 0.3195 0.4871 -0.0174 -0.0201 0.0474  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.2721 0.3047 0.4919 -0.0217 -0.0474 0.0548  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.2518 0.2832 0.4488 -0.0151 -0.0113 0.0416  10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.2545 0.2818 0.4538 -0.0138 0.0063  0.0416  10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.2743 0.2989 0.5021 -0.0122 0.0148  0.0510  10  ILE   A C   
19   O O   . ILE   A 4   ? 0.2834 0.3084 0.5179 -0.0115 0.0110  0.0529  10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.2569 0.2805 0.4298 -0.0144 0.0133  0.0321  10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.2512 0.2785 0.4022 -0.0154 0.0044  0.0246  10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.2762 0.2907 0.4435 -0.0153 0.0313  0.0306  10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.2561 0.2823 0.3886 -0.0166 0.0061  0.0189  10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.2821 0.3031 0.5296 -0.0112 0.0279  0.0576  11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.2859 0.3023 0.5647 -0.0090 0.0401  0.0679  11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.3046 0.3069 0.5724 -0.0083 0.0651  0.0636  11  TYR   A C   
27   O O   . TYR   A 5   ? 0.3124 0.3099 0.5796 -0.0088 0.0761  0.0628  11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.2817 0.3038 0.5997 -0.0088 0.0355  0.0824  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.2814 0.3132 0.6062 -0.0117 0.0094  0.0872  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.2905 0.3243 0.6349 -0.0119 0.0006  0.0940  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.2937 0.3302 0.6024 -0.0149 -0.0060 0.0846  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.2953 0.3342 0.6399 -0.0164 -0.0240 0.0969  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.3044 0.3445 0.6109 -0.0192 -0.0293 0.0876  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.3132 0.3540 0.6377 -0.0205 -0.0387 0.0938  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.3361 0.3768 0.6529 -0.0264 -0.0618 0.0952  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.3065 0.3004 0.5632 -0.0080 0.0743  0.0607  12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.3366 0.3122 0.5728 -0.0094 0.0976  0.0554  12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.3499 0.3154 0.6039 -0.0067 0.1127  0.0627  12  VAL   A C   
39   O O   . VAL   A 6   ? 0.3465 0.3176 0.6034 -0.0056 0.1031  0.0645  12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.3681 0.3400 0.5580 -0.0140 0.0926  0.0424  12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.3622 0.3453 0.5452 -0.0137 0.0741  0.0410  12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.3980 0.3471 0.5608 -0.0178 0.1145  0.0373  12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.3628 0.3134 0.6342 -0.0052 0.1374  0.0683  13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.3730 0.3120 0.6677 -0.0018 0.1562  0.0773  13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.3606 0.3175 0.7000 0.0022  0.1395  0.0903  13  GLY   A C   
46   O O   . GLY   A 7   ? 0.3619 0.3344 0.7275 0.0025  0.1229  0.0971  13  GLY   A O   
47   N N   . ASN   A 8   ? 0.3621 0.3177 0.7039 0.0038  0.1392  0.0927  14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.3438 0.3156 0.7251 0.0063  0.1209  0.1040  14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.3241 0.3093 0.6802 0.0037  0.0943  0.0954  14  ASN   A C   
50   O O   . ASN   A 8   ? 0.3118 0.3024 0.6818 0.0051  0.0856  0.0996  14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.3774 0.3400 0.7915 0.0107  0.1392  0.1157  14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.4633 0.4160 0.9173 0.0139  0.1630  0.1281  14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.4607 0.4258 0.9646 0.0153  0.1536  0.1430  14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.5065 0.4352 0.9382 0.0142  0.1940  0.1227  14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.3158 0.3056 0.6375 0.0002  0.0827  0.0839  15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.2933 0.2940 0.5923 -0.0020 0.0602  0.0758  15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.2827 0.2944 0.5799 -0.0044 0.0411  0.0738  15  TYR   A C   
58   O O   . TYR   A 9   ? 0.2908 0.3014 0.5894 -0.0051 0.0458  0.0743  15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.2912 0.2852 0.5459 -0.0044 0.0649  0.0639  15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.3057 0.2869 0.5527 -0.0035 0.0816  0.0652  15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.3175 0.3025 0.5842 -0.0008 0.0782  0.0715  15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.3465 0.3099 0.5644 -0.0063 0.1009  0.0602  15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.3402 0.3124 0.5989 0.0001  0.0944  0.0735  15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.3740 0.3222 0.5783 -0.0068 0.1164  0.0613  15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.3802 0.3335 0.6055 -0.0032 0.1133  0.0683  15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.4323 0.3697 0.6438 -0.0035 0.1296  0.0703  15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.2577 0.2780 0.5505 -0.0059 0.0208  0.0713  16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.2371 0.2642 0.5206 -0.0090 0.0027  0.0682  16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.2396 0.2679 0.4905 -0.0101 -0.0047 0.0564  16  ARG   A C   
70   O O   . ARG   A 10  ? 0.2378 0.2671 0.4911 -0.0096 -0.0097 0.0561  16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.2354 0.2676 0.5469 -0.0112 -0.0149 0.0780  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.2511 0.2857 0.5449 -0.0160 -0.0355 0.0737  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.2935 0.3302 0.6149 -0.0206 -0.0536 0.0858  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.3220 0.3554 0.6223 -0.0259 -0.0729 0.0797  16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.3553 0.3850 0.6329 -0.0313 -0.0861 0.0762  16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.3671 0.3986 0.6405 -0.0313 -0.0829 0.0780  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.3157 0.3376 0.5711 -0.0367 -0.1004 0.0697  16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.2344 0.2628 0.4587 -0.0113 -0.0050 0.0479  17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.2428 0.2726 0.4414 -0.0121 -0.0106 0.0387  17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.2578 0.2892 0.4484 -0.0142 -0.0249 0.0356  17  VAL   A C   
81   O O   . VAL   A 11  ? 0.2696 0.3010 0.4558 -0.0153 -0.0259 0.0355  17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.2519 0.2793 0.4271 -0.0127 -0.0007 0.0322  17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.2556 0.2858 0.4124 -0.0134 -0.0065 0.0260  17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.2610 0.2810 0.4373 -0.0124 0.0152  0.0349  17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.2479 0.2787 0.4337 -0.0151 -0.0343 0.0326  18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.2536 0.2805 0.4249 -0.0180 -0.0454 0.0284  18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.2493 0.2738 0.4035 -0.0174 -0.0451 0.0204  18  VAL   A C   
88   O O   . VAL   A 12  ? 0.2580 0.2856 0.4169 -0.0153 -0.0402 0.0202  18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.2742 0.2975 0.4586 -0.0220 -0.0593 0.0342  18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.2939 0.3204 0.5011 -0.0231 -0.0611 0.0449  18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.2791 0.3023 0.4769 -0.0214 -0.0612 0.0357  18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.2351 0.2526 0.3707 -0.0195 -0.0499 0.0148  19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.2394 0.2518 0.3638 -0.0190 -0.0481 0.0084  19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.2596 0.2686 0.3951 -0.0204 -0.0541 0.0099  19  ASN   A C   
95   O O   . ASN   A 13  ? 0.2568 0.2609 0.3974 -0.0246 -0.0645 0.0133  19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.2467 0.2470 0.3486 -0.0217 -0.0505 0.0026  19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.2731 0.2766 0.3655 -0.0198 -0.0437 0.0012  19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.2950 0.2994 0.3856 -0.0212 -0.0467 0.0040  19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.2538 0.2604 0.3441 -0.0166 -0.0349 -0.0017 19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.2594 0.2717 0.4015 -0.0176 -0.0486 0.0088  20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.2636 0.2733 0.4186 -0.0185 -0.0530 0.0104  20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.3018 0.2958 0.4439 -0.0240 -0.0617 0.0056  20  ARG   A C   
103  O O   . ARG   A 14  ? 0.3108 0.3011 0.4627 -0.0278 -0.0718 0.0090  20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.2634 0.2783 0.4256 -0.0148 -0.0452 0.0101  20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.2510 0.2662 0.4313 -0.0146 -0.0480 0.0133  20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.2597 0.2789 0.4454 -0.0114 -0.0404 0.0132  20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.2942 0.3146 0.4985 -0.0105 -0.0414 0.0167  20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.3551 0.3655 0.5615 -0.0123 -0.0434 0.0125  20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.3564 0.3519 0.5437 -0.0159 -0.0447 0.0044  20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.3508 0.3636 0.5765 -0.0110 -0.0434 0.0163  20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.3191 0.3022 0.4377 -0.0253 -0.0583 -0.0016 21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.3389 0.3010 0.4361 -0.0319 -0.0645 -0.0078 21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.3548 0.3101 0.4426 -0.0391 -0.0792 -0.0045 21  HIS   A C   
114  O O   . HIS   A 15  ? 0.3850 0.3217 0.4554 -0.0471 -0.0887 -0.0079 21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.3589 0.3085 0.4339 -0.0309 -0.0529 -0.0159 21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.3779 0.3272 0.4370 -0.0304 -0.0500 -0.0166 21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.3886 0.3546 0.4591 -0.0243 -0.0420 -0.0134 21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.4052 0.3377 0.4364 -0.0360 -0.0539 -0.0202 21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.3995 0.3599 0.4523 -0.0255 -0.0409 -0.0152 21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.4072 0.3477 0.4358 -0.0322 -0.0476 -0.0190 21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.3492 0.3183 0.4502 -0.0373 -0.0818 0.0030  22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.3577 0.3233 0.4578 -0.0441 -0.0966 0.0095  22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.3534 0.3315 0.4890 -0.0439 -0.1041 0.0210  22  LEU   A C   
124  O O   . LEU   A 16  ? 0.3325 0.3119 0.4775 -0.0484 -0.1155 0.0300  22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.3549 0.3246 0.4448 -0.0424 -0.0925 0.0105  22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.3825 0.3388 0.4395 -0.0426 -0.0846 0.0008  22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.3698 0.3323 0.4215 -0.0405 -0.0806 0.0031  22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.4066 0.3376 0.4327 -0.0522 -0.0944 -0.0042 22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.3487 0.3364 0.5065 -0.0383 -0.0965 0.0225  23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.3531 0.3511 0.5460 -0.0371 -0.0999 0.0339  23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.3559 0.3455 0.5580 -0.0458 -0.1190 0.0400  23  ALA   A C   
132  O O   . ALA   A 17  ? 0.3716 0.3469 0.5537 -0.0515 -0.1263 0.0328  23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.3473 0.3534 0.5565 -0.0304 -0.0881 0.0337  23  ALA   A CB  
134  N N   . THR   A 18  ? 0.3385 0.3355 0.5717 -0.0474 -0.1267 0.0536  24  THR   A N   
135  C CA  . THR   A 18  ? 0.3459 0.3366 0.5944 -0.0569 -0.1480 0.0628  24  THR   A CA  
136  C C   . THR   A 18  ? 0.3453 0.3406 0.6262 -0.0545 -0.1474 0.0681  24  THR   A C   
137  O O   . THR   A 18  ? 0.3248 0.3292 0.6176 -0.0451 -0.1298 0.0663  24  THR   A O   
138  C CB  . THR   A 18  ? 0.3696 0.3671 0.6418 -0.0601 -0.1571 0.0780  24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.3780 0.3904 0.6898 -0.0510 -0.1420 0.0875  24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.3836 0.3785 0.6275 -0.0612 -0.1557 0.0741  24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.3539 0.3432 0.6517 -0.0637 -0.1678 0.0765  25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.3723 0.3663 0.7055 -0.0616 -0.1680 0.0833  25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.3445 0.3554 0.7205 -0.0515 -0.1523 0.0958  25  HIS   A C   
144  O O   . HIS   A 19  ? 0.3348 0.3512 0.7262 -0.0437 -0.1377 0.0953  25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.4234 0.4083 0.7699 -0.0748 -0.1952 0.0928  25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.5381 0.5034 0.8500 -0.0835 -0.2055 0.0796  25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.5970 0.5497 0.8600 -0.0830 -0.1961 0.0618  25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.5619 0.5169 0.8835 -0.0925 -0.2223 0.0821  25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.6198 0.5537 0.8634 -0.0916 -0.2056 0.0537  25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.6037 0.5382 0.8799 -0.0978 -0.2219 0.0647  25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.3314 0.3484 0.7233 -0.0518 -0.1532 0.1066  26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.3387 0.3674 0.7689 -0.0429 -0.1352 0.1183  26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.3349 0.3664 0.7446 -0.0324 -0.1088 0.1067  26  ASN   A C   
154  O O   . ASN   A 20  ? 0.3352 0.3708 0.7679 -0.0250 -0.0918 0.1116  26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.3853 0.4182 0.8325 -0.0455 -0.1398 0.1305  26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.4746 0.5162 0.9731 -0.0385 -0.1240 0.1468  26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.5025 0.5472 1.0467 -0.0409 -0.1328 0.1632  26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.4995 0.5432 0.9921 -0.0301 -0.0993 0.1431  26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.3206 0.3484 0.6869 -0.0324 -0.1057 0.0924  27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.3069 0.3369 0.6529 -0.0246 -0.0848 0.0824  27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.2899 0.3197 0.6375 -0.0212 -0.0792 0.0783  27  ASP   A C   
162  O O   . ASP   A 21  ? 0.2932 0.3261 0.6445 -0.0147 -0.0617 0.0786  27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.3182 0.3441 0.6214 -0.0262 -0.0857 0.0688  27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.3333 0.3601 0.6298 -0.0277 -0.0860 0.0709  27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.3431 0.3750 0.6602 -0.0238 -0.0745 0.0786  27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.3484 0.3693 0.6184 -0.0326 -0.0962 0.0647  27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.2853 0.3095 0.6253 -0.0261 -0.0931 0.0736  28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.2965 0.3208 0.6405 -0.0228 -0.0877 0.0703  28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.2851 0.3145 0.6713 -0.0194 -0.0834 0.0834  28  TRP   A C   
170  O O   . TRP   A 22  ? 0.2727 0.3051 0.6645 -0.0133 -0.0694 0.0836  28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.3089 0.3233 0.6375 -0.0295 -0.1022 0.0623  28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.3407 0.3488 0.6298 -0.0300 -0.0987 0.0486  28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.3679 0.3655 0.6286 -0.0366 -0.1080 0.0419  28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.3358 0.3475 0.6118 -0.0239 -0.0842 0.0415  28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.3811 0.3751 0.6138 -0.0340 -0.0981 0.0308  28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.3651 0.3687 0.6088 -0.0264 -0.0844 0.0310  28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.3297 0.3500 0.6186 -0.0171 -0.0713 0.0444  28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.3663 0.3715 0.5960 -0.0222 -0.0728 0.0243  28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.3450 0.3669 0.6172 -0.0140 -0.0622 0.0378  28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.3605 0.3761 0.6059 -0.0162 -0.0628 0.0285  28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.2819 0.3118 0.6987 -0.0236 -0.0950 0.0958  29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.2746 0.3089 0.7388 -0.0204 -0.0905 0.1110  29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.2862 0.3240 0.7603 -0.0116 -0.0651 0.1160  29  ALA   A C   
184  O O   . ALA   A 23  ? 0.2906 0.3293 0.7906 -0.0060 -0.0515 0.1237  29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.2645 0.2990 0.7609 -0.0279 -0.1101 0.1249  29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.2817 0.3191 0.7334 -0.0109 -0.0579 0.1113  30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.2852 0.3215 0.7395 -0.0043 -0.0333 0.1142  30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.2809 0.3147 0.6904 -0.0020 -0.0219 0.1000  30  ASN   A C   
189  O O   . ASN   A 24  ? 0.2919 0.3225 0.6872 -0.0001 -0.0074 0.0978  30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.3130 0.3500 0.7849 -0.0056 -0.0321 0.1229  30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.3490 0.3892 0.8734 -0.0075 -0.0416 0.1409  30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.3608 0.4000 0.9204 -0.0023 -0.0265 0.1520  30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.3568 0.3997 0.8871 -0.0157 -0.0673 0.1448  30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.2562 0.2909 0.6456 -0.0027 -0.0283 0.0911  31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.2465 0.2805 0.5982 -0.0016 -0.0213 0.0797  31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.2604 0.2903 0.6048 0.0026  -0.0002 0.0816  31  LEU   A C   
197  O O   . LEU   A 25  ? 0.2514 0.2793 0.6150 0.0058  0.0088  0.0888  31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.2357 0.2713 0.5764 -0.0029 -0.0314 0.0728  31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.2503 0.2869 0.5607 -0.0018 -0.0254 0.0643  31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.2674 0.3034 0.5505 -0.0046 -0.0293 0.0558  31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.2474 0.2855 0.5589 -0.0020 -0.0320 0.0610  31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.2578 0.2848 0.5712 0.0017  0.0071  0.0746  32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.2702 0.2895 0.5649 0.0030  0.0253  0.0743  32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.2770 0.2994 0.5428 0.0011  0.0204  0.0671  32  VAL   A C   
205  O O   . VAL   A 26  ? 0.2929 0.3128 0.5535 0.0020  0.0270  0.0699  32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.2802 0.2918 0.5609 0.0017  0.0372  0.0725  32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.3066 0.3061 0.5571 0.0004  0.0540  0.0699  32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.2605 0.2691 0.5761 0.0040  0.0446  0.0822  32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.2613 0.2891 0.5117 -0.0013 0.0086  0.0596  33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.2662 0.2978 0.4950 -0.0031 0.0041  0.0545  33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.2515 0.2882 0.4752 -0.0045 -0.0087 0.0476  33  TRP   A C   
212  O O   . TRP   A 27  ? 0.2516 0.2872 0.4738 -0.0055 -0.0117 0.0451  33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.2817 0.3072 0.4820 -0.0061 0.0132  0.0527  33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.2945 0.3247 0.4752 -0.0092 0.0064  0.0493  33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.3154 0.3484 0.4919 -0.0103 0.0048  0.0531  33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.2903 0.3237 0.4569 -0.0115 0.0003  0.0433  33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.3116 0.3498 0.4750 -0.0134 -0.0026 0.0508  33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.3005 0.3390 0.4582 -0.0139 -0.0050 0.0444  33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.2969 0.3302 0.4611 -0.0116 -0.0018 0.0382  33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.3037 0.3461 0.4508 -0.0163 -0.0106 0.0408  33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.2995 0.3359 0.4498 -0.0138 -0.0067 0.0336  33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.3019 0.3429 0.4453 -0.0159 -0.0109 0.0350  33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.2272 0.2683 0.4487 -0.0045 -0.0147 0.0453  34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.2197 0.2620 0.4336 -0.0058 -0.0229 0.0385  34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.2292 0.2757 0.4372 -0.0058 -0.0229 0.0379  34  GLU   A C   
226  O O   . GLU   A 28  ? 0.2234 0.2730 0.4392 -0.0048 -0.0204 0.0433  34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.2198 0.2587 0.4465 -0.0063 -0.0317 0.0365  34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.2681 0.3078 0.5149 -0.0048 -0.0331 0.0405  34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.3181 0.3588 0.5648 -0.0042 -0.0336 0.0378  34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.3221 0.3652 0.5854 -0.0024 -0.0321 0.0423  34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.3046 0.3434 0.5372 -0.0053 -0.0342 0.0319  34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.2194 0.2662 0.4156 -0.0069 -0.0251 0.0328  35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.2172 0.2685 0.4139 -0.0068 -0.0247 0.0341  35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.2281 0.2748 0.4214 -0.0066 -0.0262 0.0273  35  ASP   A C   
235  O O   . ASP   A 29  ? 0.2378 0.2823 0.4178 -0.0077 -0.0261 0.0233  35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.2385 0.2938 0.4224 -0.0095 -0.0230 0.0378  35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.3176 0.3795 0.5068 -0.0105 -0.0245 0.0431  35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.3221 0.3848 0.5240 -0.0082 -0.0244 0.0419  35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.3447 0.4095 0.5257 -0.0143 -0.0257 0.0493  35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.2193 0.2626 0.4235 -0.0053 -0.0259 0.0258  36  SER   A N   
241  C CA  A SER   A 30  ? 0.2301 0.2637 0.4281 -0.0055 -0.0240 0.0187  36  SER   A CA  
242  C CA  B SER   A 30  ? 0.2328 0.2663 0.4298 -0.0056 -0.0242 0.0185  36  SER   A CA  
243  C C   . SER   A 30  ? 0.2342 0.2717 0.4291 -0.0049 -0.0192 0.0201  36  SER   A C   
244  O O   . SER   A 30  ? 0.2497 0.2795 0.4322 -0.0053 -0.0168 0.0143  36  SER   A O   
245  C CB  A SER   A 30  ? 0.2380 0.2659 0.4495 -0.0046 -0.0216 0.0178  36  SER   A CB  
246  C CB  B SER   A 30  ? 0.2521 0.2775 0.4597 -0.0052 -0.0224 0.0161  36  SER   A CB  
247  O OG  A SER   A 30  ? 0.2608 0.2751 0.4636 -0.0052 -0.0163 0.0105  36  SER   A OG  
248  O OG  B SER   A 30  ? 0.2696 0.3027 0.4950 -0.0027 -0.0170 0.0225  36  SER   A OG  
249  N N   . SER   A 31  ? 0.2217 0.2709 0.4289 -0.0045 -0.0185 0.0289  37  SER   A N   
250  C CA  . SER   A 31  ? 0.2293 0.2835 0.4390 -0.0048 -0.0161 0.0329  37  SER   A CA  
251  C C   . SER   A 31  ? 0.2319 0.2866 0.4235 -0.0070 -0.0184 0.0302  37  SER   A C   
252  O O   . SER   A 31  ? 0.2450 0.3014 0.4379 -0.0071 -0.0162 0.0316  37  SER   A O   
253  C CB  . SER   A 31  ? 0.2827 0.3490 0.5099 -0.0058 -0.0181 0.0451  37  SER   A CB  
254  O OG  . SER   A 31  ? 0.3388 0.4106 0.5543 -0.0095 -0.0242 0.0495  37  SER   A OG  
255  N N   . ARG   A 32  ? 0.2217 0.2748 0.3998 -0.0084 -0.0217 0.0272  38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.2259 0.2782 0.3880 -0.0103 -0.0224 0.0243  38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.2438 0.2869 0.3953 -0.0094 -0.0221 0.0162  38  ARG   A C   
258  O O   . ARG   A 32  ? 0.2444 0.2866 0.3847 -0.0105 -0.0219 0.0137  38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.2116 0.2664 0.3659 -0.0132 -0.0240 0.0276  38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.2384 0.2994 0.3946 -0.0166 -0.0262 0.0359  38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.2652 0.3229 0.4071 -0.0204 -0.0254 0.0380  38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.2688 0.3216 0.3939 -0.0231 -0.0234 0.0335  38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.2862 0.3333 0.3932 -0.0287 -0.0218 0.0350  38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.2584 0.3032 0.3587 -0.0327 -0.0226 0.0412  38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.2806 0.3223 0.3742 -0.0310 -0.0187 0.0302  38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.2436 0.2793 0.3981 -0.0085 -0.0231 0.0127  39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.2407 0.2662 0.3841 -0.0098 -0.0263 0.0070  39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.2355 0.2647 0.3778 -0.0110 -0.0299 0.0094  39  ASP   A C   
269  O O   . ASP   A 33  ? 0.2357 0.2606 0.3686 -0.0124 -0.0322 0.0071  39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.2632 0.2806 0.3919 -0.0100 -0.0228 0.0017  39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.2923 0.2969 0.4053 -0.0130 -0.0278 -0.0033 39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.2837 0.2811 0.3977 -0.0153 -0.0333 -0.0044 39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.2836 0.2849 0.3833 -0.0137 -0.0271 -0.0053 39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.2276 0.2635 0.3801 -0.0106 -0.0290 0.0148  40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.2304 0.2670 0.3847 -0.0112 -0.0285 0.0177  40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.2357 0.2715 0.4066 -0.0107 -0.0307 0.0221  40  LEU   A C   
277  O O   . LEU   A 34  ? 0.2276 0.2652 0.4073 -0.0095 -0.0304 0.0240  40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.2368 0.2772 0.3851 -0.0120 -0.0222 0.0204  40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.2406 0.2817 0.3746 -0.0135 -0.0206 0.0173  40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.2312 0.2723 0.3563 -0.0164 -0.0155 0.0198  40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.2397 0.2775 0.3697 -0.0135 -0.0216 0.0142  40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.2282 0.2624 0.4067 -0.0113 -0.0319 0.0251  41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.2382 0.2721 0.4377 -0.0106 -0.0329 0.0315  41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.2370 0.2706 0.4444 -0.0101 -0.0259 0.0368  41  LEU   A C   
285  O O   . LEU   A 35  ? 0.2615 0.2942 0.4620 -0.0114 -0.0265 0.0354  41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.2534 0.2829 0.4616 -0.0132 -0.0451 0.0316  41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.2727 0.3028 0.5080 -0.0128 -0.0479 0.0397  41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.2686 0.2945 0.5080 -0.0150 -0.0572 0.0375  41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.2948 0.3247 0.5469 -0.0147 -0.0522 0.0473  41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.2257 0.2586 0.4459 -0.0082 -0.0168 0.0426  42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.2352 0.2646 0.4666 -0.0073 -0.0061 0.0484  42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.2478 0.2772 0.5119 -0.0056 -0.0069 0.0580  42  VAL   A C   
293  O O   . VAL   A 36  ? 0.2450 0.2749 0.5167 -0.0040 -0.0059 0.0600  42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.2531 0.2765 0.4681 -0.0071 0.0099  0.0474  42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.2582 0.2739 0.4867 -0.0059 0.0246  0.0534  42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.2508 0.2745 0.4364 -0.0098 0.0087  0.0395  42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.2505 0.2798 0.5366 -0.0060 -0.0084 0.0651  43  SER   A N   
298  C CA  . SER   A 37  ? 0.2673 0.2971 0.5913 -0.0049 -0.0095 0.0769  43  SER   A CA  
299  C C   . SER   A 37  ? 0.2878 0.3130 0.6322 -0.0024 0.0078  0.0856  43  SER   A C   
300  O O   . SER   A 37  ? 0.2759 0.2980 0.6054 -0.0027 0.0162  0.0820  43  SER   A O   
301  C CB  . SER   A 37  ? 0.2667 0.3002 0.6051 -0.0093 -0.0311 0.0807  43  SER   A CB  
302  O OG  . SER   A 37  ? 0.2861 0.3201 0.6179 -0.0120 -0.0356 0.0806  43  SER   A OG  
303  N N   . SER   A 38  ? 0.2893 0.3129 0.6697 0.0003  0.0150  0.0974  44  SER   A N   
304  C CA  . SER   A 38  ? 0.3180 0.3350 0.7233 0.0033  0.0351  0.1071  44  SER   A CA  
305  C C   . SER   A 38  ? 0.3328 0.3558 0.7720 0.0013  0.0247  0.1184  44  SER   A C   
306  O O   . SER   A 38  ? 0.3460 0.3770 0.7953 -0.0029 0.0008  0.1216  44  SER   A O   
307  C CB  . SER   A 38  ? 0.3578 0.3690 0.7900 0.0077  0.0502  0.1164  44  SER   A CB  
308  O OG  . SER   A 38  ? 0.4003 0.4203 0.8608 0.0068  0.0316  0.1235  44  SER   A OG  
309  N N   . THR   A 39  ? 0.3320 0.3495 0.7859 0.0033  0.0424  0.1244  45  THR   A N   
310  C CA  . THR   A 39  ? 0.3447 0.3683 0.8354 0.0015  0.0345  0.1378  45  THR   A CA  
311  C C   . THR   A 39  ? 0.3684 0.3856 0.9072 0.0062  0.0577  0.1538  45  THR   A C   
312  O O   . THR   A 39  ? 0.3805 0.3843 0.9113 0.0107  0.0848  0.1508  45  THR   A O   
313  C CB  . THR   A 39  ? 0.3624 0.3863 0.8272 -0.0007 0.0341  0.1301  45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.3812 0.3924 0.8315 0.0027  0.0630  0.1247  45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.3682 0.3964 0.7869 -0.0047 0.0153  0.1148  45  THR   A CG2 
316  N N   . THR   A 40  ? 0.3743 0.3994 0.9628 0.0047  0.0478  0.1719  46  THR   A N   
317  C CA  . THR   A 40  ? 0.3884 0.4083 1.0320 0.0094  0.0703  0.1902  46  THR   A CA  
318  C C   . THR   A 40  ? 0.3862 0.3985 1.0300 0.0113  0.0922  0.1905  46  THR   A C   
319  O O   . THR   A 40  ? 0.3946 0.3930 1.0595 0.0166  0.1245  0.1964  46  THR   A O   
320  C CB  . THR   A 40  ? 0.4136 0.4462 1.1164 0.0063  0.0477  0.2121  46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.4466 0.4902 1.1466 -0.0010 0.0204  0.2151  46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.4198 0.4566 1.1204 0.0044  0.0297  0.2103  46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.3825 0.4016 1.0008 0.0070  0.0770  0.1833  47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.3738 0.3868 0.9913 0.0082  0.0954  0.1829  47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.3919 0.3927 0.9457 0.0083  0.1095  0.1597  47  ALA   A C   
326  O O   . ALA   A 41  ? 0.4026 0.4066 0.9112 0.0057  0.0938  0.1447  47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.3656 0.3934 0.9986 0.0031  0.0702  0.1918  47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.3867 0.3726 0.9379 0.0107  0.1389  0.1575  48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.4060 0.3785 0.8978 0.0091  0.1515  0.1368  48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.3754 0.3595 0.8410 0.0051  0.1311  0.1283  48  GLN   A C   
331  O O   . GLN   A 42  ? 0.3640 0.3575 0.8603 0.0047  0.1242  0.1392  48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.4727 0.4213 0.9676 0.0116  0.1906  0.1367  48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.5909 0.5176 1.0621 0.0130  0.2142  0.1301  48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.7317 0.6330 1.1483 0.0094  0.2375  0.1130  48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 0.7824 0.6576 1.1849 0.0099  0.2668  0.1106  48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.7561 0.6623 1.1387 0.0050  0.2253  0.1010  48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.3562 0.3395 0.7678 0.0022  0.1216  0.1104  49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.3485 0.3402 0.7313 -0.0012 0.1056  0.1009  49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.3513 0.3292 0.7102 -0.0022 0.1265  0.0915  49  GLY   A C   
340  O O   . GLY   A 43  ? 0.3758 0.3341 0.7274 -0.0016 0.1531  0.0885  49  GLY   A O   
341  N N   . CYS   A 44  ? 0.3314 0.3169 0.6761 -0.0044 0.1155  0.0865  50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.3454 0.3190 0.6719 -0.0059 0.1335  0.0786  50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.3491 0.3216 0.6254 -0.0099 0.1250  0.0618  50  CYS   A C   
344  O O   . CYS   A 44  ? 0.3615 0.3253 0.6225 -0.0120 0.1364  0.0552  50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.3565 0.3382 0.7190 -0.0045 0.1337  0.0901  50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.4063 0.3905 0.8379 -0.0003 0.1435  0.1139  50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.3311 0.3128 0.5853 -0.0111 0.1049  0.0560  51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.3340 0.3161 0.5470 -0.0147 0.0963  0.0426  51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.3540 0.3176 0.5343 -0.0186 0.1111  0.0333  51  ASP   A C   
350  O O   . ASP   A 45  ? 0.3669 0.3205 0.5503 -0.0180 0.1219  0.0361  51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.3441 0.3413 0.5489 -0.0144 0.0714  0.0410  51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.3968 0.4079 0.6199 -0.0131 0.0547  0.0476  51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.4008 0.4131 0.6304 -0.0132 0.0581  0.0494  51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.3683 0.3875 0.5977 -0.0127 0.0383  0.0511  51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.3673 0.3253 0.5159 -0.0234 0.1111  0.0232  52  THR   A N   
356  C CA  . THR   A 46  ? 0.3970 0.3367 0.5077 -0.0300 0.1200  0.0143  52  THR   A CA  
357  C C   . THR   A 46  ? 0.3766 0.3278 0.4644 -0.0328 0.0983  0.0091  52  THR   A C   
358  O O   . THR   A 46  ? 0.3741 0.3389 0.4642 -0.0318 0.0851  0.0076  52  THR   A O   
359  C CB  . THR   A 46  ? 0.4405 0.3628 0.5334 -0.0352 0.1357  0.0076  52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.4654 0.3726 0.5790 -0.0328 0.1604  0.0127  52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.4650 0.3691 0.5106 -0.0451 0.1373  -0.0025 52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.3570 0.3026 0.4255 -0.0359 0.0958  0.0076  53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.3546 0.3111 0.4064 -0.0386 0.0766  0.0048  53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.3882 0.3315 0.4059 -0.0480 0.0780  -0.0021 53  ILE   A C   
365  O O   . ILE   A 47  ? 0.4237 0.3446 0.4186 -0.0543 0.0927  -0.0050 53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.3468 0.3037 0.3957 -0.0382 0.0726  0.0082  53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.3410 0.3076 0.4239 -0.0301 0.0722  0.0156  53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.3412 0.3098 0.3778 -0.0410 0.0537  0.0070  53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.3344 0.3209 0.4411 -0.0249 0.0568  0.0177  53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.3628 0.3176 0.3761 -0.0498 0.0637  -0.0046 54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.3736 0.3180 0.3573 -0.0600 0.0604  -0.0096 54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.3778 0.3137 0.3363 -0.0677 0.0543  -0.0082 54  ALA   A C   
373  O O   . ALA   A 48  ? 0.3555 0.3041 0.3252 -0.0637 0.0446  -0.0033 54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.3598 0.3215 0.3522 -0.0589 0.0450  -0.0097 54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.4017 0.3148 0.3250 -0.0794 0.0597  -0.0123 55  ARG   A N   
376  C CA  . ARG   A 49  ? 0.4226 0.3262 0.3172 -0.0892 0.0510  -0.0100 55  ARG   A CA  
377  C C   . ARG   A 49  ? 0.4440 0.3429 0.3169 -0.1011 0.0385  -0.0124 55  ARG   A C   
378  O O   . ARG   A 49  ? 0.4711 0.3454 0.3137 -0.1112 0.0479  -0.0186 55  ARG   A O   
379  C CB  . ARG   A 49  ? 0.4480 0.3228 0.3147 -0.0946 0.0697  -0.0121 55  ARG   A CB  
380  C CG  . ARG   A 49  ? 0.4789 0.3573 0.3724 -0.0827 0.0840  -0.0085 55  ARG   A CG  
381  C CD  . ARG   A 49  ? 0.4793 0.3805 0.3957 -0.0757 0.0695  -0.0010 55  ARG   A CD  
382  N NE  . ARG   A 49  ? 0.4806 0.3859 0.4266 -0.0648 0.0817  0.0027  55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.4751 0.4012 0.4504 -0.0563 0.0718  0.0084  55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.4188 0.3625 0.3979 -0.0566 0.0521  0.0106  55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.4708 0.3994 0.4739 -0.0478 0.0819  0.0123  55  ARG   A NH2 
386  N N   . CYS   A 50  ? 0.4317 0.3535 0.3230 -0.0995 0.0187  -0.0072 56  CYS   A N   
387  C CA  . CYS   A 50  ? 0.4382 0.3607 0.3208 -0.1088 0.0054  -0.0074 56  CYS   A CA  
388  C C   . CYS   A 50  ? 0.4279 0.3752 0.3345 -0.1067 -0.0155 0.0018  56  CYS   A C   
389  O O   . CYS   A 50  ? 0.4027 0.3652 0.3310 -0.0977 -0.0178 0.0067  56  CYS   A O   
390  C CB  . CYS   A 50  ? 0.4103 0.3354 0.3077 -0.1031 0.0150  -0.0135 56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.3963 0.3518 0.3411 -0.0851 0.0133  -0.0101 56  CYS   A SG  
392  N N   . ASP   A 51  ? 0.4395 0.3910 0.3473 -0.1142 -0.0289 0.0043  57  ASP   A N   
393  C CA  . ASP   A 51  ? 0.4403 0.4151 0.3782 -0.1109 -0.0451 0.0140  57  ASP   A CA  
394  C C   . ASP   A 51  ? 0.4248 0.4119 0.3876 -0.1042 -0.0441 0.0122  57  ASP   A C   
395  O O   . ASP   A 51  ? 0.4244 0.4236 0.4056 -0.1065 -0.0572 0.0199  57  ASP   A O   
396  C CB  . ASP   A 51  ? 0.5063 0.4782 0.4312 -0.1262 -0.0654 0.0239  57  ASP   A CB  
397  C CG  . ASP   A 51  ? 0.6242 0.5800 0.5239 -0.1418 -0.0732 0.0220  57  ASP   A CG  
398  O OD1 . ASP   A 51  ? 0.6476 0.5944 0.5407 -0.1405 -0.0613 0.0122  57  ASP   A OD1 
399  O OD2 . ASP   A 51  ? 0.6923 0.6437 0.5787 -0.1566 -0.0921 0.0311  57  ASP   A OD2 
400  N N   . CYS   A 52  ? 0.3919 0.3757 0.3575 -0.0962 -0.0283 0.0035  58  CYS   A N   
401  C CA  . CYS   A 52  ? 0.3535 0.3485 0.3418 -0.0892 -0.0262 0.0022  58  CYS   A CA  
402  C C   . CYS   A 52  ? 0.3208 0.3364 0.3407 -0.0799 -0.0329 0.0094  58  CYS   A C   
403  O O   . CYS   A 52  ? 0.3056 0.3278 0.3338 -0.0740 -0.0332 0.0123  58  CYS   A O   
404  C CB  . CYS   A 52  ? 0.3447 0.3356 0.3354 -0.0807 -0.0091 -0.0056 58  CYS   A CB  
405  S SG  . CYS   A 52  ? 0.3991 0.3643 0.3601 -0.0904 0.0041  -0.0146 58  CYS   A SG  
406  N N   . GLN   A 53  ? 0.2958 0.3196 0.3334 -0.0786 -0.0365 0.0122  59  GLN   A N   
407  C CA  . GLN   A 53  ? 0.2769 0.3164 0.3443 -0.0688 -0.0378 0.0181  59  GLN   A CA  
408  C C   . GLN   A 53  ? 0.2661 0.3088 0.3451 -0.0603 -0.0279 0.0139  59  GLN   A C   
409  O O   . GLN   A 53  ? 0.2547 0.3065 0.3559 -0.0539 -0.0274 0.0186  59  GLN   A O   
410  C CB  . GLN   A 53  ? 0.3165 0.3643 0.4016 -0.0750 -0.0519 0.0297  59  GLN   A CB  
411  C CG  . GLN   A 53  ? 0.3675 0.4175 0.4515 -0.0799 -0.0619 0.0373  59  GLN   A CG  
412  C CD  . GLN   A 53  ? 0.3827 0.4436 0.4941 -0.0845 -0.0754 0.0516  59  GLN   A CD  
413  O OE1 . GLN   A 53  ? 0.4079 0.4655 0.5111 -0.0982 -0.0906 0.0588  59  GLN   A OE1 
414  N NE2 . GLN   A 53  ? 0.3558 0.4284 0.5003 -0.0738 -0.0697 0.0566  59  GLN   A NE2 
415  N N   . THR   A 54  ? 0.2575 0.2912 0.3222 -0.0605 -0.0188 0.0058  60  THR   A N   
416  C CA  . THR   A 54  ? 0.2460 0.2822 0.3202 -0.0526 -0.0093 0.0025  60  THR   A CA  
417  C C   . THR   A 54  ? 0.2397 0.2697 0.3036 -0.0484 0.0008  -0.0033 60  THR   A C   
418  O O   . THR   A 54  ? 0.2578 0.2782 0.3060 -0.0536 0.0032  -0.0063 60  THR   A O   
419  C CB  . THR   A 54  ? 0.2810 0.3146 0.3573 -0.0575 -0.0091 0.0018  60  THR   A CB  
420  O OG1 . THR   A 54  ? 0.3377 0.3573 0.3915 -0.0671 -0.0072 -0.0038 60  THR   A OG1 
421  C CG2 . THR   A 54  ? 0.2795 0.3196 0.3706 -0.0628 -0.0208 0.0100  60  THR   A CG2 
422  N N   . GLY   A 55  ? 0.2189 0.2537 0.2928 -0.0394 0.0066  -0.0037 61  GLY   A N   
423  C CA  . GLY   A 55  ? 0.2148 0.2464 0.2861 -0.0352 0.0136  -0.0060 61  GLY   A CA  
424  C C   . GLY   A 55  ? 0.2154 0.2518 0.2962 -0.0272 0.0165  -0.0047 61  GLY   A C   
425  O O   . GLY   A 55  ? 0.2365 0.2763 0.3236 -0.0251 0.0167  -0.0034 61  GLY   A O   
426  N N   . VAL   A 56  ? 0.2124 0.2476 0.2942 -0.0238 0.0191  -0.0043 62  VAL   A N   
427  C CA  . VAL   A 56  ? 0.2131 0.2504 0.2995 -0.0182 0.0198  -0.0020 62  VAL   A CA  
428  C C   . VAL   A 56  ? 0.2196 0.2566 0.3046 -0.0160 0.0147  -0.0005 62  VAL   A C   
429  O O   . VAL   A 56  ? 0.2313 0.2668 0.3174 -0.0178 0.0145  -0.0002 62  VAL   A O   
430  C CB  . VAL   A 56  ? 0.2348 0.2707 0.3275 -0.0179 0.0266  -0.0006 62  VAL   A CB  
431  C CG1 . VAL   A 56  ? 0.2503 0.2878 0.3457 -0.0135 0.0247  0.0036  62  VAL   A CG1 
432  C CG2 . VAL   A 56  ? 0.2446 0.2798 0.3386 -0.0203 0.0317  -0.0028 62  VAL   A CG2 
433  N N   . TYR   A 57  ? 0.2128 0.2487 0.2939 -0.0127 0.0115  0.0005  63  TYR   A N   
434  C CA  . TYR   A 57  ? 0.2049 0.2382 0.2827 -0.0121 0.0057  0.0015  63  TYR   A CA  
435  C C   . TYR   A 57  ? 0.2194 0.2483 0.2922 -0.0112 0.0028  0.0044  63  TYR   A C   
436  O O   . TYR   A 57  ? 0.2364 0.2636 0.3049 -0.0097 0.0062  0.0047  63  TYR   A O   
437  C CB  . TYR   A 57  ? 0.2223 0.2540 0.2958 -0.0113 0.0035  -0.0006 63  TYR   A CB  
438  C CG  . TYR   A 57  ? 0.2424 0.2680 0.3081 -0.0086 0.0061  -0.0016 63  TYR   A CG  
439  C CD1 . TYR   A 57  ? 0.2468 0.2738 0.3163 -0.0069 0.0121  -0.0014 63  TYR   A CD1 
440  C CD2 . TYR   A 57  ? 0.2709 0.2869 0.3247 -0.0083 0.0033  -0.0025 63  TYR   A CD2 
441  C CE1 . TYR   A 57  ? 0.2768 0.2957 0.3401 -0.0038 0.0179  -0.0019 63  TYR   A CE1 
442  C CE2 . TYR   A 57  ? 0.2768 0.2822 0.3190 -0.0063 0.0089  -0.0042 63  TYR   A CE2 
443  C CZ  . TYR   A 57  ? 0.2841 0.2909 0.3318 -0.0035 0.0174  -0.0037 63  TYR   A CZ  
444  O OH  . TYR   A 57  ? 0.3074 0.3017 0.3452 -0.0010 0.0263  -0.0048 63  TYR   A OH  
445  N N   . TYR   A 58  ? 0.2194 0.2459 0.2923 -0.0126 -0.0041 0.0072  64  TYR   A N   
446  C CA  . TYR   A 58  ? 0.2362 0.2570 0.3017 -0.0140 -0.0105 0.0115  64  TYR   A CA  
447  C C   . TYR   A 58  ? 0.2546 0.2645 0.3004 -0.0146 -0.0140 0.0077  64  TYR   A C   
448  O O   . TYR   A 58  ? 0.2642 0.2722 0.3098 -0.0156 -0.0178 0.0058  64  TYR   A O   
449  C CB  . TYR   A 58  ? 0.2247 0.2479 0.3039 -0.0166 -0.0181 0.0184  64  TYR   A CB  
450  C CG  . TYR   A 58  ? 0.2486 0.2652 0.3190 -0.0201 -0.0284 0.0246  64  TYR   A CG  
451  C CD1 . TYR   A 58  ? 0.2652 0.2805 0.3304 -0.0201 -0.0269 0.0280  64  TYR   A CD1 
452  C CD2 . TYR   A 58  ? 0.2615 0.2719 0.3270 -0.0245 -0.0409 0.0276  64  TYR   A CD2 
453  C CE1 . TYR   A 58  ? 0.2830 0.2906 0.3364 -0.0249 -0.0380 0.0349  64  TYR   A CE1 
454  C CE2 . TYR   A 58  ? 0.2883 0.2903 0.3420 -0.0301 -0.0532 0.0342  64  TYR   A CE2 
455  C CZ  . TYR   A 58  ? 0.3053 0.3055 0.3512 -0.0305 -0.0519 0.0379  64  TYR   A CZ  
456  O OH  . TYR   A 58  ? 0.3496 0.3397 0.3795 -0.0373 -0.0652 0.0453  64  TYR   A OH  
457  N N   . CYS   A 59  ? 0.2643 0.2646 0.2928 -0.0149 -0.0129 0.0076  65  CYS   A N   
458  C CA  . CYS   A 59  ? 0.2830 0.2670 0.2874 -0.0163 -0.0132 0.0035  65  CYS   A CA  
459  C C   . CYS   A 59  ? 0.3070 0.2794 0.2932 -0.0224 -0.0243 0.0082  65  CYS   A C   
460  O O   . CYS   A 59  ? 0.3230 0.2907 0.2989 -0.0231 -0.0232 0.0114  65  CYS   A O   
461  C CB  . CYS   A 59  ? 0.3054 0.2841 0.3021 -0.0122 -0.0002 -0.0002 65  CYS   A CB  
462  S SG  . CYS   A 59  ? 0.3538 0.3057 0.3164 -0.0138 0.0055  -0.0053 65  CYS   A SG  
463  N N   . SER   A 60  ? 0.3081 0.2751 0.2903 -0.0275 -0.0362 0.0095  66  SER   A N   
464  C CA  . SER   A 60  ? 0.3295 0.2854 0.2955 -0.0354 -0.0507 0.0158  66  SER   A CA  
465  C C   . SER   A 60  ? 0.3610 0.2928 0.2869 -0.0392 -0.0484 0.0119  66  SER   A C   
466  O O   . SER   A 60  ? 0.3870 0.3106 0.2973 -0.0453 -0.0579 0.0186  66  SER   A O   
467  C CB  . SER   A 60  ? 0.3712 0.3252 0.3422 -0.0410 -0.0648 0.0182  66  SER   A CB  
468  O OG  . SER   A 60  ? 0.4343 0.3744 0.3870 -0.0416 -0.0612 0.0089  66  SER   A OG  
469  N N   . SER   A 61  ? 0.3620 0.2808 0.2710 -0.0362 -0.0350 0.0020  67  SER   A N   
470  C CA  . SER   A 61  ? 0.3897 0.2805 0.2576 -0.0396 -0.0281 -0.0027 67  SER   A CA  
471  C C   . SER   A 61  ? 0.3981 0.2894 0.2617 -0.0357 -0.0181 0.0003  67  SER   A C   
472  O O   . SER   A 61  ? 0.4294 0.2963 0.2572 -0.0389 -0.0120 -0.0018 67  SER   A O   
473  C CB  . SER   A 61  ? 0.4124 0.2889 0.2701 -0.0363 -0.0129 -0.0128 67  SER   A CB  
474  O OG  . SER   A 61  ? 0.4118 0.3060 0.2993 -0.0264 0.0016  -0.0142 67  SER   A OG  
475  N N   . ARG   A 62  ? 0.3791 0.2952 0.2762 -0.0298 -0.0161 0.0052  68  ARG   A N   
476  C CA  . ARG   A 62  ? 0.3839 0.3030 0.2818 -0.0264 -0.0083 0.0091  68  ARG   A CA  
477  C C   . ARG   A 62  ? 0.3897 0.3267 0.3097 -0.0283 -0.0203 0.0197  68  ARG   A C   
478  O O   . ARG   A 62  ? 0.3905 0.3321 0.3151 -0.0259 -0.0153 0.0243  68  ARG   A O   
479  C CB  . ARG   A 62  ? 0.3777 0.3096 0.2997 -0.0171 0.0085  0.0049  68  ARG   A CB  
480  C CG  . ARG   A 62  ? 0.3987 0.3135 0.3059 -0.0139 0.0241  -0.0026 68  ARG   A CG  
481  C CD  . ARG   A 62  ? 0.4411 0.3327 0.3167 -0.0146 0.0346  -0.0025 68  ARG   A CD  
482  N NE  . ARG   A 62  ? 0.4889 0.3610 0.3521 -0.0111 0.0532  -0.0090 68  ARG   A NE  
483  C CZ  . ARG   A 62  ? 0.5067 0.3536 0.3403 -0.0158 0.0556  -0.0150 68  ARG   A CZ  
484  N NH1 . ARG   A 62  ? 0.4943 0.3321 0.3049 -0.0250 0.0382  -0.0153 68  ARG   A NH1 
485  N NH2 . ARG   A 62  ? 0.5229 0.3526 0.3515 -0.0116 0.0759  -0.0201 68  ARG   A NH2 
486  N N   . ARG   A 63  ? 0.3761 0.3236 0.3140 -0.0322 -0.0347 0.0245  69  ARG   A N   
487  C CA  . ARG   A 63  ? 0.3624 0.3281 0.3307 -0.0329 -0.0430 0.0355  69  ARG   A CA  
488  C C   . ARG   A 63  ? 0.3490 0.3309 0.3429 -0.0249 -0.0284 0.0345  69  ARG   A C   
489  O O   . ARG   A 63  ? 0.3624 0.3501 0.3659 -0.0244 -0.0274 0.0418  69  ARG   A O   
490  C CB  . ARG   A 63  ? 0.3854 0.3425 0.3389 -0.0406 -0.0564 0.0468  69  ARG   A CB  
491  C CG  . ARG   A 63  ? 0.4287 0.3723 0.3636 -0.0509 -0.0756 0.0506  69  ARG   A CG  
492  C CD  . ARG   A 63  ? 0.4758 0.4123 0.3985 -0.0599 -0.0917 0.0645  69  ARG   A CD  
493  N NE  . ARG   A 63  ? 0.5407 0.4578 0.4345 -0.0723 -0.1116 0.0673  69  ARG   A NE  
494  C CZ  . ARG   A 63  ? 0.5957 0.4871 0.4429 -0.0823 -0.1204 0.0689  69  ARG   A CZ  
495  N NH1 . ARG   A 63  ? 0.5936 0.4760 0.4187 -0.0801 -0.1094 0.0682  69  ARG   A NH1 
496  N NH2 . ARG   A 63  ? 0.6059 0.4781 0.4258 -0.0953 -0.1402 0.0712  69  ARG   A NH2 
497  N N   . LYS   A 64  ? 0.3253 0.3124 0.3273 -0.0195 -0.0173 0.0255  70  LYS   A N   
498  C CA  . LYS   A 64  ? 0.3095 0.3080 0.3298 -0.0137 -0.0047 0.0234  70  LYS   A CA  
499  C C   . LYS   A 64  ? 0.2880 0.2970 0.3269 -0.0115 -0.0009 0.0185  70  LYS   A C   
500  O O   . LYS   A 64  ? 0.2951 0.3007 0.3285 -0.0123 -0.0039 0.0143  70  LYS   A O   
501  C CB  . LYS   A 64  ? 0.3608 0.3494 0.3637 -0.0103 0.0065  0.0184  70  LYS   A CB  
502  C CG  . LYS   A 64  ? 0.4454 0.4429 0.4642 -0.0058 0.0172  0.0191  70  LYS   A CG  
503  C CD  . LYS   A 64  ? 0.5269 0.5138 0.5287 -0.0052 0.0217  0.0227  70  LYS   A CD  
504  C CE  . LYS   A 64  ? 0.5957 0.5872 0.6099 0.0004  0.0355  0.0209  70  LYS   A CE  
505  N NZ  . LYS   A 64  ? 0.6195 0.6281 0.6626 0.0014  0.0366  0.0225  70  LYS   A NZ  
506  N N   . HIS   A 65  ? 0.2572 0.2770 0.3158 -0.0093 0.0061  0.0186  71  HIS   A N   
507  C CA  . HIS   A 65  ? 0.2327 0.2598 0.3044 -0.0087 0.0102  0.0140  71  HIS   A CA  
508  C C   . HIS   A 65  ? 0.2490 0.2773 0.3208 -0.0063 0.0186  0.0097  71  HIS   A C   
509  O O   . HIS   A 65  ? 0.2568 0.2869 0.3334 -0.0049 0.0242  0.0115  71  HIS   A O   
510  C CB  . HIS   A 65  ? 0.2297 0.2637 0.3212 -0.0098 0.0128  0.0180  71  HIS   A CB  
511  C CG  . HIS   A 65  ? 0.2475 0.2818 0.3474 -0.0120 0.0050  0.0254  71  HIS   A CG  
512  N ND1 . HIS   A 65  ? 0.2692 0.3048 0.3781 -0.0133 0.0031  0.0255  71  HIS   A ND1 
513  C CD2 . HIS   A 65  ? 0.2567 0.2895 0.3574 -0.0137 -0.0025 0.0341  71  HIS   A CD2 
514  C CE1 . HIS   A 65  ? 0.2701 0.3062 0.3893 -0.0153 -0.0049 0.0346  71  HIS   A CE1 
515  N NE2 . HIS   A 65  ? 0.2827 0.3171 0.3965 -0.0163 -0.0100 0.0403  71  HIS   A NE2 
516  N N   . TYR   A 66  ? 0.2190 0.2463 0.2876 -0.0058 0.0192  0.0054  72  TYR   A N   
517  C CA  . TYR   A 66  ? 0.2150 0.2436 0.2879 -0.0039 0.0255  0.0037  72  TYR   A CA  
518  C C   . TYR   A 66  ? 0.2137 0.2494 0.2979 -0.0068 0.0250  0.0019  72  TYR   A C   
519  O O   . TYR   A 66  ? 0.2163 0.2529 0.2998 -0.0089 0.0206  0.0006  72  TYR   A O   
520  C CB  . TYR   A 66  ? 0.2222 0.2435 0.2867 -0.0017 0.0273  0.0022  72  TYR   A CB  
521  C CG  . TYR   A 66  ? 0.2395 0.2479 0.2858 0.0001  0.0303  0.0029  72  TYR   A CG  
522  C CD1 . TYR   A 66  ? 0.2645 0.2688 0.3090 0.0030  0.0387  0.0047  72  TYR   A CD1 
523  C CD2 . TYR   A 66  ? 0.2628 0.2610 0.2916 -0.0019 0.0249  0.0017  72  TYR   A CD2 
524  C CE1 . TYR   A 66  ? 0.2954 0.2841 0.3175 0.0036  0.0425  0.0053  72  TYR   A CE1 
525  C CE2 . TYR   A 66  ? 0.2888 0.2704 0.2938 -0.0023 0.0273  0.0018  72  TYR   A CE2 
526  C CZ  . TYR   A 66  ? 0.3176 0.2938 0.3177 0.0004  0.0365  0.0036  72  TYR   A CZ  
527  O OH  . TYR   A 66  ? 0.3621 0.3183 0.3334 -0.0009 0.0400  0.0036  72  TYR   A OH  
528  N N   . PRO   A 67  ? 0.2303 0.2693 0.3232 -0.0075 0.0291  0.0021  73  PRO   A N   
529  C CA  . PRO   A 67  ? 0.2355 0.2780 0.3344 -0.0126 0.0266  0.0007  73  PRO   A CA  
530  C C   . PRO   A 67  ? 0.2470 0.2911 0.3508 -0.0119 0.0237  0.0026  73  PRO   A C   
531  O O   . PRO   A 67  ? 0.2637 0.3061 0.3717 -0.0073 0.0285  0.0048  73  PRO   A O   
532  C CB  . PRO   A 67  ? 0.2553 0.2991 0.3621 -0.0139 0.0312  0.0010  73  PRO   A CB  
533  C CG  . PRO   A 67  ? 0.2717 0.3145 0.3801 -0.0079 0.0368  0.0036  73  PRO   A CG  
534  C CD  . PRO   A 67  ? 0.2421 0.2806 0.3387 -0.0048 0.0354  0.0042  73  PRO   A CD  
535  N N   . VAL   A 68  ? 0.2242 0.2702 0.3280 -0.0163 0.0174  0.0025  74  VAL   A N   
536  C CA  . VAL   A 68  ? 0.2424 0.2910 0.3552 -0.0159 0.0143  0.0063  74  VAL   A CA  
537  C C   . VAL   A 68  ? 0.2505 0.3028 0.3671 -0.0239 0.0058  0.0087  74  VAL   A C   
538  O O   . VAL   A 68  ? 0.2497 0.2991 0.3545 -0.0296 0.0029  0.0055  74  VAL   A O   
539  C CB  . VAL   A 68  ? 0.2757 0.3213 0.3821 -0.0126 0.0138  0.0052  74  VAL   A CB  
540  C CG1 . VAL   A 68  ? 0.3025 0.3408 0.4028 -0.0063 0.0211  0.0040  74  VAL   A CG1 
541  C CG2 . VAL   A 68  ? 0.2765 0.3211 0.3720 -0.0155 0.0095  0.0021  74  VAL   A CG2 
542  N N   . SER   A 69  ? 0.2291 0.2861 0.3622 -0.0245 0.0022  0.0153  75  SER   A N   
543  C CA  . SER   A 69  ? 0.2422 0.3032 0.3811 -0.0326 -0.0088 0.0208  75  SER   A CA  
544  C C   . SER   A 69  ? 0.2332 0.2958 0.3759 -0.0293 -0.0096 0.0232  75  SER   A C   
545  O O   . SER   A 69  ? 0.2418 0.3035 0.3934 -0.0216 -0.0018 0.0241  75  SER   A O   
546  C CB  . SER   A 69  ? 0.2743 0.3410 0.4374 -0.0349 -0.0124 0.0298  75  SER   A CB  
547  O OG  . SER   A 69  ? 0.3705 0.4355 0.5318 -0.0388 -0.0125 0.0278  75  SER   A OG  
548  N N   . PHE   A 70  ? 0.2126 0.2756 0.3473 -0.0353 -0.0180 0.0244  76  PHE   A N   
549  C CA  . PHE   A 70  ? 0.2153 0.2801 0.3546 -0.0321 -0.0186 0.0267  76  PHE   A CA  
550  C C   . PHE   A 70  ? 0.2392 0.3090 0.3858 -0.0399 -0.0304 0.0354  76  PHE   A C   
551  O O   . PHE   A 70  ? 0.2659 0.3339 0.4014 -0.0496 -0.0392 0.0367  76  PHE   A O   
552  C CB  . PHE   A 70  ? 0.2094 0.2684 0.3299 -0.0288 -0.0143 0.0185  76  PHE   A CB  
553  C CG  . PHE   A 70  ? 0.2090 0.2631 0.3098 -0.0349 -0.0165 0.0140  76  PHE   A CG  
554  C CD1 . PHE   A 70  ? 0.2129 0.2622 0.3044 -0.0345 -0.0108 0.0084  76  PHE   A CD1 
555  C CD2 . PHE   A 70  ? 0.2176 0.2700 0.3096 -0.0409 -0.0225 0.0158  76  PHE   A CD2 
556  C CE1 . PHE   A 70  ? 0.2214 0.2633 0.2966 -0.0399 -0.0093 0.0044  76  PHE   A CE1 
557  C CE2 . PHE   A 70  ? 0.2348 0.2784 0.3066 -0.0466 -0.0210 0.0114  76  PHE   A CE2 
558  C CZ  . PHE   A 70  ? 0.2259 0.2638 0.2902 -0.0459 -0.0135 0.0055  76  PHE   A CZ  
559  N N   . SER   A 71  ? 0.2436 0.3181 0.4073 -0.0365 -0.0305 0.0416  77  SER   A N   
560  C CA  . SER   A 71  ? 0.2462 0.3270 0.4214 -0.0437 -0.0425 0.0526  77  SER   A CA  
561  C C   . SER   A 71  ? 0.2701 0.3463 0.4202 -0.0494 -0.0484 0.0491  77  SER   A C   
562  O O   . SER   A 71  ? 0.2921 0.3618 0.4234 -0.0456 -0.0412 0.0391  77  SER   A O   
563  C CB  . SER   A 71  ? 0.2369 0.3234 0.4421 -0.0369 -0.0376 0.0607  77  SER   A CB  
564  O OG  . SER   A 71  ? 0.2512 0.3327 0.4467 -0.0301 -0.0291 0.0531  77  SER   A OG  
565  N N   . LYS   A 72  ? 0.2791 0.3581 0.4297 -0.0589 -0.0614 0.0586  78  LYS   A N   
566  C CA  . LYS   A 72  ? 0.3041 0.3766 0.4298 -0.0643 -0.0653 0.0563  78  LYS   A CA  
567  C C   . LYS   A 72  ? 0.2968 0.3730 0.4333 -0.0560 -0.0595 0.0566  78  LYS   A C   
568  O O   . LYS   A 72  ? 0.2856 0.3695 0.4499 -0.0494 -0.0563 0.0620  78  LYS   A O   
569  C CB  . LYS   A 72  ? 0.3495 0.4213 0.4677 -0.0788 -0.0822 0.0671  78  LYS   A CB  
570  C CG  . LYS   A 72  ? 0.4306 0.4920 0.5250 -0.0894 -0.0872 0.0629  78  LYS   A CG  
571  C CD  . LYS   A 72  ? 0.5000 0.5568 0.5812 -0.1065 -0.1062 0.0734  78  LYS   A CD  
572  C CE  . LYS   A 72  ? 0.5675 0.6064 0.6121 -0.1174 -0.1070 0.0644  78  LYS   A CE  
573  N NZ  . LYS   A 72  ? 0.6053 0.6358 0.6313 -0.1368 -0.1274 0.0741  78  LYS   A NZ  
574  N N   . PRO   A 73  ? 0.3094 0.3789 0.4256 -0.0560 -0.0565 0.0508  79  PRO   A N   
575  C CA  . PRO   A 73  ? 0.2997 0.3721 0.4270 -0.0482 -0.0513 0.0506  79  PRO   A CA  
576  C C   . PRO   A 73  ? 0.2782 0.3604 0.4308 -0.0492 -0.0581 0.0636  79  PRO   A C   
577  O O   . PRO   A 73  ? 0.2894 0.3735 0.4386 -0.0587 -0.0699 0.0733  79  PRO   A O   
578  C CB  . PRO   A 73  ? 0.3321 0.3956 0.4345 -0.0513 -0.0498 0.0460  79  PRO   A CB  
579  C CG  . PRO   A 73  ? 0.3575 0.4110 0.4365 -0.0558 -0.0467 0.0385  79  PRO   A CG  
580  C CD  . PRO   A 73  ? 0.3277 0.3846 0.4112 -0.0627 -0.0556 0.0441  79  PRO   A CD  
581  N N   A SER   A 74  ? 0.2603 0.3473 0.4379 -0.0404 -0.0508 0.0647  80  SER   A N   
582  N N   B SER   A 74  ? 0.2594 0.3463 0.4368 -0.0404 -0.0508 0.0646  80  SER   A N   
583  C CA  A SER   A 74  ? 0.2615 0.3578 0.4695 -0.0404 -0.0548 0.0783  80  SER   A CA  
584  C CA  B SER   A 74  ? 0.2597 0.3560 0.4680 -0.0403 -0.0546 0.0782  80  SER   A CA  
585  C C   A SER   A 74  ? 0.2632 0.3587 0.4875 -0.0307 -0.0434 0.0753  80  SER   A C   
586  C C   B SER   A 74  ? 0.2623 0.3577 0.4862 -0.0308 -0.0436 0.0753  80  SER   A C   
587  O O   A SER   A 74  ? 0.2648 0.3519 0.4749 -0.0249 -0.0344 0.0629  80  SER   A O   
588  O O   B SER   A 74  ? 0.2636 0.3507 0.4731 -0.0251 -0.0347 0.0629  80  SER   A O   
589  C CB  A SER   A 74  ? 0.2744 0.3780 0.5079 -0.0429 -0.0590 0.0891  80  SER   A CB  
590  C CB  B SER   A 74  ? 0.2711 0.3743 0.5058 -0.0416 -0.0572 0.0881  80  SER   A CB  
591  O OG  A SER   A 74  ? 0.2968 0.3974 0.5428 -0.0342 -0.0455 0.0834  80  SER   A OG  
592  O OG  B SER   A 74  ? 0.2964 0.3971 0.5163 -0.0474 -0.0622 0.0854  80  SER   A OG  
593  N N   . LEU   A 75  ? 0.2558 0.3589 0.5096 -0.0301 -0.0447 0.0876  81  LEU   A N   
594  C CA  . LEU   A 75  ? 0.2707 0.3713 0.5415 -0.0221 -0.0335 0.0857  81  LEU   A CA  
595  C C   . LEU   A 75  ? 0.2772 0.3739 0.5690 -0.0157 -0.0203 0.0852  81  LEU   A C   
596  O O   . LEU   A 75  ? 0.2715 0.3759 0.5928 -0.0170 -0.0216 0.0984  81  LEU   A O   
597  C CB  . LEU   A 75  ? 0.2626 0.3735 0.5582 -0.0251 -0.0405 0.1012  81  LEU   A CB  
598  C CG  . LEU   A 75  ? 0.2913 0.3997 0.6028 -0.0182 -0.0304 0.0998  81  LEU   A CG  
599  C CD1 . LEU   A 75  ? 0.2960 0.3947 0.5788 -0.0157 -0.0270 0.0850  81  LEU   A CD1 
600  C CD2 . LEU   A 75  ? 0.3030 0.4233 0.6426 -0.0216 -0.0381 0.1176  81  LEU   A CD2 
601  N N   . ILE   A 76  ? 0.2813 0.3646 0.5573 -0.0095 -0.0077 0.0710  82  ILE   A N   
602  C CA  . ILE   A 76  ? 0.3010 0.3753 0.5873 -0.0040 0.0071  0.0683  82  ILE   A CA  
603  C C   . ILE   A 76  ? 0.3070 0.3668 0.5944 0.0020  0.0223  0.0609  82  ILE   A C   
604  O O   . ILE   A 76  ? 0.3070 0.3594 0.5711 0.0021  0.0209  0.0505  82  ILE   A O   
605  C CB  . ILE   A 76  ? 0.3336 0.4010 0.5906 -0.0043 0.0074  0.0571  82  ILE   A CB  
606  C CG1 . ILE   A 76  ? 0.3649 0.4438 0.6202 -0.0109 -0.0061 0.0636  82  ILE   A CG1 
607  C CG2 . ILE   A 76  ? 0.3365 0.3893 0.5935 0.0016  0.0246  0.0513  82  ILE   A CG2 
608  C CD1 . ILE   A 76  ? 0.3916 0.4784 0.6787 -0.0120 -0.0063 0.0771  82  ILE   A CD1 
609  N N   . PHE   A 77  ? 0.3009 0.3541 0.6143 0.0066  0.0380  0.0659  83  PHE   A N   
610  C CA  . PHE   A 77  ? 0.3155 0.3496 0.6260 0.0113  0.0551  0.0576  83  PHE   A CA  
611  C C   . PHE   A 77  ? 0.3263 0.3394 0.5973 0.0124  0.0627  0.0409  83  PHE   A C   
612  O O   . PHE   A 77  ? 0.3405 0.3494 0.6041 0.0133  0.0674  0.0394  83  PHE   A O   
613  C CB  . PHE   A 77  ? 0.3192 0.3489 0.6698 0.0160  0.0733  0.0683  83  PHE   A CB  
614  C CG  . PHE   A 77  ? 0.3555 0.3649 0.7041 0.0195  0.0904  0.0605  83  PHE   A CG  
615  C CD1 . PHE   A 77  ? 0.3704 0.3857 0.7276 0.0184  0.0845  0.0625  83  PHE   A CD1 
616  C CD2 . PHE   A 77  ? 0.3954 0.3774 0.7300 0.0230  0.1129  0.0504  83  PHE   A CD2 
617  C CE1 . PHE   A 77  ? 0.3942 0.3895 0.7498 0.0208  0.1003  0.0550  83  PHE   A CE1 
618  C CE2 . PHE   A 77  ? 0.4164 0.3755 0.7443 0.0246  0.1291  0.0421  83  PHE   A CE2 
619  C CZ  . PHE   A 77  ? 0.4102 0.3765 0.7497 0.0235  0.1224  0.0442  83  PHE   A CZ  
620  N N   . VAL   A 78  ? 0.3170 0.3176 0.5624 0.0113  0.0618  0.0294  84  VAL   A N   
621  C CA  . VAL   A 78  ? 0.3306 0.3108 0.5363 0.0102  0.0651  0.0148  84  VAL   A CA  
622  C C   . VAL   A 78  ? 0.3468 0.2999 0.5415 0.0112  0.0815  0.0062  84  VAL   A C   
623  O O   . VAL   A 78  ? 0.3465 0.2976 0.5474 0.0104  0.0804  0.0053  84  VAL   A O   
624  C CB  . VAL   A 78  ? 0.3321 0.3200 0.5142 0.0059  0.0465  0.0095  84  VAL   A CB  
625  C CG1 . VAL   A 78  ? 0.3548 0.3221 0.4988 0.0035  0.0470  -0.0033 84  VAL   A CG1 
626  C CG2 . VAL   A 78  ? 0.3053 0.3142 0.4929 0.0043  0.0338  0.0162  84  VAL   A CG2 
627  N N   . GLU   A 79  ? 0.3649 0.2949 0.5418 0.0124  0.0977  -0.0002 85  GLU   A N   
628  C CA  . GLU   A 79  ? 0.3990 0.2964 0.5578 0.0120  0.1159  -0.0099 85  GLU   A CA  
629  C C   . GLU   A 79  ? 0.4230 0.3068 0.5480 0.0058  0.1048  -0.0215 85  GLU   A C   
630  O O   . GLU   A 79  ? 0.4188 0.3150 0.5286 0.0021  0.0845  -0.0231 85  GLU   A O   
631  C CB  . GLU   A 79  ? 0.4444 0.3164 0.5795 0.0130  0.1338  -0.0158 85  GLU   A CB  
632  C CG  . GLU   A 79  ? 0.5087 0.3894 0.6829 0.0196  0.1494  -0.0036 85  GLU   A CG  
633  C CD  . GLU   A 79  ? 0.6061 0.4816 0.8184 0.0238  0.1682  0.0037  85  GLU   A CD  
634  O OE1 . GLU   A 79  ? 0.6482 0.4938 0.8417 0.0226  0.1842  -0.0061 85  GLU   A OE1 
635  O OE2 . GLU   A 79  ? 0.6097 0.5104 0.8710 0.0275  0.1665  0.0197  85  GLU   A OE2 
636  N N   . ALA   A 80  ? 0.4319 0.2879 0.5455 0.0041  0.1190  -0.0292 86  ALA   A N   
637  C CA  . ALA   A 80  ? 0.4614 0.3009 0.5429 -0.0032 0.1082  -0.0399 86  ALA   A CA  
638  C C   . ALA   A 80  ? 0.4895 0.3138 0.5242 -0.0097 0.0982  -0.0486 86  ALA   A C   
639  O O   . ALA   A 80  ? 0.4976 0.3089 0.5155 -0.0087 0.1094  -0.0505 86  ALA   A O   
640  C CB  . ALA   A 80  ? 0.4793 0.2859 0.5526 -0.0050 0.1281  -0.0478 86  ALA   A CB  
641  N N   . SER   A 81  ? 0.4941 0.3209 0.5113 -0.0162 0.0772  -0.0521 87  SER   A N   
642  C CA  . SER   A 81  ? 0.5161 0.3312 0.4935 -0.0236 0.0632  -0.0576 87  SER   A CA  
643  C C   . SER   A 81  ? 0.5551 0.3517 0.5087 -0.0333 0.0500  -0.0647 87  SER   A C   
644  O O   . SER   A 81  ? 0.5535 0.3468 0.5221 -0.0333 0.0537  -0.0660 87  SER   A O   
645  C CB  . SER   A 81  ? 0.4933 0.3419 0.4868 -0.0213 0.0452  -0.0492 87  SER   A CB  
646  O OG  . SER   A 81  ? 0.4826 0.3524 0.4982 -0.0216 0.0295  -0.0445 87  SER   A OG  
647  N N   . GLU   A 82  ? 0.5832 0.3709 0.5046 -0.0419 0.0325  -0.0673 88  GLU   A N   
648  C CA  . GLU   A 82  ? 0.6113 0.3832 0.5129 -0.0525 0.0160  -0.0718 88  GLU   A CA  
649  C C   . GLU   A 82  ? 0.5790 0.3813 0.5198 -0.0498 0.0006  -0.0640 88  GLU   A C   
650  O O   . GLU   A 82  ? 0.5899 0.3812 0.5275 -0.0562 -0.0078 -0.0670 88  GLU   A O   
651  C CB  . GLU   A 82  ? 0.6984 0.4550 0.5598 -0.0630 -0.0009 -0.0733 88  GLU   A CB  
652  C CG  . GLU   A 82  ? 0.8383 0.5625 0.6571 -0.0659 0.0154  -0.0807 88  GLU   A CG  
653  C CD  . GLU   A 82  ? 1.0411 0.7216 0.8020 -0.0814 0.0085  -0.0897 88  GLU   A CD  
654  O OE1 . GLU   A 82  ? 1.1051 0.7490 0.8288 -0.0841 0.0293  -0.0989 88  GLU   A OE1 
655  O OE2 . GLU   A 82  ? 1.0995 0.7805 0.8517 -0.0916 -0.0175 -0.0870 88  GLU   A OE2 
656  N N   . TYR   A 83  ? 0.5364 0.3745 0.5139 -0.0406 -0.0011 -0.0543 89  TYR   A N   
657  C CA  . TYR   A 83  ? 0.5086 0.3734 0.5197 -0.0381 -0.0139 -0.0465 89  TYR   A CA  
658  C C   . TYR   A 83  ? 0.4662 0.3495 0.5145 -0.0297 -0.0034 -0.0415 89  TYR   A C   
659  O O   . TYR   A 83  ? 0.4550 0.3541 0.5267 -0.0288 -0.0124 -0.0362 89  TYR   A O   
660  C CB  . TYR   A 83  ? 0.5092 0.3977 0.5293 -0.0364 -0.0264 -0.0386 89  TYR   A CB  
661  C CG  . TYR   A 83  ? 0.5532 0.4290 0.5473 -0.0458 -0.0429 -0.0394 89  TYR   A CG  
662  C CD1 . TYR   A 83  ? 0.5681 0.4445 0.5687 -0.0521 -0.0605 -0.0360 89  TYR   A CD1 
663  C CD2 . TYR   A 83  ? 0.5956 0.4583 0.5603 -0.0488 -0.0414 -0.0422 89  TYR   A CD2 
664  C CE1 . TYR   A 83  ? 0.6049 0.4709 0.5859 -0.0617 -0.0782 -0.0339 89  TYR   A CE1 
665  C CE2 . TYR   A 83  ? 0.6290 0.4803 0.5702 -0.0584 -0.0584 -0.0409 89  TYR   A CE2 
666  C CZ  . TYR   A 83  ? 0.6483 0.5017 0.5987 -0.0652 -0.0777 -0.0361 89  TYR   A CZ  
667  O OH  . TYR   A 83  ? 0.7055 0.5488 0.6371 -0.0758 -0.0970 -0.0321 89  TYR   A OH  
668  N N   . TYR   A 84  ? 0.4382 0.3213 0.4951 -0.0237 0.0146  -0.0412 90  TYR   A N   
669  C CA  . TYR   A 84  ? 0.4017 0.3027 0.4959 -0.0167 0.0231  -0.0340 90  TYR   A CA  
670  C C   . TYR   A 84  ? 0.4204 0.3034 0.5163 -0.0139 0.0451  -0.0373 90  TYR   A C   
671  O O   . TYR   A 84  ? 0.4385 0.3062 0.5146 -0.0140 0.0556  -0.0414 90  TYR   A O   
672  C CB  . TYR   A 84  ? 0.3579 0.2891 0.4750 -0.0109 0.0200  -0.0237 90  TYR   A CB  
673  C CG  . TYR   A 84  ? 0.3272 0.2773 0.4472 -0.0121 0.0030  -0.0190 90  TYR   A CG  
674  C CD1 . TYR   A 84  ? 0.3130 0.2782 0.4546 -0.0111 -0.0042 -0.0131 90  TYR   A CD1 
675  C CD2 . TYR   A 84  ? 0.3307 0.2838 0.4346 -0.0137 -0.0035 -0.0195 90  TYR   A CD2 
676  C CE1 . TYR   A 84  ? 0.2924 0.2727 0.4381 -0.0116 -0.0158 -0.0082 90  TYR   A CE1 
677  C CE2 . TYR   A 84  ? 0.3189 0.2876 0.4284 -0.0144 -0.0158 -0.0147 90  TYR   A CE2 
678  C CZ  . TYR   A 84  ? 0.3099 0.2913 0.4400 -0.0133 -0.0210 -0.0092 90  TYR   A CZ  
679  O OH  . TYR   A 84  ? 0.2945 0.2878 0.4301 -0.0139 -0.0298 -0.0043 90  TYR   A OH  
680  N N   . PRO   A 85  ? 0.4155 0.3021 0.5401 -0.0104 0.0543  -0.0334 91  PRO   A N   
681  C CA  . PRO   A 85  ? 0.4208 0.2949 0.5588 -0.0060 0.0780  -0.0327 91  PRO   A CA  
682  C C   . PRO   A 85  ? 0.3994 0.2975 0.5631 0.0004  0.0813  -0.0211 91  PRO   A C   
683  O O   . PRO   A 85  ? 0.3884 0.3114 0.5573 0.0008  0.0651  -0.0148 91  PRO   A O   
684  C CB  . PRO   A 85  ? 0.4227 0.3006 0.5917 -0.0039 0.0832  -0.0286 91  PRO   A CB  
685  C CG  . PRO   A 85  ? 0.4126 0.3199 0.5983 -0.0036 0.0624  -0.0208 91  PRO   A CG  
686  C CD  . PRO   A 85  ? 0.3984 0.3039 0.5508 -0.0091 0.0448  -0.0268 91  PRO   A CD  
687  N N   . ALA   A 86  ? 0.3901 0.2804 0.5725 0.0050  0.1023  -0.0172 92  ALA   A N   
688  C CA  . ALA   A 86  ? 0.3763 0.2892 0.5883 0.0102  0.1043  -0.0043 92  ALA   A CA  
689  C C   . ALA   A 86  ? 0.3532 0.2996 0.6007 0.0117  0.0894  0.0096  92  ALA   A C   
690  O O   . ALA   A 86  ? 0.3584 0.3070 0.6255 0.0123  0.0910  0.0128  92  ALA   A O   
691  C CB  . ALA   A 86  ? 0.3845 0.2824 0.6183 0.0149  0.1308  -0.0004 92  ALA   A CB  
692  N N   . ARG   A 87  ? 0.3337 0.3034 0.5834 0.0110  0.0737  0.0164  93  ARG   A N   
693  C CA  . ARG   A 87  ? 0.3088 0.3060 0.5833 0.0106  0.0589  0.0289  93  ARG   A CA  
694  C C   . ARG   A 87  ? 0.3060 0.3228 0.5852 0.0096  0.0482  0.0376  93  ARG   A C   
695  O O   . ARG   A 87  ? 0.3303 0.3406 0.5936 0.0096  0.0514  0.0329  93  ARG   A O   
696  C CB  . ARG   A 87  ? 0.3016 0.3011 0.5586 0.0075  0.0449  0.0230  93  ARG   A CB  
697  C CG  . ARG   A 87  ? 0.2990 0.3038 0.5278 0.0043  0.0306  0.0181  93  ARG   A CG  
698  C CD  . ARG   A 87  ? 0.3103 0.3022 0.5123 0.0012  0.0242  0.0069  93  ARG   A CD  
699  N NE  . ARG   A 87  ? 0.2886 0.2920 0.4776 -0.0011 0.0103  0.0073  93  ARG   A NE  
700  C CZ  . ARG   A 87  ? 0.3097 0.3119 0.4803 -0.0023 0.0077  0.0041  93  ARG   A CZ  
701  N NH1 . ARG   A 87  ? 0.2973 0.2880 0.4589 -0.0014 0.0173  0.0004  93  ARG   A NH1 
702  N NH2 . ARG   A 87  ? 0.2763 0.2877 0.4387 -0.0042 -0.0028 0.0050  93  ARG   A NH2 
703  N N   . TYR   A 88  ? 0.2745 0.3132 0.5722 0.0076  0.0352  0.0498  94  TYR   A N   
704  C CA  . TYR   A 88  ? 0.2704 0.3240 0.5648 0.0043  0.0229  0.0563  94  TYR   A CA  
705  C C   . TYR   A 88  ? 0.2580 0.3124 0.5206 0.0010  0.0110  0.0478  94  TYR   A C   
706  O O   . TYR   A 88  ? 0.2730 0.3290 0.5329 0.0003  0.0060  0.0469  94  TYR   A O   
707  C CB  . TYR   A 88  ? 0.2658 0.3391 0.5903 0.0016  0.0138  0.0742  94  TYR   A CB  
708  C CG  . TYR   A 88  ? 0.2647 0.3411 0.6279 0.0042  0.0236  0.0868  94  TYR   A CG  
709  C CD1 . TYR   A 88  ? 0.2690 0.3508 0.6416 0.0029  0.0221  0.0935  94  TYR   A CD1 
710  C CD2 . TYR   A 88  ? 0.2770 0.3497 0.6701 0.0083  0.0360  0.0922  94  TYR   A CD2 
711  C CE1 . TYR   A 88  ? 0.2764 0.3615 0.6906 0.0055  0.0319  0.1072  94  TYR   A CE1 
712  C CE2 . TYR   A 88  ? 0.2759 0.3513 0.7108 0.0111  0.0472  0.1058  94  TYR   A CE2 
713  C CZ  . TYR   A 88  ? 0.2870 0.3687 0.7333 0.0099  0.0452  0.1136  94  TYR   A CZ  
714  O OH  . TYR   A 88  ? 0.3025 0.3870 0.7947 0.0129  0.0569  0.1287  94  TYR   A OH  
715  N N   . GLN   A 89  ? 0.2363 0.2893 0.4783 -0.0006 0.0076  0.0426  95  GLN   A N   
716  C CA  . GLN   A 89  ? 0.2337 0.2876 0.4499 -0.0036 -0.0020 0.0364  95  GLN   A CA  
717  C C   . GLN   A 89  ? 0.2289 0.2961 0.4458 -0.0082 -0.0119 0.0449  95  GLN   A C   
718  O O   . GLN   A 89  ? 0.2353 0.3067 0.4602 -0.0094 -0.0119 0.0500  95  GLN   A O   
719  C CB  . GLN   A 89  ? 0.2573 0.2991 0.4493 -0.0029 0.0015  0.0251  95  GLN   A CB  
720  C CG  . GLN   A 89  ? 0.2839 0.3273 0.4553 -0.0057 -0.0074 0.0206  95  GLN   A CG  
721  C CD  . GLN   A 89  ? 0.2983 0.3291 0.4489 -0.0054 -0.0060 0.0108  95  GLN   A CD  
722  O OE1 . GLN   A 89  ? 0.2786 0.2960 0.4236 -0.0044 -0.0010 0.0052  95  GLN   A OE1 
723  N NE2 . GLN   A 89  ? 0.2925 0.3259 0.4303 -0.0073 -0.0104 0.0091  95  GLN   A NE2 
724  N N   . SER   A 90  ? 0.2211 0.2930 0.4292 -0.0116 -0.0198 0.0467  96  SER   A N   
725  C CA  . SER   A 90  ? 0.2179 0.2973 0.4192 -0.0179 -0.0291 0.0539  96  SER   A CA  
726  C C   . SER   A 90  ? 0.2185 0.2927 0.3935 -0.0206 -0.0304 0.0461  96  SER   A C   
727  O O   . SER   A 90  ? 0.2207 0.2876 0.3846 -0.0173 -0.0259 0.0365  96  SER   A O   
728  C CB  . SER   A 90  ? 0.2293 0.3131 0.4331 -0.0207 -0.0345 0.0611  96  SER   A CB  
729  O OG  . SER   A 90  ? 0.2588 0.3360 0.4497 -0.0184 -0.0316 0.0533  96  SER   A OG  
730  N N   . HIS   A 91  ? 0.2165 0.2936 0.3823 -0.0273 -0.0371 0.0509  97  HIS   A N   
731  C CA  . HIS   A 91  ? 0.2314 0.3022 0.3731 -0.0307 -0.0370 0.0441  97  HIS   A CA  
732  C C   . HIS   A 91  ? 0.2256 0.2930 0.3658 -0.0261 -0.0309 0.0360  97  HIS   A C   
733  O O   . HIS   A 91  ? 0.2360 0.2974 0.3615 -0.0254 -0.0276 0.0287  97  HIS   A O   
734  C CB  . HIS   A 91  ? 0.2475 0.3115 0.3736 -0.0308 -0.0342 0.0397  97  HIS   A CB  
735  C CG  . HIS   A 91  ? 0.2829 0.3476 0.4059 -0.0356 -0.0386 0.0475  97  HIS   A CG  
736  N ND1 . HIS   A 91  ? 0.3348 0.3927 0.4349 -0.0440 -0.0415 0.0496  97  HIS   A ND1 
737  C CD2 . HIS   A 91  ? 0.2855 0.3551 0.4238 -0.0335 -0.0401 0.0537  97  HIS   A CD2 
738  C CE1 . HIS   A 91  ? 0.3356 0.3943 0.4360 -0.0471 -0.0453 0.0575  97  HIS   A CE1 
739  N NE2 . HIS   A 91  ? 0.3078 0.3750 0.4332 -0.0405 -0.0447 0.0607  97  HIS   A NE2 
740  N N   . LEU   A 92  ? 0.2226 0.2928 0.3797 -0.0228 -0.0283 0.0383  98  LEU   A N   
741  C CA  . LEU   A 92  ? 0.2247 0.2895 0.3786 -0.0185 -0.0213 0.0313  98  LEU   A CA  
742  C C   . LEU   A 92  ? 0.2326 0.3007 0.3878 -0.0218 -0.0233 0.0343  98  LEU   A C   
743  O O   . LEU   A 92  ? 0.2326 0.3080 0.4036 -0.0255 -0.0288 0.0442  98  LEU   A O   
744  C CB  . LEU   A 92  ? 0.2219 0.2833 0.3916 -0.0127 -0.0134 0.0313  98  LEU   A CB  
745  C CG  . LEU   A 92  ? 0.2550 0.3059 0.4167 -0.0084 -0.0043 0.0236  98  LEU   A CG  
746  C CD1 . LEU   A 92  ? 0.2671 0.3101 0.4064 -0.0082 -0.0054 0.0145  98  LEU   A CD1 
747  C CD2 . LEU   A 92  ? 0.2656 0.3088 0.4405 -0.0039 0.0059  0.0239  98  LEU   A CD2 
748  N N   . MET   A 93  ? 0.2260 0.2890 0.3678 -0.0207 -0.0196 0.0272  99  MET   A N   
749  C CA  . MET   A 93  ? 0.2175 0.2828 0.3608 -0.0234 -0.0207 0.0292  99  MET   A CA  
750  C C   . MET   A 93  ? 0.2281 0.2884 0.3752 -0.0170 -0.0111 0.0253  99  MET   A C   
751  O O   . MET   A 93  ? 0.2466 0.2994 0.3810 -0.0134 -0.0062 0.0179  99  MET   A O   
752  C CB  . MET   A 93  ? 0.2374 0.2992 0.3599 -0.0283 -0.0232 0.0242  99  MET   A CB  
753  C CG  . MET   A 93  ? 0.2576 0.3188 0.3690 -0.0352 -0.0299 0.0268  99  MET   A CG  
754  S SD  . MET   A 93  ? 0.3112 0.3627 0.3974 -0.0395 -0.0264 0.0193  99  MET   A SD  
755  C CE  . MET   A 93  ? 0.2820 0.3304 0.3683 -0.0314 -0.0186 0.0129  99  MET   A CE  
756  N N   . LEU   A 94  ? 0.2219 0.2853 0.3871 -0.0161 -0.0082 0.0313  100 LEU   A N   
757  C CA  . LEU   A 94  ? 0.2262 0.2820 0.3932 -0.0099 0.0036  0.0279  100 LEU   A CA  
758  C C   . LEU   A 94  ? 0.2229 0.2800 0.3868 -0.0114 0.0037  0.0273  100 LEU   A C   
759  O O   . LEU   A 94  ? 0.2295 0.2941 0.3999 -0.0173 -0.0047 0.0325  100 LEU   A O   
760  C CB  . LEU   A 94  ? 0.2368 0.2922 0.4314 -0.0058 0.0122  0.0358  100 LEU   A CB  
761  C CG  . LEU   A 94  ? 0.2649 0.3186 0.4693 -0.0038 0.0148  0.0380  100 LEU   A CG  
762  C CD1 . LEU   A 94  ? 0.2837 0.3342 0.5175 0.0010  0.0278  0.0458  100 LEU   A CD1 
763  C CD2 . LEU   A 94  ? 0.2884 0.3299 0.4672 -0.0015 0.0185  0.0266  100 LEU   A CD2 
764  N N   . ALA   A 95  ? 0.2174 0.2655 0.3716 -0.0065 0.0134  0.0217  101 ALA   A N   
765  C CA  . ALA   A 95  ? 0.2160 0.2637 0.3690 -0.0060 0.0167  0.0211  101 ALA   A CA  
766  C C   . ALA   A 95  ? 0.2355 0.2718 0.3887 0.0007  0.0313  0.0197  101 ALA   A C   
767  O O   . ALA   A 95  ? 0.2634 0.2887 0.4070 0.0038  0.0379  0.0159  101 ALA   A O   
768  C CB  . ALA   A 95  ? 0.2170 0.2630 0.3474 -0.0082 0.0129  0.0138  101 ALA   A CB  
769  N N   . VAL   A 96  ? 0.2077 0.2444 0.3703 0.0024  0.0370  0.0227  102 VAL   A N   
770  C CA  . VAL   A 96  ? 0.2300 0.2532 0.3884 0.0085  0.0525  0.0212  102 VAL   A CA  
771  C C   . VAL   A 96  ? 0.2696 0.2856 0.3979 0.0082  0.0517  0.0131  102 VAL   A C   
772  O O   . VAL   A 96  ? 0.2851 0.3087 0.4104 0.0055  0.0449  0.0123  102 VAL   A O   
773  C CB  . VAL   A 96  ? 0.2313 0.2592 0.4166 0.0104  0.0588  0.0296  102 VAL   A CB  
774  C CG1 . VAL   A 96  ? 0.2562 0.2676 0.4336 0.0169  0.0774  0.0277  102 VAL   A CG1 
775  C CG2 . VAL   A 96  ? 0.2185 0.2546 0.4392 0.0099  0.0580  0.0406  102 VAL   A CG2 
776  N N   . GLY   A 97  ? 0.2938 0.2942 0.3996 0.0100  0.0573  0.0074  103 GLY   A N   
777  C CA  . GLY   A 97  ? 0.3132 0.3062 0.3910 0.0084  0.0538  0.0018  103 GLY   A CA  
778  C C   . GLY   A 97  ? 0.3335 0.3070 0.3853 0.0082  0.0577  -0.0035 103 GLY   A C   
779  O O   . GLY   A 97  ? 0.3417 0.3077 0.3970 0.0093  0.0633  -0.0043 103 GLY   A O   
780  N N   . HIS   A 98  ? 0.3312 0.2947 0.3570 0.0062  0.0550  -0.0066 104 HIS   A N   
781  C CA  . HIS   A 98  ? 0.3567 0.2984 0.3525 0.0036  0.0563  -0.0115 104 HIS   A CA  
782  C C   . HIS   A 98  ? 0.3500 0.2959 0.3418 -0.0010 0.0418  -0.0135 104 HIS   A C   
783  O O   . HIS   A 98  ? 0.3309 0.2925 0.3321 -0.0030 0.0299  -0.0112 104 HIS   A O   
784  C CB  . HIS   A 98  ? 0.3839 0.3101 0.3504 0.0016  0.0578  -0.0123 104 HIS   A CB  
785  C CG  . HIS   A 98  ? 0.4426 0.3423 0.3724 -0.0035 0.0575  -0.0173 104 HIS   A CG  
786  N ND1 . HIS   A 98  ? 0.4814 0.3574 0.3967 -0.0023 0.0737  -0.0218 104 HIS   A ND1 
787  C CD2 . HIS   A 98  ? 0.4641 0.3572 0.3712 -0.0107 0.0423  -0.0180 104 HIS   A CD2 
788  C CE1 . HIS   A 98  ? 0.5093 0.3627 0.3881 -0.0095 0.0678  -0.0265 104 HIS   A CE1 
789  N NE2 . HIS   A 98  ? 0.4970 0.3607 0.3704 -0.0151 0.0475  -0.0237 104 HIS   A NE2 
790  N N   . SER   A 99  ? 0.3605 0.2904 0.3387 -0.0027 0.0444  -0.0177 105 SER   A N   
791  C CA  . SER   A 99  ? 0.3781 0.3080 0.3498 -0.0075 0.0311  -0.0197 105 SER   A CA  
792  C C   . SER   A 99  ? 0.4142 0.3168 0.3578 -0.0113 0.0352  -0.0257 105 SER   A C   
793  O O   . SER   A 99  ? 0.4413 0.3284 0.3804 -0.0085 0.0516  -0.0286 105 SER   A O   
794  C CB  . SER   A 99  ? 0.3907 0.3415 0.3918 -0.0059 0.0253  -0.0171 105 SER   A CB  
795  O OG  . SER   A 99  ? 0.4247 0.3736 0.4402 -0.0024 0.0362  -0.0171 105 SER   A OG  
796  N N   . GLU   A 100 ? 0.4061 0.3011 0.3306 -0.0183 0.0206  -0.0271 106 GLU   A N   
797  C CA  . GLU   A 100 ? 0.4424 0.3105 0.3374 -0.0247 0.0198  -0.0331 106 GLU   A CA  
798  C C   . GLU   A 100 ? 0.4479 0.3269 0.3568 -0.0280 0.0044  -0.0321 106 GLU   A C   
799  O O   . GLU   A 100 ? 0.4375 0.3405 0.3705 -0.0268 -0.0067 -0.0262 106 GLU   A O   
800  C CB  . GLU   A 100 ? 0.4939 0.3387 0.3478 -0.0325 0.0142  -0.0342 106 GLU   A CB  
801  C CG  . GLU   A 100 ? 0.5370 0.3702 0.3777 -0.0286 0.0315  -0.0349 106 GLU   A CG  
802  C CD  . GLU   A 100 ? 0.6250 0.4329 0.4214 -0.0365 0.0274  -0.0352 106 GLU   A CD  
803  O OE1 . GLU   A 100 ? 0.6481 0.4360 0.4136 -0.0469 0.0148  -0.0376 106 GLU   A OE1 
804  O OE2 . GLU   A 100 ? 0.6357 0.4434 0.4281 -0.0332 0.0358  -0.0323 106 GLU   A OE2 
805  N N   . PRO   A 101 ? 0.4767 0.3374 0.3721 -0.0322 0.0048  -0.0376 107 PRO   A N   
806  C CA  . PRO   A 101 ? 0.4701 0.3427 0.3836 -0.0345 -0.0090 -0.0358 107 PRO   A CA  
807  C C   . PRO   A 101 ? 0.4588 0.3471 0.3816 -0.0386 -0.0294 -0.0285 107 PRO   A C   
808  O O   . PRO   A 101 ? 0.4477 0.3591 0.4017 -0.0352 -0.0348 -0.0235 107 PRO   A O   
809  C CB  . PRO   A 101 ? 0.5001 0.3428 0.3862 -0.0413 -0.0072 -0.0436 107 PRO   A CB  
810  C CG  . PRO   A 101 ? 0.5230 0.3438 0.3915 -0.0380 0.0160  -0.0497 107 PRO   A CG  
811  C CD  . PRO   A 101 ? 0.4941 0.3212 0.3590 -0.0346 0.0203  -0.0459 107 PRO   A CD  
812  N N   . GLY   A 102 ? 0.4544 0.3298 0.3515 -0.0459 -0.0395 -0.0266 108 GLY   A N   
813  C CA  . GLY   A 102 ? 0.4424 0.3310 0.3511 -0.0503 -0.0583 -0.0174 108 GLY   A CA  
814  C C   . GLY   A 102 ? 0.4125 0.3285 0.3521 -0.0430 -0.0557 -0.0105 108 GLY   A C   
815  O O   . GLY   A 102 ? 0.4122 0.3413 0.3699 -0.0451 -0.0679 -0.0019 108 GLY   A O   
816  N N   . ASP   A 103 ? 0.3857 0.3093 0.3329 -0.0351 -0.0396 -0.0136 109 ASP   A N   
817  C CA  . ASP   A 103 ? 0.3508 0.2975 0.3247 -0.0291 -0.0359 -0.0088 109 ASP   A CA  
818  C C   . ASP   A 103 ? 0.3105 0.2755 0.3141 -0.0256 -0.0365 -0.0069 109 ASP   A C   
819  O O   . ASP   A 103 ? 0.2953 0.2768 0.3188 -0.0226 -0.0350 -0.0027 109 ASP   A O   
820  C CB  . ASP   A 103 ? 0.3633 0.3108 0.3354 -0.0232 -0.0204 -0.0118 109 ASP   A CB  
821  C CG  . ASP   A 103 ? 0.3848 0.3179 0.3319 -0.0254 -0.0180 -0.0117 109 ASP   A CG  
822  O OD1 . ASP   A 103 ? 0.3790 0.3106 0.3187 -0.0306 -0.0298 -0.0065 109 ASP   A OD1 
823  O OD2 . ASP   A 103 ? 0.3836 0.3066 0.3200 -0.0221 -0.0041 -0.0157 109 ASP   A OD2 
824  N N   . CYS   A 104 ? 0.3061 0.2668 0.3117 -0.0264 -0.0379 -0.0098 110 CYS   A N   
825  C CA  . CYS   A 104 ? 0.2893 0.2656 0.3210 -0.0236 -0.0387 -0.0071 110 CYS   A CA  
826  C C   . CYS   A 104 ? 0.2910 0.2783 0.3399 -0.0252 -0.0474 0.0005  110 CYS   A C   
827  O O   . CYS   A 104 ? 0.3012 0.2821 0.3450 -0.0305 -0.0586 0.0044  110 CYS   A O   
828  C CB  . CYS   A 104 ? 0.3040 0.2720 0.3347 -0.0253 -0.0408 -0.0103 110 CYS   A CB  
829  S SG  . CYS   A 104 ? 0.3437 0.3030 0.3682 -0.0214 -0.0257 -0.0170 110 CYS   A SG  
830  N N   . GLY   A 105 ? 0.2732 0.2751 0.3423 -0.0215 -0.0423 0.0033  111 GLY   A N   
831  C CA  . GLY   A 105 ? 0.2814 0.2915 0.3692 -0.0222 -0.0460 0.0108  111 GLY   A CA  
832  C C   . GLY   A 105 ? 0.2817 0.2975 0.3720 -0.0207 -0.0401 0.0129  111 GLY   A C   
833  O O   . GLY   A 105 ? 0.2884 0.3113 0.3967 -0.0199 -0.0369 0.0181  111 GLY   A O   
834  N N   . GLY   A 106 ? 0.2647 0.2760 0.3381 -0.0201 -0.0367 0.0089  112 GLY   A N   
835  C CA  . GLY   A 106 ? 0.2480 0.2646 0.3242 -0.0185 -0.0303 0.0103  112 GLY   A CA  
836  C C   . GLY   A 106 ? 0.2326 0.2577 0.3198 -0.0160 -0.0210 0.0089  112 GLY   A C   
837  O O   . GLY   A 106 ? 0.2155 0.2417 0.2999 -0.0150 -0.0181 0.0050  112 GLY   A O   
838  N N   . ILE   A 107 ? 0.2152 0.2447 0.3143 -0.0160 -0.0163 0.0125  113 ILE   A N   
839  C CA  . ILE   A 107 ? 0.2138 0.2463 0.3172 -0.0157 -0.0073 0.0106  113 ILE   A CA  
840  C C   . ILE   A 107 ? 0.2208 0.2543 0.3148 -0.0155 -0.0019 0.0061  113 ILE   A C   
841  O O   . ILE   A 107 ? 0.2292 0.2625 0.3204 -0.0148 -0.0011 0.0063  113 ILE   A O   
842  C CB  . ILE   A 107 ? 0.2350 0.2678 0.3554 -0.0162 -0.0011 0.0162  113 ILE   A CB  
843  C CG1 . ILE   A 107 ? 0.2571 0.2894 0.3903 -0.0162 -0.0037 0.0205  113 ILE   A CG1 
844  C CG2 . ILE   A 107 ? 0.2529 0.2833 0.3703 -0.0173 0.0109  0.0129  113 ILE   A CG2 
845  C CD1 . ILE   A 107 ? 0.2820 0.3136 0.4388 -0.0160 0.0026  0.0288  113 ILE   A CD1 
846  N N   . LEU   A 108 ? 0.2073 0.2415 0.2972 -0.0169 0.0008  0.0033  114 LEU   A N   
847  C CA  . LEU   A 108 ? 0.2007 0.2358 0.2848 -0.0187 0.0044  0.0006  114 LEU   A CA  
848  C C   . LEU   A 108 ? 0.2269 0.2577 0.3099 -0.0224 0.0114  0.0001  114 LEU   A C   
849  O O   . LEU   A 108 ? 0.2237 0.2514 0.3061 -0.0239 0.0128  0.0009  114 LEU   A O   
850  C CB  . LEU   A 108 ? 0.2024 0.2398 0.2833 -0.0197 0.0005  -0.0001 114 LEU   A CB  
851  C CG  . LEU   A 108 ? 0.2211 0.2597 0.2987 -0.0237 0.0012  -0.0006 114 LEU   A CG  
852  C CD1 . LEU   A 108 ? 0.2299 0.2700 0.3101 -0.0213 0.0035  -0.0012 114 LEU   A CD1 
853  C CD2 . LEU   A 108 ? 0.2374 0.2796 0.3175 -0.0252 -0.0045 0.0020  114 LEU   A CD2 
854  N N   . ARG   A 109 ? 0.2355 0.2643 0.3175 -0.0238 0.0172  -0.0012 115 ARG   A N   
855  C CA  . ARG   A 109 ? 0.2590 0.2793 0.3363 -0.0282 0.0265  -0.0029 115 ARG   A CA  
856  C C   . ARG   A 109 ? 0.2615 0.2782 0.3282 -0.0333 0.0282  -0.0067 115 ARG   A C   
857  O O   . ARG   A 109 ? 0.2339 0.2560 0.3040 -0.0318 0.0254  -0.0068 115 ARG   A O   
858  C CB  . ARG   A 109 ? 0.2966 0.3138 0.3872 -0.0260 0.0355  0.0001  115 ARG   A CB  
859  C CG  . ARG   A 109 ? 0.4124 0.4344 0.5131 -0.0230 0.0361  0.0024  115 ARG   A CG  
860  C CD  . ARG   A 109 ? 0.4902 0.5083 0.6083 -0.0220 0.0465  0.0074  115 ARG   A CD  
861  N NE  . ARG   A 109 ? 0.5341 0.5552 0.6671 -0.0194 0.0422  0.0142  115 ARG   A NE  
862  C CZ  . ARG   A 109 ? 0.5554 0.5704 0.6971 -0.0198 0.0501  0.0169  115 ARG   A CZ  
863  N NH1 . ARG   A 109 ? 0.5834 0.5862 0.7154 -0.0231 0.0640  0.0122  115 ARG   A NH1 
864  N NH2 . ARG   A 109 ? 0.5128 0.5319 0.6717 -0.0175 0.0443  0.0243  115 ARG   A NH2 
865  N N   . CYS   A 110 ? 0.2790 0.2843 0.3314 -0.0402 0.0335  -0.0095 116 CYS   A N   
866  C CA  . CYS   A 110 ? 0.3085 0.3064 0.3478 -0.0475 0.0348  -0.0133 116 CYS   A CA  
867  C C   . CYS   A 110 ? 0.3387 0.3205 0.3720 -0.0508 0.0511  -0.0168 116 CYS   A C   
868  O O   . CYS   A 110 ? 0.3377 0.3170 0.3819 -0.0463 0.0604  -0.0145 116 CYS   A O   
869  C CB  . CYS   A 110 ? 0.3157 0.3096 0.3378 -0.0554 0.0257  -0.0133 116 CYS   A CB  
870  S SG  . CYS   A 110 ? 0.3386 0.3155 0.3405 -0.0611 0.0332  -0.0147 116 CYS   A SG  
871  N N   . GLN   A 111 ? 0.3724 0.3418 0.3895 -0.0592 0.0549  -0.0217 117 GLN   A N   
872  C CA  . GLN   A 111 ? 0.4133 0.3629 0.4213 -0.0634 0.0730  -0.0261 117 GLN   A CA  
873  C C   . GLN   A 111 ? 0.4372 0.3716 0.4338 -0.0654 0.0838  -0.0265 117 GLN   A C   
874  O O   . GLN   A 111 ? 0.4739 0.3934 0.4729 -0.0652 0.1028  -0.0280 117 GLN   A O   
875  C CB  . GLN   A 111 ? 0.4604 0.3953 0.4455 -0.0749 0.0731  -0.0324 117 GLN   A CB  
876  C CG  . GLN   A 111 ? 0.5237 0.4468 0.4776 -0.0868 0.0628  -0.0344 117 GLN   A CG  
877  C CD  . GLN   A 111 ? 0.6001 0.5093 0.5324 -0.0997 0.0587  -0.0393 117 GLN   A CD  
878  O OE1 . GLN   A 111 ? 0.6040 0.5253 0.5412 -0.1027 0.0416  -0.0361 117 GLN   A OE1 
879  N NE2 . GLN   A 111 ? 0.6146 0.4967 0.5237 -0.1080 0.0750  -0.0468 117 GLN   A NE2 
880  N N   . HIS   A 112 ? 0.4283 0.3654 0.4146 -0.0669 0.0736  -0.0245 118 HIS   A N   
881  C CA  . HIS   A 112 ? 0.4337 0.3545 0.4067 -0.0693 0.0846  -0.0246 118 HIS   A CA  
882  C C   . HIS   A 112 ? 0.4179 0.3490 0.4176 -0.0590 0.0883  -0.0182 118 HIS   A C   
883  O O   . HIS   A 112 ? 0.4323 0.3498 0.4271 -0.0595 0.1007  -0.0173 118 HIS   A O   
884  C CB  . HIS   A 112 ? 0.4449 0.3588 0.3889 -0.0785 0.0731  -0.0252 118 HIS   A CB  
885  C CG  . HIS   A 112 ? 0.4722 0.3747 0.3889 -0.0911 0.0659  -0.0299 118 HIS   A CG  
886  N ND1 . HIS   A 112 ? 0.4707 0.3895 0.3920 -0.0933 0.0453  -0.0266 118 HIS   A ND1 
887  C CD2 . HIS   A 112 ? 0.5146 0.3891 0.3994 -0.1028 0.0769  -0.0369 118 HIS   A CD2 
888  C CE1 . HIS   A 112 ? 0.4972 0.4003 0.3926 -0.1063 0.0418  -0.0307 118 HIS   A CE1 
889  N NE2 . HIS   A 112 ? 0.5276 0.4027 0.3975 -0.1130 0.0600  -0.0377 118 HIS   A NE2 
890  N N   . GLY   A 113 ? 0.3743 0.3278 0.4004 -0.0505 0.0771  -0.0135 119 GLY   A N   
891  C CA  . GLY   A 113 ? 0.3466 0.3100 0.3978 -0.0423 0.0770  -0.0068 119 GLY   A CA  
892  C C   . GLY   A 113 ? 0.3170 0.2998 0.3773 -0.0378 0.0581  -0.0039 119 GLY   A C   
893  O O   . GLY   A 113 ? 0.3072 0.2981 0.3625 -0.0387 0.0479  -0.0059 119 GLY   A O   
894  N N   . VAL   A 114 ? 0.2894 0.2780 0.3641 -0.0331 0.0551  0.0011  120 VAL   A N   
895  C CA  . VAL   A 114 ? 0.2790 0.2819 0.3605 -0.0295 0.0395  0.0032  120 VAL   A CA  
896  C C   . VAL   A 114 ? 0.2747 0.2781 0.3391 -0.0333 0.0317  0.0010  120 VAL   A C   
897  O O   . VAL   A 114 ? 0.2941 0.2884 0.3469 -0.0370 0.0359  0.0012  120 VAL   A O   
898  C CB  . VAL   A 114 ? 0.2846 0.2914 0.3871 -0.0246 0.0383  0.0095  120 VAL   A CB  
899  C CG1 . VAL   A 114 ? 0.2863 0.3041 0.3918 -0.0220 0.0232  0.0103  120 VAL   A CG1 
900  C CG2 . VAL   A 114 ? 0.2967 0.3048 0.4212 -0.0215 0.0436  0.0147  120 VAL   A CG2 
901  N N   . VAL   A 115 ? 0.2574 0.2706 0.3214 -0.0325 0.0208  0.0003  121 VAL   A N   
902  C CA  . VAL   A 115 ? 0.2540 0.2706 0.3094 -0.0357 0.0118  0.0007  121 VAL   A CA  
903  C C   . VAL   A 115 ? 0.2523 0.2772 0.3193 -0.0310 0.0047  0.0038  121 VAL   A C   
904  O O   . VAL   A 115 ? 0.2580 0.2838 0.3217 -0.0331 0.0004  0.0060  121 VAL   A O   
905  C CB  . VAL   A 115 ? 0.2527 0.2742 0.3059 -0.0375 0.0065  -0.0006 121 VAL   A CB  
906  C CG1 . VAL   A 115 ? 0.2522 0.2800 0.3054 -0.0401 -0.0037 0.0028  121 VAL   A CG1 
907  C CG2 . VAL   A 115 ? 0.2512 0.2634 0.2922 -0.0434 0.0127  -0.0040 121 VAL   A CG2 
908  N N   . GLY   A 116 ? 0.2342 0.2643 0.3134 -0.0254 0.0025  0.0040  122 GLY   A N   
909  C CA  . GLY   A 116 ? 0.2339 0.2684 0.3214 -0.0219 -0.0037 0.0056  122 GLY   A CA  
910  C C   . GLY   A 116 ? 0.2308 0.2662 0.3243 -0.0182 -0.0064 0.0051  122 GLY   A C   
911  O O   . GLY   A 116 ? 0.2479 0.2819 0.3424 -0.0180 -0.0035 0.0051  122 GLY   A O   
912  N N   . ILE   A 117 ? 0.2130 0.2490 0.3092 -0.0162 -0.0118 0.0050  123 ILE   A N   
913  C CA  . ILE   A 117 ? 0.2032 0.2357 0.2984 -0.0148 -0.0159 0.0043  123 ILE   A CA  
914  C C   . ILE   A 117 ? 0.2149 0.2444 0.3031 -0.0135 -0.0169 0.0012  123 ILE   A C   
915  O O   . ILE   A 117 ? 0.2136 0.2448 0.3051 -0.0130 -0.0164 0.0011  123 ILE   A O   
916  C CB  . ILE   A 117 ? 0.2197 0.2500 0.3238 -0.0151 -0.0213 0.0074  123 ILE   A CB  
917  C CG1 . ILE   A 117 ? 0.2302 0.2616 0.3391 -0.0146 -0.0225 0.0076  123 ILE   A CG1 
918  C CG2 . ILE   A 117 ? 0.2404 0.2719 0.3564 -0.0157 -0.0185 0.0124  123 ILE   A CG2 
919  C CD1 . ILE   A 117 ? 0.2390 0.2684 0.3598 -0.0151 -0.0283 0.0113  123 ILE   A CD1 
920  N N   . VAL   A 118 ? 0.2254 0.2486 0.3041 -0.0132 -0.0175 -0.0007 124 VAL   A N   
921  C CA  . VAL   A 118 ? 0.2272 0.2427 0.2970 -0.0120 -0.0149 -0.0040 124 VAL   A CA  
922  C C   . VAL   A 118 ? 0.2444 0.2547 0.3155 -0.0123 -0.0176 -0.0052 124 VAL   A C   
923  O O   . VAL   A 118 ? 0.2343 0.2418 0.3059 -0.0145 -0.0247 -0.0042 124 VAL   A O   
924  C CB  . VAL   A 118 ? 0.2433 0.2484 0.2973 -0.0128 -0.0153 -0.0056 124 VAL   A CB  
925  C CG1 . VAL   A 118 ? 0.2703 0.2614 0.3107 -0.0121 -0.0099 -0.0099 124 VAL   A CG1 
926  C CG2 . VAL   A 118 ? 0.2545 0.2651 0.3097 -0.0117 -0.0110 -0.0043 124 VAL   A CG2 
927  N N   . SER   A 119 ? 0.2405 0.2498 0.3155 -0.0104 -0.0120 -0.0062 125 SER   A N   
928  C CA  . SER   A 119 ? 0.2495 0.2537 0.3281 -0.0105 -0.0127 -0.0073 125 SER   A CA  
929  C C   . SER   A 119 ? 0.2855 0.2770 0.3585 -0.0089 -0.0036 -0.0107 125 SER   A C   
930  O O   . SER   A 119 ? 0.3016 0.2800 0.3669 -0.0103 -0.0032 -0.0144 125 SER   A O   
931  C CB  . SER   A 119 ? 0.2357 0.2527 0.3323 -0.0098 -0.0142 -0.0026 125 SER   A CB  
932  O OG  . SER   A 119 ? 0.2762 0.2893 0.3794 -0.0093 -0.0140 -0.0029 125 SER   A OG  
933  N N   . THR   A 120 ? 0.2814 0.2748 0.3587 -0.0062 0.0050  -0.0093 126 THR   A N   
934  C CA  . THR   A 120 ? 0.3011 0.2807 0.3767 -0.0039 0.0175  -0.0114 126 THR   A CA  
935  C C   . THR   A 120 ? 0.3377 0.3102 0.4030 -0.0023 0.0257  -0.0125 126 THR   A C   
936  O O   . THR   A 120 ? 0.3312 0.3126 0.3944 -0.0029 0.0207  -0.0109 126 THR   A O   
937  C CB  . THR   A 120 ? 0.2925 0.2823 0.3964 -0.0010 0.0226  -0.0051 126 THR   A CB  
938  O OG1 . THR   A 120 ? 0.2879 0.2917 0.4068 0.0000  0.0225  0.0013  126 THR   A OG1 
939  C CG2 . THR   A 120 ? 0.2813 0.2815 0.3972 -0.0024 0.0139  -0.0021 126 THR   A CG2 
940  N N   . GLY   A 121 ? 0.3700 0.3256 0.4306 -0.0001 0.0402  -0.0147 127 GLY   A N   
941  C CA  . GLY   A 121 ? 0.3996 0.3470 0.4522 0.0021  0.0506  -0.0150 127 GLY   A CA  
942  C C   . GLY   A 121 ? 0.4463 0.3710 0.4938 0.0048  0.0702  -0.0175 127 GLY   A C   
943  O O   . GLY   A 121 ? 0.4471 0.3650 0.5039 0.0056  0.0769  -0.0180 127 GLY   A O   
944  N N   . GLY   A 122 ? 0.4905 0.4007 0.5207 0.0058  0.0805  -0.0195 128 GLY   A N   
945  C CA  . GLY   A 122 ? 0.5255 0.4092 0.5470 0.0086  0.1033  -0.0221 128 GLY   A CA  
946  C C   . GLY   A 122 ? 0.5288 0.4228 0.5842 0.0151  0.1164  -0.0132 128 GLY   A C   
947  O O   . GLY   A 122 ? 0.5118 0.4329 0.6025 0.0166  0.1072  -0.0047 128 GLY   A O   
948  N N   . ASN   A 123 ? 0.5454 0.4163 0.5892 0.0180  0.1374  -0.0146 129 ASN   A N   
949  C CA  . ASN   A 123 ? 0.5362 0.4129 0.6144 0.0246  0.1530  -0.0052 129 ASN   A CA  
950  C C   . ASN   A 123 ? 0.4960 0.3974 0.5902 0.0253  0.1408  0.0012  129 ASN   A C   
951  O O   . ASN   A 123 ? 0.4929 0.4093 0.6269 0.0292  0.1452  0.0117  129 ASN   A O   
952  C CB  . ASN   A 123 ? 0.5527 0.4404 0.6769 0.0282  0.1597  0.0039  129 ASN   A CB  
953  C CG  . ASN   A 123 ? 0.6348 0.4928 0.7514 0.0298  0.1822  -0.0007 129 ASN   A CG  
954  O OD1 . ASN   A 123 ? 0.6777 0.5022 0.7596 0.0298  0.2011  -0.0087 129 ASN   A OD1 
955  N ND2 . ASN   A 123 ? 0.6299 0.4978 0.7781 0.0308  0.1818  0.0048  129 ASN   A ND2 
956  N N   . GLY   A 124 ? 0.4615 0.3656 0.5264 0.0213  0.1264  -0.0042 130 GLY   A N   
957  C CA  . GLY   A 124 ? 0.4071 0.3325 0.4853 0.0215  0.1160  0.0008  130 GLY   A CA  
958  C C   . GLY   A 124 ? 0.3434 0.2979 0.4470 0.0188  0.0964  0.0056  130 GLY   A C   
959  O O   . GLY   A 124 ? 0.3253 0.2972 0.4452 0.0183  0.0889  0.0106  130 GLY   A O   
960  N N   . LEU   A 125 ? 0.3272 0.2851 0.4311 0.0162  0.0881  0.0037  131 LEU   A N   
961  C CA  . LEU   A 125 ? 0.3166 0.2978 0.4366 0.0128  0.0702  0.0074  131 LEU   A CA  
962  C C   . LEU   A 125 ? 0.3294 0.3096 0.4226 0.0084  0.0568  0.0000  131 LEU   A C   
963  O O   . LEU   A 125 ? 0.3619 0.3238 0.4275 0.0074  0.0597  -0.0068 131 LEU   A O   
964  C CB  . LEU   A 125 ? 0.3177 0.3065 0.4676 0.0135  0.0712  0.0143  131 LEU   A CB  
965  C CG  . LEU   A 125 ? 0.3497 0.3424 0.5359 0.0173  0.0825  0.0252  131 LEU   A CG  
966  C CD1 . LEU   A 125 ? 0.3731 0.3668 0.5859 0.0187  0.0877  0.0317  131 LEU   A CD1 
967  C CD2 . LEU   A 125 ? 0.3444 0.3577 0.5508 0.0144  0.0704  0.0332  131 LEU   A CD2 
968  N N   . VAL   A 126 ? 0.2812 0.2795 0.3823 0.0051  0.0423  0.0022  132 VAL   A N   
969  C CA  . VAL   A 126 ? 0.2645 0.2643 0.3499 0.0016  0.0308  -0.0021 132 VAL   A CA  
970  C C   . VAL   A 126 ? 0.2443 0.2601 0.3478 -0.0008 0.0216  0.0025  132 VAL   A C   
971  O O   . VAL   A 126 ? 0.2468 0.2740 0.3662 -0.0019 0.0192  0.0080  132 VAL   A O   
972  C CB  . VAL   A 126 ? 0.2664 0.2670 0.3360 -0.0003 0.0254  -0.0044 132 VAL   A CB  
973  C CG1 . VAL   A 126 ? 0.2449 0.2580 0.3275 -0.0004 0.0247  -0.0007 132 VAL   A CG1 
974  C CG2 . VAL   A 126 ? 0.2639 0.2672 0.3252 -0.0037 0.0142  -0.0063 132 VAL   A CG2 
975  N N   . GLY   A 127 ? 0.2337 0.2483 0.3341 -0.0020 0.0169  0.0007  133 GLY   A N   
976  C CA  . GLY   A 127 ? 0.2336 0.2606 0.3472 -0.0044 0.0089  0.0051  133 GLY   A CA  
977  C C   . GLY   A 127 ? 0.2380 0.2674 0.3406 -0.0072 0.0005  0.0024  133 GLY   A C   
978  O O   . GLY   A 127 ? 0.2548 0.2755 0.3445 -0.0071 -0.0007 -0.0020 133 GLY   A O   
979  N N   . PHE   A 128 ? 0.2246 0.2638 0.3321 -0.0103 -0.0052 0.0058  134 PHE   A N   
980  C CA  . PHE   A 128 ? 0.2156 0.2556 0.3155 -0.0125 -0.0096 0.0042  134 PHE   A CA  
981  C C   . PHE   A 128 ? 0.2197 0.2645 0.3261 -0.0145 -0.0135 0.0079  134 PHE   A C   
982  O O   . PHE   A 128 ? 0.2164 0.2669 0.3297 -0.0170 -0.0155 0.0127  134 PHE   A O   
983  C CB  . PHE   A 128 ? 0.2035 0.2463 0.2984 -0.0153 -0.0095 0.0042  134 PHE   A CB  
984  C CG  . PHE   A 128 ? 0.2081 0.2482 0.2994 -0.0134 -0.0054 0.0022  134 PHE   A CG  
985  C CD1 . PHE   A 128 ? 0.2106 0.2454 0.2937 -0.0121 -0.0045 -0.0005 134 PHE   A CD1 
986  C CD2 . PHE   A 128 ? 0.2101 0.2534 0.3081 -0.0136 -0.0032 0.0045  134 PHE   A CD2 
987  C CE1 . PHE   A 128 ? 0.2220 0.2539 0.3007 -0.0105 -0.0005 -0.0016 134 PHE   A CE1 
988  C CE2 . PHE   A 128 ? 0.2271 0.2675 0.3228 -0.0114 0.0018  0.0032  134 PHE   A CE2 
989  C CZ  . PHE   A 128 ? 0.2304 0.2649 0.3149 -0.0098 0.0035  -0.0002 134 PHE   A CZ  
990  N N   . ALA   A 129 ? 0.2087 0.2510 0.3137 -0.0142 -0.0153 0.0067  135 ALA   A N   
991  C CA  . ALA   A 129 ? 0.2150 0.2605 0.3252 -0.0157 -0.0177 0.0103  135 ALA   A CA  
992  C C   . ALA   A 129 ? 0.2263 0.2720 0.3284 -0.0196 -0.0169 0.0114  135 ALA   A C   
993  O O   . ALA   A 129 ? 0.2177 0.2596 0.3155 -0.0195 -0.0141 0.0092  135 ALA   A O   
994  C CB  . ALA   A 129 ? 0.2146 0.2561 0.3283 -0.0137 -0.0192 0.0090  135 ALA   A CB  
995  N N   . ASP   A 130 ? 0.2416 0.2899 0.3412 -0.0240 -0.0190 0.0155  136 ASP   A N   
996  C CA  . ASP   A 130 ? 0.2620 0.3052 0.3472 -0.0296 -0.0170 0.0155  136 ASP   A CA  
997  C C   . ASP   A 130 ? 0.2707 0.3082 0.3533 -0.0293 -0.0125 0.0158  136 ASP   A C   
998  O O   . ASP   A 130 ? 0.2656 0.3056 0.3568 -0.0273 -0.0144 0.0188  136 ASP   A O   
999  C CB  . ASP   A 130 ? 0.2690 0.3138 0.3484 -0.0366 -0.0231 0.0210  136 ASP   A CB  
1000 C CG  . ASP   A 130 ? 0.3453 0.3800 0.4025 -0.0446 -0.0211 0.0198  136 ASP   A CG  
1001 O OD1 . ASP   A 130 ? 0.3701 0.4002 0.4204 -0.0453 -0.0165 0.0149  136 ASP   A OD1 
1002 O OD2 . ASP   A 130 ? 0.3939 0.4233 0.4390 -0.0506 -0.0233 0.0236  136 ASP   A OD2 
1003 N N   . VAL   A 131 ? 0.2684 0.2973 0.3408 -0.0314 -0.0050 0.0134  137 VAL   A N   
1004 C CA  . VAL   A 131 ? 0.2830 0.3040 0.3546 -0.0313 0.0027  0.0150  137 VAL   A CA  
1005 C C   . VAL   A 131 ? 0.3053 0.3126 0.3538 -0.0387 0.0100  0.0144  137 VAL   A C   
1006 O O   . VAL   A 131 ? 0.3159 0.3136 0.3604 -0.0392 0.0189  0.0160  137 VAL   A O   
1007 C CB  . VAL   A 131 ? 0.2833 0.3033 0.3698 -0.0261 0.0084  0.0145  137 VAL   A CB  
1008 C CG1 . VAL   A 131 ? 0.2666 0.2957 0.3690 -0.0212 -0.0003 0.0147  137 VAL   A CG1 
1009 C CG2 . VAL   A 131 ? 0.2876 0.3027 0.3688 -0.0275 0.0148  0.0113  137 VAL   A CG2 
1010 N N   . ARG   A 132 ? 0.3045 0.3090 0.3366 -0.0452 0.0066  0.0124  138 ARG   A N   
1011 C CA  . ARG   A 132 ? 0.3128 0.3000 0.3168 -0.0545 0.0128  0.0106  138 ARG   A CA  
1012 C C   . ARG   A 132 ? 0.3501 0.3289 0.3367 -0.0606 0.0113  0.0150  138 ARG   A C   
1013 O O   . ARG   A 132 ? 0.3855 0.3443 0.3450 -0.0681 0.0204  0.0129  138 ARG   A O   
1014 C CB  . ARG   A 132 ? 0.2907 0.2770 0.2821 -0.0613 0.0064  0.0083  138 ARG   A CB  
1015 C CG  . ARG   A 132 ? 0.2592 0.2527 0.2662 -0.0554 0.0091  0.0043  138 ARG   A CG  
1016 C CD  . ARG   A 132 ? 0.2910 0.2850 0.2891 -0.0620 0.0018  0.0031  138 ARG   A CD  
1017 N NE  . ARG   A 132 ? 0.2830 0.2923 0.2954 -0.0610 -0.0121 0.0087  138 ARG   A NE  
1018 C CZ  . ARG   A 132 ? 0.3003 0.3149 0.3160 -0.0647 -0.0203 0.0106  138 ARG   A CZ  
1019 N NH1 . ARG   A 132 ? 0.3207 0.3262 0.3225 -0.0711 -0.0181 0.0067  138 ARG   A NH1 
1020 N NH2 . ARG   A 132 ? 0.2930 0.3213 0.3281 -0.0620 -0.0297 0.0170  138 ARG   A NH2 
1021 N N   . ASP   A 133 ? 0.3411 0.3326 0.3406 -0.0584 0.0005  0.0211  139 ASP   A N   
1022 C CA  . ASP   A 133 ? 0.3564 0.3412 0.3414 -0.0640 -0.0016 0.0270  139 ASP   A CA  
1023 C C   . ASP   A 133 ? 0.3596 0.3381 0.3515 -0.0580 0.0111  0.0278  139 ASP   A C   
1024 O O   . ASP   A 133 ? 0.3849 0.3533 0.3610 -0.0625 0.0137  0.0320  139 ASP   A O   
1025 C CB  . ASP   A 133 ? 0.3657 0.3674 0.3669 -0.0638 -0.0173 0.0348  139 ASP   A CB  
1026 C CG  . ASP   A 133 ? 0.3770 0.3940 0.4111 -0.0523 -0.0175 0.0356  139 ASP   A CG  
1027 O OD1 . ASP   A 133 ? 0.3477 0.3695 0.3956 -0.0457 -0.0140 0.0300  139 ASP   A OD1 
1028 O OD2 . ASP   A 133 ? 0.3986 0.4215 0.4432 -0.0508 -0.0213 0.0419  139 ASP   A OD2 
1029 N N   . LEU   A 134 ? 0.3360 0.3194 0.3512 -0.0488 0.0187  0.0249  140 LEU   A N   
1030 C CA  . LEU   A 134 ? 0.3411 0.3199 0.3696 -0.0430 0.0298  0.0274  140 LEU   A CA  
1031 C C   . LEU   A 134 ? 0.3761 0.3327 0.3868 -0.0462 0.0488  0.0248  140 LEU   A C   
1032 O O   . LEU   A 134 ? 0.3695 0.3240 0.3965 -0.0412 0.0591  0.0232  140 LEU   A O   
1033 C CB  . LEU   A 134 ? 0.3135 0.3069 0.3759 -0.0335 0.0267  0.0272  140 LEU   A CB  
1034 C CG  . LEU   A 134 ? 0.3110 0.3217 0.3884 -0.0306 0.0114  0.0285  140 LEU   A CG  
1035 C CD1 . LEU   A 134 ? 0.3048 0.3243 0.4065 -0.0238 0.0081  0.0269  140 LEU   A CD1 
1036 C CD2 . LEU   A 134 ? 0.3164 0.3302 0.3975 -0.0306 0.0076  0.0343  140 LEU   A CD2 
1037 N N   . LEU   A 135 ? 0.4090 0.3469 0.3852 -0.0553 0.0539  0.0251  141 LEU   A N   
1038 C CA  . LEU   A 135 ? 0.4438 0.3544 0.3945 -0.0605 0.0741  0.0214  141 LEU   A CA  
1039 C C   . LEU   A 135 ? 0.4552 0.3575 0.4264 -0.0527 0.0939  0.0244  141 LEU   A C   
1040 O O   . LEU   A 135 ? 0.4711 0.3560 0.4397 -0.0525 0.1135  0.0216  141 LEU   A O   
1041 C CB  . LEU   A 135 ? 0.4713 0.3606 0.3751 -0.0737 0.0736  0.0216  141 LEU   A CB  
1042 C CG  . LEU   A 135 ? 0.5051 0.4024 0.3905 -0.0833 0.0512  0.0220  141 LEU   A CG  
1043 C CD1 . LEU   A 135 ? 0.5539 0.4249 0.3882 -0.0990 0.0508  0.0231  141 LEU   A CD1 
1044 C CD2 . LEU   A 135 ? 0.5096 0.4135 0.4000 -0.0839 0.0465  0.0158  141 LEU   A CD2 
1045 N N   . TRP   A 136 ? 0.4413 0.3550 0.4354 -0.0464 0.0899  0.0311  142 TRP   A N   
1046 C CA  . TRP   A 136 ? 0.4351 0.3435 0.4554 -0.0388 0.1067  0.0362  142 TRP   A CA  
1047 C C   . TRP   A 136 ? 0.4395 0.3581 0.4976 -0.0310 0.1100  0.0367  142 TRP   A C   
1048 O O   . TRP   A 136 ? 0.4466 0.3574 0.5276 -0.0259 0.1265  0.0418  142 TRP   A O   
1049 C CB  . TRP   A 136 ? 0.4141 0.3350 0.4534 -0.0341 0.0985  0.0434  142 TRP   A CB  
1050 C CG  . TRP   A 136 ? 0.3854 0.3336 0.4467 -0.0305 0.0751  0.0438  142 TRP   A CG  
1051 C CD1 . TRP   A 136 ? 0.3884 0.3471 0.4372 -0.0345 0.0582  0.0439  142 TRP   A CD1 
1052 C CD2 . TRP   A 136 ? 0.3599 0.3259 0.4601 -0.0226 0.0674  0.0451  142 TRP   A CD2 
1053 N NE1 . TRP   A 136 ? 0.3802 0.3603 0.4569 -0.0289 0.0433  0.0439  142 TRP   A NE1 
1054 C CE2 . TRP   A 136 ? 0.3622 0.3460 0.4673 -0.0222 0.0479  0.0441  142 TRP   A CE2 
1055 C CE3 . TRP   A 136 ? 0.3535 0.3207 0.4853 -0.0166 0.0747  0.0481  142 TRP   A CE3 
1056 C CZ2 . TRP   A 136 ? 0.3517 0.3509 0.4851 -0.0169 0.0367  0.0440  142 TRP   A CZ2 
1057 C CZ3 . TRP   A 136 ? 0.3439 0.3286 0.5050 -0.0121 0.0601  0.0494  142 TRP   A CZ3 
1058 C CH2 . TRP   A 136 ? 0.3403 0.3392 0.4987 -0.0126 0.0419  0.0464  142 TRP   A CH2 
1059 N N   . LEU   A 137 ? 0.4372 0.3721 0.5027 -0.0305 0.0949  0.0327  143 LEU   A N   
1060 C CA  . LEU   A 137 ? 0.4442 0.3870 0.5417 -0.0248 0.0971  0.0343  143 LEU   A CA  
1061 C C   . LEU   A 137 ? 0.4944 0.4158 0.5864 -0.0264 0.1212  0.0331  143 LEU   A C   
1062 O O   . LEU   A 137 ? 0.4876 0.4115 0.6131 -0.0210 0.1291  0.0385  143 LEU   A O   
1063 C CB  . LEU   A 137 ? 0.4288 0.3889 0.5280 -0.0249 0.0786  0.0298  143 LEU   A CB  
1064 C CG  . LEU   A 137 ? 0.4151 0.3954 0.5280 -0.0219 0.0580  0.0311  143 LEU   A CG  
1065 C CD1 . LEU   A 137 ? 0.4096 0.4007 0.5158 -0.0232 0.0446  0.0257  143 LEU   A CD1 
1066 C CD2 . LEU   A 137 ? 0.4076 0.3965 0.5574 -0.0156 0.0551  0.0378  143 LEU   A CD2 
1067 N N   . ASP   A 138 ? 0.5472 0.4462 0.5973 -0.0347 0.1325  0.0267  144 ASP   A N   
1068 C CA  . ASP   A 138 ? 0.5923 0.4657 0.6299 -0.0378 0.1576  0.0235  144 ASP   A CA  
1069 C C   . ASP   A 138 ? 0.6402 0.4909 0.6841 -0.0354 0.1848  0.0288  144 ASP   A C   
1070 O O   . ASP   A 138 ? 0.6584 0.4863 0.6978 -0.0368 0.2095  0.0271  144 ASP   A O   
1071 C CB  . ASP   A 138 ? 0.6236 0.4774 0.6078 -0.0498 0.1583  0.0138  144 ASP   A CB  
1072 C CG  . ASP   A 138 ? 0.6629 0.5335 0.6391 -0.0533 0.1367  0.0085  144 ASP   A CG  
1073 O OD1 . ASP   A 138 ? 0.6339 0.5290 0.6438 -0.0461 0.1241  0.0110  144 ASP   A OD1 
1074 O OD2 . ASP   A 138 ? 0.7104 0.5682 0.6460 -0.0640 0.1320  0.0024  144 ASP   A OD2 
1075 N N   . GLU   A 139 ? 0.6593 0.5134 0.7119 -0.0322 0.1830  0.0351  145 GLU   A N   
1076 C CA  . GLU   A 139 ? 0.6945 0.5258 0.7541 -0.0294 0.2107  0.0410  145 GLU   A CA  
1077 C C   . GLU   A 139 ? 0.6859 0.5354 0.7961 -0.0195 0.2067  0.0529  145 GLU   A C   
1078 O O   . GLU   A 139 ? 0.6827 0.5566 0.8041 -0.0175 0.1817  0.0546  145 GLU   A O   
1079 C CB  . GLU   A 139 ? 0.7775 0.5804 0.7812 -0.0388 0.2209  0.0363  145 GLU   A CB  
1080 C CG  . GLU   A 139 ? 0.8647 0.6840 0.8506 -0.0423 0.1945  0.0365  145 GLU   A CG  
1081 C CD  . GLU   A 139 ? 1.0062 0.8059 0.9299 -0.0562 0.1897  0.0289  145 GLU   A CD  
1082 O OE1 . GLU   A 139 ? 1.0238 0.8233 0.9260 -0.0606 0.1793  0.0319  145 GLU   A OE1 
1083 O OE2 . GLU   A 139 ? 1.0657 0.8499 0.9630 -0.0634 0.1956  0.0209  145 GLU   A OE2 
1084 N N1  . A1B4F B .   ? 0.3258 0.3116 0.4245 -0.0084 -0.0025 -0.0105 201 A1B4F A N1  
1085 C C4  . A1B4F B .   ? 0.4242 0.3001 0.3933 -0.0125 0.0489  -0.0377 201 A1B4F A C4  
1086 C C5  . A1B4F B .   ? 0.4172 0.3119 0.4038 -0.0139 0.0335  -0.0348 201 A1B4F A C5  
1087 C C6  . A1B4F B .   ? 0.4297 0.3162 0.4210 -0.0155 0.0343  -0.0378 201 A1B4F A C6  
1088 C C7  . A1B4F B .   ? 0.3907 0.3187 0.4333 -0.0119 0.0190  -0.0275 201 A1B4F A C7  
1089 C C8  . A1B4F B .   ? 0.3809 0.3275 0.4369 -0.0134 0.0030  -0.0231 201 A1B4F A C8  
1090 C C10 . A1B4F B .   ? 0.3993 0.3316 0.4416 -0.0193 -0.0061 -0.0275 201 A1B4F A C10 
1091 C C13 . A1B4F B .   ? 0.3972 0.3149 0.3951 -0.0139 0.0192  -0.0294 201 A1B4F A C13 
1092 O O1  . A1B4F B .   ? 0.4748 0.3431 0.4274 -0.0310 0.0031  -0.0432 201 A1B4F A O1  
1093 C C12 . A1B4F B .   ? 0.4309 0.3237 0.4173 -0.0247 0.0040  -0.0376 201 A1B4F A C12 
1094 C C11 . A1B4F B .   ? 0.4212 0.3313 0.4284 -0.0258 -0.0105 -0.0330 201 A1B4F A C11 
1095 C C9  . A1B4F B .   ? 0.3500 0.3162 0.4371 -0.0091 0.0050  -0.0162 201 A1B4F A C9  
1096 O O   . A1B4F B .   ? 0.3420 0.3043 0.4418 -0.0070 0.0139  -0.0156 201 A1B4F A O   
1097 N N   . A1B4F B .   ? 0.4143 0.3177 0.4204 -0.0175 0.0178  -0.0346 201 A1B4F A N   
1098 C C3  . A1B4F B .   ? 0.4272 0.3089 0.3907 -0.0113 0.0482  -0.0351 201 A1B4F A C3  
1099 C C2  . A1B4F B .   ? 0.4067 0.3122 0.3821 -0.0117 0.0327  -0.0300 201 A1B4F A C2  
1100 C C1  . A1B4F B .   ? 0.3939 0.3168 0.3864 -0.0130 0.0189  -0.0273 201 A1B4F A C1  
1101 C C   . A1B4F B .   ? 0.3887 0.3328 0.3926 -0.0135 0.0058  -0.0221 201 A1B4F A C   
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