data_7HUH
# 
_entry.id   7HUH 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   7HUH         pdb_00007huh 10.2210/pdb7huh/pdb 
WWPDB D_1001407946 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-02-26 
_pdbx_audit_revision_history.part_number         ? 
# 
_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_database_status.entry_id                        7HUH 
_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   2025-01-10 
_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 '1-methyl-N-[(3-methyl-1,2-oxazol-5-yl)methyl]-1H-indole-3-carboxamide' 269.299   1   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                              65.409    2   ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                    78.133    1   ?         ? ? ? 
5 water       nat water                                                                   18.015    331 ?         ? ? ? 
# 
_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 '1-methyl-N-[(3-methyl-1,2-oxazol-5-yl)methyl]-1H-indole-3-carboxamide' A1BN1 
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 
A1BN1 non-polymer         . '1-methyl-N-[(3-methyl-1,2-oxazol-5-yl)methyl]-1H-indole-3-carboxamide' ? 'C15 H15 N3 O2'  269.299 
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        A1BN1 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BN1 
_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 A1BN1 1   201 201 A1BN1 LIG A . 
D 3 ZN    1   202 1   ZN    ZN  A . 
E 4 DMS   1   203 1   DMS   DMS A . 
F 3 ZN    1   201 1   ZN    ZN  C . 
G 5 HOH   1   301 246 HOH   HOH A . 
G 5 HOH   2   302 75  HOH   HOH A . 
G 5 HOH   3   303 129 HOH   HOH A . 
G 5 HOH   4   304 306 HOH   HOH A . 
G 5 HOH   5   305 293 HOH   HOH A . 
G 5 HOH   6   306 212 HOH   HOH A . 
G 5 HOH   7   307 123 HOH   HOH A . 
G 5 HOH   8   308 291 HOH   HOH A . 
G 5 HOH   9   309 86  HOH   HOH A . 
G 5 HOH   10  310 25  HOH   HOH A . 
G 5 HOH   11  311 18  HOH   HOH A . 
G 5 HOH   12  312 321 HOH   HOH A . 
G 5 HOH   13  313 201 HOH   HOH A . 
G 5 HOH   14  314 115 HOH   HOH A . 
G 5 HOH   15  315 27  HOH   HOH A . 
G 5 HOH   16  316 34  HOH   HOH A . 
G 5 HOH   17  317 50  HOH   HOH A . 
G 5 HOH   18  318 144 HOH   HOH A . 
G 5 HOH   19  319 47  HOH   HOH A . 
G 5 HOH   20  320 171 HOH   HOH A . 
G 5 HOH   21  321 204 HOH   HOH A . 
G 5 HOH   22  322 31  HOH   HOH A . 
G 5 HOH   23  323 329 HOH   HOH A . 
G 5 HOH   24  324 28  HOH   HOH A . 
G 5 HOH   25  325 136 HOH   HOH A . 
G 5 HOH   26  326 215 HOH   HOH A . 
G 5 HOH   27  327 44  HOH   HOH A . 
G 5 HOH   28  328 126 HOH   HOH A . 
G 5 HOH   29  329 251 HOH   HOH A . 
G 5 HOH   30  330 94  HOH   HOH A . 
G 5 HOH   31  331 57  HOH   HOH A . 
G 5 HOH   32  332 54  HOH   HOH A . 
G 5 HOH   33  333 284 HOH   HOH A . 
G 5 HOH   34  334 22  HOH   HOH A . 
G 5 HOH   35  335 102 HOH   HOH A . 
G 5 HOH   36  336 188 HOH   HOH A . 
G 5 HOH   37  337 250 HOH   HOH A . 
G 5 HOH   38  338 298 HOH   HOH A . 
G 5 HOH   39  339 56  HOH   HOH A . 
G 5 HOH   40  340 87  HOH   HOH A . 
G 5 HOH   41  341 205 HOH   HOH A . 
G 5 HOH   42  342 17  HOH   HOH A . 
G 5 HOH   43  343 259 HOH   HOH A . 
G 5 HOH   44  344 149 HOH   HOH A . 
G 5 HOH   45  345 262 HOH   HOH A . 
G 5 HOH   46  346 160 HOH   HOH A . 
G 5 HOH   47  347 317 HOH   HOH A . 
G 5 HOH   48  348 69  HOH   HOH A . 
G 5 HOH   49  349 314 HOH   HOH A . 
G 5 HOH   50  350 271 HOH   HOH A . 
G 5 HOH   51  351 74  HOH   HOH A . 
G 5 HOH   52  352 5   HOH   HOH A . 
G 5 HOH   53  353 52  HOH   HOH A . 
G 5 HOH   54  354 89  HOH   HOH A . 
G 5 HOH   55  355 185 HOH   HOH A . 
G 5 HOH   56  356 118 HOH   HOH A . 
G 5 HOH   57  357 66  HOH   HOH A . 
G 5 HOH   58  358 202 HOH   HOH A . 
G 5 HOH   59  359 78  HOH   HOH A . 
G 5 HOH   60  360 29  HOH   HOH A . 
G 5 HOH   61  361 19  HOH   HOH A . 
G 5 HOH   62  362 80  HOH   HOH A . 
G 5 HOH   63  363 13  HOH   HOH A . 
G 5 HOH   64  364 315 HOH   HOH A . 
G 5 HOH   65  365 84  HOH   HOH A . 
G 5 HOH   66  366 132 HOH   HOH A . 
G 5 HOH   67  367 248 HOH   HOH A . 
G 5 HOH   68  368 138 HOH   HOH A . 
G 5 HOH   69  369 253 HOH   HOH A . 
G 5 HOH   70  370 113 HOH   HOH A . 
G 5 HOH   71  371 33  HOH   HOH A . 
G 5 HOH   72  372 53  HOH   HOH A . 
G 5 HOH   73  373 273 HOH   HOH A . 
G 5 HOH   74  374 180 HOH   HOH A . 
G 5 HOH   75  375 48  HOH   HOH A . 
G 5 HOH   76  376 41  HOH   HOH A . 
G 5 HOH   77  377 266 HOH   HOH A . 
G 5 HOH   78  378 70  HOH   HOH A . 
G 5 HOH   79  379 165 HOH   HOH A . 
G 5 HOH   80  380 130 HOH   HOH A . 
G 5 HOH   81  381 4   HOH   HOH A . 
G 5 HOH   82  382 286 HOH   HOH A . 
G 5 HOH   83  383 51  HOH   HOH A . 
G 5 HOH   84  384 92  HOH   HOH A . 
G 5 HOH   85  385 178 HOH   HOH A . 
G 5 HOH   86  386 121 HOH   HOH A . 
G 5 HOH   87  387 127 HOH   HOH A . 
G 5 HOH   88  388 209 HOH   HOH A . 
G 5 HOH   89  389 9   HOH   HOH A . 
G 5 HOH   90  390 197 HOH   HOH A . 
G 5 HOH   91  391 220 HOH   HOH A . 
G 5 HOH   92  392 320 HOH   HOH A . 
G 5 HOH   93  393 153 HOH   HOH A . 
G 5 HOH   94  394 186 HOH   HOH A . 
G 5 HOH   95  395 260 HOH   HOH A . 
G 5 HOH   96  396 93  HOH   HOH A . 
G 5 HOH   97  397 117 HOH   HOH A . 
G 5 HOH   98  398 16  HOH   HOH A . 
G 5 HOH   99  399 73  HOH   HOH A . 
G 5 HOH   100 400 106 HOH   HOH A . 
G 5 HOH   101 401 71  HOH   HOH A . 
G 5 HOH   102 402 63  HOH   HOH A . 
G 5 HOH   103 403 257 HOH   HOH A . 
G 5 HOH   104 404 245 HOH   HOH A . 
G 5 HOH   105 405 326 HOH   HOH A . 
G 5 HOH   106 406 258 HOH   HOH A . 
G 5 HOH   107 407 7   HOH   HOH A . 
G 5 HOH   108 408 21  HOH   HOH A . 
G 5 HOH   109 409 131 HOH   HOH A . 
G 5 HOH   110 410 38  HOH   HOH A . 
G 5 HOH   111 411 280 HOH   HOH A . 
G 5 HOH   112 412 309 HOH   HOH A . 
G 5 HOH   113 413 232 HOH   HOH A . 
G 5 HOH   114 414 324 HOH   HOH A . 
G 5 HOH   115 415 146 HOH   HOH A . 
G 5 HOH   116 416 12  HOH   HOH A . 
G 5 HOH   117 417 32  HOH   HOH A . 
G 5 HOH   118 418 99  HOH   HOH A . 
G 5 HOH   119 419 310 HOH   HOH A . 
G 5 HOH   120 420 1   HOH   HOH A . 
G 5 HOH   121 421 112 HOH   HOH A . 
G 5 HOH   122 422 83  HOH   HOH A . 
G 5 HOH   123 423 292 HOH   HOH A . 
G 5 HOH   124 424 249 HOH   HOH A . 
G 5 HOH   125 425 274 HOH   HOH A . 
G 5 HOH   126 426 143 HOH   HOH A . 
G 5 HOH   127 427 311 HOH   HOH A . 
G 5 HOH   128 428 124 HOH   HOH A . 
G 5 HOH   129 429 125 HOH   HOH A . 
G 5 HOH   130 430 190 HOH   HOH A . 
G 5 HOH   131 431 195 HOH   HOH A . 
G 5 HOH   132 432 227 HOH   HOH A . 
G 5 HOH   133 433 263 HOH   HOH A . 
G 5 HOH   134 434 242 HOH   HOH A . 
G 5 HOH   135 435 270 HOH   HOH A . 
G 5 HOH   136 436 269 HOH   HOH A . 
G 5 HOH   137 437 116 HOH   HOH A . 
G 5 HOH   138 438 200 HOH   HOH A . 
G 5 HOH   139 439 231 HOH   HOH A . 
G 5 HOH   140 440 167 HOH   HOH A . 
G 5 HOH   141 441 290 HOH   HOH A . 
G 5 HOH   142 442 264 HOH   HOH A . 
G 5 HOH   143 443 268 HOH   HOH A . 
G 5 HOH   144 444 277 HOH   HOH A . 
G 5 HOH   145 445 331 HOH   HOH A . 
G 5 HOH   146 446 327 HOH   HOH A . 
G 5 HOH   147 447 145 HOH   HOH A . 
G 5 HOH   148 448 225 HOH   HOH A . 
G 5 HOH   149 449 179 HOH   HOH A . 
G 5 HOH   150 450 140 HOH   HOH A . 
G 5 HOH   151 451 97  HOH   HOH A . 
G 5 HOH   152 452 234 HOH   HOH A . 
G 5 HOH   153 453 295 HOH   HOH A . 
G 5 HOH   154 454 148 HOH   HOH A . 
G 5 HOH   155 455 308 HOH   HOH A . 
G 5 HOH   156 456 230 HOH   HOH A . 
G 5 HOH   157 457 170 HOH   HOH A . 
G 5 HOH   158 458 289 HOH   HOH A . 
G 5 HOH   159 459 325 HOH   HOH A . 
G 5 HOH   160 460 287 HOH   HOH A . 
G 5 HOH   161 461 161 HOH   HOH A . 
G 5 HOH   162 462 330 HOH   HOH A . 
G 5 HOH   163 463 233 HOH   HOH A . 
G 5 HOH   164 464 206 HOH   HOH A . 
G 5 HOH   165 465 328 HOH   HOH A . 
G 5 HOH   166 466 224 HOH   HOH A . 
G 5 HOH   167 467 159 HOH   HOH A . 
G 5 HOH   168 468 278 HOH   HOH A . 
G 5 HOH   169 469 203 HOH   HOH A . 
H 5 HOH   1   301 176 HOH   HOH C . 
H 5 HOH   2   302 300 HOH   HOH C . 
H 5 HOH   3   303 294 HOH   HOH C . 
H 5 HOH   4   304 182 HOH   HOH C . 
H 5 HOH   5   305 81  HOH   HOH C . 
H 5 HOH   6   306 95  HOH   HOH C . 
H 5 HOH   7   307 30  HOH   HOH C . 
H 5 HOH   8   308 247 HOH   HOH C . 
H 5 HOH   9   309 276 HOH   HOH C . 
H 5 HOH   10  310 39  HOH   HOH C . 
H 5 HOH   11  311 166 HOH   HOH C . 
H 5 HOH   12  312 151 HOH   HOH C . 
H 5 HOH   13  313 211 HOH   HOH C . 
H 5 HOH   14  314 168 HOH   HOH C . 
H 5 HOH   15  315 42  HOH   HOH C . 
H 5 HOH   16  316 128 HOH   HOH C . 
H 5 HOH   17  317 85  HOH   HOH C . 
H 5 HOH   18  318 222 HOH   HOH C . 
H 5 HOH   19  319 72  HOH   HOH C . 
H 5 HOH   20  320 134 HOH   HOH C . 
H 5 HOH   21  321 307 HOH   HOH C . 
H 5 HOH   22  322 157 HOH   HOH C . 
H 5 HOH   23  323 156 HOH   HOH C . 
H 5 HOH   24  324 261 HOH   HOH C . 
H 5 HOH   25  325 110 HOH   HOH C . 
H 5 HOH   26  326 49  HOH   HOH C . 
H 5 HOH   27  327 82  HOH   HOH C . 
H 5 HOH   28  328 181 HOH   HOH C . 
H 5 HOH   29  329 20  HOH   HOH C . 
H 5 HOH   30  330 58  HOH   HOH C . 
H 5 HOH   31  331 187 HOH   HOH C . 
H 5 HOH   32  332 6   HOH   HOH C . 
H 5 HOH   33  333 59  HOH   HOH C . 
H 5 HOH   34  334 133 HOH   HOH C . 
H 5 HOH   35  335 252 HOH   HOH C . 
H 5 HOH   36  336 11  HOH   HOH C . 
H 5 HOH   37  337 199 HOH   HOH C . 
H 5 HOH   38  338 103 HOH   HOH C . 
H 5 HOH   39  339 100 HOH   HOH C . 
H 5 HOH   40  340 68  HOH   HOH C . 
H 5 HOH   41  341 35  HOH   HOH C . 
H 5 HOH   42  342 105 HOH   HOH C . 
H 5 HOH   43  343 61  HOH   HOH C . 
H 5 HOH   44  344 55  HOH   HOH C . 
H 5 HOH   45  345 88  HOH   HOH C . 
H 5 HOH   46  346 319 HOH   HOH C . 
H 5 HOH   47  347 297 HOH   HOH C . 
H 5 HOH   48  348 275 HOH   HOH C . 
H 5 HOH   49  349 122 HOH   HOH C . 
H 5 HOH   50  350 40  HOH   HOH C . 
H 5 HOH   51  351 10  HOH   HOH C . 
H 5 HOH   52  352 256 HOH   HOH C . 
H 5 HOH   53  353 164 HOH   HOH C . 
H 5 HOH   54  354 3   HOH   HOH C . 
H 5 HOH   55  355 43  HOH   HOH C . 
H 5 HOH   56  356 108 HOH   HOH C . 
H 5 HOH   57  357 26  HOH   HOH C . 
H 5 HOH   58  358 111 HOH   HOH C . 
H 5 HOH   59  359 183 HOH   HOH C . 
H 5 HOH   60  360 316 HOH   HOH C . 
H 5 HOH   61  361 255 HOH   HOH C . 
H 5 HOH   62  362 8   HOH   HOH C . 
H 5 HOH   63  363 104 HOH   HOH C . 
H 5 HOH   64  364 45  HOH   HOH C . 
H 5 HOH   65  365 221 HOH   HOH C . 
H 5 HOH   66  366 214 HOH   HOH C . 
H 5 HOH   67  367 279 HOH   HOH C . 
H 5 HOH   68  368 15  HOH   HOH C . 
H 5 HOH   69  369 37  HOH   HOH C . 
H 5 HOH   70  370 174 HOH   HOH C . 
H 5 HOH   71  371 189 HOH   HOH C . 
H 5 HOH   72  372 91  HOH   HOH C . 
H 5 HOH   73  373 229 HOH   HOH C . 
H 5 HOH   74  374 163 HOH   HOH C . 
H 5 HOH   75  375 281 HOH   HOH C . 
H 5 HOH   76  376 243 HOH   HOH C . 
H 5 HOH   77  377 135 HOH   HOH C . 
H 5 HOH   78  378 142 HOH   HOH C . 
H 5 HOH   79  379 207 HOH   HOH C . 
H 5 HOH   80  380 14  HOH   HOH C . 
H 5 HOH   81  381 254 HOH   HOH C . 
H 5 HOH   82  382 76  HOH   HOH C . 
H 5 HOH   83  383 139 HOH   HOH C . 
H 5 HOH   84  384 158 HOH   HOH C . 
H 5 HOH   85  385 101 HOH   HOH C . 
H 5 HOH   86  386 217 HOH   HOH C . 
H 5 HOH   87  387 65  HOH   HOH C . 
H 5 HOH   88  388 107 HOH   HOH C . 
H 5 HOH   89  389 147 HOH   HOH C . 
H 5 HOH   90  390 152 HOH   HOH C . 
H 5 HOH   91  391 23  HOH   HOH C . 
H 5 HOH   92  392 46  HOH   HOH C . 
H 5 HOH   93  393 98  HOH   HOH C . 
H 5 HOH   94  394 60  HOH   HOH C . 
H 5 HOH   95  395 119 HOH   HOH C . 
H 5 HOH   96  396 114 HOH   HOH C . 
H 5 HOH   97  397 90  HOH   HOH C . 
H 5 HOH   98  398 96  HOH   HOH C . 
H 5 HOH   99  399 312 HOH   HOH C . 
H 5 HOH   100 400 162 HOH   HOH C . 
H 5 HOH   101 401 120 HOH   HOH C . 
H 5 HOH   102 402 213 HOH   HOH C . 
H 5 HOH   103 403 150 HOH   HOH C . 
H 5 HOH   104 404 272 HOH   HOH C . 
H 5 HOH   105 405 24  HOH   HOH C . 
H 5 HOH   106 406 77  HOH   HOH C . 
H 5 HOH   107 407 62  HOH   HOH C . 
H 5 HOH   108 408 282 HOH   HOH C . 
H 5 HOH   109 409 79  HOH   HOH C . 
H 5 HOH   110 410 226 HOH   HOH C . 
H 5 HOH   111 411 244 HOH   HOH C . 
H 5 HOH   112 412 177 HOH   HOH C . 
H 5 HOH   113 413 2   HOH   HOH C . 
H 5 HOH   114 414 64  HOH   HOH C . 
H 5 HOH   115 415 313 HOH   HOH C . 
H 5 HOH   116 416 36  HOH   HOH C . 
H 5 HOH   117 417 172 HOH   HOH C . 
H 5 HOH   118 418 208 HOH   HOH C . 
H 5 HOH   119 419 193 HOH   HOH C . 
H 5 HOH   120 420 109 HOH   HOH C . 
H 5 HOH   121 421 137 HOH   HOH C . 
H 5 HOH   122 422 301 HOH   HOH C . 
H 5 HOH   123 423 216 HOH   HOH C . 
H 5 HOH   124 424 184 HOH   HOH C . 
H 5 HOH   125 425 198 HOH   HOH C . 
H 5 HOH   126 426 218 HOH   HOH C . 
H 5 HOH   127 427 285 HOH   HOH C . 
H 5 HOH   128 428 241 HOH   HOH C . 
H 5 HOH   129 429 302 HOH   HOH C . 
H 5 HOH   130 430 238 HOH   HOH C . 
H 5 HOH   131 431 154 HOH   HOH C . 
H 5 HOH   132 432 192 HOH   HOH C . 
H 5 HOH   133 433 141 HOH   HOH C . 
H 5 HOH   134 434 235 HOH   HOH C . 
H 5 HOH   135 435 288 HOH   HOH C . 
H 5 HOH   136 436 210 HOH   HOH C . 
H 5 HOH   137 437 296 HOH   HOH C . 
H 5 HOH   138 438 318 HOH   HOH C . 
H 5 HOH   139 439 299 HOH   HOH C . 
H 5 HOH   140 440 237 HOH   HOH C . 
H 5 HOH   141 441 239 HOH   HOH C . 
H 5 HOH   142 442 196 HOH   HOH C . 
H 5 HOH   143 443 304 HOH   HOH C . 
H 5 HOH   144 444 175 HOH   HOH C . 
H 5 HOH   145 445 283 HOH   HOH C . 
H 5 HOH   146 446 267 HOH   HOH C . 
H 5 HOH   147 447 191 HOH   HOH C . 
H 5 HOH   148 448 322 HOH   HOH C . 
H 5 HOH   149 449 67  HOH   HOH C . 
H 5 HOH   150 450 323 HOH   HOH C . 
H 5 HOH   151 451 303 HOH   HOH C . 
H 5 HOH   152 452 305 HOH   HOH C . 
H 5 HOH   153 453 228 HOH   HOH C . 
H 5 HOH   154 454 173 HOH   HOH C . 
H 5 HOH   155 455 219 HOH   HOH C . 
H 5 HOH   156 456 194 HOH   HOH C . 
H 5 HOH   157 457 169 HOH   HOH C . 
H 5 HOH   158 458 265 HOH   HOH C . 
H 5 HOH   159 459 155 HOH   HOH C . 
H 5 HOH   160 460 240 HOH   HOH C . 
H 5 HOH   161 461 236 HOH   HOH C . 
H 5 HOH   162 462 223 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           7HUH 
_cell.length_a           86.795 
_cell.length_b           56.912 
_cell.length_c           65.120 
_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                         7HUH 
_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          7HUH 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.52 
_exptl_crystal.density_percent_sol   51.21 
_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   2024-10-03 
_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   0.92208 
_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        0.92208 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HUH 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             64.89 
_reflns.d_resolution_high            1.52 
_reflns.number_obs                   49076 
_reflns.percent_possible_obs         99.9 
_reflns.pdbx_Rmerge_I_obs            0.198 
_reflns.pdbx_netI_over_sigmaI        5.0 
_reflns.pdbx_redundancy              6.1 
_reflns.pdbx_Rrim_I_all              0.216 
_reflns.pdbx_Rpim_I_all              0.086 
_reflns.pdbx_CC_half                 0.995 
_reflns.pdbx_number_measured_all     300861 
_reflns.pdbx_chi_squared             0.76 
_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                  1.52 
_reflns_shell.d_res_low                   1.60 
_reflns_shell.number_measured_all         36380 
_reflns_shell.number_unique_obs           7102 
_reflns_shell.Rmerge_I_obs                2.613 
_reflns_shell.pdbx_chi_squared            0.66 
_reflns_shell.pdbx_redundancy             5.1 
_reflns_shell.percent_possible_obs        99.8 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.7 
_reflns_shell.pdbx_Rrim_I_all             2.900 
_reflns_shell.pdbx_Rpim_I_all             1.241 
_reflns_shell.pdbx_CC_half                0.366 
_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                                 7HUH 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     47898 
_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                             64.89 
_refine.ls_d_res_high                            1.516 
_refine.ls_percent_reflns_obs                    97.5 
_refine.ls_R_factor_obs                          0.2284 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2272 
_refine.ls_R_factor_R_free                       0.2525 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.000 
_refine.ls_number_reflns_R_free                  2396 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.936 
_refine.correlation_coeff_Fo_to_Fc_free          0.934 
_refine.B_iso_mean                               23.11 
_refine.aniso_B[1][1]                            3.73750 
_refine.aniso_B[2][2]                            -2.70270 
_refine.aniso_B[3][3]                            -1.03480 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -2.76570 
_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             0.090 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.088 
_refine.pdbx_overall_SU_R_Blow_DPI               0.095 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.092 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HUH 
_refine_analyze.Luzzati_coordinate_error_obs    0.24 
_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         26 
_refine_hist.number_atoms_solvent             331 
_refine_hist.number_atoms_total               2523 
_refine_hist.d_res_high                       1.516 
_refine_hist.d_res_low                        64.89 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
t_bond_d                  0.011 ? 2.00  2257 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               0.93  ? 2.00  3075 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  747  '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  413  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 2257 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           3.96  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           14.62 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  277  '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  1974 '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                       1.52 
_refine_ls_shell.d_res_low                        1.53 
_refine_ls_shell.number_reflns_R_work             912 
_refine_ls_shell.R_factor_R_work                  0.3971 
_refine_ls_shell.percent_reflns_obs               83.63 
_refine_ls_shell.R_factor_R_free                  0.3969 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            4.80 
_refine_ls_shell.number_reflns_R_free             46 
_refine_ls_shell.number_reflns_all                958 
_refine_ls_shell.R_factor_all                     0.3971 
# 
_struct.entry_id                  7HUH 
_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-0031591-001 (A71EV2A-x3175)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HUH 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN, HYDROLASE
;
# 
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 5 ? 
H 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 7HUH A 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
2 1 7HUH 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,G 
2 1 B,F,H     
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2  AA2 THR A 18  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
HELX_P HELX_P3  AA3 SER A 30  ? ARG A 32  ? SER A 36  ARG A 38  5 ? 3 
HELX_P HELX_P4  AA4 SER A 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
HELX_P HELX_P5  AA5 GLU A 100 ? CYS A 104 ? GLU A 106 CYS A 110 5 ? 5 
HELX_P HELX_P6  AA6 LEU A 134 ? GLU A 139 ? LEU A 140 GLU A 145 5 ? 6 
HELX_P HELX_P7  AA7 HIS B 15  ? ALA B 17  ? HIS C 21  ALA C 23  5 ? 3 
HELX_P HELX_P8  AA8 THR B 18  ? ASN B 24  ? THR C 24  ASN C 30  1 ? 7 
HELX_P HELX_P9  AA9 SER B 30  ? ARG B 32  ? SER C 36  ARG C 38  5 ? 3 
HELX_P HELX_P10 AB1 SER B 60  ? ARG B 63  ? SER C 66  ARG C 69  5 ? 4 
HELX_P HELX_P11 AB2 GLU B 100 ? CYS B 104 ? GLU C 106 CYS C 110 5 ? 5 
HELX_P HELX_P12 AB3 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 ? ? ? ? ? ? ? 2.337 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.450 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.328 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 D ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.101 ? ? 
metalc5 metalc ? ? B CYS 50  SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 56  C ZN 201 1_555 ? ? ? ? ? ? ? 2.379 ? ? 
metalc6 metalc ? ? B CYS 52  SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 58  C ZN 201 1_555 ? ? ? ? ? ? ? 2.441 ? ? 
metalc7 metalc ? ? B CYS 110 SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 116 C ZN 201 1_555 ? ? ? ? ? ? ? 2.286 ? ? 
metalc8 metalc ? ? B HIS 112 ND1 ? ? ? 1_555 F ZN . ZN ? ? C HIS 118 C ZN 201 1_555 ? ? ? ? ? ? ? 2.122 ? ? 
# 
_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_555 112.3 ? 
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_555 108.0 ? 
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_555 115.7 ? 
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_555 107.3 ? 
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_555 100.6 ? 
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_555 112.5 ? 
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_555 109.0 ? 
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_555 108.1 ? 
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_555 117.7 ? 
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_555 106.1 ? 
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_555 100.2 ? 
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_555 115.1 ? 
# 
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 SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O VAL A 126 ? O VAL A 132 N ALA A 95  ? N ALA A 101 
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 VAL B 68  ? O VAL C 74  N GLY B 55  ? N GLY C 61  
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                   7HUH 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 SER A 125 ? ? -135.41 -34.28  
2 1 CYS C 116 ? ? -123.46 -169.66 
3 1 SER C 125 ? ? -133.93 -32.95  
# 
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 14.9741 8.1466   14.5449 0.0219 -0.0515 -0.0312 0.0037 -0.0132 0.0143 2.5144 1.6466 0.6339 1.8094  
-0.8885 -0.5873 0.0190 0.1392 0.2059 0.0768 0.0918 0.0417  -0.0009 -0.0657 -0.1108 
'X-RAY DIFFRACTION' 2 ? refined 25.7261 -20.1468 17.9172 0.0303 -0.0483 -0.0259 0.0101 -0.0142 0.0241 1.1620 1.9365 0.1364 -0.8570 
-0.1254 -0.2717 0.0102 0.0118 0.1477 0.0688 0.0685 -0.0144 0.0179  -0.0065 -0.0786 
# 
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|* }' 
# 
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 
A1BN1 N1   N  Y N 1   
A1BN1 C4   C  N N 2   
A1BN1 C5   C  N N 3   
A1BN1 C6   C  Y N 4   
A1BN1 C7   C  Y N 5   
A1BN1 C8   C  N N 6   
A1BN1 C10  C  Y N 7   
A1BN1 C13  C  Y N 8   
A1BN1 O    O  N N 9   
A1BN1 C14  C  Y N 10  
A1BN1 C12  C  Y N 11  
A1BN1 C11  C  Y N 12  
A1BN1 C9   C  Y N 13  
A1BN1 N    N  N N 14  
A1BN1 C3   C  Y N 15  
A1BN1 C2   C  Y N 16  
A1BN1 O1   O  Y N 17  
A1BN1 N2   N  Y N 18  
A1BN1 C1   C  Y N 19  
A1BN1 C    C  N N 20  
A1BN1 H5   H  N N 21  
A1BN1 H4   H  N N 22  
A1BN1 H7   H  N N 23  
A1BN1 H9   H  N N 24  
A1BN1 H10  H  N N 25  
A1BN1 H8   H  N N 26  
A1BN1 H11  H  N N 27  
A1BN1 H14  H  N N 28  
A1BN1 H13  H  N N 29  
A1BN1 H12  H  N N 30  
A1BN1 H6   H  N N 31  
A1BN1 H3   H  N N 32  
A1BN1 H    H  N N 33  
A1BN1 H2   H  N N 34  
A1BN1 H1   H  N N 35  
ALA   N    N  N N 36  
ALA   CA   C  N S 37  
ALA   C    C  N N 38  
ALA   O    O  N N 39  
ALA   CB   C  N N 40  
ALA   OXT  O  N N 41  
ALA   H    H  N N 42  
ALA   H2   H  N N 43  
ALA   HA   H  N N 44  
ALA   HB1  H  N N 45  
ALA   HB2  H  N N 46  
ALA   HB3  H  N N 47  
ALA   HXT  H  N N 48  
ARG   N    N  N N 49  
ARG   CA   C  N S 50  
ARG   C    C  N N 51  
ARG   O    O  N N 52  
ARG   CB   C  N N 53  
ARG   CG   C  N N 54  
ARG   CD   C  N N 55  
ARG   NE   N  N N 56  
ARG   CZ   C  N N 57  
ARG   NH1  N  N N 58  
ARG   NH2  N  N N 59  
ARG   OXT  O  N N 60  
ARG   H    H  N N 61  
ARG   H2   H  N N 62  
ARG   HA   H  N N 63  
ARG   HB2  H  N N 64  
ARG   HB3  H  N N 65  
ARG   HG2  H  N N 66  
ARG   HG3  H  N N 67  
ARG   HD2  H  N N 68  
ARG   HD3  H  N N 69  
ARG   HE   H  N N 70  
ARG   HH11 H  N N 71  
ARG   HH12 H  N N 72  
ARG   HH21 H  N N 73  
ARG   HH22 H  N N 74  
ARG   HXT  H  N N 75  
ASN   N    N  N N 76  
ASN   CA   C  N S 77  
ASN   C    C  N N 78  
ASN   O    O  N N 79  
ASN   CB   C  N N 80  
ASN   CG   C  N N 81  
ASN   OD1  O  N N 82  
ASN   ND2  N  N N 83  
ASN   OXT  O  N N 84  
ASN   H    H  N N 85  
ASN   H2   H  N N 86  
ASN   HA   H  N N 87  
ASN   HB2  H  N N 88  
ASN   HB3  H  N N 89  
ASN   HD21 H  N N 90  
ASN   HD22 H  N N 91  
ASN   HXT  H  N N 92  
ASP   N    N  N N 93  
ASP   CA   C  N S 94  
ASP   C    C  N N 95  
ASP   O    O  N N 96  
ASP   CB   C  N N 97  
ASP   CG   C  N N 98  
ASP   OD1  O  N N 99  
ASP   OD2  O  N N 100 
ASP   OXT  O  N N 101 
ASP   H    H  N N 102 
ASP   H2   H  N N 103 
ASP   HA   H  N N 104 
ASP   HB2  H  N N 105 
ASP   HB3  H  N N 106 
ASP   HD2  H  N N 107 
ASP   HXT  H  N N 108 
CYS   N    N  N N 109 
CYS   CA   C  N R 110 
CYS   C    C  N N 111 
CYS   O    O  N N 112 
CYS   CB   C  N N 113 
CYS   SG   S  N N 114 
CYS   OXT  O  N N 115 
CYS   H    H  N N 116 
CYS   H2   H  N N 117 
CYS   HA   H  N N 118 
CYS   HB2  H  N N 119 
CYS   HB3  H  N N 120 
CYS   HG   H  N N 121 
CYS   HXT  H  N N 122 
DMS   S    S  N N 123 
DMS   O    O  N N 124 
DMS   C1   C  N N 125 
DMS   C2   C  N N 126 
DMS   H11  H  N N 127 
DMS   H12  H  N N 128 
DMS   H13  H  N N 129 
DMS   H21  H  N N 130 
DMS   H22  H  N N 131 
DMS   H23  H  N N 132 
GLN   N    N  N N 133 
GLN   CA   C  N S 134 
GLN   C    C  N N 135 
GLN   O    O  N N 136 
GLN   CB   C  N N 137 
GLN   CG   C  N N 138 
GLN   CD   C  N N 139 
GLN   OE1  O  N N 140 
GLN   NE2  N  N N 141 
GLN   OXT  O  N N 142 
GLN   H    H  N N 143 
GLN   H2   H  N N 144 
GLN   HA   H  N N 145 
GLN   HB2  H  N N 146 
GLN   HB3  H  N N 147 
GLN   HG2  H  N N 148 
GLN   HG3  H  N N 149 
GLN   HE21 H  N N 150 
GLN   HE22 H  N N 151 
GLN   HXT  H  N N 152 
GLU   N    N  N N 153 
GLU   CA   C  N S 154 
GLU   C    C  N N 155 
GLU   O    O  N N 156 
GLU   CB   C  N N 157 
GLU   CG   C  N N 158 
GLU   CD   C  N N 159 
GLU   OE1  O  N N 160 
GLU   OE2  O  N N 161 
GLU   OXT  O  N N 162 
GLU   H    H  N N 163 
GLU   H2   H  N N 164 
GLU   HA   H  N N 165 
GLU   HB2  H  N N 166 
GLU   HB3  H  N N 167 
GLU   HG2  H  N N 168 
GLU   HG3  H  N N 169 
GLU   HE2  H  N N 170 
GLU   HXT  H  N N 171 
GLY   N    N  N N 172 
GLY   CA   C  N N 173 
GLY   C    C  N N 174 
GLY   O    O  N N 175 
GLY   OXT  O  N N 176 
GLY   H    H  N N 177 
GLY   H2   H  N N 178 
GLY   HA2  H  N N 179 
GLY   HA3  H  N N 180 
GLY   HXT  H  N N 181 
HIS   N    N  N N 182 
HIS   CA   C  N S 183 
HIS   C    C  N N 184 
HIS   O    O  N N 185 
HIS   CB   C  N N 186 
HIS   CG   C  Y N 187 
HIS   ND1  N  Y N 188 
HIS   CD2  C  Y N 189 
HIS   CE1  C  Y N 190 
HIS   NE2  N  Y N 191 
HIS   OXT  O  N N 192 
HIS   H    H  N N 193 
HIS   H2   H  N N 194 
HIS   HA   H  N N 195 
HIS   HB2  H  N N 196 
HIS   HB3  H  N N 197 
HIS   HD1  H  N N 198 
HIS   HD2  H  N N 199 
HIS   HE1  H  N N 200 
HIS   HE2  H  N N 201 
HIS   HXT  H  N N 202 
HOH   O    O  N N 203 
HOH   H1   H  N N 204 
HOH   H2   H  N N 205 
ILE   N    N  N N 206 
ILE   CA   C  N S 207 
ILE   C    C  N N 208 
ILE   O    O  N N 209 
ILE   CB   C  N S 210 
ILE   CG1  C  N N 211 
ILE   CG2  C  N N 212 
ILE   CD1  C  N N 213 
ILE   OXT  O  N N 214 
ILE   H    H  N N 215 
ILE   H2   H  N N 216 
ILE   HA   H  N N 217 
ILE   HB   H  N N 218 
ILE   HG12 H  N N 219 
ILE   HG13 H  N N 220 
ILE   HG21 H  N N 221 
ILE   HG22 H  N N 222 
ILE   HG23 H  N N 223 
ILE   HD11 H  N N 224 
ILE   HD12 H  N N 225 
ILE   HD13 H  N N 226 
ILE   HXT  H  N N 227 
LEU   N    N  N N 228 
LEU   CA   C  N S 229 
LEU   C    C  N N 230 
LEU   O    O  N N 231 
LEU   CB   C  N N 232 
LEU   CG   C  N N 233 
LEU   CD1  C  N N 234 
LEU   CD2  C  N N 235 
LEU   OXT  O  N N 236 
LEU   H    H  N N 237 
LEU   H2   H  N N 238 
LEU   HA   H  N N 239 
LEU   HB2  H  N N 240 
LEU   HB3  H  N N 241 
LEU   HG   H  N N 242 
LEU   HD11 H  N N 243 
LEU   HD12 H  N N 244 
LEU   HD13 H  N N 245 
LEU   HD21 H  N N 246 
LEU   HD22 H  N N 247 
LEU   HD23 H  N N 248 
LEU   HXT  H  N N 249 
LYS   N    N  N N 250 
LYS   CA   C  N S 251 
LYS   C    C  N N 252 
LYS   O    O  N N 253 
LYS   CB   C  N N 254 
LYS   CG   C  N N 255 
LYS   CD   C  N N 256 
LYS   CE   C  N N 257 
LYS   NZ   N  N N 258 
LYS   OXT  O  N N 259 
LYS   H    H  N N 260 
LYS   H2   H  N N 261 
LYS   HA   H  N N 262 
LYS   HB2  H  N N 263 
LYS   HB3  H  N N 264 
LYS   HG2  H  N N 265 
LYS   HG3  H  N N 266 
LYS   HD2  H  N N 267 
LYS   HD3  H  N N 268 
LYS   HE2  H  N N 269 
LYS   HE3  H  N N 270 
LYS   HZ1  H  N N 271 
LYS   HZ2  H  N N 272 
LYS   HZ3  H  N N 273 
LYS   HXT  H  N N 274 
MET   N    N  N N 275 
MET   CA   C  N S 276 
MET   C    C  N N 277 
MET   O    O  N N 278 
MET   CB   C  N N 279 
MET   CG   C  N N 280 
MET   SD   S  N N 281 
MET   CE   C  N N 282 
MET   OXT  O  N N 283 
MET   H    H  N N 284 
MET   H2   H  N N 285 
MET   HA   H  N N 286 
MET   HB2  H  N N 287 
MET   HB3  H  N N 288 
MET   HG2  H  N N 289 
MET   HG3  H  N N 290 
MET   HE1  H  N N 291 
MET   HE2  H  N N 292 
MET   HE3  H  N N 293 
MET   HXT  H  N N 294 
PHE   N    N  N N 295 
PHE   CA   C  N S 296 
PHE   C    C  N N 297 
PHE   O    O  N N 298 
PHE   CB   C  N N 299 
PHE   CG   C  Y N 300 
PHE   CD1  C  Y N 301 
PHE   CD2  C  Y N 302 
PHE   CE1  C  Y N 303 
PHE   CE2  C  Y N 304 
PHE   CZ   C  Y N 305 
PHE   OXT  O  N N 306 
PHE   H    H  N N 307 
PHE   H2   H  N N 308 
PHE   HA   H  N N 309 
PHE   HB2  H  N N 310 
PHE   HB3  H  N N 311 
PHE   HD1  H  N N 312 
PHE   HD2  H  N N 313 
PHE   HE1  H  N N 314 
PHE   HE2  H  N N 315 
PHE   HZ   H  N N 316 
PHE   HXT  H  N N 317 
PRO   N    N  N N 318 
PRO   CA   C  N S 319 
PRO   C    C  N N 320 
PRO   O    O  N N 321 
PRO   CB   C  N N 322 
PRO   CG   C  N N 323 
PRO   CD   C  N N 324 
PRO   OXT  O  N N 325 
PRO   H    H  N N 326 
PRO   HA   H  N N 327 
PRO   HB2  H  N N 328 
PRO   HB3  H  N N 329 
PRO   HG2  H  N N 330 
PRO   HG3  H  N N 331 
PRO   HD2  H  N N 332 
PRO   HD3  H  N N 333 
PRO   HXT  H  N N 334 
SER   N    N  N N 335 
SER   CA   C  N S 336 
SER   C    C  N N 337 
SER   O    O  N N 338 
SER   CB   C  N N 339 
SER   OG   O  N N 340 
SER   OXT  O  N N 341 
SER   H    H  N N 342 
SER   H2   H  N N 343 
SER   HA   H  N N 344 
SER   HB2  H  N N 345 
SER   HB3  H  N N 346 
SER   HG   H  N N 347 
SER   HXT  H  N N 348 
THR   N    N  N N 349 
THR   CA   C  N S 350 
THR   C    C  N N 351 
THR   O    O  N N 352 
THR   CB   C  N R 353 
THR   OG1  O  N N 354 
THR   CG2  C  N N 355 
THR   OXT  O  N N 356 
THR   H    H  N N 357 
THR   H2   H  N N 358 
THR   HA   H  N N 359 
THR   HB   H  N N 360 
THR   HG1  H  N N 361 
THR   HG21 H  N N 362 
THR   HG22 H  N N 363 
THR   HG23 H  N N 364 
THR   HXT  H  N N 365 
TRP   N    N  N N 366 
TRP   CA   C  N S 367 
TRP   C    C  N N 368 
TRP   O    O  N N 369 
TRP   CB   C  N N 370 
TRP   CG   C  Y N 371 
TRP   CD1  C  Y N 372 
TRP   CD2  C  Y N 373 
TRP   NE1  N  Y N 374 
TRP   CE2  C  Y N 375 
TRP   CE3  C  Y N 376 
TRP   CZ2  C  Y N 377 
TRP   CZ3  C  Y N 378 
TRP   CH2  C  Y N 379 
TRP   OXT  O  N N 380 
TRP   H    H  N N 381 
TRP   H2   H  N N 382 
TRP   HA   H  N N 383 
TRP   HB2  H  N N 384 
TRP   HB3  H  N N 385 
TRP   HD1  H  N N 386 
TRP   HE1  H  N N 387 
TRP   HE3  H  N N 388 
TRP   HZ2  H  N N 389 
TRP   HZ3  H  N N 390 
TRP   HH2  H  N N 391 
TRP   HXT  H  N N 392 
TYR   N    N  N N 393 
TYR   CA   C  N S 394 
TYR   C    C  N N 395 
TYR   O    O  N N 396 
TYR   CB   C  N N 397 
TYR   CG   C  Y N 398 
TYR   CD1  C  Y N 399 
TYR   CD2  C  Y N 400 
TYR   CE1  C  Y N 401 
TYR   CE2  C  Y N 402 
TYR   CZ   C  Y N 403 
TYR   OH   O  N N 404 
TYR   OXT  O  N N 405 
TYR   H    H  N N 406 
TYR   H2   H  N N 407 
TYR   HA   H  N N 408 
TYR   HB2  H  N N 409 
TYR   HB3  H  N N 410 
TYR   HD1  H  N N 411 
TYR   HD2  H  N N 412 
TYR   HE1  H  N N 413 
TYR   HE2  H  N N 414 
TYR   HH   H  N N 415 
TYR   HXT  H  N N 416 
VAL   N    N  N N 417 
VAL   CA   C  N S 418 
VAL   C    C  N N 419 
VAL   O    O  N N 420 
VAL   CB   C  N N 421 
VAL   CG1  C  N N 422 
VAL   CG2  C  N N 423 
VAL   OXT  O  N N 424 
VAL   H    H  N N 425 
VAL   H2   H  N N 426 
VAL   HA   H  N N 427 
VAL   HB   H  N N 428 
VAL   HG11 H  N N 429 
VAL   HG12 H  N N 430 
VAL   HG13 H  N N 431 
VAL   HG21 H  N N 432 
VAL   HG22 H  N N 433 
VAL   HG23 H  N N 434 
VAL   HXT  H  N N 435 
ZN    ZN   ZN N N 436 
# 
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 
A1BN1 C   C1   sing N N 1   
A1BN1 C1  C2   sing Y N 2   
A1BN1 C2  C3   doub Y N 3   
A1BN1 C3  C4   sing N N 4   
A1BN1 C4  N    sing N N 5   
A1BN1 N   C5   sing N N 6   
A1BN1 C5  O    doub N N 7   
A1BN1 C6  C5   sing N N 8   
A1BN1 C6  C7   doub Y N 9   
A1BN1 C7  N1   sing Y N 10  
A1BN1 C8  N1   sing N N 11  
A1BN1 N1  C9   sing Y N 12  
A1BN1 C9  C10  doub Y N 13  
A1BN1 C10 C11  sing Y N 14  
A1BN1 C11 C12  doub Y N 15  
A1BN1 C12 C13  sing Y N 16  
A1BN1 C13 C14  doub Y N 17  
A1BN1 C14 C6   sing Y N 18  
A1BN1 C9  C14  sing Y N 19  
A1BN1 O1  C3   sing Y N 20  
A1BN1 N2  O1   sing Y N 21  
A1BN1 C1  N2   doub Y N 22  
A1BN1 C4  H5   sing N N 23  
A1BN1 C4  H4   sing N N 24  
A1BN1 C7  H7   sing N N 25  
A1BN1 C8  H9   sing N N 26  
A1BN1 C8  H10  sing N N 27  
A1BN1 C8  H8   sing N N 28  
A1BN1 C10 H11  sing N N 29  
A1BN1 C13 H14  sing N N 30  
A1BN1 C12 H13  sing N N 31  
A1BN1 C11 H12  sing N N 32  
A1BN1 N   H6   sing N N 33  
A1BN1 C2  H3   sing N N 34  
A1BN1 C   H    sing N N 35  
A1BN1 C   H2   sing N N 36  
A1BN1 C   H1   sing N N 37  
ALA   N   CA   sing N N 38  
ALA   N   H    sing N N 39  
ALA   N   H2   sing N N 40  
ALA   CA  C    sing N N 41  
ALA   CA  CB   sing N N 42  
ALA   CA  HA   sing N N 43  
ALA   C   O    doub N N 44  
ALA   C   OXT  sing N N 45  
ALA   CB  HB1  sing N N 46  
ALA   CB  HB2  sing N N 47  
ALA   CB  HB3  sing N N 48  
ALA   OXT HXT  sing N N 49  
ARG   N   CA   sing N N 50  
ARG   N   H    sing N N 51  
ARG   N   H2   sing N N 52  
ARG   CA  C    sing N N 53  
ARG   CA  CB   sing N N 54  
ARG   CA  HA   sing N N 55  
ARG   C   O    doub N N 56  
ARG   C   OXT  sing N N 57  
ARG   CB  CG   sing N N 58  
ARG   CB  HB2  sing N N 59  
ARG   CB  HB3  sing N N 60  
ARG   CG  CD   sing N N 61  
ARG   CG  HG2  sing N N 62  
ARG   CG  HG3  sing N N 63  
ARG   CD  NE   sing N N 64  
ARG   CD  HD2  sing N N 65  
ARG   CD  HD3  sing N N 66  
ARG   NE  CZ   sing N N 67  
ARG   NE  HE   sing N N 68  
ARG   CZ  NH1  sing N N 69  
ARG   CZ  NH2  doub N N 70  
ARG   NH1 HH11 sing N N 71  
ARG   NH1 HH12 sing N N 72  
ARG   NH2 HH21 sing N N 73  
ARG   NH2 HH22 sing N N 74  
ARG   OXT HXT  sing N N 75  
ASN   N   CA   sing N N 76  
ASN   N   H    sing N N 77  
ASN   N   H2   sing N N 78  
ASN   CA  C    sing N N 79  
ASN   CA  CB   sing N N 80  
ASN   CA  HA   sing N N 81  
ASN   C   O    doub N N 82  
ASN   C   OXT  sing N N 83  
ASN   CB  CG   sing N N 84  
ASN   CB  HB2  sing N N 85  
ASN   CB  HB3  sing N N 86  
ASN   CG  OD1  doub N N 87  
ASN   CG  ND2  sing N N 88  
ASN   ND2 HD21 sing N N 89  
ASN   ND2 HD22 sing N N 90  
ASN   OXT HXT  sing N N 91  
ASP   N   CA   sing N N 92  
ASP   N   H    sing N N 93  
ASP   N   H2   sing N N 94  
ASP   CA  C    sing N N 95  
ASP   CA  CB   sing N N 96  
ASP   CA  HA   sing N N 97  
ASP   C   O    doub N N 98  
ASP   C   OXT  sing N N 99  
ASP   CB  CG   sing N N 100 
ASP   CB  HB2  sing N N 101 
ASP   CB  HB3  sing N N 102 
ASP   CG  OD1  doub N N 103 
ASP   CG  OD2  sing N N 104 
ASP   OD2 HD2  sing N N 105 
ASP   OXT HXT  sing N N 106 
CYS   N   CA   sing N N 107 
CYS   N   H    sing N N 108 
CYS   N   H2   sing N N 109 
CYS   CA  C    sing N N 110 
CYS   CA  CB   sing N N 111 
CYS   CA  HA   sing N N 112 
CYS   C   O    doub N N 113 
CYS   C   OXT  sing N N 114 
CYS   CB  SG   sing N N 115 
CYS   CB  HB2  sing N N 116 
CYS   CB  HB3  sing N N 117 
CYS   SG  HG   sing N N 118 
CYS   OXT HXT  sing N N 119 
DMS   S   O    doub N N 120 
DMS   S   C1   sing N N 121 
DMS   S   C2   sing N N 122 
DMS   C1  H11  sing N N 123 
DMS   C1  H12  sing N N 124 
DMS   C1  H13  sing N N 125 
DMS   C2  H21  sing N N 126 
DMS   C2  H22  sing N N 127 
DMS   C2  H23  sing N N 128 
GLN   N   CA   sing N N 129 
GLN   N   H    sing N N 130 
GLN   N   H2   sing N N 131 
GLN   CA  C    sing N N 132 
GLN   CA  CB   sing N N 133 
GLN   CA  HA   sing N N 134 
GLN   C   O    doub N N 135 
GLN   C   OXT  sing N N 136 
GLN   CB  CG   sing N N 137 
GLN   CB  HB2  sing N N 138 
GLN   CB  HB3  sing N N 139 
GLN   CG  CD   sing N N 140 
GLN   CG  HG2  sing N N 141 
GLN   CG  HG3  sing N N 142 
GLN   CD  OE1  doub N N 143 
GLN   CD  NE2  sing N N 144 
GLN   NE2 HE21 sing N N 145 
GLN   NE2 HE22 sing N N 146 
GLN   OXT HXT  sing N N 147 
GLU   N   CA   sing N N 148 
GLU   N   H    sing N N 149 
GLU   N   H2   sing N N 150 
GLU   CA  C    sing N N 151 
GLU   CA  CB   sing N N 152 
GLU   CA  HA   sing N N 153 
GLU   C   O    doub N N 154 
GLU   C   OXT  sing N N 155 
GLU   CB  CG   sing N N 156 
GLU   CB  HB2  sing N N 157 
GLU   CB  HB3  sing N N 158 
GLU   CG  CD   sing N N 159 
GLU   CG  HG2  sing N N 160 
GLU   CG  HG3  sing N N 161 
GLU   CD  OE1  doub N N 162 
GLU   CD  OE2  sing N N 163 
GLU   OE2 HE2  sing N N 164 
GLU   OXT HXT  sing N N 165 
GLY   N   CA   sing N N 166 
GLY   N   H    sing N N 167 
GLY   N   H2   sing N N 168 
GLY   CA  C    sing N N 169 
GLY   CA  HA2  sing N N 170 
GLY   CA  HA3  sing N N 171 
GLY   C   O    doub N N 172 
GLY   C   OXT  sing N N 173 
GLY   OXT HXT  sing N N 174 
HIS   N   CA   sing N N 175 
HIS   N   H    sing N N 176 
HIS   N   H2   sing N N 177 
HIS   CA  C    sing N N 178 
HIS   CA  CB   sing N N 179 
HIS   CA  HA   sing N N 180 
HIS   C   O    doub N N 181 
HIS   C   OXT  sing N N 182 
HIS   CB  CG   sing N N 183 
HIS   CB  HB2  sing N N 184 
HIS   CB  HB3  sing N N 185 
HIS   CG  ND1  sing Y N 186 
HIS   CG  CD2  doub Y N 187 
HIS   ND1 CE1  doub Y N 188 
HIS   ND1 HD1  sing N N 189 
HIS   CD2 NE2  sing Y N 190 
HIS   CD2 HD2  sing N N 191 
HIS   CE1 NE2  sing Y N 192 
HIS   CE1 HE1  sing N N 193 
HIS   NE2 HE2  sing N N 194 
HIS   OXT HXT  sing N N 195 
HOH   O   H1   sing N N 196 
HOH   O   H2   sing N N 197 
ILE   N   CA   sing N N 198 
ILE   N   H    sing N N 199 
ILE   N   H2   sing N N 200 
ILE   CA  C    sing N N 201 
ILE   CA  CB   sing N N 202 
ILE   CA  HA   sing N N 203 
ILE   C   O    doub N N 204 
ILE   C   OXT  sing N N 205 
ILE   CB  CG1  sing N N 206 
ILE   CB  CG2  sing N N 207 
ILE   CB  HB   sing N N 208 
ILE   CG1 CD1  sing N N 209 
ILE   CG1 HG12 sing N N 210 
ILE   CG1 HG13 sing N N 211 
ILE   CG2 HG21 sing N N 212 
ILE   CG2 HG22 sing N N 213 
ILE   CG2 HG23 sing N N 214 
ILE   CD1 HD11 sing N N 215 
ILE   CD1 HD12 sing N N 216 
ILE   CD1 HD13 sing N N 217 
ILE   OXT HXT  sing N N 218 
LEU   N   CA   sing N N 219 
LEU   N   H    sing N N 220 
LEU   N   H2   sing N N 221 
LEU   CA  C    sing N N 222 
LEU   CA  CB   sing N N 223 
LEU   CA  HA   sing N N 224 
LEU   C   O    doub N N 225 
LEU   C   OXT  sing N N 226 
LEU   CB  CG   sing N N 227 
LEU   CB  HB2  sing N N 228 
LEU   CB  HB3  sing N N 229 
LEU   CG  CD1  sing N N 230 
LEU   CG  CD2  sing N N 231 
LEU   CG  HG   sing N N 232 
LEU   CD1 HD11 sing N N 233 
LEU   CD1 HD12 sing N N 234 
LEU   CD1 HD13 sing N N 235 
LEU   CD2 HD21 sing N N 236 
LEU   CD2 HD22 sing N N 237 
LEU   CD2 HD23 sing N N 238 
LEU   OXT HXT  sing N N 239 
LYS   N   CA   sing N N 240 
LYS   N   H    sing N N 241 
LYS   N   H2   sing N N 242 
LYS   CA  C    sing N N 243 
LYS   CA  CB   sing N N 244 
LYS   CA  HA   sing N N 245 
LYS   C   O    doub N N 246 
LYS   C   OXT  sing N N 247 
LYS   CB  CG   sing N N 248 
LYS   CB  HB2  sing N N 249 
LYS   CB  HB3  sing N N 250 
LYS   CG  CD   sing N N 251 
LYS   CG  HG2  sing N N 252 
LYS   CG  HG3  sing N N 253 
LYS   CD  CE   sing N N 254 
LYS   CD  HD2  sing N N 255 
LYS   CD  HD3  sing N N 256 
LYS   CE  NZ   sing N N 257 
LYS   CE  HE2  sing N N 258 
LYS   CE  HE3  sing N N 259 
LYS   NZ  HZ1  sing N N 260 
LYS   NZ  HZ2  sing N N 261 
LYS   NZ  HZ3  sing N N 262 
LYS   OXT HXT  sing N N 263 
MET   N   CA   sing N N 264 
MET   N   H    sing N N 265 
MET   N   H2   sing N N 266 
MET   CA  C    sing N N 267 
MET   CA  CB   sing N N 268 
MET   CA  HA   sing N N 269 
MET   C   O    doub N N 270 
MET   C   OXT  sing N N 271 
MET   CB  CG   sing N N 272 
MET   CB  HB2  sing N N 273 
MET   CB  HB3  sing N N 274 
MET   CG  SD   sing N N 275 
MET   CG  HG2  sing N N 276 
MET   CG  HG3  sing N N 277 
MET   SD  CE   sing N N 278 
MET   CE  HE1  sing N N 279 
MET   CE  HE2  sing N N 280 
MET   CE  HE3  sing N N 281 
MET   OXT HXT  sing N N 282 
PHE   N   CA   sing N N 283 
PHE   N   H    sing N N 284 
PHE   N   H2   sing N N 285 
PHE   CA  C    sing N N 286 
PHE   CA  CB   sing N N 287 
PHE   CA  HA   sing N N 288 
PHE   C   O    doub N N 289 
PHE   C   OXT  sing N N 290 
PHE   CB  CG   sing N N 291 
PHE   CB  HB2  sing N N 292 
PHE   CB  HB3  sing N N 293 
PHE   CG  CD1  doub Y N 294 
PHE   CG  CD2  sing Y N 295 
PHE   CD1 CE1  sing Y N 296 
PHE   CD1 HD1  sing N N 297 
PHE   CD2 CE2  doub Y N 298 
PHE   CD2 HD2  sing N N 299 
PHE   CE1 CZ   doub Y N 300 
PHE   CE1 HE1  sing N N 301 
PHE   CE2 CZ   sing Y N 302 
PHE   CE2 HE2  sing N N 303 
PHE   CZ  HZ   sing N N 304 
PHE   OXT HXT  sing N N 305 
PRO   N   CA   sing N N 306 
PRO   N   CD   sing N N 307 
PRO   N   H    sing N N 308 
PRO   CA  C    sing N N 309 
PRO   CA  CB   sing N N 310 
PRO   CA  HA   sing N N 311 
PRO   C   O    doub N N 312 
PRO   C   OXT  sing N N 313 
PRO   CB  CG   sing N N 314 
PRO   CB  HB2  sing N N 315 
PRO   CB  HB3  sing N N 316 
PRO   CG  CD   sing N N 317 
PRO   CG  HG2  sing N N 318 
PRO   CG  HG3  sing N N 319 
PRO   CD  HD2  sing N N 320 
PRO   CD  HD3  sing N N 321 
PRO   OXT HXT  sing N N 322 
SER   N   CA   sing N N 323 
SER   N   H    sing N N 324 
SER   N   H2   sing N N 325 
SER   CA  C    sing N N 326 
SER   CA  CB   sing N N 327 
SER   CA  HA   sing N N 328 
SER   C   O    doub N N 329 
SER   C   OXT  sing N N 330 
SER   CB  OG   sing N N 331 
SER   CB  HB2  sing N N 332 
SER   CB  HB3  sing N N 333 
SER   OG  HG   sing N N 334 
SER   OXT HXT  sing N N 335 
THR   N   CA   sing N N 336 
THR   N   H    sing N N 337 
THR   N   H2   sing N N 338 
THR   CA  C    sing N N 339 
THR   CA  CB   sing N N 340 
THR   CA  HA   sing N N 341 
THR   C   O    doub N N 342 
THR   C   OXT  sing N N 343 
THR   CB  OG1  sing N N 344 
THR   CB  CG2  sing N N 345 
THR   CB  HB   sing N N 346 
THR   OG1 HG1  sing N N 347 
THR   CG2 HG21 sing N N 348 
THR   CG2 HG22 sing N N 349 
THR   CG2 HG23 sing N N 350 
THR   OXT HXT  sing N N 351 
TRP   N   CA   sing N N 352 
TRP   N   H    sing N N 353 
TRP   N   H2   sing N N 354 
TRP   CA  C    sing N N 355 
TRP   CA  CB   sing N N 356 
TRP   CA  HA   sing N N 357 
TRP   C   O    doub N N 358 
TRP   C   OXT  sing N N 359 
TRP   CB  CG   sing N N 360 
TRP   CB  HB2  sing N N 361 
TRP   CB  HB3  sing N N 362 
TRP   CG  CD1  doub Y N 363 
TRP   CG  CD2  sing Y N 364 
TRP   CD1 NE1  sing Y N 365 
TRP   CD1 HD1  sing N N 366 
TRP   CD2 CE2  doub Y N 367 
TRP   CD2 CE3  sing Y N 368 
TRP   NE1 CE2  sing Y N 369 
TRP   NE1 HE1  sing N N 370 
TRP   CE2 CZ2  sing Y N 371 
TRP   CE3 CZ3  doub Y N 372 
TRP   CE3 HE3  sing N N 373 
TRP   CZ2 CH2  doub Y N 374 
TRP   CZ2 HZ2  sing N N 375 
TRP   CZ3 CH2  sing Y N 376 
TRP   CZ3 HZ3  sing N N 377 
TRP   CH2 HH2  sing N N 378 
TRP   OXT HXT  sing N N 379 
TYR   N   CA   sing N N 380 
TYR   N   H    sing N N 381 
TYR   N   H2   sing N N 382 
TYR   CA  C    sing N N 383 
TYR   CA  CB   sing N N 384 
TYR   CA  HA   sing N N 385 
TYR   C   O    doub N N 386 
TYR   C   OXT  sing N N 387 
TYR   CB  CG   sing N N 388 
TYR   CB  HB2  sing N N 389 
TYR   CB  HB3  sing N N 390 
TYR   CG  CD1  doub Y N 391 
TYR   CG  CD2  sing Y N 392 
TYR   CD1 CE1  sing Y N 393 
TYR   CD1 HD1  sing N N 394 
TYR   CD2 CE2  doub Y N 395 
TYR   CD2 HD2  sing N N 396 
TYR   CE1 CZ   doub Y N 397 
TYR   CE1 HE1  sing N N 398 
TYR   CE2 CZ   sing Y N 399 
TYR   CE2 HE2  sing N N 400 
TYR   CZ  OH   sing N N 401 
TYR   OH  HH   sing N N 402 
TYR   OXT HXT  sing N N 403 
VAL   N   CA   sing N N 404 
VAL   N   H    sing N N 405 
VAL   N   H2   sing N N 406 
VAL   CA  C    sing N N 407 
VAL   CA  CB   sing N N 408 
VAL   CA  HA   sing N N 409 
VAL   C   O    doub N N 410 
VAL   C   OXT  sing N N 411 
VAL   CB  CG1  sing N N 412 
VAL   CB  CG2  sing N N 413 
VAL   CB  HB   sing N N 414 
VAL   CG1 HG11 sing N N 415 
VAL   CG1 HG12 sing N N 416 
VAL   CG1 HG13 sing N N 417 
VAL   CG2 HG21 sing N N 418 
VAL   CG2 HG22 sing N N 419 
VAL   CG2 HG23 sing N N 420 
VAL   OXT HXT  sing N N 421 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171399 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002329 
_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                    7HUH 
_atom_sites.fract_transf_matrix[1][1]   0.011521 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000970 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017571 
_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]   0.015411 
_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   ? 17.973 7.817   24.923 1.00 20.45 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 19.213 7.896   24.134 1.00 21.15 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 19.296 6.720   23.160 1.00 19.70 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 18.556 5.745   23.302 1.00 19.55 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 20.418 7.867   25.075 1.00 23.45 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 20.371 6.638   25.787 1.00 26.85 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 20.170 6.829   22.166 1.00 18.22 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 20.340 5.752   21.203 1.00 17.99 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 20.753 6.259   19.831 1.00 17.48 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 20.438 7.391   19.445 1.00 16.83 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 21.469 5.418   19.101 1.00 16.98 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 21.935 5.801   17.775 1.00 16.80 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 21.903 4.610   16.821 1.00 16.40 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 21.761 3.455   17.270 1.00 17.14 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.338 6.351   17.888 1.00 17.03 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 21.959 4.884   15.523 1.00 15.44 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.106 3.857   14.501 1.00 15.55 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 23.582 3.919   14.080 1.00 16.89 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.086 5.009   13.772 1.00 17.06 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.186 4.042   13.244 1.00 15.31 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 19.739 4.223   13.596 1.00 15.44 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.354 2.859   12.278 1.00 15.09 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 18.894 4.813   12.414 1.00 17.36 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.272 2.770   14.034 1.00 16.64 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 25.657 2.706   13.599 1.00 17.51 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 25.730 1.897   12.309 1.00 18.14 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 25.644 0.665   12.338 1.00 18.60 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 26.551 2.115   14.698 1.00 17.71 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 26.638 3.003   15.913 1.00 17.78 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 27.490 4.101   15.939 1.00 19.16 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 25.831 2.781   17.021 1.00 18.90 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 27.539 4.951   17.037 1.00 18.95 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 25.904 3.600   18.146 1.00 19.80 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 26.742 4.703   18.136 1.00 20.06 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 26.787 5.538   19.224 1.00 21.64 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 25.817 2.597   11.169 1.00 17.78 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 25.848 1.981   9.842  1.00 19.01 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.077 2.481   9.090  1.00 20.35 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.296 3.692   9.032  1.00 20.91 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.552 2.253   9.032  1.00 19.95 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.199 3.751   8.957  1.00 19.45 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.668 1.658   7.641  1.00 20.98 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 27.914 1.575   8.566  1.00 21.01 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.168 1.957   7.888  1.00 21.80 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.029 2.864   8.759  1.00 21.76 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.196 2.585   9.956  1.00 22.01 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.463 4.007   8.221  1.00 21.11 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.217 4.974   9.020  1.00 21.13 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.331 6.156   9.468  1.00 20.52 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.810 7.301   9.602  1.00 21.15 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.486 5.432   8.342  1.00 22.66 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.547 4.350   8.376  1.00 27.12 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.391 4.290   9.298  1.00 28.44 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.511 3.475   7.375  1.00 26.15 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.055 5.847   9.781  1.00 19.12 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.084 6.848   10.213 1.00 18.30 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.454 6.523   11.554 1.00 17.14 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.186 5.351   11.859 1.00 17.78 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.955 6.981   9.155  1.00 18.97 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.443 7.430   7.796  1.00 20.06 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 28.025 8.679   7.624  1.00 21.54 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.319 6.610   6.682  1.00 20.87 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.460 9.107   6.383  1.00 21.78 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.752 7.032   5.426  1.00 21.55 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 28.323 8.286   5.284  1.00 22.61 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.779 8.748   4.068  1.00 23.96 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.083 7.592   12.308 1.00 16.39 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.334 7.525   13.569 1.00 15.52 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.105 8.437   13.348 1.00 15.83 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.263 9.632   13.046 1.00 15.34 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.192 8.018   14.761 1.00 15.85 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.434 8.402   16.036 1.00 15.28 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.368 8.647   17.238 1.00 17.99 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 26.905 9.733   18.125 1.00 18.55 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 26.215 9.543   19.251 1.00 20.98 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 25.853 8.319   19.620 1.00 20.82 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 25.801 10.584  19.968 1.00 21.87 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 23.898 7.856   13.401 1.00 14.76 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.636 8.580   13.186 1.00 14.18 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 21.994 8.761   14.553 1.00 14.79 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 21.730 7.778   15.234 1.00 14.70 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.705 7.838   12.206 1.00 14.51 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.498 8.701   11.846 1.00 14.71 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.458 7.378   10.953 1.00 14.16 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 21.803 10.010  14.980 1.00 14.40 ? 18  VAL   A N   1 
ATOM   86   C  CA  A VAL   A 1 12  ? 21.212 10.334  16.287 0.50 14.38 ? 18  VAL   A CA  1 
ATOM   87   C  CA  B VAL   A 1 12  ? 21.237 10.330  16.293 0.50 15.18 ? 18  VAL   A CA  1 
ATOM   88   C  C   . VAL   A 1 12  ? 20.110 11.369  16.132 1.00 14.37 ? 18  VAL   A C   1 
ATOM   89   O  O   . VAL   A 1 12  ? 20.005 12.024  15.082 1.00 14.91 ? 18  VAL   A O   1 
ATOM   90   C  CB  A VAL   A 1 12  ? 22.266 10.885  17.283 0.50 14.18 ? 18  VAL   A CB  1 
ATOM   91   C  CB  B VAL   A 1 12  ? 22.398 10.878  17.179 0.50 16.62 ? 18  VAL   A CB  1 
ATOM   92   C  CG1 A VAL   A 1 12  ? 23.235 9.818   17.718 0.50 16.14 ? 18  VAL   A CG1 1 
ATOM   93   C  CG1 B VAL   A 1 12  ? 21.940 11.338  18.550 0.50 17.12 ? 18  VAL   A CG1 1 
ATOM   94   C  CG2 A VAL   A 1 12  ? 22.967 12.128  16.733 0.50 12.64 ? 18  VAL   A CG2 1 
ATOM   95   C  CG2 B VAL   A 1 12  ? 23.492 9.853   17.333 0.50 18.41 ? 18  VAL   A CG2 1 
ATOM   96   N  N   . ASN   A 1 13  ? 19.272 11.561  17.196 1.00 13.61 ? 19  ASN   A N   1 
ATOM   97   C  CA  . ASN   A 1 13  ? 18.255 12.627  17.162 1.00 13.34 ? 19  ASN   A CA  1 
ATOM   98   C  C   . ASN   A 1 13  ? 19.079 13.948  17.174 1.00 13.83 ? 19  ASN   A C   1 
ATOM   99   O  O   . ASN   A 1 13  ? 20.036 14.063  17.965 1.00 14.35 ? 19  ASN   A O   1 
ATOM   100  C  CB  . ASN   A 1 13  ? 17.402 12.601  18.446 1.00 13.98 ? 19  ASN   A CB  1 
ATOM   101  C  CG  . ASN   A 1 13  ? 16.577 11.338  18.511 1.00 14.95 ? 19  ASN   A CG  1 
ATOM   102  O  OD1 . ASN   A 1 13  ? 16.994 10.340  19.100 1.00 15.59 ? 19  ASN   A OD1 1 
ATOM   103  N  ND2 . ASN   A 1 13  ? 15.398 11.362  17.872 1.00 14.22 ? 19  ASN   A ND2 1 
ATOM   104  N  N   . ARG   A 1 14  ? 18.729 14.905  16.331 1.00 14.47 ? 20  ARG   A N   1 
ATOM   105  C  CA  . ARG   A 1 14  ? 19.475 16.177  16.274 1.00 15.31 ? 20  ARG   A CA  1 
ATOM   106  C  C   . ARG   A 1 14  ? 19.461 16.880  17.640 1.00 16.99 ? 20  ARG   A C   1 
ATOM   107  O  O   . ARG   A 1 14  ? 20.491 17.427  18.039 1.00 17.82 ? 20  ARG   A O   1 
ATOM   108  C  CB  . ARG   A 1 14  ? 18.912 17.073  15.161 1.00 16.74 ? 20  ARG   A CB  1 
ATOM   109  C  CG  . ARG   A 1 14  ? 19.669 18.357  14.890 1.00 15.73 ? 20  ARG   A CG  1 
ATOM   110  C  CD  . ARG   A 1 14  ? 18.853 19.267  13.975 1.00 17.67 ? 20  ARG   A CD  1 
ATOM   111  N  NE  . ARG   A 1 14  ? 19.582 20.458  13.526 1.00 20.14 ? 20  ARG   A NE  1 
ATOM   112  C  CZ  . ARG   A 1 14  ? 19.676 21.592  14.218 1.00 23.35 ? 20  ARG   A CZ  1 
ATOM   113  N  NH1 . ARG   A 1 14  ? 19.142 21.683  15.436 1.00 21.30 ? 20  ARG   A NH1 1 
ATOM   114  N  NH2 . ARG   A 1 14  ? 20.314 22.643  13.702 1.00 25.34 ? 20  ARG   A NH2 1 
ATOM   115  N  N   . HIS   A 1 15  ? 18.359 16.748  18.406 1.00 17.65 ? 21  HIS   A N   1 
ATOM   116  C  CA  . HIS   A 1 15  ? 18.294 17.426  19.715 1.00 18.59 ? 21  HIS   A CA  1 
ATOM   117  C  C   . HIS   A 1 15  ? 19.172 16.773  20.792 1.00 19.25 ? 21  HIS   A C   1 
ATOM   118  O  O   . HIS   A 1 15  ? 19.363 17.353  21.864 1.00 21.10 ? 21  HIS   A O   1 
ATOM   119  C  CB  . HIS   A 1 15  ? 16.834 17.599  20.195 1.00 20.22 ? 21  HIS   A CB  1 
ATOM   120  C  CG  . HIS   A 1 15  ? 16.170 16.334  20.628 1.00 20.94 ? 21  HIS   A CG  1 
ATOM   121  N  ND1 . HIS   A 1 15  ? 15.497 15.536  19.732 1.00 21.81 ? 21  HIS   A ND1 1 
ATOM   122  C  CD2 . HIS   A 1 15  ? 16.004 15.833  21.877 1.00 21.56 ? 21  HIS   A CD2 1 
ATOM   123  C  CE1 . HIS   A 1 15  ? 14.968 14.558  20.452 1.00 22.64 ? 21  HIS   A CE1 1 
ATOM   124  N  NE2 . HIS   A 1 15  ? 15.237 14.700  21.749 1.00 22.18 ? 21  HIS   A NE2 1 
ATOM   125  N  N   . LEU   A 1 16  ? 19.657 15.542  20.546 1.00 18.48 ? 22  LEU   A N   1 
ATOM   126  C  CA  . LEU   A 1 16  ? 20.537 14.849  21.484 1.00 18.08 ? 22  LEU   A CA  1 
ATOM   127  C  C   . LEU   A 1 16  ? 22.021 14.788  20.981 1.00 18.38 ? 22  LEU   A C   1 
ATOM   128  O  O   . LEU   A 1 16  ? 22.878 14.183  21.635 1.00 19.45 ? 22  LEU   A O   1 
ATOM   129  C  CB  . LEU   A 1 16  ? 19.997 13.438  21.765 1.00 18.51 ? 22  LEU   A CB  1 
ATOM   130  C  CG  . LEU   A 1 16  ? 18.656 13.376  22.435 1.00 20.70 ? 22  LEU   A CG  1 
ATOM   131  C  CD1 . LEU   A 1 16  ? 18.238 11.904  22.622 1.00 21.42 ? 22  LEU   A CD1 1 
ATOM   132  C  CD2 . LEU   A 1 16  ? 18.671 14.163  23.822 1.00 21.70 ? 22  LEU   A CD2 1 
ATOM   133  N  N   . ALA   A 1 17  ? 22.331 15.432  19.846 1.00 17.47 ? 23  ALA   A N   1 
ATOM   134  C  CA  . ALA   A 1 17  ? 23.682 15.433  19.299 1.00 17.59 ? 23  ALA   A CA  1 
ATOM   135  C  C   . ALA   A 1 17  ? 24.676 16.073  20.295 1.00 17.78 ? 23  ALA   A C   1 
ATOM   136  O  O   . ALA   A 1 17  ? 24.356 17.063  20.949 1.00 18.01 ? 23  ALA   A O   1 
ATOM   137  C  CB  . ALA   A 1 17  ? 23.702 16.202  17.987 1.00 17.51 ? 23  ALA   A CB  1 
ATOM   138  N  N   . THR   A 1 18  ? 25.850 15.465  20.441 1.00 17.20 ? 24  THR   A N   1 
ATOM   139  C  CA  . THR   A 1 18  ? 26.890 15.980  21.357 1.00 16.20 ? 24  THR   A CA  1 
ATOM   140  C  C   . THR   A 1 18  ? 27.787 17.016  20.598 1.00 16.59 ? 24  THR   A C   1 
ATOM   141  O  O   . THR   A 1 18  ? 27.699 17.135  19.366 1.00 16.07 ? 24  THR   A O   1 
ATOM   142  C  CB  . THR   A 1 18  ? 27.787 14.784  21.786 1.00 17.87 ? 24  THR   A CB  1 
ATOM   143  O  OG1 . THR   A 1 18  ? 28.466 14.275  20.622 1.00 18.09 ? 24  THR   A OG1 1 
ATOM   144  C  CG2 . THR   A 1 18  ? 26.998 13.667  22.509 1.00 19.08 ? 24  THR   A CG2 1 
ATOM   145  N  N   . HIS   A 1 19  ? 28.736 17.680  21.313 1.00 18.11 ? 25  HIS   A N   1 
ATOM   146  C  CA  . HIS   A 1 19  ? 29.718 18.554  20.652 1.00 20.04 ? 25  HIS   A CA  1 
ATOM   147  C  C   . HIS   A 1 19  ? 30.543 17.712  19.639 1.00 19.64 ? 25  HIS   A C   1 
ATOM   148  O  O   . HIS   A 1 19  ? 30.758 18.161  18.540 1.00 19.61 ? 25  HIS   A O   1 
ATOM   149  C  CB  . HIS   A 1 19  ? 30.666 19.227  21.670 1.00 23.64 ? 25  HIS   A CB  1 
ATOM   150  C  CG  . HIS   A 1 19  ? 31.895 19.845  21.046 1.00 30.94 ? 25  HIS   A CG  1 
ATOM   151  N  ND1 . HIS   A 1 19  ? 31.893 21.162  20.569 1.00 33.92 ? 25  HIS   A ND1 1 
ATOM   152  C  CD2 . HIS   A 1 19  ? 33.121 19.299  20.806 1.00 33.61 ? 25  HIS   A CD2 1 
ATOM   153  C  CE1 . HIS   A 1 19  ? 33.112 21.378  20.092 1.00 34.58 ? 25  HIS   A CE1 1 
ATOM   154  N  NE2 . HIS   A 1 19  ? 33.889 20.285  20.200 1.00 34.88 ? 25  HIS   A NE2 1 
ATOM   155  N  N   . ASN   A 1 20  ? 30.929 16.457  20.004 1.00 19.27 ? 26  ASN   A N   1 
ATOM   156  C  CA  . ASN   A 1 20  ? 31.713 15.628  19.086 1.00 20.33 ? 26  ASN   A CA  1 
ATOM   157  C  C   . ASN   A 1 20  ? 30.928 15.338  17.795 1.00 18.94 ? 26  ASN   A C   1 
ATOM   158  O  O   . ASN   A 1 20  ? 31.502 15.400  16.708 1.00 20.22 ? 26  ASN   A O   1 
ATOM   159  C  CB  . ASN   A 1 20  ? 32.184 14.338  19.749 1.00 23.26 ? 26  ASN   A CB  1 
ATOM   160  C  CG  . ASN   A 1 20  ? 33.151 13.569  18.876 1.00 29.97 ? 26  ASN   A CG  1 
ATOM   161  O  OD1 . ASN   A 1 20  ? 34.320 13.969  18.698 1.00 32.31 ? 26  ASN   A OD1 1 
ATOM   162  N  ND2 . ASN   A 1 20  ? 32.693 12.457  18.298 1.00 30.62 ? 26  ASN   A ND2 1 
ATOM   163  N  N   . ASP   A 1 21  ? 29.613 15.092  17.892 1.00 18.02 ? 27  ASP   A N   1 
ATOM   164  C  CA  . ASP   A 1 21  ? 28.784 14.898  16.688 1.00 16.52 ? 27  ASP   A CA  1 
ATOM   165  C  C   . ASP   A 1 21  ? 28.845 16.145  15.780 1.00 16.45 ? 27  ASP   A C   1 
ATOM   166  O  O   . ASP   A 1 21  ? 29.064 16.012  14.574 1.00 16.95 ? 27  ASP   A O   1 
ATOM   167  C  CB  . ASP   A 1 21  ? 27.316 14.596  17.065 1.00 16.16 ? 27  ASP   A CB  1 
ATOM   168  C  CG  . ASP   A 1 21  ? 27.118 13.216  17.652 1.00 17.92 ? 27  ASP   A CG  1 
ATOM   169  O  OD1 . ASP   A 1 21  ? 27.746 12.283  17.163 1.00 18.88 ? 27  ASP   A OD1 1 
ATOM   170  O  OD2 . ASP   A 1 21  ? 26.304 13.082  18.602 1.00 18.60 ? 27  ASP   A OD2 1 
ATOM   171  N  N   . TRP   A 1 22  ? 28.616 17.352  16.349 1.00 15.70 ? 28  TRP   A N   1 
ATOM   172  C  CA  . TRP   A 1 22  ? 28.670 18.609  15.588 1.00 16.17 ? 28  TRP   A CA  1 
ATOM   173  C  C   . TRP   A 1 22  ? 30.078 18.862  15.021 1.00 16.87 ? 28  TRP   A C   1 
ATOM   174  O  O   . TRP   A 1 22  ? 30.203 19.380  13.920 1.00 17.94 ? 28  TRP   A O   1 
ATOM   175  C  CB  . TRP   A 1 22  ? 28.244 19.784  16.478 1.00 16.98 ? 28  TRP   A CB  1 
ATOM   176  C  CG  . TRP   A 1 22  ? 26.755 19.916  16.635 1.00 17.86 ? 28  TRP   A CG  1 
ATOM   177  C  CD1 . TRP   A 1 22  ? 26.006 19.589  17.731 1.00 18.12 ? 28  TRP   A CD1 1 
ATOM   178  C  CD2 . TRP   A 1 22  ? 25.824 20.356  15.629 1.00 17.94 ? 28  TRP   A CD2 1 
ATOM   179  N  NE1 . TRP   A 1 22  ? 24.675 19.885  17.499 1.00 17.83 ? 28  TRP   A NE1 1 
ATOM   180  C  CE2 . TRP   A 1 22  ? 24.529 20.291  16.194 1.00 17.64 ? 28  TRP   A CE2 1 
ATOM   181  C  CE3 . TRP   A 1 22  ? 25.966 20.826  14.318 1.00 18.06 ? 28  TRP   A CE3 1 
ATOM   182  C  CZ2 . TRP   A 1 22  ? 23.396 20.710  15.492 1.00 17.93 ? 28  TRP   A CZ2 1 
ATOM   183  C  CZ3 . TRP   A 1 22  ? 24.842 21.171  13.606 1.00 19.11 ? 28  TRP   A CZ3 1 
ATOM   184  C  CH2 . TRP   A 1 22  ? 23.585 21.165  14.194 1.00 18.25 ? 28  TRP   A CH2 1 
ATOM   185  N  N   . ALA   A 1 23  ? 31.130 18.502  15.781 1.00 16.01 ? 29  ALA   A N   1 
ATOM   186  C  CA  . ALA   A 1 23  ? 32.521 18.664  15.325 1.00 16.55 ? 29  ALA   A CA  1 
ATOM   187  C  C   . ALA   A 1 23  ? 32.912 17.691  14.198 1.00 16.47 ? 29  ALA   A C   1 
ATOM   188  O  O   . ALA   A 1 23  ? 33.948 17.878  13.557 1.00 16.13 ? 29  ALA   A O   1 
ATOM   189  C  CB  . ALA   A 1 23  ? 33.479 18.518  16.505 1.00 17.46 ? 29  ALA   A CB  1 
ATOM   190  N  N   . ASN   A 1 24  ? 32.096 16.624  13.980 1.00 15.87 ? 30  ASN   A N   1 
ATOM   191  C  CA  . ASN   A 1 24  ? 32.311 15.592  12.948 1.00 16.25 ? 30  ASN   A CA  1 
ATOM   192  C  C   . ASN   A 1 24  ? 31.037 15.405  12.123 1.00 16.61 ? 30  ASN   A C   1 
ATOM   193  O  O   . ASN   A 1 24  ? 30.697 14.281  11.723 1.00 16.72 ? 30  ASN   A O   1 
ATOM   194  C  CB  . ASN   A 1 24  ? 32.741 14.262  13.582 1.00 16.90 ? 30  ASN   A CB  1 
ATOM   195  C  CG  . ASN   A 1 24  ? 34.091 14.382  14.230 1.00 22.95 ? 30  ASN   A CG  1 
ATOM   196  O  OD1 . ASN   A 1 24  ? 35.124 14.313  13.549 1.00 26.86 ? 30  ASN   A OD1 1 
ATOM   197  N  ND2 . ASN   A 1 24  ? 34.116 14.665  15.541 1.00 21.93 ? 30  ASN   A ND2 1 
ATOM   198  N  N   . LEU   A 1 25  ? 30.382 16.522  11.812 1.00 16.88 ? 31  LEU   A N   1 
ATOM   199  C  CA  . LEU   A 1 25  ? 29.114 16.542  11.109 1.00 17.17 ? 31  LEU   A CA  1 
ATOM   200  C  C   . LEU   A 1 25  ? 29.200 16.050  9.652  1.00 17.92 ? 31  LEU   A C   1 
ATOM   201  O  O   . LEU   A 1 25  ? 30.044 16.530  8.884  1.00 17.52 ? 31  LEU   A O   1 
ATOM   202  C  CB  . LEU   A 1 25  ? 28.550 17.989  11.118 1.00 16.74 ? 31  LEU   A CB  1 
ATOM   203  C  CG  . LEU   A 1 25  ? 27.117 18.129  10.580 1.00 19.30 ? 31  LEU   A CG  1 
ATOM   204  C  CD1 . LEU   A 1 25  ? 26.146 17.357  11.419 1.00 19.66 ? 31  LEU   A CD1 1 
ATOM   205  C  CD2 . LEU   A 1 25  ? 26.689 19.568  10.487 1.00 21.46 ? 31  LEU   A CD2 1 
ATOM   206  N  N   . VAL   A 1 26  ? 28.232 15.200  9.247  1.00 16.23 ? 32  VAL   A N   1 
ATOM   207  C  CA  . VAL   A 1 26  ? 28.095 14.774  7.862  1.00 16.28 ? 32  VAL   A CA  1 
ATOM   208  C  C   . VAL   A 1 26  ? 26.851 15.465  7.260  1.00 16.49 ? 32  VAL   A C   1 
ATOM   209  O  O   . VAL   A 1 26  ? 26.901 16.001  6.156  1.00 16.28 ? 32  VAL   A O   1 
ATOM   210  C  CB  . VAL   A 1 26  ? 27.955 13.240  7.748  1.00 16.36 ? 32  VAL   A CB  1 
ATOM   211  C  CG1 . VAL   A 1 26  ? 27.599 12.821  6.317  1.00 17.90 ? 32  VAL   A CG1 1 
ATOM   212  C  CG2 . VAL   A 1 26  ? 29.211 12.543  8.252  1.00 16.28 ? 32  VAL   A CG2 1 
ATOM   213  N  N   . TRP   A 1 27  ? 25.726 15.448  8.013  1.00 15.65 ? 33  TRP   A N   1 
ATOM   214  C  CA  . TRP   A 1 27  ? 24.445 15.984  7.549  1.00 16.75 ? 33  TRP   A CA  1 
ATOM   215  C  C   . TRP   A 1 27  ? 23.497 16.183  8.722  1.00 16.31 ? 33  TRP   A C   1 
ATOM   216  O  O   . TRP   A 1 27  ? 23.523 15.395  9.666  1.00 16.16 ? 33  TRP   A O   1 
ATOM   217  C  CB  . TRP   A 1 27  ? 23.829 14.999  6.531  1.00 17.75 ? 33  TRP   A CB  1 
ATOM   218  C  CG  . TRP   A 1 27  ? 22.415 15.305  6.115  1.00 19.42 ? 33  TRP   A CG  1 
ATOM   219  C  CD1 . TRP   A 1 27  ? 22.012 16.145  5.118  1.00 21.77 ? 33  TRP   A CD1 1 
ATOM   220  C  CD2 . TRP   A 1 27  ? 21.224 14.663  6.607  1.00 19.67 ? 33  TRP   A CD2 1 
ATOM   221  N  NE1 . TRP   A 1 27  ? 20.631 16.106  4.995  1.00 22.31 ? 33  TRP   A NE1 1 
ATOM   222  C  CE2 . TRP   A 1 27  ? 20.124 15.219  5.912  1.00 20.83 ? 33  TRP   A CE2 1 
ATOM   223  C  CE3 . TRP   A 1 27  ? 20.977 13.717  7.605  1.00 19.85 ? 33  TRP   A CE3 1 
ATOM   224  C  CZ2 . TRP   A 1 27  ? 18.800 14.820  6.161  1.00 21.31 ? 33  TRP   A CZ2 1 
ATOM   225  C  CZ3 . TRP   A 1 27  ? 19.665 13.349  7.866  1.00 21.00 ? 33  TRP   A CZ3 1 
ATOM   226  C  CH2 . TRP   A 1 27  ? 18.600 13.888  7.140  1.00 21.49 ? 33  TRP   A CH2 1 
ATOM   227  N  N   . GLU   A 1 28  ? 22.665 17.232  8.676  1.00 16.60 ? 34  GLU   A N   1 
ATOM   228  C  CA  . GLU   A 1 28  ? 21.673 17.454  9.737  1.00 16.23 ? 34  GLU   A CA  1 
ATOM   229  C  C   . GLU   A 1 28  ? 20.412 18.086  9.149  1.00 17.42 ? 34  GLU   A C   1 
ATOM   230  O  O   . GLU   A 1 28  ? 20.486 18.836  8.161  1.00 18.63 ? 34  GLU   A O   1 
ATOM   231  C  CB  . GLU   A 1 28  ? 22.241 18.289  10.893 1.00 18.05 ? 34  GLU   A CB  1 
ATOM   232  C  CG  . GLU   A 1 28  ? 22.803 19.661  10.500 1.00 21.19 ? 34  GLU   A CG  1 
ATOM   233  C  CD  . GLU   A 1 28  ? 21.822 20.818  10.389 1.00 24.92 ? 34  GLU   A CD  1 
ATOM   234  O  OE1 . GLU   A 1 28  ? 22.153 21.809  9.698  1.00 25.05 ? 34  GLU   A OE1 1 
ATOM   235  O  OE2 . GLU   A 1 28  ? 20.717 20.733  10.974 1.00 24.53 ? 34  GLU   A OE2 1 
ATOM   236  N  N   . ASP   A 1 29  ? 19.264 17.785  9.744  1.00 17.35 ? 35  ASP   A N   1 
ATOM   237  C  CA  . ASP   A 1 29  ? 18.005 18.360  9.289  1.00 19.89 ? 35  ASP   A CA  1 
ATOM   238  C  C   . ASP   A 1 29  ? 17.072 18.553  10.492 1.00 20.86 ? 35  ASP   A C   1 
ATOM   239  O  O   . ASP   A 1 29  ? 16.585 17.580  11.043 1.00 21.40 ? 35  ASP   A O   1 
ATOM   240  C  CB  . ASP   A 1 29  ? 17.401 17.461  8.204  1.00 21.72 ? 35  ASP   A CB  1 
ATOM   241  C  CG  . ASP   A 1 29  ? 16.142 18.004  7.540  1.00 25.35 ? 35  ASP   A CG  1 
ATOM   242  O  OD1 . ASP   A 1 29  ? 15.319 18.629  8.244  1.00 26.56 ? 35  ASP   A OD1 1 
ATOM   243  O  OD2 . ASP   A 1 29  ? 15.964 17.764  6.329  1.00 27.32 ? 35  ASP   A OD2 1 
ATOM   244  N  N   . SER   A 1 30  ? 16.863 19.814  10.911 1.00 21.59 ? 36  SER   A N   1 
ATOM   245  C  CA  . SER   A 1 30  ? 16.046 20.144  12.061 1.00 22.95 ? 36  SER   A CA  1 
ATOM   246  C  C   . SER   A 1 30  ? 14.589 19.721  11.870 1.00 23.79 ? 36  SER   A C   1 
ATOM   247  O  O   . SER   A 1 30  ? 13.995 19.197  12.822 1.00 23.97 ? 36  SER   A O   1 
ATOM   248  C  CB  . SER   A 1 30  ? 16.134 21.633  12.379 1.00 25.57 ? 36  SER   A CB  1 
ATOM   249  O  OG  . SER   A 1 30  ? 15.274 21.973  13.453 1.00 28.26 ? 36  SER   A OG  1 
ATOM   250  N  N   . SER   A 1 31  ? 14.032 19.887  10.651 1.00 23.76 ? 37  SER   A N   1 
ATOM   251  C  CA  . SER   A 1 31  ? 12.645 19.479  10.409 1.00 23.87 ? 37  SER   A CA  1 
ATOM   252  C  C   . SER   A 1 31  ? 12.458 17.962  10.558 1.00 22.71 ? 37  SER   A C   1 
ATOM   253  O  O   . SER   A 1 31  ? 11.366 17.552  10.875 1.00 24.08 ? 37  SER   A O   1 
ATOM   254  C  CB  . SER   A 1 31  ? 12.131 19.967  9.053  1.00 27.45 ? 37  SER   A CB  1 
ATOM   255  O  OG  . SER   A 1 31  ? 12.553 19.153  7.976  1.00 31.50 ? 37  SER   A OG  1 
ATOM   256  N  N   . ARG   A 1 32  ? 13.536 17.146  10.399 1.00 20.48 ? 38  ARG   A N   1 
ATOM   257  C  CA  . ARG   A 1 32  ? 13.435 15.687  10.580 1.00 18.52 ? 38  ARG   A CA  1 
ATOM   258  C  C   . ARG   A 1 32  ? 13.946 15.202  11.965 1.00 17.76 ? 38  ARG   A C   1 
ATOM   259  O  O   . ARG   A 1 32  ? 13.853 13.996  12.248 1.00 18.23 ? 38  ARG   A O   1 
ATOM   260  C  CB  . ARG   A 1 32  ? 14.223 14.944  9.486  1.00 18.62 ? 38  ARG   A CB  1 
ATOM   261  C  CG  . ARG   A 1 32  ? 13.736 15.187  8.066  1.00 20.61 ? 38  ARG   A CG  1 
ATOM   262  C  CD  . ARG   A 1 32  ? 14.616 14.474  7.053  1.00 22.46 ? 38  ARG   A CD  1 
ATOM   263  N  NE  . ARG   A 1 32  ? 14.441 13.020  7.130  1.00 19.67 ? 38  ARG   A NE  1 
ATOM   264  C  CZ  . ARG   A 1 32  ? 14.544 12.204  6.084  1.00 20.38 ? 38  ARG   A CZ  1 
ATOM   265  N  NH1 . ARG   A 1 32  ? 14.838 12.690  4.873  1.00 21.42 ? 38  ARG   A NH1 1 
ATOM   266  N  NH2 . ARG   A 1 32  ? 14.353 10.898  6.236  1.00 19.84 ? 38  ARG   A NH2 1 
ATOM   267  N  N   . ASP   A 1 33  ? 14.495 16.111  12.802 1.00 15.58 ? 39  ASP   A N   1 
ATOM   268  C  CA  . ASP   A 1 33  ? 15.108 15.780  14.087 1.00 16.06 ? 39  ASP   A CA  1 
ATOM   269  C  C   . ASP   A 1 33  ? 16.229 14.767  13.898 1.00 15.89 ? 39  ASP   A C   1 
ATOM   270  O  O   . ASP   A 1 33  ? 16.437 13.911  14.773 1.00 15.48 ? 39  ASP   A O   1 
ATOM   271  C  CB  . ASP   A 1 33  ? 14.092 15.289  15.142 1.00 17.85 ? 39  ASP   A CB  1 
ATOM   272  C  CG  . ASP   A 1 33  ? 14.710 15.030  16.512 1.00 19.46 ? 39  ASP   A CG  1 
ATOM   273  O  OD1 . ASP   A 1 33  ? 15.522 15.857  16.962 1.00 19.06 ? 39  ASP   A OD1 1 
ATOM   274  O  OD2 . ASP   A 1 33  ? 14.410 13.968  17.112 1.00 19.33 ? 39  ASP   A OD2 1 
ATOM   275  N  N   . LEU   A 1 34  ? 16.994 14.878  12.764 1.00 15.37 ? 40  LEU   A N   1 
ATOM   276  C  CA  . LEU   A 1 34  ? 18.104 13.949  12.490 1.00 15.35 ? 40  LEU   A CA  1 
ATOM   277  C  C   . LEU   A 1 34  ? 19.453 14.655  12.344 1.00 15.63 ? 40  LEU   A C   1 
ATOM   278  O  O   . LEU   A 1 34  ? 19.536 15.748  11.786 1.00 16.09 ? 40  LEU   A O   1 
ATOM   279  C  CB  . LEU   A 1 34  ? 17.864 13.156  11.182 1.00 15.51 ? 40  LEU   A CB  1 
ATOM   280  C  CG  . LEU   A 1 34  ? 16.756 12.077  11.249 1.00 15.62 ? 40  LEU   A CG  1 
ATOM   281  C  CD1 . LEU   A 1 34  ? 16.670 11.329  9.967  1.00 14.63 ? 40  LEU   A CD1 1 
ATOM   282  C  CD2 . LEU   A 1 34  ? 17.021 11.071  12.401 1.00 15.50 ? 40  LEU   A CD2 1 
ATOM   283  N  N   . LEU   A 1 35  ? 20.512 13.984  12.810 1.00 14.00 ? 41  LEU   A N   1 
ATOM   284  C  CA  . LEU   A 1 35  ? 21.867 14.456  12.626 1.00 14.27 ? 41  LEU   A CA  1 
ATOM   285  C  C   . LEU   A 1 35  ? 22.720 13.202  12.417 1.00 14.24 ? 41  LEU   A C   1 
ATOM   286  O  O   . LEU   A 1 35  ? 22.535 12.170  13.104 1.00 14.31 ? 41  LEU   A O   1 
ATOM   287  C  CB  . LEU   A 1 35  ? 22.385 15.293  13.825 1.00 14.88 ? 41  LEU   A CB  1 
ATOM   288  C  CG  . LEU   A 1 35  ? 23.792 15.861  13.692 1.00 14.34 ? 41  LEU   A CG  1 
ATOM   289  C  CD1 . LEU   A 1 35  ? 23.900 17.216  14.369 1.00 13.98 ? 41  LEU   A CD1 1 
ATOM   290  C  CD2 . LEU   A 1 35  ? 24.850 14.886  14.323 1.00 14.65 ? 41  LEU   A CD2 1 
ATOM   291  N  N   . VAL   A 1 36  ? 23.606 13.268  11.437 1.00 12.77 ? 42  VAL   A N   1 
ATOM   292  C  CA  . VAL   A 1 36  ? 24.522 12.168  11.127 1.00 13.02 ? 42  VAL   A CA  1 
ATOM   293  C  C   . VAL   A 1 36  ? 25.963 12.659  11.282 1.00 14.10 ? 42  VAL   A C   1 
ATOM   294  O  O   . VAL   A 1 36  ? 26.327 13.698  10.710 1.00 16.31 ? 42  VAL   A O   1 
ATOM   295  C  CB  . VAL   A 1 36  ? 24.296 11.605  9.710  1.00 14.93 ? 42  VAL   A CB  1 
ATOM   296  C  CG1 . VAL   A 1 36  ? 25.333 10.512  9.391  1.00 16.37 ? 42  VAL   A CG1 1 
ATOM   297  C  CG2 . VAL   A 1 36  ? 22.867 11.069  9.548  1.00 15.81 ? 42  VAL   A CG2 1 
ATOM   298  N  N   . SER   A 1 37  ? 26.773 11.950  12.059 1.00 13.05 ? 43  SER   A N   1 
ATOM   299  C  CA  . SER   A 1 37  ? 28.195 12.271  12.209 1.00 14.82 ? 43  SER   A CA  1 
ATOM   300  C  C   . SER   A 1 37  ? 29.087 11.080  11.731 1.00 16.19 ? 43  SER   A C   1 
ATOM   301  O  O   . SER   A 1 37  ? 28.593 9.954   11.516 1.00 16.73 ? 43  SER   A O   1 
ATOM   302  C  CB  . SER   A 1 37  ? 28.519 12.714  13.636 1.00 17.10 ? 43  SER   A CB  1 
ATOM   303  O  OG  . SER   A 1 37  ? 28.334 11.646  14.543 1.00 16.45 ? 43  SER   A OG  1 
ATOM   304  N  N   . SER   A 1 38  ? 30.388 11.333  11.515 1.00 17.25 ? 44  SER   A N   1 
ATOM   305  C  CA  . SER   A 1 38  ? 31.297 10.274  11.062 1.00 18.51 ? 44  SER   A CA  1 
ATOM   306  C  C   . SER   A 1 38  ? 31.939 9.500   12.234 1.00 20.61 ? 44  SER   A C   1 
ATOM   307  O  O   . SER   A 1 38  ? 32.140 10.041  13.340 1.00 21.25 ? 44  SER   A O   1 
ATOM   308  C  CB  . SER   A 1 38  ? 32.392 10.882  10.176 1.00 19.71 ? 44  SER   A CB  1 
ATOM   309  O  OG  . SER   A 1 38  ? 33.031 11.933  10.889 1.00 21.28 ? 44  SER   A OG  1 
ATOM   310  N  N   . THR   A 1 39  ? 32.263 8.215   11.983 1.00 21.16 ? 45  THR   A N   1 
ATOM   311  C  CA  . THR   A 1 39  ? 32.890 7.376   12.994 1.00 23.77 ? 45  THR   A CA  1 
ATOM   312  C  C   . THR   A 1 39  ? 34.224 6.820   12.501 1.00 26.52 ? 45  THR   A C   1 
ATOM   313  O  O   . THR   A 1 39  ? 34.420 6.677   11.287 1.00 26.61 ? 45  THR   A O   1 
ATOM   314  C  CB  . THR   A 1 39  ? 31.958 6.215   13.387 1.00 23.79 ? 45  THR   A CB  1 
ATOM   315  O  OG1 . THR   A 1 39  ? 31.831 5.305   12.306 1.00 24.00 ? 45  THR   A OG1 1 
ATOM   316  C  CG2 . THR   A 1 39  ? 30.588 6.692   13.827 1.00 24.21 ? 45  THR   A CG2 1 
ATOM   317  N  N   . THR   A 1 40  ? 35.107 6.429   13.438 1.00 28.48 ? 46  THR   A N   1 
ATOM   318  C  CA  . THR   A 1 40  ? 36.368 5.808   13.045 1.00 31.16 ? 46  THR   A CA  1 
ATOM   319  C  C   . THR   A 1 40  ? 36.136 4.310   12.799 1.00 31.74 ? 46  THR   A C   1 
ATOM   320  O  O   . THR   A 1 40  ? 36.574 3.786   11.767 1.00 31.89 ? 46  THR   A O   1 
ATOM   321  C  CB  . THR   A 1 40  ? 37.513 6.155   14.008 1.00 34.75 ? 46  THR   A CB  1 
ATOM   322  O  OG1 . THR   A 1 40  ? 37.045 6.132   15.361 1.00 37.03 ? 46  THR   A OG1 1 
ATOM   323  C  CG2 . THR   A 1 40  ? 38.107 7.514   13.713 1.00 35.52 ? 46  THR   A CG2 1 
ATOM   324  N  N   . ALA   A 1 41  ? 35.381 3.644   13.688 1.00 31.98 ? 47  ALA   A N   1 
ATOM   325  C  CA  . ALA   A 1 41  ? 35.089 2.222   13.499 1.00 32.80 ? 47  ALA   A CA  1 
ATOM   326  C  C   . ALA   A 1 41  ? 33.813 2.000   12.673 1.00 33.56 ? 47  ALA   A C   1 
ATOM   327  O  O   . ALA   A 1 41  ? 32.868 2.797   12.748 1.00 33.41 ? 47  ALA   A O   1 
ATOM   328  C  CB  . ALA   A 1 41  ? 34.963 1.520   14.837 1.00 33.14 ? 47  ALA   A CB  1 
ATOM   329  N  N   . GLN   A 1 42  ? 33.773 0.891   11.913 1.00 33.33 ? 48  GLN   A N   1 
ATOM   330  C  CA  . GLN   A 1 42  ? 32.583 0.566   11.113 1.00 33.61 ? 48  GLN   A CA  1 
ATOM   331  C  C   . GLN   A 1 42  ? 31.453 0.017   12.010 1.00 32.13 ? 48  GLN   A C   1 
ATOM   332  O  O   . GLN   A 1 42  ? 31.726 -0.612  13.040 1.00 33.24 ? 48  GLN   A O   1 
ATOM   333  C  CB  . GLN   A 1 42  ? 32.918 -0.421  9.992  1.00 37.05 ? 48  GLN   A CB  1 
ATOM   334  C  CG  . GLN   A 1 42  ? 33.655 0.196   8.801  1.00 44.43 ? 48  GLN   A CG  1 
ATOM   335  C  CD  . GLN   A 1 42  ? 33.031 -0.222  7.493  1.00 54.14 ? 48  GLN   A CD  1 
ATOM   336  O  OE1 . GLN   A 1 42  ? 32.890 -1.419  7.199  1.00 57.08 ? 48  GLN   A OE1 1 
ATOM   337  N  NE2 . GLN   A 1 42  ? 32.640 0.752   6.670  1.00 55.76 ? 48  GLN   A NE2 1 
ATOM   338  N  N   . GLY   A 1 43  ? 30.196 0.258   11.618 1.00 29.24 ? 49  GLY   A N   1 
ATOM   339  C  CA  . GLY   A 1 43  ? 29.027 -0.158  12.393 1.00 27.52 ? 49  GLY   A CA  1 
ATOM   340  C  C   . GLY   A 1 43  ? 28.362 -1.424  11.892 1.00 24.91 ? 49  GLY   A C   1 
ATOM   341  O  O   . GLY   A 1 43  ? 28.602 -1.863  10.764 1.00 24.11 ? 49  GLY   A O   1 
ATOM   342  N  N   . CYS   A 1 44  ? 27.515 -2.022  12.748 1.00 23.84 ? 50  CYS   A N   1 
ATOM   343  C  CA  . CYS   A 1 44  ? 26.835 -3.309  12.516 1.00 23.72 ? 50  CYS   A CA  1 
ATOM   344  C  C   . CYS   A 1 44  ? 25.391 -3.234  11.995 1.00 22.00 ? 50  CYS   A C   1 
ATOM   345  O  O   . CYS   A 1 44  ? 24.835 -4.274  11.610 1.00 20.64 ? 50  CYS   A O   1 
ATOM   346  C  CB  . CYS   A 1 44  ? 26.880 -4.151  13.791 1.00 25.21 ? 50  CYS   A CB  1 
ATOM   347  S  SG  . CYS   A 1 44  ? 28.544 -4.606  14.326 1.00 31.28 ? 50  CYS   A SG  1 
ATOM   348  N  N   . ASP   A 1 45  ? 24.739 -2.061  12.149 1.00 20.87 ? 51  ASP   A N   1 
ATOM   349  C  CA  . ASP   A 1 45  ? 23.344 -1.943  11.761 1.00 20.86 ? 51  ASP   A CA  1 
ATOM   350  C  C   . ASP   A 1 45  ? 23.206 -1.900  10.250 1.00 22.29 ? 51  ASP   A C   1 
ATOM   351  O  O   . ASP   A 1 45  ? 24.088 -1.382  9.573  1.00 23.49 ? 51  ASP   A O   1 
ATOM   352  C  CB  . ASP   A 1 45  ? 22.713 -0.693  12.394 1.00 20.24 ? 51  ASP   A CB  1 
ATOM   353  C  CG  . ASP   A 1 45  ? 22.674 -0.747  13.910 1.00 21.68 ? 51  ASP   A CG  1 
ATOM   354  O  OD1 . ASP   A 1 45  ? 22.421 -1.859  14.461 1.00 20.99 ? 51  ASP   A OD1 1 
ATOM   355  O  OD2 . ASP   A 1 45  ? 22.900 0.312   14.558 1.00 22.69 ? 51  ASP   A OD2 1 
ATOM   356  N  N   . THR   A 1 46  ? 22.104 -2.419  9.732  1.00 23.20 ? 52  THR   A N   1 
ATOM   357  C  CA  . THR   A 1 46  ? 21.772 -2.427  8.294  1.00 24.56 ? 52  THR   A CA  1 
ATOM   358  C  C   . THR   A 1 46  ? 20.478 -1.596  8.125  1.00 22.93 ? 52  THR   A C   1 
ATOM   359  O  O   . THR   A 1 46  ? 19.545 -1.806  8.891  1.00 23.41 ? 52  THR   A O   1 
ATOM   360  C  CB  . THR   A 1 46  ? 21.512 -3.881  7.880  1.00 29.41 ? 52  THR   A CB  1 
ATOM   361  O  OG1 . THR   A 1 46  ? 22.800 -4.505  7.706  1.00 32.13 ? 52  THR   A OG1 1 
ATOM   362  C  CG2 . THR   A 1 46  ? 20.647 -4.032  6.617  1.00 32.30 ? 52  THR   A CG2 1 
ATOM   363  N  N   . ILE   A 1 47  ? 20.397 -0.715  7.106  1.00 20.48 ? 53  ILE   A N   1 
ATOM   364  C  CA  . ILE   A 1 47  ? 19.210 0.097   6.904  1.00 19.10 ? 53  ILE   A CA  1 
ATOM   365  C  C   . ILE   A 1 47  ? 18.193 -0.640  6.013  1.00 18.86 ? 53  ILE   A C   1 
ATOM   366  O  O   . ILE   A 1 47  ? 18.549 -1.208  4.969  1.00 18.91 ? 53  ILE   A O   1 
ATOM   367  C  CB  . ILE   A 1 47  ? 19.554 1.500   6.321  1.00 18.34 ? 53  ILE   A CB  1 
ATOM   368  C  CG1 . ILE   A 1 47  ? 20.634 2.244   7.147  1.00 17.74 ? 53  ILE   A CG1 1 
ATOM   369  C  CG2 . ILE   A 1 47  ? 18.280 2.372   6.158  1.00 17.62 ? 53  ILE   A CG2 1 
ATOM   370  C  CD1 . ILE   A 1 47  ? 20.237 2.574   8.565  1.00 17.79 ? 53  ILE   A CD1 1 
ATOM   371  N  N   . ALA   A 1 48  ? 16.934 -0.598  6.408  1.00 18.09 ? 54  ALA   A N   1 
ATOM   372  C  CA  . ALA   A 1 48  ? 15.842 -1.195  5.635  1.00 18.48 ? 54  ALA   A CA  1 
ATOM   373  C  C   . ALA   A 1 48  ? 15.619 -0.369  4.342  1.00 18.76 ? 54  ALA   A C   1 
ATOM   374  O  O   . ALA   A 1 48  ? 15.644 0.858   4.378  1.00 18.50 ? 54  ALA   A O   1 
ATOM   375  C  CB  . ALA   A 1 48  ? 14.563 -1.159  6.472  1.00 18.55 ? 54  ALA   A CB  1 
ATOM   376  N  N   . ARG   A 1 49  ? 15.362 -1.026  3.206  1.00 19.98 ? 55  ARG   A N   1 
ATOM   377  C  CA  . ARG   A 1 49  ? 15.025 -0.323  1.960  1.00 21.72 ? 55  ARG   A CA  1 
ATOM   378  C  C   . ARG   A 1 49  ? 13.711 -0.980  1.499  1.00 24.38 ? 55  ARG   A C   1 
ATOM   379  O  O   . ARG   A 1 49  ? 13.742 -2.034  0.856  1.00 25.02 ? 55  ARG   A O   1 
ATOM   380  C  CB  . ARG   A 1 49  ? 16.181 -0.450  0.934  1.00 23.73 ? 55  ARG   A CB  1 
ATOM   381  C  CG  . ARG   A 1 49  ? 17.553 0.032   1.467  1.00 24.97 ? 55  ARG   A CG  1 
ATOM   382  C  CD  . ARG   A 1 49  ? 17.647 1.549   1.698  1.00 26.93 ? 55  ARG   A CD  1 
ATOM   383  N  NE  . ARG   A 1 49  ? 18.960 1.955   2.221  1.00 25.14 ? 55  ARG   A NE  1 
ATOM   384  C  CZ  . ARG   A 1 49  ? 19.200 3.112   2.839  1.00 27.23 ? 55  ARG   A CZ  1 
ATOM   385  N  NH1 . ARG   A 1 49  ? 18.221 3.981   3.040  1.00 26.74 ? 55  ARG   A NH1 1 
ATOM   386  N  NH2 . ARG   A 1 49  ? 20.408 3.382   3.313  1.00 27.56 ? 55  ARG   A NH2 1 
ATOM   387  N  N   . CYS   A 1 50  ? 12.556 -0.413  1.938  1.00 25.87 ? 56  CYS   A N   1 
ATOM   388  C  CA  . CYS   A 1 50  ? 11.200 -0.998  1.809  1.00 26.36 ? 56  CYS   A CA  1 
ATOM   389  C  C   . CYS   A 1 50  ? 10.100 0.041   2.133  1.00 26.66 ? 56  CYS   A C   1 
ATOM   390  O  O   . CYS   A 1 50  ? 10.398 1.172   2.531  1.00 26.49 ? 56  CYS   A O   1 
ATOM   391  C  CB  . CYS   A 1 50  ? 11.109 -2.132  2.828  1.00 26.69 ? 56  CYS   A CB  1 
ATOM   392  S  SG  . CYS   A 1 50  ? 11.155 -1.532  4.545  1.00 25.76 ? 56  CYS   A SG  1 
ATOM   393  N  N   . ASP   A 1 51  ? 8.798  -0.407  2.093  1.00 27.15 ? 57  ASP   A N   1 
ATOM   394  C  CA  . ASP   A 1 51  ? 7.702  0.446   2.562  1.00 28.10 ? 57  ASP   A CA  1 
ATOM   395  C  C   . ASP   A 1 51  ? 6.881  -0.309  3.608  1.00 27.76 ? 57  ASP   A C   1 
ATOM   396  O  O   . ASP   A 1 51  ? 5.661  -0.148  3.684  1.00 28.03 ? 57  ASP   A O   1 
ATOM   397  C  CB  . ASP   A 1 51  ? 6.807  1.020   1.443  1.00 32.75 ? 57  ASP   A CB  1 
ATOM   398  C  CG  . ASP   A 1 51  ? 6.122  -0.002  0.587  1.00 42.54 ? 57  ASP   A CG  1 
ATOM   399  O  OD1 . ASP   A 1 51  ? 6.325  -1.232  0.837  1.00 44.42 ? 57  ASP   A OD1 1 
ATOM   400  O  OD2 . ASP   A 1 51  ? 5.381  0.409   -0.345 1.00 46.13 ? 57  ASP   A OD2 1 
ATOM   401  N  N   . CYS   A 1 52  ? 7.565  -1.099  4.469  1.00 25.51 ? 58  CYS   A N   1 
ATOM   402  C  CA  . CYS   A 1 52  ? 6.909  -1.789  5.576  1.00 22.79 ? 58  CYS   A CA  1 
ATOM   403  C  C   . CYS   A 1 52  ? 6.150  -0.805  6.468  1.00 20.28 ? 58  CYS   A C   1 
ATOM   404  O  O   . CYS   A 1 52  ? 6.577  0.339   6.666  1.00 19.04 ? 58  CYS   A O   1 
ATOM   405  C  CB  . CYS   A 1 52  ? 7.937  -2.551  6.414  1.00 23.38 ? 58  CYS   A CB  1 
ATOM   406  S  SG  . CYS   A 1 52  ? 8.427  -4.164  5.748  1.00 23.61 ? 58  CYS   A SG  1 
ATOM   407  N  N   . GLN   A 1 53  ? 5.015  -1.276  7.004  1.00 19.27 ? 59  GLN   A N   1 
ATOM   408  C  CA  . GLN   A 1 53  ? 4.261  -0.552  7.985  1.00 18.34 ? 59  GLN   A CA  1 
ATOM   409  C  C   . GLN   A 1 53  ? 4.097  -1.370  9.273  1.00 17.49 ? 59  GLN   A C   1 
ATOM   410  O  O   . GLN   A 1 53  ? 3.269  -0.996  10.084 1.00 18.22 ? 59  GLN   A O   1 
ATOM   411  C  CB  . GLN   A 1 53  ? 2.908  -0.053  7.445  1.00 21.02 ? 59  GLN   A CB  1 
ATOM   412  C  CG  . GLN   A 1 53  ? 3.052  1.114   6.494  1.00 26.79 ? 59  GLN   A CG  1 
ATOM   413  C  CD  . GLN   A 1 53  ? 1.675  1.659   6.137  1.00 30.94 ? 59  GLN   A CD  1 
ATOM   414  O  OE1 . GLN   A 1 53  ? 1.176  1.498   5.014  1.00 32.30 ? 59  GLN   A OE1 1 
ATOM   415  N  NE2 . GLN   A 1 53  ? 1.009  2.289   7.106  1.00 31.17 ? 59  GLN   A NE2 1 
ATOM   416  N  N   . THR   A 1 54  ? 4.867  -2.476  9.459  1.00 15.74 ? 60  THR   A N   1 
ATOM   417  C  CA  . THR   A 1 54  ? 4.887  -3.220  10.715 1.00 16.27 ? 60  THR   A CA  1 
ATOM   418  C  C   . THR   A 1 54  ? 6.335  -3.454  11.097 1.00 15.74 ? 60  THR   A C   1 
ATOM   419  O  O   . THR   A 1 54  ? 7.191  -3.672  10.242 1.00 17.22 ? 60  THR   A O   1 
ATOM   420  C  CB  . THR   A 1 54  ? 4.111  -4.524  10.656 1.00 18.82 ? 60  THR   A CB  1 
ATOM   421  O  OG1 . THR   A 1 54  ? 4.719  -5.367  9.679  1.00 23.11 ? 60  THR   A OG1 1 
ATOM   422  C  CG2 . THR   A 1 54  ? 2.664  -4.299  10.274 1.00 18.96 ? 60  THR   A CG2 1 
ATOM   423  N  N   . GLY   A 1 55  ? 6.597  -3.412  12.391 1.00 14.08 ? 61  GLY   A N   1 
ATOM   424  C  CA  . GLY   A 1 55  ? 7.948  -3.634  12.885 1.00 13.54 ? 61  GLY   A CA  1 
ATOM   425  C  C   . GLY   A 1 55  ? 7.961  -3.735  14.399 1.00 13.39 ? 61  GLY   A C   1 
ATOM   426  O  O   . GLY   A 1 55  ? 6.933  -4.000  15.022 1.00 14.69 ? 61  GLY   A O   1 
ATOM   427  N  N   . VAL   A 1 56  ? 9.138  -3.548  14.980 1.00 12.22 ? 62  VAL   A N   1 
ATOM   428  C  CA  . VAL   A 1 56  ? 9.335  -3.659  16.420 1.00 12.29 ? 62  VAL   A CA  1 
ATOM   429  C  C   . VAL   A 1 56  ? 10.198 -2.492  16.868 1.00 11.61 ? 62  VAL   A C   1 
ATOM   430  O  O   . VAL   A 1 56  ? 11.198 -2.199  16.209 1.00 12.29 ? 62  VAL   A O   1 
ATOM   431  C  CB  . VAL   A 1 56  ? 10.011 -5.009  16.754 1.00 14.26 ? 62  VAL   A CB  1 
ATOM   432  C  CG1 . VAL   A 1 56  ? 10.358 -5.098  18.220 1.00 15.19 ? 62  VAL   A CG1 1 
ATOM   433  C  CG2 . VAL   A 1 56  ? 9.141  -6.194  16.347 1.00 14.60 ? 62  VAL   A CG2 1 
ATOM   434  N  N   . TYR   A 1 57  ? 9.853  -1.833  17.987 1.00 11.38 ? 63  TYR   A N   1 
ATOM   435  C  CA  . TYR   A 1 57  ? 10.678 -0.718  18.476 1.00 11.13 ? 63  TYR   A CA  1 
ATOM   436  C  C   . TYR   A 1 57  ? 11.174 -0.945  19.896 1.00 11.84 ? 63  TYR   A C   1 
ATOM   437  O  O   . TYR   A 1 57  ? 10.502 -1.642  20.647 1.00 12.72 ? 63  TYR   A O   1 
ATOM   438  C  CB  . TYR   A 1 57  ? 9.984  0.669   18.380 1.00 11.27 ? 63  TYR   A CB  1 
ATOM   439  C  CG  . TYR   A 1 57  ? 9.025  1.008   19.506 1.00 12.68 ? 63  TYR   A CG  1 
ATOM   440  C  CD1 . TYR   A 1 57  ? 7.750  0.460   19.545 1.00 14.31 ? 63  TYR   A CD1 1 
ATOM   441  C  CD2 . TYR   A 1 57  ? 9.371  1.920   20.500 1.00 12.54 ? 63  TYR   A CD2 1 
ATOM   442  C  CE1 . TYR   A 1 57  ? 6.830  0.829   20.532 1.00 14.04 ? 63  TYR   A CE1 1 
ATOM   443  C  CE2 . TYR   A 1 57  ? 8.467  2.285   21.503 1.00 13.49 ? 63  TYR   A CE2 1 
ATOM   444  C  CZ  . TYR   A 1 57  ? 7.206  1.715   21.531 1.00 14.68 ? 63  TYR   A CZ  1 
ATOM   445  O  OH  . TYR   A 1 57  ? 6.295  2.046   22.524 1.00 16.56 ? 63  TYR   A OH  1 
ATOM   446  N  N   . TYR   A 1 58  ? 12.317 -0.330  20.263 1.00 11.61 ? 64  TYR   A N   1 
ATOM   447  C  CA  . TYR   A 1 58  ? 12.851 -0.467  21.606 1.00 11.51 ? 64  TYR   A CA  1 
ATOM   448  C  C   . TYR   A 1 58  ? 12.401 0.714   22.448 1.00 12.54 ? 64  TYR   A C   1 
ATOM   449  O  O   . TYR   A 1 58  ? 12.651 1.873   22.080 1.00 12.20 ? 64  TYR   A O   1 
ATOM   450  C  CB  . TYR   A 1 58  ? 14.395 -0.585  21.644 1.00 12.12 ? 64  TYR   A CB  1 
ATOM   451  C  CG  . TYR   A 1 58  ? 14.881 -0.722  23.070 1.00 13.63 ? 64  TYR   A CG  1 
ATOM   452  C  CD1 . TYR   A 1 58  ? 14.511 -1.804  23.845 1.00 14.68 ? 64  TYR   A CD1 1 
ATOM   453  C  CD2 . TYR   A 1 58  ? 15.672 0.260   23.653 1.00 15.20 ? 64  TYR   A CD2 1 
ATOM   454  C  CE1 . TYR   A 1 58  ? 14.986 -1.948  25.146 1.00 15.61 ? 64  TYR   A CE1 1 
ATOM   455  C  CE2 . TYR   A 1 58  ? 16.104 0.161   24.961 1.00 16.29 ? 64  TYR   A CE2 1 
ATOM   456  C  CZ  . TYR   A 1 58  ? 15.764 -0.943  25.708 1.00 17.46 ? 64  TYR   A CZ  1 
ATOM   457  O  OH  . TYR   A 1 58  ? 16.225 -1.013  27.001 1.00 19.61 ? 64  TYR   A OH  1 
ATOM   458  N  N   . CYS   A 1 59  ? 11.793 0.389   23.626 1.00 12.88 ? 65  CYS   A N   1 
ATOM   459  C  CA  . CYS   A 1 59  ? 11.301 1.383   24.599 1.00 13.50 ? 65  CYS   A CA  1 
ATOM   460  C  C   . CYS   A 1 59  ? 12.143 1.324   25.902 1.00 13.90 ? 65  CYS   A C   1 
ATOM   461  O  O   . CYS   A 1 59  ? 11.942 0.432   26.740 1.00 14.60 ? 65  CYS   A O   1 
ATOM   462  C  CB  . CYS   A 1 59  ? 9.820  1.136   24.873 1.00 14.44 ? 65  CYS   A CB  1 
ATOM   463  S  SG  . CYS   A 1 59  ? 9.102  2.229   26.134 1.00 16.41 ? 65  CYS   A SG  1 
ATOM   464  N  N   . SER   A 1 60  ? 13.121 2.231   26.047 1.00 13.83 ? 66  SER   A N   1 
ATOM   465  C  CA  . SER   A 1 60  ? 14.016 2.173   27.206 1.00 15.70 ? 66  SER   A CA  1 
ATOM   466  C  C   . SER   A 1 60  ? 13.270 2.344   28.540 1.00 16.23 ? 66  SER   A C   1 
ATOM   467  O  O   . SER   A 1 60  ? 13.709 1.781   29.561 1.00 17.64 ? 66  SER   A O   1 
ATOM   468  C  CB  . SER   A 1 60  ? 15.140 3.205   27.109 1.00 18.14 ? 66  SER   A CB  1 
ATOM   469  O  OG  . SER   A 1 60  ? 14.676 4.543   27.187 1.00 20.83 ? 66  SER   A OG  1 
ATOM   470  N  N   . SER   A 1 61  ? 12.192 3.169   28.560 1.00 15.12 ? 67  SER   A N   1 
ATOM   471  C  CA  . SER   A 1 61  ? 11.391 3.400   29.791 1.00 15.92 ? 67  SER   A CA  1 
ATOM   472  C  C   . SER   A 1 61  ? 10.573 2.170   30.259 1.00 15.37 ? 67  SER   A C   1 
ATOM   473  O  O   . SER   A 1 61  ? 9.954  2.202   31.352 1.00 15.34 ? 67  SER   A O   1 
ATOM   474  C  CB  . SER   A 1 61  ? 10.488 4.629   29.648 1.00 16.76 ? 67  SER   A CB  1 
ATOM   475  O  OG  . SER   A 1 61  ? 9.557  4.470   28.583 1.00 17.21 ? 67  SER   A OG  1 
ATOM   476  N  N   . ARG   A 1 62  ? 10.630 1.067   29.473 1.00 14.69 ? 68  ARG   A N   1 
ATOM   477  C  CA  . ARG   A 1 62  ? 10.015 -0.207  29.858 1.00 16.05 ? 68  ARG   A CA  1 
ATOM   478  C  C   . ARG   A 1 62  ? 11.017 -1.382  29.744 1.00 17.56 ? 68  ARG   A C   1 
ATOM   479  O  O   . ARG   A 1 62  ? 10.617 -2.507  30.027 1.00 17.83 ? 68  ARG   A O   1 
ATOM   480  C  CB  . ARG   A 1 62  ? 8.816  -0.509  28.943 1.00 17.36 ? 68  ARG   A CB  1 
ATOM   481  C  CG  . ARG   A 1 62  ? 7.672  0.494   29.056 1.00 20.06 ? 68  ARG   A CG  1 
ATOM   482  C  CD  . ARG   A 1 62  ? 6.867  0.228   30.310 1.00 18.22 ? 68  ARG   A CD  1 
ATOM   483  N  NE  . ARG   A 1 62  ? 5.751  1.159   30.497 1.00 18.83 ? 68  ARG   A NE  1 
ATOM   484  C  CZ  . ARG   A 1 62  ? 5.826  2.318   31.155 1.00 19.70 ? 68  ARG   A CZ  1 
ATOM   485  N  NH1 . ARG   A 1 62  ? 6.973  2.709   31.707 1.00 20.77 ? 68  ARG   A NH1 1 
ATOM   486  N  NH2 . ARG   A 1 62  ? 4.753  3.086   31.275 1.00 20.47 ? 68  ARG   A NH2 1 
ATOM   487  N  N   . ARG   A 1 63  ? 12.280 -1.156  29.253 1.00 16.97 ? 69  ARG   A N   1 
ATOM   488  C  CA  . ARG   A 1 63  ? 13.255 -2.213  28.973 1.00 17.87 ? 69  ARG   A CA  1 
ATOM   489  C  C   . ARG   A 1 63  ? 12.611 -3.322  28.113 1.00 18.43 ? 69  ARG   A C   1 
ATOM   490  O  O   . ARG   A 1 63  ? 12.777 -4.510  28.389 1.00 19.83 ? 69  ARG   A O   1 
ATOM   491  C  CB  . ARG   A 1 63  ? 13.894 -2.801  30.223 1.00 19.56 ? 69  ARG   A CB  1 
ATOM   492  C  CG  . ARG   A 1 63  ? 14.719 -1.794  30.970 1.00 21.95 ? 69  ARG   A CG  1 
ATOM   493  C  CD  . ARG   A 1 63  ? 15.592 -2.550  31.946 1.00 24.80 ? 69  ARG   A CD  1 
ATOM   494  N  NE  . ARG   A 1 63  ? 16.341 -1.607  32.774 1.00 27.97 ? 69  ARG   A NE  1 
ATOM   495  C  CZ  . ARG   A 1 63  ? 16.059 -1.340  34.048 1.00 29.08 ? 69  ARG   A CZ  1 
ATOM   496  N  NH1 . ARG   A 1 63  ? 15.027 -1.930  34.649 1.00 28.21 ? 69  ARG   A NH1 1 
ATOM   497  N  NH2 . ARG   A 1 63  ? 16.797 -0.469  34.729 1.00 29.43 ? 69  ARG   A NH2 1 
ATOM   498  N  N   . LYS   A 1 64  ? 11.773 -2.917  27.149 1.00 16.90 ? 70  LYS   A N   1 
ATOM   499  C  CA  . LYS   A 1 64  ? 11.059 -3.879  26.311 1.00 16.51 ? 70  LYS   A CA  1 
ATOM   500  C  C   . LYS   A 1 64  ? 11.021 -3.445  24.856 1.00 16.36 ? 70  LYS   A C   1 
ATOM   501  O  O   . LYS   A 1 64  ? 11.039 -2.247  24.561 1.00 16.11 ? 70  LYS   A O   1 
ATOM   502  C  CB  . LYS   A 1 64  ? 9.608  -4.044  26.780 1.00 19.16 ? 70  LYS   A CB  1 
ATOM   503  C  CG  . LYS   A 1 64  ? 9.470  -4.957  28.012 1.00 26.81 ? 70  LYS   A CG  1 
ATOM   504  C  CD  . LYS   A 1 64  ? 8.018  -5.264  28.348 1.00 36.08 ? 70  LYS   A CD  1 
ATOM   505  C  CE  . LYS   A 1 64  ? 7.927  -6.120  29.593 1.00 42.32 ? 70  LYS   A CE  1 
ATOM   506  N  NZ  . LYS   A 1 64  ? 8.524  -5.442  30.781 1.00 46.63 ? 70  LYS   A NZ  1 
ATOM   507  N  N   . HIS   A 1 65  ? 10.921 -4.442  23.970 1.00 14.08 ? 71  HIS   A N   1 
ATOM   508  C  CA  . HIS   A 1 65  ? 10.729 -4.225  22.539 1.00 14.48 ? 71  HIS   A CA  1 
ATOM   509  C  C   . HIS   A 1 65  ? 9.274  -4.577  22.259 1.00 15.35 ? 71  HIS   A C   1 
ATOM   510  O  O   . HIS   A 1 65  ? 8.813  -5.676  22.665 1.00 17.01 ? 71  HIS   A O   1 
ATOM   511  C  CB  . HIS   A 1 65  ? 11.621 -5.166  21.686 1.00 14.40 ? 71  HIS   A CB  1 
ATOM   512  C  CG  . HIS   A 1 65  ? 13.093 -4.896  21.793 1.00 15.58 ? 71  HIS   A CG  1 
ATOM   513  N  ND1 . HIS   A 1 65  ? 13.791 -4.203  20.802 1.00 19.22 ? 71  HIS   A ND1 1 
ATOM   514  C  CD2 . HIS   A 1 65  ? 13.947 -5.205  22.792 1.00 15.77 ? 71  HIS   A CD2 1 
ATOM   515  C  CE1 . HIS   A 1 65  ? 15.048 -4.139  21.232 1.00 16.82 ? 71  HIS   A CE1 1 
ATOM   516  N  NE2 . HIS   A 1 65  ? 15.193 -4.743  22.411 1.00 17.40 ? 71  HIS   A NE2 1 
ATOM   517  N  N   . TYR   A 1 66  ? 8.558  -3.681  21.543 1.00 13.56 ? 72  TYR   A N   1 
ATOM   518  C  CA  . TYR   A 1 66  ? 7.132  -3.855  21.246 1.00 12.58 ? 72  TYR   A CA  1 
ATOM   519  C  C   . TYR   A 1 66  ? 6.860  -3.945  19.752 1.00 12.30 ? 72  TYR   A C   1 
ATOM   520  O  O   . TYR   A 1 66  ? 7.319  -3.074  19.016 1.00 12.75 ? 72  TYR   A O   1 
ATOM   521  C  CB  . TYR   A 1 66  ? 6.340  -2.623  21.764 1.00 12.73 ? 72  TYR   A CB  1 
ATOM   522  C  CG  . TYR   A 1 66  ? 6.302  -2.477  23.280 1.00 13.36 ? 72  TYR   A CG  1 
ATOM   523  C  CD1 . TYR   A 1 66  ? 5.506  -3.313  24.063 1.00 14.07 ? 72  TYR   A CD1 1 
ATOM   524  C  CD2 . TYR   A 1 66  ? 7.062  -1.513  23.923 1.00 14.65 ? 72  TYR   A CD2 1 
ATOM   525  C  CE1 . TYR   A 1 66  ? 5.458  -3.176  25.447 1.00 16.28 ? 72  TYR   A CE1 1 
ATOM   526  C  CE2 . TYR   A 1 66  ? 6.999  -1.348  25.306 1.00 15.39 ? 72  TYR   A CE2 1 
ATOM   527  C  CZ  . TYR   A 1 66  ? 6.207  -2.190  26.066 1.00 16.77 ? 72  TYR   A CZ  1 
ATOM   528  O  OH  . TYR   A 1 66  ? 6.144  -2.022  27.430 1.00 17.90 ? 72  TYR   A OH  1 
ATOM   529  N  N   . PRO   A 1 67  ? 5.997  -4.880  19.337 1.00 12.50 ? 73  PRO   A N   1 
ATOM   530  C  CA  . PRO   A 1 67  ? 5.596  -4.942  17.913 1.00 12.89 ? 73  PRO   A CA  1 
ATOM   531  C  C   . PRO   A 1 67  ? 4.519  -3.884  17.637 1.00 13.57 ? 73  PRO   A C   1 
ATOM   532  O  O   . PRO   A 1 67  ? 3.589  -3.689  18.477 1.00 13.95 ? 73  PRO   A O   1 
ATOM   533  C  CB  . PRO   A 1 67  ? 5.018  -6.352  17.741 1.00 14.81 ? 73  PRO   A CB  1 
ATOM   534  C  CG  . PRO   A 1 67  ? 4.635  -6.819  19.109 1.00 14.99 ? 73  PRO   A CG  1 
ATOM   535  C  CD  . PRO   A 1 67  ? 5.398  -5.967  20.148 1.00 12.21 ? 73  PRO   A CD  1 
ATOM   536  N  N   . VAL   A 1 68  ? 4.689  -3.149  16.561 1.00 12.54 ? 74  VAL   A N   1 
ATOM   537  C  CA  . VAL   A 1 68  ? 3.759  -2.059  16.244 1.00 13.80 ? 74  VAL   A CA  1 
ATOM   538  C  C   . VAL   A 1 68  ? 3.468  -1.981  14.740 1.00 14.20 ? 74  VAL   A C   1 
ATOM   539  O  O   . VAL   A 1 68  ? 4.320  -2.357  13.907 1.00 13.80 ? 74  VAL   A O   1 
ATOM   540  C  CB  . VAL   A 1 68  ? 4.319  -0.674  16.676 1.00 15.35 ? 74  VAL   A CB  1 
ATOM   541  C  CG1 . VAL   A 1 68  ? 4.343  -0.510  18.183 1.00 16.01 ? 74  VAL   A CG1 1 
ATOM   542  C  CG2 . VAL   A 1 68  ? 5.687  -0.390  16.074 1.00 15.18 ? 74  VAL   A CG2 1 
ATOM   543  N  N   . SER   A 1 69  ? 2.286  -1.429  14.412 1.00 14.40 ? 75  SER   A N   1 
ATOM   544  C  CA  . SER   A 1 69  ? 1.927  -0.984  13.079 1.00 15.24 ? 75  SER   A CA  1 
ATOM   545  C  C   . SER   A 1 69  ? 2.155  0.524   13.084 1.00 14.73 ? 75  SER   A C   1 
ATOM   546  O  O   . SER   A 1 69  ? 1.784  1.193   14.064 1.00 13.58 ? 75  SER   A O   1 
ATOM   547  C  CB  . SER   A 1 69  ? 0.456  -1.255  12.745 1.00 18.90 ? 75  SER   A CB  1 
ATOM   548  O  OG  . SER   A 1 69  ? 0.229  -2.653  12.804 1.00 24.60 ? 75  SER   A OG  1 
ATOM   549  N  N   . PHE   A 1 70  ? 2.745  1.067   12.011 1.00 13.58 ? 76  PHE   A N   1 
ATOM   550  C  CA  . PHE   A 1 70  ? 3.049  2.491   11.949 1.00 14.56 ? 76  PHE   A CA  1 
ATOM   551  C  C   . PHE   A 1 70  ? 2.676  3.129   10.607 1.00 16.73 ? 76  PHE   A C   1 
ATOM   552  O  O   . PHE   A 1 70  ? 2.585  2.445   9.572  1.00 18.30 ? 76  PHE   A O   1 
ATOM   553  C  CB  . PHE   A 1 70  ? 4.539  2.757   12.335 1.00 14.68 ? 76  PHE   A CB  1 
ATOM   554  C  CG  . PHE   A 1 70  ? 5.535  1.982   11.494 1.00 15.01 ? 76  PHE   A CG  1 
ATOM   555  C  CD1 . PHE   A 1 70  ? 5.977  0.734   11.891 1.00 15.92 ? 76  PHE   A CD1 1 
ATOM   556  C  CD2 . PHE   A 1 70  ? 5.999  2.489   10.290 1.00 16.05 ? 76  PHE   A CD2 1 
ATOM   557  C  CE1 . PHE   A 1 70  ? 6.878  0.022   11.114 1.00 17.10 ? 76  PHE   A CE1 1 
ATOM   558  C  CE2 . PHE   A 1 70  ? 6.896  1.764   9.506  1.00 16.75 ? 76  PHE   A CE2 1 
ATOM   559  C  CZ  . PHE   A 1 70  ? 7.342  0.543   9.936  1.00 16.39 ? 76  PHE   A CZ  1 
ATOM   560  N  N   . SER   A 1 71  ? 2.378  4.421   10.636 1.00 16.66 ? 77  SER   A N   1 
ATOM   561  C  CA  . SER   A 1 71  ? 1.946  5.139   9.445  1.00 17.70 ? 77  SER   A CA  1 
ATOM   562  C  C   . SER   A 1 71  ? 3.146  5.410   8.517  1.00 18.45 ? 77  SER   A C   1 
ATOM   563  O  O   . SER   A 1 71  ? 4.295  5.317   8.945  1.00 18.59 ? 77  SER   A O   1 
ATOM   564  C  CB  . SER   A 1 71  ? 1.280  6.463   9.844  1.00 19.83 ? 77  SER   A CB  1 
ATOM   565  O  OG  . SER   A 1 71  ? 2.181  7.323   10.532 1.00 23.21 ? 77  SER   A OG  1 
ATOM   566  N  N   . LYS   A 1 72  ? 2.891  5.734   7.258  1.00 19.84 ? 78  LYS   A N   1 
ATOM   567  C  CA  . LYS   A 1 72  ? 3.966  6.043   6.307  1.00 21.16 ? 78  LYS   A CA  1 
ATOM   568  C  C   . LYS   A 1 72  ? 4.594  7.395   6.661  1.00 22.88 ? 78  LYS   A C   1 
ATOM   569  O  O   . LYS   A 1 72  ? 3.917  8.271   7.232  1.00 23.10 ? 78  LYS   A O   1 
ATOM   570  C  CB  . LYS   A 1 72  ? 3.417  6.032   4.860  1.00 23.08 ? 78  LYS   A CB  1 
ATOM   571  C  CG  . LYS   A 1 72  ? 3.042  4.636   4.373  1.00 27.09 ? 78  LYS   A CG  1 
ATOM   572  C  CD  . LYS   A 1 72  ? 2.880  4.563   2.852  1.00 33.33 ? 78  LYS   A CD  1 
ATOM   573  C  CE  . LYS   A 1 72  ? 2.426  3.194   2.383  1.00 39.23 ? 78  LYS   A CE  1 
ATOM   574  N  NZ  . LYS   A 1 72  ? 2.360  3.137   0.894  1.00 43.75 ? 78  LYS   A NZ  1 
ATOM   575  N  N   . PRO   A 1 73  ? 5.884  7.602   6.316  1.00 23.41 ? 79  PRO   A N   1 
ATOM   576  C  CA  . PRO   A 1 73  ? 6.538  8.874   6.679  1.00 24.30 ? 79  PRO   A CA  1 
ATOM   577  C  C   . PRO   A 1 73  ? 5.791  10.055  6.069  1.00 25.06 ? 79  PRO   A C   1 
ATOM   578  O  O   . PRO   A 1 73  ? 5.459  10.018  4.884  1.00 24.92 ? 79  PRO   A O   1 
ATOM   579  C  CB  . PRO   A 1 73  ? 7.945  8.769   6.066  1.00 25.59 ? 79  PRO   A CB  1 
ATOM   580  C  CG  . PRO   A 1 73  ? 8.132  7.361   5.724  1.00 26.66 ? 79  PRO   A CG  1 
ATOM   581  C  CD  . PRO   A 1 73  ? 6.812  6.665   5.648  1.00 23.82 ? 79  PRO   A CD  1 
ATOM   582  N  N   . SER   A 1 74  ? 5.456  11.037  6.898  1.00 25.37 ? 80  SER   A N   1 
ATOM   583  C  CA  . SER   A 1 74  ? 4.693  12.187  6.437  1.00 27.65 ? 80  SER   A CA  1 
ATOM   584  C  C   . SER   A 1 74  ? 5.072  13.466  7.213  1.00 27.64 ? 80  SER   A C   1 
ATOM   585  O  O   . SER   A 1 74  ? 5.849  13.429  8.167  1.00 27.50 ? 80  SER   A O   1 
ATOM   586  C  CB  . SER   A 1 74  ? 3.192  11.912  6.628  1.00 31.39 ? 80  SER   A CB  1 
ATOM   587  O  OG  . SER   A 1 74  ? 2.774  10.685  6.061  1.00 37.99 ? 80  SER   A OG  1 
ATOM   588  N  N   . LEU   A 1 75  ? 4.473  14.590  6.819  1.00 28.25 ? 81  LEU   A N   1 
ATOM   589  C  CA  . LEU   A 1 75  ? 4.649  15.871  7.489  1.00 29.78 ? 81  LEU   A CA  1 
ATOM   590  C  C   . LEU   A 1 75  ? 3.540  15.902  8.567  1.00 31.61 ? 81  LEU   A C   1 
ATOM   591  O  O   . LEU   A 1 75  ? 2.364  15.925  8.225  1.00 33.10 ? 81  LEU   A O   1 
ATOM   592  C  CB  . LEU   A 1 75  ? 4.422  16.987  6.448  1.00 29.89 ? 81  LEU   A CB  1 
ATOM   593  C  CG  . LEU   A 1 75  ? 4.672  18.392  6.908  1.00 32.57 ? 81  LEU   A CG  1 
ATOM   594  C  CD1 . LEU   A 1 75  ? 6.156  18.606  7.278  1.00 33.17 ? 81  LEU   A CD1 1 
ATOM   595  C  CD2 . LEU   A 1 75  ? 4.217  19.400  5.818  1.00 32.94 ? 81  LEU   A CD2 1 
ATOM   596  N  N   . ILE   A 1 76  ? 3.903  15.864  9.855  1.00 31.69 ? 82  ILE   A N   1 
ATOM   597  C  CA  . ILE   A 1 76  ? 2.953  15.794  10.974 1.00 31.89 ? 82  ILE   A CA  1 
ATOM   598  C  C   . ILE   A 1 76  ? 3.146  16.902  12.003 1.00 32.36 ? 82  ILE   A C   1 
ATOM   599  O  O   . ILE   A 1 76  ? 4.287  17.183  12.380 1.00 32.41 ? 82  ILE   A O   1 
ATOM   600  C  CB  . ILE   A 1 76  ? 3.146  14.423  11.689 1.00 32.28 ? 82  ILE   A CB  1 
ATOM   601  C  CG1 . ILE   A 1 76  ? 2.923  13.256  10.724 1.00 33.29 ? 82  ILE   A CG1 1 
ATOM   602  C  CG2 . ILE   A 1 76  ? 2.240  14.315  12.925 1.00 32.50 ? 82  ILE   A CG2 1 
ATOM   603  C  CD1 . ILE   A 1 76  ? 3.170  11.910  11.324 1.00 34.41 ? 82  ILE   A CD1 1 
ATOM   604  N  N   . PHE   A 1 77  ? 2.038  17.480  12.520 1.00 33.12 ? 83  PHE   A N   1 
ATOM   605  C  CA  . PHE   A 1 77  ? 2.150  18.495  13.551 1.00 34.00 ? 83  PHE   A CA  1 
ATOM   606  C  C   . PHE   A 1 77  ? 2.529  17.851  14.876 1.00 33.09 ? 83  PHE   A C   1 
ATOM   607  O  O   . PHE   A 1 77  ? 1.909  16.868  15.303 1.00 34.26 ? 83  PHE   A O   1 
ATOM   608  C  CB  . PHE   A 1 77  ? 0.851  19.283  13.719 1.00 35.61 ? 83  PHE   A CB  1 
ATOM   609  C  CG  . PHE   A 1 77  ? 1.052  20.533  14.535 1.00 38.57 ? 83  PHE   A CG  1 
ATOM   610  C  CD1 . PHE   A 1 77  ? 1.632  21.649  13.978 1.00 40.54 ? 83  PHE   A CD1 1 
ATOM   611  C  CD2 . PHE   A 1 77  ? 0.645  20.590  15.860 1.00 40.19 ? 83  PHE   A CD2 1 
ATOM   612  C  CE1 . PHE   A 1 77  ? 1.805  22.802  14.722 1.00 41.81 ? 83  PHE   A CE1 1 
ATOM   613  C  CE2 . PHE   A 1 77  ? 0.825  21.741  16.603 1.00 41.01 ? 83  PHE   A CE2 1 
ATOM   614  C  CZ  . PHE   A 1 77  ? 1.401  22.837  16.029 1.00 41.33 ? 83  PHE   A CZ  1 
ATOM   615  N  N   . VAL   A 1 78  ? 3.582  18.380  15.504 1.00 31.01 ? 84  VAL   A N   1 
ATOM   616  C  CA  . VAL   A 1 78  ? 4.070  17.893  16.778 1.00 30.34 ? 84  VAL   A CA  1 
ATOM   617  C  C   . VAL   A 1 78  ? 3.955  18.999  17.819 1.00 31.47 ? 84  VAL   A C   1 
ATOM   618  O  O   . VAL   A 1 78  ? 4.437  20.106  17.588 1.00 31.27 ? 84  VAL   A O   1 
ATOM   619  C  CB  . VAL   A 1 78  ? 5.519  17.383  16.654 1.00 29.32 ? 84  VAL   A CB  1 
ATOM   620  C  CG1 . VAL   A 1 78  ? 6.020  16.825  17.980 1.00 29.84 ? 84  VAL   A CG1 1 
ATOM   621  C  CG2 . VAL   A 1 78  ? 5.650  16.353  15.530 1.00 28.04 ? 84  VAL   A CG2 1 
ATOM   622  N  N   . GLU   A 1 79  ? 3.371  18.684  18.984 1.00 32.62 ? 85  GLU   A N   1 
ATOM   623  C  CA  . GLU   A 1 79  ? 3.231  19.645  20.081 1.00 33.96 ? 85  GLU   A CA  1 
ATOM   624  C  C   . GLU   A 1 79  ? 4.595  20.137  20.568 1.00 34.62 ? 85  GLU   A C   1 
ATOM   625  O  O   . GLU   A 1 79  ? 5.607  19.446  20.393 1.00 34.86 ? 85  GLU   A O   1 
ATOM   626  C  CB  . GLU   A 1 79  ? 2.468  19.016  21.264 1.00 37.35 ? 85  GLU   A CB  1 
ATOM   627  C  CG  . GLU   A 1 79  ? 0.987  18.784  21.019 1.00 43.91 ? 85  GLU   A CG  1 
ATOM   628  C  CD  . GLU   A 1 79  ? 0.219  20.008  20.562 1.00 53.20 ? 85  GLU   A CD  1 
ATOM   629  O  OE1 . GLU   A 1 79  ? 0.485  21.121  21.075 1.00 55.88 ? 85  GLU   A OE1 1 
ATOM   630  O  OE2 . GLU   A 1 79  ? -0.643 19.854  19.669 1.00 55.86 ? 85  GLU   A OE2 1 
ATOM   631  N  N   . ALA   A 1 80  ? 4.615  21.308  21.227 1.00 34.71 ? 86  ALA   A N   1 
ATOM   632  C  CA  . ALA   A 1 80  ? 5.838  21.875  21.769 1.00 35.15 ? 86  ALA   A CA  1 
ATOM   633  C  C   . ALA   A 1 80  ? 6.441  20.957  22.805 1.00 35.36 ? 86  ALA   A C   1 
ATOM   634  O  O   . ALA   A 1 80  ? 5.732  20.265  23.550 1.00 34.93 ? 86  ALA   A O   1 
ATOM   635  C  CB  . ALA   A 1 80  ? 5.562  23.239  22.394 1.00 35.23 ? 86  ALA   A CB  1 
ATOM   636  N  N   . SER   A 1 81  ? 7.763  20.931  22.826 1.00 35.75 ? 87  SER   A N   1 
ATOM   637  C  CA  . SER   A 1 81  ? 8.502  20.119  23.778 1.00 36.74 ? 87  SER   A CA  1 
ATOM   638  C  C   . SER   A 1 81  ? 9.673  20.962  24.321 1.00 37.12 ? 87  SER   A C   1 
ATOM   639  O  O   . SER   A 1 81  ? 9.827  22.147  23.967 1.00 36.68 ? 87  SER   A O   1 
ATOM   640  C  CB  . SER   A 1 81  ? 9.021  18.856  23.089 1.00 37.76 ? 87  SER   A CB  1 
ATOM   641  O  OG  . SER   A 1 81  ? 9.829  19.227  21.982 1.00 40.58 ? 87  SER   A OG  1 
ATOM   642  N  N   . GLU   A 1 82  ? 10.477 20.370  25.213 1.00 37.81 ? 88  GLU   A N   1 
ATOM   643  C  CA  . GLU   A 1 82  ? 11.654 21.047  25.762 1.00 38.57 ? 88  GLU   A CA  1 
ATOM   644  C  C   . GLU   A 1 82  ? 12.660 21.417  24.632 1.00 37.69 ? 88  GLU   A C   1 
ATOM   645  O  O   . GLU   A 1 82  ? 13.349 22.441  24.723 1.00 37.82 ? 88  GLU   A O   1 
ATOM   646  C  CB  . GLU   A 1 82  ? 12.346 20.107  26.768 1.00 42.95 ? 88  GLU   A CB  1 
ATOM   647  C  CG  . GLU   A 1 82  ? 13.493 20.753  27.522 1.00 52.38 ? 88  GLU   A CG  1 
ATOM   648  C  CD  . GLU   A 1 82  ? 14.663 19.829  27.808 1.00 62.06 ? 88  GLU   A CD  1 
ATOM   649  O  OE1 . GLU   A 1 82  ? 15.822 20.266  27.605 1.00 64.03 ? 88  GLU   A OE1 1 
ATOM   650  O  OE2 . GLU   A 1 82  ? 14.421 18.672  28.227 1.00 63.93 ? 88  GLU   A OE2 1 
ATOM   651  N  N   . TYR   A 1 83  ? 12.682 20.602  23.537 1.00 36.66 ? 89  TYR   A N   1 
ATOM   652  C  CA  . TYR   A 1 83  ? 13.627 20.694  22.415 1.00 36.18 ? 89  TYR   A CA  1 
ATOM   653  C  C   . TYR   A 1 83  ? 13.155 21.489  21.179 1.00 34.05 ? 89  TYR   A C   1 
ATOM   654  O  O   . TYR   A 1 83  ? 13.984 22.099  20.498 1.00 33.91 ? 89  TYR   A O   1 
ATOM   655  C  CB  . TYR   A 1 83  ? 14.055 19.279  21.970 1.00 37.28 ? 89  TYR   A CB  1 
ATOM   656  C  CG  . TYR   A 1 83  ? 14.125 18.276  23.104 1.00 39.69 ? 89  TYR   A CG  1 
ATOM   657  C  CD1 . TYR   A 1 83  ? 15.133 18.342  24.055 1.00 41.26 ? 89  TYR   A CD1 1 
ATOM   658  C  CD2 . TYR   A 1 83  ? 13.146 17.299  23.258 1.00 41.09 ? 89  TYR   A CD2 1 
ATOM   659  C  CE1 . TYR   A 1 83  ? 15.195 17.433  25.105 1.00 42.59 ? 89  TYR   A CE1 1 
ATOM   660  C  CE2 . TYR   A 1 83  ? 13.177 16.408  24.325 1.00 42.40 ? 89  TYR   A CE2 1 
ATOM   661  C  CZ  . TYR   A 1 83  ? 14.203 16.482  25.250 1.00 43.91 ? 89  TYR   A CZ  1 
ATOM   662  O  OH  . TYR   A 1 83  ? 14.275 15.574  26.284 1.00 46.40 ? 89  TYR   A OH  1 
ATOM   663  N  N   . TYR   A 1 84  ? 11.859 21.440  20.849 1.00 32.74 ? 90  TYR   A N   1 
ATOM   664  C  CA  . TYR   A 1 84  ? 11.342 22.185  19.694 1.00 32.26 ? 90  TYR   A CA  1 
ATOM   665  C  C   . TYR   A 1 84  ? 10.046 22.912  20.053 1.00 33.65 ? 90  TYR   A C   1 
ATOM   666  O  O   . TYR   A 1 84  ? 9.246  22.369  20.817 1.00 33.98 ? 90  TYR   A O   1 
ATOM   667  C  CB  . TYR   A 1 84  ? 11.051 21.257  18.510 1.00 30.33 ? 90  TYR   A CB  1 
ATOM   668  C  CG  . TYR   A 1 84  ? 12.251 20.506  17.977 1.00 28.88 ? 90  TYR   A CG  1 
ATOM   669  C  CD1 . TYR   A 1 84  ? 13.126 21.100  17.074 1.00 28.14 ? 90  TYR   A CD1 1 
ATOM   670  C  CD2 . TYR   A 1 84  ? 12.461 19.174  18.309 1.00 28.76 ? 90  TYR   A CD2 1 
ATOM   671  C  CE1 . TYR   A 1 84  ? 14.203 20.397  16.546 1.00 28.00 ? 90  TYR   A CE1 1 
ATOM   672  C  CE2 . TYR   A 1 84  ? 13.544 18.467  17.806 1.00 28.46 ? 90  TYR   A CE2 1 
ATOM   673  C  CZ  . TYR   A 1 84  ? 14.417 19.080  16.926 1.00 28.54 ? 90  TYR   A CZ  1 
ATOM   674  O  OH  . TYR   A 1 84  ? 15.473 18.368  16.403 1.00 26.54 ? 90  TYR   A OH  1 
ATOM   675  N  N   . PRO   A 1 85  ? 9.749  24.088  19.448 1.00 34.52 ? 91  PRO   A N   1 
ATOM   676  C  CA  . PRO   A 1 85  ? 8.411  24.663  19.653 1.00 35.17 ? 91  PRO   A CA  1 
ATOM   677  C  C   . PRO   A 1 85  ? 7.380  23.757  18.933 1.00 36.51 ? 91  PRO   A C   1 
ATOM   678  O  O   . PRO   A 1 85  ? 7.751  22.736  18.308 1.00 36.67 ? 91  PRO   A O   1 
ATOM   679  C  CB  . PRO   A 1 85  ? 8.519  26.048  19.000 1.00 36.55 ? 91  PRO   A CB  1 
ATOM   680  C  CG  . PRO   A 1 85  ? 9.529  25.876  17.927 1.00 36.63 ? 91  PRO   A CG  1 
ATOM   681  C  CD  . PRO   A 1 85  ? 10.519 24.842  18.430 1.00 34.54 ? 91  PRO   A CD  1 
ATOM   682  N  N   . ALA   A 1 86  ? 6.093  24.100  19.004 1.00 37.18 ? 92  ALA   A N   1 
ATOM   683  C  CA  . ALA   A 1 86  ? 5.053  23.317  18.314 1.00 38.00 ? 92  ALA   A CA  1 
ATOM   684  C  C   . ALA   A 1 86  ? 5.265  23.612  16.835 1.00 38.19 ? 92  ALA   A C   1 
ATOM   685  O  O   . ALA   A 1 86  ? 5.391  24.784  16.458 1.00 39.14 ? 92  ALA   A O   1 
ATOM   686  C  CB  . ALA   A 1 86  ? 3.670  23.787  18.751 1.00 38.53 ? 92  ALA   A CB  1 
ATOM   687  N  N   . ARG   A 1 87  ? 5.461  22.565  16.037 1.00 36.45 ? 93  ARG   A N   1 
ATOM   688  C  CA  . ARG   A 1 87  ? 5.797  22.748  14.628 1.00 34.57 ? 93  ARG   A CA  1 
ATOM   689  C  C   . ARG   A 1 87  ? 5.482  21.468  13.845 1.00 32.50 ? 93  ARG   A C   1 
ATOM   690  O  O   . ARG   A 1 87  ? 5.125  20.443  14.423 1.00 32.47 ? 93  ARG   A O   1 
ATOM   691  C  CB  . ARG   A 1 87  ? 7.321  23.040  14.522 1.00 35.27 ? 93  ARG   A CB  1 
ATOM   692  C  CG  . ARG   A 1 87  ? 8.161  21.866  15.057 1.00 37.03 ? 93  ARG   A CG  1 
ATOM   693  C  CD  . ARG   A 1 87  ? 9.573  21.868  14.523 1.00 37.53 ? 93  ARG   A CD  1 
ATOM   694  N  NE  . ARG   A 1 87  ? 10.212 20.568  14.725 1.00 38.80 ? 93  ARG   A NE  1 
ATOM   695  C  CZ  . ARG   A 1 87  ? 11.460 20.282  14.372 1.00 40.18 ? 93  ARG   A CZ  1 
ATOM   696  N  NH1 . ARG   A 1 87  ? 12.235 21.218  13.827 1.00 39.70 ? 93  ARG   A NH1 1 
ATOM   697  N  NH2 . ARG   A 1 87  ? 11.961 19.070  14.605 1.00 38.41 ? 93  ARG   A NH2 1 
ATOM   698  N  N   . TYR   A 1 88  ? 5.656  21.530  12.529 1.00 30.53 ? 94  TYR   A N   1 
ATOM   699  C  CA  . TYR   A 1 88  ? 5.494  20.396  11.682 1.00 30.11 ? 94  TYR   A CA  1 
ATOM   700  C  C   . TYR   A 1 88  ? 6.853  19.713  11.566 1.00 29.71 ? 94  TYR   A C   1 
ATOM   701  O  O   . TYR   A 1 88  ? 7.854  20.370  11.286 1.00 30.01 ? 94  TYR   A O   1 
ATOM   702  C  CB  . TYR   A 1 88  ? 4.984  20.832  10.315 1.00 30.99 ? 94  TYR   A CB  1 
ATOM   703  C  CG  . TYR   A 1 88  ? 3.483  21.053  10.296 1.00 32.22 ? 94  TYR   A CG  1 
ATOM   704  C  CD1 . TYR   A 1 88  ? 2.605  19.985  10.163 1.00 33.70 ? 94  TYR   A CD1 1 
ATOM   705  C  CD2 . TYR   A 1 88  ? 2.944  22.320  10.458 1.00 33.17 ? 94  TYR   A CD2 1 
ATOM   706  C  CE1 . TYR   A 1 88  ? 1.229  20.175  10.156 1.00 35.18 ? 94  TYR   A CE1 1 
ATOM   707  C  CE2 . TYR   A 1 88  ? 1.568  22.525  10.444 1.00 34.69 ? 94  TYR   A CE2 1 
ATOM   708  C  CZ  . TYR   A 1 88  ? 0.711  21.445  10.316 1.00 37.01 ? 94  TYR   A CZ  1 
ATOM   709  O  OH  . TYR   A 1 88  ? -0.650 21.636  10.310 1.00 40.71 ? 94  TYR   A OH  1 
ATOM   710  N  N   . GLN   A 1 89  ? 6.882  18.395  11.776 1.00 27.76 ? 95  GLN   A N   1 
ATOM   711  C  CA  . GLN   A 1 89  ? 8.083  17.586  11.640 1.00 26.22 ? 95  GLN   A CA  1 
ATOM   712  C  C   . GLN   A 1 89  ? 7.896  16.719  10.389 1.00 25.72 ? 95  GLN   A C   1 
ATOM   713  O  O   . GLN   A 1 89  ? 6.826  16.131  10.202 1.00 26.88 ? 95  GLN   A O   1 
ATOM   714  C  CB  . GLN   A 1 89  ? 8.316  16.723  12.900 1.00 25.19 ? 95  GLN   A CB  1 
ATOM   715  C  CG  . GLN   A 1 89  ? 9.532  15.812  12.780 1.00 24.93 ? 95  GLN   A CG  1 
ATOM   716  C  CD  . GLN   A 1 89  ? 10.128 15.326  14.096 1.00 24.50 ? 95  GLN   A CD  1 
ATOM   717  O  OE1 . GLN   A 1 89  ? 10.143 16.023  15.130 1.00 25.31 ? 95  GLN   A OE1 1 
ATOM   718  N  NE2 . GLN   A 1 89  ? 10.678 14.127  14.067 1.00 24.10 ? 95  GLN   A NE2 1 
ATOM   719  N  N   . SER   A 1 90  ? 8.908  16.663  9.513  1.00 24.71 ? 96  SER   A N   1 
ATOM   720  C  CA  . SER   A 1 90  ? 8.795  15.875  8.294  1.00 24.15 ? 96  SER   A CA  1 
ATOM   721  C  C   . SER   A 1 90  ? 9.372  14.451  8.456  1.00 24.14 ? 96  SER   A C   1 
ATOM   722  O  O   . SER   A 1 90  ? 10.078 14.170  9.436  1.00 24.44 ? 96  SER   A O   1 
ATOM   723  C  CB  . SER   A 1 90  ? 9.491  16.591  7.150  1.00 25.81 ? 96  SER   A CB  1 
ATOM   724  O  OG  . SER   A 1 90  ? 10.882 16.665  7.445  1.00 28.07 ? 96  SER   A OG  1 
ATOM   725  N  N   . HIS   A 1 91  ? 9.035  13.569  7.483  1.00 23.00 ? 97  HIS   A N   1 
ATOM   726  C  CA  . HIS   A 1 91  ? 9.470  12.185  7.403  1.00 22.33 ? 97  HIS   A CA  1 
ATOM   727  C  C   . HIS   A 1 91  ? 9.184  11.440  8.736  1.00 20.63 ? 97  HIS   A C   1 
ATOM   728  O  O   . HIS   A 1 91  ? 9.989  10.598  9.144  1.00 19.93 ? 97  HIS   A O   1 
ATOM   729  C  CB  . HIS   A 1 91  ? 10.966 12.112  6.976  1.00 24.02 ? 97  HIS   A CB  1 
ATOM   730  C  CG  . HIS   A 1 91  ? 11.234 12.771  5.646  1.00 26.58 ? 97  HIS   A CG  1 
ATOM   731  N  ND1 . HIS   A 1 91  ? 11.270 12.036  4.470  1.00 28.16 ? 97  HIS   A ND1 1 
ATOM   732  C  CD2 . HIS   A 1 91  ? 11.433 14.080  5.345  1.00 29.14 ? 97  HIS   A CD2 1 
ATOM   733  C  CE1 . HIS   A 1 91  ? 11.497 12.910  3.500  1.00 29.05 ? 97  HIS   A CE1 1 
ATOM   734  N  NE2 . HIS   A 1 91  ? 11.612 14.152  3.973  1.00 29.65 ? 97  HIS   A NE2 1 
ATOM   735  N  N   . LEU   A 1 92  ? 8.026  11.748  9.368  1.00 19.23 ? 98  LEU   A N   1 
ATOM   736  C  CA  . LEU   A 1 92  ? 7.633  11.175  10.659 1.00 18.91 ? 98  LEU   A CA  1 
ATOM   737  C  C   . LEU   A 1 92  ? 6.548  10.098  10.498 1.00 17.81 ? 98  LEU   A C   1 
ATOM   738  O  O   . LEU   A 1 92  ? 5.647  10.238  9.669  1.00 17.46 ? 98  LEU   A O   1 
ATOM   739  C  CB  . LEU   A 1 92  ? 7.160  12.299  11.602 1.00 18.95 ? 98  LEU   A CB  1 
ATOM   740  C  CG  . LEU   A 1 92  ? 6.815  11.887  13.039 1.00 19.05 ? 98  LEU   A CG  1 
ATOM   741  C  CD1 . LEU   A 1 92  ? 8.051  11.500  13.799 1.00 18.29 ? 98  LEU   A CD1 1 
ATOM   742  C  CD2 . LEU   A 1 92  ? 6.018  13.027  13.801 1.00 19.42 ? 98  LEU   A CD2 1 
ATOM   743  N  N   . MET   A 1 93  ? 6.684  8.990   11.260 1.00 17.06 ? 99  MET   A N   1 
ATOM   744  C  CA  . MET   A 1 93  ? 5.756  7.848   11.267 1.00 16.93 ? 99  MET   A CA  1 
ATOM   745  C  C   . MET   A 1 93  ? 5.194  7.720   12.698 1.00 16.95 ? 99  MET   A C   1 
ATOM   746  O  O   . MET   A 1 93  ? 5.961  7.847   13.654 1.00 18.00 ? 99  MET   A O   1 
ATOM   747  C  CB  . MET   A 1 93  ? 6.546  6.558   10.927 1.00 16.10 ? 99  MET   A CB  1 
ATOM   748  C  CG  . MET   A 1 93  ? 7.215  6.625   9.566  1.00 16.92 ? 99  MET   A CG  1 
ATOM   749  S  SD  . MET   A 1 93  ? 8.340  5.238   9.204  1.00 22.40 ? 99  MET   A SD  1 
ATOM   750  C  CE  . MET   A 1 93  ? 9.567  5.518   10.382 1.00 20.42 ? 99  MET   A CE  1 
ATOM   751  N  N   . LEU   A 1 94  ? 3.910  7.443   12.856 1.00 16.34 ? 100 LEU   A N   1 
ATOM   752  C  CA  . LEU   A 1 94  ? 3.317  7.315   14.201 1.00 16.11 ? 100 LEU   A CA  1 
ATOM   753  C  C   . LEU   A 1 94  ? 2.805  5.901   14.425 1.00 15.31 ? 100 LEU   A C   1 
ATOM   754  O  O   . LEU   A 1 94  ? 2.331  5.251   13.489 1.00 16.25 ? 100 LEU   A O   1 
ATOM   755  C  CB  . LEU   A 1 94  ? 2.108  8.280   14.373 1.00 18.21 ? 100 LEU   A CB  1 
ATOM   756  C  CG  . LEU   A 1 94  ? 2.424  9.773   14.312 1.00 21.78 ? 100 LEU   A CG  1 
ATOM   757  C  CD1 . LEU   A 1 94  ? 1.136  10.610  14.450 1.00 23.83 ? 100 LEU   A CD1 1 
ATOM   758  C  CD2 . LEU   A 1 94  ? 3.420  10.184  15.434 1.00 23.38 ? 100 LEU   A CD2 1 
ATOM   759  N  N   . ALA   A 1 95  ? 2.878  5.465   15.679 1.00 13.66 ? 101 ALA   A N   1 
ATOM   760  C  CA  . ALA   A 1 95  ? 2.355  4.176   16.135 1.00 13.51 ? 101 ALA   A CA  1 
ATOM   761  C  C   . ALA   A 1 95  ? 1.713  4.342   17.533 1.00 14.02 ? 101 ALA   A C   1 
ATOM   762  O  O   . ALA   A 1 95  ? 1.998  5.309   18.243 1.00 14.79 ? 101 ALA   A O   1 
ATOM   763  C  CB  . ALA   A 1 95  ? 3.477  3.143   16.230 1.00 13.41 ? 101 ALA   A CB  1 
ATOM   764  N  N   . VAL   A 1 96  ? 0.865  3.401   17.914 1.00 13.66 ? 102 VAL   A N   1 
ATOM   765  C  CA  . VAL   A 1 96  ? 0.274  3.403   19.245 1.00 14.20 ? 102 VAL   A CA  1 
ATOM   766  C  C   . VAL   A 1 96  ? 1.264  2.680   20.160 1.00 16.22 ? 102 VAL   A C   1 
ATOM   767  O  O   . VAL   A 1 96  ? 1.529  1.471   19.996 1.00 17.20 ? 102 VAL   A O   1 
ATOM   768  C  CB  . VAL   A 1 96  ? -1.115 2.724   19.280 1.00 15.28 ? 102 VAL   A CB  1 
ATOM   769  C  CG1 . VAL   A 1 96  ? -1.613 2.562   20.716 1.00 15.55 ? 102 VAL   A CG1 1 
ATOM   770  C  CG2 . VAL   A 1 96  ? -2.123 3.480   18.408 1.00 16.48 ? 102 VAL   A CG2 1 
ATOM   771  N  N   . GLY   A 1 97  ? 1.803  3.405   21.118 1.00 16.70 ? 103 GLY   A N   1 
ATOM   772  C  CA  . GLY   A 1 97  ? 2.728  2.812   22.072 1.00 17.26 ? 103 GLY   A CA  1 
ATOM   773  C  C   . GLY   A 1 97  ? 3.240  3.786   23.101 1.00 17.29 ? 103 GLY   A C   1 
ATOM   774  O  O   . GLY   A 1 97  ? 3.020  4.992   22.994 1.00 17.40 ? 103 GLY   A O   1 
ATOM   775  N  N   . HIS   A 1 98  ? 3.904  3.233   24.126 1.00 16.85 ? 104 HIS   A N   1 
ATOM   776  C  CA  . HIS   A 1 98  ? 4.433  4.050   25.198 1.00 16.98 ? 104 HIS   A CA  1 
ATOM   777  C  C   . HIS   A 1 98  ? 5.771  4.654   24.779 1.00 16.61 ? 104 HIS   A C   1 
ATOM   778  O  O   . HIS   A 1 98  ? 6.642  3.958   24.262 1.00 17.59 ? 104 HIS   A O   1 
ATOM   779  C  CB  . HIS   A 1 98  ? 4.623  3.225   26.516 1.00 16.13 ? 104 HIS   A CB  1 
ATOM   780  C  CG  . HIS   A 1 98  ? 5.164  4.063   27.643 1.00 18.48 ? 104 HIS   A CG  1 
ATOM   781  N  ND1 . HIS   A 1 98  ? 4.381  5.043   28.250 1.00 18.79 ? 104 HIS   A ND1 1 
ATOM   782  C  CD2 . HIS   A 1 98  ? 6.410  4.134   28.176 1.00 20.22 ? 104 HIS   A CD2 1 
ATOM   783  C  CE1 . HIS   A 1 98  ? 5.167  5.650   29.124 1.00 19.18 ? 104 HIS   A CE1 1 
ATOM   784  N  NE2 . HIS   A 1 98  ? 6.380  5.127   29.137 1.00 20.01 ? 104 HIS   A NE2 1 
ATOM   785  N  N   . SER   A 1 99  ? 5.966  5.890   25.155 1.00 16.11 ? 105 SER   A N   1 
ATOM   786  C  CA  . SER   A 1 99  ? 7.215  6.557   25.008 1.00 16.55 ? 105 SER   A CA  1 
ATOM   787  C  C   . SER   A 1 99  ? 7.252  7.748   25.962 1.00 17.75 ? 105 SER   A C   1 
ATOM   788  O  O   . SER   A 1 99  ? 6.221  8.329   26.288 1.00 18.92 ? 105 SER   A O   1 
ATOM   789  C  CB  . SER   A 1 99  ? 7.490  6.935   23.554 1.00 17.95 ? 105 SER   A CB  1 
ATOM   790  O  OG  . SER   A 1 99  ? 6.679  8.010   23.138 1.00 21.08 ? 105 SER   A OG  1 
ATOM   791  N  N   . GLU   A 1 100 ? 8.458  8.078   26.413 1.00 16.35 ? 106 GLU   A N   1 
ATOM   792  C  CA  . GLU   A 1 100 ? 8.853  9.214   27.249 1.00 17.56 ? 106 GLU   A CA  1 
ATOM   793  C  C   . GLU   A 1 100 ? 10.023 9.931   26.555 1.00 18.58 ? 106 GLU   A C   1 
ATOM   794  O  O   . GLU   A 1 100 ? 10.636 9.380   25.607 1.00 18.47 ? 106 GLU   A O   1 
ATOM   795  C  CB  . GLU   A 1 100 ? 9.221  8.726   28.659 1.00 19.56 ? 106 GLU   A CB  1 
ATOM   796  C  CG  . GLU   A 1 100 ? 8.002  8.105   29.311 1.00 19.63 ? 106 GLU   A CG  1 
ATOM   797  C  CD  . GLU   A 1 100 ? 8.219  7.498   30.689 1.00 23.77 ? 106 GLU   A CD  1 
ATOM   798  O  OE1 . GLU   A 1 100 ? 9.100  7.992   31.421 1.00 26.09 ? 106 GLU   A OE1 1 
ATOM   799  O  OE2 . GLU   A 1 100 ? 7.483  6.556   31.051 1.00 22.88 ? 106 GLU   A OE2 1 
ATOM   800  N  N   . PRO   A 1 101 ? 10.318 11.190  26.914 1.00 19.64 ? 107 PRO   A N   1 
ATOM   801  C  CA  . PRO   A 1 101 ? 11.388 11.923  26.175 1.00 19.86 ? 107 PRO   A CA  1 
ATOM   802  C  C   . PRO   A 1 101 ? 12.720 11.169  26.033 1.00 20.05 ? 107 PRO   A C   1 
ATOM   803  O  O   . PRO   A 1 101 ? 13.350 11.143  24.950 1.00 20.31 ? 107 PRO   A O   1 
ATOM   804  C  CB  . PRO   A 1 101 ? 11.523 13.243  26.983 1.00 21.26 ? 107 PRO   A CB  1 
ATOM   805  C  CG  . PRO   A 1 101 ? 10.169 13.448  27.539 1.00 20.70 ? 107 PRO   A CG  1 
ATOM   806  C  CD  . PRO   A 1 101 ? 9.660  12.055  27.918 1.00 19.36 ? 107 PRO   A CD  1 
ATOM   807  N  N   . GLY   A 1 102 ? 13.130 10.525  27.129 1.00 19.59 ? 108 GLY   A N   1 
ATOM   808  C  CA  . GLY   A 1 102 ? 14.358 9.749   27.166 1.00 18.57 ? 108 GLY   A CA  1 
ATOM   809  C  C   . GLY   A 1 102 ? 14.354 8.514   26.287 1.00 16.59 ? 108 GLY   A C   1 
ATOM   810  O  O   . GLY   A 1 102 ? 15.403 7.898   26.107 1.00 16.51 ? 108 GLY   A O   1 
ATOM   811  N  N   . ASP   A 1 103 ? 13.179 8.111   25.737 1.00 15.48 ? 109 ASP   A N   1 
ATOM   812  C  CA  . ASP   A 1 103 ? 13.117 6.960   24.812 1.00 14.65 ? 109 ASP   A CA  1 
ATOM   813  C  C   . ASP   A 1 103 ? 13.627 7.323   23.411 1.00 14.73 ? 109 ASP   A C   1 
ATOM   814  O  O   . ASP   A 1 103 ? 13.835 6.433   22.586 1.00 13.55 ? 109 ASP   A O   1 
ATOM   815  C  CB  . ASP   A 1 103 ? 11.704 6.359   24.682 1.00 14.50 ? 109 ASP   A CB  1 
ATOM   816  C  CG  . ASP   A 1 103 ? 11.269 5.708   25.987 1.00 14.65 ? 109 ASP   A CG  1 
ATOM   817  O  OD1 . ASP   A 1 103 ? 12.125 5.084   26.650 1.00 16.87 ? 109 ASP   A OD1 1 
ATOM   818  O  OD2 . ASP   A 1 103 ? 10.099 5.828   26.340 1.00 16.53 ? 109 ASP   A OD2 1 
ATOM   819  N  N   . CYS   A 1 104 ? 13.847 8.622   23.132 1.00 14.84 ? 110 CYS   A N   1 
ATOM   820  C  CA  . CYS   A 1 104 ? 14.376 9.049   21.831 1.00 14.92 ? 110 CYS   A CA  1 
ATOM   821  C  C   . CYS   A 1 104 ? 15.687 8.319   21.534 1.00 14.28 ? 110 CYS   A C   1 
ATOM   822  O  O   . CYS   A 1 104 ? 16.519 8.171   22.427 1.00 15.40 ? 110 CYS   A O   1 
ATOM   823  C  CB  . CYS   A 1 104 ? 14.583 10.563  21.823 1.00 15.55 ? 110 CYS   A CB  1 
ATOM   824  S  SG  . CYS   A 1 104 ? 13.071 11.497  21.576 1.00 18.77 ? 110 CYS   A SG  1 
ATOM   825  N  N   . GLY   A 1 105 ? 15.820 7.823   20.323 1.00 13.15 ? 111 GLY   A N   1 
ATOM   826  C  CA  . GLY   A 1 105 ? 16.991 7.069   19.906 1.00 13.61 ? 111 GLY   A CA  1 
ATOM   827  C  C   . GLY   A 1 105 ? 16.774 5.573   19.836 1.00 13.43 ? 111 GLY   A C   1 
ATOM   828  O  O   . GLY   A 1 105 ? 17.599 4.859   19.255 1.00 14.13 ? 111 GLY   A O   1 
ATOM   829  N  N   . GLY   A 1 106 ? 15.691 5.073   20.428 1.00 12.95 ? 112 GLY   A N   1 
ATOM   830  C  CA  . GLY   A 1 106 ? 15.373 3.657   20.351 1.00 13.06 ? 112 GLY   A CA  1 
ATOM   831  C  C   . GLY   A 1 106 ? 15.093 3.263   18.910 1.00 13.30 ? 112 GLY   A C   1 
ATOM   832  O  O   . GLY   A 1 106 ? 14.438 4.021   18.182 1.00 13.63 ? 112 GLY   A O   1 
ATOM   833  N  N   . ILE   A 1 107 ? 15.620 2.105   18.474 1.00 11.63 ? 113 ILE   A N   1 
ATOM   834  C  CA  . ILE   A 1 107 ? 15.442 1.709   17.082 1.00 12.49 ? 113 ILE   A CA  1 
ATOM   835  C  C   . ILE   A 1 107 ? 14.074 1.087   16.803 1.00 12.11 ? 113 ILE   A C   1 
ATOM   836  O  O   . ILE   A 1 107 ? 13.608 0.243   17.575 1.00 12.57 ? 113 ILE   A O   1 
ATOM   837  C  CB  . ILE   A 1 107 ? 16.604 0.736   16.665 1.00 13.14 ? 113 ILE   A CB  1 
ATOM   838  C  CG1 . ILE   A 1 107 ? 17.917 1.553   16.405 1.00 15.17 ? 113 ILE   A CG1 1 
ATOM   839  C  CG2 . ILE   A 1 107 ? 16.228 -0.104  15.436 1.00 12.93 ? 113 ILE   A CG2 1 
ATOM   840  C  CD1 . ILE   A 1 107 ? 19.042 0.727   16.089 1.00 17.66 ? 113 ILE   A CD1 1 
ATOM   841  N  N   . LEU   A 1 108 ? 13.514 1.431   15.635 1.00 10.16 ? 114 LEU   A N   1 
ATOM   842  C  CA  . LEU   A 1 108 ? 12.358 0.745   15.070 1.00 10.21 ? 114 LEU   A CA  1 
ATOM   843  C  C   . LEU   A 1 108 ? 12.979 -0.104  13.923 1.00 11.79 ? 114 LEU   A C   1 
ATOM   844  O  O   . LEU   A 1 108 ? 13.692 0.461   13.061 1.00 11.51 ? 114 LEU   A O   1 
ATOM   845  C  CB  . LEU   A 1 108 ? 11.410 1.768   14.437 1.00 10.91 ? 114 LEU   A CB  1 
ATOM   846  C  CG  . LEU   A 1 108 ? 10.279 1.219   13.556 1.00 12.92 ? 114 LEU   A CG  1 
ATOM   847  C  CD1 . LEU   A 1 108 ? 9.259  0.400   14.382 1.00 12.87 ? 114 LEU   A CD1 1 
ATOM   848  C  CD2 . LEU   A 1 108 ? 9.530  2.373   12.862 1.00 13.46 ? 114 LEU   A CD2 1 
ATOM   849  N  N   . ARG   A 1 109 ? 12.612 -1.395  13.844 1.00 12.70 ? 115 ARG   A N   1 
ATOM   850  C  CA  . ARG   A 1 109 ? 13.148 -2.257  12.782 1.00 13.21 ? 115 ARG   A CA  1 
ATOM   851  C  C   . ARG   A 1 109 ? 12.067 -3.163  12.188 1.00 14.00 ? 115 ARG   A C   1 
ATOM   852  O  O   . ARG   A 1 109 ? 11.068 -3.518  12.843 1.00 11.39 ? 115 ARG   A O   1 
ATOM   853  C  CB  . ARG   A 1 109 ? 14.297 -3.125  13.310 1.00 14.28 ? 115 ARG   A CB  1 
ATOM   854  C  CG  . ARG   A 1 109 ? 13.896 -4.026  14.481 1.00 14.65 ? 115 ARG   A CG  1 
ATOM   855  C  CD  . ARG   A 1 109 ? 15.113 -4.798  14.996 1.00 16.88 ? 115 ARG   A CD  1 
ATOM   856  N  NE  . ARG   A 1 109 ? 15.951 -3.987  15.889 1.00 17.17 ? 115 ARG   A NE  1 
ATOM   857  C  CZ  . ARG   A 1 109 ? 17.264 -3.793  15.736 1.00 19.43 ? 115 ARG   A CZ  1 
ATOM   858  N  NH1 . ARG   A 1 109 ? 17.901 -4.290  14.675 1.00 18.35 ? 115 ARG   A NH1 1 
ATOM   859  N  NH2 . ARG   A 1 109 ? 17.945 -3.087  16.625 1.00 17.55 ? 115 ARG   A NH2 1 
ATOM   860  N  N   . CYS   A 1 110 ? 12.313 -3.593  10.953 1.00 15.40 ? 116 CYS   A N   1 
ATOM   861  C  CA  . CYS   A 1 110 ? 11.433 -4.531  10.281 1.00 17.81 ? 116 CYS   A CA  1 
ATOM   862  C  C   . CYS   A 1 110 ? 12.276 -5.735  9.758  1.00 21.01 ? 116 CYS   A C   1 
ATOM   863  O  O   . CYS   A 1 110 ? 13.481 -5.863  10.059 1.00 20.55 ? 116 CYS   A O   1 
ATOM   864  C  CB  . CYS   A 1 110 ? 10.720 -3.803  9.144  1.00 19.41 ? 116 CYS   A CB  1 
ATOM   865  S  SG  . CYS   A 1 110 ? 11.829 -3.350  7.783  1.00 19.20 ? 116 CYS   A SG  1 
ATOM   866  N  N   . GLN   A 1 111 ? 11.649 -6.610  8.947  1.00 22.56 ? 117 GLN   A N   1 
ATOM   867  C  CA  . GLN   A 1 111 ? 12.350 -7.744  8.371  1.00 25.57 ? 117 GLN   A CA  1 
ATOM   868  C  C   . GLN   A 1 111 ? 13.550 -7.335  7.459  1.00 26.68 ? 117 GLN   A C   1 
ATOM   869  O  O   . GLN   A 1 111 ? 14.444 -8.147  7.234  1.00 30.20 ? 117 GLN   A O   1 
ATOM   870  C  CB  . GLN   A 1 111 ? 11.350 -8.633  7.598  1.00 27.83 ? 117 GLN   A CB  1 
ATOM   871  C  CG  . GLN   A 1 111 ? 10.894 -8.014  6.290  1.00 32.05 ? 117 GLN   A CG  1 
ATOM   872  C  CD  . GLN   A 1 111 ? 9.863  -8.848  5.585  1.00 39.14 ? 117 GLN   A CD  1 
ATOM   873  O  OE1 . GLN   A 1 111 ? 8.650  -8.738  5.859  1.00 41.20 ? 117 GLN   A OE1 1 
ATOM   874  N  NE2 . GLN   A 1 111 ? 10.320 -9.692  4.670  1.00 39.47 ? 117 GLN   A NE2 1 
ATOM   875  N  N   . HIS   A 1 112 ? 13.580 -6.101  6.952  1.00 24.65 ? 118 HIS   A N   1 
ATOM   876  C  CA  . HIS   A 1 112 ? 14.648 -5.648  6.041  1.00 24.21 ? 118 HIS   A CA  1 
ATOM   877  C  C   . HIS   A 1 112 ? 15.797 -4.901  6.764  1.00 23.99 ? 118 HIS   A C   1 
ATOM   878  O  O   . HIS   A 1 112 ? 16.861 -4.696  6.170  1.00 25.41 ? 118 HIS   A O   1 
ATOM   879  C  CB  . HIS   A 1 112 ? 14.054 -4.752  4.944  1.00 25.87 ? 118 HIS   A CB  1 
ATOM   880  C  CG  . HIS   A 1 112 ? 12.904 -5.371  4.205  1.00 30.20 ? 118 HIS   A CG  1 
ATOM   881  N  ND1 . HIS   A 1 112 ? 11.589 -5.084  4.540  1.00 32.95 ? 118 HIS   A ND1 1 
ATOM   882  C  CD2 . HIS   A 1 112 ? 12.907 -6.214  3.142  1.00 31.87 ? 118 HIS   A CD2 1 
ATOM   883  C  CE1 . HIS   A 1 112 ? 10.836 -5.762  3.688  1.00 33.90 ? 118 HIS   A CE1 1 
ATOM   884  N  NE2 . HIS   A 1 112 ? 11.585 -6.467  2.831  1.00 33.73 ? 118 HIS   A NE2 1 
ATOM   885  N  N   . GLY   A 1 113 ? 15.578 -4.500  8.028  1.00 21.65 ? 119 GLY   A N   1 
ATOM   886  C  CA  . GLY   A 1 113 ? 16.599 -3.791  8.799  1.00 20.27 ? 119 GLY   A CA  1 
ATOM   887  C  C   . GLY   A 1 113 ? 16.046 -2.627  9.607  1.00 17.71 ? 119 GLY   A C   1 
ATOM   888  O  O   . GLY   A 1 113 ? 14.863 -2.608  9.992  1.00 17.69 ? 119 GLY   A O   1 
ATOM   889  N  N   . VAL   A 1 114 ? 16.919 -1.661  9.916  1.00 15.82 ? 120 VAL   A N   1 
ATOM   890  C  CA  . VAL   A 1 114 ? 16.544 -0.483  10.685 1.00 14.44 ? 120 VAL   A CA  1 
ATOM   891  C  C   . VAL   A 1 114 ? 15.681 0.460   9.830  1.00 14.90 ? 120 VAL   A C   1 
ATOM   892  O  O   . VAL   A 1 114 ? 16.095 0.853   8.732  1.00 15.95 ? 120 VAL   A O   1 
ATOM   893  C  CB  . VAL   A 1 114 ? 17.795 0.247   11.252 1.00 14.49 ? 120 VAL   A CB  1 
ATOM   894  C  CG1 . VAL   A 1 114 ? 17.400 1.567   11.894 1.00 14.43 ? 120 VAL   A CG1 1 
ATOM   895  C  CG2 . VAL   A 1 114 ? 18.504 -0.633  12.259 1.00 15.29 ? 120 VAL   A CG2 1 
ATOM   896  N  N   . VAL   A 1 115 ? 14.505 0.818   10.353 1.00 14.42 ? 121 VAL   A N   1 
ATOM   897  C  CA  . VAL   A 1 115 ? 13.543 1.706   9.717  1.00 14.82 ? 121 VAL   A CA  1 
ATOM   898  C  C   . VAL   A 1 115 ? 13.710 3.164   10.168 1.00 14.92 ? 121 VAL   A C   1 
ATOM   899  O  O   . VAL   A 1 115 ? 13.619 4.094   9.363  1.00 16.09 ? 121 VAL   A O   1 
ATOM   900  C  CB  . VAL   A 1 115 ? 12.097 1.236   10.026 1.00 15.83 ? 121 VAL   A CB  1 
ATOM   901  C  CG1 . VAL   A 1 115 ? 11.069 2.228   9.475  1.00 16.97 ? 121 VAL   A CG1 1 
ATOM   902  C  CG2 . VAL   A 1 115 ? 11.846 -0.169  9.522  1.00 15.43 ? 121 VAL   A CG2 1 
ATOM   903  N  N   . GLY   A 1 116 ? 13.970 3.358   11.467 1.00 13.75 ? 122 GLY   A N   1 
ATOM   904  C  CA  . GLY   A 1 116 ? 14.098 4.700   12.017 1.00 14.23 ? 122 GLY   A CA  1 
ATOM   905  C  C   . GLY   A 1 116 ? 14.382 4.705   13.501 1.00 13.98 ? 122 GLY   A C   1 
ATOM   906  O  O   . GLY   A 1 116 ? 14.645 3.643   14.090 1.00 13.67 ? 122 GLY   A O   1 
ATOM   907  N  N   . ILE   A 1 117 ? 14.279 5.893   14.143 1.00 12.50 ? 123 ILE   A N   1 
ATOM   908  C  CA  . ILE   A 1 117 ? 14.521 5.978   15.582 1.00 12.34 ? 123 ILE   A CA  1 
ATOM   909  C  C   . ILE   A 1 117 ? 13.413 6.784   16.246 1.00 12.15 ? 123 ILE   A C   1 
ATOM   910  O  O   . ILE   A 1 117 ? 12.821 7.661   15.615 1.00 10.88 ? 123 ILE   A O   1 
ATOM   911  C  CB  . ILE   A 1 117 ? 15.887 6.616   15.920 1.00 13.15 ? 123 ILE   A CB  1 
ATOM   912  C  CG1 . ILE   A 1 117 ? 16.101 7.920   15.149 1.00 13.98 ? 123 ILE   A CG1 1 
ATOM   913  C  CG2 . ILE   A 1 117 ? 17.024 5.638   15.744 1.00 13.85 ? 123 ILE   A CG2 1 
ATOM   914  C  CD1 . ILE   A 1 117 ? 17.241 8.789   15.753 1.00 16.01 ? 123 ILE   A CD1 1 
ATOM   915  N  N   . VAL   A 1 118 ? 13.091 6.467   17.520 1.00 11.14 ? 124 VAL   A N   1 
ATOM   916  C  CA  . VAL   A 1 118 ? 12.093 7.216   18.261 1.00 11.27 ? 124 VAL   A CA  1 
ATOM   917  C  C   . VAL   A 1 118 ? 12.463 8.712   18.279 1.00 12.70 ? 124 VAL   A C   1 
ATOM   918  O  O   . VAL   A 1 118 ? 13.609 9.035   18.581 1.00 12.83 ? 124 VAL   A O   1 
ATOM   919  C  CB  . VAL   A 1 118 ? 12.016 6.680   19.706 1.00 11.10 ? 124 VAL   A CB  1 
ATOM   920  C  CG1 . VAL   A 1 118 ? 11.130 7.563   20.567 1.00 11.33 ? 124 VAL   A CG1 1 
ATOM   921  C  CG2 . VAL   A 1 118 ? 11.527 5.227   19.715 1.00 12.10 ? 124 VAL   A CG2 1 
ATOM   922  N  N   . SER   A 1 119 ? 11.501 9.589   18.019 1.00 13.78 ? 125 SER   A N   1 
ATOM   923  C  CA  . SER   A 1 119 ? 11.729 11.043  17.955 1.00 15.33 ? 125 SER   A CA  1 
ATOM   924  C  C   . SER   A 1 119 ? 10.650 11.884  18.695 1.00 17.08 ? 125 SER   A C   1 
ATOM   925  O  O   . SER   A 1 119 ? 10.951 12.965  19.194 1.00 17.91 ? 125 SER   A O   1 
ATOM   926  C  CB  . SER   A 1 119 ? 11.816 11.479  16.491 1.00 17.48 ? 125 SER   A CB  1 
ATOM   927  O  OG  . SER   A 1 119 ? 12.060 12.867  16.316 1.00 19.66 ? 125 SER   A OG  1 
ATOM   928  N  N   . THR   A 1 120 ? 9.382  11.433  18.687 1.00 17.39 ? 126 THR   A N   1 
ATOM   929  C  CA  . THR   A 1 120 ? 8.293  12.188  19.308 1.00 19.06 ? 126 THR   A CA  1 
ATOM   930  C  C   . THR   A 1 120 ? 7.387  11.255  20.148 1.00 20.84 ? 126 THR   A C   1 
ATOM   931  O  O   . THR   A 1 120 ? 7.445  10.021  20.008 1.00 20.28 ? 126 THR   A O   1 
ATOM   932  C  CB  . THR   A 1 120 ? 7.428  12.896  18.217 1.00 19.19 ? 126 THR   A CB  1 
ATOM   933  O  OG1 . THR   A 1 120 ? 6.523  11.940  17.627 1.00 20.91 ? 126 THR   A OG1 1 
ATOM   934  C  CG2 . THR   A 1 120 ? 8.233  13.616  17.175 1.00 18.12 ? 126 THR   A CG2 1 
ATOM   935  N  N   . GLY   A 1 121 ? 6.497  11.844  20.927 1.00 21.65 ? 127 GLY   A N   1 
ATOM   936  C  CA  . GLY   A 1 121 ? 5.583  11.041  21.720 1.00 24.16 ? 127 GLY   A CA  1 
ATOM   937  C  C   . GLY   A 1 121 ? 4.680  11.889  22.559 1.00 26.11 ? 127 GLY   A C   1 
ATOM   938  O  O   . GLY   A 1 121 ? 4.901  13.092  22.698 1.00 26.13 ? 127 GLY   A O   1 
ATOM   939  N  N   . GLY   A 1 122 ? 3.732  11.205  23.178 1.00 27.69 ? 128 GLY   A N   1 
ATOM   940  C  CA  . GLY   A 1 122 ? 2.721  11.790  24.043 1.00 28.92 ? 128 GLY   A CA  1 
ATOM   941  C  C   . GLY   A 1 122 ? 1.358  11.195  23.753 1.00 30.68 ? 128 GLY   A C   1 
ATOM   942  O  O   . GLY   A 1 122 ? 1.120  10.695  22.650 1.00 31.75 ? 128 GLY   A O   1 
ATOM   943  N  N   . ASN   A 1 123 ? 0.457  11.215  24.740 1.00 30.59 ? 129 ASN   A N   1 
ATOM   944  C  CA  . ASN   A 1 123 ? -0.928 10.763  24.567 1.00 30.62 ? 129 ASN   A CA  1 
ATOM   945  C  C   . ASN   A 1 123 ? -1.059 9.349   24.003 1.00 28.82 ? 129 ASN   A C   1 
ATOM   946  O  O   . ASN   A 1 123 ? -1.990 9.060   23.239 1.00 29.57 ? 129 ASN   A O   1 
ATOM   947  C  CB  . ASN   A 1 123 ? -1.709 11.760  23.690 1.00 33.15 ? 129 ASN   A CB  1 
ATOM   948  C  CG  . ASN   A 1 123 ? -1.895 13.106  24.346 1.00 38.59 ? 129 ASN   A CG  1 
ATOM   949  O  OD1 . ASN   A 1 123 ? -2.099 13.190  25.564 1.00 41.24 ? 129 ASN   A OD1 1 
ATOM   950  N  ND2 . ASN   A 1 123 ? -1.891 14.172  23.546 1.00 39.46 ? 129 ASN   A ND2 1 
ATOM   951  N  N   . GLY   A 1 124 ? -0.161 8.466   24.414 1.00 26.13 ? 130 GLY   A N   1 
ATOM   952  C  CA  . GLY   A 1 124 ? -0.228 7.079   23.986 1.00 23.89 ? 130 GLY   A CA  1 
ATOM   953  C  C   . GLY   A 1 124 ? 0.265  6.805   22.571 1.00 21.47 ? 130 GLY   A C   1 
ATOM   954  O  O   . GLY   A 1 124 ? 0.099  5.689   22.064 1.00 19.41 ? 130 GLY   A O   1 
ATOM   955  N  N   . LEU   A 1 125 ? 0.906  7.792   21.939 1.00 20.88 ? 131 LEU   A N   1 
ATOM   956  C  CA  . LEU   A 1 125 ? 1.503  7.604   20.611 1.00 21.00 ? 131 LEU   A CA  1 
ATOM   957  C  C   . LEU   A 1 125 ? 3.020  7.724   20.657 1.00 21.20 ? 131 LEU   A C   1 
ATOM   958  O  O   . LEU   A 1 125 ? 3.561  8.478   21.480 1.00 22.64 ? 131 LEU   A O   1 
ATOM   959  C  CB  . LEU   A 1 125 ? 0.993  8.657   19.623 1.00 22.28 ? 131 LEU   A CB  1 
ATOM   960  C  CG  . LEU   A 1 125 ? -0.482 8.676   19.360 1.00 24.39 ? 131 LEU   A CG  1 
ATOM   961  C  CD1 . LEU   A 1 125 ? -0.776 9.717   18.306 1.00 26.34 ? 131 LEU   A CD1 1 
ATOM   962  C  CD2 . LEU   A 1 125 ? -0.964 7.317   18.872 1.00 24.23 ? 131 LEU   A CD2 1 
ATOM   963  N  N   . VAL   A 1 126 ? 3.708  7.026   19.748 1.00 17.74 ? 132 VAL   A N   1 
ATOM   964  C  CA  . VAL   A 1 126 ? 5.148  7.118   19.652 1.00 16.83 ? 132 VAL   A CA  1 
ATOM   965  C  C   . VAL   A 1 126 ? 5.422  7.510   18.153 1.00 17.14 ? 132 VAL   A C   1 
ATOM   966  O  O   . VAL   A 1 126 ? 4.764  6.999   17.250 1.00 18.24 ? 132 VAL   A O   1 
ATOM   967  C  CB  . VAL   A 1 126 ? 5.846  5.804   20.120 1.00 17.54 ? 132 VAL   A CB  1 
ATOM   968  C  CG1 . VAL   A 1 126 ? 5.278  4.574   19.419 1.00 18.75 ? 132 VAL   A CG1 1 
ATOM   969  C  CG2 . VAL   A 1 126 ? 7.365  5.882   19.957 1.00 17.84 ? 132 VAL   A CG2 1 
ATOM   970  N  N   . GLY   A 1 127 ? 6.322  8.459   17.916 1.00 16.38 ? 133 GLY   A N   1 
ATOM   971  C  CA  . GLY   A 1 127 ? 6.675  8.878   16.566 1.00 16.58 ? 133 GLY   A CA  1 
ATOM   972  C  C   . GLY   A 1 127 ? 8.134  8.552   16.286 1.00 16.44 ? 133 GLY   A C   1 
ATOM   973  O  O   . GLY   A 1 127 ? 8.981  8.726   17.183 1.00 15.67 ? 133 GLY   A O   1 
ATOM   974  N  N   . PHE   A 1 128 ? 8.429  8.085   15.049 1.00 15.24 ? 134 PHE   A N   1 
ATOM   975  C  CA  . PHE   A 1 128 ? 9.745  7.634   14.616 1.00 14.59 ? 134 PHE   A CA  1 
ATOM   976  C  C   . PHE   A 1 128 ? 10.241 8.452   13.419 1.00 15.09 ? 134 PHE   A C   1 
ATOM   977  O  O   . PHE   A 1 128 ? 9.497  8.634   12.441 1.00 16.88 ? 134 PHE   A O   1 
ATOM   978  C  CB  . PHE   A 1 128 ? 9.681  6.166   14.197 1.00 13.82 ? 134 PHE   A CB  1 
ATOM   979  C  CG  . PHE   A 1 128 ? 9.058  5.242   15.233 1.00 13.23 ? 134 PHE   A CG  1 
ATOM   980  C  CD1 . PHE   A 1 128 ? 9.819  4.721   16.270 1.00 12.68 ? 134 PHE   A CD1 1 
ATOM   981  C  CD2 . PHE   A 1 128 ? 7.723  4.870   15.142 1.00 14.35 ? 134 PHE   A CD2 1 
ATOM   982  C  CE1 . PHE   A 1 128 ? 9.239  3.847   17.222 1.00 12.73 ? 134 PHE   A CE1 1 
ATOM   983  C  CE2 . PHE   A 1 128 ? 7.158  3.976   16.063 1.00 14.35 ? 134 PHE   A CE2 1 
ATOM   984  C  CZ  . PHE   A 1 128 ? 7.913  3.497   17.116 1.00 12.84 ? 134 PHE   A CZ  1 
ATOM   985  N  N   . ALA   A 1 129 ? 11.492 8.919   13.477 1.00 14.37 ? 135 ALA   A N   1 
ATOM   986  C  CA  . ALA   A 1 129 ? 12.108 9.625   12.345 1.00 15.20 ? 135 ALA   A CA  1 
ATOM   987  C  C   . ALA   A 1 129 ? 12.589 8.561   11.327 1.00 14.98 ? 135 ALA   A C   1 
ATOM   988  O  O   . ALA   A 1 129 ? 13.460 7.758   11.635 1.00 13.61 ? 135 ALA   A O   1 
ATOM   989  C  CB  . ALA   A 1 129 ? 13.303 10.460  12.820 1.00 15.84 ? 135 ALA   A CB  1 
ATOM   990  N  N   . ASP   A 1 130 ? 11.989 8.538   10.115 1.00 14.63 ? 136 ASP   A N   1 
ATOM   991  C  CA  . ASP   A 1 130 ? 12.374 7.559   9.099  1.00 15.30 ? 136 ASP   A CA  1 
ATOM   992  C  C   . ASP   A 1 130 ? 13.819 7.809   8.598  1.00 16.21 ? 136 ASP   A C   1 
ATOM   993  O  O   . ASP   A 1 130 ? 14.268 8.970   8.509  1.00 15.95 ? 136 ASP   A O   1 
ATOM   994  C  CB  . ASP   A 1 130 ? 11.423 7.697   7.889  1.00 17.17 ? 136 ASP   A CB  1 
ATOM   995  C  CG  . ASP   A 1 130 ? 11.678 6.685   6.798  1.00 20.80 ? 136 ASP   A CG  1 
ATOM   996  O  OD1 . ASP   A 1 130 ? 11.698 5.464   7.105  1.00 20.16 ? 136 ASP   A OD1 1 
ATOM   997  O  OD2 . ASP   A 1 130 ? 11.852 7.104   5.629  1.00 22.73 ? 136 ASP   A OD2 1 
ATOM   998  N  N   . VAL   A 1 131 ? 14.534 6.732   8.228  1.00 15.70 ? 137 VAL   A N   1 
ATOM   999  C  CA  . VAL   A 1 131 ? 15.874 6.860   7.620  1.00 15.01 ? 137 VAL   A CA  1 
ATOM   1000 C  C   . VAL   A 1 131 ? 15.977 6.031   6.311  1.00 16.53 ? 137 VAL   A C   1 
ATOM   1001 O  O   . VAL   A 1 131 ? 17.023 6.056   5.688  1.00 16.97 ? 137 VAL   A O   1 
ATOM   1002 C  CB  . VAL   A 1 131 ? 16.994 6.464   8.592  1.00 13.69 ? 137 VAL   A CB  1 
ATOM   1003 C  CG1 . VAL   A 1 131 ? 16.986 7.335   9.851  1.00 13.87 ? 137 VAL   A CG1 1 
ATOM   1004 C  CG2 . VAL   A 1 131 ? 16.935 4.975   8.939  1.00 14.11 ? 137 VAL   A CG2 1 
ATOM   1005 N  N   . ARG   A 1 132 ? 14.895 5.313   5.897  1.00 16.86 ? 138 ARG   A N   1 
ATOM   1006 C  CA  . ARG   A 1 132 ? 14.928 4.437   4.711  1.00 16.49 ? 138 ARG   A CA  1 
ATOM   1007 C  C   . ARG   A 1 132 ? 15.157 5.164   3.363  1.00 19.00 ? 138 ARG   A C   1 
ATOM   1008 O  O   . ARG   A 1 132 ? 15.575 4.521   2.392  1.00 19.64 ? 138 ARG   A O   1 
ATOM   1009 C  CB  . ARG   A 1 132 ? 13.659 3.586   4.633  1.00 16.39 ? 138 ARG   A CB  1 
ATOM   1010 C  CG  . ARG   A 1 132 ? 13.463 2.647   5.843  1.00 14.97 ? 138 ARG   A CG  1 
ATOM   1011 C  CD  . ARG   A 1 132 ? 12.095 1.965   5.702  1.00 19.52 ? 138 ARG   A CD  1 
ATOM   1012 N  NE  . ARG   A 1 132 ? 10.996 2.875   6.059  1.00 17.71 ? 138 ARG   A NE  1 
ATOM   1013 C  CZ  . ARG   A 1 132 ? 9.705  2.529   6.080  1.00 18.09 ? 138 ARG   A CZ  1 
ATOM   1014 N  NH1 . ARG   A 1 132 ? 9.337  1.292   5.775  1.00 17.65 ? 138 ARG   A NH1 1 
ATOM   1015 N  NH2 . ARG   A 1 132 ? 8.779  3.413   6.436  1.00 18.58 ? 138 ARG   A NH2 1 
ATOM   1016 N  N   . ASP   A 1 133 ? 14.844 6.465   3.301  1.00 19.42 ? 139 ASP   A N   1 
ATOM   1017 C  CA  . ASP   A 1 133 ? 15.057 7.247   2.075  1.00 20.42 ? 139 ASP   A CA  1 
ATOM   1018 C  C   . ASP   A 1 133 ? 16.505 7.772   1.933  1.00 20.38 ? 139 ASP   A C   1 
ATOM   1019 O  O   . ASP   A 1 133 ? 16.857 8.278   0.854  1.00 21.11 ? 139 ASP   A O   1 
ATOM   1020 C  CB  . ASP   A 1 133 ? 14.100 8.453   2.018  1.00 23.55 ? 139 ASP   A CB  1 
ATOM   1021 C  CG  . ASP   A 1 133 ? 14.333 9.481   3.112  1.00 27.58 ? 139 ASP   A CG  1 
ATOM   1022 O  OD1 . ASP   A 1 133 ? 14.487 9.076   4.288  1.00 26.67 ? 139 ASP   A OD1 1 
ATOM   1023 O  OD2 . ASP   A 1 133 ? 14.368 10.687  2.797  1.00 29.51 ? 139 ASP   A OD2 1 
ATOM   1024 N  N   . LEU   A 1 134 ? 17.318 7.691   3.012  1.00 19.39 ? 140 LEU   A N   1 
ATOM   1025 C  CA  . LEU   A 1 134 ? 18.702 8.165   3.031  1.00 18.74 ? 140 LEU   A CA  1 
ATOM   1026 C  C   . LEU   A 1 134 ? 19.609 7.093   2.420  1.00 19.17 ? 140 LEU   A C   1 
ATOM   1027 O  O   . LEU   A 1 134 ? 20.338 6.403   3.150  1.00 20.27 ? 140 LEU   A O   1 
ATOM   1028 C  CB  . LEU   A 1 134 ? 19.093 8.479   4.499  1.00 17.54 ? 140 LEU   A CB  1 
ATOM   1029 C  CG  . LEU   A 1 134 ? 18.257 9.574   5.172  1.00 18.75 ? 140 LEU   A CG  1 
ATOM   1030 C  CD1 . LEU   A 1 134 ? 18.700 9.804   6.631  1.00 19.67 ? 140 LEU   A CD1 1 
ATOM   1031 C  CD2 . LEU   A 1 134 ? 18.315 10.905  4.383  1.00 20.20 ? 140 LEU   A CD2 1 
ATOM   1032 N  N   . LEU   A 1 135 ? 19.592 6.966   1.084  1.00 19.07 ? 141 LEU   A N   1 
ATOM   1033 C  CA  . LEU   A 1 135 ? 20.353 5.897   0.432  1.00 19.98 ? 141 LEU   A CA  1 
ATOM   1034 C  C   . LEU   A 1 135 ? 21.882 5.980   0.637  1.00 20.05 ? 141 LEU   A C   1 
ATOM   1035 O  O   . LEU   A 1 135 ? 22.548 4.941   0.653  1.00 22.38 ? 141 LEU   A O   1 
ATOM   1036 C  CB  . LEU   A 1 135 ? 19.993 5.779   -1.082 1.00 20.67 ? 141 LEU   A CB  1 
ATOM   1037 C  CG  . LEU   A 1 135 ? 18.477 5.752   -1.384 1.00 23.38 ? 141 LEU   A CG  1 
ATOM   1038 C  CD1 . LEU   A 1 135 ? 18.217 5.598   -2.875 1.00 25.61 ? 141 LEU   A CD1 1 
ATOM   1039 C  CD2 . LEU   A 1 135 ? 17.740 4.676   -0.610 1.00 23.92 ? 141 LEU   A CD2 1 
ATOM   1040 N  N   . TRP   A 1 136 ? 22.430 7.193   0.771  1.00 18.77 ? 142 TRP   A N   1 
ATOM   1041 C  CA  . TRP   A 1 136 ? 23.871 7.411   0.966  1.00 19.53 ? 142 TRP   A CA  1 
ATOM   1042 C  C   . TRP   A 1 136 ? 24.442 6.815   2.261  1.00 20.76 ? 142 TRP   A C   1 
ATOM   1043 O  O   . TRP   A 1 136 ? 25.669 6.682   2.389  1.00 21.08 ? 142 TRP   A O   1 
ATOM   1044 C  CB  . TRP   A 1 136 ? 24.192 8.909   0.871  1.00 19.34 ? 142 TRP   A CB  1 
ATOM   1045 C  CG  . TRP   A 1 136 ? 23.371 9.755   1.805  1.00 18.76 ? 142 TRP   A CG  1 
ATOM   1046 C  CD1 . TRP   A 1 136 ? 22.230 10.438  1.509  1.00 18.80 ? 142 TRP   A CD1 1 
ATOM   1047 C  CD2 . TRP   A 1 136 ? 23.705 10.099  3.159  1.00 18.92 ? 142 TRP   A CD2 1 
ATOM   1048 N  NE1 . TRP   A 1 136 ? 21.790 11.124  2.619  1.00 19.44 ? 142 TRP   A NE1 1 
ATOM   1049 C  CE2 . TRP   A 1 136 ? 22.672 10.920  3.649  1.00 18.90 ? 142 TRP   A CE2 1 
ATOM   1050 C  CE3 . TRP   A 1 136 ? 24.754 9.752   4.018  1.00 19.28 ? 142 TRP   A CE3 1 
ATOM   1051 C  CZ2 . TRP   A 1 136 ? 22.700 11.461  4.938  1.00 19.72 ? 142 TRP   A CZ2 1 
ATOM   1052 C  CZ3 . TRP   A 1 136 ? 24.768 10.272  5.303  1.00 20.24 ? 142 TRP   A CZ3 1 
ATOM   1053 C  CH2 . TRP   A 1 136 ? 23.745 11.107  5.753  1.00 19.98 ? 142 TRP   A CH2 1 
ATOM   1054 N  N   . LEU   A 1 137 ? 23.561 6.427   3.217  1.00 21.58 ? 143 LEU   A N   1 
ATOM   1055 C  CA  . LEU   A 1 137 ? 24.022 5.798   4.455  1.00 23.85 ? 143 LEU   A CA  1 
ATOM   1056 C  C   . LEU   A 1 137 ? 24.739 4.453   4.186  1.00 27.28 ? 143 LEU   A C   1 
ATOM   1057 O  O   . LEU   A 1 137 ? 25.611 4.077   4.968  1.00 27.10 ? 143 LEU   A O   1 
ATOM   1058 C  CB  . LEU   A 1 137 ? 22.850 5.595   5.429  1.00 22.96 ? 143 LEU   A CB  1 
ATOM   1059 C  CG  . LEU   A 1 137 ? 22.332 6.853   6.119  1.00 22.91 ? 143 LEU   A CG  1 
ATOM   1060 C  CD1 . LEU   A 1 137 ? 21.043 6.545   6.903  1.00 22.89 ? 143 LEU   A CD1 1 
ATOM   1061 C  CD2 . LEU   A 1 137 ? 23.382 7.392   7.110  1.00 22.57 ? 143 LEU   A CD2 1 
ATOM   1062 N  N   . ASP   A 1 138 ? 24.411 3.775   3.051  1.00 30.14 ? 144 ASP   A N   1 
ATOM   1063 C  CA  . ASP   A 1 138 ? 24.984 2.479   2.639  1.00 33.33 ? 144 ASP   A CA  1 
ATOM   1064 C  C   . ASP   A 1 138 ? 26.299 2.586   1.873  1.00 37.99 ? 144 ASP   A C   1 
ATOM   1065 O  O   . ASP   A 1 138 ? 26.847 1.549   1.495  1.00 38.74 ? 144 ASP   A O   1 
ATOM   1066 C  CB  . ASP   A 1 138 ? 24.012 1.759   1.687  1.00 34.62 ? 144 ASP   A CB  1 
ATOM   1067 C  CG  . ASP   A 1 138 ? 22.661 1.478   2.254  1.00 40.97 ? 144 ASP   A CG  1 
ATOM   1068 O  OD1 . ASP   A 1 138 ? 22.535 1.457   3.498  1.00 41.68 ? 144 ASP   A OD1 1 
ATOM   1069 O  OD2 . ASP   A 1 138 ? 21.715 1.296   1.463  1.00 44.49 ? 144 ASP   A OD2 1 
ATOM   1070 N  N   . GLU   A 1 139 ? 26.767 3.803   1.565  1.00 40.59 ? 145 GLU   A N   1 
ATOM   1071 C  CA  . GLU   A 1 139 ? 27.961 3.964   0.730  1.00 44.09 ? 145 GLU   A CA  1 
ATOM   1072 C  C   . GLU   A 1 139 ? 28.920 5.067   1.240  1.00 46.95 ? 145 GLU   A C   1 
ATOM   1073 O  O   . GLU   A 1 139 ? 28.723 5.571   2.348  1.00 47.06 ? 145 GLU   A O   1 
ATOM   1074 C  CB  . GLU   A 1 139 ? 27.496 4.226   -0.722 1.00 47.41 ? 145 GLU   A CB  1 
ATOM   1075 C  CG  . GLU   A 1 139 ? 26.584 5.435   -0.844 1.00 52.88 ? 145 GLU   A CG  1 
ATOM   1076 C  CD  . GLU   A 1 139 ? 25.795 5.492   -2.133 1.00 59.63 ? 145 GLU   A CD  1 
ATOM   1077 O  OE1 . GLU   A 1 139 ? 25.445 6.616   -2.565 1.00 61.55 ? 145 GLU   A OE1 1 
ATOM   1078 O  OE2 . GLU   A 1 139 ? 25.537 4.414   -2.716 1.00 60.44 ? 145 GLU   A OE2 1 
ATOM   1079 N  N   . GLU   A 1 140 ? 29.972 5.409   0.446  1.00 49.24 ? 146 GLU   A N   1 
ATOM   1080 C  CA  . GLU   A 1 140 ? 30.968 6.456   0.717  1.00 51.79 ? 146 GLU   A CA  1 
ATOM   1081 C  C   . GLU   A 1 140 ? 31.791 6.175   1.966  1.00 53.18 ? 146 GLU   A C   1 
ATOM   1082 O  O   . GLU   A 1 140 ? 33.020 6.106   1.875  1.00 53.90 ? 146 GLU   A O   1 
ATOM   1083 C  CB  . GLU   A 1 140 ? 30.327 7.863   0.755  1.00 55.48 ? 146 GLU   A CB  1 
ATOM   1084 C  CG  . GLU   A 1 140 ? 31.244 8.988   1.214  1.00 63.09 ? 146 GLU   A CG  1 
ATOM   1085 C  CD  . GLU   A 1 140 ? 32.023 9.669   0.107  1.00 72.35 ? 146 GLU   A CD  1 
ATOM   1086 O  OE1 . GLU   A 1 140 ? 31.727 10.850  -0.189 1.00 74.12 ? 146 GLU   A OE1 1 
ATOM   1087 O  OE2 . GLU   A 1 140 ? 32.931 9.022   -0.464 1.00 75.90 ? 146 GLU   A OE2 1 
ATOM   1088 N  N   . SER   B 1 1   ? 21.912 -21.220 7.674  1.00 21.57 ? 7   SER   C N   1 
ATOM   1089 C  CA  . SER   B 1 1   ? 20.750 -21.080 8.561  1.00 22.75 ? 7   SER   C CA  1 
ATOM   1090 C  C   . SER   B 1 1   ? 20.747 -22.182 9.650  1.00 22.94 ? 7   SER   C C   1 
ATOM   1091 O  O   . SER   B 1 1   ? 21.435 -23.197 9.509  1.00 24.07 ? 7   SER   C O   1 
ATOM   1092 C  CB  . SER   B 1 1   ? 19.469 -21.189 7.745  1.00 25.43 ? 7   SER   C CB  1 
ATOM   1093 O  OG  . SER   B 1 1   ? 19.445 -22.462 7.116  1.00 30.37 ? 7   SER   C OG  1 
ATOM   1094 N  N   . GLY   B 1 2   ? 19.983 -21.966 10.718 1.00 21.60 ? 8   GLY   C N   1 
ATOM   1095 C  CA  . GLY   B 1 2   ? 19.863 -22.944 11.785 1.00 20.41 ? 8   GLY   C CA  1 
ATOM   1096 C  C   . GLY   B 1 2   ? 19.540 -22.316 13.128 1.00 19.20 ? 8   GLY   C C   1 
ATOM   1097 O  O   . GLY   B 1 2   ? 19.918 -21.179 13.400 1.00 19.25 ? 8   GLY   C O   1 
ATOM   1098 N  N   . ALA   B 1 3   ? 18.822 -23.065 13.973 1.00 18.77 ? 9   ALA   C N   1 
ATOM   1099 C  CA  . ALA   B 1 3   ? 18.453 -22.589 15.309 1.00 17.87 ? 9   ALA   C CA  1 
ATOM   1100 C  C   . ALA   B 1 3   ? 18.559 -23.707 16.356 1.00 16.80 ? 9   ALA   C C   1 
ATOM   1101 O  O   . ALA   B 1 3   ? 18.627 -24.892 15.995 1.00 18.54 ? 9   ALA   C O   1 
ATOM   1102 C  CB  . ALA   B 1 3   ? 17.041 -22.013 15.294 1.00 18.57 ? 9   ALA   C CB  1 
ATOM   1103 N  N   . ILE   B 1 4   ? 18.620 -23.339 17.625 1.00 15.40 ? 10  ILE   C N   1 
ATOM   1104 C  CA  . ILE   B 1 4   ? 18.556 -24.286 18.743 1.00 15.76 ? 10  ILE   C CA  1 
ATOM   1105 C  C   . ILE   B 1 4   ? 17.134 -24.117 19.352 1.00 17.57 ? 10  ILE   C C   1 
ATOM   1106 O  O   . ILE   B 1 4   ? 16.699 -22.973 19.598 1.00 18.27 ? 10  ILE   C O   1 
ATOM   1107 C  CB  . ILE   B 1 4   ? 19.597 -24.010 19.847 1.00 15.54 ? 10  ILE   C CB  1 
ATOM   1108 C  CG1 . ILE   B 1 4   ? 21.037 -23.870 19.297 1.00 15.54 ? 10  ILE   C CG1 1 
ATOM   1109 C  CG2 . ILE   B 1 4   ? 19.519 -25.114 20.945 1.00 16.37 ? 10  ILE   C CG2 1 
ATOM   1110 C  CD1 . ILE   B 1 4   ? 22.005 -23.242 20.347 1.00 15.48 ? 10  ILE   C CD1 1 
ATOM   1111 N  N   . TYR   B 1 5   ? 16.437 -25.226 19.624 1.00 18.07 ? 11  TYR   C N   1 
ATOM   1112 C  CA  . TYR   B 1 5   ? 15.104 -25.198 20.198 1.00 18.43 ? 11  TYR   C CA  1 
ATOM   1113 C  C   . TYR   B 1 5   ? 15.135 -25.876 21.569 1.00 19.69 ? 11  TYR   C C   1 
ATOM   1114 O  O   . TYR   B 1 5   ? 15.213 -27.107 21.657 1.00 20.31 ? 11  TYR   C O   1 
ATOM   1115 C  CB  . TYR   B 1 5   ? 14.084 -25.877 19.261 1.00 18.78 ? 11  TYR   C CB  1 
ATOM   1116 C  CG  . TYR   B 1 5   ? 13.895 -25.098 17.978 1.00 18.46 ? 11  TYR   C CG  1 
ATOM   1117 C  CD1 . TYR   B 1 5   ? 13.074 -23.977 17.937 1.00 20.29 ? 11  TYR   C CD1 1 
ATOM   1118 C  CD2 . TYR   B 1 5   ? 14.581 -25.444 16.824 1.00 18.76 ? 11  TYR   C CD2 1 
ATOM   1119 C  CE1 . TYR   B 1 5   ? 12.925 -23.232 16.774 1.00 20.94 ? 11  TYR   C CE1 1 
ATOM   1120 C  CE2 . TYR   B 1 5   ? 14.411 -24.728 15.644 1.00 20.28 ? 11  TYR   C CE2 1 
ATOM   1121 C  CZ  . TYR   B 1 5   ? 13.599 -23.609 15.629 1.00 21.85 ? 11  TYR   C CZ  1 
ATOM   1122 O  OH  . TYR   B 1 5   ? 13.482 -22.865 14.478 1.00 25.65 ? 11  TYR   C OH  1 
ATOM   1123 N  N   . VAL   B 1 6   ? 15.153 -25.085 22.637 1.00 18.74 ? 12  VAL   C N   1 
ATOM   1124 C  CA  . VAL   B 1 6   ? 15.225 -25.620 24.006 1.00 20.00 ? 12  VAL   C CA  1 
ATOM   1125 C  C   . VAL   B 1 6   ? 14.085 -25.043 24.847 1.00 21.05 ? 12  VAL   C C   1 
ATOM   1126 O  O   . VAL   B 1 6   ? 13.890 -23.817 24.824 1.00 21.09 ? 12  VAL   C O   1 
ATOM   1127 C  CB  . VAL   B 1 6   ? 16.600 -25.355 24.644 1.00 20.46 ? 12  VAL   C CB  1 
ATOM   1128 C  CG1 . VAL   B 1 6   ? 16.998 -23.873 24.563 1.00 21.57 ? 12  VAL   C CG1 1 
ATOM   1129 C  CG2 . VAL   B 1 6   ? 16.626 -25.877 26.084 1.00 21.02 ? 12  VAL   C CG2 1 
ATOM   1130 N  N   . GLY   B 1 7   ? 13.255 -25.898 25.486 1.00 21.82 ? 13  GLY   C N   1 
ATOM   1131 C  CA  . GLY   B 1 7   ? 12.110 -25.403 26.260 1.00 22.11 ? 13  GLY   C CA  1 
ATOM   1132 C  C   . GLY   B 1 7   ? 11.185 -24.514 25.429 1.00 22.75 ? 13  GLY   C C   1 
ATOM   1133 O  O   . GLY   B 1 7   ? 10.862 -24.865 24.297 1.00 22.41 ? 13  GLY   C O   1 
ATOM   1134 N  N   . ASN   B 1 8   ? 10.836 -23.312 25.927 1.00 22.66 ? 14  ASN   C N   1 
ATOM   1135 C  CA  . ASN   B 1 8   ? 10.030 -22.389 25.125 1.00 23.22 ? 14  ASN   C CA  1 
ATOM   1136 C  C   . ASN   B 1 8   ? 10.904 -21.296 24.500 1.00 21.78 ? 14  ASN   C C   1 
ATOM   1137 O  O   . ASN   B 1 8   ? 10.446 -20.168 24.320 1.00 22.49 ? 14  ASN   C O   1 
ATOM   1138 C  CB  . ASN   B 1 8   ? 8.842  -21.833 25.890 1.00 26.53 ? 14  ASN   C CB  1 
ATOM   1139 C  CG  . ASN   B 1 8   ? 7.751  -22.873 26.062 1.00 33.00 ? 14  ASN   C CG  1 
ATOM   1140 O  OD1 . ASN   B 1 8   ? 6.816  -22.983 25.243 1.00 35.23 ? 14  ASN   C OD1 1 
ATOM   1141 N  ND2 . ASN   B 1 8   ? 7.875  -23.681 27.113 1.00 34.07 ? 14  ASN   C ND2 1 
ATOM   1142 N  N   . TYR   B 1 9   ? 12.136 -21.663 24.096 1.00 20.53 ? 15  TYR   C N   1 
ATOM   1143 C  CA  . TYR   B 1 9   ? 13.097 -20.748 23.476 1.00 19.70 ? 15  TYR   C CA  1 
ATOM   1144 C  C   . TYR   B 1 9   ? 13.578 -21.205 22.097 1.00 17.94 ? 15  TYR   C C   1 
ATOM   1145 O  O   . TYR   B 1 9   ? 13.780 -22.404 21.882 1.00 16.82 ? 15  TYR   C O   1 
ATOM   1146 C  CB  . TYR   B 1 9   ? 14.321 -20.561 24.400 1.00 20.17 ? 15  TYR   C CB  1 
ATOM   1147 C  CG  . TYR   B 1 9   ? 13.975 -19.992 25.764 1.00 22.24 ? 15  TYR   C CG  1 
ATOM   1148 C  CD1 . TYR   B 1 9   ? 13.448 -18.716 25.894 1.00 23.37 ? 15  TYR   C CD1 1 
ATOM   1149 C  CD2 . TYR   B 1 9   ? 14.185 -20.732 26.931 1.00 23.94 ? 15  TYR   C CD2 1 
ATOM   1150 C  CE1 . TYR   B 1 9   ? 13.131 -18.184 27.141 1.00 25.27 ? 15  TYR   C CE1 1 
ATOM   1151 C  CE2 . TYR   B 1 9   ? 13.882 -20.199 28.192 1.00 25.19 ? 15  TYR   C CE2 1 
ATOM   1152 C  CZ  . TYR   B 1 9   ? 13.369 -18.914 28.290 1.00 27.46 ? 15  TYR   C CZ  1 
ATOM   1153 O  OH  . TYR   B 1 9   ? 13.038 -18.324 29.505 1.00 30.63 ? 15  TYR   C OH  1 
ATOM   1154 N  N   . ARG   B 1 10  ? 13.879 -20.230 21.209 1.00 16.81 ? 16  ARG   C N   1 
ATOM   1155 C  CA  . ARG   B 1 10  ? 14.503 -20.412 19.885 1.00 17.17 ? 16  ARG   C CA  1 
ATOM   1156 C  C   . ARG   B 1 10  ? 15.770 -19.531 19.888 1.00 17.09 ? 16  ARG   C C   1 
ATOM   1157 O  O   . ARG   B 1 10  ? 15.673 -18.326 20.114 1.00 17.26 ? 16  ARG   C O   1 
ATOM   1158 C  CB  . ARG   B 1 10  ? 13.546 -19.982 18.749 1.00 18.61 ? 16  ARG   C CB  1 
ATOM   1159 C  CG  . ARG   B 1 10  ? 14.188 -19.748 17.369 1.00 19.14 ? 16  ARG   C CG  1 
ATOM   1160 C  CD  . ARG   B 1 10  ? 13.122 -19.586 16.245 1.00 18.28 ? 16  ARG   C CD  1 
ATOM   1161 N  NE  . ARG   B 1 10  ? 13.504 -18.590 15.236 1.00 19.38 ? 16  ARG   C NE  1 
ATOM   1162 C  CZ  . ARG   B 1 10  ? 14.089 -18.876 14.070 1.00 19.54 ? 16  ARG   C CZ  1 
ATOM   1163 N  NH1 . ARG   B 1 10  ? 14.389 -20.131 13.761 1.00 18.71 ? 16  ARG   C NH1 1 
ATOM   1164 N  NH2 . ARG   B 1 10  ? 14.444 -17.902 13.241 1.00 18.68 ? 16  ARG   C NH2 1 
ATOM   1165 N  N   . VAL   B 1 11  ? 16.948 -20.143 19.739 1.00 16.31 ? 17  VAL   C N   1 
ATOM   1166 C  CA  . VAL   B 1 11  ? 18.238 -19.439 19.734 1.00 15.07 ? 17  VAL   C CA  1 
ATOM   1167 C  C   . VAL   B 1 11  ? 18.734 -19.384 18.308 1.00 15.11 ? 17  VAL   C C   1 
ATOM   1168 O  O   . VAL   B 1 11  ? 18.910 -20.422 17.684 1.00 16.11 ? 17  VAL   C O   1 
ATOM   1169 C  CB  . VAL   B 1 11  ? 19.261 -20.114 20.676 1.00 17.79 ? 17  VAL   C CB  1 
ATOM   1170 C  CG1 . VAL   B 1 11  ? 20.509 -19.240 20.820 1.00 19.60 ? 17  VAL   C CG1 1 
ATOM   1171 C  CG2 . VAL   B 1 11  ? 18.631 -20.456 22.034 1.00 18.80 ? 17  VAL   C CG2 1 
ATOM   1172 N  N   . VAL   B 1 12  ? 18.936 -18.168 17.761 1.00 14.90 ? 18  VAL   C N   1 
ATOM   1173 C  CA  A VAL   B 1 12  ? 19.405 -17.981 16.382 0.50 14.71 ? 18  VAL   C CA  1 
ATOM   1174 C  CA  B VAL   B 1 12  ? 19.379 -17.984 16.381 0.50 15.76 ? 18  VAL   C CA  1 
ATOM   1175 C  C   . VAL   B 1 12  ? 20.532 -16.938 16.336 1.00 15.05 ? 18  VAL   C C   1 
ATOM   1176 O  O   . VAL   B 1 12  ? 20.720 -16.175 17.310 1.00 14.69 ? 18  VAL   C O   1 
ATOM   1177 C  CB  A VAL   B 1 12  ? 18.260 -17.486 15.450 0.50 14.30 ? 18  VAL   C CB  1 
ATOM   1178 C  CB  B VAL   B 1 12  ? 18.138 -17.483 15.575 0.50 17.54 ? 18  VAL   C CB  1 
ATOM   1179 C  CG1 A VAL   B 1 12  ? 17.230 -18.561 15.213 0.50 15.37 ? 18  VAL   C CG1 1 
ATOM   1180 C  CG1 B VAL   B 1 12  ? 18.471 -17.147 14.141 0.50 18.14 ? 18  VAL   C CG1 1 
ATOM   1181 C  CG2 A VAL   B 1 12  ? 17.633 -16.182 15.970 0.50 12.51 ? 18  VAL   C CG2 1 
ATOM   1182 C  CG2 B VAL   B 1 12  ? 17.018 -18.495 15.619 0.50 18.66 ? 18  VAL   C CG2 1 
ATOM   1183 N  N   . ASN   B 1 13  ? 21.293 -16.871 15.208 1.00 14.76 ? 19  ASN   C N   1 
ATOM   1184 C  CA  . ASN   B 1 13  ? 22.303 -15.810 15.039 1.00 13.61 ? 19  ASN   C CA  1 
ATOM   1185 C  C   . ASN   B 1 13  ? 21.482 -14.471 14.991 1.00 12.95 ? 19  ASN   C C   1 
ATOM   1186 O  O   . ASN   B 1 13  ? 20.451 -14.412 14.325 1.00 13.51 ? 19  ASN   C O   1 
ATOM   1187 C  CB  . ASN   B 1 13  ? 23.026 -15.935 13.687 1.00 14.98 ? 19  ASN   C CB  1 
ATOM   1188 C  CG  . ASN   B 1 13  ? 23.864 -17.217 13.631 1.00 14.83 ? 19  ASN   C CG  1 
ATOM   1189 O  OD1 . ASN   B 1 13  ? 23.395 -18.270 13.187 1.00 16.88 ? 19  ASN   C OD1 1 
ATOM   1190 N  ND2 . ASN   B 1 13  ? 25.083 -17.150 14.144 1.00 14.78 ? 19  ASN   C ND2 1 
ATOM   1191 N  N   . ARG   B 1 14  ? 21.930 -13.436 15.712 1.00 14.64 ? 20  ARG   C N   1 
ATOM   1192 C  CA  . ARG   B 1 14  ? 21.204 -12.151 15.733 1.00 15.24 ? 20  ARG   C CA  1 
ATOM   1193 C  C   . ARG   B 1 14  ? 21.083 -11.567 14.332 1.00 16.37 ? 20  ARG   C C   1 
ATOM   1194 O  O   . ARG   B 1 14  ? 20.015 -11.021 13.989 1.00 19.05 ? 20  ARG   C O   1 
ATOM   1195 C  CB  . ARG   B 1 14  ? 21.873 -11.175 16.711 1.00 16.38 ? 20  ARG   C CB  1 
ATOM   1196 C  CG  . ARG   B 1 14  ? 21.122 -9.858  16.947 1.00 17.17 ? 20  ARG   C CG  1 
ATOM   1197 C  CD  . ARG   B 1 14  ? 22.024 -8.856  17.667 1.00 16.55 ? 20  ARG   C CD  1 
ATOM   1198 N  NE  . ARG   B 1 14  ? 21.318 -7.628  18.096 1.00 17.58 ? 20  ARG   C NE  1 
ATOM   1199 C  CZ  . ARG   B 1 14  ? 21.114 -6.566  17.323 1.00 19.60 ? 20  ARG   C CZ  1 
ATOM   1200 N  NH1 . ARG   B 1 14  ? 21.535 -6.562  16.063 1.00 19.35 ? 20  ARG   C NH1 1 
ATOM   1201 N  NH2 . ARG   B 1 14  ? 20.545 -5.466  17.825 1.00 21.09 ? 20  ARG   C NH2 1 
ATOM   1202 N  N   . HIS   B 1 15  ? 22.093 -11.787 13.469 1.00 16.40 ? 21  HIS   C N   1 
ATOM   1203 C  CA  . HIS   B 1 15  ? 22.028 -11.214 12.097 1.00 17.44 ? 21  HIS   C CA  1 
ATOM   1204 C  C   . HIS   B 1 15  ? 21.021 -11.943 11.179 1.00 18.16 ? 21  HIS   C C   1 
ATOM   1205 O  O   . HIS   B 1 15  ? 20.755 -11.473 10.079 1.00 19.75 ? 21  HIS   C O   1 
ATOM   1206 C  CB  . HIS   B 1 15  ? 23.423 -11.117 11.452 1.00 18.07 ? 21  HIS   C CB  1 
ATOM   1207 C  CG  . HIS   B 1 15  ? 24.016 -12.424 11.055 1.00 18.81 ? 21  HIS   C CG  1 
ATOM   1208 N  ND1 . HIS   B 1 15  ? 24.782 -13.162 11.942 1.00 20.60 ? 21  HIS   C ND1 1 
ATOM   1209 C  CD2 . HIS   B 1 15  ? 24.042 -13.030 9.841  1.00 18.94 ? 21  HIS   C CD2 1 
ATOM   1210 C  CE1 . HIS   B 1 15  ? 25.198 -14.224 11.261 1.00 21.20 ? 21  HIS   C CE1 1 
ATOM   1211 N  NE2 . HIS   B 1 15  ? 24.785 -14.181 9.988  1.00 19.04 ? 21  HIS   C NE2 1 
ATOM   1212 N  N   . LEU   B 1 16  ? 20.545 -13.127 11.598 1.00 16.88 ? 22  LEU   C N   1 
ATOM   1213 C  CA  . LEU   B 1 16  ? 19.560 -13.875 10.811 1.00 17.14 ? 22  LEU   C CA  1 
ATOM   1214 C  C   . LEU   B 1 16  ? 18.143 -13.865 11.470 1.00 18.45 ? 22  LEU   C C   1 
ATOM   1215 O  O   . LEU   B 1 16  ? 17.231 -14.549 10.982 1.00 18.44 ? 22  LEU   C O   1 
ATOM   1216 C  CB  . LEU   B 1 16  ? 20.039 -15.325 10.616 1.00 16.79 ? 22  LEU   C CB  1 
ATOM   1217 C  CG  . LEU   B 1 16  ? 21.325 -15.498 9.818  1.00 18.34 ? 22  LEU   C CG  1 
ATOM   1218 C  CD1 . LEU   B 1 16  ? 21.722 -16.985 9.770  1.00 18.95 ? 22  LEU   C CD1 1 
ATOM   1219 C  CD2 . LEU   B 1 16  ? 21.189 -14.920 8.397  1.00 17.50 ? 22  LEU   C CD2 1 
ATOM   1220 N  N   . ALA   B 1 17  ? 17.961 -13.105 12.580 1.00 18.64 ? 23  ALA   C N   1 
ATOM   1221 C  CA  . ALA   B 1 17  ? 16.679 -13.033 13.274 1.00 19.23 ? 23  ALA   C CA  1 
ATOM   1222 C  C   . ALA   B 1 17  ? 15.579 -12.484 12.366 1.00 20.01 ? 23  ALA   C C   1 
ATOM   1223 O  O   . ALA   B 1 17  ? 15.832 -11.568 11.593 1.00 21.40 ? 23  ALA   C O   1 
ATOM   1224 C  CB  . ALA   B 1 17  ? 16.806 -12.171 14.518 1.00 19.26 ? 23  ALA   C CB  1 
ATOM   1225 N  N   . THR   B 1 18  ? 14.380 -13.078 12.438 1.00 20.09 ? 24  THR   C N   1 
ATOM   1226 C  CA  . THR   B 1 18  ? 13.253 -12.631 11.601 1.00 20.23 ? 24  THR   C CA  1 
ATOM   1227 C  C   . THR   B 1 18  ? 12.414 -11.540 12.341 1.00 20.35 ? 24  THR   C C   1 
ATOM   1228 O  O   . THR   B 1 18  ? 12.615 -11.315 13.539 1.00 20.25 ? 24  THR   C O   1 
ATOM   1229 C  CB  . THR   B 1 18  ? 12.329 -13.862 11.336 1.00 20.57 ? 24  THR   C CB  1 
ATOM   1230 O  OG1 . THR   B 1 18  ? 11.736 -14.273 12.581 1.00 20.78 ? 24  THR   C OG1 1 
ATOM   1231 C  CG2 . THR   B 1 18  ? 13.029 -15.020 10.617 1.00 21.79 ? 24  THR   C CG2 1 
ATOM   1232 N  N   . HIS   B 1 19  ? 11.378 -10.952 11.668 1.00 21.14 ? 25  HIS   C N   1 
ATOM   1233 C  CA  . HIS   B 1 19  ? 10.453 -10.039 12.360 1.00 22.11 ? 25  HIS   C CA  1 
ATOM   1234 C  C   . HIS   B 1 19  ? 9.742  -10.803 13.514 1.00 21.74 ? 25  HIS   C C   1 
ATOM   1235 O  O   . HIS   B 1 19  ? 9.629  -10.257 14.600 1.00 23.13 ? 25  HIS   C O   1 
ATOM   1236 C  CB  . HIS   B 1 19  ? 9.386  -9.461  11.391 1.00 24.15 ? 25  HIS   C CB  1 
ATOM   1237 C  CG  . HIS   B 1 19  ? 8.221  -8.796  12.088 1.00 28.03 ? 25  HIS   C CG  1 
ATOM   1238 N  ND1 . HIS   B 1 19  ? 8.256  -7.455  12.437 1.00 30.34 ? 25  HIS   C ND1 1 
ATOM   1239 C  CD2 . HIS   B 1 19  ? 7.035  -9.318  12.491 1.00 30.27 ? 25  HIS   C CD2 1 
ATOM   1240 C  CE1 . HIS   B 1 19  ? 7.096  -7.199  13.020 1.00 31.26 ? 25  HIS   C CE1 1 
ATOM   1241 N  NE2 . HIS   B 1 19  ? 6.329  -8.290  13.090 1.00 31.92 ? 25  HIS   C NE2 1 
ATOM   1242 N  N   . ASN   B 1 20  ? 9.338  -12.064 13.299 1.00 20.77 ? 26  ASN   C N   1 
ATOM   1243 C  CA  . ASN   B 1 20  ? 8.662  -12.832 14.350 1.00 21.56 ? 26  ASN   C CA  1 
ATOM   1244 C  C   . ASN   B 1 20  ? 9.576  -13.013 15.581 1.00 20.88 ? 26  ASN   C C   1 
ATOM   1245 O  O   . ASN   B 1 20  ? 9.109  -12.886 16.707 1.00 21.21 ? 26  ASN   C O   1 
ATOM   1246 C  CB  . ASN   B 1 20  ? 8.162  -14.171 13.841 1.00 23.78 ? 26  ASN   C CB  1 
ATOM   1247 C  CG  . ASN   B 1 20  ? 7.294  -14.887 14.878 1.00 30.61 ? 26  ASN   C CG  1 
ATOM   1248 O  OD1 . ASN   B 1 20  ? 6.146  -14.494 15.141 1.00 32.88 ? 26  ASN   C OD1 1 
ATOM   1249 N  ND2 . ASN   B 1 20  ? 7.813  -15.936 15.491 1.00 30.50 ? 26  ASN   C ND2 1 
ATOM   1250 N  N   . ASP   B 1 21  ? 10.894 -13.223 15.366 1.00 18.98 ? 27  ASP   C N   1 
ATOM   1251 C  CA  . ASP   B 1 21  ? 11.831 -13.325 16.480 1.00 18.31 ? 27  ASP   C CA  1 
ATOM   1252 C  C   . ASP   B 1 21  ? 11.847 -12.018 17.293 1.00 18.12 ? 27  ASP   C C   1 
ATOM   1253 O  O   . ASP   B 1 21  ? 11.761 -12.071 18.522 1.00 19.30 ? 27  ASP   C O   1 
ATOM   1254 C  CB  . ASP   B 1 21  ? 13.262 -13.663 15.974 1.00 18.86 ? 27  ASP   C CB  1 
ATOM   1255 C  CG  . ASP   B 1 21  ? 13.417 -15.081 15.483 1.00 19.53 ? 27  ASP   C CG  1 
ATOM   1256 O  OD1 . ASP   B 1 21  ? 12.831 -15.976 16.097 1.00 20.57 ? 27  ASP   C OD1 1 
ATOM   1257 O  OD2 . ASP   B 1 21  ? 14.139 -15.287 14.460 1.00 19.42 ? 27  ASP   C OD2 1 
ATOM   1258 N  N   . TRP   B 1 22  ? 11.984 -10.867 16.620 1.00 17.00 ? 28  TRP   C N   1 
ATOM   1259 C  CA  . TRP   B 1 22  ? 11.995 -9.555  17.283 1.00 17.08 ? 28  TRP   C CA  1 
ATOM   1260 C  C   . TRP   B 1 22  ? 10.621 -9.256  17.956 1.00 17.55 ? 28  TRP   C C   1 
ATOM   1261 O  O   . TRP   B 1 22  ? 10.574 -8.643  19.015 1.00 18.35 ? 28  TRP   C O   1 
ATOM   1262 C  CB  . TRP   B 1 22  ? 12.332 -8.456  16.266 1.00 17.36 ? 28  TRP   C CB  1 
ATOM   1263 C  CG  . TRP   B 1 22  ? 13.807 -8.368  15.965 1.00 17.35 ? 28  TRP   C CG  1 
ATOM   1264 C  CD1 . TRP   B 1 22  ? 14.445 -8.789  14.827 1.00 18.04 ? 28  TRP   C CD1 1 
ATOM   1265 C  CD2 . TRP   B 1 22  ? 14.829 -7.823  16.816 1.00 17.10 ? 28  TRP   C CD2 1 
ATOM   1266 N  NE1 . TRP   B 1 22  ? 15.795 -8.507  14.909 1.00 18.25 ? 28  TRP   C NE1 1 
ATOM   1267 C  CE2 . TRP   B 1 22  ? 16.069 -7.991  16.148 1.00 17.95 ? 28  TRP   C CE2 1 
ATOM   1268 C  CE3 . TRP   B 1 22  ? 14.824 -7.220  18.080 1.00 17.26 ? 28  TRP   C CE3 1 
ATOM   1269 C  CZ2 . TRP   B 1 22  ? 17.259 -7.505  16.660 1.00 18.20 ? 28  TRP   C CZ2 1 
ATOM   1270 C  CZ3 . TRP   B 1 22  ? 16.035 -6.811  18.623 1.00 18.15 ? 28  TRP   C CZ3 1 
ATOM   1271 C  CH2 . TRP   B 1 22  ? 17.226 -6.924  17.899 1.00 18.50 ? 28  TRP   C CH2 1 
ATOM   1272 N  N   . ALA   B 1 23  ? 9.517  -9.686  17.340 1.00 16.72 ? 29  ALA   C N   1 
ATOM   1273 C  CA  . ALA   B 1 23  ? 8.170  -9.499  17.906 1.00 19.15 ? 29  ALA   C CA  1 
ATOM   1274 C  C   . ALA   B 1 23  ? 7.905  -10.390 19.146 1.00 20.79 ? 29  ALA   C C   1 
ATOM   1275 O  O   . ALA   B 1 23  ? 6.901  -10.198 19.862 1.00 22.71 ? 29  ALA   C O   1 
ATOM   1276 C  CB  . ALA   B 1 23  ? 7.120  -9.787  16.844 1.00 20.79 ? 29  ALA   C CB  1 
ATOM   1277 N  N   . ASN   B 1 24  ? 8.773  -11.409 19.382 1.00 20.15 ? 30  ASN   C N   1 
ATOM   1278 C  CA  . ASN   B 1 24  ? 8.661  -12.308 20.526 1.00 20.56 ? 30  ASN   C CA  1 
ATOM   1279 C  C   . ASN   B 1 24  ? 10.036 -12.396 21.225 1.00 19.73 ? 30  ASN   C C   1 
ATOM   1280 O  O   . ASN   B 1 24  ? 10.438 -13.468 21.677 1.00 19.89 ? 30  ASN   C O   1 
ATOM   1281 C  CB  . ASN   B 1 24  ? 8.201  -13.681 20.035 1.00 22.84 ? 30  ASN   C CB  1 
ATOM   1282 C  CG  . ASN   B 1 24  ? 6.799  -13.667 19.510 1.00 26.49 ? 30  ASN   C CG  1 
ATOM   1283 O  OD1 . ASN   B 1 24  ? 5.838  -13.745 20.278 1.00 28.04 ? 30  ASN   C OD1 1 
ATOM   1284 N  ND2 . ASN   B 1 24  ? 6.655  -13.568 18.197 1.00 28.54 ? 30  ASN   C ND2 1 
ATOM   1285 N  N   . LEU   B 1 25  ? 10.727 -11.254 21.350 1.00 19.47 ? 31  LEU   C N   1 
ATOM   1286 C  CA  . LEU   B 1 25  ? 12.074 -11.178 21.908 1.00 20.00 ? 31  LEU   C CA  1 
ATOM   1287 C  C   . LEU   B 1 25  ? 12.176 -11.553 23.382 1.00 21.00 ? 31  LEU   C C   1 
ATOM   1288 O  O   . LEU   B 1 25  ? 11.410 -11.050 24.196 1.00 21.76 ? 31  LEU   C O   1 
ATOM   1289 C  CB  . LEU   B 1 25  ? 12.652 -9.764  21.699 1.00 20.89 ? 31  LEU   C CB  1 
ATOM   1290 C  CG  . LEU   B 1 25  ? 14.136 -9.611  22.068 1.00 22.43 ? 31  LEU   C CG  1 
ATOM   1291 C  CD1 . LEU   B 1 25  ? 15.014 -10.471 21.185 1.00 22.43 ? 31  LEU   C CD1 1 
ATOM   1292 C  CD2 . LEU   B 1 25  ? 14.586 -8.152  22.025 1.00 24.17 ? 31  LEU   C CD2 1 
ATOM   1293 N  N   . VAL   B 1 26  ? 13.195 -12.357 23.733 1.00 19.72 ? 32  VAL   C N   1 
ATOM   1294 C  CA  . VAL   B 1 26  ? 13.490 -12.688 25.130 1.00 19.95 ? 32  VAL   C CA  1 
ATOM   1295 C  C   . VAL   B 1 26  ? 14.802 -11.997 25.519 1.00 19.17 ? 32  VAL   C C   1 
ATOM   1296 O  O   . VAL   B 1 26  ? 14.910 -11.399 26.597 1.00 18.78 ? 32  VAL   C O   1 
ATOM   1297 C  CB  . VAL   B 1 26  ? 13.610 -14.207 25.362 1.00 20.31 ? 32  VAL   C CB  1 
ATOM   1298 C  CG1 . VAL   B 1 26  ? 14.102 -14.504 26.787 1.00 21.92 ? 32  VAL   C CG1 1 
ATOM   1299 C  CG2 . VAL   B 1 26  ? 12.295 -14.909 25.073 1.00 20.07 ? 32  VAL   C CG2 1 
ATOM   1300 N  N   . TRP   B 1 27  ? 15.824 -12.109 24.646 1.00 18.32 ? 33  TRP   C N   1 
ATOM   1301 C  CA  . TRP   B 1 27  ? 17.146 -11.551 24.927 1.00 18.64 ? 33  TRP   C CA  1 
ATOM   1302 C  C   . TRP   B 1 27  ? 17.970 -11.467 23.640 1.00 18.98 ? 33  TRP   C C   1 
ATOM   1303 O  O   . TRP   B 1 27  ? 17.835 -12.325 22.766 1.00 17.79 ? 33  TRP   C O   1 
ATOM   1304 C  CB  . TRP   B 1 27  ? 17.858 -12.436 25.969 1.00 19.08 ? 33  TRP   C CB  1 
ATOM   1305 C  CG  . TRP   B 1 27  ? 19.314 -12.148 26.190 1.00 19.72 ? 33  TRP   C CG  1 
ATOM   1306 C  CD1 . TRP   B 1 27  ? 19.850 -11.222 27.037 1.00 21.23 ? 33  TRP   C CD1 1 
ATOM   1307 C  CD2 . TRP   B 1 27  ? 20.425 -12.858 25.614 1.00 19.75 ? 33  TRP   C CD2 1 
ATOM   1308 N  NE1 . TRP   B 1 27  ? 21.228 -11.309 27.022 1.00 21.21 ? 33  TRP   C NE1 1 
ATOM   1309 C  CE2 . TRP   B 1 27  ? 21.605 -12.268 26.118 1.00 20.22 ? 33  TRP   C CE2 1 
ATOM   1310 C  CE3 . TRP   B 1 27  ? 20.537 -13.887 24.660 1.00 20.13 ? 33  TRP   C CE3 1 
ATOM   1311 C  CZ2 . TRP   B 1 27  ? 22.871 -12.720 25.760 1.00 20.35 ? 33  TRP   C CZ2 1 
ATOM   1312 C  CZ3 . TRP   B 1 27  ? 21.797 -14.301 24.276 1.00 19.59 ? 33  TRP   C CZ3 1 
ATOM   1313 C  CH2 . TRP   B 1 27  ? 22.941 -13.734 24.839 1.00 19.79 ? 33  TRP   C CH2 1 
ATOM   1314 N  N   . GLU   B 1 28  ? 18.801 -10.423 23.514 1.00 18.53 ? 34  GLU   C N   1 
ATOM   1315 C  CA  . GLU   B 1 28  ? 19.661 -10.309 22.342 1.00 19.08 ? 34  GLU   C CA  1 
ATOM   1316 C  C   . GLU   B 1 28  ? 20.981 -9.663  22.724 1.00 18.82 ? 34  GLU   C C   1 
ATOM   1317 O  O   . GLU   B 1 28  ? 21.018 -8.819  23.634 1.00 19.18 ? 34  GLU   C O   1 
ATOM   1318 C  CB  . GLU   B 1 28  ? 18.973 -9.576  21.178 1.00 20.15 ? 34  GLU   C CB  1 
ATOM   1319 C  CG  . GLU   B 1 28  ? 18.463 -8.177  21.505 1.00 21.12 ? 34  GLU   C CG  1 
ATOM   1320 C  CD  . GLU   B 1 28  ? 19.449 -7.029  21.419 1.00 23.16 ? 34  GLU   C CD  1 
ATOM   1321 O  OE1 . GLU   B 1 28  ? 19.195 -5.979  22.054 1.00 25.41 ? 34  GLU   C OE1 1 
ATOM   1322 O  OE2 . GLU   B 1 28  ? 20.476 -7.172  20.722 1.00 20.32 ? 34  GLU   C OE2 1 
ATOM   1323 N  N   . ASP   B 1 29  ? 22.048 -10.024 22.030 1.00 17.64 ? 35  ASP   C N   1 
ATOM   1324 C  CA  . ASP   B 1 29  ? 23.355 -9.427  22.291 1.00 17.88 ? 35  ASP   C CA  1 
ATOM   1325 C  C   . ASP   B 1 29  ? 24.156 -9.354  20.979 1.00 18.84 ? 35  ASP   C C   1 
ATOM   1326 O  O   . ASP   B 1 29  ? 24.577 -10.394 20.459 1.00 18.75 ? 35  ASP   C O   1 
ATOM   1327 C  CB  . ASP   B 1 29  ? 24.059 -10.212 23.390 1.00 18.87 ? 35  ASP   C CB  1 
ATOM   1328 C  CG  . ASP   B 1 29  ? 25.387 -9.651  23.859 1.00 23.32 ? 35  ASP   C CG  1 
ATOM   1329 O  OD1 . ASP   B 1 29  ? 26.149 -9.128  23.012 1.00 24.29 ? 35  ASP   C OD1 1 
ATOM   1330 O  OD2 . ASP   B 1 29  ? 25.690 -9.781  25.056 1.00 24.44 ? 35  ASP   C OD2 1 
ATOM   1331 N  N   . SER   B 1 30  ? 24.328 -8.124  20.423 1.00 18.48 ? 36  SER   C N   1 
ATOM   1332 C  CA  A SER   B 1 30  ? 25.058 -7.922  19.164 0.50 18.16 ? 36  SER   C CA  1 
ATOM   1333 C  CA  B SER   B 1 30  ? 25.040 -7.961  19.162 0.50 18.81 ? 36  SER   C CA  1 
ATOM   1334 C  C   . SER   B 1 30  ? 26.508 -8.390  19.259 1.00 18.62 ? 36  SER   C C   1 
ATOM   1335 O  O   . SER   B 1 30  ? 27.021 -8.996  18.312 1.00 19.98 ? 36  SER   C O   1 
ATOM   1336 C  CB  A SER   B 1 30  ? 25.029 -6.452  18.731 0.50 17.65 ? 36  SER   C CB  1 
ATOM   1337 C  CB  B SER   B 1 30  ? 24.910 -6.527  18.644 0.50 20.23 ? 36  SER   C CB  1 
ATOM   1338 O  OG  A SER   B 1 30  ? 25.982 -6.205  17.705 0.50 15.87 ? 36  SER   C OG  1 
ATOM   1339 O  OG  B SER   B 1 30  ? 25.198 -5.582  19.658 0.50 21.74 ? 36  SER   C OG  1 
ATOM   1340 N  N   . SER   B 1 31  ? 27.187 -8.093  20.387 1.00 18.87 ? 37  SER   C N   1 
ATOM   1341 C  CA  . SER   B 1 31  ? 28.584 -8.497  20.530 1.00 19.29 ? 37  SER   C CA  1 
ATOM   1342 C  C   . SER   B 1 31  ? 28.746 -10.039 20.495 1.00 17.87 ? 37  SER   C C   1 
ATOM   1343 O  O   . SER   B 1 31  ? 29.807 -10.503 20.092 1.00 17.25 ? 37  SER   C O   1 
ATOM   1344 C  CB  . SER   B 1 31  ? 29.227 -7.899  21.772 1.00 23.48 ? 37  SER   C CB  1 
ATOM   1345 O  OG  . SER   B 1 31  ? 28.917 -8.641  22.939 1.00 28.42 ? 37  SER   C OG  1 
ATOM   1346 N  N   . ARG   B 1 32  ? 27.683 -10.817 20.848 1.00 16.55 ? 38  ARG   C N   1 
ATOM   1347 C  CA  . ARG   B 1 32  ? 27.762 -12.292 20.777 1.00 16.93 ? 38  ARG   C CA  1 
ATOM   1348 C  C   . ARG   B 1 32  ? 27.133 -12.881 19.489 1.00 16.27 ? 38  ARG   C C   1 
ATOM   1349 O  O   . ARG   B 1 32  ? 27.167 -14.101 19.278 1.00 15.62 ? 38  ARG   C O   1 
ATOM   1350 C  CB  . ARG   B 1 32  ? 27.055 -12.920 22.003 1.00 19.08 ? 38  ARG   C CB  1 
ATOM   1351 C  CG  . ARG   B 1 32  ? 27.650 -12.549 23.350 1.00 21.17 ? 38  ARG   C CG  1 
ATOM   1352 C  CD  . ARG   B 1 32  ? 26.865 -13.187 24.498 1.00 21.86 ? 38  ARG   C CD  1 
ATOM   1353 N  NE  . ARG   B 1 32  ? 27.020 -14.653 24.524 1.00 19.80 ? 38  ARG   C NE  1 
ATOM   1354 C  CZ  . ARG   B 1 32  ? 27.013 -15.393 25.638 1.00 19.31 ? 38  ARG   C CZ  1 
ATOM   1355 N  NH1 . ARG   B 1 32  ? 26.825 -14.821 26.826 1.00 18.68 ? 38  ARG   C NH1 1 
ATOM   1356 N  NH2 . ARG   B 1 32  ? 27.182 -16.713 25.569 1.00 16.12 ? 38  ARG   C NH2 1 
ATOM   1357 N  N   . ASP   B 1 33  ? 26.517 -12.036 18.644 1.00 15.22 ? 39  ASP   C N   1 
ATOM   1358 C  CA  . ASP   B 1 33  ? 25.773 -12.464 17.459 1.00 14.66 ? 39  ASP   C CA  1 
ATOM   1359 C  C   . ASP   B 1 33  ? 24.664 -13.436 17.860 1.00 14.14 ? 39  ASP   C C   1 
ATOM   1360 O  O   . ASP   B 1 33  ? 24.387 -14.378 17.102 1.00 13.85 ? 39  ASP   C O   1 
ATOM   1361 C  CB  . ASP   B 1 33  ? 26.671 -13.046 16.360 1.00 15.44 ? 39  ASP   C CB  1 
ATOM   1362 C  CG  . ASP   B 1 33  ? 25.919 -13.383 15.073 1.00 17.96 ? 39  ASP   C CG  1 
ATOM   1363 O  OD1 . ASP   B 1 33  ? 25.044 -12.598 14.678 1.00 20.23 ? 39  ASP   C OD1 1 
ATOM   1364 O  OD2 . ASP   B 1 33  ? 26.157 -14.455 14.514 1.00 16.07 ? 39  ASP   C OD2 1 
ATOM   1365 N  N   . LEU   B 1 34  ? 24.018 -13.221 19.053 1.00 14.31 ? 40  LEU   C N   1 
ATOM   1366 C  CA  . LEU   B 1 34  ? 22.912 -14.100 19.507 1.00 14.77 ? 40  LEU   C CA  1 
ATOM   1367 C  C   . LEU   B 1 34  ? 21.600 -13.356 19.725 1.00 15.76 ? 40  LEU   C C   1 
ATOM   1368 O  O   . LEU   B 1 34  ? 21.602 -12.209 20.184 1.00 15.76 ? 40  LEU   C O   1 
ATOM   1369 C  CB  . LEU   B 1 34  ? 23.272 -14.813 20.824 1.00 14.56 ? 40  LEU   C CB  1 
ATOM   1370 C  CG  . LEU   B 1 34  ? 24.357 -15.903 20.732 1.00 16.84 ? 40  LEU   C CG  1 
ATOM   1371 C  CD1 . LEU   B 1 34  ? 24.578 -16.551 22.090 1.00 17.11 ? 40  LEU   C CD1 1 
ATOM   1372 C  CD2 . LEU   B 1 34  ? 23.985 -16.990 19.715 1.00 17.91 ? 40  LEU   C CD2 1 
ATOM   1373 N  N   . LEU   B 1 35  ? 20.485 -14.059 19.451 1.00 14.37 ? 41  LEU   C N   1 
ATOM   1374 C  CA  . LEU   B 1 35  ? 19.149 -13.544 19.738 1.00 15.79 ? 41  LEU   C CA  1 
ATOM   1375 C  C   . LEU   B 1 35  ? 18.290 -14.763 20.137 1.00 15.93 ? 41  LEU   C C   1 
ATOM   1376 O  O   . LEU   B 1 35  ? 18.359 -15.830 19.503 1.00 17.40 ? 41  LEU   C O   1 
ATOM   1377 C  CB  . LEU   B 1 35  ? 18.520 -12.783 18.549 1.00 16.04 ? 41  LEU   C CB  1 
ATOM   1378 C  CG  . LEU   B 1 35  ? 17.132 -12.189 18.800 1.00 16.25 ? 41  LEU   C CG  1 
ATOM   1379 C  CD1 . LEU   B 1 35  ? 16.955 -10.884 18.038 1.00 18.17 ? 41  LEU   C CD1 1 
ATOM   1380 C  CD2 . LEU   B 1 35  ? 16.017 -13.181 18.398 1.00 15.82 ? 41  LEU   C CD2 1 
ATOM   1381 N  N   . VAL   B 1 36  ? 17.562 -14.615 21.208 1.00 14.84 ? 42  VAL   C N   1 
ATOM   1382 C  CA  . VAL   B 1 36  ? 16.641 -15.641 21.713 1.00 15.43 ? 42  VAL   C CA  1 
ATOM   1383 C  C   . VAL   B 1 36  ? 15.206 -15.116 21.678 1.00 17.10 ? 42  VAL   C C   1 
ATOM   1384 O  O   . VAL   B 1 36  ? 14.922 -14.035 22.223 1.00 17.96 ? 42  VAL   C O   1 
ATOM   1385 C  CB  . VAL   B 1 36  ? 17.006 -16.099 23.140 1.00 15.66 ? 42  VAL   C CB  1 
ATOM   1386 C  CG1 . VAL   B 1 36  ? 15.989 -17.119 23.668 1.00 16.43 ? 42  VAL   C CG1 1 
ATOM   1387 C  CG2 . VAL   B 1 36  ? 18.427 -16.663 23.187 1.00 16.10 ? 42  VAL   C CG2 1 
ATOM   1388 N  N   . SER   B 1 37  ? 14.290 -15.881 21.078 1.00 17.11 ? 43  SER   C N   1 
ATOM   1389 C  CA  . SER   B 1 37  ? 12.886 -15.528 21.058 1.00 17.70 ? 43  SER   C CA  1 
ATOM   1390 C  C   . SER   B 1 37  ? 12.032 -16.657 21.717 1.00 19.09 ? 43  SER   C C   1 
ATOM   1391 O  O   . SER   B 1 37  ? 12.522 -17.760 21.950 1.00 19.12 ? 43  SER   C O   1 
ATOM   1392 C  CB  . SER   B 1 37  ? 12.407 -15.220 19.646 1.00 17.92 ? 43  SER   C CB  1 
ATOM   1393 O  OG  . SER   B 1 37  ? 12.507 -16.357 18.807 1.00 18.57 ? 43  SER   C OG  1 
ATOM   1394 N  N   . SER   B 1 38  ? 10.778 -16.353 22.060 1.00 20.15 ? 44  SER   C N   1 
ATOM   1395 C  CA  . SER   B 1 38  ? 9.893  -17.347 22.696 1.00 21.88 ? 44  SER   C CA  1 
ATOM   1396 C  C   . SER   B 1 38  ? 9.108  -18.179 21.668 1.00 23.61 ? 44  SER   C C   1 
ATOM   1397 O  O   . SER   B 1 38  ? 8.814  -17.715 20.562 1.00 24.50 ? 44  SER   C O   1 
ATOM   1398 C  CB  . SER   B 1 38  ? 8.946  -16.663 23.683 1.00 24.90 ? 44  SER   C CB  1 
ATOM   1399 O  OG  . SER   B 1 38  ? 8.231  -15.649 23.004 1.00 28.88 ? 44  SER   C OG  1 
ATOM   1400 N  N   . THR   B 1 39  ? 8.740  -19.403 22.040 1.00 23.99 ? 45  THR   C N   1 
ATOM   1401 C  CA  . THR   B 1 39  ? 8.006  -20.286 21.147 1.00 25.12 ? 45  THR   C CA  1 
ATOM   1402 C  C   . THR   B 1 39  ? 6.704  -20.750 21.820 1.00 28.00 ? 45  THR   C C   1 
ATOM   1403 O  O   . THR   B 1 39  ? 6.611  -20.776 23.057 1.00 27.96 ? 45  THR   C O   1 
ATOM   1404 C  CB  . THR   B 1 39  ? 8.871  -21.510 20.765 1.00 25.99 ? 45  THR   C CB  1 
ATOM   1405 O  OG1 . THR   B 1 39  ? 9.089  -22.302 21.916 1.00 26.57 ? 45  THR   C OG1 1 
ATOM   1406 C  CG2 . THR   B 1 39  ? 10.219 -21.136 20.151 1.00 27.51 ? 45  THR   C CG2 1 
ATOM   1407 N  N   . THR   B 1 40  ? 5.731  -21.192 21.012 1.00 30.00 ? 46  THR   C N   1 
ATOM   1408 C  CA  . THR   B 1 40  ? 4.495  -21.748 21.568 1.00 32.64 ? 46  THR   C CA  1 
ATOM   1409 C  C   . THR   B 1 40  ? 4.719  -23.219 21.912 1.00 32.88 ? 46  THR   C C   1 
ATOM   1410 O  O   . THR   B 1 40  ? 4.365  -23.650 23.004 1.00 33.21 ? 46  THR   C O   1 
ATOM   1411 C  CB  . THR   B 1 40  ? 3.274  -21.472 20.676 1.00 37.14 ? 46  THR   C CB  1 
ATOM   1412 O  OG1 . THR   B 1 40  ? 3.642  -21.604 19.293 1.00 39.72 ? 46  THR   C OG1 1 
ATOM   1413 C  CG2 . THR   B 1 40  ? 2.705  -20.083 20.914 1.00 38.71 ? 46  THR   C CG2 1 
ATOM   1414 N  N   . ALA   B 1 41  ? 5.377  -23.970 21.010 1.00 32.48 ? 47  ALA   C N   1 
ATOM   1415 C  CA  . ALA   B 1 41  ? 5.680  -25.377 21.250 1.00 32.92 ? 47  ALA   C CA  1 
ATOM   1416 C  C   . ALA   B 1 41  ? 6.995  -25.560 22.002 1.00 32.16 ? 47  ALA   C C   1 
ATOM   1417 O  O   . ALA   B 1 41  ? 7.941  -24.795 21.794 1.00 32.76 ? 47  ALA   C O   1 
ATOM   1418 C  CB  . ALA   B 1 41  ? 5.732  -26.132 19.929 1.00 33.25 ? 47  ALA   C CB  1 
ATOM   1419 N  N   . GLN   B 1 42  ? 7.074  -26.580 22.845 1.00 32.20 ? 48  GLN   C N   1 
ATOM   1420 C  CA  . GLN   B 1 42  ? 8.308  -26.883 23.560 1.00 32.50 ? 48  GLN   C CA  1 
ATOM   1421 C  C   . GLN   B 1 42  ? 9.320  -27.529 22.597 1.00 31.22 ? 48  GLN   C C   1 
ATOM   1422 O  O   . GLN   B 1 42  ? 8.943  -28.258 21.676 1.00 31.60 ? 48  GLN   C O   1 
ATOM   1423 C  CB  . GLN   B 1 42  ? 8.036  -27.794 24.779 1.00 35.71 ? 48  GLN   C CB  1 
ATOM   1424 C  CG  . GLN   B 1 42  ? 7.495  -27.044 25.999 1.00 41.68 ? 48  GLN   C CG  1 
ATOM   1425 C  CD  . GLN   B 1 42  ? 8.281  -27.395 27.246 1.00 48.85 ? 48  GLN   C CD  1 
ATOM   1426 O  OE1 . GLN   B 1 42  ? 8.468  -28.574 27.594 1.00 51.81 ? 48  GLN   C OE1 1 
ATOM   1427 N  NE2 . GLN   B 1 42  ? 8.768  -26.379 27.950 1.00 50.20 ? 48  GLN   C NE2 1 
ATOM   1428 N  N   . GLY   B 1 43  ? 10.581 -27.165 22.775 1.00 29.43 ? 49  GLY   C N   1 
ATOM   1429 C  CA  . GLY   B 1 43  ? 11.700 -27.676 22.012 1.00 27.68 ? 49  GLY   C CA  1 
ATOM   1430 C  C   . GLY   B 1 43  ? 12.367 -28.807 22.767 1.00 26.83 ? 49  GLY   C C   1 
ATOM   1431 O  O   . GLY   B 1 43  ? 12.142 -28.971 23.980 1.00 26.71 ? 49  GLY   C O   1 
ATOM   1432 N  N   . CYS   B 1 44  ? 13.141 -29.629 22.035 1.00 25.64 ? 50  CYS   C N   1 
ATOM   1433 C  CA  . CYS   B 1 44  ? 13.743 -30.822 22.607 1.00 26.62 ? 50  CYS   C CA  1 
ATOM   1434 C  C   . CYS   B 1 44  ? 15.258 -30.882 22.580 1.00 25.95 ? 50  CYS   C C   1 
ATOM   1435 O  O   . CYS   B 1 44  ? 15.810 -31.921 22.983 1.00 27.15 ? 50  CYS   C O   1 
ATOM   1436 C  CB  . CYS   B 1 44  ? 13.147 -32.035 21.927 1.00 28.84 ? 50  CYS   C CB  1 
ATOM   1437 S  SG  . CYS   B 1 44  ? 11.373 -32.210 22.220 1.00 38.28 ? 50  CYS   C SG  1 
ATOM   1438 N  N   . ASP   B 1 45  ? 15.946 -29.825 22.120 1.00 23.69 ? 51  ASP   C N   1 
ATOM   1439 C  CA  . ASP   B 1 45  ? 17.410 -29.801 22.184 1.00 23.04 ? 51  ASP   C CA  1 
ATOM   1440 C  C   . ASP   B 1 45  ? 17.813 -29.632 23.649 1.00 23.82 ? 51  ASP   C C   1 
ATOM   1441 O  O   . ASP   B 1 45  ? 17.090 -29.002 24.442 1.00 24.07 ? 51  ASP   C O   1 
ATOM   1442 C  CB  . ASP   B 1 45  ? 18.010 -28.634 21.366 1.00 23.03 ? 51  ASP   C CB  1 
ATOM   1443 C  CG  . ASP   B 1 45  ? 17.834 -28.802 19.882 1.00 26.00 ? 51  ASP   C CG  1 
ATOM   1444 O  OD1 . ASP   B 1 45  ? 17.786 -29.980 19.412 1.00 28.96 ? 51  ASP   C OD1 1 
ATOM   1445 O  OD2 . ASP   B 1 45  ? 17.663 -27.769 19.188 1.00 22.67 ? 51  ASP   C OD2 1 
ATOM   1446 N  N   . THR   B 1 46  ? 18.952 -30.229 24.016 1.00 22.59 ? 52  THR   C N   1 
ATOM   1447 C  CA  . THR   B 1 46  ? 19.493 -30.140 25.361 1.00 22.33 ? 52  THR   C CA  1 
ATOM   1448 C  C   . THR   B 1 46  ? 20.774 -29.289 25.250 1.00 21.49 ? 52  THR   C C   1 
ATOM   1449 O  O   . THR   B 1 46  ? 21.628 -29.600 24.423 1.00 21.13 ? 52  THR   C O   1 
ATOM   1450 C  CB  . THR   B 1 46  ? 19.874 -31.552 25.820 1.00 24.11 ? 52  THR   C CB  1 
ATOM   1451 O  OG1 . THR   B 1 46  ? 18.707 -32.348 26.032 1.00 24.16 ? 52  THR   C OG1 1 
ATOM   1452 C  CG2 . THR   B 1 46  ? 20.763 -31.546 27.073 1.00 25.03 ? 52  THR   C CG2 1 
ATOM   1453 N  N   . ILE   B 1 47  ? 20.933 -28.270 26.105 1.00 20.10 ? 53  ILE   C N   1 
ATOM   1454 C  CA  . ILE   B 1 47  ? 22.125 -27.446 26.104 1.00 18.53 ? 53  ILE   C CA  1 
ATOM   1455 C  C   . ILE   B 1 47  ? 23.209 -28.138 26.954 1.00 18.26 ? 53  ILE   C C   1 
ATOM   1456 O  O   . ILE   B 1 47  ? 22.946 -28.612 28.064 1.00 19.07 ? 53  ILE   C O   1 
ATOM   1457 C  CB  . ILE   B 1 47  ? 21.836 -26.028 26.662 1.00 19.09 ? 53  ILE   C CB  1 
ATOM   1458 C  CG1 . ILE   B 1 47  ? 20.688 -25.325 25.925 1.00 19.52 ? 53  ILE   C CG1 1 
ATOM   1459 C  CG2 . ILE   B 1 47  ? 23.113 -25.169 26.633 1.00 19.72 ? 53  ILE   C CG2 1 
ATOM   1460 C  CD1 . ILE   B 1 47  ? 20.936 -25.135 24.430 1.00 19.71 ? 53  ILE   C CD1 1 
ATOM   1461 N  N   . ALA   B 1 48  ? 24.424 -28.164 26.443 1.00 17.47 ? 54  ALA   C N   1 
ATOM   1462 C  CA  . ALA   B 1 48  ? 25.567 -28.736 27.169 1.00 17.19 ? 54  ALA   C CA  1 
ATOM   1463 C  C   . ALA   B 1 48  ? 25.898 -27.816 28.345 1.00 16.57 ? 54  ALA   C C   1 
ATOM   1464 O  O   . ALA   B 1 48  ? 25.881 -26.590 28.197 1.00 16.97 ? 54  ALA   C O   1 
ATOM   1465 C  CB  . ALA   B 1 48  ? 26.764 -28.782 26.229 1.00 16.48 ? 54  ALA   C CB  1 
ATOM   1466 N  N   . ARG   B 1 49  ? 26.233 -28.398 29.503 1.00 15.13 ? 55  ARG   C N   1 
ATOM   1467 C  CA  . ARG   B 1 49  ? 26.670 -27.622 30.678 1.00 14.97 ? 55  ARG   C CA  1 
ATOM   1468 C  C   . ARG   B 1 49  ? 27.994 -28.295 31.099 1.00 15.46 ? 55  ARG   C C   1 
ATOM   1469 O  O   . ARG   B 1 49  ? 27.985 -29.322 31.801 1.00 17.31 ? 55  ARG   C O   1 
ATOM   1470 C  CB  . ARG   B 1 49  ? 25.639 -27.631 31.812 1.00 15.94 ? 55  ARG   C CB  1 
ATOM   1471 C  CG  . ARG   B 1 49  ? 24.250 -27.166 31.376 1.00 17.61 ? 55  ARG   C CG  1 
ATOM   1472 C  CD  . ARG   B 1 49  ? 24.188 -25.677 31.044 1.00 17.92 ? 55  ARG   C CD  1 
ATOM   1473 N  NE  . ARG   B 1 49  ? 22.846 -25.265 30.637 1.00 18.62 ? 55  ARG   C NE  1 
ATOM   1474 C  CZ  . ARG   B 1 49  ? 22.564 -24.142 29.974 1.00 20.23 ? 55  ARG   C CZ  1 
ATOM   1475 N  NH1 . ARG   B 1 49  ? 23.529 -23.307 29.625 1.00 17.74 ? 55  ARG   C NH1 1 
ATOM   1476 N  NH2 . ARG   B 1 49  ? 21.324 -23.880 29.605 1.00 20.12 ? 55  ARG   C NH2 1 
ATOM   1477 N  N   . CYS   B 1 50  ? 29.115 -27.775 30.559 1.00 15.45 ? 56  CYS   C N   1 
ATOM   1478 C  CA  . CYS   B 1 50  ? 30.465 -28.380 30.609 1.00 16.03 ? 56  CYS   C CA  1 
ATOM   1479 C  C   . CYS   B 1 50  ? 31.531 -27.367 30.126 1.00 16.89 ? 56  CYS   C C   1 
ATOM   1480 O  O   . CYS   B 1 50  ? 31.195 -26.265 29.684 1.00 18.12 ? 56  CYS   C O   1 
ATOM   1481 C  CB  . CYS   B 1 50  ? 30.458 -29.579 29.653 1.00 15.71 ? 56  CYS   C CB  1 
ATOM   1482 S  SG  . CYS   B 1 50  ? 30.273 -29.081 27.903 1.00 15.73 ? 56  CYS   C SG  1 
ATOM   1483 N  N   . ASP   B 1 51  ? 32.821 -27.776 30.145 1.00 17.15 ? 57  ASP   C N   1 
ATOM   1484 C  CA  . ASP   B 1 51  ? 33.896 -26.999 29.544 1.00 17.74 ? 57  ASP   C CA  1 
ATOM   1485 C  C   . ASP   B 1 51  ? 34.603 -27.851 28.464 1.00 16.83 ? 57  ASP   C C   1 
ATOM   1486 O  O   . ASP   B 1 51  ? 35.809 -27.739 28.278 1.00 17.68 ? 57  ASP   C O   1 
ATOM   1487 C  CB  . ASP   B 1 51  ? 34.879 -26.430 30.553 1.00 19.70 ? 57  ASP   C CB  1 
ATOM   1488 C  CG  . ASP   B 1 51  ? 35.627 -27.449 31.373 1.00 24.83 ? 57  ASP   C CG  1 
ATOM   1489 O  OD1 . ASP   B 1 51  ? 35.366 -28.679 31.193 1.00 23.76 ? 57  ASP   C OD1 1 
ATOM   1490 O  OD2 . ASP   B 1 51  ? 36.492 -27.029 32.188 1.00 29.39 ? 57  ASP   C OD2 1 
ATOM   1491 N  N   . CYS   B 1 52  ? 33.843 -28.686 27.724 1.00 15.61 ? 58  CYS   C N   1 
ATOM   1492 C  CA  . CYS   B 1 52  ? 34.408 -29.472 26.620 1.00 14.36 ? 58  CYS   C CA  1 
ATOM   1493 C  C   . CYS   B 1 52  ? 35.106 -28.583 25.608 1.00 14.23 ? 58  CYS   C C   1 
ATOM   1494 O  O   . CYS   B 1 52  ? 34.674 -27.435 25.374 1.00 13.92 ? 58  CYS   C O   1 
ATOM   1495 C  CB  . CYS   B 1 52  ? 33.320 -30.290 25.919 1.00 15.09 ? 58  CYS   C CB  1 
ATOM   1496 S  SG  . CYS   B 1 52  ? 32.862 -31.811 26.787 1.00 17.69 ? 58  CYS   C SG  1 
ATOM   1497 N  N   . GLN   B 1 53  ? 36.191 -29.128 25.021 1.00 13.94 ? 59  GLN   C N   1 
ATOM   1498 C  CA  . GLN   B 1 53  ? 36.888 -28.484 23.928 1.00 15.28 ? 59  GLN   C CA  1 
ATOM   1499 C  C   . GLN   B 1 53  ? 36.947 -29.402 22.697 1.00 14.86 ? 59  GLN   C C   1 
ATOM   1500 O  O   . GLN   B 1 53  ? 37.699 -29.110 21.779 1.00 15.03 ? 59  GLN   C O   1 
ATOM   1501 C  CB  . GLN   B 1 53  ? 38.270 -27.948 24.332 1.00 16.90 ? 59  GLN   C CB  1 
ATOM   1502 C  CG  . GLN   B 1 53  ? 38.183 -26.689 25.189 1.00 17.83 ? 59  GLN   C CG  1 
ATOM   1503 C  CD  . GLN   B 1 53  ? 39.563 -26.142 25.447 1.00 21.06 ? 59  GLN   C CD  1 
ATOM   1504 O  OE1 . GLN   B 1 53  ? 40.096 -26.241 26.552 1.00 25.07 ? 59  GLN   C OE1 1 
ATOM   1505 N  NE2 . GLN   B 1 53  ? 40.183 -25.583 24.414 1.00 17.93 ? 59  GLN   C NE2 1 
ATOM   1506 N  N   . THR   B 1 54  ? 36.154 -30.489 22.659 1.00 14.25 ? 60  THR   C N   1 
ATOM   1507 C  CA  . THR   B 1 54  ? 36.053 -31.325 21.455 1.00 14.28 ? 60  THR   C CA  1 
ATOM   1508 C  C   . THR   B 1 54  ? 34.561 -31.573 21.204 1.00 13.76 ? 60  THR   C C   1 
ATOM   1509 O  O   . THR   B 1 54  ? 33.778 -31.755 22.126 1.00 15.24 ? 60  THR   C O   1 
ATOM   1510 C  CB  . THR   B 1 54  ? 36.822 -32.630 21.576 1.00 17.29 ? 60  THR   C CB  1 
ATOM   1511 O  OG1 . THR   B 1 54  ? 36.265 -33.365 22.669 1.00 20.77 ? 60  THR   C OG1 1 
ATOM   1512 C  CG2 . THR   B 1 54  ? 38.313 -32.398 21.862 1.00 17.21 ? 60  THR   C CG2 1 
ATOM   1513 N  N   . GLY   B 1 55  ? 34.216 -31.640 19.939 1.00 12.49 ? 61  GLY   C N   1 
ATOM   1514 C  CA  . GLY   B 1 55  ? 32.838 -31.854 19.541 1.00 12.20 ? 61  GLY   C CA  1 
ATOM   1515 C  C   . GLY   B 1 55  ? 32.735 -32.096 18.054 1.00 12.29 ? 61  GLY   C C   1 
ATOM   1516 O  O   . GLY   B 1 55  ? 33.728 -32.389 17.378 1.00 13.01 ? 61  GLY   C O   1 
ATOM   1517 N  N   . VAL   B 1 56  ? 31.536 -31.972 17.560 1.00 11.17 ? 62  VAL   C N   1 
ATOM   1518 C  CA  . VAL   B 1 56  ? 31.233 -32.176 16.138 1.00 10.28 ? 62  VAL   C CA  1 
ATOM   1519 C  C   . VAL   B 1 56  ? 30.314 -31.052 15.689 1.00 11.35 ? 62  VAL   C C   1 
ATOM   1520 O  O   . VAL   B 1 56  ? 29.362 -30.719 16.409 1.00 12.98 ? 62  VAL   C O   1 
ATOM   1521 C  CB  . VAL   B 1 56  ? 30.517 -33.545 15.958 1.00 11.44 ? 62  VAL   C CB  1 
ATOM   1522 C  CG1 . VAL   B 1 56  ? 30.048 -33.696 14.525 1.00 11.91 ? 62  VAL   C CG1 1 
ATOM   1523 C  CG2 . VAL   B 1 56  ? 31.422 -34.702 16.381 1.00 12.66 ? 62  VAL   C CG2 1 
ATOM   1524 N  N   . TYR   B 1 57  ? 30.589 -30.446 14.518 1.00 11.45 ? 63  TYR   C N   1 
ATOM   1525 C  CA  . TYR   B 1 57  ? 29.714 -29.368 14.023 1.00 10.50 ? 63  TYR   C CA  1 
ATOM   1526 C  C   . TYR   B 1 57  ? 29.131 -29.684 12.656 1.00 12.17 ? 63  TYR   C C   1 
ATOM   1527 O  O   . TYR   B 1 57  ? 29.761 -30.423 11.909 1.00 13.63 ? 63  TYR   C O   1 
ATOM   1528 C  CB  . TYR   B 1 57  ? 30.411 -27.974 13.996 1.00 11.80 ? 63  TYR   C CB  1 
ATOM   1529 C  CG  . TYR   B 1 57  ? 31.295 -27.692 12.790 1.00 12.32 ? 63  TYR   C CG  1 
ATOM   1530 C  CD1 . TYR   B 1 57  ? 32.563 -28.239 12.691 1.00 12.55 ? 63  TYR   C CD1 1 
ATOM   1531 C  CD2 . TYR   B 1 57  ? 30.885 -26.823 11.786 1.00 13.14 ? 63  TYR   C CD2 1 
ATOM   1532 C  CE1 . TYR   B 1 57  ? 33.422 -27.904 11.632 1.00 14.03 ? 63  TYR   C CE1 1 
ATOM   1533 C  CE2 . TYR   B 1 57  ? 31.718 -26.499 10.721 1.00 13.35 ? 63  TYR   C CE2 1 
ATOM   1534 C  CZ  . TYR   B 1 57  ? 32.985 -27.062 10.626 1.00 14.73 ? 63  TYR   C CZ  1 
ATOM   1535 O  OH  . TYR   B 1 57  ? 33.851 -26.743 9.572  1.00 15.66 ? 63  TYR   C OH  1 
ATOM   1536 N  N   . TYR   B 1 58  ? 27.949 -29.113 12.343 1.00 10.50 ? 64  TYR   C N   1 
ATOM   1537 C  CA  . TYR   B 1 58  ? 27.340 -29.299 11.029 1.00 12.72 ? 64  TYR   C CA  1 
ATOM   1538 C  C   . TYR   B 1 58  ? 27.727 -28.152 10.097 1.00 13.59 ? 64  TYR   C C   1 
ATOM   1539 O  O   . TYR   B 1 58  ? 27.516 -26.969 10.418 1.00 12.82 ? 64  TYR   C O   1 
ATOM   1540 C  CB  . TYR   B 1 58  ? 25.811 -29.421 11.088 1.00 14.38 ? 64  TYR   C CB  1 
ATOM   1541 C  CG  . TYR   B 1 58  ? 25.243 -29.657 9.703  1.00 15.62 ? 64  TYR   C CG  1 
ATOM   1542 C  CD1 . TYR   B 1 58  ? 25.605 -30.782 8.954  1.00 17.82 ? 64  TYR   C CD1 1 
ATOM   1543 C  CD2 . TYR   B 1 58  ? 24.412 -28.729 9.107  1.00 16.49 ? 64  TYR   C CD2 1 
ATOM   1544 C  CE1 . TYR   B 1 58  ? 25.098 -30.998 7.662  1.00 17.58 ? 64  TYR   C CE1 1 
ATOM   1545 C  CE2 . TYR   B 1 58  ? 23.897 -28.935 7.817  1.00 17.59 ? 64  TYR   C CE2 1 
ATOM   1546 C  CZ  . TYR   B 1 58  ? 24.256 -30.062 7.092  1.00 18.05 ? 64  TYR   C CZ  1 
ATOM   1547 O  OH  . TYR   B 1 58  ? 23.758 -30.223 5.804  1.00 20.02 ? 64  TYR   C OH  1 
ATOM   1548 N  N   . CYS   B 1 59  ? 28.288 -28.524 8.922  1.00 14.49 ? 65  CYS   C N   1 
ATOM   1549 C  CA  . CYS   B 1 59  ? 28.728 -27.587 7.892  1.00 15.16 ? 65  CYS   C CA  1 
ATOM   1550 C  C   . CYS   B 1 59  ? 27.822 -27.735 6.640  1.00 16.40 ? 65  CYS   C C   1 
ATOM   1551 O  O   . CYS   B 1 59  ? 28.018 -28.672 5.837  1.00 15.98 ? 65  CYS   C O   1 
ATOM   1552 C  CB  . CYS   B 1 59  ? 30.194 -27.828 7.546  1.00 16.08 ? 65  CYS   C CB  1 
ATOM   1553 S  SG  . CYS   B 1 59  ? 30.811 -26.795 6.188  1.00 18.15 ? 65  CYS   C SG  1 
ATOM   1554 N  N   . SER   B 1 60  ? 26.823 -26.858 6.505  1.00 15.84 ? 66  SER   C N   1 
ATOM   1555 C  CA  . SER   B 1 60  ? 25.876 -27.000 5.389  1.00 18.33 ? 66  SER   C CA  1 
ATOM   1556 C  C   . SER   B 1 60  ? 26.538 -26.882 4.011  1.00 18.42 ? 66  SER   C C   1 
ATOM   1557 O  O   . SER   B 1 60  ? 26.092 -27.555 3.090  1.00 20.74 ? 66  SER   C O   1 
ATOM   1558 C  CB  . SER   B 1 60  ? 24.718 -26.024 5.494  1.00 22.79 ? 66  SER   C CB  1 
ATOM   1559 O  OG  . SER   B 1 60  ? 25.151 -24.686 5.360  1.00 29.94 ? 66  SER   C OG  1 
ATOM   1560 N  N   . SER   B 1 61  ? 27.574 -26.028 3.877  1.00 17.48 ? 67  SER   C N   1 
ATOM   1561 C  CA  . SER   B 1 61  ? 28.301 -25.830 2.594  1.00 18.31 ? 67  SER   C CA  1 
ATOM   1562 C  C   . SER   B 1 61  ? 29.118 -27.045 2.153  1.00 18.29 ? 67  SER   C C   1 
ATOM   1563 O  O   . SER   B 1 61  ? 29.657 -27.044 1.034  1.00 18.68 ? 67  SER   C O   1 
ATOM   1564 C  CB  . SER   B 1 61  ? 29.166 -24.572 2.627  1.00 19.22 ? 67  SER   C CB  1 
ATOM   1565 O  OG  . SER   B 1 61  ? 30.145 -24.612 3.646  1.00 21.10 ? 67  SER   C OG  1 
ATOM   1566 N  N   . ARG   B 1 62  ? 29.180 -28.117 3.015  1.00 16.47 ? 68  ARG   C N   1 
ATOM   1567 C  CA  . ARG   B 1 62  ? 29.813 -29.385 2.643  1.00 17.24 ? 68  ARG   C CA  1 
ATOM   1568 C  C   . ARG   B 1 62  ? 28.866 -30.584 2.851  1.00 19.00 ? 68  ARG   C C   1 
ATOM   1569 O  O   . ARG   B 1 62  ? 29.286 -31.722 2.605  1.00 19.93 ? 68  ARG   C O   1 
ATOM   1570 C  CB  . ARG   B 1 62  ? 31.072 -29.614 3.469  1.00 18.14 ? 68  ARG   C CB  1 
ATOM   1571 C  CG  . ARG   B 1 62  ? 32.139 -28.552 3.266  1.00 23.09 ? 68  ARG   C CG  1 
ATOM   1572 C  CD  . ARG   B 1 62  ? 32.865 -28.761 1.964  1.00 23.95 ? 68  ARG   C CD  1 
ATOM   1573 N  NE  . ARG   B 1 62  ? 33.930 -27.776 1.760  1.00 27.38 ? 68  ARG   C NE  1 
ATOM   1574 C  CZ  . ARG   B 1 62  ? 33.792 -26.653 1.062  1.00 29.78 ? 68  ARG   C CZ  1 
ATOM   1575 N  NH1 . ARG   B 1 62  ? 32.619 -26.334 0.525  1.00 28.39 ? 68  ARG   C NH1 1 
ATOM   1576 N  NH2 . ARG   B 1 62  ? 34.822 -25.831 0.906  1.00 30.27 ? 68  ARG   C NH2 1 
ATOM   1577 N  N   . ARG   B 1 63  ? 27.624 -30.356 3.398  1.00 18.99 ? 69  ARG   C N   1 
ATOM   1578 C  CA  . ARG   B 1 63  ? 26.679 -31.440 3.767  1.00 19.73 ? 69  ARG   C CA  1 
ATOM   1579 C  C   . ARG   B 1 63  ? 27.371 -32.485 4.629  1.00 19.52 ? 69  ARG   C C   1 
ATOM   1580 O  O   . ARG   B 1 63  ? 27.198 -33.685 4.427  1.00 19.85 ? 69  ARG   C O   1 
ATOM   1581 C  CB  . ARG   B 1 63  ? 26.035 -32.093 2.515  1.00 21.34 ? 69  ARG   C CB  1 
ATOM   1582 C  CG  . ARG   B 1 63  ? 25.212 -31.152 1.692  1.00 25.76 ? 69  ARG   C CG  1 
ATOM   1583 C  CD  . ARG   B 1 63  ? 23.849 -30.924 2.295  1.00 31.64 ? 69  ARG   C CD  1 
ATOM   1584 N  NE  . ARG   B 1 63  ? 22.836 -30.576 1.289  1.00 35.13 ? 69  ARG   C NE  1 
ATOM   1585 C  CZ  . ARG   B 1 63  ? 22.572 -29.335 0.895  1.00 35.56 ? 69  ARG   C CZ  1 
ATOM   1586 N  NH1 . ARG   B 1 63  ? 23.270 -28.313 1.378  1.00 34.46 ? 69  ARG   C NH1 1 
ATOM   1587 N  NH2 . ARG   B 1 63  ? 21.623 -29.108 0.002  1.00 35.07 ? 69  ARG   C NH2 1 
ATOM   1588 N  N   . LYS   B 1 64  ? 28.226 -32.022 5.563  1.00 18.75 ? 70  LYS   C N   1 
ATOM   1589 C  CA  . LYS   B 1 64  ? 28.975 -32.940 6.404  1.00 17.90 ? 70  LYS   C CA  1 
ATOM   1590 C  C   . LYS   B 1 64  ? 29.059 -32.426 7.834  1.00 16.95 ? 70  LYS   C C   1 
ATOM   1591 O  O   . LYS   B 1 64  ? 29.027 -31.211 8.068  1.00 16.65 ? 70  LYS   C O   1 
ATOM   1592 C  CB  . LYS   B 1 64  ? 30.414 -33.086 5.869  1.00 21.62 ? 70  LYS   C CB  1 
ATOM   1593 C  CG  . LYS   B 1 64  ? 30.533 -34.052 4.683  1.00 30.07 ? 70  LYS   C CG  1 
ATOM   1594 C  CD  . LYS   B 1 64  ? 31.962 -34.366 4.334  1.00 36.86 ? 70  LYS   C CD  1 
ATOM   1595 C  CE  . LYS   B 1 64  ? 32.027 -35.299 3.149  1.00 42.71 ? 70  LYS   C CE  1 
ATOM   1596 N  NZ  . LYS   B 1 64  ? 31.400 -34.686 1.947  1.00 45.56 ? 70  LYS   C NZ  1 
ATOM   1597 N  N   . HIS   B 1 65  ? 29.194 -33.377 8.763  1.00 15.21 ? 71  HIS   C N   1 
ATOM   1598 C  CA  . HIS   B 1 65  ? 29.451 -33.106 10.170 1.00 15.55 ? 71  HIS   C CA  1 
ATOM   1599 C  C   . HIS   B 1 65  ? 30.925 -33.417 10.382 1.00 16.43 ? 71  HIS   C C   1 
ATOM   1600 O  O   . HIS   B 1 65  ? 31.387 -34.520 10.009 1.00 18.18 ? 71  HIS   C O   1 
ATOM   1601 C  CB  . HIS   B 1 65  ? 28.606 -34.010 11.104 1.00 15.36 ? 71  HIS   C CB  1 
ATOM   1602 C  CG  . HIS   B 1 65  ? 27.129 -33.757 11.045 1.00 17.44 ? 71  HIS   C CG  1 
ATOM   1603 N  ND1 . HIS   B 1 65  ? 26.476 -33.001 12.015 1.00 19.05 ? 71  HIS   C ND1 1 
ATOM   1604 C  CD2 . HIS   B 1 65  ? 26.228 -34.129 10.108 1.00 18.62 ? 71  HIS   C CD2 1 
ATOM   1605 C  CE1 . HIS   B 1 65  ? 25.204 -32.977 11.660 1.00 18.77 ? 71  HIS   C CE1 1 
ATOM   1606 N  NE2 . HIS   B 1 65  ? 25.000 -33.644 10.521 1.00 19.03 ? 71  HIS   C NE2 1 
ATOM   1607 N  N   . TYR   B 1 66  ? 31.670 -32.471 10.985 1.00 15.15 ? 72  TYR   C N   1 
ATOM   1608 C  CA  . TYR   B 1 66  ? 33.096 -32.642 11.187 1.00 14.12 ? 72  TYR   C CA  1 
ATOM   1609 C  C   . TYR   B 1 66  ? 33.456 -32.655 12.675 1.00 13.41 ? 72  TYR   C C   1 
ATOM   1610 O  O   . TYR   B 1 66  ? 33.052 -31.750 13.400 1.00 13.37 ? 72  TYR   C O   1 
ATOM   1611 C  CB  . TYR   B 1 66  ? 33.860 -31.419 10.588 1.00 14.78 ? 72  TYR   C CB  1 
ATOM   1612 C  CG  . TYR   B 1 66  ? 33.837 -31.321 9.076  1.00 16.40 ? 72  TYR   C CG  1 
ATOM   1613 C  CD1 . TYR   B 1 66  ? 34.644 -32.136 8.295  1.00 17.96 ? 72  TYR   C CD1 1 
ATOM   1614 C  CD2 . TYR   B 1 66  ? 33.014 -30.408 8.431  1.00 17.52 ? 72  TYR   C CD2 1 
ATOM   1615 C  CE1 . TYR   B 1 66  ? 34.628 -32.048 6.904  1.00 19.35 ? 72  TYR   C CE1 1 
ATOM   1616 C  CE2 . TYR   B 1 66  ? 33.008 -30.294 7.044  1.00 18.36 ? 72  TYR   C CE2 1 
ATOM   1617 C  CZ  . TYR   B 1 66  ? 33.806 -31.130 6.283  1.00 19.96 ? 72  TYR   C CZ  1 
ATOM   1618 O  OH  . TYR   B 1 66  ? 33.812 -31.000 4.904  1.00 22.08 ? 72  TYR   C OH  1 
ATOM   1619 N  N   . PRO   B 1 67  ? 34.341 -33.585 13.074 1.00 13.90 ? 73  PRO   C N   1 
ATOM   1620 C  CA  . PRO   B 1 67  ? 34.841 -33.568 14.470 1.00 14.27 ? 73  PRO   C CA  1 
ATOM   1621 C  C   . PRO   B 1 67  ? 35.930 -32.502 14.594 1.00 15.86 ? 73  PRO   C C   1 
ATOM   1622 O  O   . PRO   B 1 67  ? 36.776 -32.361 13.694 1.00 17.37 ? 73  PRO   C O   1 
ATOM   1623 C  CB  . PRO   B 1 67  ? 35.410 -34.973 14.674 1.00 14.92 ? 73  PRO   C CB  1 
ATOM   1624 C  CG  . PRO   B 1 67  ? 35.616 -35.543 13.298 1.00 15.92 ? 73  PRO   C CG  1 
ATOM   1625 C  CD  . PRO   B 1 67  ? 34.867 -34.725 12.285 1.00 13.70 ? 73  PRO   C CD  1 
ATOM   1626 N  N   . VAL   B 1 68  ? 35.844 -31.674 15.629 1.00 14.40 ? 74  VAL   C N   1 
ATOM   1627 C  CA  . VAL   B 1 68  ? 36.791 -30.578 15.813 1.00 13.90 ? 74  VAL   C CA  1 
ATOM   1628 C  C   . VAL   B 1 68  ? 37.186 -30.397 17.264 1.00 14.43 ? 74  VAL   C C   1 
ATOM   1629 O  O   . VAL   B 1 68  ? 36.406 -30.743 18.178 1.00 14.13 ? 74  VAL   C O   1 
ATOM   1630 C  CB  . VAL   B 1 68  ? 36.215 -29.216 15.318 1.00 14.98 ? 74  VAL   C CB  1 
ATOM   1631 C  CG1 . VAL   B 1 68  ? 36.110 -29.141 13.804 1.00 16.40 ? 74  VAL   C CG1 1 
ATOM   1632 C  CG2 . VAL   B 1 68  ? 34.897 -28.872 16.008 1.00 15.47 ? 74  VAL   C CG2 1 
ATOM   1633 N  N   . SER   B 1 69  ? 38.398 -29.814 17.460 1.00 14.92 ? 75  SER   C N   1 
ATOM   1634 C  CA  . SER   B 1 69  ? 38.857 -29.286 18.743 1.00 14.72 ? 75  SER   C CA  1 
ATOM   1635 C  C   . SER   B 1 69  ? 38.618 -27.775 18.656 1.00 13.81 ? 75  SER   C C   1 
ATOM   1636 O  O   . SER   B 1 69  ? 38.830 -27.173 17.590 1.00 13.99 ? 75  SER   C O   1 
ATOM   1637 C  CB  . SER   B 1 69  ? 40.349 -29.534 18.963 1.00 17.24 ? 75  SER   C CB  1 
ATOM   1638 O  OG  . SER   B 1 69  ? 40.587 -30.930 19.055 1.00 23.92 ? 75  SER   C OG  1 
ATOM   1639 N  N   . PHE   B 1 70  ? 38.136 -27.153 19.739 1.00 12.89 ? 76  PHE   C N   1 
ATOM   1640 C  CA  . PHE   B 1 70  ? 37.817 -25.721 19.710 1.00 13.78 ? 76  PHE   C CA  1 
ATOM   1641 C  C   . PHE   B 1 70  ? 38.289 -24.996 20.959 1.00 15.09 ? 76  PHE   C C   1 
ATOM   1642 O  O   . PHE   B 1 70  ? 38.454 -25.616 22.024 1.00 15.27 ? 76  PHE   C O   1 
ATOM   1643 C  CB  . PHE   B 1 70  ? 36.322 -25.469 19.426 1.00 14.43 ? 76  PHE   C CB  1 
ATOM   1644 C  CG  . PHE   B 1 70  ? 35.365 -26.169 20.374 1.00 14.18 ? 76  PHE   C CG  1 
ATOM   1645 C  CD1 . PHE   B 1 70  ? 34.894 -27.447 20.093 1.00 14.53 ? 76  PHE   C CD1 1 
ATOM   1646 C  CD2 . PHE   B 1 70  ? 35.000 -25.579 21.573 1.00 14.95 ? 76  PHE   C CD2 1 
ATOM   1647 C  CE1 . PHE   B 1 70  ? 34.053 -28.107 20.989 1.00 14.78 ? 76  PHE   C CE1 1 
ATOM   1648 C  CE2 . PHE   B 1 70  ? 34.156 -26.235 22.454 1.00 15.15 ? 76  PHE   C CE2 1 
ATOM   1649 C  CZ  . PHE   B 1 70  ? 33.680 -27.494 22.148 1.00 13.65 ? 76  PHE   C CZ  1 
ATOM   1650 N  N   . SER   B 1 71  ? 38.588 -23.694 20.811 1.00 15.08 ? 77  SER   C N   1 
ATOM   1651 C  CA  . SER   B 1 71  ? 39.104 -22.897 21.935 1.00 16.82 ? 77  SER   C CA  1 
ATOM   1652 C  C   . SER   B 1 71  ? 37.983 -22.537 22.925 1.00 18.15 ? 77  SER   C C   1 
ATOM   1653 O  O   . SER   B 1 71  ? 36.806 -22.673 22.607 1.00 18.72 ? 77  SER   C O   1 
ATOM   1654 C  CB  . SER   B 1 71  ? 39.755 -21.626 21.391 1.00 17.88 ? 77  SER   C CB  1 
ATOM   1655 O  OG  . SER   B 1 71  ? 38.794 -20.824 20.715 1.00 18.60 ? 77  SER   C OG  1 
ATOM   1656 N  N   . LYS   B 1 72  ? 38.332 -22.102 24.148 1.00 19.50 ? 78  LYS   C N   1 
ATOM   1657 C  CA  . LYS   B 1 72  ? 37.346 -21.699 25.127 1.00 20.24 ? 78  LYS   C CA  1 
ATOM   1658 C  C   . LYS   B 1 72  ? 36.731 -20.339 24.718 1.00 21.40 ? 78  LYS   C C   1 
ATOM   1659 O  O   . LYS   B 1 72  ? 37.382 -19.530 24.023 1.00 21.99 ? 78  LYS   C O   1 
ATOM   1660 C  CB  . LYS   B 1 72  ? 37.996 -21.628 26.535 1.00 23.51 ? 78  LYS   C CB  1 
ATOM   1661 C  CG  . LYS   B 1 72  ? 38.254 -23.038 27.123 1.00 28.86 ? 78  LYS   C CG  1 
ATOM   1662 C  CD  . LYS   B 1 72  ? 38.618 -22.983 28.611 1.00 34.94 ? 78  LYS   C CD  1 
ATOM   1663 C  CE  . LYS   B 1 72  ? 39.083 -24.326 29.130 1.00 39.71 ? 78  LYS   C CE  1 
ATOM   1664 N  NZ  . LYS   B 1 72  ? 39.331 -24.293 30.612 1.00 42.96 ? 78  LYS   C NZ  1 
ATOM   1665 N  N   . PRO   B 1 73  ? 35.471 -20.082 25.132 1.00 20.89 ? 79  PRO   C N   1 
ATOM   1666 C  CA  . PRO   B 1 73  ? 34.809 -18.832 24.718 1.00 21.26 ? 79  PRO   C CA  1 
ATOM   1667 C  C   . PRO   B 1 73  ? 35.591 -17.604 25.141 1.00 21.23 ? 79  PRO   C C   1 
ATOM   1668 O  O   . PRO   B 1 73  ? 35.989 -17.514 26.292 1.00 21.21 ? 79  PRO   C O   1 
ATOM   1669 C  CB  . PRO   B 1 73  ? 33.459 -18.867 25.426 1.00 22.43 ? 79  PRO   C CB  1 
ATOM   1670 C  CG  . PRO   B 1 73  ? 33.279 -20.252 25.899 1.00 23.70 ? 79  PRO   C CG  1 
ATOM   1671 C  CD  . PRO   B 1 73  ? 34.591 -20.940 25.953 1.00 20.66 ? 79  PRO   C CD  1 
ATOM   1672 N  N   . SER   B 1 74  ? 35.901 -16.706 24.178 1.00 20.76 ? 80  SER   C N   1 
ATOM   1673 C  CA  . SER   B 1 74  ? 36.711 -15.523 24.451 1.00 21.72 ? 80  SER   C CA  1 
ATOM   1674 C  C   . SER   B 1 74  ? 36.308 -14.313 23.587 1.00 21.73 ? 80  SER   C C   1 
ATOM   1675 O  O   . SER   B 1 74  ? 35.449 -14.437 22.707 1.00 20.22 ? 80  SER   C O   1 
ATOM   1676 C  CB  . SER   B 1 74  ? 38.180 -15.842 24.198 1.00 23.75 ? 80  SER   C CB  1 
ATOM   1677 O  OG  . SER   B 1 74  ? 38.611 -17.033 24.840 1.00 27.54 ? 80  SER   C OG  1 
ATOM   1678 N  N   . LEU   B 1 75  ? 36.949 -13.157 23.818 1.00 22.72 ? 81  LEU   C N   1 
ATOM   1679 C  CA  . LEU   B 1 75  ? 36.719 -11.926 23.057 1.00 24.41 ? 81  LEU   C CA  1 
ATOM   1680 C  C   . LEU   B 1 75  ? 37.758 -11.955 21.946 1.00 26.02 ? 81  LEU   C C   1 
ATOM   1681 O  O   . LEU   B 1 75  ? 38.961 -11.902 22.237 1.00 26.91 ? 81  LEU   C O   1 
ATOM   1682 C  CB  . LEU   B 1 75  ? 36.966 -10.701 23.974 1.00 25.61 ? 81  LEU   C CB  1 
ATOM   1683 C  CG  . LEU   B 1 75  ? 36.703 -9.319  23.353 1.00 28.40 ? 81  LEU   C CG  1 
ATOM   1684 C  CD1 . LEU   B 1 75  ? 35.241 -9.135  23.021 1.00 29.69 ? 81  LEU   C CD1 1 
ATOM   1685 C  CD2 . LEU   B 1 75  ? 37.119 -8.204  24.319 1.00 29.45 ? 81  LEU   C CD2 1 
ATOM   1686 N  N   . ILE   B 1 76  ? 37.327 -12.082 20.692 1.00 25.33 ? 82  ILE   C N   1 
ATOM   1687 C  CA  . ILE   B 1 76  ? 38.255 -12.232 19.578 1.00 26.04 ? 82  ILE   C CA  1 
ATOM   1688 C  C   . ILE   B 1 76  ? 37.990 -11.234 18.465 1.00 26.39 ? 82  ILE   C C   1 
ATOM   1689 O  O   . ILE   B 1 76  ? 36.830 -10.987 18.135 1.00 26.73 ? 82  ILE   C O   1 
ATOM   1690 C  CB  . ILE   B 1 76  ? 38.100 -13.681 19.029 1.00 26.73 ? 82  ILE   C CB  1 
ATOM   1691 C  CG1 . ILE   B 1 76  ? 38.555 -14.705 20.068 1.00 27.60 ? 82  ILE   C CG1 1 
ATOM   1692 C  CG2 . ILE   B 1 76  ? 38.822 -13.879 17.698 1.00 27.84 ? 82  ILE   C CG2 1 
ATOM   1693 C  CD1 . ILE   B 1 76  ? 38.374 -16.119 19.652 1.00 28.38 ? 82  ILE   C CD1 1 
ATOM   1694 N  N   . PHE   B 1 77  ? 39.063 -10.700 17.845 1.00 26.33 ? 83  PHE   C N   1 
ATOM   1695 C  CA  . PHE   B 1 77  ? 38.867 -9.824  16.700 1.00 26.40 ? 83  PHE   C CA  1 
ATOM   1696 C  C   . PHE   B 1 77  ? 38.461 -10.684 15.499 1.00 25.97 ? 83  PHE   C C   1 
ATOM   1697 O  O   . PHE   B 1 77  ? 39.074 -11.730 15.239 1.00 26.96 ? 83  PHE   C O   1 
ATOM   1698 C  CB  . PHE   B 1 77  ? 40.128 -9.026  16.378 1.00 26.73 ? 83  PHE   C CB  1 
ATOM   1699 C  CG  . PHE   B 1 77  ? 39.841 -7.920  15.390 1.00 28.35 ? 83  PHE   C CG  1 
ATOM   1700 C  CD1 . PHE   B 1 77  ? 39.208 -6.760  15.790 1.00 29.57 ? 83  PHE   C CD1 1 
ATOM   1701 C  CD2 . PHE   B 1 77  ? 40.219 -8.037  14.067 1.00 29.80 ? 83  PHE   C CD2 1 
ATOM   1702 C  CE1 . PHE   B 1 77  ? 38.940 -5.740  14.876 1.00 30.53 ? 83  PHE   C CE1 1 
ATOM   1703 C  CE2 . PHE   B 1 77  ? 39.945 -7.028  13.156 1.00 31.05 ? 83  PHE   C CE2 1 
ATOM   1704 C  CZ  . PHE   B 1 77  ? 39.296 -5.892  13.559 1.00 30.67 ? 83  PHE   C CZ  1 
ATOM   1705 N  N   . VAL   B 1 78  ? 37.399 -10.276 14.800 1.00 23.71 ? 84  VAL   C N   1 
ATOM   1706 C  CA  . VAL   B 1 78  ? 36.909 -11.010 13.656 1.00 22.71 ? 84  VAL   C CA  1 
ATOM   1707 C  C   . VAL   B 1 78  ? 37.039 -10.136 12.420 1.00 23.00 ? 84  VAL   C C   1 
ATOM   1708 O  O   . VAL   B 1 78  ? 36.531 -9.023  12.438 1.00 22.81 ? 84  VAL   C O   1 
ATOM   1709 C  CB  . VAL   B 1 78  ? 35.418 -11.423 13.899 1.00 23.40 ? 84  VAL   C CB  1 
ATOM   1710 C  CG1 . VAL   B 1 78  ? 34.883 -12.181 12.693 1.00 24.42 ? 84  VAL   C CG1 1 
ATOM   1711 C  CG2 . VAL   B 1 78  ? 35.277 -12.267 15.166 1.00 23.79 ? 84  VAL   C CG2 1 
ATOM   1712 N  N   . GLU   B 1 79  ? 37.653 -10.638 11.333 1.00 23.01 ? 85  GLU   C N   1 
ATOM   1713 C  CA  . GLU   B 1 79  ? 37.758 -9.868  10.077 1.00 24.06 ? 85  GLU   C CA  1 
ATOM   1714 C  C   . GLU   B 1 79  ? 36.361 -9.601  9.491  1.00 24.30 ? 85  GLU   C C   1 
ATOM   1715 O  O   . GLU   B 1 79  ? 35.415 -10.325 9.799  1.00 23.65 ? 85  GLU   C O   1 
ATOM   1716 C  CB  . GLU   B 1 79  ? 38.586 -10.640 9.028  1.00 27.29 ? 85  GLU   C CB  1 
ATOM   1717 C  CG  . GLU   B 1 79  ? 40.078 -10.702 9.325  1.00 31.24 ? 85  GLU   C CG  1 
ATOM   1718 C  CD  . GLU   B 1 79  ? 40.746 -9.352  9.546  1.00 37.05 ? 85  GLU   C CD  1 
ATOM   1719 O  OE1 . GLU   B 1 79  ? 40.387 -8.366  8.856  1.00 40.08 ? 85  GLU   C OE1 1 
ATOM   1720 O  OE2 . GLU   B 1 79  ? 41.622 -9.278  10.439 1.00 36.47 ? 85  GLU   C OE2 1 
ATOM   1721 N  N   . ALA   B 1 80  ? 36.245 -8.594  8.617  1.00 25.11 ? 86  ALA   C N   1 
ATOM   1722 C  CA  . ALA   B 1 80  ? 34.970 -8.263  8.007  1.00 25.76 ? 86  ALA   C CA  1 
ATOM   1723 C  C   . ALA   B 1 80  ? 34.381 -9.453  7.218  1.00 25.95 ? 86  ALA   C C   1 
ATOM   1724 O  O   . ALA   B 1 80  ? 35.128 -10.200 6.584  1.00 25.75 ? 86  ALA   C O   1 
ATOM   1725 C  CB  . ALA   B 1 80  ? 35.132 -7.047  7.092  1.00 25.15 ? 86  ALA   C CB  1 
ATOM   1726 N  N   . SER   B 1 81  ? 33.042 -9.639  7.302  1.00 25.17 ? 87  SER   C N   1 
ATOM   1727 C  CA  . SER   B 1 81  ? 32.294 -10.682 6.588  1.00 25.76 ? 87  SER   C CA  1 
ATOM   1728 C  C   . SER   B 1 81  ? 31.170 -10.009 5.765  1.00 26.79 ? 87  SER   C C   1 
ATOM   1729 O  O   . SER   B 1 81  ? 31.075 -8.762  5.773  1.00 27.35 ? 87  SER   C O   1 
ATOM   1730 C  CB  . SER   B 1 81  ? 31.718 -11.710 7.573  1.00 25.66 ? 87  SER   C CB  1 
ATOM   1731 O  OG  . SER   B 1 81  ? 30.659 -11.141 8.330  1.00 25.13 ? 87  SER   C OG  1 
ATOM   1732 N  N   . GLU   B 1 82  ? 30.301 -10.788 5.067  1.00 26.55 ? 88  GLU   C N   1 
ATOM   1733 C  CA  . GLU   B 1 82  ? 29.228 -10.131 4.279  1.00 26.96 ? 88  GLU   C CA  1 
ATOM   1734 C  C   . GLU   B 1 82  ? 28.069 -9.555  5.157  1.00 26.00 ? 88  GLU   C C   1 
ATOM   1735 O  O   . GLU   B 1 82  ? 27.267 -8.741  4.680  1.00 25.85 ? 88  GLU   C O   1 
ATOM   1736 C  CB  . GLU   B 1 82  ? 28.688 -11.044 3.161  1.00 30.51 ? 88  GLU   C CB  1 
ATOM   1737 C  CG  . GLU   B 1 82  ? 28.110 -12.351 3.658  1.00 39.50 ? 88  GLU   C CG  1 
ATOM   1738 C  CD  . GLU   B 1 82  ? 27.173 -13.070 2.696  1.00 48.41 ? 88  GLU   C CD  1 
ATOM   1739 O  OE1 . GLU   B 1 82  ? 27.584 -13.325 1.539  1.00 48.94 ? 88  GLU   C OE1 1 
ATOM   1740 O  OE2 . GLU   B 1 82  ? 26.035 -13.399 3.114  1.00 50.77 ? 88  GLU   C OE2 1 
ATOM   1741 N  N   . TYR   B 1 83  ? 28.023 -9.955  6.447  1.00 24.94 ? 89  TYR   C N   1 
ATOM   1742 C  CA  . TYR   B 1 83  ? 26.965 -9.573  7.375  1.00 24.16 ? 89  TYR   C CA  1 
ATOM   1743 C  C   . TYR   B 1 83  ? 27.441 -8.706  8.587  1.00 24.38 ? 89  TYR   C C   1 
ATOM   1744 O  O   . TYR   B 1 83  ? 26.601 -8.162  9.299  1.00 24.78 ? 89  TYR   C O   1 
ATOM   1745 C  CB  . TYR   B 1 83  ? 26.208 -10.842 7.846  1.00 23.01 ? 89  TYR   C CB  1 
ATOM   1746 C  CG  . TYR   B 1 83  ? 27.096 -11.959 8.358  1.00 22.12 ? 89  TYR   C CG  1 
ATOM   1747 C  CD1 . TYR   B 1 83  ? 27.553 -12.963 7.506  1.00 22.25 ? 89  TYR   C CD1 1 
ATOM   1748 C  CD2 . TYR   B 1 83  ? 27.425 -12.049 9.701  1.00 22.05 ? 89  TYR   C CD2 1 
ATOM   1749 C  CE1 . TYR   B 1 83  ? 28.357 -14.000 7.973  1.00 22.30 ? 89  TYR   C CE1 1 
ATOM   1750 C  CE2 . TYR   B 1 83  ? 28.230 -13.082 10.183 1.00 22.47 ? 89  TYR   C CE2 1 
ATOM   1751 C  CZ  . TYR   B 1 83  ? 28.699 -14.050 9.314  1.00 23.14 ? 89  TYR   C CZ  1 
ATOM   1752 O  OH  . TYR   B 1 83  ? 29.474 -15.081 9.794  1.00 23.10 ? 89  TYR   C OH  1 
ATOM   1753 N  N   . TYR   B 1 84  ? 28.767 -8.570  8.814  1.00 23.30 ? 90  TYR   C N   1 
ATOM   1754 C  CA  . TYR   B 1 84  ? 29.305 -7.696  9.876  1.00 22.81 ? 90  TYR   C CA  1 
ATOM   1755 C  C   . TYR   B 1 84  ? 30.613 -7.043  9.390  1.00 24.07 ? 90  TYR   C C   1 
ATOM   1756 O  O   . TYR   B 1 84  ? 31.357 -7.652  8.625  1.00 24.23 ? 90  TYR   C O   1 
ATOM   1757 C  CB  . TYR   B 1 84  ? 29.678 -8.500  11.136 1.00 21.48 ? 90  TYR   C CB  1 
ATOM   1758 C  CG  . TYR   B 1 84  ? 28.517 -8.893  12.025 1.00 20.54 ? 90  TYR   C CG  1 
ATOM   1759 C  CD1 . TYR   B 1 84  ? 27.593 -7.950  12.461 1.00 20.67 ? 90  TYR   C CD1 1 
ATOM   1760 C  CD2 . TYR   B 1 84  ? 28.356 -10.206 12.450 1.00 20.70 ? 90  TYR   C CD2 1 
ATOM   1761 C  CE1 . TYR   B 1 84  ? 26.528 -8.311  13.290 1.00 21.02 ? 90  TYR   C CE1 1 
ATOM   1762 C  CE2 . TYR   B 1 84  ? 27.306 -10.577 13.271 1.00 20.79 ? 90  TYR   C CE2 1 
ATOM   1763 C  CZ  . TYR   B 1 84  ? 26.388 -9.628  13.694 1.00 21.55 ? 90  TYR   C CZ  1 
ATOM   1764 O  OH  . TYR   B 1 84  ? 25.353 -10.013 14.510 1.00 21.57 ? 90  TYR   C OH  1 
ATOM   1765 N  N   . PRO   B 1 85  ? 30.938 -5.836  9.889  1.00 24.81 ? 91  PRO   C N   1 
ATOM   1766 C  CA  . PRO   B 1 85  ? 32.254 -5.260  9.577  1.00 25.76 ? 91  PRO   C CA  1 
ATOM   1767 C  C   . PRO   B 1 85  ? 33.331 -5.975  10.428 1.00 26.05 ? 91  PRO   C C   1 
ATOM   1768 O  O   . PRO   B 1 85  ? 33.006 -6.886  11.218 1.00 24.71 ? 91  PRO   C O   1 
ATOM   1769 C  CB  . PRO   B 1 85  ? 32.094 -3.795  9.989  1.00 27.03 ? 91  PRO   C CB  1 
ATOM   1770 C  CG  . PRO   B 1 85  ? 31.079 -3.821  11.113 1.00 27.09 ? 91  PRO   C CG  1 
ATOM   1771 C  CD  . PRO   B 1 85  ? 30.166 -5.012  10.856 1.00 24.42 ? 91  PRO   C CD  1 
ATOM   1772 N  N   . ALA   B 1 86  ? 34.603 -5.549  10.305 1.00 25.27 ? 92  ALA   C N   1 
ATOM   1773 C  CA  . ALA   B 1 86  ? 35.661 -6.115  11.146 1.00 26.10 ? 92  ALA   C CA  1 
ATOM   1774 C  C   . ALA   B 1 86  ? 35.383 -5.617  12.597 1.00 26.69 ? 92  ALA   C C   1 
ATOM   1775 O  O   . ALA   B 1 86  ? 35.161 -4.411  12.777 1.00 27.59 ? 92  ALA   C O   1 
ATOM   1776 C  CB  . ALA   B 1 86  ? 37.008 -5.610  10.665 1.00 26.15 ? 92  ALA   C CB  1 
ATOM   1777 N  N   . ARG   B 1 87  ? 35.299 -6.535  13.600 1.00 25.47 ? 93  ARG   C N   1 
ATOM   1778 C  CA  . ARG   B 1 87  ? 35.003 -6.124  14.974 1.00 24.62 ? 93  ARG   C CA  1 
ATOM   1779 C  C   . ARG   B 1 87  ? 35.351 -7.187  16.007 1.00 24.62 ? 93  ARG   C C   1 
ATOM   1780 O  O   . ARG   B 1 87  ? 35.515 -8.358  15.642 1.00 23.26 ? 93  ARG   C O   1 
ATOM   1781 C  CB  . ARG   B 1 87  ? 33.493 -5.828  15.105 1.00 23.80 ? 93  ARG   C CB  1 
ATOM   1782 C  CG  . ARG   B 1 87  ? 32.656 -7.029  14.690 1.00 23.20 ? 93  ARG   C CG  1 
ATOM   1783 C  CD  . ARG   B 1 87  ? 31.172 -6.904  15.021 1.00 23.14 ? 93  ARG   C CD  1 
ATOM   1784 N  NE  . ARG   B 1 87  ? 30.563 -8.227  15.211 1.00 21.48 ? 93  ARG   C NE  1 
ATOM   1785 C  CZ  . ARG   B 1 87  ? 29.464 -8.450  15.932 1.00 24.04 ? 93  ARG   C CZ  1 
ATOM   1786 N  NH1 . ARG   B 1 87  ? 28.834 -7.443  16.525 1.00 23.99 ? 93  ARG   C NH1 1 
ATOM   1787 N  NH2 . ARG   B 1 87  ? 28.994 -9.687  16.074 1.00 24.34 ? 93  ARG   C NH2 1 
ATOM   1788 N  N   . TYR   B 1 88  ? 35.308 -6.820  17.323 1.00 25.24 ? 94  TYR   C N   1 
ATOM   1789 C  CA  . TYR   B 1 88  ? 35.505 -7.818  18.385 1.00 25.81 ? 94  TYR   C CA  1 
ATOM   1790 C  C   . TYR   B 1 88  ? 34.187 -8.500  18.673 1.00 24.21 ? 94  TYR   C C   1 
ATOM   1791 O  O   . TYR   B 1 88  ? 33.169 -7.823  18.815 1.00 24.88 ? 94  TYR   C O   1 
ATOM   1792 C  CB  . TYR   B 1 88  ? 36.046 -7.190  19.685 1.00 27.47 ? 94  TYR   C CB  1 
ATOM   1793 C  CG  . TYR   B 1 88  ? 37.528 -6.906  19.617 1.00 29.62 ? 94  TYR   C CG  1 
ATOM   1794 C  CD1 . TYR   B 1 88  ? 38.454 -7.903  19.869 1.00 31.38 ? 94  TYR   C CD1 1 
ATOM   1795 C  CD2 . TYR   B 1 88  ? 37.999 -5.654  19.236 1.00 31.68 ? 94  TYR   C CD2 1 
ATOM   1796 C  CE1 . TYR   B 1 88  ? 39.817 -7.650  19.795 1.00 33.17 ? 94  TYR   C CE1 1 
ATOM   1797 C  CE2 . TYR   B 1 88  ? 39.356 -5.389  19.153 1.00 32.91 ? 94  TYR   C CE2 1 
ATOM   1798 C  CZ  . TYR   B 1 88  ? 40.266 -6.393  19.421 1.00 34.54 ? 94  TYR   C CZ  1 
ATOM   1799 O  OH  . TYR   B 1 88  ? 41.617 -6.128  19.338 1.00 37.29 ? 94  TYR   C OH  1 
ATOM   1800 N  N   . GLN   B 1 89  ? 34.184 -9.822  18.706 1.00 22.35 ? 95  GLN   C N   1 
ATOM   1801 C  CA  . GLN   B 1 89  ? 32.984 -10.588 19.026 1.00 21.33 ? 95  GLN   C CA  1 
ATOM   1802 C  C   . GLN   B 1 89  ? 33.269 -11.346 20.339 1.00 20.93 ? 95  GLN   C C   1 
ATOM   1803 O  O   . GLN   B 1 89  ? 34.354 -11.928 20.494 1.00 21.45 ? 95  GLN   C O   1 
ATOM   1804 C  CB  . GLN   B 1 89  ? 32.649 -11.571 17.880 1.00 21.17 ? 95  GLN   C CB  1 
ATOM   1805 C  CG  . GLN   B 1 89  ? 31.432 -12.421 18.190 1.00 20.76 ? 95  GLN   C CG  1 
ATOM   1806 C  CD  . GLN   B 1 89  ? 30.727 -12.987 16.971 1.00 20.93 ? 95  GLN   C CD  1 
ATOM   1807 O  OE1 . GLN   B 1 89  ? 30.678 -12.390 15.891 1.00 22.38 ? 95  GLN   C OE1 1 
ATOM   1808 N  NE2 . GLN   B 1 89  ? 30.167 -14.155 17.149 1.00 21.70 ? 95  GLN   C NE2 1 
ATOM   1809 N  N   . SER   B 1 90  ? 32.334 -11.307 21.291 1.00 19.36 ? 96  SER   C N   1 
ATOM   1810 C  CA  . SER   B 1 90  ? 32.545 -11.978 22.582 1.00 18.29 ? 96  SER   C CA  1 
ATOM   1811 C  C   . SER   B 1 90  ? 31.953 -13.396 22.616 1.00 17.47 ? 96  SER   C C   1 
ATOM   1812 O  O   . SER   B 1 90  ? 31.150 -13.757 21.746 1.00 17.03 ? 96  SER   C O   1 
ATOM   1813 C  CB  . SER   B 1 90  ? 31.977 -11.135 23.728 1.00 18.87 ? 96  SER   C CB  1 
ATOM   1814 O  OG  . SER   B 1 90  ? 30.578 -11.050 23.580 1.00 20.09 ? 96  SER   C OG  1 
ATOM   1815 N  N   . HIS   B 1 91  ? 32.349 -14.176 23.629 1.00 16.77 ? 97  HIS   C N   1 
ATOM   1816 C  CA  . HIS   B 1 91  ? 31.892 -15.550 23.860 1.00 16.73 ? 97  HIS   C CA  1 
ATOM   1817 C  C   . HIS   B 1 91  ? 32.052 -16.418 22.596 1.00 16.57 ? 97  HIS   C C   1 
ATOM   1818 O  O   . HIS   B 1 91  ? 31.205 -17.283 22.318 1.00 16.91 ? 97  HIS   C O   1 
ATOM   1819 C  CB  . HIS   B 1 91  ? 30.447 -15.568 24.428 1.00 16.54 ? 97  HIS   C CB  1 
ATOM   1820 C  CG  . HIS   B 1 91  ? 30.307 -14.796 25.719 1.00 20.33 ? 97  HIS   C CG  1 
ATOM   1821 N  ND1 . HIS   B 1 91  ? 30.353 -15.436 26.946 1.00 22.04 ? 97  HIS   C ND1 1 
ATOM   1822 C  CD2 . HIS   B 1 91  ? 30.167 -13.456 25.931 1.00 22.11 ? 97  HIS   C CD2 1 
ATOM   1823 C  CE1 . HIS   B 1 91  ? 30.238 -14.481 27.862 1.00 22.56 ? 97  HIS   C CE1 1 
ATOM   1824 N  NE2 . HIS   B 1 91  ? 30.101 -13.274 27.302 1.00 22.23 ? 97  HIS   C NE2 1 
ATOM   1825 N  N   . LEU   B 1 92  ? 33.164 -16.189 21.862 1.00 15.60 ? 98  LEU   C N   1 
ATOM   1826 C  CA  . LEU   B 1 92  ? 33.439 -16.881 20.600 1.00 15.83 ? 98  LEU   C CA  1 
ATOM   1827 C  C   . LEU   B 1 92  ? 34.520 -17.954 20.786 1.00 15.65 ? 98  LEU   C C   1 
ATOM   1828 O  O   . LEU   B 1 92  ? 35.488 -17.748 21.522 1.00 15.39 ? 98  LEU   C O   1 
ATOM   1829 C  CB  . LEU   B 1 92  ? 33.890 -15.848 19.525 1.00 15.35 ? 98  LEU   C CB  1 
ATOM   1830 C  CG  . LEU   B 1 92  ? 34.076 -16.393 18.096 1.00 16.40 ? 98  LEU   C CG  1 
ATOM   1831 C  CD1 . LEU   B 1 92  ? 32.771 -16.826 17.504 1.00 15.37 ? 98  LEU   C CD1 1 
ATOM   1832 C  CD2 . LEU   B 1 92  ? 34.767 -15.362 17.164 1.00 17.64 ? 98  LEU   C CD2 1 
ATOM   1833 N  N   . MET   B 1 93  ? 34.320 -19.117 20.154 1.00 15.20 ? 99  MET   C N   1 
ATOM   1834 C  CA  . MET   B 1 93  ? 35.218 -20.280 20.190 1.00 14.73 ? 99  MET   C CA  1 
ATOM   1835 C  C   . MET   B 1 93  ? 35.671 -20.526 18.722 1.00 14.83 ? 99  MET   C C   1 
ATOM   1836 O  O   . MET   B 1 93  ? 34.838 -20.473 17.840 1.00 15.14 ? 99  MET   C O   1 
ATOM   1837 C  CB  . MET   B 1 93  ? 34.439 -21.521 20.689 1.00 16.16 ? 99  MET   C CB  1 
ATOM   1838 C  CG  . MET   B 1 93  ? 33.885 -21.327 22.088 1.00 17.97 ? 99  MET   C CG  1 
ATOM   1839 S  SD  . MET   B 1 93  ? 32.812 -22.669 22.641 1.00 21.39 ? 99  MET   C SD  1 
ATOM   1840 C  CE  . MET   B 1 93  ? 31.481 -22.496 21.514 1.00 16.51 ? 99  MET   C CE  1 
ATOM   1841 N  N   . LEU   B 1 94  ? 36.915 -20.845 18.484 1.00 14.72 ? 100 LEU   C N   1 
ATOM   1842 C  CA  . LEU   B 1 94  ? 37.419 -21.076 17.130 1.00 15.88 ? 100 LEU   C CA  1 
ATOM   1843 C  C   . LEU   B 1 94  ? 37.923 -22.503 16.991 1.00 14.75 ? 100 LEU   C C   1 
ATOM   1844 O  O   . LEU   B 1 94  ? 38.496 -23.072 17.923 1.00 15.95 ? 100 LEU   C O   1 
ATOM   1845 C  CB  . LEU   B 1 94  ? 38.602 -20.120 16.804 1.00 18.02 ? 100 LEU   C CB  1 
ATOM   1846 C  CG  . LEU   B 1 94  ? 38.307 -18.623 16.787 1.00 21.10 ? 100 LEU   C CG  1 
ATOM   1847 C  CD1 . LEU   B 1 94  ? 39.592 -17.802 16.599 1.00 23.77 ? 100 LEU   C CD1 1 
ATOM   1848 C  CD2 . LEU   B 1 94  ? 37.262 -18.280 15.723 1.00 22.09 ? 100 LEU   C CD2 1 
ATOM   1849 N  N   . ALA   B 1 95  ? 37.776 -23.036 15.781 1.00 14.14 ? 101 ALA   C N   1 
ATOM   1850 C  CA  . ALA   B 1 95  ? 38.285 -24.347 15.380 1.00 14.81 ? 101 ALA   C CA  1 
ATOM   1851 C  C   . ALA   B 1 95  ? 38.854 -24.247 13.944 1.00 15.84 ? 101 ALA   C C   1 
ATOM   1852 O  O   . ALA   B 1 95  ? 38.557 -23.299 13.208 1.00 15.88 ? 101 ALA   C O   1 
ATOM   1853 C  CB  . ALA   B 1 95  ? 37.166 -25.391 15.423 1.00 14.80 ? 101 ALA   C CB  1 
ATOM   1854 N  N   . VAL   B 1 96  ? 39.688 -25.222 13.551 1.00 16.54 ? 102 VAL   C N   1 
ATOM   1855 C  CA  . VAL   B 1 96  ? 40.200 -25.257 12.190 1.00 17.07 ? 102 VAL   C CA  1 
ATOM   1856 C  C   . VAL   B 1 96  ? 39.168 -26.023 11.379 1.00 18.12 ? 102 VAL   C C   1 
ATOM   1857 O  O   . VAL   B 1 96  ? 38.890 -27.209 11.652 1.00 19.00 ? 102 VAL   C O   1 
ATOM   1858 C  CB  . VAL   B 1 96  ? 41.596 -25.938 12.106 1.00 17.32 ? 102 VAL   C CB  1 
ATOM   1859 C  CG1 . VAL   B 1 96  ? 42.035 -26.100 10.659 1.00 17.82 ? 102 VAL   C CG1 1 
ATOM   1860 C  CG2 . VAL   B 1 96  ? 42.628 -25.170 12.932 1.00 18.18 ? 102 VAL   C CG2 1 
ATOM   1861 N  N   . GLY   B 1 97  ? 38.587 -25.358 10.407 1.00 18.05 ? 103 GLY   C N   1 
ATOM   1862 C  CA  . GLY   B 1 97  ? 37.557 -25.991 9.580  1.00 18.66 ? 103 GLY   C CA  1 
ATOM   1863 C  C   . GLY   B 1 97  ? 36.917 -25.035 8.611  1.00 19.35 ? 103 GLY   C C   1 
ATOM   1864 O  O   . GLY   B 1 97  ? 37.205 -23.838 8.623  1.00 19.84 ? 103 GLY   C O   1 
ATOM   1865 N  N   . HIS   B 1 98  ? 36.045 -25.547 7.766  1.00 18.63 ? 104 HIS   C N   1 
ATOM   1866 C  CA  . HIS   B 1 98  ? 35.401 -24.737 6.757  1.00 18.94 ? 104 HIS   C CA  1 
ATOM   1867 C  C   . HIS   B 1 98  ? 34.102 -24.079 7.272  1.00 19.15 ? 104 HIS   C C   1 
ATOM   1868 O  O   . HIS   B 1 98  ? 33.275 -24.727 7.925  1.00 18.92 ? 104 HIS   C O   1 
ATOM   1869 C  CB  . HIS   B 1 98  ? 35.125 -25.575 5.528  1.00 21.47 ? 104 HIS   C CB  1 
ATOM   1870 C  CG  . HIS   B 1 98  ? 34.549 -24.763 4.421  1.00 25.77 ? 104 HIS   C CG  1 
ATOM   1871 N  ND1 . HIS   B 1 98  ? 35.276 -23.740 3.787  1.00 28.44 ? 104 HIS   C ND1 1 
ATOM   1872 C  CD2 . HIS   B 1 98  ? 33.293 -24.774 3.935  1.00 27.48 ? 104 HIS   C CD2 1 
ATOM   1873 C  CE1 . HIS   B 1 98  ? 34.447 -23.205 2.911  1.00 29.33 ? 104 HIS   C CE1 1 
ATOM   1874 N  NE2 . HIS   B 1 98  ? 33.243 -23.805 2.951  1.00 29.24 ? 104 HIS   C NE2 1 
ATOM   1875 N  N   . SER   B 1 99  ? 33.905 -22.787 6.937  1.00 18.92 ? 105 SER   C N   1 
ATOM   1876 C  CA  . SER   B 1 99  ? 32.711 -22.008 7.304  1.00 19.08 ? 105 SER   C CA  1 
ATOM   1877 C  C   . SER   B 1 99  ? 32.488 -20.847 6.294  1.00 20.44 ? 105 SER   C C   1 
ATOM   1878 O  O   . SER   B 1 99  ? 33.356 -19.978 6.195  1.00 20.67 ? 105 SER   C O   1 
ATOM   1879 C  CB  . SER   B 1 99  ? 32.898 -21.399 8.688  1.00 19.38 ? 105 SER   C CB  1 
ATOM   1880 O  OG  . SER   B 1 99  ? 31.871 -20.464 8.983  1.00 21.60 ? 105 SER   C OG  1 
ATOM   1881 N  N   . GLU   B 1 100 ? 31.322 -20.831 5.615  1.00 20.80 ? 106 GLU   C N   1 
ATOM   1882 C  CA  . GLU   B 1 100 ? 30.843 -19.772 4.716  1.00 21.47 ? 106 GLU   C CA  1 
ATOM   1883 C  C   . GLU   B 1 100 ? 29.663 -19.066 5.396  1.00 22.29 ? 106 GLU   C C   1 
ATOM   1884 O  O   . GLU   B 1 100 ? 29.067 -19.625 6.311  1.00 21.23 ? 106 GLU   C O   1 
ATOM   1885 C  CB  . GLU   B 1 100 ? 30.412 -20.380 3.378  1.00 23.41 ? 106 GLU   C CB  1 
ATOM   1886 C  CG  . GLU   B 1 100 ? 31.611 -20.901 2.636  1.00 31.13 ? 106 GLU   C CG  1 
ATOM   1887 C  CD  . GLU   B 1 100 ? 31.304 -21.601 1.339  1.00 36.58 ? 106 GLU   C CD  1 
ATOM   1888 O  OE1 . GLU   B 1 100 ? 30.303 -21.238 0.691  1.00 44.40 ? 106 GLU   C OE1 1 
ATOM   1889 O  OE2 . GLU   B 1 100 ? 32.072 -22.510 0.965  1.00 35.93 ? 106 GLU   C OE2 1 
ATOM   1890 N  N   . PRO   B 1 101 ? 29.271 -17.853 4.955  1.00 23.07 ? 107 PRO   C N   1 
ATOM   1891 C  CA  . PRO   B 1 101 ? 28.159 -17.160 5.628  1.00 22.43 ? 107 PRO   C CA  1 
ATOM   1892 C  C   . PRO   B 1 101 ? 26.872 -17.986 5.820  1.00 21.85 ? 107 PRO   C C   1 
ATOM   1893 O  O   . PRO   B 1 101 ? 26.273 -17.954 6.909  1.00 21.22 ? 107 PRO   C O   1 
ATOM   1894 C  CB  . PRO   B 1 101 ? 27.919 -15.927 4.746  1.00 23.99 ? 107 PRO   C CB  1 
ATOM   1895 C  CG  . PRO   B 1 101 ? 29.244 -15.672 4.100  1.00 25.66 ? 107 PRO   C CG  1 
ATOM   1896 C  CD  . PRO   B 1 101 ? 29.883 -17.026 3.895  1.00 23.21 ? 107 PRO   C CD  1 
ATOM   1897 N  N   . GLY   B 1 102 ? 26.493 -18.761 4.798  1.00 21.23 ? 108 GLY   C N   1 
ATOM   1898 C  CA  . GLY   B 1 102 ? 25.311 -19.621 4.876  1.00 20.81 ? 108 GLY   C CA  1 
ATOM   1899 C  C   . GLY   B 1 102 ? 25.409 -20.755 5.889  1.00 18.96 ? 108 GLY   C C   1 
ATOM   1900 O  O   . GLY   B 1 102 ? 24.395 -21.391 6.230  1.00 18.21 ? 108 GLY   C O   1 
ATOM   1901 N  N   . ASP   B 1 103 ? 26.626 -21.033 6.389  1.00 16.83 ? 109 ASP   C N   1 
ATOM   1902 C  CA  . ASP   B 1 103 ? 26.792 -22.086 7.420  1.00 15.90 ? 109 ASP   C CA  1 
ATOM   1903 C  C   . ASP   B 1 103 ? 26.381 -21.621 8.814  1.00 15.31 ? 109 ASP   C C   1 
ATOM   1904 O  O   . ASP   B 1 103 ? 26.277 -22.441 9.727  1.00 14.28 ? 109 ASP   C O   1 
ATOM   1905 C  CB  . ASP   B 1 103 ? 28.222 -22.636 7.508  1.00 16.14 ? 109 ASP   C CB  1 
ATOM   1906 C  CG  . ASP   B 1 103 ? 28.624 -23.351 6.250  1.00 19.12 ? 109 ASP   C CG  1 
ATOM   1907 O  OD1 . ASP   B 1 103 ? 27.782 -24.048 5.674  1.00 19.67 ? 109 ASP   C OD1 1 
ATOM   1908 O  OD2 . ASP   B 1 103 ? 29.761 -23.194 5.829  1.00 21.22 ? 109 ASP   C OD2 1 
ATOM   1909 N  N   . CYS   B 1 104 ? 26.164 -20.296 8.999  1.00 14.93 ? 110 CYS   C N   1 
ATOM   1910 C  CA  . CYS   B 1 104 ? 25.752 -19.772 10.292 1.00 15.72 ? 110 CYS   C CA  1 
ATOM   1911 C  C   . CYS   B 1 104 ? 24.477 -20.481 10.769 1.00 15.00 ? 110 CYS   C C   1 
ATOM   1912 O  O   . CYS   B 1 104 ? 23.565 -20.673 9.953  1.00 14.76 ? 110 CYS   C O   1 
ATOM   1913 C  CB  . CYS   B 1 104 ? 25.529 -18.270 10.200 1.00 16.23 ? 110 CYS   C CB  1 
ATOM   1914 S  SG  . CYS   B 1 104 ? 27.063 -17.311 10.199 1.00 19.08 ? 110 CYS   C SG  1 
ATOM   1915 N  N   . GLY   B 1 105 ? 24.464 -20.883 12.019 1.00 14.38 ? 111 GLY   C N   1 
ATOM   1916 C  CA  . GLY   B 1 105 ? 23.324 -21.587 12.599 1.00 14.73 ? 111 GLY   C CA  1 
ATOM   1917 C  C   . GLY   B 1 105 ? 23.559 -23.085 12.750 1.00 14.05 ? 111 GLY   C C   1 
ATOM   1918 O  O   . GLY   B 1 105 ? 22.768 -23.763 13.419 1.00 14.67 ? 111 GLY   C O   1 
ATOM   1919 N  N   . GLY   B 1 106 ? 24.600 -23.626 12.086 1.00 12.94 ? 112 GLY   C N   1 
ATOM   1920 C  CA  . GLY   B 1 106 ? 24.934 -25.053 12.215 1.00 11.84 ? 112 GLY   C CA  1 
ATOM   1921 C  C   . GLY   B 1 106 ? 25.325 -25.366 13.643 1.00 11.64 ? 112 GLY   C C   1 
ATOM   1922 O  O   . GLY   B 1 106 ? 25.986 -24.540 14.292 1.00 11.89 ? 112 GLY   C O   1 
ATOM   1923 N  N   . ILE   B 1 107 ? 24.830 -26.501 14.185 1.00 11.49 ? 113 ILE   C N   1 
ATOM   1924 C  CA  . ILE   B 1 107 ? 25.075 -26.818 15.567 1.00 12.88 ? 113 ILE   C CA  1 
ATOM   1925 C  C   . ILE   B 1 107 ? 26.456 -27.430 15.807 1.00 13.42 ? 113 ILE   C C   1 
ATOM   1926 O  O   . ILE   B 1 107 ? 26.877 -28.334 15.081 1.00 13.76 ? 113 ILE   C O   1 
ATOM   1927 C  CB  . ILE   B 1 107 ? 23.926 -27.730 16.139 1.00 14.99 ? 113 ILE   C CB  1 
ATOM   1928 C  CG1 . ILE   B 1 107 ? 22.640 -26.828 16.512 1.00 17.56 ? 113 ILE   C CG1 1 
ATOM   1929 C  CG2 . ILE   B 1 107 ? 24.410 -28.571 17.384 1.00 15.41 ? 113 ILE   C CG2 1 
ATOM   1930 C  CD1 . ILE   B 1 107 ? 21.484 -27.543 16.975 1.00 22.33 ? 113 ILE   C CD1 1 
ATOM   1931 N  N   . LEU   B 1 108 ? 27.086 -27.007 16.906 1.00 12.84 ? 114 LEU   C N   1 
ATOM   1932 C  CA  . LEU   B 1 108 ? 28.289 -27.648 17.437 1.00 12.60 ? 114 LEU   C CA  1 
ATOM   1933 C  C   . LEU   B 1 108 ? 27.764 -28.420 18.678 1.00 11.36 ? 114 LEU   C C   1 
ATOM   1934 O  O   . LEU   B 1 108 ? 27.131 -27.809 19.542 1.00 10.66 ? 114 LEU   C O   1 
ATOM   1935 C  CB  . LEU   B 1 108 ? 29.281 -26.581 17.902 1.00 12.90 ? 114 LEU   C CB  1 
ATOM   1936 C  CG  . LEU   B 1 108 ? 30.485 -27.080 18.728 1.00 13.79 ? 114 LEU   C CG  1 
ATOM   1937 C  CD1 . LEU   B 1 108 ? 31.425 -27.978 17.896 1.00 14.58 ? 114 LEU   C CD1 1 
ATOM   1938 C  CD2 . LEU   B 1 108 ? 31.286 -25.899 19.287 1.00 14.72 ? 114 LEU   C CD2 1 
ATOM   1939 N  N   . ARG   B 1 109 ? 28.073 -29.733 18.769 1.00 11.24 ? 115 ARG   C N   1 
ATOM   1940 C  CA  . ARG   B 1 109 ? 27.619 -30.532 19.915 1.00 12.59 ? 115 ARG   C CA  1 
ATOM   1941 C  C   . ARG   B 1 109 ? 28.742 -31.370 20.502 1.00 12.54 ? 115 ARG   C C   1 
ATOM   1942 O  O   . ARG   B 1 109 ? 29.672 -31.795 19.798 1.00 12.38 ? 115 ARG   C O   1 
ATOM   1943 C  CB  . ARG   B 1 109 ? 26.457 -31.452 19.495 1.00 15.21 ? 115 ARG   C CB  1 
ATOM   1944 C  CG  . ARG   B 1 109 ? 26.897 -32.483 18.417 1.00 20.21 ? 115 ARG   C CG  1 
ATOM   1945 C  CD  . ARG   B 1 109 ? 25.766 -33.427 18.024 1.00 24.51 ? 115 ARG   C CD  1 
ATOM   1946 N  NE  . ARG   B 1 109 ? 25.024 -32.786 16.951 1.00 27.50 ? 115 ARG   C NE  1 
ATOM   1947 C  CZ  . ARG   B 1 109 ? 23.709 -32.650 16.915 1.00 31.72 ? 115 ARG   C CZ  1 
ATOM   1948 N  NH1 . ARG   B 1 109 ? 22.956 -33.138 17.895 1.00 32.29 ? 115 ARG   C NH1 1 
ATOM   1949 N  NH2 . ARG   B 1 109 ? 23.129 -32.043 15.891 1.00 31.55 ? 115 ARG   C NH2 1 
ATOM   1950 N  N   . CYS   B 1 110 ? 28.633 -31.629 21.799 1.00 11.46 ? 116 CYS   C N   1 
ATOM   1951 C  CA  . CYS   B 1 110 ? 29.553 -32.533 22.473 1.00 13.33 ? 116 CYS   C CA  1 
ATOM   1952 C  C   . CYS   B 1 110 ? 28.721 -33.666 23.153 1.00 14.50 ? 116 CYS   C C   1 
ATOM   1953 O  O   . CYS   B 1 110 ? 27.506 -33.794 22.916 1.00 15.77 ? 116 CYS   C O   1 
ATOM   1954 C  CB  . CYS   B 1 110 ? 30.361 -31.743 23.497 1.00 13.43 ? 116 CYS   C CB  1 
ATOM   1955 S  SG  . CYS   B 1 110 ? 29.359 -31.144 24.875 1.00 13.34 ? 116 CYS   C SG  1 
ATOM   1956 N  N   . GLN   B 1 111 ? 29.373 -34.483 24.006 1.00 15.44 ? 117 GLN   C N   1 
ATOM   1957 C  CA  . GLN   B 1 111 ? 28.692 -35.566 24.706 1.00 15.81 ? 117 GLN   C CA  1 
ATOM   1958 C  C   . GLN   B 1 111 ? 27.578 -35.055 25.658 1.00 16.85 ? 117 GLN   C C   1 
ATOM   1959 O  O   . GLN   B 1 111 ? 26.677 -35.819 26.003 1.00 19.02 ? 117 GLN   C O   1 
ATOM   1960 C  CB  . GLN   B 1 111 ? 29.696 -36.440 25.476 1.00 18.48 ? 117 GLN   C CB  1 
ATOM   1961 C  CG  . GLN   B 1 111 ? 30.289 -35.724 26.682 1.00 21.63 ? 117 GLN   C CG  1 
ATOM   1962 C  CD  . GLN   B 1 111 ? 31.343 -36.515 27.389 1.00 32.68 ? 117 GLN   C CD  1 
ATOM   1963 O  OE1 . GLN   B 1 111 ? 32.530 -36.409 27.078 1.00 35.98 ? 117 GLN   C OE1 1 
ATOM   1964 N  NE2 . GLN   B 1 111 ? 30.927 -37.299 28.390 1.00 36.56 ? 117 GLN   C NE2 1 
ATOM   1965 N  N   . HIS   B 1 112 ? 27.614 -33.766 26.051 1.00 16.19 ? 118 HIS   C N   1 
ATOM   1966 C  CA  . HIS   B 1 112 ? 26.626 -33.211 26.985 1.00 17.33 ? 118 HIS   C CA  1 
ATOM   1967 C  C   . HIS   B 1 112 ? 25.458 -32.513 26.306 1.00 18.15 ? 118 HIS   C C   1 
ATOM   1968 O  O   . HIS   B 1 112 ? 24.466 -32.227 26.967 1.00 19.94 ? 118 HIS   C O   1 
ATOM   1969 C  CB  . HIS   B 1 112 ? 27.311 -32.262 27.981 1.00 18.53 ? 118 HIS   C CB  1 
ATOM   1970 C  CG  . HIS   B 1 112 ? 28.494 -32.852 28.699 1.00 17.50 ? 118 HIS   C CG  1 
ATOM   1971 N  ND1 . HIS   B 1 112 ? 29.787 -32.630 28.258 1.00 18.61 ? 118 HIS   C ND1 1 
ATOM   1972 C  CD2 . HIS   B 1 112 ? 28.544 -33.654 29.793 1.00 18.42 ? 118 HIS   C CD2 1 
ATOM   1973 C  CE1 . HIS   B 1 112 ? 30.582 -33.267 29.093 1.00 19.46 ? 118 HIS   C CE1 1 
ATOM   1974 N  NE2 . HIS   B 1 112 ? 29.880 -33.914 30.036 1.00 18.75 ? 118 HIS   C NE2 1 
ATOM   1975 N  N   . GLY   B 1 113 ? 25.566 -32.237 24.995 1.00 17.26 ? 119 GLY   C N   1 
ATOM   1976 C  CA  . GLY   B 1 113 ? 24.517 -31.549 24.280 1.00 16.12 ? 119 GLY   C CA  1 
ATOM   1977 C  C   . GLY   B 1 113 ? 25.012 -30.458 23.345 1.00 14.73 ? 119 GLY   C C   1 
ATOM   1978 O  O   . GLY   B 1 113 ? 26.150 -30.500 22.856 1.00 14.27 ? 119 GLY   C O   1 
ATOM   1979 N  N   . VAL   B 1 114 ? 24.134 -29.509 23.058 1.00 14.35 ? 120 VAL   C N   1 
ATOM   1980 C  CA  . VAL   B 1 114 ? 24.426 -28.395 22.170 1.00 13.71 ? 120 VAL   C CA  1 
ATOM   1981 C  C   . VAL   B 1 114 ? 25.360 -27.396 22.870 1.00 14.40 ? 120 VAL   C C   1 
ATOM   1982 O  O   . VAL   B 1 114 ? 25.037 -26.880 23.948 1.00 15.58 ? 120 VAL   C O   1 
ATOM   1983 C  CB  . VAL   B 1 114 ? 23.139 -27.717 21.672 1.00 14.15 ? 120 VAL   C CB  1 
ATOM   1984 C  CG1 . VAL   B 1 114 ? 23.493 -26.461 20.881 1.00 16.23 ? 120 VAL   C CG1 1 
ATOM   1985 C  CG2 . VAL   B 1 114 ? 22.295 -28.690 20.829 1.00 14.72 ? 120 VAL   C CG2 1 
ATOM   1986 N  N   . VAL   B 1 115 ? 26.519 -27.154 22.246 1.00 13.28 ? 121 VAL   C N   1 
ATOM   1987 C  CA  . VAL   B 1 115 ? 27.549 -26.235 22.765 1.00 12.89 ? 121 VAL   C CA  1 
ATOM   1988 C  C   . VAL   B 1 115 ? 27.353 -24.797 22.223 1.00 12.25 ? 121 VAL   C C   1 
ATOM   1989 O  O   . VAL   B 1 115 ? 27.552 -23.811 22.946 1.00 12.59 ? 121 VAL   C O   1 
ATOM   1990 C  CB  . VAL   B 1 115 ? 28.948 -26.731 22.380 1.00 13.58 ? 121 VAL   C CB  1 
ATOM   1991 C  CG1 . VAL   B 1 115 ? 30.026 -25.696 22.759 1.00 13.95 ? 121 VAL   C CG1 1 
ATOM   1992 C  CG2 . VAL   B 1 115 ? 29.231 -28.125 22.938 1.00 13.46 ? 121 VAL   C CG2 1 
ATOM   1993 N  N   . GLY   B 1 116 ? 26.999 -24.700 20.946 1.00 10.65 ? 122 GLY   C N   1 
ATOM   1994 C  CA  . GLY   B 1 116 ? 26.840 -23.404 20.313 1.00 12.00 ? 122 GLY   C CA  1 
ATOM   1995 C  C   . GLY   B 1 116 ? 26.462 -23.525 18.849 1.00 12.79 ? 122 GLY   C C   1 
ATOM   1996 O  O   . GLY   B 1 116 ? 26.146 -24.627 18.374 1.00 13.62 ? 122 GLY   C O   1 
ATOM   1997 N  N   . ILE   B 1 117 ? 26.477 -22.387 18.139 1.00 11.75 ? 123 ILE   C N   1 
ATOM   1998 C  CA  . ILE   B 1 117 ? 26.140 -22.406 16.726 1.00 11.78 ? 123 ILE   C CA  1 
ATOM   1999 C  C   . ILE   B 1 117 ? 27.190 -21.649 15.918 1.00 12.26 ? 123 ILE   C C   1 
ATOM   2000 O  O   . ILE   B 1 117 ? 27.807 -20.690 16.412 1.00 12.61 ? 123 ILE   C O   1 
ATOM   2001 C  CB  . ILE   B 1 117 ? 24.733 -21.795 16.465 1.00 13.04 ? 123 ILE   C CB  1 
ATOM   2002 C  CG1 . ILE   B 1 117 ? 24.582 -20.423 17.162 1.00 14.15 ? 123 ILE   C CG1 1 
ATOM   2003 C  CG2 . ILE   B 1 117 ? 23.596 -22.774 16.816 1.00 14.51 ? 123 ILE   C CG2 1 
ATOM   2004 C  CD1 . ILE   B 1 117 ? 23.388 -19.585 16.594 1.00 15.50 ? 123 ILE   C CD1 1 
ATOM   2005 N  N   . VAL   B 1 118 ? 27.403 -22.064 14.666 1.00 10.62 ? 124 VAL   C N   1 
ATOM   2006 C  CA  . VAL   B 1 118 ? 28.337 -21.367 13.785 1.00 11.47 ? 124 VAL   C CA  1 
ATOM   2007 C  C   . VAL   B 1 118 ? 27.973 -19.874 13.677 1.00 11.51 ? 124 VAL   C C   1 
ATOM   2008 O  O   . VAL   B 1 118 ? 26.798 -19.536 13.487 1.00 11.76 ? 124 VAL   C O   1 
ATOM   2009 C  CB  . VAL   B 1 118 ? 28.302 -22.019 12.400 1.00 12.23 ? 124 VAL   C CB  1 
ATOM   2010 C  CG1 . VAL   B 1 118 ? 29.099 -21.205 11.386 1.00 13.89 ? 124 VAL   C CG1 1 
ATOM   2011 C  CG2 . VAL   B 1 118 ? 28.802 -23.453 12.475 1.00 13.22 ? 124 VAL   C CG2 1 
ATOM   2012 N  N   . SER   B 1 119 ? 28.977 -19.000 13.791 1.00 12.52 ? 125 SER   C N   1 
ATOM   2013 C  CA  . SER   B 1 119 ? 28.769 -17.547 13.727 1.00 12.23 ? 125 SER   C CA  1 
ATOM   2014 C  C   . SER   B 1 119 ? 29.793 -16.808 12.806 1.00 13.76 ? 125 SER   C C   1 
ATOM   2015 O  O   . SER   B 1 119 ? 29.460 -15.771 12.242 1.00 13.64 ? 125 SER   C O   1 
ATOM   2016 C  CB  . SER   B 1 119 ? 28.814 -16.962 15.132 1.00 14.70 ? 125 SER   C CB  1 
ATOM   2017 O  OG  . SER   B 1 119 ? 28.604 -15.548 15.137 1.00 17.38 ? 125 SER   C OG  1 
ATOM   2018 N  N   . THR   B 1 120 ? 31.065 -17.309 12.727 1.00 13.88 ? 126 THR   C N   1 
ATOM   2019 C  CA  . THR   B 1 120 ? 32.091 -16.657 11.925 1.00 14.80 ? 126 THR   C CA  1 
ATOM   2020 C  C   . THR   B 1 120 ? 32.834 -17.694 11.034 1.00 15.61 ? 126 THR   C C   1 
ATOM   2021 O  O   . THR   B 1 120 ? 32.798 -18.908 11.305 1.00 14.85 ? 126 THR   C O   1 
ATOM   2022 C  CB  . THR   B 1 120 ? 33.111 -15.901 12.853 1.00 16.08 ? 126 THR   C CB  1 
ATOM   2023 O  OG1 . THR   B 1 120 ? 34.021 -16.848 13.421 1.00 16.47 ? 126 THR   C OG1 1 
ATOM   2024 C  CG2 . THR   B 1 120 ? 32.443 -15.054 13.950 1.00 17.18 ? 126 THR   C CG2 1 
ATOM   2025 N  N   . GLY   B 1 121 ? 33.520 -17.178 10.017 1.00 16.95 ? 127 GLY   C N   1 
ATOM   2026 C  CA  . GLY   B 1 121 ? 34.340 -17.998 9.123  1.00 19.81 ? 127 GLY   C CA  1 
ATOM   2027 C  C   . GLY   B 1 121 ? 35.306 -17.189 8.291  1.00 22.23 ? 127 GLY   C C   1 
ATOM   2028 O  O   . GLY   B 1 121 ? 35.031 -16.039 7.931  1.00 24.48 ? 127 GLY   C O   1 
ATOM   2029 N  N   . GLY   B 1 122 ? 36.387 -17.822 7.899  1.00 23.26 ? 128 GLY   C N   1 
ATOM   2030 C  CA  . GLY   B 1 122 ? 37.405 -17.172 7.075  1.00 23.46 ? 128 GLY   C CA  1 
ATOM   2031 C  C   . GLY   B 1 122 ? 38.795 -17.660 7.417  1.00 23.80 ? 128 GLY   C C   1 
ATOM   2032 O  O   . GLY   B 1 122 ? 39.034 -18.108 8.536  1.00 22.58 ? 128 GLY   C O   1 
ATOM   2033 N  N   . ASN   B 1 123 ? 39.700 -17.626 6.442  1.00 25.01 ? 129 ASN   C N   1 
ATOM   2034 C  CA  . ASN   B 1 123 ? 41.089 -18.028 6.641  1.00 25.58 ? 129 ASN   C CA  1 
ATOM   2035 C  C   . ASN   B 1 123 ? 41.255 -19.415 7.226  1.00 24.31 ? 129 ASN   C C   1 
ATOM   2036 O  O   . ASN   B 1 123 ? 42.194 -19.642 7.988  1.00 24.98 ? 129 ASN   C O   1 
ATOM   2037 C  CB  . ASN   B 1 123 ? 41.845 -16.983 7.474  1.00 28.69 ? 129 ASN   C CB  1 
ATOM   2038 C  CG  . ASN   B 1 123 ? 42.108 -15.729 6.667  1.00 38.22 ? 129 ASN   C CG  1 
ATOM   2039 O  OD1 . ASN   B 1 123 ? 42.393 -15.788 5.460  1.00 40.70 ? 129 ASN   C OD1 1 
ATOM   2040 N  ND2 . ASN   B 1 123 ? 42.005 -14.562 7.299  1.00 40.00 ? 129 ASN   C ND2 1 
ATOM   2041 N  N   . GLY   B 1 124 ? 40.379 -20.344 6.849  1.00 23.43 ? 130 GLY   C N   1 
ATOM   2042 C  CA  . GLY   B 1 124 ? 40.481 -21.729 7.303  1.00 22.23 ? 130 GLY   C CA  1 
ATOM   2043 C  C   . GLY   B 1 124 ? 39.995 -21.984 8.722  1.00 20.24 ? 130 GLY   C C   1 
ATOM   2044 O  O   . GLY   B 1 124 ? 40.225 -23.071 9.269  1.00 19.98 ? 130 GLY   C O   1 
ATOM   2045 N  N   . LEU   B 1 125 ? 39.354 -20.987 9.346  1.00 18.58 ? 131 LEU   C N   1 
ATOM   2046 C  CA  . LEU   B 1 125 ? 38.828 -21.140 10.710 1.00 18.39 ? 131 LEU   C CA  1 
ATOM   2047 C  C   . LEU   B 1 125 ? 37.304 -21.046 10.729 1.00 17.74 ? 131 LEU   C C   1 
ATOM   2048 O  O   . LEU   B 1 125 ? 36.712 -20.377 9.869  1.00 18.31 ? 131 LEU   C O   1 
ATOM   2049 C  CB  . LEU   B 1 125 ? 39.368 -20.048 11.624 1.00 19.75 ? 131 LEU   C CB  1 
ATOM   2050 C  CG  . LEU   B 1 125 ? 40.888 -20.004 11.818 1.00 21.69 ? 131 LEU   C CG  1 
ATOM   2051 C  CD1 . LEU   B 1 125 ? 41.251 -18.917 12.753 1.00 23.82 ? 131 LEU   C CD1 1 
ATOM   2052 C  CD2 . LEU   B 1 125 ? 41.426 -21.328 12.312 1.00 21.33 ? 131 LEU   C CD2 1 
ATOM   2053 N  N   . VAL   B 1 126 ? 36.674 -21.713 11.715 1.00 15.26 ? 132 VAL   C N   1 
ATOM   2054 C  CA  . VAL   B 1 126 ? 35.237 -21.648 11.938 1.00 15.11 ? 132 VAL   C CA  1 
ATOM   2055 C  C   . VAL   B 1 126 ? 35.050 -21.165 13.376 1.00 13.88 ? 132 VAL   C C   1 
ATOM   2056 O  O   . VAL   B 1 126 ? 35.753 -21.624 14.277 1.00 14.70 ? 132 VAL   C O   1 
ATOM   2057 C  CB  . VAL   B 1 126 ? 34.510 -22.982 11.653 1.00 15.18 ? 132 VAL   C CB  1 
ATOM   2058 C  CG1 . VAL   B 1 126 ? 35.156 -24.158 12.372 1.00 16.04 ? 132 VAL   C CG1 1 
ATOM   2059 C  CG2 . VAL   B 1 126 ? 32.989 -22.911 11.949 1.00 15.06 ? 132 VAL   C CG2 1 
ATOM   2060 N  N   . GLY   B 1 127 ? 34.167 -20.208 13.570 1.00 14.14 ? 133 GLY   C N   1 
ATOM   2061 C  CA  . GLY   B 1 127 ? 33.891 -19.664 14.895 1.00 14.13 ? 133 GLY   C CA  1 
ATOM   2062 C  C   . GLY   B 1 127 ? 32.457 -19.962 15.317 1.00 14.11 ? 133 GLY   C C   1 
ATOM   2063 O  O   . GLY   B 1 127 ? 31.539 -19.837 14.499 1.00 13.44 ? 133 GLY   C O   1 
ATOM   2064 N  N   . PHE   B 1 128 ? 32.274 -20.325 16.606 1.00 12.36 ? 134 PHE   C N   1 
ATOM   2065 C  CA  . PHE   B 1 128 ? 30.981 -20.713 17.172 1.00 13.23 ? 134 PHE   C CA  1 
ATOM   2066 C  C   . PHE   B 1 128 ? 30.588 -19.803 18.324 1.00 13.39 ? 134 PHE   C C   1 
ATOM   2067 O  O   . PHE   B 1 128 ? 31.427 -19.560 19.207 1.00 13.46 ? 134 PHE   C O   1 
ATOM   2068 C  CB  . PHE   B 1 128 ? 31.053 -22.167 17.720 1.00 12.02 ? 134 PHE   C CB  1 
ATOM   2069 C  CG  . PHE   B 1 128 ? 31.603 -23.173 16.734 1.00 12.34 ? 134 PHE   C CG  1 
ATOM   2070 C  CD1 . PHE   B 1 128 ? 30.775 -23.766 15.796 1.00 13.10 ? 134 PHE   C CD1 1 
ATOM   2071 C  CD2 . PHE   B 1 128 ? 32.949 -23.539 16.764 1.00 12.61 ? 134 PHE   C CD2 1 
ATOM   2072 C  CE1 . PHE   B 1 128 ? 31.271 -24.708 14.907 1.00 13.63 ? 134 PHE   C CE1 1 
ATOM   2073 C  CE2 . PHE   B 1 128 ? 33.444 -24.512 15.881 1.00 13.66 ? 134 PHE   C CE2 1 
ATOM   2074 C  CZ  . PHE   B 1 128 ? 32.607 -25.080 14.953 1.00 13.21 ? 134 PHE   C CZ  1 
ATOM   2075 N  N   . ALA   B 1 129 ? 29.336 -19.318 18.326 1.00 13.57 ? 135 ALA   C N   1 
ATOM   2076 C  CA  . ALA   B 1 129 ? 28.830 -18.515 19.436 1.00 14.66 ? 135 ALA   C CA  1 
ATOM   2077 C  C   . ALA   B 1 129 ? 28.429 -19.498 20.561 1.00 14.24 ? 135 ALA   C C   1 
ATOM   2078 O  O   . ALA   B 1 129 ? 27.509 -20.313 20.388 1.00 14.16 ? 135 ALA   C O   1 
ATOM   2079 C  CB  . ALA   B 1 129 ? 27.606 -17.694 18.989 1.00 14.70 ? 135 ALA   C CB  1 
ATOM   2080 N  N   . ASP   B 1 130 ? 29.124 -19.433 21.697 1.00 14.85 ? 136 ASP   C N   1 
ATOM   2081 C  CA  . ASP   B 1 130 ? 28.818 -20.316 22.832 1.00 14.23 ? 136 ASP   C CA  1 
ATOM   2082 C  C   . ASP   B 1 130 ? 27.429 -20.009 23.429 1.00 15.16 ? 136 ASP   C C   1 
ATOM   2083 O  O   . ASP   B 1 130 ? 27.010 -18.844 23.477 1.00 16.00 ? 136 ASP   C O   1 
ATOM   2084 C  CB  . ASP   B 1 130 ? 29.848 -20.083 23.943 1.00 13.47 ? 136 ASP   C CB  1 
ATOM   2085 C  CG  . ASP   B 1 130 ? 29.701 -21.016 25.129 1.00 14.64 ? 136 ASP   C CG  1 
ATOM   2086 O  OD1 . ASP   B 1 130 ? 29.678 -22.255 24.919 1.00 16.29 ? 136 ASP   C OD1 1 
ATOM   2087 O  OD2 . ASP   B 1 130 ? 29.633 -20.512 26.277 1.00 17.62 ? 136 ASP   C OD2 1 
ATOM   2088 N  N   . VAL   B 1 131 ? 26.726 -21.056 23.930 1.00 14.38 ? 137 VAL   C N   1 
ATOM   2089 C  CA  . VAL   B 1 131 ? 25.461 -20.871 24.644 1.00 14.23 ? 137 VAL   C CA  1 
ATOM   2090 C  C   . VAL   B 1 131 ? 25.483 -21.570 26.035 1.00 15.41 ? 137 VAL   C C   1 
ATOM   2091 O  O   . VAL   B 1 131 ? 24.503 -21.505 26.754 1.00 16.17 ? 137 VAL   C O   1 
ATOM   2092 C  CB  . VAL   B 1 131 ? 24.246 -21.330 23.824 1.00 14.92 ? 137 VAL   C CB  1 
ATOM   2093 C  CG1 . VAL   B 1 131 ? 24.171 -20.564 22.498 1.00 14.79 ? 137 VAL   C CG1 1 
ATOM   2094 C  CG2 . VAL   B 1 131 ? 24.253 -22.842 23.581 1.00 14.23 ? 137 VAL   C CG2 1 
ATOM   2095 N  N   . ARG   B 1 132 ? 26.589 -22.272 26.389 1.00 14.79 ? 138 ARG   C N   1 
ATOM   2096 C  CA  . ARG   B 1 132 ? 26.638 -23.057 27.644 1.00 13.96 ? 138 ARG   C CA  1 
ATOM   2097 C  C   . ARG   B 1 132 ? 26.559 -22.223 28.927 1.00 15.54 ? 138 ARG   C C   1 
ATOM   2098 O  O   . ARG   B 1 132 ? 26.251 -22.790 29.987 1.00 17.06 ? 138 ARG   C O   1 
ATOM   2099 C  CB  . ARG   B 1 132 ? 27.889 -23.950 27.663 1.00 14.74 ? 138 ARG   C CB  1 
ATOM   2100 C  CG  . ARG   B 1 132 ? 27.962 -24.957 26.511 1.00 15.14 ? 138 ARG   C CG  1 
ATOM   2101 C  CD  . ARG   B 1 132 ? 29.324 -25.679 26.580 1.00 15.82 ? 138 ARG   C CD  1 
ATOM   2102 N  NE  . ARG   B 1 132 ? 30.408 -24.773 26.140 1.00 15.36 ? 138 ARG   C NE  1 
ATOM   2103 C  CZ  . ARG   B 1 132 ? 31.681 -25.138 26.017 1.00 17.47 ? 138 ARG   C CZ  1 
ATOM   2104 N  NH1 . ARG   B 1 132 ? 32.068 -26.372 26.366 1.00 15.91 ? 138 ARG   C NH1 1 
ATOM   2105 N  NH2 . ARG   B 1 132 ? 32.581 -24.277 25.558 1.00 16.53 ? 138 ARG   C NH2 1 
ATOM   2106 N  N   . ASP   B 1 133 ? 26.905 -20.916 28.850 1.00 14.71 ? 139 ASP   C N   1 
ATOM   2107 C  CA  . ASP   B 1 133 ? 26.827 -20.030 30.007 1.00 14.92 ? 139 ASP   C CA  1 
ATOM   2108 C  C   . ASP   B 1 133 ? 25.422 -19.463 30.261 1.00 16.72 ? 139 ASP   C C   1 
ATOM   2109 O  O   . ASP   B 1 133 ? 25.188 -18.867 31.331 1.00 17.87 ? 139 ASP   C O   1 
ATOM   2110 C  CB  . ASP   B 1 133 ? 27.803 -18.845 29.913 1.00 16.37 ? 139 ASP   C CB  1 
ATOM   2111 C  CG  . ASP   B 1 133 ? 27.480 -17.894 28.776 1.00 20.98 ? 139 ASP   C CG  1 
ATOM   2112 O  OD1 . ASP   B 1 133 ? 27.182 -18.387 27.668 1.00 19.06 ? 139 ASP   C OD1 1 
ATOM   2113 O  OD2 . ASP   B 1 133 ? 27.502 -16.643 29.012 1.00 23.00 ? 139 ASP   C OD2 1 
ATOM   2114 N  N   . LEU   B 1 134 ? 24.500 -19.631 29.286 1.00 16.51 ? 140 LEU   C N   1 
ATOM   2115 C  CA  . LEU   B 1 134 ? 23.138 -19.121 29.387 1.00 17.43 ? 140 LEU   C CA  1 
ATOM   2116 C  C   . LEU   B 1 134 ? 22.289 -20.135 30.166 1.00 17.66 ? 140 LEU   C C   1 
ATOM   2117 O  O   . LEU   B 1 134 ? 21.480 -20.854 29.568 1.00 17.15 ? 140 LEU   C O   1 
ATOM   2118 C  CB  . LEU   B 1 134 ? 22.593 -18.917 27.961 1.00 16.46 ? 140 LEU   C CB  1 
ATOM   2119 C  CG  . LEU   B 1 134 ? 23.366 -17.897 27.105 1.00 17.50 ? 140 LEU   C CG  1 
ATOM   2120 C  CD1 . LEU   B 1 134 ? 22.788 -17.784 25.693 1.00 17.64 ? 140 LEU   C CD1 1 
ATOM   2121 C  CD2 . LEU   B 1 134 ? 23.411 -16.506 27.788 1.00 18.63 ? 140 LEU   C CD2 1 
ATOM   2122 N  N   . LEU   B 1 135 ? 22.460 -20.181 31.501 1.00 18.61 ? 141 LEU   C N   1 
ATOM   2123 C  CA  . LEU   B 1 135 ? 21.779 -21.183 32.316 1.00 19.31 ? 141 LEU   C CA  1 
ATOM   2124 C  C   . LEU   B 1 135 ? 20.257 -21.086 32.296 1.00 20.46 ? 141 LEU   C C   1 
ATOM   2125 O  O   . LEU   B 1 135 ? 19.576 -22.115 32.504 1.00 20.75 ? 141 LEU   C O   1 
ATOM   2126 C  CB  . LEU   B 1 135 ? 22.308 -21.196 33.769 1.00 19.41 ? 141 LEU   C CB  1 
ATOM   2127 C  CG  . LEU   B 1 135 ? 23.855 -21.250 33.913 1.00 20.90 ? 141 LEU   C CG  1 
ATOM   2128 C  CD1 . LEU   B 1 135 ? 24.312 -21.221 35.422 1.00 20.45 ? 141 LEU   C CD1 1 
ATOM   2129 C  CD2 . LEU   B 1 135 ? 24.487 -22.400 33.123 1.00 21.35 ? 141 LEU   C CD2 1 
ATOM   2130 N  N   . TRP   B 1 136 ? 19.724 -19.859 32.129 1.00 20.46 ? 142 TRP   C N   1 
ATOM   2131 C  CA  . TRP   B 1 136 ? 18.274 -19.609 32.125 1.00 21.34 ? 142 TRP   C CA  1 
ATOM   2132 C  C   . TRP   B 1 136 ? 17.530 -20.285 30.957 1.00 21.33 ? 142 TRP   C C   1 
ATOM   2133 O  O   . TRP   B 1 136 ? 16.294 -20.369 30.997 1.00 21.70 ? 142 TRP   C O   1 
ATOM   2134 C  CB  . TRP   B 1 136 ? 17.993 -18.108 32.132 1.00 20.87 ? 142 TRP   C CB  1 
ATOM   2135 C  CG  . TRP   B 1 136 ? 18.712 -17.354 31.043 1.00 20.70 ? 142 TRP   C CG  1 
ATOM   2136 C  CD1 . TRP   B 1 136 ? 19.888 -16.675 31.163 1.00 21.07 ? 142 TRP   C CD1 1 
ATOM   2137 C  CD2 . TRP   B 1 136 ? 18.234 -17.094 29.715 1.00 20.19 ? 142 TRP   C CD2 1 
ATOM   2138 N  NE1 . TRP   B 1 136 ? 20.205 -16.060 29.976 1.00 21.08 ? 142 TRP   C NE1 1 
ATOM   2139 C  CE2 . TRP   B 1 136 ? 19.218 -16.323 29.058 1.00 20.98 ? 142 TRP   C CE2 1 
ATOM   2140 C  CE3 . TRP   B 1 136 ? 17.108 -17.495 28.992 1.00 21.00 ? 142 TRP   C CE3 1 
ATOM   2141 C  CZ2 . TRP   B 1 136 ? 19.056 -15.860 27.751 1.00 21.01 ? 142 TRP   C CZ2 1 
ATOM   2142 C  CZ3 . TRP   B 1 136 ? 16.956 -17.048 27.690 1.00 20.82 ? 142 TRP   C CZ3 1 
ATOM   2143 C  CH2 . TRP   B 1 136 ? 17.950 -16.285 27.065 1.00 21.35 ? 142 TRP   C CH2 1 
ATOM   2144 N  N   . LEU   B 1 137 ? 18.269 -20.779 29.941 1.00 19.56 ? 143 LEU   C N   1 
ATOM   2145 C  CA  . LEU   B 1 137 ? 17.644 -21.486 28.826 1.00 20.02 ? 143 LEU   C CA  1 
ATOM   2146 C  C   . LEU   B 1 137 ? 16.946 -22.789 29.294 1.00 23.54 ? 143 LEU   C C   1 
ATOM   2147 O  O   . LEU   B 1 137 ? 15.971 -23.206 28.666 1.00 25.04 ? 143 LEU   C O   1 
ATOM   2148 C  CB  . LEU   B 1 137 ? 18.691 -21.801 27.719 1.00 18.76 ? 143 LEU   C CB  1 
ATOM   2149 C  CG  . LEU   B 1 137 ? 19.171 -20.618 26.881 1.00 19.58 ? 143 LEU   C CG  1 
ATOM   2150 C  CD1 . LEU   B 1 137 ? 20.385 -21.010 25.962 1.00 20.16 ? 143 LEU   C CD1 1 
ATOM   2151 C  CD2 . LEU   B 1 137 ? 18.044 -20.104 25.981 1.00 20.36 ? 143 LEU   C CD2 1 
ATOM   2152 N  N   . ASP   B 1 138 ? 17.412 -23.389 30.424 1.00 23.99 ? 144 ASP   C N   1 
ATOM   2153 C  CA  . ASP   B 1 138 ? 16.876 -24.624 31.013 1.00 26.53 ? 144 ASP   C CA  1 
ATOM   2154 C  C   . ASP   B 1 138 ? 15.679 -24.410 31.942 1.00 30.32 ? 144 ASP   C C   1 
ATOM   2155 O  O   . ASP   B 1 138 ? 15.173 -25.391 32.477 1.00 31.44 ? 144 ASP   C O   1 
ATOM   2156 C  CB  . ASP   B 1 138 ? 17.949 -25.290 31.880 1.00 27.67 ? 144 ASP   C CB  1 
ATOM   2157 C  CG  . ASP   B 1 138 ? 19.219 -25.672 31.149 1.00 32.23 ? 144 ASP   C CG  1 
ATOM   2158 O  OD1 . ASP   B 1 138 ? 19.183 -25.775 29.903 1.00 32.31 ? 144 ASP   C OD1 1 
ATOM   2159 O  OD2 . ASP   B 1 138 ? 20.263 -25.848 31.829 1.00 34.72 ? 144 ASP   C OD2 1 
ATOM   2160 N  N   . GLU   B 1 139 ? 15.262 -23.158 32.182 1.00 32.44 ? 145 GLU   C N   1 
ATOM   2161 C  CA  . GLU   B 1 139 ? 14.185 -22.887 33.134 1.00 36.39 ? 145 GLU   C CA  1 
ATOM   2162 C  C   . GLU   B 1 139 ? 13.188 -21.813 32.634 1.00 39.31 ? 145 GLU   C C   1 
ATOM   2163 O  O   . GLU   B 1 139 ? 13.252 -21.427 31.465 1.00 39.67 ? 145 GLU   C O   1 
ATOM   2164 C  CB  . GLU   B 1 139 ? 14.814 -22.516 34.492 1.00 39.87 ? 145 GLU   C CB  1 
ATOM   2165 C  CG  . GLU   B 1 139 ? 15.754 -21.330 34.398 1.00 47.19 ? 145 GLU   C CG  1 
ATOM   2166 C  CD  . GLU   B 1 139 ? 16.691 -21.180 35.582 1.00 55.48 ? 145 GLU   C CD  1 
ATOM   2167 O  OE1 . GLU   B 1 139 ? 17.116 -20.035 35.861 1.00 56.57 ? 145 GLU   C OE1 1 
ATOM   2168 O  OE2 . GLU   B 1 139 ? 16.995 -22.208 36.233 1.00 57.94 ? 145 GLU   C OE2 1 
ATOM   2169 N  N   . GLU   B 1 140 ? 12.239 -21.379 33.509 1.00 41.20 ? 146 GLU   C N   1 
ATOM   2170 C  CA  . GLU   B 1 140 ? 11.218 -20.347 33.246 1.00 43.00 ? 146 GLU   C CA  1 
ATOM   2171 C  C   . GLU   B 1 140 ? 10.278 -20.721 32.105 1.00 44.92 ? 146 GLU   C C   1 
ATOM   2172 O  O   . GLU   B 1 140 ? 9.070  -20.798 32.318 1.00 46.45 ? 146 GLU   C O   1 
ATOM   2173 C  CB  . GLU   B 1 140 ? 11.845 -18.963 33.037 1.00 45.34 ? 146 GLU   C CB  1 
ATOM   2174 C  CG  . GLU   B 1 140 ? 10.877 -17.875 32.582 1.00 52.06 ? 146 GLU   C CG  1 
ATOM   2175 C  CD  . GLU   B 1 140 ? 10.191 -17.106 33.699 1.00 61.66 ? 146 GLU   C CD  1 
ATOM   2176 O  OE1 . GLU   B 1 140 ? 10.457 -15.887 33.827 1.00 65.02 ? 146 GLU   C OE1 1 
ATOM   2177 O  OE2 . GLU   B 1 140 ? 9.388  -17.716 34.445 1.00 62.66 ? 146 GLU   C OE2 1 
HETATM 2178 N  N1  . A1BN1 C 2 .   ? 8.814  11.168  23.344 1.00 28.62 ? 201 A1BN1 A N1  1 
HETATM 2179 C  C4  . A1BN1 C 2 .   ? 4.643  11.309  27.189 1.00 34.62 ? 201 A1BN1 A C4  1 
HETATM 2180 C  C5  . A1BN1 C 2 .   ? 6.322  12.353  25.788 1.00 31.85 ? 201 A1BN1 A C5  1 
HETATM 2181 C  C6  . A1BN1 C 2 .   ? 7.411  12.156  24.802 1.00 30.13 ? 201 A1BN1 A C6  1 
HETATM 2182 C  C7  . A1BN1 C 2 .   ? 7.793  10.967  24.234 1.00 29.41 ? 201 A1BN1 A C7  1 
HETATM 2183 C  C8  . A1BN1 C 2 .   ? 9.504  10.126  22.595 1.00 28.34 ? 201 A1BN1 A C8  1 
HETATM 2184 C  C10 . A1BN1 C 2 .   ? 10.079 13.206  22.587 1.00 29.51 ? 201 A1BN1 A C10 1 
HETATM 2185 C  C13 . A1BN1 C 2 .   ? 8.420  14.541  24.415 1.00 29.74 ? 201 A1BN1 A C13 1 
HETATM 2186 O  O   . A1BN1 C 2 .   ? 6.047  13.476  26.226 1.00 32.55 ? 201 A1BN1 A O   1 
HETATM 2187 C  C14 . A1BN1 C 2 .   ? 8.269  13.170  24.226 1.00 29.52 ? 201 A1BN1 A C14 1 
HETATM 2188 C  C12 . A1BN1 C 2 .   ? 9.391  15.233  23.700 1.00 30.04 ? 201 A1BN1 A C12 1 
HETATM 2189 C  C11 . A1BN1 C 2 .   ? 10.210 14.572  22.793 1.00 30.03 ? 201 A1BN1 A C11 1 
HETATM 2190 C  C9  . A1BN1 C 2 .   ? 9.114  12.516  23.313 1.00 29.37 ? 201 A1BN1 A C9  1 
HETATM 2191 N  N   . A1BN1 C 2 .   ? 5.685  11.248  26.186 1.00 32.82 ? 201 A1BN1 A N   1 
HETATM 2192 C  C3  . A1BN1 C 2 .   ? 5.087  10.867  28.535 1.00 36.11 ? 201 A1BN1 A C3  1 
HETATM 2193 C  C2  . A1BN1 C 2 .   ? 4.563  10.012  29.430 1.00 36.88 ? 201 A1BN1 A C2  1 
HETATM 2194 O  O1  . A1BN1 C 2 .   ? 6.191  11.461  29.040 1.00 36.25 ? 201 A1BN1 A O1  1 
HETATM 2195 N  N2  . A1BN1 C 2 .   ? 6.386  10.988  30.367 1.00 37.04 ? 201 A1BN1 A N2  1 
HETATM 2196 C  C1  . A1BN1 C 2 .   ? 5.380  10.101  30.567 1.00 37.44 ? 201 A1BN1 A C1  1 
HETATM 2197 C  C   . A1BN1 C 2 .   ? 5.237  9.358   31.860 1.00 38.01 ? 201 A1BN1 A C   1 
HETATM 2198 ZN ZN  . ZN    D 3 .   ? 10.793 -3.528  5.706  1.00 22.79 2 202 ZN    A ZN  1 
HETATM 2199 S  S   . DMS   E 4 .   ? 19.286 -2.271  24.417 1.00 65.81 ? 203 DMS   A S   1 
HETATM 2200 O  O   . DMS   E 4 .   ? 18.172 -2.708  23.499 1.00 65.61 ? 203 DMS   A O   1 
HETATM 2201 C  C1  . DMS   E 4 .   ? 19.572 -3.578  25.643 1.00 65.74 ? 203 DMS   A C1  1 
HETATM 2202 C  C2  . DMS   E 4 .   ? 20.867 -2.424  23.539 1.00 65.72 ? 203 DMS   A C2  1 
HETATM 2203 ZN ZN  . ZN    F 3 .   ? 30.498 -31.205 26.856 1.00 16.63 2 201 ZN    C ZN  1 
HETATM 2204 O  O   . HOH   G 5 .   ? 3.019  9.518   9.145  1.00 25.04 ? 301 HOH   A O   1 
HETATM 2205 O  O   . HOH   G 5 .   ? 11.157 9.105   4.359  1.00 28.32 ? 302 HOH   A O   1 
HETATM 2206 O  O   . HOH   G 5 .   ? 9.559  21.966  10.416 1.00 48.00 ? 303 HOH   A O   1 
HETATM 2207 O  O   . HOH   G 5 .   ? 3.932  7.415   23.712 1.00 30.34 ? 304 HOH   A O   1 
HETATM 2208 O  O   . HOH   G 5 .   ? 8.240  -2.921  0.660  1.00 26.22 ? 305 HOH   A O   1 
HETATM 2209 O  O   . HOH   G 5 .   ? 7.531  20.194  17.840 1.00 26.63 ? 306 HOH   A O   1 
HETATM 2210 O  O   . HOH   G 5 .   ? 30.763 10.271  15.528 1.00 39.36 ? 307 HOH   A O   1 
HETATM 2211 O  O   . HOH   G 5 .   ? 9.162  18.702  16.194 1.00 33.18 ? 308 HOH   A O   1 
HETATM 2212 O  O   . HOH   G 5 .   ? 10.952 9.814   31.593 1.00 33.01 ? 309 HOH   A O   1 
HETATM 2213 O  O   . HOH   G 5 .   ? 6.024  2.741   5.808  1.00 25.86 ? 310 HOH   A O   1 
HETATM 2214 O  O   . HOH   G 5 .   ? 10.859 5.947   3.491  1.00 27.92 ? 311 HOH   A O   1 
HETATM 2215 O  O   . HOH   G 5 .   ? 33.142 12.569  -1.599 1.00 57.72 ? 312 HOH   A O   1 
HETATM 2216 O  O   . HOH   G 5 .   ? 12.567 -6.078  30.511 1.00 29.01 ? 313 HOH   A O   1 
HETATM 2217 O  O   . HOH   G 5 .   ? 17.770 0.937   27.906 1.00 27.71 ? 314 HOH   A O   1 
HETATM 2218 O  O   . HOH   G 5 .   ? 19.543 9.875   19.724 1.00 16.19 ? 315 HOH   A O   1 
HETATM 2219 O  O   . HOH   G 5 .   ? -0.040 1.377   15.987 1.00 14.04 ? 316 HOH   A O   1 
HETATM 2220 O  O   . HOH   G 5 .   ? 31.633 20.102  11.800 1.00 19.37 ? 317 HOH   A O   1 
HETATM 2221 O  O   . HOH   G 5 .   ? -1.444 17.481  18.779 1.00 42.38 ? 318 HOH   A O   1 
HETATM 2222 O  O   . HOH   G 5 .   ? 4.827  -3.747  28.965 1.00 23.87 ? 319 HOH   A O   1 
HETATM 2223 O  O   . HOH   G 5 .   ? 8.372  19.183  19.749 1.00 35.05 ? 320 HOH   A O   1 
HETATM 2224 O  O   . HOH   G 5 .   ? 27.935 2.752   4.931  1.00 35.51 ? 321 HOH   A O   1 
HETATM 2225 O  O   . HOH   G 5 .   ? 5.869  5.316   32.806 1.00 19.02 ? 322 HOH   A O   1 
HETATM 2226 O  O   . HOH   G 5 .   ? 6.530  14.678  28.589 1.00 43.79 ? 323 HOH   A O   1 
HETATM 2227 O  O   . HOH   G 5 .   ? 22.582 -0.599  5.255  1.00 23.82 ? 324 HOH   A O   1 
HETATM 2228 O  O   . HOH   G 5 .   ? 34.008 14.090  9.567  1.00 32.26 ? 325 HOH   A O   1 
HETATM 2229 O  O   . HOH   G 5 .   ? 21.830 4.635   24.680 1.00 32.36 ? 326 HOH   A O   1 
HETATM 2230 O  O   . HOH   G 5 .   ? 16.796 3.717   23.708 1.00 16.91 ? 327 HOH   A O   1 
HETATM 2231 O  O   . HOH   G 5 .   ? 20.581 -2.462  16.826 1.00 21.56 ? 328 HOH   A O   1 
HETATM 2232 O  O   . HOH   G 5 .   ? 5.526  17.712  24.479 1.00 41.97 ? 329 HOH   A O   1 
HETATM 2233 O  O   . HOH   G 5 .   ? 23.689 21.654  7.452  1.00 26.25 ? 330 HOH   A O   1 
HETATM 2234 O  O   . HOH   G 5 .   ? 14.727 13.329  24.071 1.00 24.17 ? 331 HOH   A O   1 
HETATM 2235 O  O   . HOH   G 5 .   ? 22.701 0.759   17.245 1.00 22.74 ? 332 HOH   A O   1 
HETATM 2236 O  O   . HOH   G 5 .   ? 9.163  -11.072 2.615  1.00 43.55 ? 333 HOH   A O   1 
HETATM 2237 O  O   . HOH   G 5 .   ? 11.439 12.862  11.436 1.00 18.99 ? 334 HOH   A O   1 
HETATM 2238 O  O   . HOH   G 5 .   ? 2.389  -3.039  20.869 1.00 21.00 ? 335 HOH   A O   1 
HETATM 2239 O  O   . HOH   G 5 .   ? 29.553 22.086  19.447 1.00 26.07 ? 336 HOH   A O   1 
HETATM 2240 O  O   . HOH   G 5 .   ? 0.337  -0.976  19.567 1.00 23.17 ? 337 HOH   A O   1 
HETATM 2241 O  O   . HOH   G 5 .   ? 20.322 -0.788  2.900  1.00 30.82 ? 338 HOH   A O   1 
HETATM 2242 O  O   . HOH   G 5 .   ? 8.800  -7.944  21.092 1.00 31.38 ? 339 HOH   A O   1 
HETATM 2243 O  O   . HOH   G 5 .   ? 18.574 21.944  9.725  1.00 22.90 ? 340 HOH   A O   1 
HETATM 2244 O  O   . HOH   G 5 .   ? 26.935 -1.322  8.627  1.00 31.21 ? 341 HOH   A O   1 
HETATM 2245 O  O   . HOH   G 5 .   ? 28.962 3.257   12.338 1.00 21.74 ? 342 HOH   A O   1 
HETATM 2246 O  O   . HOH   G 5 .   ? 10.636 -7.457  0.428  1.00 45.32 ? 343 HOH   A O   1 
HETATM 2247 O  O   . HOH   G 5 .   ? 17.147 5.953   27.019 1.00 25.61 ? 344 HOH   A O   1 
HETATM 2248 O  O   . HOH   G 5 .   ? 16.421 23.962  14.998 1.00 38.72 ? 345 HOH   A O   1 
HETATM 2249 O  O   . HOH   G 5 .   ? 36.591 17.793  14.379 1.00 36.81 ? 346 HOH   A O   1 
HETATM 2250 O  O   . HOH   G 5 .   ? 1.814  12.268  20.470 1.00 31.93 ? 347 HOH   A O   1 
HETATM 2251 O  O   . HOH   G 5 .   ? 6.536  -6.825  23.764 1.00 23.50 ? 348 HOH   A O   1 
HETATM 2252 O  O   . HOH   G 5 .   ? 14.529 -10.580 8.578  1.00 43.50 ? 349 HOH   A O   1 
HETATM 2253 O  O   . HOH   G 5 .   ? 5.731  16.847  21.387 1.00 36.47 ? 350 HOH   A O   1 
HETATM 2254 O  O   . HOH   G 5 .   ? 8.296  -2.898  31.920 1.00 26.83 ? 351 HOH   A O   1 
HETATM 2255 O  O   . HOH   G 5 .   ? 13.975 3.833   23.622 1.00 14.97 ? 352 HOH   A O   1 
HETATM 2256 O  O   . HOH   G 5 .   ? -0.570 3.767   23.994 1.00 19.01 ? 353 HOH   A O   1 
HETATM 2257 O  O   . HOH   G 5 .   ? 8.757  11.517  31.772 1.00 32.49 ? 354 HOH   A O   1 
HETATM 2258 O  O   . HOH   G 5 .   ? 16.907 -3.537  28.021 1.00 32.07 ? 355 HOH   A O   1 
HETATM 2259 O  O   . HOH   G 5 .   ? 6.674  -2.490  -1.651 1.00 35.53 ? 356 HOH   A O   1 
HETATM 2260 O  O   . HOH   G 5 .   ? 29.135 16.065  4.448  1.00 29.92 ? 357 HOH   A O   1 
HETATM 2261 O  O   . HOH   G 5 .   ? 28.194 11.207  2.832  1.00 38.81 ? 358 HOH   A O   1 
HETATM 2262 O  O   . HOH   G 5 .   ? 25.659 19.405  21.806 1.00 24.70 ? 359 HOH   A O   1 
HETATM 2263 O  O   . HOH   G 5 .   ? 3.935  12.741  18.424 1.00 27.88 ? 360 HOH   A O   1 
HETATM 2264 O  O   . HOH   G 5 .   ? 14.397 -2.655  17.836 1.00 19.49 ? 361 HOH   A O   1 
HETATM 2265 O  O   . HOH   G 5 .   ? 19.839 20.085  5.711  1.00 31.87 ? 362 HOH   A O   1 
HETATM 2266 O  O   . HOH   G 5 .   ? 9.829  3.900   33.610 1.00 14.58 ? 363 HOH   A O   1 
HETATM 2267 O  O   . HOH   G 5 .   ? 24.965 4.921   21.300 1.00 31.87 ? 364 HOH   A O   1 
HETATM 2268 O  O   . HOH   G 5 .   ? 20.902 -4.242  14.247 1.00 23.81 ? 365 HOH   A O   1 
HETATM 2269 O  O   . HOH   G 5 .   ? 32.865 16.636  9.143  1.00 23.41 ? 366 HOH   A O   1 
HETATM 2270 O  O   . HOH   G 5 .   ? 23.676 11.506  22.127 1.00 35.88 ? 367 HOH   A O   1 
HETATM 2271 O  O   . HOH   G 5 .   ? 0.749  -5.272  13.771 1.00 46.50 ? 368 HOH   A O   1 
HETATM 2272 O  O   . HOH   G 5 .   ? 30.054 11.312  18.506 1.00 33.76 ? 369 HOH   A O   1 
HETATM 2273 O  O   . HOH   G 5 .   ? 0.193  5.943   6.391  1.00 27.92 ? 370 HOH   A O   1 
HETATM 2274 O  O   . HOH   G 5 .   ? 30.155 4.563   5.449  1.00 30.91 ? 371 HOH   A O   1 
HETATM 2275 O  O   . HOH   G 5 .   ? 17.819 19.946  17.263 1.00 24.00 ? 372 HOH   A O   1 
HETATM 2276 O  O   . HOH   G 5 .   ? 17.327 -5.171  12.024 1.00 35.38 ? 373 HOH   A O   1 
HETATM 2277 O  O   . HOH   G 5 .   ? 16.465 1.532   30.264 1.00 32.58 ? 374 HOH   A O   1 
HETATM 2278 O  O   . HOH   G 5 .   ? 13.320 11.513  9.396  1.00 20.40 ? 375 HOH   A O   1 
HETATM 2279 O  O   . HOH   G 5 .   ? 12.442 10.908  29.884 1.00 18.52 ? 376 HOH   A O   1 
HETATM 2280 O  O   . HOH   G 5 .   ? 29.925 18.863  7.216  1.00 36.93 ? 377 HOH   A O   1 
HETATM 2281 O  O   . HOH   G 5 .   ? 31.961 8.617   7.306  1.00 28.66 ? 378 HOH   A O   1 
HETATM 2282 O  O   . HOH   G 5 .   ? 29.177 6.863   20.158 1.00 41.16 ? 379 HOH   A O   1 
HETATM 2283 O  O   . HOH   G 5 .   ? 11.192 15.746  18.419 1.00 28.04 ? 380 HOH   A O   1 
HETATM 2284 O  O   . HOH   G 5 .   ? 29.462 11.566  20.961 1.00 28.77 ? 381 HOH   A O   1 
HETATM 2285 O  O   . HOH   G 5 .   ? 34.145 4.576   16.149 1.00 44.59 ? 382 HOH   A O   1 
HETATM 2286 O  O   . HOH   G 5 .   ? 11.176 -7.262  24.631 1.00 28.20 ? 383 HOH   A O   1 
HETATM 2287 O  O   . HOH   G 5 .   ? 18.058 10.431  26.207 1.00 28.60 ? 384 HOH   A O   1 
HETATM 2288 O  O   . HOH   G 5 .   ? 15.229 15.247  3.521  1.00 34.91 ? 385 HOH   A O   1 
HETATM 2289 O  O   . HOH   G 5 .   ? 2.151  14.400  16.856 1.00 29.66 ? 386 HOH   A O   1 
HETATM 2290 O  O   . HOH   G 5 .   ? 31.194 15.518  22.767 1.00 32.89 ? 387 HOH   A O   1 
HETATM 2291 O  O   . HOH   G 5 .   ? 3.391  14.639  4.092  1.00 41.84 ? 388 HOH   A O   1 
HETATM 2292 O  O   . HOH   G 5 .   ? 17.468 0.538   20.135 1.00 19.98 ? 389 HOH   A O   1 
HETATM 2293 O  O   . HOH   G 5 .   ? 33.413 11.235  15.719 1.00 54.87 ? 390 HOH   A O   1 
HETATM 2294 O  O   . HOH   G 5 .   ? 24.149 -3.467  16.234 1.00 31.28 ? 391 HOH   A O   1 
HETATM 2295 O  O   . HOH   G 5 .   ? 3.134  20.849  24.826 1.00 42.38 ? 392 HOH   A O   1 
HETATM 2296 O  O   . HOH   G 5 .   ? 34.360 7.308   16.158 1.00 33.02 ? 393 HOH   A O   1 
HETATM 2297 O  O   . HOH   G 5 .   ? 16.269 9.617   -1.723 1.00 40.79 ? 394 HOH   A O   1 
HETATM 2298 O  O   . HOH   G 5 .   ? 35.067 8.193   8.821  1.00 41.37 ? 395 HOH   A O   1 
HETATM 2299 O  O   . HOH   G 5 .   ? 19.533 2.612   19.403 1.00 21.57 ? 396 HOH   A O   1 
HETATM 2300 O  O   . HOH   G 5 .   ? 1.020  -5.051  17.838 1.00 29.05 ? 397 HOH   A O   1 
HETATM 2301 O  O   . HOH   G 5 .   ? 4.089  0.260   24.170 1.00 17.22 ? 398 HOH   A O   1 
HETATM 2302 O  O   . HOH   G 5 .   ? 0.411  -1.250  16.722 1.00 22.82 ? 399 HOH   A O   1 
HETATM 2303 O  O   . HOH   G 5 .   ? 20.138 13.576  2.200  1.00 37.54 ? 400 HOH   A O   1 
HETATM 2304 O  O   . HOH   G 5 .   ? 30.488 2.687   14.550 1.00 31.71 ? 401 HOH   A O   1 
HETATM 2305 O  O   . HOH   G 5 .   ? 28.257 17.377  24.251 1.00 23.55 ? 402 HOH   A O   1 
HETATM 2306 O  O   . HOH   G 5 .   ? 2.195  15.936  19.162 1.00 40.77 ? 403 HOH   A O   1 
HETATM 2307 O  O   . HOH   G 5 .   ? 9.587  4.025   2.950  1.00 28.23 ? 404 HOH   A O   1 
HETATM 2308 O  O   . HOH   G 5 .   ? 21.494 24.305  11.219 1.00 34.15 ? 405 HOH   A O   1 
HETATM 2309 O  O   . HOH   G 5 .   ? 2.574  8.710   25.614 1.00 32.58 ? 406 HOH   A O   1 
HETATM 2310 O  O   . HOH   G 5 .   ? 8.580  6.333   33.877 1.00 20.00 ? 407 HOH   A O   1 
HETATM 2311 O  O   . HOH   G 5 .   ? 33.975 18.737  10.655 1.00 19.99 ? 408 HOH   A O   1 
HETATM 2312 O  O   . HOH   G 5 .   ? 22.079 19.600  19.431 1.00 33.99 ? 409 HOH   A O   1 
HETATM 2313 O  O   . HOH   G 5 .   ? 7.570  14.096  4.882  1.00 27.64 ? 410 HOH   A O   1 
HETATM 2314 O  O   . HOH   G 5 .   ? 35.024 16.435  20.324 1.00 38.46 ? 411 HOH   A O   1 
HETATM 2315 O  O   . HOH   G 5 .   ? 4.049  15.317  24.851 1.00 49.64 ? 412 HOH   A O   1 
HETATM 2316 O  O   . HOH   G 5 .   ? 23.636 8.102   21.707 1.00 28.51 ? 413 HOH   A O   1 
HETATM 2317 O  O   . HOH   G 5 .   ? 4.123  14.876  20.345 1.00 65.77 ? 414 HOH   A O   1 
HETATM 2318 O  O   . HOH   G 5 .   ? 27.634 -1.222  15.695 1.00 41.07 ? 415 HOH   A O   1 
HETATM 2319 O  O   . HOH   G 5 .   ? 4.105  -4.103  6.274  1.00 31.14 ? 416 HOH   A O   1 
HETATM 2320 O  O   . HOH   G 5 .   ? 23.319 19.047  6.295  1.00 21.45 ? 417 HOH   A O   1 
HETATM 2321 O  O   . HOH   G 5 .   ? 3.236  -0.510  21.597 1.00 22.68 ? 418 HOH   A O   1 
HETATM 2322 O  O   . HOH   G 5 .   ? 3.028  0.531   29.217 1.00 37.68 ? 419 HOH   A O   1 
HETATM 2323 O  O   . HOH   G 5 .   ? 7.226  14.822  21.220 1.00 23.59 ? 420 HOH   A O   1 
HETATM 2324 O  O   . HOH   G 5 .   ? 6.024  -3.782  31.485 1.00 26.91 ? 421 HOH   A O   1 
HETATM 2325 O  O   . HOH   G 5 .   ? 1.086  11.881  27.684 1.00 36.21 ? 422 HOH   A O   1 
HETATM 2326 O  O   . HOH   G 5 .   ? 12.049 24.246  14.385 1.00 43.08 ? 423 HOH   A O   1 
HETATM 2327 O  O   . HOH   G 5 .   ? 19.670 9.401   -0.824 1.00 33.03 ? 424 HOH   A O   1 
HETATM 2328 O  O   . HOH   G 5 .   ? 11.375 -9.966  1.757  1.00 39.43 ? 425 HOH   A O   1 
HETATM 2329 O  O   . HOH   G 5 .   ? 8.576  -6.358  9.485  1.00 32.56 ? 426 HOH   A O   1 
HETATM 2330 O  O   . HOH   G 5 .   ? 23.090 15.465  24.468 1.00 48.51 ? 427 HOH   A O   1 
HETATM 2331 O  O   . HOH   G 5 .   ? 20.146 -4.297  11.276 1.00 31.06 ? 428 HOH   A O   1 
HETATM 2332 O  O   . HOH   G 5 .   ? 22.907 3.125   20.664 1.00 25.34 ? 429 HOH   A O   1 
HETATM 2333 O  O   . HOH   G 5 .   ? 16.820 -3.775  2.881  1.00 34.93 ? 430 HOH   A O   1 
HETATM 2334 O  O   . HOH   G 5 .   ? 4.325  -5.528  14.160 1.00 39.85 ? 431 HOH   A O   1 
HETATM 2335 O  O   . HOH   G 5 .   ? 21.381 9.720   21.830 1.00 18.78 ? 432 HOH   A O   1 
HETATM 2336 O  O   . HOH   G 5 .   ? 6.386  24.171  10.912 1.00 35.83 ? 433 HOH   A O   1 
HETATM 2337 O  O   . HOH   G 5 .   ? 15.581 21.834  8.363  1.00 24.21 ? 434 HOH   A O   1 
HETATM 2338 O  O   . HOH   G 5 .   ? 5.334  8.022   2.362  1.00 40.20 ? 435 HOH   A O   1 
HETATM 2339 O  O   . HOH   G 5 .   ? 25.428 -0.419  -0.652 1.00 36.46 ? 436 HOH   A O   1 
HETATM 2340 O  O   . HOH   G 5 .   ? 8.690  -8.486  2.141  1.00 45.48 ? 437 HOH   A O   1 
HETATM 2341 O  O   . HOH   G 5 .   ? 12.115 17.657  4.570  1.00 51.69 ? 438 HOH   A O   1 
HETATM 2342 O  O   . HOH   G 5 .   ? 16.895 -2.599  19.739 1.00 22.71 ? 439 HOH   A O   1 
HETATM 2343 O  O   . HOH   G 5 .   ? 5.118  27.624  18.215 1.00 49.74 ? 440 HOH   A O   1 
HETATM 2344 O  O   . HOH   G 5 .   ? 9.177  16.704  19.868 1.00 35.13 ? 441 HOH   A O   1 
HETATM 2345 O  O   . HOH   G 5 .   ? 16.352 12.916  26.387 1.00 39.37 ? 442 HOH   A O   1 
HETATM 2346 O  O   . HOH   G 5 .   ? 0.011  -1.431  9.245  1.00 35.87 ? 443 HOH   A O   1 
HETATM 2347 O  O   . HOH   G 5 .   ? 31.642 7.238   5.178  1.00 52.60 ? 444 HOH   A O   1 
HETATM 2348 O  O   . HOH   G 5 .   ? 14.717 13.141  28.883 1.00 36.25 ? 445 HOH   A O   1 
HETATM 2349 O  O   . HOH   G 5 .   ? 7.034  -4.137  2.754  1.00 30.25 ? 446 HOH   A O   1 
HETATM 2350 O  O   . HOH   G 5 .   ? -0.373 14.153  20.344 1.00 42.07 ? 447 HOH   A O   1 
HETATM 2351 O  O   . HOH   G 5 .   ? 14.016 -7.000  26.158 1.00 28.36 ? 448 HOH   A O   1 
HETATM 2352 O  O   . HOH   G 5 .   ? 35.575 10.326  14.321 1.00 51.58 ? 449 HOH   A O   1 
HETATM 2353 O  O   . HOH   G 5 .   ? 29.860 0.432   15.942 1.00 28.12 ? 450 HOH   A O   1 
HETATM 2354 O  O   . HOH   G 5 .   ? 2.875  -0.419  26.684 1.00 22.98 ? 451 HOH   A O   1 
HETATM 2355 O  O   . HOH   G 5 .   ? 27.530 -0.015  4.801  1.00 45.36 ? 452 HOH   A O   1 
HETATM 2356 O  O   . HOH   G 5 .   ? 15.383 -5.424  0.863  1.00 37.13 ? 453 HOH   A O   1 
HETATM 2357 O  O   . HOH   G 5 .   ? 30.981 12.704  23.005 1.00 37.22 ? 454 HOH   A O   1 
HETATM 2358 O  O   . HOH   G 5 .   ? 21.980 19.596  4.083  1.00 32.72 ? 455 HOH   A O   1 
HETATM 2359 O  O   . HOH   G 5 .   ? 8.384  21.548  7.634  1.00 41.38 ? 456 HOH   A O   1 
HETATM 2360 O  O   . HOH   G 5 .   ? 0.762  3.987   26.512 1.00 30.32 ? 457 HOH   A O   1 
HETATM 2361 O  O   . HOH   G 5 .   ? 33.397 17.056  23.164 1.00 39.53 ? 458 HOH   A O   1 
HETATM 2362 O  O   . HOH   G 5 .   ? 18.988 -7.030  8.881  1.00 35.66 ? 459 HOH   A O   1 
HETATM 2363 O  O   . HOH   G 5 .   ? -2.184 -0.293  8.048  1.00 37.39 ? 460 HOH   A O   1 
HETATM 2364 O  O   . HOH   G 5 .   ? 12.664 -5.165  33.257 1.00 31.71 ? 461 HOH   A O   1 
HETATM 2365 O  O   . HOH   G 5 .   ? 7.443  17.528  26.370 1.00 67.44 ? 462 HOH   A O   1 
HETATM 2366 O  O   . HOH   G 5 .   ? -0.572 13.514  16.611 1.00 29.96 ? 463 HOH   A O   1 
HETATM 2367 O  O   . HOH   G 5 .   ? 31.336 4.278   16.568 1.00 37.42 ? 464 HOH   A O   1 
HETATM 2368 O  O   . HOH   G 5 .   ? 6.848  20.093  27.787 1.00 46.96 ? 465 HOH   A O   1 
HETATM 2369 O  O   . HOH   G 5 .   ? 25.716 13.283  2.814  1.00 33.05 ? 466 HOH   A O   1 
HETATM 2370 O  O   . HOH   G 5 .   ? 1.637  -3.004  27.168 1.00 36.87 ? 467 HOH   A O   1 
HETATM 2371 O  O   . HOH   G 5 .   ? 9.866  -12.730 0.696  1.00 46.07 ? 468 HOH   A O   1 
HETATM 2372 O  O   . HOH   G 5 .   ? 1.825  -4.953  25.509 1.00 41.82 ? 469 HOH   A O   1 
HETATM 2373 O  O   . HOH   H 5 .   ? 3.530  -13.033 20.210 1.00 38.63 ? 301 HOH   C O   1 
HETATM 2374 O  O   . HOH   H 5 .   ? 27.444 -35.157 2.410  1.00 35.43 ? 302 HOH   C O   1 
HETATM 2375 O  O   . HOH   H 5 .   ? 30.878 -32.424 0.765  1.00 36.57 ? 303 HOH   C O   1 
HETATM 2376 O  O   . HOH   H 5 .   ? 22.254 -7.304  25.260 1.00 35.95 ? 304 HOH   C O   1 
HETATM 2377 O  O   . HOH   H 5 .   ? 24.043 -8.182  9.541  1.00 23.73 ? 305 HOH   C O   1 
HETATM 2378 O  O   . HOH   H 5 .   ? 38.512 -7.087  7.640  1.00 29.74 ? 306 HOH   C O   1 
HETATM 2379 O  O   . HOH   H 5 .   ? 37.382 -31.885 11.236 1.00 20.61 ? 307 HOH   C O   1 
HETATM 2380 O  O   . HOH   H 5 .   ? 38.465 -18.512 21.900 1.00 29.70 ? 308 HOH   C O   1 
HETATM 2381 O  O   . HOH   H 5 .   ? 16.500 -16.141 9.064  1.00 41.12 ? 309 HOH   C O   1 
HETATM 2382 O  O   . HOH   H 5 .   ? 31.180 -23.368 -1.325 1.00 21.93 ? 310 HOH   C O   1 
HETATM 2383 O  O   . HOH   H 5 .   ? 42.610 -11.367 11.650 1.00 28.29 ? 311 HOH   C O   1 
HETATM 2384 O  O   . HOH   H 5 .   ? 29.648 -25.500 -1.079 1.00 30.84 ? 312 HOH   C O   1 
HETATM 2385 O  O   . HOH   H 5 .   ? 17.732 -6.008  24.224 1.00 23.53 ? 313 HOH   C O   1 
HETATM 2386 O  O   . HOH   H 5 .   ? 36.195 -25.866 34.514 1.00 39.80 ? 314 HOH   C O   1 
HETATM 2387 O  O   . HOH   H 5 .   ? 20.820 -18.671 12.884 1.00 16.54 ? 315 HOH   C O   1 
HETATM 2388 O  O   . HOH   H 5 .   ? 10.231 -17.703 18.345 1.00 34.71 ? 316 HOH   C O   1 
HETATM 2389 O  O   . HOH   H 5 .   ? 17.825 -27.545 16.571 1.00 23.72 ? 317 HOH   C O   1 
HETATM 2390 O  O   . HOH   H 5 .   ? 24.174 -9.777  27.213 1.00 37.29 ? 318 HOH   C O   1 
HETATM 2391 O  O   . HOH   H 5 .   ? 30.549 -18.160 27.089 1.00 20.75 ? 319 HOH   C O   1 
HETATM 2392 O  O   . HOH   H 5 .   ? 19.473 -4.057  20.236 1.00 21.47 ? 320 HOH   C O   1 
HETATM 2393 O  O   . HOH   H 5 .   ? 23.367 -33.475 29.053 1.00 26.51 ? 321 HOH   C O   1 
HETATM 2394 O  O   . HOH   H 5 .   ? 40.150 -29.493 12.224 1.00 32.17 ? 322 HOH   C O   1 
HETATM 2395 O  O   . HOH   H 5 .   ? 17.764 -33.579 23.828 1.00 35.63 ? 323 HOH   C O   1 
HETATM 2396 O  O   . HOH   H 5 .   ? 18.065 -24.258 8.590  1.00 45.99 ? 324 HOH   C O   1 
HETATM 2397 O  O   . HOH   H 5 .   ? 26.960 -35.428 20.814 1.00 27.26 ? 325 HOH   C O   1 
HETATM 2398 O  O   . HOH   H 5 .   ? 26.052 -31.078 31.032 1.00 22.53 ? 326 HOH   C O   1 
HETATM 2399 O  O   . HOH   H 5 .   ? 22.067 -28.307 4.846  1.00 28.60 ? 327 HOH   C O   1 
HETATM 2400 O  O   . HOH   H 5 .   ? 37.274 -18.441 28.519 1.00 40.01 ? 328 HOH   C O   1 
HETATM 2401 O  O   . HOH   H 5 .   ? 29.735 -15.214 19.901 1.00 17.46 ? 329 HOH   C O   1 
HETATM 2402 O  O   . HOH   H 5 .   ? 24.852 -15.697 7.571  1.00 24.26 ? 330 HOH   C O   1 
HETATM 2403 O  O   . HOH   H 5 .   ? 29.581 -16.099 30.725 1.00 31.50 ? 331 HOH   C O   1 
HETATM 2404 O  O   . HOH   H 5 .   ? 26.187 -25.089 8.916  1.00 16.29 ? 332 HOH   C O   1 
HETATM 2405 O  O   . HOH   H 5 .   ? 11.699 -24.209 21.738 1.00 20.80 ? 333 HOH   C O   1 
HETATM 2406 O  O   . HOH   H 5 .   ? 13.009 -11.222 28.593 1.00 36.55 ? 334 HOH   C O   1 
HETATM 2407 O  O   . HOH   H 5 .   ? 36.529 -16.307 12.393 1.00 31.63 ? 335 HOH   C O   1 
HETATM 2408 O  O   . HOH   H 5 .   ? 40.647 -27.168 15.507 1.00 15.62 ? 336 HOH   C O   1 
HETATM 2409 O  O   . HOH   H 5 .   ? 23.094 -30.786 13.427 1.00 28.80 ? 337 HOH   C O   1 
HETATM 2410 O  O   . HOH   H 5 .   ? 31.622 -35.284 31.692 1.00 43.28 ? 338 HOH   C O   1 
HETATM 2411 O  O   . HOH   H 5 .   ? 41.399 -24.850 7.500  1.00 27.82 ? 339 HOH   C O   1 
HETATM 2412 O  O   . HOH   H 5 .   ? 22.815 -5.809  21.309 1.00 23.24 ? 340 HOH   C O   1 
HETATM 2413 O  O   . HOH   H 5 .   ? 27.747 -16.396 22.409 1.00 18.02 ? 341 HOH   C O   1 
HETATM 2414 O  O   . HOH   H 5 .   ? 23.270 -25.187 8.878  1.00 18.85 ? 342 HOH   C O   1 
HETATM 2415 O  O   . HOH   H 5 .   ? 18.946 -28.018 28.267 1.00 23.22 ? 343 HOH   C O   1 
HETATM 2416 O  O   . HOH   H 5 .   ? 23.074 -8.440  14.184 1.00 21.39 ? 344 HOH   C O   1 
HETATM 2417 O  O   . HOH   H 5 .   ? 34.556 -23.433 -0.493 1.00 25.61 ? 345 HOH   C O   1 
HETATM 2418 O  O   . HOH   H 5 .   ? 30.034 -10.651 28.256 1.00 43.17 ? 346 HOH   C O   1 
HETATM 2419 O  O   . HOH   H 5 .   ? 30.908 -5.986  6.116  1.00 44.94 ? 347 HOH   C O   1 
HETATM 2420 O  O   . HOH   H 5 .   ? 13.157 -29.790 19.236 1.00 42.77 ? 348 HOH   C O   1 
HETATM 2421 O  O   . HOH   H 5 .   ? 25.969 -38.028 24.424 1.00 30.60 ? 349 HOH   C O   1 
HETATM 2422 O  O   . HOH   H 5 .   ? 33.008 -9.685  11.433 1.00 20.32 ? 350 HOH   C O   1 
HETATM 2423 O  O   . HOH   H 5 .   ? 30.784 -21.545 28.631 1.00 15.58 ? 351 HOH   C O   1 
HETATM 2424 O  O   . HOH   H 5 .   ? 10.355 -17.019 14.926 1.00 40.24 ? 352 HOH   C O   1 
HETATM 2425 O  O   . HOH   H 5 .   ? 18.826 -8.673  12.975 1.00 31.83 ? 353 HOH   C O   1 
HETATM 2426 O  O   . HOH   H 5 .   ? 35.482 -13.079 9.175  1.00 20.37 ? 354 HOH   C O   1 
HETATM 2427 O  O   . HOH   H 5 .   ? 29.898 -13.064 13.255 1.00 18.20 ? 355 HOH   C O   1 
HETATM 2428 O  O   . HOH   H 5 .   ? 36.539 -21.205 7.165  1.00 29.22 ? 356 HOH   C O   1 
HETATM 2429 O  O   . HOH   H 5 .   ? 32.324 -23.688 29.317 1.00 18.71 ? 357 HOH   C O   1 
HETATM 2430 O  O   . HOH   H 5 .   ? 35.376 -24.611 25.165 1.00 27.02 ? 358 HOH   C O   1 
HETATM 2431 O  O   . HOH   H 5 .   ? 38.881 -14.352 14.157 1.00 31.85 ? 359 HOH   C O   1 
HETATM 2432 O  O   . HOH   H 5 .   ? 40.803 -22.574 25.486 1.00 37.55 ? 360 HOH   C O   1 
HETATM 2433 O  O   . HOH   H 5 .   ? 23.506 -3.324  19.232 1.00 39.15 ? 361 HOH   C O   1 
HETATM 2434 O  O   . HOH   H 5 .   ? 29.018 -36.051 7.782  1.00 23.98 ? 362 HOH   C O   1 
HETATM 2435 O  O   . HOH   H 5 .   ? 35.695 -34.290 18.227 1.00 35.33 ? 363 HOH   C O   1 
HETATM 2436 O  O   . HOH   H 5 .   ? 31.392 -12.158 10.912 1.00 19.75 ? 364 HOH   C O   1 
HETATM 2437 O  O   . HOH   H 5 .   ? 11.176 -22.311 28.598 1.00 35.98 ? 365 HOH   C O   1 
HETATM 2438 O  O   . HOH   H 5 .   ? 25.922 -15.281 30.990 1.00 30.75 ? 366 HOH   C O   1 
HETATM 2439 O  O   . HOH   H 5 .   ? 14.674 -24.133 12.187 1.00 42.17 ? 367 HOH   C O   1 
HETATM 2440 O  O   . HOH   H 5 .   ? 22.949 -28.016 12.618 1.00 20.23 ? 368 HOH   C O   1 
HETATM 2441 O  O   . HOH   H 5 .   ? 6.586  -9.231  22.557 1.00 27.43 ? 369 HOH   C O   1 
HETATM 2442 O  O   . HOH   H 5 .   ? 27.872 -4.295  18.761 1.00 42.11 ? 370 HOH   C O   1 
HETATM 2443 O  O   . HOH   H 5 .   ? 22.439 -10.857 7.814  1.00 39.92 ? 371 HOH   C O   1 
HETATM 2444 O  O   . HOH   H 5 .   ? 37.363 -31.678 25.725 1.00 27.90 ? 372 HOH   C O   1 
HETATM 2445 O  O   . HOH   H 5 .   ? 10.006 -24.795 19.764 1.00 26.56 ? 373 HOH   C O   1 
HETATM 2446 O  O   . HOH   H 5 .   ? 32.232 -10.293 14.053 1.00 26.17 ? 374 HOH   C O   1 
HETATM 2447 O  O   . HOH   H 5 .   ? 32.254 -34.687 23.699 1.00 76.94 ? 375 HOH   C O   1 
HETATM 2448 O  O   . HOH   H 5 .   ? 35.240 -3.450  8.391  1.00 26.16 ? 376 HOH   C O   1 
HETATM 2449 O  O   . HOH   H 5 .   ? 5.633  -25.090 28.328 1.00 45.58 ? 377 HOH   C O   1 
HETATM 2450 O  O   . HOH   H 5 .   ? 20.748 -25.833 13.821 1.00 23.73 ? 378 HOH   C O   1 
HETATM 2451 O  O   . HOH   H 5 .   ? 14.719 -28.803 26.139 1.00 46.43 ? 379 HOH   C O   1 
HETATM 2452 O  O   . HOH   H 5 .   ? 38.787 -13.339 11.492 1.00 28.47 ? 380 HOH   C O   1 
HETATM 2453 O  O   . HOH   H 5 .   ? 22.015 -13.760 29.671 1.00 39.99 ? 381 HOH   C O   1 
HETATM 2454 O  O   . HOH   H 5 .   ? 10.670 -17.004 12.309 1.00 34.37 ? 382 HOH   C O   1 
HETATM 2455 O  O   . HOH   H 5 .   ? 26.410 -12.099 27.869 1.00 31.53 ? 383 HOH   C O   1 
HETATM 2456 O  O   . HOH   H 5 .   ? 35.745 -32.813 3.617  1.00 37.72 ? 384 HOH   C O   1 
HETATM 2457 O  O   . HOH   H 5 .   ? 37.038 -29.093 10.332 1.00 23.59 ? 385 HOH   C O   1 
HETATM 2458 O  O   . HOH   H 5 .   ? 38.099 -23.495 4.628  1.00 39.78 ? 386 HOH   C O   1 
HETATM 2459 O  O   . HOH   H 5 .   ? 18.376 -8.348  25.577 1.00 20.07 ? 387 HOH   C O   1 
HETATM 2460 O  O   . HOH   H 5 .   ? 10.904 -21.780 13.518 1.00 40.37 ? 388 HOH   C O   1 
HETATM 2461 O  O   . HOH   H 5 .   ? 34.034 -33.565 24.609 1.00 28.25 ? 389 HOH   C O   1 
HETATM 2462 O  O   . HOH   H 5 .   ? 32.150 -15.531 7.391  1.00 32.74 ? 390 HOH   C O   1 
HETATM 2463 O  O   . HOH   H 5 .   ? 33.922 -13.479 26.066 1.00 23.45 ? 391 HOH   C O   1 
HETATM 2464 O  O   . HOH   H 5 .   ? 26.312 -31.253 14.738 1.00 21.46 ? 392 HOH   C O   1 
HETATM 2465 O  O   . HOH   H 5 .   ? 9.418  -8.877  23.690 1.00 31.16 ? 393 HOH   C O   1 
HETATM 2466 O  O   . HOH   H 5 .   ? 35.779 -28.518 8.062  1.00 21.84 ? 394 HOH   C O   1 
HETATM 2467 O  O   . HOH   H 5 .   ? 21.700 -18.744 5.995  1.00 27.73 ? 395 HOH   C O   1 
HETATM 2468 O  O   . HOH   H 5 .   ? 20.291 -32.265 22.265 1.00 34.20 ? 396 HOH   C O   1 
HETATM 2469 O  O   . HOH   H 5 .   ? 3.910  -10.392 19.687 1.00 31.27 ? 397 HOH   C O   1 
HETATM 2470 O  O   . HOH   H 5 .   ? 8.759  -13.265 10.607 1.00 28.23 ? 398 HOH   C O   1 
HETATM 2471 O  O   . HOH   H 5 .   ? 36.388 -28.589 3.288  1.00 39.39 ? 399 HOH   C O   1 
HETATM 2472 O  O   . HOH   H 5 .   ? 34.675 -3.950  17.958 1.00 31.25 ? 400 HOH   C O   1 
HETATM 2473 O  O   . HOH   H 5 .   ? 38.783 -16.184 3.966  1.00 42.50 ? 401 HOH   C O   1 
HETATM 2474 O  O   . HOH   H 5 .   ? 37.967 -20.155 5.052  1.00 44.80 ? 402 HOH   C O   1 
HETATM 2475 O  O   . HOH   H 5 .   ? 6.091  -17.077 19.439 1.00 45.38 ? 403 HOH   C O   1 
HETATM 2476 O  O   . HOH   H 5 .   ? 20.174 -23.753 34.970 1.00 30.12 ? 404 HOH   C O   1 
HETATM 2477 O  O   . HOH   H 5 .   ? 39.984 -29.779 14.888 1.00 21.97 ? 405 HOH   C O   1 
HETATM 2478 O  O   . HOH   H 5 .   ? 30.556 -17.789 8.481  1.00 29.66 ? 406 HOH   C O   1 
HETATM 2479 O  O   . HOH   H 5 .   ? 33.027 -14.182 9.780  1.00 20.58 ? 407 HOH   C O   1 
HETATM 2480 O  O   . HOH   H 5 .   ? 4.768  -11.987 14.063 1.00 44.53 ? 408 HOH   C O   1 
HETATM 2481 O  O   . HOH   H 5 .   ? 17.315 -25.420 12.728 1.00 25.88 ? 409 HOH   C O   1 
HETATM 2482 O  O   . HOH   H 5 .   ? 32.904 -30.400 31.791 1.00 18.78 ? 410 HOH   C O   1 
HETATM 2483 O  O   . HOH   H 5 .   ? 35.271 -13.272 6.640  1.00 29.15 ? 411 HOH   C O   1 
HETATM 2484 O  O   . HOH   H 5 .   ? 33.837 -35.922 8.819  1.00 39.61 ? 412 HOH   C O   1 
HETATM 2485 O  O   . HOH   H 5 .   ? 25.818 -6.096  23.317 1.00 24.75 ? 413 HOH   C O   1 
HETATM 2486 O  O   . HOH   H 5 .   ? 18.742 -19.168 10.884 1.00 25.58 ? 414 HOH   C O   1 
HETATM 2487 O  O   . HOH   H 5 .   ? 16.863 -9.344  27.800 1.00 32.40 ? 415 HOH   C O   1 
HETATM 2488 O  O   . HOH   H 5 .   ? 33.593 -32.831 0.829  1.00 32.41 ? 416 HOH   C O   1 
HETATM 2489 O  O   . HOH   H 5 .   ? 31.802 -13.469 4.670  1.00 39.79 ? 417 HOH   C O   1 
HETATM 2490 O  O   . HOH   H 5 .   ? 3.862  -12.758 17.121 1.00 47.35 ? 418 HOH   C O   1 
HETATM 2491 O  O   . HOH   H 5 .   ? 6.396  -23.136 18.202 1.00 43.54 ? 419 HOH   C O   1 
HETATM 2492 O  O   . HOH   H 5 .   ? 16.459 -20.562 11.488 1.00 25.02 ? 420 HOH   C O   1 
HETATM 2493 O  O   . HOH   H 5 .   ? 3.752  -8.402  14.819 1.00 35.95 ? 421 HOH   C O   1 
HETATM 2494 O  O   . HOH   H 5 .   ? 22.844 -33.194 5.557  1.00 34.52 ? 422 HOH   C O   1 
HETATM 2495 O  O   . HOH   H 5 .   ? 33.978 -15.420 27.432 1.00 38.89 ? 423 HOH   C O   1 
HETATM 2496 O  O   . HOH   H 5 .   ? 10.339 -31.015 25.561 1.00 46.70 ? 424 HOH   C O   1 
HETATM 2497 O  O   . HOH   H 5 .   ? 38.746 -13.108 26.417 1.00 31.32 ? 425 HOH   C O   1 
HETATM 2498 O  O   . HOH   H 5 .   ? 39.033 -14.139 8.380  1.00 33.71 ? 426 HOH   C O   1 
HETATM 2499 O  O   . HOH   H 5 .   ? 15.156 -29.665 17.623 1.00 35.56 ? 427 HOH   C O   1 
HETATM 2500 O  O   . HOH   H 5 .   ? 20.252 -19.690 36.376 1.00 31.64 ? 428 HOH   C O   1 
HETATM 2501 O  O   . HOH   H 5 .   ? 41.996 -12.405 14.105 1.00 37.87 ? 429 HOH   C O   1 
HETATM 2502 O  O   . HOH   H 5 .   ? 23.012 -17.646 33.476 1.00 20.17 ? 430 HOH   C O   1 
HETATM 2503 O  O   . HOH   H 5 .   ? 34.690 -30.249 33.982 1.00 40.12 ? 431 HOH   C O   1 
HETATM 2504 O  O   . HOH   H 5 .   ? 24.536 -16.306 3.325  1.00 40.34 ? 432 HOH   C O   1 
HETATM 2505 O  O   . HOH   H 5 .   ? 23.237 -16.947 5.819  1.00 35.98 ? 433 HOH   C O   1 
HETATM 2506 O  O   . HOH   H 5 .   ? 6.388  -20.227 17.834 1.00 39.44 ? 434 HOH   C O   1 
HETATM 2507 O  O   . HOH   H 5 .   ? 37.218 -14.708 10.276 1.00 24.68 ? 435 HOH   C O   1 
HETATM 2508 O  O   . HOH   H 5 .   ? 31.999 -16.956 29.740 1.00 40.29 ? 436 HOH   C O   1 
HETATM 2509 O  O   . HOH   H 5 .   ? 27.661 -5.371  7.316  1.00 34.90 ? 437 HOH   C O   1 
HETATM 2510 O  O   . HOH   H 5 .   ? 11.479 -12.105 8.266  1.00 43.29 ? 438 HOH   C O   1 
HETATM 2511 O  O   . HOH   H 5 .   ? 34.191 -31.734 29.622 1.00 24.15 ? 439 HOH   C O   1 
HETATM 2512 O  O   . HOH   H 5 .   ? 23.376 -15.592 31.666 1.00 31.44 ? 440 HOH   C O   1 
HETATM 2513 O  O   . HOH   H 5 .   ? 20.736 -17.599 34.798 1.00 26.26 ? 441 HOH   C O   1 
HETATM 2514 O  O   . HOH   H 5 .   ? 4.929  -17.410 22.119 1.00 51.58 ? 442 HOH   C O   1 
HETATM 2515 O  O   . HOH   H 5 .   ? 30.187 -3.863  17.218 1.00 33.57 ? 443 HOH   C O   1 
HETATM 2516 O  O   . HOH   H 5 .   ? 16.533 -27.641 14.160 1.00 34.24 ? 444 HOH   C O   1 
HETATM 2517 O  O   . HOH   H 5 .   ? 20.969 -27.059 11.891 1.00 40.44 ? 445 HOH   C O   1 
HETATM 2518 O  O   . HOH   H 5 .   ? 18.798 -26.206 10.462 1.00 31.04 ? 446 HOH   C O   1 
HETATM 2519 O  O   . HOH   H 5 .   ? 33.740 -20.263 -2.099 1.00 37.33 ? 447 HOH   C O   1 
HETATM 2520 O  O   . HOH   H 5 .   ? 37.366 -28.980 5.844  1.00 36.40 ? 448 HOH   C O   1 
HETATM 2521 O  O   . HOH   H 5 .   ? 32.391 -19.371 29.245 1.00 27.11 ? 449 HOH   C O   1 
HETATM 2522 O  O   . HOH   H 5 .   ? 38.010 -31.538 5.055  1.00 43.97 ? 450 HOH   C O   1 
HETATM 2523 O  O   . HOH   H 5 .   ? 34.588 -2.046  16.365 1.00 31.90 ? 451 HOH   C O   1 
HETATM 2524 O  O   . HOH   H 5 .   ? 41.840 -16.035 11.479 1.00 32.89 ? 452 HOH   C O   1 
HETATM 2525 O  O   . HOH   H 5 .   ? 41.708 -15.123 14.126 1.00 26.93 ? 453 HOH   C O   1 
HETATM 2526 O  O   . HOH   H 5 .   ? 34.939 -23.094 29.128 1.00 32.79 ? 454 HOH   C O   1 
HETATM 2527 O  O   . HOH   H 5 .   ? 37.820 -34.049 9.464  1.00 35.85 ? 455 HOH   C O   1 
HETATM 2528 O  O   . HOH   H 5 .   ? 3.177  -9.532  17.063 1.00 38.29 ? 456 HOH   C O   1 
HETATM 2529 O  O   . HOH   H 5 .   ? 11.215 -13.705 29.205 1.00 38.43 ? 457 HOH   C O   1 
HETATM 2530 O  O   . HOH   H 5 .   ? 19.589 -28.365 7.807  1.00 43.73 ? 458 HOH   C O   1 
HETATM 2531 O  O   . HOH   H 5 .   ? 2.831  -8.109  22.053 1.00 46.44 ? 459 HOH   C O   1 
HETATM 2532 O  O   . HOH   H 5 .   ? 18.974 -15.395 34.886 1.00 25.81 ? 460 HOH   C O   1 
HETATM 2533 O  O   . HOH   H 5 .   ? 38.362 -36.326 10.916 1.00 49.81 ? 461 HOH   C O   1 
HETATM 2534 O  O   . HOH   H 5 .   ? 20.776 -14.747 4.847  1.00 51.73 ? 462 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   ? 0.3407 0.2304 0.2059 -0.0473 -0.0277 -0.0128 7   SER   A N   
2    C CA  . SER   A 1   ? 0.3435 0.2387 0.2217 -0.0415 -0.0340 -0.0081 7   SER   A CA  
3    C C   . SER   A 1   ? 0.3191 0.2183 0.2109 -0.0300 -0.0398 -0.0005 7   SER   A C   
4    O O   . SER   A 1   ? 0.3183 0.2169 0.2076 -0.0285 -0.0413 0.0023  7   SER   A O   
5    C CB  . SER   A 1   ? 0.3727 0.2746 0.2436 -0.0535 -0.0436 -0.0040 7   SER   A CB  
6    O OG  . SER   A 1   ? 0.4159 0.3229 0.2816 -0.0581 -0.0534 0.0049  7   SER   A OG  
7    N N   . GLY   A 2   ? 0.2946 0.1971 0.2006 -0.0232 -0.0413 0.0015  8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.2862 0.1916 0.2057 -0.0146 -0.0438 0.0061  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.2754 0.1822 0.2066 -0.0078 -0.0393 0.0036  8   GLY   A C   
10   O O   . GLY   A 2   ? 0.2683 0.1733 0.1978 -0.0072 -0.0333 -0.0005 8   GLY   A O   
11   N N   . ALA   A 3   ? 0.2635 0.1736 0.2082 -0.0036 -0.0413 0.0065  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.2572 0.1695 0.2114 0.0005  -0.0366 0.0036  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.2486 0.1619 0.2125 0.0037  -0.0334 0.0030  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.2572 0.1690 0.2249 0.0039  -0.0356 0.0059  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.2562 0.1716 0.2191 -0.0008 -0.0398 0.0049  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.2346 0.1504 0.2017 0.0046  -0.0275 -0.0008 10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.2328 0.1496 0.2084 0.0046  -0.0218 -0.0042 10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.2438 0.1623 0.2358 0.0053  -0.0203 -0.0054 10  ILE   A C   
19   O O   . ILE   A 4   ? 0.2454 0.1666 0.2362 0.0048  -0.0205 -0.0060 10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.2315 0.1522 0.1979 0.0013  -0.0157 -0.0078 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.2374 0.1583 0.1908 0.0009  -0.0174 -0.0049 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.2267 0.1476 0.1993 -0.0023 -0.0080 -0.0137 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.2614 0.1902 0.2081 -0.0033 -0.0141 -0.0038 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.2350 0.1520 0.2452 0.0064  -0.0176 -0.0056 11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.2386 0.1572 0.2695 0.0073  -0.0143 -0.0067 11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.2442 0.1614 0.2837 0.0043  -0.0011 -0.0160 11  TYR   A C   
27   O O   . TYR   A 5   ? 0.2471 0.1600 0.2997 0.0047  0.0042  -0.0174 11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.2340 0.1533 0.2858 0.0102  -0.0214 0.0027  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.2375 0.1601 0.2781 0.0090  -0.0335 0.0104  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.2535 0.1801 0.2943 0.0078  -0.0365 0.0108  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.2565 0.1778 0.2840 0.0072  -0.0407 0.0158  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.2543 0.1834 0.2824 0.0039  -0.0456 0.0156  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.2711 0.1953 0.2858 0.0028  -0.0498 0.0206  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.2733 0.2012 0.2877 0.0007  -0.0517 0.0199  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.2975 0.2275 0.2973 -0.0062 -0.0587 0.0224  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.2413 0.1619 0.2723 -0.0003 0.0050  -0.0226 12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.2562 0.1768 0.2893 -0.0074 0.0187  -0.0334 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.2684 0.1917 0.3132 -0.0096 0.0248  -0.0380 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.2769 0.2049 0.3127 -0.0092 0.0189  -0.0346 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.2753 0.2006 0.2821 -0.0154 0.0204  -0.0364 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.2720 0.2040 0.2629 -0.0153 0.0122  -0.0299 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.2883 0.2153 0.2937 -0.0269 0.0349  -0.0483 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.2703 0.1900 0.3378 -0.0117 0.0375  -0.0457 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.2747 0.1964 0.3573 -0.0138 0.0451  -0.0509 13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.2698 0.1948 0.3621 -0.0057 0.0327  -0.0404 13  GLY   A C   
46   O O   . GLY   A 7   ? 0.2691 0.1930 0.3740 0.0016  0.0231  -0.0303 13  GLY   A O   
47   N N   . ASN   A 8   ? 0.2629 0.1931 0.3460 -0.0085 0.0317  -0.0416 14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.2603 0.1936 0.3489 -0.0028 0.0204  -0.0328 14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.2608 0.1963 0.3224 -0.0023 0.0092  -0.0269 14  ASN   A C   
50   O O   . ASN   A 8   ? 0.2690 0.2074 0.3273 -0.0018 0.0042  -0.0239 14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.2736 0.2101 0.3773 -0.0047 0.0269  -0.0371 14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.3186 0.2527 0.4593 -0.0020 0.0357  -0.0388 14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.3266 0.2632 0.4909 0.0044  0.0279  -0.0289 14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.3050 0.2351 0.4533 -0.0079 0.0527  -0.0509 14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.2492 0.1826 0.2948 -0.0024 0.0061  -0.0252 15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.2454 0.1797 0.2700 -0.0019 -0.0018 -0.0200 15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.2332 0.1638 0.2540 0.0022  -0.0101 -0.0140 15  TYR   A C   
58   O O   . TYR   A 9   ? 0.2403 0.1680 0.2672 0.0034  -0.0091 -0.0140 15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.2587 0.1965 0.2656 -0.0081 0.0029  -0.0225 15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.2711 0.2147 0.2764 -0.0155 0.0101  -0.0272 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.2887 0.2355 0.2942 -0.0152 0.0076  -0.0241 15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.2815 0.2276 0.2838 -0.0245 0.0204  -0.0352 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.2906 0.2436 0.2935 -0.0231 0.0138  -0.0274 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.2895 0.2422 0.2872 -0.0343 0.0274  -0.0398 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.3015 0.2580 0.2996 -0.0332 0.0234  -0.0351 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.3178 0.2815 0.3109 -0.0436 0.0297  -0.0385 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.2278 0.1580 0.2371 0.0031  -0.0168 -0.0097 16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.2208 0.1476 0.2213 0.0043  -0.0233 -0.0055 16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.2300 0.1562 0.2151 0.0033  -0.0216 -0.0054 16  ARG   A C   
70   O O   . ARG   A 10  ? 0.2240 0.1513 0.2076 0.0026  -0.0204 -0.0051 16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.2237 0.1509 0.2278 0.0035  -0.0308 -0.0014 16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.2223 0.1465 0.2118 0.0008  -0.0358 0.0008  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.2550 0.1820 0.2464 -0.0040 -0.0438 0.0051  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.2687 0.1924 0.2435 -0.0100 -0.0440 0.0026  16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.3047 0.2262 0.2664 -0.0153 -0.0469 0.0035  16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.3018 0.2245 0.2647 -0.0145 -0.0513 0.0084  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.3220 0.2391 0.2697 -0.0221 -0.0436 -0.0015 16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.2197 0.1445 0.1966 0.0033  -0.0209 -0.0048 17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.2152 0.1408 0.1828 0.0028  -0.0192 -0.0026 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.2269 0.1468 0.1881 0.0035  -0.0219 -0.0014 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.2277 0.1452 0.1858 0.0035  -0.0246 -0.0014 17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.2193 0.1495 0.1825 0.0003  -0.0160 -0.0025 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.2218 0.1563 0.1808 -0.0007 -0.0152 0.0033  17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.2118 0.1470 0.1792 -0.0038 -0.0114 -0.0065 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.2232 0.1405 0.1833 0.0030  -0.0202 -0.0010 18  VAL   A N   
86   C CA  A VAL   A 12  ? 0.2274 0.1385 0.1806 0.0011  -0.0199 -0.0024 18  VAL   A CA  
87   C CA  B VAL   A 12  ? 0.2375 0.1485 0.1906 0.0011  -0.0199 -0.0024 18  VAL   A CA  
88   C C   . VAL   A 12  ? 0.2269 0.1360 0.1830 0.0020  -0.0131 -0.0010 18  VAL   A C   
89   O O   . VAL   A 12  ? 0.2294 0.1431 0.1942 0.0038  -0.0104 0.0031  18  VAL   A O   
90   C CB  A VAL   A 12  ? 0.2266 0.1346 0.1776 -0.0033 -0.0222 -0.0053 18  VAL   A CB  
91   C CB  B VAL   A 12  ? 0.2570 0.1656 0.2090 -0.0031 -0.0225 -0.0052 18  VAL   A CB  
92   C CG1 A VAL   A 12  ? 0.2500 0.1613 0.2019 -0.0048 -0.0301 -0.0034 18  VAL   A CG1 
93   C CG1 B VAL   A 12  ? 0.2687 0.1712 0.2105 -0.0092 -0.0206 -0.0088 18  VAL   A CG1 
94   C CG2 A VAL   A 12  ? 0.2045 0.1130 0.1629 -0.0033 -0.0187 -0.0064 18  VAL   A CG2 
95   C CG2 B VAL   A 12  ? 0.2771 0.1898 0.2328 -0.0035 -0.0298 -0.0033 18  VAL   A CG2 
96   N N   . ASN   A 13  ? 0.2211 0.1239 0.1721 -0.0002 -0.0095 -0.0035 19  ASN   A N   
97   C CA  . ASN   A 13  ? 0.2157 0.1154 0.1759 0.0008  -0.0006 -0.0021 19  ASN   A CA  
98   C C   . ASN   A 13  ? 0.2205 0.1167 0.1884 -0.0008 0.0042  -0.0048 19  ASN   A C   
99   O O   . ASN   A 13  ? 0.2311 0.1235 0.1905 -0.0060 0.0025  -0.0110 19  ASN   A O   
100  C CB  . ASN   A 13  ? 0.2287 0.1204 0.1820 -0.0031 0.0047  -0.0075 19  ASN   A CB  
101  C CG  . ASN   A 13  ? 0.2425 0.1371 0.1883 -0.0018 0.0004  -0.0050 19  ASN   A CG  
102  O OD1 . ASN   A 13  ? 0.2549 0.1492 0.1882 -0.0046 -0.0063 -0.0070 19  ASN   A OD1 
103  N ND2 . ASN   A 13  ? 0.2288 0.1272 0.1843 0.0021  0.0036  0.0009  19  ASN   A ND2 
104  N N   . ARG   A 14  ? 0.2223 0.1207 0.2066 0.0026  0.0095  0.0011  20  ARG   A N   
105  C CA  . ARG   A 14  ? 0.2311 0.1256 0.2250 0.0013  0.0149  -0.0009 20  ARG   A CA  
106  C C   . ARG   A 14  ? 0.2576 0.1398 0.2482 -0.0050 0.0244  -0.0116 20  ARG   A C   
107  O O   . ARG   A 14  ? 0.2706 0.1493 0.2570 -0.0101 0.0253  -0.0179 20  ARG   A O   
108  C CB  . ARG   A 14  ? 0.2402 0.1399 0.2560 0.0058  0.0193  0.0102  20  ARG   A CB  
109  C CG  . ARG   A 14  ? 0.2241 0.1208 0.2529 0.0052  0.0247  0.0104  20  ARG   A CG  
110  C CD  . ARG   A 14  ? 0.2381 0.1399 0.2933 0.0093  0.0297  0.0243  20  ARG   A CD  
111  N NE  . ARG   A 14  ? 0.2649 0.1653 0.3348 0.0092  0.0341  0.0270  20  ARG   A NE  
112  C CZ  . ARG   A 14  ? 0.3053 0.1932 0.3888 0.0079  0.0467  0.0208  20  ARG   A CZ  
113  N NH1 . ARG   A 14  ? 0.2838 0.1596 0.3658 0.0051  0.0568  0.0099  20  ARG   A NH1 
114  N NH2 . ARG   A 14  ? 0.3256 0.2129 0.4241 0.0080  0.0504  0.0246  20  ARG   A NH2 
115  N N   . HIS   A 15  ? 0.2681 0.1447 0.2579 -0.0067 0.0311  -0.0147 21  HIS   A N   
116  C CA  . HIS   A 15  ? 0.2857 0.1501 0.2706 -0.0158 0.0427  -0.0271 21  HIS   A CA  
117  C C   . HIS   A 15  ? 0.3030 0.1669 0.2615 -0.0262 0.0354  -0.0355 21  HIS   A C   
118  O O   . HIS   A 15  ? 0.3321 0.1879 0.2815 -0.0377 0.0438  -0.0466 21  HIS   A O   
119  C CB  . HIS   A 15  ? 0.3051 0.1630 0.3002 -0.0156 0.0550  -0.0289 21  HIS   A CB  
120  C CG  . HIS   A 15  ? 0.3185 0.1794 0.2978 -0.0162 0.0484  -0.0285 21  HIS   A CG  
121  N ND1 . HIS   A 15  ? 0.3245 0.1949 0.3094 -0.0077 0.0404  -0.0172 21  HIS   A ND1 
122  C CD2 . HIS   A 15  ? 0.3347 0.1903 0.2939 -0.0259 0.0500  -0.0380 21  HIS   A CD2 
123  C CE1 . HIS   A 15  ? 0.3404 0.2100 0.3097 -0.0109 0.0376  -0.0204 21  HIS   A CE1 
124  N NE2 . HIS   A 15  ? 0.3427 0.2037 0.2965 -0.0217 0.0429  -0.0323 21  HIS   A NE2 
125  N N   . LEU   A 16  ? 0.2940 0.1670 0.2412 -0.0238 0.0206  -0.0298 22  LEU   A N   
126  C CA  . LEU   A 16  ? 0.2946 0.1702 0.2221 -0.0330 0.0113  -0.0329 22  LEU   A CA  
127  C C   . LEU   A 16  ? 0.2953 0.1783 0.2247 -0.0321 0.0014  -0.0292 22  LEU   A C   
128  O O   . LEU   A 16  ? 0.3107 0.1988 0.2293 -0.0390 -0.0082 -0.0281 22  LEU   A O   
129  C CB  . LEU   A 16  ? 0.3020 0.1817 0.2196 -0.0317 0.0030  -0.0285 22  LEU   A CB  
130  C CG  . LEU   A 16  ? 0.3334 0.2067 0.2465 -0.0346 0.0115  -0.0327 22  LEU   A CG  
131  C CD1 . LEU   A 16  ? 0.3440 0.2221 0.2477 -0.0329 0.0019  -0.0273 22  LEU   A CD1 
132  C CD2 . LEU   A 16  ? 0.3533 0.2182 0.2530 -0.0505 0.0216  -0.0449 22  LEU   A CD2 
133  N N   . ALA   A 17  ? 0.2783 0.1628 0.2229 -0.0246 0.0038  -0.0260 23  ALA   A N   
134  C CA  . ALA   A 17  ? 0.2763 0.1673 0.2247 -0.0235 -0.0036 -0.0232 23  ALA   A CA  
135  C C   . ALA   A 17  ? 0.2822 0.1716 0.2217 -0.0354 -0.0037 -0.0296 23  ALA   A C   
136  O O   . ALA   A 17  ? 0.2889 0.1700 0.2252 -0.0430 0.0069  -0.0378 23  ALA   A O   
137  C CB  . ALA   A 17  ? 0.2695 0.1615 0.2341 -0.0158 0.0010  -0.0195 23  ALA   A CB  
138  N N   . THR   A 18  ? 0.2729 0.1709 0.2099 -0.0382 -0.0151 -0.0257 24  THR   A N   
139  C CA  . THR   A 18  ? 0.2623 0.1626 0.1907 -0.0514 -0.0179 -0.0293 24  THR   A CA  
140  C C   . THR   A 18  ? 0.2633 0.1636 0.2033 -0.0491 -0.0143 -0.0310 24  THR   A C   
141  O O   . THR   A 18  ? 0.2522 0.1525 0.2061 -0.0376 -0.0119 -0.0276 24  THR   A O   
142  C CB  . THR   A 18  ? 0.2799 0.1924 0.2066 -0.0545 -0.0334 -0.0202 24  THR   A CB  
143  O OG1 . THR   A 18  ? 0.2748 0.1932 0.2195 -0.0428 -0.0382 -0.0135 24  THR   A OG1 
144  C CG2 . THR   A 18  ? 0.2981 0.2118 0.2149 -0.0568 -0.0385 -0.0164 24  THR   A CG2 
145  N N   . HIS   A 19  ? 0.2842 0.1863 0.2174 -0.0616 -0.0152 -0.0352 25  HIS   A N   
146  C CA  . HIS   A 19  ? 0.3046 0.2080 0.2486 -0.0603 -0.0133 -0.0362 25  HIS   A CA  
147  C C   . HIS   A 19  ? 0.2915 0.2052 0.2498 -0.0495 -0.0235 -0.0264 25  HIS   A C   
148  O O   . HIS   A 19  ? 0.2873 0.2000 0.2579 -0.0414 -0.0195 -0.0257 25  HIS   A O   
149  C CB  . HIS   A 19  ? 0.3532 0.2593 0.2858 -0.0777 -0.0145 -0.0417 25  HIS   A CB  
150  C CG  . HIS   A 19  ? 0.4403 0.3511 0.3841 -0.0767 -0.0164 -0.0404 25  HIS   A CG  
151  N ND1 . HIS   A 19  ? 0.4789 0.3802 0.4297 -0.0758 -0.0036 -0.0478 25  HIS   A ND1 
152  C CD2 . HIS   A 19  ? 0.4671 0.3910 0.4191 -0.0758 -0.0289 -0.0320 25  HIS   A CD2 
153  C CE1 . HIS   A 19  ? 0.4819 0.3908 0.4412 -0.0754 -0.0092 -0.0444 25  HIS   A CE1 
154  N NE2 . HIS   A 19  ? 0.4805 0.4032 0.4415 -0.0752 -0.0241 -0.0351 25  HIS   A NE2 
155  N N   . ASN   A 20  ? 0.2835 0.2067 0.2419 -0.0499 -0.0355 -0.0187 26  ASN   A N   
156  C CA  . ASN   A 20  ? 0.2884 0.2199 0.2643 -0.0405 -0.0421 -0.0110 26  ASN   A CA  
157  C C   . ASN   A 20  ? 0.2697 0.1967 0.2533 -0.0277 -0.0356 -0.0112 26  ASN   A C   
158  O O   . ASN   A 20  ? 0.2809 0.2106 0.2768 -0.0218 -0.0339 -0.0102 26  ASN   A O   
159  C CB  . ASN   A 20  ? 0.3207 0.2623 0.3009 -0.0430 -0.0543 -0.0014 26  ASN   A CB  
160  C CG  . ASN   A 20  ? 0.3952 0.3445 0.3989 -0.0346 -0.0583 0.0054  26  ASN   A CG  
161  O OD1 . ASN   A 20  ? 0.4188 0.3748 0.4339 -0.0367 -0.0609 0.0074  26  ASN   A OD1 
162  N ND2 . ASN   A 20  ? 0.4007 0.3491 0.4136 -0.0255 -0.0574 0.0082  26  ASN   A ND2 
163  N N   . ASP   A 21  ? 0.2628 0.1836 0.2382 -0.0251 -0.0316 -0.0126 27  ASP   A N   
164  C CA  . ASP   A 21  ? 0.2427 0.1613 0.2235 -0.0158 -0.0261 -0.0118 27  ASP   A CA  
165  C C   . ASP   A 21  ? 0.2405 0.1567 0.2277 -0.0137 -0.0185 -0.0135 27  ASP   A C   
166  O O   . ASP   A 21  ? 0.2427 0.1631 0.2381 -0.0090 -0.0174 -0.0110 27  ASP   A O   
167  C CB  . ASP   A 21  ? 0.2430 0.1562 0.2148 -0.0147 -0.0230 -0.0124 27  ASP   A CB  
168  C CG  . ASP   A 21  ? 0.2658 0.1819 0.2333 -0.0149 -0.0301 -0.0091 27  ASP   A CG  
169  O OD1 . ASP   A 21  ? 0.2729 0.1945 0.2498 -0.0113 -0.0347 -0.0052 27  ASP   A OD1 
170  O OD2 . ASP   A 21  ? 0.2796 0.1916 0.2357 -0.0191 -0.0297 -0.0106 27  ASP   A OD2 
171  N N   . TRP   A 22  ? 0.2344 0.1437 0.2183 -0.0186 -0.0121 -0.0179 28  TRP   A N   
172  C CA  . TRP   A 22  ? 0.2383 0.1445 0.2317 -0.0169 -0.0043 -0.0182 28  TRP   A CA  
173  C C   . TRP   A 22  ? 0.2429 0.1549 0.2430 -0.0176 -0.0075 -0.0178 28  TRP   A C   
174  O O   . TRP   A 22  ? 0.2529 0.1668 0.2620 -0.0140 -0.0042 -0.0147 28  TRP   A O   
175  C CB  . TRP   A 22  ? 0.2527 0.1486 0.2441 -0.0232 0.0053  -0.0247 28  TRP   A CB  
176  C CG  . TRP   A 22  ? 0.2653 0.1545 0.2587 -0.0205 0.0131  -0.0243 28  TRP   A CG  
177  C CD1 . TRP   A 22  ? 0.2739 0.1578 0.2569 -0.0254 0.0155  -0.0293 28  TRP   A CD1 
178  C CD2 . TRP   A 22  ? 0.2613 0.1503 0.2699 -0.0130 0.0187  -0.0168 28  TRP   A CD2 
179  N NE1 . TRP   A 22  ? 0.2687 0.1474 0.2614 -0.0205 0.0242  -0.0269 28  TRP   A NE1 
180  C CE2 . TRP   A 22  ? 0.2593 0.1424 0.2686 -0.0125 0.0250  -0.0177 28  TRP   A CE2 
181  C CE3 . TRP   A 22  ? 0.2564 0.1511 0.2787 -0.0079 0.0189  -0.0083 28  TRP   A CE3 
182  C CZ2 . TRP   A 22  ? 0.2572 0.1405 0.2838 -0.0063 0.0310  -0.0091 28  TRP   A CZ2 
183  C CZ3 . TRP   A 22  ? 0.2644 0.1607 0.3009 -0.0030 0.0232  0.0013  28  TRP   A CZ3 
184  C CH2 . TRP   A 22  ? 0.2540 0.1448 0.2948 -0.0018 0.0293  0.0015  28  TRP   A CH2 
185  N N   . ALA   A 23  ? 0.2318 0.1481 0.2285 -0.0232 -0.0144 -0.0195 29  ALA   A N   
186  C CA  . ALA   A 23  ? 0.2335 0.1563 0.2391 -0.0241 -0.0177 -0.0187 29  ALA   A CA  
187  C C   . ALA   A 23  ? 0.2265 0.1567 0.2425 -0.0171 -0.0206 -0.0144 29  ALA   A C   
188  O O   . ALA   A 23  ? 0.2173 0.1523 0.2431 -0.0169 -0.0206 -0.0142 29  ALA   A O   
189  C CB  . ALA   A 23  ? 0.2447 0.1725 0.2462 -0.0333 -0.0253 -0.0193 29  ALA   A CB  
190  N N   . ASN   A 24  ? 0.2195 0.1501 0.2334 -0.0127 -0.0217 -0.0122 30  ASN   A N   
191  C CA  . ASN   A 24  ? 0.2197 0.1556 0.2420 -0.0082 -0.0215 -0.0105 30  ASN   A CA  
192  C C   . ASN   A 24  ? 0.2268 0.1611 0.2431 -0.0053 -0.0169 -0.0096 30  ASN   A C   
193  O O   . ASN   A 24  ? 0.2274 0.1638 0.2442 -0.0034 -0.0168 -0.0094 30  ASN   A O   
194  C CB  . ASN   A 24  ? 0.2245 0.1642 0.2534 -0.0076 -0.0279 -0.0081 30  ASN   A CB  
195  C CG  . ASN   A 24  ? 0.2958 0.2412 0.3351 -0.0113 -0.0338 -0.0058 30  ASN   A CG  
196  O OD1 . ASN   A 24  ? 0.3386 0.2889 0.3930 -0.0101 -0.0323 -0.0058 30  ASN   A OD1 
197  N ND2 . ASN   A 24  ? 0.2856 0.2314 0.3162 -0.0177 -0.0402 -0.0039 30  ASN   A ND2 
198  N N   . LEU   A 25  ? 0.2323 0.1636 0.2454 -0.0057 -0.0125 -0.0082 31  LEU   A N   
199  C CA  . LEU   A 25  ? 0.2368 0.1688 0.2466 -0.0041 -0.0094 -0.0040 31  LEU   A CA  
200  C C   . LEU   A 25  ? 0.2432 0.1834 0.2542 -0.0056 -0.0076 -0.0022 31  LEU   A C   
201  O O   . LEU   A 25  ? 0.2353 0.1793 0.2512 -0.0080 -0.0055 -0.0026 31  LEU   A O   
202  C CB  . LEU   A 25  ? 0.2315 0.1594 0.2450 -0.0044 -0.0046 -0.0005 31  LEU   A CB  
203  C CG  . LEU   A 25  ? 0.2628 0.1926 0.2778 -0.0028 -0.0021 0.0072  31  LEU   A CG  
204  C CD1 . LEU   A 25  ? 0.2710 0.1969 0.2790 -0.0011 -0.0034 0.0056  31  LEU   A CD1 
205  C CD2 . LEU   A 25  ? 0.2874 0.2139 0.3142 -0.0024 0.0037  0.0128  31  LEU   A CD2 
206  N N   . VAL   A 26  ? 0.2228 0.1658 0.2279 -0.0060 -0.0075 -0.0004 32  VAL   A N   
207  C CA  . VAL   A 26  ? 0.2216 0.1732 0.2237 -0.0111 -0.0048 0.0008  32  VAL   A CA  
208  C C   . VAL   A 26  ? 0.2233 0.1805 0.2228 -0.0134 -0.0049 0.0111  32  VAL   A C   
209  O O   . VAL   A 26  ? 0.2176 0.1834 0.2175 -0.0192 -0.0037 0.0167  32  VAL   A O   
210  C CB  . VAL   A 26  ? 0.2237 0.1760 0.2220 -0.0123 -0.0037 -0.0047 32  VAL   A CB  
211  C CG1 . VAL   A 26  ? 0.2425 0.2040 0.2336 -0.0213 0.0007  -0.0047 32  VAL   A CG1 
212  C CG2 . VAL   A 26  ? 0.2206 0.1692 0.2289 -0.0098 -0.0032 -0.0117 32  VAL   A CG2 
213  N N   . TRP   A 27  ? 0.2143 0.1676 0.2129 -0.0096 -0.0065 0.0147  33  TRP   A N   
214  C CA  . TRP   A 27  ? 0.2252 0.1847 0.2265 -0.0109 -0.0069 0.0264  33  TRP   A CA  
215  C C   . TRP   A 27  ? 0.2212 0.1723 0.2264 -0.0049 -0.0064 0.0275  33  TRP   A C   
216  O O   . TRP   A 27  ? 0.2239 0.1678 0.2224 -0.0023 -0.0073 0.0196  33  TRP   A O   
217  C CB  . TRP   A 27  ? 0.2375 0.2083 0.2288 -0.0183 -0.0082 0.0289  33  TRP   A CB  
218  C CG  . TRP   A 27  ? 0.2546 0.2347 0.2488 -0.0208 -0.0106 0.0428  33  TRP   A CG  
219  C CD1 . TRP   A 27  ? 0.2776 0.2707 0.2787 -0.0267 -0.0124 0.0575  33  TRP   A CD1 
220  C CD2 . TRP   A 27  ? 0.2588 0.2384 0.2503 -0.0187 -0.0120 0.0447  33  TRP   A CD2 
221  N NE1 . TRP   A 27  ? 0.2803 0.2817 0.2857 -0.0280 -0.0154 0.0699  33  TRP   A NE1 
222  C CE2 . TRP   A 27  ? 0.2664 0.2591 0.2658 -0.0228 -0.0147 0.0614  33  TRP   A CE2 
223  C CE3 . TRP   A 27  ? 0.2664 0.2364 0.2515 -0.0139 -0.0117 0.0355  33  TRP   A CE3 
224  C CZ2 . TRP   A 27  ? 0.2708 0.2671 0.2717 -0.0221 -0.0166 0.0679  33  TRP   A CZ2 
225  C CZ3 . TRP   A 27  ? 0.2803 0.2527 0.2650 -0.0132 -0.0131 0.0410  33  TRP   A CZ3 
226  C CH2 . TRP   A 27  ? 0.2795 0.2649 0.2722 -0.0171 -0.0153 0.0565  33  TRP   A CH2 
227  N N   . GLU   A 28  ? 0.2201 0.1723 0.2382 -0.0034 -0.0041 0.0379  34  GLU   A N   
228  C CA  . GLU   A 28  ? 0.2162 0.1600 0.2406 0.0013  -0.0008 0.0381  34  GLU   A CA  
229  C C   . GLU   A 28  ? 0.2229 0.1751 0.2639 0.0015  0.0003  0.0541  34  GLU   A C   
230  O O   . GLU   A 28  ? 0.2313 0.1931 0.2835 -0.0013 -0.0006 0.0661  34  GLU   A O   
231  C CB  . GLU   A 28  ? 0.2422 0.1722 0.2716 0.0038  0.0049  0.0295  34  GLU   A CB  
232  C CG  . GLU   A 28  ? 0.2773 0.2061 0.3217 0.0035  0.0094  0.0338  34  GLU   A CG  
233  C CD  . GLU   A 28  ? 0.3167 0.2446 0.3854 0.0060  0.0165  0.0453  34  GLU   A CD  
234  O OE1 . GLU   A 28  ? 0.3122 0.2435 0.3959 0.0054  0.0185  0.0537  34  GLU   A OE1 
235  O OE2 . GLU   A 28  ? 0.3109 0.2350 0.3863 0.0084  0.0204  0.0468  34  GLU   A OE2 
236  N N   . ASP   A 29  ? 0.2217 0.1715 0.2661 0.0042  0.0019  0.0559  35  ASP   A N   
237  C CA  . ASP   A 29  ? 0.2440 0.2025 0.3092 0.0049  0.0031  0.0729  35  ASP   A CA  
238  C C   . ASP   A 29  ? 0.2565 0.2034 0.3327 0.0102  0.0110  0.0692  35  ASP   A C   
239  O O   . ASP   A 29  ? 0.2688 0.2131 0.3313 0.0103  0.0094  0.0626  35  ASP   A O   
240  C CB  . ASP   A 29  ? 0.2644 0.2408 0.3200 -0.0015 -0.0054 0.0827  35  ASP   A CB  
241  C CG  . ASP   A 29  ? 0.2979 0.2891 0.3761 -0.0030 -0.0073 0.1047  35  ASP   A CG  
242  O OD1 . ASP   A 29  ? 0.3078 0.2926 0.4087 0.0034  -0.0007 0.1095  35  ASP   A OD1 
243  O OD2 . ASP   A 29  ? 0.3181 0.3281 0.3917 -0.0119 -0.0149 0.1172  35  ASP   A OD2 
244  N N   . SER   A 30  ? 0.2600 0.1988 0.3614 0.0136  0.0210  0.0724  36  SER   A N   
245  C CA  . SER   A 30  ? 0.2773 0.2032 0.3916 0.0170  0.0323  0.0667  36  SER   A CA  
246  C C   . SER   A 30  ? 0.2807 0.2158 0.4074 0.0187  0.0310  0.0789  36  SER   A C   
247  O O   . SER   A 30  ? 0.2881 0.2148 0.4078 0.0196  0.0355  0.0694  36  SER   A O   
248  C CB  . SER   A 30  ? 0.3042 0.2197 0.4476 0.0192  0.0458  0.0679  36  SER   A CB  
249  O OG  . SER   A 30  ? 0.3377 0.2401 0.4958 0.0209  0.0597  0.0610  36  SER   A OG  
250  N N   . SER   A 31  ? 0.2687 0.2225 0.4117 0.0178  0.0240  0.1004  37  SER   A N   
251  C CA  . SER   A 31  ? 0.2618 0.2274 0.4177 0.0181  0.0213  0.1143  37  SER   A CA  
252  C C   . SER   A 31  ? 0.2571 0.2255 0.3801 0.0148  0.0134  0.1047  37  SER   A C   
253  O O   . SER   A 31  ? 0.2716 0.2423 0.4010 0.0160  0.0146  0.1083  37  SER   A O   
254  C CB  . SER   A 31  ? 0.2917 0.2802 0.4710 0.0150  0.0135  0.1417  37  SER   A CB  
255  O OG  . SER   A 31  ? 0.3465 0.3515 0.4989 0.0061  -0.0002 0.1455  37  SER   A OG  
256  N N   . ARG   A 32  ? 0.2401 0.2069 0.3310 0.0109  0.0067  0.0919  38  ARG   A N   
257  C CA  . ARG   A 32  ? 0.2244 0.1919 0.2875 0.0080  0.0010  0.0821  38  ARG   A CA  
258  C C   . ARG   A 32  ? 0.2268 0.1753 0.2728 0.0108  0.0057  0.0619  38  ARG   A C   
259  O O   . ARG   A 32  ? 0.2396 0.1872 0.2657 0.0091  0.0016  0.0544  38  ARG   A O   
260  C CB  . ARG   A 32  ? 0.2290 0.2076 0.2710 0.0006  -0.0079 0.0815  38  ARG   A CB  
261  C CG  . ARG   A 32  ? 0.2440 0.2446 0.2944 -0.0069 -0.0145 0.1010  38  ARG   A CG  
262  C CD  . ARG   A 32  ? 0.2724 0.2817 0.2994 -0.0167 -0.0201 0.0962  38  ARG   A CD  
263  N NE  . ARG   A 32  ? 0.2448 0.2534 0.2491 -0.0208 -0.0219 0.0852  38  ARG   A NE  
264  C CZ  . ARG   A 32  ? 0.2554 0.2767 0.2424 -0.0328 -0.0256 0.0848  38  ARG   A CZ  
265  N NH1 . ARG   A 32  ? 0.2634 0.3003 0.2502 -0.0431 -0.0290 0.0951  38  ARG   A NH1 
266  N NH2 . ARG   A 32  ? 0.2553 0.2737 0.2249 -0.0361 -0.0250 0.0738  38  ARG   A NH2 
267  N N   . ASP   A 33  ? 0.2014 0.1360 0.2547 0.0133  0.0140  0.0537  39  ASP   A N   
268  C CA  . ASP   A 33  ? 0.2183 0.1378 0.2542 0.0126  0.0172  0.0363  39  ASP   A CA  
269  C C   . ASP   A 33  ? 0.2233 0.1448 0.2355 0.0100  0.0080  0.0291  39  ASP   A C   
270  O O   . ASP   A 33  ? 0.2259 0.1409 0.2215 0.0085  0.0061  0.0195  39  ASP   A O   
271  C CB  . ASP   A 33  ? 0.2445 0.1570 0.2769 0.0127  0.0221  0.0309  39  ASP   A CB  
272  C CG  . ASP   A 33  ? 0.2756 0.1746 0.2892 0.0088  0.0250  0.0147  39  ASP   A CG  
273  O OD1 . ASP   A 33  ? 0.2728 0.1638 0.2875 0.0063  0.0302  0.0077  39  ASP   A OD1 
274  O OD2 . ASP   A 33  ? 0.2800 0.1775 0.2769 0.0069  0.0213  0.0099  39  ASP   A OD2 
275  N N   . LEU   A 34  ? 0.2137 0.1441 0.2262 0.0087  0.0030  0.0341  40  LEU   A N   
276  C CA  . LEU   A 34  ? 0.2185 0.1505 0.2141 0.0063  -0.0033 0.0271  40  LEU   A CA  
277  C C   . LEU   A 34  ? 0.2223 0.1518 0.2200 0.0057  -0.0028 0.0234  40  LEU   A C   
278  O O   . LEU   A 34  ? 0.2227 0.1550 0.2337 0.0059  0.0001  0.0300  40  LEU   A O   
279  C CB  . LEU   A 34  ? 0.2177 0.1634 0.2082 0.0024  -0.0084 0.0334  40  LEU   A CB  
280  C CG  . LEU   A 34  ? 0.2204 0.1696 0.2035 0.0012  -0.0104 0.0347  40  LEU   A CG  
281  C CD1 . LEU   A 34  ? 0.2061 0.1684 0.1815 -0.0057 -0.0140 0.0384  40  LEU   A CD1 
282  C CD2 . LEU   A 34  ? 0.2267 0.1649 0.1975 0.0031  -0.0109 0.0233  40  LEU   A CD2 
283  N N   . LEU   A 35  ? 0.2067 0.1320 0.1933 0.0047  -0.0060 0.0143  41  LEU   A N   
284  C CA  . LEU   A 35  ? 0.2097 0.1345 0.1981 0.0036  -0.0066 0.0108  41  LEU   A CA  
285  C C   . LEU   A 35  ? 0.2109 0.1384 0.1915 0.0025  -0.0115 0.0061  41  LEU   A C   
286  O O   . LEU   A 35  ? 0.2150 0.1397 0.1890 0.0029  -0.0141 0.0029  41  LEU   A O   
287  C CB  . LEU   A 35  ? 0.2205 0.1351 0.2096 0.0027  -0.0033 0.0045  41  LEU   A CB  
288  C CG  . LEU   A 35  ? 0.2129 0.1275 0.2045 0.0010  -0.0041 0.0013  41  LEU   A CG  
289  C CD1 . LEU   A 35  ? 0.2090 0.1155 0.2067 -0.0011 0.0029  -0.0019 41  LEU   A CD1 
290  C CD2 . LEU   A 35  ? 0.2195 0.1343 0.2029 -0.0010 -0.0107 -0.0041 41  LEU   A CD2 
291  N N   . VAL   A 36  ? 0.1894 0.1226 0.1732 0.0008  -0.0116 0.0061  42  VAL   A N   
292  C CA  . VAL   A 36  ? 0.1923 0.1275 0.1749 -0.0004 -0.0131 0.0010  42  VAL   A CA  
293  C C   . VAL   A 36  ? 0.2041 0.1381 0.1935 -0.0004 -0.0136 -0.0022 42  VAL   A C   
294  O O   . VAL   A 36  ? 0.2301 0.1663 0.2235 -0.0017 -0.0115 -0.0003 42  VAL   A O   
295  C CB  . VAL   A 36  ? 0.2144 0.1582 0.1946 -0.0051 -0.0105 0.0018  42  VAL   A CB  
296  C CG1 . VAL   A 36  ? 0.2316 0.1753 0.2151 -0.0068 -0.0083 -0.0056 42  VAL   A CG1 
297  C CG2 . VAL   A 36  ? 0.2269 0.1738 0.1999 -0.0066 -0.0109 0.0057  42  VAL   A CG2 
298  N N   . SER   A 37  ? 0.1906 0.1221 0.1831 0.0005  -0.0169 -0.0055 43  SER   A N   
299  C CA  . SER   A 37  ? 0.2098 0.1422 0.2112 -0.0001 -0.0183 -0.0072 43  SER   A CA  
300  C C   . SER   A 37  ? 0.2222 0.1579 0.2352 0.0003  -0.0173 -0.0096 43  SER   A C   
301  O O   . SER   A 37  ? 0.2290 0.1644 0.2422 0.0008  -0.0154 -0.0107 43  SER   A O   
302  C CB  . SER   A 37  ? 0.2407 0.1694 0.2398 -0.0015 -0.0232 -0.0068 43  SER   A CB  
303  O OG  . SER   A 37  ? 0.2332 0.1612 0.2307 -0.0015 -0.0283 -0.0052 43  SER   A OG  
304  N N   . SER   A 38  ? 0.2305 0.1691 0.2556 -0.0003 -0.0168 -0.0108 44  SER   A N   
305  C CA  . SER   A 38  ? 0.2400 0.1810 0.2822 0.0003  -0.0134 -0.0132 44  SER   A CA  
306  C C   . SER   A 38  ? 0.2616 0.2032 0.3182 0.0026  -0.0202 -0.0081 44  SER   A C   
307  O O   . SER   A 38  ? 0.2708 0.2132 0.3235 0.0013  -0.0285 -0.0033 44  SER   A O   
308  C CB  . SER   A 38  ? 0.2509 0.1957 0.3024 -0.0018 -0.0084 -0.0164 44  SER   A CB  
309  O OG  . SER   A 38  ? 0.2703 0.2159 0.3224 -0.0019 -0.0144 -0.0132 44  SER   A OG  
310  N N   . THR   A 39  ? 0.2626 0.2044 0.3371 0.0044  -0.0162 -0.0086 45  THR   A N   
311  C CA  . THR   A 39  ? 0.2882 0.2325 0.3826 0.0066  -0.0229 -0.0005 45  THR   A CA  
312  C C   . THR   A 39  ? 0.3109 0.2589 0.4377 0.0082  -0.0173 -0.0003 45  THR   A C   
313  O O   . THR   A 39  ? 0.3109 0.2570 0.4431 0.0073  -0.0049 -0.0096 45  THR   A O   
314  C CB  . THR   A 39  ? 0.2901 0.2305 0.3831 0.0083  -0.0232 0.0016  45  THR   A CB  
315  O OG1 . THR   A 39  ? 0.2906 0.2275 0.3938 0.0089  -0.0107 -0.0061 45  THR   A OG1 
316  C CG2 . THR   A 39  ? 0.3065 0.2431 0.3701 0.0067  -0.0271 0.0009  45  THR   A CG2 
317  N N   . THR   A 40  ? 0.3259 0.2800 0.4760 0.0095  -0.0257 0.0110  46  THR   A N   
318  C CA  . THR   A 40  ? 0.3457 0.3039 0.5342 0.0120  -0.0199 0.0134  46  THR   A CA  
319  C C   . THR   A 40  ? 0.3469 0.3003 0.5588 0.0156  -0.0108 0.0130  46  THR   A C   
320  O O   . THR   A 40  ? 0.3432 0.2930 0.5754 0.0163  0.0047  0.0039  46  THR   A O   
321  C CB  . THR   A 40  ? 0.3812 0.3507 0.5884 0.0108  -0.0326 0.0272  46  THR   A CB  
322  O OG1 . THR   A 40  ? 0.4131 0.3869 0.6070 0.0075  -0.0477 0.0387  46  THR   A OG1 
323  C CG2 . THR   A 40  ? 0.3939 0.3665 0.5890 0.0073  -0.0335 0.0225  46  THR   A CG2 
324  N N   . ALA   A 41  ? 0.3518 0.3040 0.5592 0.0166  -0.0186 0.0210  47  ALA   A N   
325  C CA  . ALA   A 41  ? 0.3566 0.3032 0.5865 0.0198  -0.0095 0.0207  47  ALA   A CA  
326  C C   . ALA   A 41  ? 0.3788 0.3155 0.5809 0.0176  0.0012  0.0060  47  ALA   A C   
327  O O   . ALA   A 41  ? 0.3897 0.3253 0.5546 0.0149  -0.0043 0.0025  47  ALA   A O   
328  C CB  . ALA   A 41  ? 0.3552 0.3066 0.5974 0.0212  -0.0231 0.0384  47  ALA   A CB  
329  N N   . GLN   A 42  ? 0.3713 0.3012 0.5936 0.0180  0.0172  -0.0021 48  GLN   A N   
330  C CA  . GLN   A 42  ? 0.3860 0.3082 0.5827 0.0135  0.0276  -0.0157 48  GLN   A CA  
331  C C   . GLN   A 42  ? 0.3728 0.2923 0.5556 0.0152  0.0186  -0.0086 48  GLN   A C   
332  O O   . GLN   A 42  ? 0.3790 0.3005 0.5835 0.0196  0.0103  0.0051  48  GLN   A O   
333  C CB  . GLN   A 42  ? 0.4240 0.3394 0.6445 0.0102  0.0498  -0.0293 48  GLN   A CB  
334  C CG  . GLN   A 42  ? 0.5169 0.4338 0.7376 0.0045  0.0621  -0.0418 48  GLN   A CG  
335  C CD  . GLN   A 42  ? 0.6471 0.5583 0.8519 -0.0064 0.0809  -0.0606 48  GLN   A CD  
336  O OE1 . GLN   A 42  ? 0.6807 0.5841 0.9041 -0.0088 0.0959  -0.0683 48  GLN   A OE1 
337  N NE2 . GLN   A 42  ? 0.6775 0.5932 0.8479 -0.0147 0.0808  -0.0680 48  GLN   A NE2 
338  N N   . GLY   A 43  ? 0.3488 0.2654 0.4968 0.0109  0.0198  -0.0166 49  GLY   A N   
339  C CA  . GLY   A 43  ? 0.3334 0.2475 0.4647 0.0118  0.0122  -0.0114 49  GLY   A CA  
340  C C   . GLY   A 43  ? 0.3010 0.2076 0.4379 0.0095  0.0248  -0.0192 49  GLY   A C   
341  O O   . GLY   A 43  ? 0.2891 0.1921 0.4347 0.0046  0.0414  -0.0320 49  GLY   A O   
342  N N   . CYS   A 44  ? 0.2902 0.1944 0.4213 0.0115  0.0178  -0.0122 50  CYS   A N   
343  C CA  . CYS   A 44  ? 0.2888 0.1855 0.4270 0.0098  0.0282  -0.0174 50  CYS   A CA  
344  C C   . CYS   A 44  ? 0.2793 0.1745 0.3820 0.0035  0.0308  -0.0265 50  CYS   A C   
345  O O   . CYS   A 44  ? 0.2630 0.1521 0.3692 -0.0002 0.0416  -0.0336 50  CYS   A O   
346  C CB  . CYS   A 44  ? 0.3011 0.1966 0.4602 0.0155  0.0192  -0.0021 50  CYS   A CB  
347  S SG  . CYS   A 44  ? 0.3592 0.2583 0.5710 0.0218  0.0176  0.0120  50  CYS   A SG  
348  N N   . ASP   A 45  ? 0.2734 0.1744 0.3452 0.0025  0.0201  -0.0241 51  ASP   A N   
349  C CA  . ASP   A 45  ? 0.2826 0.1846 0.3251 -0.0029 0.0205  -0.0289 51  ASP   A CA  
350  C C   . ASP   A 45  ? 0.3032 0.2076 0.3360 -0.0129 0.0335  -0.0419 51  ASP   A C   
351  O O   . ASP   A 45  ? 0.3155 0.2226 0.3544 -0.0152 0.0383  -0.0462 51  ASP   A O   
352  C CB  . ASP   A 45  ? 0.2809 0.1881 0.3001 -0.0008 0.0070  -0.0214 51  ASP   A CB  
353  C CG  . ASP   A 45  ? 0.2986 0.2043 0.3207 0.0050  -0.0050 -0.0102 51  ASP   A CG  
354  O OD1 . ASP   A 45  ? 0.2882 0.1894 0.3198 0.0063  -0.0048 -0.0070 51  ASP   A OD1 
355  O OD2 . ASP   A 45  ? 0.3130 0.2219 0.3274 0.0067  -0.0140 -0.0047 51  ASP   A OD2 
356  N N   . THR   A 46  ? 0.3202 0.2247 0.3367 -0.0205 0.0387  -0.0478 52  THR   A N   
357  C CA  . THR   A 46  ? 0.3408 0.2503 0.3420 -0.0345 0.0501  -0.0594 52  THR   A CA  
358  C C   . THR   A 46  ? 0.3265 0.2462 0.2985 -0.0387 0.0402  -0.0533 52  THR   A C   
359  O O   . THR   A 46  ? 0.3353 0.2537 0.3006 -0.0345 0.0330  -0.0471 52  THR   A O   
360  C CB  . THR   A 46  ? 0.4020 0.3041 0.4112 -0.0418 0.0652  -0.0706 52  THR   A CB  
361  O OG1 . THR   A 46  ? 0.4288 0.3228 0.4691 -0.0402 0.0783  -0.0777 52  THR   A OG1 
362  C CG2 . THR   A 46  ? 0.4448 0.3538 0.4286 -0.0597 0.0739  -0.0811 52  THR   A CG2 
363  N N   . ILE   A 47  ? 0.2970 0.2273 0.2539 -0.0478 0.0404  -0.0542 53  ILE   A N   
364  C CA  . ILE   A 47  ? 0.2827 0.2243 0.2187 -0.0517 0.0311  -0.0453 53  ILE   A CA  
365  C C   . ILE   A 47  ? 0.2828 0.2313 0.2023 -0.0673 0.0374  -0.0509 53  ILE   A C   
366  O O   . ILE   A 47  ? 0.2842 0.2344 0.2000 -0.0814 0.0500  -0.0628 53  ILE   A O   
367  C CB  . ILE   A 47  ? 0.2714 0.2233 0.2020 -0.0539 0.0260  -0.0392 53  ILE   A CB  
368  C CG1 . ILE   A 47  ? 0.2609 0.2062 0.2069 -0.0406 0.0209  -0.0353 53  ILE   A CG1 
369  C CG2 . ILE   A 47  ? 0.2629 0.2273 0.1792 -0.0568 0.0162  -0.0266 53  ILE   A CG2 
370  C CD1 . ILE   A 47  ? 0.2623 0.2020 0.2118 -0.0278 0.0106  -0.0264 53  ILE   A CD1 
371  N N   . ALA   A 48  ? 0.2750 0.2282 0.1842 -0.0663 0.0294  -0.0427 54  ALA   A N   
372  C CA  . ALA   A 48  ? 0.2825 0.2449 0.1748 -0.0816 0.0328  -0.0452 54  ALA   A CA  
373  C C   . ALA   A 48  ? 0.2848 0.2661 0.1617 -0.0977 0.0310  -0.0407 54  ALA   A C   
374  O O   . ALA   A 48  ? 0.2785 0.2674 0.1572 -0.0924 0.0215  -0.0284 54  ALA   A O   
375  C CB  . ALA   A 48  ? 0.2840 0.2482 0.1725 -0.0748 0.0228  -0.0346 54  ALA   A CB  
376  N N   . ARG   A 49  ? 0.3026 0.2923 0.1642 -0.1187 0.0401  -0.0498 55  ARG   A N   
377  C CA  . ARG   A 49  ? 0.3234 0.3346 0.1673 -0.1379 0.0369  -0.0431 55  ARG   A CA  
378  C C   . ARG   A 49  ? 0.3587 0.3825 0.1849 -0.1545 0.0361  -0.0415 55  ARG   A C   
379  O O   . ARG   A 49  ? 0.3712 0.3935 0.1861 -0.1719 0.0495  -0.0574 55  ARG   A O   
380  C CB  . ARG   A 49  ? 0.3503 0.3614 0.1901 -0.1523 0.0503  -0.0576 55  ARG   A CB  
381  C CG  . ARG   A 49  ? 0.3637 0.3609 0.2242 -0.1352 0.0524  -0.0606 55  ARG   A CG  
382  C CD  . ARG   A 49  ? 0.3843 0.3896 0.2493 -0.1246 0.0378  -0.0429 55  ARG   A CD  
383  N NE  . ARG   A 49  ? 0.3597 0.3523 0.2432 -0.1099 0.0399  -0.0466 55  ARG   A NE  
384  C CZ  . ARG   A 49  ? 0.3830 0.3753 0.2762 -0.0955 0.0291  -0.0343 55  ARG   A CZ  
385  N NH1 . ARG   A 49  ? 0.3746 0.3770 0.2643 -0.0924 0.0169  -0.0178 55  ARG   A NH1 
386  N NH2 . ARG   A 49  ? 0.3856 0.3671 0.2945 -0.0842 0.0314  -0.0385 55  ARG   A NH2 
387  N N   . CYS   A 50  ? 0.3739 0.4083 0.2006 -0.1483 0.0217  -0.0231 56  CYS   A N   
388  C CA  . CYS   A 50  ? 0.3804 0.4259 0.1954 -0.1591 0.0183  -0.0183 56  CYS   A CA  
389  C C   . CYS   A 50  ? 0.3767 0.4377 0.1987 -0.1518 0.0017  0.0063  56  CYS   A C   
390  O O   . CYS   A 50  ? 0.3697 0.4303 0.2064 -0.1377 -0.0056 0.0179  56  CYS   A O   
391  C CB  . CYS   A 50  ? 0.3891 0.4135 0.2117 -0.1469 0.0253  -0.0303 56  CYS   A CB  
392  S SG  . CYS   A 50  ? 0.3751 0.3834 0.2205 -0.1153 0.0156  -0.0203 56  CYS   A SG  
393  N N   . ASP   A 51  ? 0.3813 0.4540 0.1963 -0.1601 -0.0029 0.0134  57  ASP   A N   
394  C CA  . ASP   A 51  ? 0.3848 0.4696 0.2131 -0.1507 -0.0165 0.0360  57  ASP   A CA  
395  C C   . ASP   A 51  ? 0.3828 0.4561 0.2156 -0.1397 -0.0159 0.0328  57  ASP   A C   
396  O O   . ASP   A 51  ? 0.3803 0.4677 0.2169 -0.1418 -0.0238 0.0475  57  ASP   A O   
397  C CB  . ASP   A 51  ? 0.4351 0.5525 0.2569 -0.1712 -0.0269 0.0566  57  ASP   A CB  
398  C CG  . ASP   A 51  ? 0.5619 0.6944 0.3601 -0.1974 -0.0242 0.0515  57  ASP   A CG  
399  O OD1 . ASP   A 51  ? 0.5949 0.7105 0.3823 -0.1996 -0.0123 0.0297  57  ASP   A OD1 
400  O OD2 . ASP   A 51  ? 0.5997 0.7619 0.3912 -0.2173 -0.0339 0.0697  57  ASP   A OD2 
401  N N   . CYS   A 52  ? 0.3620 0.4100 0.1972 -0.1273 -0.0068 0.0153  58  CYS   A N   
402  C CA  . CYS   A 52  ? 0.3302 0.3654 0.1704 -0.1158 -0.0063 0.0125  58  CYS   A CA  
403  C C   . CYS   A 52  ? 0.2921 0.3298 0.1488 -0.1002 -0.0159 0.0293  58  CYS   A C   
404  O O   . CYS   A 52  ? 0.2721 0.3098 0.1414 -0.0904 -0.0199 0.0376  58  CYS   A O   
405  C CB  . CYS   A 52  ? 0.3445 0.3538 0.1900 -0.1035 0.0027  -0.0042 58  CYS   A CB  
406  S SG  . CYS   A 52  ? 0.3543 0.3546 0.1880 -0.1193 0.0186  -0.0262 58  CYS   A SG  
407  N N   . GLN   A 53  ? 0.2786 0.3175 0.1360 -0.0986 -0.0180 0.0331  59  GLN   A N   
408  C CA  . GLN   A 53  ? 0.2617 0.2992 0.1358 -0.0841 -0.0234 0.0449  59  GLN   A CA  
409  C C   . GLN   A 53  ? 0.2577 0.2751 0.1317 -0.0728 -0.0192 0.0349  59  GLN   A C   
410  O O   . GLN   A 53  ? 0.2637 0.2803 0.1482 -0.0642 -0.0217 0.0425  59  GLN   A O   
411  C CB  . GLN   A 53  ? 0.2851 0.3472 0.1664 -0.0924 -0.0312 0.0644  59  GLN   A CB  
412  C CG  . GLN   A 53  ? 0.3487 0.4303 0.2388 -0.0987 -0.0376 0.0806  59  GLN   A CG  
413  C CD  . GLN   A 53  ? 0.3880 0.4944 0.2932 -0.1044 -0.0463 0.1039  59  GLN   A CD  
414  O OE1 . GLN   A 53  ? 0.3998 0.5309 0.2964 -0.1241 -0.0522 0.1144  59  GLN   A OE1 
415  N NE2 . GLN   A 53  ? 0.3846 0.4859 0.3140 -0.0888 -0.0466 0.1128  59  GLN   A NE2 
416  N N   . THR   A 54  ? 0.2440 0.2457 0.1084 -0.0736 -0.0121 0.0186  60  THR   A N   
417  C CA  . THR   A 54  ? 0.2564 0.2393 0.1226 -0.0629 -0.0092 0.0112  60  THR   A CA  
418  C C   . THR   A 54  ? 0.2541 0.2203 0.1236 -0.0559 -0.0049 0.0010  60  THR   A C   
419  O O   . THR   A 54  ? 0.2735 0.2404 0.1402 -0.0629 -0.0001 -0.0060 60  THR   A O   
420  C CB  . THR   A 54  ? 0.2920 0.2743 0.1486 -0.0714 -0.0054 0.0053  60  THR   A CB  
421  O OG1 . THR   A 54  ? 0.3495 0.3316 0.1968 -0.0843 0.0022  -0.0064 60  THR   A OG1 
422  C CG2 . THR   A 54  ? 0.2882 0.2893 0.1431 -0.0792 -0.0106 0.0168  60  THR   A CG2 
423  N N   . GLY   A 55  ? 0.2356 0.1878 0.1115 -0.0433 -0.0063 0.0008  61  GLY   A N   
424  C CA  . GLY   A 55  ? 0.2313 0.1697 0.1132 -0.0367 -0.0040 -0.0057 61  GLY   A CA  
425  C C   . GLY   A 55  ? 0.2322 0.1586 0.1178 -0.0267 -0.0071 -0.0038 61  GLY   A C   
426  O O   . GLY   A 55  ? 0.2502 0.1761 0.1318 -0.0262 -0.0085 -0.0011 61  GLY   A O   
427  N N   . VAL   A 56  ? 0.2180 0.1358 0.1105 -0.0205 -0.0083 -0.0050 62  VAL   A N   
428  C CA  . VAL   A 56  ? 0.2216 0.1298 0.1157 -0.0142 -0.0122 -0.0024 62  VAL   A CA  
429  C C   . VAL   A 56  ? 0.2120 0.1192 0.1099 -0.0096 -0.0158 0.0001  62  VAL   A C   
430  O O   . VAL   A 56  ? 0.2181 0.1267 0.1221 -0.0092 -0.0148 -0.0018 62  VAL   A O   
431  C CB  . VAL   A 56  ? 0.2472 0.1460 0.1487 -0.0139 -0.0101 -0.0051 62  VAL   A CB  
432  C CG1 . VAL   A 56  ? 0.2606 0.1526 0.1640 -0.0098 -0.0162 0.0004  62  VAL   A CG1 
433  C CG2 . VAL   A 56  ? 0.2527 0.1509 0.1509 -0.0194 -0.0049 -0.0090 62  VAL   A CG2 
434  N N   . TYR   A 57  ? 0.2114 0.1158 0.1053 -0.0072 -0.0188 0.0032  63  TYR   A N   
435  C CA  . TYR   A 57  ? 0.2080 0.1109 0.1041 -0.0048 -0.0210 0.0042  63  TYR   A CA  
436  C C   . TYR   A 57  ? 0.2204 0.1165 0.1130 -0.0055 -0.0253 0.0057  63  TYR   A C   
437  O O   . TYR   A 57  ? 0.2346 0.1276 0.1210 -0.0076 -0.0261 0.0068  63  TYR   A O   
438  C CB  . TYR   A 57  ? 0.2082 0.1154 0.1048 -0.0040 -0.0185 0.0057  63  TYR   A CB  
439  C CG  . TYR   A 57  ? 0.2290 0.1323 0.1206 -0.0050 -0.0164 0.0058  63  TYR   A CG  
440  C CD1 . TYR   A 57  ? 0.2499 0.1551 0.1389 -0.0063 -0.0143 0.0070  63  TYR   A CD1 
441  C CD2 . TYR   A 57  ? 0.2297 0.1276 0.1192 -0.0060 -0.0150 0.0037  63  TYR   A CD2 
442  C CE1 . TYR   A 57  ? 0.2485 0.1502 0.1348 -0.0076 -0.0104 0.0062  63  TYR   A CE1 
443  C CE2 . TYR   A 57  ? 0.2446 0.1383 0.1295 -0.0090 -0.0100 0.0016  63  TYR   A CE2 
444  C CZ  . TYR   A 57  ? 0.2595 0.1548 0.1435 -0.0093 -0.0076 0.0028  63  TYR   A CZ  
445  O OH  . TYR   A 57  ? 0.2859 0.1766 0.1666 -0.0127 -0.0011 -0.0003 63  TYR   A OH  
446  N N   . TYR   A 58  ? 0.2168 0.1119 0.1124 -0.0052 -0.0284 0.0064  64  TYR   A N   
447  C CA  . TYR   A 58  ? 0.2182 0.1101 0.1089 -0.0090 -0.0340 0.0096  64  TYR   A CA  
448  C C   . TYR   A 58  ? 0.2354 0.1257 0.1152 -0.0133 -0.0315 0.0067  64  TYR   A C   
449  O O   . TYR   A 58  ? 0.2299 0.1211 0.1127 -0.0120 -0.0281 0.0037  64  TYR   A O   
450  C CB  . TYR   A 58  ? 0.2219 0.1152 0.1233 -0.0085 -0.0395 0.0135  64  TYR   A CB  
451  C CG  . TYR   A 58  ? 0.2429 0.1364 0.1384 -0.0152 -0.0471 0.0197  64  TYR   A CG  
452  C CD1 . TYR   A 58  ? 0.2575 0.1500 0.1504 -0.0186 -0.0513 0.0256  64  TYR   A CD1 
453  C CD2 . TYR   A 58  ? 0.2636 0.1593 0.1547 -0.0201 -0.0504 0.0200  64  TYR   A CD2 
454  C CE1 . TYR   A 58  ? 0.2703 0.1657 0.1570 -0.0273 -0.0599 0.0337  64  TYR   A CE1 
455  C CE2 . TYR   A 58  ? 0.2792 0.1777 0.1619 -0.0298 -0.0582 0.0263  64  TYR   A CE2 
456  C CZ  . TYR   A 58  ? 0.2947 0.1939 0.1749 -0.0339 -0.0635 0.0339  64  TYR   A CZ  
457  O OH  . TYR   A 58  ? 0.3234 0.2279 0.1940 -0.0462 -0.0726 0.0422  64  TYR   A OH  
458  N N   . CYS   A 59  ? 0.2447 0.1321 0.1125 -0.0196 -0.0324 0.0072  65  CYS   A N   
459  C CA  . CYS   A 59  ? 0.2575 0.1418 0.1136 -0.0267 -0.0273 0.0021  65  CYS   A CA  
460  C C   . CYS   A 59  ? 0.2664 0.1511 0.1106 -0.0377 -0.0341 0.0047  65  CYS   A C   
461  O O   . CYS   A 59  ? 0.2781 0.1632 0.1135 -0.0440 -0.0392 0.0094  65  CYS   A O   
462  C CB  . CYS   A 59  ? 0.2721 0.1538 0.1227 -0.0278 -0.0211 -0.0006 65  CYS   A CB  
463  S SG  . CYS   A 59  ? 0.3030 0.1790 0.1413 -0.0382 -0.0108 -0.0092 65  CYS   A SG  
464  N N   . SER   A 60  ? 0.2651 0.1511 0.1091 -0.0412 -0.0351 0.0031  66  SER   A N   
465  C CA  . SER   A 60  ? 0.2914 0.1810 0.1242 -0.0538 -0.0432 0.0075  66  SER   A CA  
466  C C   . SER   A 60  ? 0.3061 0.1933 0.1171 -0.0687 -0.0394 0.0028  66  SER   A C   
467  O O   . SER   A 60  ? 0.3263 0.2188 0.1254 -0.0811 -0.0487 0.0101  66  SER   A O   
468  C CB  . SER   A 60  ? 0.3206 0.2126 0.1561 -0.0564 -0.0440 0.0054  66  SER   A CB  
469  O OG  . SER   A 60  ? 0.3584 0.2445 0.1884 -0.0597 -0.0317 -0.0064 66  SER   A OG  
470  N N   . SER   A 61  ? 0.2959 0.1758 0.1029 -0.0692 -0.0252 -0.0088 67  SER   A N   
471  C CA  . SER   A 61  ? 0.3140 0.1899 0.1011 -0.0843 -0.0175 -0.0164 67  SER   A CA  
472  C C   . SER   A 61  ? 0.3093 0.1860 0.0886 -0.0865 -0.0215 -0.0110 67  SER   A C   
473  O O   . SER   A 61  ? 0.3160 0.1904 0.0766 -0.1010 -0.0163 -0.0164 67  SER   A O   
474  C CB  . SER   A 61  ? 0.3259 0.1931 0.1180 -0.0833 0.0010  -0.0300 67  SER   A CB  
475  O OG  . SER   A 61  ? 0.3258 0.1915 0.1367 -0.0674 0.0056  -0.0284 67  SER   A OG  
476  N N   . ARG   A 62  ? 0.2952 0.1750 0.0880 -0.0739 -0.0302 -0.0010 68  ARG   A N   
477  C CA  . ARG   A 62  ? 0.3137 0.1944 0.1018 -0.0753 -0.0353 0.0058  68  ARG   A CA  
478  C C   . ARG   A 62  ? 0.3273 0.2145 0.1252 -0.0725 -0.0503 0.0209  68  ARG   A C   
479  O O   . ARG   A 62  ? 0.3307 0.2185 0.1283 -0.0731 -0.0550 0.0282  68  ARG   A O   
480  C CB  . ARG   A 62  ? 0.3280 0.2047 0.1271 -0.0627 -0.0276 0.0022  68  ARG   A CB  
481  C CG  . ARG   A 62  ? 0.3648 0.2360 0.1615 -0.0643 -0.0125 -0.0096 68  ARG   A CG  
482  C CD  . ARG   A 62  ? 0.3487 0.2170 0.1266 -0.0779 -0.0081 -0.0134 68  ARG   A CD  
483  N NE  . ARG   A 62  ? 0.3580 0.2202 0.1374 -0.0801 0.0090  -0.0254 68  ARG   A NE  
484  C CZ  . ARG   A 62  ? 0.3727 0.2302 0.1456 -0.0907 0.0204  -0.0363 68  ARG   A CZ  
485  N NH1 . ARG   A 62  ? 0.3899 0.2492 0.1502 -0.1015 0.0153  -0.0369 68  ARG   A NH1 
486  N NH2 . ARG   A 62  ? 0.3820 0.2330 0.1627 -0.0914 0.0380  -0.0467 68  ARG   A NH2 
487  N N   . ARG   A 63  ? 0.3141 0.2057 0.1250 -0.0681 -0.0566 0.0258  69  ARG   A N   
488  C CA  . ARG   A 63  ? 0.3177 0.2147 0.1466 -0.0631 -0.0680 0.0398  69  ARG   A CA  
489  C C   . ARG   A 63  ? 0.3213 0.2140 0.1648 -0.0510 -0.0651 0.0412  69  ARG   A C   
490  O O   . ARG   A 63  ? 0.3354 0.2300 0.1880 -0.0513 -0.0718 0.0523  69  ARG   A O   
491  C CB  . ARG   A 63  ? 0.3384 0.2440 0.1608 -0.0772 -0.0810 0.0543  69  ARG   A CB  
492  C CG  . ARG   A 63  ? 0.3710 0.2830 0.1799 -0.0911 -0.0850 0.0540  69  ARG   A CG  
493  C CD  . ARG   A 63  ? 0.4023 0.3271 0.2128 -0.1036 -0.1014 0.0739  69  ARG   A CD  
494  N NE  . ARG   A 63  ? 0.4453 0.3786 0.2386 -0.1212 -0.1063 0.0741  69  ARG   A NE  
495  C CZ  . ARG   A 63  ? 0.4676 0.4060 0.2316 -0.1438 -0.1084 0.0737  69  ARG   A CZ  
496  N NH1 . ARG   A 63  ? 0.4623 0.3978 0.2116 -0.1503 -0.1061 0.0732  69  ARG   A NH1 
497  N NH2 . ARG   A 63  ? 0.4745 0.4212 0.2224 -0.1616 -0.1119 0.0727  69  ARG   A NH2 
498  N N   . LYS   A 64  ? 0.3031 0.1908 0.1481 -0.0423 -0.0547 0.0302  70  LYS   A N   
499  C CA  . LYS   A 64  ? 0.2960 0.1805 0.1508 -0.0339 -0.0508 0.0296  70  LYS   A CA  
500  C C   . LYS   A 64  ? 0.2906 0.1748 0.1564 -0.0242 -0.0440 0.0225  70  LYS   A C   
501  O O   . LYS   A 64  ? 0.2880 0.1731 0.1509 -0.0234 -0.0399 0.0166  70  LYS   A O   
502  C CB  . LYS   A 64  ? 0.3354 0.2167 0.1758 -0.0376 -0.0456 0.0252  70  LYS   A CB  
503  C CG  . LYS   A 64  ? 0.4352 0.3170 0.2665 -0.0470 -0.0523 0.0338  70  LYS   A CG  
504  C CD  . LYS   A 64  ? 0.5578 0.4360 0.3773 -0.0496 -0.0463 0.0291  70  LYS   A CD  
505  C CE  . LYS   A 64  ? 0.6399 0.5192 0.4488 -0.0604 -0.0534 0.0383  70  LYS   A CE  
506  N NZ  . LYS   A 64  ? 0.6985 0.5822 0.4911 -0.0748 -0.0585 0.0409  70  LYS   A NZ  
507  N N   . HIS   A 65  ? 0.2580 0.1410 0.1360 -0.0185 -0.0419 0.0231  71  HIS   A N   
508  C CA  . HIS   A 65  ? 0.2602 0.1445 0.1454 -0.0128 -0.0352 0.0165  71  HIS   A CA  
509  C C   . HIS   A 65  ? 0.2738 0.1578 0.1516 -0.0133 -0.0300 0.0129  71  HIS   A C   
510  O O   . HIS   A 65  ? 0.2962 0.1771 0.1730 -0.0152 -0.0307 0.0154  71  HIS   A O   
511  C CB  . HIS   A 65  ? 0.2534 0.1368 0.1571 -0.0091 -0.0341 0.0176  71  HIS   A CB  
512  C CG  . HIS   A 65  ? 0.2636 0.1484 0.1800 -0.0077 -0.0386 0.0220  71  HIS   A CG  
513  N ND1 . HIS   A 65  ? 0.3065 0.1939 0.2299 -0.0046 -0.0353 0.0174  71  HIS   A ND1 
514  C CD2 . HIS   A 65  ? 0.2634 0.1491 0.1868 -0.0099 -0.0468 0.0320  71  HIS   A CD2 
515  C CE1 . HIS   A 65  ? 0.2717 0.1605 0.2071 -0.0042 -0.0409 0.0236  71  HIS   A CE1 
516  N NE2 . HIS   A 65  ? 0.2785 0.1672 0.2153 -0.0075 -0.0483 0.0333  71  HIS   A NE2 
517  N N   . TYR   A 66  ? 0.2506 0.1388 0.1256 -0.0120 -0.0252 0.0085  72  TYR   A N   
518  C CA  . TYR   A 66  ? 0.2390 0.1297 0.1093 -0.0131 -0.0209 0.0069  72  TYR   A CA  
519  C C   . TYR   A 66  ? 0.2313 0.1290 0.1071 -0.0127 -0.0175 0.0050  72  TYR   A C   
520  O O   . TYR   A 66  ? 0.2338 0.1364 0.1143 -0.0112 -0.0169 0.0048  72  TYR   A O   
521  C CB  . TYR   A 66  ? 0.2418 0.1340 0.1079 -0.0138 -0.0177 0.0061  72  TYR   A CB  
522  C CG  . TYR   A 66  ? 0.2553 0.1414 0.1111 -0.0184 -0.0184 0.0056  72  TYR   A CG  
523  C CD1 . TYR   A 66  ? 0.2681 0.1512 0.1154 -0.0224 -0.0184 0.0062  72  TYR   A CD1 
524  C CD2 . TYR   A 66  ? 0.2732 0.1572 0.1262 -0.0208 -0.0188 0.0041  72  TYR   A CD2 
525  C CE1 . TYR   A 66  ? 0.3016 0.1804 0.1367 -0.0296 -0.0188 0.0056  72  TYR   A CE1 
526  C CE2 . TYR   A 66  ? 0.2884 0.1680 0.1286 -0.0288 -0.0186 0.0026  72  TYR   A CE2 
527  C CZ  . TYR   A 66  ? 0.3097 0.1871 0.1403 -0.0337 -0.0188 0.0035  72  TYR   A CZ  
528  O OH  . TYR   A 66  ? 0.3302 0.2045 0.1455 -0.0445 -0.0183 0.0017  72  TYR   A OH  
529  N N   . PRO   A 67  ? 0.2341 0.1335 0.1075 -0.0156 -0.0151 0.0040  73  PRO   A N   
530  C CA  . PRO   A 67  ? 0.2354 0.1441 0.1102 -0.0192 -0.0119 0.0024  73  PRO   A CA  
531  C C   . PRO   A 67  ? 0.2404 0.1596 0.1157 -0.0197 -0.0119 0.0071  73  PRO   A C   
532  O O   . PRO   A 67  ? 0.2461 0.1641 0.1199 -0.0186 -0.0113 0.0093  73  PRO   A O   
533  C CB  . PRO   A 67  ? 0.2616 0.1680 0.1331 -0.0239 -0.0089 -0.0006 73  PRO   A CB  
534  C CG  . PRO   A 67  ? 0.2678 0.1660 0.1357 -0.0219 -0.0110 0.0016  73  PRO   A CG  
535  C CD  . PRO   A 67  ? 0.2339 0.1275 0.1024 -0.0176 -0.0152 0.0045  73  PRO   A CD  
536  N N   . VAL   A 68  ? 0.2225 0.1516 0.1023 -0.0213 -0.0120 0.0094  74  VAL   A N   
537  C CA  . VAL   A 68  ? 0.2322 0.1729 0.1192 -0.0212 -0.0124 0.0173  74  VAL   A CA  
538  C C   . VAL   A 68  ? 0.2314 0.1885 0.1194 -0.0290 -0.0137 0.0221  74  VAL   A C   
539  O O   . VAL   A 68  ? 0.2277 0.1859 0.1108 -0.0338 -0.0131 0.0173  74  VAL   A O   
540  C CB  . VAL   A 68  ? 0.2498 0.1877 0.1458 -0.0150 -0.0121 0.0196  74  VAL   A CB  
541  C CG1 . VAL   A 68  ? 0.2632 0.1883 0.1567 -0.0110 -0.0101 0.0159  74  VAL   A CG1 
542  C CG2 . VAL   A 68  ? 0.2479 0.1847 0.1442 -0.0145 -0.0136 0.0170  74  VAL   A CG2 
543  N N   . SER   A 69  ? 0.2268 0.1976 0.1228 -0.0313 -0.0151 0.0322  75  SER   A N   
544  C CA  . SER   A 69  ? 0.2293 0.2201 0.1297 -0.0396 -0.0185 0.0420  75  SER   A CA  
545  C C   . SER   A 69  ? 0.2157 0.2102 0.1336 -0.0331 -0.0194 0.0511  75  SER   A C   
546  O O   . SER   A 69  ? 0.1995 0.1868 0.1297 -0.0245 -0.0163 0.0530  75  SER   A O   
547  C CB  . SER   A 69  ? 0.2693 0.2756 0.1731 -0.0465 -0.0207 0.0514  75  SER   A CB  
548  O OG  . SER   A 69  ? 0.3485 0.3499 0.2364 -0.0527 -0.0187 0.0420  75  SER   A OG  
549  N N   . PHE   A 70  ? 0.1971 0.2023 0.1165 -0.0381 -0.0223 0.0561  76  PHE   A N   
550  C CA  . PHE   A 70  ? 0.2025 0.2108 0.1399 -0.0321 -0.0228 0.0650  76  PHE   A CA  
551  C C   . PHE   A 70  ? 0.2188 0.2511 0.1657 -0.0413 -0.0286 0.0817  76  PHE   A C   
552  O O   . PHE   A 70  ? 0.2389 0.2848 0.1716 -0.0549 -0.0323 0.0827  76  PHE   A O   
553  C CB  . PHE   A 70  ? 0.2111 0.2034 0.1431 -0.0260 -0.0203 0.0539  76  PHE   A CB  
554  C CG  . PHE   A 70  ? 0.2207 0.2134 0.1363 -0.0337 -0.0210 0.0453  76  PHE   A CG  
555  C CD1 . PHE   A 70  ? 0.2409 0.2212 0.1429 -0.0344 -0.0181 0.0321  76  PHE   A CD1 
556  C CD2 . PHE   A 70  ? 0.2294 0.2351 0.1454 -0.0411 -0.0234 0.0508  76  PHE   A CD2 
557  C CE1 . PHE   A 70  ? 0.2595 0.2389 0.1515 -0.0415 -0.0158 0.0234  76  PHE   A CE1 
558  C CE2 . PHE   A 70  ? 0.2433 0.2485 0.1447 -0.0498 -0.0214 0.0409  76  PHE   A CE2 
559  C CZ  . PHE   A 70  ? 0.2468 0.2381 0.1379 -0.0494 -0.0167 0.0266  76  PHE   A CZ  
560  N N   . SER   A 71  ? 0.2075 0.2461 0.1795 -0.0355 -0.0289 0.0955  77  SER   A N   
561  C CA  . SER   A 71  ? 0.2075 0.2709 0.1941 -0.0439 -0.0357 0.1160  77  SER   A CA  
562  C C   . SER   A 71  ? 0.2195 0.2867 0.1949 -0.0503 -0.0384 0.1141  77  SER   A C   
563  O O   . SER   A 71  ? 0.2310 0.2799 0.1954 -0.0445 -0.0339 0.0984  77  SER   A O   
564  C CB  . SER   A 71  ? 0.2209 0.2879 0.2446 -0.0342 -0.0334 0.1322  77  SER   A CB  
565  O OG  . SER   A 71  ? 0.2672 0.3158 0.2991 -0.0231 -0.0265 0.1241  77  SER   A OG  
566  N N   . LYS   A 72  ? 0.2279 0.3197 0.2062 -0.0635 -0.0459 0.1307  78  LYS   A N   
567  C CA  . LYS   A 72  ? 0.2462 0.3437 0.2138 -0.0717 -0.0481 0.1299  78  LYS   A CA  
568  C C   . LYS   A 72  ? 0.2632 0.3525 0.2535 -0.0590 -0.0458 0.1353  78  LYS   A C   
569  O O   . LYS   A 72  ? 0.2563 0.3453 0.2762 -0.0487 -0.0443 0.1475  78  LYS   A O   
570  C CB  . LYS   A 72  ? 0.2616 0.3909 0.2245 -0.0928 -0.0576 0.1482  78  LYS   A CB  
571  C CG  . LYS   A 72  ? 0.3197 0.4559 0.2538 -0.1095 -0.0579 0.1381  78  LYS   A CG  
572  C CD  . LYS   A 72  ? 0.3935 0.5597 0.3132 -0.1354 -0.0658 0.1507  78  LYS   A CD  
573  C CE  . LYS   A 72  ? 0.4753 0.6485 0.3666 -0.1542 -0.0643 0.1397  78  LYS   A CE  
574  N NZ  . LYS   A 72  ? 0.5290 0.7316 0.4017 -0.1833 -0.0709 0.1498  78  LYS   A NZ  
575  N N   . PRO   A 73  ? 0.2761 0.3584 0.2550 -0.0601 -0.0441 0.1260  79  PRO   A N   
576  C CA  . PRO   A 73  ? 0.2836 0.3569 0.2829 -0.0485 -0.0412 0.1295  79  PRO   A CA  
577  C C   . PRO   A 73  ? 0.2760 0.3700 0.3061 -0.0504 -0.0466 0.1570  79  PRO   A C   
578  O O   . PRO   A 73  ? 0.2670 0.3860 0.2938 -0.0658 -0.0552 0.1727  79  PRO   A O   
579  C CB  . PRO   A 73  ? 0.3077 0.3770 0.2876 -0.0542 -0.0405 0.1181  79  PRO   A CB  
580  C CG  . PRO   A 73  ? 0.3310 0.3997 0.2823 -0.0649 -0.0395 0.1032  79  PRO   A CG  
581  C CD  . PRO   A 73  ? 0.2918 0.3723 0.2408 -0.0717 -0.0429 0.1101  79  PRO   A CD  
582  N N   . SER   A 74  ? 0.2727 0.3574 0.3338 -0.0365 -0.0410 0.1631  80  SER   A N   
583  C CA  . SER   A 74  ? 0.2829 0.3856 0.3823 -0.0360 -0.0442 0.1908  80  SER   A CA  
584  C C   . SER   A 74  ? 0.2785 0.3639 0.4079 -0.0212 -0.0341 0.1902  80  SER   A C   
585  O O   . SER   A 74  ? 0.2890 0.3495 0.4066 -0.0125 -0.0252 0.1681  80  SER   A O   
586  C CB  . SER   A 74  ? 0.3199 0.4348 0.4381 -0.0363 -0.0461 0.2046  80  SER   A CB  
587  O OG  . SER   A 74  ? 0.4084 0.5370 0.4981 -0.0502 -0.0537 0.2025  80  SER   A OG  
588  N N   . LEU   A 75  ? 0.2677 0.3673 0.4382 -0.0194 -0.0350 0.2157  81  LEU   A N   
589  C CA  . LEU   A 75  ? 0.2803 0.3648 0.4865 -0.0065 -0.0232 0.2175  81  LEU   A CA  
590  C C   . LEU   A 75  ? 0.2983 0.3728 0.5299 0.0030  -0.0124 0.2157  81  LEU   A C   
591  O O   . LEU   A 75  ? 0.3022 0.3956 0.5601 0.0008  -0.0165 0.2372  81  LEU   A O   
592  C CB  . LEU   A 75  ? 0.2616 0.3690 0.5049 -0.0103 -0.0295 0.2493  81  LEU   A CB  
593  C CG  . LEU   A 75  ? 0.2865 0.3805 0.5705 0.0012  -0.0172 0.2540  81  LEU   A CG  
594  C CD1 . LEU   A 75  ? 0.3103 0.3816 0.5683 0.0044  -0.0110 0.2295  81  LEU   A CD1 
595  C CD2 . LEU   A 75  ? 0.2678 0.3889 0.5950 -0.0033 -0.0252 0.2917  81  LEU   A CD2 
596  N N   . ILE   A 76  ? 0.3117 0.3580 0.5343 0.0117  0.0011  0.1905  82  ILE   A N   
597  C CA  . ILE   A 76  ? 0.3128 0.3467 0.5523 0.0186  0.0133  0.1836  82  ILE   A CA  
598  C C   . ILE   A 76  ? 0.3174 0.3283 0.5839 0.0278  0.0325  0.1732  82  ILE   A C   
599  O O   . ILE   A 76  ? 0.3296 0.3240 0.5778 0.0287  0.0370  0.1562  82  ILE   A O   
600  C CB  . ILE   A 76  ? 0.3372 0.3587 0.5308 0.0161  0.0119  0.1592  82  ILE   A CB  
601  C CG1 . ILE   A 76  ? 0.3520 0.3940 0.5189 0.0058  -0.0041 0.1663  82  ILE   A CG1 
602  C CG2 . ILE   A 76  ? 0.3404 0.3478 0.5465 0.0217  0.0251  0.1495  82  ILE   A CG2 
603  C CD1 . ILE   A 76  ? 0.3837 0.4137 0.5098 0.0034  -0.0053 0.1443  82  ILE   A CD1 
604  N N   . PHE   A 77  ? 0.3134 0.3222 0.6230 0.0336  0.0454  0.1815  83  PHE   A N   
605  C CA  . PHE   A 77  ? 0.3237 0.3089 0.6594 0.0401  0.0674  0.1686  83  PHE   A CA  
606  C C   . PHE   A 77  ? 0.3331 0.2939 0.6303 0.0386  0.0766  0.1364  83  PHE   A C   
607  O O   . PHE   A 77  ? 0.3540 0.3153 0.6325 0.0366  0.0742  0.1298  83  PHE   A O   
608  C CB  . PHE   A 77  ? 0.3223 0.3116 0.7191 0.0461  0.0811  0.1860  83  PHE   A CB  
609  C CG  . PHE   A 77  ? 0.3561 0.3223 0.7871 0.0515  0.1058  0.1751  83  PHE   A CG  
610  C CD1 . PHE   A 77  ? 0.3712 0.3384 0.8306 0.0541  0.1084  0.1870  83  PHE   A CD1 
611  C CD2 . PHE   A 77  ? 0.3830 0.3264 0.8178 0.0523  0.1274  0.1525  83  PHE   A CD2 
612  C CE1 . PHE   A 77  ? 0.3838 0.3287 0.8762 0.0580  0.1331  0.1758  83  PHE   A CE1 
613  C CE2 . PHE   A 77  ? 0.3904 0.3119 0.8557 0.0546  0.1525  0.1403  83  PHE   A CE2 
614  C CZ  . PHE   A 77  ? 0.3845 0.3064 0.8793 0.0577  0.1556  0.1518  83  PHE   A CZ  
615  N N   . VAL   A 78  ? 0.3179 0.2587 0.6017 0.0382  0.0860  0.1172  84  VAL   A N   
616  C CA  . VAL   A 78  ? 0.3286 0.2481 0.5762 0.0342  0.0941  0.0884  84  VAL   A CA  
617  C C   . VAL   A 78  ? 0.3412 0.2394 0.6153 0.0346  0.1195  0.0748  84  VAL   A C   
618  O O   . VAL   A 78  ? 0.3322 0.2255 0.6306 0.0366  0.1277  0.0780  84  VAL   A O   
619  C CB  . VAL   A 78  ? 0.3320 0.2482 0.5339 0.0299  0.0815  0.0762  84  VAL   A CB  
620  C CG1 . VAL   A 78  ? 0.3569 0.2546 0.5222 0.0241  0.0871  0.0503  84  VAL   A CG1 
621  C CG2 . VAL   A 78  ? 0.3164 0.2528 0.4962 0.0283  0.0597  0.0886  84  VAL   A CG2 
622  N N   . GLU   A 79  ? 0.3627 0.2473 0.6296 0.0310  0.1330  0.0580  85  GLU   A N   
623  C CA  . GLU   A 79  ? 0.3800 0.2428 0.6674 0.0278  0.1603  0.0406  85  GLU   A CA  
624  C C   . GLU   A 79  ? 0.4022 0.2498 0.6636 0.0210  0.1646  0.0218  85  GLU   A C   
625  O O   . GLU   A 79  ? 0.4179 0.2697 0.6370 0.0179  0.1466  0.0176  85  GLU   A O   
626  C CB  . GLU   A 79  ? 0.4316 0.2836 0.7038 0.0216  0.1718  0.0234  85  GLU   A CB  
627  C CG  . GLU   A 79  ? 0.4993 0.3622 0.8067 0.0276  0.1750  0.0390  85  GLU   A CG  
628  C CD  . GLU   A 79  ? 0.5932 0.4588 0.9695 0.0356  0.1912  0.0563  85  GLU   A CD  
629  O OE1 . GLU   A 79  ? 0.6248 0.4727 1.0255 0.0339  0.2139  0.0449  85  GLU   A OE1 
630  O OE2 . GLU   A 79  ? 0.6096 0.4958 1.0171 0.0429  0.1810  0.0826  85  GLU   A OE2 
631  N N   . ALA   A 80  ? 0.4004 0.2301 0.6883 0.0178  0.1899  0.0095  86  ALA   A N   
632  C CA  . ALA   A 80  ? 0.4183 0.2333 0.6840 0.0093  0.1966  -0.0094 86  ALA   A CA  
633  C C   . ALA   A 80  ? 0.4426 0.2505 0.6504 -0.0034 0.1909  -0.0313 86  ALA   A C   
634  O O   . ALA   A 80  ? 0.4428 0.2478 0.6366 -0.0084 0.1949  -0.0398 86  ALA   A O   
635  C CB  . ALA   A 80  ? 0.4123 0.2079 0.7183 0.0058  0.2288  -0.0211 86  ALA   A CB  
636  N N   . SER   A 81  ? 0.4586 0.2653 0.6343 -0.0089 0.1804  -0.0386 87  SER   A N   
637  C CA  . SER   A 81  ? 0.4900 0.2925 0.6134 -0.0220 0.1729  -0.0561 87  SER   A CA  
638  C C   . SER   A 81  ? 0.5031 0.2938 0.6135 -0.0333 0.1818  -0.0721 87  SER   A C   
639  O O   . SER   A 81  ? 0.4889 0.2731 0.6316 -0.0302 0.1954  -0.0709 87  SER   A O   
640  C CB  . SER   A 81  ? 0.5073 0.3265 0.6009 -0.0166 0.1436  -0.0439 87  SER   A CB  
641  O OG  . SER   A 81  ? 0.5371 0.3648 0.6399 -0.0090 0.1323  -0.0314 87  SER   A OG  
642  N N   . GLU   A 82  ? 0.5277 0.3162 0.5925 -0.0475 0.1745  -0.0864 88  GLU   A N   
643  C CA  . GLU   A 82  ? 0.5460 0.3265 0.5931 -0.0608 0.1799  -0.1008 88  GLU   A CA  
644  C C   . GLU   A 82  ? 0.5289 0.3177 0.5856 -0.0504 0.1660  -0.0877 88  GLU   A C   
645  O O   . GLU   A 82  ? 0.5307 0.3113 0.5949 -0.0560 0.1767  -0.0957 88  GLU   A O   
646  C CB  . GLU   A 82  ? 0.6174 0.4009 0.6137 -0.0772 0.1675  -0.1114 88  GLU   A CB  
647  C CG  . GLU   A 82  ? 0.7463 0.5234 0.7204 -0.0954 0.1729  -0.1270 88  GLU   A CG  
648  C CD  . GLU   A 82  ? 0.8785 0.6677 0.8116 -0.1042 0.1487  -0.1244 88  GLU   A CD  
649  O OE1 . GLU   A 82  ? 0.9047 0.6968 0.8315 -0.1073 0.1420  -0.1244 88  GLU   A OE1 
650  O OE2 . GLU   A 82  ? 0.9076 0.7038 0.8176 -0.1077 0.1367  -0.1213 88  GLU   A OE2 
651  N N   . TYR   A 83  ? 0.5102 0.3150 0.5677 -0.0362 0.1438  -0.0682 89  TYR   A N   
652  C CA  . TYR   A 83  ? 0.4995 0.3147 0.5603 -0.0276 0.1281  -0.0553 89  TYR   A CA  
653  C C   . TYR   A 83  ? 0.4566 0.2766 0.5604 -0.0139 0.1316  -0.0380 89  TYR   A C   
654  O O   . TYR   A 83  ? 0.4513 0.2740 0.5631 -0.0110 0.1279  -0.0327 89  TYR   A O   
655  C CB  . TYR   A 83  ? 0.5177 0.3476 0.5511 -0.0236 0.1030  -0.0463 89  TYR   A CB  
656  C CG  . TYR   A 83  ? 0.5603 0.3888 0.5588 -0.0346 0.0978  -0.0568 89  TYR   A CG  
657  C CD1 . TYR   A 83  ? 0.5905 0.4147 0.5623 -0.0492 0.0971  -0.0696 89  TYR   A CD1 
658  C CD2 . TYR   A 83  ? 0.5786 0.4108 0.5717 -0.0320 0.0939  -0.0531 89  TYR   A CD2 
659  C CE1 . TYR   A 83  ? 0.6174 0.4426 0.5582 -0.0611 0.0912  -0.0763 89  TYR   A CE1 
660  C CE2 . TYR   A 83  ? 0.6058 0.4369 0.5684 -0.0429 0.0895  -0.0614 89  TYR   A CE2 
661  C CZ  . TYR   A 83  ? 0.6346 0.4626 0.5714 -0.0577 0.0879  -0.0723 89  TYR   A CZ  
662  O OH  . TYR   A 83  ? 0.6755 0.5051 0.5823 -0.0699 0.0813  -0.0773 89  TYR   A OH  
663  N N   . TYR   A 84  ? 0.4297 0.2532 0.5611 -0.0060 0.1369  -0.0271 90  TYR   A N   
664  C CA  . TYR   A 84  ? 0.4064 0.2375 0.5817 0.0055  0.1389  -0.0068 90  TYR   A CA  
665  C C   . TYR   A 84  ? 0.4126 0.2354 0.6305 0.0079  0.1613  -0.0054 90  TYR   A C   
666  O O   . TYR   A 84  ? 0.4207 0.2391 0.6314 0.0045  0.1678  -0.0137 90  TYR   A O   
667  C CB  . TYR   A 84  ? 0.3760 0.2283 0.5482 0.0139  0.1168  0.0140  90  TYR   A CB  
668  C CG  . TYR   A 84  ? 0.3662 0.2276 0.5035 0.0125  0.0964  0.0144  90  TYR   A CG  
669  C CD1 . TYR   A 84  ? 0.3525 0.2195 0.4972 0.0149  0.0905  0.0226  90  TYR   A CD1 
670  C CD2 . TYR   A 84  ? 0.3756 0.2407 0.4763 0.0092  0.0834  0.0080  90  TYR   A CD2 
671  C CE1 . TYR   A 84  ? 0.3575 0.2330 0.4736 0.0136  0.0736  0.0226  90  TYR   A CE1 
672  C CE2 . TYR   A 84  ? 0.3777 0.2508 0.4527 0.0085  0.0668  0.0087  90  TYR   A CE2 
673  C CZ  . TYR   A 84  ? 0.3746 0.2527 0.4573 0.0106  0.0625  0.0153  90  TYR   A CZ  
674  O OH  . TYR   A 84  ? 0.3542 0.2398 0.4143 0.0096  0.0480  0.0153  90  TYR   A OH  
675  N N   . PRO   A 85  ? 0.4077 0.2296 0.6742 0.0146  0.1730  0.0074  91  PRO   A N   
676  C CA  . PRO   A 85  ? 0.4014 0.2183 0.7164 0.0190  0.1932  0.0132  91  PRO   A CA  
677  C C   . PRO   A 85  ? 0.4091 0.2462 0.7320 0.0271  0.1771  0.0349  91  PRO   A C   
678  O O   . PRO   A 85  ? 0.4172 0.2699 0.7064 0.0279  0.1526  0.0426  91  PRO   A O   
679  C CB  . PRO   A 85  ? 0.4028 0.2175 0.7686 0.0250  0.2050  0.0265  91  PRO   A CB  
680  C CG  . PRO   A 85  ? 0.4051 0.2349 0.7518 0.0279  0.1812  0.0400  91  PRO   A CG  
681  C CD  . PRO   A 85  ? 0.4002 0.2287 0.6836 0.0195  0.1666  0.0212  91  PRO   A CD  
682  N N   . ALA   A 86  ? 0.4024 0.2398 0.7706 0.0321  0.1914  0.0446  92  ALA   A N   
683  C CA  . ALA   A 86  ? 0.4020 0.2602 0.7815 0.0386  0.1767  0.0667  92  ALA   A CA  
684  C C   . ALA   A 86  ? 0.3904 0.2702 0.7906 0.0451  0.1588  0.0962  92  ALA   A C   
685  O O   . ALA   A 86  ? 0.3891 0.2668 0.8311 0.0489  0.1689  0.1069  92  ALA   A O   
686  C CB  . ALA   A 86  ? 0.3933 0.2465 0.8242 0.0423  0.1984  0.0714  92  ALA   A CB  
687  N N   . ARG   A 87  ? 0.3729 0.2722 0.7398 0.0443  0.1331  0.1067  93  ARG   A N   
688  C CA  . ARG   A 87  ? 0.3387 0.2596 0.7150 0.0464  0.1150  0.1319  93  ARG   A CA  
689  C C   . ARG   A 87  ? 0.3147 0.2581 0.6619 0.0438  0.0914  0.1439  93  ARG   A C   
690  O O   . ARG   A 87  ? 0.3248 0.2653 0.6435 0.0414  0.0889  0.1313  93  ARG   A O   
691  C CB  . ARG   A 87  ? 0.3602 0.2728 0.7072 0.0430  0.1109  0.1194  93  ARG   A CB  
692  C CG  . ARG   A 87  ? 0.4052 0.3114 0.6904 0.0369  0.1007  0.0962  93  ARG   A CG  
693  C CD  . ARG   A 87  ? 0.4201 0.3284 0.6774 0.0339  0.0890  0.0925  93  ARG   A CD  
694  N NE  . ARG   A 87  ? 0.4530 0.3621 0.6593 0.0293  0.0754  0.0785  93  ARG   A NE  
695  C CZ  . ARG   A 87  ? 0.4794 0.3901 0.6570 0.0262  0.0649  0.0725  93  ARG   A CZ  
696  N NH1 . ARG   A 87  ? 0.4690 0.3799 0.6595 0.0267  0.0660  0.0776  93  ARG   A NH1 
697  N NH2 . ARG   A 87  ? 0.4700 0.3812 0.6082 0.0226  0.0542  0.0612  93  ARG   A NH2 
698  N N   . TYR   A 88  ? 0.2804 0.2463 0.6334 0.0425  0.0747  0.1673  94  TYR   A N   
699  C CA  . TYR   A 88  ? 0.2777 0.2651 0.6013 0.0369  0.0536  0.1772  94  TYR   A CA  
700  C C   . TYR   A 88  ? 0.2921 0.2740 0.5627 0.0316  0.0437  0.1586  94  TYR   A C   
701  O O   . TYR   A 88  ? 0.2980 0.2750 0.5674 0.0314  0.0445  0.1563  94  TYR   A O   
702  C CB  . TYR   A 88  ? 0.2686 0.2846 0.6242 0.0346  0.0413  0.2122  94  TYR   A CB  
703  C CG  . TYR   A 88  ? 0.2641 0.2929 0.6671 0.0381  0.0452  0.2342  94  TYR   A CG  
704  C CD1 . TYR   A 88  ? 0.2829 0.3261 0.6716 0.0340  0.0353  0.2392  94  TYR   A CD1 
705  C CD2 . TYR   A 88  ? 0.2567 0.2822 0.7214 0.0456  0.0604  0.2494  94  TYR   A CD2 
706  C CE1 . TYR   A 88  ? 0.2823 0.3384 0.7161 0.0370  0.0386  0.2601  94  TYR   A CE1 
707  C CE2 . TYR   A 88  ? 0.2554 0.2933 0.7693 0.0493  0.0647  0.2711  94  TYR   A CE2 
708  C CZ  . TYR   A 88  ? 0.2851 0.3385 0.7828 0.0451  0.0535  0.2762  94  TYR   A CZ  
709  O OH  . TYR   A 88  ? 0.3106 0.3775 0.8586 0.0486  0.0576  0.2984  94  TYR   A OH  
710  N N   . GLN   A 89  ? 0.2807 0.2632 0.5109 0.0276  0.0352  0.1460  95  GLN   A N   
711  C CA  . GLN   A 89  ? 0.2776 0.2565 0.4620 0.0227  0.0259  0.1301  95  GLN   A CA  
712  C C   . GLN   A 89  ? 0.2690 0.2716 0.4368 0.0150  0.0090  0.1439  95  GLN   A C   
713  O O   . GLN   A 89  ? 0.2781 0.2930 0.4501 0.0127  0.0047  0.1536  95  GLN   A O   
714  C CB  . GLN   A 89  ? 0.2812 0.2413 0.4347 0.0230  0.0308  0.1048  95  GLN   A CB  
715  C CG  . GLN   A 89  ? 0.2925 0.2498 0.4048 0.0187  0.0213  0.0907  95  GLN   A CG  
716  C CD  . GLN   A 89  ? 0.3019 0.2396 0.3892 0.0186  0.0266  0.0677  95  GLN   A CD  
717  O OE1 . GLN   A 89  ? 0.3144 0.2368 0.4106 0.0200  0.0392  0.0577  95  GLN   A OE1 
718  N NE2 . GLN   A 89  ? 0.3069 0.2455 0.3632 0.0153  0.0175  0.0592  95  GLN   A NE2 
719  N N   . SER   A 90  ? 0.2598 0.2697 0.4094 0.0094  0.0005  0.1447  96  SER   A N   
720  C CA  . SER   A 90  ? 0.2514 0.2835 0.3829 -0.0014 -0.0133 0.1554  96  SER   A CA  
721  C C   . SER   A 90  ? 0.2676 0.2932 0.3566 -0.0060 -0.0171 0.1346  96  SER   A C   
722  O O   . SER   A 90  ? 0.2831 0.2883 0.3571 -0.0006 -0.0111 0.1142  96  SER   A O   
723  C CB  . SER   A 90  ? 0.2661 0.3117 0.4030 -0.0075 -0.0193 0.1688  96  SER   A CB  
724  O OG  . SER   A 90  ? 0.3066 0.3358 0.4241 -0.0053 -0.0156 0.1497  96  SER   A OG  
725  N N   . HIS   A 91  ? 0.2527 0.2967 0.3246 -0.0173 -0.0265 0.1412  97  HIS   A N   
726  C CA  . HIS   A 91  ? 0.2570 0.2977 0.2936 -0.0237 -0.0291 0.1243  97  HIS   A CA  
727  C C   . HIS   A 91  ? 0.2445 0.2665 0.2729 -0.0155 -0.0233 0.1079  97  HIS   A C   
728  O O   . HIS   A 91  ? 0.2474 0.2568 0.2530 -0.0152 -0.0219 0.0900  97  HIS   A O   
729  C CB  . HIS   A 91  ? 0.2866 0.3217 0.3044 -0.0271 -0.0290 0.1121  97  HIS   A CB  
730  C CG  . HIS   A 91  ? 0.3110 0.3654 0.3334 -0.0374 -0.0347 0.1277  97  HIS   A CG  
731  N ND1 . HIS   A 91  ? 0.3323 0.4041 0.3337 -0.0538 -0.0404 0.1299  97  HIS   A ND1 
732  C CD2 . HIS   A 91  ? 0.3341 0.3933 0.3797 -0.0348 -0.0349 0.1419  97  HIS   A CD2 
733  C CE1 . HIS   A 91  ? 0.3353 0.4230 0.3456 -0.0616 -0.0450 0.1459  97  HIS   A CE1 
734  N NE2 . HIS   A 91  ? 0.3359 0.4166 0.3739 -0.0498 -0.0423 0.1544  97  HIS   A NE2 
735  N N   . LEU   A 92  ? 0.2201 0.2416 0.2691 -0.0099 -0.0199 0.1156  98  LEU   A N   
736  C CA  . LEU   A 92  ? 0.2235 0.2284 0.2665 -0.0035 -0.0137 0.1019  98  LEU   A CA  
737  C C   . LEU   A 92  ? 0.2091 0.2240 0.2435 -0.0088 -0.0179 0.1053  98  LEU   A C   
738  O O   . LEU   A 92  ? 0.1934 0.2286 0.2413 -0.0146 -0.0233 0.1235  98  LEU   A O   
739  C CB  . LEU   A 92  ? 0.2179 0.2121 0.2900 0.0056  -0.0033 0.1043  98  LEU   A CB  
740  C CG  . LEU   A 92  ? 0.2275 0.2035 0.2930 0.0102  0.0051  0.0889  98  LEU   A CG  
741  C CD1 . LEU   A 92  ? 0.2322 0.1911 0.2718 0.0107  0.0063  0.0692  98  LEU   A CD1 
742  C CD2 . LEU   A 92  ? 0.2232 0.1917 0.3231 0.0165  0.0183  0.0931  98  LEU   A CD2 
743  N N   . MET   A 93  ? 0.2114 0.2135 0.2234 -0.0080 -0.0163 0.0887  99  MET   A N   
744  C CA  . MET   A 93  ? 0.2116 0.2192 0.2124 -0.0127 -0.0190 0.0882  99  MET   A CA  
745  C C   . MET   A 93  ? 0.2159 0.2077 0.2204 -0.0051 -0.0117 0.0797  99  MET   A C   
746  O O   . MET   A 93  ? 0.2374 0.2115 0.2350 0.0000  -0.0068 0.0666  99  MET   A O   
747  C CB  . MET   A 93  ? 0.2121 0.2165 0.1833 -0.0193 -0.0220 0.0747  99  MET   A CB  
748  C CG  . MET   A 93  ? 0.2203 0.2382 0.1843 -0.0291 -0.0266 0.0789  99  MET   A CG  
749  S SD  . MET   A 93  ? 0.3017 0.3120 0.2375 -0.0363 -0.0252 0.0601  99  MET   A SD  
750  C CE  . MET   A 93  ? 0.2836 0.2713 0.2210 -0.0238 -0.0209 0.0473  99  MET   A CE  
751  N N   . LEU   A 94  ? 0.2028 0.2015 0.2165 -0.0058 -0.0112 0.0869  100 LEU   A N   
752  C CA  . LEU   A 94  ? 0.2038 0.1880 0.2203 -0.0002 -0.0031 0.0784  100 LEU   A CA  
753  C C   . LEU   A 94  ? 0.2007 0.1846 0.1965 -0.0044 -0.0062 0.0720  100 LEU   A C   
754  O O   . LEU   A 94  ? 0.2092 0.2086 0.1995 -0.0116 -0.0129 0.0794  100 LEU   A O   
755  C CB  . LEU   A 94  ? 0.2165 0.2071 0.2684 0.0038  0.0034  0.0920  100 LEU   A CB  
756  C CG  . LEU   A 94  ? 0.2527 0.2416 0.3331 0.0090  0.0097  0.0991  100 LEU   A CG  
757  C CD1 . LEU   A 94  ? 0.2625 0.2583 0.3845 0.0130  0.0176  0.1141  100 LEU   A CD1 
758  C CD2 . LEU   A 94  ? 0.2842 0.2497 0.3544 0.0128  0.0189  0.0802  100 LEU   A CD2 
759  N N   . ALA   A 95  ? 0.1893 0.1561 0.1738 -0.0014 -0.0009 0.0586  101 ALA   A N   
760  C CA  . ALA   A 95  ? 0.1941 0.1577 0.1614 -0.0044 -0.0023 0.0523  101 ALA   A CA  
761  C C   . ALA   A 95  ? 0.2034 0.1542 0.1749 -0.0011 0.0066  0.0459  101 ALA   A C   
762  O O   . ALA   A 95  ? 0.2133 0.1543 0.1943 0.0022  0.0143  0.0418  101 ALA   A O   
763  C CB  . ALA   A 95  ? 0.2043 0.1587 0.1464 -0.0066 -0.0064 0.0406  101 ALA   A CB  
764  N N   . VAL   A 96  ? 0.2016 0.1524 0.1650 -0.0035 0.0065  0.0441  102 VAL   A N   
765  C CA  . VAL   A 96  ? 0.2126 0.1514 0.1757 -0.0027 0.0152  0.0366  102 VAL   A CA  
766  C C   . VAL   A 96  ? 0.2519 0.1760 0.1885 -0.0049 0.0132  0.0237  102 VAL   A C   
767  O O   . VAL   A 96  ? 0.2699 0.1940 0.1894 -0.0075 0.0064  0.0215  102 VAL   A O   
768  C CB  . VAL   A 96  ? 0.2224 0.1686 0.1897 -0.0048 0.0159  0.0414  102 VAL   A CB  
769  C CG1 . VAL   A 96  ? 0.2323 0.1647 0.1938 -0.0058 0.0250  0.0313  102 VAL   A CG1 
770  C CG2 . VAL   A 96  ? 0.2214 0.1851 0.2196 -0.0034 0.0168  0.0576  102 VAL   A CG2 
771  N N   . GLY   A 97  ? 0.2624 0.1747 0.1974 -0.0051 0.0197  0.0160  103 GLY   A N   
772  C CA  . GLY   A 97  ? 0.2810 0.1820 0.1928 -0.0091 0.0167  0.0067  103 GLY   A CA  
773  C C   . GLY   A 97  ? 0.2855 0.1759 0.1955 -0.0124 0.0246  -0.0016 103 GLY   A C   
774  O O   . GLY   A 97  ? 0.2808 0.1707 0.2094 -0.0103 0.0337  -0.0014 103 GLY   A O   
775  N N   . HIS   A 98  ? 0.2898 0.1724 0.1781 -0.0189 0.0215  -0.0082 104 HIS   A N   
776  C CA  . HIS   A 98  ? 0.2969 0.1705 0.1776 -0.0262 0.0284  -0.0170 104 HIS   A CA  
777  C C   . HIS   A 98  ? 0.2916 0.1658 0.1738 -0.0245 0.0237  -0.0165 104 HIS   A C   
778  O O   . HIS   A 98  ? 0.3045 0.1828 0.1810 -0.0219 0.0122  -0.0118 104 HIS   A O   
779  C CB  . HIS   A 98  ? 0.2965 0.1647 0.1518 -0.0372 0.0252  -0.0219 104 HIS   A CB  
780  C CG  . HIS   A 98  ? 0.3327 0.1935 0.1762 -0.0490 0.0325  -0.0315 104 HIS   A CG  
781  N ND1 . HIS   A 98  ? 0.3367 0.1905 0.1866 -0.0546 0.0500  -0.0413 104 HIS   A ND1 
782  C CD2 . HIS   A 98  ? 0.3599 0.2200 0.1884 -0.0568 0.0257  -0.0328 104 HIS   A CD2 
783  C CE1 . HIS   A 98  ? 0.3482 0.1967 0.1837 -0.0669 0.0539  -0.0498 104 HIS   A CE1 
784  N NE2 . HIS   A 98  ? 0.3620 0.2150 0.1832 -0.0691 0.0386  -0.0443 104 HIS   A NE2 
785  N N   . SER   A 99  ? 0.2850 0.1536 0.1737 -0.0276 0.0339  -0.0228 105 SER   A N   
786  C CA  . SER   A 99  ? 0.2911 0.1588 0.1789 -0.0284 0.0312  -0.0243 105 SER   A CA  
787  C C   . SER   A 99  ? 0.3096 0.1677 0.1971 -0.0375 0.0457  -0.0357 105 SER   A C   
788  O O   . SER   A 99  ? 0.3221 0.1751 0.2217 -0.0389 0.0605  -0.0407 105 SER   A O   
789  C CB  . SER   A 99  ? 0.2999 0.1752 0.2069 -0.0176 0.0272  -0.0158 105 SER   A CB  
790  O OG  . SER   A 99  ? 0.3313 0.2068 0.2629 -0.0132 0.0387  -0.0139 105 SER   A OG  
791  N N   . GLU   A 100 ? 0.2970 0.1529 0.1715 -0.0448 0.0422  -0.0400 106 GLU   A N   
792  C CA  . GLU   A 100 ? 0.3165 0.1641 0.1867 -0.0563 0.0546  -0.0519 106 GLU   A CA  
793  C C   . GLU   A 100 ? 0.3259 0.1757 0.2044 -0.0518 0.0503  -0.0495 106 GLU   A C   
794  O O   . GLU   A 100 ? 0.3205 0.1785 0.2029 -0.0422 0.0364  -0.0392 106 GLU   A O   
795  C CB  . GLU   A 100 ? 0.3529 0.1984 0.1921 -0.0744 0.0520  -0.0589 106 GLU   A CB  
796  C CG  . GLU   A 100 ? 0.3570 0.1998 0.1891 -0.0791 0.0580  -0.0619 106 GLU   A CG  
797  C CD  . GLU   A 100 ? 0.4201 0.2628 0.2202 -0.0985 0.0544  -0.0665 106 GLU   A CD  
798  O OE1 . GLU   A 100 ? 0.4553 0.2974 0.2387 -0.1136 0.0546  -0.0726 106 GLU   A OE1 
799  O OE2 . GLU   A 100 ? 0.4113 0.2554 0.2026 -0.1002 0.0514  -0.0637 106 GLU   A OE2 
800  N N   . PRO   A 101 ? 0.3400 0.1821 0.2239 -0.0585 0.0636  -0.0592 107 PRO   A N   
801  C CA  . PRO   A 101 ? 0.3388 0.1830 0.2327 -0.0534 0.0600  -0.0563 107 PRO   A CA  
802  C C   . PRO   A 101 ? 0.3438 0.1965 0.2215 -0.0543 0.0408  -0.0498 107 PRO   A C   
803  O O   . PRO   A 101 ? 0.3412 0.2001 0.2304 -0.0437 0.0323  -0.0415 107 PRO   A O   
804  C CB  . PRO   A 101 ? 0.3599 0.1928 0.2549 -0.0659 0.0786  -0.0712 107 PRO   A CB  
805  C CG  . PRO   A 101 ? 0.3528 0.1775 0.2562 -0.0692 0.0961  -0.0787 107 PRO   A CG  
806  C CD  . PRO   A 101 ? 0.3403 0.1708 0.2245 -0.0707 0.0848  -0.0740 107 PRO   A CD  
807  N N   . GLY   A 102 ? 0.3459 0.2000 0.1984 -0.0679 0.0342  -0.0526 108 GLY   A N   
808  C CA  . GLY   A 102 ? 0.3339 0.1969 0.1749 -0.0700 0.0163  -0.0444 108 GLY   A CA  
809  C C   . GLY   A 102 ? 0.3037 0.1742 0.1524 -0.0567 0.0031  -0.0320 108 GLY   A C   
810  O O   . GLY   A 102 ? 0.3006 0.1782 0.1483 -0.0556 -0.0100 -0.0244 108 GLY   A O   
811  N N   . ASP   A 103 ? 0.2869 0.1562 0.1449 -0.0474 0.0071  -0.0299 109 ASP   A N   
812  C CA  . ASP   A 103 ? 0.2719 0.1477 0.1370 -0.0364 -0.0032 -0.0201 109 ASP   A CA  
813  C C   . ASP   A 103 ? 0.2657 0.1457 0.1481 -0.0254 -0.0049 -0.0158 109 ASP   A C   
814  O O   . ASP   A 103 ? 0.2474 0.1328 0.1347 -0.0187 -0.0123 -0.0096 109 ASP   A O   
815  C CB  . ASP   A 103 ? 0.2696 0.1445 0.1369 -0.0323 0.0009  -0.0190 109 ASP   A CB  
816  C CG  . ASP   A 103 ? 0.2785 0.1506 0.1273 -0.0432 0.0004  -0.0216 109 ASP   A CG  
817  O OD1 . ASP   A 103 ? 0.3099 0.1849 0.1461 -0.0506 -0.0098 -0.0181 109 ASP   A OD1 
818  O OD2 . ASP   A 103 ? 0.3040 0.1719 0.1522 -0.0450 0.0098  -0.0260 109 ASP   A OD2 
819  N N   . CYS   A 104 ? 0.2649 0.1424 0.1567 -0.0247 0.0029  -0.0195 110 CYS   A N   
820  C CA  . CYS   A 104 ? 0.2592 0.1415 0.1661 -0.0161 0.0010  -0.0148 110 CYS   A CA  
821  C C   . CYS   A 104 ? 0.2505 0.1381 0.1540 -0.0154 -0.0106 -0.0111 110 CYS   A C   
822  O O   . CYS   A 104 ? 0.2681 0.1552 0.1617 -0.0227 -0.0155 -0.0125 110 CYS   A O   
823  C CB  . CYS   A 104 ? 0.2655 0.1431 0.1823 -0.0175 0.0109  -0.0194 110 CYS   A CB  
824  S SG  . CYS   A 104 ? 0.3008 0.1746 0.2376 -0.0134 0.0259  -0.0192 110 CYS   A SG  
825  N N   . GLY   A 105 ? 0.2313 0.1247 0.1438 -0.0080 -0.0143 -0.0060 111 GLY   A N   
826  C CA  . GLY   A 105 ? 0.2349 0.1326 0.1495 -0.0065 -0.0224 -0.0031 111 GLY   A CA  
827  C C   . GLY   A 105 ? 0.2326 0.1320 0.1456 -0.0051 -0.0273 0.0001  111 GLY   A C   
828  O O   . GLY   A 105 ? 0.2379 0.1404 0.1584 -0.0027 -0.0310 0.0023  111 GLY   A O   
829  N N   . GLY   A 106 ? 0.2299 0.1268 0.1352 -0.0068 -0.0260 0.0000  112 GLY   A N   
830  C CA  . GLY   A 106 ? 0.2313 0.1290 0.1359 -0.0056 -0.0295 0.0028  112 GLY   A CA  
831  C C   . GLY   A 106 ? 0.2303 0.1322 0.1427 -0.0010 -0.0267 0.0031  112 GLY   A C   
832  O O   . GLY   A 106 ? 0.2327 0.1378 0.1472 0.0003  -0.0223 0.0029  112 GLY   A O   
833  N N   . ILE   A 107 ? 0.2069 0.1096 0.1253 0.0000  -0.0287 0.0039  113 ILE   A N   
834  C CA  . ILE   A 107 ? 0.2149 0.1218 0.1380 0.0008  -0.0244 0.0019  113 ILE   A CA  
835  C C   . ILE   A 107 ? 0.2116 0.1200 0.1284 -0.0008 -0.0218 0.0017  113 ILE   A C   
836  O O   . ILE   A 107 ? 0.2202 0.1244 0.1332 -0.0014 -0.0233 0.0025  113 ILE   A O   
837  C CB  . ILE   A 107 ? 0.2194 0.1251 0.1547 0.0014  -0.0240 0.0006  113 ILE   A CB  
838  C CG1 . ILE   A 107 ? 0.2417 0.1493 0.1854 0.0027  -0.0250 0.0004  113 ILE   A CG1 
839  C CG2 . ILE   A 107 ? 0.2154 0.1233 0.1525 -0.0013 -0.0173 -0.0041 113 ILE   A CG2 
840  C CD1 . ILE   A 107 ? 0.2683 0.1749 0.2280 0.0036  -0.0236 -0.0003 113 ILE   A CD1 
841  N N   . LEU   A 108 ? 0.1847 0.1004 0.1008 -0.0028 -0.0185 0.0016  114 LEU   A N   
842  C CA  . LEU   A 108 ? 0.1855 0.1059 0.0965 -0.0066 -0.0162 0.0018  114 LEU   A CA  
843  C C   . LEU   A 108 ? 0.2040 0.1267 0.1172 -0.0115 -0.0120 -0.0035 114 LEU   A C   
844  O O   . LEU   A 108 ? 0.1978 0.1253 0.1142 -0.0135 -0.0105 -0.0046 114 LEU   A O   
845  C CB  . LEU   A 108 ? 0.1911 0.1214 0.1021 -0.0083 -0.0159 0.0076  114 LEU   A CB  
846  C CG  . LEU   A 108 ? 0.2146 0.1550 0.1212 -0.0149 -0.0147 0.0100  114 LEU   A CG  
847  C CD1 . LEU   A 108 ? 0.2171 0.1531 0.1188 -0.0143 -0.0147 0.0096  114 LEU   A CD1 
848  C CD2 . LEU   A 108 ? 0.2151 0.1686 0.1275 -0.0168 -0.0161 0.0199  114 LEU   A CD2 
849  N N   . ARG   A 109 ? 0.2171 0.1369 0.1285 -0.0148 -0.0087 -0.0074 115 ARG   A N   
850  C CA  . ARG   A 109 ? 0.2224 0.1426 0.1368 -0.0213 -0.0013 -0.0151 115 ARG   A CA  
851  C C   . ARG   A 109 ? 0.2342 0.1582 0.1396 -0.0300 0.0033  -0.0185 115 ARG   A C   
852  O O   . ARG   A 109 ? 0.2032 0.1259 0.1036 -0.0287 0.0006  -0.0153 115 ARG   A O   
853  C CB  . ARG   A 109 ? 0.2346 0.1439 0.1640 -0.0170 0.0015  -0.0185 115 ARG   A CB  
854  C CG  . ARG   A 109 ? 0.2411 0.1424 0.1733 -0.0130 -0.0013 -0.0152 115 ARG   A CG  
855  C CD  . ARG   A 109 ? 0.2651 0.1583 0.2179 -0.0087 0.0000  -0.0143 115 ARG   A CD  
856  N NE  . ARG   A 109 ? 0.2671 0.1605 0.2249 -0.0030 -0.0087 -0.0069 115 ARG   A NE  
857  C CZ  . ARG   A 109 ? 0.2905 0.1837 0.2642 -0.0006 -0.0082 -0.0064 115 ARG   A CZ  
858  N NH1 . ARG   A 109 ? 0.2728 0.1647 0.2597 -0.0030 0.0021  -0.0140 115 ARG   A NH1 
859  N NH2 . ARG   A 109 ? 0.2653 0.1600 0.2416 0.0027  -0.0170 0.0009  115 ARG   A NH2 
860  N N   . CYS   A 110 ? 0.2513 0.1798 0.1542 -0.0405 0.0113  -0.0262 116 CYS   A N   
861  C CA  . CYS   A 110 ? 0.2838 0.2161 0.1769 -0.0522 0.0173  -0.0317 116 CYS   A CA  
862  C C   . CYS   A 110 ? 0.3246 0.2474 0.2263 -0.0584 0.0310  -0.0453 116 CYS   A C   
863  O O   . CYS   A 110 ? 0.3163 0.2296 0.2349 -0.0514 0.0344  -0.0481 116 CYS   A O   
864  C CB  . CYS   A 110 ? 0.3026 0.2532 0.1818 -0.0642 0.0150  -0.0276 116 CYS   A CB  
865  S SG  . CYS   A 110 ? 0.2982 0.2556 0.1756 -0.0750 0.0215  -0.0341 116 CYS   A SG  
866  N N   . GLN   A 111 ? 0.3465 0.2724 0.2384 -0.0727 0.0400  -0.0540 117 GLN   A N   
867  C CA  . GLN   A 111 ? 0.3847 0.3009 0.2860 -0.0809 0.0565  -0.0691 117 GLN   A CA  
868  C C   . GLN   A 111 ? 0.3966 0.3141 0.3032 -0.0865 0.0647  -0.0769 117 GLN   A C   
869  O O   . GLN   A 111 ? 0.4392 0.3452 0.3629 -0.0884 0.0792  -0.0886 117 GLN   A O   
870  C CB  . GLN   A 111 ? 0.4170 0.3378 0.3025 -0.0987 0.0654  -0.0782 117 GLN   A CB  
871  C CG  . GLN   A 111 ? 0.4717 0.4118 0.3343 -0.1178 0.0652  -0.0795 117 GLN   A CG  
872  C CD  . GLN   A 111 ? 0.5650 0.5124 0.4097 -0.1376 0.0722  -0.0870 117 GLN   A CD  
873  O OE1 . GLN   A 111 ? 0.5915 0.5487 0.4253 -0.1384 0.0620  -0.0770 117 GLN   A OE1 
874  N NE2 . GLN   A 111 ? 0.5716 0.5143 0.4137 -0.1550 0.0908  -0.1054 117 GLN   A NE2 
875  N N   . HIS   A 112 ? 0.3702 0.3013 0.2651 -0.0891 0.0565  -0.0702 118 HIS   A N   
876  C CA  . HIS   A 112 ? 0.3629 0.2968 0.2601 -0.0959 0.0637  -0.0771 118 HIS   A CA  
877  C C   . HIS   A 112 ? 0.3561 0.2835 0.2721 -0.0788 0.0576  -0.0707 118 HIS   A C   
878  O O   . HIS   A 112 ? 0.3717 0.2980 0.2957 -0.0820 0.0652  -0.0775 118 HIS   A O   
879  C CB  . HIS   A 112 ? 0.3849 0.3394 0.2586 -0.1115 0.0585  -0.0724 118 HIS   A CB  
880  C CG  . HIS   A 112 ? 0.4430 0.4084 0.2961 -0.1309 0.0621  -0.0761 118 HIS   A CG  
881  N ND1 . HIS   A 112 ? 0.4775 0.4537 0.3206 -0.1298 0.0493  -0.0627 118 HIS   A ND1 
882  C CD2 . HIS   A 112 ? 0.4674 0.4351 0.3085 -0.1533 0.0775  -0.0919 118 HIS   A CD2 
883  C CE1 . HIS   A 112 ? 0.4922 0.4783 0.3175 -0.1509 0.0555  -0.0691 118 HIS   A CE1 
884  N NE2 . HIS   A 112 ? 0.4929 0.4739 0.3147 -0.1666 0.0728  -0.0875 118 HIS   A NE2 
885  N N   . GLY   A 113 ? 0.3255 0.2492 0.2478 -0.0627 0.0446  -0.0584 119 GLY   A N   
886  C CA  . GLY   A 113 ? 0.3046 0.2234 0.2423 -0.0487 0.0379  -0.0518 119 GLY   A CA  
887  C C   . GLY   A 113 ? 0.2730 0.1971 0.2029 -0.0396 0.0228  -0.0383 119 GLY   A C   
888  O O   . GLY   A 113 ? 0.2751 0.2025 0.1944 -0.0394 0.0171  -0.0327 119 GLY   A O   
889  N N   . VAL   A 114 ? 0.2466 0.1707 0.1839 -0.0323 0.0176  -0.0337 120 VAL   A N   
890  C CA  . VAL   A 114 ? 0.2296 0.1568 0.1622 -0.0246 0.0063  -0.0232 120 VAL   A CA  
891  C C   . VAL   A 114 ? 0.2353 0.1759 0.1548 -0.0315 0.0036  -0.0180 120 VAL   A C   
892  O O   . VAL   A 114 ? 0.2471 0.1954 0.1637 -0.0394 0.0070  -0.0202 120 VAL   A O   
893  C CB  . VAL   A 114 ? 0.2276 0.1509 0.1722 -0.0166 0.0026  -0.0207 120 VAL   A CB  
894  C CG1 . VAL   A 114 ? 0.2277 0.1539 0.1667 -0.0116 -0.0059 -0.0123 120 VAL   A CG1 
895  C CG2 . VAL   A 114 ? 0.2359 0.1493 0.1957 -0.0102 0.0020  -0.0206 120 VAL   A CG2 
896  N N   . VAL   A 115 ? 0.2301 0.1741 0.1438 -0.0290 -0.0024 -0.0102 121 VAL   A N   
897  C CA  . VAL   A 115 ? 0.2325 0.1902 0.1402 -0.0340 -0.0062 -0.0011 121 VAL   A CA  
898  C C   . VAL   A 115 ? 0.2310 0.1895 0.1465 -0.0262 -0.0112 0.0073  121 VAL   A C   
899  O O   . VAL   A 115 ? 0.2416 0.2112 0.1587 -0.0303 -0.0129 0.0144  121 VAL   A O   
900  C CB  . VAL   A 115 ? 0.2461 0.2073 0.1480 -0.0357 -0.0083 0.0032  121 VAL   A CB  
901  C CG1 . VAL   A 115 ? 0.2551 0.2321 0.1575 -0.0397 -0.0132 0.0163  121 VAL   A CG1 
902  C CG2 . VAL   A 115 ? 0.2440 0.2047 0.1376 -0.0452 -0.0024 -0.0054 121 VAL   A CG2 
903  N N   . GLY   A 116 ? 0.2183 0.1652 0.1389 -0.0163 -0.0131 0.0065  122 GLY   A N   
904  C CA  . GLY   A 116 ? 0.2225 0.1680 0.1503 -0.0103 -0.0153 0.0119  122 GLY   A CA  
905  C C   . GLY   A 116 ? 0.2231 0.1562 0.1519 -0.0036 -0.0165 0.0088  122 GLY   A C   
906  O O   . GLY   A 116 ? 0.2225 0.1490 0.1481 -0.0030 -0.0171 0.0043  122 GLY   A O   
907  N N   . ILE   A 117 ? 0.2035 0.1339 0.1374 0.0000  -0.0162 0.0118  123 ILE   A N   
908  C CA  . ILE   A 117 ? 0.2059 0.1258 0.1371 0.0025  -0.0167 0.0081  123 ILE   A CA  
909  C C   . ILE   A 117 ? 0.2032 0.1209 0.1374 0.0035  -0.0128 0.0105  123 ILE   A C   
910  O O   . ILE   A 117 ? 0.1818 0.1054 0.1264 0.0043  -0.0099 0.0165  123 ILE   A O   
911  C CB  . ILE   A 117 ? 0.2166 0.1325 0.1506 0.0033  -0.0178 0.0052  123 ILE   A CB  
912  C CG1 . ILE   A 117 ? 0.2227 0.1429 0.1655 0.0040  -0.0152 0.0083  123 ILE   A CG1 
913  C CG2 . ILE   A 117 ? 0.2254 0.1408 0.1599 0.0029  -0.0211 0.0024  123 ILE   A CG2 
914  C CD1 . ILE   A 117 ? 0.2495 0.1643 0.1946 0.0042  -0.0150 0.0049  123 ILE   A CD1 
915  N N   . VAL   A 118 ? 0.1956 0.1054 0.1225 0.0025  -0.0121 0.0067  124 VAL   A N   
916  C CA  . VAL   A 118 ? 0.1974 0.1031 0.1278 0.0022  -0.0056 0.0063  124 VAL   A CA  
917  C C   . VAL   A 118 ? 0.2125 0.1158 0.1542 0.0029  0.0003  0.0058  124 VAL   A C   
918  O O   . VAL   A 118 ? 0.2168 0.1164 0.1544 0.0012  -0.0013 0.0016  124 VAL   A O   
919  C CB  . VAL   A 118 ? 0.2025 0.0998 0.1195 -0.0021 -0.0055 0.0004  124 VAL   A CB  
920  C CG1 . VAL   A 118 ? 0.2063 0.0974 0.1266 -0.0045 0.0044  -0.0032 124 VAL   A CG1 
921  C CG2 . VAL   A 118 ? 0.2173 0.1164 0.1262 -0.0024 -0.0103 0.0019  124 VAL   A CG2 
922  N N   . SER   A 119 ? 0.2202 0.1253 0.1780 0.0050  0.0075  0.0106  125 SER   A N   
923  C CA  . SER   A 119 ? 0.2353 0.1376 0.2096 0.0062  0.0151  0.0113  125 SER   A CA  
924  C C   . SER   A 119 ? 0.2547 0.1500 0.2444 0.0060  0.0283  0.0097  125 SER   A C   
925  O O   . SER   A 119 ? 0.2649 0.1518 0.2636 0.0044  0.0379  0.0042  125 SER   A O   
926  C CB  . SER   A 119 ? 0.2537 0.1679 0.2426 0.0094  0.0115  0.0228  125 SER   A CB  
927  O OG  . SER   A 119 ? 0.2757 0.1879 0.2835 0.0110  0.0184  0.0257  125 SER   A OG  
928  N N   . THR   A 120 ? 0.2551 0.1543 0.2512 0.0074  0.0300  0.0146  126 THR   A N   
929  C CA  . THR   A 120 ? 0.2716 0.1649 0.2876 0.0077  0.0441  0.0136  126 THR   A CA  
930  C C   . THR   A 120 ? 0.2994 0.1894 0.3030 0.0047  0.0458  0.0084  126 THR   A C   
931  O O   . THR   A 120 ? 0.2973 0.1921 0.2813 0.0038  0.0348  0.0093  126 THR   A O   
932  C CB  . THR   A 120 ? 0.2581 0.1632 0.3081 0.0137  0.0463  0.0306  126 THR   A CB  
933  O OG1 . THR   A 120 ? 0.2760 0.1939 0.3245 0.0146  0.0381  0.0405  126 THR   A OG1 
934  C CG2 . THR   A 120 ? 0.2385 0.1507 0.2992 0.0160  0.0416  0.0393  126 THR   A CG2 
935  N N   . GLY   A 121 ? 0.3074 0.1895 0.3255 0.0031  0.0606  0.0037  127 GLY   A N   
936  C CA  . GLY   A 121 ? 0.3438 0.2228 0.3515 -0.0004 0.0636  -0.0013 127 GLY   A CA  
937  C C   . GLY   A 121 ? 0.3652 0.2341 0.3929 -0.0030 0.0835  -0.0082 127 GLY   A C   
938  O O   . GLY   A 121 ? 0.3615 0.2230 0.4083 -0.0034 0.0964  -0.0121 127 GLY   A O   
939  N N   . GLY   A 122 ? 0.3876 0.2551 0.4094 -0.0058 0.0870  -0.0114 128 GLY   A N   
940  C CA  . GLY   A 122 ? 0.4004 0.2583 0.4402 -0.0095 0.1074  -0.0194 128 GLY   A CA  
941  C C   . GLY   A 122 ? 0.4145 0.2813 0.4697 -0.0048 0.1069  -0.0095 128 GLY   A C   
942  O O   . GLY   A 122 ? 0.4207 0.3029 0.4827 0.0023  0.0928  0.0065  128 GLY   A O   
943  N N   . ASN   A 123 ? 0.4150 0.2730 0.4744 -0.0103 0.1226  -0.0194 129 ASN   A N   
944  C CA  . ASN   A 123 ? 0.4063 0.2721 0.4849 -0.0062 0.1250  -0.0106 129 ASN   A CA  
945  C C   . ASN   A 123 ? 0.3870 0.2658 0.4424 -0.0042 0.1041  -0.0012 129 ASN   A C   
946  O O   . ASN   A 123 ? 0.3850 0.2776 0.4609 0.0017  0.0993  0.0135  129 ASN   A O   
947  C CB  . ASN   A 123 ? 0.4175 0.2922 0.5497 0.0036  0.1331  0.0058  129 ASN   A CB  
948  C CG  . ASN   A 123 ? 0.4808 0.3407 0.6448 0.0017  0.1592  -0.0041 129 ASN   A CG  
949  O OD1 . ASN   A 123 ? 0.5232 0.3675 0.6763 -0.0079 0.1765  -0.0236 129 ASN   A OD1 
950  N ND2 . ASN   A 123 ? 0.4761 0.3411 0.6821 0.0098  0.1638  0.0093  129 ASN   A ND2 
951  N N   . GLY   A 124 ? 0.3677 0.2426 0.3826 -0.0100 0.0925  -0.0093 130 GLY   A N   
952  C CA  . GLY   A 124 ? 0.3433 0.2275 0.3369 -0.0091 0.0754  -0.0029 130 GLY   A CA  
953  C C   . GLY   A 124 ? 0.3070 0.2053 0.3035 -0.0026 0.0595  0.0108  130 GLY   A C   
954  O O   . GLY   A 124 ? 0.2825 0.1892 0.2657 -0.0025 0.0476  0.0161  130 GLY   A O   
955  N N   . LEU   A 125 ? 0.2935 0.1940 0.3059 0.0012  0.0601  0.0153  131 LEU   A N   
956  C CA  . LEU   A 125 ? 0.2907 0.2042 0.3029 0.0049  0.0460  0.0268  131 LEU   A CA  
957  C C   . LEU   A 125 ? 0.3018 0.2086 0.2950 0.0034  0.0406  0.0194  131 LEU   A C   
958  O O   . LEU   A 125 ? 0.3246 0.2192 0.3163 0.0008  0.0495  0.0094  131 LEU   A O   
959  C CB  . LEU   A 125 ? 0.2906 0.2161 0.3400 0.0102  0.0488  0.0425  131 LEU   A CB  
960  C CG  . LEU   A 125 ? 0.3044 0.2411 0.3810 0.0121  0.0525  0.0548  131 LEU   A CG  
961  C CD1 . LEU   A 125 ? 0.3116 0.2628 0.4265 0.0166  0.0524  0.0740  131 LEU   A CD1 
962  C CD2 . LEU   A 125 ? 0.3048 0.2532 0.3624 0.0090  0.0398  0.0596  131 LEU   A CD2 
963  N N   . VAL   A 126 ? 0.2595 0.1746 0.2398 0.0039  0.0274  0.0241  132 VAL   A N   
964  C CA  . VAL   A 126 ? 0.2540 0.1647 0.2208 0.0033  0.0221  0.0191  132 VAL   A CA  
965  C C   . VAL   A 126 ? 0.2489 0.1734 0.2290 0.0062  0.0158  0.0310  132 VAL   A C   
966  O O   . VAL   A 126 ? 0.2572 0.1948 0.2410 0.0055  0.0102  0.0405  132 VAL   A O   
967  C CB  . VAL   A 126 ? 0.2738 0.1798 0.2127 -0.0003 0.0137  0.0119  132 VAL   A CB  
968  C CG1 . VAL   A 126 ? 0.2881 0.2030 0.2211 -0.0006 0.0066  0.0171  132 VAL   A CG1 
969  C CG2 . VAL   A 126 ? 0.2816 0.1849 0.2115 -0.0007 0.0080  0.0086  132 VAL   A CG2 
970  N N   . GLY   A 127 ? 0.2377 0.1600 0.2248 0.0077  0.0172  0.0307  133 GLY   A N   
971  C CA  . GLY   A 127 ? 0.2324 0.1675 0.2301 0.0088  0.0115  0.0417  133 GLY   A CA  
972  C C   . GLY   A 127 ? 0.2375 0.1698 0.2174 0.0073  0.0050  0.0352  133 GLY   A C   
973  O O   . GLY   A 127 ? 0.2349 0.1550 0.2055 0.0071  0.0075  0.0249  133 GLY   A O   
974  N N   . PHE   A 128 ? 0.2197 0.1641 0.1952 0.0048  -0.0027 0.0412  134 PHE   A N   
975  C CA  . PHE   A 128 ? 0.2166 0.1597 0.1781 0.0029  -0.0076 0.0352  134 PHE   A CA  
976  C C   . PHE   A 128 ? 0.2162 0.1698 0.1875 0.0015  -0.0096 0.0434  134 PHE   A C   
977  O O   . PHE   A 128 ? 0.2309 0.1995 0.2112 -0.0020 -0.0121 0.0556  134 PHE   A O   
978  C CB  . PHE   A 128 ? 0.2108 0.1577 0.1565 -0.0015 -0.0122 0.0321  134 PHE   A CB  
979  C CG  . PHE   A 128 ? 0.2090 0.1479 0.1458 -0.0009 -0.0112 0.0266  134 PHE   A CG  
980  C CD1 . PHE   A 128 ? 0.2096 0.1361 0.1360 0.0002  -0.0116 0.0176  134 PHE   A CD1 
981  C CD2 . PHE   A 128 ? 0.2202 0.1656 0.1594 -0.0026 -0.0108 0.0319  134 PHE   A CD2 
982  C CE1 . PHE   A 128 ? 0.2153 0.1355 0.1330 -0.0006 -0.0114 0.0141  134 PHE   A CE1 
983  C CE2 . PHE   A 128 ? 0.2256 0.1638 0.1557 -0.0027 -0.0098 0.0267  134 PHE   A CE2 
984  C CZ  . PHE   A 128 ? 0.2145 0.1398 0.1336 -0.0017 -0.0100 0.0179  134 PHE   A CZ  
985  N N   . ALA   A 129 ? 0.2097 0.1572 0.1791 0.0028  -0.0093 0.0378  135 ALA   A N   
986  C CA  . ALA   A 129 ? 0.2149 0.1716 0.1911 0.0006  -0.0113 0.0444  135 ALA   A CA  
987  C C   . ALA   A 129 ? 0.2144 0.1792 0.1756 -0.0064 -0.0158 0.0418  135 ALA   A C   
988  O O   . ALA   A 129 ? 0.2034 0.1601 0.1534 -0.0063 -0.0159 0.0309  135 ALA   A O   
989  C CB  . ALA   A 129 ? 0.2254 0.1720 0.2044 0.0039  -0.0085 0.0381  135 ALA   A CB  
990  N N   . ASP   A 130 ? 0.2039 0.1855 0.1664 -0.0139 -0.0189 0.0522  136 ASP   A N   
991  C CA  . ASP   A 130 ? 0.2151 0.2044 0.1620 -0.0239 -0.0206 0.0477  136 ASP   A CA  
992  C C   . ASP   A 130 ? 0.2284 0.2152 0.1724 -0.0255 -0.0192 0.0413  136 ASP   A C   
993  O O   . ASP   A 130 ? 0.2213 0.2087 0.1760 -0.0224 -0.0194 0.0469  136 ASP   A O   
994  C CB  . ASP   A 130 ? 0.2312 0.2420 0.1792 -0.0349 -0.0248 0.0622  136 ASP   A CB  
995  C CG  . ASP   A 130 ? 0.2804 0.3004 0.2096 -0.0494 -0.0246 0.0563  136 ASP   A CG  
996  O OD1 . ASP   A 130 ? 0.2790 0.2907 0.1963 -0.0507 -0.0212 0.0438  136 ASP   A OD1 
997  O OD2 . ASP   A 130 ? 0.3005 0.3360 0.2270 -0.0607 -0.0270 0.0639  136 ASP   A OD2 
998  N N   . VAL   A 131 ? 0.2269 0.2108 0.1586 -0.0309 -0.0165 0.0296  137 VAL   A N   
999  C CA  . VAL   A 131 ? 0.2190 0.2019 0.1494 -0.0341 -0.0137 0.0231  137 VAL   A CA  
1000 C C   . VAL   A 131 ? 0.2392 0.2322 0.1567 -0.0493 -0.0100 0.0180  137 VAL   A C   
1001 O O   . VAL   A 131 ? 0.2453 0.2383 0.1613 -0.0541 -0.0059 0.0115  137 VAL   A O   
1002 C CB  . VAL   A 131 ? 0.2065 0.1730 0.1405 -0.0252 -0.0112 0.0118  137 VAL   A CB  
1003 C CG1 . VAL   A 131 ? 0.2090 0.1665 0.1515 -0.0144 -0.0139 0.0151  137 VAL   A CG1 
1004 C CG2 . VAL   A 131 ? 0.2160 0.1753 0.1448 -0.0260 -0.0080 0.0025  137 VAL   A CG2 
1005 N N   . ARG   A 132 ? 0.2436 0.2455 0.1516 -0.0585 -0.0106 0.0203  138 ARG   A N   
1006 C CA  . ARG   A 132 ? 0.2409 0.2520 0.1338 -0.0763 -0.0052 0.0130  138 ARG   A CA  
1007 C C   . ARG   A 132 ? 0.2689 0.2978 0.1552 -0.0913 -0.0064 0.0200  138 ARG   A C   
1008 O O   . ARG   A 132 ? 0.2799 0.3137 0.1528 -0.1075 0.0008  0.0099  138 ARG   A O   
1009 C CB  . ARG   A 132 ? 0.2405 0.2582 0.1240 -0.0839 -0.0061 0.0147  138 ARG   A CB  
1010 C CG  . ARG   A 132 ? 0.2270 0.2274 0.1142 -0.0722 -0.0035 0.0062  138 ARG   A CG  
1011 C CD  . ARG   A 132 ? 0.2847 0.2939 0.1629 -0.0804 -0.0053 0.0100  138 ARG   A CD  
1012 N NE  . ARG   A 132 ? 0.2559 0.2748 0.1422 -0.0749 -0.0145 0.0275  138 ARG   A NE  
1013 C CZ  . ARG   A 132 ? 0.2586 0.2866 0.1420 -0.0794 -0.0180 0.0348  138 ARG   A CZ  
1014 N NH1 . ARG   A 132 ? 0.2575 0.2860 0.1272 -0.0901 -0.0135 0.0255  138 ARG   A NH1 
1015 N NH2 . ARG   A 132 ? 0.2577 0.2937 0.1545 -0.0731 -0.0248 0.0510  138 ARG   A NH2 
1016 N N   . ASP   A 133 ? 0.2677 0.3063 0.1640 -0.0876 -0.0146 0.0373  139 ASP   A N   
1017 C CA  . ASP   A 133 ? 0.2755 0.3324 0.1678 -0.1017 -0.0175 0.0474  139 ASP   A CA  
1018 C C   . ASP   A 133 ? 0.2765 0.3250 0.1727 -0.0981 -0.0129 0.0395  139 ASP   A C   
1019 O O   . ASP   A 133 ? 0.2833 0.3458 0.1731 -0.1118 -0.0135 0.0448  139 ASP   A O   
1020 C CB  . ASP   A 133 ? 0.3052 0.3771 0.2124 -0.0992 -0.0280 0.0723  139 ASP   A CB  
1021 C CG  . ASP   A 133 ? 0.3533 0.4113 0.2834 -0.0783 -0.0291 0.0768  139 ASP   A CG  
1022 O OD1 . ASP   A 133 ? 0.3470 0.3859 0.2805 -0.0644 -0.0254 0.0653  139 ASP   A OD1 
1023 O OD2 . ASP   A 133 ? 0.3701 0.4364 0.3145 -0.0772 -0.0332 0.0920  139 ASP   A OD2 
1024 N N   . LEU   A 134 ? 0.2673 0.2953 0.1739 -0.0812 -0.0091 0.0287  140 LEU   A N   
1025 C CA  . LEU   A 134 ? 0.2599 0.2793 0.1728 -0.0763 -0.0052 0.0215  140 LEU   A CA  
1026 C C   . LEU   A 134 ? 0.2698 0.2851 0.1734 -0.0864 0.0057  0.0033  140 LEU   A C   
1027 O O   . LEU   A 134 ? 0.2864 0.2858 0.1978 -0.0770 0.0114  -0.0092 140 LEU   A O   
1028 C CB  . LEU   A 134 ? 0.2456 0.2473 0.1734 -0.0563 -0.0066 0.0190  140 LEU   A CB  
1029 C CG  . LEU   A 134 ? 0.2567 0.2595 0.1962 -0.0468 -0.0135 0.0338  140 LEU   A CG  
1030 C CD1 . LEU   A 134 ? 0.2709 0.2561 0.2204 -0.0314 -0.0130 0.0282  140 LEU   A CD1 
1031 C CD2 . LEU   A 134 ? 0.2684 0.2835 0.2154 -0.0511 -0.0169 0.0480  140 LEU   A CD2 
1032 N N   . LEU   A 135 ? 0.2686 0.2986 0.1574 -0.1068 0.0094  0.0023  141 LEU   A N   
1033 C CA  . LEU   A 135 ? 0.2844 0.3099 0.1647 -0.1193 0.0233  -0.0173 141 LEU   A CA  
1034 C C   . LEU   A 135 ? 0.2851 0.2975 0.1791 -0.1112 0.0312  -0.0289 141 LEU   A C   
1035 O O   . LEU   A 135 ? 0.3168 0.3181 0.2156 -0.1126 0.0437  -0.0457 141 LEU   A O   
1036 C CB  . LEU   A 135 ? 0.2940 0.3396 0.1518 -0.1471 0.0267  -0.0170 141 LEU   A CB  
1037 C CG  . LEU   A 135 ? 0.3266 0.3898 0.1718 -0.1578 0.0171  -0.0023 141 LEU   A CG  
1038 C CD1 . LEU   A 135 ? 0.3558 0.4409 0.1765 -0.1889 0.0200  -0.0018 141 LEU   A CD1 
1039 C CD2 . LEU   A 135 ? 0.3366 0.3896 0.1826 -0.1510 0.0192  -0.0090 141 LEU   A CD2 
1040 N N   . TRP   A 136 ? 0.2657 0.2795 0.1682 -0.1033 0.0249  -0.0197 142 TRP   A N   
1041 C CA  . TRP   A 136 ? 0.2741 0.2777 0.1903 -0.0960 0.0307  -0.0285 142 TRP   A CA  
1042 C C   . TRP   A 136 ? 0.2894 0.2750 0.2242 -0.0779 0.0322  -0.0355 142 TRP   A C   
1043 O O   . TRP   A 136 ? 0.2914 0.2692 0.2402 -0.0735 0.0387  -0.0440 142 TRP   A O   
1044 C CB  . TRP   A 136 ? 0.2681 0.2779 0.1888 -0.0919 0.0226  -0.0155 142 TRP   A CB  
1045 C CG  . TRP   A 136 ? 0.2586 0.2674 0.1868 -0.0781 0.0105  -0.0001 142 TRP   A CG  
1046 C CD1 . TRP   A 136 ? 0.2561 0.2779 0.1803 -0.0822 0.0022  0.0167  142 TRP   A CD1 
1047 C CD2 . TRP   A 136 ? 0.2602 0.2550 0.2034 -0.0596 0.0068  0.0003  142 TRP   A CD2 
1048 N NE1 . TRP   A 136 ? 0.2622 0.2766 0.1998 -0.0663 -0.0043 0.0254  142 TRP   A NE1 
1049 C CE2 . TRP   A 136 ? 0.2579 0.2557 0.2045 -0.0534 -0.0015 0.0147  142 TRP   A CE2 
1050 C CE3 . TRP   A 136 ? 0.2655 0.2466 0.2204 -0.0490 0.0098  -0.0095 142 TRP   A CE3 
1051 C CZ2 . TRP   A 136 ? 0.2683 0.2546 0.2265 -0.0387 -0.0050 0.0168  142 TRP   A CZ2 
1052 C CZ3 . TRP   A 136 ? 0.2774 0.2495 0.2420 -0.0353 0.0038  -0.0053 142 TRP   A CZ3 
1053 C CH2 . TRP   A 136 ? 0.2737 0.2476 0.2381 -0.0309 -0.0026 0.0062  142 TRP   A CH2 
1054 N N   . LEU   A 137 ? 0.3012 0.2816 0.2372 -0.0685 0.0261  -0.0310 143 LEU   A N   
1055 C CA  . LEU   A 137 ? 0.3294 0.2952 0.2815 -0.0540 0.0261  -0.0353 143 LEU   A CA  
1056 C C   . LEU   A 137 ? 0.3721 0.3302 0.3340 -0.0582 0.0398  -0.0503 143 LEU   A C   
1057 O O   . LEU   A 137 ? 0.3665 0.3148 0.3485 -0.0477 0.0411  -0.0529 143 LEU   A O   
1058 C CB  . LEU   A 137 ? 0.3203 0.2832 0.2690 -0.0463 0.0180  -0.0279 143 LEU   A CB  
1059 C CG  . LEU   A 137 ? 0.3191 0.2839 0.2676 -0.0378 0.0071  -0.0149 143 LEU   A CG  
1060 C CD1 . LEU   A 137 ? 0.3208 0.2838 0.2649 -0.0333 0.0019  -0.0094 143 LEU   A CD1 
1061 C CD2 . LEU   A 137 ? 0.3132 0.2690 0.2754 -0.0263 0.0041  -0.0150 143 LEU   A CD2 
1062 N N   . ASP   A 138 ? 0.4107 0.3742 0.3603 -0.0751 0.0506  -0.0597 144 ASP   A N   
1063 C CA  . ASP   A 138 ? 0.4504 0.4060 0.4101 -0.0821 0.0677  -0.0763 144 ASP   A CA  
1064 C C   . ASP   A 138 ? 0.5062 0.4608 0.4765 -0.0887 0.0803  -0.0869 144 ASP   A C   
1065 O O   . ASP   A 138 ? 0.5139 0.4610 0.4970 -0.0950 0.0975  -0.1019 144 ASP   A O   
1066 C CB  . ASP   A 138 ? 0.4716 0.4339 0.4099 -0.1014 0.0758  -0.0838 144 ASP   A CB  
1067 C CG  . ASP   A 138 ? 0.5551 0.5193 0.4825 -0.0983 0.0661  -0.0753 144 ASP   A CG  
1068 O OD1 . ASP   A 138 ? 0.5626 0.5184 0.5025 -0.0806 0.0572  -0.0677 144 ASP   A OD1 
1069 O OD2 . ASP   A 138 ? 0.6031 0.5784 0.5089 -0.1147 0.0672  -0.0757 144 ASP   A OD2 
1070 N N   . GLU   A 139 ? 0.5381 0.5003 0.5040 -0.0888 0.0739  -0.0803 145 GLU   A N   
1071 C CA  . GLU   A 139 ? 0.5797 0.5426 0.5529 -0.0971 0.0863  -0.0906 145 GLU   A CA  
1072 C C   . GLU   A 139 ? 0.6114 0.5739 0.5985 -0.0841 0.0774  -0.0821 145 GLU   A C   
1073 O O   . GLU   A 139 ? 0.6118 0.5715 0.6048 -0.0686 0.0633  -0.0700 145 GLU   A O   
1074 C CB  . GLU   A 139 ? 0.6265 0.6036 0.5714 -0.1214 0.0920  -0.0948 145 GLU   A CB  
1075 C CG  . GLU   A 139 ? 0.6976 0.6892 0.6224 -0.1229 0.0743  -0.0761 145 GLU   A CG  
1076 C CD  . GLU   A 139 ? 0.7870 0.7958 0.6830 -0.1481 0.0762  -0.0753 145 GLU   A CD  
1077 O OE1 . GLU   A 139 ? 0.8102 0.8336 0.6947 -0.1532 0.0647  -0.0600 145 GLU   A OE1 
1078 O OE2 . GLU   A 139 ? 0.8007 0.8091 0.6867 -0.1641 0.0895  -0.0895 145 GLU   A OE2 
1079 N N   . GLU   A 140 ? 0.6380 0.6029 0.6300 -0.0919 0.0869  -0.0896 146 GLU   A N   
1080 C CA  . GLU   A 140 ? 0.6661 0.6317 0.6700 -0.0830 0.0808  -0.0834 146 GLU   A CA  
1081 C C   . GLU   A 140 ? 0.6770 0.6323 0.7112 -0.0645 0.0773  -0.0808 146 GLU   A C   
1082 O O   . GLU   A 140 ? 0.6798 0.6322 0.7360 -0.0623 0.0851  -0.0864 146 GLU   A O   
1083 C CB  . GLU   A 140 ? 0.7157 0.6910 0.7013 -0.0817 0.0647  -0.0675 146 GLU   A CB  
1084 C CG  . GLU   A 140 ? 0.8084 0.7828 0.8061 -0.0712 0.0574  -0.0606 146 GLU   A CG  
1085 C CD  . GLU   A 140 ? 0.9246 0.9063 0.9182 -0.0829 0.0641  -0.0642 146 GLU   A CD  
1086 O OE1 . GLU   A 140 ? 0.9481 0.9379 0.9303 -0.0852 0.0553  -0.0530 146 GLU   A OE1 
1087 O OE2 . GLU   A 140 ? 0.9670 0.9460 0.9708 -0.0899 0.0790  -0.0782 146 GLU   A OE2 
1088 N N   . SER   B 1   ? 0.3281 0.2555 0.2358 0.0219  -0.0349 0.0470  7   SER   C N   
1089 C CA  . SER   B 1   ? 0.3369 0.2677 0.2596 0.0174  -0.0373 0.0474  7   SER   C CA  
1090 C C   . SER   B 1   ? 0.3381 0.2677 0.2656 0.0133  -0.0386 0.0427  7   SER   C C   
1091 O O   . SER   B 1   ? 0.3564 0.2827 0.2753 0.0138  -0.0403 0.0387  7   SER   C O   
1092 C CB  . SER   B 1   ? 0.3707 0.3018 0.2939 0.0187  -0.0465 0.0488  7   SER   C CB  
1093 O OG  . SER   B 1   ? 0.4381 0.3649 0.3511 0.0202  -0.0550 0.0438  7   SER   C OG  
1094 N N   . GLY   B 2   ? 0.3160 0.2478 0.2569 0.0100  -0.0368 0.0439  8   GLY   C N   
1095 C CA  . GLY   B 2   ? 0.2998 0.2302 0.2455 0.0072  -0.0367 0.0411  8   GLY   C CA  
1096 C C   . GLY   B 2   ? 0.2808 0.2123 0.2363 0.0056  -0.0300 0.0431  8   GLY   C C   
1097 O O   . GLY   B 2   ? 0.2809 0.2134 0.2373 0.0063  -0.0248 0.0445  8   GLY   C O   
1098 N N   . ALA   B 3   ? 0.2732 0.2036 0.2363 0.0041  -0.0298 0.0434  9   ALA   C N   
1099 C CA  . ALA   B 3   ? 0.2599 0.1895 0.2294 0.0041  -0.0227 0.0455  9   ALA   C CA  
1100 C C   . ALA   B 3   ? 0.2478 0.1740 0.2164 0.0043  -0.0204 0.0442  9   ALA   C C   
1101 O O   . ALA   B 3   ? 0.2704 0.1957 0.2385 0.0035  -0.0249 0.0424  9   ALA   C O   
1102 C CB  . ALA   B 3   ? 0.2633 0.1952 0.2473 0.0036  -0.0219 0.0507  9   ALA   C CB  
1103 N N   . ILE   B 4   ? 0.2315 0.1550 0.1986 0.0061  -0.0135 0.0449  10  ILE   C N   
1104 C CA  . ILE   B 4   ? 0.2379 0.1575 0.2036 0.0078  -0.0096 0.0454  10  ILE   C CA  
1105 C C   . ILE   B 4   ? 0.2565 0.1753 0.2356 0.0088  -0.0039 0.0517  10  ILE   C C   
1106 O O   . ILE   B 4   ? 0.2644 0.1834 0.2463 0.0098  0.0002  0.0537  10  ILE   C O   
1107 C CB  . ILE   B 4   ? 0.2410 0.1563 0.1930 0.0110  -0.0058 0.0420  10  ILE   C CB  
1108 C CG1 . ILE   B 4   ? 0.2437 0.1602 0.1865 0.0101  -0.0104 0.0365  10  ILE   C CG1 
1109 C CG2 . ILE   B 4   ? 0.2543 0.1650 0.2026 0.0139  -0.0018 0.0434  10  ILE   C CG2 
1110 C CD1 . ILE   B 4   ? 0.2474 0.1602 0.1805 0.0132  -0.0084 0.0325  10  ILE   C CD1 
1111 N N   . TYR   B 5   ? 0.2600 0.1776 0.2490 0.0088  -0.0026 0.0550  11  TYR   C N   
1112 C CA  . TYR   B 5   ? 0.2594 0.1762 0.2646 0.0101  0.0040  0.0621  11  TYR   C CA  
1113 C C   . TYR   B 5   ? 0.2791 0.1897 0.2794 0.0148  0.0132  0.0651  11  TYR   C C   
1114 O O   . TYR   B 5   ? 0.2861 0.1956 0.2900 0.0147  0.0125  0.0658  11  TYR   C O   
1115 C CB  . TYR   B 5   ? 0.2554 0.1760 0.2823 0.0065  -0.0025 0.0648  11  TYR   C CB  
1116 C CG  . TYR   B 5   ? 0.2486 0.1742 0.2785 0.0035  -0.0111 0.0629  11  TYR   C CG  
1117 C CD1 . TYR   B 5   ? 0.2678 0.1957 0.3074 0.0037  -0.0082 0.0672  11  TYR   C CD1 
1118 C CD2 . TYR   B 5   ? 0.2547 0.1821 0.2761 0.0015  -0.0213 0.0572  11  TYR   C CD2 
1119 C CE1 . TYR   B 5   ? 0.2740 0.2063 0.3152 0.0020  -0.0158 0.0662  11  TYR   C CE1 
1120 C CE2 . TYR   B 5   ? 0.2727 0.2037 0.2942 0.0004  -0.0285 0.0563  11  TYR   C CE2 
1121 C CZ  . TYR   B 5   ? 0.2884 0.2221 0.3196 0.0006  -0.0259 0.0609  11  TYR   C CZ  
1122 O OH  . TYR   B 5   ? 0.3359 0.2729 0.3658 0.0003  -0.0326 0.0607  11  TYR   C OH  
1123 N N   . VAL   B 6   ? 0.2721 0.1779 0.2622 0.0197  0.0218  0.0666  12  VAL   C N   
1124 C CA  . VAL   B 6   ? 0.2937 0.1922 0.2740 0.0263  0.0312  0.0696  12  VAL   C CA  
1125 C C   . VAL   B 6   ? 0.3060 0.2003 0.2935 0.0311  0.0431  0.0772  12  VAL   C C   
1126 O O   . VAL   B 6   ? 0.3072 0.2015 0.2928 0.0314  0.0443  0.0761  12  VAL   C O   
1127 C CB  . VAL   B 6   ? 0.3096 0.2037 0.2641 0.0298  0.0295  0.0626  12  VAL   C CB  
1128 C CG1 . VAL   B 6   ? 0.3263 0.2205 0.2726 0.0296  0.0273  0.0575  12  VAL   C CG1 
1129 C CG2 . VAL   B 6   ? 0.3240 0.2094 0.2652 0.0381  0.0388  0.0660  12  VAL   C CG2 
1130 N N   . GLY   B 7   ? 0.3131 0.2040 0.3121 0.0347  0.0523  0.0856  13  GLY   C N   
1131 C CA  . GLY   B 7   ? 0.3152 0.2017 0.3233 0.0400  0.0655  0.0942  13  GLY   C CA  
1132 C C   . GLY   B 7   ? 0.3142 0.2069 0.3434 0.0351  0.0631  0.0963  13  GLY   C C   
1133 O O   . GLY   B 7   ? 0.3008 0.2011 0.3494 0.0281  0.0536  0.0958  13  GLY   C O   
1134 N N   . ASN   B 8   ? 0.3162 0.2052 0.3398 0.0389  0.0702  0.0976  14  ASN   C N   
1135 C CA  . ASN   B 8   ? 0.3147 0.2098 0.3576 0.0344  0.0676  0.0996  14  ASN   C CA  
1136 C C   . ASN   B 8   ? 0.3003 0.1985 0.3288 0.0310  0.0583  0.0906  14  ASN   C C   
1137 O O   . ASN   B 8   ? 0.3069 0.2064 0.3413 0.0306  0.0602  0.0917  14  ASN   C O   
1138 C CB  . ASN   B 8   ? 0.3542 0.2447 0.4093 0.0398  0.0821  0.1089  14  ASN   C CB  
1139 C CG  . ASN   B 8   ? 0.4269 0.3177 0.5093 0.0407  0.0895  0.1196  14  ASN   C CG  
1140 O OD1 . ASN   B 8   ? 0.4424 0.3404 0.5558 0.0354  0.0854  0.1242  14  ASN   C OD1 
1141 N ND2 . ASN   B 8   ? 0.4463 0.3293 0.5188 0.0478  0.1001  0.1238  14  ASN   C ND2 
1142 N N   . TYR   B 9   ? 0.2891 0.1890 0.3019 0.0284  0.0486  0.0825  15  TYR   C N   
1143 C CA  . TYR   B 9   ? 0.2816 0.1844 0.2827 0.0254  0.0403  0.0745  15  TYR   C CA  
1144 C C   . TYR   B 9   ? 0.2550 0.1656 0.2611 0.0189  0.0278  0.0708  15  TYR   C C   
1145 O O   . TYR   B 9   ? 0.2402 0.1516 0.2474 0.0174  0.0239  0.0704  15  TYR   C O   
1146 C CB  . TYR   B 9   ? 0.2986 0.1944 0.2736 0.0301  0.0412  0.0674  15  TYR   C CB  
1147 C CG  . TYR   B 9   ? 0.3317 0.2178 0.2956 0.0382  0.0524  0.0692  15  TYR   C CG  
1148 C CD1 . TYR   B 9   ? 0.3453 0.2297 0.3130 0.0396  0.0571  0.0700  15  TYR   C CD1 
1149 C CD2 . TYR   B 9   ? 0.3613 0.2389 0.3094 0.0454  0.0587  0.0701  15  TYR   C CD2 
1150 C CE1 . TYR   B 9   ? 0.3769 0.2509 0.3323 0.0479  0.0677  0.0710  15  TYR   C CE1 
1151 C CE2 . TYR   B 9   ? 0.3855 0.2524 0.3193 0.0545  0.0692  0.0715  15  TYR   C CE2 
1152 C CZ  . TYR   B 9   ? 0.4139 0.2787 0.3507 0.0558  0.0735  0.0715  15  TYR   C CZ  
1153 O OH  . TYR   B 9   ? 0.4632 0.3162 0.3846 0.0655  0.0842  0.0722  15  TYR   C OH  
1154 N N   . ARG   B 10  ? 0.2391 0.1542 0.2454 0.0158  0.0220  0.0678  16  ARG   C N   
1155 C CA  . ARG   B 10  ? 0.2419 0.1629 0.2474 0.0113  0.0113  0.0640  16  ARG   C CA  
1156 C C   . ARG   B 10  ? 0.2463 0.1663 0.2368 0.0119  0.0100  0.0578  16  ARG   C C   
1157 O O   . ARG   B 10  ? 0.2483 0.1675 0.2399 0.0131  0.0138  0.0580  16  ARG   C O   
1158 C CB  . ARG   B 10  ? 0.2524 0.1796 0.2750 0.0083  0.0066  0.0682  16  ARG   C CB  
1159 C CG  . ARG   B 10  ? 0.2592 0.1910 0.2769 0.0057  -0.0029 0.0648  16  ARG   C CG  
1160 C CD  . ARG   B 10  ? 0.2414 0.1784 0.2747 0.0039  -0.0094 0.0691  16  ARG   C CD  
1161 N NE  . ARG   B 10  ? 0.2558 0.1962 0.2843 0.0039  -0.0130 0.0687  16  ARG   C NE  
1162 C CZ  . ARG   B 10  ? 0.2604 0.2024 0.2797 0.0037  -0.0211 0.0660  16  ARG   C CZ  
1163 N NH1 . ARG   B 10  ? 0.2522 0.1928 0.2659 0.0030  -0.0273 0.0623  16  ARG   C NH1 
1164 N NH2 . ARG   B 10  ? 0.2503 0.1946 0.2650 0.0049  -0.0221 0.0670  16  ARG   C NH2 
1165 N N   . VAL   B 11  ? 0.2406 0.1601 0.2191 0.0114  0.0053  0.0525  17  VAL   C N   
1166 C CA  . VAL   B 11  ? 0.2285 0.1473 0.1966 0.0119  0.0036  0.0467  17  VAL   C CA  
1167 C C   . VAL   B 11  ? 0.2267 0.1508 0.1965 0.0089  -0.0027 0.0460  17  VAL   C C   
1168 O O   . VAL   B 11  ? 0.2397 0.1652 0.2074 0.0075  -0.0075 0.0455  17  VAL   C O   
1169 C CB  . VAL   B 11  ? 0.2693 0.1830 0.2235 0.0144  0.0034  0.0417  17  VAL   C CB  
1170 C CG1 . VAL   B 11  ? 0.2947 0.2072 0.2426 0.0151  0.0014  0.0356  17  VAL   C CG1 
1171 C CG2 . VAL   B 11  ? 0.2858 0.1931 0.2355 0.0188  0.0102  0.0438  17  VAL   C CG2 
1172 N N   . VAL   B 12  ? 0.2219 0.1484 0.1956 0.0085  -0.0022 0.0465  18  VAL   C N   
1173 C CA  A VAL   B 12  ? 0.2181 0.1488 0.1920 0.0073  -0.0064 0.0472  18  VAL   C CA  
1174 C CA  B VAL   B 12  ? 0.2313 0.1621 0.2054 0.0073  -0.0064 0.0473  18  VAL   C CA  
1175 C C   . VAL   B 12  ? 0.2226 0.1532 0.1959 0.0081  -0.0043 0.0447  18  VAL   C C   
1176 O O   . VAL   B 12  ? 0.2184 0.1461 0.1937 0.0091  -0.0008 0.0422  18  VAL   C O   
1177 C CB  A VAL   B 12  ? 0.2083 0.1431 0.1919 0.0067  -0.0077 0.0530  18  VAL   C CB  
1178 C CB  B VAL   B 12  ? 0.2491 0.1837 0.2336 0.0067  -0.0073 0.0533  18  VAL   C CB  
1179 C CG1 A VAL   B 12  ? 0.2202 0.1558 0.2081 0.0056  -0.0121 0.0552  18  VAL   C CG1 
1180 C CG1 B VAL   B 12  ? 0.2562 0.1942 0.2388 0.0071  -0.0109 0.0551  18  VAL   C CG1 
1181 C CG2 A VAL   B 12  ? 0.1824 0.1173 0.1756 0.0074  -0.0019 0.0560  18  VAL   C CG2 
1182 C CG2 B VAL   B 12  ? 0.2613 0.1961 0.2514 0.0057  -0.0101 0.0557  18  VAL   C CG2 
1183 N N   . ASN   B 13  ? 0.2187 0.1518 0.1902 0.0082  -0.0063 0.0453  19  ASN   C N   
1184 C CA  . ASN   B 13  ? 0.2024 0.1359 0.1787 0.0091  -0.0032 0.0446  19  ASN   C CA  
1185 C C   . ASN   B 13  ? 0.1898 0.1250 0.1772 0.0093  0.0007  0.0487  19  ASN   C C   
1186 O O   . ASN   B 13  ? 0.1953 0.1332 0.1849 0.0093  -0.0001 0.0539  19  ASN   C O   
1187 C CB  . ASN   B 13  ? 0.2201 0.1558 0.1934 0.0103  -0.0038 0.0472  19  ASN   C CB  
1188 C CG  . ASN   B 13  ? 0.2221 0.1560 0.1854 0.0103  -0.0070 0.0434  19  ASN   C CG  
1189 O OD1 . ASN   B 13  ? 0.2509 0.1844 0.2060 0.0102  -0.0110 0.0435  19  ASN   C OD1 
1190 N ND2 . ASN   B 13  ? 0.2212 0.1536 0.1866 0.0104  -0.0058 0.0396  19  ASN   C ND2 
1191 N N   . ARG   B 14  ? 0.2094 0.1427 0.2043 0.0096  0.0041  0.0461  20  ARG   C N   
1192 C CA  . ARG   B 14  ? 0.2129 0.1472 0.2192 0.0100  0.0084  0.0497  20  ARG   C CA  
1193 C C   . ARG   B 14  ? 0.2236 0.1627 0.2357 0.0108  0.0099  0.0569  20  ARG   C C   
1194 O O   . ARG   B 14  ? 0.2548 0.1962 0.2729 0.0111  0.0114  0.0623  20  ARG   C O   
1195 C CB  . ARG   B 14  ? 0.2262 0.1566 0.2397 0.0106  0.0107  0.0441  20  ARG   C CB  
1196 C CG  . ARG   B 14  ? 0.2324 0.1623 0.2577 0.0111  0.0155  0.0465  20  ARG   C CG  
1197 C CD  . ARG   B 14  ? 0.2229 0.1487 0.2573 0.0118  0.0163  0.0401  20  ARG   C CD  
1198 N NE  . ARG   B 14  ? 0.2332 0.1568 0.2780 0.0126  0.0209  0.0406  20  ARG   C NE  
1199 C CZ  . ARG   B 14  ? 0.2524 0.1798 0.3125 0.0124  0.0253  0.0465  20  ARG   C CZ  
1200 N NH1 . ARG   B 14  ? 0.2457 0.1787 0.3108 0.0121  0.0261  0.0529  20  ARG   C NH1 
1201 N NH2 . ARG   B 14  ? 0.2690 0.1934 0.3390 0.0133  0.0294  0.0461  20  ARG   C NH2 
1202 N N   . HIS   B 15  ? 0.2245 0.1649 0.2338 0.0119  0.0096  0.0578  21  HIS   C N   
1203 C CA  . HIS   B 15  ? 0.2357 0.1794 0.2477 0.0145  0.0122  0.0656  21  HIS   C CA  
1204 C C   . HIS   B 15  ? 0.2476 0.1932 0.2491 0.0157  0.0074  0.0698  21  HIS   C C   
1205 O O   . HIS   B 15  ? 0.2673 0.2150 0.2682 0.0188  0.0084  0.0764  21  HIS   C O   
1206 C CB  . HIS   B 15  ? 0.2433 0.1868 0.2565 0.0166  0.0155  0.0665  21  HIS   C CB  
1207 C CG  . HIS   B 15  ? 0.2580 0.2001 0.2566 0.0174  0.0119  0.0642  21  HIS   C CG  
1208 N ND1 . HIS   B 15  ? 0.2823 0.2220 0.2785 0.0153  0.0093  0.0570  21  HIS   C ND1 
1209 C CD2 . HIS   B 15  ? 0.2639 0.2060 0.2497 0.0208  0.0108  0.0682  21  HIS   C CD2 
1210 C CE1 . HIS   B 15  ? 0.2943 0.2332 0.2779 0.0168  0.0071  0.0570  21  HIS   C CE1 
1211 N NE2 . HIS   B 15  ? 0.2691 0.2088 0.2454 0.0203  0.0080  0.0633  21  HIS   C NE2 
1212 N N   . LEU   B 16  ? 0.2347 0.1789 0.2277 0.0138  0.0017  0.0659  22  LEU   C N   
1213 C CA  . LEU   B 16  ? 0.2398 0.1853 0.2260 0.0145  -0.0048 0.0685  22  LEU   C CA  
1214 C C   . LEU   B 16  ? 0.2530 0.1996 0.2484 0.0122  -0.0065 0.0696  22  LEU   C C   
1215 O O   . LEU   B 16  ? 0.2530 0.2006 0.2471 0.0122  -0.0131 0.0711  22  LEU   C O   
1216 C CB  . LEU   B 16  ? 0.2407 0.1838 0.2135 0.0144  -0.0102 0.0639  22  LEU   C CB  
1217 C CG  . LEU   B 16  ? 0.2641 0.2056 0.2271 0.0175  -0.0083 0.0636  22  LEU   C CG  
1218 C CD1 . LEU   B 16  ? 0.2768 0.2154 0.2276 0.0171  -0.0135 0.0584  22  LEU   C CD1 
1219 C CD2 . LEU   B 16  ? 0.2550 0.1973 0.2127 0.0226  -0.0077 0.0703  22  LEU   C CD2 
1220 N N   . ALA   B 17  ? 0.2524 0.1981 0.2578 0.0108  -0.0008 0.0688  23  ALA   C N   
1221 C CA  . ALA   B 17  ? 0.2567 0.2026 0.2715 0.0095  0.0000  0.0707  23  ALA   C CA  
1222 C C   . ALA   B 17  ? 0.2622 0.2122 0.2859 0.0104  -0.0022 0.0779  23  ALA   C C   
1223 O O   . ALA   B 17  ? 0.2785 0.2306 0.3039 0.0124  -0.0003 0.0818  23  ALA   C O   
1224 C CB  . ALA   B 17  ? 0.2561 0.1988 0.2770 0.0093  0.0072  0.0684  23  ALA   C CB  
1225 N N   . THR   B 18  ? 0.2605 0.2117 0.2911 0.0093  -0.0062 0.0800  24  THR   C N   
1226 C CA  . THR   B 18  ? 0.2575 0.2128 0.2984 0.0103  -0.0101 0.0866  24  THR   C CA  
1227 C C   . THR   B 18  ? 0.2531 0.2092 0.3108 0.0098  -0.0024 0.0911  24  THR   C C   
1228 O O   . THR   B 18  ? 0.2526 0.2050 0.3118 0.0091  0.0051  0.0882  24  THR   C O   
1229 C CB  . THR   B 18  ? 0.2602 0.2163 0.3050 0.0090  -0.0195 0.0864  24  THR   C CB  
1230 O OG1 . THR   B 18  ? 0.2600 0.2142 0.3153 0.0069  -0.0147 0.0859  24  THR   C OG1 
1231 C CG2 . THR   B 18  ? 0.2816 0.2360 0.3103 0.0097  -0.0277 0.0814  24  THR   C CG2 
1232 N N   . HIS   B 19  ? 0.2577 0.2179 0.3279 0.0108  -0.0049 0.0979  25  HIS   C N   
1233 C CA  . HIS   B 19  ? 0.2637 0.2245 0.3516 0.0104  0.0025  0.1026  25  HIS   C CA  
1234 C C   . HIS   B 19  ? 0.2574 0.2153 0.3532 0.0087  0.0055  0.1014  25  HIS   C C   
1235 O O   . HIS   B 19  ? 0.2749 0.2291 0.3750 0.0092  0.0153  0.1012  25  HIS   C O   
1236 C CB  . HIS   B 19  ? 0.2833 0.2495 0.3847 0.0118  -0.0023 0.1106  25  HIS   C CB  
1237 C CG  . HIS   B 19  ? 0.3251 0.2922 0.4479 0.0112  0.0042  0.1161  25  HIS   C CG  
1238 N ND1 . HIS   B 19  ? 0.3521 0.3186 0.4819 0.0123  0.0140  0.1190  25  HIS   C ND1 
1239 C CD2 . HIS   B 19  ? 0.3476 0.3155 0.4870 0.0099  0.0030  0.1192  25  HIS   C CD2 
1240 C CE1 . HIS   B 19  ? 0.3575 0.3243 0.5060 0.0119  0.0185  0.1237  25  HIS   C CE1 
1241 N NE2 . HIS   B 19  ? 0.3632 0.3310 0.5188 0.0106  0.0127  0.1245  25  HIS   C NE2 
1242 N N   . ASN   B 20  ? 0.2446 0.2032 0.3413 0.0075  -0.0023 0.1005  26  ASN   C N   
1243 C CA  . ASN   B 20  ? 0.2525 0.2082 0.3587 0.0065  0.0018  0.1008  26  ASN   C CA  
1244 C C   . ASN   B 20  ? 0.2509 0.2001 0.3426 0.0072  0.0104  0.0951  26  ASN   C C   
1245 O O   . ASN   B 20  ? 0.2545 0.1996 0.3518 0.0086  0.0198  0.0967  26  ASN   C O   
1246 C CB  . ASN   B 20  ? 0.2781 0.2356 0.3899 0.0049  -0.0086 0.1004  26  ASN   C CB  
1247 C CG  . ASN   B 20  ? 0.3601 0.3152 0.4879 0.0043  -0.0029 0.1032  26  ASN   C CG  
1248 O OD1 . ASN   B 20  ? 0.3810 0.3377 0.5307 0.0045  0.0011  0.1100  26  ASN   C OD1 
1249 N ND2 . ASN   B 20  ? 0.3631 0.3142 0.4815 0.0040  -0.0014 0.0989  26  ASN   C ND2 
1250 N N   . ASP   B 21  ? 0.2335 0.1813 0.3063 0.0072  0.0076  0.0887  27  ASP   C N   
1251 C CA  . ASP   B 21  ? 0.2316 0.1732 0.2907 0.0083  0.0138  0.0827  27  ASP   C CA  
1252 C C   . ASP   B 21  ? 0.2297 0.1678 0.2910 0.0103  0.0233  0.0828  27  ASP   C C   
1253 O O   . ASP   B 21  ? 0.2480 0.1798 0.3056 0.0126  0.0305  0.0810  27  ASP   C O   
1254 C CB  . ASP   B 21  ? 0.2443 0.1858 0.2865 0.0078  0.0086  0.0765  27  ASP   C CB  
1255 C CG  . ASP   B 21  ? 0.2545 0.1969 0.2906 0.0065  0.0007  0.0745  27  ASP   C CG  
1256 O OD1 . ASP   B 21  ? 0.2669 0.2074 0.3074 0.0062  0.0015  0.0751  27  ASP   C OD1 
1257 O OD2 . ASP   B 21  ? 0.2554 0.1999 0.2827 0.0063  -0.0056 0.0725  27  ASP   C OD2 
1258 N N   . TRP   B 22  ? 0.2127 0.1539 0.2791 0.0103  0.0235  0.0847  28  TRP   C N   
1259 C CA  . TRP   B 22  ? 0.2135 0.1513 0.2844 0.0121  0.0318  0.0844  28  TRP   C CA  
1260 C C   . TRP   B 22  ? 0.2154 0.1513 0.3001 0.0135  0.0392  0.0902  28  TRP   C C   
1261 O O   . TRP   B 22  ? 0.2283 0.1576 0.3113 0.0163  0.0476  0.0880  28  TRP   C O   
1262 C CB  . TRP   B 22  ? 0.2134 0.1558 0.2904 0.0117  0.0306  0.0870  28  TRP   C CB  
1263 C CG  . TRP   B 22  ? 0.2171 0.1589 0.2831 0.0115  0.0281  0.0813  28  TRP   C CG  
1264 C CD1 . TRP   B 22  ? 0.2266 0.1725 0.2865 0.0110  0.0219  0.0821  28  TRP   C CD1 
1265 C CD2 . TRP   B 22  ? 0.2174 0.1536 0.2786 0.0124  0.0317  0.0741  28  TRP   C CD2 
1266 N NE1 . TRP   B 22  ? 0.2319 0.1757 0.2859 0.0113  0.0228  0.0769  28  TRP   C NE1 
1267 C CE2 . TRP   B 22  ? 0.2296 0.1676 0.2847 0.0118  0.0276  0.0713  28  TRP   C CE2 
1268 C CE3 . TRP   B 22  ? 0.2219 0.1509 0.2830 0.0143  0.0374  0.0693  28  TRP   C CE3 
1269 C CZ2 . TRP   B 22  ? 0.2345 0.1687 0.2882 0.0122  0.0287  0.0645  28  TRP   C CZ2 
1270 C CZ3 . TRP   B 22  ? 0.2365 0.1608 0.2925 0.0150  0.0370  0.0611  28  TRP   C CZ3 
1271 C CH2 . TRP   B 22  ? 0.2402 0.1677 0.2949 0.0136  0.0325  0.0590  28  TRP   C CH2 
1272 N N   . ALA   B 23  ? 0.1984 0.1397 0.2974 0.0122  0.0359  0.0972  29  ALA   C N   
1273 C CA  . ALA   B 23  ? 0.2238 0.1640 0.3400 0.0136  0.0431  0.1040  29  ALA   C CA  
1274 C C   . ALA   B 23  ? 0.2483 0.1817 0.3600 0.0159  0.0498  0.1030  29  ALA   C C   
1275 O O   . ALA   B 23  ? 0.2696 0.1998 0.3935 0.0184  0.0591  0.1086  29  ALA   C O   
1276 C CB  . ALA   B 23  ? 0.2355 0.1837 0.3707 0.0115  0.0357  0.1115  29  ALA   C CB  
1277 N N   . ASN   B 24  ? 0.2467 0.1775 0.3416 0.0156  0.0458  0.0970  30  ASN   C N   
1278 C CA  . ASN   B 24  ? 0.2564 0.1804 0.3444 0.0186  0.0521  0.0964  30  ASN   C CA  
1279 C C   . ASN   B 24  ? 0.2565 0.1740 0.3191 0.0207  0.0521  0.0869  30  ASN   C C   
1280 O O   . ASN   B 24  ? 0.2632 0.1777 0.3149 0.0217  0.0511  0.0843  30  ASN   C O   
1281 C CB  . ASN   B 24  ? 0.2807 0.2091 0.3781 0.0160  0.0456  0.0995  30  ASN   C CB  
1282 C CG  . ASN   B 24  ? 0.3159 0.2497 0.4409 0.0144  0.0450  0.1084  30  ASN   C CG  
1283 O OD1 . ASN   B 24  ? 0.3319 0.2626 0.4709 0.0171  0.0548  0.1148  30  ASN   C OD1 
1284 N ND2 . ASN   B 24  ? 0.3364 0.2781 0.4701 0.0108  0.0335  0.1093  30  ASN   C ND2 
1285 N N   . LEU   B 25  ? 0.2566 0.1716 0.3117 0.0216  0.0532  0.0819  31  LEU   C N   
1286 C CA  . LEU   B 25  ? 0.2718 0.1813 0.3069 0.0233  0.0511  0.0723  31  LEU   C CA  
1287 C C   . LEU   B 25  ? 0.2935 0.1921 0.3122 0.0294  0.0579  0.0689  31  LEU   C C   
1288 O O   . LEU   B 25  ? 0.3049 0.1970 0.3250 0.0340  0.0675  0.0717  31  LEU   C O   
1289 C CB  . LEU   B 25  ? 0.2826 0.1918 0.3195 0.0230  0.0509  0.0684  31  LEU   C CB  
1290 C CG  . LEU   B 25  ? 0.3085 0.2135 0.3303 0.0238  0.0463  0.0582  31  LEU   C CG  
1291 C CD1 . LEU   B 25  ? 0.3076 0.2189 0.3255 0.0199  0.0374  0.0566  31  LEU   C CD1 
1292 C CD2 . LEU   B 25  ? 0.3290 0.2324 0.3570 0.0240  0.0474  0.0545  31  LEU   C CD2 
1293 N N   . VAL   B 26  ? 0.2839 0.1796 0.2856 0.0302  0.0530  0.0626  32  VAL   C N   
1294 C CA  . VAL   B 26  ? 0.2971 0.1817 0.2791 0.0371  0.0579  0.0583  32  VAL   C CA  
1295 C C   . VAL   B 26  ? 0.2938 0.1734 0.2613 0.0386  0.0523  0.0472  32  VAL   C C   
1296 O O   . VAL   B 26  ? 0.2966 0.1657 0.2512 0.0450  0.0565  0.0422  32  VAL   C O   
1297 C CB  . VAL   B 26  ? 0.3044 0.1887 0.2786 0.0378  0.0566  0.0600  32  VAL   C CB  
1298 C CG1 . VAL   B 26  ? 0.3369 0.2091 0.2869 0.0460  0.0606  0.0551  32  VAL   C CG1 
1299 C CG2 . VAL   B 26  ? 0.2941 0.1825 0.2861 0.0366  0.0620  0.0706  32  VAL   C CG2 
1300 N N   . TRP   B 27  ? 0.2799 0.1664 0.2499 0.0333  0.0427  0.0432  33  TRP   C N   
1301 C CA  . TRP   B 27  ? 0.2880 0.1709 0.2495 0.0341  0.0363  0.0331  33  TRP   C CA  
1302 C C   . TRP   B 27  ? 0.2853 0.1778 0.2580 0.0276  0.0288  0.0326  33  TRP   C C   
1303 O O   . TRP   B 27  ? 0.2664 0.1662 0.2433 0.0239  0.0263  0.0375  33  TRP   C O   
1304 C CB  . TRP   B 27  ? 0.3033 0.1784 0.2434 0.0390  0.0336  0.0271  33  TRP   C CB  
1305 C CG  . TRP   B 27  ? 0.3145 0.1870 0.2477 0.0393  0.0245  0.0166  33  TRP   C CG  
1306 C CD1 . TRP   B 27  ? 0.3389 0.2026 0.2650 0.0437  0.0221  0.0075  33  TRP   C CD1 
1307 C CD2 . TRP   B 27  ? 0.3129 0.1910 0.2465 0.0354  0.0162  0.0139  33  TRP   C CD2 
1308 N NE1 . TRP   B 27  ? 0.3393 0.2033 0.2635 0.0426  0.0120  -0.0006 33  TRP   C NE1 
1309 C CE2 . TRP   B 27  ? 0.3218 0.1950 0.2516 0.0373  0.0090  0.0037  33  TRP   C CE2 
1310 C CE3 . TRP   B 27  ? 0.3133 0.1999 0.2518 0.0306  0.0139  0.0190  33  TRP   C CE3 
1311 C CZ2 . TRP   B 27  ? 0.3216 0.1984 0.2531 0.0346  0.0006  -0.0006 33  TRP   C CZ2 
1312 C CZ3 . TRP   B 27  ? 0.3055 0.1952 0.2436 0.0282  0.0062  0.0145  33  TRP   C CZ3 
1313 C CH2 . TRP   B 27  ? 0.3105 0.1955 0.2458 0.0302  0.0002  0.0053  33  TRP   C CH2 
1314 N N   . GLU   B 28  ? 0.2779 0.1699 0.2562 0.0269  0.0256  0.0268  34  GLU   C N   
1315 C CA  . GLU   B 28  ? 0.2785 0.1787 0.2676 0.0220  0.0203  0.0272  34  GLU   C CA  
1316 C C   . GLU   B 28  ? 0.2762 0.1726 0.2664 0.0228  0.0152  0.0179  34  GLU   C C   
1317 O O   . GLU   B 28  ? 0.2839 0.1725 0.2725 0.0263  0.0159  0.0117  34  GLU   C O   
1318 C CB  . GLU   B 28  ? 0.2839 0.1917 0.2902 0.0188  0.0237  0.0353  34  GLU   C CB  
1319 C CG  . GLU   B 28  ? 0.2938 0.1984 0.3104 0.0203  0.0290  0.0353  34  GLU   C CG  
1320 C CD  . GLU   B 28  ? 0.3164 0.2199 0.3437 0.0199  0.0272  0.0298  34  GLU   C CD  
1321 O OE1 . GLU   B 28  ? 0.3451 0.2429 0.3774 0.0222  0.0305  0.0265  34  GLU   C OE1 
1322 O OE2 . GLU   B 28  ? 0.2774 0.1853 0.3095 0.0175  0.0228  0.0289  34  GLU   C OE2 
1323 N N   . ASP   B 29  ? 0.2582 0.1595 0.2526 0.0199  0.0099  0.0168  35  ASP   C N   
1324 C CA  . ASP   B 29  ? 0.2598 0.1586 0.2609 0.0202  0.0046  0.0087  35  ASP   C CA  
1325 C C   . ASP   B 29  ? 0.2642 0.1713 0.2803 0.0163  0.0037  0.0129  35  ASP   C C   
1326 O O   . ASP   B 29  ? 0.2638 0.1747 0.2741 0.0149  0.0015  0.0150  35  ASP   C O   
1327 C CB  . ASP   B 29  ? 0.2802 0.1721 0.2647 0.0235  -0.0018 0.0003  35  ASP   C CB  
1328 C CG  . ASP   B 29  ? 0.3355 0.2235 0.3271 0.0244  -0.0096 -0.0096 35  ASP   C CG  
1329 O OD1 . ASP   B 29  ? 0.3392 0.2329 0.3507 0.0209  -0.0106 -0.0084 35  ASP   C OD1 
1330 O OD2 . ASP   B 29  ? 0.3572 0.2363 0.3350 0.0290  -0.0149 -0.0182 35  ASP   C OD2 
1331 N N   . SER   B 30  ? 0.2523 0.1619 0.2878 0.0151  0.0066  0.0147  36  SER   C N   
1332 C CA  A SER   B 30  ? 0.2411 0.1576 0.2915 0.0128  0.0081  0.0203  36  SER   C CA  
1333 C CA  B SER   B 30  ? 0.2494 0.1660 0.2993 0.0128  0.0081  0.0203  36  SER   C CA  
1334 C C   . SER   B 30  ? 0.2459 0.1620 0.2995 0.0125  0.0025  0.0149  36  SER   C C   
1335 O O   . SER   B 30  ? 0.2611 0.1822 0.3158 0.0114  0.0035  0.0199  36  SER   C O   
1336 C CB  A SER   B 30  ? 0.2268 0.1448 0.2991 0.0125  0.0131  0.0232  36  SER   C CB  
1337 C CB  B SER   B 30  ? 0.2597 0.1783 0.3308 0.0124  0.0135  0.0242  36  SER   C CB  
1338 O OG  A SER   B 30  ? 0.1973 0.1204 0.2855 0.0115  0.0151  0.0278  36  SER   C OG  
1339 O OG  B SER   B 30  ? 0.2780 0.1899 0.3580 0.0136  0.0112  0.0155  36  SER   C OG  
1340 N N   . SER   B 31  ? 0.2506 0.1602 0.3063 0.0139  -0.0037 0.0045  37  SER   C N   
1341 C CA  . SER   B 31  ? 0.2539 0.1632 0.3158 0.0136  -0.0102 -0.0009 37  SER   C CA  
1342 C C   . SER   B 31  ? 0.2420 0.1526 0.2846 0.0137  -0.0128 0.0001  37  SER   C C   
1343 O O   . SER   B 31  ? 0.2308 0.1441 0.2804 0.0128  -0.0151 0.0001  37  SER   C O   
1344 C CB  . SER   B 31  ? 0.3079 0.2093 0.3749 0.0157  -0.0185 -0.0132 37  SER   C CB  
1345 O OG  . SER   B 31  ? 0.3812 0.2755 0.4230 0.0191  -0.0240 -0.0199 37  SER   C OG  
1346 N N   . ARG   B 32  ? 0.2328 0.1418 0.2540 0.0147  -0.0115 0.0019  38  ARG   C N   
1347 C CA  . ARG   B 32  ? 0.2426 0.1529 0.2476 0.0147  -0.0134 0.0034  38  ARG   C CA  
1348 C C   . ARG   B 32  ? 0.2330 0.1498 0.2355 0.0126  -0.0081 0.0131  38  ARG   C C   
1349 O O   . ARG   B 32  ? 0.2282 0.1461 0.2192 0.0123  -0.0095 0.0145  38  ARG   C O   
1350 C CB  . ARG   B 32  ? 0.2790 0.1827 0.2632 0.0179  -0.0153 -0.0005 38  ARG   C CB  
1351 C CG  . ARG   B 32  ? 0.3099 0.2051 0.2893 0.0218  -0.0220 -0.0109 38  ARG   C CG  
1352 C CD  . ARG   B 32  ? 0.3290 0.2168 0.2848 0.0266  -0.0216 -0.0127 38  ARG   C CD  
1353 N NE  . ARG   B 32  ? 0.3068 0.1960 0.2496 0.0269  -0.0228 -0.0103 38  ARG   C NE  
1354 C CZ  . ARG   B 32  ? 0.3094 0.1915 0.2328 0.0320  -0.0254 -0.0138 38  ARG   C CZ  
1355 N NH1 . ARG   B 32  ? 0.3085 0.1810 0.2203 0.0380  -0.0270 -0.0201 38  ARG   C NH1 
1356 N NH2 . ARG   B 32  ? 0.2712 0.1553 0.1860 0.0319  -0.0259 -0.0109 38  ARG   C NH2 
1357 N N   . ASP   B 33  ? 0.2151 0.1356 0.2275 0.0116  -0.0026 0.0194  39  ASP   C N   
1358 C CA  . ASP   B 33  ? 0.2077 0.1333 0.2162 0.0107  0.0009  0.0280  39  ASP   C CA  
1359 C C   . ASP   B 33  ? 0.2066 0.1308 0.1999 0.0108  -0.0001 0.0288  39  ASP   C C   
1360 O O   . ASP   B 33  ? 0.2043 0.1313 0.1906 0.0101  -0.0009 0.0326  39  ASP   C O   
1361 C CB  . ASP   B 33  ? 0.2161 0.1452 0.2254 0.0105  0.0012  0.0313  39  ASP   C CB  
1362 C CG  . ASP   B 33  ? 0.2487 0.1816 0.2520 0.0109  0.0038  0.0392  39  ASP   C CG  
1363 O OD1 . ASP   B 33  ? 0.2752 0.2100 0.2834 0.0112  0.0068  0.0441  39  ASP   C OD1 
1364 O OD2 . ASP   B 33  ? 0.2281 0.1616 0.2211 0.0112  0.0019  0.0401  39  ASP   C OD2 
1365 N N   . LEU   B 34  ? 0.2119 0.1312 0.2007 0.0122  0.0002  0.0254  40  LEU   C N   
1366 C CA  . LEU   B 34  ? 0.2219 0.1396 0.1996 0.0129  0.0011  0.0275  40  LEU   C CA  
1367 C C   . LEU   B 34  ? 0.2331 0.1500 0.2157 0.0136  0.0061  0.0315  40  LEU   C C   
1368 O O   . LEU   B 34  ? 0.2319 0.1460 0.2208 0.0148  0.0084  0.0292  40  LEU   C O   
1369 C CB  . LEU   B 34  ? 0.2258 0.1369 0.1904 0.0157  -0.0014 0.0214  40  LEU   C CB  
1370 C CG  . LEU   B 34  ? 0.2568 0.1684 0.2148 0.0152  -0.0063 0.0184  40  LEU   C CG  
1371 C CD1 . LEU   B 34  ? 0.2672 0.1719 0.2111 0.0189  -0.0085 0.0132  40  LEU   C CD1 
1372 C CD2 . LEU   B 34  ? 0.2693 0.1858 0.2253 0.0129  -0.0064 0.0239  40  LEU   C CD2 
1373 N N   . LEU   B 35  ? 0.2153 0.1343 0.1962 0.0130  0.0075  0.0371  41  LEU   C N   
1374 C CA  . LEU   B 35  ? 0.2317 0.1499 0.2185 0.0139  0.0127  0.0417  41  LEU   C CA  
1375 C C   . LEU   B 35  ? 0.2355 0.1525 0.2173 0.0145  0.0136  0.0447  41  LEU   C C   
1376 O O   . LEU   B 35  ? 0.2537 0.1739 0.2336 0.0126  0.0094  0.0461  41  LEU   C O   
1377 C CB  . LEU   B 35  ? 0.2282 0.1528 0.2284 0.0119  0.0137  0.0483  41  LEU   C CB  
1378 C CG  . LEU   B 35  ? 0.2278 0.1522 0.2372 0.0126  0.0190  0.0537  41  LEU   C CG  
1379 C CD1 . LEU   B 35  ? 0.2466 0.1748 0.2688 0.0120  0.0210  0.0575  41  LEU   C CD1 
1380 C CD2 . LEU   B 35  ? 0.2203 0.1479 0.2331 0.0115  0.0175  0.0596  41  LEU   C CD2 
1381 N N   . VAL   B 36  ? 0.2243 0.1357 0.2040 0.0178  0.0194  0.0455  42  VAL   C N   
1382 C CA  . VAL   B 36  ? 0.2328 0.1421 0.2113 0.0193  0.0228  0.0499  42  VAL   C CA  
1383 C C   . VAL   B 36  ? 0.2489 0.1594 0.2416 0.0197  0.0290  0.0572  42  VAL   C C   
1384 O O   . VAL   B 36  ? 0.2605 0.1672 0.2547 0.0222  0.0346  0.0570  42  VAL   C O   
1385 C CB  . VAL   B 36  ? 0.2441 0.1444 0.2064 0.0247  0.0261  0.0459  42  VAL   C CB  
1386 C CG1 . VAL   B 36  ? 0.2542 0.1521 0.2178 0.0271  0.0320  0.0523  42  VAL   C CG1 
1387 C CG2 . VAL   B 36  ? 0.2540 0.1536 0.2042 0.0244  0.0191  0.0389  42  VAL   C CG2 
1388 N N   . SER   B 37  ? 0.2436 0.1587 0.2480 0.0174  0.0279  0.0635  43  SER   C N   
1389 C CA  . SER   B 37  ? 0.2449 0.1615 0.2662 0.0176  0.0333  0.0712  43  SER   C CA  
1390 C C   . SER   B 37  ? 0.2617 0.1754 0.2884 0.0197  0.0384  0.0764  43  SER   C C   
1391 O O   . SER   B 37  ? 0.2654 0.1775 0.2836 0.0200  0.0361  0.0742  43  SER   C O   
1392 C CB  . SER   B 37  ? 0.2399 0.1650 0.2761 0.0134  0.0267  0.0750  43  SER   C CB  
1393 O OG  . SER   B 37  ? 0.2463 0.1757 0.2837 0.0104  0.0181  0.0748  43  SER   C OG  
1394 N N   . SER   B 38  ? 0.2702 0.1830 0.3124 0.0215  0.0463  0.0838  44  SER   C N   
1395 C CA  . SER   B 38  ? 0.2897 0.1997 0.3418 0.0239  0.0531  0.0904  44  SER   C CA  
1396 C C   . SER   B 38  ? 0.3012 0.2191 0.3766 0.0189  0.0456  0.0953  44  SER   C C   
1397 O O   . SER   B 38  ? 0.3063 0.2312 0.3934 0.0148  0.0375  0.0958  44  SER   C O   
1398 C CB  . SER   B 38  ? 0.3281 0.2319 0.3861 0.0295  0.0670  0.0967  44  SER   C CB  
1399 O OG  . SER   B 38  ? 0.3710 0.2800 0.4464 0.0269  0.0663  0.1002  44  SER   C OG  
1400 N N   . THR   B 39  ? 0.3041 0.2204 0.3871 0.0197  0.0479  0.0988  45  THR   C N   
1401 C CA  . THR   B 39  ? 0.3084 0.2309 0.4152 0.0152  0.0397  0.1022  45  THR   C CA  
1402 C C   . THR   B 39  ? 0.3369 0.2575 0.4693 0.0178  0.0502  0.1125  45  THR   C C   
1403 O O   . THR   B 39  ? 0.3414 0.2543 0.4665 0.0239  0.0643  0.1163  45  THR   C O   
1404 C CB  . THR   B 39  ? 0.3225 0.2457 0.4192 0.0129  0.0307  0.0963  45  THR   C CB  
1405 O OG1 . THR   B 39  ? 0.3348 0.2512 0.4236 0.0173  0.0402  0.0980  45  THR   C OG1 
1406 C CG2 . THR   B 39  ? 0.3493 0.2739 0.4219 0.0110  0.0221  0.0871  45  THR   C CG2 
1407 N N   . THR   B 40  ? 0.3502 0.2770 0.5125 0.0138  0.0431  0.1168  46  THR   C N   
1408 C CA  . THR   B 40  ? 0.3741 0.2996 0.5667 0.0157  0.0524  0.1272  46  THR   C CA  
1409 C C   . THR   B 40  ? 0.3769 0.2998 0.5725 0.0162  0.0531  0.1274  46  THR   C C   
1410 O O   . THR   B 40  ? 0.3816 0.2984 0.5820 0.0216  0.0679  0.1347  46  THR   C O   
1411 C CB  . THR   B 40  ? 0.4169 0.3498 0.6447 0.0118  0.0452  0.1324  46  THR   C CB  
1412 O OG1 . THR   B 40  ? 0.4481 0.3875 0.6735 0.0062  0.0257  0.1248  46  THR   C OG1 
1413 C CG2 . THR   B 40  ? 0.4355 0.3683 0.6673 0.0142  0.0538  0.1374  46  THR   C CG2 
1414 N N   . ALA   B 41  ? 0.3726 0.2990 0.5625 0.0114  0.0380  0.1195  47  ALA   C N   
1415 C CA  . ALA   B 41  ? 0.3781 0.3022 0.5705 0.0114  0.0374  0.1188  47  ALA   C CA  
1416 C C   . ALA   B 41  ? 0.3825 0.3005 0.5388 0.0151  0.0426  0.1136  47  ALA   C C   
1417 O O   . ALA   B 41  ? 0.3991 0.3172 0.5286 0.0149  0.0384  0.1063  47  ALA   C O   
1418 C CB  . ALA   B 41  ? 0.3766 0.3062 0.5804 0.0051  0.0185  0.1124  47  ALA   C CB  
1419 N N   . GLN   B 42  ? 0.3844 0.2974 0.5416 0.0187  0.0512  0.1174  48  GLN   C N   
1420 C CA  . GLN   B 42  ? 0.4010 0.3084 0.5256 0.0226  0.0548  0.1126  48  GLN   C CA  
1421 C C   . GLN   B 42  ? 0.3872 0.2982 0.5008 0.0172  0.0392  0.1025  48  GLN   C C   
1422 O O   . GLN   B 42  ? 0.3837 0.2992 0.5177 0.0122  0.0288  0.1012  48  GLN   C O   
1423 C CB  . GLN   B 42  ? 0.4427 0.3429 0.5713 0.0294  0.0698  0.1212  48  GLN   C CB  
1424 C CG  . GLN   B 42  ? 0.5225 0.4155 0.6455 0.0379  0.0878  0.1296  48  GLN   C CG  
1425 C CD  . GLN   B 42  ? 0.6265 0.5099 0.7197 0.0468  0.0985  0.1303  48  GLN   C CD  
1426 O OE1 . GLN   B 42  ? 0.6639 0.5449 0.7598 0.0489  0.1016  0.1334  48  GLN   C OE1 
1427 N NE2 . GLN   B 42  ? 0.6555 0.5327 0.7193 0.0527  0.1037  0.1271  48  GLN   C NE2 
1428 N N   . GLY   B 43  ? 0.3758 0.2846 0.4578 0.0186  0.0373  0.0952  49  GLY   C N   
1429 C CA  . GLY   B 43  ? 0.3577 0.2687 0.4253 0.0149  0.0253  0.0862  49  GLY   C CA  
1430 C C   . GLY   B 43  ? 0.3519 0.2581 0.4096 0.0182  0.0297  0.0862  49  GLY   C C   
1431 O O   . GLY   B 43  ? 0.3534 0.2537 0.4077 0.0245  0.0425  0.0926  49  GLY   C O   
1432 N N   . CYS   B 44  ? 0.3376 0.2458 0.3907 0.0145  0.0195  0.0797  50  CYS   C N   
1433 C CA  . CYS   B 44  ? 0.3533 0.2576 0.4005 0.0169  0.0224  0.0799  50  CYS   C CA  
1434 C C   . CYS   B 44  ? 0.3543 0.2575 0.3744 0.0173  0.0175  0.0720  50  CYS   C C   
1435 O O   . CYS   B 44  ? 0.3719 0.2723 0.3875 0.0191  0.0190  0.0720  50  CYS   C O   
1436 C CB  . CYS   B 44  ? 0.3720 0.2786 0.4451 0.0129  0.0167  0.0810  50  CYS   C CB  
1437 S SG  . CYS   B 44  ? 0.4785 0.3856 0.5902 0.0133  0.0244  0.0923  50  CYS   C SG  
1438 N N   . ASP   B 45  ? 0.3302 0.2355 0.3345 0.0158  0.0121  0.0658  51  ASP   C N   
1439 C CA  . ASP   B 45  ? 0.3299 0.2340 0.3114 0.0166  0.0083  0.0589  51  ASP   C CA  
1440 C C   . ASP   B 45  ? 0.3474 0.2452 0.3125 0.0237  0.0173  0.0611  51  ASP   C C   
1441 O O   . ASP   B 45  ? 0.3514 0.2460 0.3170 0.0278  0.0258  0.0660  51  ASP   C O   
1442 C CB  . ASP   B 45  ? 0.3317 0.2394 0.3040 0.0139  0.0017  0.0530  51  ASP   C CB  
1443 C CG  . ASP   B 45  ? 0.3646 0.2771 0.3461 0.0087  -0.0079 0.0501  51  ASP   C CG  
1444 O OD1 . ASP   B 45  ? 0.3997 0.3122 0.3884 0.0069  -0.0122 0.0491  51  ASP   C OD1 
1445 O OD2 . ASP   B 45  ? 0.3212 0.2369 0.3031 0.0071  -0.0110 0.0491  51  ASP   C OD2 
1446 N N   . THR   B 46  ? 0.3376 0.2330 0.2878 0.0257  0.0154  0.0574  52  THR   C N   
1447 C CA  . THR   B 46  ? 0.3428 0.2317 0.2741 0.0332  0.0214  0.0581  52  THR   C CA  
1448 C C   . THR   B 46  ? 0.3375 0.2269 0.2520 0.0327  0.0141  0.0495  52  THR   C C   
1449 O O   . THR   B 46  ? 0.3316 0.2249 0.2464 0.0284  0.0065  0.0445  52  THR   C O   
1450 C CB  . THR   B 46  ? 0.3667 0.2528 0.2964 0.0358  0.0234  0.0606  52  THR   C CB  
1451 O OG1 . THR   B 46  ? 0.3617 0.2466 0.3097 0.0369  0.0313  0.0694  52  THR   C OG1 
1452 C CG2 . THR   B 46  ? 0.3886 0.2680 0.2945 0.0438  0.0261  0.0595  52  THR   C CG2 
1453 N N   . ILE   B 47  ? 0.3260 0.2108 0.2267 0.0377  0.0167  0.0478  53  ILE   C N   
1454 C CA  . ILE   B 47  ? 0.3102 0.1950 0.1987 0.0376  0.0096  0.0396  53  ILE   C CA  
1455 C C   . ILE   B 47  ? 0.3137 0.1939 0.1864 0.0427  0.0072  0.0368  53  ILE   C C   
1456 O O   . ILE   B 47  ? 0.3298 0.2031 0.1916 0.0501  0.0133  0.0408  53  ILE   C O   
1457 C CB  . ILE   B 47  ? 0.3207 0.2018 0.2027 0.0409  0.0121  0.0378  53  ILE   C CB  
1458 C CG1 . ILE   B 47  ? 0.3194 0.2048 0.2175 0.0367  0.0153  0.0416  53  ILE   C CG1 
1459 C CG2 . ILE   B 47  ? 0.3314 0.2126 0.2052 0.0404  0.0037  0.0288  53  ILE   C CG2 
1460 C CD1 . ILE   B 47  ? 0.3146 0.2086 0.2257 0.0286  0.0080  0.0392  53  ILE   C CD1 
1461 N N   . ALA   B 48  ? 0.3029 0.1864 0.1743 0.0395  -0.0012 0.0306  54  ALA   C N   
1462 C CA  . ALA   B 48  ? 0.3049 0.1848 0.1633 0.0439  -0.0053 0.0273  54  ALA   C CA  
1463 C C   . ALA   B 48  ? 0.3052 0.1777 0.1465 0.0512  -0.0067 0.0231  54  ALA   C C   
1464 O O   . ALA   B 48  ? 0.3096 0.1824 0.1526 0.0499  -0.0089 0.0189  54  ALA   C O   
1465 C CB  . ALA   B 48  ? 0.2919 0.1775 0.1568 0.0383  -0.0137 0.0218  54  ALA   C CB  
1466 N N   . ARG   B 49  ? 0.2950 0.1604 0.1195 0.0595  -0.0061 0.0237  55  ARG   C N   
1467 C CA  . ARG   B 49  ? 0.3025 0.1592 0.1070 0.0680  -0.0096 0.0182  55  ARG   C CA  
1468 C C   . ARG   B 49  ? 0.3122 0.1674 0.1078 0.0711  -0.0184 0.0139  55  ARG   C C   
1469 O O   . ARG   B 49  ? 0.3408 0.1917 0.1253 0.0773  -0.0150 0.0187  55  ARG   C O   
1470 C CB  . ARG   B 49  ? 0.3234 0.1704 0.1118 0.0778  0.0008  0.0240  55  ARG   C CB  
1471 C CG  . ARG   B 49  ? 0.3397 0.1887 0.1408 0.0747  0.0107  0.0301  55  ARG   C CG  
1472 C CD  . ARG   B 49  ? 0.3419 0.1919 0.1472 0.0714  0.0071  0.0239  55  ARG   C CD  
1473 N NE  . ARG   B 49  ? 0.3457 0.1979 0.1641 0.0687  0.0165  0.0304  55  ARG   C NE  
1474 C CZ  . ARG   B 49  ? 0.3608 0.2171 0.1908 0.0633  0.0150  0.0276  55  ARG   C CZ  
1475 N NH1 . ARG   B 49  ? 0.3281 0.1868 0.1593 0.0600  0.0052  0.0188  55  ARG   C NH1 
1476 N NH2 . ARG   B 49  ? 0.3544 0.2129 0.1974 0.0611  0.0233  0.0343  55  ARG   C NH2 
1477 N N   . CYS   B 50  ? 0.3076 0.1675 0.1118 0.0661  -0.0290 0.0061  56  CYS   C N   
1478 C CA  . CYS   B 50  ? 0.3143 0.1759 0.1188 0.0662  -0.0382 0.0021  56  CYS   C CA  
1479 C C   . CYS   B 50  ? 0.3199 0.1852 0.1365 0.0617  -0.0488 -0.0067 56  CYS   C C   
1480 O O   . CYS   B 50  ? 0.3321 0.1993 0.1572 0.0580  -0.0482 -0.0091 56  CYS   C O   
1481 C CB  . CYS   B 50  ? 0.3033 0.1721 0.1216 0.0599  -0.0342 0.0080  56  CYS   C CB  
1482 S SG  . CYS   B 50  ? 0.2922 0.1711 0.1345 0.0480  -0.0331 0.0078  56  CYS   C SG  
1483 N N   . ASP   B 51  ? 0.3213 0.1884 0.1421 0.0616  -0.0577 -0.0106 57  ASP   C N   
1484 C CA  . ASP   B 51  ? 0.3212 0.1931 0.1599 0.0565  -0.0664 -0.0172 57  ASP   C CA  
1485 C C   . ASP   B 51  ? 0.3012 0.1813 0.1569 0.0500  -0.0655 -0.0140 57  ASP   C C   
1486 O O   . ASP   B 51  ? 0.3070 0.1898 0.1749 0.0485  -0.0732 -0.0182 57  ASP   C O   
1487 C CB  . ASP   B 51  ? 0.3500 0.2160 0.1825 0.0626  -0.0793 -0.0262 57  ASP   C CB  
1488 C CG  . ASP   B 51  ? 0.4202 0.2825 0.2406 0.0691  -0.0857 -0.0266 57  ASP   C CG  
1489 O OD1 . ASP   B 51  ? 0.4072 0.2716 0.2241 0.0688  -0.0787 -0.0191 57  ASP   C OD1 
1490 O OD2 . ASP   B 51  ? 0.4813 0.3385 0.2968 0.0746  -0.0984 -0.0347 57  ASP   C OD2 
1491 N N   . CYS   B 52  ? 0.2840 0.1676 0.1416 0.0462  -0.0562 -0.0068 58  CYS   C N   
1492 C CA  . CYS   B 52  ? 0.2613 0.1513 0.1328 0.0406  -0.0546 -0.0042 58  CYS   C CA  
1493 C C   . CYS   B 52  ? 0.2517 0.1471 0.1418 0.0351  -0.0568 -0.0071 58  CYS   C C   
1494 O O   . CYS   B 52  ? 0.2462 0.1421 0.1405 0.0334  -0.0558 -0.0087 58  CYS   C O   
1495 C CB  . CYS   B 52  ? 0.2700 0.1620 0.1415 0.0374  -0.0454 0.0025  58  CYS   C CB  
1496 S SG  . CYS   B 52  ? 0.3087 0.1961 0.1672 0.0427  -0.0413 0.0080  58  CYS   C SG  
1497 N N   . GLN   B 53  ? 0.2430 0.1419 0.1446 0.0329  -0.0588 -0.0071 59  GLN   C N   
1498 C CA  . GLN   B 53  ? 0.2521 0.1560 0.1725 0.0284  -0.0581 -0.0077 59  GLN   C CA  
1499 C C   . GLN   B 53  ? 0.2440 0.1514 0.1692 0.0249  -0.0514 -0.0029 59  GLN   C C   
1500 O O   . GLN   B 53  ? 0.2404 0.1510 0.1798 0.0226  -0.0497 -0.0023 59  GLN   C O   
1501 C CB  . GLN   B 53  ? 0.2678 0.1721 0.2022 0.0297  -0.0669 -0.0128 59  GLN   C CB  
1502 C CG  . GLN   B 53  ? 0.2807 0.1818 0.2148 0.0321  -0.0737 -0.0188 59  GLN   C CG  
1503 C CD  . GLN   B 53  ? 0.3151 0.2170 0.2682 0.0327  -0.0834 -0.0243 59  GLN   C CD  
1504 O OE1 . GLN   B 53  ? 0.3690 0.2668 0.3166 0.0375  -0.0938 -0.0296 59  GLN   C OE1 
1505 N NE2 . GLN   B 53  ? 0.2659 0.1729 0.2426 0.0284  -0.0801 -0.0226 59  GLN   C NE2 
1506 N N   . THR   B 54  ? 0.2405 0.1464 0.1545 0.0251  -0.0473 0.0005  60  THR   C N   
1507 C CA  . THR   B 54  ? 0.2394 0.1472 0.1562 0.0222  -0.0417 0.0039  60  THR   C CA  
1508 C C   . THR   B 54  ? 0.2359 0.1427 0.1442 0.0210  -0.0373 0.0066  60  THR   C C   
1509 O O   . THR   B 54  ? 0.2583 0.1624 0.1582 0.0231  -0.0373 0.0076  60  THR   C O   
1510 C CB  . THR   B 54  ? 0.2777 0.1846 0.1948 0.0235  -0.0424 0.0047  60  THR   C CB  
1511 O OG1 . THR   B 54  ? 0.3266 0.2302 0.2323 0.0267  -0.0435 0.0057  60  THR   C OG1 
1512 C CG2 . THR   B 54  ? 0.2724 0.1807 0.2010 0.0249  -0.0475 0.0022  60  THR   C CG2 
1513 N N   . GLY   B 55  ? 0.2183 0.1266 0.1294 0.0181  -0.0336 0.0082  61  GLY   C N   
1514 C CA  . GLY   B 55  ? 0.2165 0.1242 0.1231 0.0166  -0.0310 0.0103  61  GLY   C CA  
1515 C C   . GLY   B 55  ? 0.2168 0.1252 0.1249 0.0145  -0.0289 0.0109  61  GLY   C C   
1516 O O   . GLY   B 55  ? 0.2252 0.1336 0.1357 0.0149  -0.0280 0.0103  61  GLY   C O   
1517 N N   . VAL   B 56  ? 0.2032 0.1116 0.1094 0.0131  -0.0282 0.0121  62  VAL   C N   
1518 C CA  . VAL   B 56  ? 0.1927 0.1006 0.0971 0.0122  -0.0278 0.0121  62  VAL   C CA  
1519 C C   . VAL   B 56  ? 0.2055 0.1153 0.1105 0.0113  -0.0277 0.0135  62  VAL   C C   
1520 O O   . VAL   B 56  ? 0.2253 0.1358 0.1321 0.0105  -0.0280 0.0148  62  VAL   C O   
1521 C CB  . VAL   B 56  ? 0.2089 0.1139 0.1119 0.0115  -0.0293 0.0116  62  VAL   C CB  
1522 C CG1 . VAL   B 56  ? 0.2166 0.1198 0.1158 0.0114  -0.0310 0.0103  62  VAL   C CG1 
1523 C CG2 . VAL   B 56  ? 0.2249 0.1279 0.1281 0.0126  -0.0289 0.0107  62  VAL   C CG2 
1524 N N   . TYR   B 57  ? 0.2072 0.1174 0.1104 0.0121  -0.0263 0.0141  63  TYR   C N   
1525 C CA  . TYR   B 57  ? 0.1944 0.1065 0.0981 0.0117  -0.0262 0.0161  63  TYR   C CA  
1526 C C   . TYR   B 57  ? 0.2186 0.1286 0.1153 0.0129  -0.0281 0.0161  63  TYR   C C   
1527 O O   . TYR   B 57  ? 0.2403 0.1469 0.1306 0.0149  -0.0278 0.0145  63  TYR   C O   
1528 C CB  . TYR   B 57  ? 0.2082 0.1229 0.1173 0.0126  -0.0227 0.0177  63  TYR   C CB  
1529 C CG  . TYR   B 57  ? 0.2156 0.1296 0.1231 0.0153  -0.0189 0.0194  63  TYR   C CG  
1530 C CD1 . TYR   B 57  ? 0.2184 0.1309 0.1275 0.0168  -0.0165 0.0187  63  TYR   C CD1 
1531 C CD2 . TYR   B 57  ? 0.2266 0.1411 0.1318 0.0170  -0.0166 0.0226  63  TYR   C CD2 
1532 C CE1 . TYR   B 57  ? 0.2375 0.1488 0.1466 0.0202  -0.0108 0.0215  63  TYR   C CE1 
1533 C CE2 . TYR   B 57  ? 0.2304 0.1434 0.1336 0.0209  -0.0112 0.0255  63  TYR   C CE2 
1534 C CZ  . TYR   B 57  ? 0.2477 0.1589 0.1528 0.0226  -0.0077 0.0251  63  TYR   C CZ  
1535 O OH  . TYR   B 57  ? 0.2606 0.1697 0.1648 0.0273  -0.0003 0.0291  63  TYR   C OH  
1536 N N   . TYR   B 58  ? 0.1967 0.1080 0.0943 0.0122  -0.0304 0.0176  64  TYR   C N   
1537 C CA  . TYR   B 58  ? 0.2282 0.1370 0.1180 0.0141  -0.0340 0.0172  64  TYR   C CA  
1538 C C   . TYR   B 58  ? 0.2407 0.1501 0.1256 0.0174  -0.0304 0.0203  64  TYR   C C   
1539 O O   . TYR   B 58  ? 0.2274 0.1407 0.1191 0.0166  -0.0277 0.0236  64  TYR   C O   
1540 C CB  . TYR   B 58  ? 0.2471 0.1568 0.1422 0.0120  -0.0398 0.0173  64  TYR   C CB  
1541 C CG  . TYR   B 58  ? 0.2669 0.1733 0.1533 0.0146  -0.0459 0.0157  64  TYR   C CG  
1542 C CD1 . TYR   B 58  ? 0.2999 0.2005 0.1765 0.0169  -0.0496 0.0113  64  TYR   C CD1 
1543 C CD2 . TYR   B 58  ? 0.2774 0.1856 0.1637 0.0157  -0.0484 0.0183  64  TYR   C CD2 
1544 C CE1 . TYR   B 58  ? 0.3022 0.1982 0.1677 0.0206  -0.0566 0.0086  64  TYR   C CE1 
1545 C CE2 . TYR   B 58  ? 0.2960 0.2003 0.1721 0.0193  -0.0555 0.0164  64  TYR   C CE2 
1546 C CZ  . TYR   B 58  ? 0.3078 0.2056 0.1723 0.0221  -0.0599 0.0112  64  TYR   C CZ  
1547 O OH  . TYR   B 58  ? 0.3389 0.2314 0.1902 0.0269  -0.0681 0.0084  64  TYR   C OH  
1548 N N   . CYS   B 59  ? 0.2576 0.1625 0.1303 0.0219  -0.0296 0.0197  65  CYS   C N   
1549 C CA  . CYS   B 59  ? 0.2688 0.1728 0.1345 0.0268  -0.0246 0.0238  65  CYS   C CA  
1550 C C   . CYS   B 59  ? 0.2907 0.1904 0.1419 0.0310  -0.0305 0.0231  65  CYS   C C   
1551 O O   . CYS   B 59  ? 0.2923 0.1854 0.1295 0.0348  -0.0333 0.0196  65  CYS   C O   
1552 C CB  . CYS   B 59  ? 0.2826 0.1836 0.1447 0.0304  -0.0172 0.0247  65  CYS   C CB  
1553 S SG  . CYS   B 59  ? 0.3126 0.2110 0.1660 0.0383  -0.0083 0.0313  65  CYS   C SG  
1554 N N   . SER   B 60  ? 0.2815 0.1844 0.1359 0.0305  -0.0333 0.0259  66  SER   C N   
1555 C CA  . SER   B 60  ? 0.3186 0.2176 0.1603 0.0345  -0.0413 0.0248  66  SER   C CA  
1556 C C   . SER   B 60  ? 0.3290 0.2213 0.1498 0.0435  -0.0377 0.0266  66  SER   C C   
1557 O O   . SER   B 60  ? 0.3659 0.2515 0.1706 0.0481  -0.0455 0.0225  66  SER   C O   
1558 C CB  . SER   B 60  ? 0.3705 0.2745 0.2210 0.0327  -0.0446 0.0283  66  SER   C CB  
1559 O OG  . SER   B 60  ? 0.4592 0.3663 0.3122 0.0350  -0.0359 0.0349  66  SER   C OG  
1560 N N   . SER   B 61  ? 0.3164 0.2097 0.1381 0.0466  -0.0260 0.0326  67  SER   C N   
1561 C CA  . SER   B 61  ? 0.3356 0.2221 0.1381 0.0565  -0.0193 0.0364  67  SER   C CA  
1562 C C   . SER   B 61  ? 0.3428 0.2212 0.1311 0.0605  -0.0181 0.0319  67  SER   C C   
1563 O O   . SER   B 61  ? 0.3567 0.2275 0.1256 0.0700  -0.0126 0.0345  67  SER   C O   
1564 C CB  . SER   B 61  ? 0.3424 0.2326 0.1551 0.0586  -0.0060 0.0451  67  SER   C CB  
1565 O OG  . SER   B 61  ? 0.3587 0.2530 0.1900 0.0532  0.0001  0.0449  67  SER   C OG  
1566 N N   . ARG   B 62  ? 0.3164 0.1958 0.1135 0.0540  -0.0229 0.0254  68  ARG   C N   
1567 C CA  . ARG   B 62  ? 0.3328 0.2044 0.1177 0.0571  -0.0232 0.0203  68  ARG   C CA  
1568 C C   . ARG   B 62  ? 0.3562 0.2254 0.1402 0.0531  -0.0366 0.0115  68  ARG   C C   
1569 O O   . ARG   B 62  ? 0.3730 0.2355 0.1486 0.0550  -0.0382 0.0062  68  ARG   C O   
1570 C CB  . ARG   B 62  ? 0.3386 0.2131 0.1377 0.0538  -0.0142 0.0217  68  ARG   C CB  
1571 C CG  . ARG   B 62  ? 0.3988 0.2752 0.2035 0.0576  -0.0008 0.0301  68  ARG   C CG  
1572 C CD  . ARG   B 62  ? 0.4197 0.2865 0.2039 0.0683  0.0071  0.0328  68  ARG   C CD  
1573 N NE  . ARG   B 62  ? 0.4595 0.3279 0.2529 0.0724  0.0216  0.0421  68  ARG   C NE  
1574 C CZ  . ARG   B 62  ? 0.4914 0.3596 0.2806 0.0782  0.0278  0.0496  68  ARG   C CZ  
1575 N NH1 . ARG   B 62  ? 0.4791 0.3460 0.2538 0.0804  0.0199  0.0487  68  ARG   C NH1 
1576 N NH2 . ARG   B 62  ? 0.4930 0.3626 0.2946 0.0818  0.0419  0.0584  68  ARG   C NH2 
1577 N N   . ARG   B 63  ? 0.3501 0.2249 0.1464 0.0472  -0.0455 0.0103  69  ARG   C N   
1578 C CA  . ARG   B 63  ? 0.3575 0.2315 0.1607 0.0425  -0.0573 0.0033  69  ARG   C CA  
1579 C C   . ARG   B 63  ? 0.3518 0.2258 0.1643 0.0382  -0.0543 0.0003  69  ARG   C C   
1580 O O   . ARG   B 63  ? 0.3589 0.2272 0.1681 0.0383  -0.0608 -0.0062 69  ARG   C O   
1581 C CB  . ARG   B 63  ? 0.3874 0.2519 0.1716 0.0486  -0.0687 -0.0032 69  ARG   C CB  
1582 C CG  . ARG   B 63  ? 0.4465 0.3107 0.2215 0.0532  -0.0739 -0.0006 69  ARG   C CG  
1583 C CD  . ARG   B 63  ? 0.5120 0.3831 0.3071 0.0464  -0.0832 -0.0008 69  ARG   C CD  
1584 N NE  . ARG   B 63  ? 0.5607 0.4285 0.3455 0.0514  -0.0947 -0.0021 69  ARG   C NE  
1585 C CZ  . ARG   B 63  ? 0.5666 0.4376 0.3471 0.0548  -0.0920 0.0045  69  ARG   C CZ  
1586 N NH1 . ARG   B 63  ? 0.5487 0.4258 0.3349 0.0537  -0.0780 0.0127  69  ARG   C NH1 
1587 N NH2 . ARG   B 63  ? 0.5646 0.4323 0.3358 0.0596  -0.1039 0.0029  69  ARG   C NH2 
1588 N N   . LYS   B 64  ? 0.3362 0.2161 0.1602 0.0350  -0.0447 0.0049  70  LYS   C N   
1589 C CA  . LYS   B 64  ? 0.3226 0.2028 0.1548 0.0318  -0.0417 0.0029  70  LYS   C CA  
1590 C C   . LYS   B 64  ? 0.3017 0.1902 0.1523 0.0258  -0.0380 0.0064  70  LYS   C C   
1591 O O   . LYS   B 64  ? 0.2946 0.1880 0.1501 0.0252  -0.0344 0.0109  70  LYS   C O   
1592 C CB  . LYS   B 64  ? 0.3745 0.2502 0.1969 0.0370  -0.0328 0.0042  70  LYS   C CB  
1593 C CG  . LYS   B 64  ? 0.4915 0.3566 0.2944 0.0433  -0.0358 -0.0011 70  LYS   C CG  
1594 C CD  . LYS   B 64  ? 0.5812 0.4417 0.3777 0.0480  -0.0258 0.0004  70  LYS   C CD  
1595 C CE  . LYS   B 64  ? 0.6666 0.5150 0.4411 0.0553  -0.0285 -0.0052 70  LYS   C CE  
1596 N NZ  . LYS   B 64  ? 0.7113 0.5542 0.4654 0.0625  -0.0319 -0.0051 70  LYS   C NZ  
1597 N N   . HIS   B 65  ? 0.2764 0.1655 0.1358 0.0222  -0.0389 0.0043  71  HIS   C N   
1598 C CA  . HIS   B 65  ? 0.2744 0.1693 0.1472 0.0181  -0.0356 0.0068  71  HIS   C CA  
1599 C C   . HIS   B 65  ? 0.2859 0.1799 0.1586 0.0197  -0.0296 0.0072  71  HIS   C C   
1600 O O   . HIS   B 65  ? 0.3113 0.2004 0.1791 0.0213  -0.0299 0.0042  71  HIS   C O   
1601 C CB  . HIS   B 65  ? 0.2685 0.1640 0.1510 0.0143  -0.0398 0.0053  71  HIS   C CB  
1602 C CG  . HIS   B 65  ? 0.2925 0.1895 0.1806 0.0124  -0.0453 0.0057  71  HIS   C CG  
1603 N ND1 . HIS   B 65  ? 0.3080 0.2098 0.2058 0.0098  -0.0436 0.0095  71  HIS   C ND1 
1604 C CD2 . HIS   B 65  ? 0.3095 0.2031 0.1949 0.0131  -0.0526 0.0027  71  HIS   C CD2 
1605 C CE1 . HIS   B 65  ? 0.3027 0.2047 0.2058 0.0087  -0.0490 0.0094  71  HIS   C CE1 
1606 N NE2 . HIS   B 65  ? 0.3097 0.2071 0.2064 0.0104  -0.0555 0.0052  71  HIS   C NE2 
1607 N N   . TYR   B 66  ? 0.2659 0.1642 0.1456 0.0192  -0.0248 0.0104  72  TYR   C N   
1608 C CA  . TYR   B 66  ? 0.2516 0.1498 0.1351 0.0207  -0.0198 0.0112  72  TYR   C CA  
1609 C C   . TYR   B 66  ? 0.2375 0.1397 0.1321 0.0178  -0.0208 0.0112  72  TYR   C C   
1610 O O   . TYR   B 66  ? 0.2341 0.1399 0.1340 0.0161  -0.0218 0.0123  72  TYR   C O   
1611 C CB  . TYR   B 66  ? 0.2587 0.1584 0.1445 0.0235  -0.0135 0.0151  72  TYR   C CB  
1612 C CG  . TYR   B 66  ? 0.2853 0.1800 0.1578 0.0287  -0.0103 0.0164  72  TYR   C CG  
1613 C CD1 . TYR   B 66  ? 0.3097 0.1985 0.1741 0.0331  -0.0062 0.0158  72  TYR   C CD1 
1614 C CD2 . TYR   B 66  ? 0.3012 0.1964 0.1681 0.0302  -0.0109 0.0186  72  TYR   C CD2 
1615 C CE1 . TYR   B 66  ? 0.3348 0.2173 0.1831 0.0395  -0.0027 0.0170  72  TYR   C CE1 
1616 C CE2 . TYR   B 66  ? 0.3187 0.2084 0.1705 0.0365  -0.0079 0.0202  72  TYR   C CE2 
1617 C CZ  . TYR   B 66  ? 0.3448 0.2276 0.1860 0.0415  -0.0039 0.0192  72  TYR   C CZ  
1618 O OH  . TYR   B 66  ? 0.3802 0.2560 0.2029 0.0494  -0.0004 0.0210  72  TYR   C OH  
1619 N N   . PRO   B 67  ? 0.2434 0.1441 0.1406 0.0182  -0.0200 0.0101  73  PRO   C N   
1620 C CA  . PRO   B 67  ? 0.2442 0.1479 0.1500 0.0169  -0.0216 0.0102  73  PRO   C CA  
1621 C C   . PRO   B 67  ? 0.2601 0.1668 0.1756 0.0179  -0.0192 0.0117  73  PRO   C C   
1622 O O   . PRO   B 67  ? 0.2787 0.1844 0.1967 0.0200  -0.0144 0.0133  73  PRO   C O   
1623 C CB  . PRO   B 67  ? 0.2534 0.1543 0.1590 0.0176  -0.0217 0.0090  73  PRO   C CB  
1624 C CG  . PRO   B 67  ? 0.2699 0.1663 0.1687 0.0197  -0.0187 0.0081  73  PRO   C CG  
1625 C CD  . PRO   B 67  ? 0.2445 0.1402 0.1360 0.0205  -0.0182 0.0085  73  PRO   C CD  
1626 N N   . VAL   B 68  ? 0.2388 0.1484 0.1601 0.0167  -0.0221 0.0113  74  VAL   C N   
1627 C CA  . VAL   B 68  ? 0.2273 0.1397 0.1612 0.0173  -0.0214 0.0118  74  VAL   C CA  
1628 C C   . VAL   B 68  ? 0.2317 0.1452 0.1712 0.0172  -0.0272 0.0092  74  VAL   C C   
1629 O O   . VAL   B 68  ? 0.2311 0.1435 0.1621 0.0171  -0.0307 0.0078  74  VAL   C O   
1630 C CB  . VAL   B 68  ? 0.2396 0.1539 0.1756 0.0168  -0.0192 0.0135  74  VAL   C CB  
1631 C CG1 . VAL   B 68  ? 0.2599 0.1726 0.1908 0.0186  -0.0132 0.0167  74  VAL   C CG1 
1632 C CG2 . VAL   B 68  ? 0.2479 0.1625 0.1772 0.0151  -0.0227 0.0124  74  VAL   C CG2 
1633 N N   . SER   B 69  ? 0.2323 0.1477 0.1869 0.0180  -0.0283 0.0087  75  SER   C N   
1634 C CA  . SER   B 69  ? 0.2273 0.1432 0.1889 0.0186  -0.0356 0.0051  75  SER   C CA  
1635 C C   . SER   B 69  ? 0.2124 0.1300 0.1823 0.0177  -0.0354 0.0046  75  SER   C C   
1636 O O   . SER   B 69  ? 0.2112 0.1305 0.1900 0.0172  -0.0293 0.0079  75  SER   C O   
1637 C CB  . SER   B 69  ? 0.2536 0.1706 0.2310 0.0198  -0.0382 0.0044  75  SER   C CB  
1638 O OG  . SER   B 69  ? 0.3410 0.2565 0.3115 0.0207  -0.0381 0.0051  75  SER   C OG  
1639 N N   . PHE   B 70  ? 0.2024 0.1189 0.1685 0.0181  -0.0413 0.0008  76  PHE   C N   
1640 C CA  . PHE   B 70  ? 0.2107 0.1282 0.1846 0.0173  -0.0412 -0.0002 76  PHE   C CA  
1641 C C   . PHE   B 70  ? 0.2258 0.1415 0.2063 0.0189  -0.0503 -0.0064 76  PHE   C C   
1642 O O   . PHE   B 70  ? 0.2321 0.1448 0.2032 0.0215  -0.0570 -0.0099 76  PHE   C O   
1643 C CB  . PHE   B 70  ? 0.2237 0.1406 0.1841 0.0163  -0.0371 0.0020  76  PHE   C CB  
1644 C CG  . PHE   B 70  ? 0.2275 0.1412 0.1702 0.0175  -0.0396 0.0007  76  PHE   C CG  
1645 C CD1 . PHE   B 70  ? 0.2356 0.1486 0.1678 0.0173  -0.0371 0.0034  76  PHE   C CD1 
1646 C CD2 . PHE   B 70  ? 0.2400 0.1507 0.1774 0.0196  -0.0442 -0.0030 76  PHE   C CD2 
1647 C CE1 . PHE   B 70  ? 0.2442 0.1541 0.1634 0.0190  -0.0381 0.0034  76  PHE   C CE1 
1648 C CE2 . PHE   B 70  ? 0.2492 0.1562 0.1704 0.0220  -0.0446 -0.0029 76  PHE   C CE2 
1649 C CZ  . PHE   B 70  ? 0.2327 0.1397 0.1462 0.0216  -0.0410 0.0009  76  PHE   C CZ  
1650 N N   . SER   B 71  ? 0.2195 0.1366 0.2169 0.0181  -0.0509 -0.0078 77  SER   C N   
1651 C CA  . SER   B 71  ? 0.2394 0.1540 0.2455 0.0198  -0.0610 -0.0151 77  SER   C CA  
1652 C C   . SER   B 71  ? 0.2644 0.1742 0.2510 0.0219  -0.0643 -0.0190 77  SER   C C   
1653 O O   . SER   B 71  ? 0.2764 0.1861 0.2489 0.0211  -0.0576 -0.0151 77  SER   C O   
1654 C CB  . SER   B 71  ? 0.2428 0.1601 0.2765 0.0180  -0.0598 -0.0150 77  SER   C CB  
1655 O OG  . SER   B 71  ? 0.2522 0.1707 0.2839 0.0164  -0.0519 -0.0112 77  SER   C OG  
1656 N N   . LYS   B 72  ? 0.2835 0.1886 0.2687 0.0253  -0.0749 -0.0268 78  LYS   C N   
1657 C CA  . LYS   B 72  ? 0.3014 0.2004 0.2671 0.0287  -0.0773 -0.0307 78  LYS   C CA  
1658 C C   . LYS   B 72  ? 0.3127 0.2124 0.2880 0.0265  -0.0731 -0.0307 78  LYS   C C   
1659 O O   . LYS   B 72  ? 0.3106 0.2142 0.3107 0.0234  -0.0723 -0.0304 78  LYS   C O   
1660 C CB  . LYS   B 72  ? 0.3472 0.2395 0.3065 0.0344  -0.0909 -0.0399 78  LYS   C CB  
1661 C CG  . LYS   B 72  ? 0.4213 0.3116 0.3634 0.0381  -0.0938 -0.0387 78  LYS   C CG  
1662 C CD  . LYS   B 72  ? 0.5061 0.3879 0.4335 0.0458  -0.1068 -0.0472 78  LYS   C CD  
1663 C CE  . LYS   B 72  ? 0.5711 0.4517 0.4860 0.0497  -0.1104 -0.0456 78  LYS   C CE  
1664 N NZ  . LYS   B 72  ? 0.6220 0.4930 0.5173 0.0589  -0.1230 -0.0534 78  LYS   C NZ  
1665 N N   . PRO   B 73  ? 0.3134 0.2093 0.2709 0.0282  -0.0693 -0.0302 79  PRO   C N   
1666 C CA  . PRO   B 73  ? 0.3149 0.2116 0.2813 0.0261  -0.0645 -0.0294 79  PRO   C CA  
1667 C C   . PRO   B 73  ? 0.3091 0.2034 0.2940 0.0268  -0.0726 -0.0374 79  PRO   C C   
1668 O O   . PRO   B 73  ? 0.3135 0.2012 0.2911 0.0314  -0.0830 -0.0459 79  PRO   C O   
1669 C CB  . PRO   B 73  ? 0.3392 0.2305 0.2824 0.0294  -0.0609 -0.0289 79  PRO   C CB  
1670 C CG  . PRO   B 73  ? 0.3625 0.2518 0.2862 0.0323  -0.0607 -0.0266 79  PRO   C CG  
1671 C CD  . PRO   B 73  ? 0.3212 0.2120 0.2516 0.0325  -0.0679 -0.0291 79  PRO   C CD  
1672 N N   . SER   B 74  ? 0.2930 0.1925 0.3033 0.0227  -0.0683 -0.0345 80  SER   C N   
1673 C CA  . SER   B 74  ? 0.2976 0.1955 0.3322 0.0226  -0.0755 -0.0414 80  SER   C CA  
1674 C C   . SER   B 74  ? 0.2902 0.1916 0.3440 0.0194  -0.0671 -0.0370 80  SER   C C   
1675 O O   . SER   B 74  ? 0.2719 0.1774 0.3190 0.0175  -0.0562 -0.0282 80  SER   C O   
1676 C CB  . SER   B 74  ? 0.3144 0.2160 0.3721 0.0214  -0.0809 -0.0423 80  SER   C CB  
1677 O OG  . SER   B 74  ? 0.3683 0.2677 0.4102 0.0241  -0.0877 -0.0448 80  SER   C OG  
1678 N N   . LEU   B 75  ? 0.2949 0.1947 0.3737 0.0192  -0.0728 -0.0430 81  LEU   C N   
1679 C CA  . LEU   B 75  ? 0.3076 0.2105 0.4092 0.0166  -0.0652 -0.0389 81  LEU   C CA  
1680 C C   . LEU   B 75  ? 0.3160 0.2261 0.4464 0.0138  -0.0598 -0.0317 81  LEU   C C   
1681 O O   . LEU   B 75  ? 0.3200 0.2299 0.4725 0.0138  -0.0679 -0.0366 81  LEU   C O   
1682 C CB  . LEU   B 75  ? 0.3201 0.2164 0.4364 0.0182  -0.0751 -0.0501 81  LEU   C CB  
1683 C CG  . LEU   B 75  ? 0.3465 0.2448 0.4879 0.0159  -0.0680 -0.0469 81  LEU   C CG  
1684 C CD1 . LEU   B 75  ? 0.3694 0.2681 0.4907 0.0158  -0.0573 -0.0404 81  LEU   C CD1 
1685 C CD2 . LEU   B 75  ? 0.3565 0.2475 0.5149 0.0177  -0.0799 -0.0599 81  LEU   C CD2 
1686 N N   . ILE   B 76  ? 0.3055 0.2214 0.4356 0.0121  -0.0464 -0.0200 82  ILE   C N   
1687 C CA  . ILE   B 76  ? 0.3052 0.2267 0.4573 0.0110  -0.0389 -0.0116 82  ILE   C CA  
1688 C C   . ILE   B 76  ? 0.3025 0.2277 0.4724 0.0103  -0.0265 -0.0022 82  ILE   C C   
1689 O O   . ILE   B 76  ? 0.3122 0.2376 0.4658 0.0104  -0.0206 0.0018  82  ILE   C O   
1690 C CB  . ILE   B 76  ? 0.3213 0.2450 0.4492 0.0114  -0.0344 -0.0058 82  ILE   C CB  
1691 C CG1 . ILE   B 76  ? 0.3378 0.2583 0.4526 0.0125  -0.0457 -0.0137 82  ILE   C CG1 
1692 C CG2 . ILE   B 76  ? 0.3287 0.2571 0.4720 0.0116  -0.0234 0.0046  82  ILE   C CG2 
1693 C CD1 . ILE   B 76  ? 0.3547 0.2766 0.4470 0.0129  -0.0420 -0.0090 82  ILE   C CD1 
1694 N N   . PHE   B 77  ? 0.2894 0.2176 0.4935 0.0102  -0.0218 0.0024  83  PHE   C N   
1695 C CA  . PHE   B 77  ? 0.2838 0.2153 0.5040 0.0107  -0.0081 0.0134  83  PHE   C CA  
1696 C C   . PHE   B 77  ? 0.2850 0.2193 0.4826 0.0127  0.0034  0.0246  83  PHE   C C   
1697 O O   . PHE   B 77  ? 0.2996 0.2345 0.4905 0.0135  0.0039  0.0263  83  PHE   C O   
1698 C CB  . PHE   B 77  ? 0.2724 0.2058 0.5375 0.0108  -0.0048 0.0163  83  PHE   C CB  
1699 C CG  . PHE   B 77  ? 0.2860 0.2218 0.5694 0.0120  0.0090  0.0271  83  PHE   C CG  
1700 C CD1 . PHE   B 77  ? 0.2989 0.2332 0.5916 0.0108  0.0072  0.0235  83  PHE   C CD1 
1701 C CD2 . PHE   B 77  ? 0.3008 0.2399 0.5914 0.0151  0.0244  0.0411  83  PHE   C CD2 
1702 C CE1 . PHE   B 77  ? 0.3043 0.2409 0.6146 0.0123  0.0204  0.0342  83  PHE   C CE1 
1703 C CE2 . PHE   B 77  ? 0.3111 0.2519 0.6167 0.0174  0.0377  0.0520  83  PHE   C CE2 
1704 C CZ  . PHE   B 77  ? 0.3032 0.2432 0.6190 0.0158  0.0356  0.0488  83  PHE   C CZ  
1705 N N   . VAL   B 78  ? 0.2604 0.1957 0.4450 0.0137  0.0116  0.0315  84  VAL   C N   
1706 C CA  . VAL   B 78  ? 0.2549 0.1917 0.4164 0.0163  0.0207  0.0410  84  VAL   C CA  
1707 C C   . VAL   B 78  ? 0.2524 0.1913 0.4303 0.0196  0.0347  0.0533  84  VAL   C C   
1708 O O   . VAL   B 78  ? 0.2459 0.1854 0.4353 0.0193  0.0371  0.0549  84  VAL   C O   
1709 C CB  . VAL   B 78  ? 0.2750 0.2107 0.4034 0.0153  0.0168  0.0386  84  VAL   C CB  
1710 C CG1 . VAL   B 78  ? 0.2953 0.2319 0.4006 0.0182  0.0241  0.0472  84  VAL   C CG1 
1711 C CG2 . VAL   B 78  ? 0.2861 0.2190 0.3986 0.0131  0.0046  0.0276  84  VAL   C CG2 
1712 N N   . GLU   B 79  ? 0.2526 0.1921 0.4296 0.0237  0.0447  0.0625  85  GLU   C N   
1713 C CA  . GLU   B 79  ? 0.2618 0.2021 0.4501 0.0289  0.0598  0.0760  85  GLU   C CA  
1714 C C   . GLU   B 79  ? 0.2732 0.2136 0.4365 0.0308  0.0626  0.0806  85  GLU   C C   
1715 O O   . GLU   B 79  ? 0.2747 0.2144 0.4093 0.0288  0.0545  0.0751  85  GLU   C O   
1716 C CB  . GLU   B 79  ? 0.3047 0.2438 0.4884 0.0344  0.0702  0.0848  85  GLU   C CB  
1717 C CG  . GLU   B 79  ? 0.3437 0.2833 0.5599 0.0339  0.0716  0.0842  85  GLU   C CG  
1718 C CD  . GLU   B 79  ? 0.4015 0.3431 0.6630 0.0330  0.0755  0.0867  85  GLU   C CD  
1719 O OE1 . GLU   B 79  ? 0.4367 0.3789 0.7073 0.0362  0.0862  0.0961  85  GLU   C OE1 
1720 O OE2 . GLU   B 79  ? 0.3847 0.3271 0.6739 0.0291  0.0671  0.0790  85  GLU   C OE2 
1721 N N   . ALA   B 80  ? 0.2791 0.2204 0.4546 0.0350  0.0743  0.0915  86  ALA   C N   
1722 C CA  . ALA   B 80  ? 0.2943 0.2358 0.4487 0.0374  0.0767  0.0969  86  ALA   C CA  
1723 C C   . ALA   B 80  ? 0.3103 0.2497 0.4257 0.0412  0.0759  0.0990  86  ALA   C C   
1724 O O   . ALA   B 80  ? 0.3111 0.2482 0.4191 0.0455  0.0812  0.1027  86  ALA   C O   
1725 C CB  . ALA   B 80  ? 0.2795 0.2220 0.4542 0.0429  0.0910  0.1100  86  ALA   C CB  
1726 N N   . SER   B 81  ? 0.3082 0.2479 0.4002 0.0397  0.0688  0.0961  87  SER   C N   
1727 C CA  . SER   B 81  ? 0.3280 0.2655 0.3850 0.0429  0.0656  0.0970  87  SER   C CA  
1728 C C   . SER   B 81  ? 0.3445 0.2827 0.3906 0.0471  0.0686  0.1048  87  SER   C C   
1729 O O   . SER   B 81  ? 0.3441 0.2845 0.4106 0.0474  0.0744  0.1100  87  SER   C O   
1730 C CB  . SER   B 81  ? 0.3320 0.2694 0.3737 0.0367  0.0522  0.0852  87  SER   C CB  
1731 O OG  . SER   B 81  ? 0.3236 0.2631 0.3680 0.0323  0.0461  0.0812  87  SER   C OG  
1732 N N   . GLU   B 82  ? 0.3524 0.2884 0.3680 0.0503  0.0639  0.1054  88  GLU   C N   
1733 C CA  . GLU   B 82  ? 0.3606 0.2973 0.3666 0.0548  0.0653  0.1128  88  GLU   C CA  
1734 C C   . GLU   B 82  ? 0.3443 0.2848 0.3587 0.0482  0.0578  0.1083  88  GLU   C C   
1735 O O   . GLU   B 82  ? 0.3416 0.2838 0.3568 0.0509  0.0600  0.1149  88  GLU   C O   
1736 C CB  . GLU   B 82  ? 0.4183 0.3506 0.3906 0.0616  0.0619  0.1151  88  GLU   C CB  
1737 C CG  . GLU   B 82  ? 0.5383 0.4696 0.4931 0.0566  0.0485  0.1043  88  GLU   C CG  
1738 C CD  . GLU   B 82  ? 0.6621 0.5899 0.5875 0.0619  0.0411  0.1047  88  GLU   C CD  
1739 O OE1 . GLU   B 82  ? 0.6768 0.5991 0.5837 0.0711  0.0461  0.1102  88  GLU   C OE1 
1740 O OE2 . GLU   B 82  ? 0.6928 0.6225 0.6139 0.0573  0.0300  0.0994  88  GLU   C OE2 
1741 N N   . TYR   B 83  ? 0.3282 0.2699 0.3492 0.0404  0.0498  0.0977  89  TYR   C N   
1742 C CA  . TYR   B 83  ? 0.3158 0.2598 0.3423 0.0348  0.0434  0.0928  89  TYR   C CA  
1743 C C   . TYR   B 83  ? 0.3096 0.2546 0.3621 0.0298  0.0445  0.0876  89  TYR   C C   
1744 O O   . TYR   B 83  ? 0.3124 0.2584 0.3708 0.0265  0.0415  0.0847  89  TYR   C O   
1745 C CB  . TYR   B 83  ? 0.3080 0.2510 0.3153 0.0313  0.0325  0.0850  89  TYR   C CB  
1746 C CG  . TYR   B 83  ? 0.2992 0.2400 0.3011 0.0292  0.0291  0.0778  89  TYR   C CG  
1747 C CD1 . TYR   B 83  ? 0.3075 0.2456 0.2922 0.0331  0.0291  0.0790  89  TYR   C CD1 
1748 C CD2 . TYR   B 83  ? 0.2951 0.2357 0.3069 0.0240  0.0254  0.0695  89  TYR   C CD2 
1749 C CE1 . TYR   B 83  ? 0.3101 0.2463 0.2909 0.0312  0.0262  0.0727  89  TYR   C CE1 
1750 C CE2 . TYR   B 83  ? 0.3027 0.2414 0.3095 0.0224  0.0218  0.0633  89  TYR   C CE2 
1751 C CZ  . TYR   B 83  ? 0.3166 0.2534 0.3091 0.0257  0.0226  0.0652  89  TYR   C CZ  
1752 O OH  . TYR   B 83  ? 0.3181 0.2531 0.3067 0.0242  0.0194  0.0594  89  TYR   C OH  
1753 N N   . TYR   B 84  ? 0.2909 0.2350 0.3594 0.0296  0.0485  0.0861  90  TYR   C N   
1754 C CA  . TYR   B 84  ? 0.2759 0.2201 0.3706 0.0257  0.0482  0.0805  90  TYR   C CA  
1755 C C   . TYR   B 84  ? 0.2836 0.2281 0.4031 0.0285  0.0574  0.0862  90  TYR   C C   
1756 O O   . TYR   B 84  ? 0.2876 0.2314 0.4015 0.0322  0.0621  0.0909  90  TYR   C O   
1757 C CB  . TYR   B 84  ? 0.2610 0.2031 0.3521 0.0211  0.0386  0.0683  90  TYR   C CB  
1758 C CG  . TYR   B 84  ? 0.2547 0.1957 0.3302 0.0179  0.0307  0.0617  90  TYR   C CG  
1759 C CD1 . TYR   B 84  ? 0.2541 0.1952 0.3363 0.0168  0.0311  0.0616  90  TYR   C CD1 
1760 C CD2 . TYR   B 84  ? 0.2638 0.2032 0.3195 0.0165  0.0237  0.0561  90  TYR   C CD2 
1761 C CE1 . TYR   B 84  ? 0.2633 0.2029 0.3325 0.0146  0.0254  0.0565  90  TYR   C CE1 
1762 C CE2 . TYR   B 84  ? 0.2694 0.2075 0.3131 0.0143  0.0181  0.0513  90  TYR   C CE2 
1763 C CZ  . TYR   B 84  ? 0.2768 0.2149 0.3272 0.0135  0.0193  0.0517  90  TYR   C CZ  
1764 O OH  . TYR   B 84  ? 0.2813 0.2175 0.3208 0.0121  0.0153  0.0480  90  TYR   C OH  
1765 N N   . PRO   B 85  ? 0.2830 0.2279 0.4316 0.0268  0.0601  0.0853  91  PRO   C N   
1766 C CA  . PRO   B 85  ? 0.2852 0.2304 0.4631 0.0287  0.0681  0.0899  91  PRO   C CA  
1767 C C   . PRO   B 85  ? 0.2870 0.2306 0.4722 0.0254  0.0606  0.0799  91  PRO   C C   
1768 O O   . PRO   B 85  ? 0.2772 0.2193 0.4423 0.0222  0.0500  0.0703  91  PRO   C O   
1769 C CB  . PRO   B 85  ? 0.2914 0.2372 0.4984 0.0271  0.0707  0.0899  91  PRO   C CB  
1770 C CG  . PRO   B 85  ? 0.2969 0.2412 0.4912 0.0224  0.0598  0.0790  91  PRO   C CG  
1771 C CD  . PRO   B 85  ? 0.2754 0.2199 0.4326 0.0229  0.0553  0.0790  91  PRO   C CD  
1772 N N   . ALA   B 86  ? 0.2667 0.2106 0.4827 0.0264  0.0660  0.0825  92  ALA   C N   
1773 C CA  . ALA   B 86  ? 0.2738 0.2164 0.5013 0.0233  0.0578  0.0730  92  ALA   C CA  
1774 C C   . ALA   B 86  ? 0.2792 0.2197 0.5151 0.0181  0.0450  0.0591  92  ALA   C C   
1775 O O   . ALA   B 86  ? 0.2836 0.2240 0.5408 0.0175  0.0470  0.0593  92  ALA   C O   
1776 C CB  . ALA   B 86  ? 0.2619 0.2055 0.5262 0.0256  0.0669  0.0798  92  ALA   C CB  
1777 N N   . ARG   B 87  ? 0.2710 0.2092 0.4875 0.0154  0.0325  0.0476  93  ARG   C N   
1778 C CA  . ARG   B 87  ? 0.2608 0.1952 0.4793 0.0123  0.0208  0.0346  93  ARG   C CA  
1779 C C   . ARG   B 87  ? 0.2672 0.1986 0.4697 0.0109  0.0083  0.0235  93  ARG   C C   
1780 O O   . ARG   B 87  ? 0.2558 0.1884 0.4397 0.0116  0.0088  0.0261  93  ARG   C O   
1781 C CB  . ARG   B 87  ? 0.2580 0.1916 0.4549 0.0121  0.0214  0.0350  93  ARG   C CB  
1782 C CG  . ARG   B 87  ? 0.2618 0.1966 0.4231 0.0129  0.0219  0.0387  93  ARG   C CG  
1783 C CD  . ARG   B 87  ? 0.2680 0.2017 0.4095 0.0124  0.0206  0.0377  93  ARG   C CD  
1784 N NE  . ARG   B 87  ? 0.2574 0.1904 0.3684 0.0121  0.0160  0.0357  93  ARG   C NE  
1785 C CZ  . ARG   B 87  ? 0.2965 0.2271 0.3899 0.0113  0.0120  0.0317  93  ARG   C CZ  
1786 N NH1 . ARG   B 87  ? 0.2942 0.2226 0.3949 0.0110  0.0122  0.0290  93  ARG   C NH1 
1787 N NH2 . ARG   B 87  ? 0.3083 0.2385 0.3782 0.0112  0.0085  0.0306  93  ARG   C NH2 
1788 N N   . TYR   B 88  ? 0.2759 0.2024 0.4806 0.0096  -0.0032 0.0108  94  TYR   C N   
1789 C CA  . TYR   B 88  ? 0.2911 0.2137 0.4759 0.0095  -0.0153 0.0004  94  TYR   C CA  
1790 C C   . TYR   B 88  ? 0.2837 0.2045 0.4316 0.0100  -0.0155 0.0002  94  TYR   C C   
1791 O O   . TYR   B 88  ? 0.2945 0.2139 0.4369 0.0102  -0.0128 0.0007  94  TYR   C O   
1792 C CB  . TYR   B 88  ? 0.3093 0.2258 0.5085 0.0095  -0.0283 -0.0135 94  TYR   C CB  
1793 C CG  . TYR   B 88  ? 0.3241 0.2420 0.5595 0.0088  -0.0322 -0.0155 94  TYR   C CG  
1794 C CD1 . TYR   B 88  ? 0.3467 0.2649 0.5807 0.0090  -0.0390 -0.0186 94  TYR   C CD1 
1795 C CD2 . TYR   B 88  ? 0.3369 0.2560 0.6107 0.0079  -0.0280 -0.0131 94  TYR   C CD2 
1796 C CE1 . TYR   B 88  ? 0.3566 0.2764 0.6272 0.0084  -0.0425 -0.0198 94  TYR   C CE1 
1797 C CE2 . TYR   B 88  ? 0.3393 0.2600 0.6512 0.0073  -0.0310 -0.0142 94  TYR   C CE2 
1798 C CZ  . TYR   B 88  ? 0.3603 0.2814 0.6708 0.0074  -0.0383 -0.0174 94  TYR   C CZ  
1799 O OH  . TYR   B 88  ? 0.3808 0.3036 0.7324 0.0068  -0.0413 -0.0180 94  TYR   C OH  
1800 N N   . GLN   B 89  ? 0.2675 0.1888 0.3928 0.0104  -0.0177 0.0004  95  GLN   C N   
1801 C CA  . GLN   B 89  ? 0.2658 0.1853 0.3593 0.0110  -0.0181 0.0004  95  GLN   C CA  
1802 C C   . GLN   B 89  ? 0.2677 0.1817 0.3459 0.0124  -0.0291 -0.0098 95  GLN   C C   
1803 O O   . GLN   B 89  ? 0.2722 0.1864 0.3564 0.0125  -0.0344 -0.0129 95  GLN   C O   
1804 C CB  . GLN   B 89  ? 0.2669 0.1912 0.3463 0.0108  -0.0110 0.0101  95  GLN   C CB  
1805 C CG  . GLN   B 89  ? 0.2716 0.1944 0.3229 0.0110  -0.0119 0.0102  95  GLN   C CG  
1806 C CD  . GLN   B 89  ? 0.2760 0.2029 0.3163 0.0109  -0.0052 0.0196  95  GLN   C CD  
1807 O OE1 . GLN   B 89  ? 0.2901 0.2203 0.3398 0.0114  0.0016  0.0270  95  GLN   C OE1 
1808 N NE2 . GLN   B 89  ? 0.2929 0.2189 0.3127 0.0109  -0.0076 0.0191  95  GLN   C NE2 
1809 N N   . SER   B 90  ? 0.2560 0.1646 0.3152 0.0142  -0.0320 -0.0147 96  SER   C N   
1810 C CA  . SER   B 90  ? 0.2504 0.1525 0.2920 0.0172  -0.0416 -0.0238 96  SER   C CA  
1811 C C   . SER   B 90  ? 0.2486 0.1511 0.2642 0.0180  -0.0396 -0.0199 96  SER   C C   
1812 O O   . SER   B 90  ? 0.2433 0.1504 0.2532 0.0162  -0.0317 -0.0113 96  SER   C O   
1813 C CB  . SER   B 90  ? 0.2630 0.1567 0.2974 0.0205  -0.0458 -0.0320 96  SER   C CB  
1814 O OG  . SER   B 90  ? 0.2830 0.1766 0.3037 0.0207  -0.0375 -0.0262 96  SER   C OG  
1815 N N   . HIS   B 91  ? 0.2463 0.1438 0.2471 0.0211  -0.0474 -0.0262 97  HIS   C N   
1816 C CA  . HIS   B 91  ? 0.2537 0.1505 0.2314 0.0226  -0.0462 -0.0233 97  HIS   C CA  
1817 C C   . HIS   B 91  ? 0.2478 0.1522 0.2296 0.0189  -0.0406 -0.0149 97  HIS   C C   
1818 O O   . HIS   B 91  ? 0.2564 0.1621 0.2240 0.0186  -0.0359 -0.0096 97  HIS   C O   
1819 C CB  . HIS   B 91  ? 0.2593 0.1517 0.2174 0.0252  -0.0413 -0.0214 97  HIS   C CB  
1820 C CG  . HIS   B 91  ? 0.3134 0.1963 0.2630 0.0304  -0.0463 -0.0300 97  HIS   C CG  
1821 N ND1 . HIS   B 91  ? 0.3451 0.2199 0.2726 0.0366  -0.0514 -0.0351 97  HIS   C ND1 
1822 C CD2 . HIS   B 91  ? 0.3335 0.2132 0.2933 0.0310  -0.0469 -0.0344 97  HIS   C CD2 
1823 C CE1 . HIS   B 91  ? 0.3562 0.2224 0.2788 0.0412  -0.0554 -0.0429 97  HIS   C CE1 
1824 N NE2 . HIS   B 91  ? 0.3445 0.2133 0.2868 0.0377  -0.0529 -0.0431 97  HIS   C NE2 
1825 N N   . LEU   B 92  ? 0.2273 0.1360 0.2294 0.0167  -0.0412 -0.0141 98  LEU   C N   
1826 C CA  . LEU   B 92  ? 0.2269 0.1415 0.2329 0.0144  -0.0352 -0.0065 98  LEU   C CA  
1827 C C   . LEU   B 92  ? 0.2249 0.1396 0.2302 0.0150  -0.0400 -0.0086 98  LEU   C C   
1828 O O   . LEU   B 92  ? 0.2190 0.1315 0.2341 0.0163  -0.0478 -0.0150 98  LEU   C O   
1829 C CB  . LEU   B 92  ? 0.2116 0.1305 0.2412 0.0127  -0.0295 -0.0018 98  LEU   C CB  
1830 C CG  . LEU   B 92  ? 0.2227 0.1464 0.2538 0.0119  -0.0215 0.0069  98  LEU   C CG  
1831 C CD1 . LEU   B 92  ? 0.2155 0.1401 0.2282 0.0116  -0.0168 0.0122  98  LEU   C CD1 
1832 C CD2 . LEU   B 92  ? 0.2291 0.1559 0.2851 0.0118  -0.0152 0.0119  98  LEU   C CD2 
1833 N N   . MET   B 93  ? 0.2223 0.1390 0.2162 0.0144  -0.0361 -0.0036 99  MET   C N   
1834 C CA  . MET   B 93  ? 0.2170 0.1340 0.2088 0.0150  -0.0389 -0.0042 99  MET   C CA  
1835 C C   . MET   B 93  ? 0.2138 0.1351 0.2146 0.0137  -0.0312 0.0028  99  MET   C C   
1836 O O   . MET   B 93  ? 0.2194 0.1421 0.2136 0.0130  -0.0249 0.0080  99  MET   C O   
1837 C CB  . MET   B 93  ? 0.2435 0.1580 0.2123 0.0161  -0.0396 -0.0039 99  MET   C CB  
1838 C CG  . MET   B 93  ? 0.2724 0.1816 0.2288 0.0191  -0.0448 -0.0091 99  MET   C CG  
1839 S SD  . MET   B 93  ? 0.3247 0.2307 0.2572 0.0211  -0.0427 -0.0065 99  MET   C SD  
1840 C CE  . MET   B 93  ? 0.2617 0.1713 0.1941 0.0178  -0.0343 0.0004  99  MET   C CE  
1841 N N   . LEU   B 94  ? 0.2076 0.1301 0.2215 0.0140  -0.0318 0.0029  100 LEU   C N   
1842 C CA  . LEU   B 94  ? 0.2191 0.1441 0.2401 0.0142  -0.0233 0.0098  100 LEU   C CA  
1843 C C   . LEU   B 94  ? 0.2079 0.1322 0.2201 0.0150  -0.0235 0.0103  100 LEU   C C   
1844 O O   . LEU   B 94  ? 0.2235 0.1465 0.2362 0.0153  -0.0306 0.0056  100 LEU   C O   
1845 C CB  . LEU   B 94  ? 0.2357 0.1628 0.2860 0.0145  -0.0209 0.0114  100 LEU   C CB  
1846 C CG  . LEU   B 94  ? 0.2695 0.1976 0.3348 0.0138  -0.0194 0.0117  100 LEU   C CG  
1847 C CD1 . LEU   B 94  ? 0.2915 0.2213 0.3905 0.0141  -0.0179 0.0128  100 LEU   C CD1 
1848 C CD2 . LEU   B 94  ? 0.2852 0.2143 0.3397 0.0143  -0.0103 0.0187  100 LEU   C CD2 
1849 N N   . ALA   B 95  ? 0.2028 0.1272 0.2074 0.0159  -0.0158 0.0160  101 ALA   C N   
1850 C CA  . ALA   B 95  ? 0.2140 0.1371 0.2115 0.0171  -0.0141 0.0171  101 ALA   C CA  
1851 C C   . ALA   B 95  ? 0.2253 0.1483 0.2284 0.0198  -0.0037 0.0240  101 ALA   C C   
1852 O O   . ALA   B 95  ? 0.2241 0.1480 0.2311 0.0209  0.0022  0.0284  101 ALA   C O   
1853 C CB  . ALA   B 95  ? 0.2225 0.1435 0.1964 0.0165  -0.0160 0.0160  101 ALA   C CB  
1854 N N   . VAL   B 96  ? 0.2346 0.1561 0.2377 0.0216  -0.0007 0.0254  102 VAL   C N   
1855 C CA  . VAL   B 96  ? 0.2415 0.1612 0.2458 0.0256  0.0104  0.0321  102 VAL   C CA  
1856 C C   . VAL   B 96  ? 0.2651 0.1811 0.2421 0.0273  0.0119  0.0326  102 VAL   C C   
1857 O O   . VAL   B 96  ? 0.2816 0.1954 0.2451 0.0263  0.0074  0.0288  102 VAL   C O   
1858 C CB  . VAL   B 96  ? 0.2404 0.1594 0.2583 0.0275  0.0138  0.0337  102 VAL   C CB  
1859 C CG1 . VAL   B 96  ? 0.2493 0.1646 0.2634 0.0331  0.0268  0.0410  102 VAL   C CG1 
1860 C CG2 . VAL   B 96  ? 0.2398 0.1626 0.2883 0.0258  0.0102  0.0326  102 VAL   C CG2 
1861 N N   . GLY   B 97  ? 0.2672 0.1821 0.2367 0.0299  0.0176  0.0370  103 GLY   C N   
1862 C CA  . GLY   B 97  ? 0.2846 0.1955 0.2288 0.0320  0.0172  0.0368  103 GLY   C CA  
1863 C C   . GLY   B 97  ? 0.2958 0.2060 0.2335 0.0354  0.0222  0.0419  103 GLY   C C   
1864 O O   . GLY   B 97  ? 0.2956 0.2089 0.2494 0.0357  0.0267  0.0461  103 GLY   C O   
1865 N N   . HIS   B 98  ? 0.2956 0.2016 0.2107 0.0382  0.0208  0.0415  104 HIS   C N   
1866 C CA  . HIS   B 98  ? 0.3032 0.2078 0.2087 0.0426  0.0247  0.0466  104 HIS   C CA  
1867 C C   . HIS   B 98  ? 0.3043 0.2130 0.2103 0.0382  0.0173  0.0447  104 HIS   C C   
1868 O O   . HIS   B 98  ? 0.3029 0.2124 0.2037 0.0338  0.0084  0.0391  104 HIS   C O   
1869 C CB  . HIS   B 98  ? 0.3463 0.2432 0.2261 0.0490  0.0256  0.0466  104 HIS   C CB  
1870 C CG  . HIS   B 98  ? 0.4057 0.3002 0.2732 0.0553  0.0296  0.0523  104 HIS   C CG  
1871 N ND1 . HIS   B 98  ? 0.4370 0.3311 0.3125 0.0611  0.0420  0.0613  104 HIS   C ND1 
1872 C CD2 . HIS   B 98  ? 0.4337 0.3263 0.2842 0.0565  0.0223  0.0506  104 HIS   C CD2 
1873 C CE1 . HIS   B 98  ? 0.4542 0.3459 0.3142 0.0662  0.0422  0.0650  104 HIS   C CE1 
1874 N NE2 . HIS   B 98  ? 0.4587 0.3494 0.3030 0.0637  0.0298  0.0584  104 HIS   C NE2 
1875 N N   . SER   B 99  ? 0.2981 0.2092 0.2116 0.0399  0.0221  0.0504  105 SER   C N   
1876 C CA  . SER   B 99  ? 0.2982 0.2130 0.2136 0.0366  0.0170  0.0500  105 SER   C CA  
1877 C C   . SER   B 99  ? 0.3158 0.2305 0.2305 0.0420  0.0242  0.0582  105 SER   C C   
1878 O O   . SER   B 99  ? 0.3127 0.2290 0.2438 0.0439  0.0330  0.0636  105 SER   C O   
1879 C CB  . SER   B 99  ? 0.2934 0.2133 0.2297 0.0305  0.0144  0.0470  105 SER   C CB  
1880 O OG  . SER   B 99  ? 0.3191 0.2421 0.2593 0.0283  0.0120  0.0478  105 SER   C OG  
1881 N N   . GLU   B 100 ? 0.3264 0.2396 0.2245 0.0443  0.0199  0.0590  106 GLU   C N   
1882 C CA  . GLU   B 100 ? 0.3360 0.2492 0.2307 0.0495  0.0246  0.0666  106 GLU   C CA  
1883 C C   . GLU   B 100 ? 0.3416 0.2601 0.2452 0.0441  0.0182  0.0653  106 GLU   C C   
1884 O O   . GLU   B 100 ? 0.3270 0.2473 0.2325 0.0380  0.0099  0.0587  106 GLU   C O   
1885 C CB  . GLU   B 100 ? 0.3722 0.2785 0.2390 0.0575  0.0229  0.0680  106 GLU   C CB  
1886 C CG  . GLU   B 100 ? 0.4750 0.3751 0.3327 0.0645  0.0319  0.0707  106 GLU   C CG  
1887 C CD  . GLU   B 100 ? 0.5574 0.4485 0.3840 0.0737  0.0301  0.0707  106 GLU   C CD  
1888 O OE1 . GLU   B 100 ? 0.6615 0.5512 0.4745 0.0774  0.0250  0.0723  106 GLU   C OE1 
1889 O OE2 . GLU   B 100 ? 0.5549 0.4398 0.3705 0.0777  0.0333  0.0689  106 GLU   C OE2 
1890 N N   . PRO   B 101 ? 0.3489 0.2695 0.2581 0.0468  0.0228  0.0721  107 PRO   C N   
1891 C CA  . PRO   B 101 ? 0.3360 0.2613 0.2549 0.0417  0.0176  0.0712  107 PRO   C CA  
1892 C C   . PRO   B 101 ? 0.3325 0.2576 0.2400 0.0387  0.0058  0.0657  107 PRO   C C   
1893 O O   . PRO   B 101 ? 0.3200 0.2484 0.2380 0.0324  0.0013  0.0616  107 PRO   C O   
1894 C CB  . PRO   B 101 ? 0.3547 0.2808 0.2758 0.0473  0.0245  0.0806  107 PRO   C CB  
1895 C CG  . PRO   B 101 ? 0.3758 0.2992 0.3000 0.0532  0.0363  0.0866  107 PRO   C CG  
1896 C CD  . PRO   B 101 ? 0.3515 0.2700 0.2605 0.0548  0.0343  0.0819  107 PRO   C CD  
1897 N N   . GLY   B 102 ? 0.3332 0.2537 0.2199 0.0436  0.0010  0.0653  108 GLY   C N   
1898 C CA  . GLY   B 102 ? 0.3306 0.2505 0.2095 0.0410  -0.0109 0.0599  108 GLY   C CA  
1899 C C   . GLY   B 102 ? 0.3059 0.2257 0.1886 0.0349  -0.0159 0.0522  108 GLY   C C   
1900 O O   . GLY   B 102 ? 0.2960 0.2163 0.1794 0.0314  -0.0246 0.0483  108 GLY   C O   
1901 N N   . ASP   B 103 ? 0.2778 0.1970 0.1648 0.0338  -0.0102 0.0505  109 ASP   C N   
1902 C CA  . ASP   B 103 ? 0.2647 0.1839 0.1555 0.0286  -0.0142 0.0439  109 ASP   C CA  
1903 C C   . ASP   B 103 ? 0.2505 0.1741 0.1572 0.0226  -0.0148 0.0425  109 ASP   C C   
1904 O O   . ASP   B 103 ? 0.2368 0.1601 0.1457 0.0189  -0.0183 0.0379  109 ASP   C O   
1905 C CB  . ASP   B 103 ? 0.2689 0.1856 0.1587 0.0297  -0.0091 0.0424  109 ASP   C CB  
1906 C CG  . ASP   B 103 ? 0.3147 0.2253 0.1863 0.0361  -0.0084 0.0427  109 ASP   C CG  
1907 O OD1 . ASP   B 103 ? 0.3273 0.2345 0.1857 0.0376  -0.0160 0.0399  109 ASP   C OD1 
1908 O OD2 . ASP   B 103 ? 0.3422 0.2508 0.2132 0.0400  -0.0002 0.0458  109 ASP   C OD2 
1909 N N   . CYS   B 104 ? 0.2409 0.1679 0.1584 0.0222  -0.0107 0.0465  110 CYS   C N   
1910 C CA  . CYS   B 104 ? 0.2456 0.1754 0.1762 0.0177  -0.0108 0.0448  110 CYS   C CA  
1911 C C   . CYS   B 104 ? 0.2370 0.1669 0.1660 0.0149  -0.0173 0.0426  110 CYS   C C   
1912 O O   . CYS   B 104 ? 0.2356 0.1654 0.1598 0.0162  -0.0217 0.0444  110 CYS   C O   
1913 C CB  . CYS   B 104 ? 0.2476 0.1803 0.1889 0.0184  -0.0060 0.0496  110 CYS   C CB  
1914 S SG  . CYS   B 104 ? 0.2795 0.2126 0.2329 0.0201  0.0023  0.0516  110 CYS   C SG  
1915 N N   . GLY   B 105 ? 0.2278 0.1573 0.1613 0.0119  -0.0179 0.0390  111 GLY   C N   
1916 C CA  . GLY   B 105 ? 0.2318 0.1610 0.1668 0.0097  -0.0219 0.0380  111 GLY   C CA  
1917 C C   . GLY   B 105 ? 0.2263 0.1527 0.1550 0.0090  -0.0256 0.0342  111 GLY   C C   
1918 O O   . GLY   B 105 ? 0.2330 0.1588 0.1654 0.0073  -0.0276 0.0336  111 GLY   C O   
1919 N N   . GLY   B 106 ? 0.2156 0.1402 0.1359 0.0108  -0.0258 0.0324  112 GLY   C N   
1920 C CA  . GLY   B 106 ? 0.2045 0.1261 0.1194 0.0104  -0.0288 0.0286  112 GLY   C CA  
1921 C C   . GLY   B 106 ? 0.2007 0.1220 0.1196 0.0087  -0.0267 0.0267  112 GLY   C C   
1922 O O   . GLY   B 106 ? 0.2024 0.1245 0.1247 0.0090  -0.0232 0.0265  112 GLY   C O   
1923 N N   . ILE   B 107 ? 0.1992 0.1187 0.1187 0.0075  -0.0291 0.0253  113 ILE   C N   
1924 C CA  . ILE   B 107 ? 0.2166 0.1350 0.1377 0.0073  -0.0268 0.0244  113 ILE   C CA  
1925 C C   . ILE   B 107 ? 0.2257 0.1425 0.1418 0.0083  -0.0265 0.0214  113 ILE   C C   
1926 O O   . ILE   B 107 ? 0.2319 0.1472 0.1440 0.0085  -0.0283 0.0199  113 ILE   C O   
1927 C CB  . ILE   B 107 ? 0.2421 0.1592 0.1683 0.0064  -0.0277 0.0259  113 ILE   C CB  
1928 C CG1 . ILE   B 107 ? 0.2712 0.1900 0.2059 0.0059  -0.0255 0.0298  113 ILE   C CG1 
1929 C CG2 . ILE   B 107 ? 0.2491 0.1634 0.1729 0.0076  -0.0253 0.0251  113 ILE   C CG2 
1930 C CD1 . ILE   B 107 ? 0.3290 0.2468 0.2726 0.0053  -0.0250 0.0327  113 ILE   C CD1 
1931 N N   . LEU   B 108 ? 0.2183 0.1346 0.1348 0.0092  -0.0246 0.0202  114 LEU   C N   
1932 C CA  . LEU   B 108 ? 0.2169 0.1316 0.1305 0.0104  -0.0252 0.0175  114 LEU   C CA  
1933 C C   . LEU   B 108 ? 0.2029 0.1149 0.1139 0.0115  -0.0249 0.0180  114 LEU   C C   
1934 O O   . LEU   B 108 ? 0.1944 0.1054 0.1051 0.0127  -0.0231 0.0191  114 LEU   C O   
1935 C CB  . LEU   B 108 ? 0.2193 0.1347 0.1362 0.0114  -0.0249 0.0156  114 LEU   C CB  
1936 C CG  . LEU   B 108 ? 0.2314 0.1452 0.1473 0.0131  -0.0271 0.0125  114 LEU   C CG  
1937 C CD1 . LEU   B 108 ? 0.2412 0.1552 0.1576 0.0128  -0.0271 0.0123  114 LEU   C CD1 
1938 C CD2 . LEU   B 108 ? 0.2410 0.1551 0.1632 0.0141  -0.0286 0.0097  114 LEU   C CD2 
1939 N N   . ARG   B 109 ? 0.2027 0.1129 0.1113 0.0119  -0.0258 0.0176  115 ARG   C N   
1940 C CA  . ARG   B 109 ? 0.2215 0.1288 0.1281 0.0139  -0.0241 0.0193  115 ARG   C CA  
1941 C C   . ARG   B 109 ? 0.2230 0.1284 0.1251 0.0160  -0.0253 0.0177  115 ARG   C C   
1942 O O   . ARG   B 109 ? 0.2203 0.1267 0.1234 0.0150  -0.0271 0.0156  115 ARG   C O   
1943 C CB  . ARG   B 109 ? 0.2528 0.1597 0.1653 0.0122  -0.0234 0.0222  115 ARG   C CB  
1944 C CG  . ARG   B 109 ? 0.3158 0.2226 0.2294 0.0104  -0.0266 0.0200  115 ARG   C CG  
1945 C CD  . ARG   B 109 ? 0.3679 0.2736 0.2897 0.0088  -0.0277 0.0215  115 ARG   C CD  
1946 N NE  . ARG   B 109 ? 0.4041 0.3117 0.3291 0.0068  -0.0309 0.0210  115 ARG   C NE  
1947 C CZ  . ARG   B 109 ? 0.4540 0.3624 0.3887 0.0056  -0.0315 0.0237  115 ARG   C CZ  
1948 N NH1 . ARG   B 109 ? 0.4587 0.3660 0.4021 0.0062  -0.0276 0.0277  115 ARG   C NH1 
1949 N NH2 . ARG   B 109 ? 0.4507 0.3608 0.3872 0.0043  -0.0355 0.0230  115 ARG   C NH2 
1950 N N   . CYS   B 110 ? 0.2122 0.1144 0.1090 0.0197  -0.0237 0.0191  116 CYS   C N   
1951 C CA  . CYS   B 110 ? 0.2380 0.1381 0.1302 0.0226  -0.0249 0.0184  116 CYS   C CA  
1952 C C   . CYS   B 110 ? 0.2542 0.1510 0.1456 0.0251  -0.0205 0.0234  116 CYS   C C   
1953 O O   . CYS   B 110 ? 0.2682 0.1651 0.1659 0.0236  -0.0171 0.0268  116 CYS   C O   
1954 C CB  . CYS   B 110 ? 0.2426 0.1406 0.1273 0.0266  -0.0279 0.0154  116 CYS   C CB  
1955 S SG  . CYS   B 110 ? 0.2466 0.1394 0.1208 0.0322  -0.0244 0.0177  116 CYS   C SG  
1956 N N   . GLN   B 111 ? 0.2690 0.1629 0.1545 0.0291  -0.0205 0.0243  117 GLN   C N   
1957 C CA  . GLN   B 111 ? 0.2749 0.1654 0.1605 0.0324  -0.0151 0.0301  117 GLN   C CA  
1958 C C   . GLN   B 111 ? 0.2909 0.1778 0.1717 0.0369  -0.0090 0.0347  117 GLN   C C   
1959 O O   . GLN   B 111 ? 0.3172 0.2019 0.2034 0.0387  -0.0025 0.0411  117 GLN   C O   
1960 C CB  . GLN   B 111 ? 0.3119 0.1998 0.1906 0.0370  -0.0162 0.0306  117 GLN   C CB  
1961 C CG  . GLN   B 111 ? 0.3581 0.2424 0.2214 0.0436  -0.0188 0.0289  117 GLN   C CG  
1962 C CD  . GLN   B 111 ? 0.5011 0.3831 0.3575 0.0484  -0.0217 0.0290  117 GLN   C CD  
1963 O OE1 . GLN   B 111 ? 0.5413 0.4258 0.3998 0.0468  -0.0284 0.0242  117 GLN   C OE1 
1964 N NE2 . GLN   B 111 ? 0.5545 0.4315 0.4031 0.0551  -0.0162 0.0353  117 GLN   C NE2 
1965 N N   . HIS   B 112 ? 0.2856 0.1716 0.1581 0.0387  -0.0105 0.0319  118 HIS   C N   
1966 C CA  . HIS   B 112 ? 0.3038 0.1851 0.1695 0.0439  -0.0042 0.0360  118 HIS   C CA  
1967 C C   . HIS   B 112 ? 0.3094 0.1936 0.1866 0.0395  -0.0012 0.0378  118 HIS   C C   
1968 O O   . HIS   B 112 ? 0.3337 0.2143 0.2096 0.0434  0.0059  0.0427  118 HIS   C O   
1969 C CB  . HIS   B 112 ? 0.3264 0.2030 0.1745 0.0501  -0.0078 0.0315  118 HIS   C CB  
1970 C CG  . HIS   B 112 ? 0.3182 0.1919 0.1548 0.0551  -0.0127 0.0292  118 HIS   C CG  
1971 N ND1 . HIS   B 112 ? 0.3302 0.2074 0.1694 0.0519  -0.0219 0.0225  118 HIS   C ND1 
1972 C CD2 . HIS   B 112 ? 0.3362 0.2038 0.1600 0.0633  -0.0093 0.0336  118 HIS   C CD2 
1973 C CE1 . HIS   B 112 ? 0.3457 0.2192 0.1744 0.0578  -0.0251 0.0222  118 HIS   C CE1 
1974 N NE2 . HIS   B 112 ? 0.3423 0.2098 0.1601 0.0651  -0.0178 0.0288  118 HIS   C NE2 
1975 N N   . GLY   B 113 ? 0.2925 0.1827 0.1807 0.0322  -0.0061 0.0343  119 GLY   C N   
1976 C CA  . GLY   B 113 ? 0.2736 0.1668 0.1723 0.0283  -0.0047 0.0357  119 GLY   C CA  
1977 C C   . GLY   B 113 ? 0.2540 0.1515 0.1541 0.0241  -0.0103 0.0304  119 GLY   C C   
1978 O O   . GLY   B 113 ? 0.2484 0.1478 0.1461 0.0224  -0.0154 0.0259  119 GLY   C O   
1979 N N   . VAL   B 114 ? 0.2469 0.1459 0.1525 0.0226  -0.0086 0.0318  120 VAL   C N   
1980 C CA  . VAL   B 114 ? 0.2365 0.1395 0.1448 0.0192  -0.0124 0.0283  120 VAL   C CA  
1981 C C   . VAL   B 114 ? 0.2490 0.1499 0.1482 0.0220  -0.0140 0.0238  120 VAL   C C   
1982 O O   . VAL   B 114 ? 0.2678 0.1641 0.1600 0.0264  -0.0109 0.0242  120 VAL   C O   
1983 C CB  . VAL   B 114 ? 0.2380 0.1433 0.1562 0.0170  -0.0100 0.0319  120 VAL   C CB  
1984 C CG1 . VAL   B 114 ? 0.2627 0.1714 0.1825 0.0147  -0.0129 0.0291  120 VAL   C CG1 
1985 C CG2 . VAL   B 114 ? 0.2406 0.1481 0.1705 0.0138  -0.0113 0.0349  120 VAL   C CG2 
1986 N N   . VAL   B 115 ? 0.2336 0.1372 0.1337 0.0200  -0.0189 0.0196  121 VAL   C N   
1987 C CA  . VAL   B 115 ? 0.2303 0.1325 0.1270 0.0219  -0.0222 0.0145  121 VAL   C CA  
1988 C C   . VAL   B 115 ? 0.2188 0.1235 0.1230 0.0198  -0.0219 0.0136  121 VAL   C C   
1989 O O   . VAL   B 115 ? 0.2247 0.1267 0.1270 0.0222  -0.0229 0.0103  121 VAL   C O   
1990 C CB  . VAL   B 115 ? 0.2378 0.1417 0.1362 0.0209  -0.0268 0.0113  121 VAL   C CB  
1991 C CG1 . VAL   B 115 ? 0.2419 0.1453 0.1429 0.0222  -0.0313 0.0059  121 VAL   C CG1 
1992 C CG2 . VAL   B 115 ? 0.2394 0.1409 0.1312 0.0232  -0.0272 0.0122  121 VAL   C CG2 
1993 N N   . GLY   B 116 ? 0.1944 0.1038 0.1066 0.0159  -0.0209 0.0163  122 GLY   C N   
1994 C CA  . GLY   B 116 ? 0.2080 0.1202 0.1279 0.0142  -0.0200 0.0167  122 GLY   C CA  
1995 C C   . GLY   B 116 ? 0.2148 0.1312 0.1399 0.0113  -0.0195 0.0202  122 GLY   C C   
1996 O O   . GLY   B 116 ? 0.2261 0.1428 0.1488 0.0104  -0.0204 0.0217  122 GLY   C O   
1997 N N   . ILE   B 117 ? 0.1985 0.1177 0.1303 0.0104  -0.0183 0.0214  123 ILE   C N   
1998 C CA  . ILE   B 117 ? 0.1972 0.1195 0.1310 0.0091  -0.0180 0.0249  123 ILE   C CA  
1999 C C   . ILE   B 117 ? 0.2010 0.1251 0.1397 0.0096  -0.0166 0.0252  123 ILE   C C   
2000 O O   . ILE   B 117 ? 0.2031 0.1272 0.1490 0.0100  -0.0154 0.0235  123 ILE   C O   
2001 C CB  . ILE   B 117 ? 0.2112 0.1350 0.1491 0.0084  -0.0167 0.0288  123 ILE   C CB  
2002 C CG1 . ILE   B 117 ? 0.2234 0.1470 0.1674 0.0090  -0.0136 0.0287  123 ILE   C CG1 
2003 C CG2 . ILE   B 117 ? 0.2306 0.1533 0.1674 0.0078  -0.0178 0.0304  123 ILE   C CG2 
2004 C CD1 . ILE   B 117 ? 0.2374 0.1636 0.1882 0.0084  -0.0117 0.0336  123 ILE   C CD1 
2005 N N   . VAL   B 118 ? 0.1811 0.1061 0.1163 0.0102  -0.0164 0.0274  124 VAL   C N   
2006 C CA  . VAL   B 118 ? 0.1899 0.1161 0.1298 0.0119  -0.0128 0.0295  124 VAL   C CA  
2007 C C   . VAL   B 118 ? 0.1865 0.1149 0.1361 0.0120  -0.0095 0.0326  124 VAL   C C   
2008 O O   . VAL   B 118 ? 0.1896 0.1191 0.1381 0.0116  -0.0099 0.0352  124 VAL   C O   
2009 C CB  . VAL   B 118 ? 0.2030 0.1283 0.1334 0.0140  -0.0126 0.0321  124 VAL   C CB  
2010 C CG1 . VAL   B 118 ? 0.2226 0.1484 0.1566 0.0172  -0.0067 0.0364  124 VAL   C CG1 
2011 C CG2 . VAL   B 118 ? 0.2190 0.1417 0.1416 0.0140  -0.0152 0.0287  124 VAL   C CG2 
2012 N N   . SER   B 119 ? 0.1950 0.1242 0.1564 0.0126  -0.0064 0.0325  125 SER   C N   
2013 C CA  . SER   B 119 ? 0.1867 0.1176 0.1603 0.0128  -0.0028 0.0353  125 SER   C CA  
2014 C C   . SER   B 119 ? 0.2017 0.1340 0.1870 0.0152  0.0034  0.0398  125 SER   C C   
2015 O O   . SER   B 119 ? 0.1972 0.1311 0.1897 0.0164  0.0079  0.0449  125 SER   C O   
2016 C CB  . SER   B 119 ? 0.2159 0.1454 0.1973 0.0113  -0.0053 0.0298  125 SER   C CB  
2017 O OG  . SER   B 119 ? 0.2450 0.1756 0.2396 0.0113  -0.0020 0.0316  125 SER   C OG  
2018 N N   . THR   B 120 ? 0.2023 0.1337 0.1915 0.0161  0.0043  0.0386  126 THR   C N   
2019 C CA  . THR   B 120 ? 0.2090 0.1412 0.2122 0.0188  0.0117  0.0438  126 THR   C CA  
2020 C C   . THR   B 120 ? 0.2229 0.1533 0.2167 0.0219  0.0149  0.0464  126 THR   C C   
2021 O O   . THR   B 120 ? 0.2184 0.1470 0.1989 0.0210  0.0100  0.0422  126 THR   C O   
2022 C CB  . THR   B 120 ? 0.2171 0.1499 0.2440 0.0171  0.0106  0.0398  126 THR   C CB  
2023 O OG1 . THR   B 120 ? 0.2226 0.1540 0.2493 0.0163  0.0061  0.0347  126 THR   C OG1 
2024 C CG2 . THR   B 120 ? 0.2292 0.1617 0.2620 0.0144  0.0058  0.0347  126 THR   C CG2 
2025 N N   . GLY   B 121 ? 0.2373 0.1676 0.2390 0.0262  0.0239  0.0536  127 GLY   C N   
2026 C CA  . GLY   B 121 ? 0.2771 0.2046 0.2712 0.0305  0.0293  0.0570  127 GLY   C CA  
2027 C C   . GLY   B 121 ? 0.3022 0.2296 0.3127 0.0354  0.0412  0.0657  127 GLY   C C   
2028 O O   . GLY   B 121 ? 0.3271 0.2560 0.3471 0.0372  0.0466  0.0714  127 GLY   C O   
2029 N N   . GLY   B 122 ? 0.3152 0.2403 0.3283 0.0384  0.0464  0.0676  128 GLY   C N   
2030 C CA  . GLY   B 122 ? 0.3122 0.2365 0.3425 0.0440  0.0597  0.0771  128 GLY   C CA  
2031 C C   . GLY   B 122 ? 0.3104 0.2345 0.3592 0.0436  0.0620  0.0761  128 GLY   C C   
2032 O O   . GLY   B 122 ? 0.2919 0.2180 0.3479 0.0379  0.0519  0.0675  128 GLY   C O   
2033 N N   . ASN   B 123 ? 0.3244 0.2458 0.3800 0.0504  0.0753  0.0853  129 ASN   C N   
2034 C CA  . ASN   B 123 ? 0.3244 0.2456 0.4018 0.0508  0.0794  0.0862  129 ASN   C CA  
2035 C C   . ASN   B 123 ? 0.3133 0.2333 0.3770 0.0476  0.0701  0.0776  129 ASN   C C   
2036 O O   . ASN   B 123 ? 0.3137 0.2359 0.3996 0.0444  0.0665  0.0742  129 ASN   C O   
2037 C CB  . ASN   B 123 ? 0.3482 0.2745 0.4676 0.0465  0.0781  0.0855  129 ASN   C CB  
2038 C CG  . ASN   B 123 ? 0.4616 0.3883 0.6021 0.0515  0.0923  0.0971  129 ASN   C CG  
2039 O OD1 . ASN   B 123 ? 0.4971 0.4197 0.6297 0.0599  0.1071  0.1080  129 ASN   C OD1 
2040 N ND2 . ASN   B 123 ? 0.4741 0.4048 0.6409 0.0473  0.0888  0.0955  129 ASN   C ND2 
2041 N N   . GLY   B 124 ? 0.3150 0.2313 0.3441 0.0489  0.0661  0.0744  130 GLY   C N   
2042 C CA  . GLY   B 124 ? 0.3050 0.2195 0.3204 0.0464  0.0584  0.0671  130 GLY   C CA  
2043 C C   . GLY   B 124 ? 0.2778 0.1962 0.2951 0.0384  0.0435  0.0569  130 GLY   C C   
2044 O O   . GLY   B 124 ? 0.2768 0.1943 0.2881 0.0362  0.0373  0.0514  130 GLY   C O   
2045 N N   . LEU   B 125 ? 0.2528 0.1749 0.2784 0.0346  0.0383  0.0548  131 LEU   C N   
2046 C CA  . LEU   B 125 ? 0.2497 0.1742 0.2747 0.0284  0.0253  0.0457  131 LEU   C CA  
2047 C C   . LEU   B 125 ? 0.2486 0.1729 0.2526 0.0269  0.0206  0.0437  131 LEU   C C   
2048 O O   . LEU   B 125 ? 0.2577 0.1817 0.2563 0.0296  0.0262  0.0491  131 LEU   C O   
2049 C CB  . LEU   B 125 ? 0.2563 0.1842 0.3099 0.0254  0.0219  0.0433  131 LEU   C CB  
2050 C CG  . LEU   B 125 ? 0.2711 0.2001 0.3529 0.0260  0.0240  0.0444  131 LEU   C CG  
2051 C CD1 . LEU   B 125 ? 0.2880 0.2197 0.3972 0.0229  0.0180  0.0403  131 LEU   C CD1 
2052 C CD2 . LEU   B 125 ? 0.2692 0.1970 0.3440 0.0252  0.0184  0.0398  131 LEU   C CD2 
2053 N N   . VAL   B 126 ? 0.2207 0.1450 0.2141 0.0230  0.0108  0.0365  132 VAL   C N   
2054 C CA  . VAL   B 126 ? 0.2238 0.1483 0.2021 0.0211  0.0061  0.0345  132 VAL   C CA  
2055 C C   . VAL   B 126 ? 0.2046 0.1307 0.1919 0.0174  -0.0012 0.0286  132 VAL   C C   
2056 O O   . VAL   B 126 ? 0.2134 0.1391 0.2060 0.0163  -0.0062 0.0240  132 VAL   C O   
2057 C CB  . VAL   B 126 ? 0.2331 0.1548 0.1889 0.0213  0.0027  0.0325  132 VAL   C CB  
2058 C CG1 . VAL   B 126 ? 0.2448 0.1652 0.1994 0.0200  -0.0016 0.0279  132 VAL   C CG1 
2059 C CG2 . VAL   B 126 ? 0.2350 0.1572 0.1801 0.0191  -0.0025 0.0309  132 VAL   C CG2 
2060 N N   . GLY   B 127 ? 0.2071 0.1344 0.1958 0.0163  -0.0017 0.0290  133 GLY   C N   
2061 C CA  . GLY   B 127 ? 0.2051 0.1324 0.1994 0.0140  -0.0079 0.0234  133 GLY   C CA  
2062 C C   . GLY   B 127 ? 0.2106 0.1370 0.1887 0.0128  -0.0110 0.0220  133 GLY   C C   
2063 O O   . GLY   B 127 ? 0.2042 0.1314 0.1752 0.0131  -0.0080 0.0263  133 GLY   C O   
2064 N N   . PHE   B 128 ? 0.1908 0.1150 0.1637 0.0120  -0.0169 0.0164  134 PHE   C N   
2065 C CA  . PHE   B 128 ? 0.2069 0.1295 0.1663 0.0115  -0.0187 0.0157  134 PHE   C CA  
2066 C C   . PHE   B 128 ? 0.2088 0.1292 0.1708 0.0119  -0.0209 0.0120  134 PHE   C C   
2067 O O   . PHE   B 128 ? 0.2087 0.1269 0.1757 0.0129  -0.0252 0.0066  134 PHE   C O   
2068 C CB  . PHE   B 128 ? 0.1962 0.1166 0.1438 0.0119  -0.0221 0.0134  134 PHE   C CB  
2069 C CG  . PHE   B 128 ? 0.2010 0.1221 0.1456 0.0119  -0.0206 0.0155  134 PHE   C CG  
2070 C CD1 . PHE   B 128 ? 0.2134 0.1347 0.1496 0.0116  -0.0190 0.0187  134 PHE   C CD1 
2071 C CD2 . PHE   B 128 ? 0.2024 0.1234 0.1532 0.0127  -0.0215 0.0139  134 PHE   C CD2 
2072 C CE1 . PHE   B 128 ? 0.2220 0.1425 0.1533 0.0125  -0.0180 0.0197  134 PHE   C CE1 
2073 C CE2 . PHE   B 128 ? 0.2171 0.1378 0.1640 0.0134  -0.0192 0.0158  134 PHE   C CE2 
2074 C CZ  . PHE   B 128 ? 0.2152 0.1352 0.1513 0.0135  -0.0174 0.0184  134 PHE   C CZ  
2075 N N   . ALA   B 129 ? 0.2121 0.1326 0.1709 0.0115  -0.0185 0.0144  135 ALA   C N   
2076 C CA  . ALA   B 129 ? 0.2270 0.1442 0.1856 0.0127  -0.0195 0.0111  135 ALA   C CA  
2077 C C   . ALA   B 129 ? 0.2283 0.1410 0.1718 0.0148  -0.0219 0.0085  135 ALA   C C   
2078 O O   . ALA   B 129 ? 0.2297 0.1427 0.1657 0.0144  -0.0197 0.0124  135 ALA   C O   
2079 C CB  . ALA   B 129 ? 0.2261 0.1449 0.1877 0.0119  -0.0149 0.0157  135 ALA   C CB  
2080 N N   . ASP   B 130 ? 0.2387 0.1468 0.1787 0.0176  -0.0266 0.0023  136 ASP   C N   
2081 C CA  . ASP   B 130 ? 0.2380 0.1408 0.1620 0.0212  -0.0281 0.0006  136 ASP   C CA  
2082 C C   . ASP   B 130 ? 0.2536 0.1528 0.1697 0.0234  -0.0232 0.0030  136 ASP   C C   
2083 O O   . ASP   B 130 ? 0.2626 0.1610 0.1842 0.0235  -0.0213 0.0024  136 ASP   C O   
2084 C CB  . ASP   B 130 ? 0.2312 0.1288 0.1518 0.0249  -0.0353 -0.0072 136 ASP   C CB  
2085 C CG  . ASP   B 130 ? 0.2544 0.1457 0.1560 0.0302  -0.0371 -0.0087 136 ASP   C CG  
2086 O OD1 . ASP   B 130 ? 0.2765 0.1695 0.1732 0.0296  -0.0356 -0.0049 136 ASP   C OD1 
2087 O OD2 . ASP   B 130 ? 0.2981 0.1821 0.1894 0.0355  -0.0399 -0.0137 136 ASP   C OD2 
2088 N N   . VAL   B 131 ? 0.2484 0.1449 0.1530 0.0256  -0.0203 0.0063  137 VAL   C N   
2089 C CA  . VAL   B 131 ? 0.2503 0.1424 0.1481 0.0289  -0.0144 0.0095  137 VAL   C CA  
2090 C C   . VAL   B 131 ? 0.2739 0.1578 0.1538 0.0359  -0.0139 0.0081  137 VAL   C C   
2091 O O   . VAL   B 131 ? 0.2877 0.1665 0.1602 0.0402  -0.0076 0.0113  137 VAL   C O   
2092 C CB  . VAL   B 131 ? 0.2549 0.1516 0.1602 0.0255  -0.0089 0.0173  137 VAL   C CB  
2093 C CG1 . VAL   B 131 ? 0.2463 0.1499 0.1657 0.0203  -0.0095 0.0189  137 VAL   C CG1 
2094 C CG2 . VAL   B 131 ? 0.2465 0.1447 0.1496 0.0246  -0.0092 0.0203  137 VAL   C CG2 
2095 N N   . ARG   B 132 ? 0.2687 0.1512 0.1419 0.0376  -0.0199 0.0042  138 ARG   C N   
2096 C CA  . ARG   B 132 ? 0.2670 0.1417 0.1217 0.0451  -0.0195 0.0039  138 ARG   C CA  
2097 C C   . ARG   B 132 ? 0.2956 0.1603 0.1346 0.0531  -0.0203 -0.0010 138 ARG   C C   
2098 O O   . ARG   B 132 ? 0.3235 0.1804 0.1444 0.0610  -0.0170 0.0008  138 ARG   C O   
2099 C CB  . ARG   B 132 ? 0.2771 0.1532 0.1297 0.0451  -0.0266 0.0010  138 ARG   C CB  
2100 C CG  . ARG   B 132 ? 0.2757 0.1595 0.1400 0.0387  -0.0252 0.0056  138 ARG   C CG  
2101 C CD  . ARG   B 132 ? 0.2843 0.1690 0.1476 0.0391  -0.0323 0.0020  138 ARG   C CD  
2102 N NE  . ARG   B 132 ? 0.2738 0.1615 0.1483 0.0362  -0.0392 -0.0040 138 ARG   C NE  
2103 C CZ  . ARG   B 132 ? 0.2982 0.1877 0.1779 0.0356  -0.0456 -0.0073 138 ARG   C CZ  
2104 N NH1 . ARG   B 132 ? 0.2812 0.1696 0.1538 0.0378  -0.0467 -0.0058 138 ARG   C NH1 
2105 N NH2 . ARG   B 132 ? 0.2805 0.1730 0.1746 0.0328  -0.0504 -0.0116 138 ARG   C NH2 
2106 N N   . ASP   B 133 ? 0.2831 0.1473 0.1283 0.0520  -0.0248 -0.0075 139 ASP   C N   
2107 C CA  . ASP   B 133 ? 0.2943 0.1479 0.1247 0.0598  -0.0266 -0.0138 139 ASP   C CA  
2108 C C   . ASP   B 133 ? 0.3196 0.1692 0.1465 0.0624  -0.0158 -0.0088 139 ASP   C C   
2109 O O   . ASP   B 133 ? 0.3434 0.1821 0.1535 0.0707  -0.0150 -0.0130 139 ASP   C O   
2110 C CB  . ASP   B 133 ? 0.3093 0.1628 0.1500 0.0579  -0.0366 -0.0237 139 ASP   C CB  
2111 C CG  . ASP   B 133 ? 0.3574 0.2188 0.2210 0.0500  -0.0333 -0.0215 139 ASP   C CG  
2112 O OD1 . ASP   B 133 ? 0.3259 0.1965 0.2019 0.0435  -0.0286 -0.0141 139 ASP   C OD1 
2113 O OD2 . ASP   B 133 ? 0.3826 0.2403 0.2509 0.0511  -0.0355 -0.0272 139 ASP   C OD2 
2114 N N   . LEU   B 134 ? 0.3091 0.1667 0.1514 0.0560  -0.0080 -0.0003 140 LEU   C N   
2115 C CA  . LEU   B 134 ? 0.3208 0.1762 0.1651 0.0575  0.0023  0.0056  140 LEU   C CA  
2116 C C   . LEU   B 134 ? 0.3300 0.1797 0.1613 0.0641  0.0117  0.0133  140 LEU   C C   
2117 O O   . LEU   B 134 ? 0.3176 0.1731 0.1609 0.0603  0.0180  0.0220  140 LEU   C O   
2118 C CB  . LEU   B 134 ? 0.2969 0.1636 0.1649 0.0481  0.0047  0.0113  140 LEU   C CB  
2119 C CG  . LEU   B 134 ? 0.3033 0.1758 0.1858 0.0422  -0.0022 0.0059  140 LEU   C CG  
2120 C CD1 . LEU   B 134 ? 0.2952 0.1780 0.1971 0.0346  0.0005  0.0125  140 LEU   C CD1 
2121 C CD2 . LEU   B 134 ? 0.3210 0.1864 0.2005 0.0461  -0.0030 -0.0007 140 LEU   C CD2 
2122 N N   . LEU   B 135 ? 0.3542 0.1918 0.1612 0.0747  0.0126  0.0101  141 LEU   C N   
2123 C CA  . LEU   B 135 ? 0.3698 0.2008 0.1630 0.0826  0.0224  0.0181  141 LEU   C CA  
2124 C C   . LEU   B 135 ? 0.3816 0.2120 0.1837 0.0837  0.0368  0.0284  141 LEU   C C   
2125 O O   . LEU   B 135 ? 0.3851 0.2148 0.1886 0.0864  0.0460  0.0381  141 LEU   C O   
2126 C CB  . LEU   B 135 ? 0.3863 0.2031 0.1480 0.0956  0.0203  0.0126  141 LEU   C CB  
2127 C CG  . LEU   B 135 ? 0.4080 0.2245 0.1617 0.0955  0.0045  0.0017  141 LEU   C CG  
2128 C CD1 . LEU   B 135 ? 0.4188 0.2196 0.1385 0.1100  0.0009  -0.0044 141 LEU   C CD1 
2129 C CD2 . LEU   B 135 ? 0.4057 0.2328 0.1726 0.0880  0.0000  0.0047  141 LEU   C CD2 
2130 N N   . TRP   B 136 ? 0.3796 0.2093 0.1886 0.0824  0.0393  0.0268  142 TRP   C N   
2131 C CA  . TRP   B 136 ? 0.3875 0.2163 0.2070 0.0836  0.0528  0.0364  142 TRP   C CA  
2132 C C   . TRP   B 136 ? 0.3737 0.2151 0.2215 0.0740  0.0556  0.0455  142 TRP   C C   
2133 O O   . TRP   B 136 ? 0.3746 0.2157 0.2341 0.0753  0.0668  0.0550  142 TRP   C O   
2134 C CB  . TRP   B 136 ? 0.3817 0.2077 0.2037 0.0838  0.0534  0.0317  142 TRP   C CB  
2135 C CG  . TRP   B 136 ? 0.3707 0.2066 0.2092 0.0736  0.0419  0.0247  142 TRP   C CG  
2136 C CD1 . TRP   B 136 ? 0.3785 0.2121 0.2098 0.0734  0.0306  0.0131  142 TRP   C CD1 
2137 C CD2 . TRP   B 136 ? 0.3511 0.1994 0.2165 0.0633  0.0415  0.0293  142 TRP   C CD2 
2138 N NE1 . TRP   B 136 ? 0.3678 0.2121 0.2210 0.0636  0.0246  0.0113  142 TRP   C NE1 
2139 C CE2 . TRP   B 136 ? 0.3572 0.2105 0.2294 0.0576  0.0310  0.0211  142 TRP   C CE2 
2140 C CE3 . TRP   B 136 ? 0.3524 0.2080 0.2375 0.0587  0.0482  0.0397  142 TRP   C CE3 
2141 C CZ2 . TRP   B 136 ? 0.3464 0.2107 0.2411 0.0488  0.0287  0.0237  142 TRP   C CZ2 
2142 C CZ3 . TRP   B 136 ? 0.3393 0.2059 0.2460 0.0496  0.0439  0.0411  142 TRP   C CZ3 
2143 C CH2 . TRP   B 136 ? 0.3435 0.2143 0.2532 0.0450  0.0346  0.0334  142 TRP   C CH2 
2144 N N   . LEU   B 137 ? 0.3443 0.1958 0.2032 0.0652  0.0452  0.0426  143 LEU   C N   
2145 C CA  . LEU   B 137 ? 0.3386 0.2006 0.2214 0.0570  0.0457  0.0496  143 LEU   C CA  
2146 C C   . LEU   B 137 ? 0.3833 0.2428 0.2685 0.0609  0.0545  0.0590  143 LEU   C C   
2147 O O   . LEU   B 137 ? 0.3929 0.2582 0.3003 0.0565  0.0584  0.0665  143 LEU   C O   
2148 C CB  . LEU   B 137 ? 0.3174 0.1886 0.2068 0.0486  0.0333  0.0439  143 LEU   C CB  
2149 C CG  . LEU   B 137 ? 0.3237 0.2001 0.2203 0.0430  0.0262  0.0380  143 LEU   C CG  
2150 C CD1 . LEU   B 137 ? 0.3278 0.2110 0.2271 0.0371  0.0157  0.0327  143 LEU   C CD1 
2151 C CD2 . LEU   B 137 ? 0.3245 0.2073 0.2416 0.0380  0.0296  0.0440  143 LEU   C CD2 
2152 N N   . ASP   B 138 ? 0.3992 0.2497 0.2627 0.0697  0.0577  0.0587  144 ASP   C N   
2153 C CA  . ASP   B 138 ? 0.4326 0.2792 0.2964 0.0751  0.0674  0.0681  144 ASP   C CA  
2154 C C   . ASP   B 138 ? 0.4841 0.3219 0.3460 0.0843  0.0836  0.0775  144 ASP   C C   
2155 O O   . ASP   B 138 ? 0.4989 0.3329 0.3629 0.0897  0.0937  0.0868  144 ASP   C O   
2156 C CB  . ASP   B 138 ? 0.4577 0.2975 0.2962 0.0822  0.0642  0.0643  144 ASP   C CB  
2157 C CG  . ASP   B 138 ? 0.5128 0.3598 0.3519 0.0750  0.0498  0.0560  144 ASP   C CG  
2158 O OD1 . ASP   B 138 ? 0.5033 0.3608 0.3634 0.0646  0.0439  0.0553  144 ASP   C OD1 
2159 O OD2 . ASP   B 138 ? 0.5532 0.3948 0.3710 0.0804  0.0442  0.0502  144 ASP   C OD2 
2160 N N   . GLU   B 139 ? 0.5137 0.3474 0.3716 0.0868  0.0872  0.0756  145 GLU   C N   
2161 C CA  . GLU   B 139 ? 0.5686 0.3922 0.4220 0.0970  0.1038  0.0844  145 GLU   C CA  
2162 C C   . GLU   B 139 ? 0.5977 0.4248 0.4710 0.0929  0.1083  0.0871  145 GLU   C C   
2163 O O   . GLU   B 139 ? 0.5920 0.4304 0.4848 0.0818  0.0984  0.0834  145 GLU   C O   
2164 C CB  . GLU   B 139 ? 0.6305 0.4389 0.4453 0.1105  0.1061  0.0789  145 GLU   C CB  
2165 C CG  . GLU   B 139 ? 0.7283 0.5356 0.5290 0.1085  0.0930  0.0646  145 GLU   C CG  
2166 C CD  . GLU   B 139 ? 0.8504 0.6441 0.6136 0.1201  0.0888  0.0561  145 GLU   C CD  
2167 O OE1 . GLU   B 139 ? 0.8704 0.6584 0.6205 0.1225  0.0825  0.0458  145 GLU   C OE1 
2168 O OE2 . GLU   B 139 ? 0.8885 0.6770 0.6360 0.1273  0.0913  0.0596  145 GLU   C OE2 
2169 N N   . GLU   B 140 ? 0.6266 0.4436 0.4951 0.1026  0.1239  0.0943  146 GLU   C N   
2170 C CA  . GLU   B 140 ? 0.6432 0.4615 0.5291 0.1009  0.1308  0.0981  146 GLU   C CA  
2171 C C   . GLU   B 140 ? 0.6495 0.4812 0.5760 0.0903  0.1304  0.1064  146 GLU   C C   
2172 O O   . GLU   B 140 ? 0.6630 0.4932 0.6087 0.0932  0.1440  0.1178  146 GLU   C O   
2173 C CB  . GLU   B 140 ? 0.6768 0.4945 0.5515 0.0984  0.1210  0.0859  146 GLU   C CB  
2174 C CG  . GLU   B 140 ? 0.7538 0.5748 0.6495 0.0949  0.1260  0.0893  146 GLU   C CG  
2175 C CD  . GLU   B 140 ? 0.8848 0.6916 0.7664 0.1070  0.1414  0.0926  146 GLU   C CD  
2176 O OE1 . GLU   B 140 ? 0.9321 0.7345 0.8038 0.1081  0.1383  0.0843  146 GLU   C OE1 
2177 O OE2 . GLU   B 140 ? 0.9001 0.6996 0.7811 0.1157  0.1572  0.1037  146 GLU   C OE2 
2178 N N1  . A1BN1 C .   ? 0.4252 0.2867 0.3755 -0.0181 0.0559  -0.0266 201 A1BN1 A N1  
2179 C C4  . A1BN1 C .   ? 0.5111 0.3419 0.4624 -0.0457 0.1131  -0.0617 201 A1BN1 A C4  
2180 C C5  . A1BN1 C .   ? 0.4689 0.3054 0.4359 -0.0350 0.1023  -0.0519 201 A1BN1 A C5  
2181 C C6  . A1BN1 C .   ? 0.4455 0.2911 0.4084 -0.0279 0.0848  -0.0419 201 A1BN1 A C6  
2182 C C7  . A1BN1 C .   ? 0.4381 0.2938 0.3855 -0.0234 0.0656  -0.0329 201 A1BN1 A C7  
2183 C C8  . A1BN1 C .   ? 0.4224 0.2934 0.3608 -0.0137 0.0383  -0.0187 201 A1BN1 A C8  
2184 C C10 . A1BN1 C .   ? 0.4293 0.2872 0.4049 -0.0150 0.0642  -0.0269 201 A1BN1 A C10 
2185 C C13 . A1BN1 C .   ? 0.4330 0.2686 0.4283 -0.0274 0.1030  -0.0475 201 A1BN1 A C13 
2186 O O   . A1BN1 C .   ? 0.4752 0.3014 0.4602 -0.0392 0.1221  -0.0611 201 A1BN1 A O   
2187 C C14 . A1BN1 C .   ? 0.4335 0.2784 0.4098 -0.0248 0.0864  -0.0405 201 A1BN1 A C14 
2188 C C12 . A1BN1 C .   ? 0.4333 0.2710 0.4370 -0.0234 0.0990  -0.0433 201 A1BN1 A C12 
2189 C C11 . A1BN1 C .   ? 0.4328 0.2821 0.4261 -0.0173 0.0793  -0.0329 201 A1BN1 A C11 
2190 C C9  . A1BN1 C .   ? 0.4310 0.2865 0.3982 -0.0186 0.0675  -0.0305 201 A1BN1 A C9  
2191 N N   . A1BN1 C .   ? 0.4856 0.3248 0.4365 -0.0373 0.0966  -0.0512 201 A1BN1 A N   
2192 C C3  . A1BN1 C .   ? 0.5445 0.3689 0.4587 -0.0635 0.1135  -0.0751 201 A1BN1 A C3  
2193 C C2  . A1BN1 C .   ? 0.5619 0.3852 0.4540 -0.0732 0.1132  -0.0799 201 A1BN1 A C2  
2194 O O1  . A1BN1 C .   ? 0.5530 0.3726 0.4519 -0.0744 0.1151  -0.0840 201 A1BN1 A O1  
2195 N N2  . A1BN1 C .   ? 0.5757 0.3919 0.4397 -0.0940 0.1157  -0.0949 201 A1BN1 A N2  
2196 C C1  . A1BN1 C .   ? 0.5811 0.3994 0.4419 -0.0924 0.1144  -0.0918 201 A1BN1 A C1  
2197 C C   . A1BN1 C .   ? 0.6002 0.4171 0.4269 -0.1112 0.1137  -0.0994 201 A1BN1 A C   
# 
