data_7I3O
# 
_entry.id   7I3O 
# 
_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   7I3O         pdb_00007i3o 10.2210/pdb7i3o/pdb 
WWPDB D_1001408275 ?            ?                   
# 
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                        7I3O 
_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-[(6-chloro-2,3-dihydro-4H-1,4-benzoxazin-4-yl)acetyl]piperidine-3-carboxamide' 337.801   1  ?         ? 
? ? 
3 non-polymer syn 'ZINC ION'                                                                             65.409    1  ?         ? 
? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                                   78.133    2  ?         ? 
? ? 
5 water       nat water                                                                                  18.015    85 ?         ? 
? ? 
# 
_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-[(6-chloro-2,3-dihydro-4H-1,4-benzoxazin-4-yl)acetyl]piperidine-3-carboxamide' A1B14 
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 
A1B14 non-polymer         . '(3S)-1-[(6-chloro-2,3-dihydro-4H-1,4-benzoxazin-4-yl)acetyl]piperidine-3-carboxamide' ? 
'C16 H20 Cl N3 O3' 337.801 
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        A1B14 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1B14 
_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 A1B14 1  201 201 A1B14 LIG A . 
C 3 ZN    1  202 1   ZN    ZN  A . 
D 4 DMS   1  203 2   DMS   DMS A . 
E 4 DMS   1  204 6   DMS   DMS A . 
F 5 HOH   1  301 37  HOH   HOH A . 
F 5 HOH   2  302 9   HOH   HOH A . 
F 5 HOH   3  303 18  HOH   HOH A . 
F 5 HOH   4  304 29  HOH   HOH A . 
F 5 HOH   5  305 59  HOH   HOH A . 
F 5 HOH   6  306 85  HOH   HOH A . 
F 5 HOH   7  307 47  HOH   HOH A . 
F 5 HOH   8  308 12  HOH   HOH A . 
F 5 HOH   9  309 22  HOH   HOH A . 
F 5 HOH   10 310 14  HOH   HOH A . 
F 5 HOH   11 311 27  HOH   HOH A . 
F 5 HOH   12 312 36  HOH   HOH A . 
F 5 HOH   13 313 42  HOH   HOH A . 
F 5 HOH   14 314 8   HOH   HOH A . 
F 5 HOH   15 315 60  HOH   HOH A . 
F 5 HOH   16 316 77  HOH   HOH A . 
F 5 HOH   17 317 16  HOH   HOH A . 
F 5 HOH   18 318 2   HOH   HOH A . 
F 5 HOH   19 319 25  HOH   HOH A . 
F 5 HOH   20 320 7   HOH   HOH A . 
F 5 HOH   21 321 40  HOH   HOH A . 
F 5 HOH   22 322 11  HOH   HOH A . 
F 5 HOH   23 323 24  HOH   HOH A . 
F 5 HOH   24 324 48  HOH   HOH A . 
F 5 HOH   25 325 34  HOH   HOH A . 
F 5 HOH   26 326 64  HOH   HOH A . 
F 5 HOH   27 327 72  HOH   HOH A . 
F 5 HOH   28 328 19  HOH   HOH A . 
F 5 HOH   29 329 28  HOH   HOH A . 
F 5 HOH   30 330 21  HOH   HOH A . 
F 5 HOH   31 331 4   HOH   HOH A . 
F 5 HOH   32 332 23  HOH   HOH A . 
F 5 HOH   33 333 55  HOH   HOH A . 
F 5 HOH   34 334 87  HOH   HOH A . 
F 5 HOH   35 335 54  HOH   HOH A . 
F 5 HOH   36 336 17  HOH   HOH A . 
F 5 HOH   37 337 83  HOH   HOH A . 
F 5 HOH   38 338 38  HOH   HOH A . 
F 5 HOH   39 339 82  HOH   HOH A . 
F 5 HOH   40 340 45  HOH   HOH A . 
F 5 HOH   41 341 13  HOH   HOH A . 
F 5 HOH   42 342 35  HOH   HOH A . 
F 5 HOH   43 343 67  HOH   HOH A . 
F 5 HOH   44 344 51  HOH   HOH A . 
F 5 HOH   45 345 46  HOH   HOH A . 
F 5 HOH   46 346 20  HOH   HOH A . 
F 5 HOH   47 347 6   HOH   HOH A . 
F 5 HOH   48 348 10  HOH   HOH A . 
F 5 HOH   49 349 39  HOH   HOH A . 
F 5 HOH   50 350 78  HOH   HOH A . 
F 5 HOH   51 351 33  HOH   HOH A . 
F 5 HOH   52 352 49  HOH   HOH A . 
F 5 HOH   53 353 5   HOH   HOH A . 
F 5 HOH   54 354 15  HOH   HOH A . 
F 5 HOH   55 355 30  HOH   HOH A . 
F 5 HOH   56 356 63  HOH   HOH A . 
F 5 HOH   57 357 65  HOH   HOH A . 
F 5 HOH   58 358 3   HOH   HOH A . 
F 5 HOH   59 359 80  HOH   HOH A . 
F 5 HOH   60 360 41  HOH   HOH A . 
F 5 HOH   61 361 32  HOH   HOH A . 
F 5 HOH   62 362 70  HOH   HOH A . 
F 5 HOH   63 363 75  HOH   HOH A . 
F 5 HOH   64 364 68  HOH   HOH A . 
F 5 HOH   65 365 53  HOH   HOH A . 
F 5 HOH   66 366 26  HOH   HOH A . 
F 5 HOH   67 367 56  HOH   HOH A . 
F 5 HOH   68 368 31  HOH   HOH A . 
F 5 HOH   69 369 43  HOH   HOH A . 
F 5 HOH   70 370 81  HOH   HOH A . 
F 5 HOH   71 371 66  HOH   HOH A . 
F 5 HOH   72 372 76  HOH   HOH A . 
F 5 HOH   73 373 61  HOH   HOH A . 
F 5 HOH   74 374 44  HOH   HOH A . 
F 5 HOH   75 375 73  HOH   HOH A . 
F 5 HOH   76 376 86  HOH   HOH A . 
F 5 HOH   77 377 74  HOH   HOH A . 
F 5 HOH   78 378 58  HOH   HOH A . 
F 5 HOH   79 379 52  HOH   HOH A . 
F 5 HOH   80 380 79  HOH   HOH A . 
F 5 HOH   81 381 84  HOH   HOH A . 
F 5 HOH   82 382 69  HOH   HOH A . 
F 5 HOH   83 383 71  HOH   HOH A . 
F 5 HOH   84 384 62  HOH   HOH A . 
F 5 HOH   85 385 88  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           7I3O 
_cell.length_a           72.853 
_cell.length_b           62.059 
_cell.length_c           32.744 
_cell.angle_alpha        90.00 
_cell.angle_beta         93.16 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I3O 
_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          7I3O 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.33 
_exptl_crystal.density_percent_sol   47.10 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2024-12-13 
_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   0.92203 
_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        0.92203 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7I3O 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             47.21 
_reflns.d_resolution_high            1.69 
_reflns.number_obs                   14134 
_reflns.percent_possible_obs         86.2 
_reflns.pdbx_Rmerge_I_obs            0.120 
_reflns.pdbx_netI_over_sigmaI        6.9 
_reflns.pdbx_redundancy              5.5 
_reflns.pdbx_Rrim_I_all              0.131 
_reflns.pdbx_Rpim_I_all              0.053 
_reflns.pdbx_CC_half                 0.996 
_reflns.pdbx_number_measured_all     77979 
_reflns.pdbx_chi_squared             0.67 
_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                  1.69 
_reflns_shell.d_res_low                   1.78 
_reflns_shell.number_measured_all         5533 
_reflns_shell.number_unique_obs           1580 
_reflns_shell.Rmerge_I_obs                1.601 
_reflns_shell.pdbx_chi_squared            0.42 
_reflns_shell.pdbx_redundancy             3.5 
_reflns_shell.percent_possible_obs        66.6 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.5 
_reflns_shell.pdbx_Rrim_I_all             1.857 
_reflns_shell.pdbx_Rpim_I_all             0.912 
_reflns_shell.pdbx_CC_half                0.434 
_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                                 7I3O 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     13924 
_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                             47.21 
_refine.ls_d_res_high                            1.686 
_refine.ls_percent_reflns_obs                    84.4 
_refine.ls_R_factor_obs                          0.2386 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2376 
_refine.ls_R_factor_R_free                       0.2573 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.960 
_refine.ls_number_reflns_R_free                  690 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.937 
_refine.correlation_coeff_Fo_to_Fc_free          0.918 
_refine.B_iso_mean                               31.07 
_refine.aniso_B[1][1]                            0.88710 
_refine.aniso_B[2][2]                            -3.45010 
_refine.aniso_B[3][3]                            2.56300 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            0.03320 
_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             0.152 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.134 
_refine.pdbx_overall_SU_R_Blow_DPI               0.155 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.135 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7I3O 
_refine_analyze.Luzzati_coordinate_error_obs    0.29 
_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         28 
_refine_hist.number_atoms_solvent             85 
_refine_hist.number_atoms_total               1187 
_refine_hist.d_res_high                       1.686 
_refine_hist.d_res_low                        47.21 
# 
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  1135 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               0.98  ? 2.00  1544 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  381  '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  204  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1132 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           3.61  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           15.37 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  138  'X-RAY DIFFRACTION' SEMIHARMONIC 
t_sum_occupancies         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_distance        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_angle           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_torsion         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_ideal_dist_contact      ?     ? 4.00  899  'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   35 
_refine_ls_shell.d_res_high                       1.69 
_refine_ls_shell.d_res_low                        1.71 
_refine_ls_shell.number_reflns_R_work             391 
_refine_ls_shell.R_factor_R_work                  0.3562 
_refine_ls_shell.percent_reflns_obs               52.26 
_refine_ls_shell.R_factor_R_free                  0.3726 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            4.63 
_refine_ls_shell.number_reflns_R_free             19 
_refine_ls_shell.number_reflns_all                410 
_refine_ls_shell.R_factor_all                     0.3570 
# 
_struct.entry_id                  7I3O 
_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-0036402-001 (A71EV2A-x4528)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I3O 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 4 ? 
F N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    POLG_CX16G 
_struct_ref.pdbx_db_accession          Q65900 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_struct_ref.pdbx_align_begin           869 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              7I3O 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 144 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q65900 
_struct_ref_seq.db_align_beg                  869 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1012 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       7 
_struct_ref_seq.pdbx_auth_seq_align_end       150 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2 AA2 THR A 18  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
HELX_P HELX_P3 AA3 SER A 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
HELX_P HELX_P4 AA4 LEU A 134 ? GLU A 139 ? LEU A 140 GLU A 145 5 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 50  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 56  A ZN 202 1_555 ? ? ? ? ? ? ? 2.334 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.407 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.391 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 C ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 1.983 ? ? 
# 
_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_555 106.4 ? 
2 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 108.3 ? 
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_555 114.6 ? 
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_555 117.4 ? 
5 SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 102.1 ? 
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_555 108.2 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA1 2 LEU A 34  ? CYS A 44  ? LEU A 40  CYS A 50  
AA1 3 ILE A 4   ? ASN A 13  ? ILE A 10  ASN A 19  
AA2 1 LYS A 64  ? SER A 69  ? LYS A 70  SER A 75  
AA2 2 THR A 54  ? CYS A 59  ? THR A 60  CYS A 65  
AA2 3 ILE A 107 ? CYS A 110 ? ILE A 113 CYS A 116 
AA2 4 GLY A 113 ? GLY A 122 ? GLY A 119 GLY A 128 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N TRP A 27  ? N TRP A 33  O VAL A 36  ? O VAL A 42  
AA1 2 3 N LEU A 35  ? N LEU A 41  O VAL A 12  ? O VAL A 18  
AA2 1 2 O LYS A 64  ? O LYS A 70  N CYS A 59  ? N CYS A 65  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N LEU A 108 ? N LEU A 114 O VAL A 115 ? O VAL A 121 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O ASP A 130 ? O ASP A 136 N HIS A 91  ? N HIS A 97  
AA2 6 7 O GLN A 89  ? O GLN A 95  N ILE A 76  ? N ILE A 82  
# 
_pdbx_entry_details.entry_id                   7I3O 
_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 ? ? -86.81 30.87  
2 1 GLU A 85 ? ? -45.13 -89.49 
3 1 ALA A 86 ? ? 175.24 145.67 
# 
_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         15.0958 
_pdbx_refine_tls.origin_y         6.6794 
_pdbx_refine_tls.origin_z         14.3330 
_pdbx_refine_tls.T[1][1]          0.0206 
_pdbx_refine_tls.T[2][2]          -0.0472 
_pdbx_refine_tls.T[3][3]          -0.0376 
_pdbx_refine_tls.T[1][2]          0.0293 
_pdbx_refine_tls.T[1][3]          -0.0038 
_pdbx_refine_tls.T[2][3]          -0.0131 
_pdbx_refine_tls.L[1][1]          1.3037 
_pdbx_refine_tls.L[2][2]          8.5704 
_pdbx_refine_tls.L[3][3]          1.1122 
_pdbx_refine_tls.L[1][2]          2.8605 
_pdbx_refine_tls.L[1][3]          -0.9984 
_pdbx_refine_tls.L[2][3]          -3.1597 
_pdbx_refine_tls.S[1][1]          -0.0742 
_pdbx_refine_tls.S[1][2]          0.1100 
_pdbx_refine_tls.S[1][3]          -0.0201 
_pdbx_refine_tls.S[2][1]          0.4663 
_pdbx_refine_tls.S[2][2]          0.1301 
_pdbx_refine_tls.S[2][3]          -0.3768 
_pdbx_refine_tls.S[3][1]          -0.1175 
_pdbx_refine_tls.S[3][2]          -0.2336 
_pdbx_refine_tls.S[3][3]          -0.0559 
# 
_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 
6 1 N 0 A DMS 203 ? D DMS ?   
# 
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 
A1B14 N1   N  N N 1   
A1B14 C4   C  N N 2   
A1B14 C5   C  N N 3   
A1B14 C6   C  N N 4   
A1B14 C7   C  N N 5   
A1B14 C8   C  N N 6   
A1B14 C10  C  Y N 7   
A1B14 C13  C  Y N 8   
A1B14 C15  C  N N 9   
A1B14 CL   CL N N 10  
A1B14 C12  C  Y N 11  
A1B14 C11  C  Y N 12  
A1B14 C14  C  Y N 13  
A1B14 C9   C  Y N 14  
A1B14 O2   O  N N 15  
A1B14 N2   N  N N 16  
A1B14 O1   O  N N 17  
A1B14 C3   C  N N 18  
A1B14 C2   C  N N 19  
A1B14 C1   C  N S 20  
A1B14 C    C  N N 21  
A1B14 O    O  N N 22  
A1B14 N    N  N N 23  
A1B14 H8   H  N N 24  
A1B14 H7   H  N N 25  
A1B14 H10  H  N N 26  
A1B14 H9   H  N N 27  
A1B14 H11  H  N N 28  
A1B14 H12  H  N N 29  
A1B14 H13  H  N N 30  
A1B14 H14  H  N N 31  
A1B14 H15  H  N N 32  
A1B14 H17  H  N N 33  
A1B14 H19  H  N N 34  
A1B14 H18  H  N N 35  
A1B14 H16  H  N N 36  
A1B14 H6   H  N N 37  
A1B14 H5   H  N N 38  
A1B14 H4   H  N N 39  
A1B14 H3   H  N N 40  
A1B14 H    H  N N 41  
A1B14 H1   H  N N 42  
A1B14 H2   H  N N 43  
ALA   N    N  N N 44  
ALA   CA   C  N S 45  
ALA   C    C  N N 46  
ALA   O    O  N N 47  
ALA   CB   C  N N 48  
ALA   OXT  O  N N 49  
ALA   H    H  N N 50  
ALA   H2   H  N N 51  
ALA   HA   H  N N 52  
ALA   HB1  H  N N 53  
ALA   HB2  H  N N 54  
ALA   HB3  H  N N 55  
ALA   HXT  H  N N 56  
ARG   N    N  N N 57  
ARG   CA   C  N S 58  
ARG   C    C  N N 59  
ARG   O    O  N N 60  
ARG   CB   C  N N 61  
ARG   CG   C  N N 62  
ARG   CD   C  N N 63  
ARG   NE   N  N N 64  
ARG   CZ   C  N N 65  
ARG   NH1  N  N N 66  
ARG   NH2  N  N N 67  
ARG   OXT  O  N N 68  
ARG   H    H  N N 69  
ARG   H2   H  N N 70  
ARG   HA   H  N N 71  
ARG   HB2  H  N N 72  
ARG   HB3  H  N N 73  
ARG   HG2  H  N N 74  
ARG   HG3  H  N N 75  
ARG   HD2  H  N N 76  
ARG   HD3  H  N N 77  
ARG   HE   H  N N 78  
ARG   HH11 H  N N 79  
ARG   HH12 H  N N 80  
ARG   HH21 H  N N 81  
ARG   HH22 H  N N 82  
ARG   HXT  H  N N 83  
ASN   N    N  N N 84  
ASN   CA   C  N S 85  
ASN   C    C  N N 86  
ASN   O    O  N N 87  
ASN   CB   C  N N 88  
ASN   CG   C  N N 89  
ASN   OD1  O  N N 90  
ASN   ND2  N  N N 91  
ASN   OXT  O  N N 92  
ASN   H    H  N N 93  
ASN   H2   H  N N 94  
ASN   HA   H  N N 95  
ASN   HB2  H  N N 96  
ASN   HB3  H  N N 97  
ASN   HD21 H  N N 98  
ASN   HD22 H  N N 99  
ASN   HXT  H  N N 100 
ASP   N    N  N N 101 
ASP   CA   C  N S 102 
ASP   C    C  N N 103 
ASP   O    O  N N 104 
ASP   CB   C  N N 105 
ASP   CG   C  N N 106 
ASP   OD1  O  N N 107 
ASP   OD2  O  N N 108 
ASP   OXT  O  N N 109 
ASP   H    H  N N 110 
ASP   H2   H  N N 111 
ASP   HA   H  N N 112 
ASP   HB2  H  N N 113 
ASP   HB3  H  N N 114 
ASP   HD2  H  N N 115 
ASP   HXT  H  N N 116 
CYS   N    N  N N 117 
CYS   CA   C  N R 118 
CYS   C    C  N N 119 
CYS   O    O  N N 120 
CYS   CB   C  N N 121 
CYS   SG   S  N N 122 
CYS   OXT  O  N N 123 
CYS   H    H  N N 124 
CYS   H2   H  N N 125 
CYS   HA   H  N N 126 
CYS   HB2  H  N N 127 
CYS   HB3  H  N N 128 
CYS   HG   H  N N 129 
CYS   HXT  H  N N 130 
DMS   S    S  N N 131 
DMS   O    O  N N 132 
DMS   C1   C  N N 133 
DMS   C2   C  N N 134 
DMS   H11  H  N N 135 
DMS   H12  H  N N 136 
DMS   H13  H  N N 137 
DMS   H21  H  N N 138 
DMS   H22  H  N N 139 
DMS   H23  H  N N 140 
GLN   N    N  N N 141 
GLN   CA   C  N S 142 
GLN   C    C  N N 143 
GLN   O    O  N N 144 
GLN   CB   C  N N 145 
GLN   CG   C  N N 146 
GLN   CD   C  N N 147 
GLN   OE1  O  N N 148 
GLN   NE2  N  N N 149 
GLN   OXT  O  N N 150 
GLN   H    H  N N 151 
GLN   H2   H  N N 152 
GLN   HA   H  N N 153 
GLN   HB2  H  N N 154 
GLN   HB3  H  N N 155 
GLN   HG2  H  N N 156 
GLN   HG3  H  N N 157 
GLN   HE21 H  N N 158 
GLN   HE22 H  N N 159 
GLN   HXT  H  N N 160 
GLU   N    N  N N 161 
GLU   CA   C  N S 162 
GLU   C    C  N N 163 
GLU   O    O  N N 164 
GLU   CB   C  N N 165 
GLU   CG   C  N N 166 
GLU   CD   C  N N 167 
GLU   OE1  O  N N 168 
GLU   OE2  O  N N 169 
GLU   OXT  O  N N 170 
GLU   H    H  N N 171 
GLU   H2   H  N N 172 
GLU   HA   H  N N 173 
GLU   HB2  H  N N 174 
GLU   HB3  H  N N 175 
GLU   HG2  H  N N 176 
GLU   HG3  H  N N 177 
GLU   HE2  H  N N 178 
GLU   HXT  H  N N 179 
GLY   N    N  N N 180 
GLY   CA   C  N N 181 
GLY   C    C  N N 182 
GLY   O    O  N N 183 
GLY   OXT  O  N N 184 
GLY   H    H  N N 185 
GLY   H2   H  N N 186 
GLY   HA2  H  N N 187 
GLY   HA3  H  N N 188 
GLY   HXT  H  N N 189 
HIS   N    N  N N 190 
HIS   CA   C  N S 191 
HIS   C    C  N N 192 
HIS   O    O  N N 193 
HIS   CB   C  N N 194 
HIS   CG   C  Y N 195 
HIS   ND1  N  Y N 196 
HIS   CD2  C  Y N 197 
HIS   CE1  C  Y N 198 
HIS   NE2  N  Y N 199 
HIS   OXT  O  N N 200 
HIS   H    H  N N 201 
HIS   H2   H  N N 202 
HIS   HA   H  N N 203 
HIS   HB2  H  N N 204 
HIS   HB3  H  N N 205 
HIS   HD1  H  N N 206 
HIS   HD2  H  N N 207 
HIS   HE1  H  N N 208 
HIS   HE2  H  N N 209 
HIS   HXT  H  N N 210 
HOH   O    O  N N 211 
HOH   H1   H  N N 212 
HOH   H2   H  N N 213 
ILE   N    N  N N 214 
ILE   CA   C  N S 215 
ILE   C    C  N N 216 
ILE   O    O  N N 217 
ILE   CB   C  N S 218 
ILE   CG1  C  N N 219 
ILE   CG2  C  N N 220 
ILE   CD1  C  N N 221 
ILE   OXT  O  N N 222 
ILE   H    H  N N 223 
ILE   H2   H  N N 224 
ILE   HA   H  N N 225 
ILE   HB   H  N N 226 
ILE   HG12 H  N N 227 
ILE   HG13 H  N N 228 
ILE   HG21 H  N N 229 
ILE   HG22 H  N N 230 
ILE   HG23 H  N N 231 
ILE   HD11 H  N N 232 
ILE   HD12 H  N N 233 
ILE   HD13 H  N N 234 
ILE   HXT  H  N N 235 
LEU   N    N  N N 236 
LEU   CA   C  N S 237 
LEU   C    C  N N 238 
LEU   O    O  N N 239 
LEU   CB   C  N N 240 
LEU   CG   C  N N 241 
LEU   CD1  C  N N 242 
LEU   CD2  C  N N 243 
LEU   OXT  O  N N 244 
LEU   H    H  N N 245 
LEU   H2   H  N N 246 
LEU   HA   H  N N 247 
LEU   HB2  H  N N 248 
LEU   HB3  H  N N 249 
LEU   HG   H  N N 250 
LEU   HD11 H  N N 251 
LEU   HD12 H  N N 252 
LEU   HD13 H  N N 253 
LEU   HD21 H  N N 254 
LEU   HD22 H  N N 255 
LEU   HD23 H  N N 256 
LEU   HXT  H  N N 257 
LYS   N    N  N N 258 
LYS   CA   C  N S 259 
LYS   C    C  N N 260 
LYS   O    O  N N 261 
LYS   CB   C  N N 262 
LYS   CG   C  N N 263 
LYS   CD   C  N N 264 
LYS   CE   C  N N 265 
LYS   NZ   N  N N 266 
LYS   OXT  O  N N 267 
LYS   H    H  N N 268 
LYS   H2   H  N N 269 
LYS   HA   H  N N 270 
LYS   HB2  H  N N 271 
LYS   HB3  H  N N 272 
LYS   HG2  H  N N 273 
LYS   HG3  H  N N 274 
LYS   HD2  H  N N 275 
LYS   HD3  H  N N 276 
LYS   HE2  H  N N 277 
LYS   HE3  H  N N 278 
LYS   HZ1  H  N N 279 
LYS   HZ2  H  N N 280 
LYS   HZ3  H  N N 281 
LYS   HXT  H  N N 282 
MET   N    N  N N 283 
MET   CA   C  N S 284 
MET   C    C  N N 285 
MET   O    O  N N 286 
MET   CB   C  N N 287 
MET   CG   C  N N 288 
MET   SD   S  N N 289 
MET   CE   C  N N 290 
MET   OXT  O  N N 291 
MET   H    H  N N 292 
MET   H2   H  N N 293 
MET   HA   H  N N 294 
MET   HB2  H  N N 295 
MET   HB3  H  N N 296 
MET   HG2  H  N N 297 
MET   HG3  H  N N 298 
MET   HE1  H  N N 299 
MET   HE2  H  N N 300 
MET   HE3  H  N N 301 
MET   HXT  H  N N 302 
PHE   N    N  N N 303 
PHE   CA   C  N S 304 
PHE   C    C  N N 305 
PHE   O    O  N N 306 
PHE   CB   C  N N 307 
PHE   CG   C  Y N 308 
PHE   CD1  C  Y N 309 
PHE   CD2  C  Y N 310 
PHE   CE1  C  Y N 311 
PHE   CE2  C  Y N 312 
PHE   CZ   C  Y N 313 
PHE   OXT  O  N N 314 
PHE   H    H  N N 315 
PHE   H2   H  N N 316 
PHE   HA   H  N N 317 
PHE   HB2  H  N N 318 
PHE   HB3  H  N N 319 
PHE   HD1  H  N N 320 
PHE   HD2  H  N N 321 
PHE   HE1  H  N N 322 
PHE   HE2  H  N N 323 
PHE   HZ   H  N N 324 
PHE   HXT  H  N N 325 
PRO   N    N  N N 326 
PRO   CA   C  N S 327 
PRO   C    C  N N 328 
PRO   O    O  N N 329 
PRO   CB   C  N N 330 
PRO   CG   C  N N 331 
PRO   CD   C  N N 332 
PRO   OXT  O  N N 333 
PRO   H    H  N N 334 
PRO   HA   H  N N 335 
PRO   HB2  H  N N 336 
PRO   HB3  H  N N 337 
PRO   HG2  H  N N 338 
PRO   HG3  H  N N 339 
PRO   HD2  H  N N 340 
PRO   HD3  H  N N 341 
PRO   HXT  H  N N 342 
SER   N    N  N N 343 
SER   CA   C  N S 344 
SER   C    C  N N 345 
SER   O    O  N N 346 
SER   CB   C  N N 347 
SER   OG   O  N N 348 
SER   OXT  O  N N 349 
SER   H    H  N N 350 
SER   H2   H  N N 351 
SER   HA   H  N N 352 
SER   HB2  H  N N 353 
SER   HB3  H  N N 354 
SER   HG   H  N N 355 
SER   HXT  H  N N 356 
THR   N    N  N N 357 
THR   CA   C  N S 358 
THR   C    C  N N 359 
THR   O    O  N N 360 
THR   CB   C  N R 361 
THR   OG1  O  N N 362 
THR   CG2  C  N N 363 
THR   OXT  O  N N 364 
THR   H    H  N N 365 
THR   H2   H  N N 366 
THR   HA   H  N N 367 
THR   HB   H  N N 368 
THR   HG1  H  N N 369 
THR   HG21 H  N N 370 
THR   HG22 H  N N 371 
THR   HG23 H  N N 372 
THR   HXT  H  N N 373 
TRP   N    N  N N 374 
TRP   CA   C  N S 375 
TRP   C    C  N N 376 
TRP   O    O  N N 377 
TRP   CB   C  N N 378 
TRP   CG   C  Y N 379 
TRP   CD1  C  Y N 380 
TRP   CD2  C  Y N 381 
TRP   NE1  N  Y N 382 
TRP   CE2  C  Y N 383 
TRP   CE3  C  Y N 384 
TRP   CZ2  C  Y N 385 
TRP   CZ3  C  Y N 386 
TRP   CH2  C  Y N 387 
TRP   OXT  O  N N 388 
TRP   H    H  N N 389 
TRP   H2   H  N N 390 
TRP   HA   H  N N 391 
TRP   HB2  H  N N 392 
TRP   HB3  H  N N 393 
TRP   HD1  H  N N 394 
TRP   HE1  H  N N 395 
TRP   HE3  H  N N 396 
TRP   HZ2  H  N N 397 
TRP   HZ3  H  N N 398 
TRP   HH2  H  N N 399 
TRP   HXT  H  N N 400 
TYR   N    N  N N 401 
TYR   CA   C  N S 402 
TYR   C    C  N N 403 
TYR   O    O  N N 404 
TYR   CB   C  N N 405 
TYR   CG   C  Y N 406 
TYR   CD1  C  Y N 407 
TYR   CD2  C  Y N 408 
TYR   CE1  C  Y N 409 
TYR   CE2  C  Y N 410 
TYR   CZ   C  Y N 411 
TYR   OH   O  N N 412 
TYR   OXT  O  N N 413 
TYR   H    H  N N 414 
TYR   H2   H  N N 415 
TYR   HA   H  N N 416 
TYR   HB2  H  N N 417 
TYR   HB3  H  N N 418 
TYR   HD1  H  N N 419 
TYR   HD2  H  N N 420 
TYR   HE1  H  N N 421 
TYR   HE2  H  N N 422 
TYR   HH   H  N N 423 
TYR   HXT  H  N N 424 
VAL   N    N  N N 425 
VAL   CA   C  N S 426 
VAL   C    C  N N 427 
VAL   O    O  N N 428 
VAL   CB   C  N N 429 
VAL   CG1  C  N N 430 
VAL   CG2  C  N N 431 
VAL   OXT  O  N N 432 
VAL   H    H  N N 433 
VAL   H2   H  N N 434 
VAL   HA   H  N N 435 
VAL   HB   H  N N 436 
VAL   HG11 H  N N 437 
VAL   HG12 H  N N 438 
VAL   HG13 H  N N 439 
VAL   HG21 H  N N 440 
VAL   HG22 H  N N 441 
VAL   HG23 H  N N 442 
VAL   HXT  H  N N 443 
ZN    ZN   ZN N N 444 
# 
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 
A1B14 N   C    sing N N 1   
A1B14 O   C    doub N N 2   
A1B14 C   C1   sing N N 3   
A1B14 C1  C2   sing N N 4   
A1B14 C2  C3   sing N N 5   
A1B14 C3  C4   sing N N 6   
A1B14 C4  N1   sing N N 7   
A1B14 N1  C5   sing N N 8   
A1B14 O1  C5   doub N N 9   
A1B14 C5  C6   sing N N 10  
A1B14 C6  N2   sing N N 11  
A1B14 N2  C7   sing N N 12  
A1B14 C7  C8   sing N N 13  
A1B14 C8  O2   sing N N 14  
A1B14 O2  C9   sing N N 15  
A1B14 C9  C10  sing Y N 16  
A1B14 C10 C11  doub Y N 17  
A1B14 C11 C12  sing Y N 18  
A1B14 C12 CL   sing N N 19  
A1B14 C13 C12  doub Y N 20  
A1B14 C14 C13  sing Y N 21  
A1B14 C9  C14  doub Y N 22  
A1B14 N2  C14  sing N N 23  
A1B14 C15 N1   sing N N 24  
A1B14 C1  C15  sing N N 25  
A1B14 C4  H8   sing N N 26  
A1B14 C4  H7   sing N N 27  
A1B14 C6  H10  sing N N 28  
A1B14 C6  H9   sing N N 29  
A1B14 C7  H11  sing N N 30  
A1B14 C7  H12  sing N N 31  
A1B14 C8  H13  sing N N 32  
A1B14 C8  H14  sing N N 33  
A1B14 C10 H15  sing N N 34  
A1B14 C13 H17  sing N N 35  
A1B14 C15 H19  sing N N 36  
A1B14 C15 H18  sing N N 37  
A1B14 C11 H16  sing N N 38  
A1B14 C3  H6   sing N N 39  
A1B14 C3  H5   sing N N 40  
A1B14 C2  H4   sing N N 41  
A1B14 C2  H3   sing N N 42  
A1B14 C1  H    sing N N 43  
A1B14 N   H1   sing N N 44  
A1B14 N   H2   sing N N 45  
ALA   N   CA   sing N N 46  
ALA   N   H    sing N N 47  
ALA   N   H2   sing N N 48  
ALA   CA  C    sing N N 49  
ALA   CA  CB   sing N N 50  
ALA   CA  HA   sing N N 51  
ALA   C   O    doub N N 52  
ALA   C   OXT  sing N N 53  
ALA   CB  HB1  sing N N 54  
ALA   CB  HB2  sing N N 55  
ALA   CB  HB3  sing N N 56  
ALA   OXT HXT  sing N N 57  
ARG   N   CA   sing N N 58  
ARG   N   H    sing N N 59  
ARG   N   H2   sing N N 60  
ARG   CA  C    sing N N 61  
ARG   CA  CB   sing N N 62  
ARG   CA  HA   sing N N 63  
ARG   C   O    doub N N 64  
ARG   C   OXT  sing N N 65  
ARG   CB  CG   sing N N 66  
ARG   CB  HB2  sing N N 67  
ARG   CB  HB3  sing N N 68  
ARG   CG  CD   sing N N 69  
ARG   CG  HG2  sing N N 70  
ARG   CG  HG3  sing N N 71  
ARG   CD  NE   sing N N 72  
ARG   CD  HD2  sing N N 73  
ARG   CD  HD3  sing N N 74  
ARG   NE  CZ   sing N N 75  
ARG   NE  HE   sing N N 76  
ARG   CZ  NH1  sing N N 77  
ARG   CZ  NH2  doub N N 78  
ARG   NH1 HH11 sing N N 79  
ARG   NH1 HH12 sing N N 80  
ARG   NH2 HH21 sing N N 81  
ARG   NH2 HH22 sing N N 82  
ARG   OXT HXT  sing N N 83  
ASN   N   CA   sing N N 84  
ASN   N   H    sing N N 85  
ASN   N   H2   sing N N 86  
ASN   CA  C    sing N N 87  
ASN   CA  CB   sing N N 88  
ASN   CA  HA   sing N N 89  
ASN   C   O    doub N N 90  
ASN   C   OXT  sing N N 91  
ASN   CB  CG   sing N N 92  
ASN   CB  HB2  sing N N 93  
ASN   CB  HB3  sing N N 94  
ASN   CG  OD1  doub N N 95  
ASN   CG  ND2  sing N N 96  
ASN   ND2 HD21 sing N N 97  
ASN   ND2 HD22 sing N N 98  
ASN   OXT HXT  sing N N 99  
ASP   N   CA   sing N N 100 
ASP   N   H    sing N N 101 
ASP   N   H2   sing N N 102 
ASP   CA  C    sing N N 103 
ASP   CA  CB   sing N N 104 
ASP   CA  HA   sing N N 105 
ASP   C   O    doub N N 106 
ASP   C   OXT  sing N N 107 
ASP   CB  CG   sing N N 108 
ASP   CB  HB2  sing N N 109 
ASP   CB  HB3  sing N N 110 
ASP   CG  OD1  doub N N 111 
ASP   CG  OD2  sing N N 112 
ASP   OD2 HD2  sing N N 113 
ASP   OXT HXT  sing N N 114 
CYS   N   CA   sing N N 115 
CYS   N   H    sing N N 116 
CYS   N   H2   sing N N 117 
CYS   CA  C    sing N N 118 
CYS   CA  CB   sing N N 119 
CYS   CA  HA   sing N N 120 
CYS   C   O    doub N N 121 
CYS   C   OXT  sing N N 122 
CYS   CB  SG   sing N N 123 
CYS   CB  HB2  sing N N 124 
CYS   CB  HB3  sing N N 125 
CYS   SG  HG   sing N N 126 
CYS   OXT HXT  sing N N 127 
DMS   S   O    doub N N 128 
DMS   S   C1   sing N N 129 
DMS   S   C2   sing N N 130 
DMS   C1  H11  sing N N 131 
DMS   C1  H12  sing N N 132 
DMS   C1  H13  sing N N 133 
DMS   C2  H21  sing N N 134 
DMS   C2  H22  sing N N 135 
DMS   C2  H23  sing N N 136 
GLN   N   CA   sing N N 137 
GLN   N   H    sing N N 138 
GLN   N   H2   sing N N 139 
GLN   CA  C    sing N N 140 
GLN   CA  CB   sing N N 141 
GLN   CA  HA   sing N N 142 
GLN   C   O    doub N N 143 
GLN   C   OXT  sing N N 144 
GLN   CB  CG   sing N N 145 
GLN   CB  HB2  sing N N 146 
GLN   CB  HB3  sing N N 147 
GLN   CG  CD   sing N N 148 
GLN   CG  HG2  sing N N 149 
GLN   CG  HG3  sing N N 150 
GLN   CD  OE1  doub N N 151 
GLN   CD  NE2  sing N N 152 
GLN   NE2 HE21 sing N N 153 
GLN   NE2 HE22 sing N N 154 
GLN   OXT HXT  sing N N 155 
GLU   N   CA   sing N N 156 
GLU   N   H    sing N N 157 
GLU   N   H2   sing N N 158 
GLU   CA  C    sing N N 159 
GLU   CA  CB   sing N N 160 
GLU   CA  HA   sing N N 161 
GLU   C   O    doub N N 162 
GLU   C   OXT  sing N N 163 
GLU   CB  CG   sing N N 164 
GLU   CB  HB2  sing N N 165 
GLU   CB  HB3  sing N N 166 
GLU   CG  CD   sing N N 167 
GLU   CG  HG2  sing N N 168 
GLU   CG  HG3  sing N N 169 
GLU   CD  OE1  doub N N 170 
GLU   CD  OE2  sing N N 171 
GLU   OE2 HE2  sing N N 172 
GLU   OXT HXT  sing N N 173 
GLY   N   CA   sing N N 174 
GLY   N   H    sing N N 175 
GLY   N   H2   sing N N 176 
GLY   CA  C    sing N N 177 
GLY   CA  HA2  sing N N 178 
GLY   CA  HA3  sing N N 179 
GLY   C   O    doub N N 180 
GLY   C   OXT  sing N N 181 
GLY   OXT HXT  sing N N 182 
HIS   N   CA   sing N N 183 
HIS   N   H    sing N N 184 
HIS   N   H2   sing N N 185 
HIS   CA  C    sing N N 186 
HIS   CA  CB   sing N N 187 
HIS   CA  HA   sing N N 188 
HIS   C   O    doub N N 189 
HIS   C   OXT  sing N N 190 
HIS   CB  CG   sing N N 191 
HIS   CB  HB2  sing N N 192 
HIS   CB  HB3  sing N N 193 
HIS   CG  ND1  sing Y N 194 
HIS   CG  CD2  doub Y N 195 
HIS   ND1 CE1  doub Y N 196 
HIS   ND1 HD1  sing N N 197 
HIS   CD2 NE2  sing Y N 198 
HIS   CD2 HD2  sing N N 199 
HIS   CE1 NE2  sing Y N 200 
HIS   CE1 HE1  sing N N 201 
HIS   NE2 HE2  sing N N 202 
HIS   OXT HXT  sing N N 203 
HOH   O   H1   sing N N 204 
HOH   O   H2   sing N N 205 
ILE   N   CA   sing N N 206 
ILE   N   H    sing N N 207 
ILE   N   H2   sing N N 208 
ILE   CA  C    sing N N 209 
ILE   CA  CB   sing N N 210 
ILE   CA  HA   sing N N 211 
ILE   C   O    doub N N 212 
ILE   C   OXT  sing N N 213 
ILE   CB  CG1  sing N N 214 
ILE   CB  CG2  sing N N 215 
ILE   CB  HB   sing N N 216 
ILE   CG1 CD1  sing N N 217 
ILE   CG1 HG12 sing N N 218 
ILE   CG1 HG13 sing N N 219 
ILE   CG2 HG21 sing N N 220 
ILE   CG2 HG22 sing N N 221 
ILE   CG2 HG23 sing N N 222 
ILE   CD1 HD11 sing N N 223 
ILE   CD1 HD12 sing N N 224 
ILE   CD1 HD13 sing N N 225 
ILE   OXT HXT  sing N N 226 
LEU   N   CA   sing N N 227 
LEU   N   H    sing N N 228 
LEU   N   H2   sing N N 229 
LEU   CA  C    sing N N 230 
LEU   CA  CB   sing N N 231 
LEU   CA  HA   sing N N 232 
LEU   C   O    doub N N 233 
LEU   C   OXT  sing N N 234 
LEU   CB  CG   sing N N 235 
LEU   CB  HB2  sing N N 236 
LEU   CB  HB3  sing N N 237 
LEU   CG  CD1  sing N N 238 
LEU   CG  CD2  sing N N 239 
LEU   CG  HG   sing N N 240 
LEU   CD1 HD11 sing N N 241 
LEU   CD1 HD12 sing N N 242 
LEU   CD1 HD13 sing N N 243 
LEU   CD2 HD21 sing N N 244 
LEU   CD2 HD22 sing N N 245 
LEU   CD2 HD23 sing N N 246 
LEU   OXT HXT  sing N N 247 
LYS   N   CA   sing N N 248 
LYS   N   H    sing N N 249 
LYS   N   H2   sing N N 250 
LYS   CA  C    sing N N 251 
LYS   CA  CB   sing N N 252 
LYS   CA  HA   sing N N 253 
LYS   C   O    doub N N 254 
LYS   C   OXT  sing N N 255 
LYS   CB  CG   sing N N 256 
LYS   CB  HB2  sing N N 257 
LYS   CB  HB3  sing N N 258 
LYS   CG  CD   sing N N 259 
LYS   CG  HG2  sing N N 260 
LYS   CG  HG3  sing N N 261 
LYS   CD  CE   sing N N 262 
LYS   CD  HD2  sing N N 263 
LYS   CD  HD3  sing N N 264 
LYS   CE  NZ   sing N N 265 
LYS   CE  HE2  sing N N 266 
LYS   CE  HE3  sing N N 267 
LYS   NZ  HZ1  sing N N 268 
LYS   NZ  HZ2  sing N N 269 
LYS   NZ  HZ3  sing N N 270 
LYS   OXT HXT  sing N N 271 
MET   N   CA   sing N N 272 
MET   N   H    sing N N 273 
MET   N   H2   sing N N 274 
MET   CA  C    sing N N 275 
MET   CA  CB   sing N N 276 
MET   CA  HA   sing N N 277 
MET   C   O    doub N N 278 
MET   C   OXT  sing N N 279 
MET   CB  CG   sing N N 280 
MET   CB  HB2  sing N N 281 
MET   CB  HB3  sing N N 282 
MET   CG  SD   sing N N 283 
MET   CG  HG2  sing N N 284 
MET   CG  HG3  sing N N 285 
MET   SD  CE   sing N N 286 
MET   CE  HE1  sing N N 287 
MET   CE  HE2  sing N N 288 
MET   CE  HE3  sing N N 289 
MET   OXT HXT  sing N N 290 
PHE   N   CA   sing N N 291 
PHE   N   H    sing N N 292 
PHE   N   H2   sing N N 293 
PHE   CA  C    sing N N 294 
PHE   CA  CB   sing N N 295 
PHE   CA  HA   sing N N 296 
PHE   C   O    doub N N 297 
PHE   C   OXT  sing N N 298 
PHE   CB  CG   sing N N 299 
PHE   CB  HB2  sing N N 300 
PHE   CB  HB3  sing N N 301 
PHE   CG  CD1  doub Y N 302 
PHE   CG  CD2  sing Y N 303 
PHE   CD1 CE1  sing Y N 304 
PHE   CD1 HD1  sing N N 305 
PHE   CD2 CE2  doub Y N 306 
PHE   CD2 HD2  sing N N 307 
PHE   CE1 CZ   doub Y N 308 
PHE   CE1 HE1  sing N N 309 
PHE   CE2 CZ   sing Y N 310 
PHE   CE2 HE2  sing N N 311 
PHE   CZ  HZ   sing N N 312 
PHE   OXT HXT  sing N N 313 
PRO   N   CA   sing N N 314 
PRO   N   CD   sing N N 315 
PRO   N   H    sing N N 316 
PRO   CA  C    sing N N 317 
PRO   CA  CB   sing N N 318 
PRO   CA  HA   sing N N 319 
PRO   C   O    doub N N 320 
PRO   C   OXT  sing N N 321 
PRO   CB  CG   sing N N 322 
PRO   CB  HB2  sing N N 323 
PRO   CB  HB3  sing N N 324 
PRO   CG  CD   sing N N 325 
PRO   CG  HG2  sing N N 326 
PRO   CG  HG3  sing N N 327 
PRO   CD  HD2  sing N N 328 
PRO   CD  HD3  sing N N 329 
PRO   OXT HXT  sing N N 330 
SER   N   CA   sing N N 331 
SER   N   H    sing N N 332 
SER   N   H2   sing N N 333 
SER   CA  C    sing N N 334 
SER   CA  CB   sing N N 335 
SER   CA  HA   sing N N 336 
SER   C   O    doub N N 337 
SER   C   OXT  sing N N 338 
SER   CB  OG   sing N N 339 
SER   CB  HB2  sing N N 340 
SER   CB  HB3  sing N N 341 
SER   OG  HG   sing N N 342 
SER   OXT HXT  sing N N 343 
THR   N   CA   sing N N 344 
THR   N   H    sing N N 345 
THR   N   H2   sing N N 346 
THR   CA  C    sing N N 347 
THR   CA  CB   sing N N 348 
THR   CA  HA   sing N N 349 
THR   C   O    doub N N 350 
THR   C   OXT  sing N N 351 
THR   CB  OG1  sing N N 352 
THR   CB  CG2  sing N N 353 
THR   CB  HB   sing N N 354 
THR   OG1 HG1  sing N N 355 
THR   CG2 HG21 sing N N 356 
THR   CG2 HG22 sing N N 357 
THR   CG2 HG23 sing N N 358 
THR   OXT HXT  sing N N 359 
TRP   N   CA   sing N N 360 
TRP   N   H    sing N N 361 
TRP   N   H2   sing N N 362 
TRP   CA  C    sing N N 363 
TRP   CA  CB   sing N N 364 
TRP   CA  HA   sing N N 365 
TRP   C   O    doub N N 366 
TRP   C   OXT  sing N N 367 
TRP   CB  CG   sing N N 368 
TRP   CB  HB2  sing N N 369 
TRP   CB  HB3  sing N N 370 
TRP   CG  CD1  doub Y N 371 
TRP   CG  CD2  sing Y N 372 
TRP   CD1 NE1  sing Y N 373 
TRP   CD1 HD1  sing N N 374 
TRP   CD2 CE2  doub Y N 375 
TRP   CD2 CE3  sing Y N 376 
TRP   NE1 CE2  sing Y N 377 
TRP   NE1 HE1  sing N N 378 
TRP   CE2 CZ2  sing Y N 379 
TRP   CE3 CZ3  doub Y N 380 
TRP   CE3 HE3  sing N N 381 
TRP   CZ2 CH2  doub Y N 382 
TRP   CZ2 HZ2  sing N N 383 
TRP   CZ3 CH2  sing Y N 384 
TRP   CZ3 HZ3  sing N N 385 
TRP   CH2 HH2  sing N N 386 
TRP   OXT HXT  sing N N 387 
TYR   N   CA   sing N N 388 
TYR   N   H    sing N N 389 
TYR   N   H2   sing N N 390 
TYR   CA  C    sing N N 391 
TYR   CA  CB   sing N N 392 
TYR   CA  HA   sing N N 393 
TYR   C   O    doub N N 394 
TYR   C   OXT  sing N N 395 
TYR   CB  CG   sing N N 396 
TYR   CB  HB2  sing N N 397 
TYR   CB  HB3  sing N N 398 
TYR   CG  CD1  doub Y N 399 
TYR   CG  CD2  sing Y N 400 
TYR   CD1 CE1  sing Y N 401 
TYR   CD1 HD1  sing N N 402 
TYR   CD2 CE2  doub Y N 403 
TYR   CD2 HD2  sing N N 404 
TYR   CE1 CZ   doub Y N 405 
TYR   CE1 HE1  sing N N 406 
TYR   CE2 CZ   sing Y N 407 
TYR   CE2 HE2  sing N N 408 
TYR   CZ  OH   sing N N 409 
TYR   OH  HH   sing N N 410 
TYR   OXT HXT  sing N N 411 
VAL   N   CA   sing N N 412 
VAL   N   H    sing N N 413 
VAL   N   H2   sing N N 414 
VAL   CA  C    sing N N 415 
VAL   CA  CB   sing N N 416 
VAL   CA  HA   sing N N 417 
VAL   C   O    doub N N 418 
VAL   C   OXT  sing N N 419 
VAL   CB  CG1  sing N N 420 
VAL   CB  CG2  sing N N 421 
VAL   CB  HB   sing N N 422 
VAL   CG1 HG11 sing N N 423 
VAL   CG1 HG12 sing N N 424 
VAL   CG1 HG13 sing N N 425 
VAL   CG2 HG21 sing N N 426 
VAL   CG2 HG22 sing N N 427 
VAL   CG2 HG23 sing N N 428 
VAL   OXT HXT  sing N N 429 
# 
_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                    7I3O 
_atom_sites.fract_transf_matrix[1][1]   0.013726 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000758 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016114 
_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]   0.030586 
_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  
CL 
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   ? 18.853 6.481   24.306 1.00 39.20 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 20.116 6.406   23.566 1.00 39.31 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 20.131 5.232   22.570 1.00 37.72 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 19.398 4.254   22.764 1.00 37.73 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 21.280 6.271   24.544 1.00 41.54 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 21.204 5.013   25.197 1.00 44.43 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 20.971 5.332   21.532 1.00 35.64 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 21.099 4.295   20.504 1.00 33.96 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 21.397 4.838   19.115 1.00 31.50 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 21.015 5.967   18.799 1.00 31.51 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 22.107 4.065   18.281 1.00 28.93 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 22.495 4.519   16.941 1.00 28.15 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 22.561 3.379   15.913 1.00 28.25 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 22.685 2.208   16.308 1.00 27.52 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.857 5.197   17.024 1.00 28.08 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 22.537 3.713   14.593 1.00 27.97 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.685 2.701   13.532 1.00 28.04 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 24.072 2.880   12.879 1.00 29.82 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.442 3.972   12.418 1.00 29.15 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.576 2.802   12.451 1.00 27.21 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 20.167 2.720   13.049 1.00 25.62 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.778 1.738   11.364 1.00 27.73 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.210 3.391   12.224 1.00 25.32 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.829 1.804   12.834 1.00 31.57 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 26.161 1.816   12.264 1.00 33.69 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 26.168 1.041   10.968 1.00 35.19 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 26.112 -0.183  11.001 1.00 35.69 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.136 1.206   13.273 1.00 34.07 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.286 2.074   14.499 1.00 34.62 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 28.068 3.220   14.471 1.00 35.88 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 26.611 1.774   15.674 1.00 35.23 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 28.196 4.036   15.589 1.00 36.55 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 26.740 2.574   16.802 1.00 36.32 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 27.552 3.693   16.762 1.00 37.29 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 27.674 4.494   17.865 1.00 38.99 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 26.144 1.744   9.832  1.00 35.56 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 26.159 1.133   8.501  1.00 35.88 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.308 1.719   7.688  1.00 36.01 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.362 2.933   7.456  1.00 35.98 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.805 1.248   7.759  1.00 36.85 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.239 2.666   7.817  1.00 36.99 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.933 0.769   6.324  1.00 38.06 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.274 0.863   7.312  1.00 35.72 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.451 1.285   6.571  1.00 37.38 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.211 2.379   7.303  1.00 39.22 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.354 2.305   8.529  1.00 40.89 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.596 3.443   6.598  1.00 38.77 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.285 4.561   7.238  1.00 38.59 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.276 5.594   7.821  1.00 36.54 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.619 6.784   7.925  1.00 36.67 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.250 5.248   6.246  1.00 42.10 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.385 4.356   5.762  1.00 49.71 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 33.604 3.262   6.267  1.00 52.53 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 34.143 4.816   4.770  1.00 53.42 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.079 5.146   8.262  1.00 34.10 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.095 6.094   8.810  1.00 31.99 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.562 5.726   10.175 1.00 29.31 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.405 4.551   10.502 1.00 28.49 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.891 6.290   7.849  1.00 31.19 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.255 6.853   6.495  1.00 31.72 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 27.899 8.077   6.380  1.00 32.68 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 26.922 6.180   5.330  1.00 32.24 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.265 8.584   5.139  1.00 34.09 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.253 6.690   4.084  1.00 33.40 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 27.964 7.872   3.991  1.00 34.78 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.286 8.395   2.764  1.00 36.33 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.156 6.753   10.925 1.00 26.58 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.472 6.569   12.192 1.00 24.55 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.173 7.402   12.099 1.00 22.22 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.247 8.589   11.782 1.00 21.42 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.367 7.028   13.354 1.00 25.87 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.654 7.202   14.694 1.00 30.21 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.662 7.627   15.754 1.00 34.45 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 27.161 8.686   16.641 1.00 37.03 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 26.701 8.472   17.872 1.00 38.88 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 26.643 7.237   18.362 1.00 37.90 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 26.281 9.488   18.616 1.00 37.82 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 24.002 6.783   12.327 1.00 21.19 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.683 7.430   12.298 1.00 20.91 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.158 7.570   13.709 1.00 20.37 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 21.976 6.574   14.372 1.00 21.21 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.663 6.680   11.407 1.00 21.01 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.390 7.505   11.224 1.00 20.70 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.286 6.297   10.057 1.00 20.94 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 21.880 8.792   14.173 1.00 19.04 ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 21.391 9.016   15.537 1.00 19.04 ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 20.187 9.977   15.502 1.00 19.21 ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 19.989 10.661  14.496 1.00 19.27 ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 22.501 9.662   16.425 1.00 20.20 ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 23.528 8.647   16.843 1.00 20.93 ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 23.142 10.873  15.737 1.00 20.43 ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 19.445 10.111  16.633 1.00 18.75 ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 18.388 11.123  16.743 1.00 19.22 ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 19.127 12.466  16.740 1.00 20.30 ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 20.139 12.603  17.446 1.00 20.75 ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.631 10.986  18.083 1.00 19.55 ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 16.819 9.714   18.207 1.00 20.84 ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.313 8.687   18.690 1.00 21.41 ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 15.568 9.761   17.766 1.00 19.81 ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 18.697 13.408  15.908 1.00 20.57 ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 19.357 14.713  15.812 1.00 20.73 ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 19.400 15.433  17.171 1.00 23.24 ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 20.442 15.988  17.523 1.00 24.06 ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 18.708 15.583  14.720 1.00 19.44 ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.460 16.870  14.357 1.00 19.40 ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 18.524 17.807  13.610 1.00 22.29 ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.133 19.050  13.093 1.00 24.48 ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.199 20.190  13.773 1.00 26.19 ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 18.802 20.240  15.042 1.00 26.53 ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 19.696 21.280  13.204 1.00 25.72 ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 18.316 15.349  17.967 1.00 24.08 ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 18.286 15.980  19.301 1.00 25.14 ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 19.285 15.371  20.300 1.00 26.57 ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 19.591 15.991  21.323 1.00 26.61 ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 16.863 16.031  19.885 1.00 25.54 ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 16.354 14.739  20.421 1.00 28.08 ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 15.788 13.790  19.585 1.00 28.95 ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 16.320 14.281  21.700 1.00 29.01 ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 15.455 12.770  20.370 1.00 30.21 ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 15.737 13.023  21.654 1.00 30.05 ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 19.830 14.186  19.992 1.00 27.85 ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 20.794 13.533  20.872 1.00 29.17 ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 22.239 13.503  20.321 1.00 30.92 ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 23.112 12.884  20.938 1.00 31.79 ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 20.309 12.104  21.165 1.00 28.96 ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 19.104 11.975  22.109 1.00 29.86 ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 18.686 10.483  22.291 1.00 29.28 ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 19.427 12.547  23.469 1.00 29.84 ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 22.485 14.123  19.157 1.00 31.39 ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 23.798 14.127  18.525 1.00 32.66 ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 24.876 14.780  19.390 1.00 33.79 ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 24.607 15.762  20.080 1.00 33.32 ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 23.727 14.807  17.156 1.00 32.99 ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 26.091 14.220  19.350 1.00 34.93 ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 27.251 14.686  20.119 1.00 36.98 ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 28.027 15.837  19.384 1.00 39.10 ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 27.674 16.217  18.265 1.00 39.12 ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 28.188 13.477  20.371 1.00 38.72 ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 28.814 13.154  19.133 1.00 40.27 ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 27.479 12.265  20.949 1.00 39.10 ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 29.094 16.373  20.012 1.00 40.83 ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 29.934 17.373  19.369 1.00 42.53 ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 30.699 16.707  18.214 1.00 42.26 ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 30.916 17.350  17.184 1.00 42.13 ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 30.941 17.951  20.369 1.00 45.57 ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 30.343 18.796  21.450 1.00 50.34 ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 29.811 20.036  21.178 1.00 52.99 ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 30.314 18.590  22.791 1.00 52.34 ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 29.439 20.534  22.348 1.00 53.75 ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 29.721 19.699  23.349 1.00 53.54 ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 31.128 15.435  18.398 1.00 42.07 ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 31.835 14.661  17.380 1.00 42.64 ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 30.956 14.438  16.172 1.00 40.34 ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 31.386 14.714  15.052 1.00 41.01 ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 32.317 13.321  17.915 1.00 45.78 ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 33.304 12.689  16.973 1.00 53.15 ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.319 13.303  16.613 1.00 55.08 ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 33.035 11.446  16.550 1.00 55.39 ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 29.688 14.040  16.388 1.00 37.61 ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 28.697 13.903  15.315 1.00 35.03 ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 28.613 15.193  14.475 1.00 33.92 ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 28.775 15.137  13.268 1.00 34.08 ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 27.320 13.556  15.907 1.00 33.27 ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 27.252 12.120  16.381 1.00 32.46 ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 27.895 11.277  15.770 1.00 30.43 ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 26.575 11.859  17.389 1.00 34.21 ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 28.478 16.351  15.125 1.00 32.82 ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.412 17.634  14.409 1.00 32.61 ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 29.742 18.008  13.715 1.00 34.20 ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 29.721 18.641  12.665 1.00 34.81 ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 27.955 18.763  15.360 1.00 31.20 ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 26.466 18.815  15.560 1.00 29.40 ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 25.770 18.393  16.655 1.00 29.93 ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 25.495 19.319  14.637 1.00 28.25 ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 24.419 18.579  16.457 1.00 30.02 ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 24.224 19.153  15.228 1.00 29.01 ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 25.569 19.868  13.356 1.00 28.39 ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 23.046 19.573  14.602 1.00 28.65 ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.404 20.300  12.749 1.00 28.49 ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 23.161 20.137  13.364 1.00 28.18 ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 30.887 17.631  14.301 1.00 34.93 ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.207 17.913  13.709 1.00 36.64 ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.486 17.028  12.474 1.00 37.96 ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.338 17.379  11.650 1.00 39.62 ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 33.316 17.713  14.743 1.00 35.89 ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 31.810 15.864  12.385 1.00 36.17 ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 31.899 14.939  11.267 1.00 35.51 ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.531 14.783  10.569 1.00 33.08 ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.219 13.706  10.085 1.00 33.05 ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.376 13.584  11.779 1.00 37.81 ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 33.806 13.624  12.281 1.00 42.96 ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 34.725 14.007  11.558 1.00 45.37 ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 34.016 13.213  13.520 1.00 42.59 ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 29.692 15.832  10.592 1.00 31.34 ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.362 15.860  10.006 1.00 28.73 ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.386 15.506  8.518  1.00 27.80 ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.171 16.086  7.775  1.00 28.24 ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 27.784 17.275  10.189 1.00 27.60 ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.448 17.613  9.471  1.00 27.87 ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.293 16.779  10.032 1.00 28.39 ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.131 19.110  9.544  1.00 26.56 ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.491 14.583  8.083  1.00 26.02 ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.278 14.197  6.685  1.00 24.64 ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 25.948 14.870  6.206  1.00 23.68 ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 25.939 15.606  5.222  1.00 24.38 ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.202 12.655  6.579  1.00 25.51 ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 26.581 12.219  5.255  1.00 26.52 ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 28.576 12.018  6.797  1.00 25.52 ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 24.855 14.681  6.969  1.00 21.73 ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 23.522 15.212  6.674  1.00 20.67 ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 22.680 15.213  7.967  1.00 19.39 ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 22.874 14.379  8.835  1.00 20.03 ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 22.858 14.327  5.591  1.00 20.78 ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.369 14.463  5.409  1.00 20.98 ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 20.712 15.360  4.619  1.00 22.44 ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.352 13.665  6.039  1.00 20.57 ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.351 15.154  4.698  1.00 22.45 ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.103 14.129  5.572  1.00 21.33 ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.375 12.651  6.994  1.00 19.78 ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 17.893 13.547  5.966  1.00 20.82 ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.180 12.060  7.363  1.00 20.11 ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 17.957 12.522  6.867  1.00 20.02 ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 21.776 16.164  8.088  1.00 17.70 ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 20.858 16.282  9.213  1.00 16.68 ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 19.566 16.929  8.714  1.00 16.02 ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 19.590 17.685  7.734  1.00 14.18 ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 21.492 17.055  10.392 1.00 17.04 ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.049 18.411  10.003 1.00 18.91 ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.090 19.576  9.830  1.00 24.02 ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 21.424 20.486  9.036  1.00 25.38 ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 20.009 19.584  10.464 1.00 23.25 ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 18.438 16.595  9.363  1.00 16.03 ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.130 17.136  9.011  1.00 17.40 ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.317 17.243  10.316 1.00 17.60 ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 15.905 16.227  10.861 1.00 17.52 ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.450 16.239  7.974  1.00 19.66 ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.159 16.782  7.398  1.00 25.45 ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 14.504 17.607  8.070  1.00 25.25 ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 14.786 16.360  6.290  1.00 28.98 ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.082 18.485  10.796 1.00 16.96 ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 15.322 18.707  12.020 0.50 17.11 ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 15.333 18.687  12.024 0.50 17.14 ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 13.906 18.173  11.884 1.00 17.19 ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 13.357 17.701  12.865 1.00 17.98 ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 15.260 20.193  12.374 0.50 18.54 ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 15.321 20.161  12.417 0.50 18.70 ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 16.515 20.836  12.244 0.50 20.75 ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 14.623 20.904  11.433 0.50 21.09 ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 13.299 18.289  10.667 1.00 16.54 ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 11.925 17.818  10.455 1.00 17.81 ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 11.809 16.300  10.634 1.00 17.17 ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 10.733 15.841  10.948 1.00 18.82 ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 11.346 18.269  9.112  1.00 21.35 ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 11.779 17.454  8.032  1.00 25.26 ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 12.877 15.556  10.445 1.00 15.33 ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 12.889 14.078  10.619 1.00 14.93 ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 13.481 13.611  11.950 1.00 14.63 ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 13.381 12.417  12.287 1.00 14.03 ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 13.680 13.414  9.479  1.00 14.41 ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 13.061 13.652  8.121  1.00 14.58 ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 13.846 12.999  7.009  1.00 15.71 ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 13.835 11.543  7.141  1.00 15.09 ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 13.928 10.696  6.125  1.00 16.98 ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 14.051 11.149  4.879  1.00 12.99 ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 13.897 9.382   6.342  1.00 18.24 ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 14.147 14.535  12.682 1.00 15.00 ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 14.850 14.274  13.930 1.00 15.17 ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 16.000 13.304  13.641 1.00 16.06 ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 16.198 12.380  14.421 1.00 15.78 ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 13.905 13.743  15.053 1.00 16.19 ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 14.604 13.489  16.392 1.00 18.88 ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 15.464 14.290  16.761 1.00 17.89 ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 14.339 12.414  17.025 1.00 21.86 ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 16.724 13.472  12.485 1.00 15.38 ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 17.854 12.574  12.150 1.00 15.09 ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 19.154 13.330  11.913 1.00 16.44 ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 19.165 14.470  11.449 1.00 17.39 ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.588 11.720  10.871 1.00 14.65 ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 16.465 10.670  10.911 1.00 15.14 ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 16.369 9.937   9.549  1.00 13.68 ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 16.671 9.697   12.047 1.00 15.85 ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 20.264 12.675  12.202 1.00 16.56 ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 21.575 13.206  11.899 1.00 18.22 ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 22.450 12.007  11.602 1.00 19.47 ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 22.348 10.987  12.280 1.00 19.57 ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 22.144 14.085  13.058 1.00 18.40 ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 23.502 14.748  12.802 1.00 20.27 ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 23.577 16.080  13.486 1.00 21.37 ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 24.661 13.861  13.250 1.00 21.58 ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 23.236 12.105  10.522 1.00 20.37 ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 24.196 11.094  10.100 1.00 22.13 ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 25.597 11.708  10.159 1.00 23.76 ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 25.818 12.800  9.628  1.00 23.68 ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 23.909 10.518  8.699  1.00 23.19 ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 24.974 9.481   8.319  1.00 25.00 ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 22.503 9.899   8.650  1.00 23.52 ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 26.528 11.010  10.803 1.00 25.56 ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 27.914 11.431  10.859 1.00 27.80 ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 28.843 10.337  10.325 1.00 31.15 ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 28.468 9.156   10.264 1.00 29.30 ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 28.299 11.857  12.266 1.00 29.59 ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 27.897 10.901  13.228 1.00 32.48 ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 30.054 10.740  9.925  1.00 34.36 ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 31.047 9.827   9.375  1.00 38.93 ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 31.810 9.094   10.473 1.00 43.26 ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 31.961 9.601   11.585 1.00 43.83 ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 32.027 10.583  8.479  1.00 41.01 ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 32.375 11.833  9.052  1.00 43.51 ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 32.261 7.884   10.175 1.00 46.49 ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 33.001 7.072   11.143 1.00 50.62 ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 34.251 6.505   10.496 1.00 55.82 ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 34.262 6.281   9.287  1.00 57.30 ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 32.141 5.908   11.670 1.00 51.16 ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 32.055 4.870   10.689 1.00 51.82 ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 30.757 6.338   12.114 1.00 51.06 ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? 35.265 6.185   11.298 1.00 58.49 ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? 36.485 5.570   10.782 1.00 61.25 ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? 36.352 4.036   10.766 1.00 62.93 ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? 36.970 3.363   9.936  1.00 64.47 ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? 37.677 6.015   11.630 1.00 63.65 ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? 37.467 5.525   12.952 1.00 65.84 ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? 37.809 7.512   11.685 1.00 63.98 ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? 35.584 3.478   11.711 1.00 62.13 ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? 35.370 2.053   11.779 1.00 61.68 ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 34.218 1.664   10.855 1.00 61.35 ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 33.355 2.497   10.527 1.00 61.44 ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? 35.066 1.648   13.210 1.00 61.84 ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 34.203 0.400   10.430 1.00 60.96 ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 33.165 -0.107  9.543  1.00 60.99 ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 31.963 -0.627  10.309 1.00 59.95 ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 32.113 -1.409  11.249 1.00 60.24 ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 33.713 -1.201  8.610  1.00 63.23 ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 33.114 -1.169  7.206  1.00 68.17 ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 33.510 0.084   6.446  1.00 74.76 ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 34.587 0.669   6.655  1.00 77.96 ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 32.653 0.537   5.535  1.00 74.98 ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 30.782 -0.186  9.886  1.00 57.96 ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 29.510 -0.616  10.444 1.00 56.99 ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 28.962 -1.788  9.653  1.00 55.39 ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 29.174 -1.880  8.439  1.00 55.40 ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 28.247 -2.676  10.316 1.00 53.93 ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 27.720 -3.870  9.654  1.00 52.64 ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 26.186 -4.013  9.745  1.00 49.65 ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 25.643 -5.045  9.324  1.00 50.19 ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 28.441 -5.109  10.167 1.00 55.52 ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 30.163 -5.234  9.618  1.00 66.06 ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 25.483 -2.964  10.229 1.00 45.99 ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 24.027 -3.006  10.285 1.00 43.58 ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 23.501 -2.942  8.857  1.00 41.20 ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 23.952 -2.130  8.054  1.00 42.26 ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 23.440 -1.838  11.121 1.00 44.02 ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 23.543 -2.003  12.624 1.00 47.15 ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 23.459 -3.152  13.099 1.00 49.61 ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 23.687 -0.976  13.331 1.00 46.73 ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 22.573 -3.804  8.550  1.00 38.74 ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 21.924 -3.912  7.255  1.00 37.37 ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 20.664 -3.048  7.278  1.00 34.52 ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 19.898 -3.143  8.233  1.00 34.05 ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 21.597 -5.408  7.020  1.00 39.86 ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 22.796 -6.054  6.569  1.00 42.89 ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 20.479 -5.632  6.004  1.00 39.49 ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 20.458 -2.200  6.266  1.00 32.27 ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 19.241 -1.395  6.209  1.00 30.57 ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 18.247 -2.111  5.310  1.00 29.78 ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 18.615 -2.596  4.221  1.00 29.70 ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 19.509 0.040   5.709  1.00 29.82 ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 20.678 0.693   6.465  1.00 29.58 ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 18.223 0.893   5.741  1.00 30.29 ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 20.456 0.924   7.958  1.00 29.98 ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 16.994 -2.198  5.782  1.00 28.42 ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 15.878 -2.782  5.047  1.00 27.63 ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 15.461 -1.811  3.931  1.00 28.16 ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 15.377 -0.603  4.139  1.00 28.54 ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 14.694 -2.999  5.991  1.00 26.18 ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 15.173 -2.349  2.771  1.00 28.33 ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 14.658 -1.621  1.624  1.00 28.57 ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 13.354 -2.366  1.296  1.00 29.97 ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 13.380 -3.369  0.583  1.00 32.05 ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 15.667 -1.725  0.481  1.00 29.11 ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 17.043 -1.166  0.835  1.00 30.38 ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 17.006 0.305   1.244  1.00 29.85 ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 18.349 0.786   1.558  1.00 29.80 ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 18.616 1.915   2.211  1.00 29.21 ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 17.632 2.703   2.618  1.00 27.92 ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 19.871 2.263   2.458  1.00 29.10 ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 12.238 -1.931  1.894  1.00 29.25 ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 10.958 -2.632  1.817  1.00 29.41 ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 9.804  -1.673  2.198  1.00 30.45 ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 10.040 -0.534  2.580  1.00 30.85 ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 11.005 -3.791  2.814  1.00 29.44 ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 10.993 -3.234  4.556  1.00 30.01 ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 8.565  -2.204  2.240  1.00 31.03 ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 7.392  -1.485  2.716  1.00 31.68 ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 6.737  -2.290  3.868  1.00 31.00 ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 5.517  -2.378  3.942  1.00 32.06 ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 6.399  -1.163  1.564  1.00 33.84 ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 5.455  -2.261  1.114  1.00 41.49 ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 5.718  -3.448  1.433  1.00 42.41 ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 4.433  -1.936  0.456  1.00 46.21 ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 7.547  -2.917  4.741  1.00 29.64 ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 7.022  -3.703  5.877  1.00 27.48 ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 6.244  -2.816  6.841  1.00 25.27 ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 6.578  -1.658  7.039  1.00 26.20 ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 8.141  -4.446  6.615  1.00 27.03 ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 8.696  -5.980  5.820  1.00 28.62 ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 5.201  -3.344  7.392  1.00 23.02 ? 59  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 53  ? 4.428  -2.688  8.427  1.00 22.67 ? 59  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 53  ? 4.411  -3.507  9.730  1.00 21.47 ? 59  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 53  ? 3.569  -3.268  10.577 1.00 21.25 ? 59  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 53  ? 3.018  -2.311  7.959  1.00 24.20 ? 59  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 53  ? 2.952  -0.982  7.197  1.00 25.56 ? 59  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 53  ? 1.512  -0.594  6.917  1.00 28.77 ? 59  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 53  ? 1.034  -0.675  5.786  1.00 32.26 ? 59  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 53  ? 0.772  -0.198  7.952  1.00 26.87 ? 59  GLN   A NE2 1 
ATOM   415  N  N   . THR   A 1 54  ? 5.311  -4.520  9.865  1.00 20.61 ? 60  THR   A N   1 
ATOM   416  C  CA  . THR   A 1 54  ? 5.486  -5.345  11.061 1.00 19.61 ? 60  THR   A CA  1 
ATOM   417  C  C   . THR   A 1 54  ? 6.979  -5.486  11.312 1.00 17.05 ? 60  THR   A C   1 
ATOM   418  O  O   . THR   A 1 54  ? 7.791  -5.575  10.369 1.00 16.40 ? 60  THR   A O   1 
ATOM   419  C  CB  . THR   A 1 54  ? 4.771  -6.724  10.980 1.00 22.80 ? 60  THR   A CB  1 
ATOM   420  O  OG1 . THR   A 1 54  ? 5.537  -7.631  10.183 1.00 24.60 ? 60  THR   A OG1 1 
ATOM   421  C  CG2 . THR   A 1 54  ? 3.369  -6.632  10.426 1.00 23.35 ? 60  THR   A CG2 1 
ATOM   422  N  N   . GLY   A 1 55  ? 7.326  -5.520  12.582 1.00 15.46 ? 61  GLY   A N   1 
ATOM   423  C  CA  . GLY   A 1 55  ? 8.722  -5.584  12.990 1.00 15.31 ? 61  GLY   A CA  1 
ATOM   424  C  C   . GLY   A 1 55  ? 8.867  -5.790  14.487 1.00 14.88 ? 61  GLY   A C   1 
ATOM   425  O  O   . GLY   A 1 55  ? 7.889  -6.083  15.166 1.00 14.99 ? 61  GLY   A O   1 
ATOM   426  N  N   . VAL   A 1 56  ? 10.095 -5.635  15.013 1.00 14.07 ? 62  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 56  ? 10.429 -5.822  16.418 1.00 14.41 ? 62  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 56  ? 11.321 -4.625  16.831 1.00 15.03 ? 62  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 56  ? 12.251 -4.294  16.108 1.00 15.23 ? 62  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 56  ? 11.171 -7.170  16.632 1.00 15.29 ? 62  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 56  ? 11.623 -7.330  18.086 1.00 16.12 ? 62  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 56  ? 10.291 -8.353  16.225 1.00 16.73 ? 62  VAL   A CG2 1 
ATOM   433  N  N   . TYR   A 1 57  ? 10.994 -3.935  17.935 1.00 15.82 ? 63  TYR   A N   1 
ATOM   434  C  CA  . TYR   A 1 57  ? 11.814 -2.821  18.394 1.00 16.22 ? 63  TYR   A CA  1 
ATOM   435  C  C   . TYR   A 1 57  ? 12.406 -3.064  19.793 1.00 18.12 ? 63  TYR   A C   1 
ATOM   436  O  O   . TYR   A 1 57  ? 11.814 -3.784  20.593 1.00 18.56 ? 63  TYR   A O   1 
ATOM   437  C  CB  . TYR   A 1 57  ? 11.045 -1.476  18.342 1.00 16.15 ? 63  TYR   A CB  1 
ATOM   438  C  CG  . TYR   A 1 57  ? 10.075 -1.262  19.493 1.00 17.15 ? 63  TYR   A CG  1 
ATOM   439  C  CD1 . TYR   A 1 57  ? 8.824  -1.871  19.501 1.00 17.67 ? 63  TYR   A CD1 1 
ATOM   440  C  CD2 . TYR   A 1 57  ? 10.388 -0.406  20.545 1.00 18.75 ? 63  TYR   A CD2 1 
ATOM   441  C  CE1 . TYR   A 1 57  ? 7.902  -1.616  20.515 1.00 19.66 ? 63  TYR   A CE1 1 
ATOM   442  C  CE2 . TYR   A 1 57  ? 9.485  -0.171  21.580 1.00 20.36 ? 63  TYR   A CE2 1 
ATOM   443  C  CZ  . TYR   A 1 57  ? 8.249  -0.798  21.574 1.00 20.90 ? 63  TYR   A CZ  1 
ATOM   444  O  OH  . TYR   A 1 57  ? 7.346  -0.571  22.593 1.00 21.93 ? 63  TYR   A OH  1 
ATOM   445  N  N   . TYR   A 1 58  ? 13.538 -2.416  20.100 1.00 18.83 ? 64  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 58  ? 14.131 -2.534  21.422 1.00 20.15 ? 64  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 58  ? 13.631 -1.410  22.315 1.00 20.03 ? 64  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 58  ? 13.742 -0.241  21.956 1.00 18.51 ? 64  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 58  ? 15.667 -2.550  21.382 1.00 20.87 ? 64  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 58  ? 16.259 -2.692  22.768 1.00 22.77 ? 64  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 58  ? 16.087 -3.858  23.504 1.00 24.29 ? 64  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 58  ? 16.989 -1.660  23.342 1.00 24.70 ? 64  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 58  ? 16.619 -3.986  24.784 1.00 26.61 ? 64  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 58  ? 17.504 -1.766  24.626 1.00 26.31 ? 64  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 58  ? 17.315 -2.928  25.345 1.00 28.22 ? 64  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 58  ? 17.825 -3.013  26.615 1.00 31.39 ? 64  TYR   A OH  1 
ATOM   457  N  N   . CYS   A 1 59  ? 13.112 -1.767  23.506 1.00 21.85 ? 65  CYS   A N   1 
ATOM   458  C  CA  . CYS   A 1 59  ? 12.596 -0.797  24.468 1.00 23.78 ? 65  CYS   A CA  1 
ATOM   459  C  C   . CYS   A 1 59  ? 13.493 -0.761  25.718 1.00 25.32 ? 65  CYS   A C   1 
ATOM   460  O  O   . CYS   A 1 59  ? 13.363 -1.632  26.574 1.00 25.24 ? 65  CYS   A O   1 
ATOM   461  C  CB  . CYS   A 1 59  ? 11.150 -1.130  24.816 1.00 25.13 ? 65  CYS   A CB  1 
ATOM   462  S  SG  . CYS   A 1 59  ? 10.431 -0.082  26.110 1.00 27.74 ? 65  CYS   A SG  1 
ATOM   463  N  N   . SER   A 1 60  ? 14.427 0.223   25.806 1.00 26.46 ? 66  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 60  ? 15.346 0.293   26.941 1.00 28.89 ? 66  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 60  ? 14.664 0.441   28.290 1.00 30.00 ? 66  SER   A C   1 
ATOM   466  O  O   . SER   A 1 60  ? 15.156 -0.123  29.262 1.00 31.06 ? 66  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 60  ? 16.406 1.383   26.769 1.00 32.61 ? 66  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 60  ? 15.850 2.632   26.409 1.00 37.00 ? 66  SER   A OG  1 
ATOM   469  N  N   . SER   A 1 61  ? 13.527 1.153   28.361 1.00 30.34 ? 67  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 61  ? 12.791 1.338   29.633 1.00 31.00 ? 67  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 61  ? 12.171 0.051   30.183 1.00 31.54 ? 67  SER   A C   1 
ATOM   472  O  O   . SER   A 1 61  ? 11.766 0.020   31.354 1.00 33.02 ? 67  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 61  ? 11.740 2.435   29.505 1.00 31.68 ? 67  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 61  ? 10.695 2.087   28.610 1.00 31.35 ? 67  SER   A OG  1 
ATOM   475  N  N   . ARG   A 1 62  ? 12.159 -1.027  29.381 1.00 30.14 ? 68  ARG   A N   1 
ATOM   476  C  CA  . ARG   A 1 62  ? 11.718 -2.352  29.815 1.00 29.86 ? 68  ARG   A CA  1 
ATOM   477  C  C   . ARG   A 1 62  ? 12.825 -3.425  29.654 1.00 31.44 ? 68  ARG   A C   1 
ATOM   478  O  O   . ARG   A 1 62  ? 12.602 -4.589  30.024 1.00 31.64 ? 68  ARG   A O   1 
ATOM   479  C  CB  . ARG   A 1 62  ? 10.511 -2.783  28.979 1.00 29.92 ? 68  ARG   A CB  1 
ATOM   480  C  CG  . ARG   A 1 62  ? 9.244  -2.038  29.305 1.00 30.89 ? 68  ARG   A CG  1 
ATOM   481  C  CD  . ARG   A 1 62  ? 8.750  -2.314  30.731 1.00 31.79 ? 68  ARG   A CD  1 
ATOM   482  N  NE  . ARG   A 1 62  ? 7.526  -1.560  30.949 1.00 34.90 ? 68  ARG   A NE  1 
ATOM   483  C  CZ  . ARG   A 1 62  ? 7.483  -0.337  31.472 1.00 37.56 ? 68  ARG   A CZ  1 
ATOM   484  N  NH1 . ARG   A 1 62  ? 8.592  0.241   31.920 1.00 38.61 ? 68  ARG   A NH1 1 
ATOM   485  N  NH2 . ARG   A 1 62  ? 6.326  0.309   31.567 1.00 37.86 ? 68  ARG   A NH2 1 
ATOM   486  N  N   . ARG   A 1 63  ? 13.992 -3.056  29.048 1.00 32.17 ? 69  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 63  ? 15.094 -3.957  28.689 1.00 33.37 ? 69  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 63  ? 14.554 -5.182  27.918 1.00 31.74 ? 69  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 63  ? 14.917 -6.336  28.191 1.00 32.37 ? 69  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 63  ? 15.929 -4.339  29.920 1.00 36.94 ? 69  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 63  ? 16.482 -3.109  30.600 1.00 44.34 ? 69  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 63  ? 17.561 -3.448  31.600 1.00 52.17 ? 69  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 63  ? 18.796 -3.885  30.949 1.00 59.22 ? 69  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 63  ? 19.722 -3.063  30.458 1.00 64.17 ? 69  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 63  ? 19.546 -1.746  30.506 1.00 63.92 ? 69  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 63  ? 20.820 -3.552  29.894 1.00 65.57 ? 69  ARG   A NH2 1 
ATOM   497  N  N   . LYS   A 1 64  ? 13.596 -4.921  27.011 1.00 28.93 ? 70  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 64  ? 12.916 -5.989  26.281 1.00 27.51 ? 70  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 64  ? 12.693 -5.565  24.820 1.00 24.59 ? 70  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 64  ? 12.559 -4.366  24.548 1.00 24.01 ? 70  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 64  ? 11.511 -6.196  26.886 1.00 29.37 ? 70  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 64  ? 11.293 -7.434  27.737 1.00 35.41 ? 70  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 64  ? 9.798  -7.721  27.785 1.00 41.25 ? 70  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 64  ? 9.415  -8.816  28.752 1.00 46.85 ? 70  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 64  ? 9.561  -8.377  30.172 1.00 49.76 ? 70  LYS   A NZ  1 
ATOM   506  N  N   . HIS   A 1 65  ? 12.558 -6.552  23.923 1.00 21.96 ? 71  HIS   A N   1 
ATOM   507  C  CA  . HIS   A 1 65  ? 12.204 -6.333  22.533 1.00 21.20 ? 71  HIS   A CA  1 
ATOM   508  C  C   . HIS   A 1 65  ? 10.697 -6.648  22.423 1.00 21.16 ? 71  HIS   A C   1 
ATOM   509  O  O   . HIS   A 1 65  ? 10.180 -7.550  23.112 1.00 22.16 ? 71  HIS   A O   1 
ATOM   510  C  CB  . HIS   A 1 65  ? 12.987 -7.253  21.588 1.00 21.04 ? 71  HIS   A CB  1 
ATOM   511  C  CG  . HIS   A 1 65  ? 14.469 -7.054  21.571 1.00 22.04 ? 71  HIS   A CG  1 
ATOM   512  N  ND1 . HIS   A 1 65  ? 15.092 -6.381  20.541 1.00 23.37 ? 71  HIS   A ND1 1 
ATOM   513  C  CD2 . HIS   A 1 65  ? 15.409 -7.500  22.425 1.00 22.80 ? 71  HIS   A CD2 1 
ATOM   514  C  CE1 . HIS   A 1 65  ? 16.377 -6.392  20.827 1.00 23.22 ? 71  HIS   A CE1 1 
ATOM   515  N  NE2 . HIS   A 1 65  ? 16.616 -7.062  21.947 1.00 23.83 ? 71  HIS   A NE2 1 
ATOM   516  N  N   . TYR   A 1 66  ? 9.991  -5.887  21.608 1.00 19.16 ? 72  TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 66  ? 8.567  -6.079  21.425 1.00 18.85 ? 72  TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 66  ? 8.187  -6.129  19.941 1.00 18.38 ? 72  TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 66  ? 8.606  -5.278  19.145 1.00 16.37 ? 72  TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 66  ? 7.789  -4.926  22.093 1.00 19.57 ? 72  TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 66  ? 7.834  -4.905  23.600 1.00 21.57 ? 72  TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 66  ? 7.140  -5.845  24.349 1.00 23.91 ? 72  TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 66  ? 8.489  -3.889  24.280 1.00 23.29 ? 72  TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 66  ? 7.139  -5.806  25.746 1.00 25.49 ? 72  TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 66  ? 8.477  -3.826  25.674 1.00 24.65 ? 72  TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 66  ? 7.804  -4.789  26.403 1.00 26.27 ? 72  TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 66  ? 7.778  -4.725  27.779 1.00 29.08 ? 72  TYR   A OH  1 
ATOM   528  N  N   . PRO   A 1 67  ? 7.335  -7.097  19.562 1.00 18.68 ? 73  PRO   A N   1 
ATOM   529  C  CA  . PRO   A 1 67  ? 6.822  -7.110  18.174 1.00 17.86 ? 73  PRO   A CA  1 
ATOM   530  C  C   . PRO   A 1 67  ? 5.748  -5.999  18.009 1.00 18.51 ? 73  PRO   A C   1 
ATOM   531  O  O   . PRO   A 1 67  ? 4.944  -5.797  18.941 1.00 18.82 ? 73  PRO   A O   1 
ATOM   532  C  CB  . PRO   A 1 67  ? 6.172  -8.489  18.056 1.00 18.76 ? 73  PRO   A CB  1 
ATOM   533  C  CG  . PRO   A 1 67  ? 5.721  -8.816  19.473 1.00 20.17 ? 73  PRO   A CG  1 
ATOM   534  C  CD  . PRO   A 1 67  ? 6.755  -8.183  20.395 1.00 18.91 ? 73  PRO   A CD  1 
ATOM   535  N  N   . VAL   A 1 68  ? 5.710  -5.297  16.841 1.00 17.34 ? 74  VAL   A N   1 
ATOM   536  C  CA  . VAL   A 1 68  ? 4.741  -4.214  16.588 1.00 18.19 ? 74  VAL   A CA  1 
ATOM   537  C  C   . VAL   A 1 68  ? 4.194  -4.193  15.179 1.00 19.27 ? 74  VAL   A C   1 
ATOM   538  O  O   . VAL   A 1 68  ? 4.885  -4.592  14.232 1.00 19.38 ? 74  VAL   A O   1 
ATOM   539  C  CB  . VAL   A 1 68  ? 5.328  -2.776  16.851 1.00 18.15 ? 74  VAL   A CB  1 
ATOM   540  C  CG1 . VAL   A 1 68  ? 5.388  -2.454  18.326 1.00 19.31 ? 74  VAL   A CG1 1 
ATOM   541  C  CG2 . VAL   A 1 68  ? 6.686  -2.586  16.173 1.00 18.14 ? 74  VAL   A CG2 1 
ATOM   542  N  N   . SER   A 1 69  ? 2.949  -3.692  15.029 1.00 19.11 ? 75  SER   A N   1 
ATOM   543  C  CA  . SER   A 1 69  ? 2.416  -3.336  13.723 1.00 20.25 ? 75  SER   A CA  1 
ATOM   544  C  C   . SER   A 1 69  ? 2.644  -1.805  13.703 1.00 20.27 ? 75  SER   A C   1 
ATOM   545  O  O   . SER   A 1 69  ? 2.453  -1.146  14.733 1.00 20.49 ? 75  SER   A O   1 
ATOM   546  C  CB  . SER   A 1 69  ? 0.925  -3.626  13.580 1.00 23.04 ? 75  SER   A CB  1 
ATOM   547  O  OG  . SER   A 1 69  ? 0.724  -5.007  13.349 1.00 29.11 ? 75  SER   A OG  1 
ATOM   548  N  N   . PHE   A 1 70  ? 3.117  -1.268  12.593 1.00 19.52 ? 76  PHE   A N   1 
ATOM   549  C  CA  . PHE   A 1 70  ? 3.386  0.165   12.519 1.00 20.60 ? 76  PHE   A CA  1 
ATOM   550  C  C   . PHE   A 1 70  ? 2.851  0.786   11.227 1.00 23.23 ? 76  PHE   A C   1 
ATOM   551  O  O   . PHE   A 1 70  ? 2.641  0.072   10.236 1.00 24.69 ? 76  PHE   A O   1 
ATOM   552  C  CB  . PHE   A 1 70  ? 4.873  0.466   12.771 1.00 19.68 ? 76  PHE   A CB  1 
ATOM   553  C  CG  . PHE   A 1 70  ? 5.872  -0.213  11.859 1.00 18.70 ? 76  PHE   A CG  1 
ATOM   554  C  CD1 . PHE   A 1 70  ? 6.409  -1.447  12.189 1.00 18.44 ? 76  PHE   A CD1 1 
ATOM   555  C  CD2 . PHE   A 1 70  ? 6.328  0.418   10.706 1.00 18.71 ? 76  PHE   A CD2 1 
ATOM   556  C  CE1 . PHE   A 1 70  ? 7.343  -2.056  11.365 1.00 19.00 ? 76  PHE   A CE1 1 
ATOM   557  C  CE2 . PHE   A 1 70  ? 7.285  -0.186  9.891  1.00 18.86 ? 76  PHE   A CE2 1 
ATOM   558  C  CZ  . PHE   A 1 70  ? 7.756  -1.435  10.199 1.00 18.53 ? 76  PHE   A CZ  1 
ATOM   559  N  N   . SER   A 1 71  ? 2.562  2.108   11.253 1.00 22.83 ? 77  SER   A N   1 
ATOM   560  C  CA  . SER   A 1 71  ? 2.012  2.781   10.095 1.00 24.60 ? 77  SER   A CA  1 
ATOM   561  C  C   . SER   A 1 71  ? 3.124  3.124   9.056  1.00 26.05 ? 77  SER   A C   1 
ATOM   562  O  O   . SER   A 1 71  ? 4.307  2.939   9.341  1.00 25.86 ? 77  SER   A O   1 
ATOM   563  C  CB  . SER   A 1 71  ? 1.259  4.041   10.530 1.00 25.97 ? 77  SER   A CB  1 
ATOM   564  O  OG  . SER   A 1 71  ? 2.147  4.989   11.110 1.00 28.85 ? 77  SER   A OG  1 
ATOM   565  N  N   . LYS   A 1 72  ? 2.730  3.566   7.856  1.00 27.57 ? 78  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 72  ? 3.665  3.970   6.806  1.00 29.01 ? 78  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 72  ? 4.186  5.381   7.098  1.00 29.34 ? 78  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 72  ? 3.469  6.171   7.702  1.00 29.58 ? 78  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 72  ? 2.991  3.931   5.419  1.00 33.25 ? 78  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 72  ? 2.507  2.534   5.011  1.00 39.73 ? 78  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 72  ? 2.450  2.395   3.474  1.00 46.08 ? 78  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 72  ? 2.109  0.985   3.054  1.00 52.24 ? 78  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 72  ? 1.810  0.884   1.594  1.00 56.50 ? 78  LYS   A NZ  1 
ATOM   574  N  N   . PRO   A 1 73  ? 5.432  5.708   6.697  1.00 29.19 ? 79  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 73  ? 5.980  7.041   6.997  1.00 30.38 ? 79  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 73  ? 5.110  8.225   6.582  1.00 31.63 ? 79  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 73  ? 4.687  8.325   5.420  1.00 31.75 ? 79  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 73  ? 7.314  7.042   6.252  1.00 30.78 ? 79  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 73  ? 7.716  5.617   6.237  1.00 31.19 ? 79  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 73  ? 6.426  4.868   6.011  1.00 28.67 ? 79  PRO   A CD  1 
ATOM   581  N  N   . SER   A 1 74  ? 4.872  9.146   7.528  1.00 31.99 ? 80  SER   A N   1 
ATOM   582  C  CA  . SER   A 1 74  ? 4.037  10.322  7.262  1.00 32.88 ? 80  SER   A CA  1 
ATOM   583  C  C   . SER   A 1 74  ? 4.395  11.543  8.154  1.00 32.01 ? 80  SER   A C   1 
ATOM   584  O  O   . SER   A 1 74  ? 5.256  11.437  9.042  1.00 31.14 ? 80  SER   A O   1 
ATOM   585  C  CB  . SER   A 1 74  ? 2.568  9.945   7.449  1.00 35.80 ? 80  SER   A CB  1 
ATOM   586  O  OG  . SER   A 1 74  ? 2.361  9.423   8.753  1.00 39.67 ? 80  SER   A OG  1 
ATOM   587  N  N   . LEU   A 1 75  ? 3.723  12.698  7.906  1.00 31.85 ? 81  LEU   A N   1 
ATOM   588  C  CA  . LEU   A 1 75  ? 3.870  13.945  8.661  1.00 32.92 ? 81  LEU   A CA  1 
ATOM   589  C  C   . LEU   A 1 75  ? 2.939  13.891  9.870  1.00 34.40 ? 81  LEU   A C   1 
ATOM   590  O  O   . LEU   A 1 75  ? 1.710  13.888  9.696  1.00 35.43 ? 81  LEU   A O   1 
ATOM   591  C  CB  . LEU   A 1 75  ? 3.453  15.162  7.801  1.00 33.02 ? 81  LEU   A CB  1 
ATOM   592  C  CG  . LEU   A 1 75  ? 4.513  15.827  6.961  1.00 34.33 ? 81  LEU   A CG  1 
ATOM   593  C  CD1 . LEU   A 1 75  ? 3.906  16.899  6.088  1.00 35.18 ? 81  LEU   A CD1 1 
ATOM   594  C  CD2 . LEU   A 1 75  ? 5.584  16.453  7.821  1.00 34.95 ? 81  LEU   A CD2 1 
ATOM   595  N  N   . ILE   A 1 76  ? 3.497  13.895  11.088 1.00 34.51 ? 82  ILE   A N   1 
ATOM   596  C  CA  . ILE   A 1 76  ? 2.680  13.846  12.298 1.00 36.25 ? 82  ILE   A CA  1 
ATOM   597  C  C   . ILE   A 1 76  ? 3.105  14.962  13.267 1.00 38.38 ? 82  ILE   A C   1 
ATOM   598  O  O   . ILE   A 1 76  ? 4.301  15.112  13.508 1.00 38.30 ? 82  ILE   A O   1 
ATOM   599  C  CB  . ILE   A 1 76  ? 2.828  12.447  12.964 1.00 36.03 ? 82  ILE   A CB  1 
ATOM   600  C  CG1 . ILE   A 1 76  ? 2.234  11.326  12.090 1.00 36.62 ? 82  ILE   A CG1 1 
ATOM   601  C  CG2 . ILE   A 1 76  ? 2.224  12.433  14.375 1.00 36.52 ? 82  ILE   A CG2 1 
ATOM   602  C  CD1 . ILE   A 1 76  ? 2.958  9.981   12.264 1.00 37.88 ? 82  ILE   A CD1 1 
ATOM   603  N  N   . PHE   A 1 77  ? 2.142  15.699  13.858 1.00 39.61 ? 83  PHE   A N   1 
ATOM   604  C  CA  . PHE   A 1 77  ? 2.437  16.775  14.809 1.00 42.04 ? 83  PHE   A CA  1 
ATOM   605  C  C   . PHE   A 1 77  ? 3.077  16.300  16.146 1.00 42.37 ? 83  PHE   A C   1 
ATOM   606  O  O   . PHE   A 1 77  ? 2.668  15.285  16.705 1.00 42.15 ? 83  PHE   A O   1 
ATOM   607  C  CB  . PHE   A 1 77  ? 1.160  17.593  15.063 1.00 44.14 ? 83  PHE   A CB  1 
ATOM   608  C  CG  . PHE   A 1 77  ? 1.271  18.728  16.047 1.00 46.40 ? 83  PHE   A CG  1 
ATOM   609  C  CD1 . PHE   A 1 77  ? 1.716  19.972  15.644 1.00 47.77 ? 83  PHE   A CD1 1 
ATOM   610  C  CD2 . PHE   A 1 77  ? 0.873  18.566  17.361 1.00 48.15 ? 83  PHE   A CD2 1 
ATOM   611  C  CE1 . PHE   A 1 77  ? 1.772  21.032  16.544 1.00 48.80 ? 83  PHE   A CE1 1 
ATOM   612  C  CE2 . PHE   A 1 77  ? 0.907  19.635  18.251 1.00 49.05 ? 83  PHE   A CE2 1 
ATOM   613  C  CZ  . PHE   A 1 77  ? 1.371  20.851  17.843 1.00 48.53 ? 83  PHE   A CZ  1 
ATOM   614  N  N   . VAL   A 1 78  ? 4.081  17.059  16.647 1.00 42.97 ? 84  VAL   A N   1 
ATOM   615  C  CA  . VAL   A 1 78  ? 4.845  16.831  17.882 1.00 44.32 ? 84  VAL   A CA  1 
ATOM   616  C  C   . VAL   A 1 78  ? 4.941  18.157  18.701 1.00 46.34 ? 84  VAL   A C   1 
ATOM   617  O  O   . VAL   A 1 78  ? 5.358  19.192  18.170 1.00 45.89 ? 84  VAL   A O   1 
ATOM   618  C  CB  . VAL   A 1 78  ? 6.242  16.200  17.611 1.00 44.40 ? 84  VAL   A CB  1 
ATOM   619  C  CG1 . VAL   A 1 78  ? 6.960  15.873  18.914 1.00 44.98 ? 84  VAL   A CG1 1 
ATOM   620  C  CG2 . VAL   A 1 78  ? 6.132  14.956  16.745 1.00 44.08 ? 84  VAL   A CG2 1 
ATOM   621  N  N   . GLU   A 1 79  ? 4.590  18.069  20.005 1.00 48.17 ? 85  GLU   A N   1 
ATOM   622  C  CA  . GLU   A 1 79  ? 4.387  19.093  21.037 1.00 50.92 ? 85  GLU   A CA  1 
ATOM   623  C  C   . GLU   A 1 79  ? 5.442  20.245  21.169 1.00 52.46 ? 85  GLU   A C   1 
ATOM   624  O  O   . GLU   A 1 79  ? 5.167  21.297  20.631 1.00 52.99 ? 85  GLU   A O   1 
ATOM   625  C  CB  . GLU   A 1 79  ? 4.172  18.421  22.397 1.00 54.31 ? 85  GLU   A CB  1 
ATOM   626  C  CG  . GLU   A 1 79  ? 2.940  17.538  22.421 1.00 61.95 ? 85  GLU   A CG  1 
ATOM   627  C  CD  . GLU   A 1 79  ? 1.687  18.225  22.922 1.00 71.39 ? 85  GLU   A CD  1 
ATOM   628  O  OE1 . GLU   A 1 79  ? 1.567  19.457  22.730 1.00 74.20 ? 85  GLU   A OE1 1 
ATOM   629  O  OE2 . GLU   A 1 79  ? 0.827  17.529  23.508 1.00 74.02 ? 85  GLU   A OE2 1 
ATOM   630  N  N   . ALA   A 1 80  ? 6.530  20.115  21.979 1.00 53.00 ? 86  ALA   A N   1 
ATOM   631  C  CA  . ALA   A 1 80  ? 7.611  21.099  22.233 1.00 53.04 ? 86  ALA   A CA  1 
ATOM   632  C  C   . ALA   A 1 80  ? 8.553  20.542  23.312 1.00 52.62 ? 86  ALA   A C   1 
ATOM   633  O  O   . ALA   A 1 80  ? 8.101  19.842  24.217 1.00 53.58 ? 86  ALA   A O   1 
ATOM   634  C  CB  . ALA   A 1 80  ? 7.066  22.467  22.660 1.00 53.46 ? 86  ALA   A CB  1 
ATOM   635  N  N   . SER   A 1 81  ? 9.846  20.833  23.220 1.00 51.36 ? 87  SER   A N   1 
ATOM   636  C  CA  . SER   A 1 81  ? 10.831 20.300  24.161 1.00 51.04 ? 87  SER   A CA  1 
ATOM   637  C  C   . SER   A 1 81  ? 12.089 21.192  24.213 1.00 51.30 ? 87  SER   A C   1 
ATOM   638  O  O   . SER   A 1 81  ? 12.165 22.184  23.470 1.00 51.22 ? 87  SER   A O   1 
ATOM   639  C  CB  . SER   A 1 81  ? 11.213 18.883  23.733 1.00 52.14 ? 87  SER   A CB  1 
ATOM   640  O  OG  . SER   A 1 81  ? 11.774 18.875  22.431 1.00 53.86 ? 87  SER   A OG  1 
ATOM   641  N  N   . GLU   A 1 82  ? 13.088 20.858  25.079 1.00 51.04 ? 88  GLU   A N   1 
ATOM   642  C  CA  . GLU   A 1 82  ? 14.329 21.670  25.099 1.00 51.05 ? 88  GLU   A CA  1 
ATOM   643  C  C   . GLU   A 1 82  ? 15.118 21.549  23.757 1.00 48.44 ? 88  GLU   A C   1 
ATOM   644  O  O   . GLU   A 1 82  ? 16.120 22.247  23.575 1.00 48.58 ? 88  GLU   A O   1 
ATOM   645  C  CB  . GLU   A 1 82  ? 15.215 21.382  26.351 1.00 55.01 ? 88  GLU   A CB  1 
ATOM   646  C  CG  . GLU   A 1 82  ? 16.117 20.164  26.215 1.00 62.78 ? 88  GLU   A CG  1 
ATOM   647  C  CD  . GLU   A 1 82  ? 16.862 19.683  27.451 1.00 71.45 ? 88  GLU   A CD  1 
ATOM   648  O  OE1 . GLU   A 1 82  ? 18.027 20.102  27.638 1.00 72.27 ? 88  GLU   A OE1 1 
ATOM   649  O  OE2 . GLU   A 1 82  ? 16.301 18.853  28.205 1.00 74.76 ? 88  GLU   A OE2 1 
ATOM   650  N  N   . TYR   A 1 83  ? 14.593 20.722  22.798 1.00 45.67 ? 89  TYR   A N   1 
ATOM   651  C  CA  . TYR   A 1 83  ? 15.132 20.415  21.480 1.00 43.18 ? 89  TYR   A CA  1 
ATOM   652  C  C   . TYR   A 1 83  ? 14.325 21.032  20.316 1.00 41.08 ? 89  TYR   A C   1 
ATOM   653  O  O   . TYR   A 1 83  ? 14.949 21.529  19.386 1.00 41.95 ? 89  TYR   A O   1 
ATOM   654  C  CB  . TYR   A 1 83  ? 15.238 18.883  21.267 1.00 42.58 ? 89  TYR   A CB  1 
ATOM   655  C  CG  . TYR   A 1 83  ? 15.586 18.093  22.508 1.00 42.28 ? 89  TYR   A CG  1 
ATOM   656  C  CD1 . TYR   A 1 83  ? 16.858 18.146  23.058 1.00 42.90 ? 89  TYR   A CD1 1 
ATOM   657  C  CD2 . TYR   A 1 83  ? 14.631 17.323  23.153 1.00 42.81 ? 89  TYR   A CD2 1 
ATOM   658  C  CE1 . TYR   A 1 83  ? 17.179 17.424  24.201 1.00 43.77 ? 89  TYR   A CE1 1 
ATOM   659  C  CE2 . TYR   A 1 83  ? 14.935 16.609  24.303 1.00 43.46 ? 89  TYR   A CE2 1 
ATOM   660  C  CZ  . TYR   A 1 83  ? 16.214 16.648  24.817 1.00 44.31 ? 89  TYR   A CZ  1 
ATOM   661  O  OH  . TYR   A 1 83  ? 16.505 15.932  25.956 1.00 45.25 ? 89  TYR   A OH  1 
ATOM   662  N  N   . TYR   A 1 84  ? 12.971 20.977  20.326 1.00 38.63 ? 90  TYR   A N   1 
ATOM   663  C  CA  . TYR   A 1 84  ? 12.191 21.506  19.187 1.00 37.14 ? 90  TYR   A CA  1 
ATOM   664  C  C   . TYR   A 1 84  ? 10.917 22.283  19.540 1.00 38.47 ? 90  TYR   A C   1 
ATOM   665  O  O   . TYR   A 1 84  ? 10.206 21.913  20.468 1.00 39.03 ? 90  TYR   A O   1 
ATOM   666  C  CB  . TYR   A 1 84  ? 11.721 20.355  18.256 1.00 34.55 ? 90  TYR   A CB  1 
ATOM   667  C  CG  . TYR   A 1 84  ? 12.784 19.427  17.728 1.00 31.46 ? 90  TYR   A CG  1 
ATOM   668  C  CD1 . TYR   A 1 84  ? 12.868 18.115  18.170 1.00 30.19 ? 90  TYR   A CD1 1 
ATOM   669  C  CD2 . TYR   A 1 84  ? 13.631 19.820  16.699 1.00 30.53 ? 90  TYR   A CD2 1 
ATOM   670  C  CE1 . TYR   A 1 84  ? 13.807 17.237  17.649 1.00 29.65 ? 90  TYR   A CE1 1 
ATOM   671  C  CE2 . TYR   A 1 84  ? 14.567 18.945  16.161 1.00 29.88 ? 90  TYR   A CE2 1 
ATOM   672  C  CZ  . TYR   A 1 84  ? 14.634 17.644  16.621 1.00 29.37 ? 90  TYR   A CZ  1 
ATOM   673  O  OH  . TYR   A 1 84  ? 15.614 16.796  16.165 1.00 27.71 ? 90  TYR   A OH  1 
ATOM   674  N  N   . PRO   A 1 85  ? 10.518 23.262  18.704 1.00 38.87 ? 91  PRO   A N   1 
ATOM   675  C  CA  . PRO   A 1 85  ? 9.204  23.900  18.905 1.00 39.17 ? 91  PRO   A CA  1 
ATOM   676  C  C   . PRO   A 1 85  ? 8.056  23.010  18.358 1.00 39.49 ? 91  PRO   A C   1 
ATOM   677  O  O   . PRO   A 1 85  ? 8.328  21.946  17.787 1.00 39.62 ? 91  PRO   A O   1 
ATOM   678  C  CB  . PRO   A 1 85  ? 9.341  25.201  18.105 1.00 40.17 ? 91  PRO   A CB  1 
ATOM   679  C  CG  . PRO   A 1 85  ? 10.248 24.848  16.993 1.00 39.89 ? 91  PRO   A CG  1 
ATOM   680  C  CD  . PRO   A 1 85  ? 11.209 23.795  17.511 1.00 38.40 ? 91  PRO   A CD  1 
ATOM   681  N  N   . ALA   A 1 86  ? 6.779  23.437  18.496 1.00 39.62 ? 92  ALA   A N   1 
ATOM   682  C  CA  . ALA   A 1 86  ? 5.621  22.677  17.978 1.00 39.23 ? 92  ALA   A CA  1 
ATOM   683  C  C   . ALA   A 1 86  ? 5.759  22.527  16.472 1.00 36.88 ? 92  ALA   A C   1 
ATOM   684  O  O   . ALA   A 1 86  ? 5.975  23.535  15.807 1.00 36.69 ? 92  ALA   A O   1 
ATOM   685  C  CB  . ALA   A 1 86  ? 4.328  23.413  18.296 1.00 40.51 ? 92  ALA   A CB  1 
ATOM   686  N  N   . ARG   A 1 87  ? 5.744  21.279  15.941 1.00 34.23 ? 93  ARG   A N   1 
ATOM   687  C  CA  . ARG   A 1 87  ? 5.961  21.099  14.499 1.00 32.05 ? 93  ARG   A CA  1 
ATOM   688  C  C   . ARG   A 1 87  ? 5.441  19.750  13.973 1.00 30.60 ? 93  ARG   A C   1 
ATOM   689  O  O   . ARG   A 1 87  ? 5.104  18.886  14.763 1.00 30.90 ? 93  ARG   A O   1 
ATOM   690  C  CB  . ARG   A 1 87  ? 7.475  21.246  14.198 1.00 31.02 ? 93  ARG   A CB  1 
ATOM   691  C  CG  . ARG   A 1 87  ? 8.262  19.943  14.461 1.00 30.89 ? 93  ARG   A CG  1 
ATOM   692  C  CD  . ARG   A 1 87  ? 9.675  20.129  14.941 1.00 30.45 ? 93  ARG   A CD  1 
ATOM   693  N  NE  . ARG   A 1 87  ? 10.523 18.980  14.599 1.00 29.25 ? 93  ARG   A NE  1 
ATOM   694  C  CZ  . ARG   A 1 87  ? 10.500 17.811  15.231 1.00 26.79 ? 93  ARG   A CZ  1 
ATOM   695  N  NH1 . ARG   A 1 87  ? 11.306 16.826  14.848 1.00 25.91 ? 93  ARG   A NH1 1 
ATOM   696  N  NH2 . ARG   A 1 87  ? 9.666  17.614  16.250 1.00 23.95 ? 93  ARG   A NH2 1 
ATOM   697  N  N   . TYR   A 1 88  ? 5.398  19.572  12.650 1.00 29.51 ? 94  TYR   A N   1 
ATOM   698  C  CA  . TYR   A 1 88  ? 5.078  18.284  12.060 1.00 29.47 ? 94  TYR   A CA  1 
ATOM   699  C  C   . TYR   A 1 88  ? 6.423  17.583  11.795 1.00 25.56 ? 94  TYR   A C   1 
ATOM   700  O  O   . TYR   A 1 88  ? 7.340  18.190  11.231 1.00 24.62 ? 94  TYR   A O   1 
ATOM   701  C  CB  . TYR   A 1 88  ? 4.353  18.446  10.727 1.00 32.26 ? 94  TYR   A CB  1 
ATOM   702  C  CG  . TYR   A 1 88  ? 2.930  18.937  10.880 1.00 36.61 ? 94  TYR   A CG  1 
ATOM   703  C  CD1 . TYR   A 1 88  ? 1.898  18.058  11.170 1.00 39.26 ? 94  TYR   A CD1 1 
ATOM   704  C  CD2 . TYR   A 1 88  ? 2.621  20.282  10.750 1.00 39.14 ? 94  TYR   A CD2 1 
ATOM   705  C  CE1 . TYR   A 1 88  ? 0.585  18.500  11.288 1.00 41.28 ? 94  TYR   A CE1 1 
ATOM   706  C  CE2 . TYR   A 1 88  ? 1.319  20.740  10.894 1.00 41.53 ? 94  TYR   A CE2 1 
ATOM   707  C  CZ  . TYR   A 1 88  ? 0.302  19.847  11.180 1.00 43.26 ? 94  TYR   A CZ  1 
ATOM   708  O  OH  . TYR   A 1 88  ? -0.995 20.292  11.287 1.00 47.95 ? 94  TYR   A OH  1 
ATOM   709  N  N   . GLN   A 1 89  ? 6.539  16.334  12.218 1.00 22.65 ? 95  GLN   A N   1 
ATOM   710  C  CA  . GLN   A 1 89  ? 7.767  15.562  11.997 1.00 20.90 ? 95  GLN   A CA  1 
ATOM   711  C  C   . GLN   A 1 89  ? 7.497  14.642  10.835 1.00 20.59 ? 95  GLN   A C   1 
ATOM   712  O  O   . GLN   A 1 89  ? 6.527  13.875  10.885 1.00 21.47 ? 95  GLN   A O   1 
ATOM   713  C  CB  . GLN   A 1 89  ? 8.146  14.740  13.238 1.00 20.28 ? 95  GLN   A CB  1 
ATOM   714  C  CG  . GLN   A 1 89  ? 9.393  13.881  13.005 1.00 19.89 ? 95  GLN   A CG  1 
ATOM   715  C  CD  . GLN   A 1 89  ? 10.050 13.428  14.274 1.00 21.85 ? 95  GLN   A CD  1 
ATOM   716  O  OE1 . GLN   A 1 89  ? 10.256 14.205  15.213 1.00 21.34 ? 95  GLN   A OE1 1 
ATOM   717  N  NE2 . GLN   A 1 89  ? 10.453 12.163  14.299 1.00 20.01 ? 95  GLN   A NE2 1 
ATOM   718  N  N   . SER   A 1 90  ? 8.296  14.738  9.766  1.00 18.99 ? 96  SER   A N   1 
ATOM   719  C  CA  . SER   A 1 90  ? 8.075  13.913  8.584  1.00 19.06 ? 96  SER   A CA  1 
ATOM   720  C  C   . SER   A 1 90  ? 8.768  12.545  8.686  1.00 19.51 ? 96  SER   A C   1 
ATOM   721  O  O   . SER   A 1 90  ? 9.656  12.355  9.542  1.00 19.58 ? 96  SER   A O   1 
ATOM   722  C  CB  . SER   A 1 90  ? 8.550  14.648  7.335  1.00 20.55 ? 96  SER   A CB  1 
ATOM   723  O  OG  . SER   A 1 90  ? 9.951  14.889  7.412  1.00 22.62 ? 96  SER   A OG  1 
ATOM   724  N  N   . HIS   A 1 91  ? 8.319  11.586  7.841  1.00 18.97 ? 97  HIS   A N   1 
ATOM   725  C  CA  . HIS   A 1 91  ? 8.885  10.242  7.759  1.00 18.90 ? 97  HIS   A CA  1 
ATOM   726  C  C   . HIS   A 1 91  ? 8.741  9.529   9.103  1.00 18.74 ? 97  HIS   A C   1 
ATOM   727  O  O   . HIS   A 1 91  ? 9.627  8.781   9.493  1.00 18.11 ? 97  HIS   A O   1 
ATOM   728  C  CB  . HIS   A 1 91  ? 10.376 10.325  7.329  1.00 19.63 ? 97  HIS   A CB  1 
ATOM   729  C  CG  . HIS   A 1 91  ? 10.570 10.950  5.972  1.00 23.39 ? 97  HIS   A CG  1 
ATOM   730  N  ND1 . HIS   A 1 91  ? 10.663 10.175  4.823  1.00 25.62 ? 97  HIS   A ND1 1 
ATOM   731  C  CD2 . HIS   A 1 91  ? 10.593 12.257  5.614  1.00 24.40 ? 97  HIS   A CD2 1 
ATOM   732  C  CE1 . HIS   A 1 91  ? 10.773 11.030  3.814  1.00 25.73 ? 97  HIS   A CE1 1 
ATOM   733  N  NE2 . HIS   A 1 91  ? 10.726 12.292  4.235  1.00 25.46 ? 97  HIS   A NE2 1 
ATOM   734  N  N   . LEU   A 1 92  ? 7.612  9.748   9.794  1.00 19.21 ? 98  LEU   A N   1 
ATOM   735  C  CA  . LEU   A 1 92  ? 7.367  9.178   11.118 1.00 20.25 ? 98  LEU   A CA  1 
ATOM   736  C  C   . LEU   A 1 92  ? 6.355  8.041   11.061 1.00 20.45 ? 98  LEU   A C   1 
ATOM   737  O  O   . LEU   A 1 92  ? 5.309  8.170   10.397 1.00 20.66 ? 98  LEU   A O   1 
ATOM   738  C  CB  . LEU   A 1 92  ? 6.859  10.294  12.053 1.00 20.76 ? 98  LEU   A CB  1 
ATOM   739  C  CG  . LEU   A 1 92  ? 6.700  9.920   13.538 1.00 22.63 ? 98  LEU   A CG  1 
ATOM   740  C  CD1 . LEU   A 1 92  ? 8.038  9.537   14.152 1.00 22.79 ? 98  LEU   A CD1 1 
ATOM   741  C  CD2 . LEU   A 1 92  ? 6.086  11.091  14.337 1.00 24.34 ? 98  LEU   A CD2 1 
ATOM   742  N  N   . MET   A 1 93  ? 6.638  6.945   11.801 1.00 19.39 ? 99  MET   A N   1 
ATOM   743  C  CA  . MET   A 1 93  ? 5.758  5.778   11.850 1.00 19.45 ? 99  MET   A CA  1 
ATOM   744  C  C   . MET   A 1 93  ? 5.270  5.547   13.269 1.00 21.00 ? 99  MET   A C   1 
ATOM   745  O  O   . MET   A 1 93  ? 6.068  5.630   14.187 1.00 21.91 ? 99  MET   A O   1 
ATOM   746  C  CB  . MET   A 1 93  ? 6.485  4.543   11.309 1.00 19.05 ? 99  MET   A CB  1 
ATOM   747  C  CG  . MET   A 1 93  ? 7.080  4.810   9.918  1.00 20.87 ? 99  MET   A CG  1 
ATOM   748  S  SD  . MET   A 1 93  ? 8.084  3.469   9.323  1.00 23.84 ? 99  MET   A SD  1 
ATOM   749  C  CE  . MET   A 1 93  ? 9.514  3.637   10.332 1.00 19.78 ? 99  MET   A CE  1 
ATOM   750  N  N   . LEU   A 1 94  ? 3.973  5.291   13.463 1.00 21.25 ? 100 LEU   A N   1 
ATOM   751  C  CA  . LEU   A 1 94  ? 3.445  5.052   14.806 1.00 21.66 ? 100 LEU   A CA  1 
ATOM   752  C  C   . LEU   A 1 94  ? 3.073  3.576   15.007 1.00 21.49 ? 100 LEU   A C   1 
ATOM   753  O  O   . LEU   A 1 94  ? 2.657  2.904   14.067 1.00 20.69 ? 100 LEU   A O   1 
ATOM   754  C  CB  . LEU   A 1 94  ? 2.218  5.950   15.125 1.00 23.01 ? 100 LEU   A CB  1 
ATOM   755  C  CG  . LEU   A 1 94  ? 2.444  7.466   15.143 1.00 26.25 ? 100 LEU   A CG  1 
ATOM   756  C  CD1 . LEU   A 1 94  ? 1.183  8.188   15.572 1.00 28.07 ? 100 LEU   A CD1 1 
ATOM   757  C  CD2 . LEU   A 1 94  ? 3.576  7.858   16.068 1.00 27.28 ? 100 LEU   A CD2 1 
ATOM   758  N  N   . ALA   A 1 95  ? 3.141  3.125   16.262 1.00 21.87 ? 101 ALA   A N   1 
ATOM   759  C  CA  . ALA   A 1 95  ? 2.810  1.767   16.685 1.00 22.75 ? 101 ALA   A CA  1 
ATOM   760  C  C   . ALA   A 1 95  ? 2.268  1.787   18.111 1.00 23.81 ? 101 ALA   A C   1 
ATOM   761  O  O   . ALA   A 1 95  ? 2.586  2.686   18.893 1.00 24.21 ? 101 ALA   A O   1 
ATOM   762  C  CB  . ALA   A 1 95  ? 4.064  0.896   16.637 1.00 23.09 ? 101 ALA   A CB  1 
ATOM   763  N  N   . VAL   A 1 96  ? 1.454  0.797   18.447 1.00 23.71 ? 102 VAL   A N   1 
ATOM   764  C  CA  . VAL   A 1 96  ? 0.926  0.608   19.791 1.00 24.95 ? 102 VAL   A CA  1 
ATOM   765  C  C   . VAL   A 1 96  ? 1.982  -0.193  20.549 1.00 25.83 ? 102 VAL   A C   1 
ATOM   766  O  O   . VAL   A 1 96  ? 2.364  -1.299  20.153 1.00 26.35 ? 102 VAL   A O   1 
ATOM   767  C  CB  . VAL   A 1 96  ? -0.459 -0.083  19.790 1.00 26.50 ? 102 VAL   A CB  1 
ATOM   768  C  CG1 . VAL   A 1 96  ? -0.991 -0.243  21.210 1.00 27.35 ? 102 VAL   A CG1 1 
ATOM   769  C  CG2 . VAL   A 1 96  ? -1.449 0.727   18.949 1.00 27.13 ? 102 VAL   A CG2 1 
ATOM   770  N  N   . GLY   A 1 97  ? 2.552  0.445   21.543 1.00 25.77 ? 103 GLY   A N   1 
ATOM   771  C  CA  . GLY   A 1 97  ? 3.628  -0.132  22.322 1.00 26.11 ? 103 GLY   A CA  1 
ATOM   772  C  C   . GLY   A 1 97  ? 4.158  0.854   23.337 1.00 26.06 ? 103 GLY   A C   1 
ATOM   773  O  O   . GLY   A 1 97  ? 3.943  2.069   23.230 1.00 26.82 ? 103 GLY   A O   1 
ATOM   774  N  N   . HIS   A 1 98  ? 4.861  0.331   24.319 1.00 25.24 ? 104 HIS   A N   1 
ATOM   775  C  CA  . HIS   A 1 98  ? 5.434  1.131   25.357 1.00 25.85 ? 104 HIS   A CA  1 
ATOM   776  C  C   . HIS   A 1 98  ? 6.715  1.865   24.953 1.00 25.13 ? 104 HIS   A C   1 
ATOM   777  O  O   . HIS   A 1 98  ? 7.647  1.291   24.393 1.00 24.85 ? 104 HIS   A O   1 
ATOM   778  C  CB  . HIS   A 1 98  ? 5.649  0.310   26.635 1.00 26.94 ? 104 HIS   A CB  1 
ATOM   779  C  CG  . HIS   A 1 98  ? 6.310  1.103   27.718 1.00 30.64 ? 104 HIS   A CG  1 
ATOM   780  N  ND1 . HIS   A 1 98  ? 5.636  2.085   28.396 1.00 33.83 ? 104 HIS   A ND1 1 
ATOM   781  C  CD2 . HIS   A 1 98  ? 7.602  1.110   28.107 1.00 32.48 ? 104 HIS   A CD2 1 
ATOM   782  C  CE1 . HIS   A 1 98  ? 6.524  2.629   29.212 1.00 34.60 ? 104 HIS   A CE1 1 
ATOM   783  N  NE2 . HIS   A 1 98  ? 7.722  2.067   29.068 1.00 34.01 ? 104 HIS   A NE2 1 
ATOM   784  N  N   . SER   A 1 99  ? 6.772  3.124   25.346 1.00 25.35 ? 105 SER   A N   1 
ATOM   785  C  CA  . SER   A 1 99  ? 7.922  3.991   25.199 1.00 27.37 ? 105 SER   A CA  1 
ATOM   786  C  C   . SER   A 1 99  ? 7.772  5.159   26.172 1.00 30.38 ? 105 SER   A C   1 
ATOM   787  O  O   . SER   A 1 99  ? 6.654  5.598   26.452 1.00 30.42 ? 105 SER   A O   1 
ATOM   788  C  CB  . SER   A 1 99  ? 8.060  4.514   23.770 1.00 27.45 ? 105 SER   A CB  1 
ATOM   789  O  OG  . SER   A 1 99  ? 6.982  5.364   23.407 1.00 29.69 ? 105 SER   A OG  1 
ATOM   790  N  N   . GLU   A 1 100 ? 8.892  5.637   26.698 1.00 31.99 ? 106 GLU   A N   1 
ATOM   791  C  CA  . GLU   A 1 100 ? 8.942  6.810   27.566 1.00 34.43 ? 106 GLU   A CA  1 
ATOM   792  C  C   . GLU   A 1 100 ? 10.231 7.596   27.280 1.00 37.13 ? 106 GLU   A C   1 
ATOM   793  O  O   . GLU   A 1 100 ? 11.139 7.028   26.657 1.00 37.66 ? 106 GLU   A O   1 
ATOM   794  C  CB  . GLU   A 1 100 ? 8.790  6.446   29.046 1.00 36.61 ? 106 GLU   A CB  1 
ATOM   795  C  CG  . GLU   A 1 100 ? 9.741  5.369   29.506 1.00 39.14 ? 106 GLU   A CG  1 
ATOM   796  C  CD  . GLU   A 1 100 ? 9.438  4.942   30.929 1.00 40.78 ? 106 GLU   A CD  1 
ATOM   797  O  OE1 . GLU   A 1 100 ? 9.848  5.670   31.856 1.00 42.37 ? 106 GLU   A OE1 1 
ATOM   798  O  OE2 . GLU   A 1 100 ? 8.796  3.886   31.119 1.00 40.33 ? 106 GLU   A OE2 1 
ATOM   799  N  N   . PRO   A 1 101 ? 10.349 8.906   27.660 1.00 38.63 ? 107 PRO   A N   1 
ATOM   800  C  CA  . PRO   A 1 101 ? 11.605 9.642   27.364 1.00 39.66 ? 107 PRO   A CA  1 
ATOM   801  C  C   . PRO   A 1 101 ? 12.816 8.855   27.874 1.00 39.28 ? 107 PRO   A C   1 
ATOM   802  O  O   . PRO   A 1 101 ? 12.778 8.334   29.003 1.00 41.23 ? 107 PRO   A O   1 
ATOM   803  C  CB  . PRO   A 1 101 ? 11.444 10.996  28.080 1.00 40.75 ? 107 PRO   A CB  1 
ATOM   804  C  CG  . PRO   A 1 101 ? 9.995  11.126  28.431 1.00 40.91 ? 107 PRO   A CG  1 
ATOM   805  C  CD  . PRO   A 1 101 ? 9.364  9.742   28.375 1.00 38.61 ? 107 PRO   A CD  1 
ATOM   806  N  N   . GLY   A 1 102 ? 13.794 8.667   26.999 1.00 36.24 ? 108 GLY   A N   1 
ATOM   807  C  CA  . GLY   A 1 102 ? 14.945 7.811   27.271 1.00 34.42 ? 108 GLY   A CA  1 
ATOM   808  C  C   . GLY   A 1 102 ? 14.992 6.606   26.338 1.00 32.45 ? 108 GLY   A C   1 
ATOM   809  O  O   . GLY   A 1 102 ? 16.030 5.944   26.201 1.00 32.69 ? 108 GLY   A O   1 
ATOM   810  N  N   . ASP   A 1 103 ? 13.849 6.292   25.683 1.00 29.85 ? 109 ASP   A N   1 
ATOM   811  C  CA  . ASP   A 1 103 ? 13.762 5.179   24.765 1.00 27.33 ? 109 ASP   A CA  1 
ATOM   812  C  C   . ASP   A 1 103 ? 14.220 5.514   23.337 1.00 24.44 ? 109 ASP   A C   1 
ATOM   813  O  O   . ASP   A 1 103 ? 14.359 4.593   22.539 1.00 23.08 ? 109 ASP   A O   1 
ATOM   814  C  CB  . ASP   A 1 103 ? 12.343 4.597   24.730 1.00 27.84 ? 109 ASP   A CB  1 
ATOM   815  C  CG  . ASP   A 1 103 ? 12.122 3.594   25.827 1.00 28.29 ? 109 ASP   A CG  1 
ATOM   816  O  OD1 . ASP   A 1 103 ? 13.069 2.872   26.157 1.00 27.30 ? 109 ASP   A OD1 1 
ATOM   817  O  OD2 . ASP   A 1 103 ? 11.005 3.539   26.362 1.00 29.62 ? 109 ASP   A OD2 1 
ATOM   818  N  N   . CYS   A 1 104 ? 14.459 6.810   23.024 1.00 22.95 ? 110 CYS   A N   1 
ATOM   819  C  CA  . CYS   A 1 104 ? 14.917 7.247   21.679 1.00 22.40 ? 110 CYS   A CA  1 
ATOM   820  C  C   . CYS   A 1 104 ? 16.204 6.542   21.305 1.00 20.89 ? 110 CYS   A C   1 
ATOM   821  O  O   . CYS   A 1 104 ? 17.026 6.326   22.184 1.00 21.97 ? 110 CYS   A O   1 
ATOM   822  C  CB  . CYS   A 1 104 ? 15.094 8.759   21.635 1.00 22.99 ? 110 CYS   A CB  1 
ATOM   823  S  SG  . CYS   A 1 104 ? 13.538 9.663   21.572 1.00 27.42 ? 110 CYS   A SG  1 
ATOM   824  N  N   . GLY   A 1 105 ? 16.384 6.193   20.040 1.00 19.64 ? 111 GLY   A N   1 
ATOM   825  C  CA  . GLY   A 1 105 ? 17.593 5.477   19.630 1.00 19.69 ? 111 GLY   A CA  1 
ATOM   826  C  C   . GLY   A 1 105 ? 17.410 3.967   19.577 1.00 19.92 ? 111 GLY   A C   1 
ATOM   827  O  O   . GLY   A 1 105 ? 18.201 3.264   18.949 1.00 20.85 ? 111 GLY   A O   1 
ATOM   828  N  N   . GLY   A 1 106 ? 16.354 3.451   20.192 1.00 19.22 ? 112 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 106 ? 16.028 2.022   20.094 1.00 18.06 ? 112 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 106 ? 15.715 1.648   18.646 1.00 16.90 ? 112 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 106 ? 14.961 2.330   17.977 1.00 16.27 ? 112 GLY   A O   1 
ATOM   832  N  N   . ILE   A 1 107 ? 16.347 0.599   18.140 1.00 15.35 ? 113 ILE   A N   1 
ATOM   833  C  CA  . ILE   A 1 107 ? 16.199 0.162   16.774 1.00 14.74 ? 113 ILE   A CA  1 
ATOM   834  C  C   . ILE   A 1 107 ? 14.917 -0.648  16.558 1.00 14.60 ? 113 ILE   A C   1 
ATOM   835  O  O   . ILE   A 1 107 ? 14.607 -1.552  17.349 1.00 14.61 ? 113 ILE   A O   1 
ATOM   836  C  CB  . ILE   A 1 107 ? 17.491 -0.649  16.367 1.00 17.23 ? 113 ILE   A CB  1 
ATOM   837  C  CG1 . ILE   A 1 107 ? 18.711 0.279   16.070 1.00 18.58 ? 113 ILE   A CG1 1 
ATOM   838  C  CG2 . ILE   A 1 107 ? 17.236 -1.566  15.171 1.00 18.29 ? 113 ILE   A CG2 1 
ATOM   839  C  CD1 . ILE   A 1 107 ? 20.072 -0.575  15.893 1.00 21.09 ? 113 ILE   A CD1 1 
ATOM   840  N  N   . LEU   A 1 108 ? 14.254 -0.396  15.413 1.00 13.86 ? 114 LEU   A N   1 
ATOM   841  C  CA  . LEU   A 1 108 ? 13.117 -1.133  14.883 1.00 13.72 ? 114 LEU   A CA  1 
ATOM   842  C  C   . LEU   A 1 108 ? 13.662 -1.911  13.652 1.00 14.79 ? 114 LEU   A C   1 
ATOM   843  O  O   . LEU   A 1 108 ? 14.334 -1.327  12.802 1.00 13.59 ? 114 LEU   A O   1 
ATOM   844  C  CB  . LEU   A 1 108 ? 12.053 -0.141  14.426 1.00 14.31 ? 114 LEU   A CB  1 
ATOM   845  C  CG  . LEU   A 1 108 ? 10.894 -0.713  13.571 1.00 15.90 ? 114 LEU   A CG  1 
ATOM   846  C  CD1 . LEU   A 1 108 ? 10.072 -1.745  14.351 1.00 17.02 ? 114 LEU   A CD1 1 
ATOM   847  C  CD2 . LEU   A 1 108 ? 9.939  0.431   13.132 1.00 15.88 ? 114 LEU   A CD2 1 
ATOM   848  N  N   . ARG   A 1 109 ? 13.410 -3.226  13.599 1.00 15.17 ? 115 ARG   A N   1 
ATOM   849  C  CA  . ARG   A 1 109 ? 13.891 -4.105  12.546 1.00 15.93 ? 115 ARG   A CA  1 
ATOM   850  C  C   . ARG   A 1 109 ? 12.739 -4.986  12.069 1.00 16.97 ? 115 ARG   A C   1 
ATOM   851  O  O   . ARG   A 1 109 ? 11.867 -5.324  12.851 1.00 15.07 ? 115 ARG   A O   1 
ATOM   852  C  CB  . ARG   A 1 109 ? 14.942 -5.088  13.086 1.00 17.54 ? 115 ARG   A CB  1 
ATOM   853  C  CG  . ARG   A 1 109 ? 16.246 -4.529  13.608 1.00 25.26 ? 115 ARG   A CG  1 
ATOM   854  C  CD  . ARG   A 1 109 ? 17.105 -5.682  14.135 1.00 29.83 ? 115 ARG   A CD  1 
ATOM   855  N  NE  . ARG   A 1 109 ? 17.621 -6.438  12.999 1.00 34.62 ? 115 ARG   A NE  1 
ATOM   856  C  CZ  . ARG   A 1 109 ? 18.789 -6.196  12.407 1.00 37.02 ? 115 ARG   A CZ  1 
ATOM   857  N  NH1 . ARG   A 1 109 ? 19.141 -6.873  11.327 1.00 37.35 ? 115 ARG   A NH1 1 
ATOM   858  N  NH2 . ARG   A 1 109 ? 19.624 -5.294  12.909 1.00 37.40 ? 115 ARG   A NH2 1 
ATOM   859  N  N   . CYS   A 1 110 ? 12.771 -5.365  10.793 1.00 18.34 ? 116 CYS   A N   1 
ATOM   860  C  CA  . CYS   A 1 110 ? 11.834 -6.304  10.189 1.00 20.70 ? 116 CYS   A CA  1 
ATOM   861  C  C   . CYS   A 1 110 ? 12.732 -7.469  9.678  1.00 23.96 ? 116 CYS   A C   1 
ATOM   862  O  O   . CYS   A 1 110 ? 13.940 -7.465  9.940  1.00 24.22 ? 116 CYS   A O   1 
ATOM   863  C  CB  . CYS   A 1 110 ? 11.094 -5.614  9.040  1.00 21.04 ? 116 CYS   A CB  1 
ATOM   864  S  SG  . CYS   A 1 110 ? 12.173 -5.112  7.680  1.00 23.20 ? 116 CYS   A SG  1 
ATOM   865  N  N   . GLN   A 1 111 ? 12.179 -8.451  8.930  1.00 26.47 ? 117 GLN   A N   1 
ATOM   866  C  CA  . GLN   A 1 111 ? 13.010 -9.543  8.382  1.00 29.19 ? 117 GLN   A CA  1 
ATOM   867  C  C   . GLN   A 1 111 ? 14.105 -9.033  7.402  1.00 30.49 ? 117 GLN   A C   1 
ATOM   868  O  O   . GLN   A 1 111 ? 15.039 -9.781  7.082  1.00 31.49 ? 117 GLN   A O   1 
ATOM   869  C  CB  . GLN   A 1 111 ? 12.122 -10.558 7.644  1.00 32.11 ? 117 GLN   A CB  1 
ATOM   870  C  CG  . GLN   A 1 111 ? 11.446 -9.953  6.416  1.00 36.68 ? 117 GLN   A CG  1 
ATOM   871  C  CD  . GLN   A 1 111 ? 10.496 -10.939 5.808  1.00 43.53 ? 117 GLN   A CD  1 
ATOM   872  O  OE1 . GLN   A 1 111 ? 9.277  -10.862 6.005  1.00 46.18 ? 117 GLN   A OE1 1 
ATOM   873  N  NE2 . GLN   A 1 111 ? 11.045 -11.895 5.073  1.00 43.21 ? 117 GLN   A NE2 1 
ATOM   874  N  N   . HIS   A 1 112 ? 13.975 -7.791  6.894  1.00 29.80 ? 118 HIS   A N   1 
ATOM   875  C  CA  . HIS   A 1 112 ? 14.932 -7.281  5.905  1.00 29.89 ? 118 HIS   A CA  1 
ATOM   876  C  C   . HIS   A 1 112 ? 16.105 -6.520  6.489  1.00 27.91 ? 118 HIS   A C   1 
ATOM   877  O  O   . HIS   A 1 112 ? 17.084 -6.295  5.776  1.00 28.57 ? 118 HIS   A O   1 
ATOM   878  C  CB  . HIS   A 1 112 ? 14.238 -6.423  4.834  1.00 31.49 ? 118 HIS   A CB  1 
ATOM   879  C  CG  . HIS   A 1 112 ? 13.072 -7.096  4.187  1.00 36.31 ? 118 HIS   A CG  1 
ATOM   880  N  ND1 . HIS   A 1 112 ? 11.780 -6.842  4.603  1.00 39.23 ? 118 HIS   A ND1 1 
ATOM   881  C  CD2 . HIS   A 1 112 ? 13.039 -8.022  3.198  1.00 38.93 ? 118 HIS   A CD2 1 
ATOM   882  C  CE1 . HIS   A 1 112 ? 11.000 -7.590  3.837  1.00 40.24 ? 118 HIS   A CE1 1 
ATOM   883  N  NE2 . HIS   A 1 112 ? 11.713 -8.333  2.984  1.00 40.49 ? 118 HIS   A NE2 1 
ATOM   884  N  N   . GLY   A 1 113 ? 16.003 -6.102  7.750  1.00 25.32 ? 119 GLY   A N   1 
ATOM   885  C  CA  . GLY   A 1 113 ? 17.052 -5.316  8.376  1.00 23.76 ? 119 GLY   A CA  1 
ATOM   886  C  C   . GLY   A 1 113 ? 16.512 -4.167  9.205  1.00 21.45 ? 119 GLY   A C   1 
ATOM   887  O  O   . GLY   A 1 113 ? 15.380 -4.219  9.679  1.00 20.43 ? 119 GLY   A O   1 
ATOM   888  N  N   . VAL   A 1 114 ? 17.324 -3.110  9.374  1.00 20.77 ? 120 VAL   A N   1 
ATOM   889  C  CA  . VAL   A 1 114 ? 16.981 -1.953  10.152 1.00 20.10 ? 120 VAL   A CA  1 
ATOM   890  C  C   . VAL   A 1 114 ? 15.978 -1.079  9.401  1.00 19.29 ? 120 VAL   A C   1 
ATOM   891  O  O   . VAL   A 1 114 ? 16.210 -0.726  8.236  1.00 19.55 ? 120 VAL   A O   1 
ATOM   892  C  CB  . VAL   A 1 114 ? 18.254 -1.179  10.560 1.00 20.96 ? 120 VAL   A CB  1 
ATOM   893  C  CG1 . VAL   A 1 114 ? 17.913 0.138   11.218 1.00 21.10 ? 120 VAL   A CG1 1 
ATOM   894  C  CG2 . VAL   A 1 114 ? 19.139 -2.041  11.475 1.00 21.32 ? 120 VAL   A CG2 1 
ATOM   895  N  N   . VAL   A 1 115 ? 14.836 -0.788  10.060 1.00 16.87 ? 121 VAL   A N   1 
ATOM   896  C  CA  . VAL   A 1 115 ? 13.763 0.033   9.527  1.00 16.50 ? 121 VAL   A CA  1 
ATOM   897  C  C   . VAL   A 1 115 ? 13.911 1.534   9.979  1.00 17.10 ? 121 VAL   A C   1 
ATOM   898  O  O   . VAL   A 1 115 ? 13.723 2.463   9.193  1.00 16.98 ? 121 VAL   A O   1 
ATOM   899  C  CB  . VAL   A 1 115 ? 12.368 -0.548  9.937  1.00 16.81 ? 121 VAL   A CB  1 
ATOM   900  C  CG1 . VAL   A 1 115 ? 11.254 0.421   9.567  1.00 18.35 ? 121 VAL   A CG1 1 
ATOM   901  C  CG2 . VAL   A 1 115 ? 12.112 -1.927  9.316  1.00 16.61 ? 121 VAL   A CG2 1 
ATOM   902  N  N   . GLY   A 1 116 ? 14.186 1.736   11.259 1.00 16.96 ? 122 GLY   A N   1 
ATOM   903  C  CA  . GLY   A 1 116 ? 14.314 3.065   11.825 1.00 17.53 ? 122 GLY   A CA  1 
ATOM   904  C  C   . GLY   A 1 116 ? 14.637 3.072   13.303 1.00 16.51 ? 122 GLY   A C   1 
ATOM   905  O  O   . GLY   A 1 116 ? 15.004 2.034   13.864 1.00 15.37 ? 122 GLY   A O   1 
ATOM   906  N  N   . ILE   A 1 117 ? 14.568 4.266   13.925 1.00 15.00 ? 123 ILE   A N   1 
ATOM   907  C  CA  . ILE   A 1 117 ? 14.865 4.381   15.350 1.00 14.64 ? 123 ILE   A CA  1 
ATOM   908  C  C   . ILE   A 1 117 ? 13.766 5.085   16.130 1.00 14.30 ? 123 ILE   A C   1 
ATOM   909  O  O   . ILE   A 1 117 ? 13.147 6.012   15.602 1.00 13.14 ? 123 ILE   A O   1 
ATOM   910  C  CB  . ILE   A 1 117 ? 16.221 5.092   15.594 1.00 16.69 ? 123 ILE   A CB  1 
ATOM   911  C  CG1 . ILE   A 1 117 ? 16.316 6.403   14.816 1.00 17.23 ? 123 ILE   A CG1 1 
ATOM   912  C  CG2 . ILE   A 1 117 ? 17.405 4.149   15.332 1.00 18.08 ? 123 ILE   A CG2 1 
ATOM   913  C  CD1 . ILE   A 1 117 ? 17.475 7.230   15.268 1.00 18.98 ? 123 ILE   A CD1 1 
ATOM   914  N  N   . VAL   A 1 118 ? 13.581 4.730   17.436 1.00 14.82 ? 124 VAL   A N   1 
ATOM   915  C  CA  . VAL   A 1 118 ? 12.571 5.394   18.287 1.00 14.97 ? 124 VAL   A CA  1 
ATOM   916  C  C   . VAL   A 1 118 ? 12.853 6.899   18.329 1.00 14.33 ? 124 VAL   A C   1 
ATOM   917  O  O   . VAL   A 1 118 ? 14.006 7.295   18.481 1.00 13.53 ? 124 VAL   A O   1 
ATOM   918  C  CB  . VAL   A 1 118 ? 12.506 4.822   19.723 1.00 16.95 ? 124 VAL   A CB  1 
ATOM   919  C  CG1 . VAL   A 1 118 ? 11.537 5.625   20.590 1.00 18.62 ? 124 VAL   A CG1 1 
ATOM   920  C  CG2 . VAL   A 1 118 ? 12.099 3.342   19.704 1.00 18.42 ? 124 VAL   A CG2 1 
ATOM   921  N  N   . SER   A 1 119 ? 11.833 7.724   18.103 1.00 15.41 ? 125 SER   A N   1 
ATOM   922  C  CA  . SER   A 1 119 ? 12.042 9.179   18.091 1.00 16.55 ? 125 SER   A CA  1 
ATOM   923  C  C   . SER   A 1 119 ? 11.012 9.952   18.941 1.00 19.16 ? 125 SER   A C   1 
ATOM   924  O  O   . SER   A 1 119 ? 11.281 11.093  19.321 1.00 18.44 ? 125 SER   A O   1 
ATOM   925  C  CB  . SER   A 1 119 ? 12.051 9.695   16.657 1.00 17.69 ? 125 SER   A CB  1 
ATOM   926  O  OG  . SER   A 1 119 ? 12.005 11.115  16.609 1.00 18.15 ? 125 SER   A OG  1 
ATOM   927  N  N   . THR   A 1 120 ? 9.831  9.359   19.197 1.00 21.46 ? 126 THR   A N   1 
ATOM   928  C  CA  . THR   A 1 120 ? 8.769  9.951   20.061 1.00 23.35 ? 126 THR   A CA  1 
ATOM   929  C  C   . THR   A 1 120 ? 7.848  8.805   20.573 1.00 24.77 ? 126 THR   A C   1 
ATOM   930  O  O   . THR   A 1 120 ? 8.096  7.643   20.283 1.00 24.35 ? 126 THR   A O   1 
ATOM   931  C  CB  . THR   A 1 120 ? 8.034  11.122  19.325 1.00 24.80 ? 126 THR   A CB  1 
ATOM   932  O  OG1 . THR   A 1 120 ? 7.226  11.899  20.252 1.00 26.83 ? 126 THR   A OG1 1 
ATOM   933  C  CG2 . THR   A 1 120 ? 7.227  10.640  18.142 1.00 25.09 ? 126 THR   A CG2 1 
ATOM   934  N  N   . GLY   A 1 121 ? 6.805  9.138   21.315 1.00 26.40 ? 127 GLY   A N   1 
ATOM   935  C  CA  . GLY   A 1 121 ? 5.836  8.196   21.843 1.00 28.95 ? 127 GLY   A CA  1 
ATOM   936  C  C   . GLY   A 1 121 ? 4.944  8.849   22.885 1.00 31.83 ? 127 GLY   A C   1 
ATOM   937  O  O   . GLY   A 1 121 ? 4.823  10.081  22.928 1.00 33.07 ? 127 GLY   A O   1 
ATOM   938  N  N   . GLY   A 1 122 ? 4.369  8.031   23.746 1.00 34.35 ? 128 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 122 ? 3.491  8.465   24.836 1.00 36.73 ? 128 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 122 ? 2.087  7.904   24.716 1.00 38.91 ? 128 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 122 ? 1.655  7.560   23.620 1.00 39.35 ? 128 GLY   A O   1 
ATOM   942  N  N   . ASN   A 1 123 ? 1.366  7.776   25.837 1.00 40.07 ? 129 ASN   A N   1 
ATOM   943  C  CA  . ASN   A 1 123 ? -0.006 7.259   25.858 1.00 41.11 ? 129 ASN   A CA  1 
ATOM   944  C  C   . ASN   A 1 123 ? -0.194 5.867   25.223 1.00 40.13 ? 129 ASN   A C   1 
ATOM   945  O  O   . ASN   A 1 123 ? -1.239 5.600   24.622 1.00 41.89 ? 129 ASN   A O   1 
ATOM   946  C  CB  . ASN   A 1 123 ? -0.963 8.263   25.229 1.00 44.79 ? 129 ASN   A CB  1 
ATOM   947  C  CG  . ASN   A 1 123 ? -0.978 9.583   25.960 1.00 52.13 ? 129 ASN   A CG  1 
ATOM   948  O  OD1 . ASN   A 1 123 ? -1.154 9.635   27.186 1.00 54.46 ? 129 ASN   A OD1 1 
ATOM   949  N  ND2 . ASN   A 1 123 ? -0.813 10.669  25.226 1.00 53.94 ? 129 ASN   A ND2 1 
ATOM   950  N  N   . GLY   A 1 124 ? 0.766  4.978   25.417 1.00 36.89 ? 130 GLY   A N   1 
ATOM   951  C  CA  . GLY   A 1 124 ? 0.669  3.635   24.861 1.00 35.17 ? 130 GLY   A CA  1 
ATOM   952  C  C   . GLY   A 1 124 ? 1.084  3.553   23.399 1.00 33.03 ? 130 GLY   A C   1 
ATOM   953  O  O   . GLY   A 1 124 ? 0.938  2.498   22.778 1.00 34.03 ? 130 GLY   A O   1 
ATOM   954  N  N   . LEU   A 1 125 ? 1.647  4.641   22.838 1.00 30.36 ? 131 LEU   A N   1 
ATOM   955  C  CA  . LEU   A 1 125 ? 2.151  4.685   21.467 1.00 28.23 ? 131 LEU   A CA  1 
ATOM   956  C  C   . LEU   A 1 125 ? 3.678  4.801   21.463 1.00 26.09 ? 131 LEU   A C   1 
ATOM   957  O  O   . LEU   A 1 125 ? 4.287  5.158   22.464 1.00 26.84 ? 131 LEU   A O   1 
ATOM   958  C  CB  . LEU   A 1 125 ? 1.573  5.916   20.710 1.00 28.99 ? 131 LEU   A CB  1 
ATOM   959  C  CG  . LEU   A 1 125 ? 0.054  5.941   20.570 1.00 32.12 ? 131 LEU   A CG  1 
ATOM   960  C  CD1 . LEU   A 1 125 ? -0.429 7.265   20.028 1.00 33.00 ? 131 LEU   A CD1 1 
ATOM   961  C  CD2 . LEU   A 1 125 ? -0.438 4.752   19.750 1.00 33.08 ? 131 LEU   A CD2 1 
ATOM   962  N  N   . VAL   A 1 126 ? 4.287  4.513   20.311 1.00 23.16 ? 132 VAL   A N   1 
ATOM   963  C  CA  . VAL   A 1 126 ? 5.706  4.675   20.067 1.00 21.20 ? 132 VAL   A CA  1 
ATOM   964  C  C   . VAL   A 1 126 ? 5.870  5.090   18.608 1.00 19.72 ? 132 VAL   A C   1 
ATOM   965  O  O   . VAL   A 1 126 ? 5.221  4.516   17.729 1.00 20.27 ? 132 VAL   A O   1 
ATOM   966  C  CB  . VAL   A 1 126 ? 6.547  3.420   20.452 1.00 20.81 ? 132 VAL   A CB  1 
ATOM   967  C  CG1 . VAL   A 1 126 ? 6.006  2.140   19.819 1.00 21.45 ? 132 VAL   A CG1 1 
ATOM   968  C  CG2 . VAL   A 1 126 ? 8.027  3.616   20.128 1.00 21.20 ? 132 VAL   A CG2 1 
ATOM   969  N  N   . GLY   A 1 127 ? 6.697  6.112   18.378 1.00 17.70 ? 133 GLY   A N   1 
ATOM   970  C  CA  . GLY   A 1 127 ? 6.991  6.665   17.070 1.00 17.39 ? 133 GLY   A CA  1 
ATOM   971  C  C   . GLY   A 1 127 ? 8.416  6.373   16.636 1.00 17.25 ? 133 GLY   A C   1 
ATOM   972  O  O   . GLY   A 1 127 ? 9.348  6.508   17.437 1.00 17.84 ? 133 GLY   A O   1 
ATOM   973  N  N   . PHE   A 1 128 ? 8.600  6.002   15.354 1.00 16.09 ? 134 PHE   A N   1 
ATOM   974  C  CA  . PHE   A 1 128 ? 9.897  5.652   14.793 1.00 15.72 ? 134 PHE   A CA  1 
ATOM   975  C  C   . PHE   A 1 128 ? 10.220 6.539   13.590 1.00 15.82 ? 134 PHE   A C   1 
ATOM   976  O  O   . PHE   A 1 128 ? 9.366  6.749   12.708 1.00 16.73 ? 134 PHE   A O   1 
ATOM   977  C  CB  . PHE   A 1 128 ? 9.905  4.173   14.324 1.00 14.89 ? 134 PHE   A CB  1 
ATOM   978  C  CG  . PHE   A 1 128 ? 9.450  3.159   15.356 1.00 15.48 ? 134 PHE   A CG  1 
ATOM   979  C  CD1 . PHE   A 1 128 ? 10.329 2.683   16.322 1.00 15.50 ? 134 PHE   A CD1 1 
ATOM   980  C  CD2 . PHE   A 1 128 ? 8.174  2.614   15.301 1.00 15.64 ? 134 PHE   A CD2 1 
ATOM   981  C  CE1 . PHE   A 1 128 ? 9.907  1.746   17.264 1.00 15.12 ? 134 PHE   A CE1 1 
ATOM   982  C  CE2 . PHE   A 1 128 ? 7.770  1.653   16.228 1.00 16.09 ? 134 PHE   A CE2 1 
ATOM   983  C  CZ  . PHE   A 1 128 ? 8.639  1.238   17.211 1.00 15.21 ? 134 PHE   A CZ  1 
ATOM   984  N  N   . ALA   A 1 129 ? 11.435 7.076   13.570 1.00 13.86 ? 135 ALA   A N   1 
ATOM   985  C  CA  . ALA   A 1 129 ? 11.901 7.837   12.444 1.00 14.07 ? 135 ALA   A CA  1 
ATOM   986  C  C   . ALA   A 1 129 ? 12.353 6.820   11.394 1.00 14.74 ? 135 ALA   A C   1 
ATOM   987  O  O   . ALA   A 1 129 ? 13.271 6.030   11.658 1.00 13.83 ? 135 ALA   A O   1 
ATOM   988  C  CB  . ALA   A 1 129 ? 13.082 8.736   12.858 1.00 14.30 ? 135 ALA   A CB  1 
ATOM   989  N  N   . ASP   A 1 130 ? 11.696 6.786   10.237 1.00 15.53 ? 136 ASP   A N   1 
ATOM   990  C  CA  . ASP   A 1 130 ? 12.092 5.855   9.161  1.00 17.34 ? 136 ASP   A CA  1 
ATOM   991  C  C   . ASP   A 1 130 ? 13.465 6.176   8.561  1.00 17.26 ? 136 ASP   A C   1 
ATOM   992  O  O   . ASP   A 1 130 ? 13.854 7.352   8.491  1.00 17.14 ? 136 ASP   A O   1 
ATOM   993  C  CB  . ASP   A 1 130 ? 11.043 5.893   8.048  1.00 20.58 ? 136 ASP   A CB  1 
ATOM   994  C  CG  . ASP   A 1 130 ? 11.264 4.894   6.954  1.00 26.18 ? 136 ASP   A CG  1 
ATOM   995  O  OD1 . ASP   A 1 130 ? 11.295 3.695   7.255  1.00 25.56 ? 136 ASP   A OD1 1 
ATOM   996  O  OD2 . ASP   A 1 130 ? 11.423 5.321   5.778  1.00 30.56 ? 136 ASP   A OD2 1 
ATOM   997  N  N   . VAL   A 1 131 ? 14.227 5.135   8.145  1.00 16.89 ? 137 VAL   A N   1 
ATOM   998  C  CA  . VAL   A 1 131 ? 15.518 5.351   7.440  1.00 17.95 ? 137 VAL   A CA  1 
ATOM   999  C  C   . VAL   A 1 131 ? 15.581 4.550   6.103  1.00 19.61 ? 137 VAL   A C   1 
ATOM   1000 O  O   . VAL   A 1 131 ? 16.637 4.529   5.457  1.00 21.50 ? 137 VAL   A O   1 
ATOM   1001 C  CB  . VAL   A 1 131 ? 16.780 5.031   8.285  1.00 17.42 ? 137 VAL   A CB  1 
ATOM   1002 C  CG1 . VAL   A 1 131 ? 16.865 5.904   9.544  1.00 18.42 ? 137 VAL   A CG1 1 
ATOM   1003 C  CG2 . VAL   A 1 131 ? 16.865 3.534   8.621  1.00 16.64 ? 137 VAL   A CG2 1 
ATOM   1004 N  N   . ARG   A 1 132 ? 14.513 3.818   5.737  1.00 18.98 ? 138 ARG   A N   1 
ATOM   1005 C  CA  . ARG   A 1 132 ? 14.519 2.972   4.546  1.00 20.13 ? 138 ARG   A CA  1 
ATOM   1006 C  C   . ARG   A 1 132 ? 14.624 3.726   3.211  1.00 22.75 ? 138 ARG   A C   1 
ATOM   1007 O  O   . ARG   A 1 132 ? 15.011 3.126   2.200  1.00 23.57 ? 138 ARG   A O   1 
ATOM   1008 C  CB  . ARG   A 1 132 ? 13.308 2.042   4.526  1.00 19.98 ? 138 ARG   A CB  1 
ATOM   1009 C  CG  . ARG   A 1 132 ? 13.246 1.149   5.753  1.00 20.12 ? 138 ARG   A CG  1 
ATOM   1010 C  CD  . ARG   A 1 132 ? 11.967 0.356   5.676  1.00 19.89 ? 138 ARG   A CD  1 
ATOM   1011 N  NE  . ARG   A 1 132 ? 10.863 1.224   6.075  1.00 21.77 ? 138 ARG   A NE  1 
ATOM   1012 C  CZ  . ARG   A 1 132 ? 9.609  0.828   6.209  1.00 22.06 ? 138 ARG   A CZ  1 
ATOM   1013 N  NH1 . ARG   A 1 132 ? 9.266  -0.419  5.910  1.00 21.50 ? 138 ARG   A NH1 1 
ATOM   1014 N  NH2 . ARG   A 1 132 ? 8.676  1.685   6.606  1.00 19.88 ? 138 ARG   A NH2 1 
ATOM   1015 N  N   . ASP   A 1 133 ? 14.306 5.024   3.198  1.00 23.70 ? 139 ASP   A N   1 
ATOM   1016 C  CA  . ASP   A 1 133 ? 14.411 5.814   1.967  1.00 24.91 ? 139 ASP   A CA  1 
ATOM   1017 C  C   . ASP   A 1 133 ? 15.820 6.393   1.746  1.00 26.45 ? 139 ASP   A C   1 
ATOM   1018 O  O   . ASP   A 1 133 ? 16.106 6.898   0.649  1.00 27.41 ? 139 ASP   A O   1 
ATOM   1019 C  CB  . ASP   A 1 133 ? 13.377 6.947   1.955  1.00 25.74 ? 139 ASP   A CB  1 
ATOM   1020 C  CG  . ASP   A 1 133 ? 13.593 7.963   3.057  1.00 27.56 ? 139 ASP   A CG  1 
ATOM   1021 O  OD1 . ASP   A 1 133 ? 13.924 7.545   4.202  1.00 25.92 ? 139 ASP   A OD1 1 
ATOM   1022 O  OD2 . ASP   A 1 133 ? 13.429 9.174   2.786  1.00 28.21 ? 139 ASP   A OD2 1 
ATOM   1023 N  N   . LEU   A 1 134 ? 16.694 6.372   2.784  1.00 26.58 ? 140 LEU   A N   1 
ATOM   1024 C  CA  . LEU   A 1 134 ? 18.059 6.906   2.652  1.00 27.23 ? 140 LEU   A CA  1 
ATOM   1025 C  C   . LEU   A 1 134 ? 18.940 5.893   1.949  1.00 28.62 ? 140 LEU   A C   1 
ATOM   1026 O  O   . LEU   A 1 134 ? 19.783 5.241   2.580  1.00 27.92 ? 140 LEU   A O   1 
ATOM   1027 C  CB  . LEU   A 1 134 ? 18.645 7.293   4.013  1.00 26.62 ? 140 LEU   A CB  1 
ATOM   1028 C  CG  . LEU   A 1 134 ? 17.769 8.249   4.839  1.00 27.34 ? 140 LEU   A CG  1 
ATOM   1029 C  CD1 . LEU   A 1 134 ? 18.372 8.516   6.195  1.00 27.41 ? 140 LEU   A CD1 1 
ATOM   1030 C  CD2 . LEU   A 1 134 ? 17.494 9.549   4.081  1.00 27.40 ? 140 LEU   A CD2 1 
ATOM   1031 N  N   . LEU   A 1 135 ? 18.741 5.754   0.623  1.00 30.07 ? 141 LEU   A N   1 
ATOM   1032 C  CA  . LEU   A 1 135 ? 19.474 4.771   -0.185 1.00 31.73 ? 141 LEU   A CA  1 
ATOM   1033 C  C   . LEU   A 1 135 ? 20.980 5.006   -0.197 1.00 32.49 ? 141 LEU   A C   1 
ATOM   1034 O  O   . LEU   A 1 135 ? 21.742 4.048   -0.329 1.00 33.59 ? 141 LEU   A O   1 
ATOM   1035 C  CB  . LEU   A 1 135 ? 18.946 4.715   -1.626 1.00 32.41 ? 141 LEU   A CB  1 
ATOM   1036 C  CG  . LEU   A 1 135 ? 17.439 4.647   -1.845 1.00 34.12 ? 141 LEU   A CG  1 
ATOM   1037 C  CD1 . LEU   A 1 135 ? 17.145 4.393   -3.332 1.00 34.94 ? 141 LEU   A CD1 1 
ATOM   1038 C  CD2 . LEU   A 1 135 ? 16.767 3.560   -0.981 1.00 34.63 ? 141 LEU   A CD2 1 
ATOM   1039 N  N   . TRP   A 1 136 ? 21.407 6.263   -0.017 1.00 32.19 ? 142 TRP   A N   1 
ATOM   1040 C  CA  . TRP   A 1 136 ? 22.824 6.633   0.005  1.00 33.00 ? 142 TRP   A CA  1 
ATOM   1041 C  C   . TRP   A 1 136 ? 23.600 6.051   1.190  1.00 34.67 ? 142 TRP   A C   1 
ATOM   1042 O  O   . TRP   A 1 136 ? 24.828 5.996   1.144  1.00 34.74 ? 142 TRP   A O   1 
ATOM   1043 C  CB  . TRP   A 1 136 ? 23.009 8.153   -0.078 1.00 32.01 ? 142 TRP   A CB  1 
ATOM   1044 C  CG  . TRP   A 1 136 ? 22.292 8.913   0.999  1.00 31.00 ? 142 TRP   A CG  1 
ATOM   1045 C  CD1 . TRP   A 1 136 ? 21.023 9.410   0.948  1.00 31.34 ? 142 TRP   A CD1 1 
ATOM   1046 C  CD2 . TRP   A 1 136 ? 22.822 9.291   2.272  1.00 30.62 ? 142 TRP   A CD2 1 
ATOM   1047 N  NE1 . TRP   A 1 136 ? 20.715 10.037  2.132  1.00 31.65 ? 142 TRP   A NE1 1 
ATOM   1048 C  CE2 . TRP   A 1 136 ? 21.805 9.980   2.962  1.00 31.37 ? 142 TRP   A CE2 1 
ATOM   1049 C  CE3 . TRP   A 1 136 ? 24.050 9.083   2.915  1.00 30.92 ? 142 TRP   A CE3 1 
ATOM   1050 C  CZ2 . TRP   A 1 136 ? 21.987 10.481  4.250  1.00 31.70 ? 142 TRP   A CZ2 1 
ATOM   1051 C  CZ3 . TRP   A 1 136 ? 24.226 9.579   4.192  1.00 31.50 ? 142 TRP   A CZ3 1 
ATOM   1052 C  CH2 . TRP   A 1 136 ? 23.215 10.294  4.834  1.00 31.62 ? 142 TRP   A CH2 1 
ATOM   1053 N  N   . LEU   A 1 137 ? 22.900 5.600   2.247  1.00 35.46 ? 143 LEU   A N   1 
ATOM   1054 C  CA  . LEU   A 1 137 ? 23.566 4.963   3.385  1.00 37.03 ? 143 LEU   A CA  1 
ATOM   1055 C  C   . LEU   A 1 137 ? 24.356 3.715   2.957  1.00 42.00 ? 143 LEU   A C   1 
ATOM   1056 O  O   . LEU   A 1 137 ? 25.332 3.364   3.617  1.00 42.39 ? 143 LEU   A O   1 
ATOM   1057 C  CB  . LEU   A 1 137 ? 22.530 4.565   4.463  1.00 35.04 ? 143 LEU   A CB  1 
ATOM   1058 C  CG  . LEU   A 1 137 ? 21.987 5.722   5.319  1.00 33.88 ? 143 LEU   A CG  1 
ATOM   1059 C  CD1 . LEU   A 1 137 ? 20.891 5.226   6.274  1.00 33.19 ? 143 LEU   A CD1 1 
ATOM   1060 C  CD2 . LEU   A 1 137 ? 23.113 6.409   6.106  1.00 33.32 ? 143 LEU   A CD2 1 
ATOM   1061 N  N   . ASP   A 1 138 ? 23.934 3.064   1.842  1.00 45.53 ? 144 ASP   A N   1 
ATOM   1062 C  CA  . ASP   A 1 138 ? 24.493 1.827   1.305  1.00 49.72 ? 144 ASP   A CA  1 
ATOM   1063 C  C   . ASP   A 1 138 ? 25.540 1.953   0.229  1.00 53.53 ? 144 ASP   A C   1 
ATOM   1064 O  O   . ASP   A 1 138 ? 26.131 0.943   -0.126 1.00 54.65 ? 144 ASP   A O   1 
ATOM   1065 C  CB  . ASP   A 1 138 ? 23.359 0.965   0.758  1.00 51.96 ? 144 ASP   A CB  1 
ATOM   1066 C  CG  . ASP   A 1 138 ? 22.747 0.122   1.823  1.00 55.63 ? 144 ASP   A CG  1 
ATOM   1067 O  OD1 . ASP   A 1 138 ? 23.506 -0.561  2.537  1.00 56.11 ? 144 ASP   A OD1 1 
ATOM   1068 O  OD2 . ASP   A 1 138 ? 21.511 0.146   1.954  1.00 58.06 ? 144 ASP   A OD2 1 
ATOM   1069 N  N   . GLU   A 1 139 ? 25.744 3.145   -0.330 1.00 55.54 ? 145 GLU   A N   1 
ATOM   1070 C  CA  . GLU   A 1 139 ? 26.717 3.330   -1.405 1.00 58.05 ? 145 GLU   A CA  1 
ATOM   1071 C  C   . GLU   A 1 139 ? 27.615 4.549   -1.146 1.00 59.52 ? 145 GLU   A C   1 
ATOM   1072 O  O   . GLU   A 1 139 ? 28.498 4.863   -1.961 1.00 60.38 ? 145 GLU   A O   1 
ATOM   1073 C  CB  . GLU   A 1 139 ? 25.989 3.474   -2.753 1.00 61.15 ? 145 GLU   A CB  1 
ATOM   1074 C  CG  . GLU   A 1 139 ? 25.040 4.664   -2.793 1.00 66.47 ? 145 GLU   A CG  1 
ATOM   1075 C  CD  . GLU   A 1 139 ? 23.683 4.391   -3.418 1.00 73.67 ? 145 GLU   A CD  1 
ATOM   1076 O  OE1 . GLU   A 1 139 ? 22.932 5.367   -3.650 1.00 74.57 ? 145 GLU   A OE1 1 
ATOM   1077 O  OE2 . GLU   A 1 139 ? 23.366 3.203   -3.667 1.00 76.15 ? 145 GLU   A OE2 1 
HETATM 1078 N  N1  . A1B14 B 2 .   ? 10.017 14.332  22.572 1.00 35.46 ? 201 A1B14 A N1  1 
HETATM 1079 C  C4  . A1B14 B 2 .   ? 11.258 14.818  23.193 1.00 35.13 ? 201 A1B14 A C4  1 
HETATM 1080 C  C5  . A1B14 B 2 .   ? 9.090  13.575  23.191 1.00 36.37 ? 201 A1B14 A C5  1 
HETATM 1081 C  C6  . A1B14 B 2 .   ? 9.227  13.403  24.704 1.00 36.23 ? 201 A1B14 A C6  1 
HETATM 1082 C  C7  . A1B14 B 2 .   ? 7.081  13.097  25.903 1.00 37.32 ? 201 A1B14 A C7  1 
HETATM 1083 C  C8  . A1B14 B 2 .   ? 5.872  12.170  25.893 1.00 36.88 ? 201 A1B14 A C8  1 
HETATM 1084 C  C10 . A1B14 B 2 .   ? 7.226  8.904   25.309 1.00 35.38 ? 201 A1B14 A C10 1 
HETATM 1085 C  C13 . A1B14 B 2 .   ? 9.247  10.498  24.205 1.00 35.26 ? 201 A1B14 A C13 1 
HETATM 1086 C  C15 . A1B14 B 2 .   ? 9.815  14.735  21.177 1.00 34.75 ? 201 A1B14 A C15 1 
HETATM 1087 CL CL  . A1B14 B 2 .   ? 10.461 8.385   23.033 1.00 34.92 ? 201 A1B14 A CL  1 
HETATM 1088 C  C12 . A1B14 B 2 .   ? 9.204  9.131   23.984 1.00 34.84 ? 201 A1B14 A C12 1 
HETATM 1089 C  C11 . A1B14 B 2 .   ? 8.207  8.336   24.513 1.00 35.06 ? 201 A1B14 A C11 1 
HETATM 1090 C  C14 . A1B14 B 2 .   ? 8.240  11.057  24.989 1.00 35.72 ? 201 A1B14 A C14 1 
HETATM 1091 C  C9  . A1B14 B 2 .   ? 7.235  10.269  25.535 1.00 35.55 ? 201 A1B14 A C9  1 
HETATM 1092 O  O2  . A1B14 B 2 .   ? 6.205  10.807  26.263 1.00 36.08 ? 201 A1B14 A O2  1 
HETATM 1093 N  N2  . A1B14 B 2 .   ? 8.229  12.487  25.220 1.00 36.46 ? 201 A1B14 A N2  1 
HETATM 1094 O  O1  . A1B14 B 2 .   ? 8.191  13.016  22.577 1.00 37.36 ? 201 A1B14 A O1  1 
HETATM 1095 C  C3  . A1B14 B 2 .   ? 12.477 14.453  22.359 1.00 34.53 ? 201 A1B14 A C3  1 
HETATM 1096 C  C2  . A1B14 B 2 .   ? 12.280 14.832  20.887 1.00 33.92 ? 201 A1B14 A C2  1 
HETATM 1097 C  C1  . A1B14 B 2 .   ? 10.980 14.244  20.313 1.00 33.57 ? 201 A1B14 A C1  1 
HETATM 1098 C  C   . A1B14 B 2 .   ? 10.802 14.622  18.853 1.00 32.53 ? 201 A1B14 A C   1 
HETATM 1099 O  O   . A1B14 B 2 .   ? 10.489 15.771  18.523 1.00 32.37 ? 201 A1B14 A O   1 
HETATM 1100 N  N   . A1B14 B 2 .   ? 10.985 13.649  17.980 1.00 31.72 ? 201 A1B14 A N   1 
HETATM 1101 ZN ZN  . ZN    C 3 .   ? 11.001 -5.319  5.606  1.00 26.20 2 202 ZN    A ZN  1 
HETATM 1102 S  S   . DMS   D 4 .   ? 14.614 20.677  7.850  0.00 36.50 ? 203 DMS   A S   1 
HETATM 1103 O  O   . DMS   D 4 .   ? 13.749 20.802  9.069  0.00 28.33 ? 203 DMS   A O   1 
HETATM 1104 C  C1  . DMS   D 4 .   ? 13.518 20.628  6.406  0.00 33.03 ? 203 DMS   A C1  1 
HETATM 1105 C  C2  . DMS   D 4 .   ? 15.304 22.317  7.500  0.00 32.97 ? 203 DMS   A C2  1 
HETATM 1106 S  S   . DMS   E 4 .   ? 19.725 -0.729  20.033 1.00 71.70 ? 204 DMS   A S   1 
HETATM 1107 O  O   . DMS   E 4 .   ? 18.255 -0.770  19.730 1.00 71.11 ? 204 DMS   A O   1 
HETATM 1108 C  C1  . DMS   E 4 .   ? 19.962 -0.213  21.761 1.00 71.74 ? 204 DMS   A C1  1 
HETATM 1109 C  C2  . DMS   E 4 .   ? 20.452 0.782   19.328 1.00 71.66 ? 204 DMS   A C2  1 
HETATM 1110 O  O   . HOH   F 5 .   ? 19.998 21.991  7.932  1.00 23.29 ? 301 HOH   A O   1 
HETATM 1111 O  O   . HOH   F 5 .   ? 20.022 8.263   18.982 1.00 25.86 ? 302 HOH   A O   1 
HETATM 1112 O  O   . HOH   F 5 .   ? 10.595 7.412   4.660  1.00 29.15 ? 303 HOH   A O   1 
HETATM 1113 O  O   . HOH   F 5 .   ? 23.479 21.471  7.974  1.00 28.84 ? 304 HOH   A O   1 
HETATM 1114 O  O   . HOH   F 5 .   ? 22.961 -1.959  4.557  1.00 34.09 ? 305 HOH   A O   1 
HETATM 1115 O  O   . HOH   F 5 .   ? 17.945 22.857  21.951 1.00 31.78 ? 306 HOH   A O   1 
HETATM 1116 O  O   . HOH   F 5 .   ? 8.425  19.492  18.390 1.00 32.11 ? 307 HOH   A O   1 
HETATM 1117 O  O   . HOH   F 5 .   ? 14.658 2.168   23.254 1.00 18.00 ? 308 HOH   A O   1 
HETATM 1118 O  O   . HOH   F 5 .   ? 8.952  1.762   2.922  1.00 23.99 ? 309 HOH   A O   1 
HETATM 1119 O  O   . HOH   F 5 .   ? 17.757 20.643  9.752  1.00 25.40 ? 310 HOH   A O   1 
HETATM 1120 O  O   . HOH   F 5 .   ? 10.218 18.247  20.447 1.00 33.51 ? 311 HOH   A O   1 
HETATM 1121 O  O   . HOH   F 5 .   ? 7.989  -4.624  0.892  1.00 28.52 ? 312 HOH   A O   1 
HETATM 1122 O  O   . HOH   F 5 .   ? 30.534 20.209  10.723 1.00 38.87 ? 313 HOH   A O   1 
HETATM 1123 O  O   . HOH   F 5 .   ? 0.453  -1.108  16.501 1.00 18.25 ? 314 HOH   A O   1 
HETATM 1124 O  O   . HOH   F 5 .   ? 11.116 -5.918  31.821 1.00 35.93 ? 315 HOH   A O   1 
HETATM 1125 O  O   . HOH   F 5 .   ? 3.976  5.030   25.127 1.00 26.54 ? 316 HOH   A O   1 
HETATM 1126 O  O   . HOH   F 5 .   ? 11.253 10.972  11.456 1.00 13.13 ? 317 HOH   A O   1 
HETATM 1127 O  O   . HOH   F 5 .   ? 12.992 9.758   9.444  1.00 13.12 ? 318 HOH   A O   1 
HETATM 1128 O  O   . HOH   F 5 .   ? 10.400 3.954   3.634  1.00 23.48 ? 319 HOH   A O   1 
HETATM 1129 O  O   . HOH   F 5 .   ? 10.946 1.555   33.498 1.00 26.28 ? 320 HOH   A O   1 
HETATM 1130 O  O   . HOH   F 5 .   ? 7.049  2.709   32.921 1.00 29.43 ? 321 HOH   A O   1 
HETATM 1131 O  O   . HOH   F 5 .   ? 5.252  7.023   28.382 1.00 37.52 ? 322 HOH   A O   1 
HETATM 1132 O  O   . HOH   F 5 .   ? 9.650  3.778   33.902 1.00 36.36 ? 323 HOH   A O   1 
HETATM 1133 O  O   . HOH   F 5 .   ? 6.561  -6.755  29.280 1.00 36.35 ? 324 HOH   A O   1 
HETATM 1134 O  O   . HOH   F 5 .   ? 17.712 2.032   23.191 1.00 29.78 ? 325 HOH   A O   1 
HETATM 1135 O  O   . HOH   F 5 .   ? 24.692 7.015   20.401 1.00 45.00 ? 326 HOH   A O   1 
HETATM 1136 O  O   . HOH   F 5 .   ? 12.699 24.644  22.148 1.00 25.24 ? 327 HOH   A O   1 
HETATM 1137 O  O   . HOH   F 5 .   ? 14.730 -5.229  17.148 1.00 18.74 ? 328 HOH   A O   1 
HETATM 1138 O  O   . HOH   F 5 .   ? 5.084  -2.097  29.587 1.00 43.93 ? 329 HOH   A O   1 
HETATM 1139 O  O   . HOH   F 5 .   ? 4.138  -5.861  6.517  1.00 32.22 ? 330 HOH   A O   1 
HETATM 1140 O  O   . HOH   F 5 .   ? 5.446  -2.479  24.354 1.00 23.82 ? 331 HOH   A O   1 
HETATM 1141 O  O   . HOH   F 5 .   ? 17.913 18.317  16.985 1.00 24.29 ? 332 HOH   A O   1 
HETATM 1142 O  O   . HOH   F 5 .   ? 9.069  20.431  10.672 1.00 29.12 ? 333 HOH   A O   1 
HETATM 1143 O  O   . HOH   F 5 .   ? 2.451  8.802   28.318 1.00 42.29 ? 334 HOH   A O   1 
HETATM 1144 O  O   . HOH   F 5 .   ? -2.078 0.230   8.236  1.00 38.31 ? 335 HOH   A O   1 
HETATM 1145 O  O   . HOH   F 5 .   ? 14.682 11.973  24.139 1.00 33.64 ? 336 HOH   A O   1 
HETATM 1146 O  O   . HOH   F 5 .   ? 6.652  12.068  5.518  1.00 28.44 ? 337 HOH   A O   1 
HETATM 1147 O  O   . HOH   F 5 .   ? 13.013 18.656  26.969 1.00 41.65 ? 338 HOH   A O   1 
HETATM 1148 O  O   . HOH   F 5 .   ? 13.777 -12.226 4.113  1.00 44.56 ? 339 HOH   A O   1 
HETATM 1149 O  O   . HOH   F 5 .   ? 30.808 20.259  16.997 1.00 47.21 ? 340 HOH   A O   1 
HETATM 1150 O  O   . HOH   F 5 .   ? 10.943 16.439  5.090  1.00 57.23 ? 341 HOH   A O   1 
HETATM 1151 O  O   . HOH   F 5 .   ? 30.099 10.477  18.937 1.00 32.24 ? 342 HOH   A O   1 
HETATM 1152 O  O   . HOH   F 5 .   ? 19.339 23.274  15.386 1.00 26.50 ? 343 HOH   A O   1 
HETATM 1153 O  O   . HOH   F 5 .   ? 22.563 17.874  19.572 1.00 40.40 ? 344 HOH   A O   1 
HETATM 1154 O  O   . HOH   F 5 .   ? 7.831  25.461  14.474 1.00 40.41 ? 345 HOH   A O   1 
HETATM 1155 O  O   . HOH   F 5 .   ? 1.581  -3.305  17.686 1.00 25.82 ? 346 HOH   A O   1 
HETATM 1156 O  O   . HOH   F 5 .   ? 11.740 20.645  12.346 1.00 21.36 ? 347 HOH   A O   1 
HETATM 1157 O  O   . HOH   F 5 .   ? 5.668  1.236   7.196  1.00 31.76 ? 348 HOH   A O   1 
HETATM 1158 O  O   . HOH   F 5 .   ? 8.851  -8.158  9.165  1.00 34.69 ? 349 HOH   A O   1 
HETATM 1159 O  O   . HOH   F 5 .   ? 2.632  2.340   27.876 1.00 35.81 ? 350 HOH   A O   1 
HETATM 1160 O  O   . HOH   F 5 .   ? 16.066 23.196  14.152 1.00 60.30 ? 351 HOH   A O   1 
HETATM 1161 O  O   . HOH   F 5 .   ? 18.289 11.814  1.512  1.00 39.00 ? 352 HOH   A O   1 
HETATM 1162 O  O   . HOH   F 5 .   ? 22.270 18.403  6.037  1.00 20.82 ? 353 HOH   A O   1 
HETATM 1163 O  O   . HOH   F 5 .   ? 21.798 8.274   21.073 1.00 33.40 ? 354 HOH   A O   1 
HETATM 1164 O  O   . HOH   F 5 .   ? 13.980 13.841  3.287  1.00 33.17 ? 355 HOH   A O   1 
HETATM 1165 O  O   . HOH   F 5 .   ? 2.219  14.838  19.806 1.00 52.14 ? 356 HOH   A O   1 
HETATM 1166 O  O   . HOH   F 5 .   ? 10.818 15.087  2.670  1.00 41.12 ? 357 HOH   A O   1 
HETATM 1167 O  O   . HOH   F 5 .   ? 15.750 -5.336  1.732  1.00 30.02 ? 358 HOH   A O   1 
HETATM 1168 O  O   . HOH   F 5 .   ? 17.861 9.169   25.770 1.00 35.21 ? 359 HOH   A O   1 
HETATM 1169 O  O   . HOH   F 5 .   ? 36.604 6.374   6.231  1.00 61.82 ? 360 HOH   A O   1 
HETATM 1170 O  O   . HOH   F 5 .   ? 2.263  -5.943  20.849 1.00 41.84 ? 361 HOH   A O   1 
HETATM 1171 O  O   . HOH   F 5 .   ? 28.472 21.628  18.612 1.00 38.26 ? 362 HOH   A O   1 
HETATM 1172 O  O   . HOH   F 5 .   ? -0.764 14.661  7.627  1.00 52.72 ? 363 HOH   A O   1 
HETATM 1173 O  O   . HOH   F 5 .   ? 4.037  11.926  19.327 1.00 38.84 ? 364 HOH   A O   1 
HETATM 1174 O  O   . HOH   F 5 .   ? 30.121 4.646   3.535  1.00 62.95 ? 365 HOH   A O   1 
HETATM 1175 O  O   . HOH   F 5 .   ? 12.034 -8.632  13.214 1.00 35.08 ? 366 HOH   A O   1 
HETATM 1176 O  O   . HOH   F 5 .   ? 1.747  12.492  5.121  1.00 39.92 ? 367 HOH   A O   1 
HETATM 1177 O  O   . HOH   F 5 .   ? 20.612 21.561  17.728 1.00 31.87 ? 368 HOH   A O   1 
HETATM 1178 O  O   . HOH   F 5 .   ? -1.968 -5.163  15.593 1.00 47.66 ? 369 HOH   A O   1 
HETATM 1179 O  O   . HOH   F 5 .   ? 22.346 15.874  23.716 1.00 35.06 ? 370 HOH   A O   1 
HETATM 1180 O  O   . HOH   F 5 .   ? 8.166  -7.261  2.609  1.00 47.51 ? 371 HOH   A O   1 
HETATM 1181 O  O   . HOH   F 5 .   ? 18.885 8.346   -2.067 1.00 35.19 ? 372 HOH   A O   1 
HETATM 1182 O  O   . HOH   F 5 .   ? 2.041  0.058   26.768 1.00 29.62 ? 373 HOH   A O   1 
HETATM 1183 O  O   . HOH   F 5 .   ? 8.952  5.760   2.974  1.00 36.30 ? 374 HOH   A O   1 
HETATM 1184 O  O   . HOH   F 5 .   ? 4.745  14.615  21.636 1.00 42.45 ? 375 HOH   A O   1 
HETATM 1185 O  O   . HOH   F 5 .   ? 26.659 -2.474  15.366 1.00 31.79 ? 376 HOH   A O   1 
HETATM 1186 O  O   . HOH   F 5 .   ? -1.368 14.611  12.045 1.00 32.99 ? 377 HOH   A O   1 
HETATM 1187 O  O   . HOH   F 5 .   ? -0.960 2.486   4.294  1.00 43.06 ? 378 HOH   A O   1 
HETATM 1188 O  O   . HOH   F 5 .   ? 12.216 23.135  13.862 1.00 46.68 ? 379 HOH   A O   1 
HETATM 1189 O  O   . HOH   F 5 .   ? 0.873  -2.708  23.762 1.00 33.95 ? 380 HOH   A O   1 
HETATM 1190 O  O   . HOH   F 5 .   ? 3.695  -3.994  23.202 1.00 29.76 ? 381 HOH   A O   1 
HETATM 1191 O  O   . HOH   F 5 .   ? 9.615  -9.455  12.651 1.00 32.57 ? 382 HOH   A O   1 
HETATM 1192 O  O   . HOH   F 5 .   ? 10.787 16.842  26.427 1.00 44.16 ? 383 HOH   A O   1 
HETATM 1193 O  O   . HOH   F 5 .   ? 9.491  24.463  12.641 1.00 40.47 ? 384 HOH   A O   1 
HETATM 1194 O  O   . HOH   F 5 .   ? 1.029  10.680  18.107 1.00 43.25 ? 385 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   ? 0.7878 0.3011 0.4003 -0.0656 -0.1987 0.0250  7   SER   A N   
2    C  CA  . SER   A 1   ? 0.7412 0.3014 0.4510 -0.0667 -0.2267 0.0392  7   SER   A CA  
3    C  C   . SER   A 1   ? 0.6629 0.3008 0.4694 -0.0505 -0.2093 0.0381  7   SER   A C   
4    O  O   . SER   A 1   ? 0.6642 0.3107 0.4587 -0.0465 -0.1942 0.0320  7   SER   A O   
5    C  CB  . SER   A 1   ? 0.7905 0.2979 0.4901 -0.0979 -0.2867 0.0637  7   SER   A CB  
6    O  OG  . SER   A 1   ? 0.8314 0.3284 0.5282 -0.1091 -0.3031 0.0719  7   SER   A OG  
7    N  N   . GLY   A 2   ? 0.5907 0.2769 0.4868 -0.0428 -0.2090 0.0440  8   GLY   A N   
8    C  CA  . GLY   A 2   ? 0.5210 0.2672 0.5020 -0.0303 -0.1865 0.0422  8   GLY   A CA  
9    C  C   . GLY   A 2   ? 0.4566 0.2460 0.4943 -0.0164 -0.1600 0.0361  8   GLY   A C   
10   O  O   . GLY   A 2   ? 0.4688 0.2558 0.4726 -0.0103 -0.1486 0.0272  8   GLY   A O   
11   N  N   . ALA   A 3   ? 0.3845 0.2076 0.5072 -0.0126 -0.1474 0.0416  9   ALA   A N   
12   C  CA  . ALA   A 3   ? 0.3485 0.2013 0.5196 -0.0028 -0.1189 0.0361  9   ALA   A CA  
13   C  C   . ALA   A 3   ? 0.3236 0.2036 0.5461 0.0025  -0.0821 0.0302  9   ALA   A C   
14   O  O   . ALA   A 3   ? 0.3061 0.1853 0.5544 -0.0011 -0.0850 0.0365  9   ALA   A O   
15   C  CB  . ALA   A 3   ? 0.3303 0.1743 0.5623 -0.0085 -0.1440 0.0563  9   ALA   A CB  
16   N  N   . ILE   A 4   ? 0.3106 0.2074 0.5448 0.0086  -0.0469 0.0190  10  ILE   A N   
17   C  CA  . ILE   A 4   ? 0.2967 0.2024 0.5663 0.0092  -0.0065 0.0123  10  ILE   A CA  
18   C  C   . ILE   A 4   ? 0.2914 0.1943 0.6474 0.0108  0.0100  0.0242  10  ILE   A C   
19   O  O   . ILE   A 4   ? 0.2808 0.1845 0.6423 0.0133  0.0118  0.0246  10  ILE   A O   
20   C  CB  . ILE   A 4   ? 0.3046 0.2175 0.5118 0.0084  0.0241  -0.0078 10  ILE   A CB  
21   C  CG1 . ILE   A 4   ? 0.3057 0.2247 0.4429 0.0082  0.0102  -0.0146 10  ILE   A CG1 
22   C  CG2 . ILE   A 4   ? 0.3077 0.2124 0.5336 0.0030  0.0667  -0.0155 10  ILE   A CG2 
23   C  CD1 . ILE   A 4   ? 0.3148 0.2430 0.4043 0.0067  0.0231  -0.0236 10  ILE   A CD1 
24   N  N   . TYR   A 5   ? 0.2905 0.1896 0.7195 0.0100  0.0255  0.0354  11  TYR   A N   
25   C  CA  . TYR   A 5   ? 0.2858 0.1800 0.8143 0.0128  0.0487  0.0511  11  TYR   A CA  
26   C  C   . TYR   A 5   ? 0.3080 0.1873 0.8418 0.0129  0.1134  0.0359  11  TYR   A C   
27   O  O   . TYR   A 5   ? 0.3106 0.1825 0.8628 0.0111  0.1331  0.0355  11  TYR   A O   
28   C  CB  . TYR   A 5   ? 0.2581 0.1534 0.8828 0.0103  0.0178  0.0830  11  TYR   A CB  
29   C  CG  . TYR   A 5   ? 0.2704 0.1646 0.8805 0.0033  -0.0481 0.1006  11  TYR   A CG  
30   C  CD1 . TYR   A 5   ? 0.2750 0.1677 0.9205 0.0026  -0.0675 0.1154  11  TYR   A CD1 
31   C  CD2 . TYR   A 5   ? 0.3010 0.1873 0.8501 -0.0049 -0.0891 0.1014  11  TYR   A CD2 
32   C  CE1 . TYR   A 5   ? 0.2975 0.1771 0.9140 -0.0083 -0.1281 0.1307  11  TYR   A CE1 
33   C  CE2 . TYR   A 5   ? 0.3318 0.2000 0.8481 -0.0162 -0.1462 0.1161  11  TYR   A CE2 
34   C  CZ  . TYR   A 5   ? 0.3351 0.1980 0.8839 -0.0192 -0.1668 0.1312  11  TYR   A CZ  
35   O  OH  . TYR   A 5   ? 0.3816 0.2154 0.8844 -0.0347 -0.2232 0.1451  11  TYR   A OH  
36   N  N   . VAL   A 6   ? 0.3263 0.1945 0.8301 0.0123  0.1464  0.0219  12  VAL   A N   
37   C  CA  . VAL   A 6   ? 0.3468 0.1831 0.8333 0.0066  0.2112  0.0057  12  VAL   A CA  
38   C  C   . VAL   A 6   ? 0.3323 0.1508 0.8852 0.0105  0.2480  0.0137  12  VAL   A C   
39   O  O   . VAL   A 6   ? 0.3349 0.1620 0.8701 0.0122  0.2329  0.0129  12  VAL   A O   
40   C  CB  . VAL   A 6   ? 0.4043 0.2305 0.7654 -0.0054 0.2196  -0.0204 12  VAL   A CB  
41   C  CG1 . VAL   A 6   ? 0.4162 0.2637 0.7258 -0.0043 0.1844  -0.0235 12  VAL   A CG1 
42   C  CG2 . VAL   A 6   ? 0.4470 0.2241 0.7750 -0.0183 0.2843  -0.0358 12  VAL   A CG2 
43   N  N   . GLY   A 7   ? 0.3081 0.1015 0.9477 0.0132  0.2979  0.0242  13  GLY   A N   
44   C  CA  . GLY   A 7   ? 0.3092 0.0813 1.0297 0.0185  0.3422  0.0356  13  GLY   A CA  
45   C  C   . GLY   A 7   ? 0.2943 0.1016 1.0944 0.0277  0.2920  0.0624  13  GLY   A C   
46   O  O   . GLY   A 7   ? 0.2896 0.1276 1.1363 0.0302  0.2340  0.0842  13  GLY   A O   
47   N  N   . ASN   A 8   ? 0.2916 0.0908 1.0907 0.0294  0.3078  0.0600  14  ASN   A N   
48   C  CA  . ASN   A 8   ? 0.2573 0.0861 1.1227 0.0359  0.2589  0.0846  14  ASN   A CA  
49   C  C   . ASN   A 8   ? 0.2583 0.1123 1.0178 0.0321  0.1960  0.0713  14  ASN   A C   
50   O  O   . ASN   A 8   ? 0.2522 0.1180 1.0231 0.0346  0.1691  0.0797  14  ASN   A O   
51   C  CB  . ASN   A 8   ? 0.2889 0.0972 1.2134 0.0407  0.3070  0.0908  14  ASN   A CB  
52   C  CG  . ASN   A 8   ? 0.3536 0.1327 1.4023 0.0468  0.3753  0.1096  14  ASN   A CG  
53   O  OD1 . ASN   A 8   ? 0.3674 0.1477 1.4809 0.0486  0.3804  0.1244  14  ASN   A OD1 
54   N  ND2 . ASN   A 8   ? 0.3968 0.1465 1.4864 0.0505  0.4329  0.1111  14  ASN   A ND2 
55   N  N   . TYR   A 9   ? 0.2562 0.1171 0.9225 0.0267  0.1738  0.0535  15  TYR   A N   
56   C  CA  . TYR   A 9   ? 0.2539 0.1332 0.8282 0.0246  0.1246  0.0427  15  TYR   A CA  
57   C  C   . TYR   A 9   ? 0.2229 0.1159 0.7747 0.0226  0.0730  0.0495  15  TYR   A C   
58   O  O   . TYR   A 9   ? 0.2097 0.1001 0.7726 0.0206  0.0790  0.0506  15  TYR   A O   
59   C  CB  . TYR   A 9   ? 0.2844 0.1551 0.7455 0.0181  0.1493  0.0132  15  TYR   A CB  
60   C  CG  . TYR   A 9   ? 0.3012 0.1499 0.7542 0.0150  0.1943  0.0041  15  TYR   A CG  
61   C  CD1 . TYR   A 9   ? 0.2997 0.1561 0.7858 0.0205  0.1834  0.0132  15  TYR   A CD1 
62   C  CD2 . TYR   A 9   ? 0.3367 0.1501 0.7383 0.0033  0.2469  -0.0138 15  TYR   A CD2 
63   C  CE1 . TYR   A 9   ? 0.3284 0.1608 0.8060 0.0169  0.2266  0.0052  15  TYR   A CE1 
64   C  CE2 . TYR   A 9   ? 0.3693 0.1504 0.7493 -0.0038 0.2897  -0.0226 15  TYR   A CE2 
65   C  CZ  . TYR   A 9   ? 0.3686 0.1606 0.7921 0.0042  0.2814  -0.0127 15  TYR   A CZ  
66   O  OH  . TYR   A 9   ? 0.4081 0.1655 0.8066 -0.0035 0.3245  -0.0214 15  TYR   A OH  
67   N  N   . ARG   A 10  ? 0.2015 0.1026 0.7057 0.0219  0.0266  0.0507  16  ARG   A N   
68   C  CA  . ARG   A 10  ? 0.1923 0.0936 0.6468 0.0176  -0.0174 0.0526  16  ARG   A CA  
69   C  C   . ARG   A 10  ? 0.1966 0.1012 0.5466 0.0189  -0.0208 0.0313  16  ARG   A C   
70   O  O   . ARG   A 10  ? 0.1907 0.0966 0.5264 0.0213  -0.0241 0.0292  16  ARG   A O   
71   C  CB  . ARG   A 10  ? 0.1965 0.0890 0.6973 0.0114  -0.0706 0.0806  16  ARG   A CB  
72   C  CG  . ARG   A 10  ? 0.2832 0.1587 0.7058 0.0027  -0.1169 0.0807  16  ARG   A CG  
73   C  CD  . ARG   A 10  ? 0.3307 0.1849 0.7934 -0.0110 -0.1723 0.1116  16  ARG   A CD  
74   N  NE  . ARG   A 10  ? 0.4051 0.2284 0.7734 -0.0201 -0.2085 0.1074  16  ARG   A NE  
75   C  CZ  . ARG   A 10  ? 0.4632 0.2518 0.7621 -0.0340 -0.2428 0.1104  16  ARG   A CZ  
76   N  NH1 . ARG   A 10  ? 0.4456 0.2334 0.7611 -0.0396 -0.2500 0.1178  16  ARG   A NH1 
77   N  NH2 . ARG   A 10  ? 0.4940 0.2423 0.7008 -0.0433 -0.2663 0.1052  16  ARG   A NH2 
78   N  N   . VAL   A 11  ? 0.2038 0.1106 0.4906 0.0177  -0.0179 0.0182  17  VAL   A N   
79   C  CA  . VAL   A 11  ? 0.2262 0.1380 0.4304 0.0193  -0.0188 0.0039  17  VAL   A CA  
80   C  C   . VAL   A 11  ? 0.2387 0.1364 0.3991 0.0181  -0.0523 0.0079  17  VAL   A C   
81   O  O   . VAL   A 11  ? 0.2520 0.1439 0.4099 0.0148  -0.0602 0.0105  17  VAL   A O   
82   C  CB  . VAL   A 11  ? 0.2367 0.1580 0.4037 0.0164  0.0122  -0.0106 17  VAL   A CB  
83   C  CG1 . VAL   A 11  ? 0.2505 0.1814 0.3548 0.0173  0.0103  -0.0175 17  VAL   A CG1 
84   C  CG2 . VAL   A 11  ? 0.2271 0.1432 0.4254 0.0118  0.0504  -0.0154 17  VAL   A CG2 
85   N  N   . VAL   A 12  ? 0.2394 0.1249 0.3592 0.0197  -0.0685 0.0079  18  VAL   A N   
86   C  CA  . VAL   A 12  ? 0.2686 0.1233 0.3315 0.0158  -0.0935 0.0105  18  VAL   A CA  
87   C  C   . VAL   A 12  ? 0.2919 0.1439 0.2940 0.0227  -0.0790 0.0005  18  VAL   A C   
88   O  O   . VAL   A 12  ? 0.2816 0.1563 0.2943 0.0285  -0.0613 -0.0038 18  VAL   A O   
89   C  CB  . VAL   A 12  ? 0.2913 0.1122 0.3640 0.0056  -0.1323 0.0263  18  VAL   A CB  
90   C  CG1 . VAL   A 12  ? 0.2817 0.0987 0.4148 -0.0041 -0.1553 0.0440  18  VAL   A CG1 
91   C  CG2 . VAL   A 12  ? 0.2827 0.1111 0.3825 0.0090  -0.1314 0.0289  18  VAL   A CG2 
92   N  N   . ASN   A 13  ? 0.3181 0.1361 0.2584 0.0208  -0.0855 -0.0006 19  ASN   A N   
93   C  CA  . ASN   A 13  ? 0.3436 0.1505 0.2363 0.0283  -0.0674 -0.0058 19  ASN   A CA  
94   C  C   . ASN   A 13  ? 0.3647 0.1521 0.2543 0.0266  -0.0799 -0.0028 19  ASN   A C   
95   O  O   . ASN   A 13  ? 0.3833 0.1368 0.2682 0.0148  -0.1104 0.0047  19  ASN   A O   
96   C  CB  . ASN   A 13  ? 0.3869 0.1446 0.2114 0.0249  -0.0663 -0.0070 19  ASN   A CB  
97   C  CG  . ASN   A 13  ? 0.3979 0.1718 0.2222 0.0271  -0.0537 -0.0091 19  ASN   A CG  
98   O  OD1 . ASN   A 13  ? 0.4061 0.1719 0.2356 0.0185  -0.0716 -0.0067 19  ASN   A OD1 
99   N  ND2 . ASN   A 13  ? 0.3765 0.1747 0.2016 0.0376  -0.0247 -0.0106 19  ASN   A ND2 
100  N  N   . ARG   A 14  ? 0.3577 0.1676 0.2561 0.0358  -0.0608 -0.0055 20  ARG   A N   
101  C  CA  . ARG   A 14  ? 0.3649 0.1599 0.2628 0.0354  -0.0702 -0.0032 20  ARG   A CA  
102  C  C   . ARG   A 14  ? 0.4430 0.1690 0.2712 0.0271  -0.0835 -0.0022 20  ARG   A C   
103  O  O   . ARG   A 14  ? 0.4641 0.1613 0.2886 0.0165  -0.1113 0.0039  20  ARG   A O   
104  C  CB  . ARG   A 14  ? 0.3312 0.1609 0.2467 0.0461  -0.0460 -0.0050 20  ARG   A CB  
105  C  CG  . ARG   A 14  ? 0.3282 0.1533 0.2557 0.0467  -0.0539 -0.0030 20  ARG   A CG  
106  C  CD  . ARG   A 14  ? 0.3561 0.2040 0.2867 0.0565  -0.0300 -0.0024 20  ARG   A CD  
107  N  NE  . ARG   A 14  ? 0.3781 0.2283 0.3236 0.0582  -0.0342 -0.0007 20  ARG   A NE  
108  C  CZ  . ARG   A 14  ? 0.4242 0.2352 0.3358 0.0595  -0.0360 -0.0004 20  ARG   A CZ  
109  N  NH1 . ARG   A 14  ? 0.4662 0.2226 0.3191 0.0567  -0.0336 -0.0025 20  ARG   A NH1 
110  N  NH2 . ARG   A 14  ? 0.4098 0.2281 0.3393 0.0616  -0.0388 0.0015  20  ARG   A NH2 
111  N  N   . HIS   A 15  ? 0.4840 0.1761 0.2546 0.0291  -0.0639 -0.0065 21  HIS   A N   
112  C  CA  . HIS   A 15  ? 0.5544 0.1622 0.2387 0.0174  -0.0689 -0.0077 21  HIS   A CA  
113  C  C   . HIS   A 15  ? 0.6000 0.1584 0.2512 -0.0060 -0.1122 -0.0010 21  HIS   A C   
114  O  O   . HIS   A 15  ? 0.6532 0.1318 0.2262 -0.0240 -0.1284 0.0008  21  HIS   A O   
115  C  CB  . HIS   A 15  ? 0.5868 0.1633 0.2202 0.0258  -0.0275 -0.0131 21  HIS   A CB  
116  C  CG  . HIS   A 15  ? 0.6246 0.1978 0.2443 0.0232  -0.0239 -0.0140 21  HIS   A CG  
117  N  ND1 . HIS   A 15  ? 0.5906 0.2351 0.2742 0.0349  -0.0130 -0.0126 21  HIS   A ND1 
118  C  CD2 . HIS   A 15  ? 0.6859 0.1874 0.2291 0.0080  -0.0303 -0.0158 21  HIS   A CD2 
119  C  CE1 . HIS   A 15  ? 0.6247 0.2457 0.2775 0.0292  -0.0131 -0.0137 21  HIS   A CE1 
120  N  NE2 . HIS   A 15  ? 0.6792 0.2150 0.2476 0.0134  -0.0224 -0.0157 21  HIS   A NE2 
121  N  N   . LEU   A 16  ? 0.5825 0.1831 0.2927 -0.0085 -0.1323 0.0052  22  LEU   A N   
122  C  CA  . LEU   A 16  ? 0.6154 0.1782 0.3147 -0.0313 -0.1773 0.0180  22  LEU   A CA  
123  C  C   . LEU   A 16  ? 0.5981 0.1935 0.3832 -0.0376 -0.2125 0.0343  22  LEU   A C   
124  O  O   . LEU   A 16  ? 0.6102 0.1853 0.4125 -0.0565 -0.2532 0.0518  22  LEU   A O   
125  C  CB  . LEU   A 16  ? 0.6064 0.1833 0.3108 -0.0307 -0.1721 0.0167  22  LEU   A CB  
126  C  CG  . LEU   A 16  ? 0.6663 0.1894 0.2790 -0.0324 -0.1477 0.0068  22  LEU   A CG  
127  C  CD1 . LEU   A 16  ? 0.6457 0.1916 0.2753 -0.0311 -0.1448 0.0068  22  LEU   A CD1 
128  C  CD2 . LEU   A 16  ? 0.7349 0.1550 0.2438 -0.0594 -0.1733 0.0113  22  LEU   A CD2 
129  N  N   . ALA   A 17  ? 0.5673 0.2127 0.4127 -0.0225 -0.1960 0.0315  23  ALA   A N   
130  C  CA  . ALA   A 17  ? 0.5430 0.2199 0.4782 -0.0251 -0.2181 0.0470  23  ALA   A CA  
131  C  C   . ALA   A 17  ? 0.5802 0.2031 0.5003 -0.0488 -0.2688 0.0672  23  ALA   A C   
132  O  O   . ALA   A 17  ? 0.6225 0.1870 0.4566 -0.0592 -0.2772 0.0632  23  ALA   A O   
133  C  CB  . ALA   A 17  ? 0.5142 0.2425 0.4968 -0.0062 -0.1860 0.0379  23  ALA   A CB  
134  N  N   . THR   A 18  ? 0.5611 0.1993 0.5668 -0.0590 -0.3019 0.0915  24  THR   A N   
135  C  CA  . THR   A 18  ? 0.5994 0.1922 0.6134 -0.0860 -0.3603 0.1202  24  THR   A CA  
136  C  C   . THR   A 18  ? 0.6025 0.2137 0.6697 -0.0809 -0.3635 0.1278  24  THR   A C   
137  O  O   . THR   A 18  ? 0.5771 0.2360 0.6732 -0.0565 -0.3190 0.1098  24  THR   A O   
138  C  CB  . THR   A 18  ? 0.5863 0.1938 0.6912 -0.0986 -0.3941 0.1499  24  THR   A CB  
139  O  OG1 . THR   A 18  ? 0.5401 0.2164 0.7734 -0.0783 -0.3667 0.1558  24  THR   A OG1 
140  C  CG2 . THR   A 18  ? 0.6068 0.2054 0.6733 -0.1012 -0.3883 0.1428  24  THR   A CG2 
141  N  N   . HIS   A 19  ? 0.6338 0.2045 0.7132 -0.1067 -0.4195 0.1569  25  HIS   A N   
142  C  CA  . HIS   A 19  ? 0.6289 0.2173 0.7699 -0.1036 -0.4272 0.1686  25  HIS   A CA  
143  C  C   . HIS   A 19  ? 0.5499 0.2134 0.8424 -0.0842 -0.4037 0.1812  25  HIS   A C   
144  O  O   . HIS   A 19  ? 0.5201 0.2199 0.8607 -0.0664 -0.3739 0.1742  25  HIS   A O   
145  C  CB  . HIS   A 19  ? 0.6934 0.2184 0.8195 -0.1406 -0.4998 0.2032  25  HIS   A CB  
146  C  CG  . HIS   A 19  ? 0.8376 0.2709 0.8041 -0.1643 -0.5199 0.1913  25  HIS   A CG  
147  N  ND1 . HIS   A 19  ? 0.8995 0.3155 0.7983 -0.1540 -0.4916 0.1679  25  HIS   A ND1 
148  C  CD2 . HIS   A 19  ? 0.9255 0.2725 0.7907 -0.2009 -0.5659 0.2030  25  HIS   A CD2 
149  C  CE1 . HIS   A 19  ? 0.9889 0.3068 0.7467 -0.1824 -0.5141 0.1638  25  HIS   A CE1 
150  N  NE2 . HIS   A 19  ? 1.0131 0.2825 0.7387 -0.2128 -0.5593 0.1837  25  HIS   A NE2 
151  N  N   . ASN   A 20  ? 0.5177 0.1975 0.8834 -0.0890 -0.4150 0.2009  26  ASN   A N   
152  C  CA  . ASN   A 20  ? 0.4580 0.1970 0.9652 -0.0715 -0.3839 0.2131  26  ASN   A CA  
153  C  C   . ASN   A 20  ? 0.4191 0.2009 0.9128 -0.0421 -0.3114 0.1755  26  ASN   A C   
154  O  O   . ASN   A 20  ? 0.3936 0.2085 0.9560 -0.0266 -0.2756 0.1733  26  ASN   A O   
155  C  CB  . ASN   A 20  ? 0.4730 0.2150 1.0514 -0.0825 -0.4062 0.2401  26  ASN   A CB  
156  C  CG  . ASN   A 20  ? 0.4968 0.2871 1.2358 -0.0678 -0.3758 0.2612  26  ASN   A CG  
157  O  OD1 . ASN   A 20  ? 0.4872 0.2873 1.3183 -0.0688 -0.3861 0.2869  26  ASN   A OD1 
158  N  ND2 . ASN   A 20  ? 0.5035 0.3204 1.2807 -0.0542 -0.3338 0.2515  26  ASN   A ND2 
159  N  N   . ASP   A 21  ? 0.4188 0.1939 0.8162 -0.0369 -0.2907 0.1470  27  ASP   A N   
160  C  CA  . ASP   A 21  ? 0.3844 0.1934 0.7533 -0.0149 -0.2309 0.1141  27  ASP   A CA  
161  C  C   . ASP   A 21  ? 0.3712 0.1915 0.7263 -0.0045 -0.2103 0.1015  27  ASP   A C   
162  O  O   . ASP   A 21  ? 0.3462 0.1987 0.7502 0.0085  -0.1702 0.0941  27  ASP   A O   
163  C  CB  . ASP   A 21  ? 0.4030 0.1953 0.6660 -0.0147 -0.2236 0.0918  27  ASP   A CB  
164  C  CG  . ASP   A 21  ? 0.3858 0.1799 0.6678 -0.0195 -0.2278 0.0978  27  ASP   A CG  
165  O  OD1 . ASP   A 21  ? 0.3204 0.1428 0.6932 -0.0144 -0.2110 0.1076  27  ASP   A OD1 
166  O  OD2 . ASP   A 21  ? 0.4443 0.2060 0.6494 -0.0290 -0.2455 0.0934  27  ASP   A OD2 
167  N  N   . TRP   A 22  ? 0.3901 0.1769 0.6801 -0.0129 -0.2382 0.1015  28  TRP   A N   
168  C  CA  . TRP   A 22  ? 0.3887 0.1843 0.6662 -0.0038 -0.2220 0.0915  28  TRP   A CA  
169  C  C   . TRP   A 22  ? 0.3677 0.1827 0.7489 -0.0025 -0.2257 0.1118  28  TRP   A C   
170  O  O   . TRP   A 22  ? 0.3624 0.2011 0.7593 0.0099  -0.1944 0.1011  28  TRP   A O   
171  C  CB  . TRP   A 22  ? 0.4203 0.1658 0.5993 -0.0142 -0.2479 0.0871  28  TRP   A CB  
172  C  CG  . TRP   A 22  ? 0.4319 0.1673 0.5181 -0.0062 -0.2197 0.0623  28  TRP   A CG  
173  C  CD1 . TRP   A 22  ? 0.4782 0.1715 0.4876 -0.0158 -0.2293 0.0579  28  TRP   A CD1 
174  C  CD2 . TRP   A 22  ? 0.4132 0.1793 0.4809 0.0117  -0.1773 0.0428  28  TRP   A CD2 
175  N  NE1 . TRP   A 22  ? 0.4957 0.1951 0.4498 -0.0021 -0.1909 0.0373  28  TRP   A NE1 
176  C  CE2 . TRP   A 22  ? 0.4549 0.2006 0.4469 0.0140  -0.1619 0.0297  28  TRP   A CE2 
177  C  CE3 . TRP   A 22  ? 0.3874 0.1942 0.4973 0.0242  -0.1515 0.0376  28  TRP   A CE3 
178  C  CZ2 . TRP   A 22  ? 0.4504 0.2188 0.4194 0.0285  -0.1251 0.0160  28  TRP   A CZ2 
179  C  CZ3 . TRP   A 22  ? 0.3939 0.2194 0.4692 0.0356  -0.1195 0.0228  28  TRP   A CZ3 
180  C  CH2 . TRP   A 22  ? 0.4162 0.2256 0.4288 0.0380  -0.1078 0.0141  28  TRP   A CH2 
181  N  N   . ALA   A 23  ? 0.3561 0.1597 0.8114 -0.0165 -0.2644 0.1437  29  ALA   A N   
182  C  CA  . ALA   A 23  ? 0.3325 0.1544 0.9053 -0.0152 -0.2673 0.1695  29  ALA   A CA  
183  C  C   . ALA   A 23  ? 0.3065 0.1679 0.9678 0.0023  -0.2090 0.1652  29  ALA   A C   
184  O  O   . ALA   A 23  ? 0.2943 0.1716 1.0397 0.0095  -0.1876 0.1765  29  ALA   A O   
185  C  CB  . ALA   A 23  ? 0.3099 0.1070 0.9467 -0.0384 -0.3301 0.2121  29  ALA   A CB  
186  N  N   . ASN   A 24  ? 0.2879 0.1577 0.9286 0.0070  -0.1824 0.1504  30  ASN   A N   
187  C  CA  . ASN   A 24  ? 0.2536 0.1458 0.9500 0.0197  -0.1230 0.1416  30  ASN   A CA  
188  C  C   . ASN   A 24  ? 0.2537 0.1530 0.8501 0.0277  -0.0823 0.1035  30  ASN   A C   
189  O  O   . ASN   A 24  ? 0.2502 0.1549 0.8509 0.0310  -0.0466 0.0932  30  ASN   A O   
190  C  CB  . ASN   A 24  ? 0.2583 0.1505 1.0278 0.0148  -0.1295 0.1626  30  ASN   A CB  
191  C  CG  . ASN   A 24  ? 0.2822 0.1720 1.1781 0.0058  -0.1660 0.2081  30  ASN   A CG  
192  O  OD1 . ASN   A 24  ? 0.2785 0.1781 1.2672 0.0127  -0.1432 0.2235  30  ASN   A OD1 
193  N  ND2 . ASN   A 24  ? 0.2798 0.1540 1.1843 -0.0115 -0.2238 0.2333  30  ASN   A ND2 
194  N  N   . LEU   A 25  ? 0.2621 0.1585 0.7703 0.0288  -0.0912 0.0861  31  LEU   A N   
195  C  CA  . LEU   A 25  ? 0.2549 0.1594 0.6772 0.0338  -0.0626 0.0580  31  LEU   A CA  
196  C  C   . LEU   A 25  ? 0.2336 0.1485 0.6743 0.0380  -0.0088 0.0460  31  LEU   A C   
197  O  O   . LEU   A 25  ? 0.2236 0.1388 0.7105 0.0406  0.0084  0.0514  31  LEU   A O   
198  C  CB  . LEU   A 25  ? 0.2636 0.1634 0.6215 0.0351  -0.0792 0.0502  31  LEU   A CB  
199  C  CG  . LEU   A 25  ? 0.2870 0.1993 0.5727 0.0399  -0.0528 0.0285  31  LEU   A CG  
200  C  CD1 . LEU   A 25  ? 0.3123 0.2232 0.5432 0.0386  -0.0530 0.0194  31  LEU   A CD1 
201  C  CD2 . LEU   A 25  ? 0.2843 0.1926 0.5321 0.0428  -0.0647 0.0262  31  LEU   A CD2 
202  N  N   . VAL   A 26  ? 0.2254 0.1422 0.6211 0.0361  0.0177  0.0298  32  VAL   A N   
203  C  CA  . VAL   A 26  ? 0.2150 0.1265 0.5947 0.0328  0.0670  0.0157  32  VAL   A CA  
204  C  C   . VAL   A 26  ? 0.2303 0.1493 0.5201 0.0289  0.0657  0.0004  32  VAL   A C   
205  O  O   . VAL   A 26  ? 0.2459 0.1619 0.5185 0.0256  0.0832  -0.0045 32  VAL   A O   
206  C  CB  . VAL   A 26  ? 0.2260 0.1275 0.6159 0.0287  0.0927  0.0120  32  VAL   A CB  
207  C  CG1 . VAL   A 26  ? 0.2642 0.1477 0.5958 0.0182  0.1373  -0.0062 32  VAL   A CG1 
208  C  CG2 . VAL   A 26  ? 0.1930 0.0868 0.6896 0.0327  0.1038  0.0313  32  VAL   A CG2 
209  N  N   . TRP   A 27  ? 0.2192 0.1473 0.4591 0.0290  0.0431  -0.0033 33  TRP   A N   
210  C  CA  . TRP   A 27  ? 0.2244 0.1630 0.3978 0.0260  0.0397  -0.0106 33  TRP   A CA  
211  C  C   . TRP   A 27  ? 0.2162 0.1598 0.3609 0.0316  0.0121  -0.0084 33  TRP   A C   
212  O  O   . TRP   A 27  ? 0.2226 0.1593 0.3790 0.0325  0.0017  -0.0060 33  TRP   A O   
213  C  CB  . TRP   A 27  ? 0.2405 0.1727 0.3765 0.0123  0.0676  -0.0194 33  TRP   A CB  
214  C  CG  . TRP   A 27  ? 0.2577 0.2025 0.3370 0.0054  0.0584  -0.0199 33  TRP   A CG  
215  C  CD1 . TRP   A 27  ? 0.2836 0.2352 0.3336 -0.0021 0.0565  -0.0167 33  TRP   A CD1 
216  C  CD2 . TRP   A 27  ? 0.2577 0.2108 0.3131 0.0046  0.0485  -0.0193 33  TRP   A CD2 
217  N  NE1 . TRP   A 27  ? 0.2902 0.2552 0.3076 -0.0081 0.0452  -0.0109 33  TRP   A NE1 
218  C  CE2 . TRP   A 27  ? 0.2749 0.2410 0.2946 -0.0032 0.0417  -0.0132 33  TRP   A CE2 
219  C  CE3 . TRP   A 27  ? 0.2448 0.1960 0.3105 0.0096  0.0430  -0.0205 33  TRP   A CE3 
220  C  CZ2 . TRP   A 27  ? 0.2714 0.2490 0.2708 -0.0059 0.0332  -0.0079 33  TRP   A CZ2 
221  C  CZ3 . TRP   A 27  ? 0.2562 0.2164 0.2917 0.0070  0.0364  -0.0191 33  TRP   A CZ3 
222  C  CH2 . TRP   A 27  ? 0.2604 0.2342 0.2660 0.0001  0.0322  -0.0124 33  TRP   A CH2 
223  N  N   . GLU   A 28  ? 0.2039 0.1552 0.3133 0.0347  0.0034  -0.0080 34  GLU   A N   
224  C  CA  . GLU   A 28  ? 0.2033 0.1506 0.2799 0.0401  -0.0113 -0.0063 34  GLU   A CA  
225  C  C   . GLU   A 28  ? 0.1985 0.1620 0.2482 0.0405  -0.0033 -0.0037 34  GLU   A C   
226  O  O   . GLU   A 28  ? 0.1698 0.1440 0.2249 0.0373  0.0028  -0.0016 34  GLU   A O   
227  C  CB  . GLU   A 28  ? 0.2164 0.1393 0.2920 0.0451  -0.0344 -0.0019 34  GLU   A CB  
228  C  CG  . GLU   A 28  ? 0.2362 0.1581 0.3243 0.0478  -0.0382 0.0009  34  GLU   A CG  
229  C  CD  . GLU   A 28  ? 0.3087 0.2358 0.3683 0.0533  -0.0312 0.0012  34  GLU   A CD  
230  O  OE1 . GLU   A 28  ? 0.3170 0.2544 0.3930 0.0541  -0.0274 0.0027  34  GLU   A OE1 
231  O  OE2 . GLU   A 28  ? 0.3123 0.2324 0.3389 0.0570  -0.0267 0.0015  34  GLU   A OE2 
232  N  N   . ASP   A 29  ? 0.2060 0.1705 0.2324 0.0434  -0.0032 -0.0010 35  ASP   A N   
233  C  CA  . ASP   A 29  ? 0.2204 0.2021 0.2386 0.0443  0.0038  0.0086  35  ASP   A CA  
234  C  C   . ASP   A 29  ? 0.2346 0.1997 0.2345 0.0547  0.0066  0.0118  35  ASP   A C   
235  O  O   . ASP   A 29  ? 0.2387 0.1994 0.2276 0.0538  0.0080  0.0102  35  ASP   A O   
236  C  CB  . ASP   A 29  ? 0.2430 0.2447 0.2593 0.0300  0.0088  0.0130  35  ASP   A CB  
237  C  CG  . ASP   A 29  ? 0.3076 0.3308 0.3288 0.0253  0.0086  0.0308  35  ASP   A CG  
238  O  OD1 . ASP   A 29  ? 0.3008 0.3257 0.3327 0.0381  0.0120  0.0402  35  ASP   A OD1 
239  O  OD2 . ASP   A 29  ? 0.3512 0.3844 0.3654 0.0067  0.0056  0.0377  35  ASP   A OD2 
240  N  N   . SER   A 30  ? 0.2334 0.1838 0.2270 0.0640  0.0116  0.0160  36  SER   A N   
241  C  CA  A SER   A 30  ? 0.2542 0.1739 0.2221 0.0730  0.0243  0.0182  36  SER   A CA  
242  C  CA  B SER   A 30  ? 0.2547 0.1744 0.2224 0.0729  0.0240  0.0180  36  SER   A CA  
243  C  C   . SER   A 30  ? 0.2422 0.1845 0.2267 0.0750  0.0395  0.0311  36  SER   A C   
244  O  O   . SER   A 30  ? 0.2670 0.1855 0.2307 0.0796  0.0510  0.0305  36  SER   A O   
245  C  CB  A SER   A 30  ? 0.2837 0.1786 0.2421 0.0813  0.0347  0.0211  36  SER   A CB  
246  C  CB  B SER   A 30  ? 0.2867 0.1802 0.2436 0.0810  0.0338  0.0204  36  SER   A CB  
247  O  OG  A SER   A 30  ? 0.3174 0.1999 0.2711 0.0778  0.0175  0.0136  36  SER   A OG  
248  O  OG  B SER   A 30  ? 0.2918 0.2213 0.2881 0.0841  0.0433  0.0347  36  SER   A OG  
249  N  N   . SER   A 31  ? 0.2075 0.1920 0.2291 0.0692  0.0381  0.0458  37  SER   A N   
250  C  CA  . SER   A 31  ? 0.2063 0.2152 0.2550 0.0676  0.0460  0.0655  37  SER   A CA  
251  C  C   . SER   A 31  ? 0.2022 0.2140 0.2364 0.0600  0.0401  0.0595  37  SER   A C   
252  O  O   . SER   A 31  ? 0.2151 0.2350 0.2651 0.0622  0.0494  0.0733  37  SER   A O   
253  C  CB  . SER   A 31  ? 0.2254 0.2728 0.3129 0.0562  0.0363  0.0873  37  SER   A CB  
254  O  OG  . SER   A 31  ? 0.2746 0.3364 0.3488 0.0357  0.0173  0.0829  37  SER   A OG  
255  N  N   . ARG   A 32  ? 0.1884 0.1937 0.2005 0.0519  0.0274  0.0418  38  ARG   A N   
256  C  CA  . ARG   A 32  ? 0.1878 0.1928 0.1869 0.0447  0.0233  0.0347  38  ARG   A CA  
257  C  C   . ARG   A 32  ? 0.2042 0.1753 0.1765 0.0525  0.0238  0.0204  38  ARG   A C   
258  O  O   . ARG   A 32  ? 0.2001 0.1692 0.1636 0.0487  0.0219  0.0163  38  ARG   A O   
259  C  CB  . ARG   A 32  ? 0.1791 0.1932 0.1750 0.0283  0.0140  0.0266  38  ARG   A CB  
260  C  CG  . ARG   A 32  ? 0.1715 0.2073 0.1753 0.0119  0.0090  0.0414  38  ARG   A CG  
261  C  CD  . ARG   A 32  ? 0.1955 0.2223 0.1790 -0.0074 0.0080  0.0308  38  ARG   A CD  
262  N  NE  . ARG   A 32  ? 0.1959 0.2140 0.1634 -0.0151 0.0111  0.0230  38  ARG   A NE  
263  C  CZ  . ARG   A 32  ? 0.2328 0.2384 0.1739 -0.0376 0.0140  0.0197  38  ARG   A CZ  
264  N  NH1 . ARG   A 32  ? 0.1924 0.1881 0.1131 -0.0571 0.0134  0.0234  38  ARG   A NH1 
265  N  NH2 . ARG   A 32  ? 0.2565 0.2522 0.1843 -0.0430 0.0191  0.0125  38  ARG   A NH2 
266  N  N   . ASP   A 33  ? 0.2248 0.1650 0.1801 0.0599  0.0228  0.0141  39  ASP   A N   
267  C  CA  . ASP   A 33  ? 0.2528 0.1500 0.1737 0.0606  0.0149  0.0040  39  ASP   A CA  
268  C  C   . ASP   A 33  ? 0.2569 0.1613 0.1919 0.0515  -0.0035 -0.0034 39  ASP   A C   
269  O  O   . ASP   A 33  ? 0.2642 0.1506 0.1848 0.0482  -0.0112 -0.0066 39  ASP   A O   
270  C  CB  . ASP   A 33  ? 0.2847 0.1552 0.1753 0.0647  0.0289  0.0057  39  ASP   A CB  
271  C  CG  . ASP   A 33  ? 0.3544 0.1685 0.1946 0.0595  0.0167  -0.0029 39  ASP   A CG  
272  O  OD1 . ASP   A 33  ? 0.3599 0.1415 0.1785 0.0556  0.0035  -0.0062 39  ASP   A OD1 
273  O  OD2 . ASP   A 33  ? 0.4018 0.2043 0.2245 0.0562  0.0159  -0.0048 39  ASP   A OD2 
274  N  N   . LEU   A 34  ? 0.2299 0.1583 0.1963 0.0470  -0.0067 -0.0045 40  LEU   A N   
275  C  CA  . LEU   A 34  ? 0.2171 0.1480 0.2083 0.0399  -0.0143 -0.0093 40  LEU   A CA  
276  C  C   . LEU   A 34  ? 0.2281 0.1514 0.2450 0.0395  -0.0239 -0.0089 40  LEU   A C   
277  O  O   . LEU   A 34  ? 0.2383 0.1662 0.2562 0.0425  -0.0214 -0.0074 40  LEU   A O   
278  C  CB  . LEU   A 34  ? 0.1985 0.1548 0.2033 0.0312  0.0001  -0.0112 40  LEU   A CB  
279  C  CG  . LEU   A 34  ? 0.2069 0.1732 0.1952 0.0271  0.0062  -0.0096 40  LEU   A CG  
280  C  CD1 . LEU   A 34  ? 0.1846 0.1619 0.1732 0.0120  0.0178  -0.0115 40  LEU   A CD1 
281  C  CD2 . LEU   A 34  ? 0.2228 0.1730 0.2063 0.0296  -0.0009 -0.0127 40  LEU   A CD2 
282  N  N   . LEU   A 35  ? 0.2232 0.1364 0.2695 0.0355  -0.0349 -0.0074 41  LEU   A N   
283  C  CA  . LEU   A 35  ? 0.2313 0.1407 0.3201 0.0344  -0.0429 -0.0024 41  LEU   A CA  
284  C  C   . LEU   A 35  ? 0.2286 0.1420 0.3692 0.0301  -0.0366 0.0006  41  LEU   A C   
285  O  O   . LEU   A 35  ? 0.2323 0.1392 0.3722 0.0274  -0.0439 0.0025  41  LEU   A O   
286  C  CB  . LEU   A 35  ? 0.2487 0.1262 0.3242 0.0329  -0.0733 0.0055  41  LEU   A CB  
287  C  CG  . LEU   A 35  ? 0.2566 0.1306 0.3829 0.0306  -0.0873 0.0156  41  LEU   A CG  
288  C  CD1 . LEU   A 35  ? 0.2924 0.1378 0.3819 0.0289  -0.1082 0.0189  41  LEU   A CD1 
289  C  CD2 . LEU   A 35  ? 0.2566 0.1225 0.4410 0.0231  -0.1071 0.0304  41  LEU   A CD2 
290  N  N   . VAL   A 36  ? 0.2227 0.1442 0.4072 0.0296  -0.0171 0.0010  42  VAL   A N   
291  C  CA  . VAL   A 36  ? 0.2253 0.1447 0.4711 0.0270  0.0003  0.0056  42  VAL   A CA  
292  C  C   . VAL   A 36  ? 0.2243 0.1381 0.5403 0.0288  -0.0102 0.0211  42  VAL   A C   
293  O  O   . VAL   A 36  ? 0.2226 0.1389 0.5381 0.0312  -0.0072 0.0202  42  VAL   A O   
294  C  CB  . VAL   A 36  ? 0.2421 0.1625 0.4765 0.0219  0.0431  -0.0066 42  VAL   A CB  
295  C  CG1 . VAL   A 36  ? 0.2470 0.1547 0.5482 0.0204  0.0707  -0.0016 42  VAL   A CG1 
296  C  CG2 . VAL   A 36  ? 0.2660 0.1920 0.4357 0.0168  0.0464  -0.0169 42  VAL   A CG2 
297  N  N   . SER   A 37  ? 0.2273 0.1347 0.6092 0.0268  -0.0245 0.0383  43  SER   A N   
298  C  CA  . SER   A 37  ? 0.2279 0.1320 0.6964 0.0267  -0.0363 0.0604  43  SER   A CA  
299  C  C   . SER   A 37  ? 0.2387 0.1430 0.8019 0.0281  -0.0037 0.0722  43  SER   A C   
300  O  O   . SER   A 37  ? 0.2175 0.1204 0.7752 0.0272  0.0167  0.0653  43  SER   A O   
301  C  CB  . SER   A 37  ? 0.2546 0.1441 0.7254 0.0186  -0.0947 0.0804  43  SER   A CB  
302  O  OG  . SER   A 37  ? 0.3016 0.1817 0.7506 0.0120  -0.1154 0.0838  43  SER   A OG  
303  N  N   . SER   A 38  ? 0.2491 0.1529 0.9035 0.0308  0.0048  0.0913  44  SER   A N   
304  C  CA  . SER   A 38  ? 0.2728 0.1722 1.0341 0.0341  0.0448  0.1067  44  SER   A CA  
305  C  C   . SER   A 38  ? 0.2966 0.1987 1.1485 0.0292  0.0071  0.1403  44  SER   A C   
306  O  O   . SER   A 38  ? 0.3051 0.2070 1.1530 0.0204  -0.0556 0.1587  44  SER   A O   
307  C  CB  . SER   A 38  ? 0.2772 0.1729 1.1082 0.0396  0.0749  0.1163  44  SER   A CB  
308  O  OG  . SER   A 38  ? 0.3044 0.2081 1.1407 0.0376  0.0252  0.1306  44  SER   A OG  
309  N  N   . THR   A 39  ? 0.3134 0.2118 1.2411 0.0321  0.0448  0.1495  45  THR   A N   
310  C  CA  . THR   A 39  ? 0.3308 0.2333 1.3593 0.0267  0.0114  0.1860  45  THR   A CA  
311  C  C   . THR   A 39  ? 0.3465 0.2463 1.5283 0.0343  0.0604  0.2132  45  THR   A C   
312  O  O   . THR   A 39  ? 0.3708 0.2554 1.5511 0.0431  0.1341  0.1932  45  THR   A O   
313  C  CB  . THR   A 39  ? 0.3566 0.2576 1.3295 0.0228  0.0071  0.1729  45  THR   A CB  
314  O  OG1 . THR   A 39  ? 0.3624 0.2539 1.3525 0.0303  0.0792  0.1570  45  THR   A OG1 
315  C  CG2 . THR   A 39  ? 0.4060 0.3061 1.2280 0.0183  -0.0217 0.1425  45  THR   A CG2 
316  N  N   . THR   A 40  ? 0.3339 0.2420 1.6464 0.0287  0.0224  0.2605  46  THR   A N   
317  C  CA  . THR   A 40  ? 0.3127 0.2193 1.7951 0.0371  0.0709  0.2940  46  THR   A CA  
318  C  C   . THR   A 40  ? 0.3239 0.2236 1.8437 0.0402  0.1100  0.2939  46  THR   A C   
319  O  O   . THR   A 40  ? 0.3165 0.2013 1.9319 0.0511  0.1855  0.3010  46  THR   A O   
320  C  CB  . THR   A 40  ? 0.2913 0.2122 1.9148 0.0278  0.0073  0.3531  46  THR   A CB  
321  O  OG1 . THR   A 40  ? 0.3197 0.2453 1.9364 0.0104  -0.0673 0.3755  46  THR   A OG1 
322  C  CG2 . THR   A 40  ? 0.3090 0.2325 1.8896 0.0227  -0.0341 0.3532  46  THR   A CG2 
323  N  N   . ALA   A 41  ? 0.3354 0.2412 1.7839 0.0301  0.0612  0.2878  47  ALA   A N   
324  C  CA  . ALA   A 41  ? 0.3233 0.2240 1.7964 0.0320  0.0914  0.2865  47  ALA   A CA  
325  C  C   . ALA   A 41  ? 0.3716 0.2532 1.7061 0.0378  0.1534  0.2309  47  ALA   A C   
326  O  O   . ALA   A 41  ? 0.4175 0.2967 1.6203 0.0365  0.1478  0.1962  47  ALA   A O   
327  C  CB  . ALA   A 41  ? 0.3283 0.2402 1.7813 0.0165  0.0099  0.3054  47  ALA   A CB  
328  N  N   . GLN   A 42  ? 0.3618 0.2268 1.7278 0.0422  0.2112  0.2251  48  GLN   A N   
329  C  CA  . GLN   A 42  ? 0.4138 0.2522 1.6514 0.0424  0.2683  0.1772  48  GLN   A CA  
330  C  C   . GLN   A 42  ? 0.4336 0.2840 1.5601 0.0345  0.2245  0.1574  48  GLN   A C   
331  O  O   . GLN   A 42  ? 0.4144 0.2786 1.5959 0.0315  0.1898  0.1804  48  GLN   A O   
332  C  CB  . GLN   A 42  ? 0.4306 0.2311 1.7406 0.0485  0.3613  0.1770  48  GLN   A CB  
333  C  CG  . GLN   A 42  ? 0.5496 0.3021 1.7384 0.0450  0.4362  0.1321  48  GLN   A CG  
334  C  CD  . GLN   A 42  ? 0.6396 0.3815 1.8195 0.0472  0.4544  0.1275  48  GLN   A CD  
335  O  OE1 . GLN   A 42  ? 0.6326 0.3912 1.9385 0.0556  0.4441  0.1616  48  GLN   A OE1 
336  N  NE2 . GLN   A 42  ? 0.7007 0.4138 1.7342 0.0380  0.4792  0.0881  48  GLN   A NE2 
337  N  N   . GLY   A 43  ? 0.4606 0.3046 1.4369 0.0303  0.2272  0.1178  49  GLY   A N   
338  C  CA  . GLY   A 43  ? 0.4827 0.3354 1.3472 0.0239  0.1960  0.0963  49  GLY   A CA  
339  C  C   . GLY   A 43  ? 0.4877 0.3118 1.3051 0.0206  0.2565  0.0720  49  GLY   A C   
340  O  O   . GLY   A 43  ? 0.5038 0.2922 1.3090 0.0194  0.3225  0.0569  49  GLY   A O   
341  N  N   . CYS   A 44  ? 0.4782 0.3105 1.2602 0.0168  0.2356  0.0675  50  CYS   A N   
342  C  CA  . CYS   A 44  ? 0.4870 0.2897 1.2233 0.0114  0.2883  0.0463  50  CYS   A CA  
343  C  C   . CYS   A 44  ? 0.4934 0.3017 1.0915 0.0023  0.2649  0.0190  50  CYS   A C   
344  O  O   . CYS   A 44  ? 0.5231 0.3080 1.0759 -0.0052 0.2975  0.0034  50  CYS   A O   
345  C  CB  . CYS   A 44  ? 0.4869 0.2874 1.3350 0.0156  0.3029  0.0700  50  CYS   A CB  
346  S  SG  . CYS   A 44  ? 0.5683 0.3502 1.5915 0.0258  0.3579  0.1028  50  CYS   A SG  
347  N  N   . ASP   A 45  ? 0.4599 0.2948 0.9928 0.0022  0.2129  0.0144  51  ASP   A N   
348  C  CA  . ASP   A 45  ? 0.4654 0.3072 0.8833 -0.0051 0.1939  -0.0062 51  ASP   A CA  
349  C  C   . ASP   A 45  ? 0.4724 0.2821 0.8107 -0.0173 0.2393  -0.0294 51  ASP   A C   
350  O  O   . ASP   A 45  ? 0.4909 0.2855 0.8291 -0.0186 0.2609  -0.0324 51  ASP   A O   
351  C  CB  . ASP   A 45  ? 0.4754 0.3462 0.8509 -0.0015 0.1366  -0.0033 51  ASP   A CB  
352  C  CG  . ASP   A 45  ? 0.4996 0.3876 0.9044 0.0021  0.0857  0.0146  51  ASP   A CG  
353  O  OD1 . ASP   A 45  ? 0.5251 0.4122 0.9475 0.0004  0.0855  0.0187  51  ASP   A OD1 
354  O  OD2 . ASP   A 45  ? 0.4923 0.3889 0.8942 0.0042  0.0457  0.0245  51  ASP   A OD2 
355  N  N   . THR   A 46  ? 0.4693 0.2641 0.7384 -0.0290 0.2517  -0.0439 52  THR   A N   
356  C  CA  . THR   A 46  ? 0.4962 0.2514 0.6722 -0.0488 0.2859  -0.0633 52  THR   A CA  
357  C  C   . THR   A 46  ? 0.4787 0.2594 0.5737 -0.0552 0.2437  -0.0676 52  THR   A C   
358  O  O   . THR   A 46  ? 0.4638 0.2794 0.5507 -0.0489 0.2038  -0.0625 52  THR   A O   
359  C  CB  . THR   A 46  ? 0.5477 0.2712 0.6955 -0.0609 0.3156  -0.0722 52  THR   A CB  
360  O  OG1 . THR   A 46  ? 0.5763 0.2605 0.7929 -0.0581 0.3728  -0.0698 52  THR   A OG1 
361  C  CG2 . THR   A 46  ? 0.5961 0.2818 0.6224 -0.0883 0.3276  -0.0892 52  THR   A CG2 
362  N  N   . ILE   A 47  ? 0.4746 0.2363 0.5153 -0.0676 0.2537  -0.0745 53  ILE   A N   
363  C  CA  . ILE   A 47  ? 0.4669 0.2524 0.4423 -0.0750 0.2157  -0.0737 53  ILE   A CA  
364  C  C   . ILE   A 47  ? 0.4984 0.2492 0.3839 -0.1037 0.2263  -0.0818 53  ILE   A C   
365  O  O   . ILE   A 47  ? 0.5312 0.2223 0.3749 -0.1243 0.2694  -0.0924 53  ILE   A O   
366  C  CB  . ILE   A 47  ? 0.4570 0.2471 0.4291 -0.0734 0.2103  -0.0716 53  ILE   A CB  
367  C  CG1 . ILE   A 47  ? 0.4165 0.2293 0.4781 -0.0495 0.2039  -0.0625 53  ILE   A CG1 
368  C  CG2 . ILE   A 47  ? 0.4701 0.2894 0.3913 -0.0789 0.1705  -0.0657 53  ILE   A CG2 
369  C  CD1 . ILE   A 47  ? 0.3944 0.2513 0.4932 -0.0312 0.1579  -0.0512 53  ILE   A CD1 
370  N  N   . ALA   A 48  ? 0.4811 0.2627 0.3359 -0.1069 0.1886  -0.0751 54  ALA   A N   
371  C  CA  . ALA   A 48  ? 0.5065 0.2630 0.2804 -0.1365 0.1839  -0.0755 54  ALA   A CA  
372  C  C   . ALA   A 48  ? 0.5395 0.2766 0.2538 -0.1596 0.1761  -0.0716 54  ALA   A C   
373  O  O   . ALA   A 48  ? 0.5241 0.2963 0.2638 -0.1468 0.1538  -0.0630 54  ALA   A O   
374  C  CB  . ALA   A 48  ? 0.4701 0.2737 0.2507 -0.1290 0.1439  -0.0636 54  ALA   A CB  
375  N  N   . ARG   A 49  ? 0.5899 0.2663 0.2203 -0.1961 0.1929  -0.0767 55  ARG   A N   
376  C  CA  . ARG   A 49  ? 0.6280 0.2732 0.1842 -0.2285 0.1804  -0.0699 55  ARG   A CA  
377  C  C   . ARG   A 49  ? 0.6732 0.3031 0.1623 -0.2617 0.1518  -0.0582 55  ARG   A C   
378  O  O   . ARG   A 49  ? 0.7474 0.3081 0.1624 -0.2927 0.1763  -0.0683 55  ARG   A O   
379  C  CB  . ARG   A 49  ? 0.6799 0.2432 0.1830 -0.2491 0.2330  -0.0872 55  ARG   A CB  
380  C  CG  . ARG   A 49  ? 0.6641 0.2413 0.2490 -0.2156 0.2657  -0.0959 55  ARG   A CG  
381  C  CD  . ARG   A 49  ? 0.6198 0.2585 0.2559 -0.1937 0.2306  -0.0838 55  ARG   A CD  
382  N  NE  . ARG   A 49  ? 0.5906 0.2380 0.3038 -0.1655 0.2586  -0.0896 55  ARG   A NE  
383  C  CZ  . ARG   A 49  ? 0.5441 0.2451 0.3206 -0.1394 0.2335  -0.0811 55  ARG   A CZ  
384  N  NH1 . ARG   A 49  ? 0.5131 0.2620 0.2857 -0.1356 0.1864  -0.0682 55  ARG   A NH1 
385  N  NH2 . ARG   A 49  ? 0.5181 0.2220 0.3657 -0.1179 0.2567  -0.0832 55  ARG   A NH2 
386  N  N   . CYS   A 50  ? 0.6328 0.3248 0.1537 -0.2543 0.1030  -0.0358 56  CYS   A N   
387  C  CA  . CYS   A 50  ? 0.6461 0.3394 0.1317 -0.2796 0.0703  -0.0181 56  CYS   A CA  
388  C  C   . CYS   A 50  ? 0.6226 0.3807 0.1537 -0.2730 0.0207  0.0132  56  CYS   A C   
389  O  O   . CYS   A 50  ? 0.5966 0.3948 0.1808 -0.2473 0.0160  0.0172  56  CYS   A O   
390  C  CB  . CYS   A 50  ? 0.6277 0.3399 0.1509 -0.2582 0.0822  -0.0275 56  CYS   A CB  
391  S  SG  . CYS   A 50  ? 0.5667 0.3690 0.2044 -0.2027 0.0670  -0.0217 56  CYS   A SG  
392  N  N   . ASP   A 51  ? 0.6285 0.3995 0.1510 -0.2922 -0.0129 0.0365  57  ASP   A N   
393  C  CA  . ASP   A 51  ? 0.5954 0.4288 0.1794 -0.2831 -0.0534 0.0704  57  ASP   A CA  
394  C  C   . ASP   A 51  ? 0.5560 0.4303 0.1915 -0.2608 -0.0583 0.0764  57  ASP   A C   
395  O  O   . ASP   A 51  ? 0.5532 0.4532 0.2116 -0.2730 -0.0910 0.1081  57  ASP   A O   
396  C  CB  . ASP   A 51  ? 0.6456 0.4570 0.1832 -0.3325 -0.0961 0.1046  57  ASP   A CB  
397  C  CG  . ASP   A 51  ? 0.7691 0.5506 0.2565 -0.3741 -0.1237 0.1236  57  ASP   A CG  
398  O  OD1 . ASP   A 51  ? 0.7966 0.5559 0.2590 -0.3715 -0.1014 0.1025  57  ASP   A OD1 
399  O  OD2 . ASP   A 51  ? 0.8324 0.6133 0.3100 -0.4108 -0.1707 0.1628  57  ASP   A OD2 
400  N  N   . CYS   A 52  ? 0.5310 0.4085 0.1866 -0.2308 -0.0267 0.0488  58  CYS   A N   
401  C  CA  . CYS   A 52  ? 0.4786 0.3891 0.1765 -0.2098 -0.0288 0.0520  58  CYS   A CA  
402  C  C   . CYS   A 52  ? 0.4060 0.3751 0.1788 -0.1808 -0.0440 0.0740  58  CYS   A C   
403  O  O   . CYS   A 52  ? 0.4023 0.3887 0.2045 -0.1620 -0.0402 0.0741  58  CYS   A O   
404  C  CB  . CYS   A 52  ? 0.4734 0.3731 0.1806 -0.1853 0.0050  0.0210  58  CYS   A CB  
405  S  SG  . CYS   A 52  ? 0.5400 0.3721 0.1753 -0.2154 0.0309  -0.0003 58  CYS   A SG  
406  N  N   . GLN   A 53  ? 0.3596 0.3535 0.1614 -0.1787 -0.0579 0.0934  59  GLN   A N   
407  C  CA  . GLN   A 53  ? 0.3161 0.3560 0.1894 -0.1496 -0.0607 0.1133  59  GLN   A CA  
408  C  C   . GLN   A 53  ? 0.2905 0.3405 0.1846 -0.1236 -0.0440 0.1014  59  GLN   A C   
409  O  O   . GLN   A 53  ? 0.2623 0.3395 0.2056 -0.1053 -0.0430 0.1199  59  GLN   A O   
410  C  CB  . GLN   A 53  ? 0.3151 0.3795 0.2250 -0.1688 -0.0915 0.1580  59  GLN   A CB  
411  C  CG  . GLN   A 53  ? 0.3263 0.3966 0.2483 -0.1788 -0.1059 0.1761  59  GLN   A CG  
412  C  CD  . GLN   A 53  ? 0.3366 0.4379 0.3188 -0.1944 -0.1374 0.2278  59  GLN   A CD  
413  O  OE1 . GLN   A 53  ? 0.3940 0.4809 0.3507 -0.2365 -0.1730 0.2534  59  GLN   A OE1 
414  N  NE2 . GLN   A 53  ? 0.2723 0.4116 0.3371 -0.1630 -0.1243 0.2474  59  GLN   A NE2 
415  N  N   . THR   A 54  ? 0.3004 0.3244 0.1583 -0.1239 -0.0291 0.0727  60  THR   A N   
416  C  CA  . THR   A 54  ? 0.2820 0.3099 0.1532 -0.1024 -0.0154 0.0595  60  THR   A CA  
417  C  C   . THR   A 54  ? 0.2620 0.2673 0.1187 -0.0907 0.0039  0.0291  60  THR   A C   
418  O  O   . THR   A 54  ? 0.2727 0.2510 0.0993 -0.1068 0.0117  0.0159  60  THR   A O   
419  C  CB  . THR   A 54  ? 0.3285 0.3523 0.1854 -0.1198 -0.0233 0.0664  60  THR   A CB  
420  O  OG1 . THR   A 54  ? 0.3814 0.3670 0.1864 -0.1422 -0.0157 0.0466  60  THR   A OG1 
421  C  CG2 . THR   A 54  ? 0.3239 0.3660 0.1974 -0.1406 -0.0491 0.1025  60  THR   A CG2 
422  N  N   . GLY   A 55  ? 0.2325 0.2437 0.1112 -0.0652 0.0119  0.0207  61  GLY   A N   
423  C  CA  . GLY   A 55  ? 0.2357 0.2295 0.1166 -0.0538 0.0233  -0.0002 61  GLY   A CA  
424  C  C   . GLY   A 55  ? 0.2250 0.2195 0.1209 -0.0331 0.0232  -0.0032 61  GLY   A C   
425  O  O   . GLY   A 55  ? 0.2223 0.2265 0.1206 -0.0278 0.0208  0.0070  61  GLY   A O   
426  N  N   . VAL   A 56  ? 0.2162 0.1961 0.1221 -0.0237 0.0247  -0.0146 62  VAL   A N   
427  C  CA  . VAL   A 56  ? 0.2230 0.1917 0.1327 -0.0109 0.0185  -0.0161 62  VAL   A CA  
428  C  C   . VAL   A 56  ? 0.2338 0.1892 0.1480 -0.0024 0.0119  -0.0180 62  VAL   A C   
429  O  O   . VAL   A 56  ? 0.2312 0.1853 0.1624 -0.0059 0.0139  -0.0227 62  VAL   A O   
430  C  CB  . VAL   A 56  ? 0.2328 0.1919 0.1563 -0.0156 0.0192  -0.0231 62  VAL   A CB  
431  C  CG1 . VAL   A 56  ? 0.2486 0.1907 0.1733 -0.0075 0.0053  -0.0211 62  VAL   A CG1 
432  C  CG2 . VAL   A 56  ? 0.2517 0.2192 0.1647 -0.0256 0.0258  -0.0221 62  VAL   A CG2 
433  N  N   . TYR   A 57  ? 0.2555 0.1956 0.1501 0.0070  0.0069  -0.0137 63  TYR   A N   
434  C  CA  . TYR   A 57  ? 0.2697 0.1886 0.1581 0.0114  -0.0022 -0.0147 63  TYR   A CA  
435  C  C   . TYR   A 57  ? 0.3130 0.1950 0.1807 0.0100  -0.0191 -0.0139 63  TYR   A C   
436  O  O   . TYR   A 57  ? 0.3301 0.1994 0.1756 0.0096  -0.0181 -0.0123 63  TYR   A O   
437  C  CB  . TYR   A 57  ? 0.2742 0.1927 0.1468 0.0190  0.0077  -0.0097 63  TYR   A CB  
438  C  CG  . TYR   A 57  ? 0.3063 0.1996 0.1457 0.0263  0.0184  -0.0044 63  TYR   A CG  
439  C  CD1 . TYR   A 57  ? 0.3057 0.2149 0.1509 0.0289  0.0327  0.0035  63  TYR   A CD1 
440  C  CD2 . TYR   A 57  ? 0.3554 0.2021 0.1549 0.0288  0.0171  -0.0061 63  TYR   A CD2 
441  C  CE1 . TYR   A 57  ? 0.3482 0.2300 0.1687 0.0371  0.0516  0.0097  63  TYR   A CE1 
442  C  CE2 . TYR   A 57  ? 0.4016 0.2111 0.1609 0.0341  0.0365  -0.0027 63  TYR   A CE2 
443  C  CZ  . TYR   A 57  ? 0.3976 0.2255 0.1711 0.0398  0.0566  0.0051  63  TYR   A CZ  
444  O  OH  . TYR   A 57  ? 0.4357 0.2224 0.1750 0.0464  0.0840  0.0097  63  TYR   A OH  
445  N  N   . TYR   A 58  ? 0.3276 0.1885 0.1994 0.0068  -0.0369 -0.0125 64  TYR   A N   
446  C  CA  . TYR   A 58  ? 0.3680 0.1851 0.2125 -0.0014 -0.0615 -0.0070 64  TYR   A CA  
447  C  C   . TYR   A 58  ? 0.4039 0.1752 0.1821 -0.0009 -0.0591 -0.0072 64  TYR   A C   
448  O  O   . TYR   A 58  ? 0.3867 0.1559 0.1608 0.0032  -0.0542 -0.0085 64  TYR   A O   
449  C  CB  . TYR   A 58  ? 0.3635 0.1762 0.2532 -0.0100 -0.0881 0.0010  64  TYR   A CB  
450  C  CG  . TYR   A 58  ? 0.4144 0.1773 0.2735 -0.0249 -0.1230 0.0126  64  TYR   A CG  
451  C  CD1 . TYR   A 58  ? 0.4406 0.1916 0.2906 -0.0321 -0.1329 0.0170  64  TYR   A CD1 
452  C  CD2 . TYR   A 58  ? 0.4608 0.1835 0.2943 -0.0354 -0.1493 0.0207  64  TYR   A CD2 
453  C  CE1 . TYR   A 58  ? 0.5000 0.1980 0.3130 -0.0511 -0.1698 0.0303  64  TYR   A CE1 
454  C  CE2 . TYR   A 58  ? 0.5144 0.1799 0.3055 -0.0562 -0.1872 0.0341  64  TYR   A CE2 
455  C  CZ  . TYR   A 58  ? 0.5470 0.1991 0.3263 -0.0649 -0.1983 0.0394  64  TYR   A CZ  
456  O  OH  . TYR   A 58  ? 0.6252 0.2135 0.3541 -0.0905 -0.2404 0.0550  64  TYR   A OH  
457  N  N   . CYS   A 59  ? 0.4604 0.1876 0.1820 -0.0064 -0.0599 -0.0061 65  CYS   A N   
458  C  CA  . CYS   A 59  ? 0.5313 0.1966 0.1757 -0.0085 -0.0488 -0.0075 65  CYS   A CA  
459  C  C   . CYS   A 59  ? 0.5947 0.1882 0.1793 -0.0309 -0.0842 -0.0016 65  CYS   A C   
460  O  O   . CYS   A 59  ? 0.6153 0.1779 0.1659 -0.0416 -0.0937 0.0013  65  CYS   A O   
461  C  CB  . CYS   A 59  ? 0.5592 0.2184 0.1772 0.0014  -0.0127 -0.0096 65  CYS   A CB  
462  S  SG  . CYS   A 59  ? 0.6572 0.2229 0.1741 -0.0012 0.0164  -0.0117 65  CYS   A SG  
463  N  N   . SER   A 60  ? 0.6226 0.1881 0.1946 -0.0411 -0.1078 0.0025  66  SER   A N   
464  C  CA  . SER   A 60  ? 0.6963 0.1897 0.2116 -0.0689 -0.1512 0.0135  66  SER   A CA  
465  C  C   . SER   A 60  ? 0.7814 0.1814 0.1772 -0.0838 -0.1408 0.0098  66  SER   A C   
466  O  O   . SER   A 60  ? 0.8281 0.1745 0.1773 -0.1092 -0.1762 0.0200  66  SER   A O   
467  C  CB  . SER   A 60  ? 0.7464 0.2240 0.2685 -0.0788 -0.1791 0.0208  66  SER   A CB  
468  O  OG  . SER   A 60  ? 0.8117 0.2849 0.3094 -0.0650 -0.1458 0.0095  66  SER   A OG  
469  N  N   . SER   A 61  ? 0.8095 0.1858 0.1575 -0.0696 -0.0905 -0.0024 67  SER   A N   
470  C  CA  . SER   A 61  ? 0.8913 0.1665 0.1199 -0.0824 -0.0660 -0.0075 67  SER   A CA  
471  C  C   . SER   A 61  ? 0.9041 0.1749 0.1192 -0.0839 -0.0576 -0.0072 67  SER   A C   
472  O  O   . SER   A 61  ? 0.9902 0.1661 0.0984 -0.1011 -0.0449 -0.0096 67  SER   A O   
473  C  CB  . SER   A 61  ? 0.9168 0.1700 0.1168 -0.0637 -0.0061 -0.0174 67  SER   A CB  
474  O  OG  . SER   A 61  ? 0.8569 0.1928 0.1412 -0.0334 0.0339  -0.0189 67  SER   A OG  
475  N  N   . ARG   A 62  ? 0.8225 0.1858 0.1367 -0.0695 -0.0654 -0.0042 68  ARG   A N   
476  C  CA  . ARG   A 62  ? 0.8176 0.1859 0.1311 -0.0717 -0.0648 -0.0025 68  ARG   A CA  
477  C  C   . ARG   A 62  ? 0.8036 0.2118 0.1791 -0.0843 -0.1177 0.0093  68  ARG   A C   
478  O  O   . ARG   A 62  ? 0.8030 0.2164 0.1826 -0.0882 -0.1233 0.0123  68  ARG   A O   
479  C  CB  . ARG   A 62  ? 0.7716 0.2135 0.1517 -0.0425 -0.0197 -0.0077 68  ARG   A CB  
480  C  CG  . ARG   A 62  ? 0.8123 0.2147 0.1467 -0.0294 0.0372  -0.0127 68  ARG   A CG  
481  C  CD  . ARG   A 62  ? 0.8926 0.1955 0.1199 -0.0444 0.0558  -0.0147 68  ARG   A CD  
482  N  NE  . ARG   A 62  ? 0.9535 0.2195 0.1528 -0.0285 0.1208  -0.0176 68  ARG   A NE  
483  C  CZ  . ARG   A 62  ? 1.0405 0.2237 0.1627 -0.0345 0.1471  -0.0223 68  ARG   A CZ  
484  N  NH1 . ARG   A 62  ? 1.0980 0.2198 0.1492 -0.0601 0.1077  -0.0249 68  ARG   A NH1 
485  N  NH2 . ARG   A 62  ? 1.0543 0.2117 0.1726 -0.0162 0.2137  -0.0219 68  ARG   A NH2 
486  N  N   . ARG   A 63  ? 0.7827 0.2225 0.2173 -0.0887 -0.1521 0.0175  69  ARG   A N   
487  C  CA  . ARG   A 63  ? 0.7535 0.2397 0.2747 -0.0959 -0.1931 0.0320  69  ARG   A CA  
488  C  C   . ARG   A 63  ? 0.6826 0.2442 0.2791 -0.0763 -0.1693 0.0264  69  ARG   A C   
489  O  O   . ARG   A 63  ? 0.6768 0.2483 0.3050 -0.0848 -0.1906 0.0360  69  ARG   A O   
490  C  CB  . ARG   A 63  ? 0.8380 0.2547 0.3108 -0.1305 -0.2470 0.0513  69  ARG   A CB  
491  C  CG  . ARG   A 63  ? 0.9854 0.3218 0.3774 -0.1546 -0.2741 0.0580  69  ARG   A CG  
492  C  CD  . ARG   A 63  ? 1.1135 0.3897 0.4788 -0.1945 -0.3422 0.0853  69  ARG   A CD  
493  N  NE  . ARG   A 63  ? 1.1367 0.4786 0.6347 -0.1953 -0.3817 0.1087  69  ARG   A NE  
494  C  CZ  . ARG   A 63  ? 1.1768 0.5341 0.7273 -0.1978 -0.4038 0.1205  69  ARG   A CZ  
495  N  NH1 . ARG   A 63  ? 1.2116 0.5269 0.6902 -0.1994 -0.3924 0.1091  69  ARG   A NH1 
496  N  NH2 . ARG   A 63  ? 1.1320 0.5466 0.8128 -0.1973 -0.4326 0.1443  69  ARG   A NH2 
497  N  N   . LYS   A 64  ? 0.6243 0.2322 0.2426 -0.0526 -0.1255 0.0126  70  LYS   A N   
498  C  CA  . LYS   A 64  ? 0.5683 0.2367 0.2404 -0.0380 -0.1024 0.0074  70  LYS   A CA  
499  C  C   . LYS   A 64  ? 0.4908 0.2215 0.2221 -0.0208 -0.0782 0.0005  70  LYS   A C   
500  O  O   . LYS   A 64  ? 0.4910 0.2151 0.2061 -0.0152 -0.0671 -0.0027 70  LYS   A O   
501  C  CB  . LYS   A 64  ? 0.6184 0.2637 0.2338 -0.0315 -0.0705 0.0015  70  LYS   A CB  
502  C  CG  . LYS   A 64  ? 0.7096 0.3338 0.3020 -0.0409 -0.0796 0.0052  70  LYS   A CG  
503  C  CD  . LYS   A 64  ? 0.7879 0.4180 0.3612 -0.0270 -0.0380 -0.0002 70  LYS   A CD  
504  C  CE  . LYS   A 64  ? 0.8831 0.4798 0.4171 -0.0359 -0.0406 0.0023  70  LYS   A CE  
505  N  NZ  . LYS   A 64  ? 0.9874 0.4861 0.4170 -0.0550 -0.0481 0.0038  70  LYS   A NZ  
506  N  N   . HIS   A 65  ? 0.4207 0.2038 0.2098 -0.0148 -0.0683 -0.0017 71  HIS   A N   
507  C  CA  . HIS   A 65  ? 0.3815 0.2134 0.2107 -0.0047 -0.0460 -0.0075 71  HIS   A CA  
508  C  C   . HIS   A 65  ? 0.3815 0.2289 0.1935 0.0029  -0.0206 -0.0090 71  HIS   A C   
509  O  O   . HIS   A 65  ? 0.4032 0.2404 0.1983 0.0013  -0.0191 -0.0074 71  HIS   A O   
510  C  CB  . HIS   A 65  ? 0.3473 0.2125 0.2395 -0.0077 -0.0474 -0.0083 71  HIS   A CB  
511  C  CG  . HIS   A 65  ? 0.3489 0.2059 0.2827 -0.0136 -0.0677 -0.0016 71  HIS   A CG  
512  N  ND1 . HIS   A 65  ? 0.3482 0.2222 0.3177 -0.0108 -0.0592 -0.0038 71  HIS   A ND1 
513  C  CD2 . HIS   A 65  ? 0.3600 0.1943 0.3121 -0.0235 -0.0964 0.0107  71  HIS   A CD2 
514  C  CE1 . HIS   A 65  ? 0.3355 0.1980 0.3486 -0.0168 -0.0805 0.0076  71  HIS   A CE1 
515  N  NE2 . HIS   A 65  ? 0.3526 0.1925 0.3604 -0.0256 -0.1059 0.0185  71  HIS   A NE2 
516  N  N   . TYR   A 66  ? 0.3459 0.2164 0.1658 0.0101  -0.0026 -0.0086 72  TYR   A N   
517  C  CA  . TYR   A 66  ? 0.3357 0.2247 0.1560 0.0159  0.0180  -0.0027 72  TYR   A CA  
518  C  C   . TYR   A 66  ? 0.3023 0.2362 0.1598 0.0129  0.0228  0.0004  72  TYR   A C   
519  O  O   . TYR   A 66  ? 0.2698 0.2134 0.1388 0.0121  0.0213  -0.0008 72  TYR   A O   
520  C  CB  . TYR   A 66  ? 0.3637 0.2251 0.1546 0.0254  0.0372  0.0030  72  TYR   A CB  
521  C  CG  . TYR   A 66  ? 0.4288 0.2293 0.1613 0.0241  0.0400  0.0006  72  TYR   A CG  
522  C  CD1 . TYR   A 66  ? 0.4692 0.2554 0.1839 0.0239  0.0496  0.0032  72  TYR   A CD1 
523  C  CD2 . TYR   A 66  ? 0.4829 0.2325 0.1695 0.0206  0.0347  -0.0032 72  TYR   A CD2 
524  C  CE1 . TYR   A 66  ? 0.5345 0.2526 0.1814 0.0189  0.0543  0.0009  72  TYR   A CE1 
525  C  CE2 . TYR   A 66  ? 0.5483 0.2259 0.1622 0.0133  0.0376  -0.0049 72  TYR   A CE2 
526  C  CZ  . TYR   A 66  ? 0.5822 0.2421 0.1737 0.0120  0.0482  -0.0032 72  TYR   A CZ  
527  O  OH  . TYR   A 66  ? 0.6737 0.2510 0.1803 0.0011  0.0531  -0.0053 72  TYR   A OH  
528  N  N   . PRO   A 67  ? 0.2944 0.2508 0.1646 0.0086  0.0273  0.0061  73  PRO   A N   
529  C  CA  . PRO   A 67  ? 0.2665 0.2543 0.1578 -0.0011 0.0274  0.0131  73  PRO   A CA  
530  C  C   . PRO   A 67  ? 0.2657 0.2664 0.1712 0.0051  0.0360  0.0308  73  PRO   A C   
531  O  O   . PRO   A 67  ? 0.2727 0.2637 0.1788 0.0167  0.0499  0.0403  73  PRO   A O   
532  C  CB  . PRO   A 67  ? 0.2731 0.2721 0.1677 -0.0099 0.0263  0.0168  73  PRO   A CB  
533  C  CG  . PRO   A 67  ? 0.2998 0.2826 0.1838 0.0018  0.0330  0.0192  73  PRO   A CG  
534  C  CD  . PRO   A 67  ? 0.3027 0.2520 0.1636 0.0094  0.0303  0.0085  73  PRO   A CD  
535  N  N   . VAL   A 68  ? 0.2404 0.2588 0.1595 -0.0032 0.0306  0.0373  74  VAL   A N   
536  C  CA  . VAL   A 68  ? 0.2372 0.2712 0.1829 0.0013  0.0361  0.0588  74  VAL   A CA  
537  C  C   . VAL   A 68  ? 0.2364 0.2958 0.1998 -0.0189 0.0207  0.0757  74  VAL   A C   
538  O  O   . VAL   A 68  ? 0.2472 0.3016 0.1874 -0.0365 0.0097  0.0642  74  VAL   A O   
539  C  CB  . VAL   A 68  ? 0.2433 0.2624 0.1839 0.0136  0.0437  0.0532  74  VAL   A CB  
540  C  CG1 . VAL   A 68  ? 0.2771 0.2611 0.1956 0.0305  0.0611  0.0468  74  VAL   A CG1 
541  C  CG2 . VAL   A 68  ? 0.2510 0.2637 0.1746 0.0058  0.0319  0.0346  74  VAL   A CG2 
542  N  N   . SER   A 69  ? 0.2133 0.2944 0.2185 -0.0186 0.0209  0.1059  75  SER   A N   
543  C  CA  . SER   A 69  ? 0.2145 0.3160 0.2388 -0.0406 -0.0002 0.1289  75  SER   A CA  
544  C  C   . SER   A 69  ? 0.2083 0.3112 0.2507 -0.0275 0.0086  0.1325  75  SER   A C   
545  O  O   . SER   A 69  ? 0.2075 0.3029 0.2681 -0.0033 0.0327  0.1336  75  SER   A O   
546  C  CB  . SER   A 69  ? 0.2240 0.3514 0.3000 -0.0495 -0.0101 0.1678  75  SER   A CB  
547  O  OG  . SER   A 69  ? 0.3090 0.4339 0.3633 -0.0673 -0.0236 0.1659  75  SER   A OG  
548  N  N   . PHE   A 70  ? 0.2030 0.3071 0.2317 -0.0441 -0.0073 0.1318  76  PHE   A N   
549  C  CA  . PHE   A 70  ? 0.2107 0.3166 0.2556 -0.0326 -0.0003 0.1344  76  PHE   A CA  
550  C  C   . PHE   A 70  ? 0.2305 0.3547 0.2974 -0.0558 -0.0242 0.1625  76  PHE   A C   
551  O  O   . PHE   A 70  ? 0.2568 0.3796 0.3016 -0.0867 -0.0490 0.1713  76  PHE   A O   
552  C  CB  . PHE   A 70  ? 0.2218 0.3022 0.2238 -0.0227 0.0089  0.0990  76  PHE   A CB  
553  C  CG  . PHE   A 70  ? 0.2285 0.2943 0.1878 -0.0429 -0.0018 0.0785  76  PHE   A CG  
554  C  CD1 . PHE   A 70  ? 0.2388 0.2891 0.1726 -0.0450 0.0022  0.0593  76  PHE   A CD1 
555  C  CD2 . PHE   A 70  ? 0.2347 0.2964 0.1797 -0.0589 -0.0109 0.0782  76  PHE   A CD2 
556  C  CE1 . PHE   A 70  ? 0.2638 0.2939 0.1644 -0.0618 0.0021  0.0413  76  PHE   A CE1 
557  C  CE2 . PHE   A 70  ? 0.2590 0.2959 0.1618 -0.0767 -0.0102 0.0582  76  PHE   A CE2 
558  C  CZ  . PHE   A 70  ? 0.2669 0.2874 0.1500 -0.0781 -0.0017 0.0406  76  PHE   A CZ  
559  N  N   . SER   A 71  ? 0.2075 0.3440 0.3160 -0.0439 -0.0175 0.1795  77  SER   A N   
560  C  CA  . SER   A 71  ? 0.2140 0.3691 0.3517 -0.0663 -0.0431 0.2114  77  SER   A CA  
561  C  C   . SER   A 71  ? 0.2582 0.3938 0.3378 -0.0848 -0.0564 0.1899  77  SER   A C   
562  O  O   . SER   A 71  ? 0.2790 0.3915 0.3122 -0.0744 -0.0409 0.1525  77  SER   A O   
563  C  CB  . SER   A 71  ? 0.1990 0.3746 0.4131 -0.0454 -0.0270 0.2405  77  SER   A CB  
564  O  OG  . SER   A 71  ? 0.2482 0.4054 0.4425 -0.0208 -0.0011 0.2135  77  SER   A OG  
565  N  N   . LYS   A 72  ? 0.2741 0.4157 0.3579 -0.1143 -0.0855 0.2162  78  LYS   A N   
566  C  CA  . LYS   A 72  ? 0.3193 0.4365 0.3464 -0.1342 -0.0949 0.1993  78  LYS   A CA  
567  C  C   . LYS   A 72  ? 0.3119 0.4375 0.3653 -0.1089 -0.0782 0.1925  78  LYS   A C   
568  O  O   . LYS   A 72  ? 0.2842 0.4353 0.4045 -0.0883 -0.0695 0.2154  78  LYS   A O   
569  C  CB  . LYS   A 72  ? 0.3811 0.4914 0.3908 -0.1811 -0.1359 0.2324  78  LYS   A CB  
570  C  CG  . LYS   A 72  ? 0.4836 0.5743 0.4518 -0.2132 -0.1559 0.2388  78  LYS   A CG  
571  C  CD  . LYS   A 72  ? 0.6011 0.6518 0.4978 -0.2685 -0.1918 0.2529  78  LYS   A CD  
572  C  CE  . LYS   A 72  ? 0.7106 0.7273 0.5470 -0.3035 -0.2083 0.2538  78  LYS   A CE  
573  N  NZ  . LYS   A 72  ? 0.8050 0.7742 0.5676 -0.3649 -0.2500 0.2771  78  LYS   A NZ  
574  N  N   . PRO   A 73  ? 0.3345 0.4357 0.3388 -0.1096 -0.0697 0.1620  79  PRO   A N   
575  C  CA  . PRO   A 73  ? 0.3402 0.4474 0.3666 -0.0863 -0.0553 0.1547  79  PRO   A CA  
576  C  C   . PRO   A 73  ? 0.3287 0.4618 0.4112 -0.0896 -0.0690 0.1922  79  PRO   A C   
577  O  O   . PRO   A 73  ? 0.3322 0.4664 0.4079 -0.1228 -0.0987 0.2168  79  PRO   A O   
578  C  CB  . PRO   A 73  ? 0.3755 0.4517 0.3423 -0.0982 -0.0516 0.1251  79  PRO   A CB  
579  C  CG  . PRO   A 73  ? 0.4036 0.4557 0.3257 -0.1088 -0.0458 0.1044  79  PRO   A CG  
580  C  CD  . PRO   A 73  ? 0.3651 0.4285 0.2958 -0.1300 -0.0674 0.1330  79  PRO   A CD  
581  N  N   . SER   A 74  ? 0.3112 0.4588 0.4457 -0.0576 -0.0467 0.1977  80  SER   A N   
582  C  CA  . SER   A 74  ? 0.2912 0.4640 0.4942 -0.0555 -0.0520 0.2353  80  SER   A CA  
583  C  C   . SER   A 74  ? 0.2738 0.4416 0.5008 -0.0209 -0.0189 0.2240  80  SER   A C   
584  O  O   . SER   A 74  ? 0.2849 0.4272 0.4711 -0.0009 0.0038  0.1885  80  SER   A O   
585  C  CB  . SER   A 74  ? 0.2954 0.4950 0.5698 -0.0597 -0.0595 0.2787  80  SER   A CB  
586  O  OG  . SER   A 74  ? 0.3428 0.5361 0.6286 -0.0320 -0.0269 0.2665  80  SER   A OG  
587  N  N   . LEU   A 75  ? 0.2428 0.4311 0.5362 -0.0168 -0.0181 0.2571  81  LEU   A N   
588  C  CA  . LEU   A 75  ? 0.2504 0.4296 0.5710 0.0128  0.0153  0.2527  81  LEU   A CA  
589  C  C   . LEU   A 75  ? 0.2541 0.4282 0.6245 0.0379  0.0531  0.2668  81  LEU   A C   
590  O  O   . LEU   A 75  ? 0.2307 0.4325 0.6828 0.0342  0.0513  0.3107  81  LEU   A O   
591  C  CB  . LEU   A 75  ? 0.2238 0.4273 0.6034 0.0046  0.0017  0.2871  81  LEU   A CB  
592  C  CG  . LEU   A 75  ? 0.2588 0.4545 0.5913 -0.0071 -0.0159 0.2681  81  LEU   A CG  
593  C  CD1 . LEU   A 75  ? 0.2391 0.4613 0.6361 -0.0192 -0.0342 0.3091  81  LEU   A CD1 
594  C  CD2 . LEU   A 75  ? 0.2905 0.4557 0.5818 0.0196  0.0146  0.2288  81  LEU   A CD2 
595  N  N   . ILE   A 76  ? 0.2843 0.4186 0.6083 0.0613  0.0878  0.2335  82  ILE   A N   
596  C  CA  . ILE   A 76  ? 0.3036 0.4167 0.6570 0.0836  0.1313  0.2426  82  ILE   A CA  
597  C  C   . ILE   A 76  ? 0.3559 0.4199 0.6824 0.1071  0.1739  0.2237  82  ILE   A C   
598  O  O   . ILE   A 76  ? 0.3908 0.4242 0.6402 0.1069  0.1673  0.1873  82  ILE   A O   
599  C  CB  . ILE   A 76  ? 0.3238 0.4198 0.6256 0.0819  0.1311  0.2205  82  ILE   A CB  
600  C  CG1 . ILE   A 76  ? 0.3086 0.4458 0.6370 0.0581  0.0940  0.2419  82  ILE   A CG1 
601  C  CG2 . ILE   A 76  ? 0.3417 0.3978 0.6480 0.1050  0.1821  0.2206  82  ILE   A CG2 
602  C  CD1 . ILE   A 76  ? 0.3541 0.4768 0.6085 0.0486  0.0787  0.2088  82  ILE   A CD1 
603  N  N   . PHE   A 77  ? 0.3554 0.4057 0.7439 0.1258  0.2195  0.2495  83  PHE   A N   
604  C  CA  . PHE   A 77  ? 0.4174 0.4074 0.7727 0.1456  0.2671  0.2330  83  PHE   A CA  
605  C  C   . PHE   A 77  ? 0.4815 0.3981 0.7302 0.1517  0.2910  0.1929  83  PHE   A C   
606  O  O   . PHE   A 77  ? 0.4857 0.3930 0.7229 0.1518  0.2993  0.1915  83  PHE   A O   
607  C  CB  . PHE   A 77  ? 0.4108 0.3996 0.8667 0.1633  0.3174  0.2742  83  PHE   A CB  
608  C  CG  . PHE   A 77  ? 0.4743 0.3902 0.8986 0.1832  0.3777  0.2612  83  PHE   A CG  
609  C  CD1 . PHE   A 77  ? 0.4910 0.4039 0.9201 0.1858  0.3777  0.2600  83  PHE   A CD1 
610  C  CD2 . PHE   A 77  ? 0.5334 0.3768 0.9194 0.1974  0.4376  0.2512  83  PHE   A CD2 
611  C  CE1 . PHE   A 77  ? 0.5404 0.3782 0.9356 0.2020  0.4362  0.2487  83  PHE   A CE1 
612  C  CE2 . PHE   A 77  ? 0.5850 0.3468 0.9320 0.2121  0.4989  0.2402  83  PHE   A CE2 
613  C  CZ  . PHE   A 77  ? 0.5785 0.3372 0.9281 0.2139  0.4972  0.2382  83  PHE   A CZ  
614  N  N   . VAL   A 78  ? 0.5333 0.3958 0.7035 0.1539  0.2982  0.1627  84  VAL   A N   
615  C  CA  . VAL   A 78  ? 0.6145 0.3968 0.6727 0.1527  0.3114  0.1272  84  VAL   A CA  
616  C  C   . VAL   A 78  ? 0.6816 0.3841 0.6951 0.1628  0.3587  0.1189  84  VAL   A C   
617  O  O   . VAL   A 78  ? 0.6684 0.3806 0.6948 0.1636  0.3506  0.1197  84  VAL   A O   
618  C  CB  . VAL   A 78  ? 0.6336 0.4260 0.6273 0.1356  0.2556  0.0981  84  VAL   A CB  
619  C  CG1 . VAL   A 78  ? 0.7038 0.4147 0.5906 0.1298  0.2611  0.0693  84  VAL   A CG1 
620  C  CG2 . VAL   A 78  ? 0.5935 0.4546 0.6267 0.1249  0.2171  0.1055  84  VAL   A CG2 
621  N  N   . GLU   A 79  ? 0.7546 0.3708 0.7048 0.1677  0.4080  0.1093  85  GLU   A N   
622  C  CA  . GLU   A 79  ? 0.8428 0.3570 0.7347 0.1753  0.4707  0.1023  85  GLU   A CA  
623  C  C   . GLU   A 79  ? 0.9051 0.3668 0.7213 0.1673  0.4608  0.0809  85  GLU   A C   
624  O  O   . GLU   A 79  ? 0.8854 0.3667 0.7610 0.1779  0.4786  0.0960  85  GLU   A O   
625  C  CB  . GLU   A 79  ? 0.9473 0.3696 0.7468 0.1710  0.5071  0.0868  85  GLU   A CB  
626  C  CG  . GLU   A 79  ? 1.0047 0.4647 0.8844 0.1827  0.5340  0.1114  85  GLU   A CG  
627  C  CD  . GLU   A 79  ? 1.1234 0.5347 1.0543 0.2030  0.6215  0.1352  85  GLU   A CD  
628  O  OE1 . GLU   A 79  ? 1.1572 0.5477 1.1144 0.2125  0.6547  0.1439  85  GLU   A OE1 
629  O  OE2 . GLU   A 79  ? 1.1570 0.5493 1.1061 0.2100  0.6602  0.1464  85  GLU   A OE2 
630  N  N   . ALA   A 80  ? 0.9798 0.3660 0.6679 0.1482  0.4378  0.0500  86  ALA   A N   
631  C  CA  . ALA   A 80  ? 1.0279 0.3546 0.6328 0.1352  0.4208  0.0306  86  ALA   A CA  
632  C  C   . ALA   A 80  ? 1.0959 0.3375 0.5659 0.1094  0.3918  0.0052  86  ALA   A C   
633  O  O   . ALA   A 80  ? 1.1447 0.3307 0.5605 0.1044  0.4155  0.0007  86  ALA   A O   
634  C  CB  . ALA   A 80  ? 1.0643 0.3151 0.6520 0.1456  0.4878  0.0349  86  ALA   A CB  
635  N  N   . SER   A 81  ? 1.0998 0.3311 0.5206 0.0915  0.3387  -0.0080 87  SER   A N   
636  C  CA  . SER   A 81  ? 1.1578 0.3162 0.4651 0.0627  0.2981  -0.0247 87  SER   A CA  
637  C  C   . SER   A 81  ? 1.1931 0.3121 0.4438 0.0436  0.2573  -0.0332 87  SER   A C   
638  O  O   . SER   A 81  ? 1.1625 0.3179 0.4655 0.0555  0.2631  -0.0285 87  SER   A O   
639  C  CB  . SER   A 81  ? 1.1273 0.3688 0.4852 0.0592  0.2458  -0.0225 87  SER   A CB  
640  O  OG  . SER   A 81  ? 1.0807 0.4296 0.5359 0.0670  0.2055  -0.0159 87  SER   A OG  
641  N  N   . GLU   A 82  ? 1.2490 0.2937 0.3967 0.0119  0.2123  -0.0426 88  GLU   A N   
642  C  CA  . GLU   A 82  ? 1.2739 0.2864 0.3792 -0.0088 0.1654  -0.0453 88  GLU   A CA  
643  C  C   . GLU   A 82  ? 1.1570 0.2981 0.3853 0.0025  0.1154  -0.0369 88  GLU   A C   
644  O  O   . GLU   A 82  ? 1.1640 0.2975 0.3843 -0.0097 0.0785  -0.0359 88  GLU   A O   
645  C  CB  . GLU   A 82  ? 1.4073 0.3055 0.3773 -0.0508 0.1219  -0.0503 88  GLU   A CB  
646  C  CG  . GLU   A 82  ? 1.4770 0.4274 0.4810 -0.0634 0.0598  -0.0432 88  GLU   A CG  
647  C  CD  . GLU   A 82  ? 1.6617 0.5067 0.5463 -0.1075 0.0092  -0.0410 88  GLU   A CD  
648  O  OE1 . GLU   A 82  ? 1.6932 0.5051 0.5475 -0.1331 -0.0440 -0.0338 88  GLU   A OE1 
649  O  OE2 . GLU   A 82  ? 1.7382 0.5369 0.5654 -0.1182 0.0181  -0.0435 88  GLU   A OE2 
650  N  N   . TYR   A 83  ? 1.0482 0.3003 0.3869 0.0253  0.1202  -0.0301 89  TYR   A N   
651  C  CA  . TYR   A 83  ? 0.9418 0.3086 0.3903 0.0358  0.0854  -0.0233 89  TYR   A CA  
652  C  C   . TYR   A 83  ? 0.8596 0.3021 0.3991 0.0614  0.1182  -0.0152 89  TYR   A C   
653  O  O   . TYR   A 83  ? 0.8354 0.3307 0.4277 0.0644  0.0954  -0.0122 89  TYR   A O   
654  C  CB  . TYR   A 83  ? 0.9017 0.3246 0.3917 0.0343  0.0602  -0.0210 89  TYR   A CB  
655  C  CG  . TYR   A 83  ? 0.9512 0.2992 0.3562 0.0116  0.0398  -0.0250 89  TYR   A CG  
656  C  CD1 . TYR   A 83  ? 0.9904 0.2912 0.3483 -0.0148 -0.0118 -0.0232 89  TYR   A CD1 
657  C  CD2 . TYR   A 83  ? 0.9774 0.2986 0.3505 0.0144  0.0703  -0.0273 89  TYR   A CD2 
658  C  CE1 . TYR   A 83  ? 1.0520 0.2806 0.3305 -0.0404 -0.0370 -0.0226 89  TYR   A CE1 
659  C  CE2 . TYR   A 83  ? 1.0387 0.2857 0.3268 -0.0090 0.0508  -0.0303 89  TYR   A CE2 
660  C  CZ  . TYR   A 83  ? 1.0811 0.2818 0.3206 -0.0376 -0.0051 -0.0274 89  TYR   A CZ  
661  O  OH  . TYR   A 83  ? 1.1471 0.2711 0.3011 -0.0651 -0.0301 -0.0264 89  TYR   A OH  
662  N  N   . TYR   A 84  ? 0.8175 0.2676 0.3826 0.0783  0.1683  -0.0083 90  TYR   A N   
663  C  CA  . TYR   A 84  ? 0.7408 0.2669 0.4034 0.0985  0.1907  0.0067  90  TYR   A CA  
664  C  C   . TYR   A 84  ? 0.7660 0.2570 0.4388 0.1145  0.2549  0.0174  90  TYR   A C   
665  O  O   . TYR   A 84  ? 0.8063 0.2395 0.4372 0.1160  0.2925  0.0163  90  TYR   A O   
666  C  CB  . TYR   A 84  ? 0.6495 0.2687 0.3944 0.1045  0.1761  0.0175  90  TYR   A CB  
667  C  CG  . TYR   A 84  ? 0.5920 0.2553 0.3480 0.0924  0.1246  0.0101  90  TYR   A CG  
668  C  CD1 . TYR   A 84  ? 0.5828 0.2442 0.3200 0.0848  0.1102  0.0050  90  TYR   A CD1 
669  C  CD2 . TYR   A 84  ? 0.5513 0.2617 0.3469 0.0898  0.0956  0.0102  90  TYR   A CD2 
670  C  CE1 . TYR   A 84  ? 0.5556 0.2567 0.3143 0.0753  0.0701  0.0006  90  TYR   A CE1 
671  C  CE2 . TYR   A 84  ? 0.5243 0.2717 0.3395 0.0803  0.0587  0.0053  90  TYR   A CE2 
672  C  CZ  . TYR   A 84  ? 0.5239 0.2678 0.3243 0.0736  0.0475  0.0011  90  TYR   A CZ  
673  O  OH  . TYR   A 84  ? 0.4855 0.2582 0.3090 0.0648  0.0165  -0.0026 90  TYR   A OH  
674  N  N   . PRO   A 85  ? 0.7327 0.2669 0.4772 0.1279  0.2706  0.0320  91  PRO   A N   
675  C  CA  . PRO   A 85  ? 0.7288 0.2445 0.5149 0.1458  0.3343  0.0500  91  PRO   A CA  
676  C  C   . PRO   A 85  ? 0.6768 0.2656 0.5582 0.1566  0.3440  0.0741  91  PRO   A C   
677  O  O   . PRO   A 85  ? 0.6503 0.3008 0.5544 0.1486  0.3002  0.0735  91  PRO   A O   
678  C  CB  . PRO   A 85  ? 0.7145 0.2597 0.5519 0.1532  0.3351  0.0600  91  PRO   A CB  
679  C  CG  . PRO   A 85  ? 0.6729 0.2985 0.5443 0.1439  0.2718  0.0574  91  PRO   A CG  
680  C  CD  . PRO   A 85  ? 0.6859 0.2884 0.4847 0.1272  0.2331  0.0358  91  PRO   A CD  
681  N  N   . ALA   A 86  ? 0.6600 0.2419 0.6034 0.1735  0.4012  0.0982  92  ALA   A N   
682  C  CA  . ALA   A 86  ? 0.5978 0.2488 0.6440 0.1820  0.4086  0.1284  92  ALA   A CA  
683  C  C   . ALA   A 86  ? 0.5048 0.2615 0.6349 0.1756  0.3534  0.1461  92  ALA   A C   
684  O  O   . ALA   A 86  ? 0.4841 0.2622 0.6476 0.1774  0.3462  0.1540  92  ALA   A O   
685  C  CB  . ALA   A 86  ? 0.5982 0.2250 0.7161 0.2018  0.4799  0.1577  92  ALA   A CB  
686  N  N   . ARG   A 87  ? 0.4460 0.2594 0.5952 0.1651  0.3132  0.1491  93  ARG   A N   
687  C  CA  . ARG   A 87  ? 0.3723 0.2685 0.5770 0.1528  0.2611  0.1624  93  ARG   A CA  
688  C  C   . ARG   A 87  ? 0.3247 0.2735 0.5645 0.1419  0.2334  0.1762  93  ARG   A C   
689  O  O   . ARG   A 87  ? 0.3444 0.2692 0.5605 0.1448  0.2496  0.1703  93  ARG   A O   
690  C  CB  . ARG   A 87  ? 0.3849 0.2740 0.5198 0.1411  0.2217  0.1308  93  ARG   A CB  
691  C  CG  . ARG   A 87  ? 0.4067 0.2883 0.4785 0.1291  0.1922  0.1054  93  ARG   A CG  
692  C  CD  . ARG   A 87  ? 0.4417 0.2803 0.4349 0.1224  0.1729  0.0747  93  ARG   A CD  
693  N  NE  . ARG   A 87  ? 0.4252 0.2875 0.3985 0.1089  0.1339  0.0603  93  ARG   A NE  
694  C  CZ  . ARG   A 87  ? 0.4090 0.2565 0.3525 0.1048  0.1305  0.0518  93  ARG   A CZ  
695  N  NH1 . ARG   A 87  ? 0.3936 0.2628 0.3282 0.0933  0.0984  0.0406  93  ARG   A NH1 
696  N  NH2 . ARG   A 87  ? 0.3927 0.2003 0.3168 0.1124  0.1632  0.0552  93  ARG   A NH2 
697  N  N   . TYR   A 88  ? 0.2738 0.2867 0.5609 0.1266  0.1916  0.1938  94  TYR   A N   
698  C  CA  . TYR   A 88  ? 0.2551 0.3085 0.5561 0.1100  0.1595  0.2031  94  TYR   A CA  
699  C  C   . TYR   A 88  ? 0.2344 0.2812 0.4557 0.0961  0.1257  0.1664  94  TYR   A C   
700  O  O   . TYR   A 88  ? 0.2295 0.2776 0.4285 0.0906  0.1084  0.1533  94  TYR   A O   
701  C  CB  . TYR   A 88  ? 0.2444 0.3569 0.6244 0.0936  0.1294  0.2431  94  TYR   A CB  
702  C  CG  . TYR   A 88  ? 0.2588 0.3891 0.7432 0.1045  0.1567  0.2898  94  TYR   A CG  
703  C  CD1 . TYR   A 88  ? 0.2716 0.4161 0.8040 0.1044  0.1643  0.3145  94  TYR   A CD1 
704  C  CD2 . TYR   A 88  ? 0.2701 0.4032 0.8140 0.1154  0.1769  0.3120  94  TYR   A CD2 
705  C  CE1 . TYR   A 88  ? 0.2531 0.4163 0.8991 0.1147  0.1911  0.3634  94  TYR   A CE1 
706  C  CE2 . TYR   A 88  ? 0.2573 0.4072 0.9136 0.1266  0.2063  0.3598  94  TYR   A CE2 
707  C  CZ  . TYR   A 88  ? 0.2561 0.4207 0.9667 0.1268  0.2147  0.3863  94  TYR   A CZ  
708  O  OH  . TYR   A 88  ? 0.2662 0.4502 1.1055 0.1379  0.2446  0.4397  94  TYR   A OH  
709  N  N   . GLN   A 89  ? 0.2123 0.2506 0.3976 0.0916  0.1196  0.1518  95  GLN   A N   
710  C  CA  . GLN   A 89  ? 0.2124 0.2446 0.3371 0.0793  0.0923  0.1215  95  GLN   A CA  
711  C  C   . GLN   A 89  ? 0.1892 0.2618 0.3314 0.0576  0.0624  0.1338  95  GLN   A C   
712  O  O   . GLN   A 89  ? 0.1858 0.2744 0.3555 0.0536  0.0627  0.1523  95  GLN   A O   
713  C  CB  . GLN   A 89  ? 0.2362 0.2274 0.3070 0.0857  0.1033  0.0981  95  GLN   A CB  
714  C  CG  . GLN   A 89  ? 0.2469 0.2352 0.2738 0.0735  0.0760  0.0728  95  GLN   A CG  
715  C  CD  . GLN   A 89  ? 0.3054 0.2464 0.2786 0.0783  0.0809  0.0514  95  GLN   A CD  
716  O  OE1 . GLN   A 89  ? 0.3251 0.2197 0.2659 0.0868  0.0966  0.0446  95  GLN   A OE1 
717  N  NE2 . GLN   A 89  ? 0.2857 0.2314 0.2433 0.0695  0.0655  0.0411  95  GLN   A NE2 
718  N  N   . SER   A 90  ? 0.1712 0.2547 0.2955 0.0415  0.0384  0.1256  96  SER   A N   
719  C  CA  . SER   A 90  ? 0.1654 0.2711 0.2877 0.0149  0.0121  0.1360  96  SER   A CA  
720  C  C   . SER   A 90  ? 0.1924 0.2825 0.2665 0.0066  0.0071  0.1107  96  SER   A C   
721  O  O   . SER   A 90  ? 0.2106 0.2766 0.2570 0.0203  0.0180  0.0851  96  SER   A O   
722  C  CB  . SER   A 90  ? 0.1833 0.2967 0.3007 -0.0018 -0.0056 0.1401  96  SER   A CB  
723  O  OG  . SER   A 90  ? 0.2300 0.3208 0.3085 0.0044  -0.0002 0.1088  96  SER   A OG  
724  N  N   . HIS   A 91  ? 0.1851 0.2851 0.2504 -0.0180 -0.0108 0.1212  97  HIS   A N   
725  C  CA  . HIS   A 91  ? 0.2041 0.2876 0.2264 -0.0293 -0.0131 0.1003  97  HIS   A CA  
726  C  C   . HIS   A 91  ? 0.2036 0.2804 0.2280 -0.0099 0.0015  0.0904  97  HIS   A C   
727  O  O   . HIS   A 91  ? 0.2115 0.2695 0.2069 -0.0071 0.0063  0.0663  97  HIS   A O   
728  C  CB  . HIS   A 91  ? 0.2331 0.2934 0.2192 -0.0324 -0.0086 0.0724  97  HIS   A CB  
729  C  CG  . HIS   A 91  ? 0.2865 0.3439 0.2585 -0.0541 -0.0192 0.0796  97  HIS   A CG  
730  N  ND1 . HIS   A 91  ? 0.3361 0.3732 0.2642 -0.0857 -0.0269 0.0783  97  HIS   A ND1 
731  C  CD2 . HIS   A 91  ? 0.2897 0.3565 0.2807 -0.0508 -0.0229 0.0897  97  HIS   A CD2 
732  C  CE1 . HIS   A 91  ? 0.3430 0.3747 0.2598 -0.1019 -0.0357 0.0871  97  HIS   A CE1 
733  N  NE2 . HIS   A 91  ? 0.3184 0.3720 0.2770 -0.0810 -0.0351 0.0950  97  HIS   A NE2 
734  N  N   . LEU   A 92  ? 0.1926 0.2822 0.2549 0.0022  0.0100  0.1115  98  LEU   A N   
735  C  CA  . LEU   A 92  ? 0.2117 0.2871 0.2705 0.0198  0.0280  0.1038  98  LEU   A CA  
736  C  C   . LEU   A 92  ? 0.2038 0.2950 0.2783 0.0095  0.0218  0.1206  98  LEU   A C   
737  O  O   . LEU   A 92  ? 0.1837 0.3009 0.3001 -0.0026 0.0101  0.1526  98  LEU   A O   
738  C  CB  . LEU   A 92  ? 0.2130 0.2777 0.2981 0.0427  0.0534  0.1136  98  LEU   A CB  
739  C  CG  . LEU   A 92  ? 0.2549 0.2860 0.3188 0.0599  0.0784  0.1029  98  LEU   A CG  
740  C  CD1 . LEU   A 92  ? 0.2880 0.2853 0.2927 0.0605  0.0720  0.0705  98  LEU   A CD1 
741  C  CD2 . LEU   A 92  ? 0.2775 0.2858 0.3616 0.0792  0.1122  0.1146  98  LEU   A CD2 
742  N  N   . MET   A 93  ? 0.2051 0.2805 0.2509 0.0133  0.0272  0.1024  99  MET   A N   
743  C  CA  . MET   A 93  ? 0.1984 0.2858 0.2547 0.0046  0.0223  0.1152  99  MET   A CA  
744  C  C   . MET   A 93  ? 0.2210 0.2931 0.2837 0.0258  0.0469  0.1143  99  MET   A C   
745  O  O   . MET   A 93  ? 0.2552 0.2959 0.2815 0.0384  0.0588  0.0907  99  MET   A O   
746  C  CB  . MET   A 93  ? 0.2107 0.2893 0.2240 -0.0138 0.0082  0.0954  99  MET   A CB  
747  C  CG  . MET   A 93  ? 0.2413 0.3182 0.2334 -0.0363 -0.0075 0.0924  99  MET   A CG  
748  S  SD  . MET   A 93  ? 0.3049 0.3562 0.2447 -0.0555 -0.0090 0.0663  99  MET   A SD  
749  C  CE  . MET   A 93  ? 0.2612 0.2940 0.1964 -0.0309 0.0077  0.0371  99  MET   A CE  
750  N  N   . LEU   A 94  ? 0.2034 0.2925 0.3116 0.0278  0.0545  0.1423  100 LEU   A N   
751  C  CA  . LEU   A 94  ? 0.2151 0.2819 0.3258 0.0472  0.0848  0.1419  100 LEU   A CA  
752  C  C   . LEU   A 94  ? 0.2135 0.2864 0.3166 0.0392  0.0771  0.1416  100 LEU   A C   
753  O  O   . LEU   A 94  ? 0.1878 0.2895 0.3090 0.0191  0.0518  0.1568  100 LEU   A O   
754  C  CB  . LEU   A 94  ? 0.2077 0.2806 0.3858 0.0621  0.1137  0.1751  100 LEU   A CB  
755  C  CG  . LEU   A 94  ? 0.2495 0.3093 0.4386 0.0740  0.1310  0.1768  100 LEU   A CG  
756  C  CD1 . LEU   A 94  ? 0.2482 0.3075 0.5108 0.0908  0.1695  0.2107  100 LEU   A CD1 
757  C  CD2 . LEU   A 94  ? 0.3054 0.3128 0.4183 0.0843  0.1451  0.1398  100 LEU   A CD2 
758  N  N   . ALA   A 95  ? 0.2392 0.2795 0.3124 0.0528  0.0991  0.1266  101 ALA   A N   
759  C  CA  . ALA   A 95  ? 0.2533 0.2940 0.3172 0.0488  0.0969  0.1246  101 ALA   A CA  
760  C  C   . ALA   A 95  ? 0.2820 0.2851 0.3373 0.0677  0.1346  0.1249  101 ALA   A C   
761  O  O   . ALA   A 95  ? 0.3111 0.2720 0.3368 0.0803  0.1591  0.1145  101 ALA   A O   
762  C  CB  . ALA   A 95  ? 0.2806 0.3086 0.2882 0.0387  0.0761  0.0934  101 ALA   A CB  
763  N  N   . VAL   A 96  ? 0.2718 0.2829 0.3461 0.0674  0.1408  0.1368  102 VAL   A N   
764  C  CA  . VAL   A 96  ? 0.3069 0.2759 0.3652 0.0825  0.1792  0.1360  102 VAL   A CA  
765  C  C   . VAL   A 96  ? 0.3577 0.2890 0.3349 0.0777  0.1677  0.1025  102 VAL   A C   
766  O  O   . VAL   A 96  ? 0.3595 0.3133 0.3282 0.0653  0.1391  0.0940  102 VAL   A O   
767  C  CB  . VAL   A 96  ? 0.2951 0.2916 0.4201 0.0845  0.1915  0.1678  102 VAL   A CB  
768  C  CG1 . VAL   A 96  ? 0.3308 0.2744 0.4340 0.1007  0.2392  0.1656  102 VAL   A CG1 
769  C  CG2 . VAL   A 96  ? 0.2575 0.2958 0.4776 0.0855  0.1943  0.2087  102 VAL   A CG2 
770  N  N   . GLY   A 97  ? 0.3970 0.2682 0.3140 0.0843  0.1867  0.0849  103 GLY   A N   
771  C  CA  . GLY   A 97  ? 0.4403 0.2695 0.2821 0.0763  0.1702  0.0585  103 GLY   A CA  
772  C  C   . GLY   A 97  ? 0.4879 0.2424 0.2599 0.0786  0.1885  0.0452  103 GLY   A C   
773  O  O   . GLY   A 97  ? 0.4991 0.2400 0.2799 0.0867  0.2103  0.0512  103 GLY   A O   
774  N  N   . HIS   A 98  ? 0.5192 0.2210 0.2189 0.0688  0.1773  0.0286  104 HIS   A N   
775  C  CA  . HIS   A 98  ? 0.5836 0.2006 0.1981 0.0628  0.1866  0.0165  104 HIS   A CA  
776  C  C   . HIS   A 98  ? 0.5791 0.1962 0.1793 0.0540  0.1521  0.0066  104 HIS   A C   
777  O  O   . HIS   A 98  ? 0.5550 0.2114 0.1779 0.0453  0.1110  0.0017  104 HIS   A O   
778  C  CB  . HIS   A 98  ? 0.6464 0.1964 0.1810 0.0500  0.1835  0.0071  104 HIS   A CB  
779  C  CG  . HIS   A 98  ? 0.7618 0.2110 0.1913 0.0354  0.1854  -0.0040 104 HIS   A CG  
780  N  ND1 . HIS   A 98  ? 0.8441 0.2189 0.2223 0.0407  0.2373  -0.0037 104 HIS   A ND1 
781  C  CD2 . HIS   A 98  ? 0.8155 0.2286 0.1899 0.0142  0.1399  -0.0128 104 HIS   A CD2 
782  C  CE1 . HIS   A 98  ? 0.9165 0.2044 0.1938 0.0197  0.2208  -0.0149 104 HIS   A CE1 
783  N  NE2 . HIS   A 98  ? 0.9019 0.2129 0.1776 0.0026  0.1584  -0.0185 104 HIS   A NE2 
784  N  N   . SER   A 99  ? 0.6137 0.1770 0.1726 0.0555  0.1731  0.0043  105 SER   A N   
785  C  CA  . SER   A 99  ? 0.6541 0.1994 0.1864 0.0462  0.1455  -0.0039 105 SER   A CA  
786  C  C   . SER   A 99  ? 0.7521 0.2008 0.2013 0.0432  0.1789  -0.0083 105 SER   A C   
787  O  O   . SER   A 99  ? 0.7610 0.1838 0.2110 0.0566  0.2325  -0.0018 105 SER   A O   
788  C  CB  . SER   A 99  ? 0.6008 0.2259 0.2161 0.0558  0.1342  0.0020  105 SER   A CB  
789  O  OG  . SER   A 99  ? 0.6115 0.2501 0.2663 0.0720  0.1750  0.0145  105 SER   A OG  
790  N  N   . GLU   A 100 ? 0.8153 0.2061 0.1942 0.0241  0.1486  -0.0173 106 GLU   A N   
791  C  CA  . GLU   A 100 ? 0.9117 0.1999 0.1966 0.0151  0.1739  -0.0232 106 GLU   A CA  
792  C  C   . GLU   A 100 ? 0.9517 0.2351 0.2239 0.0017  0.1296  -0.0265 106 GLU   A C   
793  O  O   . GLU   A 100 ? 0.9190 0.2659 0.2458 -0.0034 0.0796  -0.0240 106 GLU   A O   
794  C  CB  . GLU   A 100 ? 1.0182 0.1913 0.1816 -0.0050 0.1887  -0.0296 106 GLU   A CB  
795  C  CG  . GLU   A 100 ? 1.0641 0.2283 0.1947 -0.0297 0.1292  -0.0304 106 GLU   A CG  
796  C  CD  . GLU   A 100 ? 1.1638 0.2135 0.1721 -0.0513 0.1451  -0.0348 106 GLU   A CD  
797  O  OE1 . GLU   A 100 ? 1.2632 0.1966 0.1503 -0.0770 0.1443  -0.0401 106 GLU   A OE1 
798  O  OE2 . GLU   A 100 ? 1.1453 0.2152 0.1720 -0.0451 0.1581  -0.0328 106 GLU   A OE2 
799  N  N   . PRO   A 101 ? 1.0160 0.2271 0.2248 -0.0037 0.1491  -0.0308 107 PRO   A N   
800  C  CA  . PRO   A 101 ? 1.0313 0.2414 0.2342 -0.0174 0.1029  -0.0316 107 PRO   A CA  
801  C  C   . PRO   A 101 ? 1.0455 0.2335 0.2134 -0.0462 0.0376  -0.0289 107 PRO   A C   
802  O  O   . PRO   A 101 ? 1.1277 0.2341 0.2047 -0.0676 0.0329  -0.0303 107 PRO   A O   
803  C  CB  . PRO   A 101 ? 1.1125 0.2166 0.2191 -0.0253 0.1378  -0.0378 107 PRO   A CB  
804  C  CG  . PRO   A 101 ? 1.1309 0.2001 0.2233 -0.0074 0.2136  -0.0388 107 PRO   A CG  
805  C  CD  . PRO   A 101 ? 1.0672 0.1905 0.2094 0.0020  0.2167  -0.0340 107 PRO   A CD  
806  N  N   . GLY   A 102 ? 0.9538 0.2190 0.2044 -0.0456 -0.0085 -0.0226 108 GLY   A N   
807  C  CA  . GLY   A 102 ? 0.9273 0.1949 0.1857 -0.0682 -0.0696 -0.0134 108 GLY   A CA  
808  C  C   . GLY   A 102 ? 0.8297 0.2030 0.2001 -0.0522 -0.0793 -0.0095 108 GLY   A C   
809  O  O   . GLY   A 102 ? 0.8082 0.2087 0.2250 -0.0638 -0.1248 0.0007  108 GLY   A O   
810  N  N   . ASP   A 103 ? 0.7619 0.1925 0.1796 -0.0267 -0.0354 -0.0151 109 ASP   A N   
811  C  CA  . ASP   A 103 ? 0.6699 0.1898 0.1788 -0.0142 -0.0395 -0.0129 109 ASP   A CA  
812  C  C   . ASP   A 103 ? 0.5772 0.1759 0.1754 -0.0018 -0.0446 -0.0117 109 ASP   A C   
813  O  O   . ASP   A 103 ? 0.5172 0.1778 0.1820 0.0034  -0.0503 -0.0103 109 ASP   A O   
814  C  CB  . ASP   A 103 ? 0.6674 0.2074 0.1832 0.0015  0.0027  -0.0154 109 ASP   A CB  
815  C  CG  . ASP   A 103 ? 0.7069 0.1995 0.1683 -0.0108 -0.0017 -0.0154 109 ASP   A CG  
816  O  OD1 . ASP   A 103 ? 0.6966 0.1828 0.1580 -0.0275 -0.0434 -0.0111 109 ASP   A OD1 
817  O  OD2 . ASP   A 103 ? 0.7472 0.2077 0.1706 -0.0040 0.0375  -0.0174 109 ASP   A OD2 
818  N  N   . CYS   A 104 ? 0.5632 0.1524 0.1563 0.0013  -0.0404 -0.0126 110 CYS   A N   
819  C  CA  . CYS   A 104 ? 0.5092 0.1643 0.1777 0.0111  -0.0436 -0.0116 110 CYS   A CA  
820  C  C   . CYS   A 104 ? 0.4630 0.1458 0.1850 0.0018  -0.0795 -0.0062 110 CYS   A C   
821  O  O   . CYS   A 104 ? 0.4997 0.1390 0.1962 -0.0154 -0.1123 0.0008  110 CYS   A O   
822  C  CB  . CYS   A 104 ? 0.5335 0.1615 0.1783 0.0127  -0.0379 -0.0126 110 CYS   A CB  
823  S  SG  . CYS   A 104 ? 0.5986 0.2190 0.2244 0.0306  0.0157  -0.0145 110 CYS   A SG  
824  N  N   . GLY   A 105 ? 0.4017 0.1488 0.1956 0.0106  -0.0726 -0.0070 111 GLY   A N   
825  C  CA  . GLY   A 105 ? 0.3744 0.1445 0.2293 0.0039  -0.0953 -0.0008 111 GLY   A CA  
826  C  C   . GLY   A 105 ? 0.3613 0.1535 0.2421 0.0030  -0.0920 -0.0008 111 GLY   A C   
827  O  O   . GLY   A 105 ? 0.3433 0.1627 0.2863 0.0015  -0.0956 0.0030  111 GLY   A O   
828  N  N   . GLY   A 106 ? 0.3714 0.1505 0.2084 0.0045  -0.0802 -0.0047 112 GLY   A N   
829  C  CA  . GLY   A 106 ? 0.3419 0.1440 0.2004 0.0045  -0.0743 -0.0056 112 GLY   A CA  
830  C  C   . GLY   A 106 ? 0.2942 0.1490 0.1991 0.0118  -0.0507 -0.0111 112 GLY   A C   
831  O  O   . GLY   A 106 ? 0.2828 0.1550 0.1803 0.0184  -0.0326 -0.0141 112 GLY   A O   
832  N  N   . ILE   A 107 ? 0.2527 0.1264 0.2042 0.0079  -0.0511 -0.0104 113 ILE   A N   
833  C  CA  . ILE   A 107 ? 0.2245 0.1304 0.2054 0.0086  -0.0278 -0.0164 113 ILE   A CA  
834  C  C   . ILE   A 107 ? 0.2253 0.1463 0.1831 0.0083  -0.0128 -0.0201 113 ILE   A C   
835  O  O   . ILE   A 107 ? 0.2314 0.1445 0.1790 0.0071  -0.0181 -0.0187 113 ILE   A O   
836  C  CB  . ILE   A 107 ? 0.2350 0.1430 0.2767 0.0039  -0.0268 -0.0133 113 ILE   A CB  
837  C  CG1 . ILE   A 107 ? 0.2404 0.1434 0.3222 0.0045  -0.0341 -0.0071 113 ILE   A CG1 
838  C  CG2 . ILE   A 107 ? 0.2394 0.1625 0.2932 0.0000  0.0029  -0.0216 113 ILE   A CG2 
839  C  CD1 . ILE   A 107 ? 0.2459 0.1476 0.4080 0.0012  -0.0315 0.0032  113 ILE   A CD1 
840  N  N   . LEU   A 108 ? 0.2108 0.1519 0.1640 0.0061  0.0034  -0.0225 114 LEU   A N   
841  C  CA  . LEU   A 108 ? 0.2085 0.1654 0.1473 0.0003  0.0139  -0.0217 114 LEU   A CA  
842  C  C   . LEU   A 108 ? 0.2181 0.1748 0.1692 -0.0126 0.0282  -0.0285 114 LEU   A C   
843  O  O   . LEU   A 108 ? 0.2013 0.1538 0.1613 -0.0163 0.0363  -0.0317 114 LEU   A O   
844  C  CB  . LEU   A 108 ? 0.2157 0.1872 0.1408 0.0014  0.0169  -0.0137 114 LEU   A CB  
845  C  CG  . LEU   A 108 ? 0.2324 0.2218 0.1497 -0.0109 0.0210  -0.0059 114 LEU   A CG  
846  C  CD1 . LEU   A 108 ? 0.2473 0.2394 0.1599 -0.0089 0.0206  -0.0016 114 LEU   A CD1 
847  C  CD2 . LEU   A 108 ? 0.2255 0.2314 0.1464 -0.0105 0.0193  0.0094  114 LEU   A CD2 
848  N  N   . ARG   A 109 ? 0.2247 0.1792 0.1726 -0.0198 0.0348  -0.0311 115 ARG   A N   
849  C  CA  . ARG   A 109 ? 0.2384 0.1788 0.1879 -0.0337 0.0552  -0.0389 115 ARG   A CA  
850  C  C   . ARG   A 109 ? 0.2630 0.2046 0.1771 -0.0485 0.0580  -0.0376 115 ARG   A C   
851  O  O   . ARG   A 109 ? 0.2357 0.1918 0.1450 -0.0434 0.0456  -0.0309 115 ARG   A O   
852  C  CB  . ARG   A 109 ? 0.2496 0.1778 0.2390 -0.0295 0.0621  -0.0419 115 ARG   A CB  
853  C  CG  . ARG   A 109 ? 0.3323 0.2562 0.3712 -0.0191 0.0549  -0.0374 115 ARG   A CG  
854  C  CD  . ARG   A 109 ? 0.3764 0.2915 0.4654 -0.0179 0.0586  -0.0333 115 ARG   A CD  
855  N  NE  . ARG   A 109 ? 0.4377 0.3341 0.5436 -0.0266 0.0968  -0.0407 115 ARG   A NE  
856  C  CZ  . ARG   A 109 ? 0.4568 0.3386 0.6112 -0.0255 0.1192  -0.0390 115 ARG   A CZ  
857  N  NH1 . ARG   A 109 ? 0.4702 0.3229 0.6262 -0.0350 0.1633  -0.0477 115 ARG   A NH1 
858  N  NH2 . ARG   A 109 ? 0.4435 0.3336 0.6438 -0.0163 0.1000  -0.0275 115 ARG   A NH2 
859  N  N   . CYS   A 110 ? 0.2971 0.2167 0.1830 -0.0690 0.0751  -0.0431 116 CYS   A N   
860  C  CA  . CYS   A 110 ? 0.3446 0.2530 0.1888 -0.0904 0.0763  -0.0412 116 CYS   A CA  
861  C  C   . CYS   A 110 ? 0.4007 0.2698 0.2399 -0.1010 0.1079  -0.0556 116 CYS   A C   
862  O  O   . CYS   A 110 ? 0.3920 0.2534 0.2749 -0.0878 0.1250  -0.0620 116 CYS   A O   
863  C  CB  . CYS   A 110 ? 0.3657 0.2671 0.1666 -0.1128 0.0676  -0.0326 116 CYS   A CB  
864  S  SG  . CYS   A 110 ? 0.4175 0.2742 0.1898 -0.1293 0.0944  -0.0452 116 CYS   A SG  
865  N  N   . GLN   A 111 ? 0.4589 0.2986 0.2482 -0.1261 0.1174  -0.0586 117 GLN   A N   
866  C  CA  . GLN   A 111 ? 0.5130 0.3042 0.2917 -0.1374 0.1565  -0.0732 117 GLN   A CA  
867  C  C   . GLN   A 111 ? 0.5457 0.2950 0.3177 -0.1443 0.1917  -0.0835 117 GLN   A C   
868  O  O   . GLN   A 111 ? 0.5674 0.2760 0.3529 -0.1463 0.2337  -0.0944 117 GLN   A O   
869  C  CB  . GLN   A 111 ? 0.5861 0.3413 0.2928 -0.1694 0.1593  -0.0744 117 GLN   A CB  
870  C  CG  . GLN   A 111 ? 0.6794 0.4045 0.3099 -0.2024 0.1486  -0.0689 117 GLN   A CG  
871  C  CD  . GLN   A 111 ? 0.8025 0.4913 0.3599 -0.2380 0.1403  -0.0648 117 GLN   A CD  
872  O  OE1 . GLN   A 111 ? 0.8282 0.5484 0.3782 -0.2467 0.0999  -0.0450 117 GLN   A OE1 
873  N  NE2 . GLN   A 111 ? 0.8396 0.4576 0.3446 -0.2600 0.1804  -0.0816 117 GLN   A NE2 
874  N  N   . HIS   A 112 ? 0.5412 0.2966 0.2944 -0.1484 0.1787  -0.0790 118 HIS   A N   
875  C  CA  . HIS   A 112 ? 0.5616 0.2731 0.3010 -0.1572 0.2132  -0.0885 118 HIS   A CA  
876  C  C   . HIS   A 112 ? 0.5004 0.2374 0.3226 -0.1276 0.2203  -0.0875 118 HIS   A C   
877  O  O   . HIS   A 112 ? 0.5188 0.2182 0.3484 -0.1308 0.2575  -0.0948 118 HIS   A O   
878  C  CB  . HIS   A 112 ? 0.6131 0.3049 0.2783 -0.1844 0.1982  -0.0838 118 HIS   A CB  
879  C  CG  . HIS   A 112 ? 0.7118 0.3741 0.2938 -0.2204 0.1825  -0.0786 118 HIS   A CG  
880  N  ND1 . HIS   A 112 ? 0.7327 0.4422 0.3155 -0.2224 0.1340  -0.0588 118 HIS   A ND1 
881  C  CD2 . HIS   A 112 ? 0.7981 0.3843 0.2968 -0.2563 0.2098  -0.0886 118 HIS   A CD2 
882  C  CE1 . HIS   A 112 ? 0.7855 0.4521 0.2912 -0.2605 0.1266  -0.0544 118 HIS   A CE1 
883  N  NE2 . HIS   A 112 ? 0.8353 0.4233 0.2799 -0.2837 0.1704  -0.0734 118 HIS   A NE2 
884  N  N   . GLY   A 113 ? 0.4300 0.2231 0.3090 -0.1019 0.1858  -0.0772 119 GLY   A N   
885  C  CA  . GLY   A 113 ? 0.3789 0.1936 0.3301 -0.0784 0.1822  -0.0723 119 GLY   A CA  
886  C  C   . GLY   A 113 ? 0.3321 0.1916 0.2912 -0.0638 0.1397  -0.0622 119 GLY   A C   
887  O  O   . GLY   A 113 ? 0.3208 0.2025 0.2529 -0.0643 0.1145  -0.0569 119 GLY   A O   
888  N  N   . VAL   A 114 ? 0.3077 0.1762 0.3053 -0.0511 0.1350  -0.0584 120 VAL   A N   
889  C  CA  . VAL   A 114 ? 0.2871 0.1865 0.2900 -0.0379 0.1014  -0.0501 120 VAL   A CA  
890  C  C   . VAL   A 114 ? 0.2920 0.1977 0.2432 -0.0481 0.0935  -0.0488 120 VAL   A C   
891  O  O   . VAL   A 114 ? 0.3100 0.1947 0.2383 -0.0617 0.1112  -0.0533 120 VAL   A O   
892  C  CB  . VAL   A 114 ? 0.2781 0.1792 0.3389 -0.0244 0.0975  -0.0449 120 VAL   A CB  
893  C  CG1 . VAL   A 114 ? 0.2766 0.1973 0.3280 -0.0144 0.0675  -0.0385 120 VAL   A CG1 
894  C  CG2 . VAL   A 114 ? 0.2628 0.1620 0.3852 -0.0165 0.0938  -0.0376 120 VAL   A CG2 
895  N  N   . VAL   A 115 ? 0.2585 0.1893 0.1932 -0.0433 0.0688  -0.0404 121 VAL   A N   
896  C  CA  . VAL   A 115 ? 0.2596 0.2034 0.1640 -0.0513 0.0568  -0.0314 121 VAL   A CA  
897  C  C   . VAL   A 115 ? 0.2554 0.2154 0.1792 -0.0352 0.0444  -0.0256 121 VAL   A C   
898  O  O   . VAL   A 115 ? 0.2565 0.2192 0.1694 -0.0419 0.0428  -0.0210 121 VAL   A O   
899  C  CB  . VAL   A 115 ? 0.2631 0.2238 0.1519 -0.0550 0.0428  -0.0207 121 VAL   A CB  
900  C  CG1 . VAL   A 115 ? 0.2786 0.2588 0.1599 -0.0599 0.0277  -0.0034 121 VAL   A CG1 
901  C  CG2 . VAL   A 115 ? 0.2768 0.2179 0.1365 -0.0757 0.0524  -0.0250 121 VAL   A CG2 
902  N  N   . GLY   A 116 ? 0.2446 0.2098 0.1902 -0.0171 0.0345  -0.0250 122 GLY   A N   
903  C  CA  . GLY   A 116 ? 0.2477 0.2170 0.2013 -0.0039 0.0243  -0.0207 122 GLY   A CA  
904  C  C   . GLY   A 116 ? 0.2370 0.1948 0.1955 0.0087  0.0122  -0.0203 122 GLY   A C   
905  O  O   . GLY   A 116 ? 0.2228 0.1723 0.1891 0.0078  0.0094  -0.0229 122 GLY   A O   
906  N  N   . ILE   A 117 ? 0.2231 0.1737 0.1729 0.0180  0.0047  -0.0166 123 ILE   A N   
907  C  CA  . ILE   A 117 ? 0.2328 0.1561 0.1674 0.0238  -0.0082 -0.0158 123 ILE   A CA  
908  C  C   . ILE   A 117 ? 0.2441 0.1542 0.1451 0.0315  -0.0019 -0.0112 123 ILE   A C   
909  O  O   . ILE   A 117 ? 0.2242 0.1470 0.1280 0.0359  0.0085  -0.0062 123 ILE   A O   
910  C  CB  . ILE   A 117 ? 0.2598 0.1645 0.2097 0.0234  -0.0238 -0.0156 123 ILE   A CB  
911  C  CG1 . ILE   A 117 ? 0.2618 0.1756 0.2171 0.0267  -0.0184 -0.0153 123 ILE   A CG1 
912  C  CG2 . ILE   A 117 ? 0.2616 0.1688 0.2564 0.0174  -0.0291 -0.0152 123 ILE   A CG2 
913  C  CD1 . ILE   A 117 ? 0.2888 0.1801 0.2524 0.0265  -0.0363 -0.0127 123 ILE   A CD1 
914  N  N   . VAL   A 118 ? 0.2724 0.1496 0.1409 0.0324  -0.0059 -0.0113 124 VAL   A N   
915  C  CA  . VAL   A 118 ? 0.2963 0.1456 0.1269 0.0397  0.0102  -0.0075 124 VAL   A CA  
916  C  C   . VAL   A 118 ? 0.2997 0.1282 0.1167 0.0436  0.0128  -0.0072 124 VAL   A C   
917  O  O   . VAL   A 118 ? 0.2977 0.1074 0.1092 0.0376  -0.0075 -0.0106 124 VAL   A O   
918  C  CB  . VAL   A 118 ? 0.3539 0.1542 0.1358 0.0358  0.0065  -0.0096 124 VAL   A CB  
919  C  CG1 . VAL   A 118 ? 0.4053 0.1615 0.1408 0.0426  0.0333  -0.0072 124 VAL   A CG1 
920  C  CG2 . VAL   A 118 ? 0.3600 0.1827 0.1572 0.0334  0.0065  -0.0092 124 VAL   A CG2 
921  N  N   . SER   A 119 ? 0.3093 0.1450 0.1312 0.0531  0.0368  -0.0002 125 SER   A N   
922  C  CA  . SER   A 119 ? 0.3336 0.1499 0.1455 0.0576  0.0430  0.0005  125 SER   A CA  
923  C  C   . SER   A 119 ? 0.3910 0.1652 0.1717 0.0670  0.0765  0.0058  125 SER   A C   
924  O  O   . SER   A 119 ? 0.4050 0.1397 0.1560 0.0686  0.0841  0.0034  125 SER   A O   
925  C  CB  . SER   A 119 ? 0.3135 0.1821 0.1765 0.0593  0.0412  0.0063  125 SER   A CB  
926  O  OG  . SER   A 119 ? 0.3249 0.1798 0.1849 0.0657  0.0514  0.0095  125 SER   A OG  
927  N  N   . THR   A 120 ? 0.4147 0.1949 0.2058 0.0732  0.1002  0.0143  126 THR   A N   
928  C  CA  . THR   A 120 ? 0.4614 0.1955 0.2303 0.0836  0.1431  0.0215  126 THR   A CA  
929  C  C   . THR   A 120 ? 0.4787 0.2124 0.2501 0.0858  0.1593  0.0272  126 THR   A C   
930  O  O   . THR   A 120 ? 0.4580 0.2249 0.2424 0.0785  0.1343  0.0242  126 THR   A O   
931  C  CB  . THR   A 120 ? 0.4519 0.2139 0.2765 0.0957  0.1669  0.0381  126 THR   A CB  
932  O  OG1 . THR   A 120 ? 0.5051 0.2078 0.3065 0.1067  0.2160  0.0439  126 THR   A OG1 
933  C  CG2 . THR   A 120 ? 0.4021 0.2419 0.3092 0.0972  0.1598  0.0582  126 THR   A CG2 
934  N  N   . GLY   A 121 ? 0.5159 0.2096 0.2775 0.0960  0.2045  0.0359  127 GLY   A N   
935  C  CA  . GLY   A 121 ? 0.5473 0.2363 0.3164 0.1002  0.2272  0.0440  127 GLY   A CA  
936  C  C   . GLY   A 121 ? 0.6181 0.2345 0.3570 0.1109  0.2872  0.0497  127 GLY   A C   
937  O  O   . GLY   A 121 ? 0.6443 0.2307 0.3813 0.1182  0.3152  0.0531  127 GLY   A O   
938  N  N   . GLY   A 122 ? 0.6709 0.2522 0.3820 0.1113  0.3102  0.0497  128 GLY   A N   
939  C  CA  . GLY   A 122 ? 0.7411 0.2397 0.4147 0.1203  0.3763  0.0539  128 GLY   A CA  
940  C  C   . GLY   A 122 ? 0.7276 0.2635 0.4874 0.1356  0.4131  0.0802  128 GLY   A C   
941  O  O   . GLY   A 122 ? 0.6680 0.2976 0.5296 0.1402  0.3893  0.1011  128 GLY   A O   
942  N  N   . ASN   A 123 ? 0.7822 0.2405 0.4997 0.1409  0.4703  0.0810  129 ASN   A N   
943  C  CA  . ASN   A 123 ? 0.7567 0.2432 0.5622 0.1566  0.5119  0.1093  129 ASN   A CA  
944  C  C   . ASN   A 123 ? 0.6955 0.2693 0.5599 0.1516  0.4646  0.1187  129 ASN   A C   
945  O  O   . ASN   A 123 ? 0.6591 0.2972 0.6355 0.1620  0.4743  0.1511  129 ASN   A O   
946  C  CB  . ASN   A 123 ? 0.7517 0.2759 0.6743 0.1758  0.5504  0.1429  129 ASN   A CB  
947  C  CG  . ASN   A 123 ? 0.8941 0.3226 0.7642 0.1833  0.6127  0.1361  129 ASN   A CG  
948  O  OD1 . ASN   A 123 ? 0.9904 0.3093 0.7697 0.1828  0.6693  0.1226  129 ASN   A OD1 
949  N  ND2 . ASN   A 123 ? 0.8891 0.3504 0.8100 0.1888  0.6062  0.1458  129 ASN   A ND2 
950  N  N   . GLY   A 124 ? 0.6804 0.2500 0.4714 0.1346  0.4162  0.0935  130 GLY   A N   
951  C  CA  . GLY   A 124 ? 0.6197 0.2616 0.4549 0.1285  0.3745  0.0990  130 GLY   A CA  
952  C  C   . GLY   A 124 ? 0.5393 0.2746 0.4410 0.1220  0.3194  0.1057  130 GLY   A C   
953  O  O   . GLY   A 124 ? 0.5192 0.3134 0.4605 0.1150  0.2870  0.1126  130 GLY   A O   
954  N  N   . LEU   A 125 ? 0.5019 0.2444 0.4071 0.1219  0.3087  0.1025  131 LEU   A N   
955  C  CA  . LEU   A 125 ? 0.4348 0.2510 0.3867 0.1132  0.2603  0.1061  131 LEU   A CA  
956  C  C   . LEU   A 125 ? 0.4384 0.2343 0.3188 0.1013  0.2241  0.0761  131 LEU   A C   
957  O  O   . LEU   A 125 ? 0.4975 0.2229 0.2994 0.0994  0.2347  0.0576  131 LEU   A O   
958  C  CB  . LEU   A 125 ? 0.4098 0.2556 0.4360 0.1221  0.2755  0.1311  131 LEU   A CB  
959  C  CG  . LEU   A 125 ? 0.4074 0.2815 0.5314 0.1334  0.3082  0.1707  131 LEU   A CG  
960  C  CD1 . LEU   A 125 ? 0.3895 0.2798 0.5846 0.1428  0.3279  0.1964  131 LEU   A CD1 
961  C  CD2 . LEU   A 125 ? 0.3785 0.3203 0.5580 0.1211  0.2706  0.1892  131 LEU   A CD2 
962  N  N   . VAL   A 126 ? 0.3727 0.2259 0.2813 0.0910  0.1819  0.0740  132 VAL   A N   
963  C  CA  . VAL   A 126 ? 0.3635 0.2101 0.2320 0.0811  0.1492  0.0523  132 VAL   A CA  
964  C  C   . VAL   A 126 ? 0.3078 0.2125 0.2288 0.0761  0.1274  0.0611  132 VAL   A C   
965  O  O   . VAL   A 126 ? 0.2827 0.2358 0.2518 0.0701  0.1170  0.0772  132 VAL   A O   
966  C  CB  . VAL   A 126 ? 0.3750 0.2118 0.2038 0.0697  0.1222  0.0347  132 VAL   A CB  
967  C  CG1 . VAL   A 126 ? 0.3533 0.2396 0.2222 0.0643  0.1107  0.0430  132 VAL   A CG1 
968  C  CG2 . VAL   A 126 ? 0.3875 0.2218 0.1963 0.0601  0.0901  0.0188  132 VAL   A CG2 
969  N  N   . GLY   A 127 ? 0.2911 0.1842 0.1972 0.0761  0.1203  0.0523  133 GLY   A N   
970  C  CA  . GLY   A 127 ? 0.2608 0.1965 0.2035 0.0703  0.1018  0.0580  133 GLY   A CA  
971  C  C   . GLY   A 127 ? 0.2667 0.2036 0.1851 0.0596  0.0730  0.0380  133 GLY   A C   
972  O  O   . GLY   A 127 ? 0.3012 0.1985 0.1782 0.0600  0.0678  0.0225  133 GLY   A O   
973  N  N   . PHE   A 128 ? 0.2302 0.2067 0.1743 0.0476  0.0551  0.0407  134 PHE   A N   
974  C  CA  . PHE   A 128 ? 0.2291 0.2064 0.1617 0.0378  0.0367  0.0244  134 PHE   A CA  
975  C  C   . PHE   A 128 ? 0.2184 0.2147 0.1681 0.0318  0.0308  0.0280  134 PHE   A C   
976  O  O   . PHE   A 128 ? 0.2136 0.2360 0.1860 0.0245  0.0295  0.0450  134 PHE   A O   
977  C  CB  . PHE   A 128 ? 0.2133 0.2053 0.1471 0.0251  0.0285  0.0209  134 PHE   A CB  
978  C  CG  . PHE   A 128 ? 0.2291 0.2089 0.1504 0.0291  0.0331  0.0198  134 PHE   A CG  
979  C  CD1 . PHE   A 128 ? 0.2468 0.1973 0.1449 0.0314  0.0275  0.0063  134 PHE   A CD1 
980  C  CD2 . PHE   A 128 ? 0.2199 0.2178 0.1566 0.0276  0.0394  0.0352  134 PHE   A CD2 
981  C  CE1 . PHE   A 128 ? 0.2520 0.1882 0.1341 0.0331  0.0306  0.0059  134 PHE   A CE1 
982  C  CE2 . PHE   A 128 ? 0.2334 0.2194 0.1586 0.0312  0.0451  0.0338  134 PHE   A CE2 
983  C  CZ  . PHE   A 128 ? 0.2433 0.1972 0.1374 0.0341  0.0416  0.0179  134 PHE   A CZ  
984  N  N   . ALA   A 129 ? 0.2015 0.1828 0.1423 0.0330  0.0247  0.0151  135 ALA   A N   
985  C  CA  . ALA   A 129 ? 0.1956 0.1901 0.1487 0.0267  0.0205  0.0159  135 ALA   A CA  
986  C  C   . ALA   A 129 ? 0.2021 0.2043 0.1536 0.0099  0.0167  0.0095  135 ALA   A C   
987  O  O   . ALA   A 129 ? 0.1961 0.1843 0.1452 0.0089  0.0166  -0.0030 135 ALA   A O   
988  C  CB  . ALA   A 129 ? 0.2077 0.1804 0.1554 0.0341  0.0165  0.0059  135 ALA   A CB  
989  N  N   . ASP   A 130 ? 0.2071 0.2249 0.1581 -0.0058 0.0144  0.0201  136 ASP   A N   
990  C  CA  . ASP   A 130 ? 0.2395 0.2483 0.1711 -0.0268 0.0159  0.0129  136 ASP   A CA  
991  C  C   . ASP   A 130 ? 0.2451 0.2359 0.1749 -0.0292 0.0248  -0.0015 136 ASP   A C   
992  O  O   . ASP   A 130 ? 0.2387 0.2325 0.1802 -0.0214 0.0231  -0.0003 136 ASP   A O   
993  C  CB  . ASP   A 130 ? 0.2812 0.2999 0.2006 -0.0495 0.0057  0.0312  136 ASP   A CB  
994  C  CG  . ASP   A 130 ? 0.3736 0.3681 0.2530 -0.0774 0.0085  0.0248  136 ASP   A CG  
995  O  OD1 . ASP   A 130 ? 0.3726 0.3573 0.2411 -0.0802 0.0144  0.0167  136 ASP   A OD1 
996  O  OD2 . ASP   A 130 ? 0.4433 0.4219 0.2959 -0.0985 0.0065  0.0275  136 ASP   A OD2 
997  N  N   . VAL   A 131 ? 0.2508 0.2203 0.1708 -0.0392 0.0382  -0.0143 137 VAL   A N   
998  C  CA  . VAL   A 131 ? 0.2695 0.2172 0.1954 -0.0428 0.0551  -0.0253 137 VAL   A CA  
999  C  C   . VAL   A 131 ? 0.3152 0.2301 0.1998 -0.0699 0.0752  -0.0316 137 VAL   A C   
1000 O  O   . VAL   A 131 ? 0.3478 0.2345 0.2348 -0.0745 0.0998  -0.0417 137 VAL   A O   
1001 C  CB  . VAL   A 131 ? 0.2511 0.1917 0.2192 -0.0266 0.0615  -0.0331 137 VAL   A CB  
1002 C  CG1 . VAL   A 131 ? 0.2514 0.2066 0.2417 -0.0071 0.0403  -0.0275 137 VAL   A CG1 
1003 C  CG2 . VAL   A 131 ? 0.2433 0.1738 0.2151 -0.0298 0.0706  -0.0381 137 VAL   A CG2 
1004 N  N   . ARG   A 132 ? 0.3213 0.2324 0.1675 -0.0890 0.0676  -0.0253 138 ARG   A N   
1005 C  CA  . ARG   A 132 ? 0.3697 0.2358 0.1594 -0.1201 0.0854  -0.0317 138 ARG   A CA  
1006 C  C   . ARG   A 132 ? 0.4285 0.2638 0.1723 -0.1446 0.0904  -0.0299 138 ARG   A C   
1007 O  O   . ARG   A 132 ? 0.4758 0.2550 0.1648 -0.1704 0.1164  -0.0404 138 ARG   A O   
1008 C  CB  . ARG   A 132 ? 0.3783 0.2456 0.1354 -0.1381 0.0691  -0.0219 138 ARG   A CB  
1009 C  CG  . ARG   A 132 ? 0.3608 0.2495 0.1540 -0.1174 0.0687  -0.0256 138 ARG   A CG  
1010 C  CD  . ARG   A 132 ? 0.3662 0.2589 0.1305 -0.1358 0.0507  -0.0129 138 ARG   A CD  
1011 N  NE  . ARG   A 132 ? 0.3673 0.3021 0.1576 -0.1283 0.0215  0.0100  138 ARG   A NE  
1012 C  CZ  . ARG   A 132 ? 0.3650 0.3174 0.1558 -0.1381 0.0007  0.0298  138 ARG   A CZ  
1013 N  NH1 . ARG   A 132 ? 0.3770 0.3074 0.1326 -0.1591 0.0007  0.0284  138 ARG   A NH1 
1014 N  NH2 . ARG   A 132 ? 0.3119 0.3015 0.1420 -0.1279 -0.0183 0.0532  138 ARG   A NH2 
1015 N  N   . ASP   A 133 ? 0.4251 0.2893 0.1861 -0.1381 0.0689  -0.0170 139 ASP   A N   
1016 C  CA  . ASP   A 133 ? 0.4639 0.3000 0.1826 -0.1619 0.0701  -0.0134 139 ASP   A CA  
1017 C  C   . ASP   A 133 ? 0.4827 0.3005 0.2217 -0.1485 0.1002  -0.0292 139 ASP   A C   
1018 O  O   . ASP   A 133 ? 0.5213 0.3027 0.2173 -0.1697 0.1113  -0.0308 139 ASP   A O   
1019 C  CB  . ASP   A 133 ? 0.4561 0.3315 0.1906 -0.1630 0.0335  0.0115  139 ASP   A CB  
1020 C  CG  . ASP   A 133 ? 0.4398 0.3628 0.2447 -0.1245 0.0277  0.0134  139 ASP   A CG  
1021 O  OD1 . ASP   A 133 ? 0.4014 0.3403 0.2430 -0.0987 0.0349  0.0040  139 ASP   A OD1 
1022 O  OD2 . ASP   A 133 ? 0.4382 0.3771 0.2567 -0.1226 0.0154  0.0251  139 ASP   A OD2 
1023 N  N   . LEU   A 134 ? 0.4548 0.2954 0.2598 -0.1157 0.1107  -0.0378 140 LEU   A N   
1024 C  CA  . LEU   A 134 ? 0.4556 0.2829 0.2962 -0.1025 0.1360  -0.0472 140 LEU   A CA  
1025 C  C   . LEU   A 134 ? 0.4979 0.2689 0.3207 -0.1156 0.1823  -0.0616 140 LEU   A C   
1026 O  O   . LEU   A 134 ? 0.4705 0.2420 0.3485 -0.0982 0.2012  -0.0667 140 LEU   A O   
1027 C  CB  . LEU   A 134 ? 0.4092 0.2761 0.3260 -0.0686 0.1228  -0.0450 140 LEU   A CB  
1028 C  CG  . LEU   A 134 ? 0.3999 0.3103 0.3285 -0.0547 0.0861  -0.0326 140 LEU   A CG  
1029 C  CD1 . LEU   A 134 ? 0.3765 0.3069 0.3582 -0.0286 0.0739  -0.0318 140 LEU   A CD1 
1030 C  CD2 . LEU   A 134 ? 0.4045 0.3197 0.3168 -0.0618 0.0776  -0.0253 140 LEU   A CD2 
1031 N  N   . LEU   A 135 ? 0.5613 0.2769 0.3045 -0.1492 0.2019  -0.0663 141 LEU   A N   
1032 C  CA  . LEU   A 135 ? 0.6187 0.2618 0.3249 -0.1673 0.2558  -0.0815 141 LEU   A CA  
1033 C  C   . LEU   A 135 ? 0.6108 0.2389 0.3846 -0.1471 0.2990  -0.0884 141 LEU   A C   
1034 O  O   . LEU   A 135 ? 0.6326 0.2196 0.4239 -0.1467 0.3462  -0.0973 141 LEU   A O   
1035 C  CB  . LEU   A 135 ? 0.6902 0.2623 0.2790 -0.2132 0.2667  -0.0844 141 LEU   A CB  
1036 C  CG  . LEU   A 135 ? 0.7311 0.3124 0.2530 -0.2415 0.2178  -0.0697 141 LEU   A CG  
1037 C  CD1 . LEU   A 135 ? 0.8147 0.3037 0.2091 -0.2949 0.2326  -0.0726 141 LEU   A CD1 
1038 C  CD2 . LEU   A 135 ? 0.7220 0.3317 0.2619 -0.2344 0.2008  -0.0669 141 LEU   A CD2 
1039 N  N   . TRP   A 136 ? 0.5802 0.2424 0.4005 -0.1296 0.2836  -0.0816 142 TRP   A N   
1040 C  CA  . TRP   A 136 ? 0.5674 0.2222 0.4641 -0.1102 0.3176  -0.0825 142 TRP   A CA  
1041 C  C   . TRP   A 136 ? 0.5423 0.2304 0.5448 -0.0811 0.3178  -0.0760 142 TRP   A C   
1042 O  O   . TRP   A 136 ? 0.5237 0.1965 0.5997 -0.0688 0.3532  -0.0728 142 TRP   A O   
1043 C  CB  . TRP   A 136 ? 0.5389 0.2227 0.4547 -0.1010 0.2949  -0.0753 142 TRP   A CB  
1044 C  CG  . TRP   A 136 ? 0.4936 0.2473 0.4370 -0.0829 0.2353  -0.0638 142 TRP   A CG  
1045 C  CD1 . TRP   A 136 ? 0.5077 0.2843 0.3988 -0.0937 0.1972  -0.0576 142 TRP   A CD1 
1046 C  CD2 . TRP   A 136 ? 0.4445 0.2453 0.4736 -0.0533 0.2103  -0.0548 142 TRP   A CD2 
1047 N  NE1 . TRP   A 136 ? 0.4772 0.3096 0.4157 -0.0698 0.1583  -0.0481 142 TRP   A NE1 
1048 C  CE2 . TRP   A 136 ? 0.4449 0.2887 0.4584 -0.0470 0.1638  -0.0476 142 TRP   A CE2 
1049 C  CE3 . TRP   A 136 ? 0.4166 0.2228 0.5352 -0.0342 0.2217  -0.0492 142 TRP   A CE3 
1050 C  CZ2 . TRP   A 136 ? 0.4193 0.3001 0.4851 -0.0243 0.1324  -0.0394 142 TRP   A CZ2 
1051 C  CZ3 . TRP   A 136 ? 0.3920 0.2398 0.5652 -0.0143 0.1808  -0.0376 142 TRP   A CZ3 
1052 C  CH2 . TRP   A 136 ? 0.3946 0.2742 0.5328 -0.0104 0.1386  -0.0350 142 TRP   A CH2 
1053 N  N   . LEU   A 137 ? 0.5342 0.2649 0.5484 -0.0717 0.2785  -0.0709 143 LEU   A N   
1054 C  CA  . LEU   A 137 ? 0.5156 0.2718 0.6195 -0.0500 0.2728  -0.0625 143 LEU   A CA  
1055 C  C   . LEU   A 137 ? 0.5843 0.2934 0.7180 -0.0544 0.3294  -0.0670 143 LEU   A C   
1056 O  O   . LEU   A 137 ? 0.5520 0.2736 0.7852 -0.0369 0.3366  -0.0547 143 LEU   A O   
1057 C  CB  . LEU   A 137 ? 0.4827 0.2783 0.5704 -0.0451 0.2273  -0.0590 143 LEU   A CB  
1058 C  CG  . LEU   A 137 ? 0.4515 0.2942 0.5415 -0.0324 0.1759  -0.0504 143 LEU   A CG  
1059 C  CD1 . LEU   A 137 ? 0.4422 0.3110 0.5080 -0.0298 0.1435  -0.0481 143 LEU   A CD1 
1060 C  CD2 . LEU   A 137 ? 0.4109 0.2720 0.5833 -0.0131 0.1611  -0.0385 143 LEU   A CD2 
1061 N  N   . ASP   A 138 ? 0.6778 0.3276 0.7244 -0.0803 0.3693  -0.0822 144 ASP   A N   
1062 C  CA  . ASP   A 138 ? 0.7504 0.3392 0.7995 -0.0896 0.4319  -0.0902 144 ASP   A CA  
1063 C  C   . ASP   A 138 ? 0.8177 0.3403 0.8760 -0.0962 0.5017  -0.0956 144 ASP   A C   
1064 O  O   . ASP   A 138 ? 0.8431 0.3121 0.9211 -0.0999 0.5623  -0.1001 144 ASP   A O   
1065 C  CB  . ASP   A 138 ? 0.8309 0.3800 0.7632 -0.1192 0.4351  -0.1040 144 ASP   A CB  
1066 C  CG  . ASP   A 138 ? 0.8560 0.4476 0.8102 -0.1098 0.4005  -0.0993 144 ASP   A CG  
1067 O  OD1 . ASP   A 138 ? 0.8267 0.4321 0.8729 -0.0903 0.4145  -0.0920 144 ASP   A OD1 
1068 O  OD2 . ASP   A 138 ? 0.9031 0.5144 0.7884 -0.1225 0.3589  -0.1000 144 ASP   A OD2 
1069 N  N   . GLU   A 139 ? 0.8502 0.3695 0.8905 -0.0990 0.4994  -0.0955 145 GLU   A N   
1070 C  CA  . GLU   A 139 ? 0.9050 0.3545 0.9461 -0.1067 0.5700  -0.1011 145 GLU   A CA  
1071 C  C   . GLU   A 139 ? 0.8779 0.3680 1.0155 -0.0832 0.5590  -0.0861 145 GLU   A C   
1072 O  O   . GLU   A 139 ? 0.8997 0.3396 1.0550 -0.0854 0.6162  -0.0875 145 GLU   A O   
1073 C  CB  . GLU   A 139 ? 1.0221 0.3958 0.9057 -0.1467 0.5901  -0.1195 145 GLU   A CB  
1074 C  CG  . GLU   A 139 ? 1.0942 0.5135 0.9180 -0.1552 0.5217  -0.1158 145 GLU   A CG  
1075 C  CD  . GLU   A 139 ? 1.2450 0.6283 0.9258 -0.1946 0.4976  -0.1237 145 GLU   A CD  
1076 O  OE1 . GLU   A 139 ? 1.2641 0.6726 0.8965 -0.2062 0.4500  -0.1174 145 GLU   A OE1 
1077 O  OE2 . GLU   A 139 ? 1.3141 0.6437 0.9355 -0.2151 0.5243  -0.1333 145 GLU   A OE2 
1078 N  N1  . A1B14 B .   ? 0.7783 0.2466 0.3224 0.0754  0.2003  -0.0039 201 A1B14 A N1  
1079 C  C4  . A1B14 B .   ? 0.8241 0.2254 0.2852 0.0549  0.1682  -0.0165 201 A1B14 A C4  
1080 C  C5  . A1B14 B .   ? 0.8008 0.2479 0.3330 0.0796  0.2311  -0.0006 201 A1B14 A C5  
1081 C  C6  . A1B14 B .   ? 0.8785 0.2095 0.2885 0.0627  0.2450  -0.0131 201 A1B14 A C6  
1082 C  C7  . A1B14 B .   ? 0.9276 0.1783 0.3123 0.0806  0.3521  -0.0035 201 A1B14 A C7  
1083 C  C8  . A1B14 B .   ? 0.8887 0.1768 0.3358 0.0958  0.3851  0.0106  201 A1B14 A C8  
1084 C  C10 . A1B14 B .   ? 0.8149 0.2344 0.2948 0.0703  0.2525  0.0005  201 A1B14 A C10 
1085 C  C13 . A1B14 B .   ? 0.8008 0.2498 0.2890 0.0588  0.1872  -0.0089 201 A1B14 A C13 
1086 C  C15 . A1B14 B .   ? 0.7052 0.2653 0.3498 0.0889  0.1946  0.0082  201 A1B14 A C15 
1087 CL CL  . A1B14 B .   ? 0.7258 0.2998 0.3011 0.0479  0.1030  -0.0097 201 A1B14 A CL  
1088 C  C12 . A1B14 B .   ? 0.7671 0.2666 0.2902 0.0571  0.1647  -0.0070 201 A1B14 A C12 
1089 C  C11 . A1B14 B .   ? 0.7754 0.2628 0.2939 0.0624  0.1944  -0.0027 201 A1B14 A C11 
1090 C  C14 . A1B14 B .   ? 0.8435 0.2231 0.2906 0.0665  0.2466  -0.0066 201 A1B14 A C14 
1091 C  C9  . A1B14 B .   ? 0.8472 0.2112 0.2923 0.0727  0.2814  -0.0014 201 A1B14 A C9  
1092 O  O2  . A1B14 B .   ? 0.8870 0.1813 0.3027 0.0824  0.3491  0.0031  201 A1B14 A O2  
1093 N  N2  . A1B14 B .   ? 0.8851 0.2054 0.2949 0.0688  0.2775  -0.0086 201 A1B14 A N2  
1094 O  O1  . A1B14 B .   ? 0.7648 0.2784 0.3763 0.0932  0.2446  0.0132  201 A1B14 A O1  
1095 C  C3  . A1B14 B .   ? 0.7790 0.2458 0.2873 0.0470  0.1094  -0.0172 201 A1B14 A C3  
1096 C  C2  . A1B14 B .   ? 0.7065 0.2674 0.3150 0.0635  0.1104  -0.0087 201 A1B14 A C2  
1097 C  C1  . A1B14 B .   ? 0.6602 0.2797 0.3356 0.0792  0.1390  0.0032  201 A1B14 A C1  
1098 C  C   . A1B14 B .   ? 0.5905 0.2928 0.3529 0.0881  0.1328  0.0146  201 A1B14 A C   
1099 O  O   . A1B14 B .   ? 0.5810 0.2844 0.3645 0.0966  0.1522  0.0219  201 A1B14 A O   
1100 N  N   . A1B14 B .   ? 0.5439 0.3094 0.3519 0.0839  0.1069  0.0166  201 A1B14 A N   
# 
