data_7I31
# 
_entry.id   7I31 
# 
_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   7I31         pdb_00007i31 10.2210/pdb7i31/pdb 
WWPDB D_1001408252 ?            ?                   
# 
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                        7I31 
_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 2   3.4.22.29 ? ? ? 
2 non-polymer syn '(3S)-1-(ethenesulfonyl)piperidine-3-carboxamide' 218.273   1   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                        65.409    2   ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                              78.133    2   ?         ? ? ? 
5 water       nat water                                             18.015    306 ?         ? ? ? 
# 
_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,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '(3S)-1-(ethenesulfonyl)piperidine-3-carboxamide' A1B03 
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 
A1B03 non-polymer         . '(3S)-1-(ethenesulfonyl)piperidine-3-carboxamide' ? 'C8 H14 N2 O3 S' 218.273 
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 140 146 146 GLU GLU 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 
B 1 1   SER 1   7   7   SER SER C . n 
B 1 2   GLY 2   8   8   GLY GLY C . n 
B 1 3   ALA 3   9   9   ALA ALA C . n 
B 1 4   ILE 4   10  10  ILE ILE C . n 
B 1 5   TYR 5   11  11  TYR TYR C . n 
B 1 6   VAL 6   12  12  VAL VAL C . n 
B 1 7   GLY 7   13  13  GLY GLY C . n 
B 1 8   ASN 8   14  14  ASN ASN C . n 
B 1 9   TYR 9   15  15  TYR TYR C . n 
B 1 10  ARG 10  16  16  ARG ARG C . n 
B 1 11  VAL 11  17  17  VAL VAL C . n 
B 1 12  VAL 12  18  18  VAL VAL C . n 
B 1 13  ASN 13  19  19  ASN ASN C . n 
B 1 14  ARG 14  20  20  ARG ARG C . n 
B 1 15  HIS 15  21  21  HIS HIS C . n 
B 1 16  LEU 16  22  22  LEU LEU C . n 
B 1 17  ALA 17  23  23  ALA ALA C . n 
B 1 18  THR 18  24  24  THR THR C . n 
B 1 19  HIS 19  25  25  HIS HIS C . n 
B 1 20  ASN 20  26  26  ASN ASN C . n 
B 1 21  ASP 21  27  27  ASP ASP C . n 
B 1 22  TRP 22  28  28  TRP TRP C . n 
B 1 23  ALA 23  29  29  ALA ALA C . n 
B 1 24  ASN 24  30  30  ASN ASN C . n 
B 1 25  LEU 25  31  31  LEU LEU C . n 
B 1 26  VAL 26  32  32  VAL VAL C . n 
B 1 27  TRP 27  33  33  TRP TRP C . n 
B 1 28  GLU 28  34  34  GLU GLU C . n 
B 1 29  ASP 29  35  35  ASP ASP C . n 
B 1 30  SER 30  36  36  SER SER C . n 
B 1 31  SER 31  37  37  SER SER C . n 
B 1 32  ARG 32  38  38  ARG ARG C . n 
B 1 33  ASP 33  39  39  ASP ASP C . n 
B 1 34  LEU 34  40  40  LEU LEU C . n 
B 1 35  LEU 35  41  41  LEU LEU C . n 
B 1 36  VAL 36  42  42  VAL VAL C . n 
B 1 37  SER 37  43  43  SER SER C . n 
B 1 38  SER 38  44  44  SER SER C . n 
B 1 39  THR 39  45  45  THR THR C . n 
B 1 40  THR 40  46  46  THR THR C . n 
B 1 41  ALA 41  47  47  ALA ALA C . n 
B 1 42  GLN 42  48  48  GLN GLN C . n 
B 1 43  GLY 43  49  49  GLY GLY C . n 
B 1 44  CYS 44  50  50  CYS CYS C . n 
B 1 45  ASP 45  51  51  ASP ASP C . n 
B 1 46  THR 46  52  52  THR THR C . n 
B 1 47  ILE 47  53  53  ILE ILE C . n 
B 1 48  ALA 48  54  54  ALA ALA C . n 
B 1 49  ARG 49  55  55  ARG ARG C . n 
B 1 50  CYS 50  56  56  CYS CYS C . n 
B 1 51  ASP 51  57  57  ASP ASP C . n 
B 1 52  CYS 52  58  58  CYS CYS C . n 
B 1 53  GLN 53  59  59  GLN GLN C . n 
B 1 54  THR 54  60  60  THR THR C . n 
B 1 55  GLY 55  61  61  GLY GLY C . n 
B 1 56  VAL 56  62  62  VAL VAL C . n 
B 1 57  TYR 57  63  63  TYR TYR C . n 
B 1 58  TYR 58  64  64  TYR TYR C . n 
B 1 59  CYS 59  65  65  CYS CYS C . n 
B 1 60  SER 60  66  66  SER SER C . n 
B 1 61  SER 61  67  67  SER SER C . n 
B 1 62  ARG 62  68  68  ARG ARG C . n 
B 1 63  ARG 63  69  69  ARG ARG C . n 
B 1 64  LYS 64  70  70  LYS LYS C . n 
B 1 65  HIS 65  71  71  HIS HIS C . n 
B 1 66  TYR 66  72  72  TYR TYR C . n 
B 1 67  PRO 67  73  73  PRO PRO C . n 
B 1 68  VAL 68  74  74  VAL VAL C . n 
B 1 69  SER 69  75  75  SER SER C . n 
B 1 70  PHE 70  76  76  PHE PHE C . n 
B 1 71  SER 71  77  77  SER SER C . n 
B 1 72  LYS 72  78  78  LYS LYS C . n 
B 1 73  PRO 73  79  79  PRO PRO C . n 
B 1 74  SER 74  80  80  SER SER C . n 
B 1 75  LEU 75  81  81  LEU LEU C . n 
B 1 76  ILE 76  82  82  ILE ILE C . n 
B 1 77  PHE 77  83  83  PHE PHE C . n 
B 1 78  VAL 78  84  84  VAL VAL C . n 
B 1 79  GLU 79  85  85  GLU GLU C . n 
B 1 80  ALA 80  86  86  ALA ALA C . n 
B 1 81  SER 81  87  87  SER SER C . n 
B 1 82  GLU 82  88  88  GLU GLU C . n 
B 1 83  TYR 83  89  89  TYR TYR C . n 
B 1 84  TYR 84  90  90  TYR TYR C . n 
B 1 85  PRO 85  91  91  PRO PRO C . n 
B 1 86  ALA 86  92  92  ALA ALA C . n 
B 1 87  ARG 87  93  93  ARG ARG C . n 
B 1 88  TYR 88  94  94  TYR TYR C . n 
B 1 89  GLN 89  95  95  GLN GLN C . n 
B 1 90  SER 90  96  96  SER SER C . n 
B 1 91  HIS 91  97  97  HIS HIS C . n 
B 1 92  LEU 92  98  98  LEU LEU C . n 
B 1 93  MET 93  99  99  MET MET C . n 
B 1 94  LEU 94  100 100 LEU LEU C . n 
B 1 95  ALA 95  101 101 ALA ALA C . n 
B 1 96  VAL 96  102 102 VAL VAL C . n 
B 1 97  GLY 97  103 103 GLY GLY C . n 
B 1 98  HIS 98  104 104 HIS HIS C . n 
B 1 99  SER 99  105 105 SER SER C . n 
B 1 100 GLU 100 106 106 GLU GLU C . n 
B 1 101 PRO 101 107 107 PRO PRO C . n 
B 1 102 GLY 102 108 108 GLY GLY C . n 
B 1 103 ASP 103 109 109 ASP ASP C . n 
B 1 104 CYS 104 110 110 CYS CYS C . n 
B 1 105 GLY 105 111 111 GLY GLY C . n 
B 1 106 GLY 106 112 112 GLY GLY C . n 
B 1 107 ILE 107 113 113 ILE ILE C . n 
B 1 108 LEU 108 114 114 LEU LEU C . n 
B 1 109 ARG 109 115 115 ARG ARG C . n 
B 1 110 CYS 110 116 116 CYS CYS C . n 
B 1 111 GLN 111 117 117 GLN GLN C . n 
B 1 112 HIS 112 118 118 HIS HIS C . n 
B 1 113 GLY 113 119 119 GLY GLY C . n 
B 1 114 VAL 114 120 120 VAL VAL C . n 
B 1 115 VAL 115 121 121 VAL VAL C . n 
B 1 116 GLY 116 122 122 GLY GLY C . n 
B 1 117 ILE 117 123 123 ILE ILE C . n 
B 1 118 VAL 118 124 124 VAL VAL C . n 
B 1 119 SER 119 125 125 SER SER C . n 
B 1 120 THR 120 126 126 THR THR C . n 
B 1 121 GLY 121 127 127 GLY GLY C . n 
B 1 122 GLY 122 128 128 GLY GLY C . n 
B 1 123 ASN 123 129 129 ASN ASN C . n 
B 1 124 GLY 124 130 130 GLY GLY C . n 
B 1 125 LEU 125 131 131 LEU LEU C . n 
B 1 126 VAL 126 132 132 VAL VAL C . n 
B 1 127 GLY 127 133 133 GLY GLY C . n 
B 1 128 PHE 128 134 134 PHE PHE C . n 
B 1 129 ALA 129 135 135 ALA ALA C . n 
B 1 130 ASP 130 136 136 ASP ASP C . n 
B 1 131 VAL 131 137 137 VAL VAL C . n 
B 1 132 ARG 132 138 138 ARG ARG C . n 
B 1 133 ASP 133 139 139 ASP ASP C . n 
B 1 134 LEU 134 140 140 LEU LEU C . n 
B 1 135 LEU 135 141 141 LEU LEU C . n 
B 1 136 TRP 136 142 142 TRP TRP C . n 
B 1 137 LEU 137 143 143 LEU LEU C . n 
B 1 138 ASP 138 144 144 ASP ASP C . n 
B 1 139 GLU 139 145 145 GLU GLU C . n 
B 1 140 GLU 140 146 146 GLU GLU C . n 
B 1 141 ALA 141 147 ?   ?   ?   C . n 
B 1 142 MET 142 148 ?   ?   ?   C . n 
B 1 143 GLU 143 149 ?   ?   ?   C . n 
B 1 144 GLN 144 150 ?   ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1B03 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1B03 
_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 
C 2 A1B03 1   201 201 A1B03 LIG A . 
D 3 ZN    1   202 1   ZN    ZN  A . 
E 4 DMS   1   203 2   DMS   DMS A . 
F 3 ZN    1   201 1   ZN    ZN  C . 
G 4 DMS   1   202 1   DMS   DMS C . 
H 5 HOH   1   301 306 HOH   HOH A . 
H 5 HOH   2   302 299 HOH   HOH A . 
H 5 HOH   3   303 162 HOH   HOH A . 
H 5 HOH   4   304 99  HOH   HOH A . 
H 5 HOH   5   305 65  HOH   HOH A . 
H 5 HOH   6   306 107 HOH   HOH A . 
H 5 HOH   7   307 250 HOH   HOH A . 
H 5 HOH   8   308 188 HOH   HOH A . 
H 5 HOH   9   309 128 HOH   HOH A . 
H 5 HOH   10  310 298 HOH   HOH A . 
H 5 HOH   11  311 115 HOH   HOH A . 
H 5 HOH   12  312 141 HOH   HOH A . 
H 5 HOH   13  313 56  HOH   HOH A . 
H 5 HOH   14  314 277 HOH   HOH A . 
H 5 HOH   15  315 12  HOH   HOH A . 
H 5 HOH   16  316 133 HOH   HOH A . 
H 5 HOH   17  317 70  HOH   HOH A . 
H 5 HOH   18  318 11  HOH   HOH A . 
H 5 HOH   19  319 38  HOH   HOH A . 
H 5 HOH   20  320 132 HOH   HOH A . 
H 5 HOH   21  321 137 HOH   HOH A . 
H 5 HOH   22  322 84  HOH   HOH A . 
H 5 HOH   23  323 113 HOH   HOH A . 
H 5 HOH   24  324 178 HOH   HOH A . 
H 5 HOH   25  325 28  HOH   HOH A . 
H 5 HOH   26  326 121 HOH   HOH A . 
H 5 HOH   27  327 222 HOH   HOH A . 
H 5 HOH   28  328 68  HOH   HOH A . 
H 5 HOH   29  329 95  HOH   HOH A . 
H 5 HOH   30  330 184 HOH   HOH A . 
H 5 HOH   31  331 41  HOH   HOH A . 
H 5 HOH   32  332 1   HOH   HOH A . 
H 5 HOH   33  333 14  HOH   HOH A . 
H 5 HOH   34  334 122 HOH   HOH A . 
H 5 HOH   35  335 50  HOH   HOH A . 
H 5 HOH   36  336 93  HOH   HOH A . 
H 5 HOH   37  337 119 HOH   HOH A . 
H 5 HOH   38  338 33  HOH   HOH A . 
H 5 HOH   39  339 43  HOH   HOH A . 
H 5 HOH   40  340 246 HOH   HOH A . 
H 5 HOH   41  341 269 HOH   HOH A . 
H 5 HOH   42  342 3   HOH   HOH A . 
H 5 HOH   43  343 78  HOH   HOH A . 
H 5 HOH   44  344 69  HOH   HOH A . 
H 5 HOH   45  345 270 HOH   HOH A . 
H 5 HOH   46  346 53  HOH   HOH A . 
H 5 HOH   47  347 15  HOH   HOH A . 
H 5 HOH   48  348 234 HOH   HOH A . 
H 5 HOH   49  349 247 HOH   HOH A . 
H 5 HOH   50  350 90  HOH   HOH A . 
H 5 HOH   51  351 25  HOH   HOH A . 
H 5 HOH   52  352 181 HOH   HOH A . 
H 5 HOH   53  353 202 HOH   HOH A . 
H 5 HOH   54  354 194 HOH   HOH A . 
H 5 HOH   55  355 4   HOH   HOH A . 
H 5 HOH   56  356 102 HOH   HOH A . 
H 5 HOH   57  357 204 HOH   HOH A . 
H 5 HOH   58  358 304 HOH   HOH A . 
H 5 HOH   59  359 7   HOH   HOH A . 
H 5 HOH   60  360 209 HOH   HOH A . 
H 5 HOH   61  361 88  HOH   HOH A . 
H 5 HOH   62  362 10  HOH   HOH A . 
H 5 HOH   63  363 16  HOH   HOH A . 
H 5 HOH   64  364 77  HOH   HOH A . 
H 5 HOH   65  365 221 HOH   HOH A . 
H 5 HOH   66  366 192 HOH   HOH A . 
H 5 HOH   67  367 219 HOH   HOH A . 
H 5 HOH   68  368 42  HOH   HOH A . 
H 5 HOH   69  369 18  HOH   HOH A . 
H 5 HOH   70  370 167 HOH   HOH A . 
H 5 HOH   71  371 177 HOH   HOH A . 
H 5 HOH   72  372 316 HOH   HOH A . 
H 5 HOH   73  373 51  HOH   HOH A . 
H 5 HOH   74  374 103 HOH   HOH A . 
H 5 HOH   75  375 47  HOH   HOH A . 
H 5 HOH   76  376 36  HOH   HOH A . 
H 5 HOH   77  377 30  HOH   HOH A . 
H 5 HOH   78  378 117 HOH   HOH A . 
H 5 HOH   79  379 288 HOH   HOH A . 
H 5 HOH   80  380 220 HOH   HOH A . 
H 5 HOH   81  381 165 HOH   HOH A . 
H 5 HOH   82  382 156 HOH   HOH A . 
H 5 HOH   83  383 126 HOH   HOH A . 
H 5 HOH   84  384 212 HOH   HOH A . 
H 5 HOH   85  385 79  HOH   HOH A . 
H 5 HOH   86  386 147 HOH   HOH A . 
H 5 HOH   87  387 91  HOH   HOH A . 
H 5 HOH   88  388 118 HOH   HOH A . 
H 5 HOH   89  389 134 HOH   HOH A . 
H 5 HOH   90  390 17  HOH   HOH A . 
H 5 HOH   91  391 62  HOH   HOH A . 
H 5 HOH   92  392 130 HOH   HOH A . 
H 5 HOH   93  393 35  HOH   HOH A . 
H 5 HOH   94  394 64  HOH   HOH A . 
H 5 HOH   95  395 164 HOH   HOH A . 
H 5 HOH   96  396 303 HOH   HOH A . 
H 5 HOH   97  397 140 HOH   HOH A . 
H 5 HOH   98  398 146 HOH   HOH A . 
H 5 HOH   99  399 228 HOH   HOH A . 
H 5 HOH   100 400 296 HOH   HOH A . 
H 5 HOH   101 401 37  HOH   HOH A . 
H 5 HOH   102 402 57  HOH   HOH A . 
H 5 HOH   103 403 48  HOH   HOH A . 
H 5 HOH   104 404 129 HOH   HOH A . 
H 5 HOH   105 405 225 HOH   HOH A . 
H 5 HOH   106 406 87  HOH   HOH A . 
H 5 HOH   107 407 230 HOH   HOH A . 
H 5 HOH   108 408 235 HOH   HOH A . 
H 5 HOH   109 409 85  HOH   HOH A . 
H 5 HOH   110 410 248 HOH   HOH A . 
H 5 HOH   111 411 83  HOH   HOH A . 
H 5 HOH   112 412 302 HOH   HOH A . 
H 5 HOH   113 413 237 HOH   HOH A . 
H 5 HOH   114 414 286 HOH   HOH A . 
H 5 HOH   115 415 157 HOH   HOH A . 
H 5 HOH   116 416 216 HOH   HOH A . 
H 5 HOH   117 417 116 HOH   HOH A . 
H 5 HOH   118 418 275 HOH   HOH A . 
H 5 HOH   119 419 195 HOH   HOH A . 
H 5 HOH   120 420 227 HOH   HOH A . 
H 5 HOH   121 421 259 HOH   HOH A . 
H 5 HOH   122 422 223 HOH   HOH A . 
H 5 HOH   123 423 273 HOH   HOH A . 
H 5 HOH   124 424 174 HOH   HOH A . 
H 5 HOH   125 425 290 HOH   HOH A . 
H 5 HOH   126 426 171 HOH   HOH A . 
H 5 HOH   127 427 285 HOH   HOH A . 
H 5 HOH   128 428 201 HOH   HOH A . 
H 5 HOH   129 429 203 HOH   HOH A . 
H 5 HOH   130 430 251 HOH   HOH A . 
H 5 HOH   131 431 292 HOH   HOH A . 
H 5 HOH   132 432 199 HOH   HOH A . 
H 5 HOH   133 433 185 HOH   HOH A . 
H 5 HOH   134 434 187 HOH   HOH A . 
H 5 HOH   135 435 179 HOH   HOH A . 
H 5 HOH   136 436 245 HOH   HOH A . 
H 5 HOH   137 437 297 HOH   HOH A . 
H 5 HOH   138 438 293 HOH   HOH A . 
H 5 HOH   139 439 263 HOH   HOH A . 
I 5 HOH   1   301 236 HOH   HOH C . 
I 5 HOH   2   302 300 HOH   HOH C . 
I 5 HOH   3   303 166 HOH   HOH C . 
I 5 HOH   4   304 97  HOH   HOH C . 
I 5 HOH   5   305 63  HOH   HOH C . 
I 5 HOH   6   306 213 HOH   HOH C . 
I 5 HOH   7   307 76  HOH   HOH C . 
I 5 HOH   8   308 142 HOH   HOH C . 
I 5 HOH   9   309 152 HOH   HOH C . 
I 5 HOH   10  310 200 HOH   HOH C . 
I 5 HOH   11  311 217 HOH   HOH C . 
I 5 HOH   12  312 52  HOH   HOH C . 
I 5 HOH   13  313 131 HOH   HOH C . 
I 5 HOH   14  314 151 HOH   HOH C . 
I 5 HOH   15  315 191 HOH   HOH C . 
I 5 HOH   16  316 75  HOH   HOH C . 
I 5 HOH   17  317 58  HOH   HOH C . 
I 5 HOH   18  318 105 HOH   HOH C . 
I 5 HOH   19  319 20  HOH   HOH C . 
I 5 HOH   20  320 175 HOH   HOH C . 
I 5 HOH   21  321 172 HOH   HOH C . 
I 5 HOH   22  322 314 HOH   HOH C . 
I 5 HOH   23  323 196 HOH   HOH C . 
I 5 HOH   24  324 158 HOH   HOH C . 
I 5 HOH   25  325 66  HOH   HOH C . 
I 5 HOH   26  326 139 HOH   HOH C . 
I 5 HOH   27  327 163 HOH   HOH C . 
I 5 HOH   28  328 45  HOH   HOH C . 
I 5 HOH   29  329 305 HOH   HOH C . 
I 5 HOH   30  330 226 HOH   HOH C . 
I 5 HOH   31  331 9   HOH   HOH C . 
I 5 HOH   32  332 19  HOH   HOH C . 
I 5 HOH   33  333 61  HOH   HOH C . 
I 5 HOH   34  334 29  HOH   HOH C . 
I 5 HOH   35  335 67  HOH   HOH C . 
I 5 HOH   36  336 101 HOH   HOH C . 
I 5 HOH   37  337 310 HOH   HOH C . 
I 5 HOH   38  338 120 HOH   HOH C . 
I 5 HOH   39  339 8   HOH   HOH C . 
I 5 HOH   40  340 180 HOH   HOH C . 
I 5 HOH   41  341 86  HOH   HOH C . 
I 5 HOH   42  342 144 HOH   HOH C . 
I 5 HOH   43  343 106 HOH   HOH C . 
I 5 HOH   44  344 148 HOH   HOH C . 
I 5 HOH   45  345 138 HOH   HOH C . 
I 5 HOH   46  346 111 HOH   HOH C . 
I 5 HOH   47  347 40  HOH   HOH C . 
I 5 HOH   48  348 154 HOH   HOH C . 
I 5 HOH   49  349 6   HOH   HOH C . 
I 5 HOH   50  350 114 HOH   HOH C . 
I 5 HOH   51  351 311 HOH   HOH C . 
I 5 HOH   52  352 149 HOH   HOH C . 
I 5 HOH   53  353 92  HOH   HOH C . 
I 5 HOH   54  354 252 HOH   HOH C . 
I 5 HOH   55  355 73  HOH   HOH C . 
I 5 HOH   56  356 21  HOH   HOH C . 
I 5 HOH   57  357 135 HOH   HOH C . 
I 5 HOH   58  358 276 HOH   HOH C . 
I 5 HOH   59  359 260 HOH   HOH C . 
I 5 HOH   60  360 193 HOH   HOH C . 
I 5 HOH   61  361 258 HOH   HOH C . 
I 5 HOH   62  362 2   HOH   HOH C . 
I 5 HOH   63  363 24  HOH   HOH C . 
I 5 HOH   64  364 127 HOH   HOH C . 
I 5 HOH   65  365 110 HOH   HOH C . 
I 5 HOH   66  366 153 HOH   HOH C . 
I 5 HOH   67  367 240 HOH   HOH C . 
I 5 HOH   68  368 160 HOH   HOH C . 
I 5 HOH   69  369 46  HOH   HOH C . 
I 5 HOH   70  370 150 HOH   HOH C . 
I 5 HOH   71  371 231 HOH   HOH C . 
I 5 HOH   72  372 44  HOH   HOH C . 
I 5 HOH   73  373 27  HOH   HOH C . 
I 5 HOH   74  374 238 HOH   HOH C . 
I 5 HOH   75  375 265 HOH   HOH C . 
I 5 HOH   76  376 81  HOH   HOH C . 
I 5 HOH   77  377 255 HOH   HOH C . 
I 5 HOH   78  378 71  HOH   HOH C . 
I 5 HOH   79  379 34  HOH   HOH C . 
I 5 HOH   80  380 104 HOH   HOH C . 
I 5 HOH   81  381 82  HOH   HOH C . 
I 5 HOH   82  382 22  HOH   HOH C . 
I 5 HOH   83  383 39  HOH   HOH C . 
I 5 HOH   84  384 13  HOH   HOH C . 
I 5 HOH   85  385 136 HOH   HOH C . 
I 5 HOH   86  386 266 HOH   HOH C . 
I 5 HOH   87  387 49  HOH   HOH C . 
I 5 HOH   88  388 198 HOH   HOH C . 
I 5 HOH   89  389 54  HOH   HOH C . 
I 5 HOH   90  390 232 HOH   HOH C . 
I 5 HOH   91  391 161 HOH   HOH C . 
I 5 HOH   92  392 239 HOH   HOH C . 
I 5 HOH   93  393 176 HOH   HOH C . 
I 5 HOH   94  394 80  HOH   HOH C . 
I 5 HOH   95  395 159 HOH   HOH C . 
I 5 HOH   96  396 108 HOH   HOH C . 
I 5 HOH   97  397 206 HOH   HOH C . 
I 5 HOH   98  398 313 HOH   HOH C . 
I 5 HOH   99  399 72  HOH   HOH C . 
I 5 HOH   100 400 74  HOH   HOH C . 
I 5 HOH   101 401 274 HOH   HOH C . 
I 5 HOH   102 402 123 HOH   HOH C . 
I 5 HOH   103 403 143 HOH   HOH C . 
I 5 HOH   104 404 183 HOH   HOH C . 
I 5 HOH   105 405 125 HOH   HOH C . 
I 5 HOH   106 406 215 HOH   HOH C . 
I 5 HOH   107 407 182 HOH   HOH C . 
I 5 HOH   108 408 112 HOH   HOH C . 
I 5 HOH   109 409 23  HOH   HOH C . 
I 5 HOH   110 410 168 HOH   HOH C . 
I 5 HOH   111 411 59  HOH   HOH C . 
I 5 HOH   112 412 32  HOH   HOH C . 
I 5 HOH   113 413 26  HOH   HOH C . 
I 5 HOH   114 414 55  HOH   HOH C . 
I 5 HOH   115 415 124 HOH   HOH C . 
I 5 HOH   116 416 189 HOH   HOH C . 
I 5 HOH   117 417 229 HOH   HOH C . 
I 5 HOH   118 418 31  HOH   HOH C . 
I 5 HOH   119 419 210 HOH   HOH C . 
I 5 HOH   120 420 170 HOH   HOH C . 
I 5 HOH   121 421 98  HOH   HOH C . 
I 5 HOH   122 422 96  HOH   HOH C . 
I 5 HOH   123 423 5   HOH   HOH C . 
I 5 HOH   124 424 233 HOH   HOH C . 
I 5 HOH   125 425 173 HOH   HOH C . 
I 5 HOH   126 426 207 HOH   HOH C . 
I 5 HOH   127 427 308 HOH   HOH C . 
I 5 HOH   128 428 94  HOH   HOH C . 
I 5 HOH   129 429 272 HOH   HOH C . 
I 5 HOH   130 430 205 HOH   HOH C . 
I 5 HOH   131 431 60  HOH   HOH C . 
I 5 HOH   132 432 295 HOH   HOH C . 
I 5 HOH   133 433 294 HOH   HOH C . 
I 5 HOH   134 434 261 HOH   HOH C . 
I 5 HOH   135 435 190 HOH   HOH C . 
I 5 HOH   136 436 244 HOH   HOH C . 
I 5 HOH   137 437 315 HOH   HOH C . 
I 5 HOH   138 438 100 HOH   HOH C . 
I 5 HOH   139 439 145 HOH   HOH C . 
I 5 HOH   140 440 155 HOH   HOH C . 
I 5 HOH   141 441 214 HOH   HOH C . 
I 5 HOH   142 442 281 HOH   HOH C . 
I 5 HOH   143 443 312 HOH   HOH C . 
I 5 HOH   144 444 278 HOH   HOH C . 
I 5 HOH   145 445 109 HOH   HOH C . 
I 5 HOH   146 446 267 HOH   HOH C . 
I 5 HOH   147 447 307 HOH   HOH C . 
I 5 HOH   148 448 264 HOH   HOH C . 
I 5 HOH   149 449 268 HOH   HOH C . 
I 5 HOH   150 450 271 HOH   HOH C . 
I 5 HOH   151 451 287 HOH   HOH C . 
I 5 HOH   152 452 254 HOH   HOH C . 
I 5 HOH   153 453 218 HOH   HOH C . 
I 5 HOH   154 454 283 HOH   HOH C . 
I 5 HOH   155 455 241 HOH   HOH C . 
I 5 HOH   156 456 279 HOH   HOH C . 
I 5 HOH   157 457 256 HOH   HOH C . 
I 5 HOH   158 458 309 HOH   HOH C . 
I 5 HOH   159 459 211 HOH   HOH C . 
I 5 HOH   160 460 169 HOH   HOH C . 
I 5 HOH   161 461 243 HOH   HOH C . 
I 5 HOH   162 462 257 HOH   HOH C . 
I 5 HOH   163 463 301 HOH   HOH C . 
I 5 HOH   164 464 262 HOH   HOH C . 
I 5 HOH   165 465 280 HOH   HOH C . 
I 5 HOH   166 466 284 HOH   HOH C . 
I 5 HOH   167 467 289 HOH   HOH C . 
# 
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           7I31 
_cell.length_a           86.565 
_cell.length_b           56.958 
_cell.length_c           64.899 
_cell.angle_alpha        90.00 
_cell.angle_beta         94.81 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I31 
_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          7I31 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.51 
_exptl_crystal.density_percent_sol   50.96 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2024-11-13 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92202 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.92202 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7I31 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             39.17 
_reflns.d_resolution_high            1.15 
_reflns.number_obs                   84738 
_reflns.percent_possible_obs         76.0 
_reflns.pdbx_Rmerge_I_obs            0.037 
_reflns.pdbx_netI_over_sigmaI        28.8 
_reflns.pdbx_redundancy              5.3 
_reflns.pdbx_Rrim_I_all              0.040 
_reflns.pdbx_Rpim_I_all              0.016 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     449566 
_reflns.pdbx_chi_squared             1.34 
_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                  1.15 
_reflns_shell.d_res_low                   1.17 
_reflns_shell.number_measured_all         307 
_reflns_shell.number_unique_obs           307 
_reflns_shell.Rmerge_I_obs                0.260 
_reflns_shell.pdbx_chi_squared            0.15 
_reflns_shell.pdbx_redundancy             1.0 
_reflns_shell.percent_possible_obs        5.6 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.8 
_reflns_shell.pdbx_Rrim_I_all             0.500 
_reflns_shell.pdbx_Rpim_I_all             0.260 
_reflns_shell.pdbx_CC_half                0.080 
_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                                 7I31 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     84698 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             16.51 
_refine.ls_d_res_high                            1.150 
_refine.ls_percent_reflns_obs                    76.0 
_refine.ls_R_factor_obs                          0.1890 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1883 
_refine.ls_R_factor_R_free                       0.2022 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.020 
_refine.ls_number_reflns_R_free                  4253 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.961 
_refine.correlation_coeff_Fo_to_Fc_free          0.962 
_refine.B_iso_mean                               20.68 
_refine.aniso_B[1][1]                            -0.41430 
_refine.aniso_B[2][2]                            -0.90550 
_refine.aniso_B[3][3]                            1.31980 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -1.05350 
_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             0.043 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.044 
_refine.pdbx_overall_SU_R_Blow_DPI               0.045 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.045 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7I31 
_refine_analyze.Luzzati_coordinate_error_obs    0.15 
_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        2166 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         20 
_refine_hist.number_atoms_solvent             308 
_refine_hist.number_atoms_total               2494 
_refine_hist.d_res_high                       1.150 
_refine_hist.d_res_low                        16.51 
# 
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                  0.014 ? 2.00  2261 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.22  ? 2.00  3084 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  758  '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  395  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 2261 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           5.26  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           14.46 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  281  '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  1969 'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   51 
_refine_ls_shell.d_res_high                       1.15 
_refine_ls_shell.d_res_low                        1.20 
_refine_ls_shell.number_reflns_R_work             1604 
_refine_ls_shell.R_factor_R_work                  0.2895 
_refine_ls_shell.percent_reflns_obs               12.31 
_refine_ls_shell.R_factor_R_free                  0.3081 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            5.31 
_refine_ls_shell.number_reflns_R_free             90 
_refine_ls_shell.number_reflns_all                1694 
_refine_ls_shell.R_factor_all                     0.2904 
# 
_struct.entry_id                  7I31 
_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-0032235-001 (A71EV2A-x3408)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I31 
_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 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 3 ? 
G N N 4 ? 
H N N 5 ? 
I 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 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7I31 A 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
2 1 7I31 C 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,H 
2 1 B,F,G,I   
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2  AA2 THR A 18  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
HELX_P HELX_P3  AA3 SER A 30  ? ARG A 32  ? SER A 36  ARG A 38  5 ? 3 
HELX_P HELX_P4  AA4 SER A 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
HELX_P HELX_P5  AA5 LEU A 134 ? GLU A 139 ? LEU A 140 GLU A 145 5 ? 6 
HELX_P HELX_P6  AA6 HIS B 15  ? ALA B 17  ? HIS C 21  ALA C 23  5 ? 3 
HELX_P HELX_P7  AA7 THR B 18  ? ASN B 24  ? THR C 24  ASN C 30  1 ? 7 
HELX_P HELX_P8  AA8 SER B 30  ? ARG B 32  ? SER C 36  ARG C 38  5 ? 3 
HELX_P HELX_P9  AA9 SER B 60  ? ARG B 63  ? SER C 66  ARG C 69  5 ? 4 
HELX_P HELX_P10 AB1 GLU B 100 ? CYS B 104 ? GLU C 106 CYS C 110 5 ? 5 
HELX_P HELX_P11 AB2 LEU B 134 ? GLU B 139 ? LEU C 140 GLU C 145 5 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 50  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 56  A ZN 202 1_555 ? ? ? ? ? ? ? 2.287 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.244 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.325 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 D ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.167 ? ? 
metalc5 metalc ? ? B CYS 50  SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 56  C ZN 201 1_555 ? ? ? ? ? ? ? 2.335 ? ? 
metalc6 metalc ? ? B CYS 52  SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 58  C ZN 201 1_555 ? ? ? ? ? ? ? 2.323 ? ? 
metalc7 metalc ? ? B CYS 110 SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 116 C ZN 201 1_555 ? ? ? ? ? ? ? 2.291 ? ? 
metalc8 metalc ? ? B HIS 112 ND1 ? ? ? 1_555 F ZN . ZN ? ? C HIS 118 C ZN 201 1_555 ? ? ? ? ? ? ? 2.104 ? ? 
# 
_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 ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 52  ? A CYS 58  ? 1_555 114.6 ? 
2  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 108.3 ? 
3  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 117.0 ? 
4  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 103.3 ? 
5  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 101.1 ? 
6  SG ? A CYS 110 ? A CYS 116 ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 111.5 ? 
7  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 52  ? C CYS 58  ? 1_555 109.1 ? 
8  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 107.2 ? 
9  SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 118.3 ? 
10 SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 106.0 ? 
11 SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 101.0 ? 
12 SG ? B CYS 110 ? C CYS 116 ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 114.6 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 7 ? 
AA3 ? 3 ? 
AA4 ? 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 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA1 2 LEU A 34  ? CYS A 44  ? LEU A 40  CYS A 50  
AA1 3 ILE A 4   ? ASN A 13  ? ILE A 10  ASN A 19  
AA2 1 LYS A 64  ? SER A 69  ? LYS A 70  SER A 75  
AA2 2 THR A 54  ? CYS A 59  ? THR A 60  CYS A 65  
AA2 3 ILE A 107 ? CYS A 110 ? ILE A 113 CYS A 116 
AA2 4 GLY A 113 ? GLY A 122 ? GLY A 119 GLY A 128 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
AA3 1 LEU B 25  ? ASP B 29  ? LEU C 31  ASP C 35  
AA3 2 LEU B 34  ? CYS B 44  ? LEU C 40  CYS C 50  
AA3 3 ILE B 4   ? ASN B 13  ? ILE C 10  ASN C 19  
AA4 1 LYS B 64  ? SER B 69  ? LYS C 70  SER C 75  
AA4 2 THR B 54  ? CYS B 59  ? THR C 60  CYS C 65  
AA4 3 ILE B 107 ? CYS B 110 ? ILE C 113 CYS C 116 
AA4 4 GLY B 113 ? GLY B 122 ? GLY C 119 GLY C 128 
AA4 5 LEU B 125 ? ASP B 130 ? LEU C 131 ASP C 136 
AA4 6 ARG B 87  ? VAL B 96  ? ARG C 93  VAL C 102 
AA4 7 SER B 74  ? VAL B 78  ? SER C 80  VAL C 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 THR A 120 ? N THR A 126 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  
AA3 1 2 N TRP B 27  ? N TRP C 33  O VAL B 36  ? O VAL C 42  
AA3 2 3 N LEU B 35  ? N LEU C 41  O VAL B 12  ? O VAL C 18  
AA4 1 2 O LYS B 64  ? O LYS C 70  N CYS B 59  ? N CYS C 65  
AA4 2 3 N VAL B 56  ? N VAL C 62  O ARG B 109 ? O ARG C 115 
AA4 3 4 N LEU B 108 ? N LEU C 114 O VAL B 115 ? O VAL C 121 
AA4 4 5 N SER B 119 ? N SER C 125 O GLY B 127 ? O GLY C 133 
AA4 5 6 O PHE B 128 ? O PHE C 134 N MET B 93  ? N MET C 99  
AA4 6 7 O ARG B 87  ? O ARG C 93  N VAL B 78  ? N VAL C 84  
# 
_pdbx_entry_details.entry_id                   7I31 
_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_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            C 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            PRO 
_pdbx_validate_rmsd_bond.auth_seq_id_1             107 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            O 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            PRO 
_pdbx_validate_rmsd_bond.auth_seq_id_2             107 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.349 
_pdbx_validate_rmsd_bond.bond_target_value         1.228 
_pdbx_validate_rmsd_bond.bond_deviation            0.121 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.020 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CB A ARG 93  ? ? CA A ARG 93  ? ? C A ARG 93  ? ? 95.54  110.40 -14.86 2.00 N 
2 1 N  A PRO 107 ? ? CA A PRO 107 ? ? C A PRO 107 ? ? 81.59  112.10 -30.51 2.60 N 
3 1 CB A CYS 110 ? ? CA A CYS 110 ? ? C A CYS 110 ? ? 124.71 111.50 13.21  1.20 N 
4 1 O  A GLY 130 ? ? C  A GLY 130 ? ? N A LEU 131 ? ? 132.97 122.70 10.27  1.60 Y 
# 
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 CYS A 110 ? ? -38.66  137.91 
2 1 SER A 125 ? ? -166.42 -32.68 
3 1 VAL A 132 ? ? -162.14 105.64 
4 1 ALA A 135 ? ? -59.91  108.42 
# 
loop_
_pdbx_validate_main_chain_plane.id 
_pdbx_validate_main_chain_plane.PDB_model_num 
_pdbx_validate_main_chain_plane.auth_comp_id 
_pdbx_validate_main_chain_plane.auth_asym_id 
_pdbx_validate_main_chain_plane.auth_seq_id 
_pdbx_validate_main_chain_plane.PDB_ins_code 
_pdbx_validate_main_chain_plane.label_alt_id 
_pdbx_validate_main_chain_plane.improper_torsion_angle 
1 1 LEU A 81  ? ? 13.16 
2 1 VAL A 132 ? ? 10.89 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
'X-RAY DIFFRACTION' 1 ? refined 14.9003 8.2035   14.3383 -0.0153 -0.0158 0.0137 0.0149 0.0068  0.0105 2.2331 1.3635 0.8773 1.7108  
-0.9114 -0.8806 0.0349  0.1024 0.2013 0.1157 0.0866 0.0935  -0.0813 -0.1018 -0.1216 
'X-RAY DIFFRACTION' 2 ? refined 25.6666 -20.1148 17.8202 -0.0232 -0.0136 0.0211 0.0142 -0.0032 0.0222 0.9622 1.2409 0.1941 -0.6735 
-0.0964 -0.1343 -0.0264 0.0029 0.1447 0.0414 0.0622 -0.0249 0.0395  -0.0158 -0.0358 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_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 
'X-RAY DIFFRACTION' 1 1 ? ? ? ? ? ? ? ? ? '{ A|* }' 
'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? '{ C|* }' 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       439 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.91 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 ALA 147 ? A ALA 141 
2 1 Y 1 A MET 148 ? A MET 142 
3 1 Y 1 A GLU 149 ? A GLU 143 
4 1 Y 1 A GLN 150 ? A GLN 144 
5 1 Y 1 C ALA 147 ? B ALA 141 
6 1 Y 1 C MET 148 ? B MET 142 
7 1 Y 1 C GLU 149 ? B GLU 143 
8 1 Y 1 C GLN 150 ? B 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 
A1B03 N1   N  N N 1   
A1B03 C4   C  N N 2   
A1B03 C5   C  N S 3   
A1B03 C6   C  N N 4   
A1B03 C7   C  N N 5   
A1B03 O2   O  N N 6   
A1B03 C3   C  N N 7   
A1B03 C2   C  N N 8   
A1B03 N    N  N N 9   
A1B03 S    S  N N 10  
A1B03 O    O  N N 11  
A1B03 O1   O  N N 12  
A1B03 C1   C  N N 13  
A1B03 C    C  N N 14  
A1B03 H11  H  N N 15  
A1B03 H10  H  N N 16  
A1B03 H8   H  N N 17  
A1B03 H9   H  N N 18  
A1B03 H    H  N N 19  
A1B03 H12  H  N N 20  
A1B03 H13  H  N N 21  
A1B03 H6   H  N N 22  
A1B03 H7   H  N N 23  
A1B03 H4   H  N N 24  
A1B03 H5   H  N N 25  
A1B03 H3   H  N N 26  
A1B03 H2   H  N N 27  
A1B03 H1   H  N N 28  
ALA   N    N  N N 29  
ALA   CA   C  N S 30  
ALA   C    C  N N 31  
ALA   O    O  N N 32  
ALA   CB   C  N N 33  
ALA   OXT  O  N N 34  
ALA   H    H  N N 35  
ALA   H2   H  N N 36  
ALA   HA   H  N N 37  
ALA   HB1  H  N N 38  
ALA   HB2  H  N N 39  
ALA   HB3  H  N N 40  
ALA   HXT  H  N N 41  
ARG   N    N  N N 42  
ARG   CA   C  N S 43  
ARG   C    C  N N 44  
ARG   O    O  N N 45  
ARG   CB   C  N N 46  
ARG   CG   C  N N 47  
ARG   CD   C  N N 48  
ARG   NE   N  N N 49  
ARG   CZ   C  N N 50  
ARG   NH1  N  N N 51  
ARG   NH2  N  N N 52  
ARG   OXT  O  N N 53  
ARG   H    H  N N 54  
ARG   H2   H  N N 55  
ARG   HA   H  N N 56  
ARG   HB2  H  N N 57  
ARG   HB3  H  N N 58  
ARG   HG2  H  N N 59  
ARG   HG3  H  N N 60  
ARG   HD2  H  N N 61  
ARG   HD3  H  N N 62  
ARG   HE   H  N N 63  
ARG   HH11 H  N N 64  
ARG   HH12 H  N N 65  
ARG   HH21 H  N N 66  
ARG   HH22 H  N N 67  
ARG   HXT  H  N N 68  
ASN   N    N  N N 69  
ASN   CA   C  N S 70  
ASN   C    C  N N 71  
ASN   O    O  N N 72  
ASN   CB   C  N N 73  
ASN   CG   C  N N 74  
ASN   OD1  O  N N 75  
ASN   ND2  N  N N 76  
ASN   OXT  O  N N 77  
ASN   H    H  N N 78  
ASN   H2   H  N N 79  
ASN   HA   H  N N 80  
ASN   HB2  H  N N 81  
ASN   HB3  H  N N 82  
ASN   HD21 H  N N 83  
ASN   HD22 H  N N 84  
ASN   HXT  H  N N 85  
ASP   N    N  N N 86  
ASP   CA   C  N S 87  
ASP   C    C  N N 88  
ASP   O    O  N N 89  
ASP   CB   C  N N 90  
ASP   CG   C  N N 91  
ASP   OD1  O  N N 92  
ASP   OD2  O  N N 93  
ASP   OXT  O  N N 94  
ASP   H    H  N N 95  
ASP   H2   H  N N 96  
ASP   HA   H  N N 97  
ASP   HB2  H  N N 98  
ASP   HB3  H  N N 99  
ASP   HD2  H  N N 100 
ASP   HXT  H  N N 101 
CYS   N    N  N N 102 
CYS   CA   C  N R 103 
CYS   C    C  N N 104 
CYS   O    O  N N 105 
CYS   CB   C  N N 106 
CYS   SG   S  N N 107 
CYS   OXT  O  N N 108 
CYS   H    H  N N 109 
CYS   H2   H  N N 110 
CYS   HA   H  N N 111 
CYS   HB2  H  N N 112 
CYS   HB3  H  N N 113 
CYS   HG   H  N N 114 
CYS   HXT  H  N N 115 
DMS   S    S  N N 116 
DMS   O    O  N N 117 
DMS   C1   C  N N 118 
DMS   C2   C  N N 119 
DMS   H11  H  N N 120 
DMS   H12  H  N N 121 
DMS   H13  H  N N 122 
DMS   H21  H  N N 123 
DMS   H22  H  N N 124 
DMS   H23  H  N N 125 
GLN   N    N  N N 126 
GLN   CA   C  N S 127 
GLN   C    C  N N 128 
GLN   O    O  N N 129 
GLN   CB   C  N N 130 
GLN   CG   C  N N 131 
GLN   CD   C  N N 132 
GLN   OE1  O  N N 133 
GLN   NE2  N  N N 134 
GLN   OXT  O  N N 135 
GLN   H    H  N N 136 
GLN   H2   H  N N 137 
GLN   HA   H  N N 138 
GLN   HB2  H  N N 139 
GLN   HB3  H  N N 140 
GLN   HG2  H  N N 141 
GLN   HG3  H  N N 142 
GLN   HE21 H  N N 143 
GLN   HE22 H  N N 144 
GLN   HXT  H  N N 145 
GLU   N    N  N N 146 
GLU   CA   C  N S 147 
GLU   C    C  N N 148 
GLU   O    O  N N 149 
GLU   CB   C  N N 150 
GLU   CG   C  N N 151 
GLU   CD   C  N N 152 
GLU   OE1  O  N N 153 
GLU   OE2  O  N N 154 
GLU   OXT  O  N N 155 
GLU   H    H  N N 156 
GLU   H2   H  N N 157 
GLU   HA   H  N N 158 
GLU   HB2  H  N N 159 
GLU   HB3  H  N N 160 
GLU   HG2  H  N N 161 
GLU   HG3  H  N N 162 
GLU   HE2  H  N N 163 
GLU   HXT  H  N N 164 
GLY   N    N  N N 165 
GLY   CA   C  N N 166 
GLY   C    C  N N 167 
GLY   O    O  N N 168 
GLY   OXT  O  N N 169 
GLY   H    H  N N 170 
GLY   H2   H  N N 171 
GLY   HA2  H  N N 172 
GLY   HA3  H  N N 173 
GLY   HXT  H  N N 174 
HIS   N    N  N N 175 
HIS   CA   C  N S 176 
HIS   C    C  N N 177 
HIS   O    O  N N 178 
HIS   CB   C  N N 179 
HIS   CG   C  Y N 180 
HIS   ND1  N  Y N 181 
HIS   CD2  C  Y N 182 
HIS   CE1  C  Y N 183 
HIS   NE2  N  Y N 184 
HIS   OXT  O  N N 185 
HIS   H    H  N N 186 
HIS   H2   H  N N 187 
HIS   HA   H  N N 188 
HIS   HB2  H  N N 189 
HIS   HB3  H  N N 190 
HIS   HD1  H  N N 191 
HIS   HD2  H  N N 192 
HIS   HE1  H  N N 193 
HIS   HE2  H  N N 194 
HIS   HXT  H  N N 195 
HOH   O    O  N N 196 
HOH   H1   H  N N 197 
HOH   H2   H  N N 198 
ILE   N    N  N N 199 
ILE   CA   C  N S 200 
ILE   C    C  N N 201 
ILE   O    O  N N 202 
ILE   CB   C  N S 203 
ILE   CG1  C  N N 204 
ILE   CG2  C  N N 205 
ILE   CD1  C  N N 206 
ILE   OXT  O  N N 207 
ILE   H    H  N N 208 
ILE   H2   H  N N 209 
ILE   HA   H  N N 210 
ILE   HB   H  N N 211 
ILE   HG12 H  N N 212 
ILE   HG13 H  N N 213 
ILE   HG21 H  N N 214 
ILE   HG22 H  N N 215 
ILE   HG23 H  N N 216 
ILE   HD11 H  N N 217 
ILE   HD12 H  N N 218 
ILE   HD13 H  N N 219 
ILE   HXT  H  N N 220 
LEU   N    N  N N 221 
LEU   CA   C  N S 222 
LEU   C    C  N N 223 
LEU   O    O  N N 224 
LEU   CB   C  N N 225 
LEU   CG   C  N N 226 
LEU   CD1  C  N N 227 
LEU   CD2  C  N N 228 
LEU   OXT  O  N N 229 
LEU   H    H  N N 230 
LEU   H2   H  N N 231 
LEU   HA   H  N N 232 
LEU   HB2  H  N N 233 
LEU   HB3  H  N N 234 
LEU   HG   H  N N 235 
LEU   HD11 H  N N 236 
LEU   HD12 H  N N 237 
LEU   HD13 H  N N 238 
LEU   HD21 H  N N 239 
LEU   HD22 H  N N 240 
LEU   HD23 H  N N 241 
LEU   HXT  H  N N 242 
LYS   N    N  N N 243 
LYS   CA   C  N S 244 
LYS   C    C  N N 245 
LYS   O    O  N N 246 
LYS   CB   C  N N 247 
LYS   CG   C  N N 248 
LYS   CD   C  N N 249 
LYS   CE   C  N N 250 
LYS   NZ   N  N N 251 
LYS   OXT  O  N N 252 
LYS   H    H  N N 253 
LYS   H2   H  N N 254 
LYS   HA   H  N N 255 
LYS   HB2  H  N N 256 
LYS   HB3  H  N N 257 
LYS   HG2  H  N N 258 
LYS   HG3  H  N N 259 
LYS   HD2  H  N N 260 
LYS   HD3  H  N N 261 
LYS   HE2  H  N N 262 
LYS   HE3  H  N N 263 
LYS   HZ1  H  N N 264 
LYS   HZ2  H  N N 265 
LYS   HZ3  H  N N 266 
LYS   HXT  H  N N 267 
MET   N    N  N N 268 
MET   CA   C  N S 269 
MET   C    C  N N 270 
MET   O    O  N N 271 
MET   CB   C  N N 272 
MET   CG   C  N N 273 
MET   SD   S  N N 274 
MET   CE   C  N N 275 
MET   OXT  O  N N 276 
MET   H    H  N N 277 
MET   H2   H  N N 278 
MET   HA   H  N N 279 
MET   HB2  H  N N 280 
MET   HB3  H  N N 281 
MET   HG2  H  N N 282 
MET   HG3  H  N N 283 
MET   HE1  H  N N 284 
MET   HE2  H  N N 285 
MET   HE3  H  N N 286 
MET   HXT  H  N N 287 
PHE   N    N  N N 288 
PHE   CA   C  N S 289 
PHE   C    C  N N 290 
PHE   O    O  N N 291 
PHE   CB   C  N N 292 
PHE   CG   C  Y N 293 
PHE   CD1  C  Y N 294 
PHE   CD2  C  Y N 295 
PHE   CE1  C  Y N 296 
PHE   CE2  C  Y N 297 
PHE   CZ   C  Y N 298 
PHE   OXT  O  N N 299 
PHE   H    H  N N 300 
PHE   H2   H  N N 301 
PHE   HA   H  N N 302 
PHE   HB2  H  N N 303 
PHE   HB3  H  N N 304 
PHE   HD1  H  N N 305 
PHE   HD2  H  N N 306 
PHE   HE1  H  N N 307 
PHE   HE2  H  N N 308 
PHE   HZ   H  N N 309 
PHE   HXT  H  N N 310 
PRO   N    N  N N 311 
PRO   CA   C  N S 312 
PRO   C    C  N N 313 
PRO   O    O  N N 314 
PRO   CB   C  N N 315 
PRO   CG   C  N N 316 
PRO   CD   C  N N 317 
PRO   OXT  O  N N 318 
PRO   H    H  N N 319 
PRO   HA   H  N N 320 
PRO   HB2  H  N N 321 
PRO   HB3  H  N N 322 
PRO   HG2  H  N N 323 
PRO   HG3  H  N N 324 
PRO   HD2  H  N N 325 
PRO   HD3  H  N N 326 
PRO   HXT  H  N N 327 
SER   N    N  N N 328 
SER   CA   C  N S 329 
SER   C    C  N N 330 
SER   O    O  N N 331 
SER   CB   C  N N 332 
SER   OG   O  N N 333 
SER   OXT  O  N N 334 
SER   H    H  N N 335 
SER   H2   H  N N 336 
SER   HA   H  N N 337 
SER   HB2  H  N N 338 
SER   HB3  H  N N 339 
SER   HG   H  N N 340 
SER   HXT  H  N N 341 
THR   N    N  N N 342 
THR   CA   C  N S 343 
THR   C    C  N N 344 
THR   O    O  N N 345 
THR   CB   C  N R 346 
THR   OG1  O  N N 347 
THR   CG2  C  N N 348 
THR   OXT  O  N N 349 
THR   H    H  N N 350 
THR   H2   H  N N 351 
THR   HA   H  N N 352 
THR   HB   H  N N 353 
THR   HG1  H  N N 354 
THR   HG21 H  N N 355 
THR   HG22 H  N N 356 
THR   HG23 H  N N 357 
THR   HXT  H  N N 358 
TRP   N    N  N N 359 
TRP   CA   C  N S 360 
TRP   C    C  N N 361 
TRP   O    O  N N 362 
TRP   CB   C  N N 363 
TRP   CG   C  Y N 364 
TRP   CD1  C  Y N 365 
TRP   CD2  C  Y N 366 
TRP   NE1  N  Y N 367 
TRP   CE2  C  Y N 368 
TRP   CE3  C  Y N 369 
TRP   CZ2  C  Y N 370 
TRP   CZ3  C  Y N 371 
TRP   CH2  C  Y N 372 
TRP   OXT  O  N N 373 
TRP   H    H  N N 374 
TRP   H2   H  N N 375 
TRP   HA   H  N N 376 
TRP   HB2  H  N N 377 
TRP   HB3  H  N N 378 
TRP   HD1  H  N N 379 
TRP   HE1  H  N N 380 
TRP   HE3  H  N N 381 
TRP   HZ2  H  N N 382 
TRP   HZ3  H  N N 383 
TRP   HH2  H  N N 384 
TRP   HXT  H  N N 385 
TYR   N    N  N N 386 
TYR   CA   C  N S 387 
TYR   C    C  N N 388 
TYR   O    O  N N 389 
TYR   CB   C  N N 390 
TYR   CG   C  Y N 391 
TYR   CD1  C  Y N 392 
TYR   CD2  C  Y N 393 
TYR   CE1  C  Y N 394 
TYR   CE2  C  Y N 395 
TYR   CZ   C  Y N 396 
TYR   OH   O  N N 397 
TYR   OXT  O  N N 398 
TYR   H    H  N N 399 
TYR   H2   H  N N 400 
TYR   HA   H  N N 401 
TYR   HB2  H  N N 402 
TYR   HB3  H  N N 403 
TYR   HD1  H  N N 404 
TYR   HD2  H  N N 405 
TYR   HE1  H  N N 406 
TYR   HE2  H  N N 407 
TYR   HH   H  N N 408 
TYR   HXT  H  N N 409 
VAL   N    N  N N 410 
VAL   CA   C  N S 411 
VAL   C    C  N N 412 
VAL   O    O  N N 413 
VAL   CB   C  N N 414 
VAL   CG1  C  N N 415 
VAL   CG2  C  N N 416 
VAL   OXT  O  N N 417 
VAL   H    H  N N 418 
VAL   H2   H  N N 419 
VAL   HA   H  N N 420 
VAL   HB   H  N N 421 
VAL   HG11 H  N N 422 
VAL   HG12 H  N N 423 
VAL   HG13 H  N N 424 
VAL   HG21 H  N N 425 
VAL   HG22 H  N N 426 
VAL   HG23 H  N N 427 
VAL   HXT  H  N N 428 
ZN    ZN   ZN N N 429 
# 
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 
A1B03 C   C1   doub N N 1   
A1B03 C1  S    sing N N 2   
A1B03 O   S    doub N N 3   
A1B03 O1  S    doub N N 4   
A1B03 S   N    sing N N 5   
A1B03 N   C2   sing N N 6   
A1B03 C2  C3   sing N N 7   
A1B03 C3  C4   sing N N 8   
A1B03 C4  C5   sing N N 9   
A1B03 C5  C6   sing N N 10  
A1B03 N1  C6   sing N N 11  
A1B03 C6  O2   doub N N 12  
A1B03 C7  C5   sing N N 13  
A1B03 N   C7   sing N N 14  
A1B03 N1  H11  sing N N 15  
A1B03 N1  H10  sing N N 16  
A1B03 C4  H8   sing N N 17  
A1B03 C4  H9   sing N N 18  
A1B03 C5  H    sing N N 19  
A1B03 C7  H12  sing N N 20  
A1B03 C7  H13  sing N N 21  
A1B03 C3  H6   sing N N 22  
A1B03 C3  H7   sing N N 23  
A1B03 C2  H4   sing N N 24  
A1B03 C2  H5   sing N N 25  
A1B03 C1  H3   sing N N 26  
A1B03 C   H2   sing N N 27  
A1B03 C   H1   sing N N 28  
ALA   N   CA   sing N N 29  
ALA   N   H    sing N N 30  
ALA   N   H2   sing N N 31  
ALA   CA  C    sing N N 32  
ALA   CA  CB   sing N N 33  
ALA   CA  HA   sing N N 34  
ALA   C   O    doub N N 35  
ALA   C   OXT  sing N N 36  
ALA   CB  HB1  sing N N 37  
ALA   CB  HB2  sing N N 38  
ALA   CB  HB3  sing N N 39  
ALA   OXT HXT  sing N N 40  
ARG   N   CA   sing N N 41  
ARG   N   H    sing N N 42  
ARG   N   H2   sing N N 43  
ARG   CA  C    sing N N 44  
ARG   CA  CB   sing N N 45  
ARG   CA  HA   sing N N 46  
ARG   C   O    doub N N 47  
ARG   C   OXT  sing N N 48  
ARG   CB  CG   sing N N 49  
ARG   CB  HB2  sing N N 50  
ARG   CB  HB3  sing N N 51  
ARG   CG  CD   sing N N 52  
ARG   CG  HG2  sing N N 53  
ARG   CG  HG3  sing N N 54  
ARG   CD  NE   sing N N 55  
ARG   CD  HD2  sing N N 56  
ARG   CD  HD3  sing N N 57  
ARG   NE  CZ   sing N N 58  
ARG   NE  HE   sing N N 59  
ARG   CZ  NH1  sing N N 60  
ARG   CZ  NH2  doub N N 61  
ARG   NH1 HH11 sing N N 62  
ARG   NH1 HH12 sing N N 63  
ARG   NH2 HH21 sing N N 64  
ARG   NH2 HH22 sing N N 65  
ARG   OXT HXT  sing N N 66  
ASN   N   CA   sing N N 67  
ASN   N   H    sing N N 68  
ASN   N   H2   sing N N 69  
ASN   CA  C    sing N N 70  
ASN   CA  CB   sing N N 71  
ASN   CA  HA   sing N N 72  
ASN   C   O    doub N N 73  
ASN   C   OXT  sing N N 74  
ASN   CB  CG   sing N N 75  
ASN   CB  HB2  sing N N 76  
ASN   CB  HB3  sing N N 77  
ASN   CG  OD1  doub N N 78  
ASN   CG  ND2  sing N N 79  
ASN   ND2 HD21 sing N N 80  
ASN   ND2 HD22 sing N N 81  
ASN   OXT HXT  sing N N 82  
ASP   N   CA   sing N N 83  
ASP   N   H    sing N N 84  
ASP   N   H2   sing N N 85  
ASP   CA  C    sing N N 86  
ASP   CA  CB   sing N N 87  
ASP   CA  HA   sing N N 88  
ASP   C   O    doub N N 89  
ASP   C   OXT  sing N N 90  
ASP   CB  CG   sing N N 91  
ASP   CB  HB2  sing N N 92  
ASP   CB  HB3  sing N N 93  
ASP   CG  OD1  doub N N 94  
ASP   CG  OD2  sing N N 95  
ASP   OD2 HD2  sing N N 96  
ASP   OXT HXT  sing N N 97  
CYS   N   CA   sing N N 98  
CYS   N   H    sing N N 99  
CYS   N   H2   sing N N 100 
CYS   CA  C    sing N N 101 
CYS   CA  CB   sing N N 102 
CYS   CA  HA   sing N N 103 
CYS   C   O    doub N N 104 
CYS   C   OXT  sing N N 105 
CYS   CB  SG   sing N N 106 
CYS   CB  HB2  sing N N 107 
CYS   CB  HB3  sing N N 108 
CYS   SG  HG   sing N N 109 
CYS   OXT HXT  sing N N 110 
DMS   S   O    doub N N 111 
DMS   S   C1   sing N N 112 
DMS   S   C2   sing N N 113 
DMS   C1  H11  sing N N 114 
DMS   C1  H12  sing N N 115 
DMS   C1  H13  sing N N 116 
DMS   C2  H21  sing N N 117 
DMS   C2  H22  sing N N 118 
DMS   C2  H23  sing N N 119 
GLN   N   CA   sing N N 120 
GLN   N   H    sing N N 121 
GLN   N   H2   sing N N 122 
GLN   CA  C    sing N N 123 
GLN   CA  CB   sing N N 124 
GLN   CA  HA   sing N N 125 
GLN   C   O    doub N N 126 
GLN   C   OXT  sing N N 127 
GLN   CB  CG   sing N N 128 
GLN   CB  HB2  sing N N 129 
GLN   CB  HB3  sing N N 130 
GLN   CG  CD   sing N N 131 
GLN   CG  HG2  sing N N 132 
GLN   CG  HG3  sing N N 133 
GLN   CD  OE1  doub N N 134 
GLN   CD  NE2  sing N N 135 
GLN   NE2 HE21 sing N N 136 
GLN   NE2 HE22 sing N N 137 
GLN   OXT HXT  sing N N 138 
GLU   N   CA   sing N N 139 
GLU   N   H    sing N N 140 
GLU   N   H2   sing N N 141 
GLU   CA  C    sing N N 142 
GLU   CA  CB   sing N N 143 
GLU   CA  HA   sing N N 144 
GLU   C   O    doub N N 145 
GLU   C   OXT  sing N N 146 
GLU   CB  CG   sing N N 147 
GLU   CB  HB2  sing N N 148 
GLU   CB  HB3  sing N N 149 
GLU   CG  CD   sing N N 150 
GLU   CG  HG2  sing N N 151 
GLU   CG  HG3  sing N N 152 
GLU   CD  OE1  doub N N 153 
GLU   CD  OE2  sing N N 154 
GLU   OE2 HE2  sing N N 155 
GLU   OXT HXT  sing N N 156 
GLY   N   CA   sing N N 157 
GLY   N   H    sing N N 158 
GLY   N   H2   sing N N 159 
GLY   CA  C    sing N N 160 
GLY   CA  HA2  sing N N 161 
GLY   CA  HA3  sing N N 162 
GLY   C   O    doub N N 163 
GLY   C   OXT  sing N N 164 
GLY   OXT HXT  sing N N 165 
HIS   N   CA   sing N N 166 
HIS   N   H    sing N N 167 
HIS   N   H2   sing N N 168 
HIS   CA  C    sing N N 169 
HIS   CA  CB   sing N N 170 
HIS   CA  HA   sing N N 171 
HIS   C   O    doub N N 172 
HIS   C   OXT  sing N N 173 
HIS   CB  CG   sing N N 174 
HIS   CB  HB2  sing N N 175 
HIS   CB  HB3  sing N N 176 
HIS   CG  ND1  sing Y N 177 
HIS   CG  CD2  doub Y N 178 
HIS   ND1 CE1  doub Y N 179 
HIS   ND1 HD1  sing N N 180 
HIS   CD2 NE2  sing Y N 181 
HIS   CD2 HD2  sing N N 182 
HIS   CE1 NE2  sing Y N 183 
HIS   CE1 HE1  sing N N 184 
HIS   NE2 HE2  sing N N 185 
HIS   OXT HXT  sing N N 186 
HOH   O   H1   sing N N 187 
HOH   O   H2   sing N N 188 
ILE   N   CA   sing N N 189 
ILE   N   H    sing N N 190 
ILE   N   H2   sing N N 191 
ILE   CA  C    sing N N 192 
ILE   CA  CB   sing N N 193 
ILE   CA  HA   sing N N 194 
ILE   C   O    doub N N 195 
ILE   C   OXT  sing N N 196 
ILE   CB  CG1  sing N N 197 
ILE   CB  CG2  sing N N 198 
ILE   CB  HB   sing N N 199 
ILE   CG1 CD1  sing N N 200 
ILE   CG1 HG12 sing N N 201 
ILE   CG1 HG13 sing N N 202 
ILE   CG2 HG21 sing N N 203 
ILE   CG2 HG22 sing N N 204 
ILE   CG2 HG23 sing N N 205 
ILE   CD1 HD11 sing N N 206 
ILE   CD1 HD12 sing N N 207 
ILE   CD1 HD13 sing N N 208 
ILE   OXT HXT  sing N N 209 
LEU   N   CA   sing N N 210 
LEU   N   H    sing N N 211 
LEU   N   H2   sing N N 212 
LEU   CA  C    sing N N 213 
LEU   CA  CB   sing N N 214 
LEU   CA  HA   sing N N 215 
LEU   C   O    doub N N 216 
LEU   C   OXT  sing N N 217 
LEU   CB  CG   sing N N 218 
LEU   CB  HB2  sing N N 219 
LEU   CB  HB3  sing N N 220 
LEU   CG  CD1  sing N N 221 
LEU   CG  CD2  sing N N 222 
LEU   CG  HG   sing N N 223 
LEU   CD1 HD11 sing N N 224 
LEU   CD1 HD12 sing N N 225 
LEU   CD1 HD13 sing N N 226 
LEU   CD2 HD21 sing N N 227 
LEU   CD2 HD22 sing N N 228 
LEU   CD2 HD23 sing N N 229 
LEU   OXT HXT  sing N N 230 
LYS   N   CA   sing N N 231 
LYS   N   H    sing N N 232 
LYS   N   H2   sing N N 233 
LYS   CA  C    sing N N 234 
LYS   CA  CB   sing N N 235 
LYS   CA  HA   sing N N 236 
LYS   C   O    doub N N 237 
LYS   C   OXT  sing N N 238 
LYS   CB  CG   sing N N 239 
LYS   CB  HB2  sing N N 240 
LYS   CB  HB3  sing N N 241 
LYS   CG  CD   sing N N 242 
LYS   CG  HG2  sing N N 243 
LYS   CG  HG3  sing N N 244 
LYS   CD  CE   sing N N 245 
LYS   CD  HD2  sing N N 246 
LYS   CD  HD3  sing N N 247 
LYS   CE  NZ   sing N N 248 
LYS   CE  HE2  sing N N 249 
LYS   CE  HE3  sing N N 250 
LYS   NZ  HZ1  sing N N 251 
LYS   NZ  HZ2  sing N N 252 
LYS   NZ  HZ3  sing N N 253 
LYS   OXT HXT  sing N N 254 
MET   N   CA   sing N N 255 
MET   N   H    sing N N 256 
MET   N   H2   sing N N 257 
MET   CA  C    sing N N 258 
MET   CA  CB   sing N N 259 
MET   CA  HA   sing N N 260 
MET   C   O    doub N N 261 
MET   C   OXT  sing N N 262 
MET   CB  CG   sing N N 263 
MET   CB  HB2  sing N N 264 
MET   CB  HB3  sing N N 265 
MET   CG  SD   sing N N 266 
MET   CG  HG2  sing N N 267 
MET   CG  HG3  sing N N 268 
MET   SD  CE   sing N N 269 
MET   CE  HE1  sing N N 270 
MET   CE  HE2  sing N N 271 
MET   CE  HE3  sing N N 272 
MET   OXT HXT  sing N N 273 
PHE   N   CA   sing N N 274 
PHE   N   H    sing N N 275 
PHE   N   H2   sing N N 276 
PHE   CA  C    sing N N 277 
PHE   CA  CB   sing N N 278 
PHE   CA  HA   sing N N 279 
PHE   C   O    doub N N 280 
PHE   C   OXT  sing N N 281 
PHE   CB  CG   sing N N 282 
PHE   CB  HB2  sing N N 283 
PHE   CB  HB3  sing N N 284 
PHE   CG  CD1  doub Y N 285 
PHE   CG  CD2  sing Y N 286 
PHE   CD1 CE1  sing Y N 287 
PHE   CD1 HD1  sing N N 288 
PHE   CD2 CE2  doub Y N 289 
PHE   CD2 HD2  sing N N 290 
PHE   CE1 CZ   doub Y N 291 
PHE   CE1 HE1  sing N N 292 
PHE   CE2 CZ   sing Y N 293 
PHE   CE2 HE2  sing N N 294 
PHE   CZ  HZ   sing N N 295 
PHE   OXT HXT  sing N N 296 
PRO   N   CA   sing N N 297 
PRO   N   CD   sing N N 298 
PRO   N   H    sing N N 299 
PRO   CA  C    sing N N 300 
PRO   CA  CB   sing N N 301 
PRO   CA  HA   sing N N 302 
PRO   C   O    doub N N 303 
PRO   C   OXT  sing N N 304 
PRO   CB  CG   sing N N 305 
PRO   CB  HB2  sing N N 306 
PRO   CB  HB3  sing N N 307 
PRO   CG  CD   sing N N 308 
PRO   CG  HG2  sing N N 309 
PRO   CG  HG3  sing N N 310 
PRO   CD  HD2  sing N N 311 
PRO   CD  HD3  sing N N 312 
PRO   OXT HXT  sing N N 313 
SER   N   CA   sing N N 314 
SER   N   H    sing N N 315 
SER   N   H2   sing N N 316 
SER   CA  C    sing N N 317 
SER   CA  CB   sing N N 318 
SER   CA  HA   sing N N 319 
SER   C   O    doub N N 320 
SER   C   OXT  sing N N 321 
SER   CB  OG   sing N N 322 
SER   CB  HB2  sing N N 323 
SER   CB  HB3  sing N N 324 
SER   OG  HG   sing N N 325 
SER   OXT HXT  sing N N 326 
THR   N   CA   sing N N 327 
THR   N   H    sing N N 328 
THR   N   H2   sing N N 329 
THR   CA  C    sing N N 330 
THR   CA  CB   sing N N 331 
THR   CA  HA   sing N N 332 
THR   C   O    doub N N 333 
THR   C   OXT  sing N N 334 
THR   CB  OG1  sing N N 335 
THR   CB  CG2  sing N N 336 
THR   CB  HB   sing N N 337 
THR   OG1 HG1  sing N N 338 
THR   CG2 HG21 sing N N 339 
THR   CG2 HG22 sing N N 340 
THR   CG2 HG23 sing N N 341 
THR   OXT HXT  sing N N 342 
TRP   N   CA   sing N N 343 
TRP   N   H    sing N N 344 
TRP   N   H2   sing N N 345 
TRP   CA  C    sing N N 346 
TRP   CA  CB   sing N N 347 
TRP   CA  HA   sing N N 348 
TRP   C   O    doub N N 349 
TRP   C   OXT  sing N N 350 
TRP   CB  CG   sing N N 351 
TRP   CB  HB2  sing N N 352 
TRP   CB  HB3  sing N N 353 
TRP   CG  CD1  doub Y N 354 
TRP   CG  CD2  sing Y N 355 
TRP   CD1 NE1  sing Y N 356 
TRP   CD1 HD1  sing N N 357 
TRP   CD2 CE2  doub Y N 358 
TRP   CD2 CE3  sing Y N 359 
TRP   NE1 CE2  sing Y N 360 
TRP   NE1 HE1  sing N N 361 
TRP   CE2 CZ2  sing Y N 362 
TRP   CE3 CZ3  doub Y N 363 
TRP   CE3 HE3  sing N N 364 
TRP   CZ2 CH2  doub Y N 365 
TRP   CZ2 HZ2  sing N N 366 
TRP   CZ3 CH2  sing Y N 367 
TRP   CZ3 HZ3  sing N N 368 
TRP   CH2 HH2  sing N N 369 
TRP   OXT HXT  sing N N 370 
TYR   N   CA   sing N N 371 
TYR   N   H    sing N N 372 
TYR   N   H2   sing N N 373 
TYR   CA  C    sing N N 374 
TYR   CA  CB   sing N N 375 
TYR   CA  HA   sing N N 376 
TYR   C   O    doub N N 377 
TYR   C   OXT  sing N N 378 
TYR   CB  CG   sing N N 379 
TYR   CB  HB2  sing N N 380 
TYR   CB  HB3  sing N N 381 
TYR   CG  CD1  doub Y N 382 
TYR   CG  CD2  sing Y N 383 
TYR   CD1 CE1  sing Y N 384 
TYR   CD1 HD1  sing N N 385 
TYR   CD2 CE2  doub Y N 386 
TYR   CD2 HD2  sing N N 387 
TYR   CE1 CZ   doub Y N 388 
TYR   CE1 HE1  sing N N 389 
TYR   CE2 CZ   sing Y N 390 
TYR   CE2 HE2  sing N N 391 
TYR   CZ  OH   sing N N 392 
TYR   OH  HH   sing N N 393 
TYR   OXT HXT  sing N N 394 
VAL   N   CA   sing N N 395 
VAL   N   H    sing N N 396 
VAL   N   H2   sing N N 397 
VAL   CA  C    sing N N 398 
VAL   CA  CB   sing N N 399 
VAL   CA  HA   sing N N 400 
VAL   C   O    doub N N 401 
VAL   C   OXT  sing N N 402 
VAL   CB  CG1  sing N N 403 
VAL   CB  CG2  sing N N 404 
VAL   CB  HB   sing N N 405 
VAL   CG1 HG11 sing N N 406 
VAL   CG1 HG12 sing N N 407 
VAL   CG1 HG13 sing N N 408 
VAL   CG2 HG21 sing N N 409 
VAL   CG2 HG22 sing N N 410 
VAL   CG2 HG23 sing N N 411 
VAL   OXT HXT  sing N N 412 
# 
_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                    7I31 
_atom_sites.fract_transf_matrix[1][1]   0.011552 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000972 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017557 
_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]   0.015463 
_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   ? 17.726 7.961   24.851 1.00 17.72  ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 18.984 8.100   24.068 1.00 17.30  ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 19.109 6.896   23.127 1.00 16.85  ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 18.391 5.919   23.307 1.00 17.09  ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 20.176 8.153   25.026 1.00 20.05  ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 20.230 6.924   25.725 1.00 23.23  ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 19.994 6.961   22.156 1.00 15.04  ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 20.264 5.875   21.227 1.00 13.95  ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 20.638 6.368   19.845 1.00 12.83  ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 20.338 7.500   19.468 1.00 14.10  ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 21.314 5.537   19.112 1.00 12.37  ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 21.788 5.891   17.773 1.00 12.37  ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 21.740 4.686   16.866 1.00 11.92  ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 21.689 3.520   17.341 1.00 13.25  ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.237 6.423   17.889 1.00 13.53  ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 21.808 4.917   15.562 1.00 11.41  ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.022 3.889   14.545 1.00 11.47  ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 23.494 3.979   14.142 1.00 12.19  ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 23.980 5.076   13.840 1.00 12.36  ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.142 4.096   13.291 1.00 11.05  ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 19.679 4.240   13.645 1.00 12.53  ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.333 2.921   12.297 1.00 12.27  ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 18.862 4.856   12.454 1.00 13.96  ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.192 2.849   14.106 1.00 12.21  ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 25.596 2.810   13.682 1.00 13.83  ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 25.679 1.999   12.399 1.00 14.38  ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 25.640 0.758   12.450 1.00 15.11  ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 26.487 2.206   14.782 1.00 15.73  ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 26.552 3.086   16.006 1.00 14.67  ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 27.446 4.154   16.082 1.00 15.74  ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 25.722 2.864   17.090 1.00 16.14  ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 27.447 5.023   17.178 1.00 16.18  ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 25.725 3.705   18.199 1.00 17.50  ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 26.590 4.793   18.233 1.00 17.57  ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 26.607 5.651   19.324 1.00 20.60  ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 25.738 2.651   11.252 1.00 14.33  ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 25.790 2.021   9.937  1.00 15.43  ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.037 2.527   9.201  1.00 15.99  ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.291 3.748   9.150  1.00 15.03  ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.497 2.288   9.107  1.00 16.78  ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.165 3.788   9.008  1.00 17.27  ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.629 1.699   7.709  1.00 18.58  ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 27.887 1.614   8.687  1.00 17.61  ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.141 2.043   8.044  1.00 18.54  ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 29.972 2.905   8.984  1.00 17.11  ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.090 2.610   10.171 1.00 17.59  ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.451 4.060   8.476  1.00 17.12  ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.163 5.052   9.303  1.00 15.96  ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.259 6.227   9.645  1.00 15.10  ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.750 7.358   9.782  1.00 15.28  ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.513 5.505   8.708  1.00 18.17  ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.557 4.413   8.777  1.00 23.77  ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.281 4.294   9.766  1.00 25.66  ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.579 3.573   7.782  1.00 22.03  ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 28.975 5.946   9.884  1.00 13.99  ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.008 6.966   10.284 1.00 13.18  ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.360 6.632   11.623 1.00 12.78  ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.065 5.447   11.931 1.00 13.70  ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.891 7.103   9.217  1.00 13.88  ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.383 7.523   7.848  1.00 13.96  ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 28.098 8.709   7.669  1.00 16.61  ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.194 6.705   6.744  1.00 17.38  ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.551 9.093   6.414  1.00 17.74  ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.638 7.093   5.479  1.00 18.07  ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 28.286 8.302   5.322  1.00 18.61  ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.751 8.726   4.085  1.00 21.70  ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.024 7.676   12.367 1.00 11.75  ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.234 7.608   13.604 1.00 12.07  ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.027 8.492   13.371 1.00 11.18  ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.181 9.704   13.082 1.00 12.17  ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.057 8.145   14.794 1.00 12.86  ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.300 8.450   16.075 1.00 13.91  ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.255 8.831   17.230 1.00 15.98  ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 26.724 9.878   18.101 1.00 16.25  ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 26.070 9.677   19.239 1.00 16.70  ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 25.743 8.437   19.619 1.00 17.65  ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 25.620 10.714  19.943 1.00 17.91  ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 23.823 7.897   13.449 1.00 11.11  ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.538 8.612   13.225 1.00 10.54  ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 21.874 8.831   14.561 1.00 11.80  ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 21.585 7.835   15.269 1.00 12.08  ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.586 7.855   12.266 1.00 10.64  ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.378 8.727   11.952 1.00 11.81  ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.292 7.385   10.990 1.00 12.27  ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 21.654 10.089  14.939 1.00 10.67  ? 18  VAL   A N   1 
ATOM   86   C  CA  A VAL   A 1 12  ? 21.060 10.424  16.248 0.50 11.11  ? 18  VAL   A CA  1 
ATOM   87   C  CA  B VAL   A 1 12  ? 21.093 10.392  16.256 0.50 12.92  ? 18  VAL   A CA  1 
ATOM   88   C  C   . VAL   A 1 12  ? 19.955 11.414  16.089 1.00 11.43  ? 18  VAL   A C   1 
ATOM   89   O  O   . VAL   A 1 12  ? 19.808 12.064  15.011 1.00 12.80  ? 18  VAL   A O   1 
ATOM   90   C  CB  A VAL   A 1 12  ? 22.104 11.023  17.246 0.50 11.21  ? 18  VAL   A CB  1 
ATOM   91   C  CB  B VAL   A 1 12  ? 22.268 10.963  17.137 0.50 16.74  ? 18  VAL   A CB  1 
ATOM   92   C  CG1 A VAL   A 1 12  ? 23.028 9.944   17.767 0.50 12.75  ? 18  VAL   A CG1 1 
ATOM   93   C  CG1 B VAL   A 1 12  ? 21.845 11.265  18.558 0.50 17.30  ? 18  VAL   A CG1 1 
ATOM   94   C  CG2 A VAL   A 1 12  ? 22.834 12.274  16.663 0.50 7.92   ? 18  VAL   A CG2 1 
ATOM   95   C  CG2 B VAL   A 1 12  ? 23.444 10.018  17.173 0.50 19.50  ? 18  VAL   A CG2 1 
ATOM   96   N  N   . ASN   A 1 13  ? 19.131 11.586  17.133 1.00 11.48  ? 19  ASN   A N   1 
ATOM   97   C  CA  . ASN   A 1 13  ? 18.149 12.673  17.099 1.00 12.38  ? 19  ASN   A CA  1 
ATOM   98   C  C   . ASN   A 1 13  ? 18.953 13.991  17.118 1.00 12.93  ? 19  ASN   A C   1 
ATOM   99   O  O   . ASN   A 1 13  ? 19.882 14.159  17.931 1.00 13.93  ? 19  ASN   A O   1 
ATOM   100  C  CB  . ASN   A 1 13  ? 17.292 12.676  18.376 1.00 12.99  ? 19  ASN   A CB  1 
ATOM   101  C  CG  . ASN   A 1 13  ? 16.419 11.426  18.476 1.00 13.47  ? 19  ASN   A CG  1 
ATOM   102  O  OD1 . ASN   A 1 13  ? 16.826 10.407  19.043 1.00 13.74  ? 19  ASN   A OD1 1 
ATOM   103  N  ND2 . ASN   A 1 13  ? 15.255 11.475  17.882 1.00 13.54  ? 19  ASN   A ND2 1 
ATOM   104  N  N   . ARG   A 1 14  ? 18.563 14.932  16.240 1.00 13.32  ? 20  ARG   A N   1 
ATOM   105  C  CA  . ARG   A 1 14  ? 19.319 16.219  16.185 1.00 13.66  ? 20  ARG   A CA  1 
ATOM   106  C  C   . ARG   A 1 14  ? 19.311 16.893  17.553 1.00 15.68  ? 20  ARG   A C   1 
ATOM   107  O  O   . ARG   A 1 14  ? 20.343 17.416  17.982 1.00 16.53  ? 20  ARG   A O   1 
ATOM   108  C  CB  . ARG   A 1 14  ? 18.694 17.120  15.142 1.00 14.82  ? 20  ARG   A CB  1 
ATOM   109  C  CG  . ARG   A 1 14  ? 19.515 18.426  14.892 1.00 14.58  ? 20  ARG   A CG  1 
ATOM   110  C  CD  . ARG   A 1 14  ? 18.741 19.298  13.923 1.00 16.33  ? 20  ARG   A CD  1 
ATOM   111  N  NE  . ARG   A 1 14  ? 19.480 20.495  13.485 1.00 16.89  ? 20  ARG   A NE  1 
ATOM   112  C  CZ  . ARG   A 1 14  ? 19.506 21.646  14.153 1.00 18.43  ? 20  ARG   A CZ  1 
ATOM   113  N  NH1 . ARG   A 1 14  ? 18.929 21.747  15.336 1.00 20.20  ? 20  ARG   A NH1 1 
ATOM   114  N  NH2 . ARG   A 1 14  ? 20.115 22.714  13.631 1.00 20.57  ? 20  ARG   A NH2 1 
ATOM   115  N  N   . HIS   A 1 15  ? 18.177 16.772  18.298 1.00 15.28  ? 21  HIS   A N   1 
ATOM   116  C  CA  . HIS   A 1 15  ? 18.094 17.468  19.586 1.00 17.91  ? 21  HIS   A CA  1 
ATOM   117  C  C   . HIS   A 1 15  ? 18.955 16.859  20.681 1.00 18.72  ? 21  HIS   A C   1 
ATOM   118  O  O   . HIS   A 1 15  ? 19.098 17.461  21.756 1.00 21.82  ? 21  HIS   A O   1 
ATOM   119  C  CB  . HIS   A 1 15  ? 16.618 17.661  20.063 1.00 19.98  ? 21  HIS   A CB  1 
ATOM   120  C  CG  . HIS   A 1 15  ? 15.931 16.412  20.535 1.00 18.84  ? 21  HIS   A CG  1 
ATOM   121  N  ND1 . HIS   A 1 15  ? 15.294 15.547  19.656 1.00 18.28  ? 21  HIS   A ND1 1 
ATOM   122  C  CD2 . HIS   A 1 15  ? 15.757 15.945  21.801 1.00 20.12  ? 21  HIS   A CD2 1 
ATOM   123  C  CE1 . HIS   A 1 15  ? 14.760 14.575  20.416 1.00 19.33  ? 21  HIS   A CE1 1 
ATOM   124  N  NE2 . HIS   A 1 15  ? 15.010 14.785  21.708 1.00 20.05  ? 21  HIS   A NE2 1 
ATOM   125  N  N   . LEU   A 1 16  ? 19.462 15.625  20.481 1.00 18.07  ? 22  LEU   A N   1 
ATOM   126  C  CA  . LEU   A 1 16  ? 20.349 14.926  21.418 1.00 17.33  ? 22  LEU   A CA  1 
ATOM   127  C  C   . LEU   A 1 16  ? 21.803 14.856  20.967 1.00 18.22  ? 22  LEU   A C   1 
ATOM   128  O  O   . LEU   A 1 16  ? 22.639 14.244  21.611 1.00 19.80  ? 22  LEU   A O   1 
ATOM   129  C  CB  . LEU   A 1 16  ? 19.798 13.529  21.735 1.00 17.66  ? 22  LEU   A CB  1 
ATOM   130  C  CG  . LEU   A 1 16  ? 18.425 13.527  22.354 1.00 18.21  ? 22  LEU   A CG  1 
ATOM   131  C  CD1 . LEU   A 1 16  ? 18.004 12.049  22.598 1.00 18.75  ? 22  LEU   A CD1 1 
ATOM   132  C  CD2 . LEU   A 1 16  ? 18.428 14.328  23.700 1.00 20.40  ? 22  LEU   A CD2 1 
ATOM   133  N  N   . ALA   A 1 17  ? 22.146 15.514  19.814 1.00 16.83  ? 23  ALA   A N   1 
ATOM   134  C  CA  . ALA   A 1 17  ? 23.503 15.463  19.286 1.00 16.70  ? 23  ALA   A CA  1 
ATOM   135  C  C   . ALA   A 1 17  ? 24.482 16.118  20.261 1.00 17.99  ? 23  ALA   A C   1 
ATOM   136  O  O   . ALA   A 1 17  ? 24.159 17.145  20.875 1.00 19.42  ? 23  ALA   A O   1 
ATOM   137  C  CB  . ALA   A 1 17  ? 23.563 16.189  17.932 1.00 16.71  ? 23  ALA   A CB  1 
ATOM   138  N  N   . THR   A 1 18  ? 25.664 15.515  20.393 1.00 16.95  ? 24  THR   A N   1 
ATOM   139  C  CA  . THR   A 1 18  ? 26.696 16.043  21.299 1.00 16.94  ? 24  THR   A CA  1 
ATOM   140  C  C   . THR   A 1 18  ? 27.623 17.047  20.571 1.00 17.48  ? 24  THR   A C   1 
ATOM   141  O  O   . THR   A 1 18  ? 27.567 17.192  19.338 1.00 16.05  ? 24  THR   A O   1 
ATOM   142  C  CB  . THR   A 1 18  ? 27.548 14.859  21.797 1.00 19.10  ? 24  THR   A CB  1 
ATOM   143  O  OG1 . THR   A 1 18  ? 28.288 14.338  20.690 1.00 19.33  ? 24  THR   A OG1 1 
ATOM   144  C  CG2 . THR   A 1 18  ? 26.720 13.777  22.475 1.00 19.94  ? 24  THR   A CG2 1 
ATOM   145  N  N   . HIS   A 1 19  ? 28.549 17.706  21.311 1.00 18.66  ? 25  HIS   A N   1 
ATOM   146  C  CA  . HIS   A 1 19  ? 29.518 18.573  20.676 1.00 18.69  ? 25  HIS   A CA  1 
ATOM   147  C  C   . HIS   A 1 19  ? 30.383 17.779  19.700 1.00 17.27  ? 25  HIS   A C   1 
ATOM   148  O  O   . HIS   A 1 19  ? 30.650 18.247  18.600 1.00 16.39  ? 25  HIS   A O   1 
ATOM   149  C  CB  . HIS   A 1 19  ? 30.450 19.239  21.718 1.00 20.24  ? 25  HIS   A CB  1 
ATOM   150  C  CG  . HIS   A 1 19  ? 31.687 19.898  21.091 1.00 25.45  ? 25  HIS   A CG  1 
ATOM   151  N  ND1 . HIS   A 1 19  ? 31.606 21.092  20.365 1.00 29.26  ? 25  HIS   A ND1 1 
ATOM   152  C  CD2 . HIS   A 1 19  ? 32.939 19.378  20.896 1.00 29.77  ? 25  HIS   A CD2 1 
ATOM   153  C  CE1 . HIS   A 1 19  ? 32.837 21.370  19.957 1.00 29.74  ? 25  HIS   A CE1 1 
ATOM   154  N  NE2 . HIS   A 1 19  ? 33.674 20.335  20.187 1.00 31.60  ? 25  HIS   A NE2 1 
ATOM   155  N  N   . ASN   A 1 20  ? 30.763 16.522  20.073 1.00 17.84  ? 26  ASN   A N   1 
ATOM   156  C  CA  . ASN   A 1 20  ? 31.571 15.727  19.155 1.00 17.05  ? 26  ASN   A CA  1 
ATOM   157  C  C   . ASN   A 1 20  ? 30.780 15.428  17.850 1.00 15.32  ? 26  ASN   A C   1 
ATOM   158  O  O   . ASN   A 1 20  ? 31.363 15.451  16.766 1.00 16.25  ? 26  ASN   A O   1 
ATOM   159  C  CB  . ASN   A 1 20  ? 32.029 14.400  19.800 1.00 20.17  ? 26  ASN   A CB  1 
ATOM   160  C  CG  . ASN   A 1 20  ? 33.008 13.681  18.885 1.00 27.32  ? 26  ASN   A CG  1 
ATOM   161  O  OD1 . ASN   A 1 20  ? 34.169 14.101  18.723 1.00 31.25  ? 26  ASN   A OD1 1 
ATOM   162  N  ND2 . ASN   A 1 20  ? 32.558 12.596  18.247 1.00 29.11  ? 26  ASN   A ND2 1 
ATOM   163  N  N   . ASP   A 1 21  ? 29.451 15.181  17.967 1.00 14.99  ? 27  ASP   A N   1 
ATOM   164  C  CA  . ASP   A 1 21  ? 28.661 15.003  16.739 1.00 13.97  ? 27  ASP   A CA  1 
ATOM   165  C  C   . ASP   A 1 21  ? 28.709 16.250  15.820 1.00 13.31  ? 27  ASP   A C   1 
ATOM   166  O  O   . ASP   A 1 21  ? 28.926 16.143  14.599 1.00 13.72  ? 27  ASP   A O   1 
ATOM   167  C  CB  . ASP   A 1 21  ? 27.199 14.703  17.063 1.00 14.82  ? 27  ASP   A CB  1 
ATOM   168  C  CG  . ASP   A 1 21  ? 26.954 13.333  17.664 1.00 14.85  ? 27  ASP   A CG  1 
ATOM   169  O  OD1 . ASP   A 1 21  ? 27.615 12.370  17.211 1.00 16.10  ? 27  ASP   A OD1 1 
ATOM   170  O  OD2 . ASP   A 1 21  ? 26.108 13.240  18.614 1.00 15.98  ? 27  ASP   A OD2 1 
ATOM   171  N  N   . TRP   A 1 22  ? 28.496 17.430  16.410 1.00 13.72  ? 28  TRP   A N   1 
ATOM   172  C  CA  . TRP   A 1 22  ? 28.521 18.697  15.639 1.00 14.02  ? 28  TRP   A CA  1 
ATOM   173  C  C   . TRP   A 1 22  ? 29.935 18.973  15.067 1.00 13.60  ? 28  TRP   A C   1 
ATOM   174  O  O   . TRP   A 1 22  ? 30.011 19.514  13.970 1.00 14.17  ? 28  TRP   A O   1 
ATOM   175  C  CB  . TRP   A 1 22  ? 28.075 19.864  16.542 1.00 14.80  ? 28  TRP   A CB  1 
ATOM   176  C  CG  . TRP   A 1 22  ? 26.582 19.926  16.677 1.00 14.94  ? 28  TRP   A CG  1 
ATOM   177  C  CD1 . TRP   A 1 22  ? 25.838 19.634  17.784 1.00 16.54  ? 28  TRP   A CD1 1 
ATOM   178  C  CD2 . TRP   A 1 22  ? 25.653 20.394  15.684 1.00 15.08  ? 28  TRP   A CD2 1 
ATOM   179  N  NE1 . TRP   A 1 22  ? 24.485 19.852  17.530 1.00 15.81  ? 28  TRP   A NE1 1 
ATOM   180  C  CE2 . TRP   A 1 22  ? 24.355 20.333  16.243 1.00 15.48  ? 28  TRP   A CE2 1 
ATOM   181  C  CE3 . TRP   A 1 22  ? 25.800 20.895  14.380 1.00 16.77  ? 28  TRP   A CE3 1 
ATOM   182  C  CZ2 . TRP   A 1 22  ? 23.210 20.749  15.524 1.00 17.52  ? 28  TRP   A CZ2 1 
ATOM   183  C  CZ3 . TRP   A 1 22  ? 24.676 21.235  13.662 1.00 17.45  ? 28  TRP   A CZ3 1 
ATOM   184  C  CH2 . TRP   A 1 22  ? 23.420 21.239  14.243 1.00 17.15  ? 28  TRP   A CH2 1 
ATOM   185  N  N   . ALA   A 1 23  ? 30.997 18.545  15.779 1.00 14.16  ? 29  ALA   A N   1 
ATOM   186  C  CA  . ALA   A 1 23  ? 32.354 18.767  15.301 1.00 15.23  ? 29  ALA   A CA  1 
ATOM   187  C  C   . ALA   A 1 23  ? 32.791 17.752  14.232 1.00 15.43  ? 29  ALA   A C   1 
ATOM   188  O  O   . ALA   A 1 23  ? 33.808 17.927  13.572 1.00 16.98  ? 29  ALA   A O   1 
ATOM   189  C  CB  . ALA   A 1 23  ? 33.297 18.735  16.485 1.00 17.60  ? 29  ALA   A CB  1 
ATOM   190  N  N   . ASN   A 1 24  ? 31.988 16.685  14.019 1.00 15.20  ? 30  ASN   A N   1 
ATOM   191  C  CA  . ASN   A 1 24  ? 32.249 15.652  12.993 1.00 15.37  ? 30  ASN   A CA  1 
ATOM   192  C  C   . ASN   A 1 24  ? 30.992 15.488  12.145 1.00 14.30  ? 30  ASN   A C   1 
ATOM   193  O  O   . ASN   A 1 24  ? 30.594 14.356  11.800 1.00 14.29  ? 30  ASN   A O   1 
ATOM   194  C  CB  . ASN   A 1 24  ? 32.653 14.316  13.691 1.00 16.57  ? 30  ASN   A CB  1 
ATOM   195  C  CG  . ASN   A 1 24  ? 33.994 14.486  14.362 1.00 18.78  ? 30  ASN   A CG  1 
ATOM   196  O  OD1 . ASN   A 1 24  ? 35.030 14.447  13.694 1.00 21.36  ? 30  ASN   A OD1 1 
ATOM   197  N  ND2 . ASN   A 1 24  ? 34.018 14.770  15.662 1.00 19.25  ? 30  ASN   A ND2 1 
ATOM   198  N  N   . LEU   A 1 25  ? 30.322 16.588  11.842 1.00 13.92  ? 31  LEU   A N   1 
ATOM   199  C  CA  . LEU   A 1 25  ? 29.034 16.548  11.177 1.00 12.88  ? 31  LEU   A CA  1 
ATOM   200  C  C   . LEU   A 1 25  ? 29.097 16.113  9.735  1.00 14.16  ? 31  LEU   A C   1 
ATOM   201  O  O   . LEU   A 1 25  ? 29.928 16.585  8.950  1.00 15.56  ? 31  LEU   A O   1 
ATOM   202  C  CB  . LEU   A 1 25  ? 28.478 17.977  11.244 1.00 13.30  ? 31  LEU   A CB  1 
ATOM   203  C  CG  . LEU   A 1 25  ? 27.077 18.133  10.639 1.00 14.44  ? 31  LEU   A CG  1 
ATOM   204  C  CD1 . LEU   A 1 25  ? 26.042 17.349  11.457 1.00 14.51  ? 31  LEU   A CD1 1 
ATOM   205  C  CD2 . LEU   A 1 25  ? 26.652 19.637  10.566 1.00 17.06  ? 31  LEU   A CD2 1 
ATOM   206  N  N   . VAL   A 1 26  ? 28.171 15.240  9.322  1.00 12.65  ? 32  VAL   A N   1 
ATOM   207  C  CA  . VAL   A 1 26  ? 27.982 14.835  7.928  1.00 13.56  ? 32  VAL   A CA  1 
ATOM   208  C  C   . VAL   A 1 26  ? 26.749 15.564  7.360  1.00 13.28  ? 32  VAL   A C   1 
ATOM   209  O  O   . VAL   A 1 26  ? 26.771 16.097  6.248  1.00 14.91  ? 32  VAL   A O   1 
ATOM   210  C  CB  . VAL   A 1 26  ? 27.843 13.294  7.825  1.00 13.74  ? 32  VAL   A CB  1 
ATOM   211  C  CG1 . VAL   A 1 26  ? 27.464 12.891  6.381  1.00 15.88  ? 32  VAL   A CG1 1 
ATOM   212  C  CG2 . VAL   A 1 26  ? 29.139 12.608  8.276  1.00 15.09  ? 32  VAL   A CG2 1 
ATOM   213  N  N   . TRP   A 1 27  ? 25.597 15.542  8.093  1.00 13.73  ? 33  TRP   A N   1 
ATOM   214  C  CA  . TRP   A 1 27  ? 24.331 16.080  7.584  1.00 13.64  ? 33  TRP   A CA  1 
ATOM   215  C  C   . TRP   A 1 27  ? 23.390 16.303  8.747  1.00 13.55  ? 33  TRP   A C   1 
ATOM   216  O  O   . TRP   A 1 27  ? 23.414 15.502  9.721  1.00 13.28  ? 33  TRP   A O   1 
ATOM   217  C  CB  . TRP   A 1 27  ? 23.714 15.058  6.569  1.00 15.06  ? 33  TRP   A CB  1 
ATOM   218  C  CG  . TRP   A 1 27  ? 22.310 15.338  6.122  1.00 16.48  ? 33  TRP   A CG  1 
ATOM   219  C  CD1 . TRP   A 1 27  ? 21.894 16.188  5.129  1.00 18.63  ? 33  TRP   A CD1 1 
ATOM   220  C  CD2 . TRP   A 1 27  ? 21.123 14.741  6.654  1.00 16.03  ? 33  TRP   A CD2 1 
ATOM   221  N  NE1 . TRP   A 1 27  ? 20.524 16.147  5.024  1.00 20.27  ? 33  TRP   A NE1 1 
ATOM   222  C  CE2 . TRP   A 1 27  ? 20.031 15.245  5.922  1.00 18.07  ? 33  TRP   A CE2 1 
ATOM   223  C  CE3 . TRP   A 1 27  ? 20.881 13.802  7.657  1.00 16.25  ? 33  TRP   A CE3 1 
ATOM   224  C  CZ2 . TRP   A 1 27  ? 18.711 14.819  6.162  1.00 18.85  ? 33  TRP   A CZ2 1 
ATOM   225  C  CZ3 . TRP   A 1 27  ? 19.586 13.356  7.850  1.00 17.63  ? 33  TRP   A CZ3 1 
ATOM   226  C  CH2 . TRP   A 1 27  ? 18.517 13.887  7.143  1.00 19.05  ? 33  TRP   A CH2 1 
ATOM   227  N  N   . GLU   A 1 28  ? 22.563 17.337  8.698  1.00 13.83  ? 34  GLU   A N   1 
ATOM   228  C  CA  . GLU   A 1 28  ? 21.551 17.522  9.750  1.00 14.25  ? 34  GLU   A CA  1 
ATOM   229  C  C   . GLU   A 1 28  ? 20.329 18.154  9.129  1.00 15.37  ? 34  GLU   A C   1 
ATOM   230  O  O   . GLU   A 1 28  ? 20.448 18.965  8.166  1.00 16.36  ? 34  GLU   A O   1 
ATOM   231  C  CB  . GLU   A 1 28  ? 22.082 18.366  10.925 1.00 16.42  ? 34  GLU   A CB  1 
ATOM   232  C  CG  . GLU   A 1 28  ? 22.682 19.716  10.546 1.00 17.57  ? 34  GLU   A CG  1 
ATOM   233  C  CD  . GLU   A 1 28  ? 21.711 20.885  10.349 1.00 18.20  ? 34  GLU   A CD  1 
ATOM   234  O  OE1 . GLU   A 1 28  ? 22.066 21.846  9.614  1.00 19.82  ? 34  GLU   A OE1 1 
ATOM   235  O  OE2 . GLU   A 1 28  ? 20.615 20.896  10.956 1.00 18.17  ? 34  GLU   A OE2 1 
ATOM   236  N  N   . ASP   A 1 29  ? 19.157 17.891  9.714  1.00 15.14  ? 35  ASP   A N   1 
ATOM   237  C  CA  . ASP   A 1 29  ? 17.916 18.451  9.231  1.00 16.42  ? 35  ASP   A CA  1 
ATOM   238  C  C   . ASP   A 1 29  ? 16.963 18.608  10.424 1.00 16.47  ? 35  ASP   A C   1 
ATOM   239  O  O   . ASP   A 1 29  ? 16.424 17.633  10.984 1.00 16.44  ? 35  ASP   A O   1 
ATOM   240  C  CB  . ASP   A 1 29  ? 17.334 17.532  8.137  1.00 18.32  ? 35  ASP   A CB  1 
ATOM   241  C  CG  . ASP   A 1 29  ? 16.056 18.017  7.498  1.00 21.22  ? 35  ASP   A CG  1 
ATOM   242  O  OD1 . ASP   A 1 29  ? 15.212 18.548  8.220  1.00 23.83  ? 35  ASP   A OD1 1 
ATOM   243  O  OD2 . ASP   A 1 29  ? 15.872 17.780  6.297  1.00 25.80  ? 35  ASP   A OD2 1 
ATOM   244  N  N   . SER   A 1 30  ? 16.733 19.860  10.809 1.00 17.44  ? 36  SER   A N   1 
ATOM   245  C  CA  A SER   A 1 30  ? 15.894 20.209  11.939 0.50 17.87  ? 36  SER   A CA  1 
ATOM   246  C  CA  B SER   A 1 30  ? 15.902 20.163  11.960 0.50 18.83  ? 36  SER   A CA  1 
ATOM   247  C  C   . SER   A 1 30  ? 14.443 19.780  11.727 1.00 19.18  ? 36  SER   A C   1 
ATOM   248  O  O   . SER   A 1 30  ? 13.824 19.267  12.661 1.00 20.30  ? 36  SER   A O   1 
ATOM   249  C  CB  A SER   A 1 30  ? 15.959 21.715  12.193 0.50 18.83  ? 36  SER   A CB  1 
ATOM   250  C  CB  B SER   A 1 30  ? 16.044 21.628  12.375 0.50 22.61  ? 36  SER   A CB  1 
ATOM   251  O  OG  A SER   A 1 30  ? 15.012 22.098  13.170 0.50 20.25  ? 36  SER   A OG  1 
ATOM   252  O  OG  B SER   A 1 30  ? 15.684 22.482  11.307 0.50 28.67  ? 36  SER   A OG  1 
ATOM   253  N  N   . SER   A 1 31  ? 13.933 19.913  10.495 1.00 19.99  ? 37  SER   A N   1 
ATOM   254  C  CA  . SER   A 1 31  ? 12.560 19.511  10.221 1.00 20.52  ? 37  SER   A CA  1 
ATOM   255  C  C   . SER   A 1 31  ? 12.316 18.025  10.409 1.00 19.69  ? 37  SER   A C   1 
ATOM   256  O  O   . SER   A 1 31  ? 11.178 17.640  10.704 1.00 21.29  ? 37  SER   A O   1 
ATOM   257  C  CB  . SER   A 1 31  ? 12.120 19.919  8.818  1.00 23.48  ? 37  SER   A CB  1 
ATOM   258  O  OG  . SER   A 1 31  ? 12.640 19.126  7.770  1.00 27.68  ? 37  SER   A OG  1 
ATOM   259  N  N   . ARG   A 1 32  ? 13.371 17.190  10.295 1.00 17.52  ? 38  ARG   A N   1 
ATOM   260  C  CA  . ARG   A 1 32  ? 13.275 15.725  10.487 1.00 17.10  ? 38  ARG   A CA  1 
ATOM   261  C  C   . ARG   A 1 32  ? 13.737 15.280  11.877 1.00 16.48  ? 38  ARG   A C   1 
ATOM   262  O  O   . ARG   A 1 32  ? 13.649 14.071  12.179 1.00 15.52  ? 38  ARG   A O   1 
ATOM   263  C  CB  . ARG   A 1 32  ? 14.129 15.006  9.419  1.00 17.02  ? 38  ARG   A CB  1 
ATOM   264  C  CG  . ARG   A 1 32  ? 13.603 15.221  7.999  1.00 19.50  ? 38  ARG   A CG  1 
ATOM   265  C  CD  . ARG   A 1 32  ? 14.468 14.552  6.960  1.00 19.56  ? 38  ARG   A CD  1 
ATOM   266  N  NE  . ARG   A 1 32  ? 14.354 13.082  7.076  1.00 15.85  ? 38  ARG   A NE  1 
ATOM   267  C  CZ  . ARG   A 1 32  ? 14.502 12.250  6.053  1.00 18.13  ? 38  ARG   A CZ  1 
ATOM   268  N  NH1 . ARG   A 1 32  ? 14.755 12.721  4.829  1.00 20.16  ? 38  ARG   A NH1 1 
ATOM   269  N  NH2 . ARG   A 1 32  ? 14.333 10.936  6.221  1.00 18.23  ? 38  ARG   A NH2 1 
ATOM   270  N  N   . ASP   A 1 33  ? 14.310 16.156  12.695 1.00 15.62  ? 39  ASP   A N   1 
ATOM   271  C  CA  . ASP   A 1 33  ? 14.957 15.819  13.953 1.00 15.55  ? 39  ASP   A CA  1 
ATOM   272  C  C   . ASP   A 1 33  ? 16.086 14.817  13.780 1.00 14.30  ? 39  ASP   A C   1 
ATOM   273  O  O   . ASP   A 1 33  ? 16.296 13.946  14.643 1.00 14.26  ? 39  ASP   A O   1 
ATOM   274  C  CB  . ASP   A 1 33  ? 13.962 15.323  15.028 1.00 16.34  ? 39  ASP   A CB  1 
ATOM   275  C  CG  . ASP   A 1 33  ? 14.586 15.089  16.397 1.00 16.53  ? 39  ASP   A CG  1 
ATOM   276  O  OD1 . ASP   A 1 33  ? 15.434 15.906  16.836 1.00 17.21  ? 39  ASP   A OD1 1 
ATOM   277  O  OD2 . ASP   A 1 33  ? 14.184 14.101  17.081 1.00 17.95  ? 39  ASP   A OD2 1 
ATOM   278  N  N   . LEU   A 1 34  ? 16.882 14.942  12.693 1.00 13.70  ? 40  LEU   A N   1 
ATOM   279  C  CA  . LEU   A 1 34  ? 17.972 13.987  12.479 1.00 12.80  ? 40  LEU   A CA  1 
ATOM   280  C  C   . LEU   A 1 34  ? 19.320 14.706  12.338 1.00 12.75  ? 40  LEU   A C   1 
ATOM   281  O  O   . LEU   A 1 34  ? 19.419 15.808  11.742 1.00 13.51  ? 40  LEU   A O   1 
ATOM   282  C  CB  . LEU   A 1 34  ? 17.730 13.207  11.188 1.00 13.16  ? 40  LEU   A CB  1 
ATOM   283  C  CG  . LEU   A 1 34  ? 16.645 12.101  11.244 1.00 14.42  ? 40  LEU   A CG  1 
ATOM   284  C  CD1 . LEU   A 1 34  ? 16.548 11.384  9.899  1.00 15.60  ? 40  LEU   A CD1 1 
ATOM   285  C  CD2 . LEU   A 1 34  ? 16.946 11.073  12.331 1.00 14.93  ? 40  LEU   A CD2 1 
ATOM   286  N  N   . LEU   A 1 35  ? 20.368 14.018  12.787 1.00 11.67  ? 41  LEU   A N   1 
ATOM   287  C  CA  . LEU   A 1 35  ? 21.747 14.468  12.572 1.00 11.73  ? 41  LEU   A CA  1 
ATOM   288  C  C   . LEU   A 1 35  ? 22.584 13.235  12.411 1.00 11.31  ? 41  LEU   A C   1 
ATOM   289  O  O   . LEU   A 1 35  ? 22.368 12.204  13.081 1.00 11.85  ? 41  LEU   A O   1 
ATOM   290  C  CB  . LEU   A 1 35  ? 22.227 15.331  13.786 1.00 12.55  ? 41  LEU   A CB  1 
ATOM   291  C  CG  . LEU   A 1 35  ? 23.659 15.910  13.669 1.00 12.58  ? 41  LEU   A CG  1 
ATOM   292  C  CD1 . LEU   A 1 35  ? 23.762 17.276  14.364 1.00 14.43  ? 41  LEU   A CD1 1 
ATOM   293  C  CD2 . LEU   A 1 35  ? 24.667 14.964  14.284 1.00 12.66  ? 41  LEU   A CD2 1 
ATOM   294  N  N   . VAL   A 1 36  ? 23.541 13.319  11.473 1.00 11.29  ? 42  VAL   A N   1 
ATOM   295  C  CA  . VAL   A 1 36  ? 24.470 12.220  11.173 1.00 11.26  ? 42  VAL   A CA  1 
ATOM   296  C  C   . VAL   A 1 36  ? 25.890 12.748  11.351 1.00 11.52  ? 42  VAL   A C   1 
ATOM   297  O  O   . VAL   A 1 36  ? 26.226 13.795  10.766 1.00 12.47  ? 42  VAL   A O   1 
ATOM   298  C  CB  . VAL   A 1 36  ? 24.250 11.655  9.758  1.00 11.68  ? 42  VAL   A CB  1 
ATOM   299  C  CG1 . VAL   A 1 36  ? 25.249 10.553  9.480  1.00 13.42  ? 42  VAL   A CG1 1 
ATOM   300  C  CG2 . VAL   A 1 36  ? 22.787 11.141  9.613  1.00 12.84  ? 42  VAL   A CG2 1 
ATOM   301  N  N   . SER   A 1 37  ? 26.703 12.032  12.095 1.00 11.11  ? 43  SER   A N   1 
ATOM   302  C  CA  . SER   A 1 37  ? 28.130 12.376  12.296 1.00 12.12  ? 43  SER   A CA  1 
ATOM   303  C  C   . SER   A 1 37  ? 28.975 11.184  11.835 1.00 12.65  ? 43  SER   A C   1 
ATOM   304  O  O   . SER   A 1 37  ? 28.495 10.048  11.587 1.00 12.81  ? 43  SER   A O   1 
ATOM   305  C  CB  . SER   A 1 37  ? 28.416 12.710  13.765 1.00 13.33  ? 43  SER   A CB  1 
ATOM   306  O  OG  . SER   A 1 37  ? 28.076 11.618  14.598 1.00 13.84  ? 43  SER   A OG  1 
ATOM   307  N  N   . SER   A 1 38  ? 30.263 11.459  11.607 1.00 13.99  ? 44  SER   A N   1 
ATOM   308  C  CA  . SER   A 1 38  ? 31.197 10.404  11.151 1.00 15.55  ? 44  SER   A CA  1 
ATOM   309  C  C   . SER   A 1 38  ? 31.833 9.677   12.328 1.00 17.30  ? 44  SER   A C   1 
ATOM   310  O  O   . SER   A 1 38  ? 32.021 10.248  13.425 1.00 19.55  ? 44  SER   A O   1 
ATOM   311  C  CB  . SER   A 1 38  ? 32.288 11.030  10.268 1.00 16.93  ? 44  SER   A CB  1 
ATOM   312  O  OG  . SER   A 1 38  ? 32.982 11.988  11.054 1.00 19.81  ? 44  SER   A OG  1 
ATOM   313  N  N   . THR   A 1 39  ? 32.136 8.375   12.125 1.00 18.02  ? 45  THR   A N   1 
ATOM   314  C  CA  . THR   A 1 39  ? 32.738 7.563   13.173 1.00 20.13  ? 45  THR   A CA  1 
ATOM   315  C  C   . THR   A 1 39  ? 34.091 6.985   12.710 1.00 22.01  ? 45  THR   A C   1 
ATOM   316  O  O   . THR   A 1 39  ? 34.302 6.773   11.511 1.00 21.14  ? 45  THR   A O   1 
ATOM   317  C  CB  . THR   A 1 39  ? 31.813 6.364   13.556 1.00 20.44  ? 45  THR   A CB  1 
ATOM   318  O  OG1 . THR   A 1 39  ? 31.664 5.491   12.452 1.00 21.07  ? 45  THR   A OG1 1 
ATOM   319  C  CG2 . THR   A 1 39  ? 30.414 6.793   14.004 1.00 21.49  ? 45  THR   A CG2 1 
ATOM   320  N  N   . THR   A 1 40  ? 34.945 6.632   13.674 1.00 24.05  ? 46  THR   A N   1 
ATOM   321  C  CA  . THR   A 1 40  ? 36.217 6.009   13.351 1.00 26.83  ? 46  THR   A CA  1 
ATOM   322  C  C   . THR   A 1 40  ? 35.988 4.508   13.109 1.00 27.14  ? 46  THR   A C   1 
ATOM   323  O  O   . THR   A 1 40  ? 36.474 3.981   12.101 1.00 29.14  ? 46  THR   A O   1 
ATOM   324  C  CB  . THR   A 1 40  ? 37.276 6.370   14.411 1.00 31.31  ? 46  THR   A CB  1 
ATOM   325  O  OG1 . THR   A 1 40  ? 36.830 5.920   15.681 1.00 35.88  ? 46  THR   A OG1 1 
ATOM   326  C  CG2 . THR   A 1 40  ? 37.511 7.845   14.496 1.00 32.48  ? 46  THR   A CG2 1 
ATOM   327  N  N   . ALA   A 1 41  ? 35.216 3.845   13.982 1.00 27.28  ? 47  ALA   A N   1 
ATOM   328  C  CA  . ALA   A 1 41  ? 34.931 2.411   13.796 1.00 27.98  ? 47  ALA   A CA  1 
ATOM   329  C  C   . ALA   A 1 41  ? 33.663 2.155   12.948 1.00 26.10  ? 47  ALA   A C   1 
ATOM   330  O  O   . ALA   A 1 41  ? 32.725 2.952   12.989 1.00 24.43  ? 47  ALA   A O   1 
ATOM   331  C  CB  . ALA   A 1 41  ? 34.769 1.723   15.135 1.00 30.45  ? 47  ALA   A CB  1 
ATOM   332  N  N   . GLN   A 1 42  ? 33.613 1.039   12.217 1.00 24.88  ? 48  GLN   A N   1 
ATOM   333  C  CA  . GLN   A 1 42  ? 32.445 0.655   11.401 1.00 25.05  ? 48  GLN   A CA  1 
ATOM   334  C  C   . GLN   A 1 42  ? 31.366 0.034   12.254 1.00 22.92  ? 48  GLN   A C   1 
ATOM   335  O  O   . GLN   A 1 42  ? 31.647 -0.722  13.182 1.00 23.66  ? 48  GLN   A O   1 
ATOM   336  C  CB  . GLN   A 1 42  ? 32.821 -0.326  10.287 1.00 28.50  ? 48  GLN   A CB  1 
ATOM   337  C  CG  . GLN   A 1 42  ? 33.646 0.305   9.161  1.00 36.15  ? 48  GLN   A CG  1 
ATOM   338  C  CD  . GLN   A 1 42  ? 34.097 -0.746  8.195  1.00 44.66  ? 48  GLN   A CD  1 
ATOM   339  O  OE1 . GLN   A 1 42  ? 35.044 -1.510  8.468  1.00 46.35  ? 48  GLN   A OE1 1 
ATOM   340  N  NE2 . GLN   A 1 42  ? 33.409 -0.827  7.067  1.00 46.24  ? 48  GLN   A NE2 1 
ATOM   341  N  N   . GLY   A 1 43  ? 30.120 0.413   11.982 1.00 20.14  ? 49  GLY   A N   1 
ATOM   342  C  CA  . GLY   A 1 43  ? 28.955 -0.074  12.717 1.00 20.09  ? 49  GLY   A CA  1 
ATOM   343  C  C   . GLY   A 1 43  ? 28.351 -1.345  12.166 1.00 18.71  ? 49  GLY   A C   1 
ATOM   344  O  O   . GLY   A 1 43  ? 28.629 -1.739  11.026 1.00 19.98  ? 49  GLY   A O   1 
ATOM   345  N  N   . CYS   A 1 44  ? 27.416 -1.928  12.946 1.00 17.48  ? 50  CYS   A N   1 
ATOM   346  C  CA  . CYS   A 1 44  ? 26.796 -3.198  12.611 1.00 17.82  ? 50  CYS   A CA  1 
ATOM   347  C  C   . CYS   A 1 44  ? 25.344 -3.145  12.136 1.00 16.77  ? 50  CYS   A C   1 
ATOM   348  O  O   . CYS   A 1 44  ? 24.788 -4.201  11.793 1.00 17.83  ? 50  CYS   A O   1 
ATOM   349  C  CB  . CYS   A 1 44  ? 26.920 -4.164  13.787 1.00 20.19  ? 50  CYS   A CB  1 
ATOM   350  S  SG  . CYS   A 1 44  ? 28.614 -4.586  14.240 1.00 24.63  ? 50  CYS   A SG  1 
ATOM   351  N  N   . ASP   A 1 45  ? 24.685 -2.001  12.275 1.00 16.24  ? 51  ASP   A N   1 
ATOM   352  C  CA  . ASP   A 1 45  ? 23.290 -1.891  11.871 1.00 15.40  ? 51  ASP   A CA  1 
ATOM   353  C  C   . ASP   A 1 45  ? 23.199 -1.835  10.351 1.00 16.13  ? 51  ASP   A C   1 
ATOM   354  O  O   . ASP   A 1 45  ? 24.095 -1.291  9.685  1.00 18.14  ? 51  ASP   A O   1 
ATOM   355  C  CB  . ASP   A 1 45  ? 22.673 -0.626  12.486 1.00 14.10  ? 51  ASP   A CB  1 
ATOM   356  C  CG  . ASP   A 1 45  ? 22.576 -0.679  14.005 1.00 14.79  ? 51  ASP   A CG  1 
ATOM   357  O  OD1 . ASP   A 1 45  ? 22.206 -1.788  14.567 1.00 16.13  ? 51  ASP   A OD1 1 
ATOM   358  O  OD2 . ASP   A 1 45  ? 22.811 0.362   14.659 1.00 15.59  ? 51  ASP   A OD2 1 
ATOM   359  N  N   . THR   A 1 46  ? 22.160 -2.353  9.803  1.00 18.24  ? 52  THR   A N   1 
ATOM   360  C  CA  . THR   A 1 46  ? 21.853 -2.320  8.364  1.00 19.98  ? 52  THR   A CA  1 
ATOM   361  C  C   . THR   A 1 46  ? 20.541 -1.534  8.178  1.00 17.24  ? 52  THR   A C   1 
ATOM   362  O  O   . THR   A 1 46  ? 19.639 -1.675  8.996  1.00 18.43  ? 52  THR   A O   1 
ATOM   363  C  CB  . THR   A 1 46  ? 21.652 -3.759  7.862  1.00 27.89  ? 52  THR   A CB  1 
ATOM   364  O  OG1 . THR   A 1 46  ? 22.931 -4.428  7.879  1.00 32.52  ? 52  THR   A OG1 1 
ATOM   365  C  CG2 . THR   A 1 46  ? 20.993 -3.837  6.475  1.00 31.32  ? 52  THR   A CG2 1 
ATOM   366  N  N   . ILE   A 1 47  ? 20.427 -0.685  7.162  1.00 16.00  ? 53  ILE   A N   1 
ATOM   367  C  CA  . ILE   A 1 47  ? 19.227 0.094   6.921  1.00 14.80  ? 53  ILE   A CA  1 
ATOM   368  C  C   . ILE   A 1 47  ? 18.223 -0.638  6.035  1.00 14.97  ? 53  ILE   A C   1 
ATOM   369  O  O   . ILE   A 1 47  ? 18.598 -1.173  4.974  1.00 16.69  ? 53  ILE   A O   1 
ATOM   370  C  CB  . ILE   A 1 47  ? 19.548 1.487   6.329  1.00 15.35  ? 53  ILE   A CB  1 
ATOM   371  C  CG1 . ILE   A 1 47  ? 20.667 2.214   7.121  1.00 15.52  ? 53  ILE   A CG1 1 
ATOM   372  C  CG2 . ILE   A 1 47  ? 18.277 2.355   6.194  1.00 14.74  ? 53  ILE   A CG2 1 
ATOM   373  C  CD1 . ILE   A 1 47  ? 20.297 2.516   8.628  1.00 15.47  ? 53  ILE   A CD1 1 
ATOM   374  N  N   . ALA   A 1 48  ? 16.978 -0.698  6.428  1.00 14.22  ? 54  ALA   A N   1 
ATOM   375  C  CA  . ALA   A 1 48  ? 15.890 -1.244  5.614  1.00 15.29  ? 54  ALA   A CA  1 
ATOM   376  C  C   . ALA   A 1 48  ? 15.622 -0.361  4.372  1.00 15.46  ? 54  ALA   A C   1 
ATOM   377  O  O   . ALA   A 1 48  ? 15.665 0.866   4.437  1.00 16.02  ? 54  ALA   A O   1 
ATOM   378  C  CB  . ALA   A 1 48  ? 14.600 -1.289  6.450  1.00 15.66  ? 54  ALA   A CB  1 
ATOM   379  N  N   . ARG   A 1 49  ? 15.328 -1.012  3.232  1.00 17.20  ? 55  ARG   A N   1 
ATOM   380  C  CA  . ARG   A 1 49  ? 14.980 -0.261  1.998  1.00 18.88  ? 55  ARG   A CA  1 
ATOM   381  C  C   . ARG   A 1 49  ? 13.663 -0.872  1.531  1.00 21.28  ? 55  ARG   A C   1 
ATOM   382  O  O   . ARG   A 1 49  ? 13.686 -1.875  0.783  1.00 22.73  ? 55  ARG   A O   1 
ATOM   383  C  CB  . ARG   A 1 49  ? 16.108 -0.382  0.934  1.00 21.14  ? 55  ARG   A CB  1 
ATOM   384  C  CG  . ARG   A 1 49  ? 17.492 0.093   1.438  1.00 20.84  ? 55  ARG   A CG  1 
ATOM   385  C  CD  . ARG   A 1 49  ? 17.576 1.584   1.784  1.00 19.88  ? 55  ARG   A CD  1 
ATOM   386  N  NE  . ARG   A 1 49  ? 18.924 1.988   2.249  1.00 18.86  ? 55  ARG   A NE  1 
ATOM   387  C  CZ  . ARG   A 1 49  ? 19.166 3.130   2.886  1.00 18.75  ? 55  ARG   A CZ  1 
ATOM   388  N  NH1 . ARG   A 1 49  ? 18.198 4.017   3.072  1.00 19.92  ? 55  ARG   A NH1 1 
ATOM   389  N  NH2 . ARG   A 1 49  ? 20.394 3.404   3.340  1.00 20.76  ? 55  ARG   A NH2 1 
ATOM   390  N  N   . CYS   A 1 50  ? 12.515 -0.254  1.935  1.00 20.35  ? 56  CYS   A N   1 
ATOM   391  C  CA  . CYS   A 1 50  ? 11.155 -0.851  1.876  1.00 19.74  ? 56  CYS   A CA  1 
ATOM   392  C  C   . CYS   A 1 50  ? 10.062 0.163   2.216  1.00 19.85  ? 56  CYS   A C   1 
ATOM   393  O  O   . CYS   A 1 50  ? 10.320 1.286   2.650  1.00 22.03  ? 56  CYS   A O   1 
ATOM   394  C  CB  . CYS   A 1 50  ? 11.111 -2.022  2.846  1.00 18.30  ? 56  CYS   A CB  1 
ATOM   395  S  SG  . CYS   A 1 50  ? 11.093 -1.491  4.549  1.00 18.52  ? 56  CYS   A SG  1 
ATOM   396  N  N   . ASP   A 1 51  ? 8.765  -0.307  2.125  1.00 22.06  ? 57  ASP   A N   1 
ATOM   397  C  CA  . ASP   A 1 51  ? 7.610  0.487   2.554  1.00 24.29  ? 57  ASP   A CA  1 
ATOM   398  C  C   . ASP   A 1 51  ? 6.850  -0.303  3.641  1.00 22.97  ? 57  ASP   A C   1 
ATOM   399  O  O   . ASP   A 1 51  ? 5.629  -0.171  3.764  1.00 24.53  ? 57  ASP   A O   1 
ATOM   400  C  CB  . ASP   A 1 51  ? 6.686  0.889   1.377  1.00 28.59  ? 57  ASP   A CB  1 
ATOM   401  C  CG  . ASP   A 1 51  ? 6.045  -0.271  0.680  1.00 34.70  ? 57  ASP   A CG  1 
ATOM   402  O  OD1 . ASP   A 1 51  ? 6.350  -1.445  1.049  1.00 36.37  ? 57  ASP   A OD1 1 
ATOM   403  O  OD2 . ASP   A 1 51  ? 5.226  -0.026  -0.268 1.00 39.91  ? 57  ASP   A OD2 1 
ATOM   404  N  N   . CYS   A 1 52  ? 7.546  -1.112  4.513  1.00 19.90  ? 58  CYS   A N   1 
ATOM   405  C  CA  . CYS   A 1 52  ? 6.862  -1.813  5.625  1.00 18.52  ? 58  CYS   A CA  1 
ATOM   406  C  C   . CYS   A 1 52  ? 6.133  -0.791  6.500  1.00 19.02  ? 58  CYS   A C   1 
ATOM   407  O  O   . CYS   A 1 52  ? 6.606  0.350   6.691  1.00 18.65  ? 58  CYS   A O   1 
ATOM   408  C  CB  . CYS   A 1 52  ? 7.856  -2.581  6.493  1.00 19.67  ? 58  CYS   A CB  1 
ATOM   409  S  SG  . CYS   A 1 52  ? 8.558  -4.078  5.744  1.00 20.89  ? 58  CYS   A SG  1 
ATOM   410  N  N   . GLN   A 1 53  ? 5.032  -1.246  7.035  1.00 17.51  ? 59  GLN   A N   1 
ATOM   411  C  CA  . GLN   A 1 53  ? 4.239  -0.581  8.032  1.00 17.49  ? 59  GLN   A CA  1 
ATOM   412  C  C   . GLN   A 1 53  ? 4.078  -1.398  9.274  1.00 15.06  ? 59  GLN   A C   1 
ATOM   413  O  O   . GLN   A 1 53  ? 3.267  -1.050  10.076 1.00 16.15  ? 59  GLN   A O   1 
ATOM   414  C  CB  . GLN   A 1 53  ? 2.885  -0.096  7.495  1.00 21.10  ? 59  GLN   A CB  1 
ATOM   415  C  CG  . GLN   A 1 53  ? 3.027  1.079   6.519  1.00 23.94  ? 59  GLN   A CG  1 
ATOM   416  C  CD  . GLN   A 1 53  ? 1.626  1.591   6.154  1.00 28.24  ? 59  GLN   A CD  1 
ATOM   417  O  OE1 . GLN   A 1 53  ? 1.098  1.369   5.047  1.00 33.21  ? 59  GLN   A OE1 1 
ATOM   418  N  NE2 . GLN   A 1 53  ? 0.962  2.256   7.071  1.00 26.18  ? 59  GLN   A NE2 1 
ATOM   419  N  N   A THR   A 1 54  ? 4.845  -2.502  9.475  0.50 14.33  ? 60  THR   A N   1 
ATOM   420  N  N   B THR   A 1 54  ? 4.863  -2.473  9.433  0.50 14.53  ? 60  THR   A N   1 
ATOM   421  C  CA  A THR   A 1 54  ? 4.859  -3.241  10.743 0.50 13.69  ? 60  THR   A CA  1 
ATOM   422  C  CA  B THR   A 1 54  ? 4.906  -3.266  10.632 0.50 14.09  ? 60  THR   A CA  1 
ATOM   423  C  C   A THR   A 1 54  ? 6.304  -3.594  11.087 0.50 12.85  ? 60  THR   A C   1 
ATOM   424  C  C   B THR   A 1 54  ? 6.384  -3.462  11.034 0.50 12.08  ? 60  THR   A C   1 
ATOM   425  O  O   A THR   A 1 54  ? 7.084  -4.034  10.233 0.50 13.81  ? 60  THR   A O   1 
ATOM   426  O  O   B THR   A 1 54  ? 7.295  -3.480  10.158 0.50 11.42  ? 60  THR   A O   1 
ATOM   427  C  CB  A THR   A 1 54  ? 4.074  -4.548  10.737 0.50 14.38  ? 60  THR   A CB  1 
ATOM   428  C  CB  B THR   A 1 54  ? 4.160  -4.603  10.457 0.50 16.69  ? 60  THR   A CB  1 
ATOM   429  O  OG1 A THR   A 1 54  ? 4.655  -5.391  9.742  0.50 17.62  ? 60  THR   A OG1 1 
ATOM   430  O  OG1 B THR   A 1 54  ? 2.834  -4.396  9.940  0.50 17.88  ? 60  THR   A OG1 1 
ATOM   431  C  CG2 A THR   A 1 54  ? 2.554  -4.377  10.532 0.50 14.01  ? 60  THR   A CG2 1 
ATOM   432  C  CG2 B THR   A 1 54  ? 4.069  -5.391  11.730 0.50 18.29  ? 60  THR   A CG2 1 
ATOM   433  N  N   . GLY   A 1 55  ? 6.601  -3.466  12.354 1.00 12.02  ? 61  GLY   A N   1 
ATOM   434  C  CA  . GLY   A 1 55  ? 7.959  -3.679  12.837 1.00 11.62  ? 61  GLY   A CA  1 
ATOM   435  C  C   . GLY   A 1 55  ? 7.963  -3.737  14.352 1.00 10.72  ? 61  GLY   A C   1 
ATOM   436  O  O   . GLY   A 1 55  ? 6.929  -3.978  14.972 1.00 11.45  ? 61  GLY   A O   1 
ATOM   437  N  N   . VAL   A 1 56  ? 9.139  -3.526  14.951 1.00 10.15  ? 62  VAL   A N   1 
ATOM   438  C  CA  . VAL   A 1 56  ? 9.334  -3.622  16.401 1.00 9.79   ? 62  VAL   A CA  1 
ATOM   439  C  C   . VAL   A 1 56  ? 10.214 -2.454  16.835 1.00 9.56   ? 62  VAL   A C   1 
ATOM   440  O  O   . VAL   A 1 56  ? 11.200 -2.157  16.159 1.00 10.42  ? 62  VAL   A O   1 
ATOM   441  C  CB  . VAL   A 1 56  ? 10.040 -4.970  16.724 1.00 10.71  ? 62  VAL   A CB  1 
ATOM   442  C  CG1 . VAL   A 1 56  ? 10.429 -5.082  18.191 1.00 12.99  ? 62  VAL   A CG1 1 
ATOM   443  C  CG2 . VAL   A 1 56  ? 9.158  -6.155  16.355 1.00 11.55  ? 62  VAL   A CG2 1 
ATOM   444  N  N   . TYR   A 1 57  ? 9.856  -1.804  17.941 1.00 9.54   ? 63  TYR   A N   1 
ATOM   445  C  CA  . TYR   A 1 57  ? 10.711 -0.720  18.445 1.00 9.35   ? 63  TYR   A CA  1 
ATOM   446  C  C   . TYR   A 1 57  ? 11.151 -0.933  19.877 1.00 10.00  ? 63  TYR   A C   1 
ATOM   447  O  O   . TYR   A 1 57  ? 10.459 -1.598  20.664 1.00 10.93  ? 63  TYR   A O   1 
ATOM   448  C  CB  . TYR   A 1 57  ? 10.047 0.709   18.308 1.00 10.42  ? 63  TYR   A CB  1 
ATOM   449  C  CG  . TYR   A 1 57  ? 9.087  1.097   19.418 1.00 10.25  ? 63  TYR   A CG  1 
ATOM   450  C  CD1 . TYR   A 1 57  ? 7.795  0.572   19.463 1.00 11.26  ? 63  TYR   A CD1 1 
ATOM   451  C  CD2 . TYR   A 1 57  ? 9.454  2.001   20.404 1.00 11.40  ? 63  TYR   A CD2 1 
ATOM   452  C  CE1 . TYR   A 1 57  ? 6.908  0.925   20.487 1.00 12.83  ? 63  TYR   A CE1 1 
ATOM   453  C  CE2 . TYR   A 1 57  ? 8.560  2.380   21.418 1.00 12.18  ? 63  TYR   A CE2 1 
ATOM   454  C  CZ  . TYR   A 1 57  ? 7.298  1.849   21.433 1.00 13.30  ? 63  TYR   A CZ  1 
ATOM   455  O  OH  . TYR   A 1 57  ? 6.387  2.195   22.420 1.00 15.80  ? 63  TYR   A OH  1 
ATOM   456  N  N   . TYR   A 1 58  ? 12.264 -0.307  20.247 1.00 9.75   ? 64  TYR   A N   1 
ATOM   457  C  CA  . TYR   A 1 58  ? 12.750 -0.397  21.623 1.00 10.26  ? 64  TYR   A CA  1 
ATOM   458  C  C   . TYR   A 1 58  ? 12.298 0.825   22.435 1.00 10.17  ? 64  TYR   A C   1 
ATOM   459  O  O   . TYR   A 1 58  ? 12.538 1.978   22.037 1.00 10.58  ? 64  TYR   A O   1 
ATOM   460  C  CB  . TYR   A 1 58  ? 14.297 -0.457  21.654 1.00 11.26  ? 64  TYR   A CB  1 
ATOM   461  C  CG  . TYR   A 1 58  ? 14.781 -0.602  23.087 1.00 11.77  ? 64  TYR   A CG  1 
ATOM   462  C  CD1 . TYR   A 1 58  ? 14.445 -1.708  23.843 1.00 12.63  ? 64  TYR   A CD1 1 
ATOM   463  C  CD2 . TYR   A 1 58  ? 15.555 0.401   23.699 1.00 12.53  ? 64  TYR   A CD2 1 
ATOM   464  C  CE1 . TYR   A 1 58  ? 14.860 -1.820  25.170 1.00 14.09  ? 64  TYR   A CE1 1 
ATOM   465  C  CE2 . TYR   A 1 58  ? 15.934 0.309   25.032 1.00 14.40  ? 64  TYR   A CE2 1 
ATOM   466  C  CZ  . TYR   A 1 58  ? 15.621 -0.820  25.743 1.00 14.08  ? 64  TYR   A CZ  1 
ATOM   467  O  OH  . TYR   A 1 58  ? 15.987 -0.948  27.085 1.00 17.55  ? 64  TYR   A OH  1 
ATOM   468  N  N   . CYS   A 1 59  ? 11.695 0.526   23.590 1.00 10.44  ? 65  CYS   A N   1 
ATOM   469  C  CA  . CYS   A 1 59  ? 11.180 1.509   24.538 1.00 11.08  ? 65  CYS   A CA  1 
ATOM   470  C  C   . CYS   A 1 59  ? 12.008 1.481   25.833 1.00 11.78  ? 65  CYS   A C   1 
ATOM   471  O  O   . CYS   A 1 59  ? 11.820 0.559   26.670 1.00 12.06  ? 65  CYS   A O   1 
ATOM   472  C  CB  . CYS   A 1 59  ? 9.721  1.214   24.848 1.00 11.83  ? 65  CYS   A CB  1 
ATOM   473  S  SG  . CYS   A 1 59  ? 8.996  2.365   26.071 1.00 13.09  ? 65  CYS   A SG  1 
ATOM   474  N  N   . SER   A 1 60  ? 12.919 2.436   25.999 1.00 11.97  ? 66  SER   A N   1 
ATOM   475  C  CA  . SER   A 1 60  ? 13.821 2.405   27.159 1.00 13.28  ? 66  SER   A CA  1 
ATOM   476  C  C   . SER   A 1 60  ? 13.102 2.585   28.471 1.00 13.49  ? 66  SER   A C   1 
ATOM   477  O  O   . SER   A 1 60  ? 13.520 1.990   29.475 1.00 15.51  ? 66  SER   A O   1 
ATOM   478  C  CB  . SER   A 1 60  ? 14.939 3.434   27.005 1.00 15.33  ? 66  SER   A CB  1 
ATOM   479  O  OG  . SER   A 1 60  ? 14.555 4.787   27.168 1.00 19.16  ? 66  SER   A OG  1 
ATOM   480  N  N   . SER   A 1 61  ? 11.982 3.358   28.497 1.00 13.26  ? 67  SER   A N   1 
ATOM   481  C  CA  . SER   A 1 61  ? 11.218 3.552   29.706 1.00 14.41  ? 67  SER   A CA  1 
ATOM   482  C  C   . SER   A 1 61  ? 10.397 2.321   30.138 1.00 13.35  ? 67  SER   A C   1 
ATOM   483  O  O   . SER   A 1 61  ? 9.762  2.351   31.197 1.00 14.44  ? 67  SER   A O   1 
ATOM   484  C  CB  . SER   A 1 61  ? 10.336 4.787   29.622 1.00 15.55  ? 67  SER   A CB  1 
ATOM   485  O  OG  . SER   A 1 61  ? 9.335  4.598   28.641 1.00 15.36  ? 67  SER   A OG  1 
ATOM   486  N  N   . ARG   A 1 62  ? 10.456 1.236   29.351 1.00 13.21  ? 68  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 62  ? 9.875  -0.034  29.728 1.00 13.32  ? 68  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 62  ? 10.889 -1.191  29.684 1.00 15.58  ? 68  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 62  ? 10.501 -2.335  29.955 1.00 15.44  ? 68  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 62  ? 8.676  -0.343  28.800 1.00 13.94  ? 68  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 62  ? 7.505  0.626   28.943 1.00 14.55  ? 68  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 62  ? 6.732  0.352   30.211 1.00 15.66  ? 68  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 62  ? 5.606  1.291   30.385 1.00 16.28  ? 68  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 62  ? 5.667  2.449   31.031 1.00 16.22  ? 68  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 62  ? 6.823  2.870   31.563 1.00 18.26  ? 68  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 62  ? 4.567  3.195   31.186 1.00 18.80  ? 68  ARG   A NH2 1 
ATOM   497  N  N   . ARG   A 1 63  ? 12.126 -0.949  29.207 1.00 15.75  ? 69  ARG   A N   1 
ATOM   498  C  CA  . ARG   A 1 63  ? 13.119 -2.023  28.903 1.00 16.29  ? 69  ARG   A CA  1 
ATOM   499  C  C   . ARG   A 1 63  ? 12.452 -3.119  28.050 1.00 17.10  ? 69  ARG   A C   1 
ATOM   500  O  O   . ARG   A 1 63  ? 12.616 -4.329  28.331 1.00 18.99  ? 69  ARG   A O   1 
ATOM   501  C  CB  . ARG   A 1 63  ? 13.762 -2.652  30.175 1.00 18.56  ? 69  ARG   A CB  1 
ATOM   502  C  CG  . ARG   A 1 63  ? 14.685 -1.699  30.796 1.00 18.79  ? 69  ARG   A CG  1 
ATOM   503  C  CD  . ARG   A 1 63  ? 15.511 -2.472  31.831 1.00 22.50  ? 69  ARG   A CD  1 
ATOM   504  N  NE  . ARG   A 1 63  ? 16.288 -1.548  32.651 1.00 24.70  ? 69  ARG   A NE  1 
ATOM   505  C  CZ  . ARG   A 1 63  ? 15.977 -1.188  33.899 1.00 23.42  ? 69  ARG   A CZ  1 
ATOM   506  N  NH1 . ARG   A 1 63  ? 14.881 -1.674  34.489 1.00 23.21  ? 69  ARG   A NH1 1 
ATOM   507  N  NH2 . ARG   A 1 63  ? 16.753 -0.339  34.563 1.00 24.76  ? 69  ARG   A NH2 1 
ATOM   508  N  N   . LYS   A 1 64  ? 11.718 -2.715  27.028 1.00 13.95  ? 70  LYS   A N   1 
ATOM   509  C  CA  . LYS   A 1 64  ? 10.990 -3.708  26.238 1.00 14.57  ? 70  LYS   A CA  1 
ATOM   510  C  C   . LYS   A 1 64  ? 10.972 -3.313  24.795 1.00 13.61  ? 70  LYS   A C   1 
ATOM   511  O  O   . LYS   A 1 64  ? 10.901 -2.112  24.460 1.00 13.72  ? 70  LYS   A O   1 
ATOM   512  C  CB  . LYS   A 1 64  ? 9.523  -3.777  26.750 1.00 16.80  ? 70  LYS   A CB  1 
ATOM   513  C  CG  . LYS   A 1 64  ? 9.349  -4.719  27.955 1.00 26.78  ? 70  LYS   A CG  1 
ATOM   514  C  CD  . LYS   A 1 64  ? 7.877  -4.977  28.246 1.00 36.47  ? 70  LYS   A CD  1 
ATOM   515  C  CE  . LYS   A 1 64  ? 7.692  -5.779  29.514 1.00 43.49  ? 70  LYS   A CE  1 
ATOM   516  N  NZ  . LYS   A 1 64  ? 8.386  -5.153  30.669 1.00 47.83  ? 70  LYS   A NZ  1 
ATOM   517  N  N   . HIS   A 1 65  ? 10.917 -4.311  23.926 1.00 12.31  ? 71  HIS   A N   1 
ATOM   518  C  CA  . HIS   A 1 65  ? 10.694 -4.162  22.507 1.00 12.10  ? 71  HIS   A CA  1 
ATOM   519  C  C   . HIS   A 1 65  ? 9.222  -4.476  22.237 1.00 13.05  ? 71  HIS   A C   1 
ATOM   520  O  O   . HIS   A 1 65  ? 8.702  -5.539  22.691 1.00 15.72  ? 71  HIS   A O   1 
ATOM   521  C  CB  . HIS   A 1 65  ? 11.591 -5.093  21.700 1.00 11.89  ? 71  HIS   A CB  1 
ATOM   522  C  CG  . HIS   A 1 65  ? 13.054 -4.776  21.795 1.00 12.94  ? 71  HIS   A CG  1 
ATOM   523  N  ND1 . HIS   A 1 65  ? 13.775 -4.100  20.803 1.00 15.42  ? 71  HIS   A ND1 1 
ATOM   524  C  CD2 . HIS   A 1 65  ? 13.912 -5.091  22.791 1.00 13.32  ? 71  HIS   A CD2 1 
ATOM   525  C  CE1 . HIS   A 1 65  ? 15.058 -4.040  21.224 1.00 13.14  ? 71  HIS   A CE1 1 
ATOM   526  N  NE2 . HIS   A 1 65  ? 15.162 -4.615  22.406 1.00 16.66  ? 71  HIS   A NE2 1 
ATOM   527  N  N   . TYR   A 1 66  ? 8.534  -3.623  21.494 1.00 11.53  ? 72  TYR   A N   1 
ATOM   528  C  CA  . TYR   A 1 66  ? 7.115  -3.800  21.215 1.00 11.30  ? 72  TYR   A CA  1 
ATOM   529  C  C   . TYR   A 1 66  ? 6.881  -3.903  19.727 1.00 10.74  ? 72  TYR   A C   1 
ATOM   530  O  O   . TYR   A 1 66  ? 7.385  -3.063  18.956 1.00 11.15  ? 72  TYR   A O   1 
ATOM   531  C  CB  . TYR   A 1 66  ? 6.314  -2.547  21.686 1.00 12.19  ? 72  TYR   A CB  1 
ATOM   532  C  CG  . TYR   A 1 66  ? 6.230  -2.357  23.197 1.00 12.95  ? 72  TYR   A CG  1 
ATOM   533  C  CD1 . TYR   A 1 66  ? 5.387  -3.153  23.976 1.00 15.62  ? 72  TYR   A CD1 1 
ATOM   534  C  CD2 . TYR   A 1 66  ? 7.018  -1.407  23.844 1.00 13.88  ? 72  TYR   A CD2 1 
ATOM   535  C  CE1 . TYR   A 1 66  ? 5.315  -3.003  25.367 1.00 15.38  ? 72  TYR   A CE1 1 
ATOM   536  C  CE2 . TYR   A 1 66  ? 6.950  -1.235  25.240 1.00 14.56  ? 72  TYR   A CE2 1 
ATOM   537  C  CZ  . TYR   A 1 66  ? 6.078  -2.019  25.995 1.00 15.08  ? 72  TYR   A CZ  1 
ATOM   538  O  OH  . TYR   A 1 66  ? 5.994  -1.825  27.369 1.00 17.28  ? 72  TYR   A OH  1 
ATOM   539  N  N   . PRO   A 1 67  ? 6.044  -4.850  19.299 1.00 11.02  ? 73  PRO   A N   1 
ATOM   540  C  CA  . PRO   A 1 67  ? 5.628  -4.891  17.896 1.00 11.28  ? 73  PRO   A CA  1 
ATOM   541  C  C   . PRO   A 1 67  ? 4.598  -3.797  17.622 1.00 11.54  ? 73  PRO   A C   1 
ATOM   542  O  O   . PRO   A 1 67  ? 3.663  -3.655  18.447 1.00 13.18  ? 73  PRO   A O   1 
ATOM   543  C  CB  . PRO   A 1 67  ? 4.991  -6.321  17.718 1.00 13.75  ? 73  PRO   A CB  1 
ATOM   544  C  CG  . PRO   A 1 67  ? 4.588  -6.701  19.087 1.00 16.05  ? 73  PRO   A CG  1 
ATOM   545  C  CD  . PRO   A 1 67  ? 5.500  -5.969  20.101 1.00 12.39  ? 73  PRO   A CD  1 
ATOM   546  N  N   . VAL   A 1 68  ? 4.698  -3.134  16.535 1.00 10.64  ? 74  VAL   A N   1 
ATOM   547  C  CA  . VAL   A 1 68  ? 3.797  -2.010  16.176 1.00 12.58  ? 74  VAL   A CA  1 
ATOM   548  C  C   . VAL   A 1 68  ? 3.473  -2.003  14.709 1.00 12.67  ? 74  VAL   A C   1 
ATOM   549  O  O   . VAL   A 1 68  ? 4.263  -2.337  13.855 1.00 13.03  ? 74  VAL   A O   1 
ATOM   550  C  CB  . VAL   A 1 68  ? 4.411  -0.623  16.565 1.00 14.71  ? 74  VAL   A CB  1 
ATOM   551  C  CG1 . VAL   A 1 68  ? 4.369  -0.424  18.085 1.00 15.86  ? 74  VAL   A CG1 1 
ATOM   552  C  CG2 . VAL   A 1 68  ? 5.815  -0.428  15.997 1.00 15.96  ? 74  VAL   A CG2 1 
ATOM   553  N  N   . SER   A 1 69  ? 2.273  -1.463  14.403 1.00 12.94  ? 75  SER   A N   1 
ATOM   554  C  CA  . SER   A 1 69  ? 1.880  -0.998  13.084 1.00 13.97  ? 75  SER   A CA  1 
ATOM   555  C  C   . SER   A 1 69  ? 2.129  0.537   13.015 1.00 13.78  ? 75  SER   A C   1 
ATOM   556  O  O   . SER   A 1 69  ? 1.808  1.210   13.997 1.00 14.34  ? 75  SER   A O   1 
ATOM   557  C  CB  . SER   A 1 69  ? 0.398  -1.226  12.871 1.00 17.82  ? 75  SER   A CB  1 
ATOM   558  O  OG  . SER   A 1 69  ? 0.175  -2.613  12.903 1.00 25.77  ? 75  SER   A OG  1 
ATOM   559  N  N   . PHE   A 1 70  ? 2.696  1.074   11.946 1.00 13.39  ? 76  PHE   A N   1 
ATOM   560  C  CA  . PHE   A 1 70  ? 3.013  2.490   11.886 1.00 14.21  ? 76  PHE   A CA  1 
ATOM   561  C  C   . PHE   A 1 70  ? 2.610  3.076   10.581 1.00 15.69  ? 76  PHE   A C   1 
ATOM   562  O  O   . PHE   A 1 70  ? 2.549  2.382   9.565  1.00 17.08  ? 76  PHE   A O   1 
ATOM   563  C  CB  . PHE   A 1 70  ? 4.519  2.738   12.240 1.00 14.19  ? 76  PHE   A CB  1 
ATOM   564  C  CG  . PHE   A 1 70  ? 5.519  1.937   11.432 1.00 13.04  ? 76  PHE   A CG  1 
ATOM   565  C  CD1 . PHE   A 1 70  ? 5.916  0.674   11.839 1.00 12.77  ? 76  PHE   A CD1 1 
ATOM   566  C  CD2 . PHE   A 1 70  ? 6.101  2.469   10.285 1.00 13.95  ? 76  PHE   A CD2 1 
ATOM   567  C  CE1 . PHE   A 1 70  ? 6.856  -0.044  11.105 1.00 13.67  ? 76  PHE   A CE1 1 
ATOM   568  C  CE2 . PHE   A 1 70  ? 7.025  1.724   9.543  1.00 14.76  ? 76  PHE   A CE2 1 
ATOM   569  C  CZ  . PHE   A 1 70  ? 7.384  0.482   9.956  1.00 15.04  ? 76  PHE   A CZ  1 
ATOM   570  N  N   . SER   A 1 71  ? 2.355  4.381   10.578 1.00 16.79  ? 77  SER   A N   1 
ATOM   571  C  CA  . SER   A 1 71  ? 1.940  5.072   9.359  1.00 18.53  ? 77  SER   A CA  1 
ATOM   572  C  C   . SER   A 1 71  ? 3.129  5.306   8.411  1.00 18.64  ? 77  SER   A C   1 
ATOM   573  O  O   . SER   A 1 71  ? 4.304  5.149   8.777  1.00 17.62  ? 77  SER   A O   1 
ATOM   574  C  CB  . SER   A 1 71  ? 1.258  6.398   9.715  1.00 19.79  ? 77  SER   A CB  1 
ATOM   575  O  OG  . SER   A 1 71  ? 2.107  7.265   10.432 1.00 22.23  ? 77  SER   A OG  1 
ATOM   576  N  N   . LYS   A 1 72  ? 2.848  5.676   7.179  1.00 18.90  ? 78  LYS   A N   1 
ATOM   577  C  CA  . LYS   A 1 72  ? 3.883  6.009   6.216  1.00 19.34  ? 78  LYS   A CA  1 
ATOM   578  C  C   . LYS   A 1 72  ? 4.523  7.354   6.578  1.00 19.51  ? 78  LYS   A C   1 
ATOM   579  O  O   . LYS   A 1 72  ? 3.837  8.225   7.116  1.00 22.07  ? 78  LYS   A O   1 
ATOM   580  C  CB  . LYS   A 1 72  ? 3.323  6.045   4.791  1.00 22.31  ? 78  LYS   A CB  1 
ATOM   581  C  CG  . LYS   A 1 72  ? 2.871  4.666   4.373  1.00 23.97  ? 78  LYS   A CG  1 
ATOM   582  C  CD  . LYS   A 1 72  ? 2.513  4.577   2.893  1.00 30.91  ? 78  LYS   A CD  1 
ATOM   583  C  CE  . LYS   A 1 72  ? 2.115  3.164   2.523  1.00 35.87  ? 78  LYS   A CE  1 
ATOM   584  N  NZ  . LYS   A 1 72  ? 2.280  2.890   1.065  1.00 41.72  ? 78  LYS   A NZ  1 
ATOM   585  N  N   . PRO   A 1 73  ? 5.787  7.611   6.209  1.00 18.79  ? 79  PRO   A N   1 
ATOM   586  C  CA  . PRO   A 1 73  ? 6.430  8.883   6.569  1.00 18.99  ? 79  PRO   A CA  1 
ATOM   587  C  C   . PRO   A 1 73  ? 5.626  10.062  6.022  1.00 21.59  ? 79  PRO   A C   1 
ATOM   588  O  O   . PRO   A 1 73  ? 5.275  10.075  4.836  1.00 24.15  ? 79  PRO   A O   1 
ATOM   589  C  CB  . PRO   A 1 73  ? 7.824  8.769   5.942  1.00 20.83  ? 79  PRO   A CB  1 
ATOM   590  C  CG  . PRO   A 1 73  ? 8.095  7.317   5.845  1.00 23.09  ? 79  PRO   A CG  1 
ATOM   591  C  CD  . PRO   A 1 73  ? 6.728  6.675   5.551  1.00 20.90  ? 79  PRO   A CD  1 
ATOM   592  N  N   . SER   A 1 74  ? 5.357  11.029  6.880  1.00 21.94  ? 80  SER   A N   1 
ATOM   593  C  CA  . SER   A 1 74  ? 4.490  12.160  6.518  1.00 23.87  ? 80  SER   A CA  1 
ATOM   594  C  C   . SER   A 1 74  ? 4.919  13.429  7.262  1.00 23.27  ? 80  SER   A C   1 
ATOM   595  O  O   . SER   A 1 74  ? 5.739  13.409  8.179  1.00 21.05  ? 80  SER   A O   1 
ATOM   596  C  CB  . SER   A 1 74  ? 3.018  11.842  6.879  1.00 28.80  ? 80  SER   A CB  1 
ATOM   597  O  OG  . SER   A 1 74  ? 2.626  10.510  6.613  1.00 37.87  ? 80  SER   A OG  1 
ATOM   598  N  N   . LEU   A 1 75  ? 4.204  14.554  6.934  1.00 25.27  ? 81  LEU   A N   1 
ATOM   599  C  CA  . LEU   A 1 75  ? 4.406  15.835  7.584  1.00 27.09  ? 81  LEU   A CA  1 
ATOM   600  C  C   . LEU   A 1 75  ? 3.307  15.908  8.655  1.00 27.44  ? 81  LEU   A C   1 
ATOM   601  O  O   . LEU   A 1 75  ? 2.103  15.960  8.325  1.00 30.62  ? 81  LEU   A O   1 
ATOM   602  C  CB  . LEU   A 1 75  ? 4.210  16.956  6.531  1.00 28.72  ? 81  LEU   A CB  1 
ATOM   603  C  CG  . LEU   A 1 75  ? 4.482  18.370  6.993  1.00 33.54  ? 81  LEU   A CG  1 
ATOM   604  C  CD1 . LEU   A 1 75  ? 5.937  18.555  7.344  1.00 34.78  ? 81  LEU   A CD1 1 
ATOM   605  C  CD2 . LEU   A 1 75  ? 4.098  19.391  5.892  1.00 35.00  ? 81  LEU   A CD2 1 
ATOM   606  N  N   . ILE   A 1 76  ? 3.580  15.441  9.848  1.00 26.66  ? 82  ILE   A N   1 
ATOM   607  C  CA  . ILE   A 1 76  ? 2.650  15.402  11.011 1.00 27.18  ? 82  ILE   A CA  1 
ATOM   608  C  C   . ILE   A 1 76  ? 2.922  16.641  11.878 1.00 27.85  ? 82  ILE   A C   1 
ATOM   609  O  O   . ILE   A 1 76  ? 4.093  17.031  11.979 1.00 26.76  ? 82  ILE   A O   1 
ATOM   610  C  CB  . ILE   A 1 76  ? 2.892  14.178  11.933 1.00 29.44  ? 82  ILE   A CB  1 
ATOM   611  C  CG1 . ILE   A 1 76  ? 2.523  12.845  11.286 1.00 31.49  ? 82  ILE   A CG1 1 
ATOM   612  C  CG2 . ILE   A 1 76  ? 2.141  14.366  13.234 1.00 30.85  ? 82  ILE   A CG2 1 
ATOM   613  C  CD1 . ILE   A 1 76  ? 3.241  11.688  11.904 1.00 31.57  ? 82  ILE   A CD1 1 
ATOM   614  N  N   . PHE   A 1 77  ? 1.874  17.393  12.281 1.00 28.48  ? 83  PHE   A N   1 
ATOM   615  C  CA  . PHE   A 1 77  ? 2.199  18.548  13.163 1.00 29.44  ? 83  PHE   A CA  1 
ATOM   616  C  C   . PHE   A 1 77  ? 2.620  18.092  14.550 1.00 31.05  ? 83  PHE   A C   1 
ATOM   617  O  O   . PHE   A 1 77  ? 1.892  17.305  15.116 1.00 33.56  ? 83  PHE   A O   1 
ATOM   618  C  CB  . PHE   A 1 77  ? 1.086  19.593  13.246 1.00 30.46  ? 83  PHE   A CB  1 
ATOM   619  C  CG  . PHE   A 1 77  ? 1.325  20.702  14.236 1.00 33.81  ? 83  PHE   A CG  1 
ATOM   620  C  CD1 . PHE   A 1 77  ? 1.959  21.865  13.840 1.00 36.63  ? 83  PHE   A CD1 1 
ATOM   621  C  CD2 . PHE   A 1 77  ? 0.919  20.584  15.554 1.00 37.69  ? 83  PHE   A CD2 1 
ATOM   622  C  CE1 . PHE   A 1 77  ? 2.178  22.892  14.744 1.00 39.28  ? 83  PHE   A CE1 1 
ATOM   623  C  CE2 . PHE   A 1 77  ? 1.138  21.607  16.459 1.00 38.56  ? 83  PHE   A CE2 1 
ATOM   624  C  CZ  . PHE   A 1 77  ? 1.737  22.770  16.043 1.00 39.81  ? 83  PHE   A CZ  1 
ATOM   625  N  N   . VAL   A 1 78  ? 3.803  18.559  15.042 1.00 29.37  ? 84  VAL   A N   1 
ATOM   626  C  CA  . VAL   A 1 78  ? 4.338  18.275  16.410 1.00 28.94  ? 84  VAL   A CA  1 
ATOM   627  C  C   . VAL   A 1 78  ? 4.234  19.486  17.355 1.00 29.82  ? 84  VAL   A C   1 
ATOM   628  O  O   . VAL   A 1 78  ? 4.692  20.512  17.014 1.00 30.26  ? 84  VAL   A O   1 
ATOM   629  C  CB  . VAL   A 1 78  ? 5.787  17.732  16.432 1.00 27.08  ? 84  VAL   A CB  1 
ATOM   630  C  CG1 . VAL   A 1 78  ? 6.151  17.378  17.854 1.00 28.09  ? 84  VAL   A CG1 1 
ATOM   631  C  CG2 . VAL   A 1 78  ? 5.951  16.514  15.533 1.00 26.35  ? 84  VAL   A CG2 1 
ATOM   632  N  N   . GLU   A 1 79  ? 3.562  19.288  18.518 1.00 30.33  ? 85  GLU   A N   1 
ATOM   633  C  CA  . GLU   A 1 79  ? 3.299  20.313  19.555 1.00 32.80  ? 85  GLU   A CA  1 
ATOM   634  C  C   . GLU   A 1 79  ? 4.614  20.891  19.997 1.00 34.09  ? 85  GLU   A C   1 
ATOM   635  O  O   . GLU   A 1 79  ? 5.539  20.140  20.054 1.00 33.70  ? 85  GLU   A O   1 
ATOM   636  C  CB  . GLU   A 1 79  ? 2.662  19.784  20.857 1.00 35.92  ? 85  GLU   A CB  1 
ATOM   637  C  CG  . GLU   A 1 79  ? 1.211  19.402  20.619 1.00 42.17  ? 85  GLU   A CG  1 
ATOM   638  C  CD  . GLU   A 1 79  ? 0.442  20.581  20.057 1.00 50.95  ? 85  GLU   A CD  1 
ATOM   639  O  OE1 . GLU   A 1 79  ? 0.475  21.634  20.680 1.00 52.53  ? 85  GLU   A OE1 1 
ATOM   640  O  OE2 . GLU   A 1 79  ? -0.138 20.453  18.986 1.00 54.77  ? 85  GLU   A OE2 1 
ATOM   641  N  N   . ALA   A 1 80  ? 4.574  22.163  20.368 1.00 35.40  ? 86  ALA   A N   1 
ATOM   642  C  CA  . ALA   A 1 80  ? 5.737  22.767  21.053 1.00 37.24  ? 86  ALA   A CA  1 
ATOM   643  C  C   . ALA   A 1 80  ? 6.227  21.924  22.225 1.00 38.99  ? 86  ALA   A C   1 
ATOM   644  O  O   . ALA   A 1 80  ? 5.402  21.393  22.960 1.00 39.33  ? 86  ALA   A O   1 
ATOM   645  C  CB  . ALA   A 1 80  ? 5.287  24.122  21.542 1.00 38.79  ? 86  ALA   A CB  1 
ATOM   646  N  N   . SER   A 1 81  ? 7.504  21.702  22.284 1.00 38.71  ? 87  SER   A N   1 
ATOM   647  C  CA  . SER   A 1 81  ? 8.262  20.997  23.352 1.00 39.02  ? 87  SER   A CA  1 
ATOM   648  C  C   . SER   A 1 81  ? 9.479  21.846  23.744 1.00 38.12  ? 87  SER   A C   1 
ATOM   649  O  O   . SER   A 1 81  ? 9.618  22.954  23.094 1.00 37.58  ? 87  SER   A O   1 
ATOM   650  C  CB  . SER   A 1 81  ? 8.899  19.799  22.699 1.00 40.73  ? 87  SER   A CB  1 
ATOM   651  O  OG  . SER   A 1 81  ? 9.797  20.152  21.670 1.00 40.67  ? 87  SER   A OG  1 
ATOM   652  N  N   . GLU   A 1 82  ? 10.336 21.399  24.715 1.00 37.71  ? 88  GLU   A N   1 
ATOM   653  C  CA  . GLU   A 1 82  ? 11.507 22.271  24.976 1.00 37.06  ? 88  GLU   A CA  1 
ATOM   654  C  C   . GLU   A 1 82  ? 12.457 22.328  23.777 1.00 34.10  ? 88  GLU   A C   1 
ATOM   655  O  O   . GLU   A 1 82  ? 13.267 23.186  23.804 1.00 34.98  ? 88  GLU   A O   1 
ATOM   656  C  CB  . GLU   A 1 82  ? 12.207 21.770  26.239 1.00 40.45  ? 88  GLU   A CB  1 
ATOM   657  C  CG  . GLU   A 1 82  ? 11.443 20.707  27.001 1.00 49.48  ? 88  GLU   A CG  1 
ATOM   658  C  CD  . GLU   A 1 82  ? 12.416 19.657  27.505 1.00 59.94  ? 88  GLU   A CD  1 
ATOM   659  O  OE1 . GLU   A 1 82  ? 13.622 19.929  27.462 1.00 62.62  ? 88  GLU   A OE1 1 
ATOM   660  O  OE2 . GLU   A 1 82  ? 11.972 18.573  27.902 1.00 62.12  ? 88  GLU   A OE2 1 
ATOM   661  N  N   . TYR   A 1 83  ? 12.238 21.538  22.732 1.00 31.71  ? 89  TYR   A N   1 
ATOM   662  C  CA  . TYR   A 1 83  ? 13.204 21.384  21.605 1.00 28.55  ? 89  TYR   A CA  1 
ATOM   663  C  C   . TYR   A 1 83  ? 12.753 21.999  20.305 1.00 27.49  ? 89  TYR   A C   1 
ATOM   664  O  O   . TYR   A 1 83  ? 13.647 22.381  19.571 1.00 27.04  ? 89  TYR   A O   1 
ATOM   665  C  CB  . TYR   A 1 83  ? 13.426 19.892  21.319 1.00 27.92  ? 89  TYR   A CB  1 
ATOM   666  C  CG  . TYR   A 1 83  ? 14.095 19.263  22.517 1.00 28.45  ? 89  TYR   A CG  1 
ATOM   667  C  CD1 . TYR   A 1 83  ? 15.428 19.513  22.785 1.00 30.20  ? 89  TYR   A CD1 1 
ATOM   668  C  CD2 . TYR   A 1 83  ? 13.396 18.489  23.424 1.00 30.36  ? 89  TYR   A CD2 1 
ATOM   669  C  CE1 . TYR   A 1 83  ? 16.055 18.986  23.897 1.00 32.59  ? 89  TYR   A CE1 1 
ATOM   670  C  CE2 . TYR   A 1 83  ? 14.015 17.943  24.538 1.00 32.65  ? 89  TYR   A CE2 1 
ATOM   671  C  CZ  . TYR   A 1 83  ? 15.361 18.174  24.766 1.00 34.35  ? 89  TYR   A CZ  1 
ATOM   672  O  OH  . TYR   A 1 83  ? 16.017 17.666  25.849 1.00 36.80  ? 89  TYR   A OH  1 
ATOM   673  N  N   . TYR   A 1 84  ? 11.447 21.911  19.995 1.00 29.21  ? 90  TYR   A N   1 
ATOM   674  C  CA  . TYR   A 1 84  ? 11.164 22.697  18.798 1.00 28.58  ? 90  TYR   A CA  1 
ATOM   675  C  C   . TYR   A 1 84  ? 9.863  23.420  19.014 1.00 31.70  ? 90  TYR   A C   1 
ATOM   676  O  O   . TYR   A 1 84  ? 8.980  23.059  19.807 1.00 33.00  ? 90  TYR   A O   1 
ATOM   677  C  CB  . TYR   A 1 84  ? 11.019 21.849  17.542 1.00 27.15  ? 90  TYR   A CB  1 
ATOM   678  C  CG  . TYR   A 1 84  ? 12.116 20.902  17.129 1.00 24.87  ? 90  TYR   A CG  1 
ATOM   679  C  CD1 . TYR   A 1 84  ? 12.934 21.215  16.057 1.00 24.31  ? 90  TYR   A CD1 1 
ATOM   680  C  CD2 . TYR   A 1 84  ? 12.274 19.672  17.736 1.00 23.34  ? 90  TYR   A CD2 1 
ATOM   681  C  CE1 . TYR   A 1 84  ? 13.927 20.357  15.616 1.00 22.68  ? 90  TYR   A CE1 1 
ATOM   682  C  CE2 . TYR   A 1 84  ? 13.257 18.799  17.304 1.00 22.06  ? 90  TYR   A CE2 1 
ATOM   683  C  CZ  . TYR   A 1 84  ? 14.098 19.144  16.257 1.00 20.84  ? 90  TYR   A CZ  1 
ATOM   684  O  OH  . TYR   A 1 84  ? 15.053 18.278  15.803 1.00 20.31  ? 90  TYR   A OH  1 
ATOM   685  N  N   . PRO   A 1 85  ? 9.704  24.525  18.317 1.00 33.66  ? 91  PRO   A N   1 
ATOM   686  C  CA  . PRO   A 1 85  ? 8.413  25.128  18.290 1.00 35.32  ? 91  PRO   A CA  1 
ATOM   687  C  C   . PRO   A 1 85  ? 7.390  24.304  17.524 1.00 35.72  ? 91  PRO   A C   1 
ATOM   688  O  O   . PRO   A 1 85  ? 7.709  23.548  16.569 1.00 34.49  ? 91  PRO   A O   1 
ATOM   689  C  CB  . PRO   A 1 85  ? 8.751  26.189  17.251 1.00 37.42  ? 91  PRO   A CB  1 
ATOM   690  C  CG  . PRO   A 1 85  ? 9.905  25.691  16.440 1.00 38.04  ? 91  PRO   A CG  1 
ATOM   691  C  CD  . PRO   A 1 85  ? 10.773 25.127  17.521 1.00 34.12  ? 91  PRO   A CD  1 
ATOM   692  N  N   . ALA   A 1 86  ? 6.139  24.628  17.750 1.00 37.41  ? 92  ALA   A N   1 
ATOM   693  C  CA  . ALA   A 1 86  ? 5.073  23.936  17.016 1.00 37.85  ? 92  ALA   A CA  1 
ATOM   694  C  C   . ALA   A 1 86  ? 5.406  23.966  15.510 1.00 36.74  ? 92  ALA   A C   1 
ATOM   695  O  O   . ALA   A 1 86  ? 5.549  25.054  14.954 1.00 39.57  ? 92  ALA   A O   1 
ATOM   696  C  CB  . ALA   A 1 86  ? 3.764  24.626  17.439 1.00 38.39  ? 92  ALA   A CB  1 
ATOM   697  N  N   . ARG   A 1 87  ? 5.548  22.820  14.866 1.00 34.81  ? 93  ARG   A N   1 
ATOM   698  C  CA  . ARG   A 1 87  ? 5.809  22.925  13.400 1.00 32.56  ? 93  ARG   A CA  1 
ATOM   699  C  C   . ARG   A 1 87  ? 5.577  21.582  12.788 1.00 31.38  ? 93  ARG   A C   1 
ATOM   700  O  O   . ARG   A 1 87  ? 5.336  20.669  13.518 1.00 31.38  ? 93  ARG   A O   1 
ATOM   701  C  CB  . ARG   A 1 87  ? 7.295  22.989  13.056 1.00 32.22  ? 93  ARG   A CB  1 
ATOM   702  C  CG  . ARG   A 1 87  ? 8.087  21.691  13.226 1.00 31.76  ? 93  ARG   A CG  1 
ATOM   703  C  CD  . ARG   A 1 87  ? 9.364  21.689  14.065 1.00 32.09  ? 93  ARG   A CD  1 
ATOM   704  N  NE  . ARG   A 1 87  ? 10.255 20.554  13.828 1.00 33.07  ? 93  ARG   A NE  1 
ATOM   705  C  CZ  . ARG   A 1 87  ? 10.269 19.418  14.516 1.00 34.21  ? 93  ARG   A CZ  1 
ATOM   706  N  NH1 . ARG   A 1 87  ? 11.088 18.448  14.149 1.00 28.32  ? 93  ARG   A NH1 1 
ATOM   707  N  NH2 . ARG   A 1 87  ? 9.467  19.254  15.552 1.00 33.74  ? 93  ARG   A NH2 1 
ATOM   708  N  N   . TYR   A 1 88  ? 5.648  21.500  11.461 1.00 31.48  ? 94  TYR   A N   1 
ATOM   709  C  CA  . TYR   A 1 88  ? 5.470  20.239  10.730 1.00 31.65  ? 94  TYR   A CA  1 
ATOM   710  C  C   . TYR   A 1 88  ? 6.748  19.398  10.727 1.00 28.12  ? 94  TYR   A C   1 
ATOM   711  O  O   . TYR   A 1 88  ? 7.740  19.800  10.107 1.00 28.94  ? 94  TYR   A O   1 
ATOM   712  C  CB  . TYR   A 1 88  ? 4.849  20.514  9.374  1.00 32.84  ? 94  TYR   A CB  1 
ATOM   713  C  CG  . TYR   A 1 88  ? 3.372  20.770  9.540  1.00 34.48  ? 94  TYR   A CG  1 
ATOM   714  C  CD1 . TYR   A 1 88  ? 2.447  19.744  9.642  1.00 35.90  ? 94  TYR   A CD1 1 
ATOM   715  C  CD2 . TYR   A 1 88  ? 2.912  22.057  9.709  1.00 35.59  ? 94  TYR   A CD2 1 
ATOM   716  C  CE1 . TYR   A 1 88  ? 1.095  20.004  9.808  1.00 37.76  ? 94  TYR   A CE1 1 
ATOM   717  C  CE2 . TYR   A 1 88  ? 1.570  22.339  9.896  1.00 37.40  ? 94  TYR   A CE2 1 
ATOM   718  C  CZ  . TYR   A 1 88  ? 0.654  21.309  9.959  1.00 39.08  ? 94  TYR   A CZ  1 
ATOM   719  O  OH  . TYR   A 1 88  ? -0.661 21.636  10.146 1.00 43.44  ? 94  TYR   A OH  1 
ATOM   720  N  N   . GLN   A 1 89  ? 6.780  18.435  11.658 1.00 24.30  ? 95  GLN   A N   1 
ATOM   721  C  CA  . GLN   A 1 89  ? 7.990  17.594  11.526 1.00 22.12  ? 95  GLN   A CA  1 
ATOM   722  C  C   . GLN   A 1 89  ? 7.770  16.723  10.289 1.00 20.80  ? 95  GLN   A C   1 
ATOM   723  O  O   . GLN   A 1 89  ? 6.682  16.144  10.104 1.00 22.67  ? 95  GLN   A O   1 
ATOM   724  C  CB  . GLN   A 1 89  ? 8.220  16.756  12.785 1.00 22.86  ? 95  GLN   A CB  1 
ATOM   725  C  CG  . GLN   A 1 89  ? 9.459  15.912  12.680 1.00 21.91  ? 95  GLN   A CG  1 
ATOM   726  C  CD  . GLN   A 1 89  ? 10.001 15.433  14.020 1.00 18.56  ? 95  GLN   A CD  1 
ATOM   727  O  OE1 . GLN   A 1 89  ? 10.008 16.136  15.050 1.00 21.68  ? 95  GLN   A OE1 1 
ATOM   728  N  NE2 . GLN   A 1 89  ? 10.518 14.213  14.025 1.00 18.40  ? 95  GLN   A NE2 1 
ATOM   729  N  N   . SER   A 1 90  ? 8.770  16.637  9.414  1.00 20.54  ? 96  SER   A N   1 
ATOM   730  C  CA  . SER   A 1 90  ? 8.646  15.885  8.184  1.00 20.06  ? 96  SER   A CA  1 
ATOM   731  C  C   . SER   A 1 90  ? 9.249  14.460  8.351  1.00 19.39  ? 96  SER   A C   1 
ATOM   732  O  O   . SER   A 1 90  ? 10.028 14.194  9.300  1.00 18.65  ? 96  SER   A O   1 
ATOM   733  C  CB  . SER   A 1 90  ? 9.346  16.625  7.051  1.00 22.64  ? 96  SER   A CB  1 
ATOM   734  O  OG  . SER   A 1 90  ? 10.725 16.699  7.357  1.00 24.74  ? 96  SER   A OG  1 
ATOM   735  N  N   . HIS   A 1 91  ? 8.851  13.563  7.440  1.00 18.73  ? 97  HIS   A N   1 
ATOM   736  C  CA  . HIS   A 1 91  ? 9.346  12.185  7.381  1.00 18.07  ? 97  HIS   A CA  1 
ATOM   737  C  C   . HIS   A 1 91  ? 9.082  11.451  8.713  1.00 16.13  ? 97  HIS   A C   1 
ATOM   738  O  O   . HIS   A 1 91  ? 9.915  10.619  9.131  1.00 17.00  ? 97  HIS   A O   1 
ATOM   739  C  CB  . HIS   A 1 91  ? 10.867 12.178  7.005  1.00 19.19  ? 97  HIS   A CB  1 
ATOM   740  C  CG  . HIS   A 1 91  ? 11.153 12.774  5.646  1.00 20.57  ? 97  HIS   A CG  1 
ATOM   741  N  ND1 . HIS   A 1 91  ? 11.242 11.980  4.522  1.00 22.51  ? 97  HIS   A ND1 1 
ATOM   742  C  CD2 . HIS   A 1 91  ? 11.290 14.071  5.283  1.00 23.80  ? 97  HIS   A CD2 1 
ATOM   743  C  CE1 . HIS   A 1 91  ? 11.481 12.819  3.497  1.00 23.64  ? 97  HIS   A CE1 1 
ATOM   744  N  NE2 . HIS   A 1 91  ? 11.518 14.079  3.914  1.00 25.34  ? 97  HIS   A NE2 1 
ATOM   745  N  N   . LEU   A 1 92  ? 7.948  11.696  9.321  1.00 15.94  ? 98  LEU   A N   1 
ATOM   746  C  CA  . LEU   A 1 92  ? 7.611  11.161  10.651 1.00 16.73  ? 98  LEU   A CA  1 
ATOM   747  C  C   . LEU   A 1 92  ? 6.541  10.082  10.486 1.00 16.75  ? 98  LEU   A C   1 
ATOM   748  O  O   . LEU   A 1 92  ? 5.589  10.241  9.705  1.00 17.84  ? 98  LEU   A O   1 
ATOM   749  C  CB  . LEU   A 1 92  ? 7.071  12.307  11.551 1.00 18.46  ? 98  LEU   A CB  1 
ATOM   750  C  CG  . LEU   A 1 92  ? 6.776  11.903  13.019 1.00 19.44  ? 98  LEU   A CG  1 
ATOM   751  C  CD1 . LEU   A 1 92  ? 8.030  11.553  13.755 1.00 18.98  ? 98  LEU   A CD1 1 
ATOM   752  C  CD2 . LEU   A 1 92  ? 6.046  13.036  13.787 1.00 22.29  ? 98  LEU   A CD2 1 
ATOM   753  N  N   . MET   A 1 93  ? 6.673  8.983   11.232 1.00 15.42  ? 99  MET   A N   1 
ATOM   754  C  CA  . MET   A 1 93  ? 5.711  7.862   11.215 1.00 15.59  ? 99  MET   A CA  1 
ATOM   755  C  C   . MET   A 1 93  ? 5.129  7.722   12.614 1.00 15.58  ? 99  MET   A C   1 
ATOM   756  O  O   . MET   A 1 93  ? 5.880  7.820   13.586 1.00 15.87  ? 99  MET   A O   1 
ATOM   757  C  CB  . MET   A 1 93  ? 6.467  6.578   10.859 1.00 15.43  ? 99  MET   A CB  1 
ATOM   758  C  CG  . MET   A 1 93  ? 7.079  6.673   9.477  1.00 16.13  ? 99  MET   A CG  1 
ATOM   759  S  SD  . MET   A 1 93  ? 8.200  5.315   9.034  1.00 19.60  ? 99  MET   A SD  1 
ATOM   760  C  CE  . MET   A 1 93  ? 9.533  5.627   10.279 1.00 20.17  ? 99  MET   A CE  1 
ATOM   761  N  N   . LEU   A 1 94  ? 3.817  7.476   12.741 1.00 14.59  ? 100 LEU   A N   1 
ATOM   762  C  CA  . LEU   A 1 94  ? 3.223  7.335   14.066 1.00 15.28  ? 100 LEU   A CA  1 
ATOM   763  C  C   . LEU   A 1 94  ? 2.743  5.898   14.330 1.00 14.76  ? 100 LEU   A C   1 
ATOM   764  O  O   . LEU   A 1 94  ? 2.275  5.219   13.401 1.00 16.31  ? 100 LEU   A O   1 
ATOM   765  C  CB  . LEU   A 1 94  ? 2.000  8.302   14.235 1.00 17.95  ? 100 LEU   A CB  1 
ATOM   766  C  CG  . LEU   A 1 94  ? 2.305  9.771   14.244 1.00 22.92  ? 100 LEU   A CG  1 
ATOM   767  C  CD1 . LEU   A 1 94  ? 1.013  10.600  14.490 1.00 25.04  ? 100 LEU   A CD1 1 
ATOM   768  C  CD2 . LEU   A 1 94  ? 3.302  10.158  15.339 1.00 26.04  ? 100 LEU   A CD2 1 
ATOM   769  N  N   . ALA   A 1 95  ? 2.792  5.498   15.590 1.00 14.87  ? 101 ALA   A N   1 
ATOM   770  C  CA  . ALA   A 1 95  ? 2.232  4.211   16.036 1.00 14.49  ? 101 ALA   A CA  1 
ATOM   771  C  C   . ALA   A 1 95  ? 1.621  4.420   17.430 1.00 14.63  ? 101 ALA   A C   1 
ATOM   772  O  O   . ALA   A 1 95  ? 1.914  5.417   18.125 1.00 14.87  ? 101 ALA   A O   1 
ATOM   773  C  CB  . ALA   A 1 95  ? 3.341  3.141   16.156 1.00 14.01  ? 101 ALA   A CB  1 
ATOM   774  N  N   . VAL   A 1 96  ? 0.810  3.445   17.852 1.00 13.20  ? 102 VAL   A N   1 
ATOM   775  C  CA  . VAL   A 1 96  ? 0.306  3.433   19.203 1.00 12.82  ? 102 VAL   A CA  1 
ATOM   776  C  C   . VAL   A 1 96  ? 1.331  2.693   20.104 1.00 13.74  ? 102 VAL   A C   1 
ATOM   777  O  O   . VAL   A 1 96  ? 1.643  1.546   19.866 1.00 15.39  ? 102 VAL   A O   1 
ATOM   778  C  CB  . VAL   A 1 96  ? -1.070 2.734   19.228 1.00 13.73  ? 102 VAL   A CB  1 
ATOM   779  C  CG1 . VAL   A 1 96  ? -1.600 2.591   20.669 1.00 15.66  ? 102 VAL   A CG1 1 
ATOM   780  C  CG2 . VAL   A 1 96  ? -2.065 3.514   18.354 1.00 15.23  ? 102 VAL   A CG2 1 
ATOM   781  N  N   . GLY   A 1 97  ? 1.821  3.443   21.096 1.00 14.41  ? 103 GLY   A N   1 
ATOM   782  C  CA  . GLY   A 1 97  ? 2.817  2.880   22.028 1.00 15.27  ? 103 GLY   A CA  1 
ATOM   783  C  C   . GLY   A 1 97  ? 3.309  3.942   22.971 1.00 16.13  ? 103 GLY   A C   1 
ATOM   784  O  O   . GLY   A 1 97  ? 3.022  5.115   22.858 1.00 18.80  ? 103 GLY   A O   1 
ATOM   785  N  N   . HIS   A 1 98  ? 3.856  3.566   24.203 1.00 17.02  ? 104 HIS   A N   1 
ATOM   786  C  CA  . HIS   A 1 98  ? 4.477  4.532   25.194 1.00 18.29  ? 104 HIS   A CA  1 
ATOM   787  C  C   . HIS   A 1 98  ? 5.698  5.346   24.716 1.00 17.20  ? 104 HIS   A C   1 
ATOM   788  O  O   . HIS   A 1 98  ? 6.591  4.600   24.107 1.00 17.13  ? 104 HIS   A O   1 
ATOM   789  C  CB  . HIS   A 1 98  ? 4.778  3.674   26.516 1.00 18.52  ? 104 HIS   A CB  1 
ATOM   790  C  CG  . HIS   A 1 98  ? 5.151  4.587   27.606 1.00 19.22  ? 104 HIS   A CG  1 
ATOM   791  N  ND1 . HIS   A 1 98  ? 4.288  5.536   28.079 1.00 20.17  ? 104 HIS   A ND1 1 
ATOM   792  C  CD2 . HIS   A 1 98  ? 6.307  4.731   28.260 1.00 21.84  ? 104 HIS   A CD2 1 
ATOM   793  C  CE1 . HIS   A 1 98  ? 4.887  6.232   29.009 1.00 22.12  ? 104 HIS   A CE1 1 
ATOM   794  N  NE2 . HIS   A 1 98  ? 6.126  5.749   29.131 1.00 22.80  ? 104 HIS   A NE2 1 
ATOM   795  N  N   . SER   A 1 99  ? 5.953  6.637   25.046 1.00 17.64  ? 105 SER   A N   1 
ATOM   796  C  CA  . SER   A 1 99  ? 7.238  7.301   24.797 1.00 19.28  ? 105 SER   A CA  1 
ATOM   797  C  C   . SER   A 1 99  ? 7.476  8.478   25.850 1.00 22.13  ? 105 SER   A C   1 
ATOM   798  O  O   . SER   A 1 99  ? 6.476  9.170   26.138 1.00 24.37  ? 105 SER   A O   1 
ATOM   799  C  CB  . SER   A 1 99  ? 7.337  7.558   23.278 1.00 21.50  ? 105 SER   A CB  1 
ATOM   800  O  OG  . SER   A 1 99  ? 6.103  8.064   22.800 1.00 30.85  ? 105 SER   A OG  1 
ATOM   801  N  N   . GLU   A 1 100 ? 8.717  8.717   26.342 1.00 19.17  ? 106 GLU   A N   1 
ATOM   802  C  CA  . GLU   A 1 100 ? 9.007  9.831   27.286 1.00 20.00  ? 106 GLU   A CA  1 
ATOM   803  C  C   . GLU   A 1 100 ? 10.357 10.326  26.848 1.00 22.52  ? 106 GLU   A C   1 
ATOM   804  O  O   . GLU   A 1 100 ? 11.012 9.577   26.181 1.00 21.08  ? 106 GLU   A O   1 
ATOM   805  C  CB  . GLU   A 1 100 ? 9.138  9.423   28.751 1.00 21.16  ? 106 GLU   A CB  1 
ATOM   806  C  CG  . GLU   A 1 100 ? 8.415  8.129   29.162 1.00 20.92  ? 106 GLU   A CG  1 
ATOM   807  C  CD  . GLU   A 1 100 ? 8.169  7.790   30.638 1.00 23.09  ? 106 GLU   A CD  1 
ATOM   808  O  OE1 . GLU   A 1 100 ? 8.777  8.410   31.523 1.00 29.83  ? 106 GLU   A OE1 1 
ATOM   809  O  OE2 . GLU   A 1 100 ? 7.427  6.854   30.884 1.00 24.13  ? 106 GLU   A OE2 1 
ATOM   810  N  N   . PRO   A 1 101 ? 10.690 11.619  27.242 1.00 24.24  ? 107 PRO   A N   1 
ATOM   811  C  CA  . PRO   A 1 101 ? 11.842 12.180  26.673 1.00 26.31  ? 107 PRO   A CA  1 
ATOM   812  C  C   . PRO   A 1 101 ? 12.484 11.026  27.374 1.00 28.61  ? 107 PRO   A C   1 
ATOM   813  O  O   . PRO   A 1 101 ? 12.045 10.491  28.532 1.00 33.46  ? 107 PRO   A O   1 
ATOM   814  C  CB  . PRO   A 1 101 ? 12.101 13.458  27.446 1.00 25.49  ? 107 PRO   A CB  1 
ATOM   815  C  CG  . PRO   A 1 101 ? 10.722 13.815  27.975 1.00 26.55  ? 107 PRO   A CG  1 
ATOM   816  C  CD  . PRO   A 1 101 ? 10.002 12.504  28.181 1.00 24.76  ? 107 PRO   A CD  1 
ATOM   817  N  N   . GLY   A 1 102 ? 13.661 10.792  26.940 1.00 20.24  ? 108 GLY   A N   1 
ATOM   818  C  CA  . GLY   A 1 102 ? 14.307 9.603   27.432 1.00 19.16  ? 108 GLY   A CA  1 
ATOM   819  C  C   . GLY   A 1 102 ? 14.180 8.580   26.318 1.00 15.96  ? 108 GLY   A C   1 
ATOM   820  O  O   . GLY   A 1 102 ? 15.159 7.961   26.055 1.00 16.74  ? 108 GLY   A O   1 
ATOM   821  N  N   . ASP   A 1 103 ? 12.970 8.403   25.765 1.00 14.70  ? 109 ASP   A N   1 
ATOM   822  C  CA  . ASP   A 1 103 ? 12.780 7.298   24.753 1.00 13.66  ? 109 ASP   A CA  1 
ATOM   823  C  C   . ASP   A 1 103 ? 13.341 7.685   23.352 1.00 13.63  ? 109 ASP   A C   1 
ATOM   824  O  O   . ASP   A 1 103 ? 13.903 6.780   22.667 1.00 13.26  ? 109 ASP   A O   1 
ATOM   825  C  CB  . ASP   A 1 103 ? 11.337 6.812   24.724 1.00 13.62  ? 109 ASP   A CB  1 
ATOM   826  C  CG  . ASP   A 1 103 ? 10.984 5.908   25.877 1.00 14.07  ? 109 ASP   A CG  1 
ATOM   827  O  OD1 . ASP   A 1 103 ? 11.931 5.248   26.366 1.00 14.77  ? 109 ASP   A OD1 1 
ATOM   828  O  OD2 . ASP   A 1 103 ? 9.756  5.831   26.224 1.00 14.63  ? 109 ASP   A OD2 1 
ATOM   829  N  N   . CYS   A 1 104 ? 13.279 8.969   22.951 1.00 14.26  ? 110 CYS   A N   1 
ATOM   830  C  CA  . CYS   A 1 104 ? 13.916 9.322   21.625 1.00 13.84  ? 110 CYS   A CA  1 
ATOM   831  C  C   . CYS   A 1 104 ? 15.261 8.496   21.474 1.00 13.50  ? 110 CYS   A C   1 
ATOM   832  O  O   . CYS   A 1 104 ? 15.945 8.340   22.510 1.00 14.18  ? 110 CYS   A O   1 
ATOM   833  C  CB  . CYS   A 1 104 ? 13.814 10.877  21.542 1.00 15.07  ? 110 CYS   A CB  1 
ATOM   834  S  SG  . CYS   A 1 104 ? 12.287 11.480  20.796 1.00 17.87  ? 110 CYS   A SG  1 
ATOM   835  N  N   . GLY   A 1 105 ? 15.616 7.900   20.275 1.00 11.56  ? 111 GLY   A N   1 
ATOM   836  C  CA  . GLY   A 1 105 ? 16.899 7.160   20.014 1.00 11.99  ? 111 GLY   A CA  1 
ATOM   837  C  C   . GLY   A 1 105 ? 16.696 5.650   19.833 1.00 10.94  ? 111 GLY   A C   1 
ATOM   838  O  O   . GLY   A 1 105 ? 17.524 4.989   19.287 1.00 11.85  ? 111 GLY   A O   1 
ATOM   839  N  N   . GLY   A 1 106 ? 15.604 5.188   20.433 1.00 10.94  ? 112 GLY   A N   1 
ATOM   840  C  CA  . GLY   A 1 106 ? 15.297 3.761   20.315 1.00 10.86  ? 112 GLY   A CA  1 
ATOM   841  C  C   . GLY   A 1 106 ? 15.058 3.356   18.860 1.00 9.80   ? 112 GLY   A C   1 
ATOM   842  O  O   . GLY   A 1 106 ? 14.379 4.091   18.122 1.00 10.17  ? 112 GLY   A O   1 
ATOM   843  N  N   . ILE   A 1 107 ? 15.536 2.201   18.440 1.00 10.22  ? 113 ILE   A N   1 
ATOM   844  C  CA  . ILE   A 1 107 ? 15.388 1.799   17.035 1.00 9.35   ? 113 ILE   A CA  1 
ATOM   845  C  C   . ILE   A 1 107 ? 14.037 1.152   16.761 1.00 9.11   ? 113 ILE   A C   1 
ATOM   846  O  O   . ILE   A 1 107 ? 13.556 0.308   17.552 1.00 9.76   ? 113 ILE   A O   1 
ATOM   847  C  CB  . ILE   A 1 107 ? 16.524 0.820   16.676 1.00 10.54  ? 113 ILE   A CB  1 
ATOM   848  C  CG1 . ILE   A 1 107 ? 17.820 1.672   16.405 1.00 12.26  ? 113 ILE   A CG1 1 
ATOM   849  C  CG2 . ILE   A 1 107 ? 16.233 -0.084  15.442 1.00 11.16  ? 113 ILE   A CG2 1 
ATOM   850  C  CD1 . ILE   A 1 107 ? 19.097 0.835   16.193 1.00 14.68  ? 113 ILE   A CD1 1 
ATOM   851  N  N   . LEU   A 1 108 ? 13.460 1.503   15.629 1.00 8.75   ? 114 LEU   A N   1 
ATOM   852  C  CA  . LEU   A 1 108 ? 12.351 0.782   14.985 1.00 9.06   ? 114 LEU   A CA  1 
ATOM   853  C  C   . LEU   A 1 108 ? 12.951 -0.031  13.844 1.00 8.89   ? 114 LEU   A C   1 
ATOM   854  O  O   . LEU   A 1 108 ? 13.717 0.509   13.030 1.00 10.03  ? 114 LEU   A O   1 
ATOM   855  C  CB  . LEU   A 1 108 ? 11.380 1.831   14.390 1.00 9.50   ? 114 LEU   A CB  1 
ATOM   856  C  CG  . LEU   A 1 108 ? 10.241 1.226   13.528 1.00 10.14  ? 114 LEU   A CG  1 
ATOM   857  C  CD1 . LEU   A 1 108 ? 9.243  0.396   14.357 1.00 12.24  ? 114 LEU   A CD1 1 
ATOM   858  C  CD2 . LEU   A 1 108 ? 9.442  2.352   12.811 1.00 12.89  ? 114 LEU   A CD2 1 
ATOM   859  N  N   . ARG   A 1 109 ? 12.639 -1.321  13.805 1.00 9.67   ? 115 ARG   A N   1 
ATOM   860  C  CA  . ARG   A 1 109 ? 13.187 -2.226  12.759 1.00 10.06  ? 115 ARG   A CA  1 
ATOM   861  C  C   . ARG   A 1 109 ? 12.089 -3.081  12.184 1.00 11.02  ? 115 ARG   A C   1 
ATOM   862  O  O   . ARG   A 1 109 ? 11.094 -3.407  12.853 1.00 11.03  ? 115 ARG   A O   1 
ATOM   863  C  CB  . ARG   A 1 109 ? 14.311 -3.094  13.332 1.00 11.19  ? 115 ARG   A CB  1 
ATOM   864  C  CG  . ARG   A 1 109 ? 13.844 -4.072  14.427 1.00 11.69  ? 115 ARG   A CG  1 
ATOM   865  C  CD  . ARG   A 1 109 ? 15.076 -4.791  14.995 1.00 13.78  ? 115 ARG   A CD  1 
ATOM   866  N  NE  . ARG   A 1 109 ? 15.868 -3.936  15.866 1.00 14.84  ? 115 ARG   A NE  1 
ATOM   867  C  CZ  . ARG   A 1 109 ? 17.179 -3.740  15.772 1.00 13.68  ? 115 ARG   A CZ  1 
ATOM   868  N  NH1 . ARG   A 1 109 ? 17.859 -4.156  14.689 1.00 16.03  ? 115 ARG   A NH1 1 
ATOM   869  N  NH2 . ARG   A 1 109 ? 17.811 -3.021  16.685 1.00 14.97  ? 115 ARG   A NH2 1 
ATOM   870  N  N   . CYS   A 1 110 ? 12.269 -3.517  10.934 1.00 14.02  ? 116 CYS   A N   1 
ATOM   871  C  CA  . CYS   A 1 110 ? 11.294 -4.396  10.237 1.00 16.53  ? 116 CYS   A CA  1 
ATOM   872  C  C   . CYS   A 1 110 ? 12.111 -5.584  9.792  1.00 19.06  ? 116 CYS   A C   1 
ATOM   873  O  O   . CYS   A 1 110 ? 13.307 -5.767  10.122 1.00 18.36  ? 116 CYS   A O   1 
ATOM   874  C  CB  . CYS   A 1 110 ? 10.651 -3.681  9.040  1.00 15.75  ? 116 CYS   A CB  1 
ATOM   875  S  SG  . CYS   A 1 110 ? 11.831 -3.329  7.720  1.00 16.30  ? 116 CYS   A SG  1 
ATOM   876  N  N   . GLN   A 1 111 ? 11.452 -6.456  8.986  1.00 21.13  ? 117 GLN   A N   1 
ATOM   877  C  CA  . GLN   A 1 111 ? 12.126 -7.610  8.430  1.00 22.71  ? 117 GLN   A CA  1 
ATOM   878  C  C   . GLN   A 1 111 ? 13.364 -7.265  7.564  1.00 24.10  ? 117 GLN   A C   1 
ATOM   879  O  O   . GLN   A 1 111 ? 14.267 -8.100  7.427  1.00 27.94  ? 117 GLN   A O   1 
ATOM   880  C  CB  . GLN   A 1 111 ? 11.127 -8.507  7.652  1.00 25.15  ? 117 GLN   A CB  1 
ATOM   881  C  CG  . GLN   A 1 111 ? 10.757 -7.911  6.309  1.00 28.78  ? 117 GLN   A CG  1 
ATOM   882  C  CD  . GLN   A 1 111 ? 9.834  -8.845  5.557  1.00 35.52  ? 117 GLN   A CD  1 
ATOM   883  O  OE1 . GLN   A 1 111 ? 8.612  -8.772  5.685  1.00 38.07  ? 117 GLN   A OE1 1 
ATOM   884  N  NE2 . GLN   A 1 111 ? 10.425 -9.738  4.766  1.00 36.13  ? 117 GLN   A NE2 1 
ATOM   885  N  N   . HIS   A 1 112 ? 13.452 -6.050  7.027  1.00 19.43  ? 118 HIS   A N   1 
ATOM   886  C  CA  . HIS   A 1 112 ? 14.568 -5.665  6.120  1.00 20.19  ? 118 HIS   A CA  1 
ATOM   887  C  C   . HIS   A 1 112 ? 15.761 -4.994  6.862  1.00 20.10  ? 118 HIS   A C   1 
ATOM   888  O  O   . HIS   A 1 112 ? 16.801 -4.738  6.236  1.00 23.55  ? 118 HIS   A O   1 
ATOM   889  C  CB  . HIS   A 1 112 ? 14.017 -4.726  5.037  1.00 21.19  ? 118 HIS   A CB  1 
ATOM   890  C  CG  . HIS   A 1 112 ? 12.888 -5.351  4.245  1.00 22.74  ? 118 HIS   A CG  1 
ATOM   891  N  ND1 . HIS   A 1 112 ? 11.560 -4.949  4.390  1.00 19.77  ? 118 HIS   A ND1 1 
ATOM   892  C  CD2 . HIS   A 1 112 ? 12.933 -6.264  3.230  1.00 23.30  ? 118 HIS   A CD2 1 
ATOM   893  C  CE1 . HIS   A 1 112 ? 10.849 -5.716  3.572  1.00 24.66  ? 118 HIS   A CE1 1 
ATOM   894  N  NE2 . HIS   A 1 112 ? 11.646 -6.499  2.841  1.00 27.87  ? 118 HIS   A NE2 1 
ATOM   895  N  N   . GLY   A 1 113 ? 15.581 -4.537  8.133  1.00 17.38  ? 119 GLY   A N   1 
ATOM   896  C  CA  . GLY   A 1 113 ? 16.655 -3.829  8.833  1.00 16.27  ? 119 GLY   A CA  1 
ATOM   897  C  C   . GLY   A 1 113 ? 16.090 -2.662  9.638  1.00 14.41  ? 119 GLY   A C   1 
ATOM   898  O  O   . GLY   A 1 113 ? 14.892 -2.626  9.979  1.00 14.53  ? 119 GLY   A O   1 
ATOM   899  N  N   . VAL   A 1 114 ? 16.956 -1.666  9.916  1.00 13.10  ? 120 VAL   A N   1 
ATOM   900  C  CA  . VAL   A 1 114 ? 16.530 -0.489  10.696 1.00 13.08  ? 120 VAL   A CA  1 
ATOM   901  C  C   . VAL   A 1 114 ? 15.680 0.458   9.871  1.00 10.80  ? 120 VAL   A C   1 
ATOM   902  O  O   . VAL   A 1 114 ? 16.087 0.817   8.723  1.00 12.57  ? 120 VAL   A O   1 
ATOM   903  C  CB  . VAL   A 1 114 ? 17.772 0.237   11.269 1.00 11.61  ? 120 VAL   A CB  1 
ATOM   904  C  CG1 . VAL   A 1 114 ? 17.352 1.551   11.934 1.00 13.30  ? 120 VAL   A CG1 1 
ATOM   905  C  CG2 . VAL   A 1 114 ? 18.567 -0.656  12.210 1.00 13.43  ? 120 VAL   A CG2 1 
ATOM   906  N  N   . VAL   A 1 115 ? 14.550 0.868   10.367 1.00 10.78  ? 121 VAL   A N   1 
ATOM   907  C  CA  . VAL   A 1 115 ? 13.614 1.757   9.722  1.00 11.22  ? 121 VAL   A CA  1 
ATOM   908  C  C   . VAL   A 1 115 ? 13.771 3.180   10.145 1.00 11.47  ? 121 VAL   A C   1 
ATOM   909  O  O   . VAL   A 1 115 ? 13.637 4.118   9.360  1.00 12.51  ? 121 VAL   A O   1 
ATOM   910  C  CB  . VAL   A 1 115 ? 12.152 1.291   10.004 1.00 12.60  ? 121 VAL   A CB  1 
ATOM   911  C  CG1 . VAL   A 1 115 ? 11.095 2.303   9.498  1.00 14.35  ? 121 VAL   A CG1 1 
ATOM   912  C  CG2 . VAL   A 1 115 ? 11.891 -0.097  9.439  1.00 14.44  ? 121 VAL   A CG2 1 
ATOM   913  N  N   . GLY   A 1 116 ? 13.991 3.411   11.455 1.00 11.12  ? 122 GLY   A N   1 
ATOM   914  C  CA  . GLY   A 1 116 ? 14.102 4.780   11.981 1.00 11.52  ? 122 GLY   A CA  1 
ATOM   915  C  C   . GLY   A 1 116 ? 14.335 4.779   13.476 1.00 9.96   ? 122 GLY   A C   1 
ATOM   916  O  O   . GLY   A 1 116 ? 14.647 3.705   14.045 1.00 10.34  ? 122 GLY   A O   1 
ATOM   917  N  N   . ILE   A 1 117 ? 14.242 5.943   14.093 1.00 10.49  ? 123 ILE   A N   1 
ATOM   918  C  CA  . ILE   A 1 117 ? 14.454 6.063   15.542 1.00 9.97   ? 123 ILE   A CA  1 
ATOM   919  C  C   . ILE   A 1 117 ? 13.333 6.830   16.196 1.00 10.34  ? 123 ILE   A C   1 
ATOM   920  O  O   . ILE   A 1 117 ? 12.741 7.735   15.546 1.00 11.60  ? 123 ILE   A O   1 
ATOM   921  C  CB  . ILE   A 1 117 ? 15.810 6.739   15.894 1.00 10.85  ? 123 ILE   A CB  1 
ATOM   922  C  CG1 . ILE   A 1 117 ? 15.979 8.086   15.171 1.00 12.94  ? 123 ILE   A CG1 1 
ATOM   923  C  CG2 . ILE   A 1 117 ? 16.953 5.763   15.690 1.00 12.40  ? 123 ILE   A CG2 1 
ATOM   924  C  CD1 . ILE   A 1 117 ? 17.262 8.884   15.690 1.00 14.13  ? 123 ILE   A CD1 1 
ATOM   925  N  N   . VAL   A 1 118 ? 13.097 6.616   17.483 1.00 10.16  ? 124 VAL   A N   1 
ATOM   926  C  CA  . VAL   A 1 118 ? 12.027 7.336   18.245 1.00 11.13  ? 124 VAL   A CA  1 
ATOM   927  C  C   . VAL   A 1 118 ? 12.408 8.845   18.236 1.00 11.79  ? 124 VAL   A C   1 
ATOM   928  O  O   . VAL   A 1 118 ? 13.570 9.132   18.341 1.00 11.58  ? 124 VAL   A O   1 
ATOM   929  C  CB  . VAL   A 1 118 ? 11.816 6.784   19.647 1.00 11.24  ? 124 VAL   A CB  1 
ATOM   930  C  CG1 . VAL   A 1 118 ? 10.881 7.699   20.442 1.00 12.22  ? 124 VAL   A CG1 1 
ATOM   931  C  CG2 . VAL   A 1 118 ? 11.348 5.333   19.672 1.00 12.14  ? 124 VAL   A CG2 1 
ATOM   932  N  N   . SER   A 1 119 ? 11.430 9.787   18.197 1.00 13.45  ? 125 SER   A N   1 
ATOM   933  C  CA  . SER   A 1 119 ? 11.476 11.246  17.844 1.00 14.88  ? 125 SER   A CA  1 
ATOM   934  C  C   . SER   A 1 119 ? 10.108 11.796  18.341 1.00 16.66  ? 125 SER   A C   1 
ATOM   935  O  O   . SER   A 1 119 ? 10.032 12.917  18.584 1.00 18.63  ? 125 SER   A O   1 
ATOM   936  C  CB  . SER   A 1 119 ? 11.606 11.434  16.333 1.00 15.42  ? 125 SER   A CB  1 
ATOM   937  O  OG  . SER   A 1 119 ? 11.638 12.816  16.011 1.00 17.72  ? 125 SER   A OG  1 
ATOM   938  N  N   . THR   A 1 120 ? 8.963  11.024  18.327 1.00 16.54  ? 126 THR   A N   1 
ATOM   939  C  CA  . THR   A 1 120 ? 7.698  11.604  18.931 1.00 17.73  ? 126 THR   A CA  1 
ATOM   940  C  C   . THR   A 1 120 ? 6.797  10.616  19.666 1.00 18.85  ? 126 THR   A C   1 
ATOM   941  O  O   . THR   A 1 120 ? 7.130  9.458   19.775 1.00 17.48  ? 126 THR   A O   1 
ATOM   942  C  CB  . THR   A 1 120 ? 6.805  12.420  18.012 1.00 19.97  ? 126 THR   A CB  1 
ATOM   943  O  OG1 . THR   A 1 120 ? 6.058  11.522  17.184 1.00 20.39  ? 126 THR   A OG1 1 
ATOM   944  C  CG2 . THR   A 1 120 ? 7.546  13.460  17.195 1.00 20.09  ? 126 THR   A CG2 1 
ATOM   945  N  N   . GLY   A 1 121 ? 5.850  11.184  20.376 1.00 20.98  ? 127 GLY   A N   1 
ATOM   946  C  CA  . GLY   A 1 121 ? 4.974  10.341  21.190 1.00 22.81  ? 127 GLY   A CA  1 
ATOM   947  C  C   . GLY   A 1 121 ? 4.276  11.022  22.383 1.00 25.92  ? 127 GLY   A C   1 
ATOM   948  O  O   . GLY   A 1 121 ? 4.389  12.241  22.615 1.00 28.38  ? 127 GLY   A O   1 
ATOM   949  N  N   . GLY   A 1 122 ? 3.542  10.227  23.157 1.00 27.56  ? 128 GLY   A N   1 
ATOM   950  C  CA  . GLY   A 1 122 ? 2.742  10.785  24.267 1.00 27.99  ? 128 GLY   A CA  1 
ATOM   951  C  C   . GLY   A 1 122 ? 1.303  10.399  24.040 1.00 30.19  ? 128 GLY   A C   1 
ATOM   952  O  O   . GLY   A 1 122 ? 0.950  10.184  22.941 1.00 30.79  ? 128 GLY   A O   1 
ATOM   953  N  N   . ASN   A 1 123 ? 0.575  10.325  25.117 1.00 29.74  ? 129 ASN   A N   1 
ATOM   954  C  CA  . ASN   A 1 123 ? -0.837 9.830   25.117 1.00 31.09  ? 129 ASN   A CA  1 
ATOM   955  C  C   . ASN   A 1 123 ? -1.061 8.500   24.371 1.00 28.53  ? 129 ASN   A C   1 
ATOM   956  O  O   . ASN   A 1 123 ? -2.059 8.417   23.698 1.00 28.13  ? 129 ASN   A O   1 
ATOM   957  C  CB  . ASN   A 1 123 ? -1.877 10.916  24.774 1.00 34.48  ? 129 ASN   A CB  1 
ATOM   958  C  CG  . ASN   A 1 123 ? -1.706 12.213  25.529 1.00 38.97  ? 129 ASN   A CG  1 
ATOM   959  O  OD1 . ASN   A 1 123 ? -2.022 12.259  26.711 1.00 42.29  ? 129 ASN   A OD1 1 
ATOM   960  N  ND2 . ASN   A 1 123 ? -1.308 13.268  24.830 1.00 38.87  ? 129 ASN   A ND2 1 
ATOM   961  N  N   . GLY   A 1 124 ? -0.069 7.607   24.433 1.00 24.85  ? 130 GLY   A N   1 
ATOM   962  C  CA  . GLY   A 1 124 ? -0.204 6.309   23.755 1.00 22.19  ? 130 GLY   A CA  1 
ATOM   963  C  C   . GLY   A 1 124 ? 0.294  6.519   22.359 1.00 17.61  ? 130 GLY   A C   1 
ATOM   964  O  O   . GLY   A 1 124 ? 0.004  5.527   21.609 1.00 19.29  ? 130 GLY   A O   1 
ATOM   965  N  N   . LEU   A 1 125 ? 1.038  7.672   22.156 1.00 17.86  ? 131 LEU   A N   1 
ATOM   966  C  CA  . LEU   A 1 125 ? 1.736  7.848   20.818 1.00 17.95  ? 131 LEU   A CA  1 
ATOM   967  C  C   . LEU   A 1 125 ? 3.256  7.727   20.871 1.00 18.55  ? 131 LEU   A C   1 
ATOM   968  O  O   . LEU   A 1 125 ? 3.833  7.995   21.921 1.00 20.36  ? 131 LEU   A O   1 
ATOM   969  C  CB  . LEU   A 1 125 ? 1.224  8.959   19.883 1.00 19.64  ? 131 LEU   A CB  1 
ATOM   970  C  CG  . LEU   A 1 125 ? -0.293 8.988   19.650 1.00 21.48  ? 131 LEU   A CG  1 
ATOM   971  C  CD1 . LEU   A 1 125 ? -0.718 10.366  19.199 1.00 24.87  ? 131 LEU   A CD1 1 
ATOM   972  C  CD2 . LEU   A 1 125 ? -0.784 7.960   18.626 1.00 21.79  ? 131 LEU   A CD2 1 
ATOM   973  N  N   . VAL   A 1 126 ? 3.844  7.520   19.685 1.00 14.89  ? 132 VAL   A N   1 
ATOM   974  C  CA  . VAL   A 1 126 ? 5.313  7.246   19.580 1.00 13.98  ? 132 VAL   A CA  1 
ATOM   975  C  C   . VAL   A 1 126 ? 5.588  7.540   18.098 1.00 14.71  ? 132 VAL   A C   1 
ATOM   976  O  O   . VAL   A 1 126 ? 4.885  6.918   17.319 1.00 15.26  ? 132 VAL   A O   1 
ATOM   977  C  CB  . VAL   A 1 126 ? 5.724  5.819   20.020 1.00 13.62  ? 132 VAL   A CB  1 
ATOM   978  C  CG1 . VAL   A 1 126 ? 5.043  4.664   19.299 1.00 14.31  ? 132 VAL   A CG1 1 
ATOM   979  C  CG2 . VAL   A 1 126 ? 7.240  5.701   19.931 1.00 13.96  ? 132 VAL   A CG2 1 
ATOM   980  N  N   . GLY   A 1 127 ? 6.220  8.675   17.908 1.00 14.52  ? 133 GLY   A N   1 
ATOM   981  C  CA  . GLY   A 1 127 ? 6.627  9.050   16.547 1.00 14.18  ? 133 GLY   A CA  1 
ATOM   982  C  C   . GLY   A 1 127 ? 7.992  8.395   16.188 1.00 13.62  ? 133 GLY   A C   1 
ATOM   983  O  O   . GLY   A 1 127 ? 8.767  8.338   17.077 1.00 14.97  ? 133 GLY   A O   1 
ATOM   984  N  N   . PHE   A 1 128 ? 8.252  8.029   14.916 1.00 12.67  ? 134 PHE   A N   1 
ATOM   985  C  CA  . PHE   A 1 128 ? 9.580  7.496   14.387 1.00 12.08  ? 134 PHE   A CA  1 
ATOM   986  C  C   . PHE   A 1 128 ? 10.168 8.343   13.210 1.00 12.82  ? 134 PHE   A C   1 
ATOM   987  O  O   . PHE   A 1 128 ? 9.343  8.402   12.219 1.00 13.60  ? 134 PHE   A O   1 
ATOM   988  C  CB  . PHE   A 1 128 ? 9.462  6.016   14.011 1.00 12.17  ? 134 PHE   A CB  1 
ATOM   989  C  CG  . PHE   A 1 128 ? 8.944  5.104   15.114 1.00 11.42  ? 134 PHE   A CG  1 
ATOM   990  C  CD1 . PHE   A 1 128 ? 9.741  4.681   16.176 1.00 10.89  ? 134 PHE   A CD1 1 
ATOM   991  C  CD2 . PHE   A 1 128 ? 7.647  4.619   15.072 1.00 12.83  ? 134 PHE   A CD2 1 
ATOM   992  C  CE1 . PHE   A 1 128 ? 9.246  3.842   17.168 1.00 11.09  ? 134 PHE   A CE1 1 
ATOM   993  C  CE2 . PHE   A 1 128 ? 7.169  3.777   16.064 1.00 12.83  ? 134 PHE   A CE2 1 
ATOM   994  C  CZ  . PHE   A 1 128 ? 7.952  3.397   17.118 1.00 12.11  ? 134 PHE   A CZ  1 
ATOM   995  N  N   . ALA   A 1 129 ? 11.297 9.066   13.371 1.00 12.14  ? 135 ALA   A N   1 
ATOM   996  C  CA  . ALA   A 1 129 ? 12.054 9.764   12.274 1.00 12.78  ? 135 ALA   A CA  1 
ATOM   997  C  C   . ALA   A 1 129 ? 12.467 8.667   11.294 1.00 12.18  ? 135 ALA   A C   1 
ATOM   998  O  O   . ALA   A 1 129 ? 13.369 7.878   11.803 1.00 12.36  ? 135 ALA   A O   1 
ATOM   999  C  CB  . ALA   A 1 129 ? 13.270 10.518  12.895 1.00 13.34  ? 135 ALA   A CB  1 
ATOM   1000 N  N   . ASP   A 1 130 ? 11.905 8.522   10.062 1.00 12.81  ? 136 ASP   A N   1 
ATOM   1001 C  CA  . ASP   A 1 130 ? 12.318 7.541   9.069  1.00 13.70  ? 136 ASP   A CA  1 
ATOM   1002 C  C   . ASP   A 1 130 ? 13.721 7.842   8.547  1.00 12.75  ? 136 ASP   A C   1 
ATOM   1003 O  O   . ASP   A 1 130 ? 14.127 9.011   8.429  1.00 14.69  ? 136 ASP   A O   1 
ATOM   1004 C  CB  . ASP   A 1 130 ? 11.360 7.673   7.874  1.00 16.90  ? 136 ASP   A CB  1 
ATOM   1005 C  CG  . ASP   A 1 130 ? 11.610 6.690   6.787  1.00 19.17  ? 136 ASP   A CG  1 
ATOM   1006 O  OD1 . ASP   A 1 130 ? 11.644 5.454   7.068  1.00 19.93  ? 136 ASP   A OD1 1 
ATOM   1007 O  OD2 . ASP   A 1 130 ? 11.890 7.148   5.650  1.00 21.68  ? 136 ASP   A OD2 1 
ATOM   1008 N  N   . VAL   A 1 131 ? 14.451 6.767   8.250  1.00 12.24  ? 137 VAL   A N   1 
ATOM   1009 C  CA  . VAL   A 1 131 ? 15.771 6.891   7.586  1.00 12.42  ? 137 VAL   A CA  1 
ATOM   1010 C  C   . VAL   A 1 131 ? 15.866 6.076   6.300  1.00 13.15  ? 137 VAL   A C   1 
ATOM   1011 O  O   . VAL   A 1 131 ? 16.921 6.064   5.669  1.00 12.93  ? 137 VAL   A O   1 
ATOM   1012 C  CB  . VAL   A 1 131 ? 16.934 6.509   8.529  1.00 12.17  ? 137 VAL   A CB  1 
ATOM   1013 C  CG1 . VAL   A 1 131 ? 16.974 7.415   9.765  1.00 13.52  ? 137 VAL   A CG1 1 
ATOM   1014 C  CG2 . VAL   A 1 131 ? 16.955 5.039   8.933  1.00 12.56  ? 137 VAL   A CG2 1 
ATOM   1015 N  N   . ARG   A 1 132 ? 14.796 5.393   5.886  1.00 13.88  ? 138 ARG   A N   1 
ATOM   1016 C  CA  . ARG   A 1 132 ? 14.873 4.481   4.736  1.00 14.01  ? 138 ARG   A CA  1 
ATOM   1017 C  C   . ARG   A 1 132 ? 15.113 5.201   3.397  1.00 16.78  ? 138 ARG   A C   1 
ATOM   1018 O  O   . ARG   A 1 132 ? 15.584 4.549   2.442  1.00 17.32  ? 138 ARG   A O   1 
ATOM   1019 C  CB  . ARG   A 1 132 ? 13.595 3.643   4.637  1.00 14.81  ? 138 ARG   A CB  1 
ATOM   1020 C  CG  . ARG   A 1 132 ? 13.457 2.669   5.835  1.00 13.70  ? 138 ARG   A CG  1 
ATOM   1021 C  CD  . ARG   A 1 132 ? 12.130 1.942   5.713  1.00 16.25  ? 138 ARG   A CD  1 
ATOM   1022 N  NE  . ARG   A 1 132 ? 11.028 2.891   5.944  1.00 14.85  ? 138 ARG   A NE  1 
ATOM   1023 C  CZ  . ARG   A 1 132 ? 9.739  2.553   6.039  1.00 17.80  ? 138 ARG   A CZ  1 
ATOM   1024 N  NH1 . ARG   A 1 132 ? 9.354  1.330   5.756  1.00 17.28  ? 138 ARG   A NH1 1 
ATOM   1025 N  NH2 . ARG   A 1 132 ? 8.838  3.450   6.441  1.00 18.17  ? 138 ARG   A NH2 1 
ATOM   1026 N  N   . ASP   A 1 133 ? 14.788 6.512   3.301  1.00 15.87  ? 139 ASP   A N   1 
ATOM   1027 C  CA  . ASP   A 1 133 ? 15.057 7.239   2.072  1.00 17.77  ? 139 ASP   A CA  1 
ATOM   1028 C  C   . ASP   A 1 133 ? 16.499 7.739   1.980  1.00 16.74  ? 139 ASP   A C   1 
ATOM   1029 O  O   . ASP   A 1 133 ? 16.878 8.283   0.915  1.00 18.82  ? 139 ASP   A O   1 
ATOM   1030 C  CB  . ASP   A 1 133 ? 14.102 8.469   1.984  1.00 19.73  ? 139 ASP   A CB  1 
ATOM   1031 C  CG  . ASP   A 1 133 ? 14.338 9.507   3.063  1.00 23.33  ? 139 ASP   A CG  1 
ATOM   1032 O  OD1 . ASP   A 1 133 ? 14.532 9.118   4.246  1.00 21.58  ? 139 ASP   A OD1 1 
ATOM   1033 O  OD2 . ASP   A 1 133 ? 14.293 10.708  2.763  1.00 25.84  ? 139 ASP   A OD2 1 
ATOM   1034 N  N   . LEU   A 1 134 ? 17.306 7.640   3.042  1.00 15.28  ? 140 LEU   A N   1 
ATOM   1035 C  CA  . LEU   A 1 134 ? 18.691 8.174   3.058  1.00 14.66  ? 140 LEU   A CA  1 
ATOM   1036 C  C   . LEU   A 1 134 ? 19.621 7.135   2.488  1.00 15.39  ? 140 LEU   A C   1 
ATOM   1037 O  O   . LEU   A 1 134 ? 20.336 6.424   3.226  1.00 15.25  ? 140 LEU   A O   1 
ATOM   1038 C  CB  . LEU   A 1 134 ? 19.069 8.579   4.500  1.00 14.06  ? 140 LEU   A CB  1 
ATOM   1039 C  CG  . LEU   A 1 134 ? 18.138 9.635   5.186  1.00 16.02  ? 140 LEU   A CG  1 
ATOM   1040 C  CD1 . LEU   A 1 134 ? 18.514 9.828   6.663  1.00 16.95  ? 140 LEU   A CD1 1 
ATOM   1041 C  CD2 . LEU   A 1 134 ? 18.134 10.973  4.449  1.00 19.25  ? 140 LEU   A CD2 1 
ATOM   1042 N  N   . LEU   A 1 135 ? 19.616 7.017   1.133  1.00 15.39  ? 141 LEU   A N   1 
ATOM   1043 C  CA  . LEU   A 1 135 ? 20.355 5.906   0.507  1.00 16.82  ? 141 LEU   A CA  1 
ATOM   1044 C  C   . LEU   A 1 135 ? 21.849 5.980   0.671  1.00 16.37  ? 141 LEU   A C   1 
ATOM   1045 O  O   . LEU   A 1 135 ? 22.563 4.963   0.704  1.00 18.74  ? 141 LEU   A O   1 
ATOM   1046 C  CB  . LEU   A 1 135 ? 19.998 5.783   -1.008 1.00 18.76  ? 141 LEU   A CB  1 
ATOM   1047 C  CG  . LEU   A 1 135 ? 18.487 5.801   -1.307 1.00 19.79  ? 141 LEU   A CG  1 
ATOM   1048 C  CD1 . LEU   A 1 135 ? 18.263 5.472   -2.828 1.00 22.41  ? 141 LEU   A CD1 1 
ATOM   1049 C  CD2 . LEU   A 1 135 ? 17.684 4.804   -0.455 1.00 21.02  ? 141 LEU   A CD2 1 
ATOM   1050 N  N   . TRP   A 1 136 ? 22.349 7.212   0.837  1.00 15.09  ? 142 TRP   A N   1 
ATOM   1051 C  CA  . TRP   A 1 136 ? 23.768 7.463   1.015  1.00 15.92  ? 142 TRP   A CA  1 
ATOM   1052 C  C   . TRP   A 1 136 ? 24.331 6.872   2.310  1.00 16.37  ? 142 TRP   A C   1 
ATOM   1053 O  O   . TRP   A 1 136 ? 25.553 6.727   2.451  1.00 17.30  ? 142 TRP   A O   1 
ATOM   1054 C  CB  . TRP   A 1 136 ? 24.094 8.976   0.888  1.00 16.85  ? 142 TRP   A CB  1 
ATOM   1055 C  CG  . TRP   A 1 136 ? 23.284 9.809   1.841  1.00 15.10  ? 142 TRP   A CG  1 
ATOM   1056 C  CD1 . TRP   A 1 136 ? 22.162 10.512  1.547  1.00 15.91  ? 142 TRP   A CD1 1 
ATOM   1057 C  CD2 . TRP   A 1 136 ? 23.633 10.142  3.208  1.00 15.55  ? 142 TRP   A CD2 1 
ATOM   1058 N  NE1 . TRP   A 1 136 ? 21.708 11.176  2.693  1.00 17.45  ? 142 TRP   A NE1 1 
ATOM   1059 C  CE2 . TRP   A 1 136 ? 22.621 10.983  3.704  1.00 15.64  ? 142 TRP   A CE2 1 
ATOM   1060 C  CE3 . TRP   A 1 136 ? 24.696 9.812   4.052  1.00 15.53  ? 142 TRP   A CE3 1 
ATOM   1061 C  CZ2 . TRP   A 1 136 ? 22.648 11.497  5.028  1.00 16.87  ? 142 TRP   A CZ2 1 
ATOM   1062 C  CZ3 . TRP   A 1 136 ? 24.728 10.337  5.350  1.00 17.20  ? 142 TRP   A CZ3 1 
ATOM   1063 C  CH2 . TRP   A 1 136 ? 23.722 11.179  5.799  1.00 17.05  ? 142 TRP   A CH2 1 
ATOM   1064 N  N   . LEU   A 1 137 ? 23.463 6.534   3.296  1.00 14.99  ? 143 LEU   A N   1 
ATOM   1065 C  CA  . LEU   A 1 137 ? 23.971 5.866   4.512  1.00 16.97  ? 143 LEU   A CA  1 
ATOM   1066 C  C   . LEU   A 1 137 ? 24.684 4.558   4.200  1.00 18.90  ? 143 LEU   A C   1 
ATOM   1067 O  O   . LEU   A 1 137 ? 25.520 4.116   4.989  1.00 20.17  ? 143 LEU   A O   1 
ATOM   1068 C  CB  . LEU   A 1 137 ? 22.836 5.624   5.524  1.00 16.22  ? 143 LEU   A CB  1 
ATOM   1069 C  CG  . LEU   A 1 137 ? 22.293 6.875   6.214  1.00 15.17  ? 143 LEU   A CG  1 
ATOM   1070 C  CD1 . LEU   A 1 137 ? 21.052 6.520   7.003  1.00 17.18  ? 143 LEU   A CD1 1 
ATOM   1071 C  CD2 . LEU   A 1 137 ? 23.380 7.500   7.168  1.00 16.44  ? 143 LEU   A CD2 1 
ATOM   1072 N  N   . ASP   A 1 138 ? 24.349 3.927   3.029  1.00 21.65  ? 144 ASP   A N   1 
ATOM   1073 C  CA  . ASP   A 1 138 ? 24.920 2.620   2.631  1.00 24.33  ? 144 ASP   A CA  1 
ATOM   1074 C  C   . ASP   A 1 138 ? 26.247 2.706   1.907  1.00 29.52  ? 144 ASP   A C   1 
ATOM   1075 O  O   . ASP   A 1 138 ? 26.771 1.663   1.501  1.00 32.35  ? 144 ASP   A O   1 
ATOM   1076 C  CB  . ASP   A 1 138 ? 23.961 1.854   1.671  1.00 25.58  ? 144 ASP   A CB  1 
ATOM   1077 C  CG  . ASP   A 1 138 ? 22.584 1.580   2.203  1.00 27.50  ? 144 ASP   A CG  1 
ATOM   1078 O  OD1 . ASP   A 1 138 ? 22.409 1.611   3.441  1.00 30.74  ? 144 ASP   A OD1 1 
ATOM   1079 O  OD2 . ASP   A 1 138 ? 21.648 1.326   1.386  1.00 34.86  ? 144 ASP   A OD2 1 
ATOM   1080 N  N   . GLU   A 1 139 ? 26.785 3.906   1.672  1.00 30.91  ? 145 GLU   A N   1 
ATOM   1081 C  CA  . GLU   A 1 139 ? 28.024 4.053   0.884  1.00 35.03  ? 145 GLU   A CA  1 
ATOM   1082 C  C   . GLU   A 1 139 ? 29.015 5.058   1.495  1.00 38.33  ? 145 GLU   A C   1 
ATOM   1083 O  O   . GLU   A 1 139 ? 28.703 5.661   2.520  1.00 38.31  ? 145 GLU   A O   1 
ATOM   1084 C  CB  . GLU   A 1 139 ? 27.620 4.475   -0.544 1.00 39.05  ? 145 GLU   A CB  1 
ATOM   1085 C  CG  . GLU   A 1 139 ? 26.863 5.792   -0.560 1.00 46.51  ? 145 GLU   A CG  1 
ATOM   1086 C  CD  . GLU   A 1 139 ? 26.111 6.134   -1.831 1.00 54.74  ? 145 GLU   A CD  1 
ATOM   1087 O  OE1 . GLU   A 1 139 ? 25.967 7.345   -2.121 1.00 56.17  ? 145 GLU   A OE1 1 
ATOM   1088 O  OE2 . GLU   A 1 139 ? 25.659 5.199   -2.532 1.00 58.44  ? 145 GLU   A OE2 1 
ATOM   1089 N  N   . GLU   A 1 140 ? 30.191 5.251   0.835  1.00 41.04  ? 146 GLU   A N   1 
ATOM   1090 C  CA  . GLU   A 1 140 ? 31.308 6.180   1.129  1.00 44.16  ? 146 GLU   A CA  1 
ATOM   1091 C  C   . GLU   A 1 140 ? 32.323 5.570   2.073  1.00 45.95  ? 146 GLU   A C   1 
ATOM   1092 O  O   . GLU   A 1 140 ? 33.159 4.787   1.620  1.00 46.80  ? 146 GLU   A O   1 
ATOM   1093 C  CB  . GLU   A 1 140 ? 30.845 7.567   1.603  1.00 48.08  ? 146 GLU   A CB  1 
ATOM   1094 C  CG  . GLU   A 1 140 ? 31.952 8.542   1.979  1.00 55.28  ? 146 GLU   A CG  1 
ATOM   1095 C  CD  . GLU   A 1 140 ? 32.519 9.385   0.848  1.00 64.88  ? 146 GLU   A CD  1 
ATOM   1096 O  OE1 . GLU   A 1 140 ? 32.341 10.623  0.886  1.00 67.20  ? 146 GLU   A OE1 1 
ATOM   1097 O  OE2 . GLU   A 1 140 ? 33.145 8.812   -0.075 1.00 67.97  ? 146 GLU   A OE2 1 
ATOM   1098 N  N   . SER   B 1 1   ? 21.853 -21.182 7.631  1.00 17.75  ? 7   SER   C N   1 
ATOM   1099 C  CA  . SER   B 1 1   ? 20.713 -20.963 8.549  1.00 17.71  ? 7   SER   C CA  1 
ATOM   1100 C  C   . SER   B 1 1   ? 20.680 -22.089 9.629  1.00 17.80  ? 7   SER   C C   1 
ATOM   1101 O  O   . SER   B 1 1   ? 21.326 -23.137 9.473  1.00 19.03  ? 7   SER   C O   1 
ATOM   1102 C  CB  . SER   B 1 1   ? 19.413 -21.032 7.757  1.00 20.66  ? 7   SER   C CB  1 
ATOM   1103 O  OG  . SER   B 1 1   ? 19.295 -22.306 7.155  1.00 25.60  ? 7   SER   C OG  1 
ATOM   1104 N  N   . GLY   B 1 2   ? 19.903 -21.895 10.697 1.00 16.97  ? 8   GLY   C N   1 
ATOM   1105 C  CA  . GLY   B 1 2   ? 19.710 -22.902 11.733 1.00 16.58  ? 8   GLY   C CA  1 
ATOM   1106 C  C   . GLY   B 1 2   ? 19.418 -22.305 13.091 1.00 15.01  ? 8   GLY   C C   1 
ATOM   1107 O  O   . GLY   B 1 2   ? 19.822 -21.163 13.366 1.00 16.11  ? 8   GLY   C O   1 
ATOM   1108 N  N   . ALA   B 1 3   ? 18.751 -23.043 13.944 1.00 13.95  ? 9   ALA   C N   1 
ATOM   1109 C  CA  . ALA   B 1 3   ? 18.415 -22.565 15.284 1.00 14.41  ? 9   ALA   C CA  1 
ATOM   1110 C  C   . ALA   B 1 3   ? 18.533 -23.691 16.317 1.00 12.89  ? 9   ALA   C C   1 
ATOM   1111 O  O   . ALA   B 1 3   ? 18.595 -24.889 15.945 1.00 14.80  ? 9   ALA   C O   1 
ATOM   1112 C  CB  . ALA   B 1 3   ? 16.985 -21.998 15.285 1.00 16.46  ? 9   ALA   C CB  1 
ATOM   1113 N  N   . ILE   B 1 4   ? 18.535 -23.327 17.574 1.00 12.67  ? 10  ILE   C N   1 
ATOM   1114 C  CA  . ILE   B 1 4   ? 18.428 -24.252 18.700 1.00 14.46  ? 10  ILE   C CA  1 
ATOM   1115 C  C   . ILE   B 1 4   ? 17.033 -24.066 19.307 1.00 14.14  ? 10  ILE   C C   1 
ATOM   1116 O  O   . ILE   B 1 4   ? 16.600 -22.918 19.529 1.00 15.24  ? 10  ILE   C O   1 
ATOM   1117 C  CB  . ILE   B 1 4   ? 19.473 -23.953 19.787 1.00 13.01  ? 10  ILE   C CB  1 
ATOM   1118 C  CG1 . ILE   B 1 4   ? 20.910 -23.827 19.215 1.00 14.79  ? 10  ILE   C CG1 1 
ATOM   1119 C  CG2 . ILE   B 1 4   ? 19.411 -25.049 20.878 1.00 15.12  ? 10  ILE   C CG2 1 
ATOM   1120 C  CD1 . ILE   B 1 4   ? 21.867 -23.188 20.272 1.00 14.55  ? 10  ILE   C CD1 1 
ATOM   1121 N  N   . TYR   B 1 5   ? 16.325 -25.148 19.596 1.00 14.31  ? 11  TYR   C N   1 
ATOM   1122 C  CA  . TYR   B 1 5   ? 14.986 -25.114 20.179 1.00 15.40  ? 11  TYR   C CA  1 
ATOM   1123 C  C   . TYR   B 1 5   ? 15.036 -25.789 21.539 1.00 15.90  ? 11  TYR   C C   1 
ATOM   1124 O  O   . TYR   B 1 5   ? 15.129 -27.034 21.601 1.00 17.73  ? 11  TYR   C O   1 
ATOM   1125 C  CB  . TYR   B 1 5   ? 13.938 -25.839 19.258 1.00 16.43  ? 11  TYR   C CB  1 
ATOM   1126 C  CG  . TYR   B 1 5   ? 13.760 -25.076 17.952 1.00 15.72  ? 11  TYR   C CG  1 
ATOM   1127 C  CD1 . TYR   B 1 5   ? 12.932 -23.963 17.880 1.00 16.57  ? 11  TYR   C CD1 1 
ATOM   1128 C  CD2 . TYR   B 1 5   ? 14.478 -25.421 16.815 1.00 16.79  ? 11  TYR   C CD2 1 
ATOM   1129 C  CE1 . TYR   B 1 5   ? 12.812 -23.226 16.701 1.00 17.69  ? 11  TYR   C CE1 1 
ATOM   1130 C  CE2 . TYR   B 1 5   ? 14.395 -24.682 15.641 1.00 18.55  ? 11  TYR   C CE2 1 
ATOM   1131 C  CZ  . TYR   B 1 5   ? 13.541 -23.594 15.581 1.00 18.55  ? 11  TYR   C CZ  1 
ATOM   1132 O  OH  . TYR   B 1 5   ? 13.464 -22.851 14.413 1.00 21.04  ? 11  TYR   C OH  1 
ATOM   1133 N  N   . VAL   B 1 6   ? 15.086 -25.043 22.630 1.00 17.14  ? 12  VAL   C N   1 
ATOM   1134 C  CA  . VAL   B 1 6   ? 15.169 -25.585 24.006 1.00 17.64  ? 12  VAL   C CA  1 
ATOM   1135 C  C   . VAL   B 1 6   ? 14.017 -24.988 24.838 1.00 18.12  ? 12  VAL   C C   1 
ATOM   1136 O  O   . VAL   B 1 6   ? 13.815 -23.770 24.836 1.00 17.24  ? 12  VAL   C O   1 
ATOM   1137 C  CB  . VAL   B 1 6   ? 16.569 -25.303 24.625 1.00 18.67  ? 12  VAL   C CB  1 
ATOM   1138 C  CG1 . VAL   B 1 6   ? 16.950 -23.816 24.531 1.00 18.92  ? 12  VAL   C CG1 1 
ATOM   1139 C  CG2 . VAL   B 1 6   ? 16.622 -25.791 26.061 1.00 19.96  ? 12  VAL   C CG2 1 
ATOM   1140 N  N   . GLY   B 1 7   ? 13.200 -25.827 25.508 1.00 19.03  ? 13  GLY   C N   1 
ATOM   1141 C  CA  . GLY   B 1 7   ? 12.067 -25.310 26.267 1.00 19.53  ? 13  GLY   C CA  1 
ATOM   1142 C  C   . GLY   B 1 7   ? 11.140 -24.458 25.400 1.00 19.70  ? 13  GLY   C C   1 
ATOM   1143 O  O   . GLY   B 1 7   ? 10.860 -24.846 24.266 1.00 20.38  ? 13  GLY   C O   1 
ATOM   1144 N  N   . ASN   B 1 8   ? 10.783 -23.273 25.858 1.00 19.58  ? 14  ASN   C N   1 
ATOM   1145 C  CA  . ASN   B 1 8   ? 9.994  -22.340 25.024 1.00 20.07  ? 14  ASN   C CA  1 
ATOM   1146 C  C   . ASN   B 1 8   ? 10.873 -21.227 24.441 1.00 18.14  ? 14  ASN   C C   1 
ATOM   1147 O  O   . ASN   B 1 8   ? 10.416 -20.089 24.268 1.00 18.57  ? 14  ASN   C O   1 
ATOM   1148 C  CB  . ASN   B 1 8   ? 8.757  -21.766 25.754 1.00 22.67  ? 14  ASN   C CB  1 
ATOM   1149 C  CG  . ASN   B 1 8   ? 7.677  -22.813 25.906 1.00 29.47  ? 14  ASN   C CG  1 
ATOM   1150 O  OD1 . ASN   B 1 8   ? 6.825  -22.977 25.029 1.00 32.60  ? 14  ASN   C OD1 1 
ATOM   1151 N  ND2 . ASN   B 1 8   ? 7.762  -23.595 26.969 1.00 33.36  ? 14  ASN   C ND2 1 
ATOM   1152 N  N   . TYR   B 1 9   ? 12.102 -21.591 24.062 1.00 15.53  ? 15  TYR   C N   1 
ATOM   1153 C  CA  . TYR   B 1 9   ? 13.056 -20.660 23.467 1.00 16.00  ? 15  TYR   C CA  1 
ATOM   1154 C  C   . TYR   B 1 9   ? 13.542 -21.124 22.094 1.00 15.49  ? 15  TYR   C C   1 
ATOM   1155 O  O   . TYR   B 1 9   ? 13.760 -22.323 21.877 1.00 16.57  ? 15  TYR   C O   1 
ATOM   1156 C  CB  . TYR   B 1 9   ? 14.300 -20.467 24.386 1.00 17.00  ? 15  TYR   C CB  1 
ATOM   1157 C  CG  . TYR   B 1 9   ? 13.956 -19.941 25.775 1.00 18.24  ? 15  TYR   C CG  1 
ATOM   1158 C  CD1 . TYR   B 1 9   ? 13.364 -18.695 25.940 1.00 21.04  ? 15  TYR   C CD1 1 
ATOM   1159 C  CD2 . TYR   B 1 9   ? 14.248 -20.683 26.922 1.00 20.00  ? 15  TYR   C CD2 1 
ATOM   1160 C  CE1 . TYR   B 1 9   ? 13.042 -18.209 27.213 1.00 23.82  ? 15  TYR   C CE1 1 
ATOM   1161 C  CE2 . TYR   B 1 9   ? 13.960 -20.185 28.201 1.00 22.97  ? 15  TYR   C CE2 1 
ATOM   1162 C  CZ  . TYR   B 1 9   ? 13.380 -18.939 28.332 1.00 26.38  ? 15  TYR   C CZ  1 
ATOM   1163 O  OH  . TYR   B 1 9   ? 13.036 -18.400 29.564 1.00 31.85  ? 15  TYR   C OH  1 
ATOM   1164 N  N   . ARG   B 1 10  ? 13.813 -20.151 21.199 1.00 14.54  ? 16  ARG   C N   1 
ATOM   1165 C  CA  . ARG   B 1 10  ? 14.438 -20.365 19.891 1.00 13.99  ? 16  ARG   C CA  1 
ATOM   1166 C  C   . ARG   B 1 10  ? 15.703 -19.510 19.906 1.00 13.48  ? 16  ARG   C C   1 
ATOM   1167 O  O   . ARG   B 1 10  ? 15.609 -18.281 20.111 1.00 14.23  ? 16  ARG   C O   1 
ATOM   1168 C  CB  . ARG   B 1 10  ? 13.492 -19.910 18.747 1.00 15.50  ? 16  ARG   C CB  1 
ATOM   1169 C  CG  . ARG   B 1 10  ? 14.129 -19.771 17.355 1.00 15.74  ? 16  ARG   C CG  1 
ATOM   1170 C  CD  . ARG   B 1 10  ? 13.060 -19.443 16.310 1.00 16.56  ? 16  ARG   C CD  1 
ATOM   1171 N  NE  . ARG   B 1 10  ? 13.498 -18.503 15.268 1.00 16.66  ? 16  ARG   C NE  1 
ATOM   1172 C  CZ  . ARG   B 1 10  ? 14.030 -18.812 14.087 1.00 17.40  ? 16  ARG   C CZ  1 
ATOM   1173 N  NH1 . ARG   B 1 10  ? 14.302 -20.093 13.777 1.00 18.63  ? 16  ARG   C NH1 1 
ATOM   1174 N  NH2 . ARG   B 1 10  ? 14.393 -17.842 13.239 1.00 18.32  ? 16  ARG   C NH2 1 
ATOM   1175 N  N   . VAL   B 1 11  ? 16.878 -20.096 19.656 1.00 12.80  ? 17  VAL   C N   1 
ATOM   1176 C  CA  . VAL   B 1 11  ? 18.176 -19.383 19.653 1.00 11.98  ? 17  VAL   C CA  1 
ATOM   1177 C  C   . VAL   B 1 11  ? 18.661 -19.323 18.245 1.00 12.85  ? 17  VAL   C C   1 
ATOM   1178 O  O   . VAL   B 1 11  ? 18.821 -20.381 17.580 1.00 13.62  ? 17  VAL   C O   1 
ATOM   1179 C  CB  . VAL   B 1 11  ? 19.240 -20.108 20.531 1.00 13.07  ? 17  VAL   C CB  1 
ATOM   1180 C  CG1 . VAL   B 1 11  ? 20.474 -19.243 20.641 1.00 14.87  ? 17  VAL   C CG1 1 
ATOM   1181 C  CG2 . VAL   B 1 11  ? 18.686 -20.444 21.925 1.00 15.34  ? 17  VAL   C CG2 1 
ATOM   1182 N  N   . VAL   B 1 12  ? 18.896 -18.095 17.717 1.00 12.25  ? 18  VAL   C N   1 
ATOM   1183 C  CA  A VAL   B 1 12  ? 19.358 -17.916 16.330 0.50 12.01  ? 18  VAL   C CA  1 
ATOM   1184 C  CA  B VAL   B 1 12  ? 19.326 -17.949 16.331 0.50 13.65  ? 18  VAL   C CA  1 
ATOM   1185 C  C   . VAL   B 1 12  ? 20.499 -16.916 16.280 1.00 12.34  ? 18  VAL   C C   1 
ATOM   1186 O  O   . VAL   B 1 12  ? 20.745 -16.166 17.251 1.00 13.08  ? 18  VAL   C O   1 
ATOM   1187 C  CB  A VAL   B 1 12  ? 18.199 -17.378 15.412 0.50 12.20  ? 18  VAL   C CB  1 
ATOM   1188 C  CB  B VAL   B 1 12  ? 18.053 -17.433 15.549 0.50 17.36  ? 18  VAL   C CB  1 
ATOM   1189 C  CG1 A VAL   B 1 12  ? 17.223 -18.495 15.092 0.50 14.31  ? 18  VAL   C CG1 1 
ATOM   1190 C  CG1 B VAL   B 1 12  ? 18.319 -17.271 14.072 0.50 18.77  ? 18  VAL   C CG1 1 
ATOM   1191 C  CG2 A VAL   B 1 12  ? 17.555 -16.073 15.959 0.50 9.06   ? 18  VAL   C CG2 1 
ATOM   1192 C  CG2 B VAL   B 1 12  ? 16.878 -18.382 15.739 0.50 20.39  ? 18  VAL   C CG2 1 
ATOM   1193 N  N   . ASN   B 1 13  ? 21.203 -16.856 15.156 1.00 11.88  ? 19  ASN   C N   1 
ATOM   1194 C  CA  . ASN   B 1 13  ? 22.185 -15.797 14.947 1.00 12.32  ? 19  ASN   C CA  1 
ATOM   1195 C  C   . ASN   B 1 13  ? 21.370 -14.462 14.892 1.00 12.59  ? 19  ASN   C C   1 
ATOM   1196 O  O   . ASN   B 1 13  ? 20.373 -14.362 14.173 1.00 12.46  ? 19  ASN   C O   1 
ATOM   1197 C  CB  . ASN   B 1 13  ? 22.906 -15.928 13.589 1.00 12.10  ? 19  ASN   C CB  1 
ATOM   1198 C  CG  . ASN   B 1 13  ? 23.773 -17.189 13.522 1.00 12.35  ? 19  ASN   C CG  1 
ATOM   1199 O  OD1 . ASN   B 1 13  ? 23.321 -18.245 13.090 1.00 13.81  ? 19  ASN   C OD1 1 
ATOM   1200 N  ND2 . ASN   B 1 13  ? 25.011 -17.086 14.000 1.00 13.37  ? 19  ASN   C ND2 1 
ATOM   1201 N  N   . ARG   B 1 14  ? 21.885 -13.438 15.608 1.00 13.00  ? 20  ARG   C N   1 
ATOM   1202 C  CA  . ARG   B 1 14  ? 21.134 -12.140 15.625 1.00 13.12  ? 20  ARG   C CA  1 
ATOM   1203 C  C   . ARG   B 1 14  ? 20.983 -11.589 14.192 1.00 13.84  ? 20  ARG   C C   1 
ATOM   1204 O  O   . ARG   B 1 14  ? 19.919 -11.066 13.844 1.00 14.30  ? 20  ARG   C O   1 
ATOM   1205 C  CB  . ARG   B 1 14  ? 21.864 -11.140 16.489 1.00 13.46  ? 20  ARG   C CB  1 
ATOM   1206 C  CG  . ARG   B 1 14  ? 21.056 -9.818  16.720 1.00 14.09  ? 20  ARG   C CG  1 
ATOM   1207 C  CD  . ARG   B 1 14  ? 21.926 -8.859  17.508 1.00 14.67  ? 20  ARG   C CD  1 
ATOM   1208 N  NE  . ARG   B 1 14  ? 21.241 -7.596  17.912 1.00 14.58  ? 20  ARG   C NE  1 
ATOM   1209 C  CZ  . ARG   B 1 14  ? 21.147 -6.513  17.158 1.00 14.71  ? 20  ARG   C CZ  1 
ATOM   1210 N  NH1 . ARG   B 1 14  ? 21.585 -6.530  15.906 1.00 16.80  ? 20  ARG   C NH1 1 
ATOM   1211 N  NH2 . ARG   B 1 14  ? 20.655 -5.385  17.665 1.00 15.99  ? 20  ARG   C NH2 1 
ATOM   1212 N  N   . HIS   B 1 15  ? 22.007 -11.783 13.334 1.00 13.82  ? 21  HIS   C N   1 
ATOM   1213 C  CA  . HIS   B 1 15  ? 21.938 -11.250 11.962 1.00 14.47  ? 21  HIS   C CA  1 
ATOM   1214 C  C   . HIS   B 1 15  ? 20.957 -11.992 11.055 1.00 14.47  ? 21  HIS   C C   1 
ATOM   1215 O  O   . HIS   B 1 15  ? 20.676 -11.476 9.977  1.00 16.83  ? 21  HIS   C O   1 
ATOM   1216 C  CB  . HIS   B 1 15  ? 23.339 -11.138 11.312 1.00 15.10  ? 21  HIS   C CB  1 
ATOM   1217 C  CG  . HIS   B 1 15  ? 23.937 -12.456 10.881 1.00 13.75  ? 21  HIS   C CG  1 
ATOM   1218 N  ND1 . HIS   B 1 15  ? 24.681 -13.272 11.753 1.00 14.37  ? 21  HIS   C ND1 1 
ATOM   1219 C  CD2 . HIS   B 1 15  ? 23.952 -13.009 9.649  1.00 15.21  ? 21  HIS   C CD2 1 
ATOM   1220 C  CE1 . HIS   B 1 15  ? 25.075 -14.328 11.022 1.00 15.33  ? 21  HIS   C CE1 1 
ATOM   1221 N  NE2 . HIS   B 1 15  ? 24.661 -14.202 9.744  1.00 15.57  ? 21  HIS   C NE2 1 
ATOM   1222 N  N   . LEU   B 1 16  ? 20.420 -13.136 11.490 1.00 13.86  ? 22  LEU   C N   1 
ATOM   1223 C  CA  . LEU   B 1 16  ? 19.415 -13.909 10.730 1.00 14.39  ? 22  LEU   C CA  1 
ATOM   1224 C  C   . LEU   B 1 16  ? 18.026 -13.869 11.402 1.00 15.15  ? 22  LEU   C C   1 
ATOM   1225 O  O   . LEU   B 1 16  ? 17.102 -14.565 10.950 1.00 15.91  ? 22  LEU   C O   1 
ATOM   1226 C  CB  . LEU   B 1 16  ? 19.912 -15.352 10.541 1.00 14.31  ? 22  LEU   C CB  1 
ATOM   1227 C  CG  . LEU   B 1 16  ? 21.220 -15.488 9.757  1.00 15.16  ? 22  LEU   C CG  1 
ATOM   1228 C  CD1 . LEU   B 1 16  ? 21.626 -16.970 9.683  1.00 16.29  ? 22  LEU   C CD1 1 
ATOM   1229 C  CD2 . LEU   B 1 16  ? 21.069 -14.895 8.360  1.00 16.70  ? 22  LEU   C CD2 1 
ATOM   1230 N  N   . ALA   B 1 17  ? 17.864 -13.104 12.508 1.00 14.77  ? 23  ALA   C N   1 
ATOM   1231 C  CA  . ALA   B 1 17  ? 16.573 -13.028 13.207 1.00 13.93  ? 23  ALA   C CA  1 
ATOM   1232 C  C   . ALA   B 1 17  ? 15.471 -12.451 12.308 1.00 15.16  ? 23  ALA   C C   1 
ATOM   1233 O  O   . ALA   B 1 17  ? 15.744 -11.531 11.530 1.00 16.33  ? 23  ALA   C O   1 
ATOM   1234 C  CB  . ALA   B 1 17  ? 16.722 -12.190 14.473 1.00 15.80  ? 23  ALA   C CB  1 
ATOM   1235 N  N   . THR   B 1 18  ? 14.278 -13.022 12.431 1.00 16.22  ? 24  THR   C N   1 
ATOM   1236 C  CA  . THR   B 1 18  ? 13.155 -12.584 11.635 1.00 16.30  ? 24  THR   C CA  1 
ATOM   1237 C  C   . THR   B 1 18  ? 12.327 -11.546 12.418 1.00 15.28  ? 24  THR   C C   1 
ATOM   1238 O  O   . THR   B 1 18  ? 12.535 -11.255 13.586 1.00 15.90  ? 24  THR   C O   1 
ATOM   1239 C  CB  . THR   B 1 18  ? 12.242 -13.823 11.353 1.00 17.04  ? 24  THR   C CB  1 
ATOM   1240 O  OG1 . THR   B 1 18  ? 11.684 -14.239 12.580 1.00 18.00  ? 24  THR   C OG1 1 
ATOM   1241 C  CG2 . THR   B 1 18  ? 12.987 -14.996 10.679 1.00 18.79  ? 24  THR   C CG2 1 
ATOM   1242 N  N   . HIS   B 1 19  ? 11.311 -10.934 11.726 1.00 17.32  ? 25  HIS   C N   1 
ATOM   1243 C  CA  . HIS   B 1 19  ? 10.374 -10.017 12.406 1.00 17.68  ? 25  HIS   C CA  1 
ATOM   1244 C  C   . HIS   B 1 19  ? 9.685  -10.750 13.525 1.00 15.59  ? 25  HIS   C C   1 
ATOM   1245 O  O   . HIS   B 1 19  ? 9.587  -10.197 14.628 1.00 17.24  ? 25  HIS   C O   1 
ATOM   1246 C  CB  . HIS   B 1 19  ? 9.262  -9.508  11.448 1.00 19.46  ? 25  HIS   C CB  1 
ATOM   1247 C  CG  . HIS   B 1 19  ? 8.130  -8.800  12.165 1.00 19.53  ? 25  HIS   C CG  1 
ATOM   1248 N  ND1 . HIS   B 1 19  ? 8.275  -7.528  12.688 1.00 22.14  ? 25  HIS   C ND1 1 
ATOM   1249 C  CD2 . HIS   B 1 19  ? 6.942  -9.296  12.557 1.00 21.26  ? 25  HIS   C CD2 1 
ATOM   1250 C  CE1 . HIS   B 1 19  ? 7.097  -7.225  13.239 1.00 21.29  ? 25  HIS   C CE1 1 
ATOM   1251 N  NE2 . HIS   B 1 19  ? 6.276  -8.276  13.220 1.00 21.74  ? 25  HIS   C NE2 1 
ATOM   1252 N  N   . ASN   B 1 20  ? 9.237  -12.018 13.305 1.00 16.50  ? 26  ASN   C N   1 
ATOM   1253 C  CA  . ASN   B 1 20  ? 8.579  -12.749 14.382 1.00 17.91  ? 26  ASN   C CA  1 
ATOM   1254 C  C   . ASN   B 1 20  ? 9.500  -12.948 15.589 1.00 16.14  ? 26  ASN   C C   1 
ATOM   1255 O  O   . ASN   B 1 20  ? 9.063  -12.891 16.732 1.00 16.38  ? 26  ASN   C O   1 
ATOM   1256 C  CB  . ASN   B 1 20  ? 8.056  -14.117 13.906 1.00 20.10  ? 26  ASN   C CB  1 
ATOM   1257 C  CG  . ASN   B 1 20  ? 7.217  -14.815 14.979 1.00 26.12  ? 26  ASN   C CG  1 
ATOM   1258 O  OD1 . ASN   B 1 20  ? 6.075  -14.409 15.268 1.00 28.90  ? 26  ASN   C OD1 1 
ATOM   1259 N  ND2 . ASN   B 1 20  ? 7.748  -15.841 15.628 1.00 27.50  ? 26  ASN   C ND2 1 
ATOM   1260 N  N   . ASP   B 1 21  ? 10.828 -13.171 15.335 1.00 15.49  ? 27  ASP   C N   1 
ATOM   1261 C  CA  . ASP   B 1 21  ? 11.751 -13.277 16.456 1.00 15.64  ? 27  ASP   C CA  1 
ATOM   1262 C  C   . ASP   B 1 21  ? 11.811 -11.990 17.281 1.00 14.46  ? 27  ASP   C C   1 
ATOM   1263 O  O   . ASP   B 1 21  ? 11.710 -12.016 18.504 1.00 15.55  ? 27  ASP   C O   1 
ATOM   1264 C  CB  . ASP   B 1 21  ? 13.169 -13.598 15.959 1.00 14.62  ? 27  ASP   C CB  1 
ATOM   1265 C  CG  . ASP   B 1 21  ? 13.377 -15.017 15.465 1.00 15.58  ? 27  ASP   C CG  1 
ATOM   1266 O  OD1 . ASP   B 1 21  ? 12.791 -15.938 16.062 1.00 17.05  ? 27  ASP   C OD1 1 
ATOM   1267 O  OD2 . ASP   B 1 21  ? 14.083 -15.189 14.445 1.00 15.98  ? 27  ASP   C OD2 1 
ATOM   1268 N  N   . TRP   B 1 22  ? 11.922 -10.826 16.590 1.00 14.56  ? 28  TRP   C N   1 
ATOM   1269 C  CA  . TRP   B 1 22  ? 11.962 -9.529  17.275 1.00 14.94  ? 28  TRP   C CA  1 
ATOM   1270 C  C   . TRP   B 1 22  ? 10.612 -9.206  17.962 1.00 14.70  ? 28  TRP   C C   1 
ATOM   1271 O  O   . TRP   B 1 22  ? 10.620 -8.610  19.037 1.00 15.90  ? 28  TRP   C O   1 
ATOM   1272 C  CB  . TRP   B 1 22  ? 12.352 -8.424  16.301 1.00 15.53  ? 28  TRP   C CB  1 
ATOM   1273 C  CG  . TRP   B 1 22  ? 13.831 -8.392  16.047 1.00 15.08  ? 28  TRP   C CG  1 
ATOM   1274 C  CD1 . TRP   B 1 22  ? 14.489 -8.845  14.946 1.00 16.52  ? 28  TRP   C CD1 1 
ATOM   1275 C  CD2 . TRP   B 1 22  ? 14.834 -7.803  16.905 1.00 13.90  ? 28  TRP   C CD2 1 
ATOM   1276 N  NE1 . TRP   B 1 22  ? 15.858 -8.581  15.063 1.00 16.08  ? 28  TRP   C NE1 1 
ATOM   1277 C  CE2 . TRP   B 1 22  ? 16.083 -7.925  16.247 1.00 15.22  ? 28  TRP   C CE2 1 
ATOM   1278 C  CE3 . TRP   B 1 22  ? 14.782 -7.100  18.119 1.00 16.62  ? 28  TRP   C CE3 1 
ATOM   1279 C  CZ2 . TRP   B 1 22  ? 17.257 -7.397  16.762 1.00 15.35  ? 28  TRP   C CZ2 1 
ATOM   1280 C  CZ3 . TRP   B 1 22  ? 15.970 -6.605  18.635 1.00 17.03  ? 28  TRP   C CZ3 1 
ATOM   1281 C  CH2 . TRP   B 1 22  ? 17.182 -6.734  17.937 1.00 16.24  ? 28  TRP   C CH2 1 
ATOM   1282 N  N   . ALA   B 1 23  ? 9.488  -9.674  17.386 1.00 15.71  ? 29  ALA   C N   1 
ATOM   1283 C  CA  . ALA   B 1 23  ? 8.166  -9.441  17.976 1.00 16.48  ? 29  ALA   C CA  1 
ATOM   1284 C  C   . ALA   B 1 23  ? 7.890  -10.328 19.190 1.00 16.94  ? 29  ALA   C C   1 
ATOM   1285 O  O   . ALA   B 1 23  ? 6.908  -10.115 19.909 1.00 18.32  ? 29  ALA   C O   1 
ATOM   1286 C  CB  . ALA   B 1 23  ? 7.083  -9.666  16.923 1.00 17.40  ? 29  ALA   C CB  1 
ATOM   1287 N  N   . ASN   B 1 24  ? 8.740  -11.353 19.428 1.00 17.21  ? 30  ASN   C N   1 
ATOM   1288 C  CA  . ASN   B 1 24  ? 8.643  -12.280 20.565 1.00 17.40  ? 30  ASN   C CA  1 
ATOM   1289 C  C   . ASN   B 1 24  ? 9.993  -12.339 21.285 1.00 17.32  ? 30  ASN   C C   1 
ATOM   1290 O  O   . ASN   B 1 24  ? 10.437 -13.420 21.701 1.00 16.35  ? 30  ASN   C O   1 
ATOM   1291 C  CB  . ASN   B 1 24  ? 8.207  -13.664 20.035 1.00 19.21  ? 30  ASN   C CB  1 
ATOM   1292 C  CG  . ASN   B 1 24  ? 6.796  -13.613 19.531 1.00 19.83  ? 30  ASN   C CG  1 
ATOM   1293 O  OD1 . ASN   B 1 24  ? 5.816  -13.635 20.335 1.00 22.34  ? 30  ASN   C OD1 1 
ATOM   1294 N  ND2 . ASN   B 1 24  ? 6.584  -13.482 18.239 1.00 20.26  ? 30  ASN   C ND2 1 
ATOM   1295 N  N   . LEU   B 1 25  ? 10.701 -11.208 21.340 1.00 17.60  ? 31  LEU   C N   1 
ATOM   1296 C  CA  . LEU   B 1 25  ? 12.070 -11.207 21.873 1.00 16.38  ? 31  LEU   C CA  1 
ATOM   1297 C  C   . LEU   B 1 25  ? 12.182 -11.528 23.356 1.00 17.58  ? 31  LEU   C C   1 
ATOM   1298 O  O   . LEU   B 1 25  ? 11.406 -11.026 24.185 1.00 19.22  ? 31  LEU   C O   1 
ATOM   1299 C  CB  . LEU   B 1 25  ? 12.603 -9.805  21.626 1.00 16.93  ? 31  LEU   C CB  1 
ATOM   1300 C  CG  . LEU   B 1 25  ? 14.073 -9.631  22.036 1.00 16.94  ? 31  LEU   C CG  1 
ATOM   1301 C  CD1 . LEU   B 1 25  ? 15.012 -10.499 21.143 1.00 16.83  ? 31  LEU   C CD1 1 
ATOM   1302 C  CD2 . LEU   B 1 25  ? 14.508 -8.193  21.896 1.00 19.11  ? 31  LEU   C CD2 1 
ATOM   1303 N  N   . VAL   B 1 26  ? 13.167 -12.348 23.706 1.00 16.37  ? 32  VAL   C N   1 
ATOM   1304 C  CA  . VAL   B 1 26  ? 13.520 -12.635 25.092 1.00 16.88  ? 32  VAL   C CA  1 
ATOM   1305 C  C   . VAL   B 1 26  ? 14.841 -11.908 25.434 1.00 17.37  ? 32  VAL   C C   1 
ATOM   1306 O  O   . VAL   B 1 26  ? 14.952 -11.249 26.489 1.00 19.43  ? 32  VAL   C O   1 
ATOM   1307 C  CB  . VAL   B 1 26  ? 13.672 -14.158 25.311 1.00 17.94  ? 32  VAL   C CB  1 
ATOM   1308 C  CG1 . VAL   B 1 26  ? 14.209 -14.467 26.717 1.00 20.50  ? 32  VAL   C CG1 1 
ATOM   1309 C  CG2 . VAL   B 1 26  ? 12.337 -14.844 25.104 1.00 18.17  ? 32  VAL   C CG2 1 
ATOM   1310 N  N   . TRP   B 1 27  ? 15.869 -12.034 24.569 1.00 16.03  ? 33  TRP   C N   1 
ATOM   1311 C  CA  . TRP   B 1 27  ? 17.196 -11.475 24.858 1.00 16.41  ? 33  TRP   C CA  1 
ATOM   1312 C  C   . TRP   B 1 27  ? 17.973 -11.391 23.554 1.00 16.29  ? 33  TRP   C C   1 
ATOM   1313 O  O   . TRP   B 1 27  ? 17.825 -12.275 22.697 1.00 16.04  ? 33  TRP   C O   1 
ATOM   1314 C  CB  . TRP   B 1 27  ? 17.923 -12.378 25.907 1.00 17.86  ? 33  TRP   C CB  1 
ATOM   1315 C  CG  . TRP   B 1 27  ? 19.389 -12.098 26.112 1.00 18.26  ? 33  TRP   C CG  1 
ATOM   1316 C  CD1 . TRP   B 1 27  ? 19.955 -11.153 26.922 1.00 20.80  ? 33  TRP   C CD1 1 
ATOM   1317 C  CD2 . TRP   B 1 27  ? 20.474 -12.771 25.463 1.00 17.14  ? 33  TRP   C CD2 1 
ATOM   1318 N  NE1 . TRP   B 1 27  ? 21.337 -11.252 26.870 1.00 21.64  ? 33  TRP   C NE1 1 
ATOM   1319 C  CE2 . TRP   B 1 27  ? 21.675 -12.241 25.983 1.00 19.19  ? 33  TRP   C CE2 1 
ATOM   1320 C  CE3 . TRP   B 1 27  ? 20.545 -13.808 24.523 1.00 16.57  ? 33  TRP   C CE3 1 
ATOM   1321 C  CZ2 . TRP   B 1 27  ? 22.932 -12.718 25.594 1.00 18.63  ? 33  TRP   C CZ2 1 
ATOM   1322 C  CZ3 . TRP   B 1 27  ? 21.792 -14.307 24.179 1.00 17.94  ? 33  TRP   C CZ3 1 
ATOM   1323 C  CH2 . TRP   B 1 27  ? 22.958 -13.722 24.674 1.00 18.73  ? 33  TRP   C CH2 1 
ATOM   1324 N  N   . GLU   B 1 28  ? 18.838 -10.404 23.419 1.00 15.60  ? 34  GLU   C N   1 
ATOM   1325 C  CA  . GLU   B 1 28  ? 19.695 -10.308 22.233 1.00 16.71  ? 34  GLU   C CA  1 
ATOM   1326 C  C   . GLU   B 1 28  ? 20.985 -9.625  22.601 1.00 16.28  ? 34  GLU   C C   1 
ATOM   1327 O  O   . GLU   B 1 28  ? 20.998 -8.737  23.509 1.00 17.12  ? 34  GLU   C O   1 
ATOM   1328 C  CB  . GLU   B 1 28  ? 19.015 -9.623  21.034 1.00 16.98  ? 34  GLU   C CB  1 
ATOM   1329 C  CG  . GLU   B 1 28  ? 18.459 -8.253  21.333 1.00 17.96  ? 34  GLU   C CG  1 
ATOM   1330 C  CD  . GLU   B 1 28  ? 19.435 -7.092  21.270 1.00 19.01  ? 34  GLU   C CD  1 
ATOM   1331 O  OE1 . GLU   B 1 28  ? 19.147 -6.050  21.905 1.00 20.90  ? 34  GLU   C OE1 1 
ATOM   1332 O  OE2 . GLU   B 1 28  ? 20.441 -7.162  20.522 1.00 17.88  ? 34  GLU   C OE2 1 
ATOM   1333 N  N   . ASP   B 1 29  ? 22.070 -9.961  21.889 1.00 15.35  ? 35  ASP   C N   1 
ATOM   1334 C  CA  . ASP   B 1 29  ? 23.359 -9.318  22.131 1.00 15.86  ? 35  ASP   C CA  1 
ATOM   1335 C  C   . ASP   B 1 29  ? 24.142 -9.281  20.817 1.00 15.94  ? 35  ASP   C C   1 
ATOM   1336 O  O   . ASP   B 1 29  ? 24.609 -10.320 20.324 1.00 15.01  ? 35  ASP   C O   1 
ATOM   1337 C  CB  . ASP   B 1 29  ? 24.057 -10.084 23.262 1.00 17.39  ? 35  ASP   C CB  1 
ATOM   1338 C  CG  . ASP   B 1 29  ? 25.411 -9.565  23.667 1.00 21.31  ? 35  ASP   C CG  1 
ATOM   1339 O  OD1 . ASP   B 1 29  ? 26.172 -9.126  22.782 1.00 21.25  ? 35  ASP   C OD1 1 
ATOM   1340 O  OD2 . ASP   B 1 29  ? 25.776 -9.724  24.849 1.00 23.98  ? 35  ASP   C OD2 1 
ATOM   1341 N  N   . SER   B 1 30  ? 24.324 -8.073  20.260 1.00 15.58  ? 36  SER   C N   1 
ATOM   1342 C  CA  A SER   B 1 30  ? 25.042 -7.891  19.000 0.50 16.09  ? 36  SER   C CA  1 
ATOM   1343 C  CA  B SER   B 1 30  ? 25.022 -7.936  18.993 0.50 16.52  ? 36  SER   C CA  1 
ATOM   1344 C  C   . SER   B 1 30  ? 26.497 -8.341  19.094 1.00 16.26  ? 36  SER   C C   1 
ATOM   1345 O  O   . SER   B 1 30  ? 27.010 -8.960  18.135 1.00 16.00  ? 36  SER   C O   1 
ATOM   1346 C  CB  A SER   B 1 30  ? 24.987 -6.436  18.547 0.50 17.21  ? 36  SER   C CB  1 
ATOM   1347 C  CB  B SER   B 1 30  ? 24.849 -6.534  18.429 0.50 18.83  ? 36  SER   C CB  1 
ATOM   1348 O  OG  A SER   B 1 30  ? 25.899 -6.199  17.482 0.50 16.91  ? 36  SER   C OG  1 
ATOM   1349 O  OG  B SER   B 1 30  ? 25.333 -5.571  19.345 0.50 20.73  ? 36  SER   C OG  1 
ATOM   1350 N  N   . SER   B 1 31  ? 27.168 -8.060  20.231 1.00 16.59  ? 37  SER   C N   1 
ATOM   1351 C  CA  . SER   B 1 31  ? 28.563 -8.449  20.361 1.00 17.53  ? 37  SER   C CA  1 
ATOM   1352 C  C   . SER   B 1 31  ? 28.747 -9.967  20.332 1.00 15.34  ? 37  SER   C C   1 
ATOM   1353 O  O   . SER   B 1 31  ? 29.845 -10.412 19.967 1.00 16.20  ? 37  SER   C O   1 
ATOM   1354 C  CB  . SER   B 1 31  ? 29.167 -7.906  21.635 1.00 21.85  ? 37  SER   C CB  1 
ATOM   1355 O  OG  . SER   B 1 31  ? 28.796 -8.630  22.793 1.00 25.99  ? 37  SER   C OG  1 
ATOM   1356 N  N   . ARG   B 1 32  ? 27.689 -10.766 20.657 1.00 14.32  ? 38  ARG   C N   1 
ATOM   1357 C  CA  . ARG   B 1 32  ? 27.780 -12.244 20.597 1.00 14.21  ? 38  ARG   C CA  1 
ATOM   1358 C  C   . ARG   B 1 32  ? 27.159 -12.805 19.310 1.00 13.48  ? 38  ARG   C C   1 
ATOM   1359 O  O   . ARG   B 1 32  ? 27.195 -14.019 19.100 1.00 13.65  ? 38  ARG   C O   1 
ATOM   1360 C  CB  . ARG   B 1 32  ? 27.023 -12.849 21.806 1.00 16.76  ? 38  ARG   C CB  1 
ATOM   1361 C  CG  . ARG   B 1 32  ? 27.678 -12.492 23.133 1.00 17.76  ? 38  ARG   C CG  1 
ATOM   1362 C  CD  . ARG   B 1 32  ? 26.922 -13.059 24.323 1.00 15.28  ? 38  ARG   C CD  1 
ATOM   1363 N  NE  . ARG   B 1 32  ? 26.992 -14.542 24.342 1.00 15.08  ? 38  ARG   C NE  1 
ATOM   1364 C  CZ  . ARG   B 1 32  ? 26.936 -15.284 25.455 1.00 15.50  ? 38  ARG   C CZ  1 
ATOM   1365 N  NH1 . ARG   B 1 32  ? 26.819 -14.711 26.643 1.00 17.26  ? 38  ARG   C NH1 1 
ATOM   1366 N  NH2 . ARG   B 1 32  ? 27.090 -16.605 25.388 1.00 15.89  ? 38  ARG   C NH2 1 
ATOM   1367 N  N   . ASP   B 1 33  ? 26.498 -11.961 18.488 1.00 13.27  ? 39  ASP   C N   1 
ATOM   1368 C  CA  . ASP   B 1 33  ? 25.712 -12.420 17.340 1.00 13.11  ? 39  ASP   C CA  1 
ATOM   1369 C  C   . ASP   B 1 33  ? 24.606 -13.392 17.751 1.00 13.41  ? 39  ASP   C C   1 
ATOM   1370 O  O   . ASP   B 1 33  ? 24.336 -14.337 16.992 1.00 13.33  ? 39  ASP   C O   1 
ATOM   1371 C  CB  . ASP   B 1 33  ? 26.593 -13.015 16.217 1.00 13.86  ? 39  ASP   C CB  1 
ATOM   1372 C  CG  . ASP   B 1 33  ? 25.810 -13.359 14.935 1.00 14.56  ? 39  ASP   C CG  1 
ATOM   1373 O  OD1 . ASP   B 1 33  ? 24.910 -12.577 14.547 1.00 15.04  ? 39  ASP   C OD1 1 
ATOM   1374 O  OD2 . ASP   B 1 33  ? 26.137 -14.390 14.291 1.00 14.12  ? 39  ASP   C OD2 1 
ATOM   1375 N  N   . LEU   B 1 34  ? 23.940 -13.180 18.907 1.00 12.41  ? 40  LEU   C N   1 
ATOM   1376 C  CA  . LEU   B 1 34  ? 22.856 -14.085 19.314 1.00 12.24  ? 40  LEU   C CA  1 
ATOM   1377 C  C   . LEU   B 1 34  ? 21.551 -13.342 19.583 1.00 12.39  ? 40  LEU   C C   1 
ATOM   1378 O  O   . LEU   B 1 34  ? 21.555 -12.185 20.076 1.00 13.55  ? 40  LEU   C O   1 
ATOM   1379 C  CB  . LEU   B 1 34  ? 23.251 -14.789 20.624 1.00 13.45  ? 40  LEU   C CB  1 
ATOM   1380 C  CG  . LEU   B 1 34  ? 24.336 -15.899 20.534 1.00 14.14  ? 40  LEU   C CG  1 
ATOM   1381 C  CD1 . LEU   B 1 34  ? 24.556 -16.486 21.947 1.00 15.45  ? 40  LEU   C CD1 1 
ATOM   1382 C  CD2 . LEU   B 1 34  ? 23.889 -17.010 19.578 1.00 13.72  ? 40  LEU   C CD2 1 
ATOM   1383 N  N   . LEU   B 1 35  ? 20.451 -14.039 19.348 1.00 11.96  ? 41  LEU   C N   1 
ATOM   1384 C  CA  . LEU   B 1 35  ? 19.122 -13.540 19.707 1.00 12.88  ? 41  LEU   C CA  1 
ATOM   1385 C  C   . LEU   B 1 35  ? 18.292 -14.750 20.090 1.00 13.08  ? 41  LEU   C C   1 
ATOM   1386 O  O   . LEU   B 1 35  ? 18.388 -15.816 19.457 1.00 13.52  ? 41  LEU   C O   1 
ATOM   1387 C  CB  . LEU   B 1 35  ? 18.482 -12.806 18.481 1.00 12.91  ? 41  LEU   C CB  1 
ATOM   1388 C  CG  . LEU   B 1 35  ? 17.078 -12.189 18.728 1.00 13.55  ? 41  LEU   C CG  1 
ATOM   1389 C  CD1 . LEU   B 1 35  ? 16.895 -10.880 17.944 1.00 15.56  ? 41  LEU   C CD1 1 
ATOM   1390 C  CD2 . LEU   B 1 35  ? 16.009 -13.211 18.373 1.00 14.25  ? 41  LEU   C CD2 1 
ATOM   1391 N  N   . VAL   B 1 36  ? 17.491 -14.579 21.131 1.00 12.69  ? 42  VAL   C N   1 
ATOM   1392 C  CA  . VAL   B 1 36  ? 16.569 -15.597 21.633 1.00 12.96  ? 42  VAL   C CA  1 
ATOM   1393 C  C   . VAL   B 1 36  ? 15.149 -15.065 21.622 1.00 13.33  ? 42  VAL   C C   1 
ATOM   1394 O  O   . VAL   B 1 36  ? 14.895 -13.934 22.127 1.00 15.35  ? 42  VAL   C O   1 
ATOM   1395 C  CB  . VAL   B 1 36  ? 16.956 -16.046 23.063 1.00 14.15  ? 42  VAL   C CB  1 
ATOM   1396 C  CG1 . VAL   B 1 36  ? 15.970 -17.100 23.586 1.00 16.55  ? 42  VAL   C CG1 1 
ATOM   1397 C  CG2 . VAL   B 1 36  ? 18.401 -16.620 23.080 1.00 15.20  ? 42  VAL   C CG2 1 
ATOM   1398 N  N   . SER   B 1 37  ? 14.238 -15.832 21.055 1.00 13.41  ? 43  SER   C N   1 
ATOM   1399 C  CA  . SER   B 1 37  ? 12.812 -15.475 21.003 1.00 14.34  ? 43  SER   C CA  1 
ATOM   1400 C  C   . SER   B 1 37  ? 12.011 -16.583 21.678 1.00 14.65  ? 43  SER   C C   1 
ATOM   1401 O  O   . SER   B 1 37  ? 12.499 -17.684 21.971 1.00 15.80  ? 43  SER   C O   1 
ATOM   1402 C  CB  . SER   B 1 37  ? 12.354 -15.267 19.560 1.00 14.49  ? 43  SER   C CB  1 
ATOM   1403 O  OG  . SER   B 1 37  ? 12.531 -16.440 18.772 1.00 15.93  ? 43  SER   C OG  1 
ATOM   1404 N  N   . SER   B 1 38  ? 10.788 -16.251 22.068 1.00 16.18  ? 44  SER   C N   1 
ATOM   1405 C  CA  . SER   B 1 38  ? 9.891  -17.211 22.733 1.00 17.47  ? 44  SER   C CA  1 
ATOM   1406 C  C   . SER   B 1 38  ? 9.075  -18.006 21.698 1.00 19.30  ? 44  SER   C C   1 
ATOM   1407 O  O   . SER   B 1 38  ? 8.748  -17.519 20.607 1.00 21.32  ? 44  SER   C O   1 
ATOM   1408 C  CB  . SER   B 1 38  ? 8.966  -16.512 23.728 1.00 19.78  ? 44  SER   C CB  1 
ATOM   1409 O  OG  . SER   B 1 38  ? 8.153  -15.623 22.993 1.00 23.61  ? 44  SER   C OG  1 
ATOM   1410 N  N   . THR   B 1 39  ? 8.729  -19.236 22.049 1.00 19.13  ? 45  THR   C N   1 
ATOM   1411 C  CA  . THR   B 1 39  ? 7.998  -20.128 21.134 1.00 20.97  ? 45  THR   C CA  1 
ATOM   1412 C  C   . THR   B 1 39  ? 6.689  -20.598 21.816 1.00 23.42  ? 45  THR   C C   1 
ATOM   1413 O  O   . THR   B 1 39  ? 6.625  -20.692 23.042 1.00 22.41  ? 45  THR   C O   1 
ATOM   1414 C  CB  . THR   B 1 39  ? 8.841  -21.390 20.779 1.00 21.60  ? 45  THR   C CB  1 
ATOM   1415 O  OG1 . THR   B 1 39  ? 9.104  -22.142 21.950 1.00 22.86  ? 45  THR   C OG1 1 
ATOM   1416 C  CG2 . THR   B 1 39  ? 10.216 -21.080 20.102 1.00 21.87  ? 45  THR   C CG2 1 
ATOM   1417 N  N   . THR   B 1 40  ? 5.717  -21.012 21.002 1.00 25.64  ? 46  THR   C N   1 
ATOM   1418 C  CA  . THR   B 1 40  ? 4.476  -21.559 21.571 1.00 28.00  ? 46  THR   C CA  1 
ATOM   1419 C  C   . THR   B 1 40  ? 4.693  -23.028 21.926 1.00 28.87  ? 46  THR   C C   1 
ATOM   1420 O  O   . THR   B 1 40  ? 4.315  -23.474 23.017 1.00 31.72  ? 46  THR   C O   1 
ATOM   1421 C  CB  . THR   B 1 40  ? 3.287  -21.259 20.647 1.00 32.68  ? 46  THR   C CB  1 
ATOM   1422 O  OG1 . THR   B 1 40  ? 3.560  -21.846 19.377 1.00 36.44  ? 46  THR   C OG1 1 
ATOM   1423 C  CG2 . THR   B 1 40  ? 3.098  -19.770 20.444 1.00 32.43  ? 46  THR   C CG2 1 
ATOM   1424 N  N   . ALA   B 1 41  ? 5.343  -23.786 21.025 1.00 26.93  ? 47  ALA   C N   1 
ATOM   1425 C  CA  . ALA   B 1 41  ? 5.624  -25.199 21.258 1.00 27.77  ? 47  ALA   C CA  1 
ATOM   1426 C  C   . ALA   B 1 41  ? 6.947  -25.425 22.009 1.00 27.02  ? 47  ALA   C C   1 
ATOM   1427 O  O   . ALA   B 1 41  ? 7.889  -24.668 21.808 1.00 26.66  ? 47  ALA   C O   1 
ATOM   1428 C  CB  . ALA   B 1 41  ? 5.678  -25.931 19.924 1.00 28.82  ? 47  ALA   C CB  1 
ATOM   1429 N  N   . GLN   B 1 42  ? 7.053  -26.474 22.816 1.00 27.44  ? 48  GLN   C N   1 
ATOM   1430 C  CA  . GLN   B 1 42  ? 8.284  -26.805 23.513 1.00 27.82  ? 48  GLN   C CA  1 
ATOM   1431 C  C   . GLN   B 1 42  ? 9.255  -27.483 22.552 1.00 26.55  ? 48  GLN   C C   1 
ATOM   1432 O  O   . GLN   B 1 42  ? 8.865  -28.302 21.731 1.00 28.46  ? 48  GLN   C O   1 
ATOM   1433 C  CB  . GLN   B 1 42  ? 8.008  -27.709 24.726 1.00 33.07  ? 48  GLN   C CB  1 
ATOM   1434 C  CG  . GLN   B 1 42  ? 7.398  -26.961 25.912 1.00 41.31  ? 48  GLN   C CG  1 
ATOM   1435 C  CD  . GLN   B 1 42  ? 7.167  -27.955 27.015 1.00 52.25  ? 48  GLN   C CD  1 
ATOM   1436 O  OE1 . GLN   B 1 42  ? 6.200  -28.730 26.995 1.00 55.82  ? 48  GLN   C OE1 1 
ATOM   1437 N  NE2 . GLN   B 1 42  ? 8.070  -28.002 27.986 1.00 54.66  ? 48  GLN   C NE2 1 
ATOM   1438 N  N   . GLY   B 1 43  ? 10.530 -27.124 22.669 1.00 23.74  ? 49  GLY   C N   1 
ATOM   1439 C  CA  . GLY   B 1 43  ? 11.614 -27.700 21.898 1.00 22.85  ? 49  GLY   C CA  1 
ATOM   1440 C  C   . GLY   B 1 43  ? 12.305 -28.764 22.733 1.00 22.03  ? 49  GLY   C C   1 
ATOM   1441 O  O   . GLY   B 1 43  ? 12.120 -28.854 23.966 1.00 23.98  ? 49  GLY   C O   1 
ATOM   1442 N  N   . CYS   B 1 44  ? 13.090 -29.547 22.067 1.00 21.28  ? 50  CYS   C N   1 
ATOM   1443 C  CA  . CYS   B 1 44  ? 13.700 -30.731 22.676 1.00 22.02  ? 50  CYS   C CA  1 
ATOM   1444 C  C   . CYS   B 1 44  ? 15.184 -30.758 22.705 1.00 21.03  ? 50  CYS   C C   1 
ATOM   1445 O  O   . CYS   B 1 44  ? 15.738 -31.804 23.100 1.00 23.88  ? 50  CYS   C O   1 
ATOM   1446 C  CB  . CYS   B 1 44  ? 13.189 -31.974 21.970 1.00 23.33  ? 50  CYS   C CB  1 
ATOM   1447 S  SG  . CYS   B 1 44  ? 11.400 -32.134 22.042 1.00 33.04  ? 50  CYS   C SG  1 
ATOM   1448 N  N   . ASP   B 1 45  ? 15.875 -29.739 22.218 1.00 18.46  ? 51  ASP   C N   1 
ATOM   1449 C  CA  . ASP   B 1 45  ? 17.344 -29.736 22.223 1.00 18.70  ? 51  ASP   C CA  1 
ATOM   1450 C  C   . ASP   B 1 45  ? 17.777 -29.554 23.688 1.00 18.86  ? 51  ASP   C C   1 
ATOM   1451 O  O   . ASP   B 1 45  ? 17.088 -28.892 24.498 1.00 20.70  ? 51  ASP   C O   1 
ATOM   1452 C  CB  . ASP   B 1 45  ? 17.917 -28.582 21.372 1.00 18.64  ? 51  ASP   C CB  1 
ATOM   1453 C  CG  . ASP   B 1 45  ? 17.747 -28.752 19.885 1.00 23.43  ? 51  ASP   C CG  1 
ATOM   1454 O  OD1 . ASP   B 1 45  ? 17.806 -29.896 19.410 1.00 26.32  ? 51  ASP   C OD1 1 
ATOM   1455 O  OD2 . ASP   B 1 45  ? 17.625 -27.715 19.165 1.00 20.10  ? 51  ASP   C OD2 1 
ATOM   1456 N  N   . THR   B 1 46  ? 18.894 -30.181 24.027 1.00 16.71  ? 52  THR   C N   1 
ATOM   1457 C  CA  . THR   B 1 46  ? 19.488 -30.042 25.341 1.00 16.74  ? 52  THR   C CA  1 
ATOM   1458 C  C   . THR   B 1 46  ? 20.747 -29.164 25.183 1.00 15.22  ? 52  THR   C C   1 
ATOM   1459 O  O   . THR   B 1 46  ? 21.594 -29.482 24.308 1.00 16.13  ? 52  THR   C O   1 
ATOM   1460 C  CB  . THR   B 1 46  ? 19.879 -31.402 25.884 1.00 19.07  ? 52  THR   C CB  1 
ATOM   1461 O  OG1 . THR   B 1 46  ? 18.677 -32.174 26.050 1.00 21.32  ? 52  THR   C OG1 1 
ATOM   1462 C  CG2 . THR   B 1 46  ? 20.589 -31.282 27.247 1.00 21.75  ? 52  THR   C CG2 1 
ATOM   1463 N  N   . ILE   B 1 47  ? 20.919 -28.136 26.007 1.00 15.61  ? 53  ILE   C N   1 
ATOM   1464 C  CA  . ILE   B 1 47  ? 22.119 -27.302 25.965 1.00 14.68  ? 53  ILE   C CA  1 
ATOM   1465 C  C   . ILE   B 1 47  ? 23.206 -27.981 26.818 1.00 14.55  ? 53  ILE   C C   1 
ATOM   1466 O  O   . ILE   B 1 47  ? 22.944 -28.442 27.943 1.00 15.99  ? 53  ILE   C O   1 
ATOM   1467 C  CB  . ILE   B 1 47  ? 21.834 -25.921 26.540 1.00 15.82  ? 53  ILE   C CB  1 
ATOM   1468 C  CG1 . ILE   B 1 47  ? 20.620 -25.256 25.860 1.00 16.43  ? 53  ILE   C CG1 1 
ATOM   1469 C  CG2 . ILE   B 1 47  ? 23.100 -25.064 26.470 1.00 16.18  ? 53  ILE   C CG2 1 
ATOM   1470 C  CD1 . ILE   B 1 47  ? 20.842 -25.092 24.330 1.00 18.20  ? 53  ILE   C CD1 1 
ATOM   1471 N  N   . ALA   B 1 48  ? 24.420 -28.078 26.287 1.00 13.16  ? 54  ALA   C N   1 
ATOM   1472 C  CA  . ALA   B 1 48  ? 25.552 -28.635 27.043 1.00 13.13  ? 54  ALA   C CA  1 
ATOM   1473 C  C   . ALA   B 1 48  ? 25.881 -27.686 28.227 1.00 13.47  ? 54  ALA   C C   1 
ATOM   1474 O  O   . ALA   B 1 48  ? 25.848 -26.448 28.090 1.00 13.81  ? 54  ALA   C O   1 
ATOM   1475 C  CB  . ALA   B 1 48  ? 26.762 -28.722 26.112 1.00 12.92  ? 54  ALA   C CB  1 
ATOM   1476 N  N   . ARG   B 1 49  ? 26.234 -28.293 29.373 1.00 13.64  ? 55  ARG   C N   1 
ATOM   1477 C  CA  . ARG   B 1 49  ? 26.692 -27.513 30.533 1.00 13.57  ? 55  ARG   C CA  1 
ATOM   1478 C  C   . ARG   B 1 49  ? 28.009 -28.146 30.924 1.00 13.17  ? 55  ARG   C C   1 
ATOM   1479 O  O   . ARG   B 1 49  ? 28.033 -29.170 31.649 1.00 15.33  ? 55  ARG   C O   1 
ATOM   1480 C  CB  . ARG   B 1 49  ? 25.675 -27.543 31.695 1.00 15.07  ? 55  ARG   C CB  1 
ATOM   1481 C  CG  . ARG   B 1 49  ? 24.305 -26.994 31.238 1.00 15.00  ? 55  ARG   C CG  1 
ATOM   1482 C  CD  . ARG   B 1 49  ? 24.283 -25.526 30.870 1.00 15.98  ? 55  ARG   C CD  1 
ATOM   1483 N  NE  . ARG   B 1 49  ? 22.925 -25.114 30.495 1.00 16.07  ? 55  ARG   C NE  1 
ATOM   1484 C  CZ  . ARG   B 1 49  ? 22.661 -24.010 29.790 1.00 15.58  ? 55  ARG   C CZ  1 
ATOM   1485 N  NH1 . ARG   B 1 49  ? 23.636 -23.162 29.468 1.00 15.84  ? 55  ARG   C NH1 1 
ATOM   1486 N  NH2 . ARG   B 1 49  ? 21.402 -23.719 29.421 1.00 16.90  ? 55  ARG   C NH2 1 
ATOM   1487 N  N   . CYS   B 1 50  ? 29.127 -27.580 30.420 1.00 12.96  ? 56  CYS   C N   1 
ATOM   1488 C  CA  . CYS   B 1 50  ? 30.467 -28.206 30.451 1.00 13.32  ? 56  CYS   C CA  1 
ATOM   1489 C  C   . CYS   B 1 50  ? 31.500 -27.240 29.934 1.00 13.03  ? 56  CYS   C C   1 
ATOM   1490 O  O   . CYS   B 1 50  ? 31.176 -26.129 29.500 1.00 14.29  ? 56  CYS   C O   1 
ATOM   1491 C  CB  . CYS   B 1 50  ? 30.428 -29.433 29.524 1.00 12.87  ? 56  CYS   C CB  1 
ATOM   1492 S  SG  . CYS   B 1 50  ? 30.275 -29.006 27.758 1.00 12.94  ? 56  CYS   C SG  1 
ATOM   1493 N  N   . ASP   B 1 51  ? 32.791 -27.685 29.999 1.00 14.84  ? 57  ASP   C N   1 
ATOM   1494 C  CA  . ASP   B 1 51  ? 33.902 -26.944 29.409 1.00 15.89  ? 57  ASP   C CA  1 
ATOM   1495 C  C   . ASP   B 1 51  ? 34.580 -27.822 28.316 1.00 14.43  ? 57  ASP   C C   1 
ATOM   1496 O  O   . ASP   B 1 51  ? 35.789 -27.676 28.088 1.00 16.03  ? 57  ASP   C O   1 
ATOM   1497 C  CB  . ASP   B 1 51  ? 34.916 -26.462 30.453 1.00 19.32  ? 57  ASP   C CB  1 
ATOM   1498 C  CG  . ASP   B 1 51  ? 35.599 -27.543 31.203 1.00 21.32  ? 57  ASP   C CG  1 
ATOM   1499 O  OD1 . ASP   B 1 51  ? 35.313 -28.730 30.952 1.00 21.09  ? 57  ASP   C OD1 1 
ATOM   1500 O  OD2 . ASP   B 1 51  ? 36.536 -27.213 32.006 1.00 27.27  ? 57  ASP   C OD2 1 
ATOM   1501 N  N   . CYS   B 1 52  ? 33.818 -28.703 27.604 1.00 12.80  ? 58  CYS   C N   1 
ATOM   1502 C  CA  . CYS   B 1 52  ? 34.418 -29.454 26.479 1.00 12.95  ? 58  CYS   C CA  1 
ATOM   1503 C  C   . CYS   B 1 52  ? 35.085 -28.524 25.468 1.00 12.29  ? 58  CYS   C C   1 
ATOM   1504 O  O   . CYS   B 1 52  ? 34.634 -27.391 25.245 1.00 12.93  ? 58  CYS   C O   1 
ATOM   1505 C  CB  . CYS   B 1 52  ? 33.350 -30.290 25.753 1.00 13.51  ? 58  CYS   C CB  1 
ATOM   1506 S  SG  . CYS   B 1 52  ? 32.714 -31.709 26.689 1.00 14.12  ? 58  CYS   C SG  1 
ATOM   1507 N  N   . GLN   B 1 53  ? 36.123 -29.043 24.858 1.00 12.27  ? 59  GLN   C N   1 
ATOM   1508 C  CA  . GLN   B 1 53  ? 36.823 -28.446 23.730 1.00 13.07  ? 59  GLN   C CA  1 
ATOM   1509 C  C   . GLN   B 1 53  ? 36.894 -29.387 22.573 1.00 12.34  ? 59  GLN   C C   1 
ATOM   1510 O  O   . GLN   B 1 53  ? 37.669 -29.136 21.627 1.00 12.85  ? 59  GLN   C O   1 
ATOM   1511 C  CB  . GLN   B 1 53  ? 38.224 -27.960 24.127 1.00 14.08  ? 59  GLN   C CB  1 
ATOM   1512 C  CG  . GLN   B 1 53  ? 38.189 -26.694 24.997 1.00 18.92  ? 59  GLN   C CG  1 
ATOM   1513 C  CD  . GLN   B 1 53  ? 39.561 -26.125 25.232 1.00 19.26  ? 59  GLN   C CD  1 
ATOM   1514 O  OE1 . GLN   B 1 53  ? 40.084 -26.228 26.358 1.00 21.89  ? 59  GLN   C OE1 1 
ATOM   1515 N  NE2 . GLN   B 1 53  ? 40.206 -25.602 24.183 1.00 18.19  ? 59  GLN   C NE2 1 
ATOM   1516 N  N   . THR   B 1 54  ? 36.116 -30.475 22.563 1.00 11.90  ? 60  THR   C N   1 
ATOM   1517 C  CA  . THR   B 1 54  ? 36.013 -31.311 21.374 1.00 12.88  ? 60  THR   C CA  1 
ATOM   1518 C  C   . THR   B 1 54  ? 34.541 -31.597 21.112 1.00 12.46  ? 60  THR   C C   1 
ATOM   1519 O  O   . THR   B 1 54  ? 33.735 -31.727 22.056 1.00 13.37  ? 60  THR   C O   1 
ATOM   1520 C  CB  . THR   B 1 54  ? 36.779 -32.593 21.451 1.00 15.94  ? 60  THR   C CB  1 
ATOM   1521 O  OG1 . THR   B 1 54  ? 36.208 -33.373 22.426 1.00 19.65  ? 60  THR   C OG1 1 
ATOM   1522 C  CG2 . THR   B 1 54  ? 38.225 -32.398 21.764 1.00 16.05  ? 60  THR   C CG2 1 
ATOM   1523 N  N   . GLY   B 1 55  ? 34.167 -31.658 19.840 1.00 11.33  ? 61  GLY   C N   1 
ATOM   1524 C  CA  . GLY   B 1 55  ? 32.763 -31.891 19.506 1.00 10.93  ? 61  GLY   C CA  1 
ATOM   1525 C  C   . GLY   B 1 55  ? 32.651 -32.069 18.005 1.00 9.83   ? 61  GLY   C C   1 
ATOM   1526 O  O   . GLY   B 1 55  ? 33.635 -32.393 17.323 1.00 11.13  ? 61  GLY   C O   1 
ATOM   1527 N  N   . VAL   B 1 56  ? 31.420 -31.949 17.503 1.00 10.04  ? 62  VAL   C N   1 
ATOM   1528 C  CA  . VAL   B 1 56  ? 31.137 -32.150 16.062 1.00 9.69   ? 62  VAL   C CA  1 
ATOM   1529 C  C   . VAL   B 1 56  ? 30.229 -31.015 15.623 1.00 9.72   ? 62  VAL   C C   1 
ATOM   1530 O  O   . VAL   B 1 56  ? 29.281 -30.708 16.325 1.00 10.61  ? 62  VAL   C O   1 
ATOM   1531 C  CB  . VAL   B 1 56  ? 30.409 -33.531 15.886 1.00 10.33  ? 62  VAL   C CB  1 
ATOM   1532 C  CG1 . VAL   B 1 56  ? 29.899 -33.717 14.453 1.00 12.26  ? 62  VAL   C CG1 1 
ATOM   1533 C  CG2 . VAL   B 1 56  ? 31.322 -34.707 16.288 1.00 11.48  ? 62  VAL   C CG2 1 
ATOM   1534 N  N   . TYR   B 1 57  ? 30.500 -30.433 14.450 1.00 9.87   ? 63  TYR   C N   1 
ATOM   1535 C  CA  . TYR   B 1 57  ? 29.612 -29.361 13.945 1.00 8.70   ? 63  TYR   C CA  1 
ATOM   1536 C  C   . TYR   B 1 57  ? 29.055 -29.689 12.572 1.00 10.19  ? 63  TYR   C C   1 
ATOM   1537 O  O   . TYR   B 1 57  ? 29.720 -30.401 11.789 1.00 10.99  ? 63  TYR   C O   1 
ATOM   1538 C  CB  . TYR   B 1 57  ? 30.273 -27.940 13.945 1.00 10.42  ? 63  TYR   C CB  1 
ATOM   1539 C  CG  . TYR   B 1 57  ? 31.157 -27.619 12.741 1.00 10.59  ? 63  TYR   C CG  1 
ATOM   1540 C  CD1 . TYR   B 1 57  ? 32.441 -28.137 12.631 1.00 11.30  ? 63  TYR   C CD1 1 
ATOM   1541 C  CD2 . TYR   B 1 57  ? 30.706 -26.782 11.721 1.00 11.29  ? 63  TYR   C CD2 1 
ATOM   1542 C  CE1 . TYR   B 1 57  ? 33.256 -27.841 11.541 1.00 12.15  ? 63  TYR   C CE1 1 
ATOM   1543 C  CE2 . TYR   B 1 57  ? 31.523 -26.460 10.632 1.00 11.63  ? 63  TYR   C CE2 1 
ATOM   1544 C  CZ  . TYR   B 1 57  ? 32.797 -26.974 10.563 1.00 12.12  ? 63  TYR   C CZ  1 
ATOM   1545 O  OH  . TYR   B 1 57  ? 33.670 -26.684 9.518  1.00 14.19  ? 63  TYR   C OH  1 
ATOM   1546 N  N   . TYR   B 1 58  ? 27.894 -29.123 12.279 1.00 10.00  ? 64  TYR   C N   1 
ATOM   1547 C  CA  . TYR   B 1 58  ? 27.306 -29.300 10.945 1.00 10.73  ? 64  TYR   C CA  1 
ATOM   1548 C  C   . TYR   B 1 58  ? 27.693 -28.134 10.034 1.00 11.07  ? 64  TYR   C C   1 
ATOM   1549 O  O   . TYR   B 1 58  ? 27.461 -26.957 10.337 1.00 11.02  ? 64  TYR   C O   1 
ATOM   1550 C  CB  . TYR   B 1 58  ? 25.762 -29.384 11.013 1.00 11.52  ? 64  TYR   C CB  1 
ATOM   1551 C  CG  . TYR   B 1 58  ? 25.195 -29.646 9.635  1.00 12.55  ? 64  TYR   C CG  1 
ATOM   1552 C  CD1 . TYR   B 1 58  ? 25.524 -30.803 8.941  1.00 13.09  ? 64  TYR   C CD1 1 
ATOM   1553 C  CD2 . TYR   B 1 58  ? 24.340 -28.744 9.029  1.00 13.53  ? 64  TYR   C CD2 1 
ATOM   1554 C  CE1 . TYR   B 1 58  ? 25.025 -31.049 7.645  1.00 15.32  ? 64  TYR   C CE1 1 
ATOM   1555 C  CE2 . TYR   B 1 58  ? 23.833 -28.985 7.728  1.00 14.85  ? 64  TYR   C CE2 1 
ATOM   1556 C  CZ  . TYR   B 1 58  ? 24.180 -30.140 7.072  1.00 15.09  ? 64  TYR   C CZ  1 
ATOM   1557 O  OH  . TYR   B 1 58  ? 23.718 -30.389 5.772  1.00 17.79  ? 64  TYR   C OH  1 
ATOM   1558 N  N   . CYS   B 1 59  ? 28.218 -28.505 8.859  1.00 10.98  ? 65  CYS   C N   1 
ATOM   1559 C  CA  . CYS   B 1 59  ? 28.627 -27.570 7.791  1.00 11.73  ? 65  CYS   C CA  1 
ATOM   1560 C  C   . CYS   B 1 59  ? 27.710 -27.736 6.582  1.00 12.54  ? 65  CYS   C C   1 
ATOM   1561 O  O   . CYS   B 1 59  ? 27.888 -28.668 5.777  1.00 13.59  ? 65  CYS   C O   1 
ATOM   1562 C  CB  . CYS   B 1 59  ? 30.067 -27.843 7.415  1.00 12.03  ? 65  CYS   C CB  1 
ATOM   1563 S  SG  . CYS   B 1 59  ? 30.688 -26.771 6.091  1.00 13.75  ? 65  CYS   C SG  1 
ATOM   1564 N  N   . SER   B 1 60  ? 26.739 -26.837 6.459  1.00 13.40  ? 66  SER   C N   1 
ATOM   1565 C  CA  . SER   B 1 60  ? 25.769 -26.977 5.371  1.00 14.62  ? 66  SER   C CA  1 
ATOM   1566 C  C   . SER   B 1 60  ? 26.399 -26.899 3.975  1.00 14.76  ? 66  SER   C C   1 
ATOM   1567 O  O   . SER   B 1 60  ? 25.974 -27.643 3.093  1.00 16.09  ? 66  SER   C O   1 
ATOM   1568 C  CB  . SER   B 1 60  ? 24.643 -25.970 5.517  1.00 17.06  ? 66  SER   C CB  1 
ATOM   1569 O  OG  . SER   B 1 60  ? 23.721 -26.126 4.447  1.00 21.74  ? 66  SER   C OG  1 
ATOM   1570 N  N   . SER   B 1 61  ? 27.416 -26.025 3.817  1.00 13.83  ? 67  SER   C N   1 
ATOM   1571 C  CA  . SER   B 1 61  ? 28.101 -25.857 2.519  1.00 14.52  ? 67  SER   C CA  1 
ATOM   1572 C  C   . SER   B 1 61  ? 28.952 -27.061 2.138  1.00 15.63  ? 67  SER   C C   1 
ATOM   1573 O  O   . SER   B 1 61  ? 29.474 -27.033 1.011  1.00 17.39  ? 67  SER   C O   1 
ATOM   1574 C  CB  . SER   B 1 61  ? 28.940 -24.589 2.524  1.00 15.46  ? 67  SER   C CB  1 
ATOM   1575 O  OG  . SER   B 1 61  ? 30.043 -24.692 3.407  1.00 16.95  ? 67  SER   C OG  1 
ATOM   1576 N  N   . ARG   B 1 62  ? 29.046 -28.112 2.969  1.00 14.20  ? 68  ARG   C N   1 
ATOM   1577 C  CA  . ARG   B 1 62  ? 29.670 -29.370 2.591  1.00 14.62  ? 68  ARG   C CA  1 
ATOM   1578 C  C   . ARG   B 1 62  ? 28.732 -30.574 2.765  1.00 15.24  ? 68  ARG   C C   1 
ATOM   1579 O  O   . ARG   B 1 62  ? 29.148 -31.710 2.580  1.00 16.54  ? 68  ARG   C O   1 
ATOM   1580 C  CB  . ARG   B 1 62  ? 30.945 -29.587 3.416  1.00 15.08  ? 68  ARG   C CB  1 
ATOM   1581 C  CG  . ARG   B 1 62  ? 32.032 -28.544 3.228  1.00 19.05  ? 68  ARG   C CG  1 
ATOM   1582 C  CD  . ARG   B 1 62  ? 32.682 -28.761 1.898  1.00 18.59  ? 68  ARG   C CD  1 
ATOM   1583 N  NE  . ARG   B 1 62  ? 33.763 -27.783 1.643  1.00 20.97  ? 68  ARG   C NE  1 
ATOM   1584 C  CZ  . ARG   B 1 62  ? 33.593 -26.603 1.083  1.00 22.21  ? 68  ARG   C CZ  1 
ATOM   1585 N  NH1 . ARG   B 1 62  ? 32.421 -26.275 0.557  1.00 22.44  ? 68  ARG   C NH1 1 
ATOM   1586 N  NH2 . ARG   B 1 62  ? 34.652 -25.821 0.824  1.00 26.70  ? 68  ARG   C NH2 1 
ATOM   1587 N  N   . ARG   B 1 63  ? 27.521 -30.321 3.285  1.00 15.97  ? 69  ARG   C N   1 
ATOM   1588 C  CA  . ARG   B 1 63  ? 26.593 -31.409 3.688  1.00 16.94  ? 69  ARG   C CA  1 
ATOM   1589 C  C   . ARG   B 1 63  ? 27.251 -32.440 4.578  1.00 17.63  ? 69  ARG   C C   1 
ATOM   1590 O  O   . ARG   B 1 63  ? 27.122 -33.646 4.396  1.00 19.69  ? 69  ARG   C O   1 
ATOM   1591 C  CB  . ARG   B 1 63  ? 25.977 -32.076 2.450  1.00 18.11  ? 69  ARG   C CB  1 
ATOM   1592 C  CG  . ARG   B 1 63  ? 25.160 -31.122 1.607  1.00 22.05  ? 69  ARG   C CG  1 
ATOM   1593 C  CD  . ARG   B 1 63  ? 23.924 -30.720 2.330  1.00 26.87  ? 69  ARG   C CD  1 
ATOM   1594 N  NE  . ARG   B 1 63  ? 22.898 -30.266 1.390  1.00 27.73  ? 69  ARG   C NE  1 
ATOM   1595 C  CZ  . ARG   B 1 63  ? 22.680 -28.996 1.077  1.00 29.16  ? 69  ARG   C CZ  1 
ATOM   1596 N  NH1 . ARG   B 1 63  ? 21.710 -28.675 0.233  1.00 29.33  ? 69  ARG   C NH1 1 
ATOM   1597 N  NH2 . ARG   B 1 63  ? 23.445 -28.037 1.585  1.00 29.56  ? 69  ARG   C NH2 1 
ATOM   1598 N  N   . LYS   B 1 64  ? 28.075 -31.942 5.542  1.00 15.51  ? 70  LYS   C N   1 
ATOM   1599 C  CA  . LYS   B 1 64  ? 28.861 -32.864 6.371  1.00 15.44  ? 70  LYS   C CA  1 
ATOM   1600 C  C   . LYS   B 1 64  ? 28.946 -32.388 7.807  1.00 14.21  ? 70  LYS   C C   1 
ATOM   1601 O  O   . LYS   B 1 64  ? 28.960 -31.163 8.044  1.00 15.06  ? 70  LYS   C O   1 
ATOM   1602 C  CB  . LYS   B 1 64  ? 30.301 -32.911 5.798  1.00 19.32  ? 70  LYS   C CB  1 
ATOM   1603 C  CG  . LYS   B 1 64  ? 30.479 -33.904 4.649  1.00 28.77  ? 70  LYS   C CG  1 
ATOM   1604 C  CD  . LYS   B 1 64  ? 31.952 -34.178 4.354  1.00 37.15  ? 70  LYS   C CD  1 
ATOM   1605 C  CE  . LYS   B 1 64  ? 32.105 -35.052 3.135  1.00 41.88  ? 70  LYS   C CE  1 
ATOM   1606 N  NZ  . LYS   B 1 64  ? 31.448 -34.452 1.943  1.00 45.92  ? 70  LYS   C NZ  1 
ATOM   1607 N  N   . HIS   B 1 65  ? 29.051 -33.346 8.704  1.00 12.70  ? 71  HIS   C N   1 
ATOM   1608 C  CA  . HIS   B 1 65  ? 29.348 -33.091 10.102 1.00 12.91  ? 71  HIS   C CA  1 
ATOM   1609 C  C   . HIS   B 1 65  ? 30.824 -33.371 10.314 1.00 15.39  ? 71  HIS   C C   1 
ATOM   1610 O  O   . HIS   B 1 65  ? 31.315 -34.467 9.955  1.00 19.05  ? 71  HIS   C O   1 
ATOM   1611 C  CB  . HIS   B 1 65  ? 28.520 -33.975 11.005 1.00 13.35  ? 71  HIS   C CB  1 
ATOM   1612 C  CG  . HIS   B 1 65  ? 27.043 -33.709 10.989 1.00 12.60  ? 71  HIS   C CG  1 
ATOM   1613 N  ND1 . HIS   B 1 65  ? 26.382 -32.936 11.947 1.00 15.38  ? 71  HIS   C ND1 1 
ATOM   1614 C  CD2 . HIS   B 1 65  ? 26.126 -34.119 10.070 1.00 12.54  ? 71  HIS   C CD2 1 
ATOM   1615 C  CE1 . HIS   B 1 65  ? 25.086 -32.945 11.606 1.00 13.68  ? 71  HIS   C CE1 1 
ATOM   1616 N  NE2 . HIS   B 1 65  ? 24.885 -33.665 10.506 1.00 16.04  ? 71  HIS   C NE2 1 
ATOM   1617 N  N   . TYR   B 1 66  ? 31.560 -32.422 10.914 1.00 12.59  ? 72  TYR   C N   1 
ATOM   1618 C  CA  . TYR   B 1 66  ? 33.000 -32.578 11.102 1.00 12.09  ? 72  TYR   C CA  1 
ATOM   1619 C  C   . TYR   B 1 66  ? 33.340 -32.630 12.585 1.00 11.53  ? 72  TYR   C C   1 
ATOM   1620 O  O   . TYR   B 1 66  ? 32.905 -31.751 13.345 1.00 10.98  ? 72  TYR   C O   1 
ATOM   1621 C  CB  . TYR   B 1 66  ? 33.757 -31.352 10.540 1.00 12.63  ? 72  TYR   C CB  1 
ATOM   1622 C  CG  . TYR   B 1 66  ? 33.720 -31.264 9.026  1.00 13.87  ? 72  TYR   C CG  1 
ATOM   1623 C  CD1 . TYR   B 1 66  ? 34.591 -32.008 8.251  1.00 16.01  ? 72  TYR   C CD1 1 
ATOM   1624 C  CD2 . TYR   B 1 66  ? 32.885 -30.359 8.371  1.00 14.96  ? 72  TYR   C CD2 1 
ATOM   1625 C  CE1 . TYR   B 1 66  ? 34.611 -31.903 6.860  1.00 16.39  ? 72  TYR   C CE1 1 
ATOM   1626 C  CE2 . TYR   B 1 66  ? 32.890 -30.242 6.979  1.00 15.11  ? 72  TYR   C CE2 1 
ATOM   1627 C  CZ  . TYR   B 1 66  ? 33.752 -31.018 6.235  1.00 15.04  ? 72  TYR   C CZ  1 
ATOM   1628 O  OH  . TYR   B 1 66  ? 33.737 -30.845 4.858  1.00 18.05  ? 72  TYR   C OH  1 
ATOM   1629 N  N   . PRO   B 1 67  ? 34.170 -33.593 13.000 1.00 11.59  ? 73  PRO   C N   1 
ATOM   1630 C  CA  . PRO   B 1 67  ? 34.692 -33.559 14.382 1.00 11.88  ? 73  PRO   C CA  1 
ATOM   1631 C  C   . PRO   B 1 67  ? 35.781 -32.470 14.493 1.00 12.15  ? 73  PRO   C C   1 
ATOM   1632 O  O   . PRO   B 1 67  ? 36.671 -32.413 13.612 1.00 14.46  ? 73  PRO   C O   1 
ATOM   1633 C  CB  . PRO   B 1 67  ? 35.319 -34.968 14.566 1.00 13.99  ? 73  PRO   C CB  1 
ATOM   1634 C  CG  . PRO   B 1 67  ? 35.581 -35.456 13.242 1.00 16.23  ? 73  PRO   C CG  1 
ATOM   1635 C  CD  . PRO   B 1 67  ? 34.689 -34.757 12.225 1.00 12.97  ? 73  PRO   C CD  1 
ATOM   1636 N  N   . VAL   B 1 68  ? 35.780 -31.699 15.531 1.00 10.82  ? 74  VAL   C N   1 
ATOM   1637 C  CA  . VAL   B 1 68  ? 36.722 -30.584 15.697 1.00 12.13  ? 74  VAL   C CA  1 
ATOM   1638 C  C   . VAL   B 1 68  ? 37.110 -30.430 17.126 1.00 11.83  ? 74  VAL   C C   1 
ATOM   1639 O  O   . VAL   B 1 68  ? 36.364 -30.707 18.070 1.00 12.15  ? 74  VAL   C O   1 
ATOM   1640 C  CB  . VAL   B 1 68  ? 36.110 -29.215 15.222 1.00 14.67  ? 74  VAL   C CB  1 
ATOM   1641 C  CG1 . VAL   B 1 68  ? 36.031 -29.141 13.693 1.00 16.35  ? 74  VAL   C CG1 1 
ATOM   1642 C  CG2 . VAL   B 1 68  ? 34.743 -28.933 15.884 1.00 14.82  ? 74  VAL   C CG2 1 
ATOM   1643 N  N   . SER   B 1 69  ? 38.334 -29.893 17.321 1.00 12.03  ? 75  SER   C N   1 
ATOM   1644 C  CA  . SER   B 1 69  ? 38.744 -29.261 18.580 1.00 12.17  ? 75  SER   C CA  1 
ATOM   1645 C  C   . SER   B 1 69  ? 38.469 -27.759 18.509 1.00 11.54  ? 75  SER   C C   1 
ATOM   1646 O  O   . SER   B 1 69  ? 38.628 -27.151 17.426 1.00 12.46  ? 75  SER   C O   1 
ATOM   1647 C  CB  . SER   B 1 69  ? 40.249 -29.442 18.775 1.00 14.23  ? 75  SER   C CB  1 
ATOM   1648 O  OG  . SER   B 1 69  ? 40.508 -30.827 18.821 1.00 19.95  ? 75  SER   C OG  1 
ATOM   1649 N  N   . PHE   B 1 70  ? 37.998 -27.137 19.577 1.00 11.65  ? 76  PHE   C N   1 
ATOM   1650 C  CA  . PHE   B 1 70  ? 37.663 -25.717 19.544 1.00 11.67  ? 76  PHE   C CA  1 
ATOM   1651 C  C   . PHE   B 1 70  ? 38.131 -24.998 20.789 1.00 11.68  ? 76  PHE   C C   1 
ATOM   1652 O  O   . PHE   B 1 70  ? 38.299 -25.615 21.837 1.00 12.61  ? 76  PHE   C O   1 
ATOM   1653 C  CB  . PHE   B 1 70  ? 36.131 -25.492 19.289 1.00 11.85  ? 76  PHE   C CB  1 
ATOM   1654 C  CG  . PHE   B 1 70  ? 35.213 -26.215 20.270 1.00 11.07  ? 76  PHE   C CG  1 
ATOM   1655 C  CD1 . PHE   B 1 70  ? 34.803 -27.526 20.030 1.00 11.42  ? 76  PHE   C CD1 1 
ATOM   1656 C  CD2 . PHE   B 1 70  ? 34.757 -25.579 21.409 1.00 12.05  ? 76  PHE   C CD2 1 
ATOM   1657 C  CE1 . PHE   B 1 70  ? 33.951 -28.170 20.938 1.00 10.74  ? 76  PHE   C CE1 1 
ATOM   1658 C  CE2 . PHE   B 1 70  ? 33.910 -26.240 22.306 1.00 11.72  ? 76  PHE   C CE2 1 
ATOM   1659 C  CZ  . PHE   B 1 70  ? 33.535 -27.530 22.072 1.00 11.59  ? 76  PHE   C CZ  1 
ATOM   1660 N  N   . SER   B 1 71  ? 38.390 -23.721 20.650 1.00 12.11  ? 77  SER   C N   1 
ATOM   1661 C  CA  . SER   B 1 71  ? 38.975 -22.943 21.723 1.00 13.72  ? 77  SER   C CA  1 
ATOM   1662 C  C   . SER   B 1 71  ? 37.948 -22.579 22.783 1.00 14.18  ? 77  SER   C C   1 
ATOM   1663 O  O   . SER   B 1 71  ? 36.741 -22.817 22.659 1.00 15.56  ? 77  SER   C O   1 
ATOM   1664 C  CB  . SER   B 1 71  ? 39.678 -21.701 21.164 1.00 15.20  ? 77  SER   C CB  1 
ATOM   1665 O  OG  . SER   B 1 71  ? 38.753 -20.836 20.510 1.00 17.05  ? 77  SER   C OG  1 
ATOM   1666 N  N   . LYS   B 1 72  ? 38.397 -21.972 23.866 1.00 17.44  ? 78  LYS   C N   1 
ATOM   1667 C  CA  . LYS   B 1 72  ? 37.524 -21.547 24.949 1.00 17.38  ? 78  LYS   C CA  1 
ATOM   1668 C  C   . LYS   B 1 72  ? 36.823 -20.235 24.551 1.00 16.96  ? 78  LYS   C C   1 
ATOM   1669 O  O   . LYS   B 1 72  ? 37.418 -19.414 23.853 1.00 18.14  ? 78  LYS   C O   1 
ATOM   1670 C  CB  . LYS   B 1 72  ? 38.372 -21.304 26.215 1.00 21.86  ? 78  LYS   C CB  1 
ATOM   1671 C  CG  . LYS   B 1 72  ? 39.131 -22.541 26.656 1.00 25.75  ? 78  LYS   C CG  1 
ATOM   1672 C  CD  . LYS   B 1 72  ? 39.172 -22.678 28.228 1.00 37.09  ? 78  LYS   C CD  1 
ATOM   1673 C  CE  . LYS   B 1 72  ? 39.302 -24.132 28.699 1.00 43.30  ? 78  LYS   C CE  1 
ATOM   1674 N  NZ  . LYS   B 1 72  ? 39.170 -24.268 30.178 1.00 47.13  ? 78  LYS   C NZ  1 
ATOM   1675 N  N   . PRO   B 1 73  ? 35.579 -19.984 25.013 1.00 15.79  ? 79  PRO   C N   1 
ATOM   1676 C  CA  . PRO   B 1 73  ? 34.865 -18.738 24.595 1.00 16.19  ? 79  PRO   C CA  1 
ATOM   1677 C  C   . PRO   B 1 73  ? 35.625 -17.492 24.982 1.00 16.60  ? 79  PRO   C C   1 
ATOM   1678 O  O   . PRO   B 1 73  ? 36.065 -17.370 26.135 1.00 20.14  ? 79  PRO   C O   1 
ATOM   1679 C  CB  . PRO   B 1 73  ? 33.526 -18.796 25.343 1.00 17.79  ? 79  PRO   C CB  1 
ATOM   1680 C  CG  . PRO   B 1 73  ? 33.318 -20.238 25.680 1.00 20.34  ? 79  PRO   C CG  1 
ATOM   1681 C  CD  . PRO   B 1 73  ? 34.729 -20.833 25.875 1.00 17.33  ? 79  PRO   C CD  1 
ATOM   1682 N  N   . SER   B 1 74  ? 35.865 -16.604 23.999 1.00 16.47  ? 80  SER   C N   1 
ATOM   1683 C  CA  . SER   B 1 74  ? 36.724 -15.433 24.213 1.00 17.91  ? 80  SER   C CA  1 
ATOM   1684 C  C   . SER   B 1 74  ? 36.304 -14.259 23.324 1.00 18.01  ? 80  SER   C C   1 
ATOM   1685 O  O   . SER   B 1 74  ? 35.441 -14.400 22.462 1.00 17.60  ? 80  SER   C O   1 
ATOM   1686 C  CB  . SER   B 1 74  ? 38.178 -15.781 23.864 1.00 19.73  ? 80  SER   C CB  1 
ATOM   1687 O  OG  . SER   B 1 74  ? 38.605 -16.973 24.496 1.00 28.31  ? 80  SER   C OG  1 
ATOM   1688 N  N   . LEU   B 1 75  ? 36.974 -13.097 23.522 1.00 19.12  ? 81  LEU   C N   1 
ATOM   1689 C  CA  . LEU   B 1 75  ? 36.775 -11.882 22.730 1.00 20.27  ? 81  LEU   C CA  1 
ATOM   1690 C  C   . LEU   B 1 75  ? 37.807 -11.920 21.604 1.00 21.65  ? 81  LEU   C C   1 
ATOM   1691 O  O   . LEU   B 1 75  ? 39.030 -11.868 21.870 1.00 24.57  ? 81  LEU   C O   1 
ATOM   1692 C  CB  . LEU   B 1 75  ? 36.985 -10.621 23.610 1.00 22.25  ? 81  LEU   C CB  1 
ATOM   1693 C  CG  . LEU   B 1 75  ? 36.737 -9.265  22.961 1.00 25.42  ? 81  LEU   C CG  1 
ATOM   1694 C  CD1 . LEU   B 1 75  ? 35.266 -9.092  22.661 1.00 25.63  ? 81  LEU   C CD1 1 
ATOM   1695 C  CD2 . LEU   B 1 75  ? 37.219 -8.111  23.888 1.00 28.20  ? 81  LEU   C CD2 1 
ATOM   1696 N  N   . ILE   B 1 76  ? 37.355 -12.058 20.375 1.00 22.24  ? 82  ILE   C N   1 
ATOM   1697 C  CA  . ILE   B 1 76  ? 38.221 -12.256 19.223 1.00 24.04  ? 82  ILE   C CA  1 
ATOM   1698 C  C   . ILE   B 1 76  ? 37.930 -11.222 18.160 1.00 23.43  ? 82  ILE   C C   1 
ATOM   1699 O  O   . ILE   B 1 76  ? 36.761 -10.933 17.899 1.00 21.81  ? 82  ILE   C O   1 
ATOM   1700 C  CB  . ILE   B 1 76  ? 37.901 -13.682 18.657 1.00 26.30  ? 82  ILE   C CB  1 
ATOM   1701 C  CG1 . ILE   B 1 76  ? 38.115 -14.803 19.726 1.00 28.58  ? 82  ILE   C CG1 1 
ATOM   1702 C  CG2 . ILE   B 1 76  ? 38.630 -13.970 17.343 1.00 28.80  ? 82  ILE   C CG2 1 
ATOM   1703 C  CD1 . ILE   B 1 76  ? 39.475 -15.642 19.729 1.00 30.29  ? 82  ILE   C CD1 1 
ATOM   1704 N  N   . PHE   B 1 77  ? 38.985 -10.675 17.521 1.00 23.05  ? 83  PHE   C N   1 
ATOM   1705 C  CA  . PHE   B 1 77  ? 38.785 -9.784  16.380 1.00 23.16  ? 83  PHE   C CA  1 
ATOM   1706 C  C   . PHE   B 1 77  ? 38.425 -10.676 15.162 1.00 23.33  ? 83  PHE   C C   1 
ATOM   1707 O  O   . PHE   B 1 77  ? 39.097 -11.683 14.858 1.00 25.23  ? 83  PHE   C O   1 
ATOM   1708 C  CB  . PHE   B 1 77  ? 40.085 -9.000  16.091 1.00 24.03  ? 83  PHE   C CB  1 
ATOM   1709 C  CG  . PHE   B 1 77  ? 39.794 -7.856  15.143 1.00 25.34  ? 83  PHE   C CG  1 
ATOM   1710 C  CD1 . PHE   B 1 77  ? 39.047 -6.769  15.556 1.00 26.32  ? 83  PHE   C CD1 1 
ATOM   1711 C  CD2 . PHE   B 1 77  ? 40.178 -7.920  13.805 1.00 28.17  ? 83  PHE   C CD2 1 
ATOM   1712 C  CE1 . PHE   B 1 77  ? 38.756 -5.724  14.675 1.00 28.44  ? 83  PHE   C CE1 1 
ATOM   1713 C  CE2 . PHE   B 1 77  ? 39.860 -6.889  12.925 1.00 29.14  ? 83  PHE   C CE2 1 
ATOM   1714 C  CZ  . PHE   B 1 77  ? 39.187 -5.790  13.372 1.00 28.80  ? 83  PHE   C CZ  1 
ATOM   1715 N  N   . VAL   B 1 78  ? 37.325 -10.339 14.501 1.00 20.25  ? 84  VAL   C N   1 
ATOM   1716 C  CA  . VAL   B 1 78  ? 36.833 -11.076 13.360 1.00 20.16  ? 84  VAL   C CA  1 
ATOM   1717 C  C   . VAL   B 1 78  ? 36.932 -10.148 12.139 1.00 19.70  ? 84  VAL   C C   1 
ATOM   1718 O  O   . VAL   B 1 78  ? 36.422 -9.022  12.206 1.00 20.23  ? 84  VAL   C O   1 
ATOM   1719 C  CB  . VAL   B 1 78  ? 35.350 -11.492 13.635 1.00 20.65  ? 84  VAL   C CB  1 
ATOM   1720 C  CG1 . VAL   B 1 78  ? 34.819 -12.276 12.455 1.00 20.44  ? 84  VAL   C CG1 1 
ATOM   1721 C  CG2 . VAL   B 1 78  ? 35.246 -12.325 14.925 1.00 21.83  ? 84  VAL   C CG2 1 
ATOM   1722 N  N   . GLU   B 1 79  ? 37.481 -10.635 11.010 1.00 19.77  ? 85  GLU   C N   1 
ATOM   1723 C  CA  . GLU   B 1 79  ? 37.526 -9.824  9.791  1.00 20.73  ? 85  GLU   C CA  1 
ATOM   1724 C  C   . GLU   B 1 79  ? 36.131 -9.595  9.227  1.00 20.27  ? 85  GLU   C C   1 
ATOM   1725 O  O   . GLU   B 1 79  ? 35.188 -10.306 9.591  1.00 18.82  ? 85  GLU   C O   1 
ATOM   1726 C  CB  . GLU   B 1 79  ? 38.412 -10.469 8.714  1.00 23.54  ? 85  GLU   C CB  1 
ATOM   1727 C  CG  . GLU   B 1 79  ? 39.897 -10.509 9.057  1.00 28.46  ? 85  GLU   C CG  1 
ATOM   1728 C  CD  . GLU   B 1 79  ? 40.516 -9.152  9.353  1.00 33.60  ? 85  GLU   C CD  1 
ATOM   1729 O  OE1 . GLU   B 1 79  ? 40.151 -8.149  8.691  1.00 36.65  ? 85  GLU   C OE1 1 
ATOM   1730 O  OE2 . GLU   B 1 79  ? 41.358 -9.085  10.277 1.00 39.22  ? 85  GLU   C OE2 1 
ATOM   1731 N  N   . ALA   B 1 80  ? 35.973 -8.610  8.332  1.00 20.85  ? 86  ALA   C N   1 
ATOM   1732 C  CA  . ALA   B 1 80  ? 34.689 -8.289  7.746  1.00 21.91  ? 86  ALA   C CA  1 
ATOM   1733 C  C   . ALA   B 1 80  ? 34.105 -9.499  7.012  1.00 21.54  ? 86  ALA   C C   1 
ATOM   1734 O  O   . ALA   B 1 80  ? 34.852 -10.295 6.443  1.00 23.54  ? 86  ALA   C O   1 
ATOM   1735 C  CB  . ALA   B 1 80  ? 34.861 -7.118  6.757  1.00 23.65  ? 86  ALA   C CB  1 
ATOM   1736 N  N   . SER   B 1 81  ? 32.822 -9.683  7.148  1.00 20.46  ? 87  SER   C N   1 
ATOM   1737 C  CA  . SER   B 1 81  ? 32.109 -10.721 6.471  1.00 21.17  ? 87  SER   C CA  1 
ATOM   1738 C  C   . SER   B 1 81  ? 31.006 -10.053 5.632  1.00 21.62  ? 87  SER   C C   1 
ATOM   1739 O  O   . SER   B 1 81  ? 30.832 -8.789  5.643  1.00 22.69  ? 87  SER   C O   1 
ATOM   1740 C  CB  . SER   B 1 81  ? 31.517 -11.677 7.505  1.00 19.07  ? 87  SER   C CB  1 
ATOM   1741 O  OG  . SER   B 1 81  ? 30.446 -11.022 8.190  1.00 18.26  ? 87  SER   C OG  1 
ATOM   1742 N  N   . GLU   B 1 82  ? 30.179 -10.875 4.972  1.00 22.43  ? 88  GLU   C N   1 
ATOM   1743 C  CA  . GLU   B 1 82  ? 29.089 -10.244 4.217  1.00 24.25  ? 88  GLU   C CA  1 
ATOM   1744 C  C   . GLU   B 1 82  ? 28.010 -9.632  5.136  1.00 22.97  ? 88  GLU   C C   1 
ATOM   1745 O  O   . GLU   B 1 82  ? 27.227 -8.793  4.673  1.00 24.47  ? 88  GLU   C O   1 
ATOM   1746 C  CB  . GLU   B 1 82  ? 28.502 -11.204 3.187  1.00 29.65  ? 88  GLU   C CB  1 
ATOM   1747 C  CG  . GLU   B 1 82  ? 27.602 -12.262 3.762  1.00 37.79  ? 88  GLU   C CG  1 
ATOM   1748 C  CD  . GLU   B 1 82  ? 26.898 -13.065 2.687  1.00 44.65  ? 88  GLU   C CD  1 
ATOM   1749 O  OE1 . GLU   B 1 82  ? 27.521 -13.299 1.624  1.00 45.74  ? 88  GLU   C OE1 1 
ATOM   1750 O  OE2 . GLU   B 1 82  ? 25.732 -13.467 2.913  1.00 45.95  ? 88  GLU   C OE2 1 
ATOM   1751 N  N   . TYR   B 1 83  ? 28.019 -9.937  6.446  1.00 19.62  ? 89  TYR   C N   1 
ATOM   1752 C  CA  . TYR   B 1 83  ? 26.963 -9.490  7.354  1.00 18.94  ? 89  TYR   C CA  1 
ATOM   1753 C  C   . TYR   B 1 83  ? 27.449 -8.661  8.565  1.00 20.47  ? 89  TYR   C C   1 
ATOM   1754 O  O   . TYR   B 1 83  ? 26.602 -8.060  9.223  1.00 20.79  ? 89  TYR   C O   1 
ATOM   1755 C  CB  . TYR   B 1 83  ? 26.104 -10.700 7.816  1.00 18.48  ? 89  TYR   C CB  1 
ATOM   1756 C  CG  . TYR   B 1 83  ? 26.944 -11.880 8.308  1.00 17.59  ? 89  TYR   C CG  1 
ATOM   1757 C  CD1 . TYR   B 1 83  ? 27.421 -12.847 7.426  1.00 17.38  ? 89  TYR   C CD1 1 
ATOM   1758 C  CD2 . TYR   B 1 83  ? 27.300 -12.004 9.646  1.00 17.38  ? 89  TYR   C CD2 1 
ATOM   1759 C  CE1 . TYR   B 1 83  ? 28.167 -13.951 7.875  1.00 17.26  ? 89  TYR   C CE1 1 
ATOM   1760 C  CE2 . TYR   B 1 83  ? 28.087 -13.069 10.098 1.00 17.27  ? 89  TYR   C CE2 1 
ATOM   1761 C  CZ  . TYR   B 1 83  ? 28.494 -14.064 9.216  1.00 16.83  ? 89  TYR   C CZ  1 
ATOM   1762 O  OH  . TYR   B 1 83  ? 29.336 -15.085 9.605  1.00 17.56  ? 89  TYR   C OH  1 
ATOM   1763 N  N   . TYR   B 1 84  ? 28.762 -8.531  8.835  1.00 18.58  ? 90  TYR   C N   1 
ATOM   1764 C  CA  . TYR   B 1 84  ? 29.255 -7.590  9.864  1.00 18.88  ? 90  TYR   C CA  1 
ATOM   1765 C  C   . TYR   B 1 84  ? 30.569 -6.964  9.340  1.00 19.15  ? 90  TYR   C C   1 
ATOM   1766 O  O   . TYR   B 1 84  ? 31.319 -7.606  8.600  1.00 19.89  ? 90  TYR   C O   1 
ATOM   1767 C  CB  . TYR   B 1 84  ? 29.626 -8.342  11.167 1.00 17.05  ? 90  TYR   C CB  1 
ATOM   1768 C  CG  . TYR   B 1 84  ? 28.439 -8.775  12.021 1.00 15.87  ? 90  TYR   C CG  1 
ATOM   1769 C  CD1 . TYR   B 1 84  ? 27.484 -7.852  12.468 1.00 16.32  ? 90  TYR   C CD1 1 
ATOM   1770 C  CD2 . TYR   B 1 84  ? 28.267 -10.093 12.380 1.00 16.14  ? 90  TYR   C CD2 1 
ATOM   1771 C  CE1 . TYR   B 1 84  ? 26.406 -8.242  13.267 1.00 17.18  ? 90  TYR   C CE1 1 
ATOM   1772 C  CE2 . TYR   B 1 84  ? 27.183 -10.498 13.165 1.00 15.64  ? 90  TYR   C CE2 1 
ATOM   1773 C  CZ  . TYR   B 1 84  ? 26.264 -9.568  13.627 1.00 15.75  ? 90  TYR   C CZ  1 
ATOM   1774 O  OH  . TYR   B 1 84  ? 25.199 -9.957  14.432 1.00 15.92  ? 90  TYR   C OH  1 
ATOM   1775 N  N   . PRO   B 1 85  ? 30.925 -5.754  9.790  1.00 19.54  ? 91  PRO   C N   1 
ATOM   1776 C  CA  . PRO   B 1 85  ? 32.268 -5.230  9.487  1.00 20.42  ? 91  PRO   C CA  1 
ATOM   1777 C  C   . PRO   B 1 85  ? 33.277 -6.003  10.350 1.00 20.38  ? 91  PRO   C C   1 
ATOM   1778 O  O   . PRO   B 1 85  ? 32.934 -6.828  11.241 1.00 19.28  ? 91  PRO   C O   1 
ATOM   1779 C  CB  . PRO   B 1 85  ? 32.152 -3.778  9.948  1.00 22.25  ? 91  PRO   C CB  1 
ATOM   1780 C  CG  . PRO   B 1 85  ? 31.260 -3.866  11.105 1.00 21.44  ? 91  PRO   C CG  1 
ATOM   1781 C  CD  . PRO   B 1 85  ? 30.172 -4.891  10.738 1.00 20.19  ? 91  PRO   C CD  1 
ATOM   1782 N  N   . ALA   B 1 86  ? 34.582 -5.723  10.135 1.00 20.07  ? 92  ALA   C N   1 
ATOM   1783 C  CA  . ALA   B 1 86  ? 35.629 -6.205  11.000 1.00 21.44  ? 92  ALA   C CA  1 
ATOM   1784 C  C   . ALA   B 1 86  ? 35.384 -5.625  12.415 1.00 23.33  ? 92  ALA   C C   1 
ATOM   1785 O  O   . ALA   B 1 86  ? 35.062 -4.423  12.550 1.00 24.85  ? 92  ALA   C O   1 
ATOM   1786 C  CB  . ALA   B 1 86  ? 36.985 -5.750  10.475 1.00 22.57  ? 92  ALA   C CB  1 
ATOM   1787 N  N   . ARG   B 1 87  ? 35.381 -6.510  13.425 1.00 22.85  ? 93  ARG   C N   1 
ATOM   1788 C  CA  . ARG   B 1 87  ? 35.055 -6.067  14.776 1.00 22.78  ? 93  ARG   C CA  1 
ATOM   1789 C  C   . ARG   B 1 87  ? 35.467 -7.123  15.802 1.00 22.34  ? 93  ARG   C C   1 
ATOM   1790 O  O   . ARG   B 1 87  ? 35.748 -8.266  15.433 1.00 20.80  ? 93  ARG   C O   1 
ATOM   1791 C  CB  . ARG   B 1 87  ? 33.532 -5.838  14.919 1.00 22.28  ? 93  ARG   C CB  1 
ATOM   1792 C  CG  . ARG   B 1 87  ? 32.728 -7.157  14.800 1.00 21.12  ? 93  ARG   C CG  1 
ATOM   1793 C  CD  . ARG   B 1 87  ? 31.242 -6.935  14.870 1.00 20.80  ? 93  ARG   C CD  1 
ATOM   1794 N  NE  . ARG   B 1 87  ? 30.568 -8.210  15.127 1.00 19.27  ? 93  ARG   C NE  1 
ATOM   1795 C  CZ  . ARG   B 1 87  ? 29.493 -8.387  15.879 1.00 18.16  ? 93  ARG   C CZ  1 
ATOM   1796 N  NH1 . ARG   B 1 87  ? 28.846 -7.339  16.390 1.00 20.01  ? 93  ARG   C NH1 1 
ATOM   1797 N  NH2 . ARG   B 1 87  ? 29.054 -9.613  16.127 1.00 19.94  ? 93  ARG   C NH2 1 
ATOM   1798 N  N   . TYR   B 1 88  ? 35.334 -6.778  17.116 1.00 23.82  ? 94  TYR   C N   1 
ATOM   1799 C  CA  . TYR   B 1 88  ? 35.505 -7.760  18.184 1.00 24.45  ? 94  TYR   C CA  1 
ATOM   1800 C  C   . TYR   B 1 88  ? 34.147 -8.431  18.447 1.00 21.63  ? 94  TYR   C C   1 
ATOM   1801 O  O   . TYR   B 1 88  ? 33.117 -7.791  18.544 1.00 22.46  ? 94  TYR   C O   1 
ATOM   1802 C  CB  . TYR   B 1 88  ? 35.952 -7.078  19.484 1.00 26.68  ? 94  TYR   C CB  1 
ATOM   1803 C  CG  . TYR   B 1 88  ? 37.424 -6.773  19.430 1.00 28.91  ? 94  TYR   C CG  1 
ATOM   1804 C  CD1 . TYR   B 1 88  ? 38.366 -7.765  19.655 1.00 29.73  ? 94  TYR   C CD1 1 
ATOM   1805 C  CD2 . TYR   B 1 88  ? 37.877 -5.517  19.036 1.00 30.40  ? 94  TYR   C CD2 1 
ATOM   1806 C  CE1 . TYR   B 1 88  ? 39.734 -7.497  19.559 1.00 31.47  ? 94  TYR   C CE1 1 
ATOM   1807 C  CE2 . TYR   B 1 88  ? 39.231 -5.236  18.938 1.00 31.35  ? 94  TYR   C CE2 1 
ATOM   1808 C  CZ  . TYR   B 1 88  ? 40.158 -6.227  19.193 1.00 32.78  ? 94  TYR   C CZ  1 
ATOM   1809 O  OH  . TYR   B 1 88  ? 41.499 -5.905  19.077 1.00 35.89  ? 94  TYR   C OH  1 
ATOM   1810 N  N   . GLN   B 1 89  ? 34.158 -9.766  18.510 1.00 18.88  ? 95  GLN   C N   1 
ATOM   1811 C  CA  . GLN   B 1 89  ? 32.967 -10.558 18.853 1.00 17.55  ? 95  GLN   C CA  1 
ATOM   1812 C  C   . GLN   B 1 89  ? 33.285 -11.290 20.155 1.00 16.31  ? 95  GLN   C C   1 
ATOM   1813 O  O   . GLN   B 1 89  ? 34.382 -11.862 20.302 1.00 17.92  ? 95  GLN   C O   1 
ATOM   1814 C  CB  . GLN   B 1 89  ? 32.634 -11.524 17.717 1.00 18.07  ? 95  GLN   C CB  1 
ATOM   1815 C  CG  . GLN   B 1 89  ? 31.377 -12.321 18.006 1.00 18.81  ? 95  GLN   C CG  1 
ATOM   1816 C  CD  . GLN   B 1 89  ? 30.701 -12.890 16.791 1.00 15.84  ? 95  GLN   C CD  1 
ATOM   1817 O  OE1 . GLN   B 1 89  ? 30.679 -12.300 15.701 1.00 17.27  ? 95  GLN   C OE1 1 
ATOM   1818 N  NE2 . GLN   B 1 89  ? 30.123 -14.075 16.968 1.00 15.33  ? 95  GLN   C NE2 1 
ATOM   1819 N  N   . SER   B 1 90  ? 32.367 -11.283 21.085 1.00 15.68  ? 96  SER   C N   1 
ATOM   1820 C  CA  . SER   B 1 90  ? 32.543 -11.904 22.392 1.00 15.67  ? 96  SER   C CA  1 
ATOM   1821 C  C   . SER   B 1 90  ? 31.942 -13.323 22.440 1.00 14.93  ? 96  SER   C C   1 
ATOM   1822 O  O   . SER   B 1 90  ? 31.102 -13.690 21.625 1.00 14.87  ? 96  SER   C O   1 
ATOM   1823 C  CB  . SER   B 1 90  ? 31.967 -11.019 23.502 1.00 17.17  ? 96  SER   C CB  1 
ATOM   1824 O  OG  . SER   B 1 90  ? 30.571 -10.998 23.372 1.00 18.32  ? 96  SER   C OG  1 
ATOM   1825 N  N   . HIS   B 1 91  ? 32.403 -14.105 23.425 1.00 15.54  ? 97  HIS   C N   1 
ATOM   1826 C  CA  . HIS   B 1 91  ? 31.896 -15.480 23.683 1.00 15.25  ? 97  HIS   C CA  1 
ATOM   1827 C  C   . HIS   B 1 91  ? 32.025 -16.345 22.426 1.00 14.18  ? 97  HIS   C C   1 
ATOM   1828 O  O   . HIS   B 1 91  ? 31.130 -17.162 22.161 1.00 14.84  ? 97  HIS   C O   1 
ATOM   1829 C  CB  . HIS   B 1 91  ? 30.442 -15.439 24.208 1.00 15.66  ? 97  HIS   C CB  1 
ATOM   1830 C  CG  . HIS   B 1 91  ? 30.306 -14.686 25.513 1.00 17.26  ? 97  HIS   C CG  1 
ATOM   1831 N  ND1 . HIS   B 1 91  ? 30.278 -15.348 26.718 1.00 18.97  ? 97  HIS   C ND1 1 
ATOM   1832 C  CD2 . HIS   B 1 91  ? 30.204 -13.352 25.743 1.00 18.53  ? 97  HIS   C CD2 1 
ATOM   1833 C  CE1 . HIS   B 1 91  ? 30.144 -14.412 27.659 1.00 19.28  ? 97  HIS   C CE1 1 
ATOM   1834 N  NE2 . HIS   B 1 91  ? 30.080 -13.194 27.119 1.00 19.93  ? 97  HIS   C NE2 1 
ATOM   1835 N  N   . LEU   B 1 92  ? 33.120 -16.184 21.689 1.00 13.71  ? 98  LEU   C N   1 
ATOM   1836 C  CA  . LEU   B 1 92  ? 33.322 -16.869 20.425 1.00 13.69  ? 98  LEU   C CA  1 
ATOM   1837 C  C   . LEU   B 1 92  ? 34.412 -17.939 20.602 1.00 13.95  ? 98  LEU   C C   1 
ATOM   1838 O  O   . LEU   B 1 92  ? 35.384 -17.730 21.314 1.00 13.81  ? 98  LEU   C O   1 
ATOM   1839 C  CB  . LEU   B 1 92  ? 33.828 -15.838 19.372 1.00 14.80  ? 98  LEU   C CB  1 
ATOM   1840 C  CG  . LEU   B 1 92  ? 33.958 -16.374 17.944 1.00 15.69  ? 98  LEU   C CG  1 
ATOM   1841 C  CD1 . LEU   B 1 92  ? 32.612 -16.799 17.358 1.00 15.97  ? 98  LEU   C CD1 1 
ATOM   1842 C  CD2 . LEU   B 1 92  ? 34.678 -15.360 17.018 1.00 18.16  ? 98  LEU   C CD2 1 
ATOM   1843 N  N   . MET   B 1 93  ? 34.226 -19.097 19.964 1.00 13.04  ? 99  MET   C N   1 
ATOM   1844 C  CA  . MET   B 1 93  ? 35.173 -20.227 20.010 1.00 12.29  ? 99  MET   C CA  1 
ATOM   1845 C  C   . MET   B 1 93  ? 35.609 -20.494 18.577 1.00 13.10  ? 99  MET   C C   1 
ATOM   1846 O  O   . MET   B 1 93  ? 34.738 -20.526 17.687 1.00 13.78  ? 99  MET   C O   1 
ATOM   1847 C  CB  . MET   B 1 93  ? 34.425 -21.445 20.564 1.00 13.75  ? 99  MET   C CB  1 
ATOM   1848 C  CG  . MET   B 1 93  ? 33.954 -21.201 21.992 1.00 16.40  ? 99  MET   C CG  1 
ATOM   1849 S  SD  . MET   B 1 93  ? 32.939 -22.539 22.616 1.00 16.14  ? 99  MET   C SD  1 
ATOM   1850 C  CE  . MET   B 1 93  ? 31.452 -22.348 21.474 1.00 16.73  ? 99  MET   C CE  1 
ATOM   1851 N  N   . LEU   B 1 94  ? 36.881 -20.802 18.327 1.00 12.47  ? 100 LEU   C N   1 
ATOM   1852 C  CA  . LEU   B 1 94  ? 37.343 -21.070 16.966 1.00 13.29  ? 100 LEU   C CA  1 
ATOM   1853 C  C   . LEU   B 1 94  ? 37.789 -22.515 16.823 1.00 12.18  ? 100 LEU   C C   1 
ATOM   1854 O  O   . LEU   B 1 94  ? 38.335 -23.115 17.786 1.00 13.19  ? 100 LEU   C O   1 
ATOM   1855 C  CB  . LEU   B 1 94  ? 38.585 -20.190 16.597 1.00 14.77  ? 100 LEU   C CB  1 
ATOM   1856 C  CG  . LEU   B 1 94  ? 38.374 -18.690 16.530 1.00 16.78  ? 100 LEU   C CG  1 
ATOM   1857 C  CD1 . LEU   B 1 94  ? 39.699 -17.985 16.113 1.00 20.87  ? 100 LEU   C CD1 1 
ATOM   1858 C  CD2 . LEU   B 1 94  ? 37.253 -18.313 15.565 1.00 17.41  ? 100 LEU   C CD2 1 
ATOM   1859 N  N   . ALA   B 1 95  ? 37.653 -23.034 15.624 1.00 13.04  ? 101 ALA   C N   1 
ATOM   1860 C  CA  . ALA   B 1 95  ? 38.216 -24.315 15.213 1.00 12.96  ? 101 ALA   C CA  1 
ATOM   1861 C  C   . ALA   B 1 95  ? 38.776 -24.166 13.790 1.00 13.10  ? 101 ALA   C C   1 
ATOM   1862 O  O   . ALA   B 1 95  ? 38.408 -23.259 13.042 1.00 13.02  ? 101 ALA   C O   1 
ATOM   1863 C  CB  . ALA   B 1 95  ? 37.129 -25.414 15.219 1.00 13.28  ? 101 ALA   C CB  1 
ATOM   1864 N  N   . VAL   B 1 96  ? 39.646 -25.112 13.409 1.00 12.87  ? 102 VAL   C N   1 
ATOM   1865 C  CA  . VAL   B 1 96  ? 40.129 -25.169 12.041 1.00 13.55  ? 102 VAL   C CA  1 
ATOM   1866 C  C   . VAL   B 1 96  ? 39.069 -25.935 11.207 1.00 14.34  ? 102 VAL   C C   1 
ATOM   1867 O  O   . VAL   B 1 96  ? 38.746 -27.124 11.487 1.00 15.83  ? 102 VAL   C O   1 
ATOM   1868 C  CB  . VAL   B 1 96  ? 41.525 -25.846 12.034 1.00 14.87  ? 102 VAL   C CB  1 
ATOM   1869 C  CG1 . VAL   B 1 96  ? 41.997 -26.034 10.589 1.00 16.96  ? 102 VAL   C CG1 1 
ATOM   1870 C  CG2 . VAL   B 1 96  ? 42.501 -25.017 12.856 1.00 16.21  ? 102 VAL   C CG2 1 
ATOM   1871 N  N   . GLY   B 1 97  ? 38.492 -25.255 10.248 1.00 15.00  ? 103 GLY   C N   1 
ATOM   1872 C  CA  . GLY   B 1 97  ? 37.462 -25.883 9.426  1.00 16.49  ? 103 GLY   C CA  1 
ATOM   1873 C  C   . GLY   B 1 97  ? 36.781 -24.912 8.507  1.00 15.64  ? 103 GLY   C C   1 
ATOM   1874 O  O   . GLY   B 1 97  ? 37.069 -23.696 8.520  1.00 18.06  ? 103 GLY   C O   1 
ATOM   1875 N  N   . HIS   B 1 98  ? 35.890 -25.434 7.676  1.00 14.70  ? 104 HIS   C N   1 
ATOM   1876 C  CA  . HIS   B 1 98  ? 35.211 -24.639 6.683  1.00 14.78  ? 104 HIS   C CA  1 
ATOM   1877 C  C   . HIS   B 1 98  ? 33.934 -23.946 7.205  1.00 14.01  ? 104 HIS   C C   1 
ATOM   1878 O  O   . HIS   B 1 98  ? 33.106 -24.597 7.893  1.00 13.97  ? 104 HIS   C O   1 
ATOM   1879 C  CB  . HIS   B 1 98  ? 34.908 -25.510 5.480  1.00 17.85  ? 104 HIS   C CB  1 
ATOM   1880 C  CG  . HIS   B 1 98  ? 34.403 -24.692 4.364  1.00 19.62  ? 104 HIS   C CG  1 
ATOM   1881 N  ND1 . HIS   B 1 98  ? 35.216 -23.743 3.730  1.00 20.98  ? 104 HIS   C ND1 1 
ATOM   1882 C  CD2 . HIS   B 1 98  ? 33.146 -24.628 3.857  1.00 21.50  ? 104 HIS   C CD2 1 
ATOM   1883 C  CE1 . HIS   B 1 98  ? 34.416 -23.151 2.852  1.00 23.05  ? 104 HIS   C CE1 1 
ATOM   1884 N  NE2 . HIS   B 1 98  ? 33.172 -23.678 2.876  1.00 23.43  ? 104 HIS   C NE2 1 
ATOM   1885 N  N   . SER   B 1 99  ? 33.721 -22.695 6.850  1.00 15.13  ? 105 SER   C N   1 
ATOM   1886 C  CA  . SER   B 1 99  ? 32.498 -21.956 7.234  1.00 15.15  ? 105 SER   C CA  1 
ATOM   1887 C  C   . SER   B 1 99  ? 32.289 -20.767 6.243  1.00 17.09  ? 105 SER   C C   1 
ATOM   1888 O  O   . SER   B 1 99  ? 33.165 -19.887 6.144  1.00 20.15  ? 105 SER   C O   1 
ATOM   1889 C  CB  . SER   B 1 99  ? 32.714 -21.395 8.623  1.00 16.49  ? 105 SER   C CB  1 
ATOM   1890 O  OG  . SER   B 1 99  ? 31.598 -20.551 8.940  1.00 16.25  ? 105 SER   C OG  1 
ATOM   1891 N  N   . GLU   B 1 100 ? 31.205 -20.786 5.570  1.00 17.03  ? 106 GLU   C N   1 
ATOM   1892 C  CA  . GLU   B 1 100 ? 30.750 -19.710 4.676  1.00 18.01  ? 106 GLU   C CA  1 
ATOM   1893 C  C   . GLU   B 1 100 ? 29.552 -19.064 5.310  1.00 16.50  ? 106 GLU   C C   1 
ATOM   1894 O  O   . GLU   B 1 100 ? 28.975 -19.588 6.243  1.00 15.50  ? 106 GLU   C O   1 
ATOM   1895 C  CB  . GLU   B 1 100 ? 30.234 -20.371 3.398  1.00 21.39  ? 106 GLU   C CB  1 
ATOM   1896 C  CG  . GLU   B 1 100 ? 31.389 -20.942 2.642  1.00 28.58  ? 106 GLU   C CG  1 
ATOM   1897 C  CD  . GLU   B 1 100 ? 31.036 -21.585 1.329  1.00 33.02  ? 106 GLU   C CD  1 
ATOM   1898 O  OE1 . GLU   B 1 100 ? 30.067 -21.142 0.675  1.00 40.92  ? 106 GLU   C OE1 1 
ATOM   1899 O  OE2 . GLU   B 1 100 ? 31.764 -22.515 0.937  1.00 31.72  ? 106 GLU   C OE2 1 
ATOM   1900 N  N   . PRO   B 1 101 ? 29.103 -17.891 4.802  1.00 17.34  ? 107 PRO   C N   1 
ATOM   1901 C  CA  . PRO   B 1 101 ? 27.993 -17.200 5.474  1.00 16.34  ? 107 PRO   C CA  1 
ATOM   1902 C  C   . PRO   B 1 101 ? 26.738 -18.073 5.620  1.00 16.36  ? 107 PRO   C C   1 
ATOM   1903 O  O   . PRO   B 1 101 ? 26.136 -18.008 6.660  1.00 16.16  ? 107 PRO   C O   1 
ATOM   1904 C  CB  . PRO   B 1 101 ? 27.720 -15.975 4.550  1.00 18.56  ? 107 PRO   C CB  1 
ATOM   1905 C  CG  . PRO   B 1 101 ? 28.986 -15.778 3.865  1.00 22.34  ? 107 PRO   C CG  1 
ATOM   1906 C  CD  . PRO   B 1 101 ? 29.737 -17.056 3.749  1.00 19.97  ? 107 PRO   C CD  1 
ATOM   1907 N  N   . GLY   B 1 102 ? 26.379 -18.884 4.628  1.00 16.47  ? 108 GLY   C N   1 
ATOM   1908 C  CA  . GLY   B 1 102 ? 25.184 -19.722 4.706  1.00 16.46  ? 108 GLY   C CA  1 
ATOM   1909 C  C   . GLY   B 1 102 ? 25.298 -20.797 5.781  1.00 15.03  ? 108 GLY   C C   1 
ATOM   1910 O  O   . GLY   B 1 102 ? 24.305 -21.465 6.103  1.00 16.30  ? 108 GLY   C O   1 
ATOM   1911 N  N   . ASP   B 1 103 ? 26.522 -21.104 6.277  1.00 14.30  ? 109 ASP   C N   1 
ATOM   1912 C  CA  . ASP   B 1 103 ? 26.704 -22.118 7.321  1.00 13.11  ? 109 ASP   C CA  1 
ATOM   1913 C  C   . ASP   B 1 103 ? 26.282 -21.641 8.701  1.00 12.69  ? 109 ASP   C C   1 
ATOM   1914 O  O   . ASP   B 1 103 ? 26.178 -22.427 9.640  1.00 12.44  ? 109 ASP   C O   1 
ATOM   1915 C  CB  . ASP   B 1 103 ? 28.163 -22.579 7.363  1.00 14.58  ? 109 ASP   C CB  1 
ATOM   1916 C  CG  . ASP   B 1 103 ? 28.513 -23.352 6.136  1.00 15.26  ? 109 ASP   C CG  1 
ATOM   1917 O  OD1 . ASP   B 1 103 ? 27.675 -24.114 5.657  1.00 15.56  ? 109 ASP   C OD1 1 
ATOM   1918 O  OD2 . ASP   B 1 103 ? 29.649 -23.170 5.619  1.00 16.55  ? 109 ASP   C OD2 1 
ATOM   1919 N  N   . CYS   B 1 104 ? 26.098 -20.307 8.892  1.00 12.23  ? 110 CYS   C N   1 
ATOM   1920 C  CA  . CYS   B 1 104 ? 25.653 -19.785 10.200 1.00 11.80  ? 110 CYS   C CA  1 
ATOM   1921 C  C   . CYS   B 1 104 ? 24.414 -20.476 10.668 1.00 12.00  ? 110 CYS   C C   1 
ATOM   1922 O  O   . CYS   B 1 104 ? 23.487 -20.693 9.874  1.00 13.52  ? 110 CYS   C O   1 
ATOM   1923 C  CB  . CYS   B 1 104 ? 25.435 -18.273 10.132 1.00 12.52  ? 110 CYS   C CB  1 
ATOM   1924 S  SG  . CYS   B 1 104 ? 26.971 -17.291 10.040 1.00 14.90  ? 110 CYS   C SG  1 
ATOM   1925 N  N   . GLY   B 1 105 ? 24.408 -20.835 11.937 1.00 10.74  ? 111 GLY   C N   1 
ATOM   1926 C  CA  . GLY   B 1 105 ? 23.263 -21.517 12.546 1.00 11.83  ? 111 GLY   C CA  1 
ATOM   1927 C  C   . GLY   B 1 105 ? 23.488 -23.024 12.695 1.00 11.37  ? 111 GLY   C C   1 
ATOM   1928 O  O   . GLY   B 1 105 ? 22.716 -23.693 13.400 1.00 12.47  ? 111 GLY   C O   1 
ATOM   1929 N  N   . GLY   B 1 106 ? 24.503 -23.579 12.023 1.00 11.88  ? 112 GLY   C N   1 
ATOM   1930 C  CA  . GLY   B 1 106 ? 24.820 -25.016 12.178 1.00 12.14  ? 112 GLY   C CA  1 
ATOM   1931 C  C   . GLY   B 1 106 ? 25.217 -25.316 13.626 1.00 10.56  ? 112 GLY   C C   1 
ATOM   1932 O  O   . GLY   B 1 106 ? 25.948 -24.525 14.259 1.00 10.93  ? 112 GLY   C O   1 
ATOM   1933 N  N   . ILE   B 1 107 ? 24.764 -26.446 14.139 1.00 10.67  ? 113 ILE   C N   1 
ATOM   1934 C  CA  . ILE   B 1 107 ? 25.018 -26.778 15.544 1.00 10.31  ? 113 ILE   C CA  1 
ATOM   1935 C  C   . ILE   B 1 107 ? 26.394 -27.408 15.747 1.00 9.91   ? 113 ILE   C C   1 
ATOM   1936 O  O   . ILE   B 1 107 ? 26.823 -28.259 14.974 1.00 10.21  ? 113 ILE   C O   1 
ATOM   1937 C  CB  . ILE   B 1 107 ? 23.913 -27.761 16.047 1.00 12.59  ? 113 ILE   C CB  1 
ATOM   1938 C  CG1 . ILE   B 1 107 ? 22.657 -26.841 16.436 1.00 16.95  ? 113 ILE   C CG1 1 
ATOM   1939 C  CG2 . ILE   B 1 107 ? 24.330 -28.614 17.246 1.00 12.29  ? 113 ILE   C CG2 1 
ATOM   1940 C  CD1 . ILE   B 1 107 ? 21.313 -27.545 16.797 1.00 20.98  ? 113 ILE   C CD1 1 
ATOM   1941 N  N   . LEU   B 1 108 ? 27.056 -26.968 16.844 1.00 9.32   ? 114 LEU   C N   1 
ATOM   1942 C  CA  . LEU   B 1 108 ? 28.232 -27.656 17.419 1.00 9.11   ? 114 LEU   C CA  1 
ATOM   1943 C  C   . LEU   B 1 108 ? 27.710 -28.407 18.659 1.00 9.57   ? 114 LEU   C C   1 
ATOM   1944 O  O   . LEU   B 1 108 ? 27.057 -27.794 19.511 1.00 9.91   ? 114 LEU   C O   1 
ATOM   1945 C  CB  . LEU   B 1 108 ? 29.237 -26.580 17.859 1.00 10.01  ? 114 LEU   C CB  1 
ATOM   1946 C  CG  . LEU   B 1 108 ? 30.459 -27.097 18.637 1.00 10.47  ? 114 LEU   C CG  1 
ATOM   1947 C  CD1 . LEU   B 1 108 ? 31.368 -28.001 17.783 1.00 11.52  ? 114 LEU   C CD1 1 
ATOM   1948 C  CD2 . LEU   B 1 108 ? 31.267 -25.908 19.161 1.00 11.70  ? 114 LEU   C CD2 1 
ATOM   1949 N  N   . ARG   B 1 109 ? 28.005 -29.698 18.724 1.00 9.61   ? 115 ARG   C N   1 
ATOM   1950 C  CA  . ARG   B 1 109 ? 27.511 -30.515 19.852 1.00 9.85   ? 115 ARG   C CA  1 
ATOM   1951 C  C   . ARG   B 1 109 ? 28.679 -31.350 20.429 1.00 10.03  ? 115 ARG   C C   1 
ATOM   1952 O  O   . ARG   B 1 109 ? 29.606 -31.760 19.723 1.00 11.30  ? 115 ARG   C O   1 
ATOM   1953 C  CB  . ARG   B 1 109 ? 26.381 -31.478 19.377 1.00 12.68  ? 115 ARG   C CB  1 
ATOM   1954 C  CG  . ARG   B 1 109 ? 26.859 -32.476 18.322 1.00 15.10  ? 115 ARG   C CG  1 
ATOM   1955 C  CD  . ARG   B 1 109 ? 25.735 -33.405 17.850 1.00 18.28  ? 115 ARG   C CD  1 
ATOM   1956 N  NE  . ARG   B 1 109 ? 24.875 -32.647 16.946 1.00 21.88  ? 115 ARG   C NE  1 
ATOM   1957 C  CZ  . ARG   B 1 109 ? 23.552 -32.657 16.997 1.00 27.92  ? 115 ARG   C CZ  1 
ATOM   1958 N  NH1 . ARG   B 1 109 ? 22.922 -33.377 17.920 1.00 30.17  ? 115 ARG   C NH1 1 
ATOM   1959 N  NH2 . ARG   B 1 109 ? 22.843 -31.949 16.122 1.00 31.00  ? 115 ARG   C NH2 1 
ATOM   1960 N  N   . CYS   B 1 110 ? 28.580 -31.609 21.745 1.00 10.44  ? 116 CYS   C N   1 
ATOM   1961 C  CA  . CYS   B 1 110 ? 29.564 -32.486 22.444 1.00 12.21  ? 116 CYS   C CA  1 
ATOM   1962 C  C   . CYS   B 1 110 ? 28.695 -33.594 23.094 1.00 13.57  ? 116 CYS   C C   1 
ATOM   1963 O  O   . CYS   B 1 110 ? 27.464 -33.692 22.901 1.00 13.14  ? 116 CYS   C O   1 
ATOM   1964 C  CB  . CYS   B 1 110 ? 30.339 -31.693 23.506 1.00 12.20  ? 116 CYS   C CB  1 
ATOM   1965 S  SG  . CYS   B 1 110 ? 29.275 -31.074 24.829 1.00 12.14  ? 116 CYS   C SG  1 
ATOM   1966 N  N   . GLN   B 1 111 ? 29.330 -34.440 23.941 1.00 14.01  ? 117 GLN   C N   1 
ATOM   1967 C  CA  . GLN   B 1 111 ? 28.572 -35.480 24.626 1.00 15.36  ? 117 GLN   C CA  1 
ATOM   1968 C  C   . GLN   B 1 111 ? 27.504 -34.955 25.553 1.00 15.57  ? 117 GLN   C C   1 
ATOM   1969 O  O   . GLN   B 1 111 ? 26.542 -35.694 25.889 1.00 18.42  ? 117 GLN   C O   1 
ATOM   1970 C  CB  . GLN   B 1 111 ? 29.500 -36.422 25.426 1.00 16.72  ? 117 GLN   C CB  1 
ATOM   1971 C  CG  . GLN   B 1 111 ? 30.137 -35.733 26.638 1.00 17.11  ? 117 GLN   C CG  1 
ATOM   1972 C  CD  . GLN   B 1 111 ? 31.063 -36.660 27.377 1.00 29.54  ? 117 GLN   C CD  1 
ATOM   1973 O  OE1 . GLN   B 1 111 ? 32.265 -36.707 27.099 1.00 33.77  ? 117 GLN   C OE1 1 
ATOM   1974 N  NE2 . GLN   B 1 111 ? 30.518 -37.376 28.319 1.00 29.66  ? 117 GLN   C NE2 1 
ATOM   1975 N  N   . HIS   B 1 112 ? 27.569 -33.649 25.960 1.00 13.94  ? 118 HIS   C N   1 
ATOM   1976 C  CA  . HIS   B 1 112 ? 26.567 -33.130 26.897 1.00 14.96  ? 118 HIS   C CA  1 
ATOM   1977 C  C   . HIS   B 1 112 ? 25.388 -32.439 26.211 1.00 15.59  ? 118 HIS   C C   1 
ATOM   1978 O  O   . HIS   B 1 112 ? 24.450 -32.016 26.898 1.00 16.20  ? 118 HIS   C O   1 
ATOM   1979 C  CB  . HIS   B 1 112 ? 27.255 -32.140 27.867 1.00 15.57  ? 118 HIS   C CB  1 
ATOM   1980 C  CG  . HIS   B 1 112 ? 28.445 -32.753 28.577 1.00 13.75  ? 118 HIS   C CG  1 
ATOM   1981 N  ND1 . HIS   B 1 112 ? 29.756 -32.486 28.216 1.00 13.83  ? 118 HIS   C ND1 1 
ATOM   1982 C  CD2 . HIS   B 1 112 ? 28.465 -33.570 29.673 1.00 16.30  ? 118 HIS   C CD2 1 
ATOM   1983 C  CE1 . HIS   B 1 112 ? 30.524 -33.208 29.033 1.00 14.62  ? 118 HIS   C CE1 1 
ATOM   1984 N  NE2 . HIS   B 1 112 ? 29.783 -33.862 29.913 1.00 17.66  ? 118 HIS   C NE2 1 
ATOM   1985 N  N   . GLY   B 1 113 ? 25.467 -32.185 24.889 1.00 13.93  ? 119 GLY   C N   1 
ATOM   1986 C  CA  . GLY   B 1 113 ? 24.400 -31.469 24.196 1.00 14.05  ? 119 GLY   C CA  1 
ATOM   1987 C  C   . GLY   B 1 113 ? 24.943 -30.409 23.263 1.00 12.42  ? 119 GLY   C C   1 
ATOM   1988 O  O   . GLY   B 1 113 ? 26.092 -30.490 22.769 1.00 12.03  ? 119 GLY   C O   1 
ATOM   1989 N  N   . VAL   B 1 114 ? 24.099 -29.393 23.016 1.00 12.52  ? 120 VAL   C N   1 
ATOM   1990 C  CA  . VAL   B 1 114 ? 24.441 -28.329 22.069 1.00 12.35  ? 120 VAL   C CA  1 
ATOM   1991 C  C   . VAL   B 1 114 ? 25.343 -27.337 22.753 1.00 11.56  ? 120 VAL   C C   1 
ATOM   1992 O  O   . VAL   B 1 114 ? 25.030 -26.764 23.819 1.00 12.51  ? 120 VAL   C O   1 
ATOM   1993 C  CB  . VAL   B 1 114 ? 23.153 -27.641 21.573 1.00 13.15  ? 120 VAL   C CB  1 
ATOM   1994 C  CG1 . VAL   B 1 114 ? 23.504 -26.434 20.702 1.00 14.27  ? 120 VAL   C CG1 1 
ATOM   1995 C  CG2 . VAL   B 1 114 ? 22.241 -28.628 20.825 1.00 15.55  ? 120 VAL   C CG2 1 
ATOM   1996 N  N   . VAL   B 1 115 ? 26.504 -27.078 22.165 1.00 10.30  ? 121 VAL   C N   1 
ATOM   1997 C  CA  . VAL   B 1 115 ? 27.509 -26.130 22.656 1.00 10.61  ? 121 VAL   C CA  1 
ATOM   1998 C  C   . VAL   B 1 115 ? 27.274 -24.731 22.145 1.00 11.40  ? 121 VAL   C C   1 
ATOM   1999 O  O   . VAL   B 1 115 ? 27.490 -23.745 22.863 1.00 11.65  ? 121 VAL   C O   1 
ATOM   2000 C  CB  . VAL   B 1 115 ? 28.914 -26.651 22.277 1.00 11.11  ? 121 VAL   C CB  1 
ATOM   2001 C  CG1 . VAL   B 1 115 ? 29.986 -25.631 22.640 1.00 12.05  ? 121 VAL   C CG1 1 
ATOM   2002 C  CG2 . VAL   B 1 115 ? 29.207 -28.031 22.882 1.00 12.98  ? 121 VAL   C CG2 1 
ATOM   2003 N  N   . GLY   B 1 116 ? 26.916 -24.603 20.860 1.00 10.92  ? 122 GLY   C N   1 
ATOM   2004 C  CA  . GLY   B 1 116 ? 26.712 -23.283 20.262 1.00 12.54  ? 122 GLY   C CA  1 
ATOM   2005 C  C   . GLY   B 1 116 ? 26.410 -23.456 18.777 1.00 10.48  ? 122 GLY   C C   1 
ATOM   2006 O  O   . GLY   B 1 116 ? 26.104 -24.571 18.332 1.00 11.31  ? 122 GLY   C O   1 
ATOM   2007 N  N   . ILE   B 1 117 ? 26.392 -22.305 18.044 1.00 9.83   ? 123 ILE   C N   1 
ATOM   2008 C  CA  . ILE   B 1 117 ? 26.060 -22.330 16.624 1.00 9.89   ? 123 ILE   C CA  1 
ATOM   2009 C  C   . ILE   B 1 117 ? 27.108 -21.614 15.834 1.00 10.29  ? 123 ILE   C C   1 
ATOM   2010 O  O   . ILE   B 1 117 ? 27.733 -20.649 16.323 1.00 11.33  ? 123 ILE   C O   1 
ATOM   2011 C  CB  . ILE   B 1 117 ? 24.643 -21.705 16.349 1.00 11.14  ? 123 ILE   C CB  1 
ATOM   2012 C  CG1 . ILE   B 1 117 ? 24.510 -20.321 17.000 1.00 12.84  ? 123 ILE   C CG1 1 
ATOM   2013 C  CG2 . ILE   B 1 117 ? 23.526 -22.685 16.748 1.00 12.94  ? 123 ILE   C CG2 1 
ATOM   2014 C  CD1 . ILE   B 1 117 ? 23.175 -19.568 16.555 1.00 13.10  ? 123 ILE   C CD1 1 
ATOM   2015 N  N   . VAL   B 1 118 ? 27.306 -22.017 14.576 1.00 9.77   ? 124 VAL   C N   1 
ATOM   2016 C  CA  . VAL   B 1 118 ? 28.241 -21.333 13.687 1.00 10.26  ? 124 VAL   C CA  1 
ATOM   2017 C  C   . VAL   B 1 118 ? 27.867 -19.850 13.561 1.00 10.78  ? 124 VAL   C C   1 
ATOM   2018 O  O   . VAL   B 1 118 ? 26.671 -19.515 13.348 1.00 10.59  ? 124 VAL   C O   1 
ATOM   2019 C  CB  . VAL   B 1 118 ? 28.248 -21.966 12.292 1.00 10.63  ? 124 VAL   C CB  1 
ATOM   2020 C  CG1 . VAL   B 1 118 ? 29.108 -21.191 11.292 1.00 11.55  ? 124 VAL   C CG1 1 
ATOM   2021 C  CG2 . VAL   B 1 118 ? 28.722 -23.438 12.335 1.00 11.28  ? 124 VAL   C CG2 1 
ATOM   2022 N  N   . SER   B 1 119 ? 28.865 -18.969 13.686 1.00 11.05  ? 125 SER   C N   1 
ATOM   2023 C  CA  . SER   B 1 119 ? 28.660 -17.509 13.584 1.00 11.78  ? 125 SER   C CA  1 
ATOM   2024 C  C   . SER   B 1 119 ? 29.692 -16.818 12.693 1.00 12.44  ? 125 SER   C C   1 
ATOM   2025 O  O   . SER   B 1 119 ? 29.354 -15.736 12.171 1.00 13.08  ? 125 SER   C O   1 
ATOM   2026 C  CB  . SER   B 1 119 ? 28.661 -16.932 15.001 1.00 12.43  ? 125 SER   C CB  1 
ATOM   2027 O  OG  . SER   B 1 119 ? 28.564 -15.501 14.974 1.00 13.96  ? 125 SER   C OG  1 
ATOM   2028 N  N   . THR   B 1 120 ? 30.941 -17.338 12.567 1.00 12.82  ? 126 THR   C N   1 
ATOM   2029 C  CA  . THR   B 1 120 ? 31.974 -16.657 11.768 1.00 12.74  ? 126 THR   C CA  1 
ATOM   2030 C  C   . THR   B 1 120 ? 32.680 -17.666 10.862 1.00 12.21  ? 126 THR   C C   1 
ATOM   2031 O  O   . THR   B 1 120 ? 32.608 -18.902 11.095 1.00 12.33  ? 126 THR   C O   1 
ATOM   2032 C  CB  . THR   B 1 120 ? 33.051 -15.969 12.658 1.00 13.89  ? 126 THR   C CB  1 
ATOM   2033 O  OG1 . THR   B 1 120 ? 33.881 -16.917 13.299 1.00 13.92  ? 126 THR   C OG1 1 
ATOM   2034 C  CG2 . THR   B 1 120 ? 32.454 -15.010 13.655 1.00 15.42  ? 126 THR   C CG2 1 
ATOM   2035 N  N   . GLY   B 1 121 ? 33.366 -17.156 9.861  1.00 13.30  ? 127 GLY   C N   1 
ATOM   2036 C  CA  . GLY   B 1 121 ? 34.127 -18.007 8.954  1.00 16.07  ? 127 GLY   C CA  1 
ATOM   2037 C  C   . GLY   B 1 121 ? 35.168 -17.230 8.185  1.00 18.19  ? 127 GLY   C C   1 
ATOM   2038 O  O   . GLY   B 1 121 ? 35.002 -16.036 7.968  1.00 22.18  ? 127 GLY   C O   1 
ATOM   2039 N  N   . GLY   B 1 122 ? 36.057 -17.924 7.534  1.00 21.65  ? 128 GLY   C N   1 
ATOM   2040 C  CA  . GLY   B 1 122 ? 37.126 -17.273 6.758  1.00 23.49  ? 128 GLY   C CA  1 
ATOM   2041 C  C   . GLY   B 1 122 ? 38.505 -17.720 7.236  1.00 23.08  ? 128 GLY   C C   1 
ATOM   2042 O  O   . GLY   B 1 122 ? 38.702 -18.146 8.370  1.00 23.67  ? 128 GLY   C O   1 
ATOM   2043 N  N   . ASN   B 1 123 ? 39.522 -17.544 6.386  1.00 22.48  ? 129 ASN   C N   1 
ATOM   2044 C  CA  . ASN   B 1 123 ? 40.915 -17.923 6.659  1.00 24.13  ? 129 ASN   C CA  1 
ATOM   2045 C  C   . ASN   B 1 123 ? 41.057 -19.341 7.166  1.00 22.05  ? 129 ASN   C C   1 
ATOM   2046 O  O   . ASN   B 1 123 ? 41.987 -19.632 7.930  1.00 24.88  ? 129 ASN   C O   1 
ATOM   2047 C  CB  . ASN   B 1 123 ? 41.637 -16.930 7.617  1.00 29.73  ? 129 ASN   C CB  1 
ATOM   2048 C  CG  . ASN   B 1 123 ? 42.457 -15.854 6.933  1.00 39.50  ? 129 ASN   C CG  1 
ATOM   2049 O  OD1 . ASN   B 1 123 ? 42.797 -15.940 5.745  1.00 41.75  ? 129 ASN   C OD1 1 
ATOM   2050 N  ND2 . ASN   B 1 123 ? 42.817 -14.809 7.664  1.00 41.74  ? 129 ASN   C ND2 1 
ATOM   2051 N  N   . GLY   B 1 124 ? 40.169 -20.244 6.737  1.00 19.95  ? 130 GLY   C N   1 
ATOM   2052 C  CA  . GLY   B 1 124 ? 40.255 -21.651 7.177  1.00 18.77  ? 130 GLY   C CA  1 
ATOM   2053 C  C   . GLY   B 1 124 ? 39.832 -21.909 8.602  1.00 16.18  ? 130 GLY   C C   1 
ATOM   2054 O  O   . GLY   B 1 124 ? 40.132 -22.987 9.120  1.00 16.77  ? 130 GLY   C O   1 
ATOM   2055 N  N   . LEU   B 1 125 ? 39.179 -20.937 9.228  1.00 15.02  ? 131 LEU   C N   1 
ATOM   2056 C  CA  . LEU   B 1 125 ? 38.675 -21.085 10.588 1.00 15.05  ? 131 LEU   C CA  1 
ATOM   2057 C  C   . LEU   B 1 125 ? 37.134 -20.961 10.618 1.00 14.93  ? 131 LEU   C C   1 
ATOM   2058 O  O   . LEU   B 1 125 ? 36.529 -20.237 9.821  1.00 17.66  ? 131 LEU   C O   1 
ATOM   2059 C  CB  . LEU   B 1 125 ? 39.261 -20.026 11.534 1.00 18.05  ? 131 LEU   C CB  1 
ATOM   2060 C  CG  . LEU   B 1 125 ? 40.804 -20.002 11.573 1.00 21.39  ? 131 LEU   C CG  1 
ATOM   2061 C  CD1 . LEU   B 1 125 ? 41.351 -18.606 11.939 1.00 26.53  ? 131 LEU   C CD1 1 
ATOM   2062 C  CD2 . LEU   B 1 125 ? 41.340 -21.185 12.316 1.00 21.26  ? 131 LEU   C CD2 1 
ATOM   2063 N  N   . VAL   B 1 126 ? 36.549 -21.651 11.524 1.00 12.34  ? 132 VAL   C N   1 
ATOM   2064 C  CA  . VAL   B 1 126 ? 35.111 -21.570 11.795 1.00 12.25  ? 132 VAL   C CA  1 
ATOM   2065 C  C   . VAL   B 1 126 ? 34.969 -21.084 13.232 1.00 10.95  ? 132 VAL   C C   1 
ATOM   2066 O  O   . VAL   B 1 126 ? 35.619 -21.610 14.144 1.00 12.27  ? 132 VAL   C O   1 
ATOM   2067 C  CB  . VAL   B 1 126 ? 34.379 -22.916 11.560 1.00 11.92  ? 132 VAL   C CB  1 
ATOM   2068 C  CG1 . VAL   B 1 126 ? 35.038 -24.083 12.233 1.00 13.59  ? 132 VAL   C CG1 1 
ATOM   2069 C  CG2 . VAL   B 1 126 ? 32.880 -22.820 11.907 1.00 12.98  ? 132 VAL   C CG2 1 
ATOM   2070 N  N   . GLY   B 1 127 ? 34.075 -20.118 13.430 1.00 11.77  ? 133 GLY   C N   1 
ATOM   2071 C  CA  . GLY   B 1 127 ? 33.790 -19.594 14.782 1.00 11.83  ? 133 GLY   C CA  1 
ATOM   2072 C  C   . GLY   B 1 127 ? 32.365 -19.940 15.216 1.00 11.37  ? 133 GLY   C C   1 
ATOM   2073 O  O   . GLY   B 1 127 ? 31.425 -19.785 14.405 1.00 11.44  ? 133 GLY   C O   1 
ATOM   2074 N  N   . PHE   B 1 128 ? 32.231 -20.287 16.483 1.00 11.15  ? 134 PHE   C N   1 
ATOM   2075 C  CA  . PHE   B 1 128 ? 30.942 -20.674 17.088 1.00 10.95  ? 134 PHE   C CA  1 
ATOM   2076 C  C   . PHE   B 1 128 ? 30.588 -19.737 18.231 1.00 10.80  ? 134 PHE   C C   1 
ATOM   2077 O  O   . PHE   B 1 128 ? 31.426 -19.471 19.092 1.00 11.63  ? 134 PHE   C O   1 
ATOM   2078 C  CB  . PHE   B 1 128 ? 30.999 -22.127 17.671 1.00 11.07  ? 134 PHE   C CB  1 
ATOM   2079 C  CG  . PHE   B 1 128 ? 31.541 -23.141 16.672 1.00 11.24  ? 134 PHE   C CG  1 
ATOM   2080 C  CD1 . PHE   B 1 128 ? 30.707 -23.735 15.728 1.00 10.88  ? 134 PHE   C CD1 1 
ATOM   2081 C  CD2 . PHE   B 1 128 ? 32.883 -23.504 16.689 1.00 11.65  ? 134 PHE   C CD2 1 
ATOM   2082 C  CE1 . PHE   B 1 128 ? 31.189 -24.675 14.852 1.00 11.51  ? 134 PHE   C CE1 1 
ATOM   2083 C  CE2 . PHE   B 1 128 ? 33.376 -24.466 15.795 1.00 12.24  ? 134 PHE   C CE2 1 
ATOM   2084 C  CZ  . PHE   B 1 128 ? 32.533 -25.050 14.888 1.00 11.60  ? 134 PHE   C CZ  1 
ATOM   2085 N  N   . ALA   B 1 129 ? 29.338 -19.261 18.230 1.00 11.26  ? 135 ALA   C N   1 
ATOM   2086 C  CA  . ALA   B 1 129 ? 28.821 -18.475 19.343 1.00 11.71  ? 135 ALA   C CA  1 
ATOM   2087 C  C   . ALA   B 1 129 ? 28.424 -19.471 20.475 1.00 11.64  ? 135 ALA   C C   1 
ATOM   2088 O  O   . ALA   B 1 129 ? 27.518 -20.311 20.298 1.00 11.86  ? 135 ALA   C O   1 
ATOM   2089 C  CB  . ALA   B 1 129 ? 27.601 -17.671 18.888 1.00 11.87  ? 135 ALA   C CB  1 
ATOM   2090 N  N   . ASP   B 1 130 ? 29.102 -19.371 21.623 1.00 11.46  ? 136 ASP   C N   1 
ATOM   2091 C  CA  . ASP   B 1 130 ? 28.808 -20.256 22.751 1.00 11.99  ? 136 ASP   C CA  1 
ATOM   2092 C  C   . ASP   B 1 130 ? 27.452 -19.948 23.344 1.00 12.43  ? 136 ASP   C C   1 
ATOM   2093 O  O   . ASP   B 1 130 ? 27.051 -18.756 23.406 1.00 13.33  ? 136 ASP   C O   1 
ATOM   2094 C  CB  . ASP   B 1 130 ? 29.869 -20.034 23.835 1.00 13.48  ? 136 ASP   C CB  1 
ATOM   2095 C  CG  . ASP   B 1 130 ? 29.743 -20.954 25.033 1.00 15.17  ? 136 ASP   C CG  1 
ATOM   2096 O  OD1 . ASP   B 1 130 ? 29.648 -22.174 24.850 1.00 15.59  ? 136 ASP   C OD1 1 
ATOM   2097 O  OD2 . ASP   B 1 130 ? 29.638 -20.420 26.168 1.00 19.24  ? 136 ASP   C OD2 1 
ATOM   2098 N  N   . VAL   B 1 131 ? 26.748 -20.972 23.804 1.00 12.75  ? 137 VAL   C N   1 
ATOM   2099 C  CA  . VAL   B 1 131 ? 25.492 -20.794 24.565 1.00 12.75  ? 137 VAL   C CA  1 
ATOM   2100 C  C   . VAL   B 1 131 ? 25.547 -21.480 25.934 1.00 12.97  ? 137 VAL   C C   1 
ATOM   2101 O  O   . VAL   B 1 131 ? 24.550 -21.438 26.670 1.00 14.03  ? 137 VAL   C O   1 
ATOM   2102 C  CB  . VAL   B 1 131 ? 24.231 -21.265 23.801 1.00 13.51  ? 137 VAL   C CB  1 
ATOM   2103 C  CG1 . VAL   B 1 131 ? 24.062 -20.451 22.500 1.00 13.40  ? 137 VAL   C CG1 1 
ATOM   2104 C  CG2 . VAL   B 1 131 ? 24.264 -22.747 23.490 1.00 14.12  ? 137 VAL   C CG2 1 
ATOM   2105 N  N   . ARG   B 1 132 ? 26.679 -22.126 26.304 1.00 12.74  ? 138 ARG   C N   1 
ATOM   2106 C  CA  . ARG   B 1 132 ? 26.722 -22.916 27.543 1.00 13.10  ? 138 ARG   C CA  1 
ATOM   2107 C  C   . ARG   B 1 132 ? 26.647 -22.073 28.807 1.00 13.90  ? 138 ARG   C C   1 
ATOM   2108 O  O   . ARG   B 1 132 ? 26.314 -22.643 29.867 1.00 15.17  ? 138 ARG   C O   1 
ATOM   2109 C  CB  . ARG   B 1 132 ? 27.984 -23.774 27.552 1.00 13.11  ? 138 ARG   C CB  1 
ATOM   2110 C  CG  . ARG   B 1 132 ? 27.991 -24.847 26.428 1.00 12.55  ? 138 ARG   C CG  1 
ATOM   2111 C  CD  . ARG   B 1 132 ? 29.316 -25.577 26.482 1.00 12.43  ? 138 ARG   C CD  1 
ATOM   2112 N  NE  . ARG   B 1 132 ? 30.406 -24.677 26.108 1.00 12.35  ? 138 ARG   C NE  1 
ATOM   2113 C  CZ  . ARG   B 1 132 ? 31.656 -25.040 25.951 1.00 12.92  ? 138 ARG   C CZ  1 
ATOM   2114 N  NH1 . ARG   B 1 132 ? 32.047 -26.282 26.273 1.00 13.85  ? 138 ARG   C NH1 1 
ATOM   2115 N  NH2 . ARG   B 1 132 ? 32.538 -24.176 25.467 1.00 13.68  ? 138 ARG   C NH2 1 
ATOM   2116 N  N   . ASP   B 1 133 ? 26.958 -20.770 28.750 1.00 14.01  ? 139 ASP   C N   1 
ATOM   2117 C  CA  . ASP   B 1 133 ? 26.866 -19.903 29.926 1.00 15.12  ? 139 ASP   C CA  1 
ATOM   2118 C  C   . ASP   B 1 133 ? 25.446 -19.346 30.125 1.00 16.12  ? 139 ASP   C C   1 
ATOM   2119 O  O   . ASP   B 1 133 ? 25.211 -18.700 31.153 1.00 17.51  ? 139 ASP   C O   1 
ATOM   2120 C  CB  . ASP   B 1 133 ? 27.825 -18.700 29.790 1.00 17.14  ? 139 ASP   C CB  1 
ATOM   2121 C  CG  . ASP   B 1 133 ? 27.480 -17.770 28.640 1.00 18.59  ? 139 ASP   C CG  1 
ATOM   2122 O  OD1 . ASP   B 1 133 ? 27.114 -18.267 27.548 1.00 17.50  ? 139 ASP   C OD1 1 
ATOM   2123 O  OD2 . ASP   B 1 133 ? 27.567 -16.523 28.828 1.00 21.25  ? 139 ASP   C OD2 1 
ATOM   2124 N  N   . LEU   B 1 134 ? 24.506 -19.572 29.178 1.00 14.76  ? 140 LEU   C N   1 
ATOM   2125 C  CA  . LEU   B 1 134 ? 23.142 -19.012 29.265 1.00 15.13  ? 140 LEU   C CA  1 
ATOM   2126 C  C   . LEU   B 1 134 ? 22.274 -19.999 30.030 1.00 15.24  ? 140 LEU   C C   1 
ATOM   2127 O  O   . LEU   B 1 134 ? 21.474 -20.742 29.464 1.00 15.55  ? 140 LEU   C O   1 
ATOM   2128 C  CB  . LEU   B 1 134 ? 22.602 -18.763 27.837 1.00 15.59  ? 140 LEU   C CB  1 
ATOM   2129 C  CG  . LEU   B 1 134 ? 23.445 -17.787 26.970 1.00 15.43  ? 140 LEU   C CG  1 
ATOM   2130 C  CD1 . LEU   B 1 134 ? 22.906 -17.744 25.519 1.00 16.42  ? 140 LEU   C CD1 1 
ATOM   2131 C  CD2 . LEU   B 1 134 ? 23.559 -16.374 27.605 1.00 17.13  ? 140 LEU   C CD2 1 
ATOM   2132 N  N   . LEU   B 1 135 ? 22.472 -20.045 31.367 1.00 16.35  ? 141 LEU   C N   1 
ATOM   2133 C  CA  . LEU   B 1 135 ? 21.851 -21.090 32.196 1.00 17.05  ? 141 LEU   C CA  1 
ATOM   2134 C  C   . LEU   B 1 135 ? 20.343 -20.996 32.229 1.00 17.50  ? 141 LEU   C C   1 
ATOM   2135 O  O   . LEU   B 1 135 ? 19.643 -21.992 32.397 1.00 18.66  ? 141 LEU   C O   1 
ATOM   2136 C  CB  . LEU   B 1 135 ? 22.390 -21.093 33.641 1.00 17.33  ? 141 LEU   C CB  1 
ATOM   2137 C  CG  . LEU   B 1 135 ? 23.939 -21.112 33.747 1.00 19.42  ? 141 LEU   C CG  1 
ATOM   2138 C  CD1 . LEU   B 1 135 ? 24.436 -21.150 35.221 1.00 21.92  ? 141 LEU   C CD1 1 
ATOM   2139 C  CD2 . LEU   B 1 135 ? 24.621 -22.214 32.900 1.00 19.98  ? 141 LEU   C CD2 1 
ATOM   2140 N  N   . TRP   B 1 136 ? 19.830 -19.779 32.034 1.00 16.62  ? 142 TRP   C N   1 
ATOM   2141 C  CA  . TRP   B 1 136 ? 18.381 -19.503 32.042 1.00 17.69  ? 142 TRP   C CA  1 
ATOM   2142 C  C   . TRP   B 1 136 ? 17.649 -20.214 30.894 1.00 19.20  ? 142 TRP   C C   1 
ATOM   2143 O  O   . TRP   B 1 136 ? 16.423 -20.353 30.934 1.00 19.93  ? 142 TRP   C O   1 
ATOM   2144 C  CB  . TRP   B 1 136 ? 18.079 -17.990 32.039 1.00 17.56  ? 142 TRP   C CB  1 
ATOM   2145 C  CG  . TRP   B 1 136 ? 18.791 -17.264 30.945 1.00 17.63  ? 142 TRP   C CG  1 
ATOM   2146 C  CD1 . TRP   B 1 136 ? 19.970 -16.578 31.035 1.00 18.65  ? 142 TRP   C CD1 1 
ATOM   2147 C  CD2 . TRP   B 1 136 ? 18.295 -17.038 29.605 1.00 17.42  ? 142 TRP   C CD2 1 
ATOM   2148 N  NE1 . TRP   B 1 136 ? 20.272 -15.999 29.814 1.00 18.75  ? 142 TRP   C NE1 1 
ATOM   2149 C  CE2 . TRP   B 1 136 ? 19.237 -16.239 28.937 1.00 17.88  ? 142 TRP   C CE2 1 
ATOM   2150 C  CE3 . TRP   B 1 136 ? 17.141 -17.425 28.932 1.00 18.11  ? 142 TRP   C CE3 1 
ATOM   2151 C  CZ2 . TRP   B 1 136 ? 19.062 -15.839 27.601 1.00 17.63  ? 142 TRP   C CZ2 1 
ATOM   2152 C  CZ3 . TRP   B 1 136 ? 16.931 -16.969 27.644 1.00 18.62  ? 142 TRP   C CZ3 1 
ATOM   2153 C  CH2 . TRP   B 1 136 ? 17.913 -16.229 26.976 1.00 18.55  ? 142 TRP   C CH2 1 
ATOM   2154 N  N   . LEU   B 1 137 ? 18.361 -20.664 29.841 1.00 18.11  ? 143 LEU   C N   1 
ATOM   2155 C  CA  . LEU   B 1 137 ? 17.687 -21.426 28.766 1.00 18.60  ? 143 LEU   C CA  1 
ATOM   2156 C  C   . LEU   B 1 137 ? 17.060 -22.715 29.308 1.00 21.74  ? 143 LEU   C C   1 
ATOM   2157 O  O   . LEU   B 1 137 ? 16.140 -23.235 28.685 1.00 23.45  ? 143 LEU   C O   1 
ATOM   2158 C  CB  . LEU   B 1 137 ? 18.670 -21.767 27.626 1.00 16.80  ? 143 LEU   C CB  1 
ATOM   2159 C  CG  . LEU   B 1 137 ? 19.126 -20.564 26.771 1.00 16.58  ? 143 LEU   C CG  1 
ATOM   2160 C  CD1 . LEU   B 1 137 ? 20.251 -20.995 25.822 1.00 17.58  ? 143 LEU   C CD1 1 
ATOM   2161 C  CD2 . LEU   B 1 137 ? 17.956 -20.007 25.889 1.00 17.87  ? 143 LEU   C CD2 1 
ATOM   2162 N  N   . ASP   B 1 138 ? 17.574 -23.227 30.450 1.00 21.22  ? 144 ASP   C N   1 
ATOM   2163 C  CA  . ASP   B 1 138 ? 17.106 -24.486 31.064 1.00 23.81  ? 144 ASP   C CA  1 
ATOM   2164 C  C   . ASP   B 1 138 ? 15.896 -24.319 31.960 1.00 26.38  ? 144 ASP   C C   1 
ATOM   2165 O  O   . ASP   B 1 138 ? 15.472 -25.324 32.524 1.00 28.48  ? 144 ASP   C O   1 
ATOM   2166 C  CB  . ASP   B 1 138 ? 18.209 -25.164 31.923 1.00 24.38  ? 144 ASP   C CB  1 
ATOM   2167 C  CG  . ASP   B 1 138 ? 19.488 -25.538 31.178 1.00 23.27  ? 144 ASP   C CG  1 
ATOM   2168 O  OD1 . ASP   B 1 138 ? 19.462 -25.599 29.931 1.00 24.61  ? 144 ASP   C OD1 1 
ATOM   2169 O  OD2 . ASP   B 1 138 ? 20.515 -25.740 31.850 1.00 27.28  ? 144 ASP   C OD2 1 
ATOM   2170 N  N   . GLU   B 1 139 ? 15.351 -23.109 32.121 1.00 26.06  ? 145 GLU   C N   1 
ATOM   2171 C  CA  . GLU   B 1 139 ? 14.244 -22.878 33.055 1.00 31.08  ? 145 GLU   C CA  1 
ATOM   2172 C  C   . GLU   B 1 139 ? 13.174 -21.922 32.488 1.00 35.94  ? 145 GLU   C C   1 
ATOM   2173 O  O   . GLU   B 1 139 ? 13.332 -21.412 31.381 1.00 36.81  ? 145 GLU   C O   1 
ATOM   2174 C  CB  . GLU   B 1 139 ? 14.842 -22.337 34.370 1.00 35.99  ? 145 GLU   C CB  1 
ATOM   2175 C  CG  . GLU   B 1 139 ? 15.550 -21.009 34.164 1.00 44.18  ? 145 GLU   C CG  1 
ATOM   2176 C  CD  . GLU   B 1 139 ? 16.451 -20.516 35.280 1.00 53.18  ? 145 GLU   C CD  1 
ATOM   2177 O  OE1 . GLU   B 1 139 ? 16.609 -19.278 35.407 1.00 54.59  ? 145 GLU   C OE1 1 
ATOM   2178 O  OE2 . GLU   B 1 139 ? 16.997 -21.364 36.023 1.00 55.98  ? 145 GLU   C OE2 1 
ATOM   2179 N  N   . GLU   B 1 140 ? 12.098 -21.668 33.284 1.00 39.01  ? 146 GLU   C N   1 
ATOM   2180 C  CA  . GLU   B 1 140 ? 10.935 -20.787 33.038 1.00 42.12  ? 146 GLU   C CA  1 
ATOM   2181 C  C   . GLU   B 1 140 ? 9.838  -21.510 32.261 1.00 44.39  ? 146 GLU   C C   1 
ATOM   2182 O  O   . GLU   B 1 140 ? 9.129  -22.333 32.852 1.00 45.26  ? 146 GLU   C O   1 
ATOM   2183 C  CB  . GLU   B 1 140 ? 11.306 -19.439 32.410 1.00 44.55  ? 146 GLU   C CB  1 
ATOM   2184 C  CG  . GLU   B 1 140 ? 10.131 -18.537 32.068 1.00 51.04  ? 146 GLU   C CG  1 
ATOM   2185 C  CD  . GLU   B 1 140 ? 9.649  -17.612 33.175 1.00 59.30  ? 146 GLU   C CD  1 
ATOM   2186 O  OE1 . GLU   B 1 140 ? 9.729  -16.376 32.985 1.00 61.21  ? 146 GLU   C OE1 1 
ATOM   2187 O  OE2 . GLU   B 1 140 ? 9.185  -18.114 34.225 1.00 60.85  ? 146 GLU   C OE2 1 
HETATM 2188 N  N1  . A1B03 C 2 .   ? 10.546 15.193  17.315 0.50 21.61  ? 201 A1B03 A N1  1 
HETATM 2189 C  C4  . A1B03 C 2 .   ? 11.036 16.416  20.577 0.50 28.10  ? 201 A1B03 A C4  1 
HETATM 2190 C  C5  . A1B03 C 2 .   ? 10.114 15.645  19.643 0.50 27.30  ? 201 A1B03 A C5  1 
HETATM 2191 C  C6  . A1B03 C 2 .   ? 10.213 16.118  18.204 0.50 25.19  ? 201 A1B03 A C6  1 
HETATM 2192 C  C7  . A1B03 C 2 .   ? 8.710  15.914  20.161 0.50 28.49  ? 201 A1B03 A C7  1 
HETATM 2193 O  O2  . A1B03 C 2 .   ? 9.924  17.274  17.894 0.50 26.23  ? 201 A1B03 A O2  1 
HETATM 2194 C  C3  . A1B03 C 2 .   ? 10.927 15.895  22.009 0.50 29.12  ? 201 A1B03 A C3  1 
HETATM 2195 C  C2  . A1B03 C 2 .   ? 9.483  15.793  22.480 0.50 29.71  ? 201 A1B03 A C2  1 
HETATM 2196 N  N   . A1B03 C 2 .   ? 8.586  15.227  21.454 0.50 29.76  ? 201 A1B03 A N   1 
HETATM 2197 S  S   . A1B03 C 2 .   ? 7.044  14.882  21.914 0.50 30.72  ? 201 A1B03 A S   1 
HETATM 2198 O  O   . A1B03 C 2 .   ? 6.443  14.177  20.868 0.50 32.90  ? 201 A1B03 A O   1 
HETATM 2199 O  O1  . A1B03 C 2 .   ? 7.111  14.414  23.166 0.50 30.78  ? 201 A1B03 A O1  1 
HETATM 2200 C  C1  . A1B03 C 2 .   ? 6.475  16.318  21.618 0.50 31.42  ? 201 A1B03 A C1  1 
HETATM 2201 C  C   . A1B03 C 2 .   ? 6.062  17.102  22.443 0.50 31.39  ? 201 A1B03 A C   1 
HETATM 2202 ZN ZN  . ZN    D 3 .   ? 10.708 -3.437  5.687  1.00 18.37  2 202 ZN    A ZN  1 
HETATM 2203 S  S   . DMS   E 4 .   ? 8.650  11.487  22.866 1.00 20.00  ? 203 DMS   A S   1 
HETATM 2204 O  O   . DMS   E 4 .   ? 9.776  11.899  23.740 1.00 20.00  ? 203 DMS   A O   1 
HETATM 2205 C  C1  . DMS   E 4 .   ? 7.335  11.056  23.975 1.00 20.00  ? 203 DMS   A C1  1 
HETATM 2206 C  C2  . DMS   E 4 .   ? 9.069  9.864   22.313 1.00 20.00  ? 203 DMS   A C2  1 
HETATM 2207 ZN ZN  . ZN    F 3 .   ? 30.469 -31.119 26.784 1.00 12.81  2 201 ZN    C ZN  1 
HETATM 2208 S  S   . DMS   G 4 .   ? 20.635 -31.598 8.838  1.00 92.49  ? 202 DMS   C S   1 
HETATM 2209 O  O   . DMS   G 4 .   ? 20.624 -30.267 8.149  1.00 92.45  ? 202 DMS   C O   1 
HETATM 2210 C  C1  . DMS   G 4 .   ? 22.006 -31.592 10.015 1.00 92.41  ? 202 DMS   C C1  1 
HETATM 2211 C  C2  . DMS   G 4 .   ? 19.324 -31.553 10.091 1.00 92.56  ? 202 DMS   C C2  1 
HETATM 2212 O  O   . HOH   H 5 .   ? 35.273 -3.696  8.054  1.00 27.08  ? 301 HOH   A O   1 
HETATM 2213 O  O   . HOH   H 5 .   ? 6.350  15.406  25.092 1.00 103.30 ? 302 HOH   A O   1 
HETATM 2214 O  O   . HOH   H 5 .   ? 7.280  26.509  14.457 1.00 47.22  ? 303 HOH   A O   1 
HETATM 2215 O  O   . HOH   H 5 .   ? 11.097 9.256   4.488  1.00 26.54  ? 304 HOH   A O   1 
HETATM 2216 O  O   . HOH   H 5 .   ? 33.576 -2.309  13.707 1.00 33.21  ? 305 HOH   A O   1 
HETATM 2217 O  O   . HOH   H 5 .   ? 27.987 3.441   4.740  1.00 35.38  ? 306 HOH   A O   1 
HETATM 2218 O  O   . HOH   H 5 .   ? 37.533 14.924  14.043 1.00 43.66  ? 307 HOH   A O   1 
HETATM 2219 O  O   . HOH   H 5 .   ? 10.599 10.262  31.459 1.00 24.77  ? 308 HOH   A O   1 
HETATM 2220 O  O   . HOH   H 5 .   ? 17.427 0.931   28.186 1.00 25.70  ? 309 HOH   A O   1 
HETATM 2221 O  O   . HOH   H 5 .   ? 8.455  19.156  19.647 1.00 30.67  ? 310 HOH   A O   1 
HETATM 2222 O  O   . HOH   H 5 .   ? 2.856  9.573   9.144  1.00 31.46  ? 311 HOH   A O   1 
HETATM 2223 O  O   . HOH   H 5 .   ? 8.354  -2.820  31.874 1.00 24.80  ? 312 HOH   A O   1 
HETATM 2224 O  O   . HOH   H 5 .   ? 3.216  7.632   24.466 1.00 26.32  ? 313 HOH   A O   1 
HETATM 2225 O  O   . HOH   H 5 .   ? -3.812 10.486  27.530 1.00 62.14  ? 314 HOH   A O   1 
HETATM 2226 O  O   . HOH   H 5 .   ? 13.755 3.075   1.213  1.00 19.94  ? 315 HOH   A O   1 
HETATM 2227 O  O   . HOH   H 5 .   ? 20.130 20.029  5.755  1.00 45.00  ? 316 HOH   A O   1 
HETATM 2228 O  O   . HOH   H 5 .   ? 0.447  -0.794  19.450 1.00 20.24  ? 317 HOH   A O   1 
HETATM 2229 O  O   . HOH   H 5 .   ? 30.385 10.366  15.520 1.00 31.82  ? 318 HOH   A O   1 
HETATM 2230 O  O   . HOH   H 5 .   ? 10.774 6.008   3.520  1.00 22.12  ? 319 HOH   A O   1 
HETATM 2231 O  O   . HOH   H 5 .   ? 34.978 7.975   9.225  1.00 51.66  ? 320 HOH   A O   1 
HETATM 2232 O  O   . HOH   H 5 .   ? 23.460 21.681  7.334  1.00 25.64  ? 321 HOH   A O   1 
HETATM 2233 O  O   . HOH   H 5 .   ? 4.662  -3.571  28.916 1.00 26.15  ? 322 HOH   A O   1 
HETATM 2234 O  O   . HOH   H 5 .   ? 27.742 8.091   1.671  1.00 31.91  ? 323 HOH   A O   1 
HETATM 2235 O  O   . HOH   H 5 .   ? 33.830 14.166  9.713  1.00 31.38  ? 324 HOH   A O   1 
HETATM 2236 O  O   . HOH   H 5 .   ? 19.421 10.052  19.682 1.00 14.45  ? 325 HOH   A O   1 
HETATM 2237 O  O   . HOH   H 5 .   ? 8.397  -6.319  9.615  1.00 26.29  ? 326 HOH   A O   1 
HETATM 2238 O  O   . HOH   H 5 .   ? 24.926 4.970   21.354 1.00 33.42  ? 327 HOH   A O   1 
HETATM 2239 O  O   . HOH   H 5 .   ? 14.006 13.786  24.034 1.00 24.75  ? 328 HOH   A O   1 
HETATM 2240 O  O   . HOH   H 5 .   ? 2.563  -2.820  20.807 1.00 21.45  ? 329 HOH   A O   1 
HETATM 2241 O  O   . HOH   H 5 .   ? 23.496 11.673  21.985 1.00 35.83  ? 330 HOH   A O   1 
HETATM 2242 O  O   . HOH   H 5 .   ? 22.604 0.808   17.364 1.00 16.86  ? 331 HOH   A O   1 
HETATM 2243 O  O   . HOH   H 5 .   ? 13.724 3.953   23.538 1.00 13.03  ? 332 HOH   A O   1 
HETATM 2244 O  O   . HOH   H 5 .   ? -0.076 1.393   15.991 1.00 13.04  ? 333 HOH   A O   1 
HETATM 2245 O  O   . HOH   H 5 .   ? 26.641 -1.163  8.648  1.00 26.43  ? 334 HOH   A O   1 
HETATM 2246 O  O   . HOH   H 5 .   ? 20.820 -4.130  14.153 1.00 16.89  ? 335 HOH   A O   1 
HETATM 2247 O  O   . HOH   H 5 .   ? 18.405 21.980  9.715  1.00 21.81  ? 336 HOH   A O   1 
HETATM 2248 O  O   . HOH   H 5 .   ? 6.510  -6.878  23.722 1.00 25.07  ? 337 HOH   A O   1 
HETATM 2249 O  O   . HOH   H 5 .   ? 11.310 12.826  11.373 1.00 18.00  ? 338 HOH   A O   1 
HETATM 2250 O  O   . HOH   H 5 .   ? 31.588 19.968  11.733 1.00 22.02  ? 339 HOH   A O   1 
HETATM 2251 O  O   . HOH   H 5 .   ? 3.996  -8.094  9.739  1.00 50.33  ? 340 HOH   A O   1 
HETATM 2252 O  O   . HOH   H 5 .   ? 4.619  -5.468  14.536 1.00 47.39  ? 341 HOH   A O   1 
HETATM 2253 O  O   . HOH   H 5 .   ? 29.998 11.496  18.377 1.00 28.30  ? 342 HOH   A O   1 
HETATM 2254 O  O   . HOH   H 5 .   ? 16.600 3.810   23.664 1.00 18.32  ? 343 HOH   A O   1 
HETATM 2255 O  O   . HOH   H 5 .   ? 28.825 15.962  4.363  1.00 32.27  ? 344 HOH   A O   1 
HETATM 2256 O  O   . HOH   H 5 .   ? -2.376 23.807  9.758  1.00 51.71  ? 345 HOH   A O   1 
HETATM 2257 O  O   . HOH   H 5 .   ? 17.608 19.983  17.061 1.00 19.58  ? 346 HOH   A O   1 
HETATM 2258 O  O   . HOH   H 5 .   ? 28.884 3.393   12.575 1.00 18.54  ? 347 HOH   A O   1 
HETATM 2259 O  O   . HOH   H 5 .   ? 24.001 -3.380  16.014 1.00 33.95  ? 348 HOH   A O   1 
HETATM 2260 O  O   . HOH   H 5 .   ? 20.478 -0.797  2.927  1.00 27.55  ? 349 HOH   A O   1 
HETATM 2261 O  O   . HOH   H 5 .   ? 20.659 -2.514  16.792 1.00 15.92  ? 350 HOH   A O   1 
HETATM 2262 O  O   . HOH   H 5 .   ? 13.219 11.521  9.319  1.00 15.34  ? 351 HOH   A O   1 
HETATM 2263 O  O   . HOH   H 5 .   ? 17.063 6.117   27.003 1.00 29.96  ? 352 HOH   A O   1 
HETATM 2264 O  O   . HOH   H 5 .   ? 23.172 -6.519  11.914 1.00 27.35  ? 353 HOH   A O   1 
HETATM 2265 O  O   . HOH   H 5 .   ? 36.531 17.844  14.347 1.00 30.69  ? 354 HOH   A O   1 
HETATM 2266 O  O   . HOH   H 5 .   ? 30.442 2.774   14.664 1.00 27.33  ? 355 HOH   A O   1 
HETATM 2267 O  O   . HOH   H 5 .   ? 19.444 2.898   19.385 1.00 19.42  ? 356 HOH   A O   1 
HETATM 2268 O  O   . HOH   H 5 .   ? 17.213 -4.966  12.031 1.00 33.73  ? 357 HOH   A O   1 
HETATM 2269 O  O   . HOH   H 5 .   ? 16.074 23.748  15.246 1.00 41.85  ? 358 HOH   A O   1 
HETATM 2270 O  O   . HOH   H 5 .   ? 6.051  3.029   5.864  1.00 27.51  ? 359 HOH   A O   1 
HETATM 2271 O  O   . HOH   H 5 .   ? 25.514 19.498  21.774 1.00 25.53  ? 360 HOH   A O   1 
HETATM 2272 O  O   . HOH   H 5 .   ? 25.232 17.880  4.619  1.00 33.59  ? 361 HOH   A O   1 
HETATM 2273 O  O   . HOH   H 5 .   ? 7.463  20.238  17.687 1.00 29.19  ? 362 HOH   A O   1 
HETATM 2274 O  O   . HOH   H 5 .   ? 9.665  4.021   33.527 1.00 15.13  ? 363 HOH   A O   1 
HETATM 2275 O  O   . HOH   H 5 .   ? 11.451 -7.025  24.692 1.00 27.25  ? 364 HOH   A O   1 
HETATM 2276 O  O   . HOH   H 5 .   ? 35.882 15.267  11.071 1.00 41.16  ? 365 HOH   A O   1 
HETATM 2277 O  O   . HOH   H 5 .   ? 32.797 16.558  9.193  1.00 28.27  ? 366 HOH   A O   1 
HETATM 2278 O  O   . HOH   H 5 .   ? 31.045 15.582  22.786 1.00 26.58  ? 367 HOH   A O   1 
HETATM 2279 O  O   . HOH   H 5 .   ? 14.357 -2.441  17.913 1.00 17.38  ? 368 HOH   A O   1 
HETATM 2280 O  O   . HOH   H 5 .   ? 30.257 4.600   5.641  1.00 25.92  ? 369 HOH   A O   1 
HETATM 2281 O  O   . HOH   H 5 .   ? 32.107 2.280   5.653  1.00 40.45  ? 370 HOH   A O   1 
HETATM 2282 O  O   . HOH   H 5 .   ? 35.283 10.595  12.125 1.00 49.15  ? 371 HOH   A O   1 
HETATM 2283 O  O   . HOH   H 5 .   ? 13.052 -7.596  12.360 1.00 34.61  ? 372 HOH   A O   1 
HETATM 2284 O  O   . HOH   H 5 .   ? 22.666 -0.592  5.314  1.00 23.34  ? 373 HOH   A O   1 
HETATM 2285 O  O   . HOH   H 5 .   ? 34.085 4.912   16.434 1.00 44.88  ? 374 HOH   A O   1 
HETATM 2286 O  O   . HOH   H 5 .   ? 31.956 8.776   7.553  1.00 24.90  ? 375 HOH   A O   1 
HETATM 2287 O  O   . HOH   H 5 .   ? 27.170 -1.218  15.761 1.00 27.37  ? 376 HOH   A O   1 
HETATM 2288 O  O   . HOH   H 5 .   ? 3.812  -3.707  6.036  1.00 29.19  ? 377 HOH   A O   1 
HETATM 2289 O  O   . HOH   H 5 .   ? 5.596  5.475   32.703 1.00 21.23  ? 378 HOH   A O   1 
HETATM 2290 O  O   . HOH   H 5 .   ? 27.989 17.539  24.194 1.00 24.83  ? 379 HOH   A O   1 
HETATM 2291 O  O   . HOH   H 5 .   ? 3.198  0.627   28.829 1.00 35.57  ? 380 HOH   A O   1 
HETATM 2292 O  O   . HOH   H 5 .   ? 16.243 9.469   -1.704 1.00 25.31  ? 381 HOH   A O   1 
HETATM 2293 O  O   . HOH   H 5 .   ? 18.093 17.915  4.358  1.00 36.81  ? 382 HOH   A O   1 
HETATM 2294 O  O   . HOH   H 5 .   ? 22.411 19.445  19.595 1.00 30.16  ? 383 HOH   A O   1 
HETATM 2295 O  O   . HOH   H 5 .   ? 29.951 -1.431  8.397  1.00 38.89  ? 384 HOH   A O   1 
HETATM 2296 O  O   . HOH   H 5 .   ? 33.920 18.760  10.728 1.00 25.92  ? 385 HOH   A O   1 
HETATM 2297 O  O   . HOH   H 5 .   ? 17.731 10.616  26.173 1.00 24.93  ? 386 HOH   A O   1 
HETATM 2298 O  O   . HOH   H 5 .   ? 3.389  -0.201  21.517 1.00 18.39  ? 387 HOH   A O   1 
HETATM 2299 O  O   . HOH   H 5 .   ? 15.383 15.448  3.788  1.00 34.92  ? 388 HOH   A O   1 
HETATM 2300 O  O   . HOH   H 5 .   ? 31.017 -2.406  15.567 1.00 38.60  ? 389 HOH   A O   1 
HETATM 2301 O  O   . HOH   H 5 .   ? 0.439  -1.207  16.775 1.00 16.98  ? 390 HOH   A O   1 
HETATM 2302 O  O   . HOH   H 5 .   ? 8.453  6.506   33.845 1.00 20.27  ? 391 HOH   A O   1 
HETATM 2303 O  O   . HOH   H 5 .   ? 34.137 7.574   16.441 1.00 39.63  ? 392 HOH   A O   1 
HETATM 2304 O  O   . HOH   H 5 .   ? 23.219 19.129  6.338  1.00 19.39  ? 393 HOH   A O   1 
HETATM 2305 O  O   . HOH   H 5 .   ? 17.367 0.520   20.191 1.00 18.31  ? 394 HOH   A O   1 
HETATM 2306 O  O   . HOH   H 5 .   ? 5.141  26.675  19.770 1.00 45.91  ? 395 HOH   A O   1 
HETATM 2307 O  O   . HOH   H 5 .   ? 11.518 17.939  4.681  1.00 39.13  ? 396 HOH   A O   1 
HETATM 2308 O  O   . HOH   H 5 .   ? 23.452 8.233   21.639 1.00 26.64  ? 397 HOH   A O   1 
HETATM 2309 O  O   . HOH   H 5 .   ? 22.744 3.362   20.745 1.00 22.10  ? 398 HOH   A O   1 
HETATM 2310 O  O   . HOH   H 5 .   ? 16.468 21.201  19.209 1.00 31.84  ? 399 HOH   A O   1 
HETATM 2311 O  O   . HOH   H 5 .   ? 0.981  -5.002  17.650 1.00 33.12  ? 400 HOH   A O   1 
HETATM 2312 O  O   . HOH   H 5 .   ? 4.215  0.479   24.037 1.00 17.97  ? 401 HOH   A O   1 
HETATM 2313 O  O   . HOH   H 5 .   ? 17.061 -2.488  19.666 1.00 16.88  ? 402 HOH   A O   1 
HETATM 2314 O  O   . HOH   H 5 .   ? 21.087 9.886   21.913 1.00 19.63  ? 403 HOH   A O   1 
HETATM 2315 O  O   . HOH   H 5 .   ? 16.655 -3.839  2.821  1.00 32.32  ? 404 HOH   A O   1 
HETATM 2316 O  O   . HOH   H 5 .   ? 1.096  7.681   27.366 1.00 43.75  ? 405 HOH   A O   1 
HETATM 2317 O  O   . HOH   H 5 .   ? 7.249  13.888  4.729  1.00 25.93  ? 406 HOH   A O   1 
HETATM 2318 O  O   . HOH   H 5 .   ? 8.596  21.343  7.468  1.00 57.89  ? 407 HOH   A O   1 
HETATM 2319 O  O   . HOH   H 5 .   ? 3.207  26.997  15.875 1.00 59.43  ? 408 HOH   A O   1 
HETATM 2320 O  O   . HOH   H 5 .   ? 1.356  4.932   26.873 1.00 31.99  ? 409 HOH   A O   1 
HETATM 2321 O  O   . HOH   H 5 .   ? 36.742 16.199  16.652 1.00 40.67  ? 410 HOH   A O   1 
HETATM 2322 O  O   . HOH   H 5 .   ? 20.748 -4.768  11.449 1.00 31.38  ? 411 HOH   A O   1 
HETATM 2323 O  O   . HOH   H 5 .   ? 4.870  8.067   2.277  1.00 34.45  ? 412 HOH   A O   1 
HETATM 2324 O  O   . HOH   H 5 .   ? 37.714 1.256   10.520 1.00 67.45  ? 413 HOH   A O   1 
HETATM 2325 O  O   . HOH   H 5 .   ? 1.980  14.484  17.061 1.00 35.51  ? 414 HOH   A O   1 
HETATM 2326 O  O   . HOH   H 5 .   ? 15.234 14.317  26.349 1.00 36.36  ? 415 HOH   A O   1 
HETATM 2327 O  O   . HOH   H 5 .   ? 33.086 -4.087  5.719  1.00 48.84  ? 416 HOH   A O   1 
HETATM 2328 O  O   . HOH   H 5 .   ? 13.787 -6.651  25.753 1.00 44.62  ? 417 HOH   A O   1 
HETATM 2329 O  O   . HOH   H 5 .   ? 30.750 12.986  23.114 1.00 42.33  ? 418 HOH   A O   1 
HETATM 2330 O  O   . HOH   H 5 .   ? 29.739 0.473   16.235 1.00 38.24  ? 419 HOH   A O   1 
HETATM 2331 O  O   . HOH   H 5 .   ? 8.848  12.206  31.672 1.00 38.86  ? 420 HOH   A O   1 
HETATM 2332 O  O   . HOH   H 5 .   ? 18.588 2.165   22.634 1.00 39.51  ? 421 HOH   A O   1 
HETATM 2333 O  O   . HOH   H 5 .   ? 16.761 -5.017  34.335 1.00 31.63  ? 422 HOH   A O   1 
HETATM 2334 O  O   . HOH   H 5 .   ? 18.525 3.162   25.994 1.00 40.21  ? 423 HOH   A O   1 
HETATM 2335 O  O   . HOH   H 5 .   ? 21.659 19.736  4.177  1.00 38.58  ? 424 HOH   A O   1 
HETATM 2336 O  O   . HOH   H 5 .   ? 2.104  -5.463  14.771 1.00 39.84  ? 425 HOH   A O   1 
HETATM 2337 O  O   . HOH   H 5 .   ? 6.376  3.745   3.420  1.00 39.51  ? 426 HOH   A O   1 
HETATM 2338 O  O   . HOH   H 5 .   ? 22.901 -8.430  7.129  1.00 43.54  ? 427 HOH   A O   1 
HETATM 2339 O  O   . HOH   H 5 .   ? 27.621 10.400  0.015  1.00 43.16  ? 428 HOH   A O   1 
HETATM 2340 O  O   . HOH   H 5 .   ? 37.673 -4.305  6.999  1.00 38.38  ? 429 HOH   A O   1 
HETATM 2341 O  O   . HOH   H 5 .   ? 9.445  8.275   2.399  1.00 35.03  ? 430 HOH   A O   1 
HETATM 2342 O  O   . HOH   H 5 .   ? 8.323  16.855  26.531 1.00 46.93  ? 431 HOH   A O   1 
HETATM 2343 O  O   . HOH   H 5 .   ? 21.261 -0.984  18.842 1.00 32.28  ? 432 HOH   A O   1 
HETATM 2344 O  O   . HOH   H 5 .   ? 2.287  -4.906  22.548 1.00 30.86  ? 433 HOH   A O   1 
HETATM 2345 O  O   . HOH   H 5 .   ? 28.069 16.773  1.819  1.00 56.86  ? 434 HOH   A O   1 
HETATM 2346 O  O   . HOH   H 5 .   ? 32.098 11.379  6.434  1.00 34.33  ? 435 HOH   A O   1 
HETATM 2347 O  O   . HOH   H 5 .   ? 28.995 1.481   18.663 1.00 47.89  ? 436 HOH   A O   1 
HETATM 2348 O  O   . HOH   H 5 .   ? 0.724  -7.579  17.577 1.00 53.45  ? 437 HOH   A O   1 
HETATM 2349 O  O   . HOH   H 5 .   ? 18.675 20.579  2.181  1.00 66.78  ? 438 HOH   A O   1 
HETATM 2350 O  O   . HOH   H 5 .   ? -1.027 27.285  8.459  1.00 78.40  ? 439 HOH   A O   1 
HETATM 2351 O  O   . HOH   I 5 .   ? 31.013 -32.290 0.747  1.00 34.65  ? 301 HOH   C O   1 
HETATM 2352 O  O   . HOH   I 5 .   ? 31.149 -23.554 -1.267 1.00 23.36  ? 302 HOH   C O   1 
HETATM 2353 O  O   . HOH   I 5 .   ? 17.561 -33.394 23.844 1.00 42.65  ? 303 HOH   C O   1 
HETATM 2354 O  O   . HOH   I 5 .   ? 38.286 -7.185  7.236  1.00 26.55  ? 304 HOH   C O   1 
HETATM 2355 O  O   . HOH   I 5 .   ? 38.226 -18.438 21.628 1.00 28.89  ? 305 HOH   C O   1 
HETATM 2356 O  O   . HOH   I 5 .   ? 35.906 -26.134 34.305 1.00 31.82  ? 306 HOH   C O   1 
HETATM 2357 O  O   . HOH   I 5 .   ? 30.557 -18.079 26.954 1.00 19.85  ? 307 HOH   C O   1 
HETATM 2358 O  O   . HOH   I 5 .   ? 17.676 -6.046  24.106 1.00 24.37  ? 308 HOH   C O   1 
HETATM 2359 O  O   . HOH   I 5 .   ? 36.135 -2.340  11.304 1.00 43.03  ? 309 HOH   C O   1 
HETATM 2360 O  O   . HOH   I 5 .   ? 24.532 -5.872  15.228 1.00 29.50  ? 310 HOH   C O   1 
HETATM 2361 O  O   . HOH   I 5 .   ? 14.504 -9.250  10.919 1.00 31.90  ? 311 HOH   C O   1 
HETATM 2362 O  O   . HOH   I 5 .   ? 17.766 -27.523 16.497 1.00 19.34  ? 312 HOH   C O   1 
HETATM 2363 O  O   . HOH   I 5 .   ? 22.679 -5.859  21.211 1.00 20.91  ? 313 HOH   C O   1 
HETATM 2364 O  O   . HOH   I 5 .   ? 14.511 -18.676 31.789 1.00 40.89  ? 314 HOH   C O   1 
HETATM 2365 O  O   . HOH   I 5 .   ? 43.180 -3.816  19.209 1.00 48.24  ? 315 HOH   C O   1 
HETATM 2366 O  O   . HOH   I 5 .   ? 19.594 -4.048  20.170 1.00 19.93  ? 316 HOH   C O   1 
HETATM 2367 O  O   . HOH   I 5 .   ? 10.114 -17.537 18.289 1.00 29.38  ? 317 HOH   C O   1 
HETATM 2368 O  O   . HOH   I 5 .   ? 42.571 -11.177 11.468 1.00 34.10  ? 318 HOH   C O   1 
HETATM 2369 O  O   . HOH   I 5 .   ? 20.665 -18.652 12.857 1.00 14.40  ? 319 HOH   C O   1 
HETATM 2370 O  O   . HOH   I 5 .   ? 37.037 -18.668 28.303 1.00 29.68  ? 320 HOH   C O   1 
HETATM 2371 O  O   . HOH   I 5 .   ? 14.668 -23.967 12.260 1.00 29.07  ? 321 HOH   C O   1 
HETATM 2372 O  O   . HOH   I 5 .   ? 40.100 -29.409 12.034 1.00 22.82  ? 322 HOH   C O   1 
HETATM 2373 O  O   . HOH   I 5 .   ? 18.457 -8.784  13.714 1.00 27.47  ? 323 HOH   C O   1 
HETATM 2374 O  O   . HOH   I 5 .   ? 22.072 -28.454 4.801  1.00 26.06  ? 324 HOH   C O   1 
HETATM 2375 O  O   . HOH   I 5 .   ? 24.733 -15.644 7.437  1.00 19.60  ? 325 HOH   C O   1 
HETATM 2376 O  O   . HOH   I 5 .   ? 41.261 -24.833 7.465  1.00 27.56  ? 326 HOH   C O   1 
HETATM 2377 O  O   . HOH   I 5 .   ? 13.734 -24.410 29.222 1.00 34.54  ? 327 HOH   C O   1 
HETATM 2378 O  O   . HOH   I 5 .   ? 32.314 -23.655 29.185 1.00 17.40  ? 328 HOH   C O   1 
HETATM 2379 O  O   . HOH   I 5 .   ? 26.439 -5.399  9.910  1.00 24.00  ? 329 HOH   C O   1 
HETATM 2380 O  O   . HOH   I 5 .   ? 27.926 -4.644  18.518 1.00 44.34  ? 330 HOH   C O   1 
HETATM 2381 O  O   . HOH   I 5 .   ? 40.477 -27.102 15.368 1.00 12.53  ? 331 HOH   C O   1 
HETATM 2382 O  O   . HOH   I 5 .   ? 26.044 -25.121 8.825  1.00 13.55  ? 332 HOH   C O   1 
HETATM 2383 O  O   . HOH   I 5 .   ? 13.092 -11.187 28.545 1.00 38.30  ? 333 HOH   C O   1 
HETATM 2384 O  O   . HOH   I 5 .   ? 30.717 -21.479 28.498 1.00 16.75  ? 334 HOH   C O   1 
HETATM 2385 O  O   . HOH   I 5 .   ? 37.337 -31.826 10.975 1.00 23.80  ? 335 HOH   C O   1 
HETATM 2386 O  O   . HOH   I 5 .   ? 9.711  -8.832  23.948 1.00 29.33  ? 336 HOH   C O   1 
HETATM 2387 O  O   . HOH   I 5 .   ? 29.670 -15.907 30.549 1.00 34.50  ? 337 HOH   C O   1 
HETATM 2388 O  O   . HOH   I 5 .   ? 23.825 -8.110  9.464  1.00 22.80  ? 338 HOH   C O   1 
HETATM 2389 O  O   . HOH   I 5 .   ? 11.762 -24.260 21.634 1.00 19.66  ? 339 HOH   C O   1 
HETATM 2390 O  O   . HOH   I 5 .   ? 23.467 -33.553 29.016 1.00 28.91  ? 340 HOH   C O   1 
HETATM 2391 O  O   . HOH   I 5 .   ? 35.174 -13.020 8.916  1.00 22.19  ? 341 HOH   C O   1 
HETATM 2392 O  O   . HOH   I 5 .   ? 25.889 -37.949 24.365 1.00 33.49  ? 342 HOH   C O   1 
HETATM 2393 O  O   . HOH   I 5 .   ? 19.055 -27.702 28.127 1.00 19.11  ? 343 HOH   C O   1 
HETATM 2394 O  O   . HOH   I 5 .   ? 35.368 -32.644 3.460  1.00 32.27  ? 344 HOH   C O   1 
HETATM 2395 O  O   . HOH   I 5 .   ? 20.718 -25.617 13.801 1.00 21.30  ? 345 HOH   C O   1 
HETATM 2396 O  O   . HOH   I 5 .   ? 4.128  -10.442 19.728 1.00 30.58  ? 346 HOH   C O   1 
HETATM 2397 O  O   . HOH   I 5 .   ? 26.992 -35.448 20.762 1.00 25.13  ? 347 HOH   C O   1 
HETATM 2398 O  O   . HOH   I 5 .   ? 14.529 -28.745 25.644 1.00 32.71  ? 348 HOH   C O   1 
HETATM 2399 O  O   . HOH   I 5 .   ? 29.729 -15.198 19.692 1.00 16.40  ? 349 HOH   C O   1 
HETATM 2400 O  O   . HOH   I 5 .   ? 9.055  -8.064  21.306 1.00 24.12  ? 350 HOH   C O   1 
HETATM 2401 O  O   . HOH   I 5 .   ? 16.703 -9.417  27.719 1.00 34.74  ? 351 HOH   C O   1 
HETATM 2402 O  O   . HOH   I 5 .   ? 13.128 -29.575 19.250 1.00 33.53  ? 352 HOH   C O   1 
HETATM 2403 O  O   . HOH   I 5 .   ? 34.724 -34.855 18.166 1.00 27.78  ? 353 HOH   C O   1 
HETATM 2404 O  O   . HOH   I 5 .   ? 31.080 -35.490 31.820 1.00 38.56  ? 354 HOH   C O   1 
HETATM 2405 O  O   . HOH   I 5 .   ? 31.943 -10.370 13.926 1.00 20.87  ? 355 HOH   C O   1 
HETATM 2406 O  O   . HOH   I 5 .   ? 10.329 -16.934 15.074 1.00 32.30  ? 356 HOH   C O   1 
HETATM 2407 O  O   . HOH   I 5 .   ? 21.558 -26.186 34.448 1.00 28.61  ? 357 HOH   C O   1 
HETATM 2408 O  O   . HOH   I 5 .   ? 17.437 -23.853 8.636  1.00 37.10  ? 358 HOH   C O   1 
HETATM 2409 O  O   . HOH   I 5 .   ? 36.183 -28.467 2.960  1.00 38.33  ? 359 HOH   C O   1 
HETATM 2410 O  O   . HOH   I 5 .   ? 31.987 -34.614 24.926 1.00 26.49  ? 360 HOH   C O   1 
HETATM 2411 O  O   . HOH   I 5 .   ? 4.840  -11.957 14.539 1.00 58.20  ? 361 HOH   C O   1 
HETATM 2412 O  O   . HOH   I 5 .   ? 28.874 -36.061 7.864  1.00 21.44  ? 362 HOH   C O   1 
HETATM 2413 O  O   . HOH   I 5 .   ? 29.724 -12.987 13.105 1.00 16.21  ? 363 HOH   C O   1 
HETATM 2414 O  O   . HOH   I 5 .   ? 8.761  -13.166 10.738 1.00 22.38  ? 364 HOH   C O   1 
HETATM 2415 O  O   . HOH   I 5 .   ? 36.352 -21.193 7.139  1.00 22.88  ? 365 HOH   C O   1 
HETATM 2416 O  O   . HOH   I 5 .   ? 22.871 -33.096 5.440  1.00 28.27  ? 366 HOH   C O   1 
HETATM 2417 O  O   . HOH   I 5 .   ? 22.009 -13.751 29.493 1.00 39.72  ? 367 HOH   C O   1 
HETATM 2418 O  O   . HOH   I 5 .   ? 6.688  -9.230  22.621 1.00 34.41  ? 368 HOH   C O   1 
HETATM 2419 O  O   . HOH   I 5 .   ? 22.790 -8.445  14.079 1.00 17.41  ? 369 HOH   C O   1 
HETATM 2420 O  O   . HOH   I 5 .   ? 5.770  -25.001 28.479 1.00 66.35  ? 370 HOH   C O   1 
HETATM 2421 O  O   . HOH   I 5 .   ? 14.797 -18.270 10.418 1.00 35.18  ? 371 HOH   C O   1 
HETATM 2422 O  O   . HOH   I 5 .   ? 11.258 -22.516 28.598 1.00 30.58  ? 372 HOH   C O   1 
HETATM 2423 O  O   . HOH   I 5 .   ? 27.917 -16.307 22.157 1.00 13.86  ? 373 HOH   C O   1 
HETATM 2424 O  O   . HOH   I 5 .   ? 37.893 -23.361 4.731  1.00 32.65  ? 374 HOH   C O   1 
HETATM 2425 O  O   . HOH   I 5 .   ? 10.926 -21.667 13.721 1.00 42.32  ? 375 HOH   C O   1 
HETATM 2426 O  O   . HOH   I 5 .   ? 23.191 -25.271 8.916  1.00 20.29  ? 376 HOH   C O   1 
HETATM 2427 O  O   . HOH   I 5 .   ? 33.556 -32.821 0.826  1.00 38.45  ? 377 HOH   C O   1 
HETATM 2428 O  O   . HOH   I 5 .   ? 37.236 -31.556 25.753 1.00 29.94  ? 378 HOH   C O   1 
HETATM 2429 O  O   . HOH   I 5 .   ? 32.863 -9.746  11.230 1.00 16.59  ? 379 HOH   C O   1 
HETATM 2430 O  O   . HOH   I 5 .   ? 3.759  -8.124  14.660 1.00 26.15  ? 380 HOH   C O   1 
HETATM 2431 O  O   . HOH   I 5 .   ? 10.897 -6.357  13.143 1.00 23.41  ? 381 HOH   C O   1 
HETATM 2432 O  O   . HOH   I 5 .   ? 25.849 -30.950 30.931 1.00 17.55  ? 382 HOH   C O   1 
HETATM 2433 O  O   . HOH   I 5 .   ? 22.873 -28.051 12.619 1.00 19.77  ? 383 HOH   C O   1 
HETATM 2434 O  O   . HOH   I 5 .   ? 31.216 -12.081 10.788 1.00 15.72  ? 384 HOH   C O   1 
HETATM 2435 O  O   . HOH   I 5 .   ? 36.596 -16.169 12.560 1.00 33.84  ? 385 HOH   C O   1 
HETATM 2436 O  O   . HOH   I 5 .   ? 4.356  -16.253 16.738 1.00 51.30  ? 386 HOH   C O   1 
HETATM 2437 O  O   . HOH   I 5 .   ? 9.896  -24.883 19.691 1.00 24.10  ? 387 HOH   C O   1 
HETATM 2438 O  O   . HOH   I 5 .   ? 10.732 -11.785 8.988  1.00 30.97  ? 388 HOH   C O   1 
HETATM 2439 O  O   . HOH   I 5 .   ? 34.112 -13.353 25.677 1.00 22.72  ? 389 HOH   C O   1 
HETATM 2440 O  O   . HOH   I 5 .   ? 22.307 -23.609 6.062  1.00 32.25  ? 390 HOH   C O   1 
HETATM 2441 O  O   . HOH   I 5 .   ? 21.689 -18.782 5.960  1.00 25.38  ? 391 HOH   C O   1 
HETATM 2442 O  O   . HOH   I 5 .   ? 23.495 -3.297  19.106 1.00 35.89  ? 392 HOH   C O   1 
HETATM 2443 O  O   . HOH   I 5 .   ? 26.484 -12.008 27.740 1.00 28.88  ? 393 HOH   C O   1 
HETATM 2444 O  O   . HOH   I 5 .   ? 26.269 -31.172 14.812 1.00 19.16  ? 394 HOH   C O   1 
HETATM 2445 O  O   . HOH   I 5 .   ? 4.546  -27.917 23.371 1.00 39.78  ? 395 HOH   C O   1 
HETATM 2446 O  O   . HOH   I 5 .   ? 36.957 -29.114 10.249 1.00 21.04  ? 396 HOH   C O   1 
HETATM 2447 O  O   . HOH   I 5 .   ? 38.642 -12.895 25.951 1.00 28.92  ? 397 HOH   C O   1 
HETATM 2448 O  O   . HOH   I 5 .   ? 20.175 -23.673 34.768 1.00 35.17  ? 398 HOH   C O   1 
HETATM 2449 O  O   . HOH   I 5 .   ? 43.117 -25.156 23.901 1.00 26.53  ? 399 HOH   C O   1 
HETATM 2450 O  O   . HOH   I 5 .   ? 35.741 -28.383 7.867  1.00 19.00  ? 400 HOH   C O   1 
HETATM 2451 O  O   . HOH   I 5 .   ? 29.877 -10.328 27.829 1.00 46.54  ? 401 HOH   C O   1 
HETATM 2452 O  O   . HOH   I 5 .   ? 5.648  -16.984 22.189 1.00 42.93  ? 402 HOH   C O   1 
HETATM 2453 O  O   . HOH   I 5 .   ? 24.418 -13.700 5.563  1.00 37.78  ? 403 HOH   C O   1 
HETATM 2454 O  O   . HOH   I 5 .   ? 3.983  -12.671 17.056 1.00 39.40  ? 404 HOH   C O   1 
HETATM 2455 O  O   . HOH   I 5 .   ? 31.572 -13.461 4.503  1.00 34.50  ? 405 HOH   C O   1 
HETATM 2456 O  O   . HOH   I 5 .   ? 34.527 -23.226 -0.626 1.00 32.44  ? 406 HOH   C O   1 
HETATM 2457 O  O   . HOH   I 5 .   ? 9.578  -18.443 26.602 1.00 33.98  ? 407 HOH   C O   1 
HETATM 2458 O  O   . HOH   I 5 .   ? 17.162 -25.250 12.731 1.00 23.50  ? 408 HOH   C O   1 
HETATM 2459 O  O   . HOH   I 5 .   ? 32.789 -14.244 9.586  1.00 16.82  ? 409 HOH   C O   1 
HETATM 2460 O  O   . HOH   I 5 .   ? 37.865 -20.453 4.844  1.00 35.25  ? 410 HOH   C O   1 
HETATM 2461 O  O   . HOH   I 5 .   ? 32.869 -30.244 31.777 1.00 19.51  ? 411 HOH   C O   1 
HETATM 2462 O  O   . HOH   I 5 .   ? 30.303 -17.893 8.478  1.00 25.03  ? 412 HOH   C O   1 
HETATM 2463 O  O   . HOH   I 5 .   ? 35.451 -24.549 24.766 1.00 18.87  ? 413 HOH   C O   1 
HETATM 2464 O  O   . HOH   I 5 .   ? 18.430 -8.309  25.531 1.00 22.49  ? 414 HOH   C O   1 
HETATM 2465 O  O   . HOH   I 5 .   ? 26.320 -5.974  22.222 1.00 29.18  ? 415 HOH   C O   1 
HETATM 2466 O  O   . HOH   I 5 .   ? 34.613 -3.949  17.868 1.00 31.53  ? 416 HOH   C O   1 
HETATM 2467 O  O   . HOH   I 5 .   ? 33.819 -35.792 8.903  1.00 37.23  ? 417 HOH   C O   1 
HETATM 2468 O  O   . HOH   I 5 .   ? 39.976 -29.764 14.776 1.00 17.82  ? 418 HOH   C O   1 
HETATM 2469 O  O   . HOH   I 5 .   ? 31.016 -5.790  6.090  1.00 50.12  ? 419 HOH   C O   1 
HETATM 2470 O  O   . HOH   I 5 .   ? 20.269 -32.111 22.126 1.00 34.55  ? 420 HOH   C O   1 
HETATM 2471 O  O   . HOH   I 5 .   ? 18.760 -19.079 10.874 1.00 18.77  ? 421 HOH   C O   1 
HETATM 2472 O  O   . HOH   I 5 .   ? 38.617 -14.469 13.705 1.00 33.06  ? 422 HOH   C O   1 
HETATM 2473 O  O   . HOH   I 5 .   ? 41.601 -12.163 18.074 1.00 36.94  ? 423 HOH   C O   1 
HETATM 2474 O  O   . HOH   I 5 .   ? 23.289 -31.012 13.241 1.00 30.68  ? 424 HOH   C O   1 
HETATM 2475 O  O   . HOH   I 5 .   ? 16.342 -20.500 11.514 1.00 24.43  ? 425 HOH   C O   1 
HETATM 2476 O  O   . HOH   I 5 .   ? 35.157 -13.479 6.268  1.00 35.83  ? 426 HOH   C O   1 
HETATM 2477 O  O   . HOH   I 5 .   ? 33.860 -15.506 27.295 1.00 37.94  ? 427 HOH   C O   1 
HETATM 2478 O  O   . HOH   I 5 .   ? 6.315  -22.830 18.200 1.00 32.01  ? 428 HOH   C O   1 
HETATM 2479 O  O   . HOH   I 5 .   ? 4.517  -24.887 26.038 1.00 85.55  ? 429 HOH   C O   1 
HETATM 2480 O  O   . HOH   I 5 .   ? 5.869  -12.485 23.289 1.00 57.37  ? 430 HOH   C O   1 
HETATM 2481 O  O   . HOH   I 5 .   ? 24.272 -16.289 3.233  1.00 34.54  ? 431 HOH   C O   1 
HETATM 2482 O  O   . HOH   I 5 .   ? 22.997 -17.561 33.311 1.00 25.66  ? 432 HOH   C O   1 
HETATM 2483 O  O   . HOH   I 5 .   ? 24.455 -7.204  5.116  1.00 51.75  ? 433 HOH   C O   1 
HETATM 2484 O  O   . HOH   I 5 .   ? 6.492  -17.148 18.303 1.00 42.98  ? 434 HOH   C O   1 
HETATM 2485 O  O   . HOH   I 5 .   ? 37.211 -14.426 9.775  1.00 33.33  ? 435 HOH   C O   1 
HETATM 2486 O  O   . HOH   I 5 .   ? 41.816 -31.392 15.850 1.00 28.68  ? 436 HOH   C O   1 
HETATM 2487 O  O   . HOH   I 5 .   ? 31.568 -15.634 7.242  1.00 30.32  ? 437 HOH   C O   1 
HETATM 2488 O  O   . HOH   I 5 .   ? 6.395  -19.976 17.897 1.00 37.92  ? 438 HOH   C O   1 
HETATM 2489 O  O   . HOH   I 5 .   ? 36.434 -24.452 27.288 1.00 35.65  ? 439 HOH   C O   1 
HETATM 2490 O  O   . HOH   I 5 .   ? 33.998 -31.744 29.682 1.00 24.04  ? 440 HOH   C O   1 
HETATM 2491 O  O   . HOH   I 5 .   ? 20.060 -19.550 36.084 1.00 32.44  ? 441 HOH   C O   1 
HETATM 2492 O  O   . HOH   I 5 .   ? 23.362 -15.602 31.480 1.00 31.84  ? 442 HOH   C O   1 
HETATM 2493 O  O   . HOH   I 5 .   ? 20.776 -17.507 34.625 1.00 34.15  ? 443 HOH   C O   1 
HETATM 2494 O  O   . HOH   I 5 .   ? 24.134 -12.288 28.910 1.00 52.74  ? 444 HOH   C O   1 
HETATM 2495 O  O   . HOH   I 5 .   ? 8.874  -19.228 16.604 1.00 43.87  ? 445 HOH   C O   1 
HETATM 2496 O  O   . HOH   I 5 .   ? 21.499 -26.753 10.398 1.00 36.42  ? 446 HOH   C O   1 
HETATM 2497 O  O   . HOH   I 5 .   ? 22.857 -16.510 5.522  1.00 42.20  ? 447 HOH   C O   1 
HETATM 2498 O  O   . HOH   I 5 .   ? 1.665  -19.249 17.291 1.00 66.56  ? 448 HOH   C O   1 
HETATM 2499 O  O   . HOH   I 5 .   ? 20.495 -11.735 30.631 1.00 40.38  ? 449 HOH   C O   1 
HETATM 2500 O  O   . HOH   I 5 .   ? 13.255 -27.021 29.216 1.00 52.42  ? 450 HOH   C O   1 
HETATM 2501 O  O   . HOH   I 5 .   ? 6.607  -18.542 26.328 1.00 47.98  ? 451 HOH   C O   1 
HETATM 2502 O  O   . HOH   I 5 .   ? 16.279 -27.548 14.130 1.00 30.23  ? 452 HOH   C O   1 
HETATM 2503 O  O   . HOH   I 5 .   ? 32.342 -19.316 29.273 1.00 32.27  ? 453 HOH   C O   1 
HETATM 2504 O  O   . HOH   I 5 .   ? 19.803 -12.595 5.881  1.00 60.94  ? 454 HOH   C O   1 
HETATM 2505 O  O   . HOH   I 5 .   ? 18.090 -17.900 8.295  1.00 31.51  ? 455 HOH   C O   1 
HETATM 2506 O  O   . HOH   I 5 .   ? 22.631 -11.817 6.054  1.00 37.39  ? 456 HOH   C O   1 
HETATM 2507 O  O   . HOH   I 5 .   ? 18.167 -16.322 38.276 1.00 35.25  ? 457 HOH   C O   1 
HETATM 2508 O  O   . HOH   I 5 .   ? 35.049 -20.196 29.461 1.00 40.77  ? 458 HOH   C O   1 
HETATM 2509 O  O   . HOH   I 5 .   ? 8.845  -23.633 17.544 1.00 32.67  ? 459 HOH   C O   1 
HETATM 2510 O  O   . HOH   I 5 .   ? 35.009 -22.859 29.090 1.00 30.26  ? 460 HOH   C O   1 
HETATM 2511 O  O   . HOH   I 5 .   ? 22.873 -34.848 3.365  1.00 43.99  ? 461 HOH   C O   1 
HETATM 2512 O  O   . HOH   I 5 .   ? 37.672 -34.059 9.496  1.00 44.06  ? 462 HOH   C O   1 
HETATM 2513 O  O   . HOH   I 5 .   ? 37.181 -22.946 -1.651 1.00 35.47  ? 463 HOH   C O   1 
HETATM 2514 O  O   . HOH   I 5 .   ? 19.225 -17.583 5.949  1.00 37.46  ? 464 HOH   C O   1 
HETATM 2515 O  O   . HOH   I 5 .   ? 39.250 -2.629  10.914 1.00 36.79  ? 465 HOH   C O   1 
HETATM 2516 O  O   . HOH   I 5 .   ? 24.851 -35.265 0.398  1.00 52.24  ? 466 HOH   C O   1 
HETATM 2517 O  O   . HOH   I 5 .   ? 20.626 -15.234 4.849  1.00 44.00  ? 467 HOH   C 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   ? 0.2594 0.2188 0.1952 -0.0447 0.0041  -0.0175 7   SER   A N   
2    C CA  . SER   A 1   ? 0.2498 0.2131 0.1943 -0.0419 -0.0028 -0.0127 7   SER   A CA  
3    C C   . SER   A 1   ? 0.2351 0.2078 0.1972 -0.0309 -0.0103 -0.0046 7   SER   A C   
4    O O   . SER   A 1   ? 0.2359 0.2127 0.2008 -0.0285 -0.0120 -0.0020 7   SER   A O   
5    C CB  . SER   A 1   ? 0.2867 0.2555 0.2197 -0.0574 -0.0102 -0.0090 7   SER   A CB  
6    O OG  . SER   A 1   ? 0.3229 0.3033 0.2566 -0.0626 -0.0194 -0.0001 7   SER   A OG  
7    N N   . GLY   A 2   ? 0.2075 0.1829 0.1809 -0.0256 -0.0136 -0.0016 8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.1858 0.1683 0.1758 -0.0175 -0.0180 0.0040  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.1691 0.1503 0.1682 -0.0102 -0.0155 0.0022  8   GLY   A C   
10   O O   . GLY   A 2   ? 0.1885 0.1637 0.1835 -0.0086 -0.0100 -0.0025 8   GLY   A O   
11   N N   . ALA   A 3   ? 0.1568 0.1436 0.1695 -0.0066 -0.0184 0.0061  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.1540 0.1411 0.1747 -0.0019 -0.0160 0.0042  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.1428 0.1339 0.1762 0.0022  -0.0144 0.0048  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.1566 0.1500 0.1968 0.0019  -0.0160 0.0083  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.1672 0.1559 0.1909 -0.0056 -0.0198 0.0071  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.1348 0.1268 0.1719 0.0045  -0.0107 0.0015  10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.1310 0.1257 0.1790 0.0054  -0.0067 -0.0003 10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.1360 0.1319 0.1954 0.0050  -0.0066 0.0009  10  ILE   A C   
19   O O   . ILE   A 4   ? 0.1395 0.1355 0.1946 0.0043  -0.0079 0.0003  10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.1266 0.1238 0.1693 0.0047  -0.0022 -0.0046 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.1483 0.1460 0.1818 0.0054  -0.0026 -0.0037 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.1389 0.1377 0.1896 0.0020  0.0040  -0.0087 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.1656 0.1694 0.1953 0.0036  -0.0004 -0.0035 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.1303 0.1272 0.2063 0.0055  -0.0041 0.0030  11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.1450 0.1438 0.2366 0.0057  -0.0023 0.0050  11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.1493 0.1465 0.2507 0.0051  0.0085  -0.0022 11  TYR   A C   
27   O O   . TYR   A 5   ? 0.1546 0.1495 0.2701 0.0058  0.0143  -0.0021 11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.1623 0.1648 0.2708 0.0061  -0.0072 0.0160  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.1522 0.1575 0.2477 0.0025  -0.0173 0.0221  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.1663 0.1737 0.2579 -0.0004 -0.0213 0.0241  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.1742 0.1795 0.2597 0.0002  -0.0218 0.0250  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.1768 0.1852 0.2527 -0.0065 -0.0286 0.0273  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.1960 0.2028 0.2661 -0.0061 -0.0288 0.0282  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.1983 0.2061 0.2630 -0.0100 -0.0317 0.0288  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.2426 0.2505 0.2898 -0.0188 -0.0367 0.0301  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.1508 0.1489 0.2447 0.0022  0.0122  -0.0088 12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.1638 0.1610 0.2616 -0.0023 0.0235  -0.0176 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.1675 0.1665 0.2735 -0.0037 0.0269  -0.0193 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.1573 0.1597 0.2540 -0.0037 0.0202  -0.0169 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.1865 0.1865 0.2644 -0.0081 0.0246  -0.0233 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.1958 0.2007 0.2595 -0.0080 0.0165  -0.0196 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.2091 0.2096 0.2871 -0.0171 0.0365  -0.0331 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.1824 0.1786 0.3081 -0.0047 0.0382  -0.0231 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.1900 0.1882 0.3262 -0.0058 0.0424  -0.0244 13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.1688 0.1712 0.3100 -0.0005 0.0307  -0.0131 13  GLY   A C   
46   O O   . GLY   A 7   ? 0.1716 0.1749 0.3219 0.0039  0.0239  -0.0034 13  GLY   A O   
47   N N   . ASN   A 8   ? 0.1708 0.1769 0.3027 -0.0027 0.0271  -0.0140 14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.1552 0.1648 0.2865 -0.0002 0.0159  -0.0048 14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.1527 0.1617 0.2593 -0.0012 0.0067  -0.0045 14  ASN   A C   
50   O O   . ASN   A 8   ? 0.1568 0.1672 0.2567 -0.0021 0.0008  -0.0017 14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.1779 0.1914 0.3209 -0.0014 0.0185  -0.0041 14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.2380 0.2526 0.4126 0.0015  0.0267  0.0001  14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.2549 0.2743 0.4456 0.0045  0.0202  0.0127  14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.2138 0.2245 0.3987 -0.0006 0.0416  -0.0094 14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.1433 0.1497 0.2387 -0.0009 0.0061  -0.0065 15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.1397 0.1446 0.2164 -0.0009 -0.0002 -0.0056 15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.1368 0.1388 0.2100 0.0013  -0.0049 -0.0014 15  TYR   A C   
58   O O   . TYR   A 9   ? 0.1460 0.1475 0.2269 0.0026  -0.0025 -0.0009 15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.1515 0.1584 0.2175 -0.0039 0.0035  -0.0106 15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.1510 0.1628 0.2165 -0.0090 0.0075  -0.0143 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.1848 0.1978 0.2485 -0.0093 0.0037  -0.0118 15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.1931 0.2080 0.2591 -0.0153 0.0157  -0.0209 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.1975 0.2162 0.2604 -0.0150 0.0069  -0.0146 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.2008 0.2215 0.2641 -0.0227 0.0197  -0.0246 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.2074 0.2305 0.2692 -0.0221 0.0146  -0.0208 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.2453 0.2752 0.3041 -0.0302 0.0178  -0.0237 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.1288 0.1281 0.1896 0.0008  -0.0101 0.0005  16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.1367 0.1326 0.1892 0.0008  -0.0133 0.0026  16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.1308 0.1231 0.1711 0.0016  -0.0113 -0.0006 16  ARG   A C   
70   O O   . ARG   A 10  ? 0.1455 0.1356 0.1813 0.0009  -0.0111 -0.0011 16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.1480 0.1435 0.1972 -0.0034 -0.0193 0.0074  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.1673 0.1586 0.2027 -0.0070 -0.0215 0.0076  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.1944 0.1878 0.2249 -0.0154 -0.0276 0.0128  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.2067 0.1924 0.2182 -0.0218 -0.0261 0.0083  16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.2166 0.2005 0.2172 -0.0275 -0.0265 0.0079  16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.2245 0.2144 0.2316 -0.0262 -0.0296 0.0128  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.2408 0.2155 0.2243 -0.0344 -0.0220 0.0015  16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.1307 0.1230 0.1683 0.0033  -0.0093 -0.0015 17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.1262 0.1172 0.1572 0.0048  -0.0068 -0.0019 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.1466 0.1315 0.1702 0.0047  -0.0069 -0.0019 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.1502 0.1356 0.1730 0.0043  -0.0083 -0.0015 17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.1247 0.1221 0.1576 0.0049  -0.0043 -0.0022 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.1395 0.1390 0.1703 0.0061  -0.0027 0.0013  17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.1417 0.1448 0.1797 0.0016  -0.0023 -0.0044 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.1361 0.1146 0.1548 0.0043  -0.0042 -0.0027 18  VAL   A N   
86   C CA  A VAL   A 12  ? 0.1470 0.1178 0.1572 0.0020  -0.0014 -0.0050 18  VAL   A CA  
87   C CA  B VAL   A 12  ? 0.1699 0.1408 0.1801 0.0019  -0.0017 -0.0049 18  VAL   A CA  
88   C C   . VAL   A 12  ? 0.1520 0.1178 0.1645 0.0052  0.0060  -0.0051 18  VAL   A C   
89   O O   . VAL   A 12  ? 0.1654 0.1343 0.1866 0.0085  0.0076  -0.0016 18  VAL   A O   
90   C CB  A VAL   A 12  ? 0.1533 0.1182 0.1545 -0.0054 -0.0030 -0.0072 18  VAL   A CB  
91   C CB  B VAL   A 12  ? 0.2226 0.1885 0.2248 -0.0053 -0.0038 -0.0067 18  VAL   A CB  
92   C CG1 A VAL   A 12  ? 0.1703 0.1420 0.1720 -0.0094 -0.0107 -0.0037 18  VAL   A CG1 
93   C CG1 B VAL   A 12  ? 0.2365 0.1949 0.2260 -0.0121 -0.0005 -0.0105 18  VAL   A CG1 
94   C CG2 A VAL   A 12  ? 0.1124 0.0734 0.1152 -0.0060 -0.0011 -0.0081 18  VAL   A CG2 
95   C CG2 B VAL   A 12  ? 0.2535 0.2273 0.2601 -0.0077 -0.0115 -0.0028 18  VAL   A CG2 
96   N N   . ASN   A 13  ? 0.1568 0.1156 0.1637 0.0038  0.0114  -0.0080 19  ASN   A N   
97   C CA  . ASN   A 13  ? 0.1682 0.1202 0.1818 0.0071  0.0213  -0.0079 19  ASN   A CA  
98   C C   . ASN   A 13  ? 0.1785 0.1210 0.1916 0.0042  0.0257  -0.0108 19  ASN   A C   
99   O O   . ASN   A 13  ? 0.1975 0.1340 0.1978 -0.0037 0.0245  -0.0163 19  ASN   A O   
100  C CB  . ASN   A 13  ? 0.1811 0.1248 0.1877 0.0042  0.0289  -0.0130 19  ASN   A CB  
101  C CG  . ASN   A 13  ? 0.1843 0.1364 0.1910 0.0066  0.0252  -0.0103 19  ASN   A CG  
102  O OD1 . ASN   A 13  ? 0.1898 0.1453 0.1870 0.0024  0.0185  -0.0116 19  ASN   A OD1 
103  N ND2 . ASN   A 13  ? 0.1795 0.1364 0.1985 0.0130  0.0290  -0.0049 19  ASN   A ND2 
104  N N   . ARG   A 14  ? 0.1787 0.1210 0.2064 0.0095  0.0306  -0.0057 20  ARG   A N   
105  C CA  . ARG   A 14  ? 0.1858 0.1183 0.2148 0.0070  0.0354  -0.0081 20  ARG   A CA  
106  C C   . ARG   A 14  ? 0.2209 0.1362 0.2389 -0.0002 0.0462  -0.0183 20  ARG   A C   
107  O O   . ARG   A 14  ? 0.2378 0.1458 0.2444 -0.0081 0.0463  -0.0240 20  ARG   A O   
108  C CB  . ARG   A 14  ? 0.1926 0.1277 0.2427 0.0139  0.0403  0.0011  20  ARG   A CB  
109  C CG  . ARG   A 14  ? 0.1913 0.1174 0.2455 0.0120  0.0446  0.0002  20  ARG   A CG  
110  C CD  . ARG   A 14  ? 0.2036 0.1337 0.2831 0.0191  0.0497  0.0123  20  ARG   A CD  
111  N NE  . ARG   A 14  ? 0.2105 0.1342 0.2972 0.0181  0.0527  0.0140  20  ARG   A NE  
112  C CZ  . ARG   A 14  ? 0.2348 0.1394 0.3260 0.0165  0.0665  0.0083  20  ARG   A CZ  
113  N NH1 . ARG   A 14  ? 0.2637 0.1534 0.3502 0.0143  0.0789  -0.0013 20  ARG   A NH1 
114  N NH2 . ARG   A 14  ? 0.2605 0.1602 0.3608 0.0161  0.0691  0.0114  20  ARG   A NH2 
115  N N   . HIS   A 15  ? 0.2173 0.1270 0.2362 0.0005  0.0552  -0.0212 21  HIS   A N   
116  C CA  . HIS   A 15  ? 0.2604 0.1525 0.2678 -0.0087 0.0685  -0.0328 21  HIS   A CA  
117  C C   . HIS   A 15  ? 0.2793 0.1714 0.2607 -0.0222 0.0619  -0.0403 21  HIS   A C   
118  O O   . HIS   A 15  ? 0.3279 0.2065 0.2945 -0.0343 0.0719  -0.0508 21  HIS   A O   
119  C CB  . HIS   A 15  ? 0.2854 0.1702 0.3037 -0.0047 0.0831  -0.0344 21  HIS   A CB  
120  C CG  . HIS   A 15  ? 0.2702 0.1642 0.2814 -0.0045 0.0775  -0.0337 21  HIS   A CG  
121  N ND1 . HIS   A 15  ? 0.2536 0.1636 0.2772 0.0053  0.0684  -0.0227 21  HIS   A ND1 
122  C CD2 . HIS   A 15  ? 0.2943 0.1834 0.2867 -0.0143 0.0807  -0.0426 21  HIS   A CD2 
123  C CE1 . HIS   A 15  ? 0.2694 0.1827 0.2826 0.0024  0.0665  -0.0254 21  HIS   A CE1 
124  N NE2 . HIS   A 15  ? 0.2884 0.1900 0.2834 -0.0090 0.0733  -0.0367 21  HIS   A NE2 
125  N N   . LEU   A 16  ? 0.2677 0.1750 0.2440 -0.0217 0.0462  -0.0346 22  LEU   A N   
126  C CA  . LEU   A 16  ? 0.2630 0.1751 0.2202 -0.0339 0.0372  -0.0366 22  LEU   A CA  
127  C C   . LEU   A 16  ? 0.2722 0.1921 0.2280 -0.0367 0.0258  -0.0321 22  LEU   A C   
128  O O   . LEU   A 16  ? 0.2932 0.2206 0.2385 -0.0461 0.0167  -0.0298 22  LEU   A O   
129  C CB  . LEU   A 16  ? 0.2640 0.1869 0.2200 -0.0320 0.0299  -0.0324 22  LEU   A CB  
130  C CG  . LEU   A 16  ? 0.2735 0.1899 0.2286 -0.0313 0.0406  -0.0371 22  LEU   A CG  
131  C CD1 . LEU   A 16  ? 0.2766 0.2052 0.2305 -0.0296 0.0313  -0.0318 22  LEU   A CD1 
132  C CD2 . LEU   A 16  ? 0.3122 0.2145 0.2485 -0.0469 0.0524  -0.0487 22  LEU   A CD2 
133  N N   . ALA   A 17  ? 0.2505 0.1700 0.2190 -0.0289 0.0261  -0.0291 23  ALA   A N   
134  C CA  . ALA   A 17  ? 0.2461 0.1732 0.2153 -0.0307 0.0162  -0.0249 23  ALA   A CA  
135  C C   . ALA   A 17  ? 0.2700 0.1913 0.2222 -0.0460 0.0166  -0.0297 23  ALA   A C   
136  O O   . ALA   A 17  ? 0.2961 0.2026 0.2391 -0.0533 0.0285  -0.0383 23  ALA   A O   
137  C CB  . ALA   A 17  ? 0.2412 0.1681 0.2254 -0.0215 0.0182  -0.0217 23  ALA   A CB  
138  N N   . THR   A 18  ? 0.2539 0.1870 0.2030 -0.0518 0.0046  -0.0237 24  THR   A N   
139  C CA  . THR   A 18  ? 0.2596 0.1918 0.1922 -0.0687 0.0023  -0.0255 24  THR   A CA  
140  C C   . THR   A 18  ? 0.2665 0.1953 0.2023 -0.0687 0.0028  -0.0258 24  THR   A C   
141  O O   . THR   A 18  ? 0.2427 0.1725 0.1946 -0.0555 0.0029  -0.0231 24  THR   A O   
142  C CB  . THR   A 18  ? 0.2809 0.2311 0.2136 -0.0750 -0.0120 -0.0148 24  THR   A CB  
143  O OG1 . THR   A 18  ? 0.2738 0.2347 0.2258 -0.0640 -0.0197 -0.0064 24  THR   A OG1 
144  C CG2 . THR   A 18  ? 0.2904 0.2457 0.2216 -0.0751 -0.0139 -0.0126 24  THR   A CG2 
145  N N   . HIS   A 19  ? 0.2875 0.2142 0.2073 -0.0852 0.0019  -0.0281 25  HIS   A N   
146  C CA  . HIS   A 19  ? 0.2876 0.2126 0.2099 -0.0862 0.0009  -0.0275 25  HIS   A CA  
147  C C   . HIS   A 19  ? 0.2579 0.2000 0.1982 -0.0763 -0.0116 -0.0160 25  HIS   A C   
148  O O   . HIS   A 19  ? 0.2433 0.1843 0.1950 -0.0673 -0.0106 -0.0152 25  HIS   A O   
149  C CB  . HIS   A 19  ? 0.3153 0.2384 0.2154 -0.1085 0.0002  -0.0306 25  HIS   A CB  
150  C CG  . HIS   A 19  ? 0.3790 0.3056 0.2825 -0.1106 -0.0047 -0.0268 25  HIS   A CG  
151  N ND1 . HIS   A 19  ? 0.4309 0.3425 0.3383 -0.1055 0.0051  -0.0336 25  HIS   A ND1 
152  C CD2 . HIS   A 19  ? 0.4255 0.3705 0.3353 -0.1133 -0.0187 -0.0150 25  HIS   A CD2 
153  C CE1 . HIS   A 19  ? 0.4337 0.3535 0.3428 -0.1092 -0.0028 -0.0279 25  HIS   A CE1 
154  N NE2 . HIS   A 19  ? 0.4492 0.3898 0.3616 -0.1127 -0.0173 -0.0163 25  HIS   A NE2 
155  N N   . ASN   A 20  ? 0.2581 0.2163 0.2033 -0.0777 -0.0223 -0.0066 26  ASN   A N   
156  C CA  . ASN   A 20  ? 0.2366 0.2092 0.2022 -0.0682 -0.0309 0.0034  26  ASN   A CA  
157  C C   . ASN   A 20  ? 0.2103 0.1801 0.1915 -0.0507 -0.0260 0.0010  26  ASN   A C   
158  O O   . ASN   A 20  ? 0.2164 0.1910 0.2102 -0.0439 -0.0275 0.0036  26  ASN   A O   
159  C CB  . ASN   A 20  ? 0.2679 0.2571 0.2414 -0.0718 -0.0410 0.0152  26  ASN   A CB  
160  C CG  . ASN   A 20  ? 0.3460 0.3484 0.3437 -0.0632 -0.0469 0.0249  26  ASN   A CG  
161  O OD1 . ASN   A 20  ? 0.3924 0.4013 0.3937 -0.0682 -0.0513 0.0302  26  ASN   A OD1 
162  N ND2 . ASN   A 20  ? 0.3618 0.3676 0.3768 -0.0507 -0.0457 0.0269  26  ASN   A ND2 
163  N N   . ASP   A 21  ? 0.2091 0.1722 0.1883 -0.0452 -0.0201 -0.0037 27  ASP   A N   
164  C CA  . ASP   A 21  ? 0.1922 0.1545 0.1841 -0.0317 -0.0160 -0.0048 27  ASP   A CA  
165  C C   . ASP   A 21  ? 0.1853 0.1407 0.1797 -0.0287 -0.0108 -0.0076 27  ASP   A C   
166  O O   . ASP   A 21  ? 0.1845 0.1462 0.1904 -0.0220 -0.0122 -0.0048 27  ASP   A O   
167  C CB  . ASP   A 21  ? 0.2057 0.1624 0.1951 -0.0276 -0.0102 -0.0083 27  ASP   A CB  
168  C CG  . ASP   A 21  ? 0.2030 0.1676 0.1937 -0.0278 -0.0152 -0.0047 27  ASP   A CG  
169  O OD1 . ASP   A 21  ? 0.2113 0.1865 0.2139 -0.0247 -0.0211 0.0013  27  ASP   A OD1 
170  O OD2 . ASP   A 21  ? 0.2223 0.1817 0.2031 -0.0316 -0.0119 -0.0079 27  ASP   A OD2 
171  N N   . TRP   A 22  ? 0.1983 0.1406 0.1823 -0.0347 -0.0038 -0.0132 28  TRP   A N   
172  C CA  . TRP   A 22  ? 0.2031 0.1376 0.1919 -0.0322 0.0021  -0.0147 28  TRP   A CA  
173  C C   . TRP   A 22  ? 0.1950 0.1363 0.1856 -0.0353 -0.0047 -0.0113 28  TRP   A C   
174  O O   . TRP   A 22  ? 0.1986 0.1411 0.1988 -0.0298 -0.0036 -0.0091 28  TRP   A O   
175  C CB  . TRP   A 22  ? 0.2226 0.1390 0.2008 -0.0395 0.0135  -0.0227 28  TRP   A CB  
176  C CG  . TRP   A 22  ? 0.2249 0.1334 0.2091 -0.0331 0.0234  -0.0250 28  TRP   A CG  
177  C CD1 . TRP   A 22  ? 0.2508 0.1526 0.2252 -0.0378 0.0292  -0.0306 28  TRP   A CD1 
178  C CD2 . TRP   A 22  ? 0.2210 0.1283 0.2237 -0.0218 0.0292  -0.0205 28  TRP   A CD2 
179  N NE1 . TRP   A 22  ? 0.2392 0.1352 0.2264 -0.0288 0.0389  -0.0304 28  TRP   A NE1 
180  C CE2 . TRP   A 22  ? 0.2274 0.1275 0.2331 -0.0190 0.0386  -0.0230 28  TRP   A CE2 
181  C CE3 . TRP   A 22  ? 0.2355 0.1485 0.2532 -0.0152 0.0272  -0.0132 28  TRP   A CE3 
182  C CZ2 . TRP   A 22  ? 0.2467 0.1462 0.2728 -0.0089 0.0456  -0.0168 28  TRP   A CZ2 
183  C CZ3 . TRP   A 22  ? 0.2376 0.1518 0.2735 -0.0064 0.0327  -0.0065 28  TRP   A CZ3 
184  C CH2 . TRP   A 22  ? 0.2344 0.1415 0.2758 -0.0032 0.0421  -0.0077 28  TRP   A CH2 
185  N N   . ALA   A 23  ? 0.2023 0.1503 0.1856 -0.0441 -0.0119 -0.0093 29  ALA   A N   
186  C CA  . ALA   A 23  ? 0.2119 0.1677 0.1989 -0.0473 -0.0182 -0.0050 29  ALA   A CA  
187  C C   . ALA   A 23  ? 0.2040 0.1742 0.2081 -0.0384 -0.0237 0.0011  29  ALA   A C   
188  O O   . ALA   A 23  ? 0.2192 0.1960 0.2299 -0.0388 -0.0270 0.0043  29  ALA   A O   
189  C CB  . ALA   A 23  ? 0.2448 0.2044 0.2195 -0.0616 -0.0239 -0.0028 29  ALA   A CB  
190  N N   . ASN   A 24  ? 0.1973 0.1716 0.2086 -0.0311 -0.0231 0.0018  30  ASN   A N   
191  C CA  . ASN   A 24  ? 0.1906 0.1760 0.2174 -0.0241 -0.0249 0.0051  30  ASN   A CA  
192  C C   . ASN   A 24  ? 0.1767 0.1602 0.2063 -0.0169 -0.0198 0.0022  30  ASN   A C   
193  O O   . ASN   A 24  ? 0.1724 0.1616 0.2091 -0.0128 -0.0192 0.0026  30  ASN   A O   
194  C CB  . ASN   A 24  ? 0.2004 0.1944 0.2348 -0.0250 -0.0294 0.0104  30  ASN   A CB  
195  C CG  . ASN   A 24  ? 0.2259 0.2265 0.2613 -0.0332 -0.0359 0.0169  30  ASN   A CG  
196  O OD1 . ASN   A 24  ? 0.2521 0.2601 0.2994 -0.0323 -0.0375 0.0206  30  ASN   A OD1 
197  N ND2 . ASN   A 24  ? 0.2369 0.2357 0.2589 -0.0430 -0.0394 0.0186  30  ASN   A ND2 
198  N N   . LEU   A 25  ? 0.1758 0.1519 0.2013 -0.0160 -0.0156 0.0003  31  LEU   A N   
199  C CA  . LEU   A 25  ? 0.1612 0.1376 0.1906 -0.0106 -0.0116 0.0007  31  LEU   A CA  
200  C C   . LEU   A 25  ? 0.1709 0.1585 0.2085 -0.0087 -0.0124 0.0029  31  LEU   A C   
201  O O   . LEU   A 25  ? 0.1864 0.1782 0.2268 -0.0109 -0.0136 0.0040  31  LEU   A O   
202  C CB  . LEU   A 25  ? 0.1704 0.1366 0.1984 -0.0105 -0.0064 0.0008  31  LEU   A CB  
203  C CG  . LEU   A 25  ? 0.1816 0.1493 0.2177 -0.0052 -0.0022 0.0047  31  LEU   A CG  
204  C CD1 . LEU   A 25  ? 0.1844 0.1495 0.2175 -0.0028 0.0001  0.0027  31  LEU   A CD1 
205  C CD2 . LEU   A 25  ? 0.2159 0.1741 0.2581 -0.0043 0.0043  0.0075  31  LEU   A CD2 
206  N N   . VAL   A 26  ? 0.1492 0.1421 0.1893 -0.0063 -0.0110 0.0032  32  VAL   A N   
207  C CA  . VAL   A 26  ? 0.1556 0.1597 0.2001 -0.0079 -0.0104 0.0044  32  VAL   A CA  
208  C C   . VAL   A 26  ? 0.1503 0.1575 0.1967 -0.0073 -0.0092 0.0105  32  VAL   A C   
209  O O   . VAL   A 26  ? 0.1670 0.1827 0.2166 -0.0108 -0.0101 0.0151  32  VAL   A O   
210  C CB  . VAL   A 26  ? 0.1558 0.1644 0.2019 -0.0081 -0.0088 0.0008  32  VAL   A CB  
211  C CG1 . VAL   A 26  ? 0.1791 0.1987 0.2257 -0.0133 -0.0064 0.0005  32  VAL   A CG1 
212  C CG2 . VAL   A 26  ? 0.1714 0.1790 0.2227 -0.0082 -0.0093 -0.0019 32  VAL   A CG2 
213  N N   . TRP   A 27  ? 0.1578 0.1599 0.2041 -0.0035 -0.0072 0.0120  33  TRP   A N   
214  C CA  . TRP   A 27  ? 0.1526 0.1600 0.2057 -0.0023 -0.0057 0.0203  33  TRP   A CA  
215  C C   . TRP   A 27  ? 0.1546 0.1514 0.2090 0.0029  -0.0015 0.0201  33  TRP   A C   
216  O O   . TRP   A 27  ? 0.1557 0.1463 0.2026 0.0039  -0.0011 0.0135  33  TRP   A O   
217  C CB  . TRP   A 27  ? 0.1658 0.1883 0.2182 -0.0068 -0.0074 0.0227  33  TRP   A CB  
218  C CG  . TRP   A 27  ? 0.1780 0.2100 0.2380 -0.0070 -0.0074 0.0334  33  TRP   A CG  
219  C CD1 . TRP   A 27  ? 0.1981 0.2423 0.2675 -0.0105 -0.0094 0.0458  33  TRP   A CD1 
220  C CD2 . TRP   A 27  ? 0.1720 0.2042 0.2328 -0.0041 -0.0058 0.0350  33  TRP   A CD2 
221  N NE1 . TRP   A 27  ? 0.2131 0.2662 0.2909 -0.0099 -0.0093 0.0561  33  TRP   A NE1 
222  C CE2 . TRP   A 27  ? 0.1897 0.2353 0.2615 -0.0059 -0.0069 0.0489  33  TRP   A CE2 
223  C CE3 . TRP   A 27  ? 0.1797 0.2038 0.2340 -0.0007 -0.0041 0.0272  33  TRP   A CE3 
224  C CZ2 . TRP   A 27  ? 0.1964 0.2473 0.2727 -0.0043 -0.0060 0.0547  33  TRP   A CZ2 
225  C CZ3 . TRP   A 27  ? 0.1948 0.2234 0.2517 0.0007  -0.0031 0.0316  33  TRP   A CZ3 
226  C CH2 . TRP   A 27  ? 0.2049 0.2462 0.2727 -0.0007 -0.0038 0.0449  33  TRP   A CH2 
227  N N   . GLU   A 28  ? 0.1552 0.1498 0.2205 0.0058  0.0026  0.0277  34  GLU   A N   
228  C CA  . GLU   A 28  ? 0.1627 0.1472 0.2314 0.0105  0.0092  0.0270  34  GLU   A CA  
229  C C   . GLU   A 28  ? 0.1681 0.1604 0.2555 0.0136  0.0122  0.0403  34  GLU   A C   
230  O O   . GLU   A 28  ? 0.1742 0.1743 0.2732 0.0124  0.0107  0.0503  34  GLU   A O   
231  C CB  . GLU   A 28  ? 0.1983 0.1636 0.2619 0.0104  0.0157  0.0190  34  GLU   A CB  
232  C CG  . GLU   A 28  ? 0.2123 0.1719 0.2834 0.0095  0.0186  0.0219  34  GLU   A CG  
233  C CD  . GLU   A 28  ? 0.2147 0.1700 0.3068 0.0142  0.0276  0.0312  34  GLU   A CD  
234  O OE1 . GLU   A 28  ? 0.2310 0.1879 0.3344 0.0140  0.0278  0.0383  34  GLU   A OE1 
235  O OE2 . GLU   A 28  ? 0.2136 0.1635 0.3135 0.0181  0.0353  0.0321  34  GLU   A OE2 
236  N N   . ASP   A 29  ? 0.1639 0.1545 0.2567 0.0175  0.0169  0.0423  35  ASP   A N   
237  C CA  . ASP   A 29  ? 0.1699 0.1693 0.2847 0.0211  0.0203  0.0573  35  ASP   A CA  
238  C C   . ASP   A 29  ? 0.1729 0.1589 0.2941 0.0267  0.0311  0.0541  35  ASP   A C   
239  O O   . ASP   A 29  ? 0.1752 0.1621 0.2873 0.0270  0.0305  0.0491  35  ASP   A O   
240  C CB  . ASP   A 29  ? 0.1862 0.2089 0.3011 0.0165  0.0114  0.0669  35  ASP   A CB  
241  C CG  . ASP   A 29  ? 0.2097 0.2479 0.3486 0.0179  0.0121  0.0867  35  ASP   A CG  
242  O OD1 . ASP   A 29  ? 0.2402 0.2700 0.3954 0.0251  0.0211  0.0906  35  ASP   A OD1 
243  O OD2 . ASP   A 29  ? 0.2597 0.3196 0.4010 0.0106  0.0039  0.0984  35  ASP   A OD2 
244  N N   . SER   A 30  ? 0.1838 0.1569 0.3220 0.0308  0.0424  0.0567  36  SER   A N   
245  C CA  A SER   A 30  ? 0.1918 0.1493 0.3381 0.0352  0.0564  0.0522  36  SER   A CA  
246  C CA  B SER   A 30  ? 0.2042 0.1618 0.3495 0.0350  0.0562  0.0517  36  SER   A CA  
247  C C   . SER   A 30  ? 0.1979 0.1689 0.3617 0.0397  0.0574  0.0648  36  SER   A C   
248  O O   . SER   A 30  ? 0.2165 0.1804 0.3743 0.0410  0.0632  0.0573  36  SER   A O   
249  C CB  A SER   A 30  ? 0.2030 0.1438 0.3685 0.0380  0.0707  0.0534  36  SER   A CB  
250  C CB  B SER   A 30  ? 0.2532 0.1916 0.4141 0.0372  0.0710  0.0502  36  SER   A CB  
251  O OG  A SER   A 30  ? 0.2218 0.1479 0.3997 0.0419  0.0873  0.0497  36  SER   A OG  
252  O OG  B SER   A 30  ? 0.3164 0.2657 0.5071 0.0414  0.0713  0.0692  36  SER   A OG  
253  N N   . SER   A 31  ? 0.1944 0.1871 0.3780 0.0405  0.0506  0.0845  37  SER   A N   
254  C CA  . SER   A 31  ? 0.1898 0.1989 0.3910 0.0432  0.0500  0.0992  37  SER   A CA  
255  C C   . SER   A 31  ? 0.1844 0.2015 0.3622 0.0393  0.0417  0.0917  37  SER   A C   
256  O O   . SER   A 31  ? 0.1995 0.2224 0.3869 0.0421  0.0448  0.0975  37  SER   A O   
257  C CB  . SER   A 31  ? 0.2106 0.2455 0.4360 0.0414  0.0422  0.1241  37  SER   A CB  
258  O OG  . SER   A 31  ? 0.2637 0.3179 0.4701 0.0317  0.0267  0.1262  37  SER   A OG  
259  N N   . ARG   A 32  ? 0.1667 0.1831 0.3159 0.0330  0.0324  0.0787  38  ARG   A N   
260  C CA  . ARG   A 32  ? 0.1667 0.1884 0.2946 0.0290  0.0256  0.0705  38  ARG   A CA  
261  C C   . ARG   A 32  ? 0.1717 0.1735 0.2807 0.0301  0.0303  0.0521  38  ARG   A C   
262  O O   . ARG   A 32  ? 0.1638 0.1682 0.2575 0.0275  0.0256  0.0457  38  ARG   A O   
263  C CB  . ARG   A 32  ? 0.1665 0.2011 0.2790 0.0208  0.0141  0.0691  38  ARG   A CB  
264  C CG  . ARG   A 32  ? 0.1855 0.2442 0.3113 0.0152  0.0077  0.0876  38  ARG   A CG  
265  C CD  . ARG   A 32  ? 0.1882 0.2579 0.2970 0.0047  -0.0008 0.0837  38  ARG   A CD  
266  N NE  . ARG   A 32  ? 0.1468 0.2185 0.2371 -0.0002 -0.0034 0.0738  38  ARG   A NE  
267  C CZ  . ARG   A 32  ? 0.1747 0.2608 0.2533 -0.0117 -0.0087 0.0734  38  ARG   A CZ  
268  N NH1 . ARG   A 32  ? 0.1942 0.2961 0.2756 -0.0208 -0.0132 0.0827  38  ARG   A NH1 
269  N NH2 . ARG   A 32  ? 0.1809 0.2664 0.2453 -0.0157 -0.0088 0.0640  38  ARG   A NH2 
270  N N   . ASP   A 33  ? 0.1676 0.1505 0.2754 0.0316  0.0386  0.0435  39  ASP   A N   
271  C CA  . ASP   A 33  ? 0.1790 0.1456 0.2662 0.0287  0.0413  0.0272  39  ASP   A CA  
272  C C   . ASP   A 33  ? 0.1683 0.1394 0.2357 0.0235  0.0299  0.0204  39  ASP   A C   
273  O O   . ASP   A 33  ? 0.1742 0.1411 0.2265 0.0207  0.0279  0.0120  39  ASP   A O   
274  C CB  . ASP   A 33  ? 0.1918 0.1529 0.2763 0.0299  0.0480  0.0227  39  ASP   A CB  
275  C CG  . ASP   A 33  ? 0.2064 0.1523 0.2695 0.0241  0.0510  0.0074  39  ASP   A CG  
276  O OD1 . ASP   A 33  ? 0.2214 0.1543 0.2781 0.0201  0.0557  0.0001  39  ASP   A OD1 
277  O OD2 . ASP   A 33  ? 0.2275 0.1749 0.2796 0.0222  0.0489  0.0033  39  ASP   A OD2 
278  N N   . LEU   A 34  ? 0.1574 0.1370 0.2261 0.0216  0.0231  0.0244  40  LEU   A N   
279  C CA  . LEU   A 34  ? 0.1496 0.1330 0.2039 0.0172  0.0146  0.0182  40  LEU   A CA  
280  C C   . LEU   A 34  ? 0.1520 0.1296 0.2028 0.0146  0.0133  0.0146  40  LEU   A C   
281  O O   . LEU   A 34  ? 0.1583 0.1358 0.2192 0.0156  0.0156  0.0201  40  LEU   A O   
282  C CB  . LEU   A 34  ? 0.1475 0.1483 0.2041 0.0148  0.0082  0.0246  40  LEU   A CB  
283  C CG  . LEU   A 34  ? 0.1615 0.1700 0.2165 0.0146  0.0072  0.0264  40  LEU   A CG  
284  C CD1 . LEU   A 34  ? 0.1712 0.1963 0.2252 0.0085  0.0020  0.0309  40  LEU   A CD1 
285  C CD2 . LEU   A 34  ? 0.1748 0.1749 0.2176 0.0144  0.0066  0.0166  40  LEU   A CD2 
286  N N   . LEU   A 35  ? 0.1432 0.1183 0.1820 0.0111  0.0088  0.0074  41  LEU   A N   
287  C CA  . LEU   A 35  ? 0.1458 0.1186 0.1814 0.0080  0.0058  0.0050  41  LEU   A CA  
288  C C   . LEU   A 35  ? 0.1397 0.1192 0.1708 0.0056  -0.0004 0.0024  41  LEU   A C   
289  O O   . LEU   A 35  ? 0.1478 0.1274 0.1749 0.0054  -0.0017 0.0002  41  LEU   A O   
290  C CB  . LEU   A 35  ? 0.1637 0.1217 0.1916 0.0048  0.0103  -0.0009 41  LEU   A CB  
291  C CG  . LEU   A 35  ? 0.1660 0.1218 0.1900 0.0003  0.0072  -0.0029 41  LEU   A CG  
292  C CD1 . LEU   A 35  ? 0.1956 0.1366 0.2162 -0.0031 0.0150  -0.0068 41  LEU   A CD1 
293  C CD2 . LEU   A 35  ? 0.1689 0.1280 0.1843 -0.0044 0.0005  -0.0054 41  LEU   A CD2 
294  N N   . VAL   A 36  ? 0.1366 0.1219 0.1706 0.0038  -0.0033 0.0032  42  VAL   A N   
295  C CA  . VAL   A 36  ? 0.1341 0.1250 0.1687 0.0018  -0.0066 0.0008  42  VAL   A CA  
296  C C   . VAL   A 36  ? 0.1383 0.1267 0.1727 -0.0007 -0.0090 -0.0001 42  VAL   A C   
297  O O   . VAL   A 36  ? 0.1501 0.1382 0.1855 -0.0016 -0.0085 0.0013  42  VAL   A O   
298  C CB  . VAL   A 36  ? 0.1345 0.1362 0.1732 0.0000  -0.0059 0.0018  42  VAL   A CB  
299  C CG1 . VAL   A 36  ? 0.1543 0.1588 0.1966 -0.0021 -0.0057 -0.0022 42  VAL   A CG1 
300  C CG2 . VAL   A 36  ? 0.1479 0.1539 0.1859 0.0007  -0.0044 0.0040  42  VAL   A CG2 
301  N N   . SER   A 37  ? 0.1331 0.1213 0.1679 -0.0022 -0.0118 -0.0008 43  SER   A N   
302  C CA  . SER   A 37  ? 0.1450 0.1339 0.1817 -0.0056 -0.0151 0.0004  43  SER   A CA  
303  C C   . SER   A 37  ? 0.1449 0.1416 0.1941 -0.0049 -0.0156 0.0017  43  SER   A C   
304  O O   . SER   A 37  ? 0.1442 0.1434 0.1992 -0.0028 -0.0130 0.0007  43  SER   A O   
305  C CB  . SER   A 37  ? 0.1650 0.1485 0.1930 -0.0104 -0.0180 0.0013  43  SER   A CB  
306  O OG  . SER   A 37  ? 0.1705 0.1562 0.1992 -0.0107 -0.0199 0.0031  43  SER   A OG  
307  N N   . SER   A 38  ? 0.1587 0.1588 0.2141 -0.0071 -0.0175 0.0037  44  SER   A N   
308  C CA  . SER   A 38  ? 0.1705 0.1774 0.2428 -0.0061 -0.0157 0.0054  44  SER   A CA  
309  C C   . SER   A 38  ? 0.1884 0.1986 0.2702 -0.0071 -0.0202 0.0130  44  SER   A C   
310  O O   . SER   A 38  ? 0.2201 0.2296 0.2931 -0.0116 -0.0264 0.0172  44  SER   A O   
311  C CB  . SER   A 38  ? 0.1851 0.1957 0.2625 -0.0080 -0.0148 0.0051  44  SER   A CB  
312  O OG  . SER   A 38  ? 0.2238 0.2333 0.2954 -0.0115 -0.0209 0.0094  44  SER   A OG  
313  N N   . THR   A 39  ? 0.1898 0.2041 0.2906 -0.0042 -0.0163 0.0152  45  THR   A N   
314  C CA  . THR   A 39  ? 0.2097 0.2297 0.3256 -0.0048 -0.0207 0.0259  45  THR   A CA  
315  C C   . THR   A 39  ? 0.2217 0.2491 0.3653 -0.0032 -0.0173 0.0320  45  THR   A C   
316  O O   . THR   A 39  ? 0.2086 0.2342 0.3603 -0.0008 -0.0080 0.0248  45  THR   A O   
317  C CB  . THR   A 39  ? 0.2126 0.2307 0.3334 -0.0019 -0.0181 0.0260  45  THR   A CB  
318  O OG1 . THR   A 39  ? 0.2172 0.2329 0.3506 0.0020  -0.0075 0.0194  45  THR   A OG1 
319  C CG2 . THR   A 39  ? 0.2360 0.2475 0.3330 -0.0028 -0.0201 0.0204  45  THR   A CG2 
320  N N   . THR   A 40  ? 0.2392 0.2758 0.3988 -0.0054 -0.0239 0.0461  46  THR   A N   
321  C CA  . THR   A 40  ? 0.2608 0.3058 0.4529 -0.0031 -0.0201 0.0551  46  THR   A CA  
322  C C   . THR   A 40  ? 0.2567 0.2998 0.4747 0.0031  -0.0101 0.0560  46  THR   A C   
323  O O   . THR   A 40  ? 0.2759 0.3168 0.5143 0.0069  0.0024  0.0510  46  THR   A O   
324  C CB  . THR   A 40  ? 0.3104 0.3689 0.5105 -0.0095 -0.0321 0.0724  46  THR   A CB  
325  O OG1 . THR   A 40  ? 0.3675 0.4308 0.5649 -0.0136 -0.0405 0.0824  46  THR   A OG1 
326  C CG2 . THR   A 40  ? 0.3342 0.3918 0.5081 -0.0165 -0.0390 0.0686  46  THR   A CG2 
327  N N   . ALA   A 41  ? 0.2591 0.3018 0.4756 0.0032  -0.0139 0.0607  47  ALA   A N   
328  C CA  . ALA   A 41  ? 0.2609 0.3003 0.5020 0.0086  -0.0037 0.0613  47  ALA   A CA  
329  C C   . ALA   A 41  ? 0.2477 0.2740 0.4700 0.0103  0.0059  0.0431  47  ALA   A C   
330  O O   . ALA   A 41  ? 0.2385 0.2606 0.4291 0.0076  0.0007  0.0350  47  ALA   A O   
331  C CB  . ALA   A 41  ? 0.2858 0.3330 0.5381 0.0073  -0.0127 0.0775  47  ALA   A CB  
332  N N   . GLN   A 42  ? 0.2274 0.2477 0.4701 0.0137  0.0206  0.0373  48  GLN   A N   
333  C CA  . GLN   A 42  ? 0.2388 0.2484 0.4646 0.0125  0.0303  0.0210  48  GLN   A CA  
334  C C   . GLN   A 42  ? 0.2148 0.2223 0.4336 0.0133  0.0256  0.0240  48  GLN   A C   
335  O O   . GLN   A 42  ? 0.2155 0.2272 0.4561 0.0159  0.0224  0.0374  48  GLN   A O   
336  C CB  . GLN   A 42  ? 0.2773 0.2799 0.5257 0.0129  0.0501  0.0117  48  GLN   A CB  
337  C CG  . GLN   A 42  ? 0.3739 0.3771 0.6225 0.0099  0.0576  0.0035  48  GLN   A CG  
338  C CD  . GLN   A 42  ? 0.4760 0.4714 0.7496 0.0089  0.0796  -0.0060 48  GLN   A CD  
339  O OE1 . GLN   A 42  ? 0.4841 0.4803 0.7968 0.0140  0.0876  0.0033  48  GLN   A OE1 
340  N NE2 . GLN   A 42  ? 0.5052 0.4935 0.7582 0.0010  0.0906  -0.0239 48  GLN   A NE2 
341  N N   . GLY   A 43  ? 0.1912 0.1940 0.3801 0.0107  0.0241  0.0135  49  GLY   A N   
342  C CA  . GLY   A 43  ? 0.1949 0.1955 0.3731 0.0109  0.0198  0.0146  49  GLY   A CA  
343  C C   . GLY   A 43  ? 0.1768 0.1699 0.3641 0.0109  0.0327  0.0071  49  GLY   A C   
344  O O   . GLY   A 43  ? 0.1920 0.1801 0.3870 0.0086  0.0466  -0.0031 49  GLY   A O   
345  N N   . CYS   A 44  ? 0.1632 0.1552 0.3457 0.0116  0.0287  0.0104  50  CYS   A N   
346  C CA  . CYS   A 44  ? 0.1670 0.1516 0.3584 0.0110  0.0401  0.0045  50  CYS   A CA  
347  C C   . CYS   A 44  ? 0.1644 0.1455 0.3272 0.0063  0.0412  -0.0068 50  CYS   A C   
348  O O   . CYS   A 44  ? 0.1785 0.1532 0.3459 0.0040  0.0513  -0.0129 50  CYS   A O   
349  C CB  . CYS   A 44  ? 0.1888 0.1753 0.4032 0.0149  0.0365  0.0186  50  CYS   A CB  
350  S SG  . CYS   A 44  ? 0.2281 0.2209 0.4868 0.0195  0.0377  0.0358  50  CYS   A SG  
351  N N   . ASP   A 45  ? 0.1650 0.1507 0.3014 0.0051  0.0308  -0.0074 51  ASP   A N   
352  C CA  . ASP   A 45  ? 0.1623 0.1477 0.2752 0.0010  0.0308  -0.0146 51  ASP   A CA  
353  C C   . ASP   A 45  ? 0.1745 0.1591 0.2794 -0.0065 0.0410  -0.0264 51  ASP   A C   
354  O O   . ASP   A 45  ? 0.1982 0.1841 0.3068 -0.0079 0.0439  -0.0289 51  ASP   A O   
355  C CB  . ASP   A 45  ? 0.1509 0.1413 0.2435 0.0024  0.0185  -0.0103 51  ASP   A CB  
356  C CG  . ASP   A 45  ? 0.1586 0.1502 0.2531 0.0060  0.0093  -0.0007 51  ASP   A CG  
357  O OD1 . ASP   A 45  ? 0.1734 0.1632 0.2764 0.0067  0.0105  0.0024  51  ASP   A OD1 
358  O OD2 . ASP   A 45  ? 0.1706 0.1649 0.2570 0.0066  0.0013  0.0037  51  ASP   A OD2 
359  N N   . THR   A 46  ? 0.2054 0.1893 0.2983 -0.0129 0.0460  -0.0331 52  THR   A N   
360  C CA  . THR   A 46  ? 0.2310 0.2171 0.3108 -0.0244 0.0546  -0.0437 52  THR   A CA  
361  C C   . THR   A 46  ? 0.2010 0.1967 0.2573 -0.0284 0.0455  -0.0408 52  THR   A C   
362  O O   . THR   A 46  ? 0.2173 0.2137 0.2692 -0.0244 0.0392  -0.0356 52  THR   A O   
363  C CB  . THR   A 46  ? 0.3319 0.3098 0.4181 -0.0318 0.0698  -0.0535 52  THR   A CB  
364  O OG1 . THR   A 46  ? 0.3845 0.3535 0.4977 -0.0281 0.0811  -0.0556 52  THR   A OG1 
365  C CG2 . THR   A 46  ? 0.3808 0.3628 0.4465 -0.0482 0.0779  -0.0645 52  THR   A CG2 
366  N N   . ILE   A 47  ? 0.1868 0.1909 0.2303 -0.0359 0.0445  -0.0424 53  ILE   A N   
367  C CA  . ILE   A 47  ? 0.1732 0.1887 0.2004 -0.0397 0.0361  -0.0365 53  ILE   A CA  
368  C C   . ILE   A 47  ? 0.1777 0.1993 0.1918 -0.0540 0.0417  -0.0413 53  ILE   A C   
369  O O   . ILE   A 47  ? 0.2010 0.2223 0.2110 -0.0669 0.0523  -0.0512 53  ILE   A O   
370  C CB  . ILE   A 47  ? 0.1788 0.2030 0.2014 -0.0408 0.0304  -0.0317 53  ILE   A CB  
371  C CG1 . ILE   A 47  ? 0.1793 0.1970 0.2133 -0.0292 0.0260  -0.0283 53  ILE   A CG1 
372  C CG2 . ILE   A 47  ? 0.1703 0.2070 0.1829 -0.0427 0.0217  -0.0217 53  ILE   A CG2 
373  C CD1 . ILE   A 47  ? 0.1792 0.1924 0.2163 -0.0175 0.0180  -0.0210 53  ILE   A CD1 
374  N N   . ALA   A 48  ? 0.1688 0.1960 0.1756 -0.0538 0.0358  -0.0353 54  ALA   A N   
375  C CA  . ALA   A 48  ? 0.1839 0.2206 0.1764 -0.0688 0.0386  -0.0370 54  ALA   A CA  
376  C C   . ALA   A 48  ? 0.1841 0.2382 0.1650 -0.0822 0.0352  -0.0323 54  ALA   A C   
377  O O   . ALA   A 48  ? 0.1876 0.2491 0.1719 -0.0758 0.0265  -0.0222 54  ALA   A O   
378  C CB  . ALA   A 48  ? 0.1879 0.2290 0.1782 -0.0632 0.0309  -0.0281 54  ALA   A CB  
379  N N   . ARG   A 49  ? 0.2086 0.2697 0.1755 -0.1024 0.0426  -0.0394 55  ARG   A N   
380  C CA  . ARG   A 49  ? 0.2272 0.3089 0.1813 -0.1193 0.0383  -0.0329 55  ARG   A CA  
381  C C   . ARG   A 49  ? 0.2580 0.3534 0.1972 -0.1360 0.0374  -0.0297 55  ARG   A C   
382  O O   . ARG   A 49  ? 0.2816 0.3749 0.2072 -0.1549 0.0489  -0.0428 55  ARG   A O   
383  C CB  . ARG   A 49  ? 0.2585 0.3377 0.2072 -0.1326 0.0489  -0.0455 55  ARG   A CB  
384  C CG  . ARG   A 49  ? 0.2539 0.3189 0.2191 -0.1160 0.0507  -0.0490 55  ARG   A CG  
385  C CD  . ARG   A 49  ? 0.2365 0.3096 0.2092 -0.1034 0.0370  -0.0341 55  ARG   A CD  
386  N NE  . ARG   A 49  ? 0.2234 0.2836 0.2097 -0.0900 0.0388  -0.0379 55  ARG   A NE  
387  C CZ  . ARG   A 49  ? 0.2190 0.2793 0.2141 -0.0761 0.0292  -0.0279 55  ARG   A CZ  
388  N NH1 . ARG   A 49  ? 0.2305 0.3018 0.2247 -0.0729 0.0189  -0.0140 55  ARG   A NH1 
389  N NH2 . ARG   A 49  ? 0.2443 0.2937 0.2506 -0.0657 0.0307  -0.0313 55  ARG   A NH2 
390  N N   . CYS   A 50  ? 0.2405 0.3502 0.1826 -0.1305 0.0251  -0.0123 56  CYS   A N   
391  C CA  . CYS   A 50  ? 0.2318 0.3535 0.1647 -0.1409 0.0224  -0.0063 56  CYS   A CA  
392  C C   . CYS   A 50  ? 0.2239 0.3638 0.1664 -0.1332 0.0088  0.0161  56  CYS   A C   
393  O O   . CYS   A 50  ? 0.2467 0.3864 0.2041 -0.1179 0.0028  0.0256  56  CYS   A O   
394  C CB  . CYS   A 50  ? 0.2194 0.3209 0.1552 -0.1317 0.0295  -0.0177 56  CYS   A CB  
395  S SG  . CYS   A 50  ? 0.2196 0.3086 0.1756 -0.1019 0.0222  -0.0100 56  CYS   A SG  
396  N N   . ASP   A 51  ? 0.2492 0.4037 0.1853 -0.1431 0.0051  0.0245  57  ASP   A N   
397  C CA  . ASP   A 51  ? 0.2675 0.4384 0.2170 -0.1348 -0.0056 0.0462  57  ASP   A CA  
398  C C   . ASP   A 51  ? 0.2533 0.4142 0.2052 -0.1247 -0.0043 0.0435  57  ASP   A C   
399  O O   . ASP   A 51  ? 0.2660 0.4435 0.2226 -0.1262 -0.0106 0.0588  57  ASP   A O   
400  C CB  . ASP   A 51  ? 0.3124 0.5170 0.2567 -0.1566 -0.0138 0.0652  57  ASP   A CB  
401  C CG  . ASP   A 51  ? 0.3938 0.6090 0.3157 -0.1818 -0.0109 0.0600  57  ASP   A CG  
402  O OD1 . ASP   A 51  ? 0.4257 0.6197 0.3364 -0.1822 -0.0006 0.0397  57  ASP   A OD1 
403  O OD2 . ASP   A 51  ? 0.4517 0.6974 0.3674 -0.2029 -0.0186 0.0771  57  ASP   A OD2 
404  N N   . CYS   A 52  ? 0.2233 0.3580 0.1746 -0.1134 0.0036  0.0260  58  CYS   A N   
405  C CA  . CYS   A 52  ? 0.2080 0.3334 0.1624 -0.1034 0.0041  0.0246  58  CYS   A CA  
406  C C   . CYS   A 52  ? 0.2067 0.3380 0.1780 -0.0868 -0.0034 0.0404  58  CYS   A C   
407  O O   . CYS   A 52  ? 0.1983 0.3282 0.1820 -0.0757 -0.0058 0.0461  58  CYS   A O   
408  C CB  . CYS   A 52  ? 0.2306 0.3292 0.1876 -0.0920 0.0118  0.0079  58  CYS   A CB  
409  S SG  . CYS   A 52  ? 0.2548 0.3407 0.1982 -0.1089 0.0254  -0.0124 58  CYS   A SG  
410  N N   . GLN   A 53  ? 0.1857 0.3219 0.1577 -0.0856 -0.0052 0.0460  59  GLN   A N   
411  C CA  . GLN   A 53  ? 0.1796 0.3178 0.1673 -0.0704 -0.0087 0.0576  59  GLN   A CA  
412  C C   . GLN   A 53  ? 0.1549 0.2764 0.1411 -0.0607 -0.0056 0.0486  59  GLN   A C   
413  O O   . GLN   A 53  ? 0.1646 0.2885 0.1606 -0.0513 -0.0071 0.0567  59  GLN   A O   
414  C CB  . GLN   A 53  ? 0.2135 0.3790 0.2091 -0.0778 -0.0150 0.0787  59  GLN   A CB  
415  C CG  . GLN   A 53  ? 0.2403 0.4236 0.2458 -0.0828 -0.0196 0.0932  59  GLN   A CG  
416  C CD  . GLN   A 53  ? 0.2801 0.4923 0.3006 -0.0879 -0.0261 0.1184  59  GLN   A CD  
417  O OE1 . GLN   A 53  ? 0.3372 0.5743 0.3502 -0.1083 -0.0317 0.1297  59  GLN   A OE1 
418  N NE2 . GLN   A 53  ? 0.2471 0.4579 0.2898 -0.0713 -0.0251 0.1286  59  GLN   A NE2 
419  N N   A THR   A 54  ? 0.1547 0.2592 0.1306 -0.0629 -0.0003 0.0324  60  THR   A N   
420  N N   B THR   A 54  ? 0.1571 0.2619 0.1330 -0.0631 -0.0004 0.0325  60  THR   A N   
421  C CA  A THR   A 54  ? 0.1516 0.2400 0.1287 -0.0529 0.0019  0.0252  60  THR   A CA  
422  C CA  B THR   A 54  ? 0.1568 0.2455 0.1332 -0.0541 0.0021  0.0247  60  THR   A CA  
423  C C   A THR   A 54  ? 0.1471 0.2157 0.1253 -0.0475 0.0064  0.0123  60  THR   A C   
424  C C   B THR   A 54  ? 0.1371 0.2059 0.1159 -0.0472 0.0063  0.0126  60  THR   A C   
425  O O   A THR   A 54  ? 0.1622 0.2270 0.1355 -0.0563 0.0112  0.0039  60  THR   A O   
426  O O   B THR   A 54  ? 0.1304 0.1970 0.1065 -0.0537 0.0097  0.0062  60  THR   A O   
427  C CB  A THR   A 54  ? 0.1631 0.2529 0.1304 -0.0624 0.0038  0.0219  60  THR   A CB  
428  C CB  B THR   A 54  ? 0.1926 0.2836 0.1580 -0.0656 0.0044  0.0210  60  THR   A CB  
429  O OG1 A THR   A 54  ? 0.2089 0.2952 0.1653 -0.0770 0.0098  0.0112  60  THR   A OG1 
430  O OG1 B THR   A 54  ? 0.2011 0.3140 0.1643 -0.0746 -0.0003 0.0342  60  THR   A OG1 
431  C CG2 A THR   A 54  ? 0.1516 0.2622 0.1186 -0.0683 -0.0011 0.0360  60  THR   A CG2 
432  C CG2 B THR   A 54  ? 0.2168 0.2937 0.1845 -0.0565 0.0058  0.0160  60  THR   A CG2 
433  N N   . GLY   A 55  ? 0.1383 0.1952 0.1233 -0.0346 0.0055  0.0112  61  GLY   A N   
434  C CA  . GLY   A 55  ? 0.1369 0.1781 0.1266 -0.0286 0.0079  0.0031  61  GLY   A CA  
435  C C   . GLY   A 55  ? 0.1268 0.1595 0.1209 -0.0185 0.0055  0.0043  61  GLY   A C   
436  O O   . GLY   A 55  ? 0.1356 0.1719 0.1274 -0.0175 0.0039  0.0082  61  GLY   A O   
437  N N   . VAL   A 56  ? 0.1210 0.1436 0.1210 -0.0125 0.0052  0.0016  62  VAL   A N   
438  C CA  . VAL   A 56  ? 0.1178 0.1336 0.1204 -0.0063 0.0023  0.0030  62  VAL   A CA  
439  C C   . VAL   A 56  ? 0.1153 0.1276 0.1204 -0.0012 0.0003  0.0038  62  VAL   A C   
440  O O   . VAL   A 56  ? 0.1255 0.1358 0.1345 -0.0015 0.0014  0.0014  62  VAL   A O   
441  C CB  . VAL   A 56  ? 0.1300 0.1378 0.1392 -0.0077 0.0040  0.0002  62  VAL   A CB  
442  C CG1 . VAL   A 56  ? 0.1590 0.1627 0.1719 -0.0036 -0.0006 0.0042  62  VAL   A CG1 
443  C CG2 . VAL   A 56  ? 0.1412 0.1504 0.1473 -0.0136 0.0073  -0.0017 62  VAL   A CG2 
444  N N   . TYR   A 57  ? 0.1165 0.1275 0.1187 0.0022  -0.0015 0.0062  63  TYR   A N   
445  C CA  . TYR   A 57  ? 0.1155 0.1219 0.1180 0.0047  -0.0023 0.0057  63  TYR   A CA  
446  C C   . TYR   A 57  ? 0.1262 0.1279 0.1257 0.0035  -0.0053 0.0062  63  TYR   A C   
447  O O   . TYR   A 57  ? 0.1389 0.1416 0.1349 0.0018  -0.0063 0.0077  63  TYR   A O   
448  C CB  . TYR   A 57  ? 0.1285 0.1370 0.1304 0.0076  0.0009  0.0073  63  TYR   A CB  
449  C CG  . TYR   A 57  ? 0.1281 0.1350 0.1262 0.0086  0.0038  0.0079  63  TYR   A CG  
450  C CD1 . TYR   A 57  ? 0.1390 0.1520 0.1370 0.0085  0.0050  0.0108  63  TYR   A CD1 
451  C CD2 . TYR   A 57  ? 0.1465 0.1460 0.1407 0.0082  0.0065  0.0049  63  TYR   A CD2 
452  C CE1 . TYR   A 57  ? 0.1601 0.1715 0.1559 0.0093  0.0093  0.0108  63  TYR   A CE1 
453  C CE2 . TYR   A 57  ? 0.1587 0.1554 0.1488 0.0075  0.0119  0.0035  63  TYR   A CE2 
454  C CZ  . TYR   A 57  ? 0.1701 0.1729 0.1622 0.0087  0.0135  0.0065  63  TYR   A CZ  
455  O OH  . TYR   A 57  ? 0.2035 0.2036 0.1931 0.0079  0.0203  0.0048  63  TYR   A OH  
456  N N   . TYR   A 58  ? 0.1242 0.1223 0.1241 0.0028  -0.0071 0.0059  64  TYR   A N   
457  C CA  . TYR   A 58  ? 0.1327 0.1291 0.1279 -0.0017 -0.0110 0.0080  64  TYR   A CA  
458  C C   . TYR   A 58  ? 0.1365 0.1295 0.1205 -0.0042 -0.0073 0.0045  64  TYR   A C   
459  O O   . TYR   A 58  ? 0.1430 0.1324 0.1266 -0.0025 -0.0035 0.0015  64  TYR   A O   
460  C CB  . TYR   A 58  ? 0.1430 0.1393 0.1456 -0.0035 -0.0155 0.0110  64  TYR   A CB  
461  C CG  . TYR   A 58  ? 0.1503 0.1489 0.1479 -0.0112 -0.0212 0.0161  64  TYR   A CG  
462  C CD1 . TYR   A 58  ? 0.1592 0.1619 0.1587 -0.0144 -0.0251 0.0217  64  TYR   A CD1 
463  C CD2 . TYR   A 58  ? 0.1629 0.1605 0.1526 -0.0171 -0.0229 0.0157  64  TYR   A CD2 
464  C CE1 . TYR   A 58  ? 0.1779 0.1857 0.1718 -0.0240 -0.0314 0.0282  64  TYR   A CE1 
465  C CE2 . TYR   A 58  ? 0.1878 0.1899 0.1695 -0.0279 -0.0285 0.0208  64  TYR   A CE2 
466  C CZ  . TYR   A 58  ? 0.1807 0.1890 0.1653 -0.0315 -0.0334 0.0280  64  TYR   A CZ  
467  O OH  . TYR   A 58  ? 0.2250 0.2407 0.2010 -0.0447 -0.0402 0.0351  64  TYR   A OH  
468  N N   . CYS   A 59  ? 0.1426 0.1361 0.1180 -0.0093 -0.0075 0.0047  65  CYS   A N   
469  C CA  . CYS   A 59  ? 0.1562 0.1451 0.1198 -0.0142 -0.0014 -0.0003 65  CYS   A CA  
470  C C   . CYS   A 59  ? 0.1687 0.1581 0.1209 -0.0262 -0.0061 0.0007  65  CYS   A C   
471  O O   . CYS   A 59  ? 0.1718 0.1667 0.1199 -0.0323 -0.0112 0.0051  65  CYS   A O   
472  C CB  . CYS   A 59  ? 0.1660 0.1562 0.1272 -0.0129 0.0035  -0.0013 65  CYS   A CB  
473  S SG  . CYS   A 59  ? 0.1888 0.1714 0.1373 -0.0198 0.0152  -0.0094 65  CYS   A SG  
474  N N   . SER   A 60  ? 0.1740 0.1595 0.1212 -0.0310 -0.0052 -0.0019 66  SER   A N   
475  C CA  . SER   A 60  ? 0.1931 0.1823 0.1290 -0.0452 -0.0113 0.0010  66  SER   A CA  
476  C C   . SER   A 60  ? 0.2023 0.1903 0.1200 -0.0577 -0.0066 -0.0038 66  SER   A C   
477  O O   . SER   A 60  ? 0.2279 0.2244 0.1372 -0.0705 -0.0146 0.0025  66  SER   A O   
478  C CB  . SER   A 60  ? 0.2213 0.2068 0.1543 -0.0491 -0.0110 -0.0012 66  SER   A CB  
479  O OG  . SER   A 60  ? 0.2770 0.2513 0.1998 -0.0518 0.0010  -0.0122 66  SER   A OG  
480  N N   . SER   A 61  ? 0.2041 0.1828 0.1171 -0.0549 0.0067  -0.0138 67  SER   A N   
481  C CA  . SER   A 61  ? 0.2250 0.2011 0.1214 -0.0669 0.0143  -0.0204 67  SER   A CA  
482  C C   . SER   A 61  ? 0.2088 0.1933 0.1052 -0.0672 0.0092  -0.0149 67  SER   A C   
483  O O   . SER   A 61  ? 0.2276 0.2116 0.1094 -0.0785 0.0147  -0.0198 67  SER   A O   
484  C CB  . SER   A 61  ? 0.2441 0.2067 0.1401 -0.0636 0.0324  -0.0323 67  SER   A CB  
485  O OG  . SER   A 61  ? 0.2354 0.1985 0.1497 -0.0470 0.0359  -0.0296 67  SER   A OG  
486  N N   . ARG   A 62  ? 0.1994 0.1912 0.1115 -0.0564 -0.0004 -0.0054 68  ARG   A N   
487  C CA  . ARG   A 62  ? 0.1975 0.1974 0.1112 -0.0572 -0.0067 0.0012  68  ARG   A CA  
488  C C   . ARG   A 62  ? 0.2193 0.2291 0.1434 -0.0585 -0.0209 0.0142  68  ARG   A C   
489  O O   . ARG   A 62  ? 0.2139 0.2302 0.1425 -0.0588 -0.0265 0.0213  68  ARG   A O   
490  C CB  . ARG   A 62  ? 0.2020 0.2003 0.1273 -0.0431 -0.0014 -0.0001 68  ARG   A CB  
491  C CG  . ARG   A 62  ? 0.2134 0.2047 0.1346 -0.0413 0.0130  -0.0093 68  ARG   A CG  
492  C CD  . ARG   A 62  ? 0.2317 0.2246 0.1388 -0.0522 0.0166  -0.0123 68  ARG   A CD  
493  N NE  . ARG   A 62  ? 0.2422 0.2273 0.1489 -0.0502 0.0330  -0.0214 68  ARG   A NE  
494  C CZ  . ARG   A 62  ? 0.2480 0.2232 0.1450 -0.0585 0.0459  -0.0317 68  ARG   A CZ  
495  N NH1 . ARG   A 62  ? 0.2793 0.2519 0.1627 -0.0709 0.0429  -0.0346 68  ARG   A NH1 
496  N NH2 . ARG   A 62  ? 0.2816 0.2493 0.1833 -0.0557 0.0629  -0.0391 68  ARG   A NH2 
497  N N   . ARG   A 63  ? 0.2186 0.2290 0.1507 -0.0571 -0.0257 0.0181  69  ARG   A N   
498  C CA  . ARG   A 63  ? 0.2167 0.2352 0.1671 -0.0547 -0.0365 0.0312  69  ARG   A CA  
499  C C   . ARG   A 63  ? 0.2221 0.2397 0.1879 -0.0426 -0.0356 0.0330  69  ARG   A C   
500  O O   . ARG   A 63  ? 0.2399 0.2642 0.2173 -0.0439 -0.0422 0.0434  69  ARG   A O   
501  C CB  . ARG   A 63  ? 0.2421 0.2733 0.1897 -0.0699 -0.0474 0.0441  69  ARG   A CB  
502  C CG  . ARG   A 63  ? 0.2483 0.2823 0.1832 -0.0830 -0.0498 0.0443  69  ARG   A CG  
503  C CD  . ARG   A 63  ? 0.2884 0.3396 0.2271 -0.0979 -0.0634 0.0623  69  ARG   A CD  
504  N NE  . ARG   A 63  ? 0.3206 0.3772 0.2409 -0.1162 -0.0664 0.0627  69  ARG   A NE  
505  C CZ  . ARG   A 63  ? 0.3113 0.3730 0.2055 -0.1370 -0.0664 0.0602  69  ARG   A CZ  
506  N NH1 . ARG   A 63  ? 0.3118 0.3740 0.1962 -0.1407 -0.0638 0.0573  69  ARG   A NH1 
507  N NH2 . ARG   A 63  ? 0.3327 0.3991 0.2090 -0.1557 -0.0684 0.0598  69  ARG   A NH2 
508  N N   . LYS   A 64  ? 0.1841 0.1947 0.1511 -0.0324 -0.0276 0.0243  70  LYS   A N   
509  C CA  . LYS   A 64  ? 0.1885 0.1990 0.1659 -0.0244 -0.0261 0.0250  70  LYS   A CA  
510  C C   . LYS   A 64  ? 0.1756 0.1815 0.1601 -0.0151 -0.0207 0.0196  70  LYS   A C   
511  O O   . LYS   A 64  ? 0.1800 0.1824 0.1590 -0.0132 -0.0159 0.0138  70  LYS   A O   
512  C CB  . LYS   A 64  ? 0.2205 0.2314 0.1866 -0.0258 -0.0220 0.0213  70  LYS   A CB  
513  C CG  . LYS   A 64  ? 0.3460 0.3633 0.3083 -0.0346 -0.0283 0.0284  70  LYS   A CG  
514  C CD  . LYS   A 64  ? 0.4711 0.4892 0.4254 -0.0344 -0.0240 0.0251  70  LYS   A CD  
515  C CE  . LYS   A 64  ? 0.5597 0.5848 0.5079 -0.0448 -0.0301 0.0319  70  LYS   A CE  
516  N NZ  . LYS   A 64  ? 0.6179 0.6464 0.5530 -0.0580 -0.0332 0.0331  70  LYS   A NZ  
517  N N   . HIS   A 65  ? 0.1552 0.1612 0.1515 -0.0107 -0.0203 0.0211  71  HIS   A N   
518  C CA  . HIS   A 65  ? 0.1517 0.1557 0.1524 -0.0051 -0.0150 0.0161  71  HIS   A CA  
519  C C   . HIS   A 65  ? 0.1647 0.1712 0.1598 -0.0043 -0.0117 0.0142  71  HIS   A C   
520  O O   . HIS   A 65  ? 0.1979 0.2059 0.1935 -0.0065 -0.0133 0.0169  71  HIS   A O   
521  C CB  . HIS   A 65  ? 0.1446 0.1465 0.1606 -0.0036 -0.0145 0.0176  71  HIS   A CB  
522  C CG  . HIS   A 65  ? 0.1552 0.1561 0.1805 -0.0036 -0.0171 0.0208  71  HIS   A CG  
523  N ND1 . HIS   A 65  ? 0.1860 0.1848 0.2149 -0.0009 -0.0141 0.0167  71  HIS   A ND1 
524  C CD2 . HIS   A 65  ? 0.1565 0.1604 0.1891 -0.0070 -0.0233 0.0294  71  HIS   A CD2 
525  C CE1 . HIS   A 65  ? 0.1537 0.1532 0.1925 -0.0019 -0.0180 0.0223  71  HIS   A CE1 
526  N NE2 . HIS   A 65  ? 0.1959 0.1994 0.2375 -0.0058 -0.0238 0.0307  71  HIS   A NE2 
527  N N   . TYR   A 66  ? 0.1461 0.1544 0.1376 -0.0017 -0.0075 0.0112  72  TYR   A N   
528  C CA  . TYR   A 66  ? 0.1425 0.1562 0.1308 -0.0015 -0.0049 0.0118  72  TYR   A CA  
529  C C   . TYR   A 66  ? 0.1328 0.1508 0.1245 -0.0017 -0.0027 0.0113  72  TYR   A C   
530  O O   . TYR   A 66  ? 0.1369 0.1554 0.1312 -0.0002 -0.0014 0.0104  72  TYR   A O   
531  C CB  . TYR   A 66  ? 0.1546 0.1696 0.1390 0.0007  -0.0009 0.0117  72  TYR   A CB  
532  C CG  . TYR   A 66  ? 0.1680 0.1794 0.1446 -0.0023 -0.0005 0.0104  72  TYR   A CG  
533  C CD1 . TYR   A 66  ? 0.2024 0.2167 0.1743 -0.0054 -0.0014 0.0119  72  TYR   A CD1 
534  C CD2 . TYR   A 66  ? 0.1831 0.1887 0.1556 -0.0043 0.0008  0.0073  72  TYR   A CD2 
535  C CE1 . TYR   A 66  ? 0.2031 0.2153 0.1657 -0.0109 -0.0009 0.0104  72  TYR   A CE1 
536  C CE2 . TYR   A 66  ? 0.1960 0.1991 0.1580 -0.0109 0.0018  0.0052  72  TYR   A CE2 
537  C CZ  . TYR   A 66  ? 0.2032 0.2100 0.1600 -0.0144 0.0011  0.0067  72  TYR   A CZ  
538  O OH  . TYR   A 66  ? 0.2357 0.2410 0.1800 -0.0234 0.0027  0.0041  72  TYR   A OH  
539  N N   . PRO   A 67  ? 0.1353 0.1578 0.1254 -0.0052 -0.0021 0.0121  73  PRO   A N   
540  C CA  . PRO   A 67  ? 0.1365 0.1661 0.1262 -0.0092 0.0000  0.0122  73  PRO   A CA  
541  C C   . PRO   A 67  ? 0.1359 0.1761 0.1263 -0.0074 0.0005  0.0183  73  PRO   A C   
542  O O   . PRO   A 67  ? 0.1559 0.1988 0.1460 -0.0050 0.0009  0.0217  73  PRO   A O   
543  C CB  . PRO   A 67  ? 0.1685 0.1993 0.1548 -0.0156 0.0009  0.0110  73  PRO   A CB  
544  C CG  . PRO   A 67  ? 0.1989 0.2269 0.1842 -0.0127 -0.0015 0.0132  73  PRO   A CG  
545  C CD  . PRO   A 67  ? 0.1538 0.1754 0.1416 -0.0074 -0.0036 0.0132  73  PRO   A CD  
546  N N   . VAL   A 68  ? 0.1215 0.1683 0.1145 -0.0092 0.0010  0.0207  74  VAL   A N   
547  C CA  . VAL   A 68  ? 0.1398 0.1984 0.1396 -0.0072 0.0015  0.0299  74  VAL   A CA  
548  C C   . VAL   A 68  ? 0.1363 0.2093 0.1360 -0.0157 0.0000  0.0355  74  VAL   A C   
549  O O   . VAL   A 68  ? 0.1429 0.2145 0.1376 -0.0220 0.0000  0.0305  74  VAL   A O   
550  C CB  . VAL   A 68  ? 0.1665 0.2188 0.1736 0.0005  0.0037  0.0301  74  VAL   A CB  
551  C CG1 . VAL   A 68  ? 0.1850 0.2268 0.1907 0.0059  0.0064  0.0262  74  VAL   A CG1 
552  C CG2 . VAL   A 68  ? 0.1851 0.2309 0.1907 -0.0004 0.0027  0.0246  74  VAL   A CG2 
553  N N   . SER   A 69  ? 0.1318 0.2206 0.1392 -0.0165 -0.0008 0.0478  75  SER   A N   
554  C CA  . SER   A 69  ? 0.1372 0.2446 0.1489 -0.0245 -0.0035 0.0587  75  SER   A CA  
555  C C   . SER   A 69  ? 0.1289 0.2379 0.1566 -0.0162 -0.0022 0.0664  75  SER   A C   
556  O O   . SER   A 69  ? 0.1346 0.2370 0.1730 -0.0056 0.0020  0.0681  75  SER   A O   
557  C CB  . SER   A 69  ? 0.1782 0.3046 0.1941 -0.0298 -0.0057 0.0717  75  SER   A CB  
558  O OG  . SER   A 69  ? 0.2848 0.4089 0.2855 -0.0383 -0.0063 0.0642  75  SER   A OG  
559  N N   . PHE   A 70  ? 0.1211 0.2372 0.1503 -0.0214 -0.0044 0.0700  76  PHE   A N   
560  C CA  . PHE   A 70  ? 0.1263 0.2422 0.1714 -0.0135 -0.0028 0.0769  76  PHE   A CA  
561  C C   . PHE   A 70  ? 0.1344 0.2730 0.1888 -0.0220 -0.0073 0.0932  76  PHE   A C   
562  O O   . PHE   A 70  ? 0.1517 0.3034 0.1939 -0.0368 -0.0118 0.0946  76  PHE   A O   
563  C CB  . PHE   A 70  ? 0.1351 0.2308 0.1735 -0.0084 -0.0006 0.0626  76  PHE   A CB  
564  C CG  . PHE   A 70  ? 0.1263 0.2196 0.1495 -0.0180 -0.0028 0.0527  76  PHE   A CG  
565  C CD1 . PHE   A 70  ? 0.1308 0.2130 0.1414 -0.0205 -0.0016 0.0403  76  PHE   A CD1 
566  C CD2 . PHE   A 70  ? 0.1349 0.2364 0.1588 -0.0245 -0.0048 0.0560  76  PHE   A CD2 
567  C CE1 . PHE   A 70  ? 0.1469 0.2249 0.1477 -0.0288 -0.0006 0.0308  76  PHE   A CE1 
568  C CE2 . PHE   A 70  ? 0.1507 0.2488 0.1613 -0.0341 -0.0044 0.0454  76  PHE   A CE2 
569  C CZ  . PHE   A 70  ? 0.1618 0.2477 0.1621 -0.0358 -0.0013 0.0326  76  PHE   A CZ  
570  N N   . SER   A 71  ? 0.1390 0.2829 0.2159 -0.0143 -0.0054 0.1062  77  SER   A N   
571  C CA  . SER   A 71  ? 0.1482 0.3168 0.2393 -0.0221 -0.0106 0.1264  77  SER   A CA  
572  C C   . SER   A 71  ? 0.1531 0.3214 0.2340 -0.0297 -0.0139 0.1214  77  SER   A C   
573  O O   . SER   A 71  ? 0.1513 0.2988 0.2193 -0.0258 -0.0110 0.1034  77  SER   A O   
574  C CB  . SER   A 71  ? 0.1515 0.3248 0.2757 -0.0100 -0.0057 0.1434  77  SER   A CB  
575  O OG  . SER   A 71  ? 0.1879 0.3386 0.3180 0.0023  0.0019  0.1332  77  SER   A OG  
576  N N   . LYS   A 72  ? 0.1462 0.3390 0.2330 -0.0419 -0.0203 0.1381  78  LYS   A N   
577  C CA  . LYS   A 72  ? 0.1535 0.3489 0.2323 -0.0504 -0.0232 0.1356  78  LYS   A CA  
578  C C   . LYS   A 72  ? 0.1533 0.3368 0.2512 -0.0360 -0.0194 0.1379  78  LYS   A C   
579  O O   . LYS   A 72  ? 0.1767 0.3614 0.3005 -0.0243 -0.0158 0.1508  78  LYS   A O   
580  C CB  . LYS   A 72  ? 0.1800 0.4085 0.2590 -0.0706 -0.0319 0.1549  78  LYS   A CB  
581  C CG  . LYS   A 72  ? 0.2063 0.4437 0.2607 -0.0883 -0.0342 0.1484  78  LYS   A CG  
582  C CD  . LYS   A 72  ? 0.2863 0.5559 0.3324 -0.1140 -0.0424 0.1637  78  LYS   A CD  
583  C CE  . LYS   A 72  ? 0.3564 0.6314 0.3750 -0.1336 -0.0424 0.1538  78  LYS   A CE  
584  N NZ  . LYS   A 72  ? 0.4296 0.7273 0.4282 -0.1629 -0.0470 0.1574  78  LYS   A NZ  
585  N N   . PRO   A 73  ? 0.1508 0.3244 0.2389 -0.0376 -0.0193 0.1273  79  PRO   A N   
586  C CA  . PRO   A 73  ? 0.1520 0.3131 0.2566 -0.0249 -0.0153 0.1286  79  PRO   A CA  
587  C C   . PRO   A 73  ? 0.1678 0.3497 0.3030 -0.0239 -0.0175 0.1553  79  PRO   A C   
588  O O   . PRO   A 73  ? 0.1905 0.3993 0.3278 -0.0385 -0.0256 0.1719  79  PRO   A O   
589  C CB  . PRO   A 73  ? 0.1834 0.3378 0.2701 -0.0319 -0.0171 0.1155  79  PRO   A CB  
590  C CG  . PRO   A 73  ? 0.2220 0.3721 0.2831 -0.0414 -0.0172 0.0993  79  PRO   A CG  
591  C CD  . PRO   A 73  ? 0.1876 0.3577 0.2487 -0.0507 -0.0208 0.1111  79  PRO   A CD  
592  N N   . SER   A 74  ? 0.1681 0.3380 0.3276 -0.0082 -0.0095 0.1598  80  SER   A N   
593  C CA  . SER   A 74  ? 0.1743 0.3618 0.3709 -0.0044 -0.0087 0.1869  80  SER   A CA  
594  C C   . SER   A 74  ? 0.1669 0.3325 0.3849 0.0112  0.0026  0.1842  80  SER   A C   
595  O O   . SER   A 74  ? 0.1531 0.2910 0.3558 0.0184  0.0096  0.1618  80  SER   A O   
596  C CB  . SER   A 74  ? 0.2266 0.4275 0.4403 -0.0022 -0.0071 0.2010  80  SER   A CB  
597  O OG  . SER   A 74  ? 0.3460 0.5579 0.5348 -0.0144 -0.0142 0.1960  80  SER   A OG  
598  N N   . LEU   A 75  ? 0.1743 0.3537 0.4322 0.0161  0.0057  0.2096  81  LEU   A N   
599  C CA  . LEU   A 75  ? 0.1951 0.3546 0.4795 0.0302  0.0192  0.2098  81  LEU   A CA  
600  C C   . LEU   A 75  ? 0.1955 0.3461 0.5011 0.0415  0.0323  0.2114  81  LEU   A C   
601  O O   . LEU   A 75  ? 0.2187 0.3923 0.5525 0.0415  0.0311  0.2353  81  LEU   A O   
602  C CB  . LEU   A 75  ? 0.1967 0.3780 0.5166 0.0284  0.0156  0.2391  81  LEU   A CB  
603  C CG  . LEU   A 75  ? 0.2539 0.4157 0.6049 0.0415  0.0300  0.2416  81  LEU   A CG  
604  C CD1 . LEU   A 75  ? 0.2880 0.4227 0.6106 0.0423  0.0326  0.2155  81  LEU   A CD1 
605  C CD2 . LEU   A 75  ? 0.2496 0.4380 0.6421 0.0395  0.0255  0.2762  81  LEU   A CD2 
606  N N   . ILE   A 76  ? 0.2001 0.3199 0.4928 0.0496  0.0446  0.1874  82  ILE   A N   
607  C CA  . ILE   A 76  ? 0.2067 0.3143 0.5116 0.0584  0.0585  0.1827  82  ILE   A CA  
608  C C   . ILE   A 76  ? 0.2191 0.2979 0.5412 0.0688  0.0786  0.1725  82  ILE   A C   
609  O O   . ILE   A 76  ? 0.2184 0.2770 0.5212 0.0678  0.0807  0.1549  82  ILE   A O   
610  C CB  . ILE   A 76  ? 0.2525 0.3497 0.5165 0.0538  0.0543  0.1594  82  ILE   A CB  
611  C CG1 . ILE   A 76  ? 0.2764 0.3992 0.5209 0.0418  0.0364  0.1665  82  ILE   A CG1 
612  C CG2 . ILE   A 76  ? 0.2730 0.3555 0.5436 0.0612  0.0688  0.1510  82  ILE   A CG2 
613  C CD1 . ILE   A 76  ? 0.2886 0.4066 0.5045 0.0379  0.0329  0.1512  82  ILE   A CD1 
614  N N   . PHE   A 77  ? 0.2157 0.2918 0.5746 0.0778  0.0946  0.1830  83  PHE   A N   
615  C CA  . PHE   A 77  ? 0.2326 0.2788 0.6073 0.0860  0.1176  0.1707  83  PHE   A CA  
616  C C   . PHE   A 77  ? 0.2739 0.2952 0.6107 0.0833  0.1245  0.1399  83  PHE   A C   
617  O O   . PHE   A 77  ? 0.3081 0.3355 0.6314 0.0814  0.1210  0.1362  83  PHE   A O   
618  C CB  . PHE   A 77  ? 0.2254 0.2769 0.6549 0.0962  0.1350  0.1919  83  PHE   A CB  
619  C CG  . PHE   A 77  ? 0.2707 0.2915 0.7224 0.1035  0.1605  0.1816  83  PHE   A CG  
620  C CD1 . PHE   A 77  ? 0.3027 0.3185 0.7706 0.1049  0.1624  0.1881  83  PHE   A CD1 
621  C CD2 . PHE   A 77  ? 0.3279 0.3234 0.7808 0.1069  0.1833  0.1631  83  PHE   A CD2 
622  C CE1 . PHE   A 77  ? 0.3394 0.3252 0.8280 0.1105  0.1877  0.1777  83  PHE   A CE1 
623  C CE2 . PHE   A 77  ? 0.3422 0.3078 0.8150 0.1113  0.2095  0.1519  83  PHE   A CE2 
624  C CZ  . PHE   A 77  ? 0.3538 0.3141 0.8446 0.1132  0.2118  0.1591  83  PHE   A CZ  
625  N N   . VAL   A 78  ? 0.2683 0.2635 0.5841 0.0810  0.1316  0.1182  84  VAL   A N   
626  C CA  . VAL   A 78  ? 0.2823 0.2552 0.5621 0.0758  0.1376  0.0906  84  VAL   A CA  
627  C C   . VAL   A 78  ? 0.2977 0.2421 0.5932 0.0786  0.1647  0.0784  84  VAL   A C   
628  O O   . VAL   A 78  ? 0.3014 0.2352 0.6129 0.0807  0.1729  0.0801  84  VAL   A O   
629  C CB  . VAL   A 78  ? 0.2742 0.2427 0.5119 0.0672  0.1218  0.0753  84  VAL   A CB  
630  C CG1 . VAL   A 78  ? 0.3051 0.2547 0.5073 0.0602  0.1259  0.0505  84  VAL   A CG1 
631  C CG2 . VAL   A 78  ? 0.2600 0.2552 0.4859 0.0637  0.0984  0.0870  84  VAL   A CG2 
632  N N   . GLU   A 79  ? 0.3120 0.2426 0.5979 0.0765  0.1783  0.0635  85  GLU   A N   
633  C CA  . GLU   A 79  ? 0.3495 0.2509 0.6458 0.0759  0.2069  0.0480  85  GLU   A CA  
634  C C   . GLU   A 79  ? 0.3840 0.2631 0.6480 0.0658  0.2092  0.0262  85  GLU   A C   
635  O O   . GLU   A 79  ? 0.3886 0.2743 0.6178 0.0591  0.1887  0.0204  85  GLU   A O   
636  C CB  . GLU   A 79  ? 0.3943 0.2874 0.6831 0.0731  0.2206  0.0357  85  GLU   A CB  
637  C CG  . GLU   A 79  ? 0.4543 0.3661 0.7819 0.0834  0.2243  0.0570  85  GLU   A CG  
638  C CD  . GLU   A 79  ? 0.5460 0.4580 0.9320 0.0952  0.2422  0.0770  85  GLU   A CD  
639  O OE1 . GLU   A 79  ? 0.5701 0.4558 0.9700 0.0953  0.2661  0.0657  85  GLU   A OE1 
640  O OE2 . GLU   A 79  ? 0.5743 0.5135 0.9932 0.1033  0.2321  0.1050  85  GLU   A OE2 
641  N N   . ALA   A 80  ? 0.4054 0.2577 0.6820 0.0640  0.2357  0.0138  86  ALA   A N   
642  C CA  . ALA   A 80  ? 0.4461 0.2760 0.6931 0.0523  0.2410  -0.0072 86  ALA   A CA  
643  C C   . ALA   A 80  ? 0.4866 0.3131 0.6818 0.0375  0.2312  -0.0275 86  ALA   A C   
644  O O   . ALA   A 80  ? 0.4933 0.3230 0.6782 0.0348  0.2330  -0.0325 86  ALA   A O   
645  C CB  . ALA   A 80  ? 0.4683 0.2684 0.7374 0.0507  0.2752  -0.0190 86  ALA   A CB  
646  N N   . SER   A 81  ? 0.4944 0.3176 0.6587 0.0282  0.2189  -0.0365 87  SER   A N   
647  C CA  . SER   A 81  ? 0.5145 0.3361 0.6319 0.0128  0.2082  -0.0530 87  SER   A CA  
648  C C   . SER   A 81  ? 0.5176 0.3170 0.6137 -0.0017 0.2189  -0.0709 87  SER   A C   
649  O O   . SER   A 81  ? 0.5078 0.2932 0.6269 0.0021  0.2346  -0.0704 87  SER   A O   
650  C CB  . SER   A 81  ? 0.5335 0.3792 0.6347 0.0151  0.1774  -0.0422 87  SER   A CB  
651  O OG  . SER   A 81  ? 0.5317 0.3792 0.6343 0.0166  0.1678  -0.0372 87  SER   A OG  
652  N N   . GLU   A 82  ? 0.5268 0.3255 0.5807 -0.0186 0.2084  -0.0840 88  GLU   A N   
653  C CA  . GLU   A 82  ? 0.5315 0.3127 0.5637 -0.0341 0.2156  -0.0987 88  GLU   A CA  
654  C C   . GLU   A 82  ? 0.4882 0.2765 0.5308 -0.0260 0.2013  -0.0871 88  GLU   A C   
655  O O   . GLU   A 82  ? 0.5058 0.2779 0.5452 -0.0334 0.2117  -0.0954 88  GLU   A O   
656  C CB  . GLU   A 82  ? 0.5884 0.3738 0.5749 -0.0547 0.2030  -0.1101 88  GLU   A CB  
657  C CG  . GLU   A 82  ? 0.7091 0.4923 0.6786 -0.0657 0.2116  -0.1204 88  GLU   A CG  
658  C CD  . GLU   A 82  ? 0.8452 0.6479 0.7843 -0.0751 0.1869  -0.1172 88  GLU   A CD  
659  O OE1 . GLU   A 82  ? 0.8861 0.6926 0.8006 -0.0886 0.1744  -0.1195 88  GLU   A OE1 
660  O OE2 . GLU   A 82  ? 0.8676 0.6826 0.8100 -0.0692 0.1804  -0.1111 88  GLU   A OE2 
661  N N   . TYR   A 83  ? 0.4459 0.2574 0.5017 -0.0119 0.1796  -0.0687 89  TYR   A N   
662  C CA  . TYR   A 83  ? 0.4010 0.2225 0.4612 -0.0066 0.1636  -0.0584 89  TYR   A CA  
663  C C   . TYR   A 83  ? 0.3729 0.1990 0.4727 0.0093  0.1669  -0.0418 89  TYR   A C   
664  O O   . TYR   A 83  ? 0.3648 0.1928 0.4698 0.0112  0.1603  -0.0362 89  TYR   A O   
665  C CB  . TYR   A 83  ? 0.3911 0.2353 0.4344 -0.0058 0.1373  -0.0510 89  TYR   A CB  
666  C CG  . TYR   A 83  ? 0.4104 0.2529 0.4177 -0.0220 0.1316  -0.0635 89  TYR   A CG  
667  C CD1 . TYR   A 83  ? 0.4413 0.2796 0.4264 -0.0349 0.1262  -0.0706 89  TYR   A CD1 
668  C CD2 . TYR   A 83  ? 0.4372 0.2825 0.4337 -0.0262 0.1330  -0.0676 89  TYR   A CD2 
669  C CE1 . TYR   A 83  ? 0.4809 0.3221 0.4352 -0.0512 0.1187  -0.0781 89  TYR   A CE1 
670  C CE2 . TYR   A 83  ? 0.4765 0.3228 0.4413 -0.0428 0.1268  -0.0766 89  TYR   A CE2 
671  C CZ  . TYR   A 83  ? 0.5053 0.3501 0.4495 -0.0557 0.1196  -0.0811 89  TYR   A CZ  
672  O OH  . TYR   A 83  ? 0.5444 0.3943 0.4595 -0.0733 0.1115  -0.0862 89  TYR   A OH  
673  N N   . TYR   A 84  ? 0.3836 0.2140 0.5125 0.0201  0.1760  -0.0320 90  TYR   A N   
674  C CA  . TYR   A 84  ? 0.3589 0.1984 0.5286 0.0341  0.1773  -0.0118 90  TYR   A CA  
675  C C   . TYR   A 84  ? 0.3910 0.2189 0.5944 0.0406  0.2022  -0.0094 90  TYR   A C   
676  O O   . TYR   A 84  ? 0.4106 0.2362 0.6071 0.0384  0.2093  -0.0166 90  TYR   A O   
677  C CB  . TYR   A 84  ? 0.3285 0.1984 0.5046 0.0422  0.1541  0.0074  90  TYR   A CB  
678  C CG  . TYR   A 84  ? 0.3043 0.1875 0.4534 0.0373  0.1306  0.0071  90  TYR   A CG  
679  C CD1 . TYR   A 84  ? 0.2959 0.1799 0.4477 0.0370  0.1247  0.0112  90  TYR   A CD1 
680  C CD2 . TYR   A 84  ? 0.2900 0.1842 0.4126 0.0329  0.1156  0.0025  90  TYR   A CD2 
681  C CE1 . TYR   A 84  ? 0.2791 0.1746 0.4081 0.0325  0.1052  0.0102  90  TYR   A CE1 
682  C CE2 . TYR   A 84  ? 0.2770 0.1821 0.3793 0.0290  0.0969  0.0024  90  TYR   A CE2 
683  C CZ  . TYR   A 84  ? 0.2607 0.1655 0.3656 0.0285  0.0926  0.0051  90  TYR   A CZ  
684  O OH  . TYR   A 84  ? 0.2563 0.1713 0.3442 0.0248  0.0761  0.0048  90  TYR   A OH  
685  N N   . PRO   A 85  ? 0.4034 0.2281 0.6473 0.0499  0.2140  0.0042  91  PRO   A N   
686  C CA  . PRO   A 85  ? 0.4125 0.2308 0.6986 0.0591  0.2371  0.0121  91  PRO   A CA  
687  C C   . PRO   A 85  ? 0.4019 0.2503 0.7050 0.0686  0.2214  0.0338  91  PRO   A C   
688  O O   . PRO   A 85  ? 0.3850 0.2569 0.6687 0.0677  0.1946  0.0421  91  PRO   A O   
689  C CB  . PRO   A 85  ? 0.4278 0.2398 0.7544 0.0666  0.2482  0.0257  91  PRO   A CB  
690  C CG  . PRO   A 85  ? 0.4329 0.2654 0.7470 0.0666  0.2207  0.0375  91  PRO   A CG  
691  C CD  . PRO   A 85  ? 0.4031 0.2323 0.6612 0.0534  0.2064  0.0159  91  PRO   A CD  
692  N N   . ALA   A 86  ? 0.4101 0.2596 0.7517 0.0774  0.2380  0.0447  92  ALA   A N   
693  C CA  . ALA   A 86  ? 0.3986 0.2786 0.7608 0.0857  0.2237  0.0685  92  ALA   A CA  
694  C C   . ALA   A 86  ? 0.3687 0.2717 0.7555 0.0913  0.2070  0.0950  92  ALA   A C   
695  O O   . ALA   A 86  ? 0.3988 0.2918 0.8131 0.0950  0.2183  0.1014  92  ALA   A O   
696  C CB  . ALA   A 86  ? 0.3925 0.2677 0.7983 0.0944  0.2480  0.0768  92  ALA   A CB  
697  N N   . ARG   A 87  ? 0.3405 0.2718 0.7105 0.0891  0.1801  0.1066  93  ARG   A N   
698  C CA  . ARG   A 87  ? 0.3002 0.2544 0.6827 0.0899  0.1621  0.1282  93  ARG   A CA  
699  C C   . ARG   A 87  ? 0.2797 0.2658 0.6467 0.0861  0.1375  0.1406  93  ARG   A C   
700  O O   . ARG   A 87  ? 0.2874 0.2749 0.6302 0.0832  0.1335  0.1298  93  ARG   A O   
701  C CB  . ARG   A 87  ? 0.3115 0.2524 0.6605 0.0825  0.1547  0.1115  93  ARG   A CB  
702  C CG  . ARG   A 87  ? 0.3219 0.2668 0.6181 0.0731  0.1357  0.0939  93  ARG   A CG  
703  C CD  . ARG   A 87  ? 0.3435 0.2698 0.6061 0.0656  0.1341  0.0728  93  ARG   A CD  
704  N NE  . ARG   A 87  ? 0.3624 0.3031 0.5911 0.0589  0.1113  0.0689  93  ARG   A NE  
705  C CZ  . ARG   A 87  ? 0.3843 0.3307 0.5849 0.0545  0.1012  0.0599  93  ARG   A CZ  
706  N NH1 . ARG   A 87  ? 0.3150 0.2712 0.4899 0.0489  0.0838  0.0562  93  ARG   A NH1 
707  N NH2 . ARG   A 87  ? 0.3801 0.3221 0.5799 0.0558  0.1093  0.0548  93  ARG   A NH2 
708  N N   . TYR   A 88  ? 0.2693 0.2799 0.6467 0.0841  0.1212  0.1613  94  TYR   A N   
709  C CA  . TYR   A 88  ? 0.2682 0.3076 0.6268 0.0770  0.0985  0.1709  94  TYR   A CA  
710  C C   . TYR   A 88  ? 0.2413 0.2745 0.5526 0.0681  0.0850  0.1504  94  TYR   A C   
711  O O   . TYR   A 88  ? 0.2556 0.2817 0.5625 0.0663  0.0833  0.1469  94  TYR   A O   
712  C CB  . TYR   A 88  ? 0.2617 0.3319 0.6540 0.0760  0.0883  0.2037  94  TYR   A CB  
713  C CG  . TYR   A 88  ? 0.2619 0.3481 0.7001 0.0830  0.0963  0.2288  94  TYR   A CG  
714  C CD1 . TYR   A 88  ? 0.2747 0.3820 0.7071 0.0794  0.0872  0.2367  94  TYR   A CD1 
715  C CD2 . TYR   A 88  ? 0.2618 0.3401 0.7506 0.0935  0.1150  0.2438  94  TYR   A CD2 
716  C CE1 . TYR   A 88  ? 0.2784 0.4018 0.7543 0.0856  0.0944  0.2609  94  TYR   A CE1 
717  C CE2 . TYR   A 88  ? 0.2639 0.3572 0.7998 0.1008  0.1238  0.2683  94  TYR   A CE2 
718  C CZ  . TYR   A 88  ? 0.2799 0.3964 0.8086 0.0969  0.1130  0.2768  94  TYR   A CZ  
719  O OH  . TYR   A 88  ? 0.3138 0.4471 0.8895 0.1036  0.1209  0.3022  94  TYR   A OH  
720  N N   . GLN   A 89  ? 0.2025 0.2405 0.4805 0.0625  0.0748  0.1385  95  GLN   A N   
721  C CA  . GLN   A 89  ? 0.1895 0.2245 0.4265 0.0542  0.0619  0.1212  95  GLN   A CA  
722  C C   . GLN   A 89  ? 0.1652 0.2297 0.3955 0.0461  0.0443  0.1349  95  GLN   A C   
723  O O   . GLN   A 89  ? 0.1803 0.2619 0.4191 0.0450  0.0412  0.1467  95  GLN   A O   
724  C CB  . GLN   A 89  ? 0.2149 0.2315 0.4222 0.0531  0.0655  0.0978  95  GLN   A CB  
725  C CG  . GLN   A 89  ? 0.2154 0.2295 0.3874 0.0458  0.0535  0.0829  95  GLN   A CG  
726  C CD  . GLN   A 89  ? 0.1886 0.1819 0.3348 0.0441  0.0581  0.0610  95  GLN   A CD  
727  O OE1 . GLN   A 89  ? 0.2339 0.2076 0.3823 0.0461  0.0718  0.0515  95  GLN   A OE1 
728  N NE2 . GLN   A 89  ? 0.1935 0.1911 0.3145 0.0387  0.0471  0.0527  95  GLN   A NE2 
729  N N   . SER   A 90  ? 0.1646 0.2359 0.3799 0.0388  0.0336  0.1336  96  SER   A N   
730  C CA  . SER   A 90  ? 0.1525 0.2506 0.3593 0.0278  0.0190  0.1447  96  SER   A CA  
731  C C   . SER   A 90  ? 0.1578 0.2516 0.3271 0.0208  0.0123  0.1248  96  SER   A C   
732  O O   . SER   A 90  ? 0.1621 0.2335 0.3131 0.0243  0.0167  0.1044  96  SER   A O   
733  C CB  . SER   A 90  ? 0.1790 0.2885 0.3925 0.0222  0.0126  0.1555  96  SER   A CB  
734  O OG  . SER   A 90  ? 0.2195 0.3091 0.4114 0.0224  0.0136  0.1355  96  SER   A OG  
735  N N   . HIS   A 91  ? 0.1452 0.2612 0.3052 0.0098  0.0025  0.1321  97  HIS   A N   
736  C CA  . HIS   A 91  ? 0.1478 0.2619 0.2769 0.0016  -0.0026 0.1157  97  HIS   A CA  
737  C C   . HIS   A 91  ? 0.1325 0.2288 0.2515 0.0088  0.0031  0.1011  97  HIS   A C   
738  O O   . HIS   A 91  ? 0.1551 0.2384 0.2522 0.0072  0.0025  0.0834  97  HIS   A O   
739  C CB  . HIS   A 91  ? 0.1708 0.2756 0.2825 -0.0025 -0.0050 0.1021  97  HIS   A CB  
740  C CG  . HIS   A 91  ? 0.1801 0.3037 0.2978 -0.0120 -0.0112 0.1154  97  HIS   A CG  
741  N ND1 . HIS   A 91  ? 0.2039 0.3455 0.3059 -0.0279 -0.0181 0.1164  97  HIS   A ND1 
742  C CD2 . HIS   A 91  ? 0.2130 0.3402 0.3510 -0.0088 -0.0107 0.1285  97  HIS   A CD2 
743  C CE1 . HIS   A 91  ? 0.2100 0.3670 0.3213 -0.0349 -0.0227 0.1302  97  HIS   A CE1 
744  N NE2 . HIS   A 91  ? 0.2265 0.3757 0.3606 -0.0230 -0.0190 0.1386  97  HIS   A NE2 
745  N N   . LEU   A 92  ? 0.1241 0.2216 0.2600 0.0154  0.0085  0.1095  98  LEU   A N   
746  C CA  . LEU   A 92  ? 0.1420 0.2233 0.2704 0.0217  0.0149  0.0969  98  LEU   A CA  
747  C C   . LEU   A 92  ? 0.1385 0.2351 0.2628 0.0165  0.0106  0.1026  98  LEU   A C   
748  O O   . LEU   A 92  ? 0.1396 0.2584 0.2799 0.0125  0.0070  0.1217  98  LEU   A O   
749  C CB  . LEU   A 92  ? 0.1602 0.2292 0.3120 0.0327  0.0275  0.1006  98  LEU   A CB  
750  C CG  . LEU   A 92  ? 0.1817 0.2326 0.3243 0.0375  0.0360  0.0863  98  LEU   A CG  
751  C CD1 . LEU   A 92  ? 0.1908 0.2226 0.3077 0.0356  0.0355  0.0660  98  LEU   A CD1 
752  C CD2 . LEU   A 92  ? 0.2127 0.2529 0.3812 0.0463  0.0516  0.0905  98  LEU   A CD2 
753  N N   . MET   A 93  ? 0.1319 0.2180 0.2359 0.0157  0.0105  0.0877  99  MET   A N   
754  C CA  . MET   A 93  ? 0.1325 0.2299 0.2299 0.0106  0.0071  0.0903  99  MET   A CA  
755  C C   . MET   A 93  ? 0.1364 0.2202 0.2353 0.0188  0.0146  0.0838  99  MET   A C   
756  O O   . MET   A 93  ? 0.1498 0.2136 0.2395 0.0233  0.0192  0.0695  99  MET   A O   
757  C CB  . MET   A 93  ? 0.1396 0.2349 0.2116 0.0015  0.0015  0.0772  99  MET   A CB  
758  C CG  . MET   A 93  ? 0.1458 0.2535 0.2136 -0.0088 -0.0040 0.0812  99  MET   A CG  
759  S SD  . MET   A 93  ? 0.2006 0.3012 0.2428 -0.0191 -0.0059 0.0631  99  MET   A SD  
760  C CE  . MET   A 93  ? 0.2177 0.2912 0.2576 -0.0067 -0.0015 0.0478  99  MET   A CE  
761  N N   . LEU   A 94  ? 0.1163 0.2119 0.2260 0.0194  0.0158  0.0943  100 LEU   A N   
762  C CA  . LEU   A 94  ? 0.1288 0.2122 0.2396 0.0261  0.0239  0.0876  100 LEU   A CA  
763  C C   . LEU   A 94  ? 0.1266 0.2140 0.2200 0.0206  0.0190  0.0825  100 LEU   A C   
764  O O   . LEU   A 94  ? 0.1414 0.2468 0.2316 0.0122  0.0115  0.0909  100 LEU   A O   
765  C CB  . LEU   A 94  ? 0.1496 0.2406 0.2919 0.0333  0.0327  0.1036  100 LEU   A CB  
766  C CG  . LEU   A 94  ? 0.2078 0.2908 0.3724 0.0405  0.0418  0.1082  100 LEU   A CG  
767  C CD1 . LEU   A 94  ? 0.2204 0.3100 0.4211 0.0484  0.0532  0.1244  100 LEU   A CD1 
768  C CD2 . LEU   A 94  ? 0.2612 0.3164 0.4118 0.0439  0.0502  0.0877  100 LEU   A CD2 
769  N N   . ALA   A 95  ? 0.1368 0.2085 0.2198 0.0239  0.0237  0.0699  101 ALA   A N   
770  C CA  . ALA   A 95  ? 0.1356 0.2096 0.2053 0.0200  0.0205  0.0659  101 ALA   A CA  
771  C C   . ALA   A 95  ? 0.1399 0.2031 0.2130 0.0257  0.0298  0.0611  101 ALA   A C   
772  O O   . ALA   A 95  ? 0.1452 0.1951 0.2249 0.0308  0.0390  0.0562  101 ALA   A O   
773  C CB  . ALA   A 95  ? 0.1405 0.2046 0.1873 0.0148  0.0146  0.0520  101 ALA   A CB  
774  N N   . VAL   A 96  ? 0.1223 0.1903 0.1888 0.0232  0.0281  0.0611  102 VAL   A N   
775  C CA  . VAL   A 96  ? 0.1214 0.1794 0.1863 0.0261  0.0362  0.0545  102 VAL   A CA  
776  C C   . VAL   A 96  ? 0.1460 0.1889 0.1872 0.0221  0.0329  0.0392  102 VAL   A C   
777  O O   . VAL   A 96  ? 0.1703 0.2159 0.1986 0.0173  0.0243  0.0369  102 VAL   A O   
778  C CB  . VAL   A 96  ? 0.1265 0.1985 0.1966 0.0249  0.0355  0.0633  102 VAL   A CB  
779  C CG1 . VAL   A 96  ? 0.1558 0.2176 0.2215 0.0263  0.0439  0.0553  102 VAL   A CG1 
780  C CG2 . VAL   A 96  ? 0.1303 0.2204 0.2279 0.0282  0.0381  0.0821  102 VAL   A CG2 
781  N N   . GLY   A 97  ? 0.1605 0.1884 0.1987 0.0233  0.0408  0.0302  103 GLY   A N   
782  C CA  . GLY   A 97  ? 0.1820 0.1985 0.1998 0.0178  0.0371  0.0186  103 GLY   A CA  
783  C C   . GLY   A 97  ? 0.1987 0.2007 0.2134 0.0166  0.0469  0.0099  103 GLY   A C   
784  O O   . GLY   A 97  ? 0.2293 0.2271 0.2579 0.0208  0.0574  0.0111  103 GLY   A O   
785  N N   . HIS   A 98  ? 0.2189 0.2132 0.2146 0.0090  0.0438  0.0012  104 HIS   A N   
786  C CA  . HIS   A 98  ? 0.2424 0.2237 0.2287 0.0030  0.0521  -0.0084 104 HIS   A CA  
787  C C   . HIS   A 98  ? 0.2309 0.2062 0.2162 0.0026  0.0499  -0.0108 104 HIS   A C   
788  O O   . HIS   A 98  ? 0.2297 0.2099 0.2112 0.0022  0.0375  -0.0077 104 HIS   A O   
789  C CB  . HIS   A 98  ? 0.2524 0.2327 0.2187 -0.0077 0.0478  -0.0136 104 HIS   A CB  
790  C CG  . HIS   A 98  ? 0.2694 0.2380 0.2228 -0.0177 0.0579  -0.0241 104 HIS   A CG  
791  N ND1 . HIS   A 98  ? 0.2827 0.2434 0.2402 -0.0185 0.0752  -0.0304 104 HIS   A ND1 
792  C CD2 . HIS   A 98  ? 0.3094 0.2733 0.2469 -0.0285 0.0541  -0.0291 104 HIS   A CD2 
793  C CE1 . HIS   A 98  ? 0.3164 0.2662 0.2580 -0.0308 0.0822  -0.0411 104 HIS   A CE1 
794  N NE2 . HIS   A 98  ? 0.3283 0.2812 0.2566 -0.0376 0.0685  -0.0396 104 HIS   A NE2 
795  N N   . SER   A 99  ? 0.2392 0.2034 0.2276 0.0018  0.0617  -0.0165 105 SER   A N   
796  C CA  . SER   A 99  ? 0.2626 0.2206 0.2493 0.0006  0.0602  -0.0190 105 SER   A CA  
797  C C   . SER   A 99  ? 0.3057 0.2479 0.2873 -0.0062 0.0762  -0.0299 105 SER   A C   
798  O O   . SER   A 99  ? 0.3306 0.2662 0.3291 -0.0006 0.0911  -0.0304 105 SER   A O   
799  C CB  . SER   A 99  ? 0.2820 0.2465 0.2885 0.0110  0.0578  -0.0098 105 SER   A CB  
800  O OG  . SER   A 99  ? 0.3928 0.3599 0.4194 0.0183  0.0681  -0.0039 105 SER   A OG  
801  N N   . GLU   A 100 ? 0.2770 0.2134 0.2381 -0.0184 0.0734  -0.0375 106 GLU   A N   
802  C CA  . GLU   A 100 ? 0.2961 0.2169 0.2469 -0.0289 0.0875  -0.0495 106 GLU   A CA  
803  C C   . GLU   A 100 ? 0.3289 0.2462 0.2808 -0.0285 0.0832  -0.0491 106 GLU   A C   
804  O O   . GLU   A 100 ? 0.3054 0.2329 0.2625 -0.0222 0.0684  -0.0403 106 GLU   A O   
805  C CB  . GLU   A 100 ? 0.3200 0.2409 0.2432 -0.0472 0.0845  -0.0567 106 GLU   A CB  
806  C CG  . GLU   A 100 ? 0.3166 0.2411 0.2372 -0.0489 0.0887  -0.0575 106 GLU   A CG  
807  C CD  . GLU   A 100 ? 0.3523 0.2793 0.2459 -0.0683 0.0857  -0.0630 106 GLU   A CD  
808  O OE1 . GLU   A 100 ? 0.4462 0.3672 0.3200 -0.0853 0.0887  -0.0710 106 GLU   A OE1 
809  O OE2 . GLU   A 100 ? 0.3630 0.2989 0.2549 -0.0680 0.0808  -0.0588 106 GLU   A OE2 
810  N N   . PRO   A 101 ? 0.3571 0.2586 0.3054 -0.0355 0.0981  -0.0592 107 PRO   A N   
811  C CA  . PRO   A 101 ? 0.3857 0.2837 0.3303 -0.0382 0.0934  -0.0598 107 PRO   A CA  
812  C C   . PRO   A 101 ? 0.4229 0.3253 0.3388 -0.0566 0.0833  -0.0637 107 PRO   A C   
813  O O   . PRO   A 101 ? 0.4934 0.3904 0.3875 -0.0742 0.0907  -0.0735 107 PRO   A O   
814  C CB  . PRO   A 101 ? 0.3814 0.2594 0.3277 -0.0437 0.1154  -0.0717 107 PRO   A CB  
815  C CG  . PRO   A 101 ? 0.3942 0.2653 0.3492 -0.0419 0.1325  -0.0765 107 PRO   A CG  
816  C CD  . PRO   A 101 ? 0.3700 0.2554 0.3152 -0.0433 0.1206  -0.0719 107 PRO   A CD  
817  N N   . GLY   A 102 ? 0.3116 0.2264 0.2311 -0.0514 0.0660  -0.0538 108 GLY   A N   
818  C CA  . GLY   A 102 ? 0.2978 0.2245 0.2056 -0.0597 0.0487  -0.0476 108 GLY   A CA  
819  C C   . GLY   A 102 ? 0.2475 0.1878 0.1710 -0.0459 0.0350  -0.0357 108 GLY   A C   
820  O O   . GLY   A 102 ? 0.2542 0.2037 0.1781 -0.0473 0.0219  -0.0285 108 GLY   A O   
821  N N   . ASP   A 103 ? 0.2266 0.1690 0.1631 -0.0341 0.0384  -0.0331 109 ASP   A N   
822  C CA  . ASP   A 103 ? 0.2052 0.1592 0.1545 -0.0235 0.0276  -0.0237 109 ASP   A CA  
823  C C   . ASP   A 103 ? 0.1994 0.1555 0.1631 -0.0137 0.0245  -0.0194 109 ASP   A C   
824  O O   . ASP   A 103 ? 0.1891 0.1542 0.1606 -0.0083 0.0155  -0.0131 109 ASP   A O   
825  C CB  . ASP   A 103 ? 0.2014 0.1582 0.1579 -0.0168 0.0323  -0.0221 109 ASP   A CB  
826  C CG  . ASP   A 103 ? 0.2111 0.1701 0.1536 -0.0264 0.0308  -0.0239 109 ASP   A CG  
827  O OD1 . ASP   A 103 ? 0.2210 0.1858 0.1544 -0.0347 0.0202  -0.0207 109 ASP   A OD1 
828  O OD2 . ASP   A 103 ? 0.2189 0.1755 0.1616 -0.0257 0.0400  -0.0270 109 ASP   A OD2 
829  N N   . CYS   A 104 ? 0.2089 0.1565 0.1764 -0.0123 0.0327  -0.0230 110 CYS   A N   
830  C CA  . CYS   A 104 ? 0.1985 0.1491 0.1783 -0.0048 0.0291  -0.0185 110 CYS   A CA  
831  C C   . CYS   A 104 ? 0.1931 0.1503 0.1696 -0.0076 0.0169  -0.0153 110 CYS   A C   
832  O O   . CYS   A 104 ? 0.2057 0.1621 0.1709 -0.0171 0.0129  -0.0169 110 CYS   A O   
833  C CB  . CYS   A 104 ? 0.2169 0.1562 0.1995 -0.0054 0.0394  -0.0229 110 CYS   A CB  
834  S SG  . CYS   A 104 ? 0.2481 0.1817 0.2492 0.0031  0.0552  -0.0217 110 CYS   A SG  
835  N N   . GLY   A 105 ? 0.1620 0.1272 0.1499 -0.0005 0.0114  -0.0099 111 GLY   A N   
836  C CA  . GLY   A 105 ? 0.1649 0.1359 0.1548 -0.0018 0.0024  -0.0069 111 GLY   A CA  
837  C C   . GLY   A 105 ? 0.1478 0.1262 0.1417 -0.0004 -0.0030 -0.0031 111 GLY   A C   
838  O O   . GLY   A 105 ? 0.1553 0.1382 0.1567 0.0005  -0.0077 -0.0004 111 GLY   A O   
839  N N   . GLY   A 106 ? 0.1489 0.1278 0.1389 -0.0008 -0.0012 -0.0034 112 GLY   A N   
840  C CA  . GLY   A 106 ? 0.1444 0.1293 0.1387 0.0005  -0.0053 0.0000  112 GLY   A CA  
841  C C   . GLY   A 106 ? 0.1264 0.1159 0.1300 0.0056  -0.0044 0.0009  112 GLY   A C   
842  O O   . GLY   A 106 ? 0.1301 0.1209 0.1355 0.0086  -0.0004 0.0008  112 GLY   A O   
843  N N   . ILE   A 107 ? 0.1285 0.1211 0.1389 0.0055  -0.0071 0.0024  113 ILE   A N   
844  C CA  . ILE   A 107 ? 0.1143 0.1107 0.1304 0.0068  -0.0046 0.0012  113 ILE   A CA  
845  C C   . ILE   A 107 ? 0.1106 0.1112 0.1243 0.0064  -0.0026 0.0016  113 ILE   A C   
846  O O   . ILE   A 107 ? 0.1197 0.1196 0.1317 0.0057  -0.0038 0.0026  113 ILE   A O   
847  C CB  . ILE   A 107 ? 0.1261 0.1219 0.1524 0.0058  -0.0051 0.0010  113 ILE   A CB  
848  C CG1 . ILE   A 107 ? 0.1471 0.1416 0.1773 0.0061  -0.0062 0.0009  113 ILE   A CG1 
849  C CG2 . ILE   A 107 ? 0.1319 0.1299 0.1623 0.0038  -0.0001 -0.0025 113 ILE   A CG2 
850  C CD1 . ILE   A 107 ? 0.1730 0.1671 0.2177 0.0057  -0.0058 0.0023  113 ILE   A CD1 
851  N N   . LEU   A 108 ? 0.1042 0.1105 0.1178 0.0057  -0.0004 0.0021  114 LEU   A N   
852  C CA  . LEU   A 108 ? 0.1064 0.1198 0.1180 0.0025  0.0011  0.0032  114 LEU   A CA  
853  C C   . LEU   A 108 ? 0.1032 0.1180 0.1165 -0.0032 0.0037  -0.0011 114 LEU   A C   
854  O O   . LEU   A 108 ? 0.1166 0.1326 0.1319 -0.0048 0.0046  -0.0025 114 LEU   A O   
855  C CB  . LEU   A 108 ? 0.1089 0.1311 0.1211 0.0028  0.0017  0.0090  114 LEU   A CB  
856  C CG  . LEU   A 108 ? 0.1137 0.1477 0.1238 -0.0032 0.0020  0.0128  114 LEU   A CG  
857  C CD1 . LEU   A 108 ? 0.1413 0.1752 0.1484 -0.0026 0.0020  0.0134  114 LEU   A CD1 
858  C CD2 . LEU   A 108 ? 0.1425 0.1888 0.1584 -0.0036 0.0015  0.0227  114 LEU   A CD2 
859  N N   . ARG   A 109 ? 0.1136 0.1274 0.1265 -0.0069 0.0060  -0.0038 115 ARG   A N   
860  C CA  . ARG   A 109 ? 0.1184 0.1306 0.1332 -0.0140 0.0120  -0.0103 115 ARG   A CA  
861  C C   . ARG   A 109 ? 0.1312 0.1487 0.1386 -0.0223 0.0151  -0.0119 115 ARG   A C   
862  O O   . ARG   A 109 ? 0.1317 0.1513 0.1359 -0.0209 0.0126  -0.0083 115 ARG   A O   
863  C CB  . ARG   A 109 ? 0.1322 0.1339 0.1592 -0.0108 0.0148  -0.0131 115 ARG   A CB  
864  C CG  . ARG   A 109 ? 0.1386 0.1365 0.1690 -0.0084 0.0134  -0.0105 115 ARG   A CG  
865  C CD  . ARG   A 109 ? 0.1618 0.1522 0.2096 -0.0051 0.0150  -0.0091 115 ARG   A CD  
866  N NE  . ARG   A 109 ? 0.1738 0.1649 0.2251 0.0000  0.0080  -0.0031 115 ARG   A NE  
867  C CZ  . ARG   A 109 ? 0.1557 0.1449 0.2192 0.0019  0.0085  -0.0018 115 ARG   A CZ  
868  N NH1 . ARG   A 109 ? 0.1834 0.1692 0.2566 -0.0003 0.0171  -0.0075 115 ARG   A NH1 
869  N NH2 . ARG   A 109 ? 0.1711 0.1622 0.2355 0.0043  0.0013  0.0045  115 ARG   A NH2 
870  N N   . CYS   A 110 ? 0.1698 0.1896 0.1733 -0.0330 0.0215  -0.0181 116 CYS   A N   
871  C CA  . CYS   A 110 ? 0.2031 0.2284 0.1965 -0.0453 0.0256  -0.0210 116 CYS   A CA  
872  C C   . CYS   A 110 ? 0.2376 0.2508 0.2357 -0.0515 0.0372  -0.0326 116 CYS   A C   
873  O O   . CYS   A 110 ? 0.2278 0.2300 0.2399 -0.0448 0.0411  -0.0359 116 CYS   A O   
874  C CB  . CYS   A 110 ? 0.1914 0.2333 0.1736 -0.0566 0.0234  -0.0169 116 CYS   A CB  
875  S SG  . CYS   A 110 ? 0.1989 0.2413 0.1791 -0.0661 0.0294  -0.0243 116 CYS   A SG  
876  N N   . GLN   A 111 ? 0.2666 0.2821 0.2540 -0.0662 0.0443  -0.0389 117 GLN   A N   
877  C CA  . GLN   A 111 ? 0.2895 0.2921 0.2812 -0.0748 0.0591  -0.0520 117 GLN   A CA  
878  C C   . GLN   A 111 ? 0.3069 0.3056 0.3031 -0.0786 0.0669  -0.0595 117 GLN   A C   
879  O O   . GLN   A 111 ? 0.3559 0.3402 0.3654 -0.0795 0.0802  -0.0691 117 GLN   A O   
880  C CB  . GLN   A 111 ? 0.3247 0.3310 0.3000 -0.0934 0.0662  -0.0586 117 GLN   A CB  
881  C CG  . GLN   A 111 ? 0.3717 0.3941 0.3277 -0.1114 0.0658  -0.0596 117 GLN   A CG  
882  C CD  . GLN   A 111 ? 0.4616 0.4884 0.3994 -0.1329 0.0731  -0.0664 117 GLN   A CD  
883  O OE1 . GLN   A 111 ? 0.4927 0.5335 0.4202 -0.1371 0.0642  -0.0571 117 GLN   A OE1 
884  N NE2 . GLN   A 111 ? 0.4746 0.4891 0.4089 -0.1477 0.0907  -0.0830 117 GLN   A NE2 
885  N N   . HIS   A 112 ? 0.2462 0.2573 0.2348 -0.0801 0.0596  -0.0545 118 HIS   A N   
886  C CA  . HIS   A 112 ? 0.2557 0.2652 0.2463 -0.0854 0.0666  -0.0615 118 HIS   A CA  
887  C C   . HIS   A 112 ? 0.2507 0.2534 0.2597 -0.0682 0.0623  -0.0570 118 HIS   A C   
888  O O   . HIS   A 112 ? 0.2936 0.2935 0.3076 -0.0707 0.0685  -0.0626 118 HIS   A O   
889  C CB  . HIS   A 112 ? 0.2681 0.2967 0.2403 -0.0989 0.0607  -0.0572 118 HIS   A CB  
890  C CG  . HIS   A 112 ? 0.2907 0.3295 0.2436 -0.1192 0.0639  -0.0598 118 HIS   A CG  
891  N ND1 . HIS   A 112 ? 0.2506 0.3062 0.1945 -0.1212 0.0520  -0.0468 118 HIS   A ND1 
892  C CD2 . HIS   A 112 ? 0.3030 0.3387 0.2435 -0.1404 0.0783  -0.0739 118 HIS   A CD2 
893  C CE1 . HIS   A 112 ? 0.3159 0.3783 0.2427 -0.1426 0.0580  -0.0522 118 HIS   A CE1 
894  N NE2 . HIS   A 112 ? 0.3620 0.4124 0.2846 -0.1556 0.0742  -0.0695 118 HIS   A NE2 
895  N N   . GLY   A 113 ? 0.2138 0.2164 0.2301 -0.0528 0.0508  -0.0464 119 GLY   A N   
896  C CA  . GLY   A 113 ? 0.1966 0.1951 0.2266 -0.0398 0.0458  -0.0414 119 GLY   A CA  
897  C C   . GLY   A 113 ? 0.1722 0.1782 0.1970 -0.0310 0.0322  -0.0304 119 GLY   A C   
898  O O   . GLY   A 113 ? 0.1747 0.1864 0.1910 -0.0313 0.0272  -0.0256 119 GLY   A O   
899  N N   . VAL   A 114 ? 0.1540 0.1596 0.1843 -0.0239 0.0275  -0.0267 120 VAL   A N   
900  C CA  . VAL   A 114 ? 0.1536 0.1634 0.1801 -0.0164 0.0176  -0.0181 120 VAL   A CA  
901  C C   . VAL   A 114 ? 0.1241 0.1457 0.1406 -0.0214 0.0145  -0.0139 120 VAL   A C   
902  O O   . VAL   A 114 ? 0.1455 0.1727 0.1592 -0.0287 0.0169  -0.0161 120 VAL   A O   
903  C CB  . VAL   A 114 ? 0.1338 0.1387 0.1688 -0.0093 0.0144  -0.0160 120 VAL   A CB  
904  C CG1 . VAL   A 114 ? 0.1561 0.1635 0.1857 -0.0040 0.0072  -0.0096 120 VAL   A CG1 
905  C CG2 . VAL   A 114 ? 0.1550 0.1521 0.2033 -0.0047 0.0153  -0.0154 120 VAL   A CG2 
906  N N   . VAL   A 115 ? 0.1233 0.1500 0.1361 -0.0185 0.0098  -0.0071 121 VAL   A N   
907  C CA  . VAL   A 115 ? 0.1258 0.1656 0.1350 -0.0220 0.0066  0.0009  121 VAL   A CA  
908  C C   . VAL   A 115 ? 0.1272 0.1664 0.1422 -0.0140 0.0030  0.0073  121 VAL   A C   
909  O O   . VAL   A 115 ? 0.1366 0.1851 0.1536 -0.0166 0.0013  0.0138  121 VAL   A O   
910  C CB  . VAL   A 115 ? 0.1421 0.1887 0.1478 -0.0237 0.0052  0.0060  121 VAL   A CB  
911  C CG1 . VAL   A 115 ? 0.1583 0.2206 0.1665 -0.0256 0.0013  0.0187  121 VAL   A CG1 
912  C CG2 . VAL   A 115 ? 0.1676 0.2153 0.1658 -0.0344 0.0097  -0.0006 121 VAL   A CG2 
913  N N   . GLY   A 116 ? 0.1254 0.1539 0.1433 -0.0049 0.0021  0.0064  122 GLY   A N   
914  C CA  . GLY   A 116 ? 0.1301 0.1553 0.1524 0.0015  0.0011  0.0105  122 GLY   A CA  
915  C C   . GLY   A 116 ? 0.1146 0.1282 0.1356 0.0070  0.0012  0.0073  122 GLY   A C   
916  O O   . GLY   A 116 ? 0.1217 0.1310 0.1402 0.0063  0.0005  0.0033  122 GLY   A O   
917  N N   . ILE   A 117 ? 0.1223 0.1310 0.1454 0.0110  0.0028  0.0092  123 ILE   A N   
918  C CA  . ILE   A 117 ? 0.1207 0.1190 0.1391 0.0127  0.0037  0.0054  123 ILE   A CA  
919  C C   . ILE   A 117 ? 0.1257 0.1213 0.1460 0.0155  0.0091  0.0075  123 ILE   A C   
920  O O   . ILE   A 117 ? 0.1371 0.1368 0.1669 0.0181  0.0124  0.0133  123 ILE   A O   
921  C CB  . ILE   A 117 ? 0.1350 0.1258 0.1513 0.0118  0.0027  0.0020  123 ILE   A CB  
922  C CG1 . ILE   A 117 ? 0.1597 0.1503 0.1816 0.0134  0.0053  0.0044  123 ILE   A CG1 
923  C CG2 . ILE   A 117 ? 0.1540 0.1462 0.1710 0.0095  -0.0017 0.0002  123 ILE   A CG2 
924  C CD1 . ILE   A 117 ? 0.1789 0.1608 0.1971 0.0115  0.0049  0.0005  123 ILE   A CD1 
925  N N   . VAL   A 118 ? 0.1278 0.1171 0.1414 0.0146  0.0108  0.0039  124 VAL   A N   
926  C CA  . VAL   A 118 ? 0.1408 0.1255 0.1565 0.0164  0.0187  0.0040  124 VAL   A CA  
927  C C   . VAL   A 118 ? 0.1504 0.1266 0.1709 0.0175  0.0254  0.0025  124 VAL   A C   
928  O O   . VAL   A 118 ? 0.1523 0.1219 0.1658 0.0139  0.0237  -0.0023 124 VAL   A O   
929  C CB  . VAL   A 118 ? 0.1483 0.1268 0.1522 0.0120  0.0195  -0.0016 124 VAL   A CB  
930  C CG1 . VAL   A 118 ? 0.1626 0.1337 0.1681 0.0125  0.0310  -0.0042 124 VAL   A CG1 
931  C CG2 . VAL   A 118 ? 0.1581 0.1441 0.1591 0.0112  0.0136  0.0006  124 VAL   A CG2 
932  N N   . SER   A 119 ? 0.1665 0.1432 0.2013 0.0222  0.0334  0.0077  125 SER   A N   
933  C CA  . SER   A 119 ? 0.1842 0.1521 0.2289 0.0242  0.0422  0.0077  125 SER   A CA  
934  C C   . SER   A 119 ? 0.2060 0.1656 0.2615 0.0269  0.0566  0.0071  125 SER   A C   
935  O O   . SER   A 119 ? 0.2349 0.1803 0.2925 0.0257  0.0673  0.0012  125 SER   A O   
936  C CB  . SER   A 119 ? 0.1827 0.1616 0.2417 0.0276  0.0380  0.0181  125 SER   A CB  
937  O OG  . SER   A 119 ? 0.2096 0.1813 0.2826 0.0305  0.0464  0.0207  125 SER   A OG  
938  N N   . THR   A 120 ? 0.1995 0.1666 0.2622 0.0299  0.0586  0.0123  126 THR   A N   
939  C CA  . THR   A 120 ? 0.2124 0.1716 0.2895 0.0331  0.0745  0.0122  126 THR   A CA  
940  C C   . THR   A 120 ? 0.2301 0.1900 0.2962 0.0303  0.0755  0.0075  126 THR   A C   
941  O O   . THR   A 120 ? 0.2134 0.1836 0.2672 0.0280  0.0629  0.0088  126 THR   A O   
942  C CB  . THR   A 120 ? 0.2263 0.1967 0.3358 0.0416  0.0790  0.0292  126 THR   A CB  
943  O OG1 . THR   A 120 ? 0.2241 0.2139 0.3365 0.0426  0.0689  0.0399  126 THR   A OG1 
944  C CG2 . THR   A 120 ? 0.2232 0.1963 0.3440 0.0435  0.0758  0.0362  126 THR   A CG2 
945  N N   . GLY   A 121 ? 0.2585 0.2078 0.3309 0.0303  0.0915  0.0024  127 GLY   A N   
946  C CA  . GLY   A 121 ? 0.2848 0.2346 0.3471 0.0269  0.0938  -0.0023 127 GLY   A CA  
947  C C   . GLY   A 121 ? 0.3211 0.2624 0.4013 0.0298  0.1141  -0.0038 127 GLY   A C   
948  O O   . GLY   A 121 ? 0.3494 0.2806 0.4482 0.0333  0.1282  -0.0036 127 GLY   A O   
949  N N   . GLY   A 122 ? 0.3430 0.2872 0.4169 0.0275  0.1163  -0.0062 128 GLY   A N   
950  C CA  . GLY   A 122 ? 0.3464 0.2823 0.4347 0.0287  0.1367  -0.0096 128 GLY   A CA  
951  C C   . GLY   A 122 ? 0.3635 0.3159 0.4676 0.0352  0.1341  0.0029  128 GLY   A C   
952  O O   . GLY   A 122 ? 0.3608 0.3314 0.4777 0.0416  0.1211  0.0187  128 GLY   A O   
953  N N   . ASN   A 123 ? 0.3604 0.3064 0.4633 0.0320  0.1478  -0.0045 129 ASN   A N   
954  C CA  . ASN   A 123 ? 0.3670 0.3259 0.4886 0.0379  0.1509  0.0061  129 ASN   A CA  
955  C C   . ASN   A 123 ? 0.3299 0.3101 0.4438 0.0392  0.1290  0.0178  129 ASN   A C   
956  O O   . ASN   A 123 ? 0.3118 0.3089 0.4483 0.0459  0.1271  0.0337  129 ASN   A O   
957  C CB  . ASN   A 123 ? 0.3943 0.3555 0.5602 0.0495  0.1664  0.0200  129 ASN   A CB  
958  C CG  . ASN   A 123 ? 0.4554 0.3929 0.6323 0.0478  0.1943  0.0065  129 ASN   A CG  
959  O OD1 . ASN   A 123 ? 0.5069 0.4328 0.6673 0.0395  0.2064  -0.0090 129 ASN   A OD1 
960  N ND2 . ASN   A 123 ? 0.4477 0.3776 0.6517 0.0543  0.2055  0.0117  129 ASN   A ND2 
961  N N   . GLY   A 124 ? 0.2940 0.2737 0.3765 0.0313  0.1138  0.0098  130 GLY   A N   
962  C CA  . GLY   A 124 ? 0.2579 0.2542 0.3311 0.0307  0.0956  0.0177  130 GLY   A CA  
963  C C   . GLY   A 124 ? 0.1927 0.2016 0.2747 0.0349  0.0827  0.0298  130 GLY   A C   
964  O O   . GLY   A 124 ? 0.2117 0.2339 0.2875 0.0334  0.0701  0.0359  130 GLY   A O   
965  N N   . LEU   A 125 ? 0.1941 0.1977 0.2867 0.0380  0.0860  0.0312  131 LEU   A N   
966  C CA  . LEU   A 125 ? 0.1903 0.2052 0.2864 0.0393  0.0731  0.0407  131 LEU   A CA  
967  C C   . LEU   A 125 ? 0.2087 0.2119 0.2843 0.0347  0.0672  0.0291  131 LEU   A C   
968  O O   . LEU   A 125 ? 0.2401 0.2266 0.3069 0.0318  0.0758  0.0170  131 LEU   A O   
969  C CB  . LEU   A 125 ? 0.1984 0.2208 0.3271 0.0465  0.0798  0.0556  131 LEU   A CB  
970  C CG  . LEU   A 125 ? 0.2077 0.2459 0.3626 0.0512  0.0847  0.0717  131 LEU   A CG  
971  C CD1 . LEU   A 125 ? 0.2369 0.2770 0.4312 0.0595  0.0982  0.0856  131 LEU   A CD1 
972  C CD2 . LEU   A 125 ? 0.2057 0.2670 0.3552 0.0470  0.0682  0.0838  131 LEU   A CD2 
973  N N   . VAL   A 126 ? 0.1611 0.1738 0.2307 0.0330  0.0537  0.0334  132 VAL   A N   
974  C CA  . VAL   A 126 ? 0.1568 0.1615 0.2127 0.0298  0.0477  0.0257  132 VAL   A CA  
975  C C   . VAL   A 126 ? 0.1580 0.1742 0.2266 0.0318  0.0422  0.0364  132 VAL   A C   
976  O O   . VAL   A 126 ? 0.1578 0.1903 0.2318 0.0308  0.0358  0.0466  132 VAL   A O   
977  C CB  . VAL   A 126 ? 0.1603 0.1634 0.1939 0.0237  0.0379  0.0179  132 VAL   A CB  
978  C CG1 . VAL   A 126 ? 0.1647 0.1820 0.1972 0.0224  0.0293  0.0243  132 VAL   A CG1 
979  C CG2 . VAL   A 126 ? 0.1697 0.1666 0.1939 0.0209  0.0321  0.0123  132 VAL   A CG2 
980  N N   . GLY   A 127 ? 0.1572 0.1657 0.2289 0.0329  0.0445  0.0342  133 GLY   A N   
981  C CA  . GLY   A 127 ? 0.1459 0.1650 0.2278 0.0333  0.0389  0.0438  133 GLY   A CA  
982  C C   . GLY   A 127 ? 0.1460 0.1605 0.2110 0.0289  0.0308  0.0354  133 GLY   A C   
983  O O   . GLY   A 127 ? 0.1719 0.1721 0.2248 0.0275  0.0327  0.0242  133 GLY   A O   
984  N N   . PHE   A 128 ? 0.1296 0.1574 0.1944 0.0255  0.0224  0.0415  134 PHE   A N   
985  C CA  . PHE   A 128 ? 0.1274 0.1523 0.1792 0.0212  0.0160  0.0342  134 PHE   A CA  
986  C C   . PHE   A 128 ? 0.1313 0.1639 0.1919 0.0200  0.0138  0.0413  134 PHE   A C   
987  O O   . PHE   A 128 ? 0.1321 0.1807 0.2039 0.0180  0.0119  0.0540  134 PHE   A O   
988  C CB  . PHE   A 128 ? 0.1296 0.1624 0.1705 0.0153  0.0096  0.0320  134 PHE   A CB  
989  C CG  . PHE   A 128 ? 0.1238 0.1527 0.1575 0.0157  0.0104  0.0278  134 PHE   A CG  
990  C CD1 . PHE   A 128 ? 0.1245 0.1412 0.1479 0.0155  0.0099  0.0183  134 PHE   A CD1 
991  C CD2 . PHE   A 128 ? 0.1367 0.1761 0.1749 0.0151  0.0108  0.0350  134 PHE   A CD2 
992  C CE1 . PHE   A 128 ? 0.1299 0.1445 0.1471 0.0148  0.0099  0.0158  134 PHE   A CE1 
993  C CE2 . PHE   A 128 ? 0.1401 0.1761 0.1712 0.0150  0.0113  0.0311  134 PHE   A CE2 
994  C CZ  . PHE   A 128 ? 0.1387 0.1623 0.1591 0.0147  0.0108  0.0214  134 PHE   A CZ  
995  N N   . ALA   A 129 ? 0.1274 0.1503 0.1834 0.0201  0.0136  0.0346  135 ALA   A N   
996  C CA  . ALA   A 129 ? 0.1316 0.1610 0.1931 0.0178  0.0108  0.0397  135 ALA   A CA  
997  C C   . ALA   A 129 ? 0.1243 0.1634 0.1752 0.0100  0.0043  0.0373  135 ALA   A C   
998  O O   . ALA   A 129 ? 0.1330 0.1640 0.1727 0.0085  0.0031  0.0267  135 ALA   A O   
999  C CB  . ALA   A 129 ? 0.1444 0.1591 0.2035 0.0201  0.0135  0.0323  135 ALA   A CB  
1000 N N   . ASP   A 130 ? 0.1249 0.1817 0.1801 0.0036  0.0010  0.0473  136 ASP   A N   
1001 C CA  . ASP   A 130 ? 0.1372 0.2025 0.1808 -0.0069 -0.0026 0.0433  136 ASP   A CA  
1002 C C   . ASP   A 130 ? 0.1280 0.1886 0.1678 -0.0092 -0.0031 0.0369  136 ASP   A C   
1003 O O   . ASP   A 130 ? 0.1503 0.2095 0.1983 -0.0058 -0.0031 0.0415  136 ASP   A O   
1004 C CB  . ASP   A 130 ? 0.1686 0.2565 0.2171 -0.0162 -0.0062 0.0576  136 ASP   A CB  
1005 C CG  . ASP   A 130 ? 0.1987 0.2966 0.2329 -0.0308 -0.0081 0.0530  136 ASP   A CG  
1006 O OD1 . ASP   A 130 ? 0.2143 0.3057 0.2372 -0.0337 -0.0057 0.0421  136 ASP   A OD1 
1007 O OD2 . ASP   A 130 ? 0.2263 0.3373 0.2603 -0.0402 -0.0108 0.0591  136 ASP   A OD2 
1008 N N   . VAL   A 131 ? 0.1261 0.1838 0.1553 -0.0151 -0.0023 0.0264  137 VAL   A N   
1009 C CA  . VAL   A 131 ? 0.1300 0.1853 0.1564 -0.0190 -0.0017 0.0202  137 VAL   A CA  
1010 C C   . VAL   A 131 ? 0.1386 0.2045 0.1563 -0.0333 -0.0001 0.0166  137 VAL   A C   
1011 O O   . VAL   A 131 ? 0.1372 0.2016 0.1525 -0.0380 0.0021  0.0104  137 VAL   A O   
1012 C CB  . VAL   A 131 ? 0.1326 0.1713 0.1585 -0.0124 0.0003  0.0098  137 VAL   A CB  
1013 C CG1 . VAL   A 131 ? 0.1516 0.1800 0.1820 -0.0024 -0.0006 0.0119  137 VAL   A CG1 
1014 C CG2 . VAL   A 131 ? 0.1406 0.1737 0.1628 -0.0137 0.0032  0.0019  137 VAL   A CG2 
1015 N N   . ARG   A 132 ? 0.1462 0.2229 0.1584 -0.0417 -0.0003 0.0198  138 ARG   A N   
1016 C CA  . ARG   A 132 ? 0.1490 0.2339 0.1494 -0.0584 0.0033  0.0135  138 ARG   A CA  
1017 C C   . ARG   A 132 ? 0.1799 0.2808 0.1769 -0.0713 0.0011  0.0195  138 ARG   A C   
1018 O O   . ARG   A 132 ? 0.1895 0.2936 0.1751 -0.0862 0.0064  0.0103  138 ARG   A O   
1019 C CB  . ARG   A 132 ? 0.1584 0.2524 0.1519 -0.0664 0.0031  0.0165  138 ARG   A CB  
1020 C CG  . ARG   A 132 ? 0.1493 0.2274 0.1440 -0.0567 0.0065  0.0085  138 ARG   A CG  
1021 C CD  . ARG   A 132 ? 0.1804 0.2687 0.1684 -0.0648 0.0056  0.0127  138 ARG   A CD  
1022 N NE  . ARG   A 132 ? 0.1555 0.2569 0.1519 -0.0599 -0.0015 0.0295  138 ARG   A NE  
1023 C CZ  . ARG   A 132 ? 0.1894 0.3019 0.1852 -0.0635 -0.0041 0.0378  138 ARG   A CZ  
1024 N NH1 . ARG   A 132 ? 0.1865 0.3004 0.1697 -0.0748 -0.0009 0.0309  138 ARG   A NH1 
1025 N NH2 . ARG   A 132 ? 0.1867 0.3080 0.1959 -0.0555 -0.0086 0.0531  138 ARG   A NH2 
1026 N N   . ASP   A 133 ? 0.1617 0.2726 0.1689 -0.0669 -0.0057 0.0346  139 ASP   A N   
1027 C CA  . ASP   A 133 ? 0.1807 0.3079 0.1864 -0.0792 -0.0089 0.0424  139 ASP   A CA  
1028 C C   . ASP   A 133 ? 0.1709 0.2871 0.1780 -0.0750 -0.0064 0.0340  139 ASP   A C   
1029 O O   . ASP   A 133 ? 0.1939 0.3229 0.1982 -0.0863 -0.0085 0.0386  139 ASP   A O   
1030 C CB  . ASP   A 133 ? 0.1949 0.3383 0.2163 -0.0758 -0.0168 0.0649  139 ASP   A CB  
1031 C CG  . ASP   A 133 ? 0.2399 0.3682 0.2784 -0.0558 -0.0165 0.0681  139 ASP   A CG  
1032 O OD1 . ASP   A 133 ? 0.2243 0.3331 0.2625 -0.0434 -0.0125 0.0573  139 ASP   A OD1 
1033 O OD2 . ASP   A 133 ? 0.2645 0.4005 0.3169 -0.0534 -0.0199 0.0818  139 ASP   A OD2 
1034 N N   . LEU   A 134 ? 0.1578 0.2530 0.1697 -0.0603 -0.0030 0.0239  140 LEU   A N   
1035 C CA  . LEU   A 134 ? 0.1521 0.2377 0.1672 -0.0556 -0.0014 0.0177  140 LEU   A CA  
1036 C C   . LEU   A 134 ? 0.1657 0.2466 0.1725 -0.0647 0.0065  0.0027  140 LEU   A C   
1037 O O   . LEU   A 134 ? 0.1679 0.2333 0.1783 -0.0570 0.0117  -0.0077 140 LEU   A O   
1038 C CB  . LEU   A 134 ? 0.1474 0.2153 0.1714 -0.0380 -0.0019 0.0160  140 LEU   A CB  
1039 C CG  . LEU   A 134 ? 0.1688 0.2373 0.2027 -0.0287 -0.0060 0.0285  140 LEU   A CG  
1040 C CD1 . LEU   A 134 ? 0.1854 0.2355 0.2230 -0.0156 -0.0044 0.0232  140 LEU   A CD1 
1041 C CD2 . LEU   A 134 ? 0.2034 0.2824 0.2456 -0.0308 -0.0096 0.0408  140 LEU   A CD2 
1042 N N   . LEU   A 135 ? 0.1643 0.2596 0.1610 -0.0828 0.0084  0.0021  141 LEU   A N   
1043 C CA  . LEU   A 135 ? 0.1868 0.2769 0.1752 -0.0943 0.0196  -0.0142 141 LEU   A CA  
1044 C C   . LEU   A 135 ? 0.1828 0.2599 0.1792 -0.0874 0.0252  -0.0236 141 LEU   A C   
1045 O O   . LEU   A 135 ? 0.2158 0.2814 0.2149 -0.0885 0.0362  -0.0370 141 LEU   A O   
1046 C CB  . LEU   A 135 ? 0.2103 0.3198 0.1828 -0.1192 0.0216  -0.0140 141 LEU   A CB  
1047 C CG  . LEU   A 135 ? 0.2195 0.3476 0.1848 -0.1292 0.0142  -0.0008 141 LEU   A CG  
1048 C CD1 . LEU   A 135 ? 0.2526 0.4004 0.1983 -0.1588 0.0174  -0.0026 141 LEU   A CD1 
1049 C CD2 . LEU   A 135 ? 0.2381 0.3571 0.2034 -0.1228 0.0168  -0.0046 141 LEU   A CD2 
1050 N N   . TRP   A 136 ? 0.1638 0.2422 0.1671 -0.0793 0.0180  -0.0154 142 TRP   A N   
1051 C CA  . TRP   A 136 ? 0.1750 0.2434 0.1864 -0.0728 0.0212  -0.0216 142 TRP   A CA  
1052 C C   . TRP   A 136 ? 0.1825 0.2338 0.2057 -0.0577 0.0238  -0.0265 142 TRP   A C   
1053 O O   . TRP   A 136 ? 0.1938 0.2375 0.2261 -0.0539 0.0284  -0.0321 142 TRP   A O   
1054 C CB  . TRP   A 136 ? 0.1837 0.2579 0.1985 -0.0690 0.0126  -0.0109 142 TRP   A CB  
1055 C CG  . TRP   A 136 ? 0.1602 0.2325 0.1811 -0.0567 0.0040  0.0010  142 TRP   A CG  
1056 C CD1 . TRP   A 136 ? 0.1662 0.2509 0.1873 -0.0594 -0.0023 0.0144  142 TRP   A CD1 
1057 C CD2 . TRP   A 136 ? 0.1681 0.2255 0.1973 -0.0411 0.0019  0.0012  142 TRP   A CD2 
1058 N NE1 . TRP   A 136 ? 0.1855 0.2615 0.2158 -0.0451 -0.0059 0.0211  142 TRP   A NE1 
1059 C CE2 . TRP   A 136 ? 0.1675 0.2266 0.2003 -0.0351 -0.0035 0.0122  142 TRP   A CE2 
1060 C CE3 . TRP   A 136 ? 0.1703 0.2146 0.2050 -0.0331 0.0043  -0.0059 142 TRP   A CE3 
1061 C CZ2 . TRP   A 136 ? 0.1855 0.2315 0.2238 -0.0227 -0.0049 0.0133  142 TRP   A CZ2 
1062 C CZ3 . TRP   A 136 ? 0.1935 0.2276 0.2325 -0.0220 0.0004  -0.0027 142 TRP   A CZ3 
1063 C CH2 . TRP   A 136 ? 0.1915 0.2257 0.2305 -0.0177 -0.0034 0.0054  142 TRP   A CH2 
1064 N N   . LEU   A 137 ? 0.1661 0.2127 0.1907 -0.0496 0.0204  -0.0229 143 LEU   A N   
1065 C CA  . LEU   A 137 ? 0.1921 0.2251 0.2275 -0.0381 0.0222  -0.0262 143 LEU   A CA  
1066 C C   . LEU   A 137 ? 0.2163 0.2429 0.2589 -0.0422 0.0342  -0.0371 143 LEU   A C   
1067 O O   . LEU   A 137 ? 0.2305 0.2482 0.2876 -0.0337 0.0363  -0.0379 143 LEU   A O   
1068 C CB  . LEU   A 137 ? 0.1841 0.2143 0.2177 -0.0314 0.0176  -0.0213 143 LEU   A CB  
1069 C CG  . LEU   A 137 ? 0.1708 0.2021 0.2033 -0.0239 0.0087  -0.0114 143 LEU   A CG  
1070 C CD1 . LEU   A 137 ? 0.1975 0.2276 0.2276 -0.0200 0.0065  -0.0079 143 LEU   A CD1 
1071 C CD2 . LEU   A 137 ? 0.1876 0.2097 0.2271 -0.0151 0.0057  -0.0105 143 LEU   A CD2 
1072 N N   . ASP   A 138 ? 0.2525 0.2841 0.2860 -0.0569 0.0431  -0.0451 144 ASP   A N   
1073 C CA  . ASP   A 138 ? 0.2866 0.3100 0.3276 -0.0629 0.0586  -0.0578 144 ASP   A CA  
1074 C C   . ASP   A 138 ? 0.3502 0.3718 0.3995 -0.0671 0.0679  -0.0650 144 ASP   A C   
1075 O O   . ASP   A 138 ? 0.3857 0.3994 0.4441 -0.0726 0.0837  -0.0763 144 ASP   A O   
1076 C CB  . ASP   A 138 ? 0.3061 0.3346 0.3310 -0.0804 0.0667  -0.0657 144 ASP   A CB  
1077 C CG  . ASP   A 138 ? 0.3323 0.3637 0.3488 -0.0791 0.0598  -0.0599 144 ASP   A CG  
1078 O OD1 . ASP   A 138 ? 0.3722 0.3976 0.3981 -0.0639 0.0526  -0.0529 144 ASP   A OD1 
1079 O OD2 . ASP   A 138 ? 0.4279 0.4690 0.4276 -0.0948 0.0616  -0.0618 144 ASP   A OD2 
1080 N N   . GLU   A 139 ? 0.3664 0.3947 0.4134 -0.0657 0.0601  -0.0592 145 GLU   A N   
1081 C CA  . GLU   A 139 ? 0.4164 0.4447 0.4697 -0.0711 0.0689  -0.0660 145 GLU   A CA  
1082 C C   . GLU   A 139 ? 0.4546 0.4826 0.5191 -0.0590 0.0599  -0.0575 145 GLU   A C   
1083 O O   . GLU   A 139 ? 0.4545 0.4816 0.5196 -0.0479 0.0474  -0.0473 145 GLU   A O   
1084 C CB  . GLU   A 139 ? 0.4699 0.5113 0.5025 -0.0906 0.0709  -0.0700 145 GLU   A CB  
1085 C CG  . GLU   A 139 ? 0.5642 0.6186 0.5845 -0.0900 0.0540  -0.0559 145 GLU   A CG  
1086 C CD  . GLU   A 139 ? 0.6693 0.7409 0.6698 -0.1101 0.0525  -0.0544 145 GLU   A CD  
1087 O OE1 . GLU   A 139 ? 0.6847 0.7682 0.6812 -0.1110 0.0411  -0.0425 145 GLU   A OE1 
1088 O OE2 . GLU   A 139 ? 0.7190 0.7929 0.7085 -0.1262 0.0627  -0.0641 145 GLU   A OE2 
1089 N N   . GLU   A 140 ? 0.4863 0.5148 0.5582 -0.0629 0.0672  -0.0625 146 GLU   A N   
1090 C CA  . GLU   A 140 ? 0.5222 0.5519 0.6038 -0.0552 0.0608  -0.0561 146 GLU   A CA  
1091 C C   . GLU   A 140 ? 0.5393 0.5607 0.6460 -0.0422 0.0625  -0.0523 146 GLU   A C   
1092 O O   . GLU   A 140 ? 0.5452 0.5626 0.6704 -0.0433 0.0761  -0.0585 146 GLU   A O   
1093 C CB  . GLU   A 140 ? 0.5740 0.6102 0.6427 -0.0516 0.0441  -0.0448 146 GLU   A CB  
1094 C CG  . GLU   A 140 ? 0.6625 0.6984 0.7394 -0.0441 0.0370  -0.0382 146 GLU   A CG  
1095 C CD  . GLU   A 140 ? 0.7832 0.8269 0.8551 -0.0527 0.0381  -0.0399 146 GLU   A CD  
1096 O OE1 . GLU   A 140 ? 0.8135 0.8609 0.8790 -0.0508 0.0276  -0.0318 146 GLU   A OE1 
1097 O OE2 . GLU   A 140 ? 0.8208 0.8662 0.8955 -0.0621 0.0506  -0.0496 146 GLU   A OE2 
1098 N N   . SER   B 1   ? 0.2130 0.2323 0.2291 0.0147  -0.0133 0.0437  7   SER   C N   
1099 C CA  . SER   B 1   ? 0.2084 0.2301 0.2344 0.0115  -0.0149 0.0432  7   SER   C CA  
1100 C C   . SER   B 1   ? 0.2102 0.2291 0.2370 0.0086  -0.0154 0.0389  7   SER   C C   
1101 O O   . SER   B 1   ? 0.2295 0.2449 0.2489 0.0088  -0.0161 0.0361  7   SER   C O   
1102 C CB  . SER   B 1   ? 0.2451 0.2690 0.2709 0.0117  -0.0204 0.0440  7   SER   C CB  
1103 O OG  . SER   B 1   ? 0.3114 0.3325 0.3287 0.0118  -0.0252 0.0403  7   SER   C OG  
1104 N N   . GLY   B 2   ? 0.1964 0.2166 0.2318 0.0065  -0.0147 0.0388  8   GLY   C N   
1105 C CA  . GLY   B 2   ? 0.1918 0.2095 0.2285 0.0045  -0.0144 0.0361  8   GLY   C CA  
1106 C C   . GLY   B 2   ? 0.1694 0.1877 0.2132 0.0042  -0.0107 0.0368  8   GLY   C C   
1107 O O   . GLY   B 2   ? 0.1819 0.2015 0.2286 0.0055  -0.0083 0.0379  8   GLY   C O   
1108 N N   . ALA   B 3   ? 0.1553 0.1724 0.2022 0.0031  -0.0101 0.0362  9   ALA   C N   
1109 C CA  . ALA   B 3   ? 0.1597 0.1766 0.2113 0.0039  -0.0061 0.0369  9   ALA   C CA  
1110 C C   . ALA   B 3   ? 0.1427 0.1558 0.1913 0.0043  -0.0038 0.0355  9   ALA   C C   
1111 O O   . ALA   B 3   ? 0.1683 0.1795 0.2145 0.0030  -0.0057 0.0345  9   ALA   C O   
1112 C CB  . ALA   B 3   ? 0.1812 0.2015 0.2427 0.0031  -0.0060 0.0400  9   ALA   C CB  
1113 N N   . ILE   B 4   ? 0.1402 0.1521 0.1890 0.0066  0.0000  0.0356  10  ILE   C N   
1114 C CA  . ILE   B 4   ? 0.1649 0.1733 0.2111 0.0082  0.0034  0.0357  10  ILE   C CA  
1115 C C   . ILE   B 4   ? 0.1576 0.1672 0.2123 0.0086  0.0068  0.0394  10  ILE   C C   
1116 O O   . ILE   B 4   ? 0.1695 0.1812 0.2281 0.0097  0.0081  0.0404  10  ILE   C O   
1117 C CB  . ILE   B 4   ? 0.1501 0.1558 0.1884 0.0120  0.0054  0.0332  10  ILE   C CB  
1118 C CG1 . ILE   B 4   ? 0.1746 0.1799 0.2076 0.0118  0.0022  0.0299  10  ILE   C CG1 
1119 C CG2 . ILE   B 4   ? 0.1797 0.1814 0.2133 0.0146  0.0089  0.0339  10  ILE   C CG2 
1120 C CD1 . ILE   B 4   ? 0.1736 0.1771 0.2021 0.0157  0.0028  0.0267  10  ILE   C CD1 
1121 N N   . TYR   B 5   ? 0.1588 0.1670 0.2178 0.0079  0.0088  0.0416  11  TYR   C N   
1122 C CA  . TYR   B 5   ? 0.1689 0.1781 0.2381 0.0085  0.0131  0.0459  11  TYR   C CA  
1123 C C   . TYR   B 5   ? 0.1782 0.1830 0.2428 0.0126  0.0196  0.0478  11  TYR   C C   
1124 O O   . TYR   B 5   ? 0.2021 0.2044 0.2671 0.0119  0.0204  0.0485  11  TYR   C O   
1125 C CB  . TYR   B 5   ? 0.1768 0.1884 0.2591 0.0041  0.0100  0.0478  11  TYR   C CB  
1126 C CG  . TYR   B 5   ? 0.1653 0.1813 0.2508 0.0014  0.0035  0.0465  11  TYR   C CG  
1127 C CD1 . TYR   B 5   ? 0.1721 0.1920 0.2654 0.0016  0.0041  0.0490  11  TYR   C CD1 
1128 C CD2 . TYR   B 5   ? 0.1809 0.1967 0.2602 -0.0005 -0.0025 0.0431  11  TYR   C CD2 
1129 C CE1 . TYR   B 5   ? 0.1844 0.2082 0.2795 -0.0001 -0.0015 0.0484  11  TYR   C CE1 
1130 C CE2 . TYR   B 5   ? 0.2019 0.2213 0.2816 -0.0016 -0.0077 0.0424  11  TYR   C CE2 
1131 C CZ  . TYR   B 5   ? 0.1978 0.2212 0.2856 -0.0014 -0.0073 0.0453  11  TYR   C CZ  
1132 O OH  . TYR   B 5   ? 0.2284 0.2552 0.3160 -0.0018 -0.0122 0.0453  11  TYR   C OH  
1133 N N   . VAL   B 6   ? 0.1962 0.1996 0.2553 0.0174  0.0242  0.0483  12  VAL   C N   
1134 C CA  . VAL   B 6   ? 0.2066 0.2053 0.2582 0.0231  0.0308  0.0503  12  VAL   C CA  
1135 C C   . VAL   B 6   ? 0.2109 0.2097 0.2679 0.0268  0.0376  0.0548  12  VAL   C C   
1136 O O   . VAL   B 6   ? 0.1988 0.1996 0.2566 0.0276  0.0370  0.0536  12  VAL   C O   
1137 C CB  . VAL   B 6   ? 0.2261 0.2216 0.2616 0.0273  0.0290  0.0453  12  VAL   C CB  
1138 C CG1 . VAL   B 6   ? 0.2294 0.2268 0.2628 0.0280  0.0258  0.0414  12  VAL   C CG1 
1139 C CG2 . VAL   B 6   ? 0.2474 0.2380 0.2731 0.0345  0.0354  0.0474  12  VAL   C CG2 
1140 N N   . GLY   B 7   ? 0.2212 0.2181 0.2837 0.0290  0.0448  0.0606  13  GLY   C N   
1141 C CA  . GLY   B 7   ? 0.2255 0.2225 0.2942 0.0329  0.0524  0.0657  13  GLY   C CA  
1142 C C   . GLY   B 7   ? 0.2207 0.2233 0.3045 0.0282  0.0496  0.0666  13  GLY   C C   
1143 O O   . GLY   B 7   ? 0.2243 0.2305 0.3196 0.0218  0.0440  0.0664  13  GLY   C O   
1144 N N   . ASN   B 8   ? 0.2194 0.2225 0.3019 0.0316  0.0523  0.0668  14  ASN   C N   
1145 C CA  . ASN   B 8   ? 0.2193 0.2278 0.3153 0.0276  0.0493  0.0675  14  ASN   C CA  
1146 C C   . ASN   B 8   ? 0.1969 0.2068 0.2854 0.0262  0.0423  0.0614  14  ASN   C C   
1147 O O   . ASN   B 8   ? 0.1998 0.2123 0.2937 0.0262  0.0421  0.0616  14  ASN   C O   
1148 C CB  . ASN   B 8   ? 0.2491 0.2580 0.3541 0.0315  0.0576  0.0732  14  ASN   C CB  
1149 C CG  . ASN   B 8   ? 0.3299 0.3395 0.4505 0.0307  0.0635  0.0804  14  ASN   C CG  
1150 O OD1 . ASN   B 8   ? 0.3615 0.3762 0.5009 0.0252  0.0604  0.0829  14  ASN   C OD1 
1151 N ND2 . ASN   B 8   ? 0.3831 0.3878 0.4968 0.0362  0.0714  0.0837  14  ASN   C ND2 
1152 N N   . TYR   B 9   ? 0.1677 0.1763 0.2460 0.0246  0.0367  0.0565  15  TYR   C N   
1153 C CA  . TYR   B 9   ? 0.1752 0.1849 0.2480 0.0232  0.0306  0.0512  15  TYR   C CA  
1154 C C   . TYR   B 9   ? 0.1668 0.1794 0.2421 0.0174  0.0235  0.0496  15  TYR   C C   
1155 O O   . TYR   B 9   ? 0.1814 0.1928 0.2553 0.0157  0.0224  0.0497  15  TYR   C O   
1156 C CB  . TYR   B 9   ? 0.1946 0.1996 0.2517 0.0281  0.0306  0.0461  15  TYR   C CB  
1157 C CG  . TYR   B 9   ? 0.2137 0.2149 0.2645 0.0353  0.0368  0.0465  15  TYR   C CG  
1158 C CD1 . TYR   B 9   ? 0.2472 0.2494 0.3029 0.0370  0.0385  0.0466  15  TYR   C CD1 
1159 C CD2 . TYR   B 9   ? 0.2418 0.2378 0.2805 0.0413  0.0411  0.0466  15  TYR   C CD2 
1160 C CE1 . TYR   B 9   ? 0.2863 0.2842 0.3347 0.0444  0.0443  0.0464  15  TYR   C CE1 
1161 C CE2 . TYR   B 9   ? 0.2837 0.2754 0.3138 0.0492  0.0467  0.0467  15  TYR   C CE2 
1162 C CZ  . TYR   B 9   ? 0.3250 0.3176 0.3596 0.0507  0.0482  0.0461  15  TYR   C CZ  
1163 O OH  . TYR   B 9   ? 0.3989 0.3868 0.4245 0.0592  0.0539  0.0458  15  TYR   C OH  
1164 N N   . ARG   B 10  ? 0.1529 0.1688 0.2308 0.0152  0.0190  0.0479  16  ARG   C N   
1165 C CA  . ARG   B 10  ? 0.1454 0.1634 0.2226 0.0113  0.0127  0.0461  16  ARG   C CA  
1166 C C   . ARG   B 10  ? 0.1418 0.1587 0.2117 0.0128  0.0110  0.0421  16  ARG   C C   
1167 O O   . ARG   B 10  ? 0.1499 0.1677 0.2231 0.0143  0.0120  0.0418  16  ARG   C O   
1168 C CB  . ARG   B 10  ? 0.1591 0.1822 0.2475 0.0081  0.0095  0.0490  16  ARG   C CB  
1169 C CG  . ARG   B 10  ? 0.1623 0.1876 0.2481 0.0057  0.0035  0.0476  16  ARG   C CG  
1170 C CD  . ARG   B 10  ? 0.1678 0.1980 0.2636 0.0036  0.0000  0.0507  16  ARG   C CD  
1171 N NE  . ARG   B 10  ? 0.1688 0.2014 0.2629 0.0037  -0.0031 0.0510  16  ARG   C NE  
1172 C CZ  . ARG   B 10  ? 0.1798 0.2130 0.2682 0.0029  -0.0077 0.0501  16  ARG   C CZ  
1173 N NH1 . ARG   B 10  ? 0.1980 0.2291 0.2809 0.0016  -0.0106 0.0477  16  ARG   C NH1 
1174 N NH2 . ARG   B 10  ? 0.1911 0.2264 0.2785 0.0040  -0.0089 0.0515  16  ARG   C NH2 
1175 N N   . VAL   B 11  ? 0.1365 0.1514 0.1985 0.0123  0.0084  0.0390  17  VAL   C N   
1176 C CA  . VAL   B 11  ? 0.1279 0.1419 0.1855 0.0136  0.0067  0.0353  17  VAL   C CA  
1177 C C   . VAL   B 11  ? 0.1376 0.1541 0.1966 0.0107  0.0031  0.0358  17  VAL   C C   
1178 O O   . VAL   B 11  ? 0.1486 0.1648 0.2040 0.0089  0.0011  0.0360  17  VAL   C O   
1179 C CB  . VAL   B 11  ? 0.1464 0.1561 0.1940 0.0162  0.0068  0.0316  17  VAL   C CB  
1180 C CG1 . VAL   B 11  ? 0.1698 0.1789 0.2164 0.0176  0.0047  0.0275  17  VAL   C CG1 
1181 C CG2 . VAL   B 11  ? 0.1776 0.1841 0.2209 0.0202  0.0110  0.0319  17  VAL   C CG2 
1182 N N   . VAL   B 12  ? 0.1274 0.1462 0.1917 0.0107  0.0025  0.0363  18  VAL   C N   
1183 C CA  A VAL   B 12  ? 0.1234 0.1444 0.1884 0.0091  0.0002  0.0379  18  VAL   C CA  
1184 C CA  B VAL   B 12  ? 0.1442 0.1653 0.2091 0.0091  0.0001  0.0379  18  VAL   C CA  
1185 C C   . VAL   B 12  ? 0.1268 0.1476 0.1946 0.0104  0.0007  0.0364  18  VAL   C C   
1186 O O   . VAL   B 12  ? 0.1354 0.1549 0.2066 0.0122  0.0019  0.0339  18  VAL   C O   
1187 C CB  A VAL   B 12  ? 0.1223 0.1474 0.1939 0.0079  -0.0007 0.0423  18  VAL   C CB  
1188 C CB  B VAL   B 12  ? 0.1875 0.2126 0.2595 0.0079  -0.0005 0.0423  18  VAL   C CB  
1189 C CG1 A VAL   B 12  ? 0.1490 0.1748 0.2198 0.0061  -0.0028 0.0435  18  VAL   C CG1 
1190 C CG1 B VAL   B 12  ? 0.2050 0.2324 0.2759 0.0074  -0.0029 0.0446  18  VAL   C CG1 
1191 C CG2 A VAL   B 12  ? 0.0790 0.1056 0.1595 0.0091  0.0018  0.0437  18  VAL   C CG2 
1192 C CG2 B VAL   B 12  ? 0.2254 0.2509 0.2986 0.0066  -0.0011 0.0435  18  VAL   C CG2 
1193 N N   . ASN   B 13  ? 0.1207 0.1427 0.1880 0.0100  -0.0001 0.0380  19  ASN   C N   
1194 C CA  . ASN   B 13  ? 0.1239 0.1463 0.1978 0.0111  0.0012  0.0381  19  ASN   C CA  
1195 C C   . ASN   B 13  ? 0.1232 0.1481 0.2070 0.0114  0.0027  0.0409  19  ASN   C C   
1196 O O   . ASN   B 13  ? 0.1205 0.1480 0.2050 0.0108  0.0024  0.0450  19  ASN   C O   
1197 C CB  . ASN   B 13  ? 0.1215 0.1449 0.1933 0.0113  0.0015  0.0412  19  ASN   C CB  
1198 C CG  . ASN   B 13  ? 0.1285 0.1495 0.1914 0.0112  0.0005  0.0387  19  ASN   C CG  
1199 O OD1 . ASN   B 13  ? 0.1500 0.1704 0.2045 0.0104  -0.0013 0.0389  19  ASN   C OD1 
1200 N ND2 . ASN   B 13  ? 0.1410 0.1604 0.2067 0.0120  0.0012  0.0360  19  ASN   C ND2 
1201 N N   . ARG   B 14  ? 0.1260 0.1498 0.2180 0.0126  0.0038  0.0385  20  ARG   C N   
1202 C CA  . ARG   B 14  ? 0.1235 0.1491 0.2258 0.0131  0.0055  0.0409  20  ARG   C CA  
1203 C C   . ARG   B 14  ? 0.1301 0.1590 0.2368 0.0130  0.0068  0.0474  20  ARG   C C   
1204 O O   . ARG   B 14  ? 0.1338 0.1652 0.2443 0.0130  0.0074  0.0512  20  ARG   C O   
1205 C CB  . ARG   B 14  ? 0.1256 0.1490 0.2369 0.0145  0.0059  0.0365  20  ARG   C CB  
1206 C CG  . ARG   B 14  ? 0.1298 0.1539 0.2518 0.0153  0.0077  0.0379  20  ARG   C CG  
1207 C CD  . ARG   B 14  ? 0.1348 0.1561 0.2666 0.0168  0.0072  0.0325  20  ARG   C CD  
1208 N NE  . ARG   B 14  ? 0.1304 0.1513 0.2724 0.0180  0.0088  0.0323  20  ARG   C NE  
1209 C CZ  . ARG   B 14  ? 0.1269 0.1499 0.2821 0.0177  0.0112  0.0369  20  ARG   C CZ  
1210 N NH1 . ARG   B 14  ? 0.1513 0.1772 0.3097 0.0166  0.0129  0.0430  20  ARG   C NH1 
1211 N NH2 . ARG   B 14  ? 0.1402 0.1620 0.3053 0.0190  0.0124  0.0356  20  ARG   C NH2 
1212 N N   . HIS   B 15  ? 0.1302 0.1592 0.2356 0.0134  0.0075  0.0492  21  HIS   C N   
1213 C CA  . HIS   B 15  ? 0.1368 0.1685 0.2447 0.0146  0.0095  0.0561  21  HIS   C CA  
1214 C C   . HIS   B 15  ? 0.1395 0.1732 0.2370 0.0147  0.0072  0.0593  21  HIS   C C   
1215 O O   . HIS   B 15  ? 0.1683 0.2044 0.2666 0.0166  0.0083  0.0651  21  HIS   C O   
1216 C CB  . HIS   B 15  ? 0.1441 0.1751 0.2547 0.0160  0.0122  0.0579  21  HIS   C CB  
1217 C CG  . HIS   B 15  ? 0.1318 0.1613 0.2294 0.0161  0.0109  0.0567  21  HIS   C CG  
1218 N ND1 . HIS   B 15  ? 0.1416 0.1685 0.2359 0.0149  0.0092  0.0507  21  HIS   C ND1 
1219 C CD2 . HIS   B 15  ? 0.1534 0.1834 0.2411 0.0179  0.0113  0.0607  21  HIS   C CD2 
1220 C CE1 . HIS   B 15  ? 0.1578 0.1838 0.2409 0.0155  0.0088  0.0515  21  HIS   C CE1 
1221 N NE2 . HIS   B 15  ? 0.1618 0.1895 0.2403 0.0174  0.0100  0.0571  21  HIS   C NE2 
1222 N N   . LEU   B 16  ? 0.1349 0.1677 0.2239 0.0130  0.0039  0.0558  22  LEU   C N   
1223 C CA  . LEU   B 16  ? 0.1435 0.1781 0.2250 0.0127  0.0004  0.0576  22  LEU   C CA  
1224 C C   . LEU   B 16  ? 0.1511 0.1872 0.2375 0.0112  -0.0011 0.0572  22  LEU   C C   
1225 O O   . LEU   B 16  ? 0.1613 0.1989 0.2444 0.0104  -0.0047 0.0580  22  LEU   C O   
1226 C CB  . LEU   B 16  ? 0.1473 0.1793 0.2172 0.0121  -0.0021 0.0544  22  LEU   C CB  
1227 C CG  . LEU   B 16  ? 0.1604 0.1909 0.2248 0.0141  -0.0002 0.0554  22  LEU   C CG  
1228 C CD1 . LEU   B 16  ? 0.1795 0.2070 0.2326 0.0134  -0.0026 0.0516  22  LEU   C CD1 
1229 C CD2 . LEU   B 16  ? 0.1799 0.2124 0.2421 0.0173  0.0005  0.0613  22  LEU   C CD2 
1230 N N   . ALA   B 17  ? 0.1436 0.1792 0.2383 0.0110  0.0015  0.0558  23  ALA   C N   
1231 C CA  . ALA   B 17  ? 0.1309 0.1676 0.2307 0.0102  0.0015  0.0560  23  ALA   C CA  
1232 C C   . ALA   B 17  ? 0.1430 0.1842 0.2487 0.0106  0.0001  0.0613  23  ALA   C C   
1233 O O   . ALA   B 17  ? 0.1563 0.1991 0.2652 0.0122  0.0012  0.0650  23  ALA   C O   
1234 C CB  . ALA   B 17  ? 0.1532 0.1878 0.2593 0.0111  0.0049  0.0533  23  ALA   C CB  
1235 N N   . THR   B 18  ? 0.1552 0.1982 0.2628 0.0093  -0.0021 0.0619  24  THR   C N   
1236 C CA  . THR   B 18  ? 0.1527 0.2001 0.2666 0.0097  -0.0044 0.0665  24  THR   C CA  
1237 C C   . THR   B 18  ? 0.1353 0.1841 0.2612 0.0102  -0.0007 0.0685  24  THR   C C   
1238 O O   . THR   B 18  ? 0.1434 0.1893 0.2715 0.0104  0.0033  0.0658  24  THR   C O   
1239 C CB  . THR   B 18  ? 0.1619 0.2108 0.2746 0.0079  -0.0095 0.0657  24  THR   C CB  
1240 O OG1 . THR   B 18  ? 0.1729 0.2204 0.2908 0.0065  -0.0069 0.0640  24  THR   C OG1 
1241 C CG2 . THR   B 18  ? 0.1889 0.2355 0.2894 0.0075  -0.0134 0.0628  24  THR   C CG2 
1242 N N   . HIS   B 19  ? 0.1570 0.2103 0.2907 0.0109  -0.0024 0.0733  25  HIS   C N   
1243 C CA  . HIS   B 19  ? 0.1570 0.2119 0.3030 0.0114  0.0011  0.0757  25  HIS   C CA  
1244 C C   . HIS   B 19  ? 0.1300 0.1836 0.2788 0.0101  0.0027  0.0734  25  HIS   C C   
1245 O O   . HIS   B 19  ? 0.1503 0.2016 0.3031 0.0113  0.0079  0.0722  25  HIS   C O   
1246 C CB  . HIS   B 19  ? 0.1749 0.2354 0.3291 0.0123  -0.0021 0.0813  25  HIS   C CB  
1247 C CG  . HIS   B 19  ? 0.1705 0.2331 0.3384 0.0126  0.0013  0.0838  25  HIS   C CG  
1248 N ND1 . HIS   B 19  ? 0.2019 0.2632 0.3763 0.0143  0.0068  0.0849  25  HIS   C ND1 
1249 C CD2 . HIS   B 19  ? 0.1890 0.2538 0.3651 0.0114  0.0005  0.0848  25  HIS   C CD2 
1250 C CE1 . HIS   B 19  ? 0.1867 0.2500 0.3722 0.0146  0.0089  0.0871  25  HIS   C CE1 
1251 N NE2 . HIS   B 19  ? 0.1911 0.2566 0.3785 0.0128  0.0057  0.0873  25  HIS   C NE2 
1252 N N   . ASN   B 20  ? 0.1419 0.1964 0.2886 0.0082  -0.0012 0.0725  26  ASN   C N   
1253 C CA  . ASN   B 20  ? 0.1588 0.2119 0.3096 0.0073  0.0016  0.0715  26  ASN   C CA  
1254 C C   . ASN   B 20  ? 0.1413 0.1885 0.2835 0.0084  0.0065  0.0672  26  ASN   C C   
1255 O O   . ASN   B 20  ? 0.1440 0.1892 0.2893 0.0099  0.0116  0.0671  26  ASN   C O   
1256 C CB  . ASN   B 20  ? 0.1858 0.2403 0.3375 0.0049  -0.0037 0.0710  26  ASN   C CB  
1257 C CG  . ASN   B 20  ? 0.2597 0.3132 0.4194 0.0043  0.0003  0.0716  26  ASN   C CG  
1258 O OD1 . ASN   B 20  ? 0.2894 0.3459 0.4626 0.0046  0.0026  0.0754  26  ASN   C OD1 
1259 N ND2 . ASN   B 20  ? 0.2810 0.3303 0.4335 0.0038  0.0021  0.0686  26  ASN   C ND2 
1260 N N   . ASP   B 21  ? 0.1377 0.1821 0.2687 0.0084  0.0049  0.0637  27  ASP   C N   
1261 C CA  . ASP   B 21  ? 0.1439 0.1831 0.2672 0.0099  0.0085  0.0593  27  ASP   C CA  
1262 C C   . ASP   B 21  ? 0.1282 0.1656 0.2555 0.0126  0.0130  0.0585  27  ASP   C C   
1263 O O   . ASP   B 21  ? 0.1439 0.1778 0.2691 0.0149  0.0169  0.0563  27  ASP   C O   
1264 C CB  . ASP   B 21  ? 0.1350 0.1722 0.2483 0.0094  0.0060  0.0561  27  ASP   C CB  
1265 C CG  . ASP   B 21  ? 0.1497 0.1863 0.2559 0.0075  0.0024  0.0550  27  ASP   C CG  
1266 O OD1 . ASP   B 21  ? 0.1685 0.2041 0.2752 0.0069  0.0032  0.0547  27  ASP   C OD1 
1267 O OD2 . ASP   B 21  ? 0.1563 0.1935 0.2572 0.0069  -0.0009 0.0548  27  ASP   C OD2 
1268 N N   . TRP   B 22  ? 0.1267 0.1664 0.2601 0.0129  0.0125  0.0606  28  TRP   C N   
1269 C CA  . TRP   B 22  ? 0.1302 0.1681 0.2695 0.0153  0.0162  0.0596  28  TRP   C CA  
1270 C C   . TRP   B 22  ? 0.1242 0.1629 0.2713 0.0168  0.0201  0.0622  28  TRP   C C   
1271 O O   . TRP   B 22  ? 0.1406 0.1757 0.2879 0.0198  0.0240  0.0594  28  TRP   C O   
1272 C CB  . TRP   B 22  ? 0.1347 0.1749 0.2805 0.0153  0.0153  0.0623  28  TRP   C CB  
1273 C CG  . TRP   B 22  ? 0.1315 0.1693 0.2721 0.0151  0.0141  0.0591  28  TRP   C CG  
1274 C CD1 . TRP   B 22  ? 0.1508 0.1902 0.2868 0.0139  0.0113  0.0608  28  TRP   C CD1 
1275 C CD2 . TRP   B 22  ? 0.1179 0.1513 0.2590 0.0167  0.0155  0.0536  28  TRP   C CD2 
1276 N NE1 . TRP   B 22  ? 0.1466 0.1831 0.2813 0.0144  0.0118  0.0575  28  TRP   C NE1 
1277 C CE2 . TRP   B 22  ? 0.1355 0.1684 0.2743 0.0159  0.0138  0.0529  28  TRP   C CE2 
1278 C CE3 . TRP   B 22  ? 0.1526 0.1821 0.2966 0.0191  0.0178  0.0492  28  TRP   C CE3 
1279 C CZ2 . TRP   B 22  ? 0.1373 0.1669 0.2790 0.0168  0.0139  0.0480  28  TRP   C CZ2 
1280 C CZ3 . TRP   B 22  ? 0.1588 0.1844 0.3037 0.0204  0.0171  0.0435  28  TRP   C CZ3 
1281 C CH2 . TRP   B 22  ? 0.1487 0.1746 0.2939 0.0189  0.0150  0.0431  28  TRP   C CH2 
1282 N N   . ALA   B 23  ? 0.1334 0.1768 0.2868 0.0151  0.0187  0.0670  29  ALA   C N   
1283 C CA  . ALA   B 23  ? 0.1395 0.1842 0.3026 0.0164  0.0228  0.0703  29  ALA   C CA  
1284 C C   . ALA   B 23  ? 0.1480 0.1891 0.3065 0.0180  0.0270  0.0687  29  ALA   C C   
1285 O O   . ALA   B 23  ? 0.1633 0.2043 0.3287 0.0202  0.0322  0.0713  29  ALA   C O   
1286 C CB  . ALA   B 23  ? 0.1454 0.1967 0.3189 0.0141  0.0191  0.0759  29  ALA   C CB  
1287 N N   . ASN   B 24  ? 0.1563 0.1942 0.3032 0.0174  0.0255  0.0650  30  ASN   C N   
1288 C CA  . ASN   B 24  ? 0.1623 0.1962 0.3028 0.0196  0.0297  0.0638  30  ASN   C CA  
1289 C C   . ASN   B 24  ? 0.1680 0.1962 0.2940 0.0220  0.0296  0.0575  30  ASN   C C   
1290 O O   . ASN   B 24  ? 0.1596 0.1850 0.2766 0.0223  0.0297  0.0557  30  ASN   C O   
1291 C CB  . ASN   B 24  ? 0.1835 0.2199 0.3266 0.0162  0.0270  0.0663  30  ASN   C CB  
1292 C CG  . ASN   B 24  ? 0.1841 0.2259 0.3435 0.0145  0.0269  0.0720  30  ASN   C CG  
1293 O OD1 . ASN   B 24  ? 0.2133 0.2548 0.3806 0.0167  0.0331  0.0754  30  ASN   C OD1 
1294 N ND2 . ASN   B 24  ? 0.1859 0.2327 0.3513 0.0113  0.0204  0.0735  30  ASN   C ND2 
1295 N N   . LEU   B 25  ? 0.1725 0.1990 0.2972 0.0234  0.0288  0.0540  31  LEU   C N   
1296 C CA  . LEU   B 25  ? 0.1623 0.1841 0.2758 0.0253  0.0270  0.0475  31  LEU   C CA  
1297 C C   . LEU   B 25  ? 0.1831 0.1989 0.2859 0.0306  0.0309  0.0439  31  LEU   C C   
1298 O O   . LEU   B 25  ? 0.2042 0.2179 0.3083 0.0347  0.0360  0.0447  31  LEU   C O   
1299 C CB  . LEU   B 25  ? 0.1675 0.1890 0.2867 0.0257  0.0256  0.0450  31  LEU   C CB  
1300 C CG  . LEU   B 25  ? 0.1715 0.1888 0.2833 0.0272  0.0227  0.0380  31  LEU   C CG  
1301 C CD1 . LEU   B 25  ? 0.1709 0.1900 0.2787 0.0235  0.0183  0.0380  31  LEU   C CD1 
1302 C CD2 . LEU   B 25  ? 0.1961 0.2129 0.3170 0.0278  0.0219  0.0356  31  LEU   C CD2 
1303 N N   . VAL   B 26  ? 0.1726 0.1853 0.2639 0.0313  0.0287  0.0400  32  VAL   C N   
1304 C CA  . VAL   B 26  ? 0.1854 0.1920 0.2639 0.0374  0.0312  0.0358  32  VAL   C CA  
1305 C C   . VAL   B 26  ? 0.1946 0.1977 0.2678 0.0395  0.0266  0.0278  32  VAL   C C   
1306 O O   . VAL   B 26  ? 0.2241 0.2224 0.2917 0.0452  0.0277  0.0230  32  VAL   C O   
1307 C CB  . VAL   B 26  ? 0.2021 0.2077 0.2720 0.0373  0.0319  0.0374  32  VAL   C CB  
1308 C CG1 . VAL   B 26  ? 0.2419 0.2409 0.2962 0.0444  0.0339  0.0330  32  VAL   C CG1 
1309 C CG2 . VAL   B 26  ? 0.2014 0.2099 0.2791 0.0356  0.0366  0.0448  32  VAL   C CG2 
1310 N N   . TRP   B 27  ? 0.1761 0.1814 0.2515 0.0352  0.0212  0.0261  33  TRP   C N   
1311 C CA  . TRP   B 27  ? 0.1827 0.1851 0.2559 0.0368  0.0165  0.0188  33  TRP   C CA  
1312 C C   . TRP   B 27  ? 0.1770 0.1835 0.2585 0.0312  0.0127  0.0201  33  TRP   C C   
1313 O O   . TRP   B 27  ? 0.1728 0.1826 0.2540 0.0274  0.0125  0.0246  33  TRP   C O   
1314 C CB  . TRP   B 27  ? 0.2077 0.2053 0.2656 0.0412  0.0152  0.0141  33  TRP   C CB  
1315 C CG  . TRP   B 27  ? 0.2141 0.2095 0.2703 0.0422  0.0090  0.0066  33  TRP   C CG  
1316 C CD1 . TRP   B 27  ? 0.2476 0.2391 0.3036 0.0466  0.0058  -0.0010 33  TRP   C CD1 
1317 C CD2 . TRP   B 27  ? 0.1992 0.1965 0.2557 0.0387  0.0050  0.0060  33  TRP   C CD2 
1318 N NE1 . TRP   B 27  ? 0.2583 0.2491 0.3149 0.0460  -0.0004 -0.0064 33  TRP   C NE1 
1319 C CE2 . TRP   B 27  ? 0.2260 0.2204 0.2828 0.0412  -0.0004 -0.0018 33  TRP   C CE2 
1320 C CE3 . TRP   B 27  ? 0.1909 0.1916 0.2472 0.0340  0.0054  0.0110  33  TRP   C CE3 
1321 C CZ2 . TRP   B 27  ? 0.2181 0.2135 0.2762 0.0391  -0.0048 -0.0040 33  TRP   C CZ2 
1322 C CZ3 . TRP   B 27  ? 0.2086 0.2094 0.2637 0.0325  0.0014  0.0085  33  TRP   C CZ3 
1323 C CH2 . TRP   B 27  ? 0.2186 0.2172 0.2757 0.0348  -0.0033 0.0016  33  TRP   C CH2 
1324 N N   . GLU   B 28  ? 0.1660 0.1719 0.2549 0.0311  0.0096  0.0159  34  GLU   C N   
1325 C CA  . GLU   B 28  ? 0.1762 0.1855 0.2731 0.0269  0.0071  0.0176  34  GLU   C CA  
1326 C C   . GLU   B 28  ? 0.1700 0.1766 0.2719 0.0283  0.0032  0.0108  34  GLU   C C   
1327 O O   . GLU   B 28  ? 0.1810 0.1841 0.2854 0.0319  0.0023  0.0053  34  GLU   C O   
1328 C CB  . GLU   B 28  ? 0.1742 0.1881 0.2827 0.0236  0.0092  0.0243  34  GLU   C CB  
1329 C CG  . GLU   B 28  ? 0.1835 0.1967 0.3021 0.0253  0.0110  0.0238  34  GLU   C CG  
1330 C CD  . GLU   B 28  ? 0.1933 0.2052 0.3238 0.0256  0.0091  0.0200  34  GLU   C CD  
1331 O OE1 . GLU   B 28  ? 0.2160 0.2253 0.3529 0.0281  0.0099  0.0168  34  GLU   C OE1 
1332 O OE2 . GLU   B 28  ? 0.1769 0.1904 0.3122 0.0234  0.0074  0.0207  34  GLU   C OE2 
1333 N N   . ASP   B 29  ? 0.1567 0.1649 0.2617 0.0257  0.0008  0.0110  35  ASP   C N   
1334 C CA  . ASP   B 29  ? 0.1608 0.1674 0.2746 0.0266  -0.0030 0.0051  35  ASP   C CA  
1335 C C   . ASP   B 29  ? 0.1572 0.1675 0.2811 0.0228  -0.0025 0.0098  35  ASP   C C   
1336 O O   . ASP   B 29  ? 0.1472 0.1587 0.2642 0.0213  -0.0027 0.0118  35  ASP   C O   
1337 C CB  . ASP   B 29  ? 0.1855 0.1880 0.2873 0.0300  -0.0071 -0.0020 35  ASP   C CB  
1338 C CG  . ASP   B 29  ? 0.2328 0.2334 0.3433 0.0314  -0.0126 -0.0093 35  ASP   C CG  
1339 O OD1 . ASP   B 29  ? 0.2263 0.2296 0.3515 0.0283  -0.0128 -0.0073 35  ASP   C OD1 
1340 O OD2 . ASP   B 29  ? 0.2708 0.2672 0.3730 0.0359  -0.0168 -0.0169 35  ASP   C OD2 
1341 N N   . SER   B 30  ? 0.1467 0.1582 0.2871 0.0218  -0.0012 0.0115  36  SER   C N   
1342 C CA  A SER   B 30  ? 0.1486 0.1634 0.2995 0.0193  0.0007  0.0171  36  SER   C CA  
1343 C CA  B SER   B 30  ? 0.1541 0.1690 0.3045 0.0193  0.0008  0.0172  36  SER   C CA  
1344 C C   . SER   B 30  ? 0.1501 0.1640 0.3039 0.0192  -0.0022 0.0133  36  SER   C C   
1345 O O   . SER   B 30  ? 0.1464 0.1626 0.2988 0.0177  -0.0003 0.0182  36  SER   C O   
1346 C CB  A SER   B 30  ? 0.1562 0.1719 0.3259 0.0190  0.0032  0.0197  36  SER   C CB  
1347 C CB  B SER   B 30  ? 0.1770 0.1932 0.3451 0.0188  0.0037  0.0208  36  SER   C CB  
1348 O OG  A SER   B 30  ? 0.1476 0.1657 0.3291 0.0176  0.0056  0.0247  36  SER   C OG  
1349 O OG  B SER   B 30  ? 0.1982 0.2111 0.3784 0.0204  0.0008  0.0134  36  SER   C OG  
1350 N N   . SER   B 31  ? 0.1541 0.1646 0.3115 0.0214  -0.0072 0.0044  37  SER   C N   
1351 C CA  . SER   B 31  ? 0.1646 0.1746 0.3268 0.0215  -0.0107 0.0005  37  SER   C CA  
1352 C C   . SER   B 31  ? 0.1426 0.1529 0.2873 0.0214  -0.0113 0.0015  37  SER   C C   
1353 O O   . SER   B 31  ? 0.1518 0.1630 0.3008 0.0206  -0.0121 0.0017  37  SER   C O   
1354 C CB  . SER   B 31  ? 0.2186 0.2249 0.3868 0.0244  -0.0174 -0.0100 37  SER   C CB  
1355 O OG  . SER   B 31  ? 0.2785 0.2814 0.4276 0.0278  -0.0210 -0.0158 37  SER   C OG  
1356 N N   . ARG   B 32  ? 0.1360 0.1455 0.2626 0.0221  -0.0102 0.0027  38  ARG   C N   
1357 C CA  . ARG   B 32  ? 0.1398 0.1493 0.2509 0.0218  -0.0102 0.0040  38  ARG   C CA  
1358 C C   . ARG   B 32  ? 0.1310 0.1435 0.2375 0.0189  -0.0057 0.0123  38  ARG   C C   
1359 O O   . ARG   B 32  ? 0.1370 0.1495 0.2322 0.0184  -0.0055 0.0137  38  ARG   C O   
1360 C CB  . ARG   B 32  ? 0.1784 0.1847 0.2736 0.0249  -0.0116 0.0003  38  ARG   C CB  
1361 C CG  . ARG   B 32  ? 0.1925 0.1950 0.2874 0.0292  -0.0170 -0.0087 38  ARG   C CG  
1362 C CD  . ARG   B 32  ? 0.1681 0.1669 0.2456 0.0335  -0.0172 -0.0114 38  ARG   C CD  
1363 N NE  . ARG   B 32  ? 0.1702 0.1689 0.2340 0.0336  -0.0162 -0.0089 38  ARG   C NE  
1364 C CZ  . ARG   B 32  ? 0.1816 0.1767 0.2306 0.0383  -0.0175 -0.0120 38  ARG   C CZ  
1365 N NH1 . ARG   B 32  ? 0.2069 0.1981 0.2508 0.0439  -0.0200 -0.0180 38  ARG   C NH1 
1366 N NH2 . ARG   B 32  ? 0.1899 0.1848 0.2290 0.0381  -0.0163 -0.0093 38  ARG   C NH2 
1367 N N   . ASP   B 33  ? 0.1249 0.1398 0.2394 0.0175  -0.0024 0.0176  39  ASP   C N   
1368 C CA  . ASP   B 33  ? 0.1239 0.1416 0.2327 0.0157  0.0007  0.0248  39  ASP   C CA  
1369 C C   . ASP   B 33  ? 0.1326 0.1495 0.2274 0.0156  0.0004  0.0249  39  ASP   C C   
1370 O O   . ASP   B 33  ? 0.1338 0.1518 0.2207 0.0143  0.0009  0.0283  39  ASP   C O   
1371 C CB  . ASP   B 33  ? 0.1332 0.1523 0.2411 0.0148  0.0021  0.0285  39  ASP   C CB  
1372 C CG  . ASP   B 33  ? 0.1435 0.1649 0.2450 0.0139  0.0045  0.0353  39  ASP   C CG  
1373 O OD1 . ASP   B 33  ? 0.1474 0.1707 0.2534 0.0138  0.0060  0.0390  39  ASP   C OD1 
1374 O OD2 . ASP   B 33  ? 0.1409 0.1621 0.2333 0.0137  0.0045  0.0368  39  ASP   C OD2 
1375 N N   . LEU   B 34  ? 0.1214 0.1364 0.2137 0.0174  -0.0002 0.0214  40  LEU   C N   
1376 C CA  . LEU   B 34  ? 0.1231 0.1374 0.2045 0.0176  0.0006  0.0225  40  LEU   C CA  
1377 C C   . LEU   B 34  ? 0.1234 0.1385 0.2087 0.0182  0.0029  0.0246  40  LEU   C C   
1378 O O   . LEU   B 34  ? 0.1360 0.1501 0.2288 0.0199  0.0031  0.0222  40  LEU   C O   
1379 C CB  . LEU   B 34  ? 0.1429 0.1532 0.2147 0.0205  -0.0010 0.0171  40  LEU   C CB  
1380 C CG  . LEU   B 34  ? 0.1543 0.1635 0.2194 0.0203  -0.0030 0.0154  40  LEU   C CG  
1381 C CD1 . LEU   B 34  ? 0.1757 0.1808 0.2306 0.0243  -0.0044 0.0105  40  LEU   C CD1 
1382 C CD2 . LEU   B 34  ? 0.1503 0.1611 0.2100 0.0175  -0.0016 0.0202  40  LEU   C CD2 
1383 N N   . LEU   B 35  ? 0.1190 0.1354 0.1999 0.0170  0.0044  0.0285  41  LEU   C N   
1384 C CA  . LEU   B 35  ? 0.1292 0.1464 0.2136 0.0178  0.0069  0.0308  41  LEU   C CA  
1385 C C   . LEU   B 35  ? 0.1344 0.1510 0.2116 0.0178  0.0083  0.0326  41  LEU   C C   
1386 O O   . LEU   B 35  ? 0.1410 0.1585 0.2142 0.0156  0.0069  0.0342  41  LEU   C O   
1387 C CB  . LEU   B 35  ? 0.1249 0.1467 0.2189 0.0155  0.0074  0.0364  41  LEU   C CB  
1388 C CG  . LEU   B 35  ? 0.1305 0.1538 0.2307 0.0162  0.0100  0.0395  41  LEU   C CG  
1389 C CD1 . LEU   B 35  ? 0.1511 0.1774 0.2627 0.0157  0.0106  0.0427  41  LEU   C CD1 
1390 C CD2 . LEU   B 35  ? 0.1392 0.1648 0.2373 0.0144  0.0100  0.0434  41  LEU   C CD2 
1391 N N   . VAL   B 36  ? 0.1304 0.1451 0.2067 0.0207  0.0114  0.0323  42  VAL   C N   
1392 C CA  . VAL   B 36  ? 0.1354 0.1493 0.2076 0.0214  0.0143  0.0350  42  VAL   C CA  
1393 C C   . VAL   B 36  ? 0.1363 0.1527 0.2174 0.0214  0.0176  0.0395  42  VAL   C C   
1394 O O   . VAL   B 36  ? 0.1610 0.1765 0.2458 0.0240  0.0196  0.0384  42  VAL   C O   
1395 C CB  . VAL   B 36  ? 0.1559 0.1645 0.2171 0.0264  0.0163  0.0313  42  VAL   C CB  
1396 C CG1 . VAL   B 36  ? 0.1876 0.1952 0.2462 0.0276  0.0208  0.0354  42  VAL   C CG1 
1397 C CG2 . VAL   B 36  ? 0.1726 0.1792 0.2259 0.0265  0.0124  0.0268  42  VAL   C CG2 
1398 N N   . SER   B 37  ? 0.1349 0.1541 0.2206 0.0186  0.0180  0.0441  43  SER   C N   
1399 C CA  . SER   B 37  ? 0.1421 0.1643 0.2385 0.0184  0.0209  0.0489  43  SER   C CA  
1400 C C   . SER   B 37  ? 0.1464 0.1673 0.2429 0.0194  0.0250  0.0518  43  SER   C C   
1401 O O   . SER   B 37  ? 0.1644 0.1825 0.2533 0.0196  0.0249  0.0506  43  SER   C O   
1402 C CB  . SER   B 37  ? 0.1391 0.1668 0.2447 0.0142  0.0168  0.0522  43  SER   C CB  
1403 O OG  . SER   B 37  ? 0.1578 0.1865 0.2608 0.0111  0.0128  0.0524  43  SER   C OG  
1404 N N   . SER   B 38  ? 0.1623 0.1845 0.2678 0.0208  0.0296  0.0560  44  SER   C N   
1405 C CA  . SER   B 38  ? 0.1779 0.1990 0.2870 0.0221  0.0350  0.0601  44  SER   C CA  
1406 C C   . SER   B 38  ? 0.1951 0.2210 0.3173 0.0169  0.0316  0.0639  44  SER   C C   
1407 O O   . SER   B 38  ? 0.2163 0.2470 0.3468 0.0135  0.0266  0.0647  44  SER   C O   
1408 C CB  . SER   B 38  ? 0.2062 0.2260 0.3194 0.0269  0.0426  0.0632  44  SER   C CB  
1409 O OG  . SER   B 38  ? 0.2484 0.2733 0.3752 0.0245  0.0412  0.0659  44  SER   C OG  
1410 N N   . THR   B 39  ? 0.1926 0.2170 0.3171 0.0167  0.0343  0.0663  45  THR   C N   
1411 C CA  . THR   B 39  ? 0.2101 0.2384 0.3481 0.0118  0.0302  0.0688  45  THR   C CA  
1412 C C   . THR   B 39  ? 0.2360 0.2649 0.3890 0.0131  0.0374  0.0751  45  THR   C C   
1413 O O   . THR   B 39  ? 0.2262 0.2510 0.3743 0.0181  0.0459  0.0773  45  THR   C O   
1414 C CB  . THR   B 39  ? 0.2215 0.2474 0.3519 0.0095  0.0262  0.0657  45  THR   C CB  
1415 O OG1 . THR   B 39  ? 0.2414 0.2622 0.3650 0.0132  0.0329  0.0667  45  THR   C OG1 
1416 C CG2 . THR   B 39  ? 0.2299 0.2549 0.3461 0.0085  0.0200  0.0600  45  THR   C CG2 
1417 N N   . THR   B 40  ? 0.2566 0.2901 0.4275 0.0088  0.0335  0.0778  46  THR   C N   
1418 C CA  . THR   B 40  ? 0.2801 0.3146 0.4692 0.0095  0.0402  0.0842  46  THR   C CA  
1419 C C   . THR   B 40  ? 0.2923 0.3230 0.4816 0.0090  0.0424  0.0849  46  THR   C C   
1420 O O   . THR   B 40  ? 0.3285 0.3561 0.5208 0.0129  0.0523  0.0898  46  THR   C O   
1421 C CB  . THR   B 40  ? 0.3298 0.3712 0.5406 0.0056  0.0351  0.0869  46  THR   C CB  
1422 O OG1 . THR   B 40  ? 0.3762 0.4199 0.5883 0.0006  0.0239  0.0827  46  THR   C OG1 
1423 C CG2 . THR   B 40  ? 0.3260 0.3704 0.5358 0.0071  0.0345  0.0871  46  THR   C CG2 
1424 N N   . ALA   B 41  ? 0.2690 0.2997 0.4544 0.0048  0.0338  0.0802  47  ALA   C N   
1425 C CA  . ALA   B 41  ? 0.2808 0.3077 0.4666 0.0040  0.0351  0.0802  47  ALA   C CA  
1426 C C   . ALA   B 41  ? 0.2809 0.3018 0.4438 0.0079  0.0386  0.0773  47  ALA   C C   
1427 O O   . ALA   B 41  ? 0.2819 0.3023 0.4287 0.0088  0.0349  0.0727  47  ALA   C O   
1428 C CB  . ALA   B 41  ? 0.2913 0.3204 0.4835 -0.0018 0.0239  0.0758  47  ALA   C CB  
1429 N N   . GLN   B 42  ? 0.2880 0.3045 0.4502 0.0102  0.0450  0.0801  48  GLN   C N   
1430 C CA  . GLN   B 42  ? 0.3017 0.3126 0.4429 0.0141  0.0475  0.0776  48  GLN   C CA  
1431 C C   . GLN   B 42  ? 0.2881 0.2984 0.4224 0.0098  0.0385  0.0715  48  GLN   C C   
1432 O O   . GLN   B 42  ? 0.3075 0.3192 0.4545 0.0051  0.0336  0.0710  48  GLN   C O   
1433 C CB  . GLN   B 42  ? 0.3692 0.3754 0.5119 0.0190  0.0583  0.0837  48  GLN   C CB  
1434 C CG  . GLN   B 42  ? 0.4746 0.4796 0.6155 0.0259  0.0688  0.0892  48  GLN   C CG  
1435 C CD  . GLN   B 42  ? 0.6145 0.6146 0.7561 0.0314  0.0798  0.0959  48  GLN   C CD  
1436 O OE1 . GLN   B 42  ? 0.6525 0.6535 0.8151 0.0295  0.0844  0.1021  48  GLN   C OE1 
1437 N NE2 . GLN   B 42  ? 0.6543 0.6489 0.7738 0.0384  0.0841  0.0950  48  GLN   C NE2 
1438 N N   . GLY   B 43  ? 0.2598 0.2677 0.3744 0.0119  0.0363  0.0667  49  GLY   C N   
1439 C CA  . GLY   B 43  ? 0.2521 0.2587 0.3576 0.0091  0.0292  0.0613  49  GLY   C CA  
1440 C C   . GLY   B 43  ? 0.2464 0.2475 0.3431 0.0123  0.0339  0.0620  49  GLY   C C   
1441 O O   . GLY   B 43  ? 0.2732 0.2714 0.3666 0.0177  0.0423  0.0662  49  GLY   C O   
1442 N N   . CYS   B 44  ? 0.2389 0.2386 0.3312 0.0095  0.0286  0.0581  50  CYS   C N   
1443 C CA  . CYS   B 44  ? 0.2518 0.2464 0.3383 0.0117  0.0322  0.0590  50  CYS   C CA  
1444 C C   . CYS   B 44  ? 0.2460 0.2382 0.3147 0.0135  0.0292  0.0542  50  CYS   C C   
1445 O O   . CYS   B 44  ? 0.2850 0.2732 0.3493 0.0151  0.0315  0.0547  50  CYS   C O   
1446 C CB  . CYS   B 44  ? 0.2637 0.2578 0.3649 0.0071  0.0297  0.0595  50  CYS   C CB  
1447 S SG  . CYS   B 44  ? 0.3772 0.3741 0.5042 0.0051  0.0337  0.0658  50  CYS   C SG  
1448 N N   . ASP   B 45  ? 0.2156 0.2100 0.2758 0.0130  0.0242  0.0497  51  ASP   C N   
1449 C CA  . ASP   B 45  ? 0.2241 0.2165 0.2698 0.0146  0.0213  0.0452  51  ASP   C CA  
1450 C C   . ASP   B 45  ? 0.2309 0.2200 0.2656 0.0214  0.0268  0.0464  51  ASP   C C   
1451 O O   . ASP   B 45  ? 0.2539 0.2432 0.2893 0.0249  0.0315  0.0492  51  ASP   C O   
1452 C CB  . ASP   B 45  ? 0.2235 0.2193 0.2655 0.0127  0.0154  0.0410  51  ASP   C CB  
1453 C CG  . ASP   B 45  ? 0.2813 0.2796 0.3293 0.0076  0.0094  0.0392  51  ASP   C CG  
1454 O OD1 . ASP   B 45  ? 0.3180 0.3143 0.3678 0.0055  0.0077  0.0385  51  ASP   C OD1 
1455 O OD2 . ASP   B 45  ? 0.2374 0.2393 0.2871 0.0061  0.0061  0.0382  51  ASP   C OD2 
1456 N N   . THR   B 46  ? 0.2082 0.1942 0.2325 0.0238  0.0262  0.0444  52  THR   C N   
1457 C CA  . THR   B 46  ? 0.2139 0.1965 0.2255 0.0309  0.0296  0.0444  52  THR   C CA  
1458 C C   . THR   B 46  ? 0.1972 0.1810 0.1999 0.0316  0.0236  0.0381  52  THR   C C   
1459 O O   . THR   B 46  ? 0.2085 0.1930 0.2112 0.0281  0.0188  0.0350  52  THR   C O   
1460 C CB  . THR   B 46  ? 0.2463 0.2247 0.2535 0.0336  0.0330  0.0468  52  THR   C CB  
1461 O OG1 . THR   B 46  ? 0.2714 0.2488 0.2898 0.0330  0.0392  0.0531  52  THR   C OG1 
1462 C CG2 . THR   B 46  ? 0.2866 0.2614 0.2783 0.0421  0.0355  0.0465  52  THR   C CG2 
1463 N N   . ILE   B 47  ? 0.2046 0.1880 0.2006 0.0364  0.0238  0.0362  53  ILE   C N   
1464 C CA  . ILE   B 47  ? 0.1945 0.1786 0.1847 0.0374  0.0180  0.0301  53  ILE   C CA  
1465 C C   . ILE   B 47  ? 0.1979 0.1784 0.1764 0.0427  0.0172  0.0282  53  ILE   C C   
1466 O O   . ILE   B 47  ? 0.2201 0.1970 0.1904 0.0490  0.0218  0.0308  53  ILE   C O   
1467 C CB  . ILE   B 47  ? 0.2090 0.1938 0.1980 0.0406  0.0179  0.0280  53  ILE   C CB  
1468 C CG1 . ILE   B 47  ? 0.2117 0.2000 0.2124 0.0363  0.0196  0.0309  53  ILE   C CG1 
1469 C CG2 . ILE   B 47  ? 0.2143 0.1999 0.2007 0.0412  0.0114  0.0214  53  ILE   C CG2 
1470 C CD1 . ILE   B 47  ? 0.2297 0.2221 0.2395 0.0291  0.0149  0.0299  53  ILE   C CD1 
1471 N N   . ALA   B 48  ? 0.1803 0.1616 0.1580 0.0408  0.0119  0.0242  54  ALA   C N   
1472 C CA  . ALA   B 48  ? 0.1842 0.1627 0.1520 0.0458  0.0100  0.0218  54  ALA   C CA  
1473 C C   . ALA   B 48  ? 0.1919 0.1689 0.1510 0.0529  0.0079  0.0178  54  ALA   C C   
1474 O O   . ALA   B 48  ? 0.1942 0.1732 0.1575 0.0520  0.0050  0.0143  54  ALA   C O   
1475 C CB  . ALA   B 48  ? 0.1795 0.1601 0.1512 0.0418  0.0047  0.0183  54  ALA   C CB  
1476 N N   . ARG   B 49  ? 0.1995 0.1725 0.1462 0.0604  0.0090  0.0181  55  ARG   C N   
1477 C CA  . ARG   B 49  ? 0.2030 0.1737 0.1389 0.0684  0.0056  0.0131  55  ARG   C CA  
1478 C C   . ARG   B 49  ? 0.2007 0.1700 0.1296 0.0720  0.0007  0.0100  55  ARG   C C   
1479 O O   . ARG   B 49  ? 0.2327 0.1985 0.1513 0.0775  0.0042  0.0136  55  ARG   C O   
1480 C CB  . ARG   B 49  ? 0.2270 0.1937 0.1520 0.0761  0.0122  0.0169  55  ARG   C CB  
1481 C CG  . ARG   B 49  ? 0.2222 0.1908 0.1568 0.0719  0.0176  0.0208  55  ARG   C CG  
1482 C CD  . ARG   B 49  ? 0.2314 0.2028 0.1729 0.0692  0.0130  0.0155  55  ARG   C CD  
1483 N NE  . ARG   B 49  ? 0.2291 0.2022 0.1793 0.0660  0.0187  0.0202  55  ARG   C NE  
1484 C CZ  . ARG   B 49  ? 0.2183 0.1948 0.1791 0.0611  0.0162  0.0179  55  ARG   C CZ  
1485 N NH1 . ARG   B 49  ? 0.2199 0.1981 0.1839 0.0594  0.0089  0.0113  55  ARG   C NH1 
1486 N NH2 . ARG   B 49  ? 0.2314 0.2098 0.2008 0.0582  0.0212  0.0226  55  ARG   C NH2 
1487 N N   . CYS   B 50  ? 0.1948 0.1669 0.1306 0.0691  -0.0069 0.0039  56  CYS   C N   
1488 C CA  . CYS   B 50  ? 0.1999 0.1720 0.1342 0.0703  -0.0120 0.0012  56  CYS   C CA  
1489 C C   . CYS   B 50  ? 0.1914 0.1670 0.1367 0.0672  -0.0197 -0.0054 56  CYS   C C   
1490 O O   . CYS   B 50  ? 0.2037 0.1815 0.1578 0.0638  -0.0208 -0.0075 56  CYS   C O   
1491 C CB  . CYS   B 50  ? 0.1923 0.1651 0.1317 0.0646  -0.0076 0.0067  56  CYS   C CB  
1492 S SG  . CYS   B 50  ? 0.1859 0.1634 0.1422 0.0537  -0.0075 0.0073  56  CYS   C SG  
1493 N N   . ASP   B 51  ? 0.2139 0.1900 0.1601 0.0686  -0.0249 -0.0083 57  ASP   C N   
1494 C CA  . ASP   B 51  ? 0.2214 0.2011 0.1814 0.0652  -0.0315 -0.0135 57  ASP   C CA  
1495 C C   . ASP   B 51  ? 0.1994 0.1812 0.1675 0.0597  -0.0297 -0.0102 57  ASP   C C   
1496 O O   . ASP   B 51  ? 0.2161 0.2000 0.1930 0.0591  -0.0348 -0.0136 57  ASP   C O   
1497 C CB  . ASP   B 51  ? 0.2660 0.2447 0.2232 0.0721  -0.0406 -0.0212 57  ASP   C CB  
1498 C CG  . ASP   B 51  ? 0.2957 0.2722 0.2420 0.0783  -0.0427 -0.0210 57  ASP   C CG  
1499 O OD1 . ASP   B 51  ? 0.2950 0.2703 0.2359 0.0772  -0.0364 -0.0146 57  ASP   C OD1 
1500 O OD2 . ASP   B 51  ? 0.3718 0.3479 0.3164 0.0842  -0.0514 -0.0277 57  ASP   C OD2 
1501 N N   . CYS   B 52  ? 0.1796 0.1607 0.1460 0.0556  -0.0227 -0.0039 58  CYS   C N   
1502 C CA  . CYS   B 52  ? 0.1787 0.1613 0.1522 0.0505  -0.0210 -0.0015 58  CYS   C CA  
1503 C C   . CYS   B 52  ? 0.1642 0.1507 0.1523 0.0458  -0.0235 -0.0037 58  CYS   C C   
1504 O O   . CYS   B 52  ? 0.1695 0.1579 0.1637 0.0439  -0.0240 -0.0049 58  CYS   C O   
1505 C CB  . CYS   B 52  ? 0.1869 0.1682 0.1583 0.0464  -0.0142 0.0043  58  CYS   C CB  
1506 S SG  . CYS   B 52  ? 0.2005 0.1769 0.1590 0.0510  -0.0093 0.0088  58  CYS   C SG  
1507 N N   . GLN   B 53  ? 0.1615 0.1492 0.1555 0.0443  -0.0241 -0.0034 59  GLN   C N   
1508 C CA  . GLN   B 53  ? 0.1659 0.1569 0.1738 0.0401  -0.0242 -0.0036 59  GLN   C CA  
1509 C C   . GLN   B 53  ? 0.1568 0.1473 0.1646 0.0366  -0.0193 0.0006  59  GLN   C C   
1510 O O   . GLN   B 53  ? 0.1594 0.1520 0.1770 0.0344  -0.0184 0.0013  59  GLN   C O   
1511 C CB  . GLN   B 53  ? 0.1745 0.1677 0.1928 0.0426  -0.0303 -0.0081 59  GLN   C CB  
1512 C CG  . GLN   B 53  ? 0.2341 0.2281 0.2566 0.0453  -0.0361 -0.0135 59  GLN   C CG  
1513 C CD  . GLN   B 53  ? 0.2328 0.2293 0.2699 0.0469  -0.0428 -0.0184 59  GLN   C CD  
1514 O OE1 . GLN   B 53  ? 0.2677 0.2632 0.3009 0.0523  -0.0495 -0.0233 59  GLN   C OE1 
1515 N NE2 . GLN   B 53  ? 0.2123 0.2121 0.2666 0.0428  -0.0411 -0.0168 59  GLN   C NE2 
1516 N N   . THR   B 54  ? 0.1558 0.1432 0.1533 0.0363  -0.0156 0.0036  60  THR   C N   
1517 C CA  . THR   B 54  ? 0.1687 0.1549 0.1656 0.0328  -0.0114 0.0068  60  THR   C CA  
1518 C C   . THR   B 54  ? 0.1659 0.1505 0.1572 0.0304  -0.0082 0.0094  60  THR   C C   
1519 O O   . THR   B 54  ? 0.1798 0.1628 0.1653 0.0324  -0.0078 0.0099  60  THR   C O   
1520 C CB  . THR   B 54  ? 0.2095 0.1932 0.2030 0.0346  -0.0106 0.0075  60  THR   C CB  
1521 O OG1 . THR   B 54  ? 0.2606 0.2412 0.2449 0.0374  -0.0100 0.0084  60  THR   C OG1 
1522 C CG2 . THR   B 54  ? 0.2080 0.1936 0.2083 0.0373  -0.0141 0.0051  60  THR   C CG2 
1523 N N   . GLY   B 55  ? 0.1509 0.1357 0.1440 0.0266  -0.0059 0.0111  61  GLY   C N   
1524 C CA  . GLY   B 55  ? 0.1471 0.1308 0.1372 0.0241  -0.0040 0.0130  61  GLY   C CA  
1525 C C   . GLY   B 55  ? 0.1330 0.1166 0.1240 0.0210  -0.0027 0.0140  61  GLY   C C   
1526 O O   . GLY   B 55  ? 0.1495 0.1326 0.1410 0.0214  -0.0021 0.0136  61  GLY   C O   
1527 N N   . VAL   B 56  ? 0.1357 0.1195 0.1264 0.0184  -0.0024 0.0151  62  VAL   C N   
1528 C CA  . VAL   B 56  ? 0.1317 0.1151 0.1212 0.0162  -0.0022 0.0156  62  VAL   C CA  
1529 C C   . VAL   B 56  ? 0.1299 0.1166 0.1227 0.0146  -0.0030 0.0167  62  VAL   C C   
1530 O O   . VAL   B 56  ? 0.1402 0.1278 0.1350 0.0139  -0.0033 0.0173  62  VAL   C O   
1531 C CB  . VAL   B 56  ? 0.1424 0.1216 0.1284 0.0149  -0.0020 0.0153  62  VAL   C CB  
1532 C CG1 . VAL   B 56  ? 0.1680 0.1463 0.1518 0.0131  -0.0033 0.0146  62  VAL   C CG1 
1533 C CG2 . VAL   B 56  ? 0.1592 0.1347 0.1421 0.0168  -0.0007 0.0146  62  VAL   C CG2 
1534 N N   . TYR   B 57  ? 0.1312 0.1194 0.1244 0.0144  -0.0028 0.0174  63  TYR   C N   
1535 C CA  . TYR   B 57  ? 0.1143 0.1057 0.1105 0.0132  -0.0035 0.0191  63  TYR   C CA  
1536 C C   . TYR   B 57  ? 0.1351 0.1255 0.1263 0.0126  -0.0045 0.0195  63  TYR   C C   
1537 O O   . TYR   B 57  ? 0.1482 0.1358 0.1336 0.0139  -0.0039 0.0187  63  TYR   C O   
1538 C CB  . TYR   B 57  ? 0.1326 0.1277 0.1356 0.0143  -0.0024 0.0204  63  TYR   C CB  
1539 C CG  . TYR   B 57  ? 0.1346 0.1302 0.1376 0.0158  -0.0002 0.0222  63  TYR   C CG  
1540 C CD1 . TYR   B 57  ? 0.1442 0.1382 0.1468 0.0176  0.0017  0.0218  63  TYR   C CD1 
1541 C CD2 . TYR   B 57  ? 0.1426 0.1403 0.1461 0.0161  0.0006  0.0250  63  TYR   C CD2 
1542 C CE1 . TYR   B 57  ? 0.1548 0.1490 0.1579 0.0197  0.0050  0.0243  63  TYR   C CE1 
1543 C CE2 . TYR   B 57  ? 0.1471 0.1449 0.1500 0.0185  0.0039  0.0277  63  TYR   C CE2 
1544 C CZ  . TYR   B 57  ? 0.1538 0.1499 0.1569 0.0203  0.0064  0.0275  63  TYR   C CZ  
1545 O OH  . TYR   B 57  ? 0.1799 0.1759 0.1832 0.0234  0.0109  0.0309  63  TYR   C OH  
1546 N N   . TYR   B 58  ? 0.1314 0.1240 0.1247 0.0112  -0.0063 0.0206  64  TYR   C N   
1547 C CA  . TYR   B 58  ? 0.1426 0.1346 0.1307 0.0114  -0.0085 0.0206  64  TYR   C CA  
1548 C C   . TYR   B 58  ? 0.1461 0.1408 0.1337 0.0136  -0.0069 0.0235  64  TYR   C C   
1549 O O   . TYR   B 58  ? 0.1420 0.1404 0.1364 0.0132  -0.0059 0.0259  64  TYR   C O   
1550 C CB  . TYR   B 58  ? 0.1510 0.1441 0.1427 0.0089  -0.0120 0.0204  64  TYR   C CB  
1551 C CG  . TYR   B 58  ? 0.1663 0.1585 0.1522 0.0096  -0.0159 0.0194  64  TYR   C CG  
1552 C CD1 . TYR   B 58  ? 0.1773 0.1648 0.1554 0.0107  -0.0177 0.0162  64  TYR   C CD1 
1553 C CD2 . TYR   B 58  ? 0.1769 0.1726 0.1646 0.0098  -0.0181 0.0213  64  TYR   C CD2 
1554 C CE1 . TYR   B 58  ? 0.2084 0.1945 0.1793 0.0123  -0.0222 0.0143  64  TYR   C CE1 
1555 C CE2 . TYR   B 58  ? 0.1963 0.1909 0.1771 0.0114  -0.0227 0.0200  64  TYR   C CE2 
1556 C CZ  . TYR   B 58  ? 0.2039 0.1936 0.1759 0.0128  -0.0249 0.0161  64  TYR   C CZ  
1557 O OH  . TYR   B 58  ? 0.2415 0.2295 0.2048 0.0154  -0.0303 0.0139  64  TYR   C OH  
1558 N N   . CYS   B 59  ? 0.1486 0.1410 0.1277 0.0163  -0.0064 0.0236  65  CYS   C N   
1559 C CA  . CYS   B 59  ? 0.1584 0.1524 0.1349 0.0196  -0.0038 0.0272  65  CYS   C CA  
1560 C C   . CYS   B 59  ? 0.1720 0.1651 0.1393 0.0214  -0.0076 0.0269  65  CYS   C C   
1561 O O   . CYS   B 59  ? 0.1903 0.1791 0.1469 0.0237  -0.0091 0.0244  65  CYS   C O   
1562 C CB  . CYS   B 59  ? 0.1640 0.1558 0.1373 0.0227  0.0008  0.0281  65  CYS   C CB  
1563 S SG  . CYS   B 59  ? 0.1862 0.1793 0.1568 0.0280  0.0061  0.0341  65  CYS   C SG  
1564 N N   . SER   B 60  ? 0.1804 0.1771 0.1518 0.0207  -0.0096 0.0291  66  SER   C N   
1565 C CA  . SER   B 60  ? 0.1986 0.1949 0.1620 0.0225  -0.0147 0.0283  66  SER   C CA  
1566 C C   . SER   B 60  ? 0.2056 0.1996 0.1557 0.0287  -0.0127 0.0303  66  SER   C C   
1567 O O   . SER   B 60  ? 0.2273 0.2180 0.1660 0.0311  -0.0176 0.0270  66  SER   C O   
1568 C CB  . SER   B 60  ? 0.2253 0.2264 0.1966 0.0209  -0.0169 0.0309  66  SER   C CB  
1569 O OG  . SER   B 60  ? 0.2871 0.2880 0.2509 0.0231  -0.0227 0.0299  66  SER   C OG  
1570 N N   . SER   B 61  ? 0.1926 0.1880 0.1448 0.0315  -0.0056 0.0354  67  SER   C N   
1571 C CA  . SER   B 61  ? 0.2061 0.1993 0.1463 0.0384  -0.0017 0.0389  67  SER   C CA  
1572 C C   . SER   B 61  ? 0.2258 0.2132 0.1551 0.0410  -0.0004 0.0356  67  SER   C C   
1573 O O   . SER   B 61  ? 0.2530 0.2377 0.1700 0.0477  0.0030  0.0382  67  SER   C O   
1574 C CB  . SER   B 61  ? 0.2139 0.2103 0.1631 0.0405  0.0064  0.0461  67  SER   C CB  
1575 O OG  . SER   B 61  ? 0.2294 0.2258 0.1890 0.0381  0.0109  0.0458  67  SER   C OG  
1576 N N   . ARG   B 62  ? 0.2074 0.1926 0.1398 0.0368  -0.0029 0.0302  68  ARG   C N   
1577 C CA  . ARG   B 62  ? 0.2181 0.1974 0.1401 0.0390  -0.0029 0.0263  68  ARG   C CA  
1578 C C   . ARG   B 62  ? 0.2281 0.2041 0.1470 0.0358  -0.0109 0.0191  68  ARG   C C   
1579 O O   . ARG   B 62  ? 0.2486 0.2193 0.1606 0.0369  -0.0116 0.0149  68  ARG   C O   
1580 C CB  . ARG   B 62  ? 0.2212 0.2002 0.1514 0.0376  0.0031  0.0273  68  ARG   C CB  
1581 C CG  . ARG   B 62  ? 0.2687 0.2503 0.2048 0.0407  0.0113  0.0339  68  ARG   C CG  
1582 C CD  . ARG   B 62  ? 0.2689 0.2465 0.1909 0.0482  0.0159  0.0363  68  ARG   C CD  
1583 N NE  . ARG   B 62  ? 0.2958 0.2757 0.2252 0.0517  0.0251  0.0438  68  ARG   C NE  
1584 C CZ  . ARG   B 62  ? 0.3098 0.2928 0.2412 0.0547  0.0285  0.0500  68  ARG   C CZ  
1585 N NH1 . ARG   B 62  ? 0.3153 0.2990 0.2385 0.0557  0.0235  0.0498  68  ARG   C NH1 
1586 N NH2 . ARG   B 62  ? 0.3634 0.3479 0.3034 0.0582  0.0376  0.0572  68  ARG   C NH2 
1587 N N   . ARG   B 63  ? 0.2334 0.2128 0.1606 0.0314  -0.0163 0.0179  69  ARG   C N   
1588 C CA  . ARG   B 63  ? 0.2455 0.2226 0.1757 0.0273  -0.0232 0.0120  69  ARG   C CA  
1589 C C   . ARG   B 63  ? 0.2538 0.2277 0.1882 0.0246  -0.0209 0.0094  69  ARG   C C   
1590 O O   . ARG   B 63  ? 0.2829 0.2518 0.2134 0.0243  -0.0244 0.0043  69  ARG   C O   
1591 C CB  . ARG   B 63  ? 0.2659 0.2388 0.1834 0.0308  -0.0303 0.0071  69  ARG   C CB  
1592 C CG  . ARG   B 63  ? 0.3162 0.2924 0.2294 0.0338  -0.0340 0.0093  69  ARG   C CG  
1593 C CD  . ARG   B 63  ? 0.3707 0.3518 0.2985 0.0283  -0.0384 0.0096  69  ARG   C CD  
1594 N NE  . ARG   B 63  ? 0.3825 0.3655 0.3057 0.0311  -0.0453 0.0091  69  ARG   C NE  
1595 C CZ  . ARG   B 63  ? 0.3989 0.3867 0.3223 0.0333  -0.0435 0.0148  69  ARG   C CZ  
1596 N NH1 . ARG   B 63  ? 0.4020 0.3913 0.3209 0.0361  -0.0506 0.0141  69  ARG   C NH1 
1597 N NH2 . ARG   B 63  ? 0.4013 0.3921 0.3298 0.0332  -0.0348 0.0211  69  ARG   C NH2 
1598 N N   . LYS   B 64  ? 0.2234 0.2000 0.1659 0.0232  -0.0149 0.0130  70  LYS   C N   
1599 C CA  . LYS   B 64  ? 0.2225 0.1963 0.1679 0.0217  -0.0123 0.0113  70  LYS   C CA  
1600 C C   . LYS   B 64  ? 0.2016 0.1792 0.1592 0.0183  -0.0100 0.0136  70  LYS   C C   
1601 O O   . LYS   B 64  ? 0.2090 0.1912 0.1720 0.0182  -0.0081 0.0171  70  LYS   C O   
1602 C CB  . LYS   B 64  ? 0.2748 0.2462 0.2131 0.0262  -0.0067 0.0129  70  LYS   C CB  
1603 C CG  . LYS   B 64  ? 0.4012 0.3663 0.3256 0.0301  -0.0083 0.0092  70  LYS   C CG  
1604 C CD  . LYS   B 64  ? 0.5099 0.4722 0.4295 0.0341  -0.0017 0.0107  70  LYS   C CD  
1605 C CE  . LYS   B 64  ? 0.5773 0.5329 0.4812 0.0392  -0.0029 0.0070  70  LYS   C CE  
1606 N NZ  . LYS   B 64  ? 0.6320 0.5877 0.5249 0.0434  -0.0055 0.0076  70  LYS   C NZ  
1607 N N   . HIS   B 65  ? 0.1822 0.1573 0.1431 0.0162  -0.0100 0.0115  71  HIS   C N   
1608 C CA  . HIS   B 65  ? 0.1812 0.1588 0.1506 0.0145  -0.0076 0.0131  71  HIS   C CA  
1609 C C   . HIS   B 65  ? 0.2136 0.1897 0.1816 0.0168  -0.0037 0.0135  71  HIS   C C   
1610 O O   . HIS   B 65  ? 0.2632 0.2347 0.2259 0.0180  -0.0033 0.0113  71  HIS   C O   
1611 C CB  . HIS   B 65  ? 0.1858 0.1616 0.1598 0.0117  -0.0094 0.0116  71  HIS   C CB  
1612 C CG  . HIS   B 65  ? 0.1741 0.1518 0.1530 0.0092  -0.0128 0.0117  71  HIS   C CG  
1613 N ND1 . HIS   B 65  ? 0.2054 0.1870 0.1921 0.0077  -0.0120 0.0142  71  HIS   C ND1 
1614 C CD2 . HIS   B 65  ? 0.1741 0.1504 0.1517 0.0083  -0.0174 0.0094  71  HIS   C CD2 
1615 C CE1 . HIS   B 65  ? 0.1821 0.1646 0.1729 0.0056  -0.0154 0.0139  71  HIS   C CE1 
1616 N NE2 . HIS   B 65  ? 0.2145 0.1940 0.2008 0.0058  -0.0192 0.0108  71  HIS   C NE2 
1617 N N   . TYR   B 66  ? 0.1748 0.1546 0.1489 0.0174  -0.0011 0.0159  72  TYR   C N   
1618 C CA  . TYR   B 66  ? 0.1682 0.1474 0.1437 0.0196  0.0021  0.0164  72  TYR   C CA  
1619 C C   . TYR   B 66  ? 0.1587 0.1390 0.1405 0.0190  0.0017  0.0159  72  TYR   C C   
1620 O O   . TYR   B 66  ? 0.1488 0.1325 0.1361 0.0179  0.0006  0.0165  72  TYR   C O   
1621 C CB  . TYR   B 66  ? 0.1725 0.1551 0.1523 0.0217  0.0052  0.0196  72  TYR   C CB  
1622 C CG  . TYR   B 66  ? 0.1914 0.1725 0.1632 0.0243  0.0069  0.0211  72  TYR   C CG  
1623 C CD1 . TYR   B 66  ? 0.2219 0.1992 0.1870 0.0275  0.0100  0.0210  72  TYR   C CD1 
1624 C CD2 . TYR   B 66  ? 0.2048 0.1883 0.1754 0.0244  0.0060  0.0231  72  TYR   C CD2 
1625 C CE1 . TYR   B 66  ? 0.2306 0.2060 0.1862 0.0313  0.0121  0.0226  72  TYR   C CE1 
1626 C CE2 . TYR   B 66  ? 0.2103 0.1922 0.1717 0.0280  0.0077  0.0248  72  TYR   C CE2 
1627 C CZ  . TYR   B 66  ? 0.2135 0.1912 0.1668 0.0317  0.0108  0.0245  72  TYR   C CZ  
1628 O OH  . TYR   B 66  ? 0.2559 0.2316 0.1981 0.0365  0.0127  0.0265  72  TYR   C OH  
1629 N N   . PRO   B 67  ? 0.1607 0.1384 0.1414 0.0202  0.0027  0.0148  73  PRO   C N   
1630 C CA  . PRO   B 67  ? 0.1622 0.1411 0.1479 0.0209  0.0021  0.0144  73  PRO   C CA  
1631 C C   . PRO   B 67  ? 0.1616 0.1445 0.1556 0.0224  0.0028  0.0153  73  PRO   C C   
1632 O O   . PRO   B 67  ? 0.1903 0.1732 0.1859 0.0239  0.0055  0.0166  73  PRO   C O   
1633 C CB  . PRO   B 67  ? 0.1916 0.1662 0.1736 0.0222  0.0031  0.0134  73  PRO   C CB  
1634 C CG  . PRO   B 67  ? 0.2226 0.1944 0.1997 0.0228  0.0050  0.0132  73  PRO   C CG  
1635 C CD  . PRO   B 67  ? 0.1819 0.1548 0.1562 0.0216  0.0043  0.0137  73  PRO   C CD  
1636 N N   . VAL   B 68  ? 0.1419 0.1276 0.1416 0.0226  0.0006  0.0146  74  VAL   C N   
1637 C CA  . VAL   B 68  ? 0.1536 0.1432 0.1641 0.0237  0.0002  0.0148  74  VAL   C CA  
1638 C C   . VAL   B 68  ? 0.1482 0.1387 0.1624 0.0254  -0.0034 0.0122  74  VAL   C C   
1639 O O   . VAL   B 68  ? 0.1546 0.1439 0.1630 0.0257  -0.0053 0.0109  74  VAL   C O   
1640 C CB  . VAL   B 68  ? 0.1830 0.1757 0.1987 0.0223  0.0006  0.0163  74  VAL   C CB  
1641 C CG1 . VAL   B 68  ? 0.2053 0.1977 0.2184 0.0222  0.0043  0.0194  74  VAL   C CG1 
1642 C CG2 . VAL   B 68  ? 0.1861 0.1790 0.1980 0.0207  -0.0017 0.0154  74  VAL   C CG2 
1643 N N   . SER   B 69  ? 0.1464 0.1393 0.1713 0.0269  -0.0045 0.0113  75  SER   C N   
1644 C CA  . SER   B 69  ? 0.1454 0.1403 0.1767 0.0288  -0.0095 0.0079  75  SER   C CA  
1645 C C   . SER   B 69  ? 0.1331 0.1312 0.1741 0.0277  -0.0106 0.0074  75  SER   C C   
1646 O O   . SER   B 69  ? 0.1417 0.1416 0.1900 0.0261  -0.0070 0.0104  75  SER   C O   
1647 C CB  . SER   B 69  ? 0.1679 0.1640 0.2088 0.0311  -0.0110 0.0068  75  SER   C CB  
1648 O OG  . SER   B 69  ? 0.2443 0.2373 0.2765 0.0323  -0.0097 0.0075  75  SER   C OG  
1649 N N   . PHE   B 70  ? 0.1344 0.1329 0.1751 0.0287  -0.0147 0.0042  76  PHE   C N   
1650 C CA  . PHE   B 70  ? 0.1308 0.1318 0.1809 0.0276  -0.0157 0.0034  76  PHE   C CA  
1651 C C   . PHE   B 70  ? 0.1284 0.1302 0.1851 0.0303  -0.0221 -0.0021 76  PHE   C C   
1652 O O   . PHE   B 70  ? 0.1435 0.1434 0.1922 0.0336  -0.0259 -0.0053 76  PHE   C O   
1653 C CB  . PHE   B 70  ? 0.1361 0.1364 0.1777 0.0256  -0.0134 0.0056  76  PHE   C CB  
1654 C CG  . PHE   B 70  ? 0.1318 0.1292 0.1598 0.0270  -0.0145 0.0043  76  PHE   C CG  
1655 C CD1 . PHE   B 70  ? 0.1406 0.1353 0.1581 0.0265  -0.0119 0.0066  76  PHE   C CD1 
1656 C CD2 . PHE   B 70  ? 0.1447 0.1418 0.1712 0.0293  -0.0177 0.0011  76  PHE   C CD2 
1657 C CE1 . PHE   B 70  ? 0.1363 0.1283 0.1436 0.0281  -0.0119 0.0065  76  PHE   C CE1 
1658 C CE2 . PHE   B 70  ? 0.1457 0.1399 0.1597 0.0315  -0.0173 0.0011  76  PHE   C CE2 
1659 C CZ  . PHE   B 70  ? 0.1477 0.1396 0.1532 0.0309  -0.0142 0.0042  76  PHE   C CZ  
1660 N N   . SER   B 71  ? 0.1282 0.1325 0.1995 0.0295  -0.0235 -0.0034 77  SER   C N   
1661 C CA  . SER   B 71  ? 0.1452 0.1502 0.2258 0.0322  -0.0306 -0.0097 77  SER   C CA  
1662 C C   . SER   B 71  ? 0.1554 0.1582 0.2251 0.0344  -0.0338 -0.0134 77  SER   C C   
1663 O O   . SER   B 71  ? 0.1774 0.1788 0.2350 0.0333  -0.0299 -0.0104 77  SER   C O   
1664 C CB  . SER   B 71  ? 0.1553 0.1635 0.2587 0.0304  -0.0307 -0.0097 77  SER   C CB  
1665 O OG  . SER   B 71  ? 0.1777 0.1867 0.2833 0.0278  -0.0265 -0.0064 77  SER   C OG  
1666 N N   . LYS   B 72  ? 0.1953 0.1977 0.2695 0.0379  -0.0411 -0.0202 78  LYS   C N   
1667 C CA  . LYS   B 72  ? 0.1991 0.1989 0.2625 0.0413  -0.0442 -0.0243 78  LYS   C CA  
1668 C C   . LYS   B 72  ? 0.1902 0.1911 0.2632 0.0386  -0.0424 -0.0240 78  LYS   C C   
1669 O O   . LYS   B 72  ? 0.1979 0.2015 0.2899 0.0358  -0.0422 -0.0235 78  LYS   C O   
1670 C CB  . LYS   B 72  ? 0.2556 0.2542 0.3207 0.0469  -0.0539 -0.0328 78  LYS   C CB  
1671 C CG  . LYS   B 72  ? 0.3081 0.3057 0.3645 0.0502  -0.0563 -0.0331 78  LYS   C CG  
1672 C CD  . LYS   B 72  ? 0.4577 0.4518 0.4998 0.0582  -0.0640 -0.0400 78  LYS   C CD  
1673 C CE  . LYS   B 72  ? 0.5427 0.5347 0.5678 0.0621  -0.0629 -0.0373 78  LYS   C CE  
1674 N NZ  . LYS   B 72  ? 0.5981 0.5863 0.6063 0.0708  -0.0689 -0.0426 78  LYS   C NZ  
1675 N N   . PRO   B 73  ? 0.1799 0.1786 0.2413 0.0398  -0.0407 -0.0239 79  PRO   C N   
1676 C CA  . PRO   B 73  ? 0.1815 0.1814 0.2524 0.0372  -0.0385 -0.0231 79  PRO   C CA  
1677 C C   . PRO   B 73  ? 0.1806 0.1810 0.2690 0.0384  -0.0448 -0.0297 79  PRO   C C   
1678 O O   . PRO   B 73  ? 0.2272 0.2253 0.3126 0.0433  -0.0522 -0.0373 79  PRO   C O   
1679 C CB  . PRO   B 73  ? 0.2081 0.2050 0.2627 0.0399  -0.0367 -0.0230 79  PRO   C CB  
1680 C CG  . PRO   B 73  ? 0.2469 0.2418 0.2842 0.0419  -0.0347 -0.0204 79  PRO   C CG  
1681 C CD  . PRO   B 73  ? 0.2076 0.2028 0.2480 0.0436  -0.0395 -0.0235 79  PRO   C CD  
1682 N N   . SER   B 74  ? 0.1716 0.1750 0.2792 0.0342  -0.0421 -0.0268 80  SER   C N   
1683 C CA  . SER   B 74  ? 0.1822 0.1865 0.3117 0.0345  -0.0476 -0.0325 80  SER   C CA  
1684 C C   . SER   B 74  ? 0.1775 0.1837 0.3231 0.0308  -0.0426 -0.0283 80  SER   C C   
1685 O O   . SER   B 74  ? 0.1741 0.1814 0.3133 0.0282  -0.0353 -0.0208 80  SER   C O   
1686 C CB  . SER   B 74  ? 0.1996 0.2062 0.3438 0.0338  -0.0498 -0.0327 80  SER   C CB  
1687 O OG  . SER   B 74  ? 0.3135 0.3189 0.4433 0.0369  -0.0533 -0.0349 80  SER   C OG  
1688 N N   . LEU   B 75  ? 0.1839 0.1906 0.3518 0.0309  -0.0471 -0.0333 81  LEU   C N   
1689 C CA  . LEU   B 75  ? 0.1914 0.1997 0.3788 0.0278  -0.0427 -0.0295 81  LEU   C CA  
1690 C C   . LEU   B 75  ? 0.2015 0.2135 0.4078 0.0249  -0.0381 -0.0232 81  LEU   C C   
1691 O O   . LEU   B 75  ? 0.2325 0.2455 0.4554 0.0256  -0.0431 -0.0274 81  LEU   C O   
1692 C CB  . LEU   B 75  ? 0.2119 0.2182 0.4152 0.0298  -0.0502 -0.0388 81  LEU   C CB  
1693 C CG  . LEU   B 75  ? 0.2446 0.2519 0.4695 0.0271  -0.0461 -0.0358 81  LEU   C CG  
1694 C CD1 . LEU   B 75  ? 0.2523 0.2590 0.4624 0.0264  -0.0397 -0.0305 81  LEU   C CD1 
1695 C CD2 . LEU   B 75  ? 0.2742 0.2790 0.5182 0.0292  -0.0551 -0.0467 81  LEU   C CD2 
1696 N N   . ILE   B 76  ? 0.2090 0.2230 0.4129 0.0224  -0.0289 -0.0132 82  ILE   C N   
1697 C CA  . ILE   B 76  ? 0.2266 0.2436 0.4433 0.0207  -0.0228 -0.0058 82  ILE   C CA  
1698 C C   . ILE   B 76  ? 0.2134 0.2321 0.4449 0.0189  -0.0151 0.0020  82  ILE   C C   
1699 O O   . ILE   B 76  ? 0.1965 0.2147 0.4174 0.0184  -0.0119 0.0051  82  ILE   C O   
1700 C CB  . ILE   B 76  ? 0.2631 0.2800 0.4561 0.0206  -0.0183 -0.0004 82  ILE   C CB  
1701 C CG1 . ILE   B 76  ? 0.2981 0.3130 0.4748 0.0227  -0.0251 -0.0071 82  ILE   C CG1 
1702 C CG2 . ILE   B 76  ? 0.2914 0.3106 0.4924 0.0197  -0.0106 0.0082  82  ILE   C CG2 
1703 C CD1 . ILE   B 76  ? 0.3176 0.3334 0.5000 0.0236  -0.0269 -0.0080 82  ILE   C CD1 
1704 N N   . PHE   B 77  ? 0.1993 0.2202 0.4561 0.0183  -0.0116 0.0058  83  PHE   C N   
1705 C CA  . PHE   B 77  ? 0.1957 0.2183 0.4660 0.0175  -0.0026 0.0152  83  PHE   C CA  
1706 C C   . PHE   B 77  ? 0.2040 0.2275 0.4551 0.0179  0.0059  0.0250  83  PHE   C C   
1707 O O   . PHE   B 77  ? 0.2302 0.2540 0.4747 0.0186  0.0074  0.0266  83  PHE   C O   
1708 C CB  . PHE   B 77  ? 0.1946 0.2191 0.4992 0.0172  -0.0006 0.0170  83  PHE   C CB  
1709 C CG  . PHE   B 77  ? 0.2054 0.2310 0.5264 0.0169  0.0081  0.0258  83  PHE   C CG  
1710 C CD1 . PHE   B 77  ? 0.2157 0.2402 0.5440 0.0162  0.0059  0.0228  83  PHE   C CD1 
1711 C CD2 . PHE   B 77  ? 0.2389 0.2664 0.5650 0.0180  0.0193  0.0378  83  PHE   C CD2 
1712 C CE1 . PHE   B 77  ? 0.2372 0.2627 0.5806 0.0162  0.0143  0.0317  83  PHE   C CE1 
1713 C CE2 . PHE   B 77  ? 0.2466 0.2749 0.5858 0.0186  0.0279  0.0469  83  PHE   C CE2 
1714 C CZ  . PHE   B 77  ? 0.2392 0.2667 0.5882 0.0175  0.0252  0.0438  83  PHE   C CZ  
1715 N N   . VAL   B 78  ? 0.1682 0.1918 0.4094 0.0178  0.0108  0.0308  84  VAL   C N   
1716 C CA  . VAL   B 78  ? 0.1733 0.1974 0.3954 0.0188  0.0175  0.0390  84  VAL   C CA  
1717 C C   . VAL   B 78  ? 0.1623 0.1879 0.3984 0.0202  0.0269  0.0494  84  VAL   C C   
1718 O O   . VAL   B 78  ? 0.1649 0.1910 0.4127 0.0197  0.0276  0.0504  84  VAL   C O   
1719 C CB  . VAL   B 78  ? 0.1880 0.2108 0.3857 0.0181  0.0145  0.0369  84  VAL   C CB  
1720 C CG1 . VAL   B 78  ? 0.1917 0.2148 0.3703 0.0193  0.0199  0.0442  84  VAL   C CG1 
1721 C CG2 . VAL   B 78  ? 0.2079 0.2287 0.3930 0.0176  0.0062  0.0273  84  VAL   C CG2 
1722 N N   . GLU   B 79  ? 0.1640 0.1903 0.3969 0.0225  0.0345  0.0575  85  GLU   C N   
1723 C CA  . GLU   B 79  ? 0.1725 0.1999 0.4153 0.0251  0.0445  0.0686  85  GLU   C CA  
1724 C C   . GLU   B 79  ? 0.1725 0.1999 0.3979 0.0260  0.0460  0.0727  85  GLU   C C   
1725 O O   . GLU   B 79  ? 0.1616 0.1882 0.3653 0.0247  0.0403  0.0679  85  GLU   C O   
1726 C CB  . GLU   B 79  ? 0.2090 0.2364 0.4491 0.0286  0.0527  0.0765  85  GLU   C CB  
1727 C CG  . GLU   B 79  ? 0.2634 0.2915 0.5266 0.0283  0.0535  0.0750  85  GLU   C CG  
1728 C CD  . GLU   B 79  ? 0.3161 0.3458 0.6149 0.0273  0.0550  0.0760  85  GLU   C CD  
1729 O OE1 . GLU   B 79  ? 0.3512 0.3815 0.6596 0.0288  0.0618  0.0837  85  GLU   C OE1 
1730 O OE2 . GLU   B 79  ? 0.3807 0.4109 0.6985 0.0251  0.0489  0.0686  85  GLU   C OE2 
1731 N N   . ALA   B 80  ? 0.1761 0.2045 0.4117 0.0285  0.0538  0.0821  86  ALA   C N   
1732 C CA  . ALA   B 80  ? 0.1942 0.2230 0.4155 0.0298  0.0552  0.0866  86  ALA   C CA  
1733 C C   . ALA   B 80  ? 0.1999 0.2279 0.3906 0.0320  0.0548  0.0882  86  ALA   C C   
1734 O O   . ALA   B 80  ? 0.2280 0.2549 0.4114 0.0344  0.0583  0.0907  86  ALA   C O   
1735 C CB  . ALA   B 80  ? 0.2104 0.2403 0.4480 0.0335  0.0652  0.0981  86  ALA   C CB  
1736 N N   . SER   B 81  ? 0.1916 0.2196 0.3660 0.0309  0.0498  0.0857  87  SER   C N   
1737 C CA  . SER   B 81  ? 0.2098 0.2371 0.3576 0.0327  0.0482  0.0865  87  SER   C CA  
1738 C C   . SER   B 81  ? 0.2171 0.2458 0.3586 0.0354  0.0504  0.0932  87  SER   C C   
1739 O O   . SER   B 81  ? 0.2245 0.2547 0.3830 0.0357  0.0537  0.0974  87  SER   C O   
1740 C CB  . SER   B 81  ? 0.1877 0.2140 0.3229 0.0285  0.0392  0.0765  87  SER   C CB  
1741 O OG  . SER   B 81  ? 0.1759 0.2034 0.3147 0.0260  0.0350  0.0736  87  SER   C OG  
1742 N N   . GLU   B 82  ? 0.2352 0.2634 0.3534 0.0373  0.0477  0.0937  88  GLU   C N   
1743 C CA  . GLU   B 82  ? 0.2597 0.2895 0.3721 0.0401  0.0485  0.0996  88  GLU   C CA  
1744 C C   . GLU   B 82  ? 0.2403 0.2720 0.3603 0.0358  0.0431  0.0953  88  GLU   C C   
1745 O O   . GLU   B 82  ? 0.2580 0.2915 0.3804 0.0377  0.0446  0.1007  88  GLU   C O   
1746 C CB  . GLU   B 82  ? 0.3369 0.3657 0.4238 0.0440  0.0463  0.1011  88  GLU   C CB  
1747 C CG  . GLU   B 82  ? 0.4448 0.4731 0.5179 0.0400  0.0369  0.0924  88  GLU   C CG  
1748 C CD  . GLU   B 82  ? 0.5396 0.5670 0.5900 0.0440  0.0337  0.0936  88  GLU   C CD  
1749 O OE1 . GLU   B 82  ? 0.5574 0.5828 0.5977 0.0499  0.0385  0.0986  88  GLU   C OE1 
1750 O OE2 . GLU   B 82  ? 0.5581 0.5864 0.6012 0.0416  0.0263  0.0894  88  GLU   C OE2 
1751 N N   . TYR   B 83  ? 0.1965 0.2276 0.3215 0.0307  0.0376  0.0864  89  TYR   C N   
1752 C CA  . TYR   B 83  ? 0.1860 0.2182 0.3153 0.0273  0.0328  0.0820  89  TYR   C CA  
1753 C C   . TYR   B 83  ? 0.1989 0.2305 0.3484 0.0244  0.0324  0.0771  89  TYR   C C   
1754 O O   . TYR   B 83  ? 0.2010 0.2332 0.3556 0.0227  0.0299  0.0746  89  TYR   C O   
1755 C CB  . TYR   B 83  ? 0.1862 0.2177 0.2982 0.0249  0.0258  0.0756  89  TYR   C CB  
1756 C CG  . TYR   B 83  ? 0.1781 0.2071 0.2832 0.0234  0.0236  0.0696  89  TYR   C CG  
1757 C CD1 . TYR   B 83  ? 0.1803 0.2080 0.2720 0.0257  0.0246  0.0714  89  TYR   C CD1 
1758 C CD2 . TYR   B 83  ? 0.1736 0.2013 0.2853 0.0203  0.0205  0.0623  89  TYR   C CD2 
1759 C CE1 . TYR   B 83  ? 0.1815 0.2069 0.2672 0.0244  0.0228  0.0662  89  TYR   C CE1 
1760 C CE2 . TYR   B 83  ? 0.1750 0.2006 0.2806 0.0194  0.0185  0.0574  89  TYR   C CE2 
1761 C CZ  . TYR   B 83  ? 0.1740 0.1985 0.2670 0.0212  0.0197  0.0594  89  TYR   C CZ  
1762 O OH  . TYR   B 83  ? 0.1856 0.2080 0.2738 0.0206  0.0184  0.0552  89  TYR   C OH  
1763 N N   . TYR   B 84  ? 0.1711 0.2015 0.3333 0.0243  0.0347  0.0757  90  TYR   C N   
1764 C CA  . TYR   B 84  ? 0.1679 0.1977 0.3516 0.0222  0.0337  0.0710  90  TYR   C CA  
1765 C C   . TYR   B 84  ? 0.1647 0.1946 0.3681 0.0240  0.0401  0.0762  90  TYR   C C   
1766 O O   . TYR   B 84  ? 0.1760 0.2058 0.3740 0.0260  0.0438  0.0801  90  TYR   C O   
1767 C CB  . TYR   B 84  ? 0.1466 0.1743 0.3268 0.0196  0.0269  0.0604  90  TYR   C CB  
1768 C CG  . TYR   B 84  ? 0.1364 0.1634 0.3030 0.0179  0.0212  0.0546  90  TYR   C CG  
1769 C CD1 . TYR   B 84  ? 0.1400 0.1674 0.3127 0.0174  0.0204  0.0539  90  TYR   C CD1 
1770 C CD2 . TYR   B 84  ? 0.1461 0.1720 0.2950 0.0170  0.0173  0.0504  90  TYR   C CD2 
1771 C CE1 . TYR   B 84  ? 0.1549 0.1816 0.3162 0.0164  0.0163  0.0493  90  TYR   C CE1 
1772 C CE2 . TYR   B 84  ? 0.1435 0.1688 0.2817 0.0159  0.0133  0.0460  90  TYR   C CE2 
1773 C CZ  . TYR   B 84  ? 0.1427 0.1684 0.2873 0.0157  0.0129  0.0455  90  TYR   C CZ  
1774 O OH  . TYR   B 84  ? 0.1484 0.1733 0.2832 0.0150  0.0099  0.0419  90  TYR   C OH  
1775 N N   . PRO   B 85  ? 0.1617 0.1916 0.3893 0.0232  0.0414  0.0756  91  PRO   C N   
1776 C CA  . PRO   B 85  ? 0.1652 0.1951 0.4156 0.0243  0.0468  0.0792  91  PRO   C CA  
1777 C C   . PRO   B 85  ? 0.1644 0.1930 0.4170 0.0223  0.0414  0.0705  91  PRO   C C   
1778 O O   . PRO   B 85  ? 0.1560 0.1834 0.3933 0.0204  0.0338  0.0618  91  PRO   C O   
1779 C CB  . PRO   B 85  ? 0.1801 0.2098 0.4554 0.0233  0.0474  0.0786  91  PRO   C CB  
1780 C CG  . PRO   B 85  ? 0.1734 0.2018 0.4395 0.0207  0.0389  0.0687  91  PRO   C CG  
1781 C CD  . PRO   B 85  ? 0.1672 0.1964 0.4034 0.0212  0.0373  0.0701  91  PRO   C CD  
1782 N N   . ALA   B 86  ? 0.1534 0.1823 0.4270 0.0230  0.0455  0.0730  92  ALA   C N   
1783 C CA  . ALA   B 86  ? 0.1682 0.1962 0.4503 0.0213  0.0400  0.0648  92  ALA   C CA  
1784 C C   . ALA   B 86  ? 0.1894 0.2160 0.4812 0.0186  0.0308  0.0534  92  ALA   C C   
1785 O O   . ALA   B 86  ? 0.2031 0.2294 0.5118 0.0183  0.0318  0.0539  92  ALA   C O   
1786 C CB  . ALA   B 86  ? 0.1732 0.2022 0.4820 0.0225  0.0467  0.0706  92  ALA   C CB  
1787 N N   . ARG   B 87  ? 0.1885 0.2137 0.4659 0.0175  0.0223  0.0436  93  ARG   C N   
1788 C CA  . ARG   B 87  ? 0.1872 0.2103 0.4681 0.0163  0.0136  0.0326  93  ARG   C CA  
1789 C C   . ARG   B 87  ? 0.1864 0.2079 0.4544 0.0163  0.0053  0.0231  93  ARG   C C   
1790 O O   . ARG   B 87  ? 0.1717 0.1939 0.4249 0.0166  0.0066  0.0254  93  ARG   C O   
1791 C CB  . ARG   B 87  ? 0.1866 0.2089 0.4511 0.0163  0.0132  0.0328  93  ARG   C CB  
1792 C CG  . ARG   B 87  ? 0.1822 0.2046 0.4158 0.0164  0.0124  0.0336  93  ARG   C CG  
1793 C CD  . ARG   B 87  ? 0.1825 0.2048 0.4031 0.0164  0.0125  0.0346  93  ARG   C CD  
1794 N NE  . ARG   B 87  ? 0.1718 0.1935 0.3669 0.0162  0.0097  0.0326  93  ARG   C NE  
1795 C CZ  . ARG   B 87  ? 0.1624 0.1828 0.3448 0.0161  0.0065  0.0286  93  ARG   C CZ  
1796 N NH1 . ARG   B 87  ? 0.1834 0.2030 0.3741 0.0164  0.0058  0.0265  93  ARG   C NH1 
1797 N NH2 . ARG   B 87  ? 0.1918 0.2117 0.3542 0.0160  0.0044  0.0270  93  ARG   C NH2 
1798 N N   . TYR   B 88  ? 0.2053 0.2244 0.4752 0.0165  -0.0033 0.0123  94  TYR   C N   
1799 C CA  . TYR   B 88  ? 0.2194 0.2365 0.4730 0.0175  -0.0112 0.0034  94  TYR   C CA  
1800 C C   . TYR   B 88  ? 0.1937 0.2096 0.4186 0.0180  -0.0113 0.0034  94  TYR   C C   
1801 O O   . TYR   B 88  ? 0.2053 0.2205 0.4276 0.0180  -0.0100 0.0041  94  TYR   C O   
1802 C CB  . TYR   B 88  ? 0.2442 0.2587 0.5109 0.0187  -0.0206 -0.0085 94  TYR   C CB  
1803 C CG  . TYR   B 88  ? 0.2630 0.2788 0.5567 0.0183  -0.0230 -0.0105 94  TYR   C CG  
1804 C CD1 . TYR   B 88  ? 0.2744 0.2909 0.5644 0.0190  -0.0265 -0.0130 94  TYR   C CD1 
1805 C CD2 . TYR   B 88  ? 0.2714 0.2880 0.5959 0.0171  -0.0205 -0.0085 94  TYR   C CD2 
1806 C CE1 . TYR   B 88  ? 0.2868 0.3050 0.6039 0.0185  -0.0284 -0.0142 94  TYR   C CE1 
1807 C CE2 . TYR   B 88  ? 0.2735 0.2916 0.6261 0.0166  -0.0220 -0.0095 94  TYR   C CE2 
1808 C CZ  . TYR   B 88  ? 0.2924 0.3115 0.6415 0.0172  -0.0260 -0.0124 94  TYR   C CZ  
1809 O OH  . TYR   B 88  ? 0.3209 0.3419 0.7009 0.0166  -0.0273 -0.0131 94  TYR   C OH  
1810 N N   . GLN   B 89  ? 0.1655 0.1813 0.3704 0.0184  -0.0121 0.0035  95  GLN   C N   
1811 C CA  . GLN   B 89  ? 0.1576 0.1720 0.3372 0.0189  -0.0124 0.0032  95  GLN   C CA  
1812 C C   . GLN   B 89  ? 0.1466 0.1582 0.3149 0.0213  -0.0197 -0.0056 95  GLN   C C   
1813 O O   . GLN   B 89  ? 0.1658 0.1777 0.3374 0.0218  -0.0226 -0.0080 95  GLN   C O   
1814 C CB  . GLN   B 89  ? 0.1681 0.1844 0.3342 0.0177  -0.0066 0.0116  95  GLN   C CB  
1815 C CG  . GLN   B 89  ? 0.1852 0.2003 0.3290 0.0178  -0.0069 0.0117  95  GLN   C CG  
1816 C CD  . GLN   B 89  ? 0.1504 0.1674 0.2840 0.0166  -0.0017 0.0197  95  GLN   C CD  
1817 O OE1 . GLN   B 89  ? 0.1652 0.1843 0.3067 0.0160  0.0030  0.0262  95  GLN   C OE1 
1818 N NE2 . GLN   B 89  ? 0.1503 0.1663 0.2658 0.0165  -0.0026 0.0193  95  GLN   C NE2 
1819 N N   . SER   B 90  ? 0.1438 0.1529 0.2991 0.0232  -0.0223 -0.0099 96  SER   C N   
1820 C CA  . SER   B 90  ? 0.1490 0.1549 0.2914 0.0268  -0.0288 -0.0179 96  SER   C CA  
1821 C C   . SER   B 90  ? 0.1476 0.1528 0.2669 0.0273  -0.0264 -0.0147 96  SER   C C   
1822 O O   . SER   B 90  ? 0.1485 0.1553 0.2610 0.0249  -0.0208 -0.0077 96  SER   C O   
1823 C CB  . SER   B 90  ? 0.1694 0.1719 0.3109 0.0301  -0.0328 -0.0251 96  SER   C CB  
1824 O OG  . SER   B 90  ? 0.1878 0.1900 0.3182 0.0297  -0.0277 -0.0205 96  SER   C OG  
1825 N N   . HIS   B 91  ? 0.1598 0.1626 0.2681 0.0307  -0.0313 -0.0202 97  HIS   C N   
1826 C CA  . HIS   B 91  ? 0.1635 0.1650 0.2509 0.0319  -0.0294 -0.0178 97  HIS   C CA  
1827 C C   . HIS   B 91  ? 0.1494 0.1536 0.2358 0.0280  -0.0244 -0.0103 97  HIS   C C   
1828 O O   . HIS   B 91  ? 0.1621 0.1660 0.2357 0.0270  -0.0206 -0.0059 97  HIS   C O   
1829 C CB  . HIS   B 91  ? 0.1738 0.1732 0.2481 0.0336  -0.0266 -0.0166 97  HIS   C CB  
1830 C CG  . HIS   B 91  ? 0.1960 0.1918 0.2678 0.0387  -0.0313 -0.0244 97  HIS   C CG  
1831 N ND1 . HIS   B 91  ? 0.2245 0.2165 0.2797 0.0445  -0.0341 -0.0286 97  HIS   C ND1 
1832 C CD2 . HIS   B 91  ? 0.2086 0.2037 0.2919 0.0394  -0.0333 -0.0284 97  HIS   C CD2 
1833 C CE1 . HIS   B 91  ? 0.2295 0.2183 0.2846 0.0490  -0.0381 -0.0355 97  HIS   C CE1 
1834 N NE2 . HIS   B 91  ? 0.2314 0.2219 0.3038 0.0459  -0.0379 -0.0359 97  HIS   C NE2 
1835 N N   . LEU   B 92  ? 0.1381 0.1445 0.2383 0.0261  -0.0244 -0.0091 98  LEU   C N   
1836 C CA  . LEU   B 92  ? 0.1373 0.1459 0.2370 0.0232  -0.0193 -0.0023 98  LEU   C CA  
1837 C C   . LEU   B 92  ? 0.1420 0.1500 0.2383 0.0244  -0.0215 -0.0039 98  LEU   C C   
1838 O O   . LEU   B 92  ? 0.1376 0.1453 0.2419 0.0264  -0.0267 -0.0094 98  LEU   C O   
1839 C CB  . LEU   B 92  ? 0.1440 0.1554 0.2630 0.0211  -0.0161 0.0016  98  LEU   C CB  
1840 C CG  . LEU   B 92  ? 0.1552 0.1684 0.2726 0.0192  -0.0100 0.0094  98  LEU   C CG  
1841 C CD1 . LEU   B 92  ? 0.1637 0.1769 0.2663 0.0180  -0.0066 0.0140  98  LEU   C CD1 
1842 C CD2 . LEU   B 92  ? 0.1789 0.1946 0.3165 0.0185  -0.0062 0.0137  98  LEU   C CD2 
1843 N N   . MET   B 93  ? 0.1343 0.1420 0.2191 0.0233  -0.0179 0.0005  99  MET   C N   
1844 C CA  . MET   B 93  ? 0.1264 0.1334 0.2071 0.0243  -0.0188 -0.0001 99  MET   C CA  
1845 C C   . MET   B 93  ? 0.1347 0.1433 0.2198 0.0221  -0.0134 0.0059  99  MET   C C   
1846 O O   . MET   B 93  ? 0.1451 0.1541 0.2244 0.0204  -0.0092 0.0107  99  MET   C O   
1847 C CB  . MET   B 93  ? 0.1522 0.1564 0.2137 0.0255  -0.0188 -0.0002 99  MET   C CB  
1848 C CG  . MET   B 93  ? 0.1887 0.1907 0.2436 0.0289  -0.0229 -0.0053 99  MET   C CG  
1849 S SD  . MET   B 93  ? 0.1934 0.1920 0.2279 0.0306  -0.0209 -0.0036 99  MET   C SD  
1850 C CE  . MET   B 93  ? 0.2005 0.2007 0.2344 0.0261  -0.0150 0.0027  99  MET   C CE  
1851 N N   . LEU   B 94  ? 0.1237 0.1331 0.2170 0.0228  -0.0134 0.0060  100 LEU   C N   
1852 C CA  . LEU   B 94  ? 0.1327 0.1432 0.2291 0.0218  -0.0074 0.0120  100 LEU   C CA  
1853 C C   . LEU   B 94  ? 0.1231 0.1316 0.2083 0.0227  -0.0065 0.0125  100 LEU   C C   
1854 O O   . LEU   B 94  ? 0.1368 0.1443 0.2201 0.0243  -0.0109 0.0081  100 LEU   C O   
1855 C CB  . LEU   B 94  ? 0.1430 0.1561 0.2620 0.0222  -0.0060 0.0132  100 LEU   C CB  
1856 C CG  . LEU   B 94  ? 0.1625 0.1776 0.2974 0.0213  -0.0057 0.0137  100 LEU   C CG  
1857 C CD1 . LEU   B 94  ? 0.2052 0.2227 0.3649 0.0217  -0.0036 0.0157  100 LEU   C CD1 
1858 C CD2 . LEU   B 94  ? 0.1728 0.1881 0.3005 0.0202  -0.0004 0.0196  100 LEU   C CD2 
1859 N N   . ALA   B 95  ? 0.1363 0.1442 0.2150 0.0222  -0.0011 0.0175  101 ALA   C N   
1860 C CA  . ALA   B 95  ? 0.1387 0.1445 0.2093 0.0232  0.0009  0.0186  101 ALA   C CA  
1861 C C   . ALA   B 95  ? 0.1388 0.1452 0.2138 0.0240  0.0077  0.0243  101 ALA   C C   
1862 O O   . ALA   B 95  ? 0.1357 0.1436 0.2152 0.0238  0.0110  0.0282  101 ALA   C O   
1863 C CB  . ALA   B 95  ? 0.1501 0.1528 0.2017 0.0224  0.0005  0.0181  101 ALA   C CB  
1864 N N   . VAL   B 96  ? 0.1371 0.1420 0.2098 0.0256  0.0102  0.0254  102 VAL   C N   
1865 C CA  . VAL   B 96  ? 0.1459 0.1503 0.2187 0.0276  0.0174  0.0310  102 VAL   C CA  
1866 C C   . VAL   B 96  ? 0.1638 0.1648 0.2161 0.0277  0.0188  0.0322  102 VAL   C C   
1867 O O   . VAL   B 96  ? 0.1880 0.1859 0.2276 0.0272  0.0163  0.0291  102 VAL   C O   
1868 C CB  . VAL   B 96  ? 0.1605 0.1644 0.2402 0.0296  0.0195  0.0314  102 VAL   C CB  
1869 C CG1 . VAL   B 96  ? 0.1883 0.1907 0.2653 0.0326  0.0280  0.0376  102 VAL   C CG1 
1870 C CG2 . VAL   B 96  ? 0.1687 0.1763 0.2709 0.0294  0.0166  0.0297  102 VAL   C CG2 
1871 N N   . GLY   B 97  ? 0.1728 0.1744 0.2226 0.0284  0.0222  0.0363  103 GLY   C N   
1872 C CA  . GLY   B 97  ? 0.1988 0.1974 0.2302 0.0289  0.0222  0.0367  103 GLY   C CA  
1873 C C   . GLY   B 97  ? 0.1879 0.1880 0.2182 0.0300  0.0248  0.0412  103 GLY   C C   
1874 O O   . GLY   B 97  ? 0.2128 0.2162 0.2574 0.0302  0.0273  0.0445  103 GLY   C O   
1875 N N   . HIS   B 98  ? 0.1822 0.1798 0.1964 0.0311  0.0241  0.0414  104 HIS   C N   
1876 C CA  . HIS   B 98  ? 0.1843 0.1829 0.1944 0.0332  0.0262  0.0458  104 HIS   C CA  
1877 C C   . HIS   B 98  ? 0.1728 0.1741 0.1853 0.0298  0.0213  0.0444  104 HIS   C C   
1878 O O   . HIS   B 98  ? 0.1743 0.1747 0.1816 0.0266  0.0157  0.0396  104 HIS   C O   
1879 C CB  . HIS   B 98  ? 0.2309 0.2253 0.2220 0.0369  0.0269  0.0461  104 HIS   C CB  
1880 C CG  . HIS   B 98  ? 0.2548 0.2501 0.2406 0.0407  0.0296  0.0513  104 HIS   C CG  
1881 N ND1 . HIS   B 98  ? 0.2689 0.2657 0.2626 0.0448  0.0376  0.0586  104 HIS   C ND1 
1882 C CD2 . HIS   B 98  ? 0.2821 0.2773 0.2573 0.0409  0.0252  0.0506  104 HIS   C CD2 
1883 C CE1 . HIS   B 98  ? 0.2976 0.2949 0.2834 0.0478  0.0380  0.0623  104 HIS   C CE1 
1884 N NE2 . HIS   B 98  ? 0.3066 0.3029 0.2806 0.0457  0.0302  0.0574  104 HIS   C NE2 
1885 N N   . SER   B 99  ? 0.1834 0.1877 0.2037 0.0308  0.0239  0.0491  105 SER   C N   
1886 C CA  . SER   B 99  ? 0.1819 0.1888 0.2050 0.0281  0.0201  0.0485  105 SER   C CA  
1887 C C   . SER   B 99  ? 0.2047 0.2138 0.2310 0.0313  0.0245  0.0555  105 SER   C C   
1888 O O   . SER   B 99  ? 0.2384 0.2491 0.2782 0.0329  0.0300  0.0598  105 SER   C O   
1889 C CB  . SER   B 99  ? 0.1932 0.2023 0.2312 0.0247  0.0180  0.0454  105 SER   C CB  
1890 O OG  . SER   B 99  ? 0.1881 0.1995 0.2298 0.0228  0.0155  0.0456  105 SER   C OG  
1891 N N   . GLU   B 100 ? 0.2076 0.2166 0.2229 0.0324  0.0221  0.0565  106 GLU   C N   
1892 C CA  . GLU   B 100 ? 0.2191 0.2301 0.2352 0.0357  0.0252  0.0630  106 GLU   C CA  
1893 C C   . GLU   B 100 ? 0.1970 0.2110 0.2191 0.0321  0.0205  0.0615  106 GLU   C C   
1894 O O   . GLU   B 100 ? 0.1843 0.1982 0.2064 0.0279  0.0152  0.0558  106 GLU   C O   
1895 C CB  . GLU   B 100 ? 0.2695 0.2779 0.2654 0.0403  0.0239  0.0641  106 GLU   C CB  
1896 C CG  . GLU   B 100 ? 0.3642 0.3692 0.3526 0.0452  0.0296  0.0663  106 GLU   C CG  
1897 C CD  . GLU   B 100 ? 0.4289 0.4303 0.3956 0.0512  0.0288  0.0671  106 GLU   C CD  
1898 O OE1 . GLU   B 100 ? 0.5309 0.5335 0.4904 0.0536  0.0261  0.0692  106 GLU   C OE1 
1899 O OE2 . GLU   B 100 ? 0.4170 0.4144 0.3740 0.0540  0.0307  0.0655  106 GLU   C OE2 
1900 N N   . PRO   B 101 ? 0.2048 0.2215 0.2323 0.0340  0.0230  0.0672  107 PRO   C N   
1901 C CA  . PRO   B 101 ? 0.1887 0.2083 0.2238 0.0306  0.0192  0.0660  107 PRO   C CA  
1902 C C   . PRO   B 101 ? 0.1928 0.2120 0.2169 0.0283  0.0117  0.0612  107 PRO   C C   
1903 O O   . PRO   B 101 ? 0.1876 0.2079 0.2184 0.0242  0.0085  0.0576  107 PRO   C O   
1904 C CB  . PRO   B 101 ? 0.2148 0.2367 0.2537 0.0346  0.0235  0.0740  107 PRO   C CB  
1905 C CG  . PRO   B 101 ? 0.2624 0.2829 0.3034 0.0389  0.0311  0.0793  107 PRO   C CG  
1906 C CD  . PRO   B 101 ? 0.2372 0.2543 0.2673 0.0396  0.0307  0.0756  107 PRO   C CD  
1907 N N   . GLY   B 102 ? 0.2001 0.2173 0.2085 0.0311  0.0091  0.0610  108 GLY   C N   
1908 C CA  . GLY   B 102 ? 0.2026 0.2195 0.2034 0.0289  0.0016  0.0564  108 GLY   C CA  
1909 C C   . GLY   B 102 ? 0.1848 0.1995 0.1866 0.0244  -0.0012 0.0499  108 GLY   C C   
1910 O O   . GLY   B 102 ? 0.2016 0.2162 0.2016 0.0217  -0.0067 0.0461  108 GLY   C O   
1911 N N   . ASP   B 103 ? 0.1754 0.1882 0.1796 0.0241  0.0025  0.0485  109 ASP   C N   
1912 C CA  . ASP   B 103 ? 0.1610 0.1716 0.1656 0.0207  0.0003  0.0430  109 ASP   C CA  
1913 C C   . ASP   B 103 ? 0.1512 0.1638 0.1671 0.0170  -0.0006 0.0412  109 ASP   C C   
1914 O O   . ASP   B 103 ? 0.1487 0.1597 0.1644 0.0147  -0.0025 0.0372  109 ASP   C O   
1915 C CB  . ASP   B 103 ? 0.1808 0.1889 0.1843 0.0222  0.0041  0.0424  109 ASP   C CB  
1916 C CG  . ASP   B 103 ? 0.1950 0.1999 0.1849 0.0260  0.0048  0.0430  109 ASP   C CG  
1917 O OD1 . ASP   B 103 ? 0.2027 0.2058 0.1827 0.0261  0.0000  0.0404  109 ASP   C OD1 
1918 O OD2 . ASP   B 103 ? 0.2117 0.2156 0.2014 0.0294  0.0102  0.0461  109 ASP   C OD2 
1919 N N   . CYS   B 104 ? 0.1409 0.1567 0.1671 0.0171  0.0014  0.0443  110 CYS   C N   
1920 C CA  . CYS   B 104 ? 0.1319 0.1490 0.1676 0.0145  0.0006  0.0422  110 CYS   C CA  
1921 C C   . CYS   B 104 ? 0.1355 0.1524 0.1679 0.0122  -0.0032 0.0398  110 CYS   C C   
1922 O O   . CYS   B 104 ? 0.1559 0.1737 0.1842 0.0123  -0.0058 0.0412  110 CYS   C O   
1923 C CB  . CYS   B 104 ? 0.1364 0.1566 0.1829 0.0151  0.0029  0.0459  110 CYS   C CB  
1924 S SG  . CYS   B 104 ? 0.1626 0.1831 0.2204 0.0171  0.0081  0.0482  110 CYS   C SG  
1925 N N   . GLY   B 105 ? 0.1193 0.1349 0.1540 0.0107  -0.0036 0.0364  111 GLY   C N   
1926 C CA  . GLY   B 105 ? 0.1336 0.1487 0.1673 0.0088  -0.0058 0.0349  111 GLY   C CA  
1927 C C   . GLY   B 105 ? 0.1313 0.1430 0.1576 0.0081  -0.0072 0.0320  111 GLY   C C   
1928 O O   . GLY   B 105 ? 0.1454 0.1561 0.1724 0.0067  -0.0080 0.0309  111 GLY   C O   
1929 N N   . GLY   B 106 ? 0.1405 0.1502 0.1606 0.0093  -0.0069 0.0313  112 GLY   C N   
1930 C CA  . GLY   B 106 ? 0.1473 0.1532 0.1608 0.0088  -0.0079 0.0284  112 GLY   C CA  
1931 C C   . GLY   B 106 ? 0.1271 0.1315 0.1425 0.0087  -0.0064 0.0264  112 GLY   C C   
1932 O O   . GLY   B 106 ? 0.1302 0.1355 0.1495 0.0099  -0.0048 0.0261  112 GLY   C O   
1933 N N   . ILE   B 107 ? 0.1301 0.1320 0.1432 0.0078  -0.0071 0.0250  113 ILE   C N   
1934 C CA  . ILE   B 107 ? 0.1261 0.1262 0.1394 0.0087  -0.0054 0.0238  113 ILE   C CA  
1935 C C   . ILE   B 107 ? 0.1234 0.1209 0.1320 0.0103  -0.0048 0.0218  113 ILE   C C   
1936 O O   . ILE   B 107 ? 0.1294 0.1250 0.1337 0.0100  -0.0053 0.0212  113 ILE   C O   
1937 C CB  . ILE   B 107 ? 0.1553 0.1536 0.1695 0.0075  -0.0052 0.0244  113 ILE   C CB  
1938 C CG1 . ILE   B 107 ? 0.2072 0.2085 0.2284 0.0069  -0.0045 0.0267  113 ILE   C CG1 
1939 C CG2 . ILE   B 107 ? 0.1537 0.1486 0.1647 0.0093  -0.0030 0.0236  113 ILE   C CG2 
1940 C CD1 . ILE   B 107 ? 0.2566 0.2573 0.2832 0.0054  -0.0038 0.0285  113 ILE   C CD1 
1941 N N   . LEU   B 108 ? 0.1156 0.1131 0.1254 0.0124  -0.0040 0.0206  114 LEU   C N   
1942 C CA  . LEU   B 108 ? 0.1149 0.1100 0.1211 0.0144  -0.0039 0.0186  114 LEU   C CA  
1943 C C   . LEU   B 108 ? 0.1228 0.1154 0.1254 0.0159  -0.0029 0.0185  114 LEU   C C   
1944 O O   . LEU   B 108 ? 0.1266 0.1198 0.1304 0.0172  -0.0023 0.0188  114 LEU   C O   
1945 C CB  . LEU   B 108 ? 0.1242 0.1212 0.1351 0.0163  -0.0047 0.0169  114 LEU   C CB  
1946 C CG  . LEU   B 108 ? 0.1312 0.1264 0.1402 0.0190  -0.0057 0.0143  114 LEU   C CG  
1947 C CD1 . LEU   B 108 ? 0.1456 0.1395 0.1526 0.0186  -0.0049 0.0147  114 LEU   C CD1 
1948 C CD2 . LEU   B 108 ? 0.1436 0.1409 0.1600 0.0207  -0.0077 0.0119  114 LEU   C CD2 
1949 N N   . ARG   B 109 ? 0.1259 0.1152 0.1240 0.0162  -0.0023 0.0184  115 ARG   C N   
1950 C CA  . ARG   B 109 ? 0.1309 0.1174 0.1259 0.0182  -0.0003 0.0195  115 ARG   C CA  
1951 C C   . ARG   B 109 ? 0.1359 0.1197 0.1257 0.0211  -0.0003 0.0182  115 ARG   C C   
1952 O O   . ARG   B 109 ? 0.1522 0.1355 0.1415 0.0204  -0.0013 0.0170  115 ARG   C O   
1953 C CB  . ARG   B 109 ? 0.1665 0.1514 0.1637 0.0154  0.0010  0.0216  115 ARG   C CB  
1954 C CG  . ARG   B 109 ? 0.1984 0.1811 0.1941 0.0135  -0.0002 0.0204  115 ARG   C CG  
1955 C CD  . ARG   B 109 ? 0.2380 0.2188 0.2379 0.0107  -0.0002 0.0214  115 ARG   C CD  
1956 N NE  . ARG   B 109 ? 0.2810 0.2650 0.2852 0.0081  -0.0026 0.0215  115 ARG   C NE  
1957 C CZ  . ARG   B 109 ? 0.3549 0.3398 0.3662 0.0062  -0.0026 0.0232  115 ARG   C CZ  
1958 N NH1 . ARG   B 109 ? 0.3827 0.3655 0.3982 0.0067  0.0006  0.0256  115 ARG   C NH1 
1959 N NH2 . ARG   B 109 ? 0.3916 0.3796 0.4066 0.0042  -0.0056 0.0232  115 ARG   C NH2 
1960 N N   . CYS   B 110 ? 0.1432 0.1250 0.1287 0.0251  0.0012  0.0189  116 CYS   C N   
1961 C CA  . CYS   B 110 ? 0.1683 0.1473 0.1481 0.0288  0.0013  0.0183  116 CYS   C CA  
1962 C C   . CYS   B 110 ? 0.1877 0.1631 0.1649 0.0303  0.0056  0.0221  116 CYS   C C   
1963 O O   . CYS   B 110 ? 0.1808 0.1561 0.1623 0.0279  0.0081  0.0247  116 CYS   C O   
1964 C CB  . CYS   B 110 ? 0.1692 0.1490 0.1455 0.0337  -0.0014 0.0155  116 CYS   C CB  
1965 S SG  . CYS   B 110 ? 0.1704 0.1493 0.1417 0.0381  0.0007  0.0167  116 CYS   C SG  
1966 N N   . GLN   B 111 ? 0.1963 0.1687 0.1674 0.0347  0.0068  0.0229  117 GLN   C N   
1967 C CA  . GLN   B 111 ? 0.2152 0.1838 0.1846 0.0369  0.0119  0.0274  117 GLN   C CA  
1968 C C   . GLN   B 111 ? 0.2185 0.1870 0.1862 0.0400  0.0154  0.0304  117 GLN   C C   
1969 O O   . GLN   B 111 ? 0.2545 0.2205 0.2248 0.0405  0.0209  0.0353  117 GLN   C O   
1970 C CB  . GLN   B 111 ? 0.2359 0.2013 0.1981 0.0421  0.0128  0.0283  117 GLN   C CB  
1971 C CG  . GLN   B 111 ? 0.2438 0.2095 0.1967 0.0491  0.0105  0.0266  117 GLN   C CG  
1972 C CD  . GLN   B 111 ? 0.4047 0.3675 0.3503 0.0547  0.0106  0.0275  117 GLN   C CD  
1973 O OE1 . GLN   B 111 ? 0.4577 0.4217 0.4037 0.0547  0.0062  0.0241  117 GLN   C OE1 
1974 N NE2 . GLN   B 111 ? 0.4093 0.3685 0.3491 0.0598  0.0159  0.0325  117 GLN   C NE2 
1975 N N   . HIS   B 112 ? 0.1979 0.1689 0.1627 0.0421  0.0128  0.0277  118 HIS   C N   
1976 C CA  . HIS   B 112 ? 0.2120 0.1823 0.1740 0.0460  0.0166  0.0303  118 HIS   C CA  
1977 C C   . HIS   B 112 ? 0.2159 0.1891 0.1874 0.0410  0.0177  0.0315  118 HIS   C C   
1978 O O   . HIS   B 112 ? 0.2240 0.1967 0.1949 0.0438  0.0216  0.0343  118 HIS   C O   
1979 C CB  . HIS   B 112 ? 0.2229 0.1933 0.1754 0.0522  0.0130  0.0262  118 HIS   C CB  
1980 C CG  . HIS   B 112 ? 0.2038 0.1718 0.1469 0.0578  0.0107  0.0246  118 HIS   C CG  
1981 N ND1 . HIS   B 112 ? 0.2037 0.1736 0.1480 0.0569  0.0041  0.0194  118 HIS   C ND1 
1982 C CD2 . HIS   B 112 ? 0.2408 0.2048 0.1737 0.0651  0.0144  0.0281  118 HIS   C CD2 
1983 C CE1 . HIS   B 112 ? 0.2175 0.1849 0.1531 0.0629  0.0034  0.0195  118 HIS   C CE1 
1984 N NE2 . HIS   B 112 ? 0.2599 0.2235 0.1877 0.0681  0.0094  0.0247  118 HIS   C NE2 
1985 N N   . GLY   B 113 ? 0.1912 0.1674 0.1707 0.0343  0.0141  0.0292  119 GLY   C N   
1986 C CA  . GLY   B 113 ? 0.1888 0.1680 0.1770 0.0300  0.0141  0.0301  119 GLY   C CA  
1987 C C   . GLY   B 113 ? 0.1660 0.1489 0.1570 0.0267  0.0090  0.0261  119 GLY   C C   
1988 O O   . GLY   B 113 ? 0.1616 0.1448 0.1507 0.0260  0.0057  0.0231  119 GLY   C O   
1989 N N   . VAL   B 114 ? 0.1644 0.1502 0.1609 0.0250  0.0090  0.0267  120 VAL   C N   
1990 C CA  . VAL   B 114 ? 0.1596 0.1491 0.1604 0.0220  0.0052  0.0242  120 VAL   C CA  
1991 C C   . VAL   B 114 ? 0.1507 0.1406 0.1481 0.0256  0.0030  0.0206  120 VAL   C C   
1992 O O   . VAL   B 114 ? 0.1640 0.1529 0.1582 0.0297  0.0043  0.0201  120 VAL   C O   
1993 C CB  . VAL   B 114 ? 0.1662 0.1585 0.1749 0.0192  0.0060  0.0265  120 VAL   C CB  
1994 C CG1 . VAL   B 114 ? 0.1779 0.1738 0.1906 0.0171  0.0027  0.0247  120 VAL   C CG1 
1995 C CG2 . VAL   B 114 ? 0.1948 0.1870 0.2090 0.0154  0.0066  0.0292  120 VAL   C CG2 
1996 N N   . VAL   B 115 ? 0.1340 0.1250 0.1325 0.0245  -0.0004 0.0177  121 VAL   C N   
1997 C CA  . VAL   B 115 ? 0.1374 0.1292 0.1364 0.0272  -0.0035 0.0136  121 VAL   C CA  
1998 C C   . VAL   B 115 ? 0.1437 0.1387 0.1509 0.0253  -0.0046 0.0130  121 VAL   C C   
1999 O O   . VAL   B 115 ? 0.1462 0.1413 0.1550 0.0280  -0.0064 0.0099  121 VAL   C O   
2000 C CB  . VAL   B 115 ? 0.1440 0.1355 0.1428 0.0271  -0.0060 0.0116  121 VAL   C CB  
2001 C CG1 . VAL   B 115 ? 0.1538 0.1467 0.1573 0.0292  -0.0099 0.0073  121 VAL   C CG1 
2002 C CG2 . VAL   B 115 ? 0.1715 0.1596 0.1621 0.0296  -0.0049 0.0123  121 VAL   C CG2 
2003 N N   . GLY   B 116 ? 0.1348 0.1323 0.1476 0.0210  -0.0040 0.0156  122 GLY   C N   
2004 C CA  . GLY   B 116 ? 0.1516 0.1522 0.1727 0.0194  -0.0045 0.0159  122 GLY   C CA  
2005 C C   . GLY   B 116 ? 0.1240 0.1266 0.1478 0.0157  -0.0039 0.0192  122 GLY   C C   
2006 O O   . GLY   B 116 ? 0.1364 0.1378 0.1557 0.0143  -0.0035 0.0206  122 GLY   C O   
2007 N N   . ILE   B 117 ? 0.1122 0.1178 0.1434 0.0145  -0.0040 0.0204  123 ILE   C N   
2008 C CA  . ILE   B 117 ? 0.1120 0.1195 0.1442 0.0123  -0.0035 0.0237  123 ILE   C CA  
2009 C C   . ILE   B 117 ? 0.1148 0.1238 0.1522 0.0127  -0.0030 0.0245  123 ILE   C C   
2010 O O   . ILE   B 117 ? 0.1252 0.1350 0.1703 0.0138  -0.0031 0.0230  123 ILE   C O   
2011 C CB  . ILE   B 117 ? 0.1258 0.1356 0.1617 0.0110  -0.0032 0.0265  123 ILE   C CB  
2012 C CG1 . ILE   B 117 ? 0.1444 0.1556 0.1879 0.0121  -0.0025 0.0260  123 ILE   C CG1 
2013 C CG2 . ILE   B 117 ? 0.1502 0.1588 0.1826 0.0101  -0.0031 0.0271  123 ILE   C CG2 
2014 C CD1 . ILE   B 117 ? 0.1450 0.1591 0.1937 0.0110  -0.0018 0.0295  123 ILE   C CD1 
2015 N N   . VAL   B 118 ? 0.1091 0.1185 0.1434 0.0122  -0.0023 0.0269  124 VAL   C N   
2016 C CA  . VAL   B 118 ? 0.1133 0.1240 0.1527 0.0132  -0.0003 0.0292  124 VAL   C CA  
2017 C C   . VAL   B 118 ? 0.1156 0.1292 0.1650 0.0133  0.0008  0.0316  124 VAL   C C   
2018 O O   . VAL   B 118 ? 0.1128 0.1278 0.1616 0.0125  0.0003  0.0335  124 VAL   C O   
2019 C CB  . VAL   B 118 ? 0.1208 0.1309 0.1524 0.0137  0.0006  0.0320  124 VAL   C CB  
2020 C CG1 . VAL   B 118 ? 0.1303 0.1417 0.1667 0.0158  0.0042  0.0359  124 VAL   C CG1 
2021 C CG2 . VAL   B 118 ? 0.1330 0.1397 0.1557 0.0138  -0.0003 0.0294  124 VAL   C CG2 
2022 N N   . SER   B 119 ? 0.1151 0.1296 0.1751 0.0143  0.0023  0.0316  125 SER   C N   
2023 C CA  . SER   B 119 ? 0.1196 0.1364 0.1917 0.0145  0.0038  0.0338  125 SER   C CA  
2024 C C   . SER   B 119 ? 0.1242 0.1423 0.2062 0.0159  0.0077  0.0379  125 SER   C C   
2025 O O   . SER   B 119 ? 0.1289 0.1490 0.2189 0.0164  0.0101  0.0420  125 SER   C O   
2026 C CB  . SER   B 119 ? 0.1258 0.1420 0.2047 0.0144  0.0013  0.0288  125 SER   C CB  
2027 O OG  . SER   B 119 ? 0.1401 0.1580 0.2324 0.0147  0.0026  0.0301  125 SER   C OG  
2028 N N   . THR   B 120 ? 0.1289 0.1459 0.2123 0.0168  0.0088  0.0372  126 THR   C N   
2029 C CA  . THR   B 120 ? 0.1235 0.1417 0.2189 0.0185  0.0136  0.0418  126 THR   C CA  
2030 C C   . THR   B 120 ? 0.1202 0.1370 0.2065 0.0204  0.0166  0.0444  126 THR   C C   
2031 O O   . THR   B 120 ? 0.1268 0.1415 0.2003 0.0198  0.0139  0.0410  126 THR   C O   
2032 C CB  . THR   B 120 ? 0.1317 0.1504 0.2455 0.0183  0.0124  0.0382  126 THR   C CB  
2033 O OG1 . THR   B 120 ? 0.1337 0.1509 0.2444 0.0183  0.0096  0.0335  126 THR   C OG1 
2034 C CG2 . THR   B 120 ? 0.1482 0.1674 0.2702 0.0171  0.0089  0.0342  126 THR   C CG2 
2035 N N   . GLY   B 121 ? 0.1315 0.1492 0.2248 0.0229  0.0225  0.0505  127 GLY   C N   
2036 C CA  . GLY   B 121 ? 0.1698 0.1858 0.2551 0.0256  0.0265  0.0535  127 GLY   C CA  
2037 C C   . GLY   B 121 ? 0.1914 0.2085 0.2910 0.0286  0.0340  0.0602  127 GLY   C C   
2038 O O   . GLY   B 121 ? 0.2372 0.2563 0.3491 0.0291  0.0369  0.0644  127 GLY   C O   
2039 N N   . GLY   B 122 ? 0.2373 0.2528 0.3328 0.0314  0.0383  0.0628  128 GLY   C N   
2040 C CA  . GLY   B 122 ? 0.2554 0.2717 0.3653 0.0350  0.0470  0.0703  128 GLY   C CA  
2041 C C   . GLY   B 122 ? 0.2461 0.2623 0.3684 0.0348  0.0480  0.0682  128 GLY   C C   
2042 O O   . GLY   B 122 ? 0.2525 0.2688 0.3781 0.0315  0.0412  0.0608  128 GLY   C O   
2043 N N   . ASN   B 123 ? 0.2355 0.2517 0.3668 0.0388  0.0568  0.0754  129 ASN   C N   
2044 C CA  . ASN   B 123 ? 0.2516 0.2680 0.3972 0.0393  0.0591  0.0750  129 ASN   C CA  
2045 C C   . ASN   B 123 ? 0.2310 0.2451 0.3615 0.0381  0.0536  0.0682  129 ASN   C C   
2046 O O   . ASN   B 123 ? 0.2624 0.2773 0.4057 0.0366  0.0511  0.0644  129 ASN   C O   
2047 C CB  . ASN   B 123 ? 0.3112 0.3309 0.4876 0.0363  0.0567  0.0726  129 ASN   C CB  
2048 C CG  . ASN   B 123 ? 0.4260 0.4477 0.6273 0.0390  0.0663  0.0817  129 ASN   C CG  
2049 O OD1 . ASN   B 123 ? 0.4563 0.4768 0.6531 0.0441  0.0764  0.0907  129 ASN   C OD1 
2050 N ND2 . ASN   B 123 ? 0.4443 0.4687 0.6729 0.0362  0.0636  0.0796  129 ASN   C ND2 
2051 N N   . GLY   B 124 ? 0.2142 0.2253 0.3186 0.0388  0.0516  0.0666  130 GLY   C N   
2052 C CA  . GLY   B 124 ? 0.2049 0.2132 0.2951 0.0378  0.0469  0.0604  130 GLY   C CA  
2053 C C   . GLY   B 124 ? 0.1716 0.1806 0.2627 0.0330  0.0374  0.0520  130 GLY   C C   
2054 O O   . GLY   B 124 ? 0.1820 0.1891 0.2663 0.0323  0.0340  0.0475  130 GLY   C O   
2055 N N   . LEU   B 125 ? 0.1533 0.1648 0.2527 0.0303  0.0335  0.0503  131 LEU   C N   
2056 C CA  . LEU   B 125 ? 0.1539 0.1655 0.2524 0.0268  0.0250  0.0427  131 LEU   C CA  
2057 C C   . LEU   B 125 ? 0.1569 0.1682 0.2420 0.0251  0.0219  0.0415  131 LEU   C C   
2058 O O   . LEU   B 125 ? 0.1915 0.2036 0.2758 0.0260  0.0251  0.0462  131 LEU   C O   
2059 C CB  . LEU   B 125 ? 0.1833 0.1978 0.3045 0.0254  0.0221  0.0400  131 LEU   C CB  
2060 C CG  . LEU   B 125 ? 0.2190 0.2349 0.3589 0.0268  0.0244  0.0410  131 LEU   C CG  
2061 C CD1 . LEU   B 125 ? 0.2740 0.2929 0.4411 0.0261  0.0241  0.0412  131 LEU   C CD1 
2062 C CD2 . LEU   B 125 ? 0.2201 0.2344 0.3534 0.0267  0.0198  0.0357  131 LEU   C CD2 
2063 N N   . VAL   B 126 ? 0.1278 0.1377 0.2034 0.0232  0.0161  0.0359  132 VAL   C N   
2064 C CA  . VAL   B 126 ? 0.1299 0.1396 0.1959 0.0213  0.0127  0.0343  132 VAL   C CA  
2065 C C   . VAL   B 126 ? 0.1106 0.1212 0.1843 0.0197  0.0075  0.0290  132 VAL   C C   
2066 O O   . VAL   B 126 ? 0.1272 0.1369 0.2022 0.0199  0.0043  0.0247  132 VAL   C O   
2067 C CB  . VAL   B 126 ? 0.1330 0.1397 0.1802 0.0209  0.0110  0.0328  132 VAL   C CB  
2068 C CG1 . VAL   B 126 ? 0.1564 0.1607 0.1994 0.0210  0.0090  0.0290  132 VAL   C CG1 
2069 C CG2 . VAL   B 126 ? 0.1486 0.1555 0.1892 0.0189  0.0075  0.0314  132 VAL   C CG2 
2070 N N   . GLY   B 127 ? 0.1193 0.1314 0.1967 0.0187  0.0066  0.0293  133 GLY   C N   
2071 C CA  . GLY   B 127 ? 0.1182 0.1306 0.2008 0.0179  0.0018  0.0241  133 GLY   C CA  
2072 C C   . GLY   B 127 ? 0.1170 0.1282 0.1869 0.0169  -0.0003 0.0228  133 GLY   C C   
2073 O O   . GLY   B 127 ? 0.1191 0.1311 0.1845 0.0161  0.0017  0.0266  133 GLY   C O   
2074 N N   . PHE   B 128 ? 0.1160 0.1257 0.1821 0.0174  -0.0041 0.0178  134 PHE   C N   
2075 C CA  . PHE   B 128 ? 0.1174 0.1258 0.1730 0.0170  -0.0053 0.0168  134 PHE   C CA  
2076 C C   . PHE   B 128 ? 0.1139 0.1222 0.1742 0.0182  -0.0078 0.0132  134 PHE   C C   
2077 O O   . PHE   B 128 ? 0.1231 0.1306 0.1882 0.0201  -0.0109 0.0086  134 PHE   C O   
2078 C CB  . PHE   B 128 ? 0.1239 0.1294 0.1674 0.0177  -0.0066 0.0149  134 PHE   C CB  
2079 C CG  . PHE   B 128 ? 0.1279 0.1325 0.1666 0.0171  -0.0046 0.0172  134 PHE   C CG  
2080 C CD1 . PHE   B 128 ? 0.1260 0.1302 0.1573 0.0156  -0.0030 0.0202  134 PHE   C CD1 
2081 C CD2 . PHE   B 128 ? 0.1322 0.1364 0.1741 0.0184  -0.0049 0.0159  134 PHE   C CD2 
2082 C CE1 . PHE   B 128 ? 0.1363 0.1389 0.1620 0.0157  -0.0016 0.0214  134 PHE   C CE1 
2083 C CE2 . PHE   B 128 ? 0.1417 0.1446 0.1786 0.0184  -0.0026 0.0179  134 PHE   C CE2 
2084 C CZ  . PHE   B 128 ? 0.1370 0.1388 0.1649 0.0172  -0.0010 0.0204  134 PHE   C CZ  
2085 N N   . ALA   B 129 ? 0.1200 0.1289 0.1789 0.0174  -0.0067 0.0149  135 ALA   C N   
2086 C CA  . ALA   B 129 ? 0.1253 0.1333 0.1861 0.0191  -0.0084 0.0115  135 ALA   C CA  
2087 C C   . ALA   B 129 ? 0.1298 0.1348 0.1777 0.0214  -0.0094 0.0090  135 ALA   C C   
2088 O O   . ALA   B 129 ? 0.1354 0.1399 0.1754 0.0204  -0.0073 0.0121  135 ALA   C O   
2089 C CB  . ALA   B 129 ? 0.1256 0.1355 0.1899 0.0176  -0.0060 0.0151  135 ALA   C CB  
2090 N N   . ASP   B 130 ? 0.1286 0.1314 0.1752 0.0248  -0.0129 0.0036  136 ASP   C N   
2091 C CA  . ASP   B 130 ? 0.1409 0.1404 0.1743 0.0283  -0.0134 0.0018  136 ASP   C CA  
2092 C C   . ASP   B 130 ? 0.1485 0.1469 0.1772 0.0298  -0.0108 0.0030  136 ASP   C C   
2093 O O   . ASP   B 130 ? 0.1572 0.1564 0.1929 0.0299  -0.0109 0.0020  136 ASP   C O   
2094 C CB  . ASP   B 130 ? 0.1606 0.1581 0.1935 0.0328  -0.0185 -0.0048 136 ASP   C CB  
2095 C CG  . ASP   B 130 ? 0.1882 0.1820 0.2061 0.0378  -0.0192 -0.0066 136 ASP   C CG  
2096 O OD1 . ASP   B 130 ? 0.1962 0.1892 0.2067 0.0371  -0.0167 -0.0031 136 ASP   C OD1 
2097 O OD2 . ASP   B 130 ? 0.2422 0.2334 0.2553 0.0428  -0.0217 -0.0111 136 ASP   C OD2 
2098 N N   . VAL   B 131 ? 0.1567 0.1530 0.1749 0.0312  -0.0081 0.0054  137 VAL   C N   
2099 C CA  . VAL   B 131 ? 0.1587 0.1534 0.1721 0.0338  -0.0048 0.0070  137 VAL   C CA  
2100 C C   . VAL   B 131 ? 0.1674 0.1578 0.1676 0.0401  -0.0042 0.0052  137 VAL   C C   
2101 O O   . VAL   B 131 ? 0.1833 0.1717 0.1782 0.0435  -0.0004 0.0071  137 VAL   C O   
2102 C CB  . VAL   B 131 ? 0.1670 0.1636 0.1828 0.0299  -0.0004 0.0133  137 VAL   C CB  
2103 C CG1 . VAL   B 131 ? 0.1604 0.1612 0.1875 0.0250  -0.0010 0.0151  137 VAL   C CG1 
2104 C CG2 . VAL   B 131 ? 0.1766 0.1723 0.1875 0.0284  0.0010  0.0161  137 VAL   C CG2 
2105 N N   . ARG   B 132 ? 0.1669 0.1557 0.1616 0.0425  -0.0075 0.0022  138 ARG   C N   
2106 C CA  . ARG   B 132 ? 0.1775 0.1621 0.1583 0.0491  -0.0066 0.0016  138 ARG   C CA  
2107 C C   . ARG   B 132 ? 0.1912 0.1726 0.1645 0.0564  -0.0085 -0.0032 138 ARG   C C   
2108 O O   . ARG   B 132 ? 0.2130 0.1904 0.1728 0.0630  -0.0058 -0.0021 138 ARG   C O   
2109 C CB  . ARG   B 132 ? 0.1788 0.1628 0.1564 0.0499  -0.0102 -0.0003 138 ARG   C CB  
2110 C CG  . ARG   B 132 ? 0.1699 0.1556 0.1515 0.0440  -0.0075 0.0046  138 ARG   C CG  
2111 C CD  . ARG   B 132 ? 0.1693 0.1543 0.1485 0.0453  -0.0111 0.0023  138 ARG   C CD  
2112 N NE  . ARG   B 132 ? 0.1643 0.1518 0.1530 0.0439  -0.0166 -0.0026 138 ARG   C NE  
2113 C CZ  . ARG   B 132 ? 0.1704 0.1585 0.1619 0.0440  -0.0202 -0.0048 138 ARG   C CZ  
2114 N NH1 . ARG   B 132 ? 0.1856 0.1717 0.1690 0.0463  -0.0195 -0.0034 138 ARG   C NH1 
2115 N NH2 . ARG   B 132 ? 0.1750 0.1659 0.1789 0.0420  -0.0241 -0.0081 138 ARG   C NH2 
2116 N N   . ASP   B 133 ? 0.1895 0.1719 0.1707 0.0560  -0.0129 -0.0084 139 ASP   C N   
2117 C CA  . ASP   B 133 ? 0.2071 0.1859 0.1814 0.0632  -0.0154 -0.0142 139 ASP   C CA  
2118 C C   . ASP   B 133 ? 0.2204 0.1983 0.1938 0.0642  -0.0092 -0.0107 139 ASP   C C   
2119 O O   . ASP   B 133 ? 0.2419 0.2160 0.2072 0.0711  -0.0100 -0.0150 139 ASP   C O   
2120 C CB  . ASP   B 133 ? 0.2284 0.2084 0.2143 0.0622  -0.0231 -0.0219 139 ASP   C CB  
2121 C CG  . ASP   B 133 ? 0.2396 0.2237 0.2429 0.0550  -0.0215 -0.0196 139 ASP   C CG  
2122 O OD1 . ASP   B 133 ? 0.2228 0.2103 0.2317 0.0489  -0.0172 -0.0130 139 ASP   C OD1 
2123 O OD2 . ASP   B 133 ? 0.2708 0.2544 0.2821 0.0559  -0.0247 -0.0247 139 ASP   C OD2 
2124 N N   . LEU   B 134 ? 0.1994 0.1807 0.1809 0.0580  -0.0035 -0.0036 140 LEU   C N   
2125 C CA  . LEU   B 134 ? 0.2034 0.1846 0.1870 0.0583  0.0023  0.0002  140 LEU   C CA  
2126 C C   . LEU   B 134 ? 0.2096 0.1878 0.1818 0.0630  0.0093  0.0057  140 LEU   C C   
2127 O O   . LEU   B 134 ? 0.2113 0.1915 0.1882 0.0590  0.0145  0.0127  140 LEU   C O   
2128 C CB  . LEU   B 134 ? 0.2022 0.1888 0.2013 0.0496  0.0039  0.0050  140 LEU   C CB  
2129 C CG  . LEU   B 134 ? 0.1949 0.1847 0.2067 0.0451  -0.0015 0.0012  140 LEU   C CG  
2130 C CD1 . LEU   B 134 ? 0.2018 0.1966 0.2254 0.0377  0.0005  0.0071  140 LEU   C CD1 
2131 C CD2 . LEU   B 134 ? 0.2161 0.2039 0.2310 0.0488  -0.0043 -0.0049 140 LEU   C CD2 
2132 N N   . LEU   B 135 ? 0.2305 0.2034 0.1873 0.0724  0.0094  0.0024  141 LEU   C N   
2133 C CA  . LEU   B 135 ? 0.2447 0.2140 0.1890 0.0784  0.0166  0.0081  141 LEU   C CA  
2134 C C   . LEU   B 135 ? 0.2489 0.2185 0.1975 0.0784  0.0256  0.0153  141 LEU   C C   
2135 O O   . LEU   B 135 ? 0.2644 0.2332 0.2115 0.0794  0.0329  0.0227  141 LEU   C O   
2136 C CB  . LEU   B 135 ? 0.2569 0.2201 0.1815 0.0899  0.0147  0.0032  141 LEU   C CB  
2137 C CG  . LEU   B 135 ? 0.2847 0.2475 0.2056 0.0909  0.0045  -0.0048 141 LEU   C CG  
2138 C CD1 . LEU   B 135 ? 0.3255 0.2820 0.2254 0.1034  0.0017  -0.0101 141 LEU   C CD1 
2139 C CD2 . LEU   B 135 ? 0.2887 0.2548 0.2158 0.0843  0.0031  -0.0018 141 LEU   C CD2 
2140 N N   . TRP   B 136 ? 0.2348 0.2057 0.1910 0.0771  0.0253  0.0133  142 TRP   C N   
2141 C CA  . TRP   B 136 ? 0.2460 0.2176 0.2085 0.0771  0.0335  0.0197  142 TRP   C CA  
2142 C C   . TRP   B 136 ? 0.2583 0.2351 0.2362 0.0682  0.0367  0.0273  142 TRP   C C   
2143 O O   . TRP   B 136 ? 0.2651 0.2428 0.2494 0.0682  0.0441  0.0340  142 TRP   C O   
2144 C CB  . TRP   B 136 ? 0.2424 0.2142 0.2105 0.0775  0.0318  0.0154  142 TRP   C CB  
2145 C CG  . TRP   B 136 ? 0.2374 0.2137 0.2187 0.0696  0.0240  0.0109  142 TRP   C CG  
2146 C CD1 . TRP   B 136 ? 0.2511 0.2264 0.2312 0.0704  0.0158  0.0023  142 TRP   C CD1 
2147 C CD2 . TRP   B 136 ? 0.2270 0.2094 0.2256 0.0605  0.0241  0.0152  142 TRP   C CD2 
2148 N NE1 . TRP   B 136 ? 0.2452 0.2256 0.2414 0.0622  0.0119  0.0019  142 TRP   C NE1 
2149 C CE2 . TRP   B 136 ? 0.2295 0.2141 0.2358 0.0565  0.0168  0.0097  142 TRP   C CE2 
2150 C CE3 . TRP   B 136 ? 0.2311 0.2172 0.2398 0.0559  0.0294  0.0231  142 TRP   C CE3 
2151 C CZ2 . TRP   B 136 ? 0.2194 0.2096 0.2410 0.0487  0.0155  0.0126  142 TRP   C CZ2 
2152 C CZ3 . TRP   B 136 ? 0.2308 0.2225 0.2544 0.0483  0.0268  0.0249  142 TRP   C CZ3 
2153 C CH2 . TRP   B 136 ? 0.2276 0.2211 0.2562 0.0449  0.0202  0.0200  142 TRP   C CH2 
2154 N N   . LEU   B 137 ? 0.2410 0.2215 0.2258 0.0608  0.0311  0.0263  143 LEU   C N   
2155 C CA  . LEU   B 137 ? 0.2414 0.2262 0.2391 0.0532  0.0331  0.0325  143 LEU   C CA  
2156 C C   . LEU   B 137 ? 0.2829 0.2653 0.2778 0.0560  0.0403  0.0391  143 LEU   C C   
2157 O O   . LEU   B 137 ? 0.2995 0.2847 0.3067 0.0513  0.0435  0.0448  143 LEU   C O   
2158 C CB  . LEU   B 137 ? 0.2160 0.2039 0.2183 0.0464  0.0261  0.0298  143 LEU   C CB  
2159 C CG  . LEU   B 137 ? 0.2094 0.2007 0.2197 0.0422  0.0204  0.0256  143 LEU   C CG  
2160 C CD1 . LEU   B 137 ? 0.2209 0.2142 0.2329 0.0374  0.0147  0.0232  143 LEU   C CD1 
2161 C CD2 . LEU   B 137 ? 0.2196 0.2154 0.2437 0.0373  0.0222  0.0299  143 LEU   C CD2 
2162 N N   . ASP   B 138 ? 0.2833 0.2605 0.2626 0.0639  0.0426  0.0384  144 ASP   C N   
2163 C CA  . ASP   B 138 ? 0.3183 0.2925 0.2939 0.0677  0.0502  0.0452  144 ASP   C CA  
2164 C C   . ASP   B 138 ? 0.3520 0.3237 0.3267 0.0741  0.0602  0.0514  144 ASP   C C   
2165 O O   . ASP   B 138 ? 0.3802 0.3492 0.3529 0.0780  0.0679  0.0581  144 ASP   C O   
2166 C CB  . ASP   B 138 ? 0.3329 0.3023 0.2909 0.0744  0.0488  0.0426  144 ASP   C CB  
2167 C CG  . ASP   B 138 ? 0.3182 0.2895 0.2765 0.0692  0.0401  0.0374  144 ASP   C CG  
2168 O OD1 . ASP   B 138 ? 0.3292 0.3050 0.3009 0.0602  0.0366  0.0373  144 ASP   C OD1 
2169 O OD2 . ASP   B 138 ? 0.3745 0.3427 0.3193 0.0747  0.0367  0.0334  144 ASP   C OD2 
2170 N N   . GLU   B 139 ? 0.3471 0.3194 0.3237 0.0758  0.0610  0.0498  145 GLU   C N   
2171 C CA  . GLU   B 139 ? 0.4124 0.3817 0.3867 0.0832  0.0713  0.0555  145 GLU   C CA  
2172 C C   . GLU   B 139 ? 0.4673 0.4407 0.4576 0.0789  0.0730  0.0575  145 GLU   C C   
2173 O O   . GLU   B 139 ? 0.4727 0.4512 0.4746 0.0706  0.0659  0.0542  145 GLU   C O   
2174 C CB  . GLU   B 139 ? 0.4844 0.4471 0.4358 0.0949  0.0715  0.0504  145 GLU   C CB  
2175 C CG  . GLU   B 139 ? 0.5889 0.5523 0.5376 0.0938  0.0620  0.0403  145 GLU   C CG  
2176 C CD  . GLU   B 139 ? 0.7121 0.6694 0.6393 0.1039  0.0579  0.0323  145 GLU   C CD  
2177 O OE1 . GLU   B 139 ? 0.7306 0.6871 0.6567 0.1054  0.0532  0.0251  145 GLU   C OE1 
2178 O OE2 . GLU   B 139 ? 0.7539 0.7071 0.6659 0.1107  0.0591  0.0329  145 GLU   C OE2 
2179 N N   . GLU   B 140 ? 0.5069 0.4779 0.4972 0.0856  0.0831  0.0632  146 GLU   C N   
2180 C CA  . GLU   B 140 ? 0.5407 0.5147 0.5451 0.0839  0.0870  0.0663  146 GLU   C CA  
2181 C C   . GLU   B 140 ? 0.5596 0.5394 0.5877 0.0757  0.0899  0.0741  146 GLU   C C   
2182 O O   . GLU   B 140 ? 0.5692 0.5476 0.6028 0.0789  0.0997  0.0826  146 GLU   C O   
2183 C CB  . GLU   B 140 ? 0.5705 0.5465 0.5757 0.0809  0.0787  0.0581  146 GLU   C CB  
2184 C CG  . GLU   B 140 ? 0.6461 0.6258 0.6673 0.0783  0.0818  0.0613  146 GLU   C CG  
2185 C CD  . GLU   B 140 ? 0.7553 0.7300 0.7677 0.0880  0.0891  0.0613  146 GLU   C CD  
2186 O OE1 . GLU   B 140 ? 0.7781 0.7537 0.7939 0.0872  0.0857  0.0568  146 GLU   C OE1 
2187 O OE2 . GLU   B 140 ? 0.7801 0.7498 0.7822 0.0970  0.0985  0.0661  146 GLU   C OE2 
2188 N N1  . A1B03 C .   ? 0.2599 0.2011 0.3599 0.0353  0.0792  0.0159  201 A1B03 A N1  
2189 C C4  . A1B03 C .   ? 0.3675 0.2627 0.4374 0.0191  0.1120  -0.0201 201 A1B03 A C4  
2190 C C5  . A1B03 C .   ? 0.3441 0.2598 0.4335 0.0295  0.1028  -0.0033 201 A1B03 A C5  
2191 C C6  . A1B03 C .   ? 0.3065 0.2333 0.4173 0.0366  0.0967  0.0115  201 A1B03 A C6  
2192 C C7  . A1B03 C .   ? 0.3538 0.2663 0.4622 0.0342  0.1182  -0.0009 201 A1B03 A C7  
2193 O O2  . A1B03 C .   ? 0.3112 0.2353 0.4504 0.0429  0.1083  0.0202  201 A1B03 A O2  
2194 C C3  . A1B03 C .   ? 0.3907 0.2799 0.4359 0.0089  0.1147  -0.0328 201 A1B03 A C3  
2195 C C2  . A1B03 C .   ? 0.3935 0.2819 0.4535 0.0135  0.1275  -0.0312 201 A1B03 A C2  
2196 N N   . A1B03 C .   ? 0.3798 0.2869 0.4640 0.0261  0.1198  -0.0136 201 A1B03 A N   
2197 S S   . A1B03 C .   ? 0.3855 0.2971 0.4845 0.0309  0.1288  -0.0092 201 A1B03 A S   
2198 O O   . A1B03 C .   ? 0.4022 0.3361 0.5117 0.0380  0.1137  0.0069  201 A1B03 A O   
2199 O O1  . A1B03 C .   ? 0.3982 0.3001 0.4714 0.0203  0.1337  -0.0245 201 A1B03 A O1  
2200 C C1  . A1B03 C .   ? 0.3855 0.2861 0.5221 0.0389  0.1522  -0.0041 201 A1B03 A C1  
2201 C C   . A1B03 C .   ? 0.3899 0.2712 0.5316 0.0356  0.1750  -0.0156 201 A1B03 A C   
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