data_7I49
# 
_entry.id   7I49 
# 
_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   7I49         pdb_00007i49 10.2210/pdb7i49/pdb 
WWPDB D_1001408296 ?            ?                   
# 
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                        7I49 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2025-03-12 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frank.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lithgo, R.M.'        1  ? 
'Fairhead, M.'        2  ? 
'Koekemoer, L.'       3  ? 
'Balcomb, B.H.'       4  ? 
'Capkin, E.'          5  ? 
'Chandran, A.V.'      6  ? 
'Golding, M.'         7  ? 
'Godoy, A.S.'         8  ? 
'Aschenbrenner, J.C.' 9  ? 
'Marples, P.G.'       10 ? 
'Ni, X.'              11 ? 
'Thompson, W.'        12 ? 
'Tomlinson, C.W.E.'   13 ? 
'Wild, C.'            14 ? 
'Winokan, M.'         15 ? 
'Xavier, M.-A.E.'     16 ? 
'Kenton, N.'          17 ? 
'Tucker, J.'          18 ? 
'DiPoto, M.'          19 ? 
'Lee, A.'             20 ? 
'Fearon, D.'          21 ? 
'von Delft, F.'       22 ? 
# 
_citation.id                        primary 
_citation.title                     
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Lithgo, R.M.'        ? 1  
primary 'Fairhead, M.'        ? 2  
primary 'Koekemoer, L.'       ? 3  
primary 'Balcomb, B.H.'       ? 4  
primary 'Capkin, E.'          ? 5  
primary 'Chandran, A.V.'      ? 6  
primary 'Golding, M.'         ? 7  
primary 'Godoy, A.S.'         ? 8  
primary 'Aschenbrenner, J.C.' ? 9  
primary 'Marples, P.G.'       ? 10 
primary 'Ni, X.'              ? 11 
primary 'Thompson, W.'        ? 12 
primary 'Tomlinson, C.W.E.'   ? 13 
primary 'Wild, C.'            ? 14 
primary 'Winokan, M.'         ? 15 
primary 'Xavier, M.-A.E.'     ? 16 
primary 'Kenton, N.'          ? 17 
primary 'Tucker, J.'          ? 18 
primary 'DiPoto, M.'          ? 19 
primary 'Lee, A.'             ? 20 
primary 'Fearon, D.'          ? 21 
primary 'von Delft, F.'       ? 22 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Protease 2A'                                                        15892.732 1  3.4.22.29 ? ? ? 
2 non-polymer syn '(3S)-1-{[2-(methanesulfonyl)phenyl]acetyl}piperidine-3-carboxamide' 324.395   1  ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                           65.409    1  ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                 78.133    1  ?         ? ? ? 
5 water       nat water                                                                18.015    70 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'P2A,Picornain 2A,Protein 2A' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '(3S)-1-{[2-(methanesulfonyl)phenyl]acetyl}piperidine-3-carboxamide' A1B2N 
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 
A1B2N non-polymer         . '(3S)-1-{[2-(methanesulfonyl)phenyl]acetyl}piperidine-3-carboxamide' ? 'C15 H20 N2 O4 S' 324.395 
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        A1B2N 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1B2N 
_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 A1B2N 1  201 201 A1B2N LIG A . 
C 3 ZN    1  202 1   ZN    ZN  A . 
D 4 DMS   1  203 6   DMS   DMS A . 
E 5 HOH   1  301 37  HOH   HOH A . 
E 5 HOH   2  302 18  HOH   HOH A . 
E 5 HOH   3  303 36  HOH   HOH A . 
E 5 HOH   4  304 59  HOH   HOH A . 
E 5 HOH   5  305 22  HOH   HOH A . 
E 5 HOH   6  306 29  HOH   HOH A . 
E 5 HOH   7  307 9   HOH   HOH A . 
E 5 HOH   8  308 12  HOH   HOH A . 
E 5 HOH   9  309 27  HOH   HOH A . 
E 5 HOH   10 310 48  HOH   HOH A . 
E 5 HOH   11 311 16  HOH   HOH A . 
E 5 HOH   12 312 14  HOH   HOH A . 
E 5 HOH   13 313 33  HOH   HOH A . 
E 5 HOH   14 314 42  HOH   HOH A . 
E 5 HOH   15 315 8   HOH   HOH A . 
E 5 HOH   16 316 24  HOH   HOH A . 
E 5 HOH   17 317 60  HOH   HOH A . 
E 5 HOH   18 318 2   HOH   HOH A . 
E 5 HOH   19 319 10  HOH   HOH A . 
E 5 HOH   20 320 40  HOH   HOH A . 
E 5 HOH   21 321 32  HOH   HOH A . 
E 5 HOH   22 322 47  HOH   HOH A . 
E 5 HOH   23 323 25  HOH   HOH A . 
E 5 HOH   24 324 23  HOH   HOH A . 
E 5 HOH   25 325 55  HOH   HOH A . 
E 5 HOH   26 326 7   HOH   HOH A . 
E 5 HOH   27 327 57  HOH   HOH A . 
E 5 HOH   28 328 72  HOH   HOH A . 
E 5 HOH   29 329 19  HOH   HOH A . 
E 5 HOH   30 330 34  HOH   HOH A . 
E 5 HOH   31 331 4   HOH   HOH A . 
E 5 HOH   32 332 41  HOH   HOH A . 
E 5 HOH   33 333 50  HOH   HOH A . 
E 5 HOH   34 334 13  HOH   HOH A . 
E 5 HOH   35 335 30  HOH   HOH A . 
E 5 HOH   36 336 51  HOH   HOH A . 
E 5 HOH   37 337 11  HOH   HOH A . 
E 5 HOH   38 338 21  HOH   HOH A . 
E 5 HOH   39 339 35  HOH   HOH A . 
E 5 HOH   40 340 74  HOH   HOH A . 
E 5 HOH   41 341 54  HOH   HOH A . 
E 5 HOH   42 342 58  HOH   HOH A . 
E 5 HOH   43 343 46  HOH   HOH A . 
E 5 HOH   44 344 67  HOH   HOH A . 
E 5 HOH   45 345 6   HOH   HOH A . 
E 5 HOH   46 346 17  HOH   HOH A . 
E 5 HOH   47 347 20  HOH   HOH A . 
E 5 HOH   48 348 5   HOH   HOH A . 
E 5 HOH   49 349 73  HOH   HOH A . 
E 5 HOH   50 350 39  HOH   HOH A . 
E 5 HOH   51 351 49  HOH   HOH A . 
E 5 HOH   52 352 66  HOH   HOH A . 
E 5 HOH   53 353 3   HOH   HOH A . 
E 5 HOH   54 354 63  HOH   HOH A . 
E 5 HOH   55 355 56  HOH   HOH A . 
E 5 HOH   56 356 26  HOH   HOH A . 
E 5 HOH   57 357 64  HOH   HOH A . 
E 5 HOH   58 358 28  HOH   HOH A . 
E 5 HOH   59 359 61  HOH   HOH A . 
E 5 HOH   60 360 15  HOH   HOH A . 
E 5 HOH   61 361 70  HOH   HOH A . 
E 5 HOH   62 362 68  HOH   HOH A . 
E 5 HOH   63 363 43  HOH   HOH A . 
E 5 HOH   64 364 31  HOH   HOH A . 
E 5 HOH   65 365 71  HOH   HOH A . 
E 5 HOH   66 366 75  HOH   HOH A . 
E 5 HOH   67 367 52  HOH   HOH A . 
E 5 HOH   68 368 44  HOH   HOH A . 
E 5 HOH   69 369 69  HOH   HOH A . 
E 5 HOH   70 370 62  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           7I49 
_cell.length_a           72.932 
_cell.length_b           62.050 
_cell.length_c           32.832 
_cell.angle_alpha        90.00 
_cell.angle_beta         92.79 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I49 
_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          7I49 
_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   47.31 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2025-01-17 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92201 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.92201 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7I49 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             36.42 
_reflns.d_resolution_high            1.86 
_reflns.number_obs                   11517 
_reflns.percent_possible_obs         92.9 
_reflns.pdbx_Rmerge_I_obs            0.085 
_reflns.pdbx_netI_over_sigmaI        6.7 
_reflns.pdbx_redundancy              2.9 
_reflns.pdbx_Rrim_I_all              0.099 
_reflns.pdbx_Rpim_I_all              0.049 
_reflns.pdbx_CC_half                 0.994 
_reflns.pdbx_number_measured_all     33238 
_reflns.pdbx_chi_squared             0.85 
_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                  1.86 
_reflns_shell.d_res_low                   1.96 
_reflns_shell.number_measured_all         1817 
_reflns_shell.number_unique_obs           1384 
_reflns_shell.Rmerge_I_obs                0.829 
_reflns_shell.pdbx_chi_squared            0.62 
_reflns_shell.pdbx_redundancy             1.3 
_reflns_shell.percent_possible_obs        77.2 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.9 
_reflns_shell.pdbx_Rrim_I_all             1.117 
_reflns_shell.pdbx_Rpim_I_all             0.742 
_reflns_shell.pdbx_CC_half                0.417 
_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                                 7I49 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     11507 
_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                             32.79 
_refine.ls_d_res_high                            1.857 
_refine.ls_percent_reflns_obs                    92.7 
_refine.ls_R_factor_obs                          0.2312 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2295 
_refine.ls_R_factor_R_free                       0.2622 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.140 
_refine.ls_number_reflns_R_free                  591 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.928 
_refine.correlation_coeff_Fo_to_Fc_free          0.897 
_refine.B_iso_mean                               31.13 
_refine.aniso_B[1][1]                            -2.32410 
_refine.aniso_B[2][2]                            -3.01850 
_refine.aniso_B[3][3]                            5.34250 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -0.97230 
_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             0.181 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.159 
_refine.pdbx_overall_SU_R_Blow_DPI               0.183 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.159 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7I49 
_refine_analyze.Luzzati_coordinate_error_obs    0.30 
_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         27 
_refine_hist.number_atoms_solvent             70 
_refine_hist.number_atoms_total               1171 
_refine_hist.d_res_high                       1.857 
_refine_hist.d_res_low                        32.79 
# 
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                  0.009 ? 2.00  1130 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               0.92  ? 2.00  1539 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  377  'X-RAY DIFFRACTION' SINUSOIDAL   
t_incorr_chiral_ct        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_pseud_angle             ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_trig_c_planes           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_gen_planes              ?     ? 5.00  203  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1130 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           3.51  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           15.99 ? ?     ?    '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  813  'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   30 
_refine_ls_shell.d_res_high                       1.86 
_refine_ls_shell.d_res_low                        1.88 
_refine_ls_shell.number_reflns_R_work             373 
_refine_ls_shell.R_factor_R_work                  0.3320 
_refine_ls_shell.percent_reflns_obs               75.49 
_refine_ls_shell.R_factor_R_free                  0.2813 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            6.05 
_refine_ls_shell.number_reflns_R_free             24 
_refine_ls_shell.number_reflns_all                397 
_refine_ls_shell.R_factor_all                     0.3288 
# 
_struct.entry_id                  7I49 
_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-0036582-001 (A71EV2A-x4675)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I49 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    POLG_CX16G 
_struct_ref.pdbx_db_accession          Q65900 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_struct_ref.pdbx_align_begin           869 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              7I49 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 144 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q65900 
_struct_ref_seq.db_align_beg                  869 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1012 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       7 
_struct_ref_seq.pdbx_auth_seq_align_end       150 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2 AA2 THR A 18  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
HELX_P HELX_P3 AA3 SER A 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
HELX_P HELX_P4 AA4 LEU A 134 ? ASP A 138 ? LEU A 140 ASP A 144 5 ? 5 
# 
_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 ? ? ? ? ? ? ? 2.342 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.468 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.369 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 C ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.199 ? ? 
# 
_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_555 108.5 ? 
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_555 107.3 ? 
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_555 116.5 ? 
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_555 105.2 ? 
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_555 101.0 ? 
6 SG ? A CYS 110 ? A CYS 116 ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 117.6 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA1 2 LEU A 34  ? CYS A 44  ? LEU A 40  CYS A 50  
AA1 3 ILE A 4   ? ASN A 13  ? ILE A 10  ASN A 19  
AA2 1 LYS A 64  ? SER A 69  ? LYS A 70  SER A 75  
AA2 2 THR A 54  ? CYS A 59  ? THR A 60  CYS A 65  
AA2 3 ILE A 107 ? CYS A 110 ? ILE A 113 CYS A 116 
AA2 4 GLY A 113 ? GLY A 121 ? GLY A 119 GLY A 127 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N TRP A 27  ? N TRP A 33  O VAL A 36  ? O VAL A 42  
AA1 2 3 N LEU A 35  ? N LEU A 41  O VAL A 12  ? O VAL A 18  
AA2 1 2 O LYS A 64  ? O LYS A 70  N CYS A 59  ? N CYS A 65  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N LEU A 108 ? N LEU A 114 O VAL A 115 ? O VAL A 121 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O PHE A 128 ? O PHE A 134 N MET A 93  ? N MET A 99  
AA2 6 7 O ARG A 87  ? O ARG A 93  N VAL A 78  ? N VAL A 84  
# 
_pdbx_entry_details.entry_id                   7I49 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    327 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    362 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.16 
# 
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  ? ? -87.15  32.88  
2 1 SER A 125 ? ? -132.85 -32.89 
3 1 ASN A 129 ? ? 78.38   33.54  
# 
_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         15.2080 
_pdbx_refine_tls.origin_y         6.6615 
_pdbx_refine_tls.origin_z         14.3495 
_pdbx_refine_tls.T[1][1]          0.0036 
_pdbx_refine_tls.T[2][2]          -0.0820 
_pdbx_refine_tls.T[3][3]          -0.0103 
_pdbx_refine_tls.T[1][2]          0.0215 
_pdbx_refine_tls.T[1][3]          -0.0034 
_pdbx_refine_tls.T[2][3]          -0.0156 
_pdbx_refine_tls.L[1][1]          0.9254 
_pdbx_refine_tls.L[2][2]          9.9644 
_pdbx_refine_tls.L[3][3]          1.4035 
_pdbx_refine_tls.L[1][2]          2.8038 
_pdbx_refine_tls.L[1][3]          -0.8155 
_pdbx_refine_tls.L[2][3]          -3.2784 
_pdbx_refine_tls.S[1][1]          -0.0876 
_pdbx_refine_tls.S[1][2]          0.1325 
_pdbx_refine_tls.S[1][3]          -0.0438 
_pdbx_refine_tls.S[2][1]          0.5725 
_pdbx_refine_tls.S[2][2]          0.1441 
_pdbx_refine_tls.S[2][3]          -0.3282 
_pdbx_refine_tls.S[3][1]          -0.1644 
_pdbx_refine_tls.S[3][2]          -0.1797 
_pdbx_refine_tls.S[3][3]          -0.0566 
# 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   '{ A|* }' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A GLU 146 ? A GLU 140 
2 1 Y 1 A ALA 147 ? A ALA 141 
3 1 Y 1 A MET 148 ? A MET 142 
4 1 Y 1 A GLU 149 ? A GLU 143 
5 1 Y 1 A GLN 150 ? A GLN 144 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1B2N N1   N  N N 1   
A1B2N C4   C  Y N 2   
A1B2N C5   C  Y N 3   
A1B2N C6   C  Y N 4   
A1B2N C7   C  N N 5   
A1B2N C8   C  N N 6   
A1B2N C10  C  N N 7   
A1B2N C13  C  N N 8   
A1B2N O3   O  N N 9   
A1B2N C12  C  N S 10  
A1B2N C11  C  N N 11  
A1B2N C9   C  N N 12  
A1B2N C14  C  N N 13  
A1B2N N    N  N N 14  
A1B2N O2   O  N N 15  
A1B2N C1   C  Y N 16  
A1B2N S    S  N N 17  
A1B2N O    O  N N 18  
A1B2N O1   O  N N 19  
A1B2N C    C  N N 20  
A1B2N C3   C  Y N 21  
A1B2N C2   C  Y N 22  
A1B2N H17  H  N N 23  
A1B2N H16  H  N N 24  
A1B2N H6   H  N N 25  
A1B2N H7   H  N N 26  
A1B2N H9   H  N N 27  
A1B2N H8   H  N N 28  
A1B2N H12  H  N N 29  
A1B2N H13  H  N N 30  
A1B2N H    H  N N 31  
A1B2N H14  H  N N 32  
A1B2N H15  H  N N 33  
A1B2N H11  H  N N 34  
A1B2N H10  H  N N 35  
A1B2N H18  H  N N 36  
A1B2N H19  H  N N 37  
A1B2N H2   H  N N 38  
A1B2N H1   H  N N 39  
A1B2N H3   H  N N 40  
A1B2N H5   H  N N 41  
A1B2N H4   H  N N 42  
ALA   N    N  N N 43  
ALA   CA   C  N S 44  
ALA   C    C  N N 45  
ALA   O    O  N N 46  
ALA   CB   C  N N 47  
ALA   OXT  O  N N 48  
ALA   H    H  N N 49  
ALA   H2   H  N N 50  
ALA   HA   H  N N 51  
ALA   HB1  H  N N 52  
ALA   HB2  H  N N 53  
ALA   HB3  H  N N 54  
ALA   HXT  H  N N 55  
ARG   N    N  N N 56  
ARG   CA   C  N S 57  
ARG   C    C  N N 58  
ARG   O    O  N N 59  
ARG   CB   C  N N 60  
ARG   CG   C  N N 61  
ARG   CD   C  N N 62  
ARG   NE   N  N N 63  
ARG   CZ   C  N N 64  
ARG   NH1  N  N N 65  
ARG   NH2  N  N N 66  
ARG   OXT  O  N N 67  
ARG   H    H  N N 68  
ARG   H2   H  N N 69  
ARG   HA   H  N N 70  
ARG   HB2  H  N N 71  
ARG   HB3  H  N N 72  
ARG   HG2  H  N N 73  
ARG   HG3  H  N N 74  
ARG   HD2  H  N N 75  
ARG   HD3  H  N N 76  
ARG   HE   H  N N 77  
ARG   HH11 H  N N 78  
ARG   HH12 H  N N 79  
ARG   HH21 H  N N 80  
ARG   HH22 H  N N 81  
ARG   HXT  H  N N 82  
ASN   N    N  N N 83  
ASN   CA   C  N S 84  
ASN   C    C  N N 85  
ASN   O    O  N N 86  
ASN   CB   C  N N 87  
ASN   CG   C  N N 88  
ASN   OD1  O  N N 89  
ASN   ND2  N  N N 90  
ASN   OXT  O  N N 91  
ASN   H    H  N N 92  
ASN   H2   H  N N 93  
ASN   HA   H  N N 94  
ASN   HB2  H  N N 95  
ASN   HB3  H  N N 96  
ASN   HD21 H  N N 97  
ASN   HD22 H  N N 98  
ASN   HXT  H  N N 99  
ASP   N    N  N N 100 
ASP   CA   C  N S 101 
ASP   C    C  N N 102 
ASP   O    O  N N 103 
ASP   CB   C  N N 104 
ASP   CG   C  N N 105 
ASP   OD1  O  N N 106 
ASP   OD2  O  N N 107 
ASP   OXT  O  N N 108 
ASP   H    H  N N 109 
ASP   H2   H  N N 110 
ASP   HA   H  N N 111 
ASP   HB2  H  N N 112 
ASP   HB3  H  N N 113 
ASP   HD2  H  N N 114 
ASP   HXT  H  N N 115 
CYS   N    N  N N 116 
CYS   CA   C  N R 117 
CYS   C    C  N N 118 
CYS   O    O  N N 119 
CYS   CB   C  N N 120 
CYS   SG   S  N N 121 
CYS   OXT  O  N N 122 
CYS   H    H  N N 123 
CYS   H2   H  N N 124 
CYS   HA   H  N N 125 
CYS   HB2  H  N N 126 
CYS   HB3  H  N N 127 
CYS   HG   H  N N 128 
CYS   HXT  H  N N 129 
DMS   S    S  N N 130 
DMS   O    O  N N 131 
DMS   C1   C  N N 132 
DMS   C2   C  N N 133 
DMS   H11  H  N N 134 
DMS   H12  H  N N 135 
DMS   H13  H  N N 136 
DMS   H21  H  N N 137 
DMS   H22  H  N N 138 
DMS   H23  H  N N 139 
GLN   N    N  N N 140 
GLN   CA   C  N S 141 
GLN   C    C  N N 142 
GLN   O    O  N N 143 
GLN   CB   C  N N 144 
GLN   CG   C  N N 145 
GLN   CD   C  N N 146 
GLN   OE1  O  N N 147 
GLN   NE2  N  N N 148 
GLN   OXT  O  N N 149 
GLN   H    H  N N 150 
GLN   H2   H  N N 151 
GLN   HA   H  N N 152 
GLN   HB2  H  N N 153 
GLN   HB3  H  N N 154 
GLN   HG2  H  N N 155 
GLN   HG3  H  N N 156 
GLN   HE21 H  N N 157 
GLN   HE22 H  N N 158 
GLN   HXT  H  N N 159 
GLU   N    N  N N 160 
GLU   CA   C  N S 161 
GLU   C    C  N N 162 
GLU   O    O  N N 163 
GLU   CB   C  N N 164 
GLU   CG   C  N N 165 
GLU   CD   C  N N 166 
GLU   OE1  O  N N 167 
GLU   OE2  O  N N 168 
GLU   OXT  O  N N 169 
GLU   H    H  N N 170 
GLU   H2   H  N N 171 
GLU   HA   H  N N 172 
GLU   HB2  H  N N 173 
GLU   HB3  H  N N 174 
GLU   HG2  H  N N 175 
GLU   HG3  H  N N 176 
GLU   HE2  H  N N 177 
GLU   HXT  H  N N 178 
GLY   N    N  N N 179 
GLY   CA   C  N N 180 
GLY   C    C  N N 181 
GLY   O    O  N N 182 
GLY   OXT  O  N N 183 
GLY   H    H  N N 184 
GLY   H2   H  N N 185 
GLY   HA2  H  N N 186 
GLY   HA3  H  N N 187 
GLY   HXT  H  N N 188 
HIS   N    N  N N 189 
HIS   CA   C  N S 190 
HIS   C    C  N N 191 
HIS   O    O  N N 192 
HIS   CB   C  N N 193 
HIS   CG   C  Y N 194 
HIS   ND1  N  Y N 195 
HIS   CD2  C  Y N 196 
HIS   CE1  C  Y N 197 
HIS   NE2  N  Y N 198 
HIS   OXT  O  N N 199 
HIS   H    H  N N 200 
HIS   H2   H  N N 201 
HIS   HA   H  N N 202 
HIS   HB2  H  N N 203 
HIS   HB3  H  N N 204 
HIS   HD1  H  N N 205 
HIS   HD2  H  N N 206 
HIS   HE1  H  N N 207 
HIS   HE2  H  N N 208 
HIS   HXT  H  N N 209 
HOH   O    O  N N 210 
HOH   H1   H  N N 211 
HOH   H2   H  N N 212 
ILE   N    N  N N 213 
ILE   CA   C  N S 214 
ILE   C    C  N N 215 
ILE   O    O  N N 216 
ILE   CB   C  N S 217 
ILE   CG1  C  N N 218 
ILE   CG2  C  N N 219 
ILE   CD1  C  N N 220 
ILE   OXT  O  N N 221 
ILE   H    H  N N 222 
ILE   H2   H  N N 223 
ILE   HA   H  N N 224 
ILE   HB   H  N N 225 
ILE   HG12 H  N N 226 
ILE   HG13 H  N N 227 
ILE   HG21 H  N N 228 
ILE   HG22 H  N N 229 
ILE   HG23 H  N N 230 
ILE   HD11 H  N N 231 
ILE   HD12 H  N N 232 
ILE   HD13 H  N N 233 
ILE   HXT  H  N N 234 
LEU   N    N  N N 235 
LEU   CA   C  N S 236 
LEU   C    C  N N 237 
LEU   O    O  N N 238 
LEU   CB   C  N N 239 
LEU   CG   C  N N 240 
LEU   CD1  C  N N 241 
LEU   CD2  C  N N 242 
LEU   OXT  O  N N 243 
LEU   H    H  N N 244 
LEU   H2   H  N N 245 
LEU   HA   H  N N 246 
LEU   HB2  H  N N 247 
LEU   HB3  H  N N 248 
LEU   HG   H  N N 249 
LEU   HD11 H  N N 250 
LEU   HD12 H  N N 251 
LEU   HD13 H  N N 252 
LEU   HD21 H  N N 253 
LEU   HD22 H  N N 254 
LEU   HD23 H  N N 255 
LEU   HXT  H  N N 256 
LYS   N    N  N N 257 
LYS   CA   C  N S 258 
LYS   C    C  N N 259 
LYS   O    O  N N 260 
LYS   CB   C  N N 261 
LYS   CG   C  N N 262 
LYS   CD   C  N N 263 
LYS   CE   C  N N 264 
LYS   NZ   N  N N 265 
LYS   OXT  O  N N 266 
LYS   H    H  N N 267 
LYS   H2   H  N N 268 
LYS   HA   H  N N 269 
LYS   HB2  H  N N 270 
LYS   HB3  H  N N 271 
LYS   HG2  H  N N 272 
LYS   HG3  H  N N 273 
LYS   HD2  H  N N 274 
LYS   HD3  H  N N 275 
LYS   HE2  H  N N 276 
LYS   HE3  H  N N 277 
LYS   HZ1  H  N N 278 
LYS   HZ2  H  N N 279 
LYS   HZ3  H  N N 280 
LYS   HXT  H  N N 281 
MET   N    N  N N 282 
MET   CA   C  N S 283 
MET   C    C  N N 284 
MET   O    O  N N 285 
MET   CB   C  N N 286 
MET   CG   C  N N 287 
MET   SD   S  N N 288 
MET   CE   C  N N 289 
MET   OXT  O  N N 290 
MET   H    H  N N 291 
MET   H2   H  N N 292 
MET   HA   H  N N 293 
MET   HB2  H  N N 294 
MET   HB3  H  N N 295 
MET   HG2  H  N N 296 
MET   HG3  H  N N 297 
MET   HE1  H  N N 298 
MET   HE2  H  N N 299 
MET   HE3  H  N N 300 
MET   HXT  H  N N 301 
PHE   N    N  N N 302 
PHE   CA   C  N S 303 
PHE   C    C  N N 304 
PHE   O    O  N N 305 
PHE   CB   C  N N 306 
PHE   CG   C  Y N 307 
PHE   CD1  C  Y N 308 
PHE   CD2  C  Y N 309 
PHE   CE1  C  Y N 310 
PHE   CE2  C  Y N 311 
PHE   CZ   C  Y N 312 
PHE   OXT  O  N N 313 
PHE   H    H  N N 314 
PHE   H2   H  N N 315 
PHE   HA   H  N N 316 
PHE   HB2  H  N N 317 
PHE   HB3  H  N N 318 
PHE   HD1  H  N N 319 
PHE   HD2  H  N N 320 
PHE   HE1  H  N N 321 
PHE   HE2  H  N N 322 
PHE   HZ   H  N N 323 
PHE   HXT  H  N N 324 
PRO   N    N  N N 325 
PRO   CA   C  N S 326 
PRO   C    C  N N 327 
PRO   O    O  N N 328 
PRO   CB   C  N N 329 
PRO   CG   C  N N 330 
PRO   CD   C  N N 331 
PRO   OXT  O  N N 332 
PRO   H    H  N N 333 
PRO   HA   H  N N 334 
PRO   HB2  H  N N 335 
PRO   HB3  H  N N 336 
PRO   HG2  H  N N 337 
PRO   HG3  H  N N 338 
PRO   HD2  H  N N 339 
PRO   HD3  H  N N 340 
PRO   HXT  H  N N 341 
SER   N    N  N N 342 
SER   CA   C  N S 343 
SER   C    C  N N 344 
SER   O    O  N N 345 
SER   CB   C  N N 346 
SER   OG   O  N N 347 
SER   OXT  O  N N 348 
SER   H    H  N N 349 
SER   H2   H  N N 350 
SER   HA   H  N N 351 
SER   HB2  H  N N 352 
SER   HB3  H  N N 353 
SER   HG   H  N N 354 
SER   HXT  H  N N 355 
THR   N    N  N N 356 
THR   CA   C  N S 357 
THR   C    C  N N 358 
THR   O    O  N N 359 
THR   CB   C  N R 360 
THR   OG1  O  N N 361 
THR   CG2  C  N N 362 
THR   OXT  O  N N 363 
THR   H    H  N N 364 
THR   H2   H  N N 365 
THR   HA   H  N N 366 
THR   HB   H  N N 367 
THR   HG1  H  N N 368 
THR   HG21 H  N N 369 
THR   HG22 H  N N 370 
THR   HG23 H  N N 371 
THR   HXT  H  N N 372 
TRP   N    N  N N 373 
TRP   CA   C  N S 374 
TRP   C    C  N N 375 
TRP   O    O  N N 376 
TRP   CB   C  N N 377 
TRP   CG   C  Y N 378 
TRP   CD1  C  Y N 379 
TRP   CD2  C  Y N 380 
TRP   NE1  N  Y N 381 
TRP   CE2  C  Y N 382 
TRP   CE3  C  Y N 383 
TRP   CZ2  C  Y N 384 
TRP   CZ3  C  Y N 385 
TRP   CH2  C  Y N 386 
TRP   OXT  O  N N 387 
TRP   H    H  N N 388 
TRP   H2   H  N N 389 
TRP   HA   H  N N 390 
TRP   HB2  H  N N 391 
TRP   HB3  H  N N 392 
TRP   HD1  H  N N 393 
TRP   HE1  H  N N 394 
TRP   HE3  H  N N 395 
TRP   HZ2  H  N N 396 
TRP   HZ3  H  N N 397 
TRP   HH2  H  N N 398 
TRP   HXT  H  N N 399 
TYR   N    N  N N 400 
TYR   CA   C  N S 401 
TYR   C    C  N N 402 
TYR   O    O  N N 403 
TYR   CB   C  N N 404 
TYR   CG   C  Y N 405 
TYR   CD1  C  Y N 406 
TYR   CD2  C  Y N 407 
TYR   CE1  C  Y N 408 
TYR   CE2  C  Y N 409 
TYR   CZ   C  Y N 410 
TYR   OH   O  N N 411 
TYR   OXT  O  N N 412 
TYR   H    H  N N 413 
TYR   H2   H  N N 414 
TYR   HA   H  N N 415 
TYR   HB2  H  N N 416 
TYR   HB3  H  N N 417 
TYR   HD1  H  N N 418 
TYR   HD2  H  N N 419 
TYR   HE1  H  N N 420 
TYR   HE2  H  N N 421 
TYR   HH   H  N N 422 
TYR   HXT  H  N N 423 
VAL   N    N  N N 424 
VAL   CA   C  N S 425 
VAL   C    C  N N 426 
VAL   O    O  N N 427 
VAL   CB   C  N N 428 
VAL   CG1  C  N N 429 
VAL   CG2  C  N N 430 
VAL   OXT  O  N N 431 
VAL   H    H  N N 432 
VAL   H2   H  N N 433 
VAL   HA   H  N N 434 
VAL   HB   H  N N 435 
VAL   HG11 H  N N 436 
VAL   HG12 H  N N 437 
VAL   HG13 H  N N 438 
VAL   HG21 H  N N 439 
VAL   HG22 H  N N 440 
VAL   HG23 H  N N 441 
VAL   HXT  H  N N 442 
ZN    ZN   ZN N N 443 
# 
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 
A1B2N C   S    sing N N 1   
A1B2N O   S    doub N N 2   
A1B2N O1  S    doub N N 3   
A1B2N S   C1   sing N N 4   
A1B2N C1  C2   doub Y N 5   
A1B2N C2  C3   sing Y N 6   
A1B2N C3  C4   doub Y N 7   
A1B2N C4  C5   sing Y N 8   
A1B2N C5  C6   doub Y N 9   
A1B2N C1  C6   sing Y N 10  
A1B2N C6  C7   sing N N 11  
A1B2N C7  C8   sing N N 12  
A1B2N O2  C8   doub N N 13  
A1B2N C8  N    sing N N 14  
A1B2N N   C9   sing N N 15  
A1B2N C9  C10  sing N N 16  
A1B2N C10 C11  sing N N 17  
A1B2N C11 C12  sing N N 18  
A1B2N C12 C13  sing N N 19  
A1B2N N1  C13  sing N N 20  
A1B2N C13 O3   doub N N 21  
A1B2N C14 C12  sing N N 22  
A1B2N N   C14  sing N N 23  
A1B2N N1  H17  sing N N 24  
A1B2N N1  H16  sing N N 25  
A1B2N C4  H6   sing N N 26  
A1B2N C5  H7   sing N N 27  
A1B2N C7  H9   sing N N 28  
A1B2N C7  H8   sing N N 29  
A1B2N C10 H12  sing N N 30  
A1B2N C10 H13  sing N N 31  
A1B2N C12 H    sing N N 32  
A1B2N C11 H14  sing N N 33  
A1B2N C11 H15  sing N N 34  
A1B2N C9  H11  sing N N 35  
A1B2N C9  H10  sing N N 36  
A1B2N C14 H18  sing N N 37  
A1B2N C14 H19  sing N N 38  
A1B2N C   H2   sing N N 39  
A1B2N C   H1   sing N N 40  
A1B2N C   H3   sing N N 41  
A1B2N C3  H5   sing N N 42  
A1B2N C2  H4   sing N N 43  
ALA   N   CA   sing N N 44  
ALA   N   H    sing N N 45  
ALA   N   H2   sing N N 46  
ALA   CA  C    sing N N 47  
ALA   CA  CB   sing N N 48  
ALA   CA  HA   sing N N 49  
ALA   C   O    doub N N 50  
ALA   C   OXT  sing N N 51  
ALA   CB  HB1  sing N N 52  
ALA   CB  HB2  sing N N 53  
ALA   CB  HB3  sing N N 54  
ALA   OXT HXT  sing N N 55  
ARG   N   CA   sing N N 56  
ARG   N   H    sing N N 57  
ARG   N   H2   sing N N 58  
ARG   CA  C    sing N N 59  
ARG   CA  CB   sing N N 60  
ARG   CA  HA   sing N N 61  
ARG   C   O    doub N N 62  
ARG   C   OXT  sing N N 63  
ARG   CB  CG   sing N N 64  
ARG   CB  HB2  sing N N 65  
ARG   CB  HB3  sing N N 66  
ARG   CG  CD   sing N N 67  
ARG   CG  HG2  sing N N 68  
ARG   CG  HG3  sing N N 69  
ARG   CD  NE   sing N N 70  
ARG   CD  HD2  sing N N 71  
ARG   CD  HD3  sing N N 72  
ARG   NE  CZ   sing N N 73  
ARG   NE  HE   sing N N 74  
ARG   CZ  NH1  sing N N 75  
ARG   CZ  NH2  doub N N 76  
ARG   NH1 HH11 sing N N 77  
ARG   NH1 HH12 sing N N 78  
ARG   NH2 HH21 sing N N 79  
ARG   NH2 HH22 sing N N 80  
ARG   OXT HXT  sing N N 81  
ASN   N   CA   sing N N 82  
ASN   N   H    sing N N 83  
ASN   N   H2   sing N N 84  
ASN   CA  C    sing N N 85  
ASN   CA  CB   sing N N 86  
ASN   CA  HA   sing N N 87  
ASN   C   O    doub N N 88  
ASN   C   OXT  sing N N 89  
ASN   CB  CG   sing N N 90  
ASN   CB  HB2  sing N N 91  
ASN   CB  HB3  sing N N 92  
ASN   CG  OD1  doub N N 93  
ASN   CG  ND2  sing N N 94  
ASN   ND2 HD21 sing N N 95  
ASN   ND2 HD22 sing N N 96  
ASN   OXT HXT  sing N N 97  
ASP   N   CA   sing N N 98  
ASP   N   H    sing N N 99  
ASP   N   H2   sing N N 100 
ASP   CA  C    sing N N 101 
ASP   CA  CB   sing N N 102 
ASP   CA  HA   sing N N 103 
ASP   C   O    doub N N 104 
ASP   C   OXT  sing N N 105 
ASP   CB  CG   sing N N 106 
ASP   CB  HB2  sing N N 107 
ASP   CB  HB3  sing N N 108 
ASP   CG  OD1  doub N N 109 
ASP   CG  OD2  sing N N 110 
ASP   OD2 HD2  sing N N 111 
ASP   OXT HXT  sing N N 112 
CYS   N   CA   sing N N 113 
CYS   N   H    sing N N 114 
CYS   N   H2   sing N N 115 
CYS   CA  C    sing N N 116 
CYS   CA  CB   sing N N 117 
CYS   CA  HA   sing N N 118 
CYS   C   O    doub N N 119 
CYS   C   OXT  sing N N 120 
CYS   CB  SG   sing N N 121 
CYS   CB  HB2  sing N N 122 
CYS   CB  HB3  sing N N 123 
CYS   SG  HG   sing N N 124 
CYS   OXT HXT  sing N N 125 
DMS   S   O    doub N N 126 
DMS   S   C1   sing N N 127 
DMS   S   C2   sing N N 128 
DMS   C1  H11  sing N N 129 
DMS   C1  H12  sing N N 130 
DMS   C1  H13  sing N N 131 
DMS   C2  H21  sing N N 132 
DMS   C2  H22  sing N N 133 
DMS   C2  H23  sing N N 134 
GLN   N   CA   sing N N 135 
GLN   N   H    sing N N 136 
GLN   N   H2   sing N N 137 
GLN   CA  C    sing N N 138 
GLN   CA  CB   sing N N 139 
GLN   CA  HA   sing N N 140 
GLN   C   O    doub N N 141 
GLN   C   OXT  sing N N 142 
GLN   CB  CG   sing N N 143 
GLN   CB  HB2  sing N N 144 
GLN   CB  HB3  sing N N 145 
GLN   CG  CD   sing N N 146 
GLN   CG  HG2  sing N N 147 
GLN   CG  HG3  sing N N 148 
GLN   CD  OE1  doub N N 149 
GLN   CD  NE2  sing N N 150 
GLN   NE2 HE21 sing N N 151 
GLN   NE2 HE22 sing N N 152 
GLN   OXT HXT  sing N N 153 
GLU   N   CA   sing N N 154 
GLU   N   H    sing N N 155 
GLU   N   H2   sing N N 156 
GLU   CA  C    sing N N 157 
GLU   CA  CB   sing N N 158 
GLU   CA  HA   sing N N 159 
GLU   C   O    doub N N 160 
GLU   C   OXT  sing N N 161 
GLU   CB  CG   sing N N 162 
GLU   CB  HB2  sing N N 163 
GLU   CB  HB3  sing N N 164 
GLU   CG  CD   sing N N 165 
GLU   CG  HG2  sing N N 166 
GLU   CG  HG3  sing N N 167 
GLU   CD  OE1  doub N N 168 
GLU   CD  OE2  sing N N 169 
GLU   OE2 HE2  sing N N 170 
GLU   OXT HXT  sing N N 171 
GLY   N   CA   sing N N 172 
GLY   N   H    sing N N 173 
GLY   N   H2   sing N N 174 
GLY   CA  C    sing N N 175 
GLY   CA  HA2  sing N N 176 
GLY   CA  HA3  sing N N 177 
GLY   C   O    doub N N 178 
GLY   C   OXT  sing N N 179 
GLY   OXT HXT  sing N N 180 
HIS   N   CA   sing N N 181 
HIS   N   H    sing N N 182 
HIS   N   H2   sing N N 183 
HIS   CA  C    sing N N 184 
HIS   CA  CB   sing N N 185 
HIS   CA  HA   sing N N 186 
HIS   C   O    doub N N 187 
HIS   C   OXT  sing N N 188 
HIS   CB  CG   sing N N 189 
HIS   CB  HB2  sing N N 190 
HIS   CB  HB3  sing N N 191 
HIS   CG  ND1  sing Y N 192 
HIS   CG  CD2  doub Y N 193 
HIS   ND1 CE1  doub Y N 194 
HIS   ND1 HD1  sing N N 195 
HIS   CD2 NE2  sing Y N 196 
HIS   CD2 HD2  sing N N 197 
HIS   CE1 NE2  sing Y N 198 
HIS   CE1 HE1  sing N N 199 
HIS   NE2 HE2  sing N N 200 
HIS   OXT HXT  sing N N 201 
HOH   O   H1   sing N N 202 
HOH   O   H2   sing N N 203 
ILE   N   CA   sing N N 204 
ILE   N   H    sing N N 205 
ILE   N   H2   sing N N 206 
ILE   CA  C    sing N N 207 
ILE   CA  CB   sing N N 208 
ILE   CA  HA   sing N N 209 
ILE   C   O    doub N N 210 
ILE   C   OXT  sing N N 211 
ILE   CB  CG1  sing N N 212 
ILE   CB  CG2  sing N N 213 
ILE   CB  HB   sing N N 214 
ILE   CG1 CD1  sing N N 215 
ILE   CG1 HG12 sing N N 216 
ILE   CG1 HG13 sing N N 217 
ILE   CG2 HG21 sing N N 218 
ILE   CG2 HG22 sing N N 219 
ILE   CG2 HG23 sing N N 220 
ILE   CD1 HD11 sing N N 221 
ILE   CD1 HD12 sing N N 222 
ILE   CD1 HD13 sing N N 223 
ILE   OXT HXT  sing N N 224 
LEU   N   CA   sing N N 225 
LEU   N   H    sing N N 226 
LEU   N   H2   sing N N 227 
LEU   CA  C    sing N N 228 
LEU   CA  CB   sing N N 229 
LEU   CA  HA   sing N N 230 
LEU   C   O    doub N N 231 
LEU   C   OXT  sing N N 232 
LEU   CB  CG   sing N N 233 
LEU   CB  HB2  sing N N 234 
LEU   CB  HB3  sing N N 235 
LEU   CG  CD1  sing N N 236 
LEU   CG  CD2  sing N N 237 
LEU   CG  HG   sing N N 238 
LEU   CD1 HD11 sing N N 239 
LEU   CD1 HD12 sing N N 240 
LEU   CD1 HD13 sing N N 241 
LEU   CD2 HD21 sing N N 242 
LEU   CD2 HD22 sing N N 243 
LEU   CD2 HD23 sing N N 244 
LEU   OXT HXT  sing N N 245 
LYS   N   CA   sing N N 246 
LYS   N   H    sing N N 247 
LYS   N   H2   sing N N 248 
LYS   CA  C    sing N N 249 
LYS   CA  CB   sing N N 250 
LYS   CA  HA   sing N N 251 
LYS   C   O    doub N N 252 
LYS   C   OXT  sing N N 253 
LYS   CB  CG   sing N N 254 
LYS   CB  HB2  sing N N 255 
LYS   CB  HB3  sing N N 256 
LYS   CG  CD   sing N N 257 
LYS   CG  HG2  sing N N 258 
LYS   CG  HG3  sing N N 259 
LYS   CD  CE   sing N N 260 
LYS   CD  HD2  sing N N 261 
LYS   CD  HD3  sing N N 262 
LYS   CE  NZ   sing N N 263 
LYS   CE  HE2  sing N N 264 
LYS   CE  HE3  sing N N 265 
LYS   NZ  HZ1  sing N N 266 
LYS   NZ  HZ2  sing N N 267 
LYS   NZ  HZ3  sing N N 268 
LYS   OXT HXT  sing N N 269 
MET   N   CA   sing N N 270 
MET   N   H    sing N N 271 
MET   N   H2   sing N N 272 
MET   CA  C    sing N N 273 
MET   CA  CB   sing N N 274 
MET   CA  HA   sing N N 275 
MET   C   O    doub N N 276 
MET   C   OXT  sing N N 277 
MET   CB  CG   sing N N 278 
MET   CB  HB2  sing N N 279 
MET   CB  HB3  sing N N 280 
MET   CG  SD   sing N N 281 
MET   CG  HG2  sing N N 282 
MET   CG  HG3  sing N N 283 
MET   SD  CE   sing N N 284 
MET   CE  HE1  sing N N 285 
MET   CE  HE2  sing N N 286 
MET   CE  HE3  sing N N 287 
MET   OXT HXT  sing N N 288 
PHE   N   CA   sing N N 289 
PHE   N   H    sing N N 290 
PHE   N   H2   sing N N 291 
PHE   CA  C    sing N N 292 
PHE   CA  CB   sing N N 293 
PHE   CA  HA   sing N N 294 
PHE   C   O    doub N N 295 
PHE   C   OXT  sing N N 296 
PHE   CB  CG   sing N N 297 
PHE   CB  HB2  sing N N 298 
PHE   CB  HB3  sing N N 299 
PHE   CG  CD1  doub Y N 300 
PHE   CG  CD2  sing Y N 301 
PHE   CD1 CE1  sing Y N 302 
PHE   CD1 HD1  sing N N 303 
PHE   CD2 CE2  doub Y N 304 
PHE   CD2 HD2  sing N N 305 
PHE   CE1 CZ   doub Y N 306 
PHE   CE1 HE1  sing N N 307 
PHE   CE2 CZ   sing Y N 308 
PHE   CE2 HE2  sing N N 309 
PHE   CZ  HZ   sing N N 310 
PHE   OXT HXT  sing N N 311 
PRO   N   CA   sing N N 312 
PRO   N   CD   sing N N 313 
PRO   N   H    sing N N 314 
PRO   CA  C    sing N N 315 
PRO   CA  CB   sing N N 316 
PRO   CA  HA   sing N N 317 
PRO   C   O    doub N N 318 
PRO   C   OXT  sing N N 319 
PRO   CB  CG   sing N N 320 
PRO   CB  HB2  sing N N 321 
PRO   CB  HB3  sing N N 322 
PRO   CG  CD   sing N N 323 
PRO   CG  HG2  sing N N 324 
PRO   CG  HG3  sing N N 325 
PRO   CD  HD2  sing N N 326 
PRO   CD  HD3  sing N N 327 
PRO   OXT HXT  sing N N 328 
SER   N   CA   sing N N 329 
SER   N   H    sing N N 330 
SER   N   H2   sing N N 331 
SER   CA  C    sing N N 332 
SER   CA  CB   sing N N 333 
SER   CA  HA   sing N N 334 
SER   C   O    doub N N 335 
SER   C   OXT  sing N N 336 
SER   CB  OG   sing N N 337 
SER   CB  HB2  sing N N 338 
SER   CB  HB3  sing N N 339 
SER   OG  HG   sing N N 340 
SER   OXT HXT  sing N N 341 
THR   N   CA   sing N N 342 
THR   N   H    sing N N 343 
THR   N   H2   sing N N 344 
THR   CA  C    sing N N 345 
THR   CA  CB   sing N N 346 
THR   CA  HA   sing N N 347 
THR   C   O    doub N N 348 
THR   C   OXT  sing N N 349 
THR   CB  OG1  sing N N 350 
THR   CB  CG2  sing N N 351 
THR   CB  HB   sing N N 352 
THR   OG1 HG1  sing N N 353 
THR   CG2 HG21 sing N N 354 
THR   CG2 HG22 sing N N 355 
THR   CG2 HG23 sing N N 356 
THR   OXT HXT  sing N N 357 
TRP   N   CA   sing N N 358 
TRP   N   H    sing N N 359 
TRP   N   H2   sing N N 360 
TRP   CA  C    sing N N 361 
TRP   CA  CB   sing N N 362 
TRP   CA  HA   sing N N 363 
TRP   C   O    doub N N 364 
TRP   C   OXT  sing N N 365 
TRP   CB  CG   sing N N 366 
TRP   CB  HB2  sing N N 367 
TRP   CB  HB3  sing N N 368 
TRP   CG  CD1  doub Y N 369 
TRP   CG  CD2  sing Y N 370 
TRP   CD1 NE1  sing Y N 371 
TRP   CD1 HD1  sing N N 372 
TRP   CD2 CE2  doub Y N 373 
TRP   CD2 CE3  sing Y N 374 
TRP   NE1 CE2  sing Y N 375 
TRP   NE1 HE1  sing N N 376 
TRP   CE2 CZ2  sing Y N 377 
TRP   CE3 CZ3  doub Y N 378 
TRP   CE3 HE3  sing N N 379 
TRP   CZ2 CH2  doub Y N 380 
TRP   CZ2 HZ2  sing N N 381 
TRP   CZ3 CH2  sing Y N 382 
TRP   CZ3 HZ3  sing N N 383 
TRP   CH2 HH2  sing N N 384 
TRP   OXT HXT  sing N N 385 
TYR   N   CA   sing N N 386 
TYR   N   H    sing N N 387 
TYR   N   H2   sing N N 388 
TYR   CA  C    sing N N 389 
TYR   CA  CB   sing N N 390 
TYR   CA  HA   sing N N 391 
TYR   C   O    doub N N 392 
TYR   C   OXT  sing N N 393 
TYR   CB  CG   sing N N 394 
TYR   CB  HB2  sing N N 395 
TYR   CB  HB3  sing N N 396 
TYR   CG  CD1  doub Y N 397 
TYR   CG  CD2  sing Y N 398 
TYR   CD1 CE1  sing Y N 399 
TYR   CD1 HD1  sing N N 400 
TYR   CD2 CE2  doub Y N 401 
TYR   CD2 HD2  sing N N 402 
TYR   CE1 CZ   doub Y N 403 
TYR   CE1 HE1  sing N N 404 
TYR   CE2 CZ   sing Y N 405 
TYR   CE2 HE2  sing N N 406 
TYR   CZ  OH   sing N N 407 
TYR   OH  HH   sing N N 408 
TYR   OXT HXT  sing N N 409 
VAL   N   CA   sing N N 410 
VAL   N   H    sing N N 411 
VAL   N   H2   sing N N 412 
VAL   CA  C    sing N N 413 
VAL   CA  CB   sing N N 414 
VAL   CA  HA   sing N N 415 
VAL   C   O    doub N N 416 
VAL   C   OXT  sing N N 417 
VAL   CB  CG1  sing N N 418 
VAL   CB  CG2  sing N N 419 
VAL   CB  HB   sing N N 420 
VAL   CG1 HG11 sing N N 421 
VAL   CG1 HG12 sing N N 422 
VAL   CG1 HG13 sing N N 423 
VAL   CG2 HG21 sing N N 424 
VAL   CG2 HG22 sing N N 425 
VAL   CG2 HG23 sing N N 426 
VAL   OXT HXT  sing N N 427 
# 
_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                    7I49 
_atom_sites.fract_transf_matrix[1][1]   0.013711 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000668 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016116 
_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]   0.030494 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER   A 1 1   ? 18.873 6.151   24.399 1.00 39.26 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 20.082 6.307   23.583 1.00 39.75 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 20.275 5.109   22.621 1.00 38.54 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 19.699 4.040   22.847 1.00 39.31 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 21.301 6.498   24.481 1.00 42.07 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 21.347 5.456   25.440 1.00 45.49 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 21.053 5.312   21.552 1.00 36.54 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 21.315 4.288   20.539 1.00 34.96 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 21.581 4.837   19.144 1.00 32.92 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 21.152 5.950   18.825 1.00 33.02 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 22.286 4.059   18.294 1.00 30.92 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 22.646 4.469   16.934 1.00 29.93 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 22.689 3.288   15.932 1.00 28.76 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 22.742 2.131   16.351 1.00 28.38 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 24.008 5.147   16.971 1.00 30.61 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 22.684 3.583   14.607 1.00 28.16 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.819 2.589   13.541 1.00 27.90 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 24.199 2.800   12.916 1.00 29.39 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.573 3.921   12.565 1.00 28.66 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.735 2.739   12.446 1.00 27.06 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 20.313 2.800   13.034 1.00 25.81 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.862 1.624   11.407 1.00 27.51 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.345 3.428   12.119 1.00 25.31 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.940 1.723   12.756 1.00 31.14 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 26.274 1.763   12.198 1.00 33.20 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 26.307 0.978   10.895 1.00 35.11 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 26.301 -0.254  10.937 1.00 35.71 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.239 1.150   13.220 1.00 33.96 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.418 2.021   14.441 1.00 35.07 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 28.269 3.117   14.417 1.00 36.36 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 26.716 1.767   15.609 1.00 36.03 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 28.407 3.950   15.521 1.00 37.08 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 26.839 2.597   16.716 1.00 37.19 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 27.704 3.676   16.675 1.00 38.07 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 27.854 4.475   17.774 1.00 39.53 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 26.299 1.676   9.741  1.00 36.00 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 26.346 1.041   8.419  1.00 37.14 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.481 1.632   7.583  1.00 38.37 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.474 2.822   7.258  1.00 38.58 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.995 1.064   7.660  1.00 38.07 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.406 2.472   7.592  1.00 38.26 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 25.155 0.477   6.262  1.00 38.84 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.489 0.815   7.269  1.00 38.51 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.647 1.277   6.520  1.00 40.04 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.378 2.354   7.294  1.00 41.41 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.460 2.261   8.523  1.00 41.97 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.811 3.430   6.615  1.00 41.60 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.474 4.525   7.307  1.00 41.55 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.468 5.564   7.848  1.00 39.45 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.813 6.740   7.940  1.00 39.71 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.519 5.177   6.408  1.00 45.05 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.671 4.255   6.115  1.00 51.14 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 33.999 3.363   6.902  1.00 52.26 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 34.320 4.456   4.980  1.00 54.36 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.258 5.134   8.257  1.00 36.83 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.268 6.084   8.786  1.00 34.25 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.749 5.716   10.170 1.00 31.60 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.687 4.544   10.532 1.00 31.34 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 27.062 6.228   7.829  1.00 33.21 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.411 6.812   6.483  1.00 33.09 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 28.038 8.045   6.380  1.00 33.93 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.056 6.164   5.312  1.00 33.80 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.352 8.594   5.143  1.00 35.20 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.350 6.705   4.071  1.00 35.22 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 28.023 7.909   3.988  1.00 36.62 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.319 8.443   2.755  1.00 38.29 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.295 6.730   10.910 1.00 28.38 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.649 6.541   12.195 1.00 26.16 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.340 7.354   12.123 1.00 24.37 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.378 8.539   11.807 1.00 24.22 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.565 7.008   13.336 1.00 27.04 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.848 7.255   14.662 1.00 29.51 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.852 7.540   15.747 1.00 33.52 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 27.434 8.610   16.654 1.00 36.76 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 26.935 8.407   17.871 1.00 38.86 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 26.736 7.171   18.317 1.00 37.87 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 26.601 9.438   18.640 1.00 38.14 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 24.193 6.720   12.349 1.00 22.95 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.899 7.411   12.290 1.00 22.81 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.374 7.553   13.691 1.00 22.53 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 22.239 6.553   14.370 1.00 22.82 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.867 6.666   11.421 1.00 22.80 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.636 7.541   11.198 1.00 22.72 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.481 6.222   10.088 1.00 22.25 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 22.090 8.768   14.142 1.00 21.79 ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 21.590 8.990   15.510 1.00 21.87 ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 20.363 9.924   15.500 1.00 21.19 ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 20.142 10.617  14.504 1.00 21.72 ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 22.703 9.636   16.390 1.00 22.39 ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 23.784 8.639   16.735 1.00 23.73 ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 23.289 10.869  15.718 1.00 22.39 ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 19.626 10.043  16.639 1.00 19.76 ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 18.558 11.055  16.745 1.00 19.87 ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 19.268 12.407  16.741 1.00 20.43 ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 20.280 12.569  17.449 1.00 21.36 ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.765 10.937  18.067 1.00 20.18 ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 16.934 9.674   18.185 1.00 22.01 ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.370 8.676   18.776 1.00 23.81 ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 15.738 9.690   17.627 1.00 20.45 ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 18.808 13.355  15.920 1.00 19.83 ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 19.444 14.673  15.857 1.00 19.46 ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 19.482 15.369  17.224 1.00 21.87 ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 20.530 15.922  17.582 1.00 22.24 ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 18.785 15.569  14.790 1.00 17.53 ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.567 16.854  14.413 1.00 16.85 ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 18.622 17.751  13.630 1.00 16.27 ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.174 19.007  13.084 1.00 18.60 ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.278 20.144  13.765 1.00 20.30 ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 19.028 20.170  15.071 1.00 18.98 ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 19.677 21.256  13.156 1.00 20.65 ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 18.385 15.292  18.019 1.00 23.18 ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 18.355 15.939  19.353 1.00 24.52 ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 19.353 15.369  20.355 1.00 26.73 ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 19.667 16.036  21.345 1.00 26.89 ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 16.947 15.971  19.960 1.00 24.75 ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 16.413 14.657  20.436 1.00 26.68 ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 15.710 13.817  19.587 1.00 27.77 ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 16.424 14.115  21.683 1.00 28.18 ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 15.358 12.767  20.326 1.00 29.21 ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 15.753 12.905  21.598 1.00 28.99 ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 19.890 14.171  20.085 1.00 28.25 ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 20.857 13.519  20.964 1.00 29.70 ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 22.297 13.484  20.399 1.00 31.45 ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 23.166 12.854  21.011 1.00 32.31 ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 20.384 12.075  21.245 1.00 29.24 ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 19.124 11.924  22.120 1.00 30.35 ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 18.761 10.446  22.335 1.00 30.24 ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 19.308 12.609  23.470 1.00 30.84 ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 22.533 14.068  19.213 1.00 31.79 ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 23.849 14.051  18.575 1.00 32.92 ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 24.905 14.744  19.433 1.00 34.61 ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 24.603 15.722  20.121 1.00 34.01 ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 23.781 14.702  17.193 1.00 32.73 ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 26.145 14.237  19.377 1.00 36.39 ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 27.281 14.743  20.161 1.00 38.67 ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 28.092 15.856  19.416 1.00 40.54 ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 27.777 16.183  18.271 1.00 40.14 ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 28.180 13.541  20.548 1.00 40.23 ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 28.864 13.096  19.379 1.00 41.13 ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 27.408 12.396  21.183 1.00 41.41 ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 29.140 16.425  20.065 1.00 42.31 ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 30.013 17.411  19.433 1.00 44.21 ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 30.769 16.741  18.282 1.00 44.04 ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 30.966 17.367  17.243 1.00 43.96 ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 31.044 17.953  20.435 1.00 47.40 ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 30.495 18.852  21.497 1.00 52.55 ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 30.168 20.165  21.230 1.00 55.43 ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 30.338 18.620  22.824 1.00 54.71 ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 29.783 20.679  22.389 1.00 56.39 ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 29.864 19.782  23.376 1.00 56.19 ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 31.218 15.483  18.484 1.00 43.70 ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 31.939 14.707  17.480 1.00 44.07 ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 31.065 14.452  16.263 1.00 41.81 ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 31.544 14.603  15.141 1.00 42.73 ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 32.421 13.392  18.059 1.00 47.86 ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 33.314 12.618  17.120 1.00 54.57 ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.402 13.077  16.748 1.00 56.10 ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 32.876 11.410  16.735 1.00 56.20 ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 29.775 14.116  16.474 1.00 38.62 ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 28.795 13.937  15.393 1.00 35.41 ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 28.697 15.224  14.561 1.00 33.57 ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 28.764 15.172  13.344 1.00 33.64 ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 27.418 13.578  15.974 1.00 34.58 ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 27.313 12.144  16.447 1.00 36.25 ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 27.779 11.257  15.729 1.00 35.96 ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 26.774 11.920  17.550 1.00 37.34 ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 28.587 16.376  15.212 1.00 32.50 ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.505 17.664  14.511 1.00 32.19 ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 29.836 18.047  13.813 1.00 34.11 ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 29.819 18.688  12.771 1.00 34.45 ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 28.023 18.780  15.468 1.00 30.52 ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 26.528 18.841  15.609 1.00 28.12 ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 25.776 18.350  16.635 1.00 28.52 ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 25.608 19.391  14.664 1.00 26.68 ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 24.438 18.563  16.385 1.00 28.25 ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 24.308 19.197  15.178 1.00 27.34 ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 25.750 19.987  13.410 1.00 26.63 ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 23.164 19.639  14.505 1.00 27.05 ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.620 20.459  12.766 1.00 27.18 ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 23.343 20.246  13.293 1.00 26.85 ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 30.981 17.641  14.377 1.00 35.81 ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.292 17.921  13.768 1.00 37.90 ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.567 17.005  12.551 1.00 39.19 ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.405 17.340  11.709 1.00 40.92 ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 33.406 17.747  14.799 1.00 38.06 ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 31.906 15.837  12.488 1.00 37.81 ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 32.041 14.897  11.375 1.00 37.02 ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.696 14.719  10.639 1.00 34.28 ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.397 13.637  10.168 1.00 34.17 ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.552 13.551  11.880 1.00 39.08 ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 34.000 13.582  12.350 1.00 44.58 ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 34.927 13.872  11.586 1.00 47.48 ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 34.232 13.262  13.614 1.00 44.84 ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 29.898 15.787  10.562 1.00 32.01 ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.566 15.841  9.958  1.00 29.30 ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.559 15.510  8.471  1.00 28.43 ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.326 16.103  7.719  1.00 28.74 ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 28.003 17.259  10.156 1.00 28.09 ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.634 17.566  9.503  1.00 27.80 ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.517 16.719  10.144 1.00 27.19 ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.307 19.053  9.559  1.00 26.69 ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.643 14.605  8.042  1.00 27.01 ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.420 14.235  6.648  1.00 26.19 ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 26.097 14.881  6.141  1.00 25.90 ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 26.069 15.530  5.095  1.00 27.30 ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.374 12.701  6.502  1.00 26.91 ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 26.877 12.304  5.122  1.00 27.83 ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 28.739 12.081  6.794  1.00 27.19 ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 25.027 14.731  6.917  1.00 23.79 ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 23.676 15.191  6.607  1.00 21.94 ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 22.850 15.239  7.905  1.00 19.60 ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 23.057 14.433  8.802  1.00 19.18 ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 23.021 14.201  5.605  1.00 21.55 ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.545 14.386  5.379  1.00 22.23 ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 20.945 15.325  4.593  1.00 23.53 ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.481 13.623  5.974  1.00 22.11 ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.575 15.181  4.644  1.00 23.91 ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.265 14.145  5.485  1.00 23.28 ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.439 12.558  6.885  1.00 21.93 ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 18.023 13.621  5.860  1.00 23.33 ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.210 12.044  7.253  1.00 22.50 ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 18.021 12.575  6.749  1.00 22.77 ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 21.943 16.202  8.012  1.00 17.75 ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 21.037 16.297  9.144  1.00 17.09 ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 19.693 16.910  8.660  1.00 16.71 ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 19.664 17.655  7.680  1.00 16.46 ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 21.649 17.070  10.332 1.00 16.87 ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.209 18.442  9.969  1.00 18.42 ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.230 19.595  9.809  1.00 21.38 ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 21.534 20.521  9.020  1.00 21.33 ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 20.148 19.561  10.438 1.00 21.24 ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 18.597 16.544  9.306  1.00 16.33 ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.280 17.071  8.964  1.00 16.21 ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.481 17.191  10.269 1.00 15.84 ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 16.066 16.192  10.854 1.00 16.13 ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.571 16.193  7.931  1.00 18.46 ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.321 16.818  7.333  1.00 24.89 ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 14.674 17.620  8.019  1.00 24.23 ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 14.995 16.499  6.176  1.00 28.72 ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.271 18.436  10.712 1.00 14.49 ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 15.526 18.758  11.924 0.50 14.52 ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 15.540 18.683  11.948 0.50 14.60 ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 14.088 18.217  11.820 1.00 14.83 ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 13.532 17.747  12.801 1.00 14.88 ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 15.480 20.276  12.096 0.50 14.90 ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 15.594 20.161  12.329 0.50 15.30 ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 15.729 20.691  13.424 0.50 16.10 ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 14.852 20.927  11.395 0.50 17.39 ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 13.478 18.316  10.614 1.00 14.97 ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 12.098 17.852  10.436 1.00 16.23 ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 11.941 16.333  10.594 1.00 15.38 ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 10.829 15.880  10.790 1.00 15.66 ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 11.514 18.323  9.107  1.00 19.40 ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 11.913 17.493  8.028  1.00 23.53 ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 13.017 15.565  10.479 1.00 13.72 ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 12.989 14.099  10.657 1.00 13.01 ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 13.617 13.640  11.957 1.00 13.48 ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 13.541 12.449  12.271 1.00 13.59 ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 13.730 13.403  9.499  1.00 12.70 ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 13.081 13.687  8.150  1.00 12.06 ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 13.828 13.023  6.999  1.00 14.16 ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 13.878 11.560  7.102  1.00 14.08 ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 14.091 10.743  6.069  1.00 16.88 ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 14.259 11.233  4.847  1.00 15.52 ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 14.145 9.430   6.254  1.00 18.34 ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 14.304 14.563  12.685 1.00 14.08 ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 15.034 14.288  13.919 1.00 13.83 ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 16.163 13.278  13.606 1.00 13.85 ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 16.388 12.372  14.394 1.00 13.87 ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 14.105 13.777  15.045 1.00 14.18 ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 14.796 13.462  16.365 1.00 18.39 ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 15.617 14.284  16.812 1.00 17.12 ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 14.521 12.360  16.948 1.00 21.46 ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 16.845 13.412  12.454 1.00 14.03 ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 17.972 12.527  12.109 1.00 14.13 ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 19.258 13.323  11.874 1.00 15.92 ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 19.248 14.427  11.337 1.00 17.13 ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.728 11.685  10.831 1.00 13.70 ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 16.679 10.541  10.879 1.00 14.42 ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 16.574 9.845   9.511  1.00 12.99 ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 16.995 9.501   11.999 1.00 14.90 ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 20.373 12.726  12.231 1.00 16.71 ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 21.684 13.284  11.957 1.00 17.50 ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 22.551 12.095  11.602 1.00 18.64 ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 22.457 11.036  12.231 1.00 19.44 ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 22.255 14.088  13.161 1.00 17.55 ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 23.580 14.797  12.896 1.00 19.14 ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 23.637 16.136  13.599 1.00 20.21 ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 24.750 13.937  13.312 1.00 20.36 ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 23.355 12.234  10.553 1.00 19.33 ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 24.291 11.193  10.145 1.00 20.66 ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 25.715 11.765  10.155 1.00 22.76 ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 25.955 12.841  9.584  1.00 21.65 ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 23.951 10.560  8.777  1.00 20.84 ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 25.009 9.518   8.392  1.00 21.66 ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 22.555 9.928   8.798  1.00 20.22 ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 26.639 11.073  10.833 1.00 25.17 ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 28.039 11.484  10.861 1.00 29.21 ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 28.968 10.371  10.321 1.00 33.50 ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 28.556 9.213   10.221 1.00 31.72 ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 28.455 11.916  12.263 1.00 30.62 ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 28.160 10.911  13.217 1.00 32.65 ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 30.218 10.730  9.962  1.00 37.92 ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 31.166 9.754   9.422  1.00 42.82 ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 31.970 9.030   10.503 1.00 46.99 ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 32.196 9.578   11.578 1.00 47.81 ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 32.121 10.432  8.452  1.00 45.04 ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 32.793 11.473  9.137  1.00 48.60 ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 32.381 7.790   10.231 1.00 49.72 ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 33.165 7.006   11.190 1.00 53.53 ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 34.430 6.450   10.542 1.00 57.84 ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 34.456 6.232   9.331  1.00 58.46 ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 32.349 5.846   11.787 1.00 54.62 ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 32.164 4.823   10.806 1.00 56.07 ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 31.019 6.286   12.358 1.00 54.40 ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? 35.460 6.179   11.347 1.00 60.64 ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? 36.696 5.595   10.827 1.00 63.21 ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? 36.573 4.069   10.711 1.00 64.98 ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? 37.221 3.459   9.855  1.00 66.46 ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? 37.890 5.973   11.713 1.00 65.51 ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? 37.647 5.500   13.036 1.00 67.59 ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? 38.149 7.462   11.747 1.00 65.69 ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? 35.809 3.442   11.614 1.00 64.40 ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? 35.630 2.001   11.598 1.00 64.23 ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 34.396 1.616   10.777 1.00 63.48 ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 33.505 2.440   10.560 1.00 63.71 ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? 35.513 1.482   13.021 1.00 64.72 ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 34.352 0.369   10.300 1.00 62.82 ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 33.244 -0.118  9.486  1.00 62.40 ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 32.062 -0.556  10.341 1.00 61.05 ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 32.242 -1.211  11.367 1.00 61.55 ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 33.703 -1.290  8.599  1.00 64.62 ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 33.095 -1.286  7.201  1.00 69.14 ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 33.763 -0.254  6.319  1.00 74.71 ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 34.993 -0.217  6.189  1.00 77.56 ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 32.974 0.605   5.678  1.00 74.42 ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 30.863 -0.201  9.895  1.00 59.08 ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 29.609 -0.586  10.526 1.00 57.42 ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 28.998 -1.747  9.765  1.00 55.01 ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 29.036 -1.766  8.532  1.00 54.55 ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 28.406 -2.701  10.476 1.00 53.41 ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 27.878 -3.901  9.831  1.00 52.04 ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 26.360 -4.067  9.905  1.00 49.10 ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 25.868 -5.167  9.631  1.00 49.40 ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 28.592 -5.132  10.373 1.00 54.16 ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 30.276 -5.349  9.743  1.00 62.31 ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 25.611 -3.000  10.250 1.00 45.87 ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 24.158 -3.089  10.291 1.00 43.47 ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 23.626 -3.097  8.856  1.00 40.85 ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 24.067 -2.314  8.028  1.00 41.48 ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 23.535 -1.898  11.067 1.00 44.94 ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 23.571 -2.020  12.577 1.00 49.27 ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 23.326 -3.133  13.088 1.00 50.73 ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 23.823 -0.997  13.251 1.00 50.85 ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 22.690 -3.968  8.567  1.00 38.43 ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 22.054 -4.053  7.256  1.00 36.95 ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 20.809 -3.141  7.290  1.00 33.74 ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 20.078 -3.184  8.270  1.00 33.63 ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 21.658 -5.531  6.988  1.00 39.15 ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 22.837 -6.268  6.620  1.00 41.96 ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 20.596 -5.678  5.894  1.00 38.83 ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 20.579 -2.315  6.256  1.00 30.94 ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 19.385 -1.472  6.224  1.00 29.14 ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 18.331 -2.162  5.354  1.00 27.87 ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 18.658 -2.709  4.293  1.00 27.91 ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 19.701 -0.037  5.719  1.00 29.05 ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 20.840 0.612   6.537  1.00 29.78 ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 18.442 0.850   5.700  1.00 29.07 ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 20.504 0.865   8.023  1.00 30.42 ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 17.082 -2.172  5.810  1.00 26.15 ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 15.992 -2.766  5.042  1.00 25.34 ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 15.604 -1.834  3.888  1.00 25.31 ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 15.620 -0.615  4.034  1.00 25.03 ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 14.780 -3.001  5.944  1.00 24.13 ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 15.229 -2.412  2.757  1.00 26.13 ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 14.734 -1.684  1.595  1.00 27.43 ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 13.378 -2.342  1.280  1.00 29.28 ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 13.323 -3.286  0.485  1.00 31.36 ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 15.734 -1.806  0.435  1.00 28.77 ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 17.116 -1.194  0.725  1.00 30.06 ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 17.113 0.255   1.235  1.00 30.79 ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 18.472 0.695   1.562  1.00 30.87 ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 18.773 1.819   2.205  1.00 30.49 ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 17.814 2.638   2.607  1.00 28.02 ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 20.036 2.123   2.469  1.00 30.43 ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 12.292 -1.889  1.947  1.00 29.06 ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 10.979 -2.553  1.871  1.00 29.48 ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 9.814  -1.612  2.296  1.00 30.81 ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 10.052 -0.510  2.784  1.00 30.84 ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 11.025 -3.758  2.808  1.00 29.32 ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 11.149 -3.295  4.566  1.00 30.61 ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 8.557  -2.128  2.235  1.00 31.31 ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 7.349  -1.450  2.711  1.00 31.54 ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 6.716  -2.254  3.873  1.00 30.67 ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 5.502  -2.233  4.025  1.00 31.58 ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 6.321  -1.226  1.573  1.00 34.73 ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 5.574  -2.463  1.095  1.00 44.11 ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 5.975  -3.587  1.476  1.00 46.08 ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 4.571  -2.308  0.349  1.00 48.63 ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 7.521  -2.993  4.665  1.00 28.62 ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 7.051  -3.776  5.819  1.00 25.99 ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 6.327  -2.870  6.797  1.00 23.08 ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 6.772  -1.756  7.027  1.00 23.11 ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 8.232  -4.444  6.522  1.00 25.91 ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 8.703  -6.053  5.852  1.00 25.63 ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 5.260  -3.347  7.389  1.00 21.25 ? 59  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 53  ? 4.549  -2.620  8.439  1.00 20.87 ? 59  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 53  ? 4.486  -3.426  9.754  1.00 19.49 ? 59  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 53  ? 3.599  -3.182  10.562 1.00 19.57 ? 59  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 53  ? 3.131  -2.213  7.996  1.00 22.39 ? 59  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 53  ? 3.068  -0.967  7.103  1.00 25.55 ? 59  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 53  ? 1.620  -0.581  6.835  1.00 30.36 ? 59  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 53  ? 1.135  -0.624  5.699  1.00 31.73 ? 59  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 53  ? 0.886  -0.228  7.887  1.00 29.92 ? 59  GLN   A NE2 1 
ATOM   415  N  N   . THR   A 1 54  ? 5.347  -4.459  9.917  1.00 18.53 ? 60  THR   A N   1 
ATOM   416  C  CA  . THR   A 1 54  ? 5.478  -5.284  11.137 1.00 18.04 ? 60  THR   A CA  1 
ATOM   417  C  C   . THR   A 1 54  ? 6.976  -5.452  11.408 1.00 16.59 ? 60  THR   A C   1 
ATOM   418  O  O   . THR   A 1 54  ? 7.779  -5.523  10.473 1.00 16.24 ? 60  THR   A O   1 
ATOM   419  C  CB  . THR   A 1 54  ? 4.771  -6.667  11.066 1.00 20.52 ? 60  THR   A CB  1 
ATOM   420  O  OG1 . THR   A 1 54  ? 5.508  -7.561  10.227 1.00 22.16 ? 60  THR   A OG1 1 
ATOM   421  C  CG2 . THR   A 1 54  ? 3.306  -6.589  10.620 1.00 21.02 ? 60  THR   A CG2 1 
ATOM   422  N  N   . GLY   A 1 55  ? 7.337  -5.551  12.672 1.00 15.43 ? 61  GLY   A N   1 
ATOM   423  C  CA  . GLY   A 1 55  ? 8.737  -5.643  13.057 1.00 15.74 ? 61  GLY   A CA  1 
ATOM   424  C  C   . GLY   A 1 55  ? 8.903  -5.742  14.557 1.00 15.37 ? 61  GLY   A C   1 
ATOM   425  O  O   . GLY   A 1 55  ? 7.924  -5.989  15.263 1.00 15.80 ? 61  GLY   A O   1 
ATOM   426  N  N   . VAL   A 1 56  ? 10.155 -5.622  15.038 1.00 14.30 ? 62  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 56  ? 10.535 -5.742  16.437 1.00 14.07 ? 62  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 56  ? 11.423 -4.555  16.826 1.00 13.81 ? 62  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 56  ? 12.393 -4.253  16.120 1.00 13.32 ? 62  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 56  ? 11.258 -7.088  16.699 1.00 15.46 ? 62  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 56  ? 11.693 -7.217  18.161 1.00 16.50 ? 62  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 56  ? 10.376 -8.279  16.305 1.00 16.32 ? 62  VAL   A CG2 1 
ATOM   433  N  N   . TYR   A 1 57  ? 11.124 -3.901  17.955 1.00 13.73 ? 63  TYR   A N   1 
ATOM   434  C  CA  . TYR   A 1 57  ? 11.949 -2.780  18.405 1.00 14.42 ? 63  TYR   A CA  1 
ATOM   435  C  C   . TYR   A 1 57  ? 12.529 -3.028  19.829 1.00 15.61 ? 63  TYR   A C   1 
ATOM   436  O  O   . TYR   A 1 57  ? 11.933 -3.757  20.607 1.00 15.44 ? 63  TYR   A O   1 
ATOM   437  C  CB  . TYR   A 1 57  ? 11.173 -1.432  18.353 1.00 13.86 ? 63  TYR   A CB  1 
ATOM   438  C  CG  . TYR   A 1 57  ? 10.241 -1.194  19.530 1.00 15.25 ? 63  TYR   A CG  1 
ATOM   439  C  CD1 . TYR   A 1 57  ? 8.995  -1.805  19.590 1.00 16.02 ? 63  TYR   A CD1 1 
ATOM   440  C  CD2 . TYR   A 1 57  ? 10.562 -0.280  20.527 1.00 16.98 ? 63  TYR   A CD2 1 
ATOM   441  C  CE1 . TYR   A 1 57  ? 8.109  -1.541  20.626 1.00 17.35 ? 63  TYR   A CE1 1 
ATOM   442  C  CE2 . TYR   A 1 57  ? 9.694  -0.033  21.590 1.00 18.23 ? 63  TYR   A CE2 1 
ATOM   443  C  CZ  . TYR   A 1 57  ? 8.469  -0.675  21.634 1.00 19.13 ? 63  TYR   A CZ  1 
ATOM   444  O  OH  . TYR   A 1 57  ? 7.579  -0.457  22.650 1.00 22.23 ? 63  TYR   A OH  1 
ATOM   445  N  N   . TYR   A 1 58  ? 13.663 -2.396  20.152 1.00 16.56 ? 64  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 58  ? 14.267 -2.515  21.470 1.00 18.83 ? 64  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 58  ? 13.772 -1.404  22.407 1.00 19.79 ? 64  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 58  ? 13.853 -0.225  22.069 1.00 18.39 ? 64  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 58  ? 15.803 -2.491  21.384 1.00 19.62 ? 64  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 58  ? 16.418 -2.667  22.751 1.00 21.25 ? 64  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 58  ? 16.233 -3.838  23.469 1.00 22.94 ? 64  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 58  ? 17.091 -1.622  23.373 1.00 23.10 ? 64  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 58  ? 16.770 -3.996  24.735 1.00 24.96 ? 64  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 58  ? 17.632 -1.767  24.643 1.00 24.66 ? 64  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 58  ? 17.462 -2.956  25.321 1.00 26.95 ? 64  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 58  ? 17.937 -3.105  26.595 1.00 31.06 ? 64  TYR   A OH  1 
ATOM   457  N  N   . CYS   A 1 59  ? 13.260 -1.775  23.596 1.00 21.67 ? 65  CYS   A N   1 
ATOM   458  C  CA  . CYS   A 1 59  ? 12.754 -0.786  24.552 1.00 23.55 ? 65  CYS   A CA  1 
ATOM   459  C  C   . CYS   A 1 59  ? 13.671 -0.754  25.777 1.00 25.71 ? 65  CYS   A C   1 
ATOM   460  O  O   . CYS   A 1 59  ? 13.537 -1.633  26.624 1.00 26.07 ? 65  CYS   A O   1 
ATOM   461  C  CB  . CYS   A 1 59  ? 11.315 -1.123  24.936 1.00 24.38 ? 65  CYS   A CB  1 
ATOM   462  S  SG  . CYS   A 1 59  ? 10.611 -0.052  26.226 1.00 26.85 ? 65  CYS   A SG  1 
ATOM   463  N  N   . SER   A 1 60  ? 14.632 0.214   25.856 1.00 26.74 ? 66  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 60  ? 15.577 0.234   26.969 1.00 29.02 ? 66  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 60  ? 14.932 0.435   28.326 1.00 30.83 ? 66  SER   A C   1 
ATOM   466  O  O   . SER   A 1 60  ? 15.417 -0.153  29.291 1.00 31.53 ? 66  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 60  ? 16.713 1.232   26.770 1.00 31.53 ? 66  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 60  ? 16.227 2.517   26.444 1.00 35.69 ? 66  SER   A OG  1 
ATOM   469  N  N   . SER   A 1 61  ? 13.812 1.175   28.410 1.00 31.16 ? 67  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 61  ? 13.101 1.339   29.693 1.00 32.51 ? 67  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 61  ? 12.467 0.024   30.210 1.00 32.81 ? 67  SER   A C   1 
ATOM   472  O  O   . SER   A 1 61  ? 12.096 -0.056  31.380 1.00 34.10 ? 67  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 61  ? 12.066 2.457   29.602 1.00 33.05 ? 67  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 61  ? 10.974 2.093   28.770 1.00 34.11 ? 67  SER   A OG  1 
ATOM   475  N  N   . ARG   A 1 62  ? 12.394 -1.025  29.372 1.00 31.82 ? 68  ARG   A N   1 
ATOM   476  C  CA  . ARG   A 1 62  ? 11.917 -2.337  29.823 1.00 31.49 ? 68  ARG   A CA  1 
ATOM   477  C  C   . ARG   A 1 62  ? 12.991 -3.439  29.683 1.00 32.65 ? 68  ARG   A C   1 
ATOM   478  O  O   . ARG   A 1 62  ? 12.712 -4.601  30.022 1.00 32.93 ? 68  ARG   A O   1 
ATOM   479  C  CB  . ARG   A 1 62  ? 10.683 -2.776  29.012 1.00 31.64 ? 68  ARG   A CB  1 
ATOM   480  C  CG  . ARG   A 1 62  ? 9.413  -2.018  29.358 1.00 34.13 ? 68  ARG   A CG  1 
ATOM   481  C  CD  . ARG   A 1 62  ? 8.920  -2.281  30.777 1.00 35.47 ? 68  ARG   A CD  1 
ATOM   482  N  NE  . ARG   A 1 62  ? 7.701  -1.515  31.038 1.00 39.45 ? 68  ARG   A NE  1 
ATOM   483  C  CZ  . ARG   A 1 62  ? 7.680  -0.290  31.557 1.00 42.86 ? 68  ARG   A CZ  1 
ATOM   484  N  NH1 . ARG   A 1 62  ? 8.809  0.296   31.942 1.00 43.58 ? 68  ARG   A NH1 1 
ATOM   485  N  NH2 . ARG   A 1 62  ? 6.529  0.348   31.721 1.00 43.41 ? 68  ARG   A NH2 1 
ATOM   486  N  N   . ARG   A 1 63  ? 14.185 -3.112  29.111 1.00 32.80 ? 69  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 63  ? 15.258 -4.067  28.801 1.00 33.32 ? 69  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 63  ? 14.697 -5.266  28.008 1.00 31.99 ? 69  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 63  ? 15.025 -6.438  28.281 1.00 32.33 ? 69  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 63  ? 15.979 -4.528  30.072 1.00 36.61 ? 69  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 63  ? 16.952 -3.511  30.605 1.00 42.64 ? 69  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 63  ? 17.651 -4.049  31.826 1.00 49.10 ? 69  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 63  ? 18.112 -2.955  32.670 1.00 56.44 ? 69  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 63  ? 18.456 -3.081  33.947 1.00 60.38 ? 69  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 63  ? 18.389 -4.262  34.547 1.00 60.08 ? 69  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 63  ? 18.839 -2.018  34.643 1.00 61.04 ? 69  ARG   A NH2 1 
ATOM   497  N  N   . LYS   A 1 64  ? 13.780 -4.969  27.070 1.00 29.60 ? 70  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 64  ? 13.093 -6.016  26.304 1.00 27.58 ? 70  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 64  ? 12.850 -5.560  24.852 1.00 24.03 ? 70  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 64  ? 12.731 -4.357  24.599 1.00 23.23 ? 70  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 64  ? 11.689 -6.259  26.910 1.00 30.36 ? 70  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 64  ? 11.582 -7.275  28.022 1.00 37.21 ? 70  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 64  ? 10.138 -7.800  28.078 1.00 43.94 ? 70  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 64  ? 9.860  -8.681  29.276 1.00 48.84 ? 70  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 64  ? 9.798  -7.896  30.536 1.00 51.22 ? 70  LYS   A NZ  1 
ATOM   506  N  N   . HIS   A 1 65  ? 12.677 -6.530  23.944 1.00 21.26 ? 71  HIS   A N   1 
ATOM   507  C  CA  . HIS   A 1 65  ? 12.308 -6.328  22.548 1.00 20.29 ? 71  HIS   A CA  1 
ATOM   508  C  C   . HIS   A 1 65  ? 10.795 -6.622  22.431 1.00 20.42 ? 71  HIS   A C   1 
ATOM   509  O  O   . HIS   A 1 65  ? 10.293 -7.568  23.056 1.00 21.85 ? 71  HIS   A O   1 
ATOM   510  C  CB  . HIS   A 1 65  ? 13.064 -7.304  21.635 1.00 20.17 ? 71  HIS   A CB  1 
ATOM   511  C  CG  . HIS   A 1 65  ? 14.534 -7.070  21.564 1.00 21.11 ? 71  HIS   A CG  1 
ATOM   512  N  ND1 . HIS   A 1 65  ? 15.101 -6.343  20.529 1.00 22.79 ? 71  HIS   A ND1 1 
ATOM   513  C  CD2 . HIS   A 1 65  ? 15.509 -7.463  22.405 1.00 21.71 ? 71  HIS   A CD2 1 
ATOM   514  C  CE1 . HIS   A 1 65  ? 16.396 -6.327  20.777 1.00 22.68 ? 71  HIS   A CE1 1 
ATOM   515  N  NE2 . HIS   A 1 65  ? 16.681 -6.962  21.909 1.00 23.11 ? 71  HIS   A NE2 1 
ATOM   516  N  N   . TYR   A 1 66  ? 10.078 -5.836  21.641 1.00 18.93 ? 72  TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 66  ? 8.643  -6.023  21.469 1.00 18.70 ? 72  TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 66  ? 8.251  -6.098  19.986 1.00 18.57 ? 72  TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 66  ? 8.685  -5.279  19.177 1.00 17.04 ? 72  TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 66  ? 7.869  -4.853  22.123 1.00 19.24 ? 72  TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 66  ? 7.878  -4.819  23.634 1.00 20.96 ? 72  TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 66  ? 7.108  -5.705  24.373 1.00 22.95 ? 72  TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 66  ? 8.613  -3.869  24.322 1.00 22.45 ? 72  TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 66  ? 7.097  -5.667  25.768 1.00 24.43 ? 72  TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 66  ? 8.586  -3.802  25.714 1.00 23.60 ? 72  TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 66  ? 7.831  -4.705  26.432 1.00 25.28 ? 72  TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 66  ? 7.792  -4.627  27.806 1.00 28.23 ? 72  TYR   A OH  1 
ATOM   528  N  N   . PRO   A 1 67  ? 7.381  -7.059  19.625 1.00 19.31 ? 73  PRO   A N   1 
ATOM   529  C  CA  . PRO   A 1 67  ? 6.854  -7.080  18.247 1.00 18.80 ? 73  PRO   A CA  1 
ATOM   530  C  C   . PRO   A 1 67  ? 5.756  -5.999  18.097 1.00 18.67 ? 73  PRO   A C   1 
ATOM   531  O  O   . PRO   A 1 67  ? 4.945  -5.806  19.025 1.00 18.62 ? 73  PRO   A O   1 
ATOM   532  C  CB  . PRO   A 1 67  ? 6.286  -8.490  18.110 1.00 19.76 ? 73  PRO   A CB  1 
ATOM   533  C  CG  . PRO   A 1 67  ? 5.869  -8.868  19.539 1.00 20.67 ? 73  PRO   A CG  1 
ATOM   534  C  CD  . PRO   A 1 67  ? 6.792  -8.122  20.478 1.00 19.19 ? 73  PRO   A CD  1 
ATOM   535  N  N   . VAL   A 1 68  ? 5.737  -5.282  16.953 1.00 17.57 ? 74  VAL   A N   1 
ATOM   536  C  CA  . VAL   A 1 68  ? 4.788  -4.188  16.701 1.00 18.06 ? 74  VAL   A CA  1 
ATOM   537  C  C   . VAL   A 1 68  ? 4.304  -4.137  15.254 1.00 18.15 ? 74  VAL   A C   1 
ATOM   538  O  O   . VAL   A 1 68  ? 5.017  -4.549  14.328 1.00 18.38 ? 74  VAL   A O   1 
ATOM   539  C  CB  . VAL   A 1 68  ? 5.411  -2.789  17.028 1.00 18.20 ? 74  VAL   A CB  1 
ATOM   540  C  CG1 . VAL   A 1 68  ? 5.515  -2.539  18.519 1.00 18.74 ? 74  VAL   A CG1 1 
ATOM   541  C  CG2 . VAL   A 1 68  ? 6.765  -2.622  16.350 1.00 18.81 ? 74  VAL   A CG2 1 
ATOM   542  N  N   . SER   A 1 69  ? 3.107  -3.579  15.069 1.00 17.36 ? 75  SER   A N   1 
ATOM   543  C  CA  . SER   A 1 69  ? 2.548  -3.223  13.776 1.00 18.34 ? 75  SER   A CA  1 
ATOM   544  C  C   . SER   A 1 69  ? 2.760  -1.725  13.740 1.00 18.08 ? 75  SER   A C   1 
ATOM   545  O  O   . SER   A 1 69  ? 2.519  -1.063  14.752 1.00 18.03 ? 75  SER   A O   1 
ATOM   546  C  CB  . SER   A 1 69  ? 1.050  -3.495  13.703 1.00 20.89 ? 75  SER   A CB  1 
ATOM   547  O  OG  . SER   A 1 69  ? 0.827  -4.855  13.385 1.00 26.40 ? 75  SER   A OG  1 
ATOM   548  N  N   . PHE   A 1 70  ? 3.251  -1.191  12.625 1.00 17.42 ? 76  PHE   A N   1 
ATOM   549  C  CA  . PHE   A 1 70  ? 3.484  0.249   12.554 1.00 17.95 ? 76  PHE   A CA  1 
ATOM   550  C  C   . PHE   A 1 70  ? 2.927  0.870   11.268 1.00 20.02 ? 76  PHE   A C   1 
ATOM   551  O  O   . PHE   A 1 70  ? 2.684  0.170   10.282 1.00 21.81 ? 76  PHE   A O   1 
ATOM   552  C  CB  . PHE   A 1 70  ? 4.969  0.569   12.798 1.00 16.39 ? 76  PHE   A CB  1 
ATOM   553  C  CG  . PHE   A 1 70  ? 5.962  -0.113  11.882 1.00 15.11 ? 76  PHE   A CG  1 
ATOM   554  C  CD1 . PHE   A 1 70  ? 6.492  -1.350  12.207 1.00 14.97 ? 76  PHE   A CD1 1 
ATOM   555  C  CD2 . PHE   A 1 70  ? 6.406  0.512   10.722 1.00 14.75 ? 76  PHE   A CD2 1 
ATOM   556  C  CE1 . PHE   A 1 70  ? 7.441  -1.956  11.382 1.00 14.68 ? 76  PHE   A CE1 1 
ATOM   557  C  CE2 . PHE   A 1 70  ? 7.340  -0.096  9.894  1.00 14.63 ? 76  PHE   A CE2 1 
ATOM   558  C  CZ  . PHE   A 1 70  ? 7.847  -1.331  10.227 1.00 14.55 ? 76  PHE   A CZ  1 
ATOM   559  N  N   . SER   A 1 71  ? 2.661  2.180   11.296 1.00 19.96 ? 77  SER   A N   1 
ATOM   560  C  CA  . SER   A 1 71  ? 2.075  2.872   10.159 1.00 20.97 ? 77  SER   A CA  1 
ATOM   561  C  C   . SER   A 1 71  ? 3.116  3.215   9.063  1.00 21.89 ? 77  SER   A C   1 
ATOM   562  O  O   . SER   A 1 71  ? 4.313  3.070   9.294  1.00 21.62 ? 77  SER   A O   1 
ATOM   563  C  CB  . SER   A 1 71  ? 1.381  4.142   10.647 1.00 21.79 ? 77  SER   A CB  1 
ATOM   564  O  OG  . SER   A 1 71  ? 2.354  5.091   11.060 1.00 21.72 ? 77  SER   A OG  1 
ATOM   565  N  N   . LYS   A 1 72  ? 2.660  3.636   7.877  1.00 22.92 ? 78  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 72  ? 3.565  4.052   6.791  1.00 25.61 ? 78  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 72  ? 4.207  5.430   7.126  1.00 26.38 ? 78  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 72  ? 3.577  6.236   7.808  1.00 26.66 ? 78  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 72  ? 2.788  4.150   5.455  1.00 29.40 ? 78  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 72  ? 2.036  2.872   5.120  1.00 36.25 ? 78  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 72  ? 1.718  2.775   3.631  1.00 43.97 ? 78  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 72  ? 2.657  1.853   2.885  1.00 49.25 ? 78  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 72  ? 1.895  0.885   2.037  1.00 53.27 ? 78  LYS   A NZ  1 
ATOM   574  N  N   . PRO   A 1 73  ? 5.444  5.714   6.675  1.00 26.89 ? 79  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 73  ? 6.070  7.012   7.005  1.00 27.55 ? 79  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 73  ? 5.216  8.228   6.646  1.00 28.67 ? 79  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 73  ? 4.749  8.341   5.507  1.00 28.70 ? 79  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 73  ? 7.381  6.980   6.230  1.00 28.23 ? 79  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 73  ? 7.667  5.531   6.015  1.00 28.59 ? 79  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 73  ? 6.339  4.868   5.865  1.00 26.68 ? 79  PRO   A CD  1 
ATOM   581  N  N   . SER   A 1 74  ? 4.985  9.128   7.619  1.00 29.17 ? 80  SER   A N   1 
ATOM   582  C  CA  . SER   A 1 74  ? 4.118  10.278  7.380  1.00 30.76 ? 80  SER   A CA  1 
ATOM   583  C  C   . SER   A 1 74  ? 4.466  11.524  8.230  1.00 30.95 ? 80  SER   A C   1 
ATOM   584  O  O   . SER   A 1 74  ? 5.328  11.455  9.112  1.00 30.16 ? 80  SER   A O   1 
ATOM   585  C  CB  . SER   A 1 74  ? 2.664  9.858   7.609  1.00 33.72 ? 80  SER   A CB  1 
ATOM   586  O  OG  . SER   A 1 74  ? 2.434  9.498   8.962  1.00 36.91 ? 80  SER   A OG  1 
ATOM   587  N  N   . LEU   A 1 75  ? 3.814  12.671  7.922  1.00 31.79 ? 81  LEU   A N   1 
ATOM   588  C  CA  . LEU   A 1 75  ? 3.964  13.954  8.617  1.00 33.17 ? 81  LEU   A CA  1 
ATOM   589  C  C   . LEU   A 1 75  ? 3.058  13.898  9.845  1.00 34.80 ? 81  LEU   A C   1 
ATOM   590  O  O   . LEU   A 1 75  ? 1.839  13.834  9.684  1.00 36.01 ? 81  LEU   A O   1 
ATOM   591  C  CB  . LEU   A 1 75  ? 3.458  15.110  7.714  1.00 33.41 ? 81  LEU   A CB  1 
ATOM   592  C  CG  . LEU   A 1 75  ? 4.479  15.931  6.951  1.00 34.78 ? 81  LEU   A CG  1 
ATOM   593  C  CD1 . LEU   A 1 75  ? 3.798  17.068  6.202  1.00 35.85 ? 81  LEU   A CD1 1 
ATOM   594  C  CD2 . LEU   A 1 75  ? 5.518  16.523  7.883  1.00 35.34 ? 81  LEU   A CD2 1 
ATOM   595  N  N   . ILE   A 1 76  ? 3.625  13.910  11.056 1.00 34.63 ? 82  ILE   A N   1 
ATOM   596  C  CA  . ILE   A 1 76  ? 2.819  13.829  12.266 1.00 35.56 ? 82  ILE   A CA  1 
ATOM   597  C  C   . ILE   A 1 76  ? 3.201  14.943  13.237 1.00 37.15 ? 82  ILE   A C   1 
ATOM   598  O  O   . ILE   A 1 76  ? 4.389  15.158  13.478 1.00 36.53 ? 82  ILE   A O   1 
ATOM   599  C  CB  . ILE   A 1 76  ? 2.946  12.415  12.909 1.00 35.44 ? 82  ILE   A CB  1 
ATOM   600  C  CG1 . ILE   A 1 76  ? 2.338  11.330  12.002 1.00 36.28 ? 82  ILE   A CG1 1 
ATOM   601  C  CG2 . ILE   A 1 76  ? 2.319  12.368  14.302 1.00 35.41 ? 82  ILE   A CG2 1 
ATOM   602  C  CD1 . ILE   A 1 76  ? 2.798  10.008  12.292 1.00 37.81 ? 82  ILE   A CD1 1 
ATOM   603  N  N   . PHE   A 1 77  ? 2.197  15.648  13.792 1.00 38.60 ? 83  PHE   A N   1 
ATOM   604  C  CA  . PHE   A 1 77  ? 2.422  16.725  14.755 1.00 41.20 ? 83  PHE   A CA  1 
ATOM   605  C  C   . PHE   A 1 77  ? 3.084  16.209  16.041 1.00 41.49 ? 83  PHE   A C   1 
ATOM   606  O  O   . PHE   A 1 77  ? 2.706  15.162  16.566 1.00 41.17 ? 83  PHE   A O   1 
ATOM   607  C  CB  . PHE   A 1 77  ? 1.100  17.457  15.077 1.00 43.14 ? 83  PHE   A CB  1 
ATOM   608  C  CG  . PHE   A 1 77  ? 1.232  18.603  16.049 1.00 44.85 ? 83  PHE   A CG  1 
ATOM   609  C  CD1 . PHE   A 1 77  ? 1.861  19.773  15.681 1.00 46.36 ? 83  PHE   A CD1 1 
ATOM   610  C  CD2 . PHE   A 1 77  ? 0.768  18.488  17.344 1.00 46.78 ? 83  PHE   A CD2 1 
ATOM   611  C  CE1 . PHE   A 1 77  ? 1.983  20.828  16.579 1.00 47.73 ? 83  PHE   A CE1 1 
ATOM   612  C  CE2 . PHE   A 1 77  ? 0.851  19.562  18.228 1.00 47.84 ? 83  PHE   A CE2 1 
ATOM   613  C  CZ  . PHE   A 1 77  ? 1.481  20.713  17.848 1.00 47.42 ? 83  PHE   A CZ  1 
ATOM   614  N  N   . VAL   A 1 78  ? 4.119  16.924  16.504 1.00 41.73 ? 84  VAL   A N   1 
ATOM   615  C  CA  . VAL   A 1 78  ? 4.897  16.597  17.694 1.00 42.55 ? 84  VAL   A CA  1 
ATOM   616  C  C   . VAL   A 1 78  ? 5.011  17.841  18.583 1.00 44.30 ? 84  VAL   A C   1 
ATOM   617  O  O   . VAL   A 1 78  ? 5.513  18.890  18.143 1.00 43.89 ? 84  VAL   A O   1 
ATOM   618  C  CB  . VAL   A 1 78  ? 6.298  16.023  17.345 1.00 42.44 ? 84  VAL   A CB  1 
ATOM   619  C  CG1 . VAL   A 1 78  ? 7.085  15.691  18.606 1.00 42.55 ? 84  VAL   A CG1 1 
ATOM   620  C  CG2 . VAL   A 1 78  ? 6.192  14.801  16.445 1.00 42.65 ? 84  VAL   A CG2 1 
ATOM   621  N  N   . GLU   A 1 79  ? 4.528  17.712  19.833 1.00 45.56 ? 85  GLU   A N   1 
ATOM   622  C  CA  . GLU   A 1 79  ? 4.514  18.757  20.857 1.00 47.08 ? 85  GLU   A CA  1 
ATOM   623  C  C   . GLU   A 1 79  ? 5.910  19.269  21.211 1.00 47.47 ? 85  GLU   A C   1 
ATOM   624  O  O   . GLU   A 1 79  ? 6.884  18.530  21.097 1.00 47.42 ? 85  GLU   A O   1 
ATOM   625  C  CB  . GLU   A 1 79  ? 3.796  18.247  22.117 1.00 51.33 ? 85  GLU   A CB  1 
ATOM   626  C  CG  . GLU   A 1 79  ? 2.413  18.841  22.323 1.00 59.93 ? 85  GLU   A CG  1 
ATOM   627  C  CD  . GLU   A 1 79  ? 1.599  18.154  23.403 1.00 71.44 ? 85  GLU   A CD  1 
ATOM   628  O  OE1 . GLU   A 1 79  ? 1.133  18.858  24.327 1.00 76.09 ? 85  GLU   A OE1 1 
ATOM   629  O  OE2 . GLU   A 1 79  ? 1.431  16.913  23.335 1.00 74.75 ? 85  GLU   A OE2 1 
ATOM   630  N  N   . ALA   A 1 80  ? 6.000  20.550  21.628 1.00 47.52 ? 86  ALA   A N   1 
ATOM   631  C  CA  . ALA   A 1 80  ? 7.252  21.232  21.994 1.00 48.21 ? 86  ALA   A CA  1 
ATOM   632  C  C   . ALA   A 1 80  ? 8.097  20.506  23.059 1.00 49.10 ? 86  ALA   A C   1 
ATOM   633  O  O   . ALA   A 1 80  ? 7.552  19.754  23.859 1.00 50.59 ? 86  ALA   A O   1 
ATOM   634  C  CB  . ALA   A 1 80  ? 6.943  22.647  22.464 1.00 48.03 ? 86  ALA   A CB  1 
ATOM   635  N  N   . SER   A 1 81  ? 9.410  20.763  23.095 1.00 48.39 ? 87  SER   A N   1 
ATOM   636  C  CA  . SER   A 1 81  ? 10.334 20.146  24.056 1.00 48.56 ? 87  SER   A CA  1 
ATOM   637  C  C   . SER   A 1 81  ? 11.612 21.005  24.210 1.00 48.82 ? 87  SER   A C   1 
ATOM   638  O  O   . SER   A 1 81  ? 11.761 22.009  23.503 1.00 48.67 ? 87  SER   A O   1 
ATOM   639  C  CB  . SER   A 1 81  ? 10.692 18.722  23.618 1.00 49.67 ? 87  SER   A CB  1 
ATOM   640  O  OG  . SER   A 1 81  ? 11.559 18.695  22.494 1.00 51.85 ? 87  SER   A OG  1 
ATOM   641  N  N   . GLU   A 1 82  ? 12.540 20.626  25.127 1.00 48.64 ? 88  GLU   A N   1 
ATOM   642  C  CA  . GLU   A 1 82  ? 13.788 21.397  25.269 1.00 48.76 ? 88  GLU   A CA  1 
ATOM   643  C  C   . GLU   A 1 82  ? 14.696 21.316  24.014 1.00 47.18 ? 88  GLU   A C   1 
ATOM   644  O  O   . GLU   A 1 82  ? 15.638 22.112  23.888 1.00 47.76 ? 88  GLU   A O   1 
ATOM   645  C  CB  . GLU   A 1 82  ? 14.554 21.050  26.567 1.00 52.96 ? 88  GLU   A CB  1 
ATOM   646  C  CG  . GLU   A 1 82  ? 14.708 19.563  26.874 1.00 61.17 ? 88  GLU   A CG  1 
ATOM   647  C  CD  . GLU   A 1 82  ? 15.556 19.286  28.105 1.00 69.54 ? 88  GLU   A CD  1 
ATOM   648  O  OE1 . GLU   A 1 82  ? 16.342 20.181  28.504 1.00 70.82 ? 88  GLU   A OE1 1 
ATOM   649  O  OE2 . GLU   A 1 82  ? 15.448 18.170  28.663 1.00 71.34 ? 88  GLU   A OE2 1 
ATOM   650  N  N   . TYR   A 1 83  ? 14.330 20.428  23.044 1.00 44.41 ? 89  TYR   A N   1 
ATOM   651  C  CA  . TYR   A 1 83  ? 15.009 20.157  21.785 1.00 41.79 ? 89  TYR   A CA  1 
ATOM   652  C  C   . TYR   A 1 83  ? 14.333 20.818  20.563 1.00 39.49 ? 89  TYR   A C   1 
ATOM   653  O  O   . TYR   A 1 83  ? 15.047 21.282  19.684 1.00 40.01 ? 89  TYR   A O   1 
ATOM   654  C  CB  . TYR   A 1 83  ? 15.131 18.626  21.566 1.00 41.00 ? 89  TYR   A CB  1 
ATOM   655  C  CG  . TYR   A 1 83  ? 15.656 17.888  22.776 1.00 40.87 ? 89  TYR   A CG  1 
ATOM   656  C  CD1 . TYR   A 1 83  ? 16.969 18.043  23.193 1.00 41.55 ? 89  TYR   A CD1 1 
ATOM   657  C  CD2 . TYR   A 1 83  ? 14.826 17.076  23.534 1.00 41.28 ? 89  TYR   A CD2 1 
ATOM   658  C  CE1 . TYR   A 1 83  ? 17.452 17.385  24.319 1.00 42.28 ? 89  TYR   A CE1 1 
ATOM   659  C  CE2 . TYR   A 1 83  ? 15.295 16.417  24.663 1.00 42.04 ? 89  TYR   A CE2 1 
ATOM   660  C  CZ  . TYR   A 1 83  ? 16.612 16.570  25.050 1.00 43.21 ? 89  TYR   A CZ  1 
ATOM   661  O  OH  . TYR   A 1 83  ? 17.079 15.929  26.179 1.00 45.08 ? 89  TYR   A OH  1 
ATOM   662  N  N   . TYR   A 1 84  ? 12.989 20.846  20.481 1.00 37.49 ? 90  TYR   A N   1 
ATOM   663  C  CA  . TYR   A 1 84  ? 12.311 21.440  19.312 1.00 36.74 ? 90  TYR   A CA  1 
ATOM   664  C  C   . TYR   A 1 84  ? 11.038 22.233  19.658 1.00 37.54 ? 90  TYR   A C   1 
ATOM   665  O  O   . TYR   A 1 84  ? 10.307 21.823  20.553 1.00 37.47 ? 90  TYR   A O   1 
ATOM   666  C  CB  . TYR   A 1 84  ? 11.843 20.323  18.341 1.00 35.05 ? 90  TYR   A CB  1 
ATOM   667  C  CG  . TYR   A 1 84  ? 12.909 19.421  17.775 1.00 33.11 ? 90  TYR   A CG  1 
ATOM   668  C  CD1 . TYR   A 1 84  ? 13.014 18.098  18.181 1.00 32.48 ? 90  TYR   A CD1 1 
ATOM   669  C  CD2 . TYR   A 1 84  ? 13.751 19.858  16.758 1.00 32.29 ? 90  TYR   A CD2 1 
ATOM   670  C  CE1 . TYR   A 1 84  ? 13.951 17.242  17.619 1.00 32.10 ? 90  TYR   A CE1 1 
ATOM   671  C  CE2 . TYR   A 1 84  ? 14.709 19.019  16.209 1.00 31.66 ? 90  TYR   A CE2 1 
ATOM   672  C  CZ  . TYR   A 1 84  ? 14.785 17.701  16.619 1.00 31.73 ? 90  TYR   A CZ  1 
ATOM   673  O  OH  . TYR   A 1 84  ? 15.754 16.877  16.115 1.00 30.35 ? 90  TYR   A OH  1 
ATOM   674  N  N   . PRO   A 1 85  ? 10.665 23.268  18.870 1.00 38.06 ? 91  PRO   A N   1 
ATOM   675  C  CA  . PRO   A 1 85  ? 9.339  23.899  19.084 1.00 38.88 ? 91  PRO   A CA  1 
ATOM   676  C  C   . PRO   A 1 85  ? 8.222  22.979  18.529 1.00 39.25 ? 91  PRO   A C   1 
ATOM   677  O  O   . PRO   A 1 85  ? 8.525  21.967  17.890 1.00 38.90 ? 91  PRO   A O   1 
ATOM   678  C  CB  . PRO   A 1 85  ? 9.442  25.211  18.296 1.00 39.61 ? 91  PRO   A CB  1 
ATOM   679  C  CG  . PRO   A 1 85  ? 10.415 24.895  17.191 1.00 39.44 ? 91  PRO   A CG  1 
ATOM   680  C  CD  . PRO   A 1 85  ? 11.379 23.861  17.719 1.00 37.52 ? 91  PRO   A CD  1 
ATOM   681  N  N   . ALA   A 1 86  ? 6.934  23.309  18.767 1.00 39.31 ? 92  ALA   A N   1 
ATOM   682  C  CA  . ALA   A 1 86  ? 5.829  22.456  18.274 1.00 38.59 ? 92  ALA   A CA  1 
ATOM   683  C  C   . ALA   A 1 86  ? 5.859  22.429  16.731 1.00 36.69 ? 92  ALA   A C   1 
ATOM   684  O  O   . ALA   A 1 86  ? 6.019  23.484  16.125 1.00 36.01 ? 92  ALA   A O   1 
ATOM   685  C  CB  . ALA   A 1 86  ? 4.492  22.988  18.779 1.00 38.82 ? 92  ALA   A CB  1 
ATOM   686  N  N   . ARG   A 1 87  ? 5.842  21.221  16.098 1.00 34.69 ? 93  ARG   A N   1 
ATOM   687  C  CA  . ARG   A 1 87  ? 5.987  21.154  14.627 1.00 32.89 ? 93  ARG   A CA  1 
ATOM   688  C  C   . ARG   A 1 87  ? 5.490  19.816  14.034 1.00 31.44 ? 93  ARG   A C   1 
ATOM   689  O  O   . ARG   A 1 87  ? 5.200  18.901  14.786 1.00 31.45 ? 93  ARG   A O   1 
ATOM   690  C  CB  . ARG   A 1 87  ? 7.489  21.365  14.261 1.00 32.07 ? 93  ARG   A CB  1 
ATOM   691  C  CG  . ARG   A 1 87  ? 8.341  20.063  14.354 1.00 31.27 ? 93  ARG   A CG  1 
ATOM   692  C  CD  . ARG   A 1 87  ? 9.668  20.175  15.061 1.00 30.04 ? 93  ARG   A CD  1 
ATOM   693  N  NE  . ARG   A 1 87  ? 10.582 19.103  14.638 1.00 29.14 ? 93  ARG   A NE  1 
ATOM   694  C  CZ  . ARG   A 1 87  ? 10.674 17.916  15.232 1.00 25.64 ? 93  ARG   A CZ  1 
ATOM   695  N  NH1 . ARG   A 1 87  ? 11.532 17.008  14.784 1.00 21.92 ? 93  ARG   A NH1 1 
ATOM   696  N  NH2 . ARG   A 1 87  ? 9.917  17.632  16.284 1.00 23.72 ? 93  ARG   A NH2 1 
ATOM   697  N  N   . TYR   A 1 88  ? 5.449  19.683  12.689 1.00 30.48 ? 94  TYR   A N   1 
ATOM   698  C  CA  . TYR   A 1 88  ? 5.163  18.382  12.072 1.00 30.07 ? 94  TYR   A CA  1 
ATOM   699  C  C   . TYR   A 1 88  ? 6.522  17.697  11.825 1.00 26.37 ? 94  TYR   A C   1 
ATOM   700  O  O   . TYR   A 1 88  ? 7.438  18.334  11.310 1.00 25.27 ? 94  TYR   A O   1 
ATOM   701  C  CB  . TYR   A 1 88  ? 4.449  18.526  10.728 1.00 32.08 ? 94  TYR   A CB  1 
ATOM   702  C  CG  . TYR   A 1 88  ? 3.007  18.951  10.856 1.00 35.71 ? 94  TYR   A CG  1 
ATOM   703  C  CD1 . TYR   A 1 88  ? 1.991  18.013  10.957 1.00 38.24 ? 94  TYR   A CD1 1 
ATOM   704  C  CD2 . TYR   A 1 88  ? 2.661  20.292  10.899 1.00 37.90 ? 94  TYR   A CD2 1 
ATOM   705  C  CE1 . TYR   A 1 88  ? 0.660  18.401  11.079 1.00 40.04 ? 94  TYR   A CE1 1 
ATOM   706  C  CE2 . TYR   A 1 88  ? 1.341  20.692  11.037 1.00 40.04 ? 94  TYR   A CE2 1 
ATOM   707  C  CZ  . TYR   A 1 88  ? 0.343  19.744  11.138 1.00 41.99 ? 94  TYR   A CZ  1 
ATOM   708  O  OH  . TYR   A 1 88  ? -0.963 20.164  11.245 1.00 46.12 ? 94  TYR   A OH  1 
ATOM   709  N  N   . GLN   A 1 89  ? 6.647  16.417  12.187 1.00 23.61 ? 95  GLN   A N   1 
ATOM   710  C  CA  . GLN   A 1 89  ? 7.874  15.639  11.952 1.00 21.49 ? 95  GLN   A CA  1 
ATOM   711  C  C   . GLN   A 1 89  ? 7.587  14.713  10.777 1.00 20.58 ? 95  GLN   A C   1 
ATOM   712  O  O   . GLN   A 1 89  ? 6.544  14.063  10.755 1.00 21.41 ? 95  GLN   A O   1 
ATOM   713  C  CB  . GLN   A 1 89  ? 8.310  14.839  13.204 1.00 21.55 ? 95  GLN   A CB  1 
ATOM   714  C  CG  . GLN   A 1 89  ? 9.599  13.998  12.977 1.00 21.49 ? 95  GLN   A CG  1 
ATOM   715  C  CD  . GLN   A 1 89  ? 10.232 13.488  14.247 1.00 21.64 ? 95  GLN   A CD  1 
ATOM   716  O  OE1 . GLN   A 1 89  ? 10.409 14.224  15.216 1.00 23.85 ? 95  GLN   A OE1 1 
ATOM   717  N  NE2 . GLN   A 1 89  ? 10.616 12.210  14.273 1.00 18.17 ? 95  GLN   A NE2 1 
ATOM   718  N  N   . SER   A 1 90  ? 8.430  14.730  9.747  1.00 18.77 ? 96  SER   A N   1 
ATOM   719  C  CA  . SER   A 1 90  ? 8.211  13.916  8.554  1.00 18.05 ? 96  SER   A CA  1 
ATOM   720  C  C   . SER   A 1 90  ? 8.891  12.550  8.649  1.00 18.44 ? 96  SER   A C   1 
ATOM   721  O  O   . SER   A 1 90  ? 9.753  12.335  9.531  1.00 18.50 ? 96  SER   A O   1 
ATOM   722  C  CB  . SER   A 1 90  ? 8.671  14.668  7.309  1.00 18.87 ? 96  SER   A CB  1 
ATOM   723  O  OG  . SER   A 1 90  ? 10.050 14.986  7.410  1.00 20.60 ? 96  SER   A OG  1 
ATOM   724  N  N   . HIS   A 1 91  ? 8.450  11.605  7.782  1.00 17.55 ? 97  HIS   A N   1 
ATOM   725  C  CA  . HIS   A 1 91  ? 9.010  10.262  7.707  1.00 17.27 ? 97  HIS   A CA  1 
ATOM   726  C  C   . HIS   A 1 91  ? 8.870  9.521   9.056  1.00 17.11 ? 97  HIS   A C   1 
ATOM   727  O  O   . HIS   A 1 91  ? 9.744  8.750   9.424  1.00 16.95 ? 97  HIS   A O   1 
ATOM   728  C  CB  . HIS   A 1 91  ? 10.486 10.355  7.252  1.00 17.08 ? 97  HIS   A CB  1 
ATOM   729  C  CG  . HIS   A 1 91  ? 10.632 10.970  5.889  1.00 19.33 ? 97  HIS   A CG  1 
ATOM   730  N  ND1 . HIS   A 1 91  ? 10.693 10.184  4.742  1.00 21.48 ? 97  HIS   A ND1 1 
ATOM   731  C  CD2 . HIS   A 1 91  ? 10.649 12.274  5.519  1.00 20.10 ? 97  HIS   A CD2 1 
ATOM   732  C  CE1 . HIS   A 1 91  ? 10.783 11.034  3.725  1.00 21.68 ? 97  HIS   A CE1 1 
ATOM   733  N  NE2 . HIS   A 1 91  ? 10.749 12.298  4.140  1.00 20.83 ? 97  HIS   A NE2 1 
ATOM   734  N  N   . LEU   A 1 92  ? 7.767  9.771   9.781  1.00 17.40 ? 98  LEU   A N   1 
ATOM   735  C  CA  . LEU   A 1 92  ? 7.496  9.212   11.118 1.00 17.71 ? 98  LEU   A CA  1 
ATOM   736  C  C   . LEU   A 1 92  ? 6.459  8.086   11.061 1.00 17.06 ? 98  LEU   A C   1 
ATOM   737  O  O   . LEU   A 1 92  ? 5.443  8.216   10.375 1.00 16.96 ? 98  LEU   A O   1 
ATOM   738  C  CB  . LEU   A 1 92  ? 7.003  10.352  12.054 1.00 17.75 ? 98  LEU   A CB  1 
ATOM   739  C  CG  . LEU   A 1 92  ? 6.850  10.009  13.557 1.00 19.23 ? 98  LEU   A CG  1 
ATOM   740  C  CD1 . LEU   A 1 92  ? 8.169  9.550   14.146 1.00 19.11 ? 98  LEU   A CD1 1 
ATOM   741  C  CD2 . LEU   A 1 92  ? 6.304  11.228  14.360 1.00 20.33 ? 98  LEU   A CD2 1 
ATOM   742  N  N   . MET   A 1 93  ? 6.708  6.985   11.790 1.00 16.82 ? 99  MET   A N   1 
ATOM   743  C  CA  . MET   A 1 93  ? 5.820  5.817   11.830 1.00 16.99 ? 99  MET   A CA  1 
ATOM   744  C  C   . MET   A 1 93  ? 5.377  5.534   13.252 1.00 18.80 ? 99  MET   A C   1 
ATOM   745  O  O   . MET   A 1 93  ? 6.232  5.386   14.124 1.00 19.70 ? 99  MET   A O   1 
ATOM   746  C  CB  . MET   A 1 93  ? 6.560  4.589   11.281 1.00 16.43 ? 99  MET   A CB  1 
ATOM   747  C  CG  . MET   A 1 93  ? 7.062  4.801   9.862  1.00 17.85 ? 99  MET   A CG  1 
ATOM   748  S  SD  . MET   A 1 93  ? 8.155  3.488   9.282  1.00 19.31 ? 99  MET   A SD  1 
ATOM   749  C  CE  . MET   A 1 93  ? 9.478  3.622   10.407 1.00 16.57 ? 99  MET   A CE  1 
ATOM   750  N  N   . LEU   A 1 94  ? 4.059  5.397   13.495 1.00 18.91 ? 100 LEU   A N   1 
ATOM   751  C  CA  . LEU   A 1 94  ? 3.578  5.122   14.847 1.00 19.91 ? 100 LEU   A CA  1 
ATOM   752  C  C   . LEU   A 1 94  ? 3.181  3.663   15.058 1.00 20.14 ? 100 LEU   A C   1 
ATOM   753  O  O   . LEU   A 1 94  ? 2.722  3.000   14.126 1.00 19.53 ? 100 LEU   A O   1 
ATOM   754  C  CB  . LEU   A 1 94  ? 2.380  6.043   15.194 1.00 20.86 ? 100 LEU   A CB  1 
ATOM   755  C  CG  . LEU   A 1 94  ? 2.673  7.555   15.228 1.00 23.37 ? 100 LEU   A CG  1 
ATOM   756  C  CD1 . LEU   A 1 94  ? 1.448  8.352   15.661 1.00 24.59 ? 100 LEU   A CD1 1 
ATOM   757  C  CD2 . LEU   A 1 94  ? 3.786  7.871   16.193 1.00 24.45 ? 100 LEU   A CD2 1 
ATOM   758  N  N   . ALA   A 1 95  ? 3.285  3.202   16.314 1.00 20.61 ? 101 ALA   A N   1 
ATOM   759  C  CA  . ALA   A 1 95  ? 2.914  1.858   16.754 1.00 21.91 ? 101 ALA   A CA  1 
ATOM   760  C  C   . ALA   A 1 95  ? 2.357  1.915   18.171 1.00 23.38 ? 101 ALA   A C   1 
ATOM   761  O  O   . ALA   A 1 95  ? 2.716  2.796   18.954 1.00 22.88 ? 101 ALA   A O   1 
ATOM   762  C  CB  . ALA   A 1 95  ? 4.140  0.952   16.751 1.00 21.60 ? 101 ALA   A CB  1 
ATOM   763  N  N   . VAL   A 1 96  ? 1.504  0.955   18.511 1.00 24.56 ? 102 VAL   A N   1 
ATOM   764  C  CA  . VAL   A 1 96  ? 0.971  0.834   19.857 1.00 26.55 ? 102 VAL   A CA  1 
ATOM   765  C  C   . VAL   A 1 96  ? 2.031  0.019   20.610 1.00 27.96 ? 102 VAL   A C   1 
ATOM   766  O  O   . VAL   A 1 96  ? 2.408  -1.073  20.192 1.00 28.35 ? 102 VAL   A O   1 
ATOM   767  C  CB  . VAL   A 1 96  ? -0.433 0.160   19.883 1.00 28.06 ? 102 VAL   A CB  1 
ATOM   768  C  CG1 . VAL   A 1 96  ? -0.899 -0.108  21.317 1.00 28.75 ? 102 VAL   A CG1 1 
ATOM   769  C  CG2 . VAL   A 1 96  ? -1.469 1.018   19.138 1.00 28.48 ? 102 VAL   A CG2 1 
ATOM   770  N  N   . GLY   A 1 97  ? 2.598  0.631   21.624 1.00 28.46 ? 103 GLY   A N   1 
ATOM   771  C  CA  . GLY   A 1 97  ? 3.656  0.032   22.412 1.00 29.33 ? 103 GLY   A CA  1 
ATOM   772  C  C   . GLY   A 1 97  ? 4.180  0.996   23.455 1.00 29.97 ? 103 GLY   A C   1 
ATOM   773  O  O   . GLY   A 1 97  ? 3.928  2.206   23.391 1.00 30.76 ? 103 GLY   A O   1 
ATOM   774  N  N   . HIS   A 1 98  ? 4.928  0.470   24.416 1.00 29.50 ? 104 HIS   A N   1 
ATOM   775  C  CA  . HIS   A 1 98  ? 5.524  1.281   25.451 1.00 29.48 ? 104 HIS   A CA  1 
ATOM   776  C  C   . HIS   A 1 98  ? 6.805  2.019   24.986 1.00 29.53 ? 104 HIS   A C   1 
ATOM   777  O  O   . HIS   A 1 98  ? 7.656  1.459   24.291 1.00 28.36 ? 104 HIS   A O   1 
ATOM   778  C  CB  . HIS   A 1 98  ? 5.809  0.434   26.699 1.00 30.25 ? 104 HIS   A CB  1 
ATOM   779  C  CG  . HIS   A 1 98  ? 6.534  1.190   27.763 1.00 32.64 ? 104 HIS   A CG  1 
ATOM   780  N  ND1 . HIS   A 1 98  ? 5.904  2.153   28.509 1.00 35.42 ? 104 HIS   A ND1 1 
ATOM   781  C  CD2 . HIS   A 1 98  ? 7.840  1.153   28.106 1.00 34.12 ? 104 HIS   A CD2 1 
ATOM   782  C  CE1 . HIS   A 1 98  ? 6.839  2.668   29.293 1.00 35.89 ? 104 HIS   A CE1 1 
ATOM   783  N  NE2 . HIS   A 1 98  ? 8.018  2.082   29.090 1.00 35.49 ? 104 HIS   A NE2 1 
ATOM   784  N  N   . SER   A 1 99  ? 6.950  3.264   25.469 1.00 30.22 ? 105 SER   A N   1 
ATOM   785  C  CA  . SER   A 1 99  ? 8.113  4.113   25.296 1.00 32.02 ? 105 SER   A CA  1 
ATOM   786  C  C   . SER   A 1 99  ? 8.035  5.288   26.289 1.00 34.00 ? 105 SER   A C   1 
ATOM   787  O  O   . SER   A 1 99  ? 6.945  5.692   26.688 1.00 33.79 ? 105 SER   A O   1 
ATOM   788  C  CB  . SER   A 1 99  ? 8.244  4.610   23.861 1.00 33.01 ? 105 SER   A CB  1 
ATOM   789  O  OG  . SER   A 1 99  ? 7.227  5.529   23.505 1.00 35.68 ? 105 SER   A OG  1 
ATOM   790  N  N   . GLU   A 1 100 ? 9.187  5.776   26.735 1.00 35.34 ? 106 GLU   A N   1 
ATOM   791  C  CA  . GLU   A 1 100 ? 9.273  6.917   27.642 1.00 37.57 ? 106 GLU   A CA  1 
ATOM   792  C  C   . GLU   A 1 100 ? 10.613 7.653   27.436 1.00 39.21 ? 106 GLU   A C   1 
ATOM   793  O  O   . GLU   A 1 100 ? 11.525 7.054   26.862 1.00 39.27 ? 106 GLU   A O   1 
ATOM   794  C  CB  . GLU   A 1 100 ? 9.076  6.483   29.103 1.00 39.98 ? 106 GLU   A CB  1 
ATOM   795  C  CG  . GLU   A 1 100 ? 9.960  5.327   29.521 1.00 45.47 ? 106 GLU   A CG  1 
ATOM   796  C  CD  . GLU   A 1 100 ? 9.647  4.829   30.921 1.00 49.14 ? 106 GLU   A CD  1 
ATOM   797  O  OE1 . GLU   A 1 100 ? 10.095 5.473   31.894 1.00 50.73 ? 106 GLU   A OE1 1 
ATOM   798  O  OE2 . GLU   A 1 100 ? 8.934  3.812   31.046 1.00 48.46 ? 106 GLU   A OE2 1 
ATOM   799  N  N   . PRO   A 1 101 ? 10.809 8.917   27.922 1.00 40.10 ? 107 PRO   A N   1 
ATOM   800  C  CA  . PRO   A 1 101 ? 12.116 9.587   27.726 1.00 40.49 ? 107 PRO   A CA  1 
ATOM   801  C  C   . PRO   A 1 101 ? 13.269 8.686   28.156 1.00 39.52 ? 107 PRO   A C   1 
ATOM   802  O  O   . PRO   A 1 101 ? 13.158 8.022   29.179 1.00 40.61 ? 107 PRO   A O   1 
ATOM   803  C  CB  . PRO   A 1 101 ? 12.002 10.856  28.583 1.00 41.93 ? 107 PRO   A CB  1 
ATOM   804  C  CG  . PRO   A 1 101 ? 10.544 11.166  28.610 1.00 42.30 ? 107 PRO   A CG  1 
ATOM   805  C  CD  . PRO   A 1 101 ? 9.852  9.801   28.613 1.00 40.25 ? 107 PRO   A CD  1 
ATOM   806  N  N   . GLY   A 1 102 ? 14.261 8.533   27.292 1.00 37.14 ? 108 GLY   A N   1 
ATOM   807  C  CA  . GLY   A 1 102 ? 15.348 7.580   27.513 1.00 35.18 ? 108 GLY   A CA  1 
ATOM   808  C  C   . GLY   A 1 102 ? 15.354 6.455   26.483 1.00 32.83 ? 108 GLY   A C   1 
ATOM   809  O  O   . GLY   A 1 102 ? 16.383 5.809   26.262 1.00 33.08 ? 108 GLY   A O   1 
ATOM   810  N  N   . ASP   A 1 103 ? 14.202 6.227   25.814 1.00 30.03 ? 109 ASP   A N   1 
ATOM   811  C  CA  . ASP   A 1 103 ? 14.041 5.195   24.812 1.00 26.99 ? 109 ASP   A CA  1 
ATOM   812  C  C   . ASP   A 1 103 ? 14.425 5.580   23.384 1.00 24.57 ? 109 ASP   A C   1 
ATOM   813  O  O   . ASP   A 1 103 ? 14.530 4.676   22.555 1.00 23.72 ? 109 ASP   A O   1 
ATOM   814  C  CB  . ASP   A 1 103 ? 12.614 4.632   24.826 1.00 27.10 ? 109 ASP   A CB  1 
ATOM   815  C  CG  . ASP   A 1 103 ? 12.413 3.663   25.973 1.00 28.16 ? 109 ASP   A CG  1 
ATOM   816  O  OD1 . ASP   A 1 103 ? 13.370 2.963   26.322 1.00 26.99 ? 109 ASP   A OD1 1 
ATOM   817  O  OD2 . ASP   A 1 103 ? 11.306 3.629   26.534 1.00 29.71 ? 109 ASP   A OD2 1 
ATOM   818  N  N   . CYS   A 1 104 ? 14.633 6.877   23.068 1.00 22.94 ? 110 CYS   A N   1 
ATOM   819  C  CA  . CYS   A 1 104 ? 15.036 7.261   21.688 1.00 22.52 ? 110 CYS   A CA  1 
ATOM   820  C  C   . CYS   A 1 104 ? 16.347 6.577   21.294 1.00 21.40 ? 110 CYS   A C   1 
ATOM   821  O  O   . CYS   A 1 104 ? 17.205 6.442   22.148 1.00 21.56 ? 110 CYS   A O   1 
ATOM   822  C  CB  . CYS   A 1 104 ? 15.144 8.779   21.547 1.00 23.05 ? 110 CYS   A CB  1 
ATOM   823  S  SG  . CYS   A 1 104 ? 13.550 9.632   21.594 1.00 28.07 ? 110 CYS   A SG  1 
ATOM   824  N  N   . GLY   A 1 105 ? 16.495 6.140   20.050 1.00 20.55 ? 111 GLY   A N   1 
ATOM   825  C  CA  . GLY   A 1 105 ? 17.725 5.452   19.642 1.00 20.64 ? 111 GLY   A CA  1 
ATOM   826  C  C   . GLY   A 1 105 ? 17.593 3.938   19.591 1.00 20.67 ? 111 GLY   A C   1 
ATOM   827  O  O   . GLY   A 1 105 ? 18.388 3.264   18.929 1.00 21.70 ? 111 GLY   A O   1 
ATOM   828  N  N   . GLY   A 1 106 ? 16.555 3.390   20.221 1.00 19.17 ? 112 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 106 ? 16.266 1.957   20.135 1.00 17.63 ? 112 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 106 ? 15.935 1.587   18.696 1.00 16.39 ? 112 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 106 ? 15.208 2.311   18.021 1.00 15.14 ? 112 GLY   A O   1 
ATOM   832  N  N   . ILE   A 1 107 ? 16.541 0.512   18.188 1.00 15.59 ? 113 ILE   A N   1 
ATOM   833  C  CA  . ILE   A 1 107 ? 16.377 0.118   16.804 1.00 16.20 ? 113 ILE   A CA  1 
ATOM   834  C  C   . ILE   A 1 107 ? 15.087 -0.661  16.558 1.00 15.53 ? 113 ILE   A C   1 
ATOM   835  O  O   . ILE   A 1 107 ? 14.710 -1.521  17.372 1.00 16.52 ? 113 ILE   A O   1 
ATOM   836  C  CB  . ILE   A 1 107 ? 17.660 -0.669  16.349 1.00 18.28 ? 113 ILE   A CB  1 
ATOM   837  C  CG1 . ILE   A 1 107 ? 18.874 0.283   16.176 1.00 19.64 ? 113 ILE   A CG1 1 
ATOM   838  C  CG2 . ILE   A 1 107 ? 17.423 -1.474  15.066 1.00 19.24 ? 113 ILE   A CG2 1 
ATOM   839  C  CD1 . ILE   A 1 107 ? 20.231 -0.483  16.034 1.00 21.49 ? 113 ILE   A CD1 1 
ATOM   840  N  N   . LEU   A 1 108 ? 14.440 -0.387  15.420 1.00 14.15 ? 114 LEU   A N   1 
ATOM   841  C  CA  . LEU   A 1 108 ? 13.294 -1.125  14.889 1.00 14.53 ? 114 LEU   A CA  1 
ATOM   842  C  C   . LEU   A 1 108 ? 13.808 -1.969  13.674 1.00 15.65 ? 114 LEU   A C   1 
ATOM   843  O  O   . LEU   A 1 108 ? 14.496 -1.439  12.802 1.00 15.43 ? 114 LEU   A O   1 
ATOM   844  C  CB  . LEU   A 1 108 ? 12.191 -0.166  14.423 1.00 13.90 ? 114 LEU   A CB  1 
ATOM   845  C  CG  . LEU   A 1 108 ? 10.992 -0.786  13.634 1.00 14.29 ? 114 LEU   A CG  1 
ATOM   846  C  CD1 . LEU   A 1 108 ? 10.174 -1.715  14.516 1.00 14.33 ? 114 LEU   A CD1 1 
ATOM   847  C  CD2 . LEU   A 1 108 ? 10.049 0.327   13.107 1.00 15.12 ? 114 LEU   A CD2 1 
ATOM   848  N  N   . ARG   A 1 109 ? 13.537 -3.285  13.659 1.00 16.50 ? 115 ARG   A N   1 
ATOM   849  C  CA  . ARG   A 1 109 ? 13.977 -4.178  12.589 1.00 17.81 ? 115 ARG   A CA  1 
ATOM   850  C  C   . ARG   A 1 109 ? 12.818 -5.055  12.090 1.00 18.87 ? 115 ARG   A C   1 
ATOM   851  O  O   . ARG   A 1 109 ? 11.998 -5.473  12.887 1.00 18.31 ? 115 ARG   A O   1 
ATOM   852  C  CB  . ARG   A 1 109 ? 15.039 -5.160  13.113 1.00 19.79 ? 115 ARG   A CB  1 
ATOM   853  C  CG  . ARG   A 1 109 ? 16.366 -4.560  13.506 1.00 25.97 ? 115 ARG   A CG  1 
ATOM   854  C  CD  . ARG   A 1 109 ? 17.308 -5.633  14.042 1.00 31.37 ? 115 ARG   A CD  1 
ATOM   855  N  NE  . ARG   A 1 109 ? 17.615 -6.611  12.998 1.00 36.37 ? 115 ARG   A NE  1 
ATOM   856  C  CZ  . ARG   A 1 109 ? 18.601 -6.483  12.114 1.00 39.79 ? 115 ARG   A CZ  1 
ATOM   857  N  NH1 . ARG   A 1 109 ? 18.783 -7.402  11.179 1.00 41.46 ? 115 ARG   A NH1 1 
ATOM   858  N  NH2 . ARG   A 1 109 ? 19.432 -5.454  12.181 1.00 39.63 ? 115 ARG   A NH2 1 
ATOM   859  N  N   . CYS   A 1 110 ? 12.824 -5.406  10.792 1.00 19.42 ? 116 CYS   A N   1 
ATOM   860  C  CA  . CYS   A 1 110 ? 11.899 -6.356  10.181 1.00 20.34 ? 116 CYS   A CA  1 
ATOM   861  C  C   . CYS   A 1 110 ? 12.802 -7.528  9.696  1.00 22.39 ? 116 CYS   A C   1 
ATOM   862  O  O   . CYS   A 1 110 ? 13.998 -7.529  9.994  1.00 22.13 ? 116 CYS   A O   1 
ATOM   863  C  CB  . CYS   A 1 110 ? 11.168 -5.693  9.011  1.00 20.18 ? 116 CYS   A CB  1 
ATOM   864  S  SG  . CYS   A 1 110 ? 12.272 -5.143  7.683  1.00 21.76 ? 116 CYS   A SG  1 
ATOM   865  N  N   . GLN   A 1 111 ? 12.259 -8.528  8.962  1.00 24.36 ? 117 GLN   A N   1 
ATOM   866  C  CA  . GLN   A 1 111 ? 13.085 -9.623  8.435  1.00 26.47 ? 117 GLN   A CA  1 
ATOM   867  C  C   . GLN   A 1 111 ? 14.169 -9.121  7.441  1.00 27.79 ? 117 GLN   A C   1 
ATOM   868  O  O   . GLN   A 1 111 ? 15.124 -9.854  7.160  1.00 28.58 ? 117 GLN   A O   1 
ATOM   869  C  CB  . GLN   A 1 111 ? 12.191 -10.630 7.697  1.00 29.34 ? 117 GLN   A CB  1 
ATOM   870  C  CG  . GLN   A 1 111 ? 11.500 -10.017 6.481  1.00 33.68 ? 117 GLN   A CG  1 
ATOM   871  C  CD  . GLN   A 1 111 ? 10.459 -10.921 5.892  1.00 40.27 ? 117 GLN   A CD  1 
ATOM   872  O  OE1 . GLN   A 1 111 ? 9.260  -10.606 5.906  1.00 42.75 ? 117 GLN   A OE1 1 
ATOM   873  N  NE2 . GLN   A 1 111 ? 10.904 -12.054 5.344  1.00 39.90 ? 117 GLN   A NE2 1 
ATOM   874  N  N   . HIS   A 1 112 ? 14.007 -7.900  6.879  1.00 27.46 ? 118 HIS   A N   1 
ATOM   875  C  CA  . HIS   A 1 112 ? 14.952 -7.367  5.885  1.00 27.39 ? 118 HIS   A CA  1 
ATOM   876  C  C   . HIS   A 1 112 ? 16.109 -6.562  6.473  1.00 25.77 ? 118 HIS   A C   1 
ATOM   877  O  O   . HIS   A 1 112 ? 17.051 -6.242  5.737  1.00 26.61 ? 118 HIS   A O   1 
ATOM   878  C  CB  . HIS   A 1 112 ? 14.231 -6.538  4.798  1.00 29.49 ? 118 HIS   A CB  1 
ATOM   879  C  CG  . HIS   A 1 112 ? 13.115 -7.264  4.099  1.00 34.53 ? 118 HIS   A CG  1 
ATOM   880  N  ND1 . HIS   A 1 112 ? 11.805 -6.822  4.185  1.00 37.07 ? 118 HIS   A ND1 1 
ATOM   881  C  CD2 . HIS   A 1 112 ? 13.141 -8.405  3.365  1.00 36.81 ? 118 HIS   A CD2 1 
ATOM   882  C  CE1 . HIS   A 1 112 ? 11.084 -7.678  3.478  1.00 38.25 ? 118 HIS   A CE1 1 
ATOM   883  N  NE2 . HIS   A 1 112 ? 11.839 -8.663  2.982  1.00 38.33 ? 118 HIS   A NE2 1 
ATOM   884  N  N   . GLY   A 1 113 ? 16.023 -6.201  7.756  1.00 23.02 ? 119 GLY   A N   1 
ATOM   885  C  CA  . GLY   A 1 113 ? 17.062 -5.424  8.405  1.00 21.23 ? 119 GLY   A CA  1 
ATOM   886  C  C   . GLY   A 1 113 ? 16.565 -4.230  9.203  1.00 18.61 ? 119 GLY   A C   1 
ATOM   887  O  O   . GLY   A 1 113 ? 15.425 -4.230  9.673  1.00 18.11 ? 119 GLY   A O   1 
ATOM   888  N  N   . VAL   A 1 114 ? 17.430 -3.195  9.360  1.00 17.18 ? 120 VAL   A N   1 
ATOM   889  C  CA  . VAL   A 1 114 ? 17.130 -1.990  10.114 1.00 16.90 ? 120 VAL   A CA  1 
ATOM   890  C  C   . VAL   A 1 114 ? 16.118 -1.120  9.383  1.00 16.20 ? 120 VAL   A C   1 
ATOM   891  O  O   . VAL   A 1 114 ? 16.317 -0.789  8.216  1.00 16.69 ? 120 VAL   A O   1 
ATOM   892  C  CB  . VAL   A 1 114 ? 18.409 -1.196  10.509 1.00 18.48 ? 120 VAL   A CB  1 
ATOM   893  C  CG1 . VAL   A 1 114 ? 18.048 0.147   11.144 1.00 19.10 ? 120 VAL   A CG1 1 
ATOM   894  C  CG2 . VAL   A 1 114 ? 19.291 -2.010  11.462 1.00 19.08 ? 120 VAL   A CG2 1 
ATOM   895  N  N   . VAL   A 1 115 ? 14.999 -0.814  10.049 1.00 14.61 ? 121 VAL   A N   1 
ATOM   896  C  CA  . VAL   A 1 115 ? 13.923 -0.004  9.497  1.00 14.44 ? 121 VAL   A CA  1 
ATOM   897  C  C   . VAL   A 1 115 ? 14.035 1.474   9.981  1.00 14.16 ? 121 VAL   A C   1 
ATOM   898  O  O   . VAL   A 1 115 ? 13.807 2.423   9.217  1.00 14.26 ? 121 VAL   A O   1 
ATOM   899  C  CB  . VAL   A 1 115 ? 12.550 -0.633  9.897  1.00 14.95 ? 121 VAL   A CB  1 
ATOM   900  C  CG1 . VAL   A 1 115 ? 11.379 0.273   9.519  1.00 15.76 ? 121 VAL   A CG1 1 
ATOM   901  C  CG2 . VAL   A 1 115 ? 12.384 -2.024  9.282  1.00 14.99 ? 121 VAL   A CG2 1 
ATOM   902  N  N   . GLY   A 1 116 ? 14.318 1.646   11.268 1.00 13.86 ? 122 GLY   A N   1 
ATOM   903  C  CA  . GLY   A 1 116 ? 14.402 2.971   11.849 1.00 14.03 ? 122 GLY   A CA  1 
ATOM   904  C  C   . GLY   A 1 116 ? 14.755 2.960   13.314 1.00 14.44 ? 122 GLY   A C   1 
ATOM   905  O  O   . GLY   A 1 116 ? 15.187 1.933   13.847 1.00 13.78 ? 122 GLY   A O   1 
ATOM   906  N  N   . ILE   A 1 117 ? 14.675 4.140   13.946 1.00 14.26 ? 123 ILE   A N   1 
ATOM   907  C  CA  . ILE   A 1 117 ? 15.010 4.275   15.365 1.00 14.46 ? 123 ILE   A CA  1 
ATOM   908  C  C   . ILE   A 1 117 ? 13.894 5.005   16.127 1.00 14.36 ? 123 ILE   A C   1 
ATOM   909  O  O   . ILE   A 1 117 ? 13.301 5.940   15.582 1.00 13.58 ? 123 ILE   A O   1 
ATOM   910  C  CB  . ILE   A 1 117 ? 16.375 5.002   15.556 1.00 15.56 ? 123 ILE   A CB  1 
ATOM   911  C  CG1 . ILE   A 1 117 ? 16.465 6.298   14.741 1.00 17.39 ? 123 ILE   A CG1 1 
ATOM   912  C  CG2 . ILE   A 1 117 ? 17.575 4.082   15.288 1.00 16.35 ? 123 ILE   A CG2 1 
ATOM   913  C  CD1 . ILE   A 1 117 ? 17.499 7.260   15.319 1.00 19.47 ? 123 ILE   A CD1 1 
ATOM   914  N  N   . VAL   A 1 118 ? 13.666 4.664   17.442 1.00 14.34 ? 124 VAL   A N   1 
ATOM   915  C  CA  . VAL   A 1 118 ? 12.673 5.373   18.275 1.00 14.23 ? 124 VAL   A CA  1 
ATOM   916  C  C   . VAL   A 1 118 ? 12.990 6.881   18.277 1.00 14.17 ? 124 VAL   A C   1 
ATOM   917  O  O   . VAL   A 1 118 ? 14.152 7.268   18.422 1.00 12.94 ? 124 VAL   A O   1 
ATOM   918  C  CB  . VAL   A 1 118 ? 12.608 4.833   19.744 1.00 15.43 ? 124 VAL   A CB  1 
ATOM   919  C  CG1 . VAL   A 1 118 ? 11.608 5.638   20.578 1.00 16.64 ? 124 VAL   A CG1 1 
ATOM   920  C  CG2 . VAL   A 1 118 ? 12.245 3.350   19.774 1.00 16.09 ? 124 VAL   A CG2 1 
ATOM   921  N  N   . SER   A 1 119 ? 11.982 7.723   18.042 1.00 15.39 ? 125 SER   A N   1 
ATOM   922  C  CA  . SER   A 1 119 ? 12.186 9.174   17.984 1.00 17.08 ? 125 SER   A CA  1 
ATOM   923  C  C   . SER   A 1 119 ? 11.141 9.943   18.809 1.00 20.88 ? 125 SER   A C   1 
ATOM   924  O  O   . SER   A 1 119 ? 11.452 11.010  19.338 1.00 21.33 ? 125 SER   A O   1 
ATOM   925  C  CB  . SER   A 1 119 ? 12.221 9.638   16.526 1.00 17.86 ? 125 SER   A CB  1 
ATOM   926  O  OG  . SER   A 1 119 ? 12.311 11.050  16.383 1.00 20.19 ? 125 SER   A OG  1 
ATOM   927  N  N   . THR   A 1 120 ? 9.891  9.434   18.898 1.00 23.42 ? 126 THR   A N   1 
ATOM   928  C  CA  . THR   A 1 120 ? 8.803  10.064  19.686 1.00 26.08 ? 126 THR   A CA  1 
ATOM   929  C  C   . THR   A 1 120 ? 8.049  8.950   20.499 1.00 28.77 ? 126 THR   A C   1 
ATOM   930  O  O   . THR   A 1 120 ? 8.342  7.773   20.324 1.00 28.03 ? 126 THR   A O   1 
ATOM   931  C  CB  . THR   A 1 120 ? 7.819  10.857  18.769 1.00 27.23 ? 126 THR   A CB  1 
ATOM   932  O  OG1 . THR   A 1 120 ? 6.956  9.951   18.090 1.00 28.17 ? 126 THR   A OG1 1 
ATOM   933  C  CG2 . THR   A 1 120 ? 8.496  11.792  17.784 1.00 27.77 ? 126 THR   A CG2 1 
ATOM   934  N  N   . GLY   A 1 121 ? 7.041  9.312   21.293 1.00 31.58 ? 127 GLY   A N   1 
ATOM   935  C  CA  . GLY   A 1 121 ? 6.230  8.346   22.015 1.00 34.87 ? 127 GLY   A CA  1 
ATOM   936  C  C   . GLY   A 1 121 ? 5.229  8.977   22.961 1.00 38.69 ? 127 GLY   A C   1 
ATOM   937  O  O   . GLY   A 1 121 ? 4.871  10.150  22.816 1.00 39.03 ? 127 GLY   A O   1 
ATOM   938  N  N   . GLY   A 1 122 ? 4.803  8.195   23.933 1.00 41.06 ? 128 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 122 ? 3.831  8.591   24.942 1.00 43.90 ? 128 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 122 ? 2.387  8.287   24.584 1.00 46.25 ? 128 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 122 ? 1.990  8.446   23.423 1.00 46.88 ? 128 GLY   A O   1 
ATOM   942  N  N   . ASN   A 1 123 ? 1.594  7.908   25.616 1.00 46.95 ? 129 ASN   A N   1 
ATOM   943  C  CA  . ASN   A 1 123 ? 0.161  7.559   25.657 1.00 47.74 ? 129 ASN   A CA  1 
ATOM   944  C  C   . ASN   A 1 123 ? -0.131 6.133   25.148 1.00 45.40 ? 129 ASN   A C   1 
ATOM   945  O  O   . ASN   A 1 123 ? -1.204 5.869   24.606 1.00 46.36 ? 129 ASN   A O   1 
ATOM   946  C  CB  . ASN   A 1 123 ? -0.701 8.608   24.947 1.00 52.12 ? 129 ASN   A CB  1 
ATOM   947  C  CG  . ASN   A 1 123 ? -0.897 9.879   25.756 1.00 59.54 ? 129 ASN   A CG  1 
ATOM   948  O  OD1 . ASN   A 1 123 ? -1.153 9.832   26.973 1.00 62.42 ? 129 ASN   A OD1 1 
ATOM   949  N  ND2 . ASN   A 1 123 ? -0.834 11.039  25.096 1.00 60.68 ? 129 ASN   A ND2 1 
ATOM   950  N  N   . GLY   A 1 124 ? 0.793  5.215   25.390 1.00 41.93 ? 130 GLY   A N   1 
ATOM   951  C  CA  . GLY   A 1 124 ? 0.676  3.864   24.865 1.00 39.73 ? 130 GLY   A CA  1 
ATOM   952  C  C   . GLY   A 1 124 ? 1.069  3.802   23.393 1.00 37.51 ? 130 GLY   A C   1 
ATOM   953  O  O   . GLY   A 1 124 ? 0.744  2.838   22.702 1.00 38.04 ? 130 GLY   A O   1 
ATOM   954  N  N   . LEU   A 1 125 ? 1.804  4.811   22.903 1.00 35.08 ? 131 LEU   A N   1 
ATOM   955  C  CA  . LEU   A 1 125 ? 2.275  4.914   21.528 1.00 33.02 ? 131 LEU   A CA  1 
ATOM   956  C  C   . LEU   A 1 125 ? 3.796  5.043   21.494 1.00 30.32 ? 131 LEU   A C   1 
ATOM   957  O  O   . LEU   A 1 125 ? 4.393  5.527   22.452 1.00 31.62 ? 131 LEU   A O   1 
ATOM   958  C  CB  . LEU   A 1 125 ? 1.663  6.161   20.853 1.00 33.53 ? 131 LEU   A CB  1 
ATOM   959  C  CG  . LEU   A 1 125 ? 0.137  6.193   20.737 1.00 36.25 ? 131 LEU   A CG  1 
ATOM   960  C  CD1 . LEU   A 1 125 ? -0.347 7.552   20.342 1.00 36.88 ? 131 LEU   A CD1 1 
ATOM   961  C  CD2 . LEU   A 1 125 ? -0.352 5.143   19.750 1.00 37.59 ? 131 LEU   A CD2 1 
ATOM   962  N  N   . VAL   A 1 126 ? 4.413  4.657   20.367 1.00 26.32 ? 132 VAL   A N   1 
ATOM   963  C  CA  . VAL   A 1 126 ? 5.833  4.806   20.114 1.00 23.00 ? 132 VAL   A CA  1 
ATOM   964  C  C   . VAL   A 1 126 ? 5.998  5.250   18.650 1.00 21.19 ? 132 VAL   A C   1 
ATOM   965  O  O   . VAL   A 1 126 ? 5.319  4.713   17.767 1.00 21.02 ? 132 VAL   A O   1 
ATOM   966  C  CB  . VAL   A 1 126 ? 6.689  3.554   20.499 1.00 22.05 ? 132 VAL   A CB  1 
ATOM   967  C  CG1 . VAL   A 1 126 ? 6.199  2.277   19.809 1.00 22.40 ? 132 VAL   A CG1 1 
ATOM   968  C  CG2 . VAL   A 1 126 ? 8.180  3.783   20.223 1.00 22.06 ? 132 VAL   A CG2 1 
ATOM   969  N  N   . GLY   A 1 127 ? 6.842  6.263   18.426 1.00 19.26 ? 133 GLY   A N   1 
ATOM   970  C  CA  . GLY   A 1 127 ? 7.137  6.810   17.108 1.00 18.43 ? 133 GLY   A CA  1 
ATOM   971  C  C   . GLY   A 1 127 ? 8.552  6.511   16.639 1.00 18.08 ? 133 GLY   A C   1 
ATOM   972  O  O   . GLY   A 1 127 ? 9.510  6.700   17.390 1.00 18.71 ? 133 GLY   A O   1 
ATOM   973  N  N   . PHE   A 1 128 ? 8.698  6.051   15.383 1.00 15.93 ? 134 PHE   A N   1 
ATOM   974  C  CA  . PHE   A 1 128 ? 9.986  5.677   14.793 1.00 13.98 ? 134 PHE   A CA  1 
ATOM   975  C  C   . PHE   A 1 128 ? 10.366 6.567   13.598 1.00 12.60 ? 134 PHE   A C   1 
ATOM   976  O  O   . PHE   A 1 128 ? 9.560  6.755   12.674 1.00 12.20 ? 134 PHE   A O   1 
ATOM   977  C  CB  . PHE   A 1 128 ? 9.944  4.213   14.310 1.00 13.40 ? 134 PHE   A CB  1 
ATOM   978  C  CG  . PHE   A 1 128 ? 9.502  3.205   15.348 1.00 13.88 ? 134 PHE   A CG  1 
ATOM   979  C  CD1 . PHE   A 1 128 ? 10.404 2.689   16.265 1.00 13.98 ? 134 PHE   A CD1 1 
ATOM   980  C  CD2 . PHE   A 1 128 ? 8.200  2.713   15.357 1.00 14.10 ? 134 PHE   A CD2 1 
ATOM   981  C  CE1 . PHE   A 1 128 ? 9.990  1.774   17.235 1.00 14.24 ? 134 PHE   A CE1 1 
ATOM   982  C  CE2 . PHE   A 1 128 ? 7.798  1.775   16.307 1.00 14.64 ? 134 PHE   A CE2 1 
ATOM   983  C  CZ  . PHE   A 1 128 ? 8.703  1.299   17.230 1.00 14.13 ? 134 PHE   A CZ  1 
ATOM   984  N  N   . ALA   A 1 129 ? 11.591 7.095   13.607 1.00 11.42 ? 135 ALA   A N   1 
ATOM   985  C  CA  . ALA   A 1 129 ? 12.094 7.842   12.467 1.00 12.71 ? 135 ALA   A CA  1 
ATOM   986  C  C   . ALA   A 1 129 ? 12.552 6.800   11.432 1.00 13.90 ? 135 ALA   A C   1 
ATOM   987  O  O   . ALA   A 1 129 ? 13.477 6.045   11.707 1.00 13.10 ? 135 ALA   A O   1 
ATOM   988  C  CB  . ALA   A 1 129 ? 13.276 8.728   12.883 1.00 12.78 ? 135 ALA   A CB  1 
ATOM   989  N  N   . ASP   A 1 130 ? 11.899 6.747   10.255 1.00 15.15 ? 136 ASP   A N   1 
ATOM   990  C  CA  . ASP   A 1 130 ? 12.247 5.798   9.179  1.00 16.65 ? 136 ASP   A CA  1 
ATOM   991  C  C   . ASP   A 1 130 ? 13.587 6.132   8.513  1.00 17.48 ? 136 ASP   A C   1 
ATOM   992  O  O   . ASP   A 1 130 ? 13.895 7.318   8.334  1.00 18.10 ? 136 ASP   A O   1 
ATOM   993  C  CB  . ASP   A 1 130 ? 11.152 5.844   8.117  1.00 19.36 ? 136 ASP   A CB  1 
ATOM   994  C  CG  . ASP   A 1 130 ? 11.322 4.859   6.990  1.00 25.96 ? 136 ASP   A CG  1 
ATOM   995  O  OD1 . ASP   A 1 130 ? 11.297 3.655   7.257  1.00 26.17 ? 136 ASP   A OD1 1 
ATOM   996  O  OD2 . ASP   A 1 130 ? 11.473 5.304   5.826  1.00 29.48 ? 136 ASP   A OD2 1 
ATOM   997  N  N   . VAL   A 1 131 ? 14.389 5.090   8.138  1.00 16.56 ? 137 VAL   A N   1 
ATOM   998  C  CA  . VAL   A 1 131 ? 15.663 5.284   7.421  1.00 17.21 ? 137 VAL   A CA  1 
ATOM   999  C  C   . VAL   A 1 131 ? 15.731 4.487   6.082  1.00 18.81 ? 137 VAL   A C   1 
ATOM   1000 O  O   . VAL   A 1 131 ? 16.753 4.537   5.386  1.00 20.28 ? 137 VAL   A O   1 
ATOM   1001 C  CB  . VAL   A 1 131 ? 16.900 5.006   8.314  1.00 16.74 ? 137 VAL   A CB  1 
ATOM   1002 C  CG1 . VAL   A 1 131 ? 16.853 5.841   9.598  1.00 16.71 ? 137 VAL   A CG1 1 
ATOM   1003 C  CG2 . VAL   A 1 131 ? 17.029 3.513   8.629  1.00 16.74 ? 137 VAL   A CG2 1 
ATOM   1004 N  N   . ARG   A 1 132 ? 14.665 3.755   5.722  1.00 18.48 ? 138 ARG   A N   1 
ATOM   1005 C  CA  . ARG   A 1 132 ? 14.638 2.920   4.518  1.00 19.23 ? 138 ARG   A CA  1 
ATOM   1006 C  C   . ARG   A 1 132 ? 14.758 3.686   3.183  1.00 21.09 ? 138 ARG   A C   1 
ATOM   1007 O  O   . ARG   A 1 132 ? 15.184 3.100   2.186  1.00 21.96 ? 138 ARG   A O   1 
ATOM   1008 C  CB  . ARG   A 1 132 ? 13.386 2.039   4.506  1.00 19.13 ? 138 ARG   A CB  1 
ATOM   1009 C  CG  . ARG   A 1 132 ? 13.253 1.124   5.711  1.00 17.58 ? 138 ARG   A CG  1 
ATOM   1010 C  CD  . ARG   A 1 132 ? 11.933 0.376   5.646  1.00 16.36 ? 138 ARG   A CD  1 
ATOM   1011 N  NE  . ARG   A 1 132 ? 10.803 1.227   6.027  1.00 17.15 ? 138 ARG   A NE  1 
ATOM   1012 C  CZ  . ARG   A 1 132 ? 9.562  0.786   6.197  1.00 20.05 ? 138 ARG   A CZ  1 
ATOM   1013 N  NH1 . ARG   A 1 132 ? 9.260  -0.482  5.941  1.00 18.62 ? 138 ARG   A NH1 1 
ATOM   1014 N  NH2 . ARG   A 1 132 ? 8.606  1.613   6.604  1.00 20.65 ? 138 ARG   A NH2 1 
ATOM   1015 N  N   . ASP   A 1 133 ? 14.413 4.978   3.153  1.00 21.25 ? 139 ASP   A N   1 
ATOM   1016 C  CA  . ASP   A 1 133 ? 14.537 5.779   1.926  1.00 22.05 ? 139 ASP   A CA  1 
ATOM   1017 C  C   . ASP   A 1 133 ? 15.961 6.337   1.712  1.00 23.08 ? 139 ASP   A C   1 
ATOM   1018 O  O   . ASP   A 1 133 ? 16.258 6.838   0.625  1.00 23.43 ? 139 ASP   A O   1 
ATOM   1019 C  CB  . ASP   A 1 133 ? 13.539 6.944   1.918  1.00 22.87 ? 139 ASP   A CB  1 
ATOM   1020 C  CG  . ASP   A 1 133 ? 13.757 7.934   3.050  1.00 25.28 ? 139 ASP   A CG  1 
ATOM   1021 O  OD1 . ASP   A 1 133 ? 14.121 7.489   4.169  1.00 24.38 ? 139 ASP   A OD1 1 
ATOM   1022 O  OD2 . ASP   A 1 133 ? 13.530 9.151   2.830  1.00 26.01 ? 139 ASP   A OD2 1 
ATOM   1023 N  N   . LEU   A 1 134 ? 16.837 6.262   2.733  1.00 23.57 ? 140 LEU   A N   1 
ATOM   1024 C  CA  . LEU   A 1 134 ? 18.204 6.803   2.653  1.00 24.08 ? 140 LEU   A CA  1 
ATOM   1025 C  C   . LEU   A 1 134 ? 19.110 5.796   1.981  1.00 26.23 ? 140 LEU   A C   1 
ATOM   1026 O  O   . LEU   A 1 134 ? 19.912 5.137   2.647  1.00 26.22 ? 140 LEU   A O   1 
ATOM   1027 C  CB  . LEU   A 1 134 ? 18.730 7.171   4.060  1.00 23.58 ? 140 LEU   A CB  1 
ATOM   1028 C  CG  . LEU   A 1 134 ? 17.811 8.076   4.890  1.00 24.48 ? 140 LEU   A CG  1 
ATOM   1029 C  CD1 . LEU   A 1 134 ? 18.364 8.315   6.301  1.00 24.73 ? 140 LEU   A CD1 1 
ATOM   1030 C  CD2 . LEU   A 1 134 ? 17.536 9.394   4.176  1.00 24.84 ? 140 LEU   A CD2 1 
ATOM   1031 N  N   . LEU   A 1 135 ? 18.976 5.664   0.643  1.00 27.89 ? 141 LEU   A N   1 
ATOM   1032 C  CA  . LEU   A 1 135 ? 19.721 4.666   -0.143 1.00 29.53 ? 141 LEU   A CA  1 
ATOM   1033 C  C   . LEU   A 1 135 ? 21.233 4.896   -0.121 1.00 30.84 ? 141 LEU   A C   1 
ATOM   1034 O  O   . LEU   A 1 135 ? 21.993 3.929   -0.232 1.00 31.16 ? 141 LEU   A O   1 
ATOM   1035 C  CB  . LEU   A 1 135 ? 19.243 4.636   -1.601 1.00 30.01 ? 141 LEU   A CB  1 
ATOM   1036 C  CG  . LEU   A 1 135 ? 17.751 4.653   -1.890 1.00 31.91 ? 141 LEU   A CG  1 
ATOM   1037 C  CD1 . LEU   A 1 135 ? 17.513 4.394   -3.372 1.00 32.72 ? 141 LEU   A CD1 1 
ATOM   1038 C  CD2 . LEU   A 1 135 ? 17.016 3.585   -1.115 1.00 33.16 ? 141 LEU   A CD2 1 
ATOM   1039 N  N   . TRP   A 1 136 ? 21.669 6.159   0.077  1.00 31.06 ? 142 TRP   A N   1 
ATOM   1040 C  CA  . TRP   A 1 136 ? 23.089 6.502   0.100  1.00 32.18 ? 142 TRP   A CA  1 
ATOM   1041 C  C   . TRP   A 1 136 ? 23.858 5.914   1.289  1.00 35.24 ? 142 TRP   A C   1 
ATOM   1042 O  O   . TRP   A 1 136 ? 25.085 5.903   1.259  1.00 35.53 ? 142 TRP   A O   1 
ATOM   1043 C  CB  . TRP   A 1 136 ? 23.305 8.021   0.004  1.00 30.98 ? 142 TRP   A CB  1 
ATOM   1044 C  CG  . TRP   A 1 136 ? 22.545 8.827   1.013  1.00 29.49 ? 142 TRP   A CG  1 
ATOM   1045 C  CD1 . TRP   A 1 136 ? 21.310 9.388   0.859  1.00 29.67 ? 142 TRP   A CD1 1 
ATOM   1046 C  CD2 . TRP   A 1 136 ? 22.998 9.207   2.317  1.00 28.74 ? 142 TRP   A CD2 1 
ATOM   1047 N  NE1 . TRP   A 1 136 ? 20.951 10.062  2.006  1.00 29.46 ? 142 TRP   A NE1 1 
ATOM   1048 C  CE2 . TRP   A 1 136 ? 21.973 9.967   2.914  1.00 28.99 ? 142 TRP   A CE2 1 
ATOM   1049 C  CE3 . TRP   A 1 136 ? 24.161 8.954   3.050  1.00 29.09 ? 142 TRP   A CE3 1 
ATOM   1050 C  CZ2 . TRP   A 1 136 ? 22.088 10.491  4.198  1.00 29.53 ? 142 TRP   A CZ2 1 
ATOM   1051 C  CZ3 . TRP   A 1 136 ? 24.279 9.493   4.317  1.00 29.56 ? 142 TRP   A CZ3 1 
ATOM   1052 C  CH2 . TRP   A 1 136 ? 23.255 10.254  4.875  1.00 29.51 ? 142 TRP   A CH2 1 
ATOM   1053 N  N   . LEU   A 1 137 ? 23.160 5.398   2.317  1.00 37.10 ? 143 LEU   A N   1 
ATOM   1054 C  CA  . LEU   A 1 137 ? 23.829 4.793   3.465  1.00 39.69 ? 143 LEU   A CA  1 
ATOM   1055 C  C   . LEU   A 1 137 ? 24.642 3.549   3.075  1.00 44.50 ? 143 LEU   A C   1 
ATOM   1056 O  O   . LEU   A 1 137 ? 25.604 3.219   3.768  1.00 44.97 ? 143 LEU   A O   1 
ATOM   1057 C  CB  . LEU   A 1 137 ? 22.813 4.435   4.556  1.00 38.73 ? 143 LEU   A CB  1 
ATOM   1058 C  CG  . LEU   A 1 137 ? 22.159 5.615   5.274  1.00 38.70 ? 143 LEU   A CG  1 
ATOM   1059 C  CD1 . LEU   A 1 137 ? 21.047 5.124   6.205  1.00 38.68 ? 143 LEU   A CD1 1 
ATOM   1060 C  CD2 . LEU   A 1 137 ? 23.194 6.429   6.068  1.00 38.51 ? 143 LEU   A CD2 1 
ATOM   1061 N  N   . ASP   A 1 138 ? 24.259 2.863   1.972  1.00 47.76 ? 144 ASP   A N   1 
ATOM   1062 C  CA  . ASP   A 1 138 ? 24.925 1.659   1.473  1.00 51.42 ? 144 ASP   A CA  1 
ATOM   1063 C  C   . ASP   A 1 138 ? 26.075 1.948   0.552  1.00 55.27 ? 144 ASP   A C   1 
ATOM   1064 O  O   . ASP   A 1 138 ? 26.980 1.121   0.449  1.00 56.43 ? 144 ASP   A O   1 
ATOM   1065 C  CB  . ASP   A 1 138 ? 23.943 0.811   0.672  1.00 53.38 ? 144 ASP   A CB  1 
ATOM   1066 C  CG  . ASP   A 1 138 ? 22.809 0.287   1.492  1.00 57.06 ? 144 ASP   A CG  1 
ATOM   1067 O  OD1 . ASP   A 1 138 ? 23.048 -0.089  2.654  1.00 57.71 ? 144 ASP   A OD1 1 
ATOM   1068 O  OD2 . ASP   A 1 138 ? 21.678 0.244   0.970  1.00 59.17 ? 144 ASP   A OD2 1 
ATOM   1069 N  N   . GLU   A 1 139 ? 26.000 3.054   -0.204 1.00 57.12 ? 145 GLU   A N   1 
ATOM   1070 C  CA  . GLU   A 1 139 ? 27.015 3.392   -1.193 1.00 59.42 ? 145 GLU   A CA  1 
ATOM   1071 C  C   . GLU   A 1 139 ? 27.886 4.570   -0.788 1.00 60.70 ? 145 GLU   A C   1 
ATOM   1072 O  O   . GLU   A 1 139 ? 28.806 4.925   -1.537 1.00 61.85 ? 145 GLU   A O   1 
ATOM   1073 C  CB  . GLU   A 1 139 ? 26.358 3.652   -2.559 1.00 62.52 ? 145 GLU   A CB  1 
ATOM   1074 C  CG  . GLU   A 1 139 ? 25.284 4.726   -2.525 1.00 67.33 ? 145 GLU   A CG  1 
ATOM   1075 C  CD  . GLU   A 1 139 ? 24.047 4.411   -3.345 1.00 73.69 ? 145 GLU   A CD  1 
ATOM   1076 O  OE1 . GLU   A 1 139 ? 23.434 5.363   -3.881 1.00 74.61 ? 145 GLU   A OE1 1 
ATOM   1077 O  OE2 . GLU   A 1 139 ? 23.685 3.215   -3.445 1.00 76.29 ? 145 GLU   A OE2 1 
HETATM 1078 N  N1  . A1B2N B 2 .   ? 11.404 13.744  17.911 1.00 34.74 ? 201 A1B2N A N1  1 
HETATM 1079 C  C4  . A1B2N B 2 .   ? 10.542 8.639   23.672 1.00 50.57 ? 201 A1B2N A C4  1 
HETATM 1080 C  C5  . A1B2N B 2 .   ? 10.696 10.005  23.781 1.00 49.56 ? 201 A1B2N A C5  1 
HETATM 1081 C  C6  . A1B2N B 2 .   ? 9.692  10.806  24.322 1.00 49.68 ? 201 A1B2N A C6  1 
HETATM 1082 C  C7  . A1B2N B 2 .   ? 9.867  12.307  24.302 1.00 45.59 ? 201 A1B2N A C7  1 
HETATM 1083 C  C8  . A1B2N B 2 .   ? 9.444  12.888  22.966 1.00 41.71 ? 201 A1B2N A C8  1 
HETATM 1084 C  C10 . A1B2N B 2 .   ? 12.606 14.400  22.422 1.00 37.49 ? 201 A1B2N A C10 1 
HETATM 1085 C  C13 . A1B2N B 2 .   ? 11.092 14.622  18.847 1.00 35.31 ? 201 A1B2N A C13 1 
HETATM 1086 O  O3  . A1B2N B 2 .   ? 10.686 15.758  18.590 1.00 34.71 ? 201 A1B2N A O3  1 
HETATM 1087 C  C12 . A1B2N B 2 .   ? 11.260 14.153  20.283 1.00 36.57 ? 201 A1B2N A C12 1 
HETATM 1088 C  C11 . A1B2N B 2 .   ? 12.430 14.870  20.975 1.00 36.80 ? 201 A1B2N A C11 1 
HETATM 1089 C  C9  . A1B2N B 2 .   ? 11.308 14.539  23.197 1.00 38.01 ? 201 A1B2N A C9  1 
HETATM 1090 C  C14 . A1B2N B 2 .   ? 9.995  14.390  21.114 1.00 37.86 ? 201 A1B2N A C14 1 
HETATM 1091 N  N   . A1B2N B 2 .   ? 10.201 13.891  22.477 1.00 39.09 ? 201 A1B2N A N   1 
HETATM 1092 O  O2  . A1B2N B 2 .   ? 8.475  12.451  22.361 1.00 40.62 ? 201 A1B2N A O2  1 
HETATM 1093 C  C1  . A1B2N B 2 .   ? 8.529  10.165  24.768 1.00 52.97 ? 201 A1B2N A C1  1 
HETATM 1094 S  S   . A1B2N B 2 .   ? 7.079  11.043  25.307 1.00 56.74 ? 201 A1B2N A S   1 
HETATM 1095 O  O   . A1B2N B 2 .   ? 6.177  10.088  25.887 1.00 56.87 ? 201 A1B2N A O   1 
HETATM 1096 O  O1  . A1B2N B 2 .   ? 6.606  11.827  24.200 1.00 57.27 ? 201 A1B2N A O1  1 
HETATM 1097 C  C   . A1B2N B 2 .   ? 7.601  12.136  26.576 1.00 57.01 ? 201 A1B2N A C   1 
HETATM 1098 C  C3  . A1B2N B 2 .   ? 9.400  8.034   24.123 1.00 51.67 ? 201 A1B2N A C3  1 
HETATM 1099 C  C2  . A1B2N B 2 .   ? 8.388  8.787   24.691 1.00 52.25 ? 201 A1B2N A C2  1 
HETATM 1100 ZN ZN  . ZN    C 3 .   ? 11.065 -5.366  5.657  1.00 25.55 2 202 ZN    A ZN  1 
HETATM 1101 S  S   . DMS   D 4 .   ? 20.004 -0.566  20.288 1.00 72.66 ? 203 DMS   A S   1 
HETATM 1102 O  O   . DMS   D 4 .   ? 18.579 -0.727  19.836 1.00 72.37 ? 203 DMS   A O   1 
HETATM 1103 C  C1  . DMS   D 4 .   ? 20.006 0.278   21.896 1.00 72.68 ? 203 DMS   A C1  1 
HETATM 1104 C  C2  . DMS   D 4 .   ? 20.753 0.827   19.403 1.00 72.62 ? 203 DMS   A C2  1 
HETATM 1105 O  O   . HOH   E 5 .   ? 20.198 22.144  7.954  1.00 25.68 ? 301 HOH   A O   1 
HETATM 1106 O  O   . HOH   E 5 .   ? 10.670 7.407   4.705  1.00 39.98 ? 302 HOH   A O   1 
HETATM 1107 O  O   . HOH   E 5 .   ? 8.183  -4.538  0.716  1.00 33.66 ? 303 HOH   A O   1 
HETATM 1108 O  O   . HOH   E 5 .   ? 22.669 -2.039  4.244  1.00 36.52 ? 304 HOH   A O   1 
HETATM 1109 O  O   . HOH   E 5 .   ? 8.804  1.735   2.909  1.00 30.86 ? 305 HOH   A O   1 
HETATM 1110 O  O   . HOH   E 5 .   ? 23.671 21.543  7.997  1.00 30.57 ? 306 HOH   A O   1 
HETATM 1111 O  O   . HOH   E 5 .   ? 20.253 8.366   19.003 1.00 20.26 ? 307 HOH   A O   1 
HETATM 1112 O  O   . HOH   E 5 .   ? 14.703 2.143   23.314 1.00 17.92 ? 308 HOH   A O   1 
HETATM 1113 O  O   . HOH   E 5 .   ? 10.243 17.861  20.312 1.00 44.07 ? 309 HOH   A O   1 
HETATM 1114 O  O   . HOH   E 5 .   ? 6.654  -6.553  29.297 1.00 34.65 ? 310 HOH   A O   1 
HETATM 1115 O  O   . HOH   E 5 .   ? 11.208 11.057  11.407 1.00 15.65 ? 311 HOH   A O   1 
HETATM 1116 O  O   . HOH   E 5 .   ? 17.828 20.594  9.506  1.00 26.64 ? 312 HOH   A O   1 
HETATM 1117 O  O   . HOH   E 5 .   ? 16.194 23.101  14.572 1.00 48.67 ? 313 HOH   A O   1 
HETATM 1118 O  O   . HOH   E 5 .   ? 30.576 20.137  10.598 1.00 47.02 ? 314 HOH   A O   1 
HETATM 1119 O  O   . HOH   E 5 .   ? 0.476  -0.897  16.572 1.00 21.15 ? 315 HOH   A O   1 
HETATM 1120 O  O   . HOH   E 5 .   ? 10.002 3.701   34.023 1.00 32.13 ? 316 HOH   A O   1 
HETATM 1121 O  O   . HOH   E 5 .   ? 11.078 -5.786  31.956 1.00 35.90 ? 317 HOH   A O   1 
HETATM 1122 O  O   . HOH   E 5 .   ? 13.137 9.797   9.381  1.00 11.48 ? 318 HOH   A O   1 
HETATM 1123 O  O   . HOH   E 5 .   ? 5.846  0.817   6.430  1.00 34.92 ? 319 HOH   A O   1 
HETATM 1124 O  O   . HOH   E 5 .   ? 7.190  2.949   33.058 1.00 25.50 ? 320 HOH   A O   1 
HETATM 1125 O  O   . HOH   E 5 .   ? 2.645  -5.558  20.667 1.00 41.06 ? 321 HOH   A O   1 
HETATM 1126 O  O   . HOH   E 5 .   ? 8.596  19.175  18.446 1.00 34.48 ? 322 HOH   A O   1 
HETATM 1127 O  O   . HOH   E 5 .   ? 10.249 4.155   3.517  1.00 25.04 ? 323 HOH   A O   1 
HETATM 1128 O  O   . HOH   E 5 .   ? 18.047 18.334  17.025 1.00 17.94 ? 324 HOH   A O   1 
HETATM 1129 O  O   . HOH   E 5 .   ? 9.170  20.527  10.694 1.00 30.66 ? 325 HOH   A O   1 
HETATM 1130 O  O   . HOH   E 5 .   ? 11.395 1.537   33.660 1.00 22.17 ? 326 HOH   A O   1 
HETATM 1131 O  O   . HOH   E 5 .   ? 4.227  10.390  18.918 1.00 39.76 ? 327 HOH   A O   1 
HETATM 1132 O  O   . HOH   E 5 .   ? 15.230 9.286   24.676 1.00 31.38 ? 328 HOH   A O   1 
HETATM 1133 O  O   . HOH   E 5 .   ? 14.833 -5.234  17.320 1.00 25.13 ? 329 HOH   A O   1 
HETATM 1134 O  O   . HOH   E 5 .   ? 17.527 2.210   23.396 1.00 29.59 ? 330 HOH   A O   1 
HETATM 1135 O  O   . HOH   E 5 .   ? 5.471  -2.372  24.492 1.00 24.85 ? 331 HOH   A O   1 
HETATM 1136 O  O   . HOH   E 5 .   ? 35.042 8.396   7.471  1.00 41.18 ? 332 HOH   A O   1 
HETATM 1137 O  O   . HOH   E 5 .   ? 18.860 19.039  27.564 1.00 54.11 ? 333 HOH   A O   1 
HETATM 1138 O  O   . HOH   E 5 .   ? 10.496 16.624  5.010  1.00 45.72 ? 334 HOH   A O   1 
HETATM 1139 O  O   . HOH   E 5 .   ? 14.225 13.864  3.534  1.00 30.70 ? 335 HOH   A O   1 
HETATM 1140 O  O   . HOH   E 5 .   ? 22.726 18.012  19.914 1.00 38.16 ? 336 HOH   A O   1 
HETATM 1141 O  O   . HOH   E 5 .   ? 4.815  7.065   28.264 1.00 46.87 ? 337 HOH   A O   1 
HETATM 1142 O  O   . HOH   E 5 .   ? 4.245  -6.064  6.667  1.00 30.29 ? 338 HOH   A O   1 
HETATM 1143 O  O   . HOH   E 5 .   ? 30.253 10.447  18.922 1.00 38.48 ? 339 HOH   A O   1 
HETATM 1144 O  O   . HOH   E 5 .   ? 14.472 20.641  8.333  1.00 32.76 ? 340 HOH   A O   1 
HETATM 1145 O  O   . HOH   E 5 .   ? -2.103 0.203   8.291  1.00 36.72 ? 341 HOH   A O   1 
HETATM 1146 O  O   . HOH   E 5 .   ? -1.112 1.405   5.304  1.00 73.93 ? 342 HOH   A O   1 
HETATM 1147 O  O   . HOH   E 5 .   ? 7.368  25.638  14.430 1.00 48.83 ? 343 HOH   A O   1 
HETATM 1148 O  O   . HOH   E 5 .   ? 19.551 23.154  15.572 1.00 24.26 ? 344 HOH   A O   1 
HETATM 1149 O  O   . HOH   E 5 .   ? 11.755 20.692  12.283 1.00 21.48 ? 345 HOH   A O   1 
HETATM 1150 O  O   . HOH   E 5 .   ? 14.639 12.020  24.330 1.00 31.34 ? 346 HOH   A O   1 
HETATM 1151 O  O   . HOH   E 5 .   ? 1.637  -3.080  17.767 1.00 27.24 ? 347 HOH   A O   1 
HETATM 1152 O  O   . HOH   E 5 .   ? 22.385 18.469  5.917  1.00 25.16 ? 348 HOH   A O   1 
HETATM 1153 O  O   . HOH   E 5 .   ? 21.985 -6.304  10.601 1.00 30.86 ? 349 HOH   A O   1 
HETATM 1154 O  O   . HOH   E 5 .   ? 8.485  -8.241  9.060  1.00 39.41 ? 350 HOH   A O   1 
HETATM 1155 O  O   . HOH   E 5 .   ? 18.359 11.830  1.706  1.00 34.39 ? 351 HOH   A O   1 
HETATM 1156 O  O   . HOH   E 5 .   ? 7.303  -6.124  2.803  1.00 51.18 ? 352 HOH   A O   1 
HETATM 1157 O  O   . HOH   E 5 .   ? 15.815 -5.388  1.810  1.00 30.87 ? 353 HOH   A O   1 
HETATM 1158 O  O   . HOH   E 5 .   ? 2.701  14.498  19.688 1.00 57.23 ? 354 HOH   A O   1 
HETATM 1159 O  O   . HOH   E 5 .   ? -3.139 12.369  27.264 1.00 41.97 ? 355 HOH   A O   1 
HETATM 1160 O  O   . HOH   E 5 .   ? 12.054 -8.735  13.028 1.00 43.10 ? 356 HOH   A O   1 
HETATM 1161 O  O   . HOH   E 5 .   ? 24.611 6.853   20.777 1.00 40.43 ? 357 HOH   A O   1 
HETATM 1162 O  O   . HOH   E 5 .   ? 5.071  -2.092  29.097 1.00 40.07 ? 358 HOH   A O   1 
HETATM 1163 O  O   . HOH   E 5 .   ? 2.651  1.798   27.588 1.00 37.06 ? 359 HOH   A O   1 
HETATM 1164 O  O   . HOH   E 5 .   ? 22.213 8.536   20.883 1.00 30.49 ? 360 HOH   A O   1 
HETATM 1165 O  O   . HOH   E 5 .   ? 28.605 21.769  18.550 1.00 36.00 ? 361 HOH   A O   1 
HETATM 1166 O  O   . HOH   E 5 .   ? 3.092  12.182  18.500 1.00 36.06 ? 362 HOH   A O   1 
HETATM 1167 O  O   . HOH   E 5 .   ? -1.940 -4.866  15.695 1.00 47.19 ? 363 HOH   A O   1 
HETATM 1168 O  O   . HOH   E 5 .   ? 21.015 21.536  17.823 1.00 35.24 ? 364 HOH   A O   1 
HETATM 1169 O  O   . HOH   E 5 .   ? 5.287  14.058  21.498 1.00 37.04 ? 365 HOH   A O   1 
HETATM 1170 O  O   . HOH   E 5 .   ? 26.682 -2.522  15.319 1.00 28.27 ? 366 HOH   A O   1 
HETATM 1171 O  O   . HOH   E 5 .   ? 11.987 22.970  14.366 1.00 37.43 ? 367 HOH   A O   1 
HETATM 1172 O  O   . HOH   E 5 .   ? 8.900  6.536   2.568  1.00 45.67 ? 368 HOH   A O   1 
HETATM 1173 O  O   . HOH   E 5 .   ? 9.407  -9.588  12.865 1.00 31.48 ? 369 HOH   A O   1 
HETATM 1174 O  O   . HOH   E 5 .   ? 9.851  24.423  13.464 1.00 58.02 ? 370 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   ? 0.8364 0.2398 0.4154 -0.0710 -0.2115 0.0248  7   SER   A N   
2    C CA  . SER   A 1   ? 0.7881 0.2511 0.4710 -0.0725 -0.2424 0.0370  7   SER   A CA  
3    C C   . SER   A 1   ? 0.7028 0.2590 0.5024 -0.0583 -0.2304 0.0364  7   SER   A C   
4    O O   . SER   A 1   ? 0.7126 0.2754 0.5056 -0.0544 -0.2169 0.0310  7   SER   A O   
5    C CB  . SER   A 1   ? 0.8475 0.2425 0.5083 -0.1040 -0.3100 0.0609  7   SER   A CB  
6    O OG  . SER   A 1   ? 0.9185 0.2664 0.5434 -0.1216 -0.3380 0.0700  7   SER   A OG  
7    N N   . GLY   A 2   ? 0.6236 0.2429 0.5219 -0.0512 -0.2305 0.0413  8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.5449 0.2383 0.5453 -0.0393 -0.2104 0.0397  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.4772 0.2292 0.5444 -0.0263 -0.1816 0.0336  8   GLY   A C   
10   O O   . GLY   A 2   ? 0.4914 0.2416 0.5215 -0.0209 -0.1674 0.0254  8   GLY   A O   
11   N N   . ALA   A 3   ? 0.4045 0.2023 0.5679 -0.0219 -0.1689 0.0380  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.3583 0.1990 0.5800 -0.0129 -0.1372 0.0326  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.3124 0.1889 0.5914 -0.0060 -0.0979 0.0253  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.3018 0.1758 0.6007 -0.0079 -0.1019 0.0296  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.3458 0.1816 0.6358 -0.0202 -0.1652 0.0535  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.2905 0.1914 0.5881 -0.0006 -0.0592 0.0146  10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.2692 0.1853 0.6057 0.0016  -0.0162 0.0070  10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.2551 0.1756 0.6861 0.0023  -0.0008 0.0196  10  ILE   A C   
19   O O   . ILE   A 4   ? 0.2425 0.1652 0.6812 0.0025  -0.0030 0.0222  10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.2776 0.2010 0.5497 0.0011  0.0178  -0.0129 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.2878 0.2112 0.4816 0.0018  0.0032  -0.0197 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.2789 0.1978 0.5684 -0.0025 0.0612  -0.0212 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.2948 0.2268 0.4400 -0.0007 0.0201  -0.0289 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.2516 0.1721 0.7593 0.0035  0.0188  0.0287  11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.2407 0.1631 0.8578 0.0060  0.0422  0.0451  11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.2663 0.1764 0.8914 0.0080  0.1125  0.0302  11  TYR   A C   
27   O O   . TYR   A 5   ? 0.2690 0.1716 0.9162 0.0089  0.1324  0.0300  11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.2158 0.1403 0.9343 0.0044  0.0062  0.0763  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.2365 0.1546 0.9414 -0.0046 -0.0652 0.0950  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.2354 0.1550 0.9911 -0.0079 -0.0859 0.1131  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.2792 0.1799 0.9097 -0.0120 -0.1100 0.0941  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.2615 0.1613 0.9861 -0.0207 -0.1526 0.1297  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.3152 0.1899 0.9080 -0.0248 -0.1714 0.1091  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.3120 0.1843 0.9503 -0.0303 -0.1946 0.1274  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.3595 0.1933 0.9492 -0.0474 -0.2572 0.1433  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.2911 0.1902 0.8864 0.0062  0.1508  0.0169  12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.3221 0.1883 0.9009 0.0023  0.2214  0.0015  12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.3185 0.1698 0.9695 0.0049  0.2641  0.0100  12  VAL   A C   
39   O O   . VAL   A 6   ? 0.3280 0.1845 0.9535 0.0030  0.2538  0.0075  12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.3859 0.2328 0.8279 -0.0099 0.2332  -0.0251 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.4029 0.2656 0.7852 -0.0128 0.2012  -0.0296 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.4249 0.2175 0.8335 -0.0208 0.3046  -0.0396 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.2935 0.1258 1.0439 0.0104  0.3143  0.0224  13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.2893 0.1044 1.1275 0.0148  0.3639  0.0344  13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.2627 0.1199 1.1907 0.0206  0.3084  0.0620  13  GLY   A C   
46   O O   . GLY   A 7   ? 0.2442 0.1339 1.2168 0.0224  0.2432  0.0821  13  GLY   A O   
47   N N   . ASN   A 8   ? 0.2651 0.1155 1.2001 0.0200  0.3273  0.0618  14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.2278 0.1133 1.2376 0.0228  0.2720  0.0878  14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.2345 0.1384 1.1259 0.0163  0.2064  0.0733  14  ASN   A C   
50   O O   . ASN   A 8   ? 0.2290 0.1450 1.1347 0.0154  0.1797  0.0825  14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.2494 0.1207 1.3415 0.0265  0.3237  0.0991  14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.2810 0.1374 1.5247 0.0356  0.3849  0.1238  14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.2597 0.1335 1.5923 0.0398  0.3633  0.1468  14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.3219 0.1413 1.6020 0.0385  0.4655  0.1214  14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.2368 0.1418 1.0209 0.0124  0.1817  0.0537  15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.2341 0.1518 0.9154 0.0082  0.1292  0.0423  15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.2050 0.1338 0.8619 0.0071  0.0704  0.0492  15  TYR   A C   
58   O O   . TYR   A 9   ? 0.1955 0.1223 0.8730 0.0080  0.0742  0.0519  15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.2680 0.1698 0.8239 0.0021  0.1580  0.0116  15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.2778 0.1562 0.8232 -0.0024 0.2082  0.0025  15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.2735 0.1614 0.8541 -0.0002 0.1970  0.0123  15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.3202 0.1584 0.8055 -0.0121 0.2650  -0.0163 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.3035 0.1652 0.8688 -0.0054 0.2447  0.0036  15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.3597 0.1616 0.8168 -0.0205 0.3121  -0.0253 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.3580 0.1736 0.8598 -0.0160 0.3037  -0.0153 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.4034 0.1783 0.8731 -0.0253 0.3523  -0.0245 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.1821 0.1146 0.7816 0.0042  0.0206  0.0498  16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.1737 0.1004 0.7198 0.0007  -0.0290 0.0523  16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.1911 0.1146 0.6201 0.0012  -0.0320 0.0307  16  ARG   A C   
70   O O   . ARG   A 10  ? 0.1953 0.1193 0.6057 0.0012  -0.0351 0.0289  16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.1706 0.0872 0.7695 -0.0071 -0.0879 0.0819  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.2415 0.1307 0.7491 -0.0155 -0.1395 0.0818  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.2849 0.1495 0.8393 -0.0308 -0.2017 0.1148  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.3736 0.1960 0.8269 -0.0422 -0.2443 0.1139  16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.4438 0.2195 0.8133 -0.0546 -0.2814 0.1158  16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.4295 0.2031 0.8062 -0.0561 -0.2844 0.1179  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.4852 0.2086 0.7552 -0.0662 -0.3112 0.1143  16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.1965 0.1182 0.5571 0.0021  -0.0280 0.0167  17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.2253 0.1463 0.4949 0.0035  -0.0278 0.0021  17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.2457 0.1454 0.4649 0.0028  -0.0641 0.0066  17  VAL   A C   
81   O O   . VAL   A 11  ? 0.2525 0.1441 0.4706 0.0012  -0.0734 0.0091  17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.2355 0.1658 0.4649 0.0027  0.0060  -0.0136 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.2557 0.1904 0.4172 0.0031  0.0050  -0.0206 17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.2169 0.1464 0.4820 -0.0017 0.0475  -0.0187 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.2576 0.1402 0.4301 0.0028  -0.0815 0.0075  18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.2941 0.1361 0.4008 -0.0004 -0.1086 0.0107  18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.3114 0.1450 0.3485 0.0064  -0.0921 0.0010  18  VAL   A C   
88   O O   . VAL   A 12  ? 0.3060 0.1658 0.3536 0.0111  -0.0730 -0.0038 18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.3103 0.1146 0.4260 -0.0123 -0.1528 0.0284  18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.3022 0.1078 0.4917 -0.0209 -0.1776 0.0460  18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.2986 0.1134 0.4389 -0.0116 -0.1524 0.0313  18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.3316 0.1210 0.2984 0.0058  -0.0985 0.0007  19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.3567 0.1295 0.2689 0.0135  -0.0781 -0.0040 19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.3737 0.1253 0.2772 0.0096  -0.0935 0.0003  19  ASN   A C   
95   O O   . ASN   A 13  ? 0.4009 0.1143 0.2965 -0.0033 -0.1283 0.0091  19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.4067 0.1187 0.2413 0.0127  -0.0741 -0.0044 19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.4232 0.1519 0.2613 0.0172  -0.0573 -0.0077 19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.4518 0.1650 0.2880 0.0091  -0.0762 -0.0059 19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.3893 0.1497 0.2380 0.0286  -0.0251 -0.0094 19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.3558 0.1317 0.2660 0.0178  -0.0730 -0.0028 20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.3598 0.1175 0.2621 0.0147  -0.0856 0.0007  20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.4450 0.1207 0.2652 0.0067  -0.1015 0.0042  20  ARG   A C   
103  O O   . ARG   A 14  ? 0.4626 0.1065 0.2758 -0.0063 -0.1346 0.0119  20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.3181 0.1120 0.2360 0.0246  -0.0600 -0.0021 20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.3081 0.0977 0.2342 0.0217  -0.0716 0.0007  20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.2932 0.1058 0.2193 0.0313  -0.0460 -0.0001 20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.3186 0.1342 0.2540 0.0303  -0.0516 0.0017  20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.3704 0.1392 0.2616 0.0303  -0.0571 0.0039  20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.3972 0.1010 0.2230 0.0281  -0.0592 0.0041  20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.3678 0.1454 0.2715 0.0301  -0.0600 0.0056  20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.4977 0.1300 0.2528 0.0115  -0.0781 0.0003  21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.5821 0.1138 0.2356 0.0006  -0.0845 0.0016  21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.6421 0.1159 0.2576 -0.0230 -0.1321 0.0093  21  HIS   A C   
114  O O   . HIS   A 15  ? 0.7053 0.0859 0.2306 -0.0408 -0.1517 0.0134  21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.6184 0.1084 0.2136 0.0118  -0.0376 -0.0033 21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.6452 0.1341 0.2344 0.0125  -0.0290 -0.0051 21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.6068 0.1773 0.2711 0.0267  -0.0091 -0.0058 21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.7184 0.1260 0.2262 -0.0012 -0.0369 -0.0057 21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.6431 0.1878 0.2789 0.0235  -0.0055 -0.0072 21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.7042 0.1514 0.2459 0.0074  -0.0204 -0.0075 21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.6228 0.1452 0.3054 -0.0259 -0.1530 0.0137  22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.6607 0.1382 0.3297 -0.0491 -0.2032 0.0269  22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.6360 0.1570 0.4020 -0.0582 -0.2445 0.0432  22  LEU   A C   
124  O O   . LEU   A 16  ? 0.6491 0.1457 0.4329 -0.0774 -0.2902 0.0607  22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.6468 0.1390 0.3253 -0.0461 -0.1947 0.0238  22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.7143 0.1447 0.2942 -0.0428 -0.1610 0.0134  22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.6994 0.1509 0.2987 -0.0406 -0.1568 0.0117  22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.8057 0.1091 0.2567 -0.0670 -0.1824 0.0181  22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.5947 0.1809 0.4322 -0.0446 -0.2264 0.0400  23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.5606 0.1896 0.5007 -0.0499 -0.2523 0.0555  23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.6102 0.1760 0.5290 -0.0755 -0.3104 0.0780  23  ALA   A C   
132  O O   . ALA   A 17  ? 0.6597 0.1548 0.4778 -0.0858 -0.3199 0.0755  23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.5187 0.2113 0.5137 -0.0328 -0.2168 0.0457  23  ALA   A CB  
134  N N   . THR   A 18  ? 0.5928 0.1800 0.6097 -0.0872 -0.3483 0.1025  24  THR   A N   
135  C CA  . THR   A 18  ? 0.6388 0.1711 0.6594 -0.1165 -0.4157 0.1333  24  THR   A CA  
136  C C   . THR   A 18  ? 0.6317 0.1919 0.7165 -0.1154 -0.4216 0.1434  24  THR   A C   
137  O O   . THR   A 18  ? 0.5931 0.2145 0.7176 -0.0916 -0.3712 0.1250  24  THR   A O   
138  C CB  . THR   A 18  ? 0.6249 0.1671 0.7364 -0.1309 -0.4572 0.1622  24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.5559 0.1861 0.8208 -0.1130 -0.4305 0.1694  24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.6650 0.1867 0.7215 -0.1306 -0.4487 0.1516  24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.6677 0.1787 0.7610 -0.1441 -0.4866 0.1748  25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.6595 0.1957 0.8246 -0.1455 -0.4981 0.1894  25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.5679 0.1989 0.9067 -0.1268 -0.4700 0.2000  25  HIS   A C   
144  O O   . HIS   A 19  ? 0.5334 0.2112 0.9257 -0.1109 -0.4349 0.1923  25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.7291 0.1912 0.8808 -0.1853 -0.5832 0.2286  25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.8925 0.2412 0.8630 -0.2094 -0.6102 0.2204  25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.9596 0.2863 0.8601 -0.2040 -0.5893 0.2036  25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.9960 0.2386 0.8443 -0.2422 -0.6578 0.2303  25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 1.0662 0.2729 0.8033 -0.2316 -0.6178 0.2018  25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 1.0978 0.2458 0.7914 -0.2565 -0.6589 0.2170  25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.5285 0.1795 0.9524 -0.1302 -0.4833 0.2190  26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.4533 0.1803 1.0408 -0.1132 -0.4488 0.2306  26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.4109 0.1908 0.9868 -0.0819 -0.3647 0.1905  26  ASN   A C   
154  O O   . ASN   A 20  ? 0.3777 0.2037 1.0422 -0.0678 -0.3233 0.1897  26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.4758 0.2034 1.1394 -0.1232 -0.4775 0.2572  26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.4783 0.2724 1.3227 -0.1076 -0.4408 0.2758  26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.4505 0.2648 1.4163 -0.1113 -0.4521 0.3064  26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.4816 0.3053 1.3485 -0.0905 -0.3930 0.2591  26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.4131 0.1793 0.8751 -0.0735 -0.3403 0.1592  27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.3684 0.1751 0.8018 -0.0498 -0.2714 0.1242  27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.3471 0.1665 0.7618 -0.0423 -0.2484 0.1121  27  ASP   A C   
162  O O   . ASP   A 21  ? 0.3181 0.1783 0.7819 -0.0293 -0.2010 0.1015  27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.4061 0.1875 0.7203 -0.0463 -0.2617 0.1006  27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.4203 0.2030 0.7541 -0.0480 -0.2654 0.1046  27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.3711 0.1955 0.7998 -0.0399 -0.2391 0.1085  27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.4781 0.2128 0.7279 -0.0582 -0.2921 0.1038  27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.3729 0.1493 0.7128 -0.0528 -0.2816 0.1146  28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.3725 0.1575 0.6932 -0.0467 -0.2643 0.1049  28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.3476 0.1616 0.7867 -0.0491 -0.2682 0.1264  28  TRP   A C   
170  O O   . TRP   A 22  ? 0.3375 0.1791 0.7923 -0.0386 -0.2326 0.1150  28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.4118 0.1326 0.6151 -0.0579 -0.2950 0.1022  28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.4214 0.1273 0.5198 -0.0461 -0.2613 0.0754  28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.4700 0.1283 0.4854 -0.0510 -0.2683 0.0701  28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.3994 0.1381 0.4761 -0.0281 -0.2144 0.0544  28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.4853 0.1488 0.4394 -0.0347 -0.2245 0.0481  28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.4436 0.1579 0.4371 -0.0215 -0.1947 0.0400  28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.3684 0.1525 0.4910 -0.0186 -0.1874 0.0487  28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.4410 0.1787 0.4079 -0.0059 -0.1541 0.0247  28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.3838 0.1847 0.4644 -0.0060 -0.1516 0.0317  28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.4086 0.1907 0.4208 0.0004  -0.1366 0.0218  28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.3423 0.1484 0.8699 -0.0638 -0.3111 0.1602  29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.3143 0.1490 0.9768 -0.0656 -0.3128 0.1871  29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.2790 0.1653 1.0447 -0.0469 -0.2459 0.1810  29  ALA   A C   
184  O O   . ALA   A 23  ? 0.2610 0.1710 1.1227 -0.0420 -0.2198 0.1926  29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.3004 0.1085 1.0373 -0.0900 -0.3852 0.2327  29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.2658 0.1609 1.0099 -0.0384 -0.2168 0.1644  30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.2220 0.1486 1.0362 -0.0238 -0.1495 0.1549  30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.2231 0.1535 0.9259 -0.0130 -0.1007 0.1138  30  ASN   A C   
189  O O   . ASN   A 24  ? 0.2164 0.1548 0.9270 -0.0067 -0.0605 0.1021  30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.2175 0.1485 1.1190 -0.0260 -0.1585 0.1766  30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.2368 0.1712 1.2858 -0.0370 -0.1995 0.2252  30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.2303 0.1832 1.3905 -0.0317 -0.1696 0.2418  30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.2450 0.1574 1.3012 -0.0545 -0.2694 0.2521  30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.2304 0.1520 0.8337 -0.0128 -0.1072 0.0956  31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.2289 0.1534 0.7310 -0.0061 -0.0746 0.0644  31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.2080 0.1450 0.7272 -0.0016 -0.0127 0.0499  31  LEU   A C   
197  O O   . LEU   A 25  ? 0.1949 0.1342 0.7627 -0.0018 0.0081  0.0554  31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.2437 0.1559 0.6676 -0.0074 -0.0956 0.0574  31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.2678 0.1855 0.6028 -0.0016 -0.0677 0.0329  31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.2816 0.1933 0.5581 0.0008  -0.0709 0.0236  31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.2741 0.1816 0.5586 -0.0014 -0.0819 0.0306  31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.2074 0.1440 0.6749 -0.0003 0.0165  0.0313  32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.2060 0.1355 0.6535 -0.0028 0.0720  0.0153  32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.2380 0.1656 0.5804 -0.0070 0.0713  -0.0022 32  VAL   A C   
205  O O   . VAL   A 26  ? 0.2673 0.1855 0.5843 -0.0128 0.0943  -0.0090 32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.2121 0.1340 0.6765 -0.0032 0.1017  0.0111  32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.2521 0.1487 0.6565 -0.0121 0.1541  -0.0083 32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.1740 0.0977 0.7614 0.0012  0.1114  0.0325  32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.2271 0.1613 0.5154 -0.0047 0.0440  -0.0059 33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.2292 0.1658 0.4386 -0.0076 0.0403  -0.0152 33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.2083 0.1492 0.3873 -0.0002 0.0076  -0.0120 33  TRP   A C   
212  O O   . TRP   A 27  ? 0.1980 0.1353 0.3952 0.0027  -0.0048 -0.0081 33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.2403 0.1666 0.4119 -0.0186 0.0709  -0.0257 33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.2693 0.2006 0.3749 -0.0245 0.0598  -0.0279 33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.2988 0.2285 0.3667 -0.0329 0.0572  -0.0266 33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.2729 0.2129 0.3544 -0.0227 0.0478  -0.0271 33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.3128 0.2516 0.3440 -0.0371 0.0429  -0.0218 33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.2999 0.2454 0.3392 -0.0303 0.0389  -0.0225 33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.2646 0.2079 0.3610 -0.0161 0.0427  -0.0273 33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.3034 0.2594 0.3236 -0.0305 0.0279  -0.0166 33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.2794 0.2303 0.3450 -0.0162 0.0337  -0.0255 33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.2916 0.2499 0.3237 -0.0227 0.0275  -0.0195 33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.1992 0.1419 0.3332 0.0023  -0.0031 -0.0121 34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.2049 0.1409 0.3034 0.0095  -0.0207 -0.0096 34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.2090 0.1548 0.2711 0.0104  -0.0133 -0.0087 34  GLU   A C   
226  O O   . GLU   A 28  ? 0.2036 0.1571 0.2646 0.0051  -0.0069 -0.0080 34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.2118 0.1226 0.3065 0.0132  -0.0475 -0.0028 34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.2306 0.1379 0.3313 0.0124  -0.0535 0.0005  34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.2827 0.1877 0.3419 0.0174  -0.0479 -0.0002 34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.2757 0.1896 0.3451 0.0155  -0.0441 0.0004  34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.2969 0.1908 0.3193 0.0234  -0.0441 0.0001  34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.2120 0.1567 0.2517 0.0157  -0.0136 -0.0059 35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.2111 0.1674 0.2373 0.0175  -0.0075 0.0022  35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.2194 0.1564 0.2262 0.0302  -0.0052 0.0071  35  ASP   A C   
235  O O   . ASP   A 29  ? 0.2262 0.1595 0.2273 0.0321  -0.0020 0.0062  35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.2326 0.2080 0.2607 0.0047  -0.0015 0.0051  35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.3086 0.2989 0.3383 0.0006  -0.0038 0.0212  35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.2981 0.2874 0.3352 0.0139  -0.0015 0.0309  35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.3572 0.3538 0.3801 -0.0181 -0.0076 0.0263  35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.2133 0.1314 0.2060 0.0385  -0.0024 0.0119  36  SER   A N   
241  C CA  A SER   A 30  ? 0.2354 0.1175 0.1989 0.0501  0.0106  0.0161  36  SER   A CA  
242  C CA  B SER   A 30  ? 0.2365 0.1185 0.1996 0.0498  0.0102  0.0157  36  SER   A CA  
243  C C   . SER   A 30  ? 0.2251 0.1280 0.2104 0.0552  0.0286  0.0282  36  SER   A C   
244  O O   . SER   A 30  ? 0.2406 0.1175 0.2072 0.0624  0.0428  0.0292  36  SER   A O   
245  C CB  A SER   A 30  ? 0.2534 0.1111 0.2014 0.0566  0.0174  0.0204  36  SER   A CB  
246  C CB  B SER   A 30  ? 0.2641 0.1133 0.2040 0.0563  0.0161  0.0185  36  SER   A CB  
247  O OG  A SER   A 30  ? 0.3092 0.1018 0.2007 0.0600  0.0208  0.0159  36  SER   A OG  
248  O OG  B SER   A 30  ? 0.2684 0.1496 0.2428 0.0594  0.0257  0.0304  36  SER   A OG  
249  N N   . SER   A 31  ? 0.1997 0.1449 0.2243 0.0489  0.0261  0.0403  37  SER   A N   
250  C CA  . SER   A 31  ? 0.1967 0.1646 0.2556 0.0502  0.0356  0.0592  37  SER   A CA  
251  C C   . SER   A 31  ? 0.1841 0.1602 0.2400 0.0442  0.0321  0.0545  37  SER   A C   
252  O O   . SER   A 31  ? 0.1754 0.1621 0.2574 0.0476  0.0419  0.0701  37  SER   A O   
253  C CB  . SER   A 31  ? 0.2121 0.2154 0.3097 0.0382  0.0231  0.0783  37  SER   A CB  
254  O OG  . SER   A 31  ? 0.2620 0.2819 0.3502 0.0167  0.0030  0.0729  37  SER   A OG  
255  N N   . ARG   A 32  ? 0.1719 0.1441 0.2053 0.0357  0.0199  0.0363  38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.1629 0.1392 0.1920 0.0303  0.0179  0.0303  38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.1896 0.1325 0.1901 0.0385  0.0199  0.0175  38  ARG   A C   
258  O O   . ARG   A 32  ? 0.1918 0.1353 0.1893 0.0360  0.0193  0.0135  38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.1548 0.1448 0.1829 0.0124  0.0071  0.0215  38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.1375 0.1461 0.1746 -0.0043 -0.0005 0.0352  38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.1740 0.1746 0.1893 -0.0253 -0.0029 0.0243  38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.1786 0.1731 0.1832 -0.0316 0.0017  0.0164  38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.2284 0.2068 0.2060 -0.0535 0.0048  0.0112  38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.2254 0.1874 0.1771 -0.0734 0.0031  0.0129  38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.2526 0.2227 0.2214 -0.0573 0.0117  0.0038  38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.2171 0.1258 0.1921 0.0446  0.0178  0.0121  39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.2416 0.1051 0.1787 0.0453  0.0095  0.0036  39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.2302 0.1084 0.1877 0.0352  -0.0097 -0.0041 39  ASP   A C   
269  O O   . ASP   A 33  ? 0.2411 0.1002 0.1856 0.0332  -0.0170 -0.0068 39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.2674 0.0979 0.1735 0.0522  0.0268  0.0063  39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.3596 0.1291 0.2100 0.0473  0.0140  -0.0007 39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.3681 0.0973 0.1853 0.0419  -0.0015 -0.0026 39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.4060 0.1652 0.2442 0.0458  0.0155  -0.0023 39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.2116 0.1193 0.2024 0.0288  -0.0137 -0.0063 40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.1998 0.1160 0.2211 0.0211  -0.0215 -0.0115 40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.2165 0.1271 0.2615 0.0181  -0.0329 -0.0105 40  LEU   A C   
277  O O   . LEU   A 34  ? 0.2311 0.1464 0.2734 0.0189  -0.0302 -0.0094 40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.1784 0.1233 0.2189 0.0131  -0.0058 -0.0150 40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.1883 0.1422 0.2174 0.0111  0.0017  -0.0143 40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.1652 0.1312 0.1970 -0.0034 0.0140  -0.0173 40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.1995 0.1380 0.2287 0.0147  -0.0054 -0.0169 40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.2182 0.1209 0.2958 0.0140  -0.0461 -0.0082 41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.2137 0.1156 0.3355 0.0102  -0.0564 -0.0024 41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.2035 0.1176 0.3872 0.0067  -0.0480 0.0000  41  LEU   A C   
285  O O   . LEU   A 35  ? 0.2143 0.1231 0.4014 0.0061  -0.0541 0.0015  41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.2332 0.0972 0.3364 0.0067  -0.0917 0.0079  41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.2356 0.1000 0.3914 0.0013  -0.1078 0.0187  41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.2777 0.1049 0.3851 -0.0025 -0.1326 0.0238  41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.2289 0.0907 0.4540 -0.0061 -0.1293 0.0343  41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.1916 0.1186 0.4244 0.0046  -0.0279 0.0004  42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.1835 0.1152 0.4863 0.0028  -0.0089 0.0047  42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.1839 0.1148 0.5662 0.0017  -0.0187 0.0215  42  VAL   A C   
293  O O   . VAL   A 36  ? 0.1696 0.1022 0.5506 0.0014  -0.0134 0.0208  42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.1892 0.1234 0.4791 -0.0010 0.0381  -0.0092 42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.1766 0.1045 0.5419 -0.0015 0.0680  -0.0041 42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.2038 0.1395 0.4251 -0.0032 0.0401  -0.0198 42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.1905 0.1189 0.6469 0.0001  -0.0365 0.0398  43  SER   A N   
298  C CA  . SER   A 37  ? 0.2081 0.1385 0.7633 -0.0023 -0.0487 0.0635  43  SER   A CA  
299  C C   . SER   A 37  ? 0.2236 0.1622 0.8871 0.0007  -0.0117 0.0749  43  SER   A C   
300  O O   . SER   A 37  ? 0.2045 0.1422 0.8585 0.0030  0.0114  0.0657  43  SER   A O   
301  C CB  . SER   A 37  ? 0.2306 0.1425 0.7905 -0.0117 -0.1147 0.0860  43  SER   A CB  
302  O OG  . SER   A 37  ? 0.2654 0.1649 0.8101 -0.0157 -0.1385 0.0906  43  SER   A OG  
303  N N   . SER   A 38  ? 0.2421 0.1861 1.0127 0.0011  -0.0024 0.0964  44  SER   A N   
304  C CA  . SER   A 38  ? 0.2637 0.2107 1.1525 0.0059  0.0429  0.1109  44  SER   A CA  
305  C C   . SER   A 38  ? 0.2791 0.2325 1.2740 0.0023  0.0000  0.1462  44  SER   A C   
306  O O   . SER   A 38  ? 0.2895 0.2401 1.2868 -0.0080 -0.0697 0.1672  44  SER   A O   
307  C CB  . SER   A 38  ? 0.2659 0.2129 1.2323 0.0091  0.0835  0.1201  44  SER   A CB  
308  O OG  . SER   A 38  ? 0.2914 0.2482 1.3070 0.0035  0.0268  0.1464  44  SER   A OG  
309  N N   . THR   A 39  ? 0.2861 0.2405 1.3624 0.0081  0.0399  0.1541  45  THR   A N   
310  C CA  . THR   A 39  ? 0.2935 0.2553 1.4853 0.0040  0.0003  0.1920  45  THR   A CA  
311  C C   . THR   A 39  ? 0.2876 0.2563 1.6537 0.0125  0.0532  0.2207  45  THR   A C   
312  O O   . THR   A 39  ? 0.2993 0.2555 1.6666 0.0225  0.1366  0.2009  45  THR   A O   
313  C CB  . THR   A 39  ? 0.3297 0.2855 1.4602 0.0031  -0.0102 0.1791  45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.3477 0.2974 1.4854 0.0137  0.0685  0.1594  45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.3857 0.3308 1.3504 -0.0027 -0.0476 0.1505  45  THR   A CG2 
316  N N   . THR   A 40  ? 0.2702 0.2515 1.7823 0.0065  0.0071  0.2695  46  THR   A N   
317  C CA  . THR   A 40  ? 0.2355 0.2255 1.9405 0.0160  0.0584  0.3049  46  THR   A CA  
318  C C   . THR   A 40  ? 0.2481 0.2312 1.9896 0.0249  0.1061  0.3011  46  THR   A C   
319  O O   . THR   A 40  ? 0.2338 0.2083 2.0831 0.0381  0.1895  0.3088  46  THR   A O   
320  C CB  . THR   A 40  ? 0.2049 0.2130 2.0711 0.0034  -0.0164 0.3673  46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.2407 0.2454 2.0820 -0.0132 -0.1026 0.3856  46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.2141 0.2244 2.0573 -0.0061 -0.0581 0.3744  46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.2685 0.2503 1.9282 0.0171  0.0549  0.2925  47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.2599 0.2353 1.9451 0.0241  0.0920  0.2886  47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.3138 0.2661 1.8322 0.0305  0.1541  0.2309  47  ALA   A C   
326  O O   . ALA   A 41  ? 0.3673 0.3140 1.7396 0.0264  0.1432  0.1975  47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.2626 0.2447 1.9516 0.0101  0.0028  0.3128  47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.3027 0.2381 1.8462 0.0389  0.2186  0.2222  48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.3585 0.2633 1.7492 0.0402  0.2755  0.1728  48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.3801 0.2924 1.6473 0.0328  0.2190  0.1536  48  GLN   A C   
331  O O   . GLN   A 42  ? 0.3623 0.2894 1.6870 0.0304  0.1710  0.1773  48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.3755 0.2452 1.8345 0.0496  0.3731  0.1712  48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.4946 0.3106 1.8220 0.0469  0.4568  0.1275  48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.5596 0.3598 1.9194 0.0488  0.4996  0.1301  48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 0.5391 0.3430 2.0650 0.0586  0.5318  0.1645  48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.6122 0.3937 1.8219 0.0389  0.5017  0.0968  48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.4140 0.3135 1.5172 0.0280  0.2262  0.1134  49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.4328 0.3357 1.4132 0.0222  0.1867  0.0924  49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.4319 0.3056 1.3527 0.0221  0.2480  0.0669  49  GLY   A C   
340  O O   . GLY   A 43  ? 0.4477 0.2871 1.3377 0.0209  0.3165  0.0492  49  GLY   A O   
341  N N   . CYS   A 44  ? 0.4198 0.2982 1.3115 0.0206  0.2236  0.0642  50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.4297 0.2772 1.2702 0.0188  0.2778  0.0432  50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.4434 0.2884 1.1338 0.0097  0.2559  0.0152  50  CYS   A C   
344  O O   . CYS   A 44  ? 0.4684 0.2908 1.1176 0.0059  0.2847  0.0021  50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.4176 0.2669 1.3735 0.0255  0.2862  0.0665  50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.4641 0.2984 1.6052 0.0368  0.3531  0.0973  50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.4213 0.2864 1.0350 0.0061  0.2085  0.0078  51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.4322 0.2974 0.9220 -0.0016 0.1906  -0.0132 51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.4390 0.2682 0.8450 -0.0133 0.2411  -0.0354 51  ASP   A C   
350  O O   . ASP   A 45  ? 0.4520 0.2659 0.8582 -0.0160 0.2668  -0.0380 51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.4582 0.3492 0.9002 -0.0010 0.1332  -0.0114 51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.5002 0.4065 0.9653 0.0024  0.0773  0.0044  51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.5188 0.4225 0.9864 0.0021  0.0729  0.0056  51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.5162 0.4293 0.9865 0.0028  0.0373  0.0155  51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.4402 0.2502 0.7700 -0.0234 0.2522  -0.0495 52  THR   A N   
356  C CA  . THR   A 46  ? 0.4699 0.2338 0.7004 -0.0425 0.2888  -0.0677 52  THR   A CA  
357  C C   . THR   A 46  ? 0.4490 0.2355 0.5974 -0.0506 0.2442  -0.0716 52  THR   A C   
358  O O   . THR   A 46  ? 0.4371 0.2599 0.5806 -0.0442 0.2010  -0.0666 52  THR   A O   
359  C CB  . THR   A 46  ? 0.5232 0.2506 0.7139 -0.0526 0.3169  -0.0768 52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.5470 0.2383 0.8087 -0.0470 0.3756  -0.0741 52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.5787 0.2575 0.6392 -0.0800 0.3296  -0.0923 52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.4414 0.2036 0.5304 -0.0648 0.2564  -0.0782 53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.4331 0.2165 0.4577 -0.0732 0.2157  -0.0770 53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.4631 0.2055 0.3902 -0.1005 0.2217  -0.0836 53  ILE   A C   
365  O O   . ILE   A 47  ? 0.5016 0.1792 0.3799 -0.1198 0.2648  -0.0934 53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.4311 0.2178 0.4549 -0.0737 0.2132  -0.0752 53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.3970 0.2165 0.5178 -0.0506 0.2057  -0.0661 53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.4413 0.2515 0.4116 -0.0813 0.1720  -0.0700 53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.3780 0.2456 0.5321 -0.0341 0.1553  -0.0557 53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.4412 0.2133 0.3392 -0.1041 0.1806  -0.0765 54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.4708 0.2082 0.2838 -0.1333 0.1738  -0.0758 54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.5026 0.2089 0.2501 -0.1586 0.1670  -0.0723 54  ALA   A C   
373  O O   . ALA   A 48  ? 0.4788 0.2185 0.2538 -0.1482 0.1488  -0.0657 54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.4366 0.2211 0.2592 -0.1275 0.1318  -0.0636 54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.5673 0.2036 0.2217 -0.1945 0.1788  -0.0753 55  ARG   A N   
376  C CA  . ARG   A 49  ? 0.6255 0.2176 0.1993 -0.2280 0.1648  -0.0686 55  ARG   A CA  
377  C C   . ARG   A 49  ? 0.6771 0.2497 0.1857 -0.2604 0.1262  -0.0535 55  ARG   A C   
378  O O   . ARG   A 49  ? 0.7600 0.2520 0.1794 -0.2930 0.1445  -0.0603 55  ARG   A O   
379  C CB  . ARG   A 49  ? 0.6955 0.1952 0.2025 -0.2482 0.2207  -0.0858 55  ARG   A CB  
380  C CG  . ARG   A 49  ? 0.6778 0.1983 0.2660 -0.2164 0.2604  -0.0959 55  ARG   A CG  
381  C CD  . ARG   A 49  ? 0.6418 0.2338 0.2943 -0.1947 0.2262  -0.0855 55  ARG   A CD  
382  N NE  . ARG   A 49  ? 0.6100 0.2188 0.3441 -0.1669 0.2606  -0.0923 55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.5617 0.2307 0.3661 -0.1430 0.2379  -0.0852 55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.5150 0.2318 0.3181 -0.1406 0.1878  -0.0731 55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.5322 0.2110 0.4131 -0.1220 0.2660  -0.0876 55  ARG   A NH2 
386  N N   . CYS   A 50  ? 0.6351 0.2771 0.1918 -0.2516 0.0755  -0.0314 56  CYS   A N   
387  C CA  . CYS   A 50  ? 0.6510 0.2910 0.1781 -0.2767 0.0356  -0.0109 56  CYS   A CA  
388  C C   . CYS   A 50  ? 0.6249 0.3335 0.2123 -0.2706 -0.0157 0.0203  56  CYS   A C   
389  O O   . CYS   A 50  ? 0.5884 0.3461 0.2374 -0.2431 -0.0159 0.0218  56  CYS   A O   
390  C CB  . CYS   A 50  ? 0.6295 0.2920 0.1925 -0.2563 0.0499  -0.0200 56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.5700 0.3340 0.2589 -0.2006 0.0455  -0.0190 56  CYS   A SG  
392  N N   . ASP   A 51  ? 0.6316 0.3454 0.2126 -0.2932 -0.0555 0.0465  57  ASP   A N   
393  C CA  . ASP   A 51  ? 0.5875 0.3664 0.2446 -0.2861 -0.0980 0.0815  57  ASP   A CA  
394  C C   . ASP   A 51  ? 0.5383 0.3673 0.2597 -0.2627 -0.0998 0.0883  57  ASP   A C   
395  O O   . ASP   A 51  ? 0.5249 0.3844 0.2906 -0.2713 -0.1348 0.1222  57  ASP   A O   
396  C CB  . ASP   A 51  ? 0.6550 0.3979 0.2665 -0.3370 -0.1501 0.1174  57  ASP   A CB  
397  C CG  . ASP   A 51  ? 0.8093 0.5053 0.3615 -0.3782 -0.1777 0.1328  57  ASP   A CG  
398  O OD1 . ASP   A 51  ? 0.8481 0.5270 0.3758 -0.3698 -0.1486 0.1093  57  ASP   A OD1 
399  O OD2 . ASP   A 51  ? 0.8799 0.5550 0.4129 -0.4206 -0.2322 0.1714  57  ASP   A OD2 
400  N N   . CYS   A 52  ? 0.5081 0.3419 0.2376 -0.2353 -0.0630 0.0594  58  CYS   A N   
401  C CA  . CYS   A 52  ? 0.4442 0.3179 0.2253 -0.2125 -0.0605 0.0619  58  CYS   A CA  
402  C C   . CYS   A 52  ? 0.3566 0.2946 0.2259 -0.1832 -0.0702 0.0823  58  CYS   A C   
403  O O   . CYS   A 52  ? 0.3423 0.2981 0.2377 -0.1635 -0.0607 0.0776  58  CYS   A O   
404  C CB  . CYS   A 52  ? 0.4452 0.3126 0.2265 -0.1866 -0.0211 0.0286  58  CYS   A CB  
405  S SG  . CYS   A 52  ? 0.4908 0.2899 0.1933 -0.2132 -0.0008 0.0098  58  CYS   A SG  
406  N N   . GLN   A 53  ? 0.3089 0.2759 0.2226 -0.1798 -0.0838 0.1043  59  GLN   A N   
407  C CA  . GLN   A 53  ? 0.2594 0.2768 0.2569 -0.1495 -0.0796 0.1229  59  GLN   A CA  
408  C C   . GLN   A 53  ? 0.2291 0.2611 0.2502 -0.1229 -0.0571 0.1120  59  GLN   A C   
409  O O   . GLN   A 53  ? 0.2002 0.2612 0.2823 -0.1057 -0.0520 0.1326  59  GLN   A O   
410  C CB  . GLN   A 53  ? 0.2525 0.2931 0.3050 -0.1681 -0.1136 0.1699  59  GLN   A CB  
411  C CG  . GLN   A 53  ? 0.2907 0.3305 0.3495 -0.1827 -0.1341 0.1875  59  GLN   A CG  
412  C CD  . GLN   A 53  ? 0.3153 0.3846 0.4535 -0.1984 -0.1693 0.2414  59  GLN   A CD  
413  O OE1 . GLN   A 53  ? 0.3472 0.3951 0.4632 -0.2409 -0.2141 0.2687  59  GLN   A OE1 
414  N NE2 . GLN   A 53  ? 0.2637 0.3761 0.4970 -0.1666 -0.1494 0.2608  59  GLN   A NE2 
415  N N   . THR   A 54  ? 0.2409 0.2479 0.2153 -0.1226 -0.0428 0.0831  60  THR   A N   
416  C CA  . THR   A 54  ? 0.2289 0.2418 0.2146 -0.1003 -0.0240 0.0699  60  THR   A CA  
417  C C   . THR   A 54  ? 0.2280 0.2192 0.1832 -0.0879 -0.0039 0.0365  60  THR   A C   
418  O O   . THR   A 54  ? 0.2446 0.2096 0.1629 -0.1032 -0.0009 0.0232  60  THR   A O   
419  C CB  . THR   A 54  ? 0.2652 0.2730 0.2415 -0.1175 -0.0346 0.0789  60  THR   A CB  
420  O OG1 . THR   A 54  ? 0.3203 0.2884 0.2331 -0.1399 -0.0339 0.0597  60  THR   A OG1 
421  C CG2 . THR   A 54  ? 0.2522 0.2795 0.2668 -0.1372 -0.0626 0.1190  60  THR   A CG2 
422  N N   . GLY   A 55  ? 0.2066 0.2023 0.1775 -0.0628 0.0100  0.0259  61  GLY   A N   
423  C CA  . GLY   A 55  ? 0.2201 0.1984 0.1796 -0.0516 0.0216  0.0023  61  GLY   A CA  
424  C C   . GLY   A 55  ? 0.2129 0.1885 0.1825 -0.0300 0.0271  -0.0022 61  GLY   A C   
425  O O   . GLY   A 55  ? 0.2137 0.1957 0.1910 -0.0242 0.0291  0.0090  61  GLY   A O   
426  N N   . VAL   A 56  ? 0.2049 0.1648 0.1736 -0.0212 0.0287  -0.0163 62  VAL   A N   
427  C CA  . VAL   A 56  ? 0.2094 0.1513 0.1738 -0.0079 0.0259  -0.0200 62  VAL   A CA  
428  C C   . VAL   A 56  ? 0.2108 0.1386 0.1751 0.0000  0.0199  -0.0228 62  VAL   A C   
429  O O   . VAL   A 56  ? 0.1980 0.1290 0.1791 -0.0036 0.0180  -0.0282 62  VAL   A O   
430  C CB  . VAL   A 56  ? 0.2293 0.1600 0.1980 -0.0114 0.0233  -0.0285 62  VAL   A CB  
431  C CG1 . VAL   A 56  ? 0.2550 0.1590 0.2129 -0.0032 0.0120  -0.0288 62  VAL   A CG1 
432  C CG2 . VAL   A 56  ? 0.2393 0.1792 0.2014 -0.0210 0.0289  -0.0262 62  VAL   A CG2 
433  N N   . TYR   A 57  ? 0.2254 0.1296 0.1668 0.0093  0.0193  -0.0189 63  TYR   A N   
434  C CA  . TYR   A 57  ? 0.2460 0.1262 0.1756 0.0131  0.0099  -0.0205 63  TYR   A CA  
435  C C   . TYR   A 57  ? 0.2890 0.1200 0.1840 0.0120  -0.0061 -0.0213 63  TYR   A C   
436  O O   . TYR   A 57  ? 0.3021 0.1132 0.1712 0.0121  -0.0014 -0.0204 63  TYR   A O   
437  C CB  . TYR   A 57  ? 0.2428 0.1219 0.1617 0.0204  0.0234  -0.0137 63  TYR   A CB  
438  C CG  . TYR   A 57  ? 0.2852 0.1271 0.1670 0.0282  0.0406  -0.0080 63  TYR   A CG  
439  C CD1 . TYR   A 57  ? 0.2863 0.1420 0.1802 0.0315  0.0595  0.0007  63  TYR   A CD1 
440  C CD2 . TYR   A 57  ? 0.3420 0.1282 0.1751 0.0309  0.0417  -0.0096 63  TYR   A CD2 
441  C CE1 . TYR   A 57  ? 0.3255 0.1421 0.1915 0.0402  0.0859  0.0074  63  TYR   A CE1 
442  C CE2 . TYR   A 57  ? 0.3899 0.1256 0.1772 0.0369  0.0680  -0.0055 63  TYR   A CE2 
443  C CZ  . TYR   A 57  ? 0.3889 0.1411 0.1969 0.0431  0.0936  0.0028  63  TYR   A CZ  
444  O OH  . TYR   A 57  ? 0.4585 0.1574 0.2286 0.0505  0.1293  0.0082  63  TYR   A OH  
445  N N   . TYR   A 58  ? 0.3099 0.1169 0.2023 0.0082  -0.0275 -0.0207 64  TYR   A N   
446  C CA  . TYR   A 58  ? 0.3713 0.1209 0.2233 0.0001  -0.0529 -0.0167 64  TYR   A CA  
447  C C   . TYR   A 58  ? 0.4284 0.1181 0.2054 0.0002  -0.0466 -0.0155 64  TYR   A C   
448  O O   . TYR   A 58  ? 0.4115 0.1013 0.1859 0.0037  -0.0415 -0.0154 64  TYR   A O   
449  C CB  . TYR   A 58  ? 0.3671 0.1159 0.2625 -0.0086 -0.0861 -0.0101 64  TYR   A CB  
450  C CG  . TYR   A 58  ? 0.4233 0.1075 0.2765 -0.0234 -0.1234 0.0000  64  TYR   A CG  
451  C CD1 . TYR   A 58  ? 0.4572 0.1211 0.2933 -0.0295 -0.1321 0.0021  64  TYR   A CD1 
452  C CD2 . TYR   A 58  ? 0.4756 0.1093 0.2927 -0.0347 -0.1522 0.0085  64  TYR   A CD2 
453  C CE1 . TYR   A 58  ? 0.5223 0.1170 0.3090 -0.0482 -0.1716 0.0138  64  TYR   A CE1 
454  C CE2 . TYR   A 58  ? 0.5378 0.0981 0.3012 -0.0554 -0.1938 0.0210  64  TYR   A CE2 
455  C CZ  . TYR   A 58  ? 0.5792 0.1188 0.3261 -0.0628 -0.2041 0.0239  64  TYR   A CZ  
456  O OH  . TYR   A 58  ? 0.6808 0.1375 0.3620 -0.0878 -0.2487 0.0379  64  TYR   A OH  
457  N N   . CYS   A 59  ? 0.4946 0.1246 0.2042 -0.0047 -0.0430 -0.0149 65  CYS   A N   
458  C CA  . CYS   A 59  ? 0.5730 0.1258 0.1958 -0.0065 -0.0266 -0.0150 65  CYS   A CA  
459  C C   . CYS   A 59  ? 0.6557 0.1191 0.2019 -0.0290 -0.0662 -0.0103 65  CYS   A C   
460  O O   . CYS   A 59  ? 0.6896 0.1093 0.1915 -0.0390 -0.0736 -0.0091 65  CYS   A O   
461  C CB  . CYS   A 59  ? 0.5971 0.1360 0.1933 0.0040  0.0187  -0.0163 65  CYS   A CB  
462  S SG  . CYS   A 59  ? 0.7056 0.1283 0.1862 0.0023  0.0562  -0.0167 65  CYS   A SG  
463  N N   . SER   A 60  ? 0.6835 0.1178 0.2147 -0.0403 -0.0968 -0.0050 66  SER   A N   
464  C CA  . SER   A 60  ? 0.7649 0.1112 0.2267 -0.0683 -0.1469 0.0055  66  SER   A CA  
465  C C   . SER   A 60  ? 0.8751 0.1001 0.1962 -0.0830 -0.1322 0.0025  66  SER   A C   
466  O O   . SER   A 60  ? 0.9277 0.0820 0.1882 -0.1081 -0.1710 0.0111  66  SER   A O   
467  C CB  . SER   A 60  ? 0.7941 0.1320 0.2717 -0.0799 -0.1856 0.0153  66  SER   A CB  
468  O OG  . SER   A 60  ? 0.8589 0.1888 0.3083 -0.0686 -0.1523 0.0072  66  SER   A OG  
469  N N   . SER   A 61  ? 0.9054 0.1018 0.1767 -0.0683 -0.0737 -0.0076 67  SER   A N   
470  C CA  . SER   A 61  ? 1.0112 0.0803 0.1439 -0.0804 -0.0431 -0.0118 67  SER   A CA  
471  C C   . SER   A 61  ? 1.0230 0.0826 0.1409 -0.0804 -0.0283 -0.0137 67  SER   A C   
472  O O   . SER   A 61  ? 1.1200 0.0615 0.1140 -0.0971 -0.0125 -0.0158 67  SER   A O   
473  C CB  . SER   A 61  ? 1.0364 0.0801 0.1395 -0.0615 0.0249  -0.0190 67  SER   A CB  
474  O OG  . SER   A 61  ? 0.9845 0.1249 0.1865 -0.0309 0.0735  -0.0208 67  SER   A OG  
475  N N   . ARG   A 62  ? 0.9343 0.1070 0.1678 -0.0649 -0.0343 -0.0131 68  ARG   A N   
476  C CA  . ARG   A 62  ? 0.9336 0.1029 0.1599 -0.0665 -0.0280 -0.0139 68  ARG   A CA  
477  C C   . ARG   A 62  ? 0.9144 0.1267 0.1994 -0.0798 -0.0896 -0.0055 68  ARG   A C   
478  O O   . ARG   A 62  ? 0.9171 0.1314 0.2028 -0.0821 -0.0906 -0.0054 68  ARG   A O   
479  C CB  . ARG   A 62  ? 0.8782 0.1361 0.1878 -0.0371 0.0257  -0.0182 68  ARG   A CB  
480  C CG  . ARG   A 62  ? 0.9411 0.1507 0.2050 -0.0232 0.0946  -0.0205 68  ARG   A CG  
481  C CD  . ARG   A 62  ? 1.0427 0.1251 0.1799 -0.0370 0.1220  -0.0230 68  ARG   A CD  
482  N NE  . ARG   A 62  ? 1.1176 0.1541 0.2271 -0.0203 0.1995  -0.0230 68  ARG   A NE  
483  C CZ  . ARG   A 62  ? 1.2217 0.1627 0.2441 -0.0253 0.2278  -0.0255 68  ARG   A CZ  
484  N NH1 . ARG   A 62  ? 1.2805 0.1544 0.2211 -0.0505 0.1787  -0.0283 68  ARG   A NH1 
485  N NH2 . ARG   A 62  ? 1.2417 0.1479 0.2597 -0.0065 0.3064  -0.0228 68  ARG   A NH2 
486  N N   . ARG   A 63  ? 0.8811 0.1349 0.2304 -0.0860 -0.1360 0.0030  69  ARG   A N   
487  C CA  . ARG   A 63  ? 0.8415 0.1473 0.2773 -0.0942 -0.1863 0.0149  69  ARG   A CA  
488  C C   . ARG   A 63  ? 0.7653 0.1625 0.2878 -0.0737 -0.1587 0.0077  69  ARG   A C   
489  O O   . ARG   A 63  ? 0.7595 0.1625 0.3063 -0.0817 -0.1821 0.0141  69  ARG   A O   
490  C CB  . ARG   A 63  ? 0.9395 0.1501 0.3012 -0.1281 -0.2424 0.0305  69  ARG   A CB  
491  C CG  . ARG   A 63  ? 1.0586 0.1945 0.3669 -0.1550 -0.2924 0.0455  69  ARG   A CG  
492  C CD  . ARG   A 63  ? 1.1973 0.2354 0.4329 -0.1942 -0.3568 0.0661  69  ARG   A CD  
493  N NE  . ARG   A 63  ? 1.3699 0.2887 0.4860 -0.2270 -0.3932 0.0764  69  ARG   A NE  
494  C CZ  . ARG   A 63  ? 1.5056 0.2926 0.4959 -0.2698 -0.4439 0.0920  69  ARG   A CZ  
495  N NH1 . ARG   A 63  ? 1.5155 0.2782 0.4888 -0.2831 -0.4639 0.0992  69  ARG   A NH1 
496  N NH2 . ARG   A 63  ? 1.5932 0.2630 0.4631 -0.3022 -0.4751 0.1007  69  ARG   A NH2 
497  N N   . LYS   A 64  ? 0.7006 0.1614 0.2628 -0.0499 -0.1097 -0.0037 70  LYS   A N   
498  C CA  . LYS   A 64  ? 0.6280 0.1638 0.2560 -0.0345 -0.0832 -0.0095 70  LYS   A CA  
499  C C   . LYS   A 64  ? 0.5294 0.1490 0.2346 -0.0175 -0.0593 -0.0142 70  LYS   A C   
500  O O   . LYS   A 64  ? 0.5248 0.1398 0.2182 -0.0124 -0.0475 -0.0151 70  LYS   A O   
501  C CB  . LYS   A 64  ? 0.6938 0.1968 0.2631 -0.0278 -0.0413 -0.0145 70  LYS   A CB  
502  C CG  . LYS   A 64  ? 0.8195 0.2639 0.3304 -0.0409 -0.0522 -0.0128 70  LYS   A CG  
503  C CD  . LYS   A 64  ? 0.9029 0.3584 0.4080 -0.0273 -0.0029 -0.0168 70  LYS   A CD  
504  C CE  . LYS   A 64  ? 1.0132 0.3977 0.4448 -0.0398 -0.0042 -0.0164 70  LYS   A CE  
505  N NZ  . LYS   A 64  ? 1.1268 0.3876 0.4318 -0.0550 0.0037  -0.0166 70  LYS   A NZ  
506  N N   . HIS   A 65  ? 0.4502 0.1356 0.2218 -0.0110 -0.0503 -0.0169 71  HIS   A N   
507  C CA  . HIS   A 65  ? 0.3965 0.1491 0.2252 -0.0011 -0.0288 -0.0205 71  HIS   A CA  
508  C C   . HIS   A 65  ? 0.3955 0.1647 0.2156 0.0066  0.0035  -0.0200 71  HIS   A C   
509  O O   . HIS   A 65  ? 0.4250 0.1790 0.2261 0.0050  0.0081  -0.0195 71  HIS   A O   
510  C CB  . HIS   A 65  ? 0.3587 0.1552 0.2526 -0.0040 -0.0371 -0.0224 71  HIS   A CB  
511  C CG  . HIS   A 65  ? 0.3596 0.1510 0.2915 -0.0095 -0.0628 -0.0176 71  HIS   A CG  
512  N ND1 . HIS   A 65  ? 0.3575 0.1776 0.3309 -0.0066 -0.0568 -0.0188 71  HIS   A ND1 
513  C CD2 . HIS   A 65  ? 0.3750 0.1348 0.3151 -0.0189 -0.0956 -0.0079 71  HIS   A CD2 
514  C CE1 . HIS   A 65  ? 0.3468 0.1552 0.3598 -0.0123 -0.0823 -0.0096 71  HIS   A CE1 
515  N NE2 . HIS   A 65  ? 0.3694 0.1421 0.3665 -0.0207 -0.1097 -0.0008 71  HIS   A NE2 
516  N N   . TYR   A 66  ? 0.3595 0.1598 0.2001 0.0136  0.0234  -0.0169 72  TYR   A N   
517  C CA  . TYR   A 66  ? 0.3459 0.1663 0.1984 0.0195  0.0499  -0.0086 72  TYR   A CA  
518  C C   . TYR   A 66  ? 0.3067 0.1870 0.2120 0.0161  0.0502  -0.0034 72  TYR   A C   
519  O O   . TYR   A 66  ? 0.2762 0.1737 0.1976 0.0148  0.0446  -0.0042 72  TYR   A O   
520  C CB  . TYR   A 66  ? 0.3734 0.1589 0.1989 0.0293  0.0769  -0.0013 72  TYR   A CB  
521  C CG  . TYR   A 66  ? 0.4463 0.1524 0.1978 0.0289  0.0872  -0.0047 72  TYR   A CG  
522  C CD1 . TYR   A 66  ? 0.4859 0.1687 0.2172 0.0297  0.1054  -0.0020 72  TYR   A CD1 
523  C CD2 . TYR   A 66  ? 0.5049 0.1502 0.1979 0.0248  0.0792  -0.0096 72  TYR   A CD2 
524  C CE1 . TYR   A 66  ? 0.5624 0.1567 0.2092 0.0256  0.1177  -0.0056 72  TYR   A CE1 
525  C CE2 . TYR   A 66  ? 0.5801 0.1328 0.1836 0.0184  0.0882  -0.0121 72  TYR   A CE2 
526  C CZ  . TYR   A 66  ? 0.6196 0.1442 0.1967 0.0184  0.1089  -0.0107 72  TYR   A CZ  
527  O OH  . TYR   A 66  ? 0.7268 0.1456 0.2003 0.0087  0.1211  -0.0137 72  TYR   A OH  
528  N N   . PRO   A 67  ? 0.3007 0.2062 0.2266 0.0118  0.0551  0.0037  73  PRO   A N   
529  C CA  . PRO   A 67  ? 0.2684 0.2162 0.2299 0.0019  0.0506  0.0133  73  PRO   A CA  
530  C C   . PRO   A 67  ? 0.2522 0.2144 0.2427 0.0080  0.0638  0.0337  73  PRO   A C   
531  O O   . PRO   A 67  ? 0.2556 0.2018 0.2499 0.0197  0.0858  0.0439  73  PRO   A O   
532  C CB  . PRO   A 67  ? 0.2750 0.2337 0.2420 -0.0074 0.0477  0.0168  73  PRO   A CB  
533  C CG  . PRO   A 67  ? 0.3016 0.2328 0.2510 0.0040  0.0621  0.0176  73  PRO   A CG  
534  C CD  . PRO   A 67  ? 0.3090 0.1989 0.2212 0.0128  0.0629  0.0057  73  PRO   A CD  
535  N N   . VAL   A 68  ? 0.2228 0.2097 0.2351 -0.0001 0.0536  0.0411  74  VAL   A N   
536  C CA  . VAL   A 68  ? 0.2101 0.2139 0.2623 0.0046  0.0621  0.0642  74  VAL   A CA  
537  C C   . VAL   A 68  ? 0.1907 0.2265 0.2722 -0.0162 0.0393  0.0821  74  VAL   A C   
538  O O   . VAL   A 68  ? 0.2040 0.2375 0.2567 -0.0336 0.0213  0.0696  74  VAL   A O   
539  C CB  . VAL   A 68  ? 0.2229 0.2077 0.2610 0.0176  0.0721  0.0565  74  VAL   A CB  
540  C CG1 . VAL   A 68  ? 0.2568 0.1949 0.2602 0.0343  0.0967  0.0484  74  VAL   A CG1 
541  C CG2 . VAL   A 68  ? 0.2401 0.2227 0.2518 0.0093  0.0532  0.0365  74  VAL   A CG2 
542  N N   . SER   A 69  ? 0.1544 0.2124 0.2927 -0.0158 0.0415  0.1137  75  SER   A N   
543  C CA  . SER   A 69  ? 0.1478 0.2305 0.3184 -0.0378 0.0140  0.1390  75  SER   A CA  
544  C C   . SER   A 69  ? 0.1385 0.2228 0.3256 -0.0253 0.0237  0.1419  75  SER   A C   
545  O O   . SER   A 69  ? 0.1344 0.2092 0.3415 -0.0008 0.0552  0.1441  75  SER   A O   
546  C CB  . SER   A 69  ? 0.1468 0.2560 0.3909 -0.0449 0.0073  0.1804  75  SER   A CB  
547  O OG  . SER   A 69  ? 0.2233 0.3314 0.4482 -0.0651 -0.0125 0.1813  75  SER   A OG  
548  N N   . PHE   A 70  ? 0.1354 0.2220 0.3046 -0.0424 0.0008  0.1400  76  PHE   A N   
549  C CA  . PHE   A 70  ? 0.1363 0.2250 0.3207 -0.0310 0.0086  0.1426  76  PHE   A CA  
550  C C   . PHE   A 70  ? 0.1457 0.2533 0.3618 -0.0546 -0.0221 0.1719  76  PHE   A C   
551  O O   . PHE   A 70  ? 0.1743 0.2807 0.3738 -0.0857 -0.0541 0.1827  76  PHE   A O   
552  C CB  . PHE   A 70  ? 0.1452 0.2082 0.2693 -0.0215 0.0179  0.1050  76  PHE   A CB  
553  C CG  . PHE   A 70  ? 0.1504 0.2005 0.2231 -0.0421 0.0007  0.0838  76  PHE   A CG  
554  C CD1 . PHE   A 70  ? 0.1641 0.1993 0.2052 -0.0440 0.0045  0.0644  76  PHE   A CD1 
555  C CD2 . PHE   A 70  ? 0.1530 0.1991 0.2082 -0.0590 -0.0138 0.0831  76  PHE   A CD2 
556  C CE1 . PHE   A 70  ? 0.1809 0.1967 0.1802 -0.0608 -0.0006 0.0455  76  PHE   A CE1 
557  C CE2 . PHE   A 70  ? 0.1766 0.1983 0.1808 -0.0773 -0.0180 0.0630  76  PHE   A CE2 
558  C CZ  . PHE   A 70  ? 0.1891 0.1952 0.1686 -0.0773 -0.0087 0.0447  76  PHE   A CZ  
559  N N   . SER   A 71  ? 0.1268 0.2455 0.3860 -0.0426 -0.0139 0.1877  77  SER   A N   
560  C CA  . SER   A 71  ? 0.1206 0.2571 0.4191 -0.0649 -0.0457 0.2208  77  SER   A CA  
561  C C   . SER   A 71  ? 0.1625 0.2785 0.3906 -0.0861 -0.0676 0.1999  77  SER   A C   
562  O O   . SER   A 71  ? 0.1871 0.2809 0.3535 -0.0770 -0.0512 0.1612  77  SER   A O   
563  C CB  . SER   A 71  ? 0.0978 0.2526 0.4775 -0.0418 -0.0232 0.2475  77  SER   A CB  
564  O OG  . SER   A 71  ? 0.1168 0.2522 0.4562 -0.0212 0.0013  0.2178  77  SER   A OG  
565  N N   . LYS   A 72  ? 0.1709 0.2899 0.4102 -0.1162 -0.1048 0.2281  78  LYS   A N   
566  C CA  . LYS   A 72  ? 0.2379 0.3284 0.4066 -0.1385 -0.1213 0.2109  78  LYS   A CA  
567  C C   . LYS   A 72  ? 0.2414 0.3386 0.4225 -0.1120 -0.0981 0.1973  78  LYS   A C   
568  O O   . LYS   A 72  ? 0.2123 0.3351 0.4654 -0.0881 -0.0827 0.2169  78  LYS   A O   
569  C CB  . LYS   A 72  ? 0.2888 0.3701 0.4581 -0.1835 -0.1728 0.2497  78  LYS   A CB  
570  C CG  . LYS   A 72  ? 0.3826 0.4529 0.5417 -0.2140 -0.2024 0.2699  78  LYS   A CG  
571  C CD  . LYS   A 72  ? 0.5125 0.5418 0.6165 -0.2705 -0.2571 0.2953  78  LYS   A CD  
572  C CE  . LYS   A 72  ? 0.6470 0.6073 0.6170 -0.2990 -0.2538 0.2583  78  LYS   A CE  
573  N NZ  . LYS   A 72  ? 0.7276 0.6462 0.6501 -0.3508 -0.3010 0.2855  78  LYS   A NZ  
574  N N   . PRO   A 73  ? 0.2789 0.3496 0.3934 -0.1155 -0.0916 0.1653  79  PRO   A N   
575  C CA  . PRO   A 73  ? 0.2817 0.3577 0.4075 -0.0920 -0.0729 0.1537  79  PRO   A CA  
576  C C   . PRO   A 73  ? 0.2680 0.3661 0.4554 -0.0940 -0.0880 0.1897  79  PRO   A C   
577  O O   . PRO   A 73  ? 0.2707 0.3645 0.4554 -0.1270 -0.1243 0.2149  79  PRO   A O   
578  C CB  . PRO   A 73  ? 0.3262 0.3688 0.3776 -0.1060 -0.0714 0.1230  79  PRO   A CB  
579  C CG  . PRO   A 73  ? 0.3553 0.3733 0.3578 -0.1223 -0.0706 0.1074  79  PRO   A CG  
580  C CD  . PRO   A 73  ? 0.3182 0.3481 0.3473 -0.1406 -0.0960 0.1395  79  PRO   A CD  
581  N N   . SER   A 74  ? 0.2512 0.3657 0.4916 -0.0612 -0.0603 0.1947  80  SER   A N   
582  C CA  . SER   A 74  ? 0.2390 0.3757 0.5539 -0.0589 -0.0675 0.2321  80  SER   A CA  
583  C C   . SER   A 74  ? 0.2371 0.3698 0.5690 -0.0252 -0.0306 0.2213  80  SER   A C   
584  O O   . SER   A 74  ? 0.2509 0.3608 0.5343 -0.0050 -0.0029 0.1866  80  SER   A O   
585  C CB  . SER   A 74  ? 0.2381 0.4014 0.6416 -0.0606 -0.0737 0.2759  80  SER   A CB  
586  O OG  . SER   A 74  ? 0.2713 0.4334 0.6975 -0.0288 -0.0300 0.2669  80  SER   A OG  
587  N N   . LEU   A 75  ? 0.2201 0.3695 0.6183 -0.0225 -0.0339 0.2535  81  LEU   A N   
588  C CA  . LEU   A 75  ? 0.2336 0.3741 0.6525 0.0065  0.0017  0.2497  81  LEU   A CA  
589  C C   . LEU   A 75  ? 0.2356 0.3727 0.7141 0.0345  0.0467  0.2654  81  LEU   A C   
590  O O   . LEU   A 75  ? 0.2101 0.3743 0.7837 0.0318  0.0436  0.3092  81  LEU   A O   
591  C CB  . LEU   A 75  ? 0.2097 0.3706 0.6892 -0.0041 -0.0200 0.2849  81  LEU   A CB  
592  C CG  . LEU   A 75  ? 0.2505 0.3993 0.6719 -0.0152 -0.0378 0.2646  81  LEU   A CG  
593  C CD1 . LEU   A 75  ? 0.2336 0.4025 0.7260 -0.0243 -0.0580 0.3051  81  LEU   A CD1 
594  C CD2 . LEU   A 75  ? 0.2853 0.4050 0.6525 0.0122  -0.0002 0.2253  81  LEU   A CD2 
595  N N   . ILE   A 76  ? 0.2644 0.3625 0.6889 0.0586  0.0880  0.2334  82  ILE   A N   
596  C CA  . ILE   A 76  ? 0.2712 0.3479 0.7319 0.0832  0.1388  0.2444  82  ILE   A CA  
597  C C   . ILE   A 76  ? 0.3217 0.3452 0.7444 0.1078  0.1864  0.2274  82  ILE   A C   
598  O O   . ILE   A 76  ? 0.3547 0.3463 0.6869 0.1067  0.1798  0.1911  82  ILE   A O   
599  C CB  . ILE   A 76  ? 0.2894 0.3529 0.7040 0.0816  0.1420  0.2245  82  ILE   A CB  
600  C CG1 . ILE   A 76  ? 0.2702 0.3795 0.7287 0.0569  0.1002  0.2474  82  ILE   A CG1 
601  C CG2 . ILE   A 76  ? 0.3003 0.3219 0.7232 0.1069  0.2017  0.2271  82  ILE   A CG2 
602  C CD1 . ILE   A 76  ? 0.3131 0.4124 0.7112 0.0496  0.0915  0.2217  82  ILE   A CD1 
603  N N   . PHE   A 77  ? 0.3214 0.3301 0.8151 0.1285  0.2355  0.2560  83  PHE   A N   
604  C CA  . PHE   A 77  ? 0.3907 0.3329 0.8416 0.1504  0.2895  0.2423  83  PHE   A CA  
605  C C   . PHE   A 77  ? 0.4584 0.3258 0.7920 0.1566  0.3173  0.2037  83  PHE   A C   
606  O O   . PHE   A 77  ? 0.4582 0.3183 0.7880 0.1573  0.3289  0.2031  83  PHE   A O   
607  C CB  . PHE   A 77  ? 0.3806 0.3166 0.9420 0.1717  0.3464  0.2849  83  PHE   A CB  
608  C CG  . PHE   A 77  ? 0.4456 0.2996 0.9588 0.1935  0.4116  0.2727  83  PHE   A CG  
609  C CD1 . PHE   A 77  ? 0.4772 0.3214 0.9629 0.1930  0.4016  0.2637  83  PHE   A CD1 
610  C CD2 . PHE   A 77  ? 0.5066 0.2825 0.9882 0.2119  0.4843  0.2685  83  PHE   A CD2 
611  C CE1 . PHE   A 77  ? 0.5413 0.3000 0.9722 0.2104  0.4619  0.2524  83  PHE   A CE1 
612  C CE2 . PHE   A 77  ? 0.5705 0.2535 0.9938 0.2284  0.5492  0.2579  83  PHE   A CE2 
613  C CZ  . PHE   A 77  ? 0.5776 0.2518 0.9723 0.2269  0.5358  0.2490  83  PHE   A CZ  
614  N N   . VAL   A 78  ? 0.5132 0.3239 0.7486 0.1572  0.3208  0.1730  84  VAL   A N   
615  C CA  . VAL   A 78  ? 0.5921 0.3206 0.7041 0.1562  0.3352  0.1389  84  VAL   A CA  
616  C C   . VAL   A 78  ? 0.6670 0.3026 0.7137 0.1677  0.3846  0.1311  84  VAL   A C   
617  O O   . VAL   A 78  ? 0.6632 0.3007 0.7036 0.1666  0.3720  0.1284  84  VAL   A O   
618  C CB  . VAL   A 78  ? 0.6080 0.3530 0.6514 0.1362  0.2737  0.1088  84  VAL   A CB  
619  C CG1 . VAL   A 78  ? 0.6782 0.3362 0.6024 0.1312  0.2801  0.0807  84  VAL   A CG1 
620  C CG2 . VAL   A 78  ? 0.5667 0.3900 0.6636 0.1237  0.2322  0.1149  84  VAL   A CG2 
621  N N   . GLU   A 79  ? 0.7312 0.2776 0.7223 0.1771  0.4436  0.1275  85  GLU   A N   
622  C CA  . GLU   A 79  ? 0.8178 0.2472 0.7238 0.1854  0.5036  0.1193  85  GLU   A CA  
623  C C   . GLU   A 79  ? 0.8881 0.2538 0.6618 0.1675  0.4675  0.0877  85  GLU   A C   
624  O O   . GLU   A 79  ? 0.8948 0.2829 0.6241 0.1493  0.4072  0.0692  85  GLU   A O   
625  C CB  . GLU   A 79  ? 0.9198 0.2564 0.7742 0.1931  0.5712  0.1188  85  GLU   A CB  
626  C CG  . GLU   A 79  ? 1.0049 0.3207 0.9514 0.2187  0.6571  0.1512  85  GLU   A CG  
627  C CD  . GLU   A 79  ? 1.1853 0.4244 1.1046 0.2272  0.7263  0.1548  85  GLU   A CD  
628  O OE1 . GLU   A 79  ? 1.3018 0.4231 1.1661 0.2388  0.8120  0.1557  85  GLU   A OE1 
629  O OE2 . GLU   A 79  ? 1.2013 0.4905 1.1485 0.2217  0.6989  0.1561  85  GLU   A OE2 
630  N N   . ALA   A 80  ? 0.9341 0.2194 0.6522 0.1720  0.5048  0.0848  86  ALA   A N   
631  C CA  . ALA   A 80  ? 1.0077 0.2219 0.6020 0.1535  0.4727  0.0602  86  ALA   A CA  
632  C C   . ALA   A 80  ? 1.0968 0.2204 0.5482 0.1295  0.4470  0.0358  86  ALA   A C   
633  O O   . ALA   A 80  ? 1.1464 0.2168 0.5592 0.1301  0.4812  0.0347  86  ALA   A O   
634  C CB  . ALA   A 80  ? 1.0523 0.1720 0.6007 0.1630  0.5341  0.0635  86  ALA   A CB  
635  N N   . SER   A 81  ? 1.1207 0.2217 0.4963 0.1071  0.3869  0.0196  87  SER   A N   
636  C CA  . SER   A 81  ? 1.1936 0.2099 0.4415 0.0791  0.3481  0.0027  87  SER   A CA  
637  C C   . SER   A 81  ? 1.2435 0.2050 0.4063 0.0557  0.2987  -0.0069 87  SER   A C   
638  O O   . SER   A 81  ? 1.2131 0.2138 0.4225 0.0639  0.2963  -0.0027 87  SER   A O   
639  C CB  . SER   A 81  ? 1.1551 0.2662 0.4658 0.0735  0.2948  0.0017  87  SER   A CB  
640  O OG  . SER   A 81  ? 1.1212 0.3382 0.5105 0.0695  0.2327  0.0021  87  SER   A OG  
641  N N   . GLU   A 82  ? 1.3123 0.1822 0.3535 0.0242  0.2550  -0.0165 88  GLU   A N   
642  C CA  . GLU   A 82  ? 1.3539 0.1741 0.3247 -0.0017 0.1991  -0.0197 88  GLU   A CA  
643  C C   . GLU   A 82  ? 1.2452 0.2063 0.3413 0.0010  0.1348  -0.0146 88  GLU   A C   
644  O O   . GLU   A 82  ? 1.2666 0.2098 0.3383 -0.0142 0.0950  -0.0136 88  GLU   A O   
645  C CB  . GLU   A 82  ? 1.5063 0.1869 0.3188 -0.0416 0.1598  -0.0243 88  GLU   A CB  
646  C CG  . GLU   A 82  ? 1.5977 0.3041 0.4225 -0.0512 0.1274  -0.0235 88  GLU   A CG  
647  C CD  . GLU   A 82  ? 1.8010 0.3685 0.4727 -0.0958 0.0763  -0.0230 88  GLU   A CD  
648  O OE1 . GLU   A 82  ? 1.8784 0.3559 0.4567 -0.1236 0.0414  -0.0203 88  GLU   A OE1 
649  O OE2 . GLU   A 82  ? 1.8398 0.3865 0.4844 -0.1057 0.0664  -0.0231 88  GLU   A OE2 
650  N N   . TYR   A 83  ? 1.1212 0.2161 0.3499 0.0207  0.1324  -0.0106 89  TYR   A N   
651  C CA  . TYR   A 83  ? 1.0057 0.2294 0.3526 0.0248  0.0868  -0.0069 89  TYR   A CA  
652  C C   . TYR   A 83  ? 0.9118 0.2269 0.3618 0.0494  0.1160  -0.0007 89  TYR   A C   
653  O O   . TYR   A 83  ? 0.8818 0.2553 0.3833 0.0475  0.0847  0.0007  89  TYR   A O   
654  C CB  . TYR   A 83  ? 0.9541 0.2454 0.3583 0.0234  0.0615  -0.0068 89  TYR   A CB  
655  C CG  . TYR   A 83  ? 1.0130 0.2164 0.3235 -0.0006 0.0334  -0.0093 89  TYR   A CG  
656  C CD1 . TYR   A 83  ? 1.0521 0.2097 0.3168 -0.0281 -0.0269 -0.0057 89  TYR   A CD1 
657  C CD2 . TYR   A 83  ? 1.0473 0.2070 0.3142 0.0018  0.0655  -0.0120 89  TYR   A CD2 
658  C CE1 . TYR   A 83  ? 1.1197 0.1900 0.2965 -0.0551 -0.0607 -0.0031 89  TYR   A CE1 
659  C CE2 . TYR   A 83  ? 1.1189 0.1888 0.2898 -0.0236 0.0374  -0.0133 89  TYR   A CE2 
660  C CZ  . TYR   A 83  ? 1.1642 0.1886 0.2889 -0.0533 -0.0285 -0.0080 89  TYR   A CZ  
661  O OH  . TYR   A 83  ? 1.2516 0.1812 0.2799 -0.0833 -0.0643 -0.0045 89  TYR   A OH  
662  N N   . TYR   A 84  ? 0.8701 0.1979 0.3565 0.0704  0.1731  0.0062  90  TYR   A N   
663  C CA  . TYR   A 84  ? 0.7967 0.2109 0.3884 0.0896  0.1925  0.0185  90  TYR   A CA  
664  C C   . TYR   A 84  ? 0.8197 0.1903 0.4165 0.1090  0.2624  0.0303  90  TYR   A C   
665  O O   . TYR   A 84  ? 0.8528 0.1610 0.4100 0.1140  0.3059  0.0313  90  TYR   A O   
666  C CB  . TYR   A 84  ? 0.7036 0.2278 0.4003 0.0960  0.1796  0.0266  90  TYR   A CB  
667  C CG  . TYR   A 84  ? 0.6533 0.2335 0.3712 0.0814  0.1240  0.0180  90  TYR   A CG  
668  C CD1 . TYR   A 84  ? 0.6481 0.2303 0.3556 0.0748  0.1109  0.0129  90  TYR   A CD1 
669  C CD2 . TYR   A 84  ? 0.6117 0.2453 0.3698 0.0756  0.0905  0.0167  90  TYR   A CD2 
670  C CE1 . TYR   A 84  ? 0.6157 0.2490 0.3549 0.0636  0.0679  0.0073  90  TYR   A CE1 
671  C CE2 . TYR   A 84  ? 0.5790 0.2587 0.3651 0.0641  0.0508  0.0106  90  TYR   A CE2 
672  C CZ  . TYR   A 84  ? 0.5813 0.2624 0.3620 0.0588  0.0412  0.0066  90  TYR   A CZ  
673  O OH  . TYR   A 84  ? 0.5398 0.2600 0.3533 0.0486  0.0084  0.0021  90  TYR   A OH  
674  N N   . PRO   A 85  ? 0.7909 0.2017 0.4533 0.1215  0.2774  0.0428  91  PRO   A N   
675  C CA  . PRO   A 85  ? 0.7968 0.1817 0.4988 0.1431  0.3477  0.0612  91  PRO   A CA  
676  C C   . PRO   A 85  ? 0.7344 0.2041 0.5529 0.1556  0.3606  0.0826  91  PRO   A C   
677  O O   . PRO   A 85  ? 0.6918 0.2372 0.5488 0.1461  0.3133  0.0803  91  PRO   A O   
678  C CB  . PRO   A 85  ? 0.7814 0.1954 0.5281 0.1491  0.3454  0.0702  91  PRO   A CB  
679  C CG  . PRO   A 85  ? 0.7361 0.2416 0.5209 0.1351  0.2737  0.0639  91  PRO   A CG  
680  C CD  . PRO   A 85  ? 0.7428 0.2262 0.4567 0.1170  0.2342  0.0438  91  PRO   A CD  
681  N N   . ALA   A 86  ? 0.7203 0.1743 0.5989 0.1757  0.4251  0.1058  92  ALA   A N   
682  C CA  . ALA   A 86  ? 0.6451 0.1774 0.6436 0.1853  0.4339  0.1324  92  ALA   A CA  
683  C C   . ALA   A 86  ? 0.5453 0.1985 0.6504 0.1784  0.3764  0.1496  92  ALA   A C   
684  O O   . ALA   A 86  ? 0.5221 0.1922 0.6537 0.1798  0.3683  0.1567  92  ALA   A O   
685  C CB  . ALA   A 86  ? 0.6407 0.1328 0.7015 0.2088  0.5162  0.1602  92  ALA   A CB  
686  N N   . ARG   A 87  ? 0.4820 0.2079 0.6283 0.1668  0.3328  0.1525  93  ARG   A N   
687  C CA  . ARG   A 87  ? 0.4046 0.2237 0.6215 0.1531  0.2762  0.1651  93  ARG   A CA  
688  C C   . ARG   A 87  ? 0.3460 0.2295 0.6192 0.1419  0.2463  0.1784  93  ARG   A C   
689  O O   . ARG   A 87  ? 0.3599 0.2213 0.6136 0.1456  0.2649  0.1732  93  ARG   A O   
690  C CB  . ARG   A 87  ? 0.4214 0.2376 0.5595 0.1376  0.2304  0.1339  93  ARG   A CB  
691  C CG  . ARG   A 87  ? 0.4270 0.2502 0.5107 0.1227  0.1949  0.1093  93  ARG   A CG  
692  C CD  . ARG   A 87  ? 0.4638 0.2302 0.4476 0.1158  0.1810  0.0787  93  ARG   A CD  
693  N NE  . ARG   A 87  ? 0.4457 0.2454 0.4159 0.0999  0.1375  0.0631  93  ARG   A NE  
694  C CZ  . ARG   A 87  ? 0.4144 0.2016 0.3580 0.0960  0.1338  0.0539  93  ARG   A CZ  
695  N NH1 . ARG   A 87  ? 0.3582 0.1753 0.2992 0.0828  0.0985  0.0418  93  ARG   A NH1 
696  N NH2 . ARG   A 87  ? 0.4139 0.1536 0.3338 0.1054  0.1695  0.0574  93  ARG   A NH2 
697  N N   . TYR   A 88  ? 0.2918 0.2453 0.6209 0.1248  0.1981  0.1940  94  TYR   A N   
698  C CA  . TYR   A 88  ? 0.2617 0.2627 0.6180 0.1075  0.1632  0.2020  94  TYR   A CA  
699  C C   . TYR   A 88  ? 0.2456 0.2426 0.5139 0.0913  0.1275  0.1641  94  TYR   A C   
700  O O   . TYR   A 88  ? 0.2433 0.2391 0.4776 0.0841  0.1077  0.1493  94  TYR   A O   
701  C CB  . TYR   A 88  ? 0.2379 0.2991 0.6817 0.0900  0.1259  0.2394  94  TYR   A CB  
702  C CG  . TYR   A 88  ? 0.2388 0.3175 0.8004 0.1027  0.1531  0.2873  94  TYR   A CG  
703  C CD1 . TYR   A 88  ? 0.2403 0.3428 0.8699 0.1005  0.1551  0.3151  94  TYR   A CD1 
704  C CD2 . TYR   A 88  ? 0.2522 0.3225 0.8652 0.1176  0.1797  0.3071  94  TYR   A CD2 
705  C CE1 . TYR   A 88  ? 0.2144 0.3352 0.9718 0.1129  0.1823  0.3650  94  TYR   A CE1 
706  C CE2 . TYR   A 88  ? 0.2323 0.3182 0.9707 0.1313  0.2106  0.3555  94  TYR   A CE2 
707  C CZ  . TYR   A 88  ? 0.2228 0.3347 1.0381 0.1294  0.2127  0.3857  94  TYR   A CZ  
708  O OH  . TYR   A 88  ? 0.2210 0.3514 1.1801 0.1432  0.2442  0.4398  94  TYR   A OH  
709  N N   . GLN   A 89  ? 0.2211 0.2155 0.4606 0.0863  0.1221  0.1509  95  GLN   A N   
710  C CA  . GLN   A 89  ? 0.2166 0.2089 0.3909 0.0720  0.0928  0.1201  95  GLN   A CA  
711  C C   . GLN   A 89  ? 0.1810 0.2178 0.3831 0.0494  0.0591  0.1315  95  GLN   A C   
712  O O   . GLN   A 89  ? 0.1697 0.2261 0.4178 0.0469  0.0602  0.1540  95  GLN   A O   
713  C CB  . GLN   A 89  ? 0.2509 0.2006 0.3672 0.0797  0.1086  0.0974  95  GLN   A CB  
714  C CG  . GLN   A 89  ? 0.2661 0.2164 0.3342 0.0658  0.0790  0.0709  95  GLN   A CG  
715  C CD  . GLN   A 89  ? 0.3040 0.2051 0.3131 0.0709  0.0866  0.0512  95  GLN   A CD  
716  O OE1 . GLN   A 89  ? 0.3638 0.2117 0.3307 0.0798  0.1041  0.0458  95  GLN   A OE1 
717  N NE2 . GLN   A 89  ? 0.2606 0.1706 0.2591 0.0624  0.0717  0.0410  95  GLN   A NE2 
718  N N   . SER   A 90  ? 0.1636 0.2106 0.3388 0.0310  0.0307  0.1199  96  SER   A N   
719  C CA  . SER   A 90  ? 0.1459 0.2152 0.3247 0.0038  0.0006  0.1292  96  SER   A CA  
720  C C   . SER   A 90  ? 0.1698 0.2280 0.3028 -0.0045 -0.0030 0.1052  96  SER   A C   
721  O O   . SER   A 90  ? 0.1880 0.2253 0.2895 0.0094  0.0114  0.0806  96  SER   A O   
722  C CB  . SER   A 90  ? 0.1596 0.2321 0.3253 -0.0150 -0.0217 0.1313  96  SER   A CB  
723  O OG  . SER   A 90  ? 0.2041 0.2561 0.3226 -0.0097 -0.0144 0.1004  96  SER   A OG  
724  N N   . HIS   A 91  ? 0.1564 0.2237 0.2867 -0.0290 -0.0239 0.1155  97  HIS   A N   
725  C CA  . HIS   A 91  ? 0.1713 0.2250 0.2598 -0.0396 -0.0252 0.0952  97  HIS   A CA  
726  C C   . HIS   A 91  ? 0.1677 0.2192 0.2633 -0.0187 -0.0059 0.0868  97  HIS   A C   
727  O O   . HIS   A 91  ? 0.1816 0.2175 0.2449 -0.0163 0.0004  0.0631  97  HIS   A O   
728  C CB  . HIS   A 91  ? 0.1918 0.2233 0.2338 -0.0446 -0.0209 0.0667  97  HIS   A CB  
729  C CG  . HIS   A 91  ? 0.2301 0.2526 0.2517 -0.0684 -0.0359 0.0730  97  HIS   A CG  
730  N ND1 . HIS   A 91  ? 0.2811 0.2785 0.2566 -0.1003 -0.0467 0.0719  97  HIS   A ND1 
731  C CD2 . HIS   A 91  ? 0.2340 0.2617 0.2680 -0.0671 -0.0414 0.0819  97  HIS   A CD2 
732  C CE1 . HIS   A 91  ? 0.2946 0.2786 0.2504 -0.1186 -0.0589 0.0793  97  HIS   A CE1 
733  N NE2 . HIS   A 91  ? 0.2632 0.2698 0.2583 -0.0988 -0.0576 0.0863  97  HIS   A NE2 
734  N N   . LEU   A 92  ? 0.1523 0.2154 0.2933 -0.0043 0.0056  0.1083  98  LEU   A N   
735  C CA  . LEU   A 92  ? 0.1603 0.2107 0.3020 0.0152  0.0294  0.1027  98  LEU   A CA  
736  C C   . LEU   A 92  ? 0.1364 0.2041 0.3075 0.0063  0.0238  0.1212  98  LEU   A C   
737  O O   . LEU   A 92  ? 0.1102 0.2025 0.3318 -0.0060 0.0088  0.1529  98  LEU   A O   
738  C CB  . LEU   A 92  ? 0.1576 0.1934 0.3236 0.0390  0.0590  0.1130  98  LEU   A CB  
739  C CG  . LEU   A 92  ? 0.1961 0.1951 0.3394 0.0582  0.0912  0.1038  98  LEU   A CG  
740  C CD1 . LEU   A 92  ? 0.2288 0.1951 0.3022 0.0572  0.0840  0.0714  98  LEU   A CD1 
741  C CD2 . LEU   A 92  ? 0.2154 0.1841 0.3731 0.0788  0.1291  0.1153  98  LEU   A CD2 
742  N N   . MET   A 93  ? 0.1473 0.2013 0.2905 0.0106  0.0321  0.1045  99  MET   A N   
743  C CA  . MET   A 93  ? 0.1376 0.2050 0.3030 0.0026  0.0276  0.1190  99  MET   A CA  
744  C C   . MET   A 93  ? 0.1642 0.2141 0.3360 0.0248  0.0593  0.1180  99  MET   A C   
745  O O   . MET   A 93  ? 0.2032 0.2208 0.3244 0.0353  0.0714  0.0920  99  MET   A O   
746  C CB  . MET   A 93  ? 0.1485 0.2092 0.2664 -0.0164 0.0098  0.0986  99  MET   A CB  
747  C CG  . MET   A 93  ? 0.1752 0.2346 0.2683 -0.0413 -0.0133 0.0964  99  MET   A CG  
748  S SD  . MET   A 93  ? 0.2231 0.2565 0.2540 -0.0599 -0.0167 0.0679  99  MET   A SD  
749  C CE  . MET   A 93  ? 0.1971 0.2165 0.2160 -0.0337 0.0048  0.0387  99  MET   A CE  
750  N N   . LEU   A 94  ? 0.1399 0.2055 0.3732 0.0296  0.0719  0.1483  100 LEU   A N   
751  C CA  . LEU   A 94  ? 0.1610 0.1998 0.3956 0.0501  0.1104  0.1478  100 LEU   A CA  
752  C C   . LEU   A 94  ? 0.1613 0.2076 0.3964 0.0426  0.1046  0.1491  100 LEU   A C   
753  O O   . LEU   A 94  ? 0.1322 0.2120 0.3979 0.0223  0.0745  0.1660  100 LEU   A O   
754  C CB  . LEU   A 94  ? 0.1466 0.1879 0.4579 0.0667  0.1450  0.1817  100 LEU   A CB  
755  C CG  . LEU   A 94  ? 0.1846 0.2085 0.4948 0.0786  0.1616  0.1809  100 LEU   A CG  
756  C CD1 . LEU   A 94  ? 0.1736 0.1937 0.5672 0.0975  0.2061  0.2160  100 LEU   A CD1 
757  C CD2 . LEU   A 94  ? 0.2501 0.2149 0.4642 0.0888  0.1792  0.1436  100 LEU   A CD2 
758  N N   . ALA   A 95  ? 0.1929 0.2006 0.3897 0.0569  0.1334  0.1334  101 ALA   A N   
759  C CA  . ALA   A 95  ? 0.2110 0.2182 0.4034 0.0536  0.1349  0.1325  101 ALA   A CA  
760  C C   . ALA   A 95  ? 0.2483 0.2091 0.4310 0.0739  0.1839  0.1343  101 ALA   A C   
761  O O   . ALA   A 95  ? 0.2732 0.1837 0.4123 0.0869  0.2119  0.1224  101 ALA   A O   
762  C CB  . ALA   A 95  ? 0.2347 0.2292 0.3569 0.0430  0.1104  0.0997  101 ALA   A CB  
763  N N   . VAL   A 96  ? 0.2502 0.2186 0.4643 0.0744  0.1957  0.1485  102 VAL   A N   
764  C CA  . VAL   A 96  ? 0.2992 0.2145 0.4951 0.0912  0.2467  0.1488  102 VAL   A CA  
765  C C   . VAL   A 96  ? 0.3661 0.2367 0.4596 0.0856  0.2345  0.1129  102 VAL   A C   
766  O O   . VAL   A 96  ? 0.3644 0.2632 0.4494 0.0720  0.1997  0.1036  102 VAL   A O   
767  C CB  . VAL   A 96  ? 0.2789 0.2234 0.5640 0.0941  0.2658  0.1836  102 VAL   A CB  
768  C CG1 . VAL   A 96  ? 0.3202 0.1988 0.5733 0.1105  0.3246  0.1800  102 VAL   A CG1 
769  C CG2 . VAL   A 96  ? 0.2295 0.2196 0.6330 0.0976  0.2720  0.2271  102 VAL   A CG2 
770  N N   . GLY   A 97  ? 0.4230 0.2208 0.4376 0.0930  0.2583  0.0941  103 GLY   A N   
771  C CA  . GLY   A 97  ? 0.4834 0.2295 0.4014 0.0845  0.2409  0.0654  103 GLY   A CA  
772  C C   . GLY   A 97  ? 0.5519 0.2069 0.3799 0.0877  0.2641  0.0516  103 GLY   A C   
773  O O   . GLY   A 97  ? 0.5639 0.2024 0.4023 0.0970  0.2902  0.0594  103 GLY   A O   
774  N N   . HIS   A 98  ? 0.5986 0.1881 0.3342 0.0773  0.2518  0.0327  104 HIS   A N   
775  C CA  . HIS   A 98  ? 0.6681 0.1550 0.2971 0.0719  0.2632  0.0200  104 HIS   A CA  
776  C C   . HIS   A 98  ? 0.6719 0.1674 0.2825 0.0622  0.2177  0.0096  104 HIS   A C   
777  O O   . HIS   A 98  ? 0.6268 0.1801 0.2705 0.0536  0.1692  0.0040  104 HIS   A O   
778  C CB  . HIS   A 98  ? 0.7390 0.1413 0.2691 0.0586  0.2610  0.0085  104 HIS   A CB  
779  C CG  . HIS   A 98  ? 0.8519 0.1346 0.2537 0.0439  0.2600  -0.0030 104 HIS   A CG  
780  N ND1 . HIS   A 98  ? 0.9402 0.1288 0.2767 0.0495  0.3194  -0.0011 104 HIS   A ND1 
781  C CD2 . HIS   A 98  ? 0.9060 0.1497 0.2407 0.0220  0.2044  -0.0131 104 HIS   A CD2 
782  C CE1 . HIS   A 98  ? 1.0204 0.1077 0.2356 0.0281  0.2960  -0.0125 104 HIS   A CE1 
783  N NE2 . HIS   A 98  ? 1.0044 0.1244 0.2197 0.0103  0.2229  -0.0178 104 HIS   A NE2 
784  N N   . SER   A 99  ? 0.7238 0.1492 0.2751 0.0629  0.2386  0.0073  105 SER   A N   
785  C CA  . SER   A 99  ? 0.7631 0.1730 0.2805 0.0525  0.2017  -0.0010 105 SER   A CA  
786  C C   . SER   A 99  ? 0.8617 0.1541 0.2762 0.0497  0.2373  -0.0041 105 SER   A C   
787  O O   . SER   A 99  ? 0.8751 0.1263 0.2826 0.0634  0.3006  0.0030  105 SER   A O   
788  C CB  . SER   A 99  ? 0.7084 0.2200 0.3260 0.0611  0.1840  0.0051  105 SER   A CB  
789  O OG  . SER   A 99  ? 0.7219 0.2479 0.3860 0.0779  0.2288  0.0186  105 SER   A OG  
790  N N   . GLU   A 100 ? 0.9266 0.1565 0.2596 0.0299  0.1982  -0.0129 106 GLU   A N   
791  C CA  . GLU   A 100 ? 1.0349 0.1405 0.2519 0.0207  0.2236  -0.0169 106 GLU   A CA  
792  C C   . GLU   A 100 ? 1.0674 0.1642 0.2582 0.0032  0.1654  -0.0200 106 GLU   A C   
793  O O   . GLU   A 100 ? 1.0243 0.1937 0.2740 -0.0044 0.1072  -0.0191 106 GLU   A O   
794  C CB  . GLU   A 100 ? 1.1574 0.1252 0.2366 0.0028  0.2448  -0.0225 106 GLU   A CB  
795  C CG  . GLU   A 100 ? 1.2408 0.2005 0.2864 -0.0213 0.1808  -0.0253 106 GLU   A CG  
796  C CD  . GLU   A 100 ? 1.3791 0.2014 0.2865 -0.0407 0.2027  -0.0295 106 GLU   A CD  
797  O OE1 . GLU   A 100 ? 1.4948 0.1764 0.2564 -0.0675 0.1963  -0.0332 106 GLU   A OE1 
798  O OE2 . GLU   A 100 ? 1.3520 0.1996 0.2896 -0.0313 0.2267  -0.0287 106 GLU   A OE2 
799  N N   . PRO   A 101 ? 1.1392 0.1423 0.2420 -0.0050 0.1801  -0.0225 107 PRO   A N   
800  C CA  . PRO   A 101 ? 1.1524 0.1494 0.2366 -0.0238 0.1194  -0.0224 107 PRO   A CA  
801  C C   . PRO   A 101 ? 1.1550 0.1357 0.2110 -0.0522 0.0459  -0.0196 107 PRO   A C   
802  O O   . PRO   A 101 ? 1.2278 0.1220 0.1932 -0.0697 0.0443  -0.0207 107 PRO   A O   
803  C CB  . PRO   A 101 ? 1.2607 0.1190 0.2136 -0.0350 0.1522  -0.0260 107 PRO   A CB  
804  C CG  . PRO   A 101 ? 1.2633 0.1108 0.2330 -0.0074 0.2418  -0.0259 107 PRO   A CG  
805  C CD  . PRO   A 101 ? 1.2019 0.1012 0.2260 0.0029  0.2560  -0.0238 107 PRO   A CD  
806  N N   . GLY   A 102 ? 1.0621 0.1359 0.2131 -0.0538 -0.0086 -0.0141 108 GLY   A N   
807  C CA  . GLY   A 102 ? 1.0287 0.1119 0.1959 -0.0758 -0.0760 -0.0058 108 GLY   A CA  
808  C C   . GLY   A 102 ? 0.9086 0.1251 0.2136 -0.0574 -0.0817 -0.0051 108 GLY   A C   
809  O O   . GLY   A 102 ? 0.8792 0.1350 0.2425 -0.0686 -0.1328 0.0038  108 GLY   A O   
810  N N   . ASP   A 103 ? 0.8319 0.1154 0.1936 -0.0304 -0.0284 -0.0119 109 ASP   A N   
811  C CA  . ASP   A 103 ? 0.7190 0.1142 0.1923 -0.0158 -0.0281 -0.0121 109 ASP   A CA  
812  C C   . ASP   A 103 ? 0.6211 0.1151 0.1975 -0.0038 -0.0343 -0.0114 109 ASP   A C   
813  O O   . ASP   A 103 ? 0.5583 0.1291 0.2138 0.0017  -0.0403 -0.0116 109 ASP   A O   
814  C CB  . ASP   A 103 ? 0.7121 0.1240 0.1936 0.0013  0.0238  -0.0150 109 ASP   A CB  
815  C CG  . ASP   A 103 ? 0.7718 0.1154 0.1826 -0.0109 0.0223  -0.0161 109 ASP   A CG  
816  O OD1 . ASP   A 103 ? 0.7642 0.0948 0.1666 -0.0288 -0.0260 -0.0132 109 ASP   A OD1 
817  O OD2 . ASP   A 103 ? 0.8205 0.1205 0.1879 -0.0028 0.0707  -0.0176 109 ASP   A OD2 
818  N N   . CYS   A 104 ? 0.6048 0.0916 0.1753 -0.0013 -0.0307 -0.0109 110 CYS   A N   
819  C CA  . CYS   A 104 ? 0.5403 0.1139 0.2015 0.0077  -0.0363 -0.0103 110 CYS   A CA  
820  C C   . CYS   A 104 ? 0.4946 0.1042 0.2145 -0.0029 -0.0790 -0.0063 110 CYS   A C   
821  O O   . CYS   A 104 ? 0.5254 0.0821 0.2119 -0.0203 -0.1162 0.0007  110 CYS   A O   
822  C CB  . CYS   A 104 ? 0.5624 0.1128 0.2006 0.0099  -0.0294 -0.0097 110 CYS   A CB  
823  S SG  . CYS   A 104 ? 0.6395 0.1732 0.2537 0.0288  0.0321  -0.0098 110 CYS   A SG  
824  N N   . GLY   A 105 ? 0.4290 0.1187 0.2332 0.0051  -0.0727 -0.0081 111 GLY   A N   
825  C CA  . GLY   A 105 ? 0.3981 0.1178 0.2682 -0.0025 -0.1007 -0.0029 111 GLY   A CA  
826  C C   . GLY   A 105 ? 0.3801 0.1244 0.2809 -0.0024 -0.0976 -0.0043 111 GLY   A C   
827  O O   . GLY   A 105 ? 0.3576 0.1386 0.3281 -0.0038 -0.1035 -0.0015 111 GLY   A O   
828  N N   . GLY   A 106 ? 0.3838 0.1076 0.2369 0.0004  -0.0820 -0.0084 112 GLY   A N   
829  C CA  . GLY   A 106 ? 0.3477 0.0962 0.2258 0.0013  -0.0758 -0.0106 112 GLY   A CA  
830  C C   . GLY   A 106 ? 0.2909 0.1056 0.2261 0.0088  -0.0511 -0.0162 112 GLY   A C   
831  O O   . GLY   A 106 ? 0.2691 0.1048 0.2015 0.0151  -0.0309 -0.0184 112 GLY   A O   
832  N N   . ILE   A 107 ? 0.2555 0.0960 0.2410 0.0056  -0.0534 -0.0168 113 ILE   A N   
833  C CA  . ILE   A 107 ? 0.2365 0.1198 0.2591 0.0068  -0.0297 -0.0228 113 ILE   A CA  
834  C C   . ILE   A 107 ? 0.2299 0.1285 0.2319 0.0075  -0.0114 -0.0263 113 ILE   A C   
835  O O   . ILE   A 107 ? 0.2524 0.1375 0.2376 0.0075  -0.0153 -0.0256 113 ILE   A O   
836  C CB  . ILE   A 107 ? 0.2390 0.1311 0.3245 0.0025  -0.0315 -0.0209 113 ILE   A CB  
837  C CG1 . ILE   A 107 ? 0.2439 0.1327 0.3696 0.0017  -0.0438 -0.0136 113 ILE   A CG1 
838  C CG2 . ILE   A 107 ? 0.2381 0.1524 0.3404 -0.0004 -0.0006 -0.0293 113 ILE   A CG2 
839  C CD1 . ILE   A 107 ? 0.2392 0.1309 0.4463 -0.0011 -0.0468 -0.0038 113 ILE   A CD1 
840  N N   . LEU   A 108 ? 0.2033 0.1271 0.2073 0.0053  0.0050  -0.0278 114 LEU   A N   
841  C CA  . LEU   A 108 ? 0.2057 0.1462 0.2000 0.0002  0.0166  -0.0263 114 LEU   A CA  
842  C C   . LEU   A 108 ? 0.2137 0.1596 0.2215 -0.0123 0.0277  -0.0331 114 LEU   A C   
843  O O   . LEU   A 108 ? 0.2080 0.1526 0.2256 -0.0169 0.0349  -0.0366 114 LEU   A O   
844  C CB  . LEU   A 108 ? 0.1954 0.1508 0.1817 0.0006  0.0213  -0.0169 114 LEU   A CB  
845  C CG  . LEU   A 108 ? 0.1941 0.1686 0.1804 -0.0109 0.0247  -0.0076 114 LEU   A CG  
846  C CD1 . LEU   A 108 ? 0.1959 0.1690 0.1793 -0.0066 0.0272  -0.0027 114 LEU   A CD1 
847  C CD2 . LEU   A 108 ? 0.1956 0.1866 0.1922 -0.0122 0.0233  0.0085  114 LEU   A CD2 
848  N N   . ARG   A 109 ? 0.2266 0.1700 0.2303 -0.0181 0.0330  -0.0356 115 ARG   A N   
849  C CA  . ARG   A 109 ? 0.2471 0.1795 0.2502 -0.0314 0.0505  -0.0431 115 ARG   A CA  
850  C C   . ARG   A 109 ? 0.2717 0.2034 0.2419 -0.0458 0.0521  -0.0402 115 ARG   A C   
851  O O   . ARG   A 109 ? 0.2617 0.2043 0.2298 -0.0408 0.0422  -0.0339 115 ARG   A O   
852  C CB  . ARG   A 109 ? 0.2646 0.1853 0.3019 -0.0261 0.0564  -0.0477 115 ARG   A CB  
853  C CG  . ARG   A 109 ? 0.3281 0.2458 0.4128 -0.0169 0.0512  -0.0452 115 ARG   A CG  
854  C CD  . ARG   A 109 ? 0.3834 0.2919 0.5167 -0.0137 0.0526  -0.0425 115 ARG   A CD  
855  N NE  . ARG   A 109 ? 0.4487 0.3421 0.5910 -0.0216 0.0884  -0.0499 115 ARG   A NE  
856  C CZ  . ARG   A 109 ? 0.4854 0.3638 0.6628 -0.0235 0.1182  -0.0518 115 ARG   A CZ  
857  N NH1 . ARG   A 109 ? 0.5190 0.3682 0.6880 -0.0326 0.1585  -0.0601 115 ARG   A NH1 
858  N NH2 . ARG   A 109 ? 0.4669 0.3526 0.6862 -0.0170 0.1112  -0.0448 115 ARG   A NH2 
859  N N   . CYS   A 110 ? 0.2959 0.2058 0.2363 -0.0662 0.0657  -0.0442 116 CYS   A N   
860  C CA  . CYS   A 110 ? 0.3259 0.2212 0.2259 -0.0872 0.0642  -0.0406 116 CYS   A CA  
861  C C   . CYS   A 110 ? 0.3692 0.2251 0.2563 -0.0956 0.0934  -0.0553 116 CYS   A C   
862  O O   . CYS   A 110 ? 0.3539 0.2059 0.2811 -0.0814 0.1110  -0.0633 116 CYS   A O   
863  C CB  . CYS   A 110 ? 0.3407 0.2250 0.2010 -0.1109 0.0532  -0.0304 116 CYS   A CB  
864  S SG  . CYS   A 110 ? 0.3873 0.2262 0.2134 -0.1260 0.0784  -0.0432 116 CYS   A SG  
865  N N   . GLN   A 111 ? 0.4227 0.2449 0.2579 -0.1196 0.0995  -0.0565 117 GLN   A N   
866  C CA  . GLN   A 111 ? 0.4723 0.2451 0.2883 -0.1285 0.1361  -0.0709 117 GLN   A CA  
867  C C   . GLN   A 111 ? 0.5075 0.2374 0.3111 -0.1349 0.1720  -0.0814 117 GLN   A C   
868  O O   . GLN   A 111 ? 0.5272 0.2183 0.3406 -0.1338 0.2136  -0.0923 117 GLN   A O   
869  C CB  . GLN   A 111 ? 0.5476 0.2782 0.2889 -0.1596 0.1339  -0.0694 117 GLN   A CB  
870  C CG  . GLN   A 111 ? 0.6385 0.3346 0.3065 -0.1929 0.1186  -0.0610 117 GLN   A CG  
871  C CD  . GLN   A 111 ? 0.7593 0.4160 0.3547 -0.2280 0.1007  -0.0520 117 GLN   A CD  
872  O OE1 . GLN   A 111 ? 0.7826 0.4660 0.3755 -0.2410 0.0574  -0.0296 117 GLN   A OE1 
873  N NE2 . GLN   A 111 ? 0.7967 0.3848 0.3347 -0.2454 0.1343  -0.0667 117 GLN   A NE2 
874  N N   . HIS   A 112 ? 0.5087 0.2414 0.2931 -0.1421 0.1602  -0.0767 118 HIS   A N   
875  C CA  . HIS   A 112 ? 0.5295 0.2167 0.2944 -0.1505 0.1954  -0.0861 118 HIS   A CA  
876  C C   . HIS   A 112 ? 0.4689 0.1905 0.3198 -0.1212 0.2057  -0.0870 118 HIS   A C   
877  O O   . HIS   A 112 ? 0.4912 0.1762 0.3437 -0.1241 0.2426  -0.0941 118 HIS   A O   
878  C CB  . HIS   A 112 ? 0.5911 0.2500 0.2796 -0.1798 0.1780  -0.0798 118 HIS   A CB  
879  C CG  . HIS   A 112 ? 0.6992 0.3141 0.2987 -0.2167 0.1596  -0.0731 118 HIS   A CG  
880  N ND1 . HIS   A 112 ? 0.7226 0.3721 0.3139 -0.2286 0.1075  -0.0516 118 HIS   A ND1 
881  C CD2 . HIS   A 112 ? 0.7799 0.3173 0.3014 -0.2444 0.1861  -0.0824 118 HIS   A CD2 
882  C CE1 . HIS   A 112 ? 0.7825 0.3774 0.2935 -0.2654 0.0969  -0.0460 118 HIS   A CE1 
883  N NE2 . HIS   A 112 ? 0.8252 0.3481 0.2832 -0.2769 0.1431  -0.0659 118 HIS   A NE2 
884  N N   . GLY   A 113 ? 0.3922 0.1753 0.3071 -0.0963 0.1735  -0.0785 119 GLY   A N   
885  C CA  . GLY   A 113 ? 0.3350 0.1461 0.3255 -0.0733 0.1721  -0.0753 119 GLY   A CA  
886  C C   . GLY   A 113 ? 0.2818 0.1386 0.2866 -0.0607 0.1317  -0.0658 119 GLY   A C   
887  O O   . GLY   A 113 ? 0.2768 0.1543 0.2569 -0.0615 0.1055  -0.0597 119 GLY   A O   
888  N N   . VAL   A 114 ? 0.2458 0.1139 0.2931 -0.0491 0.1300  -0.0630 120 VAL   A N   
889  C CA  . VAL   A 114 ? 0.2287 0.1279 0.2855 -0.0375 0.0975  -0.0551 120 VAL   A CA  
890  C C   . VAL   A 114 ? 0.2356 0.1383 0.2418 -0.0487 0.0890  -0.0528 120 VAL   A C   
891  O O   . VAL   A 114 ? 0.2582 0.1379 0.2381 -0.0630 0.1064  -0.0568 120 VAL   A O   
892  C CB  . VAL   A 114 ? 0.2269 0.1318 0.3435 -0.0249 0.0944  -0.0505 120 VAL   A CB  
893  C CG1 . VAL   A 114 ? 0.2317 0.1554 0.3387 -0.0170 0.0645  -0.0441 120 VAL   A CG1 
894  C CG2 . VAL   A 114 ? 0.2136 0.1193 0.3922 -0.0156 0.0884  -0.0439 120 VAL   A CG2 
895  N N   . VAL   A 115 ? 0.2121 0.1379 0.2051 -0.0441 0.0644  -0.0441 121 VAL   A N   
896  C CA  . VAL   A 115 ? 0.2162 0.1517 0.1809 -0.0534 0.0520  -0.0345 121 VAL   A CA  
897  C C   . VAL   A 115 ? 0.2002 0.1530 0.1846 -0.0387 0.0406  -0.0290 121 VAL   A C   
898  O O   . VAL   A 115 ? 0.2046 0.1592 0.1779 -0.0461 0.0376  -0.0240 121 VAL   A O   
899  C CB  . VAL   A 115 ? 0.2218 0.1710 0.1751 -0.0569 0.0383  -0.0234 121 VAL   A CB  
900  C CG1 . VAL   A 115 ? 0.2276 0.1938 0.1773 -0.0635 0.0219  -0.0050 121 VAL   A CG1 
901  C CG2 . VAL   A 115 ? 0.2399 0.1662 0.1635 -0.0758 0.0470  -0.0280 121 VAL   A CG2 
902  N N   . GLY   A 116 ? 0.1876 0.1461 0.1930 -0.0207 0.0325  -0.0288 122 GLY   A N   
903  C CA  . GLY   A 116 ? 0.1867 0.1486 0.1978 -0.0088 0.0232  -0.0242 122 GLY   A CA  
904  C C   . GLY   A 116 ? 0.1959 0.1437 0.2092 0.0039  0.0127  -0.0243 122 GLY   A C   
905  O O   . GLY   A 116 ? 0.1877 0.1267 0.2090 0.0038  0.0097  -0.0276 122 GLY   A O   
906  N N   . ILE   A 117 ? 0.2011 0.1382 0.2026 0.0123  0.0061  -0.0201 123 ILE   A N   
907  C CA  . ILE   A 117 ? 0.2215 0.1253 0.2026 0.0184  -0.0064 -0.0193 123 ILE   A CA  
908  C C   . ILE   A 117 ? 0.2389 0.1228 0.1838 0.0267  0.0036  -0.0135 123 ILE   A C   
909  O O   . ILE   A 117 ? 0.2225 0.1203 0.1731 0.0304  0.0142  -0.0082 123 ILE   A O   
910  C CB  . ILE   A 117 ? 0.2367 0.1238 0.2308 0.0165  -0.0244 -0.0190 123 ILE   A CB  
911  C CG1 . ILE   A 117 ? 0.2534 0.1532 0.2541 0.0179  -0.0190 -0.0184 123 ILE   A CG1 
912  C CG2 . ILE   A 117 ? 0.2284 0.1227 0.2702 0.0106  -0.0321 -0.0195 123 ILE   A CG2 
913  C CD1 . ILE   A 117 ? 0.2897 0.1620 0.2879 0.0170  -0.0395 -0.0149 123 ILE   A CD1 
914  N N   . VAL   A 118 ? 0.2656 0.1079 0.1714 0.0289  0.0025  -0.0132 124 VAL   A N   
915  C CA  . VAL   A 118 ? 0.2899 0.0957 0.1549 0.0372  0.0232  -0.0082 124 VAL   A CA  
916  C C   . VAL   A 118 ? 0.3022 0.0862 0.1501 0.0399  0.0239  -0.0070 124 VAL   A C   
917  O O   . VAL   A 118 ? 0.2964 0.0614 0.1339 0.0327  -0.0006 -0.0105 124 VAL   A O   
918  C CB  . VAL   A 118 ? 0.3462 0.0887 0.1513 0.0346  0.0231  -0.0102 124 VAL   A CB  
919  C CG1 . VAL   A 118 ? 0.3955 0.0853 0.1516 0.0431  0.0570  -0.0059 124 VAL   A CG1 
920  C CG2 . VAL   A 118 ? 0.3414 0.1058 0.1641 0.0327  0.0235  -0.0111 124 VAL   A CG2 
921  N N   . SER   A 119 ? 0.3129 0.1032 0.1686 0.0497  0.0504  0.0009  125 SER   A N   
922  C CA  . SER   A 119 ? 0.3455 0.1160 0.1875 0.0534  0.0549  0.0026  125 SER   A CA  
923  C C   . SER   A 119 ? 0.4215 0.1421 0.2298 0.0646  0.0935  0.0098  125 SER   A C   
924  O O   . SER   A 119 ? 0.4608 0.1278 0.2217 0.0651  0.0997  0.0074  125 SER   A O   
925  C CB  . SER   A 119 ? 0.3150 0.1481 0.2153 0.0528  0.0488  0.0071  125 SER   A CB  
926  O OG  . SER   A 119 ? 0.3508 0.1712 0.2451 0.0574  0.0547  0.0103  125 SER   A OG  
927  N N   . THR   A 120 ? 0.4398 0.1743 0.2758 0.0734  0.1230  0.0205  126 THR   A N   
928  C CA  . THR   A 120 ? 0.4958 0.1805 0.3146 0.0867  0.1721  0.0308  126 THR   A CA  
929  C C   . THR   A 120 ? 0.5427 0.2032 0.3472 0.0892  0.1950  0.0331  126 THR   A C   
930  O O   . THR   A 120 ? 0.5196 0.2114 0.3339 0.0809  0.1685  0.0276  126 THR   A O   
931  C CB  . THR   A 120 ? 0.4650 0.2018 0.3676 0.0983  0.1931  0.0524  126 THR   A CB  
932  O OG1 . THR   A 120 ? 0.4305 0.2320 0.4080 0.0980  0.1898  0.0687  126 THR   A OG1 
933  C CG2 . THR   A 120 ? 0.4533 0.2246 0.3772 0.0940  0.1673  0.0512  126 THR   A CG2 
934  N N   . GLY   A 121 ? 0.6010 0.2082 0.3906 0.1014  0.2482  0.0427  127 GLY   A N   
935  C CA  . GLY   A 121 ? 0.6525 0.2362 0.4360 0.1053  0.2772  0.0473  127 GLY   A CA  
936  C C   . GLY   A 121 ? 0.7353 0.2406 0.4941 0.1196  0.3480  0.0574  127 GLY   A C   
937  O O   . GLY   A 121 ? 0.7366 0.2285 0.5178 0.1306  0.3793  0.0678  127 GLY   A O   
938  N N   . GLY   A 122 ? 0.8000 0.2484 0.5116 0.1192  0.3766  0.0544  128 GLY   A N   
939  C CA  . GLY   A 122 ? 0.8771 0.2353 0.5557 0.1318  0.4547  0.0628  128 GLY   A CA  
940  C C   . GLY   A 122 ? 0.8451 0.2611 0.6512 0.1511  0.4992  0.0935  128 GLY   A C   
941  O O   . GLY   A 122 ? 0.7782 0.2965 0.7066 0.1573  0.4782  0.1151  128 GLY   A O   
942  N N   . ASN   A 123 ? 0.8897 0.2302 0.6640 0.1586  0.5623  0.0980  129 ASN   A N   
943  C CA  . ASN   A 123 ? 0.8548 0.2204 0.7386 0.1772  0.6203  0.1292  129 ASN   A CA  
944  C C   . ASN   A 123 ? 0.7706 0.2275 0.7271 0.1712  0.5779  0.1382  129 ASN   A C   
945  O O   . ASN   A 123 ? 0.7140 0.2421 0.8055 0.1822  0.5929  0.1721  129 ASN   A O   
946  C CB  . ASN   A 123 ? 0.8492 0.2648 0.8664 0.1966  0.6545  0.1634  129 ASN   A CB  
947  C CG  . ASN   A 123 ? 1.0013 0.3021 0.9587 0.2093  0.7334  0.1618  129 ASN   A CG  
948  O OD1 . ASN   A 123 ? 1.1113 0.2892 0.9713 0.2118  0.8009  0.1512  129 ASN   A OD1 
949  N ND2 . ASN   A 123 ? 0.9878 0.3185 0.9990 0.2167  0.7313  0.1732  129 ASN   A ND2 
950  N N   . GLY   A 124 ? 0.7599 0.2062 0.6272 0.1528  0.5273  0.1108  130 GLY   A N   
951  C CA  . GLY   A 124 ? 0.6864 0.2142 0.6091 0.1449  0.4831  0.1152  130 GLY   A CA  
952  C C   . GLY   A 124 ? 0.5933 0.2350 0.5972 0.1366  0.4153  0.1218  130 GLY   A C   
953  O O   . GLY   A 124 ? 0.5526 0.2687 0.6239 0.1301  0.3832  0.1335  130 GLY   A O   
954  N N   . LEU   A 125 ? 0.5662 0.2133 0.5533 0.1341  0.3932  0.1134  131 LEU   A N   
955  C CA  . LEU   A 125 ? 0.4912 0.2274 0.5359 0.1243  0.3350  0.1168  131 LEU   A CA  
956  C C   . LEU   A 125 ? 0.4934 0.2094 0.4493 0.1109  0.2905  0.0852  131 LEU   A C   
957  O O   . LEU   A 125 ? 0.5690 0.2017 0.4306 0.1102  0.3053  0.0674  131 LEU   A O   
958  C CB  . LEU   A 125 ? 0.4597 0.2265 0.5879 0.1348  0.3529  0.1429  131 LEU   A CB  
959  C CG  . LEU   A 125 ? 0.4437 0.2410 0.6926 0.1481  0.3936  0.1847  131 LEU   A CG  
960  C CD1 . LEU   A 125 ? 0.4244 0.2318 0.7451 0.1600  0.4183  0.2096  131 LEU   A CD1 
961  C CD2 . LEU   A 125 ? 0.4037 0.2879 0.7365 0.1342  0.3474  0.2059  131 LEU   A CD2 
962  N N   . VAL   A 126 ? 0.4091 0.1948 0.3962 0.0982  0.2374  0.0811  132 VAL   A N   
963  C CA  . VAL   A 126 ? 0.3863 0.1673 0.3203 0.0867  0.1967  0.0576  132 VAL   A CA  
964  C C   . VAL   A 126 ? 0.3193 0.1705 0.3152 0.0806  0.1675  0.0660  132 VAL   A C   
965  O O   . VAL   A 126 ? 0.2769 0.1848 0.3370 0.0748  0.1557  0.0831  132 VAL   A O   
966  C CB  . VAL   A 126 ? 0.3944 0.1637 0.2797 0.0745  0.1668  0.0383  132 VAL   A CB  
967  C CG1 . VAL   A 126 ? 0.3607 0.1903 0.2999 0.0683  0.1519  0.0459  132 VAL   A CG1 
968  C CG2 . VAL   A 126 ? 0.4066 0.1728 0.2589 0.0636  0.1275  0.0206  132 VAL   A CG2 
969  N N   . GLY   A 127 ? 0.3071 0.1463 0.2784 0.0795  0.1559  0.0562  133 GLY   A N   
970  C CA  . GLY   A 127 ? 0.2653 0.1566 0.2786 0.0724  0.1305  0.0613  133 GLY   A CA  
971  C C   . GLY   A 127 ? 0.2687 0.1669 0.2514 0.0598  0.0951  0.0401  133 GLY   A C   
972  O O   . GLY   A 127 ? 0.3087 0.1633 0.2390 0.0597  0.0890  0.0244  133 GLY   A O   
973  N N   . PHE   A 128 ? 0.2147 0.1608 0.2298 0.0467  0.0721  0.0423  134 PHE   A N   
974  C CA  . PHE   A 128 ? 0.1935 0.1457 0.1921 0.0352  0.0486  0.0248  134 PHE   A CA  
975  C C   . PHE   A 128 ? 0.1634 0.1373 0.1782 0.0277  0.0379  0.0269  134 PHE   A C   
976  O O   . PHE   A 128 ? 0.1394 0.1408 0.1832 0.0196  0.0343  0.0432  134 PHE   A O   
977  C CB  . PHE   A 128 ? 0.1774 0.1490 0.1828 0.0230  0.0389  0.0217  134 PHE   A CB  
978  C CG  . PHE   A 128 ? 0.1928 0.1484 0.1860 0.0283  0.0474  0.0208  134 PHE   A CG  
979  C CD1 . PHE   A 128 ? 0.2155 0.1392 0.1763 0.0304  0.0422  0.0061  134 PHE   A CD1 
980  C CD2 . PHE   A 128 ? 0.1816 0.1537 0.2003 0.0286  0.0573  0.0378  134 PHE   A CD2 
981  C CE1 . PHE   A 128 ? 0.2318 0.1350 0.1744 0.0333  0.0490  0.0055  134 PHE   A CE1 
982  C CE2 . PHE   A 128 ? 0.1982 0.1536 0.2046 0.0334  0.0677  0.0366  134 PHE   A CE2 
983  C CZ  . PHE   A 128 ? 0.2181 0.1375 0.1813 0.0355  0.0640  0.0189  134 PHE   A CZ  
984  N N   . ALA   A 129 ? 0.1591 0.1179 0.1568 0.0278  0.0300  0.0133  135 ALA   A N   
985  C CA  . ALA   A 129 ? 0.1665 0.1411 0.1752 0.0197  0.0222  0.0128  135 ALA   A CA  
986  C C   . ALA   A 129 ? 0.1772 0.1635 0.1872 0.0030  0.0163  0.0056  135 ALA   A C   
987  O O   . ALA   A 129 ? 0.1722 0.1469 0.1785 0.0024  0.0159  -0.0068 135 ALA   A O   
988  C CB  . ALA   A 129 ? 0.1795 0.1315 0.1748 0.0253  0.0171  0.0028  135 ALA   A CB  
989  N N   . ASP   A 130 ? 0.1871 0.1884 0.2000 -0.0130 0.0120  0.0157  136 ASP   A N   
990  C CA  . ASP   A 130 ? 0.2150 0.2087 0.2089 -0.0340 0.0113  0.0087  136 ASP   A CA  
991  C C   . ASP   A 130 ? 0.2341 0.2110 0.2190 -0.0389 0.0197  -0.0060 136 ASP   A C   
992  O O   . ASP   A 130 ? 0.2390 0.2186 0.2302 -0.0345 0.0175  -0.0043 136 ASP   A O   
993  C CB  . ASP   A 130 ? 0.2497 0.2498 0.2360 -0.0557 -0.0022 0.0277  136 ASP   A CB  
994  C CG  . ASP   A 130 ? 0.3560 0.3300 0.3004 -0.0839 -0.0032 0.0223  136 ASP   A CG  
995  O OD1 . ASP   A 130 ? 0.3646 0.3307 0.2992 -0.0865 0.0024  0.0158  136 ASP   A OD1 
996  O OD2 . ASP   A 130 ? 0.4177 0.3712 0.3313 -0.1055 -0.0081 0.0247  136 ASP   A OD2 
997  N N   . VAL   A 131 ? 0.2322 0.1896 0.2074 -0.0472 0.0335  -0.0192 137 VAL   A N   
998  C CA  . VAL   A 131 ? 0.2469 0.1834 0.2235 -0.0521 0.0513  -0.0307 137 VAL   A CA  
999  C C   . VAL   A 131 ? 0.2946 0.1935 0.2267 -0.0782 0.0708  -0.0371 137 VAL   A C   
1000 O O   . VAL   A 131 ? 0.3237 0.1942 0.2527 -0.0839 0.0964  -0.0468 137 VAL   A O   
1001 C CB  . VAL   A 131 ? 0.2262 0.1628 0.2471 -0.0351 0.0581  -0.0380 137 VAL   A CB  
1002 C CG1 . VAL   A 131 ? 0.2141 0.1668 0.2540 -0.0168 0.0363  -0.0316 137 VAL   A CG1 
1003 C CG2 . VAL   A 131 ? 0.2269 0.1546 0.2544 -0.0363 0.0681  -0.0429 137 VAL   A CG2 
1004 N N   . ARG   A 132 ? 0.3056 0.1963 0.2002 -0.0960 0.0608  -0.0303 138 ARG   A N   
1005 C CA  . ARG   A 132 ? 0.3533 0.1920 0.1852 -0.1265 0.0765  -0.0357 138 ARG   A CA  
1006 C C   . ARG   A 132 ? 0.4084 0.2065 0.1864 -0.1520 0.0808  -0.0348 138 ARG   A C   
1007 O O   . ARG   A 132 ? 0.4605 0.1956 0.1781 -0.1761 0.1079  -0.0452 138 ARG   A O   
1008 C CB  . ARG   A 132 ? 0.3618 0.1999 0.1651 -0.1431 0.0551  -0.0238 138 ARG   A CB  
1009 C CG  . ARG   A 132 ? 0.3193 0.1862 0.1626 -0.1223 0.0551  -0.0262 138 ARG   A CG  
1010 C CD  . ARG   A 132 ? 0.3107 0.1798 0.1313 -0.1396 0.0321  -0.0108 138 ARG   A CD  
1011 N NE  . ARG   A 132 ? 0.2955 0.2063 0.1501 -0.1338 0.0021  0.0128  138 ARG   A NE  
1012 C CZ  . ARG   A 132 ? 0.3233 0.2504 0.1880 -0.1426 -0.0204 0.0337  138 ARG   A CZ  
1013 N NH1 . ARG   A 132 ? 0.3246 0.2277 0.1553 -0.1613 -0.0221 0.0328  138 ARG   A NH1 
1014 N NH2 . ARG   A 132 ? 0.3020 0.2672 0.2154 -0.1330 -0.0391 0.0578  138 ARG   A NH2 
1015 N N   . ASP   A 133 ? 0.3961 0.2212 0.1900 -0.1481 0.0580  -0.0227 139 ASP   A N   
1016 C CA  . ASP   A 133 ? 0.4361 0.2225 0.1790 -0.1728 0.0587  -0.0205 139 ASP   A CA  
1017 C C   . ASP   A 133 ? 0.4494 0.2194 0.2082 -0.1606 0.0943  -0.0374 139 ASP   A C   
1018 O O   . ASP   A 133 ? 0.4863 0.2103 0.1936 -0.1824 0.1062  -0.0400 139 ASP   A O   
1019 C CB  . ASP   A 133 ? 0.4289 0.2509 0.1893 -0.1748 0.0189  0.0029  139 ASP   A CB  
1020 C CG  . ASP   A 133 ? 0.4148 0.2944 0.2512 -0.1371 0.0155  0.0043  139 ASP   A CG  
1021 O OD1 . ASP   A 133 ? 0.3814 0.2853 0.2597 -0.1111 0.0258  -0.0046 139 ASP   A OD1 
1022 O OD2 . ASP   A 133 ? 0.4153 0.3094 0.2636 -0.1362 0.0006  0.0156  139 ASP   A OD2 
1023 N N   . LEU   A 134 ? 0.4207 0.2240 0.2509 -0.1287 0.1091  -0.0458 140 LEU   A N   
1024 C CA  . LEU   A 134 ? 0.4171 0.2129 0.2848 -0.1156 0.1379  -0.0553 140 LEU   A CA  
1025 C C   . LEU   A 134 ? 0.4691 0.2082 0.3195 -0.1261 0.1879  -0.0689 140 LEU   A C   
1026 O O   . LEU   A 134 ? 0.4445 0.1947 0.3571 -0.1075 0.2073  -0.0727 140 LEU   A O   
1027 C CB  . LEU   A 134 ? 0.3650 0.2139 0.3170 -0.0823 0.1236  -0.0521 140 LEU   A CB  
1028 C CG  . LEU   A 134 ? 0.3578 0.2508 0.3214 -0.0700 0.0839  -0.0400 140 LEU   A CG  
1029 C CD1 . LEU   A 134 ? 0.3320 0.2540 0.3536 -0.0439 0.0712  -0.0382 140 LEU   A CD1 
1030 C CD2 . LEU   A 134 ? 0.3699 0.2622 0.3116 -0.0785 0.0736  -0.0337 140 LEU   A CD2 
1031 N N   . LEU   A 135 ? 0.5426 0.2120 0.3050 -0.1585 0.2103  -0.0744 141 LEU   A N   
1032 C CA  . LEU   A 135 ? 0.6018 0.1948 0.3254 -0.1737 0.2686  -0.0885 141 LEU   A CA  
1033 C C   . LEU   A 135 ? 0.5958 0.1819 0.3943 -0.1534 0.3181  -0.0947 141 LEU   A C   
1034 O O   . LEU   A 135 ? 0.6050 0.1537 0.4254 -0.1503 0.3685  -0.1020 141 LEU   A O   
1035 C CB  . LEU   A 135 ? 0.6823 0.1839 0.2742 -0.2185 0.2807  -0.0924 141 LEU   A CB  
1036 C CG  . LEU   A 135 ? 0.7322 0.2313 0.2489 -0.2477 0.2245  -0.0783 141 LEU   A CG  
1037 C CD1 . LEU   A 135 ? 0.8283 0.2123 0.2024 -0.2991 0.2410  -0.0821 141 LEU   A CD1 
1038 C CD2 . LEU   A 135 ? 0.7306 0.2627 0.2668 -0.2414 0.2018  -0.0734 141 LEU   A CD2 
1039 N N   . TRP   A 136 ? 0.5687 0.1936 0.4176 -0.1386 0.3034  -0.0886 142 TRP   A N   
1040 C CA  . TRP   A 136 ? 0.5556 0.1792 0.4879 -0.1205 0.3437  -0.0887 142 TRP   A CA  
1041 C C   . TRP   A 136 ? 0.5381 0.2103 0.5908 -0.0910 0.3434  -0.0806 142 TRP   A C   
1042 O O   . TRP   A 136 ? 0.5168 0.1811 0.6522 -0.0787 0.3821  -0.0760 142 TRP   A O   
1043 C CB  . TRP   A 136 ? 0.5255 0.1762 0.4755 -0.1151 0.3225  -0.0828 142 TRP   A CB  
1044 C CG  . TRP   A 136 ? 0.4739 0.1983 0.4482 -0.1005 0.2562  -0.0722 142 TRP   A CG  
1045 C CD1 . TRP   A 136 ? 0.4935 0.2301 0.4039 -0.1133 0.2152  -0.0679 142 TRP   A CD1 
1046 C CD2 . TRP   A 136 ? 0.4124 0.1986 0.4808 -0.0725 0.2265  -0.0620 142 TRP   A CD2 
1047 N NE1 . TRP   A 136 ? 0.4528 0.2536 0.4131 -0.0915 0.1708  -0.0580 142 TRP   A NE1 
1048 C CE2 . TRP   A 136 ? 0.4098 0.2360 0.4556 -0.0684 0.1756  -0.0557 142 TRP   A CE2 
1049 C CE3 . TRP   A 136 ? 0.3769 0.1819 0.5464 -0.0531 0.2364  -0.0545 142 TRP   A CE3 
1050 C CZ2 . TRP   A 136 ? 0.3828 0.2550 0.4841 -0.0472 0.1401  -0.0466 142 TRP   A CZ2 
1051 C CZ3 . TRP   A 136 ? 0.3477 0.2019 0.5736 -0.0353 0.1902  -0.0425 142 TRP   A CZ3 
1052 C CH2 . TRP   A 136 ? 0.3525 0.2340 0.5347 -0.0331 0.1452  -0.0408 142 TRP   A CH2 
1053 N N   . LEU   A 137 ? 0.5418 0.2596 0.6081 -0.0815 0.3006  -0.0759 143 LEU   A N   
1054 C CA  . LEU   A 137 ? 0.5278 0.2837 0.6965 -0.0587 0.2929  -0.0661 143 LEU   A CA  
1055 C C   . LEU   A 137 ? 0.5913 0.3029 0.7967 -0.0594 0.3531  -0.0690 143 LEU   A C   
1056 O O   . LEU   A 137 ? 0.5524 0.2872 0.8692 -0.0415 0.3589  -0.0555 143 LEU   A O   
1057 C CB  . LEU   A 137 ? 0.5062 0.3047 0.6605 -0.0526 0.2407  -0.0627 143 LEU   A CB  
1058 C CG  . LEU   A 137 ? 0.4939 0.3373 0.6391 -0.0449 0.1867  -0.0558 143 LEU   A CG  
1059 C CD1 . LEU   A 137 ? 0.4934 0.3629 0.6132 -0.0413 0.1502  -0.0537 143 LEU   A CD1 
1060 C CD2 . LEU   A 137 ? 0.4540 0.3252 0.6841 -0.0278 0.1686  -0.0433 143 LEU   A CD2 
1061 N N   . ASP   A 138 ? 0.6872 0.3289 0.7985 -0.0824 0.3970  -0.0841 144 ASP   A N   
1062 C CA  . ASP   A 138 ? 0.7489 0.3306 0.8742 -0.0860 0.4653  -0.0897 144 ASP   A CA  
1063 C C   . ASP   A 138 ? 0.8062 0.3317 0.9620 -0.0873 0.5367  -0.0908 144 ASP   A C   
1064 O O   . ASP   A 138 ? 0.8077 0.3016 1.0347 -0.0786 0.5965  -0.0871 144 ASP   A O   
1065 C CB  . ASP   A 138 ? 0.8422 0.3557 0.8305 -0.1158 0.4812  -0.1059 144 ASP   A CB  
1066 C CG  . ASP   A 138 ? 0.8816 0.4414 0.8449 -0.1156 0.4228  -0.1037 144 ASP   A CG  
1067 O OD1 . ASP   A 138 ? 0.8390 0.4582 0.8954 -0.0917 0.3984  -0.0936 144 ASP   A OD1 
1068 O OD2 . ASP   A 138 ? 0.9547 0.4874 0.8061 -0.1414 0.4000  -0.1094 144 ASP   A OD2 
1069 N N   . GLU   A 139 ? 0.8562 0.3602 0.9537 -0.1000 0.5375  -0.0958 145 GLU   A N   
1070 C CA  . GLU   A 139 ? 0.9033 0.3424 1.0120 -0.1047 0.6108  -0.0987 145 GLU   A CA  
1071 C C   . GLU   A 139 ? 0.8623 0.3589 1.0853 -0.0833 0.5950  -0.0822 145 GLU   A C   
1072 O O   . GLU   A 139 ? 0.8822 0.3325 1.1353 -0.0837 0.6569  -0.0811 145 GLU   A O   
1073 C CB  . GLU   A 139 ? 1.0308 0.3759 0.9687 -0.1425 0.6348  -0.1174 145 GLU   A CB  
1074 C CG  . GLU   A 139 ? 1.1025 0.4887 0.9672 -0.1548 0.5576  -0.1164 145 GLU   A CG  
1075 C CD  . GLU   A 139 ? 1.2610 0.5802 0.9589 -0.1951 0.5408  -0.1272 145 GLU   A CD  
1076 O OE1 . GLU   A 139 ? 1.3008 0.6114 0.9227 -0.2152 0.5058  -0.1259 145 GLU   A OE1 
1077 O OE2 . GLU   A 139 ? 1.3262 0.6005 0.9721 -0.2084 0.5586  -0.1341 145 GLU   A OE2 
1078 N N1  . A1B2N B .   ? 0.6012 0.3038 0.4148 0.0769  0.1125  0.0192  201 A1B2N A N1  
1079 C C4  . A1B2N B .   ? 0.9986 0.4115 0.5114 0.0473  0.1467  -0.0059 201 A1B2N A C4  
1080 C C5  . A1B2N B .   ? 1.0141 0.3804 0.4887 0.0482  0.1598  -0.0061 201 A1B2N A C5  
1081 C C6  . A1B2N B .   ? 1.0492 0.3510 0.4872 0.0601  0.2217  -0.0017 201 A1B2N A C6  
1082 C C7  . A1B2N B .   ? 1.0230 0.2808 0.4285 0.0621  0.2371  -0.0016 201 A1B2N A C7  
1083 C C8  . A1B2N B .   ? 0.8981 0.2621 0.4246 0.0806  0.2435  0.0101  201 A1B2N A C8  
1084 C C10 . A1B2N B .   ? 0.8706 0.2209 0.3330 0.0442  0.1243  -0.0063 201 A1B2N A C10 
1085 C C13 . A1B2N B .   ? 0.6526 0.2801 0.4090 0.0828  0.1429  0.0198  201 A1B2N A C13 
1086 O O3  . A1B2N B .   ? 0.6411 0.2646 0.4133 0.0919  0.1654  0.0279  201 A1B2N A O3  
1087 C C12 . A1B2N B .   ? 0.7307 0.2661 0.3925 0.0752  0.1506  0.0104  201 A1B2N A C12 
1088 C C11 . A1B2N B .   ? 0.7893 0.2468 0.3623 0.0591  0.1238  0.0005  201 A1B2N A C11 
1089 C C9  . A1B2N B .   ? 0.9133 0.1973 0.3335 0.0566  0.1910  -0.0033 201 A1B2N A C9  
1090 C C14 . A1B2N B .   ? 0.7765 0.2510 0.4109 0.0884  0.2125  0.0179  201 A1B2N A C14 
1091 N N   . A1B2N B .   ? 0.8619 0.2352 0.3882 0.0765  0.2190  0.0075  201 A1B2N A N   
1092 O O2  . A1B2N B .   ? 0.8300 0.2649 0.4485 0.0955  0.2656  0.0233  201 A1B2N A O2  
1093 C C1  . A1B2N B .   ? 1.0927 0.3801 0.5400 0.0715  0.2706  0.0045  201 A1B2N A C1  
1094 S S   . A1B2N B .   ? 1.1652 0.3851 0.6056 0.0925  0.3644  0.0166  201 A1B2N A S   
1095 O O   . A1B2N B .   ? 1.1728 0.3726 0.6154 0.0985  0.4028  0.0217  201 A1B2N A O   
1096 O O1  . A1B2N B .   ? 1.1056 0.4113 0.6592 0.1103  0.3749  0.0322  201 A1B2N A O1  
1097 C C   . A1B2N B .   ? 1.2820 0.3324 0.5518 0.0762  0.3878  0.0028  201 A1B2N A C   
1098 C C3  . A1B2N B .   ? 1.0173 0.4153 0.5306 0.0571  0.1901  -0.0012 201 A1B2N A C3  
1099 C C2  . A1B2N B .   ? 1.0559 0.3909 0.5385 0.0693  0.2528  0.0047  201 A1B2N A C2  
# 
